LOCUS       WP_357519306             390 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Micromonospora sp.
            NPDC047187].
ACCESSION   WP_357519306
VERSION     WP_357519306.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047187
  ORGANISM  Micromonospora sp. NPDC047187
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Micromonospora sp. NPDC047187"
                     /db_xref="taxon:3155262"
     Protein         1..390
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39943
     Region          51..387
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 miaeagsrpa pleilgpghg ggrladvlps alavlgvpgs tdplglrpel agvrriavll
       61 vdglgwyqlp taapyaptia glaatvarpl iagfpsttpt slvslgtgva pgahgvlgft
      121 vrvpgtdrvl thtdwaadps plrwqpvptq leraraagvt tsvvsrpefg gsgltlaanr
      181 ggdfrgaagg davatamlaa laagagptlv sgyhadldrh ghvsgvdsap wrvaatevda
      241 lvtrlvdglp pdaallvtad hgqldipaah rfdldtdprl ragvrlvage arvrylhvep
      301 gavddvraaw sevlgatarv rtrdevvatg wfgpvpeehl grigdvvvic ndtyavmasr
      361 terpmasklv ayhgsdtaae ltvpllvvrg
//
LOCUS       WP_357519246             239 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Polymorphospora
            rubra].
ACCESSION   WP_357519246
VERSION     WP_357519246.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=26433
     Region          4..138
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 maldfaaayd dlnpddhdyr fyasladdlq atrvldlgcg tgmlarllas pgrtvvgidp
       61 dpemlrvake ksgaeqvewr qgfsdcadtd sadfavmsgh vaqvfredea wsralgdlnr
      121 alvphgtlaf esrnpaasaw erwtrqatlr tlnadegpie fwhetawvsl plvaydtftr
      181 nlrtgveess rdvlafrdas slvrsldkag fsvlrqyggw qrepltavap eiiliaqrr
//
LOCUS       WP_357519326             407 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357519326
VERSION     WP_357519326.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..407
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..407
                     /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=43513
     Region          16..367
                     /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 mmmriaiagg glggltlari lhrhgidavv yereasrsar sqggmldlhp esgqqalada
       61 glaarfrsaa rpegeehril dptgrtlvhh rpqpgsfsgr peidrrvlrd llldslpadt
      121 vawqhrlvaa tprtdggfgl tfhgghsadc dvligadgar svvrslltdt tlsyvatlve
      181 ltisdadrrh pdlaelvgpg nlwcigvnri laaqrlgdgs irvgislpad drhldayrsk
      241 ralldmfdgw npgltaliea gdspptprri eamptgtrwa hqpgitllgd aahlmppvge
      301 ganqamldaa elaaelaael aanptdpdsa irtyeqamft rirpiaemsa rvqammlspt
      361 aaddiirfft prptepapas grpderarrs trppgkpvag grhrmsg
//
LOCUS       WP_357519336             194 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357519336
VERSION     WP_357519336.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 194)
  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..194
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..194
                     /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=20646
     Region          30..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpridaptva qhraqrrral ldaarallae nphhaptlaa vavraglprs svyeyfrsrd
       61 dlllelvqev lpnwsrrvtd amaaadspge qvlayaaanl rlvaegehal ataliesvpg
      121 eqvnastqrm heqmsqplsa alsalglpdp tatagligsv vytasrmiet gsdataieer
      181 vrellapfll grav
//
LOCUS       WP_357519372            1845 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Polymorphospora rubra].
ACCESSION   WP_357519372
VERSION     WP_357519372.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 1845)
  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 1845)
  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 1845)
  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 1845)
  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 11463197
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1845
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..1845
                     /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]"
                     /calculated_mol_wt=197889
     Region          9..1285
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1359..1629
                     /region_name="hot_dog"
                     /note="The hotdog fold was initially identified in the E.
                     coli FabA (beta-hydroxydecanoyl-acyl carrier protein
                     (ACP)-dehydratase) structure and subsequently in 4HBT
                     (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A
                     number of other seemingly unrelated...; cl00509"
                     /db_xref="CDD:469797"
     Region          <1707..1825
                     /region_name="PRK12316"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237054"
ORIGIN      
        1 msgvedahia iiglagrfpg ardvnefwhn lvggvesitf fsddelreag vseesiadas
       61 yvkaapiteg admfdagyfg mspreaeild pqqrifleec etalqhsgyd pasyagrigv
      121 ygglgfnnyl ednvnknpdv vdvmgrlstn isntadylat gvsyrlglrg psftclsacs
      181 tsmvaihlas qalrsgecem alaggveefi prvsgyfyse gglyspdghc rtfdakargt
      241 vfgsgagvvl lkrldaalad gdnvlavira tainndgndk gaftapsisg qfaavsdala
      301 rsgvdpatis yveahgtstf vgdpievnal tkafrahtdr rqycgigsvk tnvghlgaaa
      361 gvtgliktvl amqhrvlpps infdepnpqi dfenspfyvn tdltpwksds gplrasvssf
      421 gvggtnghlv leeapaveps srpirahqll llsartptal eanatavgah lrdrpeelad
      481 aaytlavgrt arpvrsflvt tdgteagdrl aagvpqpspg vipprgvkre vafvfpgqga
      541 qypqmgrdly etepvfrtei dqcaevlreq tgwdlrellf psdddaaaaa drlnqtavtq
      601 palfvveyam aklvlswglr pesmvghsvg eyvaatlagv ftrddalrlv aargalmqel
      661 pagsmlsvpm seqvvtsmlp adlslaavna pdlvvvsgpd qaveqfkavl avqgmegral
      721 htshafhsqm mdpildrfte lvaavprsep tipfvsnlsg dwitaeqatd paywaahlrg
      781 avrfadavgl lsaaarvlve lgpgqtlssl arrqlgadrq glavstmrhp qqrqpdtavl
      841 laalgqvwqt gadidfaalw ggerrhrval prvpyekqrs wleggaqtta stqdvaante
      901 tgpyyvpvwk etsppapadv dtaaawvvfe padggvvael tarlrtagat vvsvragaeq
      961 hadgdaytvr pgeladysav vaaaladqpe rlkivhgwlv gdlagdtgrd rardglsrgf
     1021 fsilaaaqav srnpasppld lylltselrd vvggeriepv ksgvdgfvkl lpkefsdttc
     1081 rsidvsagra vadqllreis sgsadqvvay rgrkrwlwsh eevaldgvga arrllrdggv
     1141 ylitgglggi glvtardlae hhgaklvlvg rsglppreew rdllagpeta vtariravee
     1201 ieaaggevlv iaadvtdtes lravrtqaea afgpvngvlh aagitgggml etrrfadaea
     1261 vlaakvfgtl aieevfgdsi dllvlyssft vfsgdfglfd ycsansilds yaqsrsggnt
     1321 hvvsinwpiw tklgmafdid vpdlltsfel gdryekvahp llgsrlvrag sdqvifvknl
     1381 stedwvtaeh qldslptmpg tslvelvraa yeevtgsrta evrdvvfmrp vqfvdsrtvh
     1441 iiltpkpngv ydvmiadads eggnpveftt akvgpgprdd aprhdvsawk atchvedepe
     1501 gvtegiitlg prwqqsirah whgdqtdqgl fdelvllelg eeflgdldef glhpalldka
     1561 talgqtvvas qtshlpfgyd ritvraalpr rfysyirhld dtrgalirtd itladedgve
     1621 lvaikgftmf eyndtsmsts egsdtapaaa adeedesrfs iarqlerall rsnekafgie
     1681 pedgyrmlrq mldsaaapqi ivcpdsfvkr mrmagevtrd alreqlmaap katasvatrs
     1741 lmtpyvepes dvqrvltqmw adtlgldkvg idddffdlng nsliavqlva rireqfqvdl
     1801 tvaglfeart sralseriee llvemlssls deeaaarles ittrn
//
LOCUS       WP_357519392             124 aa            linear   BCT 28-DEC-2024
DEFINITION  VOC family protein [Polymorphospora rubra].
ACCESSION   WP_357519392
VERSION     WP_357519392.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 124)
  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 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..124
                     /product="VOC family protein"
                     /calculated_mol_wt=13145
     Region          7..113
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mailktyarl wvddldralp lltelvgaap dlrfgfggve laavgdflvi agpaeqrary
       61 adasatvvvs dldevvtrla ahggrvtvpv avsetgrfly aehaggaqve yvewvpelvr
      121 rilg
//
LOCUS       WP_357519393             226 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Polymorphospora rubra].
ACCESSION   WP_357519393
VERSION     WP_357519393.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 226)
  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 226)
  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 226)
  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..226
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..226
                     /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=24052
     Region          <1..211
                     /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 mvrtgndpva viglgrfgta lalelvrngt evlaidsqsk ivqgltgqip hvitadstdi
       61 ealrqlglpe fqravvaigt diqasiftts lladmgipdi wakaisglhg dilarvgahh
      121 ivapendmge rvahllsgrv leyvefdtdf aivktkppgd ivgvplrear vrkkygvtiv
      181 avkpqatipt geprftdttp dtvlsygdli lvqgtienie rfaate
//
LOCUS       WP_357519406             395 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora sp.
            NPDC047187].
ACCESSION   WP_357519406
VERSION     WP_357519406.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047187
  ORGANISM  Micromonospora sp. NPDC047187
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047187"
                     /db_xref="taxon:3155262"
     Protein         1..395
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41948
     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 mtapldgvtv vdlatlfagp laaaflgdfg advikvehpa kpdpsrghgp ardgvglwwk
       61 vlgrnkrtvt lnlsdpdgaa llrrlladad vlvenfrpgt lerwglgpae lhavnprlvi
      121 trisgfgqvg pyarrpgfgt laeamsgfaa atgepdgppt lppfgladsv salaaayavm
      181 lalrardvtg agqvvdlaii epimamlgpq itwydqlgyv qprlgnrsnn naprntyrca
      241 dgrwvavsts aqsiaervlr lvgrpelide pwfatgsgra ahadeldaav sawvarrdrd
      301 evvaafeeaq aavapvydvr diladpqyaa lgtvrtvpde elgevrmqnv pfrlaetpge
      361 irhagrrhgq dtdavfgalg lsaeelaalr ergvl
//
LOCUS       WP_357519424             175 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC047187].
ACCESSION   WP_357519424
VERSION     WP_357519424.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047187
  ORGANISM  Micromonospora sp. NPDC047187
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 175)
  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 175)
  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 175)
  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 175)
  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..175
                     /organism="Micromonospora sp. NPDC047187"
                     /db_xref="taxon:3155262"
     Protein         1..175
                     /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=19152
     Region          12..172
                     /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 mrylrtggpa airrprptds defvaaarrs rdlhhpwlaa paspeeyely lrrirrrdsa
       61 gylicdrasg eiagyanisg ivlgalrggy lgyaaflpys gtghasagva lvidhvftsv
      121 glhrleaniq pgnepsrrva rklgfrlegf spdyllidga wrdherwait aptpa
//
LOCUS       WP_357519469             388 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora sp.
            NPDC047187].
ACCESSION   WP_357519469
VERSION     WP_357519469.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047187
  ORGANISM  Micromonospora sp. NPDC047187
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..388
                     /organism="Micromonospora sp. NPDC047187"
                     /db_xref="taxon:3155262"
     Protein         1..388
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41584
     Region          159..367
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mgglfslwrq rvadnahrav dayqeelley rnlaampqvr semldfavfl rqrtvdlaad
       61 sapfhvqdld lmaamgrqrg ekgltltaqr qvllvhtrlt lrevyeaagp ndiaatmhtl
      121 awlapaglaa qgaytrgwie gqrrtlataa qvrlltvmll agddsatdla sslhmpvpdh
      181 vvatvvrvag gspgpdqaar defagallkt hwmplswpep hevvalipss pgarqpaver
      241 glalardvas mtgrpcaagt apgrvrafgd avalarqvse vapvravprh aytvtdvfae
      301 lgaarltevg qwlqvvgaql dagpnlvatl dayyqhdmnr ldtaaalcih prtldyrltr
      361 vrdltgleag strgvrvlst avarilag
//
LOCUS       WP_357519482             577 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase, partial
            [Micromonospora sp. NPDC047187].
ACCESSION   WP_357519482
VERSION     WP_357519482.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047187
  ORGANISM  Micromonospora sp. NPDC047187
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 577)
  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 577)
  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..577
                     /organism="Micromonospora sp. NPDC047187"
                     /db_xref="taxon:3155262"
     Protein         <1..577
                     /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          23..553
                     /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 attpliaaap aqaagaarpr twdltllgts dthgnvynwd yyrdaeydds kqndigvakl
       61 atlinqirre rrgkatlvld agdtiqgtpl atyyakqepi tatgekhpma ramnvidyda
      121 vtlgnhefny glplldlwir qlgfpalaan avnaktgkpa flpyvikkvs lgfaaptlrv
      181 gilgltnpgv aiwdkgnveg klrfddmvat aakwvpimra rgadlvlisa hggdsgtssy
      241 gpelpnenpv aliaqqvpgi dailfghahn evverfvtne rtgtqvllse pskwgqrltr
      301 mdftltrerg rwaitkkaat mlntntvved pkvlaavraq hqktvayvnq vvatstvels
      361 aaesrykdtp ildfinhvqt evvgaalagt ayadlpvlsi aapfsrtavf pagdvkirdv
      421 aglyvydntl eavvlsgaev rayleysaky frtfapgapv dpeqisdpav pdynydvfsg
      481 ldydidiskp vgqritrlvl agtdtpvadn aqfvvavnny rrsgggnfpg ivktqvynaq
      541 qeirqllidw aqakgtidpa dffqpnwrlv regvpvf
//
LOCUS       WP_357519545             317 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Polymorphospora rubra].
ACCESSION   WP_357519545
VERSION     WP_357519545.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   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 317)
  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..317
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..317
                     /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=33726
     Region          28..302
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mtaetltpdt lrpatsptmy fvgvttgssa ihrvfaawrp llglddvalv gidvpvgadp
       61 avyrrvvahl rddelshgal vtthkldlya astdllrrvn ddaarlrevs alvardgwid
      121 ghaldtitsq lslqaivprl agrdvlvmga ggaalalcdy fahragadap grvvvtdiad
      181 drlasirtdi gggnpaiewv thrlspgeth dellaglapg avvvnatgmg kdrpgspltd
      241 aavfpnggya wefnyrgelg flrqararae adgltvedgw ryfvhgwtra vdavfdlgip
      301 tagpdferly daaqevr
//
LOCUS       WP_357519594             192 aa            linear   BCT 28-DEC-2024
DEFINITION  Dps family protein [Polymorphospora rubra].
ACCESSION   WP_357519594
VERSION     WP_357519594.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 192)
  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   3  (residues 1 to 192)
  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 192)
  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 192)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..192
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=21436
     Region          32..186
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mtryavqttd sqpllhqhgr qiqefgsvrq lpvglsydar myscervnll ladsqilysl
       61 ykkhhwlmrg htfyqlhlll dkhageqlai idmlaervqt lggvavgdpr hvaemtrvpr
      121 ppngaeevpa mlsrlleahe tilidahdaa srvaemgddg tndllvsnvi rtgelqtwfi
      181 aehlvdtpav ra
//
LOCUS       WP_357519608             520 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Polymorphospora rubra].
ACCESSION   WP_357519608
VERSION     WP_357519608.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 520)
  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 520)
  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..520
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..520
                     /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=53780
     Region          <89..>259
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          182..395
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 makknsrrqh rqdgpisfvl rpvawsalla avatmaiaap ayadpplptt ipdsgsrplp
       61 tgpfqlpgtt tpptggtntp tvpavngpla adimakqiey griseqllkl qidrdaattt
      121 lasaeatlrt aredlaraes ladqsatdal kgaaalppgt fgtdlhglga lsriqkgaqt
      181 gadtgtaare varartaeqa anqaylaant taqgligqyn tlatthtqqe atlqslmqqn
      241 qaqlvvaeqq rdareqqlap gydgsesvag kvahpkalga vqyalnqrgk pyewaaegph
      301 rfdcsglmwa ayrsvghtln rvandqyygt rhkpvartal lpgdmlffss ssrwqdihhv
      361 gmyigdgkmv hspttgdvvk vstvwwsrff aatrvfdavp apnkpptsps ptprpttptp
      421 spttptprpt tptpspttpt prpttptpgp ttgspspdpt psattpgptt hpeptvsast
      481 sasasasast sastgqsasa tpsggspsgg sptpgstsgh
//
LOCUS       WP_357519632             236 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357519632
VERSION     WP_357519632.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 236)
  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..236
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..236
                     /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=24899
     Region          9..231
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtlsstgsra garqtlvrqv idqlneqvts gawplgskip tepqlvaslg vgrntvreav
       61 ralvhagvle crqgsgtyvt stdelsgvva rrlapteape vvratravea vevrrafeve
      121 aarlaalrrt pedlaaldaa laareaawes grlavfvaad aelhttivaa ahnsmladly
      181 asfgtamrat lteaigpelh pdryvdhsal veairagdte ratreagafl etplra
//
LOCUS       WP_357519644             183 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Polymorphospora rubra].
ACCESSION   WP_357519644
VERSION     WP_357519644.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 183)
  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 183)
  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..183
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..183
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19550
     Region          40..178
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mtvllallaa valagctsgg weqdcdttpd gviecapdnr paapdvagel ltggrydltq
       61 drgqvvvvnf wgswcapcra eaadleatyq atkdsgvrfl ginvqdardk aiafeegrvs
      121 ypslfdpasr lalefevlpp ntvpatvvld rdgriavvir kavrqetlep ivariaaerp
      181 qdr
//
LOCUS       WP_357519699             712 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Polymorphospora rubra].
ACCESSION   WP_357519699
VERSION     WP_357519699.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=77223
     Region          32..700
                     /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 mhgtesdqat agpelsdlte rwvsavrasg ylapdgdrlr vflrelvrrm sealetpadh
       61 erighdvgva lvraglvape vlrdsittls rlpadagvsg plvgvrlgel lgglsagfca
      121 aerertlmgq eriraaalaa vdtaeharrd searlravfs aagtaiaiad lsgrlveanp
      181 avslmlgipa adlvgrrvld ffhpddvpsi rheiverllg pggglvrlek rfvdatgttg
      241 wltlsvslvh gddgrpaylv amaddvtdrh rlqtelhhqa hhdpltglpn rtllyrwlrd
      301 tiasatpdrr igvcfldldd fkiindtlgh gigdqllvav aarlhqrvtd aghvmarvgg
      361 defvvllrdt dgpeqvttla eqlldvldtp vevdgnrlsv sasigvlerp aygedfqevl
      421 raadatlyla kadgrgrwal fdpdrnaaqm rrydlagrlp ealrrdefql eyqpivsltd
      481 hglrgaeall rwhhpelgrl spntfipvae qsgvivalgr wvlrqacada arwqhdgqpl
      541 fvsvnvsmrq ftepdladev aralrdsglp pqalqleite savmqsydrp vatlqaiadm
      601 gvrividdfg tgysnlahlr hlpvhglkla gafmagmrlp tpdrvdeqiv etvvrlahml
      661 gmsvtaegve taeqaerlat lgsdlaqgwh fgpagpsehi gthprhvahp an
//
LOCUS       WP_357519533             374 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora rubra].
ACCESSION   WP_357519533
VERSION     WP_357519533.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 374)
  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 374)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 374)
  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..374
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..374
                     /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=38222
     Region          <175..372
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtadprrggl rllgdvalal avvvvlwlpa lasadgarrw vgvglavvvv agtaarwrlp
       61 lagapvvava tllaavlgvt gdpfvaaawa lypaavrwgs rspwfpvalf vavvagttmv
      121 gapataaale tvryvtvsva llagswivgs mvgrqaraaa etararaerr aaehrlrvar
      181 emhdvvahtl gtigieagva rhvtatspee mrrtltsies sarhaleqvq gllrtlrdee
      241 dadrtpapgl adlpglaera tragspttvt vtgtpalgaa geltvyrivq eavtngvrha
      301 pgaacrvevr ggptatvvtv rdtgpgrpag saegnglagi reraslaggg vefgnhpdgg
      361 fqvrvtipta grdd
//
LOCUS       WP_357519821             419 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polymorphospora rubra].
ACCESSION   WP_357519821
VERSION     WP_357519821.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..419
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45262
     Region          4..410
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mderaagave avfreergrl laslvhrfgd ldlaedvase aieaalehwp rrgvparpga
       61 wllttarrra vdrlrrdqay aariallqae agragpaapp dpdgdlpder lslfftcahp
      121 alpaedrgal tlrclaglat pevaraylvp vptmaqrivr akkkirdari pfrvpgpdel
      181 pqrlpgvlqv vysiftegya asagphlqrl dlaeeairla rilrrllpae revtgllalm
      241 llvharrdar tgpdggivll ddqdrgrwdr amieegrqlv vtaltggppg pygvqaaiaa
      301 lhdeaadvat tdwpqvvaly dvlvvltpsp vvalnraaav amrdgpaagl alldeladep
      361 rlrayhpfpa aradllsrlg rfaeaaaayr qaldlvgtep eraylrrrle saelsasdg
//
LOCUS       WP_357519827             117 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor
            [Polymorphospora].
ACCESSION   WP_357519827
VERSION     WP_357519827.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     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=12584
     Region          6..105
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mtvaqptgdq lvemlaalan plrlrimakl aggrdyvshl areigisrpl lhmhlqrlet
       61 aglivgslel sedgkamkyy qvaefdvhlt astlveaaet ltrsdpvpgp apketpr
//
LOCUS       WP_357519863             566 aa            linear   BCT 28-DEC-2024
DEFINITION  murein biosynthesis integral membrane protein MurJ [Polymorphospora
            rubra].
ACCESSION   WP_357519863
VERSION     WP_357519863.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Kuk,A.C.Y., Hao,A. and Lee,S.Y.
  TITLE     Structure and Mechanism of the Lipid Flippase MurJ
  JOURNAL   Annu Rev Biochem 91, 705-729 (2022)
   PUBMED   35320686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     gene            1..566
                     /gene="murJ"
     Protein         1..566
                     /product="murein biosynthesis integral membrane protein
                     MurJ"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=56211
     Region          19..>406
                     /region_name="MurJ"
                     /note="Lipid II flippase MurJ/MviN (peptidoglycan
                     biosynthesis) [Cell wall/membrane/envelope biogenesis];
                     COG0728"
                     /db_xref="CDD:440492"
ORIGIN      
        1 mgtpgtvtga griagaaali avltvasrla gfartgvftw vvgdtdlggv yviantvpni
       61 ifeivaggal aslvvpllag aiaagdrgav aattgalltw tvtllvplav vvavfagpiv
      121 aaianeptpa evavgarmlr ifapqlplyg igivltgvlq ahrrfawpvi apllssvtvm
      181 taylvfagtq grgvdiagvd lagelilavg ttagvvvlsl slliplralr lrptptyafd
      241 adarrrvggl avagavtvag qqvallvsln lvsggatgva avvpynlaqt iyllpwavla
      301 vplavaaypa latahstgdd dgyratlapt vrrvlllsal gaaalaavar pvaqffftgv
      361 aaeqtaagiv gfapgllgyg lfavlsraly argdtraaaa atglgwlavp aaavllaavv
      421 pddqrvpavt gansvgmlvl gavlvvavar ragpgsvagl praagvalla gglaalagtv
      481 lvnwlagagp slwpaadagg dtptqtvall qgmlagavva lvfagvaypl drhdlrpmva
      541 avgrrlrggr rdgpdrhdda egtdpr
//
LOCUS       WP_357519873             150 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Polymorphospora
            rubra].
ACCESSION   WP_357519873
VERSION     WP_357519873.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..150
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16547
     Region          27..126
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 matrntgvrt tldshrlpip vpideyeccp vtdvlrrvsd kwtlllitll grqpyrfnel
       61 hravegisqr mltrtlrvle sdglverevf ptsppsveyr ltplgaslle plsalanwav
      121 dhhaeiaasr tgtgyprqag rppagfppsp
//
LOCUS       WP_357519937             587 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Polymorphospora rubra].
ACCESSION   WP_357519937
VERSION     WP_357519937.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 587)
  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 587)
  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 587)
  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 587)
  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 587)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..587
                     /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=62274
     Region          24..535
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mdgppyrnpr lpvavrvedl lhrmtlpeka gllfhtmvgi gpagslapdd pdagllsaae
       61 mvrgrrmnhf nllgtagpad larwhnrlqe laastrlgip vtvssdprha ysanpntaal
      121 agafsvwpep lgmaatrdaa lvrgwadvvr qeyaavgirv alhpqadlat eprwprtlgt
      181 fgedaglaae lvrayvgglq gpvlgpagva amvkhfpggg athdgedphf rygreqvypg
      241 grfadhlrpf vaaldagcsq vmlgygmprd tgyeevgfsf nrdvvggllr rrmgfggivc
      301 tdwgvltgaa frgqvrpara wglerlspar rarrvldaga dqiggeavpg lvvdlvrtgq
      361 vgvgrldasv rrvlrekftl glfdrpyvdp draagvvgca rfraaglaaq racvtllsna
      421 apdrpahlpl rpglriwcdg mdpavvardg rvvarpadad vailrlqapy dhrpgqfeaf
      481 fhagslefaa getarvlaia aavptvvdvy ldrpavlprl aagvdallvs fgvgdealmd
      541 vlagraaprg rlpfdlprss aavragrpdv afdtadpvfr fghglty
//
LOCUS       WP_357520005             104 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357520005
VERSION     WP_357520005.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   Wintjens,R. and Rooman,M.
  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 104)
  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..104
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..104
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11648
     Region          38..93
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(39,43,68)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(42,67)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(49..50,61,64,68..69)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mtefhdwedi raelddgnsd aldterarte awvsafhlae erkrlgltqr evaelmgvtp
       61 grvsqiengd ldanevatlg ryaralgarm riifdygndl rqia
//
LOCUS       WP_357520012             459 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357520012
VERSION     WP_357520012.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..459
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..459
                     /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=49640
     Region          13..400
                     /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 mtdgqnpfsr qervvvigag lsgslaavyl arhgylvdvy errpdprtap aglggrsinl
       61 glsargmral devglladvl krsvpmrgrv vhspdgavrf qpygvrehei lhsvlrdeli
      121 allvdaaets agvrfhfgwr lnrldrdtat vevlpeaggd pvevgadlvv gadgihsvvr
      181 qhlqrglrad ysqeflewgy keltipvgdd geprvrleal hvwpgesamm vahpnvdgsl
      241 tcslfmpheg pvsfatldtp eavlgffran fadaeelmpn lveeiaghpv ghlvtvrtap
      301 wrhgdrvvli gdaahavvpf ygqgmnsafe dclvlsdcla rhtdraaala afeaarkpht
      361 dvladlsian fvdlrdrvhk pgytahavad rllsrllpdr wtplytmvah tttpyadala
      421 rakrqdrilr gataaagala algavttiga alrrrsrgr
//
LOCUS       WP_357520099             220 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357520099
VERSION     WP_357520099.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 220)
  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 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   3  (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   4  (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 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=22815
     Region          63..220
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          159..214
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msdvpggapv vaairsrdpi sqagvtaqla stapddtgpp vvvvteqdvp phvlvivgdt
       61 vddwllaqld alaggagpvp rpvlvvghld dtaglravea gglslvrrse stapllrevv
      121 rsaargearl ppdllssllt qvgrtqrdvl aprgltilsl sprqlavlrm iaagadvati
      181 arelsysers ikhivheitt rlgvrnrtqa vahairagli
//
LOCUS       WP_357520141             916 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357520141
VERSION     WP_357520141.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 916)
  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 916)
  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 916)
  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 916)
  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..916
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..916
                     /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=98895
     Region          13..224
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          110..913
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          743..773
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          784..812
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          817..853
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkqrlllvtl llrpneivgt nelaamlwgd dqpasaaanl rtyvrglrqs lgggaswegi
       61 taaaggyllr vepgerdldl fdaaaargrd alaasnanra eselsaalgl wrgdplsdlp
      121 lppalarrva qveerrllae edyagallal gapadvihrl ralldrhplr qrawgqlmvg
      181 lyrigdvaga ldtfrqarqv laeetgldpa peltqlyddi lhhrpelaac pppgpdgpap
      241 etppgpliqr peqlpravpe fvgredelas ldalldsraq gpttvviavv sgmagvgkta
      301 lalhwahraa drfpdgqlyv nlrgydeagv vsppdalsgf lealgvphar ipsdleartg
      361 lyrsllasrr mlvvldnard saqvrallpg aggcmvvvts rdrlggliaa esaapltlsv
      421 ltaeestsll asrlgagrla sepaavadiv eatgrlplal sivaarvath ptfpldaiaa
      481 elhsaearld aladgdvrrv fswsylalgq daarlfallg lhpgpdltpa aaaalaqvsa
      541 advtprlrel trlhllaeht pgryafhdll rvyaaelaes peradeheaa rarlydhylh
      601 daypaalllq pqwppiepvp plpvparrpv tdhdgalawf taehrvliqv vqqaaetgfe
      661 ayawqiawal ntflaprglw qdqlatqlva laaaekiddl agqaaanrll araltrlgdh
      721 dtaehrlkra lelherlgds tgqaqtlhny celcyldgrl dealehgrea lrlyrlvgnr
      781 sgeartlnai gwllattgdy vqaiesctea laqqrrsgdr ngqaatldsl gfaydrlgdr
      841 draadcyeqa iqlfrdsvdr yheaetlirl gdtrdgmgdr aaasaawrqa vriyedvgdp
      901 aaeetrrrle ryeseg
//
LOCUS       WP_357520188             215 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357520188
VERSION     WP_357520188.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 215)
  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..215
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..215
                     /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=23796
     Region          22..183
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matlhtprrr pgrprrddrr dtaqtilrva talfarhgfd avgvrhvaaa agvdvstvhh
       61 htggkadlye acfarvfeae rramepalar arerldagge glldalhdvl dafvdfltgq
      121 pettglwlrr wleperhrgl deryslplye averlladad aagvlrephp rtavrslvws
      181 vhahvvavlg gqagpaadge lrtfvhrwld rmygt
//
LOCUS       WP_357520213             387 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Polymorphospora rubra].
ACCESSION   WP_357520213
VERSION     WP_357520213.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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..387
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..387
                     /product="LolA family protein"
                     /calculated_mol_wt=40021
     Region          44..265
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mslfqsrpal rwlvptsaav vvlgggaaig tlaaasepnl pprdaaqllv dlqtarldgl
       61 sgtvvqradl glppaletla gnsgselaal atgrhtlrvw yngpdqarva lvgtlgetdv
      121 irngadawvw ssqkkeavhy kldpgkedap pelpgglpat peeaadkala aidpttevrv
      181 grsatiagrd ayelilaprd kaslveeiri aidaeekvpl rfeifaegvg epafevaftq
      241 vdfnrpapeq fvfnpppgtk vteggaegag pdggpfgghr pdgeaaepga apeqrpetrt
      301 vgtgwttvlv gtlpesapga paaggepgtd vaqfagllnq fpavsgdwgs grllsthlfs
      361 vlltddgrvi gglvtperly evaaqtr
//
LOCUS       WP_357520244             476 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora rubra].
ACCESSION   WP_357520244
VERSION     WP_357520244.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=50527
     Region          114..449
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mvigvaglav glvlggialv gtlafalqrs adnearriae avamlvteda lpdplpvvgs
       61 tvrvqvvdpq rrvrsasida drlvpmlfgd eldralddgp vfipgdrlgl rgpvrvvavr
      121 agpaddpqtv lvgksmadva hsvdllktsl ligfplllal lavvawrvig atlrpvealr
      181 agaeeitgga rpgqlpvpes hdeihrlavt lngmldrles argrqrafva daahelrspl
      241 anmrtqleva qrlgprndwp avaddlladt erlsrlvndl lllarvddag prpakvgrve
      301 lgeliagaag rhpsppvrve asdtalwtfg dpdalgrvva nlvdnavrha rgevvvsaya
      361 eppyqvvsvt ddgpgipaad rdrvfdrftr lddarardag gaglglaivr elvrqhggtv
      421 rlddarpdpa epatnpglrv evrlpaapad rqprfvqdrq prsvqagser ptrsve
//
LOCUS       WP_357520227             372 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357520227
VERSION     WP_357520227.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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..372
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..372
                     /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=38718
     Region          7..346
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgdphlvgiv glgvisrayl dtlanhpavr vaaladldas raaeaaalip gaealsverl
       61 lahpdvrtvl nltipaahad islatidagk nvyvekplav tfpegrtiie raasagvrvg
      121 capdtvlgtg tqtaraaidg gligrpmsas avmvtagher whpnpdfyya pgggplldmg
      181 pyyisalihl lgpvravlga asrlraervi gsgprtgqri pvevdthvtg vlehangals
      241 tittsfdgvt taaapievrg etgtlavpdp nhfdgevrlf alggtewrvl epqagyaess
      301 rgiglidfvr adaqrpprag gdlalhvlet mttllqsaae grrielttgv rrptpvpltp
      361 aeewkaydah gh
//
LOCUS       WP_357520259             820 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357520259
VERSION     WP_357520259.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 820)
  AUTHORS   ter Beek,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 820)
  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 820)
  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..820
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..820
                     /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=82884
     Region          129..812
                     /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          140..379
                     /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 mtlalatvra rwasflgsfv alglgvavla stllvlvaaq pgvpdryaga qvlvraapag
       61 adpeafpefl pwsradadtv tgrlaalpgv etavpdlsfy aqlvrdgrpv gapsegqhng
      121 hawsaaalap ypivagrapa adgevaldrd lghapgervt lltaagpvpl tvtgtvdgpg
      181 fhvadptatr laggvtvigl rlspgadpdt vaaaardvvg dradvyagaa rtalepefeg
      241 rtrwigaqll iamaslagfv tifvvastfg fgiaqrrrel gllravgatp gqvrrivyge
      301 avvvgllaag ggavlgaafg pvlgdlmvev glqpagftvs pdplvllgvv algltvallg
      361 vwsasrragr vrplealrea avdrrpmtpa rwifgvlgta ggltvvasap vldpevlvnl
      421 miyavmsliv glfllapvii ppvvrlvtrp argatgelvr egalvavrrv astaapvlvt
      481 vgfavfltgl feiqshafgt qraervpadv vvspdgvpgl sdavaaavaa gggtsaaelp
      541 trifvtgpag aarpveasgv epaalaaasv tvssgslddl sapdalvatv gtaqrhgwql
      601 ggtarvvlad getatlrvva laddhdlpap vlinratara hdpsaltpvl yaagiapdrv
      661 gaeglgglag tpaeyahrad aeedrlvrlf llvllglsag ytgiaiantl lmattarrrd
      721 favlrlagat pgqvtrtvaa ettltvtiga vlgglvafaa lvglrngyte llgspvdlvv
      781 pwstvlalvg vcyllallas vlpahrlaaa pptalvadrd
//
LOCUS       WP_357520265             286 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357520265
VERSION     WP_357520265.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   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 286)
  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..286
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..286
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31292
     Region          14..277
                     /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 mpyvtvgten sapidlyyed hgsgqpvvli hgfplssaaw ekqvpallma gyrtiaydrr
       61 gfgqsarptt gydydtfasd lnmlineldl sdvvlighsm gtgevtrylg tygsqrisra
      121 vlvstippyl lktsdnpegv dkavfdgfqq aivadryayq tsflndffny dqtrgkqvse
      181 eayranwnla vsaspigtye cvsswltdfr advaridvpt liihgdadrv lpypvtaprl
      241 namlpdselv tlpgaphaip wthadevnna imqfigagap amsrkk
//
LOCUS       WP_357520283             771 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357520283
VERSION     WP_357520283.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 771)
  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..771
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..771
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81903
     Region          4..766
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          563..591
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          603..637
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          643..671
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(644,647..648,651..652,654,684,687..688,691..692,
                     694..695,724,727..728,731..732,735)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          682..712
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          723..751
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mggraldatg aqtlddlagl lralrrrhar qlgggeltyr elaartgwsh taiaeyltgk
       61 tlpptdrldd larllgatpa eqgalatard ridesrrraa rapdrlaprq lpadvarlag
      121 rddelarldk lataptavvv aaisgtagvg ktalavhwah rvaerfddgq lyvnlrgfdp
      181 ggqalsaata lrgfldalav paarvpaeld aqaalyrsvl agrrilivld nardaeqvrp
      241 llpgapgtlv lvtsrnqlts lvsldgahpl plglltrqaa ndlltnrlga qrvaaepeaa
      301 eaiitacarl plalsiaaar aqqsgfplat lagelgtagq rfgvldagda vgevravfsw
      361 sytsltapaa glfrllglhp gpditvpaaa slagltaaaa rrllteltra nllteyrpgr
      421 ftahdllray ateladdtdp esdrraattr lldhytdtah aadellrpna dpvdhlraap
      481 vagvlsdrpt thaealawlt aehpvllavl rqaagagfdv hvwrlgrald tfldrqghwh
      541 drvescraal laaerlgdgv aqavahrfla gahtvvghya dahdhleral alyvlggdte
      601 gearthqnla alwdrqgepr kalahsmrtl tlaraaghdr aqadalnavg wchaqlgehs
      661 salayceqal qllqqlgdha geaatwdslg fahhhlgqyd qavhcyertl eltrdlgdrw
      721 geadtlsrlg dtraalgdpt saradwqlal diltalnhpd aaavraklvl p
//
LOCUS       WP_357520298             193 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357520298
VERSION     WP_357520298.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 193)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..193
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..193
                     /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=20389
     Region          4..185
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mnsgrrprdp qgrrqailda alelvievgi artshraiae ragvplgstt yyfptlpdlv
       61 aaaleqaaer vrreirdlag kigdgrdlvg aliwmtglav gdrqrmlley elylaavrnd
      121 elrglaglwl relrtlltpl igagpaaavg alldgvilqa mvtgeapdpd vleaaltalv
      181 grpagkspgv vte
//
LOCUS       WP_357520291             456 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357520291
VERSION     WP_357520291.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 456)
  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..456
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=48146
     Region          186..435
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtgravvirl wshirslarp vgqlpqlsrr gqlfdallal glgllaiqag tgdadlprpy
       61 rvevdrgelw rgppvppdpv wppflpvedd gtgwtaalll lvvlplvfrr ryplgtlwvv
      121 lasaglvdgn paalrlsffa cvvagysaav fspykilala slpaaailha glqsdassvs
      181 dsavpflill piavaadglr rwkehadegr armvameheq vealrratev erariarelh
      241 dvvthnvsvm viqagaarkv mesrpedara allaveaggr aamtelrhvm glltmdddvl
      301 gqeggsdlvp qpgldgldal vqrvrdsgvt velvvrgqrg plpsgieltv yrlvqealtn
      361 avkhaasasv rvlveyggeh lrvevtdtgg ragvttgtgr gliglrerla vyggtlaagp
      421 rltggyrvqa lipmenvvvd gvagdgrtga plggea
//
LOCUS       WP_357520344             292 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357520344
VERSION     WP_357520344.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 292)
  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..292
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..292
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=30369
     Region          6..264
                     /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 mspgeawrrr arvalgavga lavgvllweg ykavgdpdgt vvagvrilpr addsamphvv
       61 dilgrfadpe laggdpiglv vlsaclftlr svavgfglga avglllavlm qrlrvvergl
      121 lpyvvlsqtv plialapvia gwggglslgp ypwqpwmsva tiasylaffp vavgmlrglq
      181 spapiaeelm hsyaagwwrt lvklrlpasm pylfpalrla gaaavvgavv geistgtrgg
      241 igrlvieysr eatsdpakvy tamigaallg lvvaavvgvl efllsrqrka yp
//
LOCUS       WP_357520399             609 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357520399
VERSION     WP_357520399.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 609)
  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 609)
  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..609
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..609
                     /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=64658
     Region          282..603
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msgdqvplrh slvtrllvaa vvialaaisa tawlaatttt rainyeqgga vadqkavyqa
       61 llgyaathhd wsgaaalvrs raaeldrrit lttddhrvil dsqtgpalrn tspaavvdpl
      121 qvdlgltggd ehideravgp yvvptedryv lsevaknsla cfhkvgydgv ievattgrps
      181 vvltnvraea erpltrsvte scgfaldslv saaekkalqt lttltahcln lgdrtselri
      241 tptfdaylge savvrtahek tevkppslle pagpvgvvrg cvesarrtql rpyvaprall
      301 fvtapgtgdt tlrlsggsig rivavtgavl latvaatvlv grrlvrplrt ltdaadqrtp
      361 apvsgrdeig rlaralndst qrrdraeaqr rtmvndvahe lrtplsnirt wleaaqddla
      421 ptdaqllall heealllqhi iddlgdlaaa dagtlridpe ptylrdvltq vvdshrgsal
      481 aagvrlelsv vsdpvvradq vrlrqvvgnl isnairytpp ggsvtvgadg ttisvrdtgs
      541 giapadlpki fdrfwrades rsrvtggsgl glaiarhlte ahggtievrs evgrgthfti
      601 rlpgptttr
//
LOCUS       WP_357520549             509 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357520549
VERSION     WP_357520549.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 509)
  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 509)
  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 509)
  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 509)
  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..509
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..509
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=54950
     Region          54..485
                     /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 mstrrrvlgw lgavgglvvl paagfagyly adsgrsnvgt ltfrnrlrip pilpptvaad
       61 gvrrfrltla agrtellpgt ttntwgangp ilgptlrasr gdrvsvdvrn nlpettslhw
      121 hgmhlparmd ggphqpiepg vtwrpswtie qraatlwyhp hlhrstaahv yrgvaglfiv
      181 dddpavrlpt eygvddvpli vqdrriaddg tldesdltfg gltitgllgd kilvngtydp
      241 yvevltervr lrllngcnar ilyvgftddr eftlvatdag llsspqplrr lllspgerae
      301 ivvefrages vvlrgfpapl ranplygrla ggsdthdlik mtaagvlrps ppvpaeltpa
      361 spaptvtrpe pfrlemgdfl lngatmdpar idrvtrtgsv evwevangqs iphnlhvhga
      421 sfhvlgvdga ppapesrgek dtvyvppgsv vrlavrflqh sdvrtpymfh chvlahedag
      481 mmgqfltvsa qdepsvpvtl daghaqhgg
//
LOCUS       WP_357520505             461 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357520505
VERSION     WP_357520505.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..461
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..461
                     /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=49130
     Region          2..360
                     /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 mtsrsrvavv gaglagclla cylarrghrv tvyerrpdpr ggtaergrsi nlalsergld
       61 alrridldkq vmadalpmrg rmihpvagpl dlqlysaggd rainsisrga lnnalldaae
      121 aadgveivfs hrlvgldpat gamtyqtpdg eahadadvvi gtdgagsavr gqllahdllt
      181 esldfldygy keltippvdg dfaldpgalh iwprgtsmmi alpnpdrsft ctlfwptggt
      241 gsfaslsspa aierhfathy pdlpplapnl vddyqhnpvg llgtvrcgpw hangrvallg
      301 daahaivpfy gqgancafed vvvldrcldd tgddwahalp lfeerrrddt eaiaqmalan
      361 fvemrdkvas pvfqygrkie halekalpgr yvsryemvsf sttpyaqvqr rvrtqhrvlg
      421 aagagaaall igalgaavtk ravgaggtsr rrrpgtgege a
//
LOCUS       WP_357520514             290 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357520514
VERSION     WP_357520514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..290
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31773
     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          99..280
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgdatgstvp rrqlgralrd lraeagmtld avaealecsr qkmwrvesgl gpvrgidvra
       61 mcelygarpe ltaalvalag etrakgwwha ygdpvpdwfd lhgglesaac rlrehagvqv
      121 pvllqtrgya seacrrrpge ererlvearl rrqgllrrrl prpprfevil ceavllrevg
      181 gaatmaeqlr hlaeasrlph vsirvlplaa gahdgvlags fvlldfplgl rvdpdppvvy
      241 qesltgalyl drpaevtaye qvwagldala lseeesrrli vkigeevhhg
//
LOCUS       WP_357520592             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357520592
VERSION     WP_357520592.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32471
     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          99..287
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpddigstvp rrqlgrllrq frneagvtld aaaealeysr qkiwrlecgq gsvrvldvka
       61 mcelygvspe maeamrglav etkskgwwha ygdavpnwfe lyvglesaaa rlreygetli
      121 pgllqtrsya lglfqpgsrl speereqave vrlqrqallr rrlpkpprld avlseaalrr
      181 vvgshgvmsd qlkhllevse qpnvsvqvvp laagphpgav agsfvildfp ttnggrtape
      241 psvvyseslt galyldkpde lmayedtwrg laalsldaae srdmikriig emrhd
//
LOCUS       WP_357520624             391 aa            linear   BCT 28-DEC-2024
DEFINITION  lactonase family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357520624
VERSION     WP_357520624.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..391
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..391
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40501
     Region          52..370
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mkrsvalaaa llagltsvgs vpgtaladgg gpgyhddrkg gdnhhgddeg avfvqtnkae
       61 gntikvydrd edgrltkage yetgglggft igapldalas qgsliyhkgl lfavnagsnt
      121 vtvfgvegtk lhklqviwsg gllpvsiaar gdlvyvlnag gegsvqgfev rkghlsried
      181 anrslglhng nppafgtapa qvkidpdsef vlvstkganv mfsyeigrhg elasnpvisd
      241 agntpfgftf dsedsllvte sganavsrfe leddgtldqv gesvpngqla pcwiqrvgdy
      301 ffvanagsst issyrvnddg kleivknvaa dtnggsidmt aedgflyvqn atagnvqgye
      361 vnkdgslrlv ttveglpkfe ngigmegiaa s
//
LOCUS       WP_357520641             939 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357520641
VERSION     WP_357520641.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 939)
  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 939)
  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 939)
  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 939)
  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..939
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..939
                     /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=101894
     Region          2..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          119..924
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          763..787
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          799..827
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(800,803..804,807..808,810,840,843..844,847..848,
                     850..851,880,883..884,887..888,891)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          832..868
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          879..907
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mavefgllge iqahldgral plgalrqrav laalltdanq lvsveslvvr vwgeeppdgv
       61 rdtlysylsr lrqaltaapg aeiarrsggy vlavdeqsvd lhrfhclvdq arstgdqdra
      121 ltlfaralgl wrgeafarld spwfngvrdg ldrqrleaes dhadlmlllg rhhelladlp
      181 araaarplde riagqfmlsl yrrgrpaeal ehyerirlrl adelgadpsp plrhlhqril
      241 aadptlaape qahrqapsvv prqlpappgl ftaraeelay ltaaaaager settvvisai
      301 ggsggigkts lalrwahthi arftdgqlya dlrgfgpgfg pvspstvirg flealgvapn
      361 aipvdpdtqa alyrslvagr rmlivldnar danqvvpllp gsptctvlvt srrelaalta
      421 thrarpiald vlspdesrel lighlgperv gaeapaistl vdqcaglpla lgivaaraaa
      481 rpqlplatla relqdasarl daldagelnv nlravfsssc aalpreaatv fallglvptd
      541 dislaavasl vggpasrare llrqleatyl vhqhvpgrfr mhdlvrlhaa eqatetleaa
      601 tcdgalrrlv dfylhtacaa drlldpwrpp itigrpapgc tperlcdvpd smawfdrehp
      661 hllsvlkvsv rhgwhrqvwq varalatfha rrgrlrdqlt vwqagvaaad aegdpavqam
      721 ahrflgqaih wlgdigatva rfqvamayae qagdlaeggr idfalgvtws vegdhhlslt
      781 hnrlaletfr slgdpveear slngvgwala hlgrydeart aceeavelyr rhrhpdaaad
      841 alhslgyidh qtkrhaesla hyqqarqvya dvgstrgevd cltslgelyt smdkraeaqq
      901 awqeavdllh vqrrteeaal lrarmsvlpa pvrphepvs
//
LOCUS       WP_357520673             408 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049171].
ACCESSION   WP_357520673
VERSION     WP_357520673.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..408
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43398
     Region          3..408
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mgtadveavw rvesarivaa ltrftgdfel aedaaqeava ealvswpras panpagwlma
       61 tarrraidai rrrvalhdry allaadpavh svldrdvdld ridddvlalm fvschpvlsp
      121 qgrvaltlrv vgglsseeva raflvpvptv qaritrakkt iaaagvpfel ppagerrdrl
      181 agvlsvlyvi faegstatsg drllrpdvay eavrltrtla alqpdepevh gllalcelta
      241 arfpartgpd gapvlladqd rrlwdssair rgltalsras arglgpyglq aaiaathasa
      301 psvtetdwdr ivvlyealgr atpspvveln ravavamasg paralaivde liaanrlpgs
      361 hlvptvrgel ltrlgrrtea rtelelaarl canqreravl lgkaaals
//
LOCUS       WP_357520696             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            sp. NPDC049171].
ACCESSION   WP_357520696
VERSION     WP_357520696.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..416
                     /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=44448
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..371
                     /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"
ORIGIN      
        1 mveeltqagd avaacvddas walaedelia aldaahrleq rlaavklalv reidgrgtar
       61 aqgasstavw lrerlhltis tarrlvdlaa aldagnpgir aalangditv dqarviadtv
      121 atvhtaadaq aadkavgvlv gwagqfdpal lrklgtrild hvapdiadaa aqaaleaear
      181 rasrdrhltl saltdgrlrl tgildtetag llraaidpls apsgpddqrs pgqrrhdalg
      241 dvcrlalrtd elpehggdaa qivvitsydg ltrqlgsgtl dtglhltpet vrrlacdaai
      301 lpavlgsasq pldlarqrrl itgplrralv lrdrgcafpg cdrpprwcda hhihhwadgg
      361 tttltnavll cghhhrhlhh sdwtvrlggd ghpefvppaw ldpdqlprrn hyhrrt
//
LOCUS       WP_357520700             307 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049171].
ACCESSION   WP_357520700
VERSION     WP_357520700.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 307)
  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..307
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..307
                     /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=33090
     Region          26..172
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtqgdmelvl laqagdaaal gallarheae mravalgvlg ygpdaedavq damvvalrri
       61 gevrdpaavg pwlraivrnn srmtvrghra vpvaepewfa gpadtptpee aldraamrdw
      121 vwhaigqlse pdrlvtllry fsdassyeqi aavcgvpvgt vrsrlsharr altgglraaa
      181 gaahtdvtat naarwregrd miatamagdf drvvreswwp daemivpggp rggrdlavag
      241 mdhdltagvr qrlrnvvasg dvliwetdli sppddpehcp paalwlqvlr egrvrqltlf
      301 hpvpalr
//
LOCUS       WP_357520727             411 aa            linear   BCT 28-DEC-2024
DEFINITION  YeiH family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357520727
VERSION     WP_357520727.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..411
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..411
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42850
     Region          56..394
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 matdetrtad paataveprt tdgtrtpdgt adpapvsgpp ttvdqagptg tardgrfwaw
       61 tllglvivvg lgaltryleq nvpgwaegta vedigaaiey pvyaillgll gnvavtllgw
      121 rdriaaafrt effiktglvl lgasinlavi asaagpavaq aillisgvff ftwwlagkfg
      181 lddklralla savsicgvsa aiaaagavra rreqlaytas lviifalpsi filpwladvf
      241 glsdavagaw iggnidttaa vtaagaiage ealqiasivk vtqnalmgvv avaltayftl
      301 rverrpgaer pglrelwirf pkfvlgfiaa sviatwyldg agadgkatia ivndlrvwfl
      361 ilafvsigle vrvaslreag wrpvavfasa tvfnlalala lasllfrnfs v
//
LOCUS       WP_357520750             288 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357520750
VERSION     WP_357520750.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 288)
  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..288
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..288
                     /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=32893
     Region          6..250
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mslsprlrav sdlhiaypen rsfvqelhpd hdgdwllvag dvaeryadve walallstrf
       61 akvvwapgnh elwtppddpv qlrgraryqe lvrmcrqlgv vtpedpypvw dgvggpatva
      121 plfvlydytf rvpaartkqe sldlaykagv vcsdesmlhp dpypsreawc dariteterr
      181 lserdpalpt vlvnhyplvr eptdvlwype faqwcgtvrt rdwhlrfgaa tmvyghlhip
      241 rttfhdgvrf eevslgypre wrrrgsvpdp vrtidpaedl rrrasvtg
//
LOCUS       WP_357520877             302 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357520877
VERSION     WP_357520877.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   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 302)
  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..302
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..302
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32293
     Region          5..286
                     /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 mltgeekfvr sgqvrlwter fgrpddptvl lvmgtstqgi gwpddlveal vnsgrqvirf
       61 dhrdtgrsds vdftthpyal admaadtaav ldghgvpaah ivgsslgaai gqwlavhqav
      121 rvrtltalas spmgnnpgpa waramagqpa aadelpppta rflnhvmdsv kaprttaqqr
      181 mdadvqtwrv lsgdvlpfde aaarlfvehc yarahnvaaa anhdlagrrw dddrraslsr
      241 itaatlvlhg sddplfpqah gealaaqipt aqlevvpgmg hhpffspglt eriagsiirh
      301 tt
//
LOCUS       WP_357520818             327 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357520818
VERSION     WP_357520818.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 327)
  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..327
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..327
                     /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=34114
     Region          30..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(41,43..44,47,129,133,153..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 mireayacwv repgaaeirp vslptpgped vlvrarysgv srgtetlvfa gqvppdqyaa
       61 mrapfqegdf pgpvkygyls vgeveqgppe llgrtvfclh phqsayvvpa tavvpvpdgv
      121 pparavlagt vetainalwd aaplvgdrvt vigagmvgcc vaallarfpg vhvelvdids
      181 rragvagalg vgfappadas gdrdlvvhas atgaglqqal dllapegtvi elswygdrpv
      241 qvslggafhs grltvrssqv gmvaparrgr rsyrdrlala ldllddpafd alitgasrfa
      301 elpdvlarls tgdlpalchl ityddge
//
LOCUS       WP_357520976             376 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357520976
VERSION     WP_357520976.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..376
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39369
     Region          3..356
                     /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 mtaarggpla gvrvvelasl apapfgcmvl adlgadvvrv drpggpgagr laaptggplq
       61 rgrrvtaldl kspagvadll rlaeradvlv eayrpgvaer lgfgpevcqa rnprlvyarm
      121 tgwgqdgpla araghdidyi avagaleplg rvgerpyppm nlladfaggg mllavgvlaa
      181 llerersgvg qvidaamvdg salltaflhg llgsglwsap rgrnlfdgga pfydtyatad
      241 ggfmavgave pvfyavllsg ldladdpdlp aqydpsgwde lrrrfterfa ertrdewtav
      301 ftdldacvap vlapgaahqh phnaargtfv evggeiqpap aprfdrtpad rptpapdper
      361 dvqpaaaild swprrt
//
LOCUS       WP_357521007             431 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357521007
VERSION     WP_357521007.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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 431)
  AUTHORS   ter Beek,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..431
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..431
                     /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=46353
     Region          29..381
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msdfdpgrrr flghlglagl galgassfls acassasgpt asggsgavti qsnlsspqak
       61 aameklietf naqgkgtasl ntiasetfrt qlptyltsan ppdlytwyag svandyaskn
      121 llldvsdvwk slgdypqslr tlstdasgkq vfvpmnnyww gffyrksnfa kwgvrepktw
      181 teflavcetl kskgvppigi glgdtpwvas awfdylniri ngapfhrell agkqrfddpk
      241 vkavltrwre alpyfdpkgk aypfqeatta llagktgmfl igtffadaap kdalgdldff
      301 rfpiidpavp laeeaptdgf fasaktanpt gtkallsyls gveaqeayvk assgivlpan
      361 pkakasdspl vakgkamlde akeltqffnr dssdalqpta dtaltkfidk pdqidailre
      421 wqagaekvfk g
//
LOCUS       WP_357521009             305 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357521009
VERSION     WP_357521009.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 305)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..305
                     /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=33556
     Region          8..304
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtatisptsv tptrrrrrsa rlspllvafv lvpfavesiw vfwpalqgfw fsltrwdgms
       61 sptfvgtdny velagdatfr galvntviwl vlfgglsvlg gfgmalvlqk errgvgfyra
      121 alftpvvfsl vvtalvwrvf yqpdgiadti lravglesli rpwladpqta lyavilpalw
      181 rqigyvmvlf laglkaidpa lheaarmdga nawqrlrhvt ipqlkavnav vlsvividsl
      241 rsfdivwslt kggpyhssel lstymystaf qslrlgyasa iavvifvlal avilgylvra
      301 freea
//
LOCUS       WP_357521050             313 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357521050
VERSION     WP_357521050.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 313)
  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..313
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..313
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32755
     Region          19..298
                     /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 mpsavteptv tvvpaefsdg vpahvesigp pdapltvvll hgwtldgriw hrqraalrea
       61 lgdrvrtvty darghgrsgs aslssatlaq lgddlaalle rvaptgpvvl aghsmggmti
      121 meyahrhpea fadriagllf vsttaeghth tayglpavla rlvrlaetag aevlsrcgsc
      181 rpphllmqal rpslrwllfg adctdddvrl agsavsrarm caigglrpsi gaqhrldtla
      241 algdvpaaal vgdldrltpp pcaesiadal ptteltlcpg aghmlmlerp devntalltv
      301 ttralrsrla lta
//
LOCUS       WP_357521159             246 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Polymorphospora
            rubra].
ACCESSION   WP_357521159
VERSION     WP_357521159.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=26552
     Region          <40..>144
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mddpdgyfge dvaatyddpa semfraevvg atvdvladla gggralelai gtgrialpla
       61 drgvpvhgid msramvarlr akpggdavgv tigdfattrv dgtfsvaylv fntimnlttq
      121 eaqvacfrtv adhlepggcf vvevmvpdlr klpagqnvvp frtsatgway drydvatqem
      181 ssnyvevvdg rgsfwsvpfr yvwpaeldlm aqlaglrlre rwdgwgrepf tsesgqhvsv
      241 wekpaa
//
LOCUS       WP_357521193             309 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357521193
VERSION     WP_357521193.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   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 309)
  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..309
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..309
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32807
     Region          6..301
                     /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 mpdtivdsgp vpvtardlgg sghpllllhg aggnlaqmta laerlrpahr vvtvdlrghg
       61 rsgdgpwhwd dvltdlvgva dslgllrpav vghslggmla tlwahrhpdc pgavsldgnp
      121 tldrldqlsg mdpeqaagdl trlratfdam gamlaeplga dqvaaalagq ramaqrydad
      181 pdewaaafer nlvpyddgrs rlrpgpglta qlrvamssld llpayretrs plllvlated
      241 lpeqqpfhdl yaayrratae rlttvdnsal rvrhlagash amvaedpari aalvtdflae
      301 agqpkrplt
//
LOCUS       WP_357521216             277 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357521216
VERSION     WP_357521216.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   2  (residues 1 to 277)
  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..277
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..277
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29815
     Region          2..273
                     /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 mshvtaadga qiffkdwgag rpvvlshgwp lnsdsweaqa lfladngyrv vahdrrghgr
       61 stqtwhgnem dtyaddlatl idtldlraat lvgfstggge varyigrhgt arvaqavlvs
      121 avpplmlrtd dnpdgvpvev fdqiragsla drsqlyrnla dgpffgnnrp gatvsqgird
      181 afwsqgmqag hrnayeciaa fsatdfrpdl dafdvptlvi hgdddqvvpf evggrasaar
      241 iknaelrvyp gaphgitdth kerlgadlla fldtyaa
//
LOCUS       WP_357521218             275 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357521218
VERSION     WP_357521218.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 275)
  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..275
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..275
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28442
     Region          39..266
                     /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 mpasasrrsl lvgtalvaat alaatpaasa htgqqpqpkp tvvlvhgafa dasgwaevtr
       61 rlqrsghtvl apanplrsvd sdsaylasil qtipgpivlv ghsyggvvit naaagnpnvk
      121 alvyvaafap degetvyglq grfpgtklte ealdlrpypl pdggvsydgy vkpalfrdif
      181 agdlpaataa vmataqrpgd ahtlqqpsgv pawrsvpswy lvarndnlip aatqrfmaqr
      241 agartvevra shvamisqpd attdlikaaa raaar
//
LOCUS       WP_357521234             245 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357521234
VERSION     WP_357521234.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 245)
  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..245
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..245
                     /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=26417
     Region          16..236
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 maeasrdavr taapvlhdav ldalgleitg gqhapgtalt leqlqhrfgv srtvmreamr
       61 ileslnlvas rrrvglvvqp mhrwrvldpr virwrldgpg radqlrtltd lrvaveplaa
      121 agaarhatad drarlrtlat rmrqlgeage ldaflaadve fhalllqacl nemftaltgv
      181 iaevlagrte hglmpkcprp valdlhdeva ncvaagdawg aetamrelve evrdaisttp
      241 svgtv
//
LOCUS       WP_357521303             419 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora sp. NPDC049171].
ACCESSION   WP_357521303
VERSION     WP_357521303.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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 419)
  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 419)
  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 419)
  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..419
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..419
                     /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=41382
     Region          145..416
                     /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 mgpsagwpvp tagatgtaga spwwsdalad pwrdpaapaa vvvpgvvaag tepepvsdpd
       61 apgrpklrhl llipvltall agalggalgy afavrggvgg gvvlggapae vpalaqrkpe
      121 slagvaervl psvvtvrvss lggtsegsgf iatadghvit ndhvvaggsg kasvvfndgs
      181 tapativgqd pesdiavikv srtglrpvef gdsdslavgd pvlaigspls lantvtagiv
      241 savdrtmqag epggpmryya aiqtdaavnh gnsggplvdg agrvvgvnst ikslvaegqe
      301 agniglafai pinqakrvtq diigtgkarr tvigaraegp tgapggglrl aevepsgpad
      361 saglkvgdvi lkingrpmte ptdltalvrk fapgsvvsve frrgsarqnt svtltadak
//
LOCUS       WP_357521323             183 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357521323
VERSION     WP_357521323.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   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 183)
  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 183)
  AUTHORS   Rosinski,J.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..183
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..183
                     /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=19041
     Region          3..82
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          94..170
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(95,110,112,122,125,131,165,167)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mnasplatia valrrerdra glsltelarr agiakstlsq leagngnpsv etlwslgval
       61 gvpfsrlvep pspavrvvra gegpavrsdh adltatllaa gspharrdiy rlavepgsgr
      121 haqphipgsv ehillaagrl rtgpvsdpve lgpgdyatfa gdvphhyeal epgtfgilvm
      181 ehp
//
LOCUS       WP_357521333             498 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357521333
VERSION     WP_357521333.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   3  (residues 1 to 498)
  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 12993645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=49528
     Region          11..262
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <281..485
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mpsmgqlvgd ryrlvesias ggmgdvwrav detldrcvav ktlqarlvnd agfgerfrre
       61 aramaalrhp gvaqvydyge vsrpggpvla yivmecvqgq plseriaeag rlsvaetmsi
      121 aaqtaralqa ahdagvvhrd vkpnnliiep dghvvlvdfg vavtqeaasl tgtnqvvgta
      181 lymapeqisk neigppidiy algavvyhcl sgrpphqgen avavalrhle edpaplpdgt
      241 paavrglvat amakepaqrf ptaaamataa qaladpsdhl vrtaagatsi gardertaal
      301 rpghggapgr sgssgarala vllgtvaaaa avlvfgdptg mlpgptgrps tppavspsap
      361 vdggidtatd tdtatdtdtg tdtgidagpg vgggqpattg pgglpvrasg sptptasgpa
      421 agpdqsapsd dsggdtpapa tsesadedpt adptgaptaa pteesteepv adpsggpaee
      481 ssgeptagtt ggtaaprg
//
LOCUS       WP_357521355             393 aa            linear   BCT 28-DEC-2024
DEFINITION  NRAMP family divalent metal transporter [Polymorphospora rubra].
ACCESSION   WP_357521355
VERSION     WP_357521355.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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 393)
  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..393
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..393
                     /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=40084
     Region          3..388
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msgaadtdpt tvatlvvvga asgyglawlt llsipavavv qvlatrvgtl tgrnlqsavr
       61 dgygrlaggl llvsvltvnt vtvgadlaag aaaigllvgl esrwlvpvfa aavltllfvg
      121 rydevervlk wvmvgllayg aavvlarpdw aavargsflp plsitsthla gavailgtll
      181 ttymylwqtv eqveergart slrvrefdav agatlaclia wcilvasgat lgthhesvdt
      241 aqqaaqvlrp lagplaself avgllaaavv aapvimaagg yaaasafgwg rgltrsprqa
      301 pgfytlialq avvgavlamg tvspirllfv aslvagvatp fglvmlvlca gnaklvggrp
      361 iarglrvagw lvaagtaals lvfllqqlhv lrr
//
LOCUS       WP_357521421             166 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC049171].
ACCESSION   WP_357521421
VERSION     WP_357521421.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 166)
  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 166)
  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..166
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..166
                     /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=18403
     Region          23..151
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msaarspada srltflpadv itamqistih rrsqkifnea lrplgfeerh favlavldgr
       61 gpltqrqlah lldldksalg rivddlerqr lverravptd rrahtihltd lgrqrideaq
      121 riagnvgrql fahlapstrr afdqalrqll dgpevdpstp ategqp
//
LOCUS       WP_357521441             471 aa            linear   BCT 28-DEC-2024
DEFINITION  xylulokinase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357521441
VERSION     WP_357521441.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 471)
  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 471)
  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 471)
  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 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..471
                     /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=47636
     Region          3..431
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 mplvagvdss tqsckvvird aetgelvreg raphphgtav ppaaweasls dalaqaggld
       61 dvaalsvagq qqgmvcldae gavvrdallw ndtrsagaat dlisdlggge agrrawaeav
      121 glvpvasftv sklrwlasve penaartaav clphdwltwr lggapgldal ctdrsdasgt
      181 gywsaaagay rsdlirlafg rdglllprvl gptgraghlr tgaplgpgag dcaaaalgvg
      241 aesgdvivsi gtsgivstvs dvpaadasgi vagfadttgr flpvvctlna arvldaaatm
      301 lrvdhaalst lalsappgad glvlvpyleg ertpnrphat gavhgltlrt stpahlaraa
      361 vegilcalad gldamiaqgt tvnriilvgg garseavrri aptvfgcpvl vpplgeyvad
      421 gaarqaawvl sgdqrppawt igqvevydad avpavrerya aaranvsdra d
//
LOCUS       WP_357521472             387 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora rubra].
ACCESSION   WP_357521472
VERSION     WP_357521472.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   3  (residues 1 to 387)
  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..387
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40662
     Region          138..386
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mglrrlgrrg vqlikaddpe tgwlvrivvs allgwslvfl tppslavrav lvaslacwga
       61 flvadtrwpr fargalalat llpatvagvp qsasapifly smlftfvllp rtpmrailal
      121 tgativvflt gmwltgrgpt amltqpalia vlvlfsvhrr eyrlraeqta mlleqtsrtq
      181 eaqaqaaals erariarelh dvlahslgal rvqlevaevq ltekgdigga aarirqarrl
      241 agdglvears avaalrtdtp plphalgdlv aahradhlat valhtegspr glpsgaevsl
      301 lrttrealtn aakhapgapv avtldyrgpa vrltvrnpap vdsatatddg vgghgligar
      361 erlalvggtl eagvvdgawr vtaevpg
//
LOCUS       WP_357521490             255 aa            linear   BCT 28-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357521490
VERSION     WP_357521490.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 255)
  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..255
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..255
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=27750
     Region          11..240
                     /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 mwteefvagr pawrhvpsgv vfrevpggtf rmglseaeld avraiersgg vedtiepfla
       61 sardaqpvrd vrvepfllar hpltvaqvqh wlpeyeddya dadtgtarle gdlhdllkll
      121 pfqlpseaqw eyaaragttt ltsrgdgkpd edqllddfgd emrtaasena fglaamgsan
      181 eicadvwipg fdgapsdarp rtgdgprtvr ggaadlfpwq gcdewlllls atryehadfa
      241 avrpaaplpp nrgrp
//
LOCUS       WP_357521545             214 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357521545
VERSION     WP_357521545.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   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 214)
  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..214
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..214
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=23270
     Region          3..212
                     /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 matfilihgg ggsawdwhll vpelvgrghd vvvpelpien rsagfaefce tvvdaigdrs
       61 dlvvvghsyg aftapliadk lpvrlivllt pmvpvpgerp gdwwdntgyr gaeglseeqq
      121 fyngvpaevv aeaaahgreq vsaewnepwp ldawpdvptk vliaredrff padfqrrvaa
      181 drlgvtpdei dgchavalsh ptqladrlta ylph
//
LOCUS       WP_357521553             283 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Polymorphospora rubra].
ACCESSION   WP_357521553
VERSION     WP_357521553.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=29887
     Region          4..235
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mtairilhls dphltasgfd edgvdaaral rrlmttvrev edldlivstg diaddgsvag
       61 cerfrdtvgg farrrgvphi yttgnhdrrs sftevfgsgh ltadgadaad argpsgtcaa
      121 vshlgdlrmi tldslvpgsg hglvgdeqla wlrnvlatpa prgtvvalhh pplvlprhpl
      181 anlllhdfaa fsqvlagtdv ravlcghlhh erygtvgavp vyvapgivtr idfdprttrl
      241 igvlgaaaav velredlapv aytvtardsr agevvyrvds apn
//
LOCUS       WP_357521585             496 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357521585
VERSION     WP_357521585.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Smith,T.F., Gaitatzes,C., Saxena,K. and Neer,E.J.
  TITLE     The WD repeat: a common architecture for diverse functions
  JOURNAL   Trends Biochem Sci 24 (5), 181-185 (1999)
   PUBMED   10322433
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Neer,E.J., Schmidt,C.J., Nambudripad,R. and Smith,T.F.
  TITLE     The ancient regulatory-protein family of WD-repeat proteins
  JOURNAL   Nature 371 (6495), 297-300 (1994)
   PUBMED   8090199
  REMARK    Erratum:[Nature 1994 Oct 27;371(6500):812]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..496
                     /product="WD40 repeat domain-containing protein"
                     /calculated_mol_wt=52504
     Region          131..>313
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
ORIGIN      
        1 mlaaeadrmt parvpedlwr rgrrryrrrv agavtavlav alalpgllvl aaepppvvga
       61 stegavpgrv fdpwpwqapv aqsppgpaai llsgsgnglg gvdlpgaygs kvaavgrdgs
      121 yrmlryadty lqvgqqvqls pdgryvvgpd sveelivpgr agrlsvvdlv tgqarrykel
      181 padvpvawqp dgaalllwhr pepppvygdt ppfdgneary gyaggslwll dlatgesrkv
      241 ldlgaavfdp insvafapdg rhlavqvdra lvlvntadgg srtlatlgag qrlagtgaft
      301 adgarlavld ldgcaaacts aarnqrqwrl ttldaatgqa gpdggfdrvp gaavrivgwq
      361 rdgtavlvty qdehhpyydr epsieapaay ravsaaklla vrpgggttql irqegvwvwd
      421 idvahdlvvd grfggpspep tafpaawwly rlvltptagl lllvvlvawl rrraprravp
      481 lstpnlakad qdmert
//
LOCUS       WP_357521638             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357521638
VERSION     WP_357521638.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=34880
     Region          20..313
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msaviapdka psranvmpdt pgwarwandh rkwlfaapam afvaaliifp lgwtiylslt
       61 dssgsvraes efigfrnyid vlsdtdrfwp avgrtaaftg vallfevvlg maialllwrp
      121 fkgekwvrva illplvatpv avgmmwrlif dpniglanqa lgwigigpqp wlagqhtalp
      181 ttifidiwqw tpmvvlilla gltslseepq eaamidgasp wqrfrhvtlp llmptvivav
      241 llrgidalkt fdilyatkgr gggsfnevet lnvyayglsf dyneyglsst vlilffliii
      301 gsmwaltsrr kkearr
//
LOCUS       WP_357521697             490 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora sp. NPDC049171].
ACCESSION   WP_357521697
VERSION     WP_357521697.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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..490
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..490
                     /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=50278
     Region          10..386
                     /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 midesrvlpp giaadvalse irqlragdrp thggqlfayv ydsavsglde ltaaahresa
       61 hvngldptaf psllamenal vaaagrvlga gpgttapdvv gsvtsggtes lilavktard
      121 ahpeitapri vvpstahaaf akaahylrva ldvvpvspdt lrpdpaamaa airpetvlva
      181 csapsyahgv vdpvaeiaaa aaaagvrchv dacfggwtlp ylrrlgepvp afdfavagvt
      241 sisvdlhkya yapkgvsvll hrdarlrapq yfafadwpgy tminpviast rsggpiaaay
      301 atvrhlgddg ylrlatrtre avagladavr avdglrlmae pestvvcfta teggpdlfvl
      361 vdeltargwh tqpqlsyagl pasvhltvta svaprvaefg pdlaaavtaa raagpvalpp
      421 elvalatslt pdaltpdlva glagglglgg gdaptpdrma lvntlldaaa palrerllve
      481 fvgllqrpaw
//
LOCUS       WP_357521726             258 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357521726
VERSION     WP_357521726.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  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 258)
  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..258
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..258
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27524
     Region          7..219
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 menltqlvsv itpvhapsie hlpgayesla kqempdgwdw ewlvqedgqt galvdalpdd
       61 prislgtgrp ggpgvartla lsrvsgqlik vldaddqltp galardiaaf dahpqigwtt
      121 srvldllpdg stagwdkdpa ggvidrgsvl tfwqandyra svhpatlclr rdlvfalggw
      181 malpasedtg lllaanavta gyftreygll yrkwpgqvts qaahrepaey qarmriiear
      241 analasmipn gfgssata
//
LOCUS       WP_357521727             177 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polymorphospora rubra].
ACCESSION   WP_357521727
VERSION     WP_357521727.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 177)
  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..177
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..177
                     /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=19966
     Region          1..150
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrdvkdrgpd wfrgvyaehy pdvvryglrr ldgmaaaeel aqevflvawr rrwevpartl
       61 pwlyavarrl lanhwrakra aapaveltea vgpdrqdgiv rlidvrtalg rlsdddqeil
      121 rlvgweqlsl setalvlgcg paaakvrlhr arrrlaellr drpeqttsvs gqlggvr
//
LOCUS       WP_357521735             293 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Polymorphospora rubra].
ACCESSION   WP_357521735
VERSION     WP_357521735.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 293)
  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 293)
  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..293
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..293
                     /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=29952
     Region          1..248
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mallvgaavv glgarpaaai aygedatdgd yrfsvlltmt glpdgdggsr dsscsgalia
       61 prwvitaghc frdrngrqvs rtvahhttat vgrtdlgghd ghevevvavh qagttdvala
      121 elgtavtdia plrigtgppr vgevvrltgy grtahsgpdt aswlqtgqft vdrvgdtlle
      181 tsghapqpdt spcpqdsggp yfreqpdgta vlvavvstgp gcphagadfs artdnlgdwi
      241 agtiaadpas lhrnpvvvgg gvlvsltavs lvvfarlrgn rrrsaaahrv prp
//
LOCUS       WP_357521746             477 aa            linear   BCT 28-DEC-2024
DEFINITION  pentapeptide repeat-containing protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357521746
VERSION     WP_357521746.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..477
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=50561
     Region          242..413
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mpelrlwgir rsitsavgaa lllvgvliaa alwyaewpgl ergatvtaat lfdllklvfa
       61 vvagiggvaa lvvayrrqrv aehtnalaef ahqlahaadl raevtkalae aaderaktet
      121 drngvrlfne rfakaseqlg sekaavrlag vyamagladd wrhgrqtcid vlcayvrmpy
      181 tppdvagetp tqdedhaalg aadraraare erevrhtvir lvgrhlriae ddaaswcgyd
      241 fdftgavfdg gdlsgarfsg gdvsfegatf nggdvsfgga afsggtvsfg ratfsgghvs
      301 fgdatftggr vffdgvtfgg gdvtfggatf sggevffdda tfsggevffg gvtfsggrvf
      361 fdrttfsgar vlylakfdgg wvsfenaafr dgevffagat fsggdvsfdg atflggkvsf
      421 dratfsgarv ffnyvifngg hvsfrtarfh vpptfedgll ghppdglilp refsdrp
//
LOCUS       WP_357521800             383 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357521800
VERSION     WP_357521800.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 383)
  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..383
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=40300
     Region          167..383
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtverrvgpr lrlpvlvaag satgavelaf lvvaavalgv sapvppaarv aarltqryag
       61 rlvrlergrl drllpgselp avdalatrrq vgylaarllp aalgllayam lgvglvlagi
      121 vlraavrgel slldtlaqva vgvvllllnv qalasvaald vrmarrllga gsraelarrv
      181 deltssragv iaavdaerqr ierdlhdglq qrlvalgmll grarrardad rtaallvqah
      241 edvqraitel revawrvyps aldgsdlgev lamvarrsav pvrircdlpv rpdrqietvl
      301 yfvacealtn aakhaaatlv aveigvregw vrmrvhddgv ggadpggrgl sglarrvaal
      361 dgrlrvtspa ggpttvlvel pcg
//
LOCUS       WP_357521815             133 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049171].
ACCESSION   WP_357521815
VERSION     WP_357521815.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..133
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14602
     Region          15..121
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtmtagerr erdrrsynaf laecpghell atlsdkwltl vvsaladgpr rhselartva
       61 gasqkmltqt lrklerdglv srsvtvgvpa rvdyqltplg esllpvqrai kawaethige
      121 vhaararyda pen
//
LOCUS       WP_357521943             348 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357521943
VERSION     WP_357521943.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=34822
     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 mtalasrptq drsrsgtrtg rrvavtagaa lvlllavlas falgsrhlgi dqvwhalvap
       61 ddgdastivr elrmprtalg lavglalava gvlfqaltrn plaeprilgi sagasfgvvl
      121 aisvfgvgtl agyvwfgigg aliagllvfa iatraregas pvtlalvgaa ldaslasgvy
      181 allsidartf eeyrfwvvgg lagrdlsvta qvlpfvlagl llaalvargl dalalgddva
      241 rglghriglv rlggglaavl ltgaavaaag pvafvglavp hlaralvgad hrwtlavsal
      301 lgpalllgad vvgrlvappg eipagiital igapllavlv rrarvvta
//
LOCUS       WP_357521828             464 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357521828
VERSION     WP_357521828.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 464)
  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 464)
  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 464)
  AUTHORS   ter Beek,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..464
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..464
                     /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=48698
     Region          6..346
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msapprrila ttlimaltas sllacgddep dsnskkitvw sledvadrvt atkaiiadft
       61 aktgiqvdlv tvnedqfpsl iaanaaagdl pdvvgsvsla girtlagnel lhasanaevv
      121 dklgkqtfsp raleltsddg kqlsvpsdgw gqllvyrkdl faaaglpapd tyeritdaaa
      181 rlntggvagi taatsssdvf tqqtfehlal angcqltdds gkvtldspqc veafrfygdl
      241 irtssvkgaq dvdttratyf agkaamviws pfildelagl rndakptcpq cqsdpaflak
      301 nsgfvtaikg pngtepaqyg eisswavldg avadpaksfv eymlgdgypr wfgmspegrf
      361 pvrkgtpaep eayltawnts qagvdakkpl advfgdevla nlrrspdtfq rwgltqgqgk
      421 lvgamlgelp vpkalsdvys gksdaaaaag rakkdveaik agvn
//
LOCUS       WP_357521944             346 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Polymorphospora rubra].
ACCESSION   WP_357521944
VERSION     WP_357521944.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 346)
  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 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   3  (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 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..346
                     /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=36975
     Region          <67..319
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mthpgnppav wftscrvpta tataqhhhll ddvtattgvs lrhlrdlepe haehhhqhhd
       61 valfreggni pplwtrsrga atrligltwi eegqvilarp dsgitgpvdl rglraavpaa
      121 rvrqpqlqrp valhgltgal alagldldav elvevgsgea pvdafwrgrg apahpaidav
      181 adgradiaya vgpvaadhaa rlglvtvidl daypdrttrv nlgspraltv dqstlddhpq
      241 lvvdyltrll raadraradn aglvasivaq sgaspsavra iygphadtdl rprltdellg
      301 lyrrqkdfll rhgfihtdfd vhawadpepl rlatlavdat aarlaa
//
LOCUS       WP_357521980             166 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357521980
VERSION     WP_357521980.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=18093
     Region          2..164
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrllvtadth vpkrardlpg plwaaidesd vvvhagdwvd eslldamsar srrlvgvygn
       61 ndgpalrarl pevarvdldg lrvavvhetg prtgreqrca arfpdvdllv fghshipwdt
      121 gapgglrlln pgsptdrrsq pyatyltaei dagrltkvtl rrlprp
//
LOCUS       WP_357521999             213 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Polymorphospora rubra].
ACCESSION   WP_357521999
VERSION     WP_357521999.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..213
                     /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=22643
     Region          44..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 mtarlagtvv dghaaalagl rcdrvdddgr qtvlpvrrwh gvaepvmrrl idrcagpvld
       61 vgcgpgrlsa evaarglpal gidtspravr ltrergaaal crsvfdrlpg egrwrhvlla
      121 dgnlgiggdp aallrrcagl lrrsgtvvve vdepgsglwr grsrlhhqrg eglpfewarv
      181 gldalpalvt dtplvigvvl cdedrwfael apa
//
LOCUS       WP_357522009             521 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522009
VERSION     WP_357522009.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   3  (residues 1 to 521)
  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 12993645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..521
                     /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=54053
     Region          9..291
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(9,33..34,63,68,73..76,89)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,71,88..91,95,97,133,135,
                     137..138,140,143,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,71,88..91,95,135,137..138,
                     140)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(20,95,97,133,135,137,143,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(141..147,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <184..422
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mtaplrigpy aierllgvgs fatvwlgydp aldahvaikv laenwshdlr vrerfrdear
       61 llrrleherl vrvhavgelp dgrpyavlaw adggslrdrl atgelpapaa lrllgeicag
      121 vavlhrhgvv hrdltpgnil fhsagpddpd aervliadlg lakalaaasg ltaragtpgy
      181 mapeqddpga vvdtradvyg lgrlgirllg adpsdghpsr pdppghapdp pgqapdppry
      241 aaradptrha peirlragvp pavaavlaqa tahhpadrys daatlhaalt rasgpvgrpv
      301 sgpterpvap tpasgpvgla aasgparqrp aprrgdrrpy rlrmagaavv avaavgavga
      361 epggagsarp vggtyttgpl tvvlpagwsa agatwagqyg adgepepalv mspqprrwaa
      421 dphlpgafvg lsattaartt pagflaerth gdcapapart trqadvewtv vtyrcdrgrp
      481 sivesaglhp arhalvyaqi tppvdsgpdf vdtllagvrl r
//
LOCUS       WP_357522043             158 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049171].
ACCESSION   WP_357522043
VERSION     WP_357522043.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..158
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17935
     Region          7..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrpaaldwsv enctiarame ilgerwtvvv lrevftgirr fddmrvrtgi prqvltkrla
       61 slveqgvlrr epyrepgsrl rheyrltekg ldlwpvlvav lgwgdrylad aegslltvth
      121 rdcdapvrle lrcadghdvg rlrdvvsrpg pgarrrtp
//
LOCUS       WP_357522131             156 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Polymorphospora rubra].
ACCESSION   WP_357522131
VERSION     WP_357522131.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 156)
  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 156)
  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 156)
  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 156)
  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..156
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..156
                     /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=17862
     Region          10..147
                     /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 mgsevspgdi rlrdvetadl pvffeqehdp eatrrsnfpp rererfmthw atrvlwdptv
       61 fvqavtvdge lagnavawwe gdrrfigywl grrfwgrgvg traltlflar ernrplyadp
      121 yvgntgsirl lercgfsrtg svwdgehehv mlvlge
//
LOCUS       WP_357522143             177 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522143
VERSION     WP_357522143.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..177
                     /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=19371
     Region          24..161
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 msarselasp agansanrvy tprraarvll vdaagqvllf qgfdparpeh rywftpgggl
       61 npgeapavga arelaeetgl rldpaelgep vwsdttefpf dgvwyrqvqd ffllrvgswq
      121 vdtagfddie qrsitghrww lpddlaasge rfypaelpal lnrlghstat drdeasc
//
LOCUS       WP_357522202             349 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Micromonospora].
ACCESSION   WP_357522202
VERSION     WP_357522202.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 349)
  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 349)
  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 349)
  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 349)
  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 349)
  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..349
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..349
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37725
     Region          25..321
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtdisdtlas mpssvdpept gveleqtlfe vkrvivgqdr lvqrlltali anghcllegv
       61 pgvaktlaaq tlatvvggtf sriqftpdlv psdivgtriy rasketfdie lgpimanlvl
      121 adeinrapak vqsalleama erqvsiggrs wpvpqpflvl atqnpieseg vyqlpeaqrd
      181 rflmkvvvdy psdadelail yrmstdrpsp rpvldaqrlr dlqahaervf vhhalaeyvv
      241 rlilatrdpg rfglpeiapl laygasprat lglvaaaraq allrgreyvl pedvrdlavd
      301 vlahrlvlsf davadgvsae svvrrlveav ppprlatghp qqtpdlaaa
//
LOCUS       WP_357522212             793 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522212
VERSION     WP_357522212.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=83102
     Region          60..736
                     /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 mhippgmvav aalsglvaaa aavlltviag rrvgprrpah vllavaagva llsllagvva
       61 alsahhhwaa eqgqrtgwat avaigttvsg lafaagllwl pgvaataagr arlaldglvv
      121 aaalwfvgwv lfseptrllg matpmacpai lvatvsaalg aglaatvifr aalrrrltal
      181 glgisavtcg gmglsaglcq agptmaltga avlaagllav alaahwadrp graevdlmdr
      241 dgeygiapmi amtasaihhl aqdgrftapg vvaasvegfa lvarqyltlr dvreyagrlv
      301 ereahfrela htdpltalan rrgllralha aaaagtpcvl lgldldgfkn vndmhghdvg
      361 davlaevgrr lrsnlrpgdv aarlggdefa vlmqgqpaea drvaerllgv lnrpydepeg
      421 pvflsvsigv agwagepdve lllrhadlal ryakqrgknr ierydaaydk llrrrttveh
      481 elrgaidrde lrlafqpvas lpsvrpvgae allrwhhpel gnvgpdefip laeecgmiap
      541 lgawvlhqac yqlsrwladg hdvwvsvnvs phelhapayv vqvaealrah hvppqrlvle
      601 vtehavatdl delirrltal rltgvriald dfgagysslg qlrrlpidil kidhslvaeh
      661 epvrpvdrdg pafapmvdiv mrlghqlgle viaegvtapt elaavvaagc rfgqgalfgw
      721 gvpaehleam leaatspgar sapppapppa prrvpggyaq vtppadgass gdaptsvdqh
      781 vgavdssrem rqa
//
LOCUS       WP_357522238             335 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357522238
VERSION     WP_357522238.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..335
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35257
     Region          5..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msavieiegl rktfhslrng rrvavdgfdl lveagqvhgf lgpngsgktt tlrallglvr
       61 adggrmtvlg apspqllprv agqvgaives pqffgnftgy rtlrllarag gvpisrvdea
      121 ldlvglrdrg dervkgyslg mkqrlavasa llkdprllil depangldpa giremrdlmr
      181 slaangvtvl vsshilgeiq licdhvtiis rgrrvaagrv devlaghdrh eflvrvaepe
      241 raaellnaae ltavvdggal vvsgvddptv isralgeqgl wvgeltplrp dlesvflelt
      301 ganaqpsvpr qvdgsalpag gqgeavidld rgvda
//
LOCUS       WP_357522295             410 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522295
VERSION     WP_357522295.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..410
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45207
     Region          3..408
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mndtvvaava qahrrdwaqv fsttaqltrd ldlaeectqd afaqaletwa esgipdrpga
       61 wlttiarnra rdvlrresvf rrkmpllvad etvpgpddgl vddrlrlift cvhpalsrqa
      121 rvaltlrlvc glstpevara flvppttmaa ritrakrkia aaripyrvpg pdqlgertga
      181 vlevvhlift tghtapvgah lvrqdlvdca iglarmlhll mptdaevsal lallllttar
      241 qdtrtsadgr lvllseqdrs rwnrqligeg lslltealrr rpptryalea aiaavhaeap
      301 twhdtdwnqi vglydtllrl wpspvvglnr avaiglrdgp eagldaltpm ladpalatyg
      361 ylsaaradfl rqlrrwpqav tayeealtlt dndveraflv erladvrrqh
//
LOCUS       WP_357522317             266 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522317
VERSION     WP_357522317.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 266)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..266
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..266
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28538
     Region          2..263
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 maaagtavvf vhgmflhaas wtswvelfra aghdpvnpgw pgepstvala rqepdrvagi
       61 giddvvthya qiiralgrrp vvighstgal vaqrlldqgl aaaavalqpp pirgvanlap
      121 ssipvgwpll rnpanrrral sltarqfrys hgnaltties dqlyrqwaip spgrpvfelv
      181 sanlsrrspa tidaanpdrg plfvvaggrd rsapaavvqa tvrrylassa vtdyqaypdr
      241 ghsmpvdsgw reiadatlvw irrqlh
//
LOCUS       WP_357522328             823 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522328
VERSION     WP_357522328.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 823)
  AUTHORS   ter Beek,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 823)
  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 823)
  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..823
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..823
                     /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=84209
     Region          131..340
                     /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          132..815
                     /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 mtglaarllr hrvgpaaatl laliagvlil vsmgtlvesg lrfrteprlw atadvvvanr
       61 tvshtfkefg gdtttstvtl peggtvdavl vdrirqvpgv aavtgdervl igspaavghg
      121 wdtyaftgrp igagaaprad devlvdtrlg vapgdridlv vggvsrsyrv sgtaetgsaa
      181 vfftdvqaar lsahpgrvda igvrmvpgad lgpvreiasa agattyagkd rgnveqsedq
      241 aaqtllievg svfggyvvll ivfvvagtig lsvrhrrrdl allravaatp gqvrrmlvae
      301 aallaligsa iggpagllaa rwvhgelvgr gfvpasfpmt gglfavpaav lvavlvavla
      361 alvaarrvtg ikpiealgei aveprrsgrv rliagvltlv aattsgaftl gaagstgala
      421 gavgmlylfv iavallapri nayaarlltp llprmwrvsg ylaaanlran aqgmatvlta
      481 lvlsvgfggs vwflqnnler qtttqssagt laervlvapg glpadaarei relpgvqaat
      541 gvhrtqvvvr alggiepvsa qsvdpagits tmdlavregn ladlragtva lsamqastsg
      601 wdvgdqaelw lgdgtpvtld viaiygrglg fgdvtlaaet vaehtaggtd deilvragpe
      661 adtalatwsa ghpgtevlda atrtrlistd mafgawlnrl ligvmvgyaa laaattmvla
      721 alarrrelal lqlvgvtrrq irrmvqaeqa gllgtavlig atiaaltlsa ivngltgspi
      781 pyvpplgwva vlggttllal tttvlpvrrl lsappidnig vke
//
LOCUS       WP_357522331             343 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522331
VERSION     WP_357522331.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 343)
  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 343)
  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 343)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..343
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..343
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37221
     Region          94..292
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mdtsmpagtl neeaanrdpr dspararrsp rgrftrgltv vltlvvvavl avygwplrtd
       61 elqraapetl sfavaserat rtasaesidp evrpecrsqf lshgrtsaka vlllhgytdc
      121 ptqyrglakl ffdrgynvwv praprhgvtd rsahatldan elvdyandam nvaaglgdsv
      181 gvvgisggav latwlvghrp davhrallls plykpdpaqv pdlavkplvv lfgshlvpdr
      241 vnadgfssaa lsqylrivrn fatdprsphl relaivtsqd ddvidrraav dipkdiadrn
      301 dtafsvhelp relgighdiv dpdglrgrad einqcyldly egn
//
LOCUS       WP_357522334              79 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357522334
VERSION     WP_357522334.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..79
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..79
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=7994
     Region          5..>79
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtavaddglp lvgtltlpvg pgphpavlll hgsgrldrds ntarlrmelg pplakslana
       61 giatlrydrr gvgatggdw
//
LOCUS       WP_357522354            1065 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522354
VERSION     WP_357522354.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1065)
  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 1065)
  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 1065)
  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 1065)
  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..1065
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..1065
                     /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=116710
     Region          6..1065
                     /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 mtrtgrasft qerfyflnel qpgnpayvva falrmegsld realaqalrr vvgkhdalrt
       61 sfavidgelt qqvsdaaepe itirdsapve qsvqdrqlre lvadearrpf nlgsgpvlra
      121 witswdadqh alvvlvhhia cdgwavglll ndladtyntg asgapgpsyv dyaeaqrvmw
      181 skntrrldhw rqlltgapql slhtdhprpt vlsfqgsvlr rpvdpelihr ltewakargv
      241 tlfavalagy awvlsrharq pevvigvpaa nrldeaeesl vgclvntlpv rvdlsgqptf
      301 tdlvsrtwrt altalghqdv pfeqivqalg eqrqlshapl fqtmltvqnf tftvpdfggl
      361 kvhevdveid aakfdvamtl dvstrspflr aefstelfek ttvegmlehy hallesvvae
      421 adgepsmvdh eertllttgw nppipeepvd hpsvlrsfva hatrspdava vrhrgrqlty
      481 rqldqwssri aagladlgva ggsrvglllg rspavlasil gvwklggvyv pldpeyprhr
      541 ldlivdsarp stmlvepdti dlarqlaaph gialldahta ngdatvpttf pdpddlayli
      601 ytsgstgvpk gvmvrhrgln alcdpspagl dvdetdrwlg ahsfsfdvsv wemwgalssg
      661 grliiadqad lvdpqrlarl vhaeevtvls ltpgalyrvl pplfdsldre rssvryvvla
      721 gealswsrva tlvdpkrlpa vfvnmygite gtihvtivav paaelhgvre gdigvplpsa
      781 rcyvldeqrq ptgvnvpgel yvggelvaag yvgapeltsa rfgpdpyapg vlyrtgdivr
      841 wgpdgkliyl gredaqvkvr gyrvelaeie aaflrqtavl acvavaeade lvvflrcgpg
      901 vgterelraa vrdelpgymv psrihvvpei plnangkvdt rrlvaesrlt apaprpvdta
      961 vrdslsarir riwadvlgrp dieptdnffd vgghsfalit vqqrmaeigl eisvtdlfrf
     1021 gtvadcaayf rraeapltdd rvaqrrrard eftrrrrisr ggeha
//
LOCUS       WP_357522365             347 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357522365
VERSION     WP_357522365.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 347)
  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 347)
  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 347)
  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..347
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..347
                     /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=36496
     Region          7..330
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 matvgnvavy gayghtgrfv vaelqergyv plllgrdqdk lqalvrdhpn lkarqasvdd
       61 pasldraldg vdavintagp faftagpvve aalragipyv dvaaeieanv dtfahfaera
      121 raagtvvvpa maffgglgdl lvttamgdwt aadevhvayg lsswhptdgt lasgmvssqr
      181 rggrrvrytg gqlqyhddal ptlewsfpap lgpqsviggf tmadvvtvps hldvpevrty
      241 mtaravsdlf spdpttptav dernrsaqtf vidvfvrsgd terrvaatgq diyavsapla
      301 veavdrlltg rtratgvvsa gaafdapnfl nalsahltlh apadars
//
LOCUS       WP_357522389             279 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522389
VERSION     WP_357522389.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 279)
  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..279
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..279
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29529
     Region          34..271
                     /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 mrprpggrfg paqlrlamaa prpaagltse wrlvdglrth trrstgpqvg appvvlvhgl
       61 avshryltpl avalsathpv yvpdlpgfgl tehpvgaydv rghaehlaaw laayrlppvc
      121 llghsfgaev aaslaanhpd avralvlagp tsdpaarsrr aqfgrwlldt lgeaplqapv
      181 lgrdiwnarp wrvlatlshs vrnaieadlv ritaptlila ggrdpiapar wrdqvtrlvp
      241 eadlvvvpgg phnvattqpv avaaairhll aprsaltdr
//
LOCUS       WP_357522441             415 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522441
VERSION     WP_357522441.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..415
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..415
                     /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=44637
     Region          4..409
                     /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 mvastdfsva iagaglsglc laqylmragi dvhvyerdpg pfvrrqgyri ildrygleal
       61 raslprslyn lalttgdepg ghlrftdsrl rdaftitfkd ephatrqvdr ltlrsilqsg
      121 ldgrihygkd avavdsgdpa rprlrfsdgg aatasvvvga dgvgsalraq lmpdadpant
      181 pmagiygrsp lrrngvsvip dalrssgvla iadrpglaff ftsmrfgesp seafarlapg
      241 syaptgddyv mwglllrqee vpvdvrgdll alwrlaarrg tdfhplirrl vdsaeldatv
      301 lnlfatgrrp rrwavpratl mgdavhampp fgahggntal rdaallghrl vearasgapv
      361 qeaiasyqde mvsyafravd taaglmrrlt ggaaaphwvl trvlprlhrv tvpea
//
LOCUS       WP_357522491              65 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF362 domain-containing protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522491
VERSION     WP_357522491.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..65
                     /product="DUF362 domain-containing protein"
                     /calculated_mol_wt=6623
     Region          1..62
                     /region_name="COG2768"
                     /note="Uncharacterized Fe-S cluster protein [Function
                     unknown]"
                     /db_xref="CDD:442050"
ORIGIN      
        1 maivtidacq gcgaclltcp thaiqpvagg ltvradrctg clecleicpv dairvldpdp
       61 regar
//
LOCUS       WP_357522514             449 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522514
VERSION     WP_357522514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..449
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..449
                     /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=48725
     Region          7..395
                     /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 msgapphvlv igagtgglcl ahglrragis vavyerhrdr adgllgyrvg igptgsralr
       61 eclppelfat flatcarpph yfnvvtqglr qtasfplrps adpvhtehsv armvlrqvll
      121 tglddvvhfd ktftryeqrd dgtvtayfad gtsatgnllv aadgthsavr rqylphavtr
      181 dagtiniatr ipltahtrgl vpervrqgis lifgvggmmg vlhvmefkwd arraikpgvs
      241 dadaallrnw pglahdtttd ninliiwstg rrfpadvmer rgedlvrval dltsnwhsnl
      301 relltradpa salpirvsts epvppwksst vtmlgdaiht mtpgrgvgan talrdarllc
      361 eqlgraatgd ktlvqavady eaamvpygfa rvaeslnrsg tsgddrmyrp vvgrlallga
      421 rgyfgvtsrv prlrrrfvdd fhtyegdqa
//
LOCUS       WP_357522530             434 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522530
VERSION     WP_357522530.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..434
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..434
                     /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=47220
     Region          18..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 mttpalirsr gtladllsgr sngiglirlc lavgvvlshs kplgfgaadl gysltgrqtn
       61 vgtmavygff vlsgllitrs arrtgvirya whralrilpg lwvcllital viaplvalre
      121 hgttagyfdn pgepggplay lrgnwwtgve qygihdlfiq stpwgrktst svfngalwsl
      181 kyemfcyvvv gvlaatavlr harrfvlvlt vvlylsilqd wvatgrisgp astagwtfda
      241 plvgpmgfhy ivylgflfal gatfdlyrer vpisdvlgig aavalglsll vggffviglp
      301 afayllvwls vrlprqvhwv grkndysygi yiygfifqql maslgwnrwg yvpfaamsva
      361 vafvaaflsw klveqpalrl kdwtpgfvar rssqrvpveq qtavaeeppa tppvqvggpt
      421 eelpqqsatl vpgr
//
LOCUS       WP_357522535             316 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            sp. NPDC049171].
ACCESSION   WP_357522535
VERSION     WP_357522535.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=34288
     Region          59..314
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mdqqlnrpis asesisrrgv lraatvsaaa vgaagllasp ataapagqsq grrrvpvdri
       61 siqlytlrdq laadlpgtld alrrigyrrv ehagfvgrta aqfraaldea glrstsghtg
      121 ipqpfdaatw eqaladanvv gckkivhpyf grdangqair dpnvyralar dlnkagrlae
      181 ragldfgyhn hqlefvpltd gstgfeiltg qtdprlvhfe ldlywtwrga hdpvdviran
      241 rgrirqvhvk dldveggfad lgdgvidfgr ifahereagi eeyiverdda gttprspada
      301 ldtarvgfdf laslry
//
LOCUS       WP_357522600             468 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357522600
VERSION     WP_357522600.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..468
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50265
     Region          3..462
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 msrrlvvldv vgltprllah mprlrgvadg gfraelgtvl pavtcsvqst fltgeppsgh
       61 givgngwyfr elgevllwrq hnalvggdkl wqaarraepg ytvanvcwwy amgadvnwtv
      121 tprpvyyadg rkepdcytdp pelhdaltgr lgtfplftyw gptaglpssr wicqaaeqil
      181 advspdltlv yvphldydlq rfgpssaqaa aaaaeldtvl gplldaarar datvvvlsey
      241 gitdvsrpvd vnrllraegl lrvhtqagme yldpwtskaf avadhqiahv yvkdpadvpa
      301 vaklcaslpg vaevldaegk aahgldhpra gelvlvaepd awftyyywld ddrapdfarl
      361 veihrkpgyd paelffdpan pgaakaragv alarkklgmr ylmsavglda garavkgshg
      421 rlpsdpadap vllcsdptaa rdkiaatevk alllelaglr dggpgegs
//
LOCUS       WP_357522685             203 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522685
VERSION     WP_357522685.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 203)
  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 203)
  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 203)
  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 203)
  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..203
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..203
                     /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=21920
     Region          128..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 mttpeitlat ptdrdavvat lvaafvkdpi lrhlfpdedt ypryaavffg dlfdkrvhrs
       61 siwtigggas vaiweppaep paeppvdapp dapgvgpgsp eeprypadvl arvrgyddtv
      121 haalptypfw ylgvlgthpd sagrrwgrav mraglaraaa dglpailets ypanvelyrr
      181 agwevlgtls epvptwimqq par
//
LOCUS       WP_357522691            1106 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522691
VERSION     WP_357522691.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1106)
  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 1106)
  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..1106
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..1106
                     /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=122342
     Region          161..1105
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mpdtlsyada vrllggensr fftwfdkltg wsllgasvag vpgalgifda kaefvrlghe
       61 lvrnvseqrs glsrydrtqr leaahaviav taffealhdv dlpfdaadla vdkreqlala
      121 ssgsvsdgiv dsffgtaapl pgphlpypal raalvtyfdg ltgrvlhfve glavweqadh
      181 qlrsraatal srlpdvairr hrdlltrlae dffevnfwlg lqeheatrqq lraisvglae
      241 mrralavmst grppddrrag laaaytsdlr rpivssgdvp aglrmptlge ayvpplcria
      301 elgagarasd eswwrdrplr edlwqslvvh ltsagattap llvlgqpgsg ksvltrilaa
      361 qlpaadflvi rvvlrevyaa gdlqdqieqa lraatgerlt wpdlvrsagd ampvvlldgf
      421 dellqatgas qtdylrrvaa fqrreadqgr svavlvttrt svadraqppp gavavllepf
      481 datridtwva twnrvnadcf rasgtgpldp dvvrahrela eqpllllmla lydadghdlr
      541 sagalgrgel yerllkrfah revlkqssgl serdlarate eelrrlsvva fsmfnrgvqw
      601 vseddldadl aalpflgrra stvrqdergs lstaeivlgr fffvhrstav rehgpshtye
      661 flhatfgefl iartvtlvlr dlvvreaatl lddapvdddr lyallsfavl snrapvvtfv
      721 vealaawpeq hraealdlll rlfrvtsepr pvgrhesyqp rrlhlperca vyaanlllla
      781 lsiadlpcgd vfpssaqpvr swrrravqwr ahlddaaylg lltlvhpirg wqdgeprltl
      841 slspgvdste pdprwhlpvr lglptsdgdg ahryvpdvdv dlwrrsvhfe cdphaeamlh
      901 aveparlsll errfdtltyf lsfpdgdrse arllldvall plhptplpqr ervyrrllas
      961 iephrptsrd esvaaflldr laldtelssa faadvlqhld aldltaghaa pavrcvlafv
     1021 grddqvdarw valagdllar arggaagrgh pldwldettc elvvrmyele lhrewisaae
     1081 aqhfafwygs rrpdlvqrlr rfadgp
//
LOCUS       WP_357522698             399 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522698
VERSION     WP_357522698.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 399)
  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 399)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 399)
  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..399
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..399
                     /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=41466
     Region          137..394
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrpppwlgsg tlgrdlalaa aslagglvly slgwqpqvrp ntgvpsalfl ppllvmcaav
       61 gmrrvapras lavgtgalvv dtalgnslgt ilvytqvlyd acvygpprlw rwllrvtigl
      121 sllgavvgvv sldnwrgvti gvlvvlagll pvltgisvrq yrdqaaaera raeqtarlve
      181 ldrrqavsae rarmarelhd vvanhlsava ihatavlsvp gldrgqvtsa lhviressvq
      241 glaemrqmie vlrepatgdg pagdgpavpe vvtarlaead glveriqaag lavrvstdgt
      301 pgplpvgvdl aayrivqesl tnalkhgtgk aeltiayrpa evvvtvenpv rvpgggvpga
      361 gagligmrer vtllagrfta gprdgrwqvr atlptgqgg
//
LOCUS       WP_357522715             590 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522715
VERSION     WP_357522715.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 590)
  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 590)
  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..590
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..590
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=64066
     Region          45..353
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          308..583
                     /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 mpptatrprq wlpytaavta glvviagafv ivrqrdadct ttlevnsste kaallvdlae
       61 rynrgdrsid gggcaqvhvs alnsgkatea langwantgl pqpqvwlpts slwtgqlrll
      121 dqgagrepqt pdrypsians plviampqpk aelvrqrgsl gwgeilglsg rdgwasfgkp
      181 ewgrftfgkd npnlstsgla atiatyyaav qrsndltrsd lanpavtqfv rrieanvshy
      241 sddsvdllrn laeadlagga grtddmsaiv lqeelvdlyn tgalsarqdg qeqgrrpnvp
      301 lvavhpregt fnldhpfvvl psadgrqraa aadfqkflte ddqqksfarl gfrdherras
      361 aellasvgae ptggltyfep pdpqvvgaml dgwrtlrkka nilialdtsg smqapvdttr
      421 trfqvataaa gkglallnse drvglwsfss eipsrpktpy rrevplgefd qrqiksriag
      481 lhvegataly atvraahrel rdrydpqrin aivvltdgkn eyskdneldr llaevtldpe
      541 rpvkvfciaf drdsdfatld riakassgka fdatdpakvd eafvklvssf
//
LOCUS       WP_357522748             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522748
VERSION     WP_357522748.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   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 265)
  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..265
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..265
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27531
     Region          37..265
                     /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 mtttrrslla gsvaaatgav lgapaaqahp rpgnqpkptv vlvhgafada sgwndvatrl
       61 iregypvlap anplrgvaad saylasvlat lggpivlaah syggivttna aagnpnvkal
      121 vyvaafapdq getllglqtt ypgsrlseaa ldfrpyaegl vdgyikreff revfagdvpk
      181 tttelmwagq rpadlralge psgapawkti pswylvarnd qvlpaaaqrf marragaqvr
      241 evgashvami sqpavtadli kraar
//
LOCUS       WP_357522832             241 aa            linear   BCT 28-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357522832
VERSION     WP_357522832.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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 241)
  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..241
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..241
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=25224
     Region          1..237
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mrirpvgaha llldctapad vpeaalveaw raelwrrrer gellaveivp aastvlldgl
       61 pdpavttkql tqwapevana tparpsaaaa draadrpaav deralddhgv ddhgdnaevv
      121 vlvefdgpdl pavaehwgvt vpavlrrlts trfrvafcgf apgfpyltgl paelalprla
      181 tprprvpags valagpyagi ypsaspggwl lvgrtelvlf dvsadpparl apgtlvrmaa
      241 a
//
LOCUS       WP_357522957              94 aa            linear   BCT 28-DEC-2024
DEFINITION  putative quinol monooxygenase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357522957
VERSION     WP_357522957.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 94)
  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..94
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..94
                     /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=9826
     Region          2..>68
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mliiagslqv epatreayls gceevitqar aaagcldfll aadplepgri hvyerwesae
       61 qlaafrgsgp sgaqeaaild advqryliag veap
//
LOCUS       WP_357522971             463 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357522971
VERSION     WP_357522971.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 463)
  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 463)
  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
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..463
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=48364
     Region          15..456
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpadvwpqpv ldllaaggdr pvfedgptvt tasamaglir rvaaglrssg agpgvgvtld
       61 lpvtapafaa tiaafavgar vsgwradlsp aqlsgslvvd sarlaalteh pddglplvaa
      121 graeeparii wtsgstgtpk gvvqtyaams aawvpypdrw ppaiadlatr mrrylvfgsl
      181 asqvmleygi lalaaggtlv vapqpvfpaa lvehratasv itvgklhqli rdqranpvdl
      241 rhlralmvsg splapgrlae aldvlgpvlf hgygqtetsm ismvtpaeml tdaatlatvg
      301 rpavdvsvrg geiyvrtpaq assywqdpde saevfvdgwv rtrdlgelga dgylrllgra
      361 rdviivnaqm vhagpveral aaddavaeay vvgrpdemtg eavhayvvpv agrtpdpdvl
      421 rklvavrvhd lavprtvtvi drvplapsgk pdksqlpppd dev
//
LOCUS       WP_357523080             393 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357523080
VERSION     WP_357523080.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=43194
     Region          68..388
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mstsdpikki tlrsgktryr fvldvgrkpd grrdqrtytf dtrkeakaey arikhetdrg
       61 tyvkpgritv defldewlas atrdvekata anyrdallpv rarlggkplq dvteadieal
      121 idwmltegrr rggkpgtglg vrsvrltlgr lrtalnvavr rqlvvrnvaa fvaipraaak
      181 aaieasaerk pwtqeevkaf ltgitaerly apcllslmgl rpaevcglrw sdvdfeagti
      241 aagentrtlv dgeieekeak saagkrglpm patvtkalka lhtlqkkerl kagnaytdsg
      301 yvlvnelgqp qrtdwlrrrv yelmakvgvr kvrpydarha cltylagagv pdvvlaawag
      361 hadggtlakr vyvhpdsshl kvaaehlesg lfg
//
LOCUS       WP_357523107             157 aa            linear   BCT 28-DEC-2024
DEFINITION  TadE/TadG family type IV pilus assembly protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357523107
VERSION     WP_357523107.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..157
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..157
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=15616
     Region          7..>42
                     /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 mstwwirdqr gsasiemavv apailalfag aviggrvnla rqaleaaayd aartaslars
       61 gseanaqala aanstldaqg lsctdvdvvv stvgfgvpvg qpatvtatvs ctatfsdval
      121 pgmpgtvpla asftspldty rsralgftns eapiggn
//
LOCUS       WP_357523235             479 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Polymorphospora rubra].
ACCESSION   WP_357523235
VERSION     WP_357523235.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..479
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..479
                     /product="ATP-binding protein"
                     /calculated_mol_wt=52522
     Region          8..338
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
     Region          326..418
                     /region_name="DUF4143"
                     /note="Domain of unknown function (DUF4143); cl24018"
                     /db_xref="CDD:474127"
ORIGIN      
        1 mgdtltafvg rdtelallst elgrvlpdtd rpgrcllirg rrrvgksrlv ekfvedrava
       61 nffftaagss pgeeirrfca daaestlpdr ellatanprd wdaafrllat alpdqtpsvv
      121 videvpylmd servfegllq rawdrqlsrk pvlliligsd lsmmealndy crpfhqrgre
      181 mvvgplnpad lavmmnlpaa eaidaalvtg glplictewp sgtglwdlla aatadptsal
      241 ivsaerslaa efpsqvqara vlsaigsger tfgniaraag elaatslqrs lttltdkrlv
      301 vgelplsttp skerryriid pylrfwlqfi apnmpeierg rgdltlarir rgwtswrgrt
      361 veplirdala rilpdnrlpa agtvggywtr tndveidivg adrgpvarel lfvgsikwld
      421 rdtfdvrdlt alqrqrdrlt neplplvavs rsgvscpgvd asygpeqlla awrtardaa
//
LOCUS       WP_357523191             318 aa            linear   BCT 28-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Polymorphospora
            rubra].
ACCESSION   WP_357523191
VERSION     WP_357523191.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 318)
  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 318)
  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 318)
  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..318
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..318
                     /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=33996
     Region          60..261
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 mpeprppfhg adphdsesph pdasdlaaml aegylgsvwl tgqhpsrdlr rgrytpesmt
       61 hpgkmlptip ryairtytqp gdvvldpmag igttvieamh lgrhgvgvey eaewvakaad
      121 nirhtvaaga pgqgeiyhgd stalpsllpa slhgrvslvi tsppygpsth ghvrtpgprr
      181 gkvrkvhhry ggvdnlayrs hgeladgfta ilagcrqllr pgghvvvtar pyrrhgelid
      241 ipgmvaaagi naglelveec ialicgvrdg viiprasffq qknirdaiat gdpqwlvqhe
      301 dvlvlraptg gaevpdgr
//
LOCUS       WP_357523241             303 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357523241
VERSION     WP_357523241.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 303)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..303
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..303
                     /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=33034
     Region          2..301
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtqpaflsrt ltgrqqragm afavpaallf aiilaypife sfrtslfsid lltgdasyvg
       61 ldnyaalggd rnllstignt llwtvvslag qlilgliaal lidtnwrgmr wirqlllipy
      121 vvpviatalv wqwmldghyg iistnlqswg flpagatplg legtalftvi lvniwrgfpf
      181 amlvywarmq sidkgqyeaa rvdgagawre fvhitlpnlk satiallalr giwtlmyfel
      241 vwllsrggpa gssevlstyi ykvvmgefri gyaaaiasav glflaavgva gwlvvrtrgr
      301 rsk
//
LOCUS       WP_357523218             539 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357523218
VERSION     WP_357523218.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 539)
  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 539)
  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 539)
  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..539
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..539
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58142
     Region          13..>235
                     /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 mshpeqhrgr wrprldrpal vallfglagv gyrlvltlft vpasnsdeat fglaalhigq
       61 grerpvflyg qhymgmlesy laaplvalag pswpvlrlpm lvlyalflyl ihrltrrlct
      121 pwfatavvgl lalggervvr dqltvvggrp evkpavllml litvglaagt vrrrrlaval
      181 fgllvglaaw sdwlilpyla vaglalvwav rrellgwsgl llvagvvvgi apmvldnlra
      241 gpgedsltvf revstkagps ppwsdrirgg llegvplahg lcpvegcgrw qqwfgvaypv
      301 llvvgaalaa layrgaaagp rgdrvgpvvq lalvagaalt llsyvrspla atspldnary
      361 lsvlqlslpa vlwplwvaal tawrgtssvl grvagalsaa vlvalaattl vitvlfattg
      421 taasrteerq arelaaalra ngphqvygdy wtcnrlifnt detvicavld gdlspgqnry
      481 rpywrqvgra erpgyvvevd spmdrrlrrl ladradttpv revggyrvyh pkapvrpwr
//
LOCUS       WP_357523284             267 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Polymorphospora rubra].
ACCESSION   WP_357523284
VERSION     WP_357523284.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..267
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27831
     Region          9..264
                     /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 midqvsalir eaaaevvlpm fqhlssadvs ekapgevvtv adqrteevlg agltallpgs
       61 vvvgeegvaa dpalldrlgg tdpvwlvdpi dgtanyaagr tpfaimvalv rdgtavagwi
      121 hdpvadsltv aeagsgayvd gvrmrisadp pppgglrgpi mtrffppgvr eafrerarvl
      181 gevlpglhca greyadlvag vqhfavfwrt lpwdhvagsf lvreaggmac rldgrpyeat
      241 sggsglvaaa sepiwhevre vlraagv
//
LOCUS       WP_357523243             456 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Polymorphospora rubra].
ACCESSION   WP_357523243
VERSION     WP_357523243.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 456)
  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 456)
  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 456)
  AUTHORS   ter Beek,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..456
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..456
                     /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=48778
     Region          24..387
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mtrnhprarl avtaaavagt vallaacspp gagsgnsagr addggpinlt fwtnltvstq
       61 agaiqqqaeq catqqqdvsv tfeavpfdsm ypkmvtafka gngpdimnti eggvaaaeag
      121 gfivpvddvv eshgkddfip sflhavgkdd qtwavpdwal hqevwyrkdl fqakgieipk
      181 swpellaaak qlddpangvr gfavpmgsal vapqtyyqfl yangvhtfdp qtgeyaldrd
      241 pakaieatqf mldlyqaasp pesrtwtwnd frtgyaqgkl amvldfgavv glaaeqnpsm
      301 idnmgvfplp gptaevkpqg sigggyffmv gksnerreka aktlvecmmq pdlaaartnt
      361 rpvfalpatn saaesatytg netvrrfape iqtirenilp ewyrygmeag lnqlagqiea
      421 ttfvgdqlqa aaagnitaeq afnninaemk rlakvs
//
LOCUS       WP_357523288              72 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Polymorphospora
            rubra].
ACCESSION   WP_357523288
VERSION     WP_357523288.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 72)
  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 72)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 72)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..72
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7136
     Region          4..69
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 msvtntytvv gmtcghcvqa vtgeltalpg vrdvqvelpt gavsvtsdap leldtvraav
       61 deagyelagt ga
//
LOCUS       WP_357523312             488 aa            linear   BCT 28-DEC-2024
DEFINITION  NADH-quinone oxidoreductase subunit N [Polymorphospora rubra].
ACCESSION   WP_357523312
VERSION     WP_357523312.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 488)
  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 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..488
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [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:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=48469
     Region          32..487
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mtqtidhval lpaylaagta vlvlladllv grraataava mlgaagtavg avlvgrgadr
       61 etfctvdgcs wlatsrgalv atvfavltlg vlllsgpllr agavpageyc fllacsmtgg
      121 vvlgaagdli tlivaletlt iplyilvglr rrtvasaeaa mtfflvsvva tavtllgaal
      181 lyavrgtlhl aalaaapale agaearlgrv avvlllagla fkvaavplha wapatydgap
      241 lpvaaylsta sklggvvavi avvvdglgpw lavsgpalav lavltmtvgn lvalrqtrmv
      301 rllawssvaq agyilaplga avavagrdad alsvavaatv ayavffvvle laafasvval
      361 rpadadggei tayrgagrrh pfvaaafvla lvglaglppg laglfakvvv vrslldggag
      421 wlavvvalna vvglayylrv cgtlyaagdv agtarrvpws vglalggata vavvvgfapq
      481 tildavql
//
LOCUS       WP_357523333             238 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357523333
VERSION     WP_357523333.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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 238)
  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..238
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..238
                     /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=24811
     Region          1..234
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msssqgqqvv vitgasqgig adlvdayrkl gygvvatsrs idasddpevv tvrgdiaead
       61 taervvraal drfgridtlv nnagvfvakp ftdytdeefd lvtrvnlagf fhltrrvlph
      121 llaggsghiv sittsfvdqp sshvpsalas ltkgglssat kslaieyaar gvrvnavapg
      181 iiktpmhpve thqtlaglhp vgrmgetsdv vdavlylesa pfvtgeilhv dggqnagh
//
LOCUS       WP_357523367             309 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Polymorphospora rubra].
ACCESSION   WP_357523367
VERSION     WP_357523367.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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 309)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..309
                     /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=31937
     Region          1..131
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
     Region          169..304
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mdrrrriaay gicrapdgrl llvrasaatd rpgvwqvpgg giehgehpad avvrefaekt
       61 gltvevrglr avvadvqtgp daalhtdriv ydvaplggtp reatagssdr vewvepgrla
      121 glplmpftae lfgrpvepvp adrtvpstag tghgtvtpag gdrpargqrf aayglvtdpa
      181 grvlltliap gfpgagswhl pgggtdhgeq pvaallrela eeadqvgrvt alldvshrrn
      241 paalgpegyp idwhavraif rvvvdaptaa rvteaaggst adaawfpsae aaglpltdva
      301 aavlprlap
//
LOCUS       WP_357523362             215 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357523362
VERSION     WP_357523362.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   ter Beek,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 215)
  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 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..215
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /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=22447
     Region          1..209
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mlsmhgasvg yggepavlre isvtlrpgri lavtgssgag kttllhalag llrprdgsvt
       61 vdgqplrdrd havehrivlv pqdnglapil taaenlqval vadgvtppea rrqtaamlel
      121 lglagqadql veelsggqqq rtavarglal rgsvlladev tseldagnrr rvldllhdea
      181 rrgaavvfat hdpevaaace aevhlvegra eilrd
//
LOCUS       WP_357523437             843 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Polymorphospora rubra].
ACCESSION   WP_357523437
VERSION     WP_357523437.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 843)
  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 843)
  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 843)
  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 843)
  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..843
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..843
                     /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=88770
     Region          143..825
                     /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 mtsgpawpar psapsglrri vpltgalltl aitavvlgpi faggspaeps dlllrsgiva
       61 gvfaagqlar lrvrtgsggf svtwgeaali vglhlvpagw lpaatlvgag vawsilavfv
      121 drrgvlevlh cvaslttavg vaaavtqala pplgaplspa lagalllgaa tylatttala
      181 tvtmavrhrr pvvplllgil rgkllmfagn vlvglaaivm idsdprwlll vppalwllqq
      241 tylhrfradd erqawstlaa avnglnrlde ravvsaales aarlfqaerv eldvtradgs
      301 rrryrlapdg elavravpad srpdsdsgry dveltaggir vgdlrvrfps svtpghrera
      361 alsifgaala talhdaiihr elriltsrsa yeavhdpltk lvnraavlsk gdvalhrlah
      421 dhpvalllld innfkevndt lghaagdell qvtagrlkas mrpgellgrl ggdefallit
      481 avpvradvag ggsslpaalr rardlverla vpvevggvkm sveasvgvvv agagtadmte
      541 llrradiamy qakdggsnia sydsgrdaas tdqlallael realvvddql vlhlqpavdl
      601 vtgrptgvea lirwhhprrg tlgpgdfvra vegsdllapf tryvidralt vaaewaragl
      661 dvpisvnlsa rslldprlpv evgeslrrhq vparrlvlei tetvvmseld viddvlaelr
      721 algvqlavdd fgtgfsslsf lariavhelk vdrsfvmgmv dspeaaaivr ttvelahelg
      781 lrvvaegvet adqrtalaal gctsaqgyhf fkpmpadkiv avlrnlsdsa qaqilplrad
      841 gas
//
LOCUS       WP_357523490             235 aa            linear   BCT 28-DEC-2024
DEFINITION  ComF family protein [Polymorphospora rubra].
ACCESSION   WP_357523490
VERSION     WP_357523490.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 235)
  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 235)
  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..235
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..235
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=24302
     Region          6..231
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mvaaaglwda ltdlvlpasc agcradrtpl ragacaacaa dlqalragpv rptpappglp
       61 dcvalgpyag vlresllsyk ergrhglarp lgrllaevva tavgpdrpvl lvpvpstara
      121 vrarhgdhlg rltrhaarrl rgagwrvrva rpvralprpd saeltsaqra raagaafrlr
      181 spsvravaag rrvvvlddiv ttgatlaavt tllaaagvrv daaavlaatr krdrr
//
LOCUS       WP_357523448             227 aa            linear   BCT 28-DEC-2024
DEFINITION  TVP38/TMEM64 family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357523448
VERSION     WP_357523448.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..227
                     /product="TVP38/TMEM64 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23595
     Region          38..218
                     /region_name="TVP38"
                     /note="Uncharacterized membrane protein YdjX, related to
                     fungal oxalate transporter, TVP38/TMEM64 family [Function
                     unknown]; COG0398"
                     /db_xref="CDD:440167"
ORIGIN      
        1 miravrrllr qpsaarfall vlliggcgll lllaprpdpk qlplladrlg dlapvaailg
       61 galllvalvp rtfvtlaaga ifgplegaay algaalvaaa igftvgrllg refvaervrg
      121 rlarldgwfa rqsvvgvvtv rllpiagfgl vsygygttga rvlpflagsv iasaptafgy
      181 aaigasvssp ghinwyaaap aslgliasvv lihqwwraer rrrrlpv
//
LOCUS       WP_357523620             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357523620
VERSION     WP_357523620.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=36161
     Region          14..310
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrllsll lllqqhgrlt atqlaerltv sprtvyrdve slhaagiply geaghaggyq
       61 lvdgwrtrlt gltteeadrl flaglpgpad elgygdvvaa lqlklhaalp aplrdratql
      121 qqrfhldtpg wyadgdaspe lartaeavwr qhrvevryrg wngettrvle pyglvlkggr
      181 wyvvadqpgr gapatyrvnq ilaltplpqe fvrpadfdlp awwrahvvqf rarlhrdeat
      241 vrlspagrqr lrevgsdpvv aamdasaqpp daqgwvtavl pieslthahg ellrlgadve
      301 vltpvalrer laataaglaa lyapdattpp ta
//
LOCUS       WP_357523594             174 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357523594
VERSION     WP_357523594.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 174)
  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 174)
  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 174)
  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 174)
  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 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..174
                     /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=18451
     Region          3..154
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mlirretpad vdavravhsa afatsdggng vpveatlvda lradegwlpa yslvatvadg
       61 qvvghvvatr grvggepval glgplgvlpd wqrrgvghal mhavlgaada rdeplvvllg
      121 hpdyyprfgf rpavelgvsp pqpwgpqyfq arpltawres irgefryagp fddl
//
LOCUS       WP_357523642             224 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357523642
VERSION     WP_357523642.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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 224)
  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 224)
  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..224
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..224
                     /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=23478
     Region          4..222
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mssiaifgag gragraitae aharghrvta vvrnpettgd igtdgvtvvr gdvtdphstf
       61 tisrghdavv stvspasgpe alaalgrldd qfyvdavdal lhglteagvr rlvliglfan
      121 lrdehdrlil ddpaafpshl rpfalshtag ldrlraadta vdwlmltppa mldaagprlg
      181 ryqvggdsvp psgsttlsya dlavavidei eaprhhrtrv svfd
//
LOCUS       WP_357523651             473 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357523651
VERSION     WP_357523651.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 473)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..473
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..473
                     /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=52381
     Region          1..405
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkrsgrvart alavvtvlla gvalnghsae pteeltvlgp wtddeevafr avlekfrkss
       61 giharyqghr dvsqvlqvai erdrppdvav lprvndlqry vnagrlvple gpittdpgaa
      121 pqlvklapkv gevrdklpya vsvtthlksv vwyaptelkr fgqsapstwd elvgltqrri
      181 gaeqvrwclg msaqsvsgwp gtdwiedill hrsgedsyek wtrgdlhwns pevkgawetw
      241 gallgvsseq taraslyttf qtaakglfpr evekgdgekv vipprchldh qgsfvvrkyp
      301 rkpstptnad ppftffstpp igpkatqslh evsddvavmf rhtrdskdvk dsdnterare
      361 lmsylaseqa qtawrepteg vafsrrgdap epqdrvlaav aeqlrtgtlc wdasdlmpaa
      421 mataferail vyleaperld sllaeleklr dkgpkaewld ltcvsprerg per
//
LOCUS       WP_357523720             325 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357523720
VERSION     WP_357523720.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 325)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..325
                     /product="phosphotransferase 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=35753
     Region          9..273
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtrtflqsde lhdlvaeqfg snsrlagldr ltggskkgvy rlglddqttv ilyvwaagen
       61 ywppsptipd dpftdasgae lfaashaala aagvriprli mldrdgryld adialledag
      121 alrlealmer dpaaatapla tlgdalrrmh ttlgphygkl aaitrgeasq trrtediivd
      181 ralghldaav ardarlaeah rriaahvhhl rgrvaprqty alvhgelgpd hvlvtpagep
      241 vmidfeglay fdvewehawl qmrfgeaypa lrpvdldphr lelyryaqvl sliegplria
      301 dtdfpdrqwm ldlaewniak alaai
//
LOCUS       WP_357523891             257 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357523891
VERSION     WP_357523891.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  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..257
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..257
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25459
     Region          40..235
                     /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 mdavslstll aaaamagwvd avvgggglll lpallvaapg lpvatalgtn klaaifgtat
       61 aaatyarrte vdwrvvapaa glavvsagvg aalagavpas ayrpvvlvvl vavavfvllr
      121 prlgvvavpr rrtpvrvaav iavagvgial ydgligpgtg tflvlafttl vgadfvhgsa
      181 makvvnagtn lgalvvfgmt ghvwwllgag mavcniagav lgarmalrrg sgfvrvvllv
      241 vvlalvaklg hdqwvar
//
LOCUS       WP_357523814             200 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357523814
VERSION     WP_357523814.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=21473
     Region          11..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtepsprltr aqqrrqteds iltaarqmfa elgferttir avaraagvda glvmhyygtk
       61 dnlfsraael padelpsggg eeivdvllas lasrldgepv aslavlrsml tntdaaeryr
      121 aaaepqlsqi itaiptedae lrasllsaiv hgviieryll rlgrladasp driiellrpc
      181 fqtlataelp pslvrpagan
//
LOCUS       WP_357523865             426 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora rubra].
ACCESSION   WP_357523865
VERSION     WP_357523865.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 426)
  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 426)
  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 426)
  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 426)
  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 426)
  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 426)
  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..426
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..426
                     /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=43646
     Region          133..420
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrrlsllva attilvlvaf lvplalllrs vaqdravgaa taemqgivaa vgaadpdtlr
       61 lsaeqvaaas gqpvtiflpd gsvlgtpapr tpavelaarg rsftaesdgg heivvavqgr
      121 pdgtavvrtf vpdaeltrgv trawlvlagl gatlvllgll vadrlarnlv rpigelsevs
      181 hrlaraelta ratptgppel revagalnhl agriqellre ereqvadlsh rlrtpltalr
      241 leaesladps daaritagvd aleravtgvi tqarkrsdtp apegceaaav vrdrvnfwsv
      301 laedtgrava ldlapgplpv glsaddlaaa ldallgnvfa htpdgtaftv tlaarpdgga
      361 llavaddgpg lpadqvrrge srggstglgl diarraaqss gghldltasp tggaqltltl
      421 gppthp
//
LOCUS       WP_357523816             165 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC049171].
ACCESSION   WP_357523816
VERSION     WP_357523816.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=18576
     Region          16..149
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mariqadwrr erpdldispq gvigrlhrla gylteelclv ygryglsege fdvlcalrrv
       61 gepyerapge laahtmvttg amtkridrle raglvtrrrs dddqrgriva ltqpgrelid
      121 qaftdhmhne rrllslltta ettalegllt twishvenlr psgsr
//
LOCUS       WP_357523977             345 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Polymorphospora rubra].
ACCESSION   WP_357523977
VERSION     WP_357523977.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=38182
     Region          5..342
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtvgavaerr lqrgsdfarl srrineaglm rrrpgwyaak ialtvglflg gwtafflvgd
       61 swlqllvavf lafattqvaf lghdaghrqm frkrriseva gltagnlavg lsygwwidkh
      121 nrhhanpnhe ehdpdveagv lvwsteqaaq tsgfgrwive rqaylffpll tleglalhva
      181 svkallgstp irhrraelll lavhtvgyfa avfavlsplk aiafivihqg lfgvymgcsf
      241 apnhkgmlmp tdsddldflr kqvltsrnvr ggvlvdfalg glnyqiehhl fpsmprsnlr
      301 raqpivaayc aengipyeet glidsyrqal ahlheagaql raekr
//
LOCUS       WP_357523989             240 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polymorphospora rubra].
ACCESSION   WP_357523989
VERSION     WP_357523989.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 240)
  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..240
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..240
                     /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=25086
     Region          39..212
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtgggpsgpv ggggrgghpv gggpsgpegv dapagpagli aaasagdela waelvrrytp
       61 lvlsvirsyg lnrtdaadvn qtvwlrlveq ldrlrepral aawlattsrr ecyrlvrigr
      121 rtqpfdpydd aghapgsllv daaspdedll raerhqalrd afaqlparcq ellsllaadp
      181 pasyrqvger lgmpigsigp tqtrclrklr scpalapfla tapdteptgg erdaavaaec
//
LOCUS       WP_357524003             388 aa            linear   BCT 28-DEC-2024
DEFINITION  homogentisate 1,2-dioxygenase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357524003
VERSION     WP_357524003.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..388
                     /product="homogentisate 1,2-dioxygenase"
                     /calculated_mol_wt=43401
     Region          1..385
                     /region_name="HmgA"
                     /note="Homogentisate 1,2-dioxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3508"
                     /db_xref="CDD:442731"
ORIGIN      
        1 mpyyrsvgev prkrhtqfrq pdgslyaeel mgqegfssds sllyhrhapt ailaadeftp
       61 paftrapnlp lkprhlrthk ldtggadpil grqyllandd vrigyvladr psplfrdatg
      121 dhclyvesgt lrvespfgal dvvagdyvvi ptstihrlvp tgdqparlla veasghigpp
      181 krylsvrgqf lehspycerd vrgpdapllv dgeevevlvr hrrgwtryvy ahhpfdvvgw
      241 dghlypwaff ihdfepitgr ihqpppvhqt fqgpnfvics fvprkvdyhp dsipvpynhh
      301 nvdsdemlfy tggnyearrg sgieqgsisl hpsgfthgpq pgaaersiga dyfdelavmv
      361 dtfrpldlcd aantcedegy awtwarrs
//
LOCUS       WP_357524016             992 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357524016
VERSION     WP_357524016.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 992)
  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 992)
  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 992)
  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 992)
  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..992
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..992
                     /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=108635
     Region          1..244
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          126..992
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          700..733
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          746..772
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(748..749,752..753,755,779,788..789,792..793,
                     795..796,819,828..829,832..833,836)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          777..813
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          818..852
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfgilgplr vgggestvta grdrivlaml llragrlvpv eelvdavwee qppatvraql
       61 qtcvsrlrrr faelglspea ivtdpagygi rtapndldve vfvrgvevar aaaaagrldd
      121 artgfraala lwrgpalsgi psqsirrraq aldeqrltal eecvdvemrl grgvelidel
      181 aesidqhplr erlrgqlmla lssvgrqaea lavyregrrl yadelgiepg aelqelhqrv
      241 lagdlvlagr asspsvpvrs lpraigdftg rqqtlarlvk dveagariql idgmagsgkt
      301 tlavhvatal addypdaqly idlhghsert pltpaaavat llrqlgvpae rvptnqddrl
      361 alwrtelagr rallvldnaa tadqvtpllp ngshclvlit srrrlvgvde grpsslpvld
      421 tdeaiellgh vvgvdrvaae peaatevvrr cghlplairl agarlahrpr wriadlaerl
      481 trrsdplaef eagdrsvara falsyaqvpp taqrafrllg lhpgvrfdks vaavlaelpl
      541 pdaqdlldel vdahlveete pgryrlhdlv reyartlvae peraaerrdg ierlldhhlh
      601 vataiartke lsslhslivv agplrpdlva lvaeqgqawl denlagwtal vrlaeteafl
      661 qycwqlarac wyaqfeggrl deliethtig lraaevlgdd ravatmlnyl asahyrlgdf
      721 pesirvmers laifrrlglr ggfrntlgnl gssyaanfef rrarecfdea ravatrmrdt
      781 valtnelnnl amtlllwgrh dealrvarrh lgiarevgdp rrignalghl gmirhrmgdv
      841 vpaarllrva lrfkrqagsr fgegevlnei gmmereagrp eqaadlhraa lvamtevgdr
      901 vaqcgsrnll araildqgdv tsaldlhrrv lvdatglgsr heqgralegi arclrttdpa
      961 aarahlsral vlfrqiespg rheverllae lg
//
LOCUS       WP_357524159             285 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Micromonospora].
ACCESSION   WP_357524159
VERSION     WP_357524159.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 285)
  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..285
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31258
     Region          13..76
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(19,23,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..281
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mplptspvir rarlgaelrq lrrrealtle qvcdrlgwas tsklsrielg qsrpdladvl
       61 dlldiykvpt ptrdalivia rdaatsrgww ktlgemserq rtyaeleaga adiveyqptv
      121 vpgllqtpay trvlveagaq ltpeidveae vraralrqev lrrayppryt avlaaavcdp
      181 gdlpvavwre qlrhlvtvtg lshvtvrllp rgaaggglhp ltpyscyafp dpadprtvmi
      241 ealttdvrla tvldvgryer mtealleaal speetvtala rrage
//
LOCUS       WP_357524027             395 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Polymorphospora rubra].
ACCESSION   WP_357524027
VERSION     WP_357524027.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=39833
     Region          1..395
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mseaflvggi rtpigryggm lagvrpddla alvvgaaver agvdpaavde vilgaanqag
       61 ednrnvarma vllaglpdtv aaytvnrlca sgltavanaa qavrtgdadi vvaggvesmt
      121 rapwvtekpa tawakpgatf dtalgwrlvn prmtaldggr atismgetae evakldgvsr
      181 aasdayalrs qeraaaavaa grftaeivpv ptrtgpvdtd ecprqtsler laglrpvfra
      241 dgivtagsss plsdgaaaiv vasadavrry gltprarvla gtsagvpphl mglgpvpate
      301 kalartglsi gdvdavelne afaaqvlaca grlgidderl nadggaialg hplgssgtrl
      361 vvtllgrler aggrrglatm cvgvgqgaal lverl
//
LOCUS       WP_357524034             206 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357524034
VERSION     WP_357524034.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 206)
  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..206
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..206
                     /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=22531
     Region          4..201
                     /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 metvedvtrm hlvggnlald fvntrtgpps gpsdddvltg ypelvawgvy agalteteat
       61 alrrlsrndp dgtraafsra lstrdyldev frplaggrsp stpalarlrd deadalahaq
      121 laggstfawv wrddrtlarp lrpvvhaavq llttgaldri kgcggcrfif ndesknrsrr
      181 wcsmddcgta ekmrryvaar rirapr
//
LOCUS       WP_357524215             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357524215
VERSION     WP_357524215.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  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..190
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..190
                     /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=20932
     Region          10..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprvsqdqld arrqeiltaa racfarlgye gatvrrleea tglsrgaifh hfrdkdslfl
       61 avaeddaaam vetvarnglv qvmrdllara mspdttgwlg sqlevsrrlr tdpafakrwa
      121 ersaaiaeat rdrltrqrda gvlredvpid vlaqflelay dglvlhlamg rpagdlgpvl
      181 dlveeavrrp
//
LOCUS       WP_357524221             417 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049171].
ACCESSION   WP_357524221
VERSION     WP_357524221.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..417
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44431
     Region          31..417
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mstpqrrpvp tpapagavaa eavaaagvea yprivatlir vtgdwalaed caqealaval
       61 erwpgdgvpa npggwlltva rnraldvlrr atverrklhd lalltpaeeq peerpdvvdd
      121 rlrliftcch palaldarva ltlrtvcgvp tadiarlllv sestmtrrlt rartriaqag
      181 ipyrvptgpa lterlpgvla vlyllftrgy vadgepafad eavrlaglld rlmpgqsevt
      241 allalvlfqh srrdarrdaa gnlltlerqd rrrwdraaia eglaaldrvr hdgpyawqar
      301 iaachataas aedtdwptia raydaladlr pspvialnra vahgyaygpa agldlldaar
      361 ggggldgnpl avavradlva rqgdrlraad lfreaaaavg saaerralld raaelag
//
LOCUS       WP_357524224             381 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora rubra].
ACCESSION   WP_357524224
VERSION     WP_357524224.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   3  (residues 1 to 381)
  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..381
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=40573
     Region          125..369
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mngvraarqt sygrialvll ltvysgydav vfatgmrsva vgiasvagav lllrrrfhwl
       61 laplfltaat gllgesfllp llcvalfdla adrragtavs cilaslgina ilttpssled
      121 aspylasalf mmgcvlgglw rgsrrravql ladqvehlkv easlreeaar irerariaae
      181 mhdvlahrls lialhtgvla arsddlpdrv adrlrllrtv stealtdlre vlyalhapep
      241 gtdqrrpaig qvndlvdegr tagqrigllv egtpemvptt hrfavyrvvq ealtnarkha
      301 dgatvtvrvd yrppatsvev antggqpapg aidsgyglvg lrerltalgg rlqvgpaggg
      361 swrltaelph pvdiaedrst a
//
LOCUS       WP_357524231             305 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357524231
VERSION     WP_357524231.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   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 305)
  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..305
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..305
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=34369
     Region          7..286
                     /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 mkhvaktrhr yrdveglrvr yreagapsst avvllhgaps ssysfrevlp tlgehayvva
       61 pdipgfgfsd appveeyeyt yeglshvtea llddlgvery ivfvtdystp vgyflatrhp
      121 ervlglvvqn gnaheaglge awdsgrrywa epteenkaal pdwltfegtr dtylgglrae
      181 vaelhppesw hldwerlsrp gntdvyfqff ydyrkhvarf geiaeyhath qppclmlwgr
      241 hdptfdiaev layhqalttf eahifdaghf llethaaeva dllvtftrdv ldrhdvpaal
      301 tssps
//
LOCUS       WP_357524248             980 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357524248
VERSION     WP_357524248.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 980)
  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 980)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 980)
  AUTHORS   Rosinski,J.A. 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 980)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..980
                     /product="helix-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=105443
     Region          <3..938
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <912..966
                     /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 mnptqltspv ligrddeiaa itqaagqvrh ghgralfvtg epgigksrlv raasrtvtgm
       61 avlsgratat gtsmpfrplv ealntrlrag ttpagpelep frpalsrlfp ewrtndgags
      121 gtddstlvla egvlrllavl greqplllvl edlhdadpet levlgyltan laglpvlvla
      181 tlrtgpsaal dlayrvrrdh dvrllelsal tsaqvsqlaa rclrtdpadl peqlaerlar
      241 ssdgvpfvve ellagmvang vlrhhdsrwh syhdlagpvp vtvvravadr adrlgprgrr
      301 lleaaaviga rfpipvlqtm ldlsptatde lvhaatathl lrpdpadpdw yafrhalian
      361 allgelshhe rtrlaataar altarypdlp gelcplaadl rlaagdgaga alllteagnr
      421 alaqgaansa atllerahhl lrrcgdrtgs iatlgtllaa leengefdra qrlvdavlal
      481 pdlptseaia lhtrlgwmaf hsgrtadads rigaarmllg pdagaaqlaa vdvvdahvls
      541 lqegradeae rvalraatea qriplpevvc rarqllalma rrrgfaeadr hlleivrvae
      601 ehrlplwrir asirlasnrm irsghseqlr qardaawamg avhtgyeada slamhdvffg
      661 ryddalrvag dcaaamlrfg kmgdlryala vkaaahahra dragmdatla efarrggvds
      721 yhmpivyglc hafcalleed rttarselda arafderrst iyyqygrygl allldvlaga
      781 agaeeyeeva ahpaaalrwn rqfvhfahaa llgatgepga avaalaqare aatvfptahr
      841 lglrlvaeaa lehgwgdpat wlreaelhfq tigtplvaaa crtlirragh rapqrrtghd
      901 llptrlrewg vtvreyevlv llaerhgnke iarrlylshr tvekhvasll rktahphrsa
      961 lcdyaaaipp pgpgnegpig
//
LOCUS       WP_357524320             264 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357524320
VERSION     WP_357524320.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..264
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29755
     Region          2..262
                     /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 mdlttlrhqe rgagtpllli nghfqsrdsw dptvaqlsrh crtltfefpn qgssptdtgm
       61 dtiahyaryt aayldrigvd padcvvhgys fggnvcrylh lemgvefrai ilggvashrl
      121 aeyqlrrlat wrellakget dlfvrtvllq ifspdfvcrh trhfdvtrka fagqygrrpe
      181 avlaligale dffrldrdgp dsyrcpvhlv gssadlltpw qyveeyakev gsvsthclqg
      241 ghqtrvehhq dfvdlmielm aqyg
//
LOCUS       WP_357524373             245 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357524373
VERSION     WP_357524373.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 245)
  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..245
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..245
                     /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=26408
     Region          16..236
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 maeasrdavr taapvlhdav ldalgleitg gqhapgtalt leqlqqrfgv srtvmreamr
       61 ileslnlvas rrrvglvvqp mhrwrvldpr virwrldgpg radqlrtltd lrvaveplaa
      121 agaarhatad drarlrtlat rmrqlgeage ldaflaadve fhalllqacl nemftaltgv
      181 iaevlagrte hglmpkcprp valdlhdeva ncvaagdawg aetamrelve evrdaisttp
      241 svgtv
//
LOCUS       WP_357524348             275 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357524348
VERSION     WP_357524348.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 275)
  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 275)
  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 275)
  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 275)
  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 275)
  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 275)
  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..275
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..275
                     /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=28742
     Region          8..260
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mviaynaqtv lltgassgig rsfaialaar gadlvlvarr adrleslate lrdrhgvtvh
       61 tfpfdlsaps agadlrdaaa qrgirvtsli nnagfgsfgp ftdadpehla revavdvsap
      121 vqltaaflpq ilaagggfvi nvasmaayap sprmavygaa kafvlsftea lwaelcgtgv
      181 tvfalspgat stefnqvvgt ddatagarmr tpeavvatal dhldrrdpsp svidgrgnrl
      241 sanavrlltr ratvslmrri tdpsrrdrer araak
//
LOCUS       WP_357524374             327 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357524374
VERSION     WP_357524374.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..327
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..327
                     /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=34918
     Region          1..326
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mrafryhrpa dvadavavlg aephaaylgg gtnlvdlmkl gvqrpdvlvd vtglaldtvd
       61 elpdgglrig atvrnsdlaa hpvvrrdypv larallaaas gqlrnmattg gnllqrtrcv
      121 yfqdtgkacn krepgsgcaa lhgqnrdlav ldwseqcvat hpsdlavalt aldtvvevhe
      181 adgarelpit tlyrspgthp erettlargt litavrlppl paahrstylk vrdrasfafa
      241 agsvaavldl dgdvvrdvrl aygavahrpw rayraeeelr grpfspelag raadaelaea
      301 rplrhngfkv pltraitvra lselass
//
LOCUS       WP_357524391             147 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049171].
ACCESSION   WP_357524391
VERSION     WP_357524391.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..147
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16123
     Region          18..135
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mttttaarkr aqtkveydaf laqcpsrkll driadkwvtl vlaalrsdgs hqfgadcage
       61 prplrysels rllagvsqkm ltqtlrsler dglltrtvvp tvpvtvtyel tdlgvslhev
      121 vrglkgwaet hmddvlanra tyddhag
//
LOCUS       WP_357524485             351 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357524485
VERSION     WP_357524485.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..351
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..351
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=38380
     Region          61..>195
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 msagppgsgp grrpgwrhsl artlfqglaa alavvtlgtp avatppeppp sghgtdgpql
       61 lrdvlestnr efvkakaale esrvrqlhlt lelskaeqqy eeltgqvqlv gaqsyregrl
      121 qaaavmlnst apdaflsrli mleelnmvnt rkvrdlgqar sraqqakqai daevlqqqrq
      181 haimgkqksd aekelrslgg asltanglvs atspvarpap nggngnwppe acnqkdptts
      241 gcltrrtlha yhevkragfd rfvgcfrtgd rwehpkgrac dwslqsrgfs parttdqrly
      301 gnnlaaflvr nadllgiyyv iwykqiwmpa tgwqpysgds dhtdhvhmsm l
//
LOCUS       WP_357524486             364 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357524486
VERSION     WP_357524486.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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..364
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..364
                     /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=39840
     Region          46..316
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtmdpdrvat aramlehlgl taadltgsnr pavptvaeyl pvvlaaaspa trrtygsswr
       61 rmvaahgdrr idavrasdie alqrqataga rprrnsrhgr yagehlvaaa rafynraiad
      121 gyltiadspa hrfrkprrlp ntrraltpde lsdinaaars ggndivldal ilrlhtetac
      181 rrsgalalrl idldtnhali rlsekggtqr wqpitpmlas rlndhararg avaptdallr
      241 yrngqpatyr rydliwkrig rqlpwvavqg itthwlrhtt ltwverhsgy gvarayaght
      301 dprgaattty ikadphavat alaaltgqph plaapeseqq fpaqdaedgh gatrspqtra
      361 rrrg
//
LOCUS       WP_357524527             402 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357524527
VERSION     WP_357524527.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,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 402)
  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..402
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..402
                     /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=43650
     Region          1..389
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 madivldkvs ksfpdgtvav qdvdleiadg efvilvgpsg cgksttlnmi agledissge
       61 lriggqrvnd kaprdrdiam vfqsyalypn mtvrenmafp lrlakldket inqkvdeaak
      121 vleltalldr kpanlsggqr qrvamgraiv rqpkaflmde plsnldaklr vqmrtvvsrl
      181 qkqlgtttvy vthdqteamt lgdrvvimrg gavqqvgppq elydhprnlf vagfigspsm
      241 nflhaavqeg glhtalgdvp lgdrirrele aadaprelil girpehfeda elvdddtrrr
      301 gmefeapvdi vesmgsdkyv yftvegekat aaeleelaad agvadfaggg gnlvtrlsae
      361 spvaegqsrr vwfnlekihl fdpatgrnlt lregraagal ad
//
LOCUS       WP_357524615             192 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357524615
VERSION     WP_357524615.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18527266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..192
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20073
     Region          23..88
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          94..189
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 mdsrrttrrp avdgggegag vgrrvrelre argislsals rragvgkatl sglengtrnp
       61 tletlyavta elgvplaavi appgtesati rgtaveatll rafdeddvtf elyrlrvppg
      121 ppqtspahqr gvtehltvfs gvlragpada pvlagtgrhi swtsdvphvy gavgdeevha
      181 sllirypgrs lp
//
LOCUS       WP_357524623             235 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357524623
VERSION     WP_357524623.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 235)
  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..235
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..235
                     /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=24866
     Region          15..183
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrkqpkrryt sdlrqeqaaa trqriaeaar elmlehgyag ttmadvaraa gvavqtlyts
       61 cpggkpglar lvydvtlagd aqpvpqsdrp qvhaiiaepd ptrklelyaa matgvfqrig
      121 avhrvlraaa sagsgdvgid elladterqr lvgsrgpadh laqvgalrag ltvdraadhi
      181 yaltsievfe rltgicgwsa vdyerwlart lidtllagqg ggapahevsp papad
//
LOCUS       WP_357524716             241 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357524716
VERSION     WP_357524716.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 241)
  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..241
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..241
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26679
     Region          14..98
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msddgavaaa pagrlnlrlg qllrlerera rlsqralaar agtsqqcvsr fetgfyaptt
       61 avverlfeal gcqvradvea ldadldesia varrerdddi rfmlgnlrsl lrwsggldyv
      121 idgelaaalq gvpvrvtrad vavaaadlpr ltdwiftlpn cerwnewwrd fvgadrdpnr
      181 pgplrwwtpl aelrvrllet wptpvplvag agevpvrpll dvlrddpqld rvarraralg
      241 a
//
LOCUS       WP_357524763             161 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Polymorphospora rubra].
ACCESSION   WP_357524763
VERSION     WP_357524763.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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 161)
  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 161)
  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..161
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..161
                     /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=17752
     Region          1..156
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mhiramrtdd adavlriyqa gldtghasfe ltapswlafd agklpehrhv avidgtvagw
       61 vavspvstra vyvgvvehsv yvdpaahgrg varrlldtmi tsteaagiwt iqamifpene
      121 vslalheryg frfvgtrerm grhhgrwrdv vllerrskvv g
//
LOCUS       WP_357524775             200 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Polymorphospora rubra].
ACCESSION   WP_357524775
VERSION     WP_357524775.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 200)
  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 200)
  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..200
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..200
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20940
     Region          4..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 mdpvqalwtg vtehpylllg plvlvegpaa tvvagslvga glarfwpiwl ivvvadvvad
       61 salyvlgrfg nhrrvapllg clglpthrrr rltvavrral prvvlgakvv dvaavpafla
      121 aglartpyrr fvawvagast vraglligvg vlfgqevahl ltepgtglai vaglalavva
      181 thlltrrlag trfdpvrekp
//
LOCUS       WP_357524791             445 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357524791
VERSION     WP_357524791.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 445)
  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..445
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..445
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46561
     Region          51..429
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtliadrpgp gaarpyrfpp vvrravaggq vvaahlpgqn lavalllldv gasqepvgke
       61 glsgvlakal eegtaqrdaa ayalaveglg talttgldwd sfqasvvvpv drlsaavell
      121 aeavrtprld padvrrvrdd eatalrmdwa npgpradaal radlfgaqnr wgrpmygdpe
      181 svaaldvedv tvfhsewflr pgtlivagdl dridldalaa aafagtgggp aerggpievp
      241 lqagrriilv drpgsvqstl rlghpsphra hpdhvamtla gtvlggafts rlnhllrevh
      301 gytygvrgdf assrrfgrfg vssgvqtavt vpalveavge isrtqaagvt edelevarsw
      361 ragqlsvelq spraiasalt tlvvhdlpdd yharlresll aadvdqvsaa aathlhpdal
      421 tlviegdaav irddltaaal gtllp
//
LOCUS       WP_357524846             312 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ribose-phosphate diphosphokinase [unclassified
            Micromonospora].
ACCESSION   WP_357524846
VERSION     WP_357524846.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=33462
     Region          1..311
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mrdiavfsgt ahpdlaaeic ahlgvplhpv rvsrfandcl evqlqancre rdvfliqplv
       61 ppvqenlvel llmidaarga sagritvvlp hyayarsdkk daprisigar lvadlltsag
      121 adrvlamtlh spqvhgffsv pvdhlhalre lathfrrydl sdtvvvspdl gnakeaaafa
      181 rllgtpvaag akqrfsddlv kisavigevt drdvivldde iakgstvvel mehlrglkvr
      241 sirlacthgl fsgdalqrls dqdgvleivc tntvpipaak rvpalevlsv apalaeamrr
      301 ihngesvsal fa
//
LOCUS       WP_357524901             655 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA cytosine methyltransferase [Polymorphospora rubra].
ACCESSION   WP_357524901
VERSION     WP_357524901.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12774760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..655
                     /product="DNA cytosine methyltransferase"
                     /calculated_mol_wt=73590
     Region          62..429
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
     Region          445..>655
                     /region_name="mutY"
                     /note="A/G-specific adenine glycosylase; TIGR01084"
                     /db_xref="CDD:130156"
ORIGIN      
        1 mtaadstptq pardpsarrg aygvklirgp fvqlpkhpda cedvpgmlry aeqarnrgek
       61 laadlfsgag glslglqeag yrvvlavdhy peavethrhh haglsvdwdl gdpervreva
      121 dlvqlagiel laggppcqpf skagrsmirh kvrhglrdpy derrdlwrsf levirlarpp
      181 avlmenvpdm aldkemfilr tmvheleslg yaveeravdt wrygvpqfrq rlilvalheg
      241 tafqwpaesp erptvwnais dlpeveggwr paggaegwad yqgpktdfqr rmrrnmpaed
      301 aakvfdhitr pvrdddlqaf qlmdadtrys dlpeemkryr ddifddkykr ldkdglsrti
      361 tahiakdgyw yihpeqhrti tvreaarlqt fpddfrfagp psaafkqign avppllgehl
      421 aravsnslev grvahvstre vaailaswfa agevngipwl raqtrwqviq aeilldrahp
      481 dvirqiwrml qtwrqpqdtl areedlrrig rfisrearad tvaelartfa nhptilrddd
      541 vlrgirglne sladlailav lagpddeaee pvlatkgvlr vaarfsgnpv nsrnrltdgr
      601 levarmigid anardahlgl idlantlcrp qdpvcqecpl skkcveariq seplf
//
LOCUS       WP_357524971             448 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Polymorphospora rubra].
ACCESSION   WP_357524971
VERSION     WP_357524971.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 448)
  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 448)
  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 448)
  AUTHORS   ter Beek,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..448
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..448
                     /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=48932
     Region          23..383
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mhpassptad aprdhrtpfr rgrrlralva avvalplvlg aaacggedne astdpnapve
       61 lsifwwggea ranlteqala lytqkhpnvt fkktwqanqg yfdklatlta ggdapdifqi
      121 ddnflteyas rnttldltsy kdenkldvtk fpeslwqygv vdgklagias gentqglvyn
      181 ktllqkhnlp epttgmtwea fiswaeqvsk ttgtpgtmdp sadykafwvw lrqqgkdlyk
      241 gkdlgfdead vtrwfelwkg ardrgatpta dvihegnatd itkqlvvtgk aatsfvwvnq
      301 lpelkkntkd elgviaypgd psaqwarasm ywsvfrgtkh kdvavdvlnf lsndpeagki
      361 lgtdrglpsn ldvrktvsda vtdpamktsi qvetdlatkf gpspqvplkg hskvraelik
      421 saeeaqynrq tpaqaaaafl tacksaiv
//
LOCUS       WP_357525060             387 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Polymorphospora rubra].
ACCESSION   WP_357525060
VERSION     WP_357525060.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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 387)
  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..387
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..387
                     /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=43289
     Region          1..384
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 marktigivl ngvtgrmgyr qhlvrsllai reqgglplsg gdrlwpelvl vgrsetklre
       61 iadrhgltew ttdltaalar pdveiyfdaq vtaqrekalr laieagkaiy tekptaedla
      121 gavdlarlad aagikhgvvq dklflpglrk ldrlvkgdff gqilsirgef gywvfegdwq
      181 aaqrpswnyr aadgggitvd mfphwhyvle qifgrvtsvn ahlsthidrr wdeageayda
      241 taddaaygif eidrpgqgkv vaqinsswav rvyrdelvef qvdgtegsav aglrncriqh
      301 rsttpkpvwn pdlpatedfr sqwqvvpdne efdngfkaqw elflrhvved tpytwdlwag
      361 argvqlaelg iqsaregrrv eipeles
//
LOCUS       WP_357525002             370 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357525002
VERSION     WP_357525002.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=39278
     Region          2..369
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msqqlrigvl gagwgaglhl egfrrvpgvt laalssrtrs raerraaefg vplvtddide
       61 lieavdvvsv atppaahlda vlaavragrh vlcdkpvalt apdaramlda aeragvrhas
      121 gfiwrndpal velrrllreg aigpvlevhs tgalgvpvlp mtwmyeagdg ggalaqhgsh
      181 vidrarwlvg aevtavcgrl hhdvkeavva adfhditdaf awarqhhgtt vdaprapvra
      241 dtgydfvatf dsgvrarfwe awhlagpaed evvvfgetgt lrwrgasglt lhrigaapev
      301 rdvdraagsg antpreigla rwgelaaafv aaingaadtg hptltdgwrv aaisdavrrs
      361 hhsgrweevr
//
LOCUS       WP_357525101             537 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357525101
VERSION     WP_357525101.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 537)
  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   2  (residues 1 to 537)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..537
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=57016
     Region          37..537
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mtripyprwa vvlgavalla ppiavgpaaa tddrrgaavv ridqgtvrgs vsadhlsfqg
       61 ipyvrpplga lrwappqpgp vwagvrdatk pgaacaqlqg lpmdhaadse dclhlnvttp
      121 ltaartprpv mvwlhggdfr fgrgdvydgq rlaangdvvv vtvnyrlgal gflahpalag
      181 pggvtgnfgl qdqqaalrwv rhnaaafggd pgnvtlfgqs agatsvcahl aapgsaglfh
      241 railqsnsca npvqtrveaa raaeefarni gcadpgtvaa clrgrdparl vetagypgag
      301 vdlgpvvdgr tlpvdpahal atgklhqvpv ltgmnrdesr lvvwgiehsg lncpqpqpqp
      361 gdeaescplt ddqyrdqvrg mfgdraeevl aryprsdkqv asetlgavlt dhgyaepiys
      421 aalafarrvp tylyefaddd apfftkgpep tfptgayhca elpylftvdy aeaftpaqqr
      481 lsdemvrvws dfartgrasw prlrggtpyv rvfagggesg ttdfaaahsy dfwrslr
//
LOCUS       WP_357525179             250 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Polymorphospora
            rubra].
ACCESSION   WP_357525179
VERSION     WP_357525179.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   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 250)
  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..250
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..250
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26776
     Region          5..102
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkeqrerrty gqqcglayal divgerwtll ivremllrpr ryrelldalp gigtnllaer
       61 lnfltqagvi eptdpdrrtg gyaltelgek lrepvlamar fglavmsgqs epspgtvtra
      121 swavlaieam cqaerstade tyefdvagev fhviagegkv ttssgpavdp vlristdtqt
      181 ffdlgsglie pveavlsgsv aiegppaavp rclyllglgs epaersllgp arrtarrpaa
      241 gpdpalssar
//
LOCUS       WP_357525210             643 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357525210
VERSION     WP_357525210.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 643)
  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 643)
  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..643
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..643
                     /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=71609
     Region          <80..>180
                     /region_name="PTZ00306"
                     /note="NADH-dependent fumarate reductase; Provisional"
                     /db_xref="CDD:140327"
     Region          139..595
                     /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 mtttpgeamp aikpitaddd tlrahlsdae apallmtvah ltgdlsilrd dlrpngwlfl
       61 pqggltdeqq dharelalna lrrlregaav prldrgtlrr vtswamggdt edlvplleqe
      121 lilpgedpka pdwrldqvap drdarvvvig aglsgllaah rltqagvpvv vyeknpdlgg
      181 twfdnhypgc rvdvpshlys ysfatrtdwp dhfckhdell sylrdfakqh glldlirfns
      241 eiraahwdea agqwrltadt pdgprteqct vlvsavgqln rphvpqfpgs eefagpafhs
      301 arwdhrvdlt gkrvavigtg asafqfipev akqasrltvl qrtppwlrpt phyhdavpag
      361 vqwlyehlpy yaawqrfwll apglrgvleg wvvdpdypps eravsalndq lratlttyle
      421 sqltdrpdll plllprypvg akrvlrdngk wlatlksdhv rlvttavdrl tpdgvrdadg
      481 elhpadviiy gtgfqasqfl apmtvtgrdg vdlhdywsgd araylgltvp gfpnlfclyg
      541 pntnlsgqgg siiyfsecgv tylvdavrrl vqgghramev rpevfrefnt wvdeansqra
      601 wgfsnvsswf vnaagrtaqn wpfpaqdywr rtravdpady elr
//
LOCUS       WP_357525221             994 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357525221
VERSION     WP_357525221.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 994)
  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 994)
  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 994)
  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 994)
  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..994
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..994
                     /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=106089
     Region          27..276
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          162..959
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          814..841
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(815,818..819,822..823,825,848,851..852,855..856,
                     858..859,888,891..892,895..896,899)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          846..876
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          887..915
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          927..953
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkqelelsks aaarhaddga rpvsgslrfq ilgplriwrd dvelsagprq qgnllallla
       61 ragrpisvsn liellwgeda ptsatnvihk yvgtlrrlme pslppratgs ylrrhgggyl
      121 fapgagtldl vsfreftsaa raslalgdrd raldsyveal qlwrgpagdt yaagsaatsi
      181 faaldrefld vcvsaaelav slncsgrvlq plrlaasmap lnepvqasli salgtaghqa
      241 dalkvfrtvr srlledlgid pgtaleaahr hvltqattaq daagagrgqt vdrlppeplv
      301 rpaqlppdlp tfvgrteela tlgalrsgsd gagrtgpliv aldgmggvgk stlaahfahl
      361 vsgdftdgql yldlrgdqtt desvsagdav gsllssqgvh vssipetlaa rvgtfrslta
      421 gksilvfldn asdcaqvrsl lpnspeslvl vtsrkplvel aaidgahllh ldppdmltar
      481 elvrrrlvsa pnravaglas pagildeiie lcgrlplala ilagrlsarp rlaladvaae
      541 lrdgtqrlaa fssshsvrdp raafawsyrq lspdaarlfr lssaamapgl saaasaslag
      601 hpgpvaratl reladaalld eddrgrltsh vlvkayaqel flthepasdr aaattrllqh
      661 ylhsgyraam vlaperpiva pspvpagvap eqpttydeam rwfddhrevl peavrraaeg
      721 dfgiagwqla ltmqpwlrrs grfhdwqdim rvalasasdr gdrvgaahvm csladsrsyl
      781 aahaealdll sgarqifaeh gllaeqgvvh stlhrihtel gqhqraleen eralaryraa
      841 gieqgeiwas aaqgrslvrl galdeamscl dealarseks ewttdeadir ismaeclgam
      901 gqqhravehl eravdaaaea qnrisvfeas illceahlgl devpgacraw rqacdamham
      961 qnggtrnmrd kvcdmgdklt evtefcprsq dtqr
//
LOCUS       WP_357525250             357 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357525250
VERSION     WP_357525250.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   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 357)
  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..357
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..357
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=38633
     Region          58..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 mkgsrepgcp ssctraasem vsgnqlrsdm ldlgvaggll ivirghrgaa mntgsekaht
       61 vrvgdlslic hirgrgplcf vhpggpglsg dylrmpller rltmvylepv gtggssrlpa
      121 gatydletya dhldavianl sdvpvlvlgh ghggfvaqsl alrrpdrtag lilyatapma
      181 dhhtraaare klrqyalaha drtdaeamia afdrpadrwv hestarlwql lpayfadywr
      241 rrtefahllg alpcwprpat dfdlrgalps isaptivvag vhdfafgpep aemlrsaipd
      301 avlaefsdsg hfphleeaer fshvvlefal rvcggvpgrp rragelaltg rhdarww
//
LOCUS       WP_357525442             175 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Polymorphospora rubra].
ACCESSION   WP_357525442
VERSION     WP_357525442.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=18853
     Region          6..145
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtisplriav ivgstrkgrf gptvanwfsg haahrpdlhv eivdlagpgp vsaalaaadg
       61 fvvvtpeynh sypaplkeai dahykewhak pvafvsyggv sgglravehl rgvfaelham
      121 tvrdtvsfhr vqqcfdpqgr ptdpapaeaa dtlldrlaww gdalrearar tpyvd
//
LOCUS       WP_357525464             285 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357525464
VERSION     WP_357525464.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..285
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..285
                     /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=30242
     Region          28..226
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mgrkraadrv iepvdtgqae lvpdpdrags wtllldgapq shvdltdpth lefeyvrrla
       61 aavdlvapag aplrvlhlgg galtlpryvs atrpgstqrv aevdgalvel vrrvlpwpsd
      121 arlrvrvqda ramltatrda sydvvvadvf agartpahlt sveyaaevar vlrpagwyla
      181 nladgpplrh argqvatvra vlpqaclvgd aavlrgrryg nlvlvagrat ppvpeltrra
      241 agdwfpgrvv agdeldrfas gaqvvhdada tgsdppppgl fsvrr
//
LOCUS       WP_357525429             337 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357525429
VERSION     WP_357525429.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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..337
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..337
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35397
     Region          1..230
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mnplvsvivp synsivtlel clrsvatqty qpielivvdd astdgsaqva ramgatvvgt
       61 gsnsgqsvar nlgaehatge ilffldsdva ldptgveiav svlrdqpgvg aicgvydaep
      121 llpgtlatry rtaqqyvwfn evegtipglh talfairaev faetgpfdpr lrhtedqdyg
      181 yrlgrrydvr vtteirgrhd hdatlrtilr kvfhrtrmgm plwlrhrtlp ggaatgsral
      241 asvavagaaa alplpllvgp vgavatpalv ataigldaat yrhvfatggv gfgvyftavq
      301 llvtltaava agvgvaqyal trrpgppqsh ptshana
//
LOCUS       WP_357525493             225 aa            linear   BCT 28-DEC-2024
DEFINITION  MIP/aquaporin family protein [Polymorphospora rubra].
ACCESSION   WP_357525493
VERSION     WP_357525493.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..225
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22873
     Region          4..203
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mddtrryaae flgtlllvfi gvgatisare sggvvvvala fgfvaavlfy tlgplsgfha
       61 npaitlgvll sgkispagav aywvaqflga tvaglllwgl trwgdvadqt gvlgtngygq
      121 hinlggamvl etvltflfvl vvlvvtgrpe yagsaglvig falaavllag itldgtsvnp
      181 arsfgpavfe ggtalrqlwv fvifplvgaa laaavaplvv gretr
//
LOCUS       WP_357525528             389 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357525528
VERSION     WP_357525528.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 389)
  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..389
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..389
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41662
     Region          1..49
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(2,6,31)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(5,30)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(12..13,24,27,31..32)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mrqlrdaqhi slrnlakitf hgktylhele tgvktptsqv aqriddalna agelvalaaq
       61 ptiprrefva aaglaaalph tlvshgrhvg pgtagrlaer tarlrrldnf lggadtqhly
      121 aaeadstarl ikdgsyseav grqllavlae qtqlagwaaf dagrhtdanr lyrtsisaag
      181 dandhalvgn ayaflayqql algrpaadta taacdaavaa tptvrallhl raawahavag
      241 nadaadrqla qgttclsehd drpepdwvyw vddvegeimt grcwtvlhrp mraipvlera
      301 larfddthsr dkalylswla dayldaneve hacataaaav rlaggvgsvr paqrlnsfln
      361 rlrphggmpc vvelrtlaae astrprlsv
//
LOCUS       WP_357525618             946 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357525618
VERSION     WP_357525618.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 946)
  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..946
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..946
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=101273
     Region          44..946
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mspriqlpsg wvtfvftdie gstrlaqllg pdyrpvlaeh rrllrrtlas tggaellteg
       61 dsfflafeda asaltaclta qralsnhdwp taeaaprvrm glhtgyaepr dgdyaspevh
      121 raarvaaaah ggqvlcsast arraeplppg atlldlglhr lrgfddrerl fqlvapgler
      181 qfprprtada vahnlptqvt sfvgrqaerv elgllvkqhr litvlgagga gktrlavela
      241 sgmveaypdg vwfvdiaavt dpglvafaia avlglrpepg rpmldtlvey aaarrmlvvl
      301 dtcdtqpaac aeviarllsg gsgvrvlats resfslpgev vwripplsvd pradgtesda
      361 vallldrtaa arggrrpdpa esadlrrvvq rldglplaie laaarlrvls vgqlaerldd
      421 vlgtldagrq dpdpppverg wsgnqqdtvd lvaaasgasp ptpasravqr saterhltmq
      481 atvtwsyrtl gpraarllrw lsvfagpvdl atvewllgdd pldplsvlvd ksmvlaepra
      541 tgstyrmldp irayaarrla eageaqaard rhvawsahav drahlgqdgr pvtlslyald
      601 plagevraal rwcatggsar aglglaggld qwwlerglar egrlwlfrly griaetgeri
      661 peaelaavyh mhslhagadg efaeelrysq raeaaarqag dagllarvla graaplvdmg
      721 qfveaervcr evidwahgqd vvgeallavf slaellwrrg aleeaadllg avrpveaarp
      781 vergrrsvdm llgmvalarg dviaahehll valrsrmghg yhgracdtln aiavrcaigg
      841 drltaarlfg aaqatrasmr atpgifggyw aeqqaelrav lgdtvfdday gegaelglde
      901 aaalaldveh pdlaadstrf stglsqptpr rpldpdrhpa trtera
//
LOCUS       WP_357525698             251 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Polymorphospora rubra].
ACCESSION   WP_357525698
VERSION     WP_357525698.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..251
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27241
     Region          15..245
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtvsdwfcra sdveapvrlf cfpfaggnaa aflpwqrmlg pdvelwvaql pgrgarllea
       61 plddldelva rlaaavaerg drpfalfghs lgalvafeva rslrrdglpg phslwvagae
      121 gpgtrsvedr lhdlpdpeli ealrdyggtp aellddpemm elllpglrad faldecytyr
      181 agapldlpvh vlladrdphv dparaagwaq etsrpvhrhv fpgghfflfp hqatitalla
      241 rvlaadptpt r
//
LOCUS       WP_357525655             254 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357525655
VERSION     WP_357525655.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25913
     Region          15..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 marvvvvsgg gtgigravar sfvadgeqvv llgrraeplr eaarelaaaa paapvalplt
       61 vdlaeptevt rvrdelvdrf gavdvlvnna ggnalvggga pddglagvrw hwesnfrtnv
      121 ltavllteal rdvltspggr vlflssiaay rgsgsgsygg akaalhpyaf dlsaalgerg
      181 itvnvvapgy vvdteffggg lpaarhdvlv gqthtgrasr pddvaasvhw laapeaaqit
      241 aqivqvngga ergr
//
LOCUS       WP_357525620             272 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Polymorphospora rubra].
ACCESSION   WP_357525620
VERSION     WP_357525620.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..272
                     /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=28667
     Region          31..229
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mgrrttrtrq agieqavdlg vaelrpdpqr aggvtllvdg vpqsyvdptd ptylhfdyvr
       61 riasvvdaia pagtplrvlh lgggaltlpr yvaatrpgst qlvverdaal velvgralpl
      121 padfdvrirv ddvrevvgrs tdgpfdlvig dvyrgaamag gvgtasfatg lrrmlsadgv
      181 ytlnvtdlpp lvlsrvqaat lraaygdvcv laartmlrgr rygnvvlaas gtpgrlpvdr
      241 lvraalrdpv pgivlhgpal deftahtqps pd
//
LOCUS       WP_357525728             290 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357525728
VERSION     WP_357525728.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   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 290)
  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..290
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..290
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30526
     Region          1..289
                     /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 mhehtvdrdg rqlhvvedgl pegwpvvvhh gtpgapllwp twsddardrg irlvgvarpg
       61 yagstrlpgr svadvaadia avadalgidr fatwgvsggg phalacaall pgrvtavasl
      121 gglapwdapg fdvldgmred nvaelvaarq gqqalnplle ptatamatvd rqdlidqldg
      181 fldeadaqva rtgfggplvd girtglrpgl dgwsdddlal vrpwgfdlas itcpvgvwhg
      241 kqdamvpaah adwlaatlra eridipptdg hlavlahrvt dvhawllqhq
//
LOCUS       WP_357525743             712 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxypeptidase-like regulatory domain-containing protein
            [Micromonospora sp. NPDC049171].
ACCESSION   WP_357525743
VERSION     WP_357525743.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10613039
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..712
                     /product="carboxypeptidase-like regulatory
                     domain-containing protein"
                     /calculated_mol_wt=69530
     Region          147..225
                     /region_name="CarboxypepD_reg"
                     /note="Carboxypeptidase regulatory-like domain; pfam13620"
                     /db_xref="CDD:433354"
     Region          <419..>593
                     /region_name="PTZ00395"
                     /note="Sec24-related protein; Provisional"
                     /db_xref="CDD:185594"
ORIGIN      
        1 msthryawkq ragvvvalva gallavpapp alaakistad nsvtidagks stvnvvvrpd
       61 pdeksadldi tdlpdgvscg gcgpvnfgds tdpkavtltl saaanapaan gssakitvsg
      121 dgnsrtlrvt vkaaaapppp qtqtvqsisg kvvvqadska vpnavvmlld stgkrfdtts
      181 dgsgnfrftg ttsapiapgr idlgatfdnv qarktltaaa gqaitgqris laikvevtps
      241 atpsatadat psedpadaga gdqatdeasp gapanasnsd dggsgpylii llggllvaag
      301 vgtivmlwmk rresggdddd apaaaggggv vppsrgafrs pddqtrmvgg rpgggadptm
      361 vggaalseap tmmhrpvvdd vppdpygapa qayggagqqg wggagygdeq apggygaggy
      421 gnapasgggy gnapasgggy gtpagseggy gagegygaap gsgagyggga papaggygna
      481 pgsgagygna pasgagygna pgsgagygna pasgggygsr dyngpagtaa yppapaggap
      541 ygerydeptg rytgdntqyp apadpyatgv yqpeqgqgyg gqpdsapygg raaeptagyg
      601 gqqaggydqg gyggqpaggy dqggtygqep ppqqrggydd rgydqggygg qpaggydqgg
      661 tygqepppqq rggyddrgyd qggygqppag rarpetppqt drggrrldwl dd
//
LOCUS       WP_357525785             513 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357525785
VERSION     WP_357525785.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 513)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..513
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56370
     Region          86..485
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvsadp rqqppgatst epplagpngr hhqsvpmpqp tptatpppas tprprmdfqv
       61 vrelrrelte rltlwqrgre ftvdeedter arlavmvvaa yadfvrragt pmaageerll
      121 ldqvtaelvg lgrlqtllvd dtieevhilg cdqvriarhg ggvdwaepia dsdaelveil
      181 qaaarragat erslstvkpt ldlqlpdgsr laavflvshr pyavirkhnt ldvslddiag
      241 argdldemid pllrdflraa mraglnimva glagagktti iralmneipp depyvllees
      301 rellparrre rhravmsfea reghgergfd grpagevtia dliplslrmg vlriivgevr
      361 sreivpmlqa mttsrgsmct ihartaagvg erivelalah gremtvdqar rmagnaldli
      421 vyvtvedeta iggrkhrfvs hveevigpge agrittttvf gpgpdgravp rhlpervrdq
      481 llrvgydarl ltrwveagag awrrprqtrl arr
//
LOCUS       WP_357525822             310 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357525822
VERSION     WP_357525822.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   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 310)
  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..310
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..310
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33926
     Region          21..310
                     /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 mtdqrggvvd escvltegpw thrfvgangt rfhvveagtg pmvlflhgfp ehwwawhrml
       61 pavadagfra vavdlrgyga sdkpprgydg ytlaadiagl iralgerstt ivgsgvggmv
      121 gwtvasfhpp lvrrlvvlga phplrlragi fadprgqfaa stpalkfqlp ryehvltrdg
      181 aaavaeilrr wggphwvtgp dfdayaercr eamcipqaaf calegyrwaf rsllrlhgyr
      241 fvrlmqkpla tptlqlhgal dpaslprtal gsgryvvapy ewrlldgvgh fphleapelv
      301 lgeilrwaks
//
LOCUS       WP_357525860             390 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Polymorphospora rubra].
ACCESSION   WP_357525860
VERSION     WP_357525860.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=40333
     Region          1..390
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mrdavivgav rtpvgrrkgg lsgvhpvdls atvlralaer tgldpadved vvwgcvsqvg
       61 eqswnvgrnv vlaagwpeav pgttldrqcg ssqqalhfaa atvvsgqadl vvaggvesms
      121 rvqmgasatg glpygdqvrd ryrgvegfav depvpfnqgv gaemiaqrwg fsrtrldefa
      181 lasheraaaa qdagafdaei tpvgtpdggk vtadegirrd tsldrlaelk tpfradgvvt
      241 agsasqisdg aaalavttse warshglrpl arvhtavvaa ddpvimltap ipatakalrr
      301 agldiadigv yevneafapv plawlaetga dparlnprgg aialghplgg sgarimttml
      361 hhmrdngiry glqsmceggg manativell
//
LOCUS       WP_357525876             482 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora rubra].
ACCESSION   WP_357525876
VERSION     WP_357525876.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=51553
     Region          171..>263
                     /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          256..481
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mperpdysal iagqtvviem tnsgeagipv lthllrvaqr algaggmtfv eyrpdsgrii
       61 aatggvgwal grpvdradpt tarllrgprt dealvddlpg dlahqlagqg lrrvvsarae
      121 vgglvvgslh ayyadpvgsa ehhavlsyla vcaahmygdq aglpihgdgp vvaaladgla
      181 ivdrdgyvrl wnpaaeqvtg hsaahilnrp apfplppsgq vidhslpdgr wleitagdlp
      241 gatssrvvtf rditdqhrrd hdlfvavtsh elrtpatvik gyadtlcnhw dsltdsdrrq
      301 aarvigqrad elarlldrll atahdagpvg dappvpfdlv ealraaaldl padlrrrlvv
      361 dlrgdlpkal gdraslatvl telatnadky sppdtlielt aqadgrtvgf rvsdrgigvr
      421 pdhverafdr fwqgesgdrr rypgaglglf lvrriverqn gwvslrprdg ggtvaevrlp
      481 rg
//
LOCUS       WP_357525905             272 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome c biogenesis CcdA family protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357525905
VERSION     WP_357525905.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..272
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=28080
     Region          27..233
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mgetfrelal tgplllaiga aalaglvsfl spcvlplvpg ylsyvtglag adlegrrpaa
       61 epppptggva vkervarvga vkgrvlagtl lfiggftvvf vatailfasi grvffdykre
      121 lqigvgvlii vaglsylgmi palqrefris rlpsagllga pvfgavfals wvpctgptlg
      181 avmgmatasg qsdravvlav ayclglgipf ivfglgferl lgvfravrrn srwvtrvgga
      241 lliliglalv tggwqsfviw lqttvgvgev si
//
LOCUS       WP_357525953             268 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357525953
VERSION     WP_357525953.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 268)
  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..268
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..268
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29167
     Region          1..264
                     /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 mpvsyldrge griayevtgt gplvvclpgm gdlrsvyrft vpalvdagyr vatvdlrghg
       61 dsddgfsrhd dvalgtdlla lveelggpav vlgnsmgaga avwaaaeapd riaglvllgp
      121 fvrdpdlnpa mnlafrlllt kpwgpaawhw yyqkfypgrp padltghrar ireslrrgdh
      181 wrsfvkttrt shrpaeqrld svhaptlvvm gtkdpdfpdp aaearfvaer lrgelllvpd
      241 aghypmaeyp emvnpelvrf lgtvhada
//
LOCUS       WP_357525970             890 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Polymorphospora rubra].
ACCESSION   WP_357525970
VERSION     WP_357525970.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 890)
  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..890
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..890
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=92760
     Region          31..887
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtlsdhddcd pseqstdpsa qgrdeggagf dellrqrrla agltqadlaa ragigvrtvr
       61 dlergrssrp qrttvallgt algltgsdrd aflvaargat alpvgaaaae paggtpgaap
      121 avadtaprtf glpapvqlig rdadvaeiad litagpaagi vnlvglagvg ktglalavga
      181 rlgpahpggv agiviteess agevlaaiat vfgvgrsadl aarlagaqal lvvdaverap
      241 davaeilrsl aasaptlril atgrhpvgvp gervwpvapl evppaeagad lasvarypaa
      301 alflarlrqv rrdpldpgev saladlvrrl gglplalela aargrvldln emldrygdrv
      361 ldlasrpatr eavavnlrda vaasyrllep geqaalrrls mfrnrwsvel aeamladvpg
      421 pdgdpvgtsd qvplldrlva lgllsvrgsg pyrfrlldvv rdfaveqaaa vgettsirrr
      481 hamifarlag riageltgan lpagvgrlde vssdlsaala hsanddphta lflasrlprw
      541 wrfrgrdvag rqwlrrvldd prtsdadptt rawakvglgq laaehhagrq elpaveeala
      601 tfqqlgdvag elaahtilcr vwtaaggydr arrhgeavla lasrtsrvrd mavaqnnltw
      661 heirvgdlra arrrlaavdq laaqcgddrl raltvanlae varldgryad avtlgrrasa
      721 aladlgdpgh rrrvlgtvgl alaqdgrlde aaavlaelra rpagavaepc padepdpsai
      781 relppgygac asieatmalr rgdrelaaew yavaartyat ghdlrdvaea lvglvattdd
      841 ppertavrdr laavcveggi tllpgervli rssgavpsaq rrtgapagtq
//
LOCUS       WP_357525980             293 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357525980
VERSION     WP_357525980.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   Wintjens,R. and Rooman,M.
  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 293)
  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..293
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32423
     Region          14..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          99..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mterrsptvr rrrlgaelrr rredagvtie mvaerldcss skisrietgh tsatprdvad
       61 mlaiygvvgp egeelvqiar earqkgwwhp ystvltgayv gleaaahsvr ayeqqvvpgl
      121 lqtgdyakam irsarpdita eeverrvrvr lqrqslltqd dpievwvvld eavvsrpvgg
      181 devmraqlar lveaadlpnv tlqilpfevg ahagmdgtft ildfaeardp gvvyaenatg
      241 glflekaeel rkyvfifdhi raaalrpees vaaiaklaee plwrsrpkgs gwt
//
LOCUS       WP_357526004             381 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Polymorphospora
            rubra].
ACCESSION   WP_357526004
VERSION     WP_357526004.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 381)
  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..381
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..381
                     /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=40143
     Region          1..369
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mltelldrvr rilqvdvati lhldahaqql vrvavsgsvh gggvdvrvpv gqgtagrvlr
       61 drlpvvveqa epgelpgpas apalrsllav pmiagtdvig vlqvggsrpr kfssddigll
      121 qlaadratqa tqarlshldr aaalalqrsl lpprlpavpg vdlaarylpg hdtgvggdwy
      181 difslpsgwl gvvigdvagh glhaavvmgr lrsalrayel ecadpaevlt rldrkirhfe
      241 aghlataiya mlppgrdcvh lsvaghpppv lvsrdrpael lslpvdhplg fgggqsrrtt
      301 vidfpdgavl lcytdglver rgelidtgld rlraavepgp aetvcstvmt klvnrepidd
      361 ialltihrqa epgrlatgga a
//
LOCUS       WP_357526027             326 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357526027
VERSION     WP_357526027.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=34873
     Region          32..323
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msigntepsv rlaqagragg aapnsaghrh gaqprrsrgg lraerlapyi lvapavliiv
       61 vlrlyplllg vnfsftgdga qngtavgfgn yrelfhdplf rtalsnvgll vlllpvavai
      121 pgllatfiyl rvpghrfyrs vyffpavlsp vivgaifnll lafdgplnai lgsvgispvd
      181 wlgdpdlamf mvvgvhiwat fgmalvvfla gfatldpall daarvdgasl rqvvwhviip
      241 slsrtiqfvf vttmigmlts mfgllfvmts ggpegstylp eyyiwiqqgq mnrpalasaa
      301 stilfiimlv vgllqiklle rsgked
//
LOCUS       WP_357526049             231 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent F420 reductase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357526049
VERSION     WP_357526049.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..231
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23778
     Region          11..201
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mfdndrpqtl gvlgagkvgt vlarlavaag yrvlvagsgd pakialtvev lapgaaatta
       61 vdavaaadiv ilalplgkyr svpaealrgk lvvdamnyww eidgirddlt dprtssseiv
      121 qaflsgsriv kafnhmgyhd ledearpags agrkaiaiag ddatdlatva alvdalgfdp
      181 vvagrlaegv rlepgselfg anvsadevra mldrfpeser grtiaaaraa s
//
LOCUS       WP_357526054             226 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357526054
VERSION     WP_357526054.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 226)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..226
                     /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=24524
     Region          14..203
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtspasdpld lrgvrraydt vaedyatllp dtraeapvdl amvdafaeav tsggdarvld
       61 agcgpgrmsr yltdrgclvh gvdlspgmia rarrdhrdlm ftvgslsalp ypdarfagvl
      121 lwystihtpp agqarvfaea arvlrpgghl lvgfqagdgt rdlsaayrrr fgheirlarh
      181 ryppdrvaae ieaaglreec rlvrrargte rddqafllat arrvng
//
LOCUS       WP_357526055             412 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Polymorphospora rubra].
ACCESSION   WP_357526055
VERSION     WP_357526055.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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 412)
  AUTHORS   ter Beek,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..412
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..412
                     /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=43729
     Region          17..389
                     /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(129,131,255,257,292..294,337)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mtlsacgggg dsgasdtvrv tlvnhvwten irkvipqfeq etglkvevtq lgedqlsdqy
       61 nvklnagsrd idvmmyrplq egrlfaengy ladltdkaeg sadfdfadfq etpvgatshe
      121 dklvgipiit eqqvlyyrkd lleksgftap patldelkaq atkiqadnpg vagfvartgk
      181 aaavtqfssf lysfggdfvd asgkaavntp aakqayafyg gllrengpan vstdmswsea
      241 maiftqgqaa fypeanslyk natdpakskv setvgfapmp agpagskpyn ipswglavne
      301 ssenqdnawk fiewaagkaq tleqqkagvp gartsvwenp egistypadm adaitvslan
      361 gvghdrpvve rvaqareivg qpivdaitgg daaasaetan aafqkfldde ar
//
LOCUS       WP_357526102             225 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357526102
VERSION     WP_357526102.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=24650
     Region          10..216
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtasiprlpl rdelfllghd ddtghphvhr qtlalglaga vlidlylagr vildpnddtr
       61 pvshlriyph idrpvgdlia daatatirht hpllrgwlrg fsadlydrtr nglvaggilr
      121 rhtrrrfggl iradtylpth skwaviarsr lrylaagreq pdnhtaalag lvadlglthh
      181 lyldddttvl aarlkavaaq hyqpvrhita avdaavgdla tatyr
//
LOCUS       WP_357526105             303 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Polymorphospora rubra].
ACCESSION   WP_357526105
VERSION     WP_357526105.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 303)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..303
                     /product="phosphotransferase 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=33525
     Region          5..253
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mgtvetaair wvesvwrrri tatrpltggw tstvlrltaa dggdavlrlm tkepwrrhaa
       61 glltreanvq eqlgrssipv prslaldpsg aeagvpahlm sylpgqlrld rasdqvigtl
      121 adllvavhrf dpgpakprdf qswagpdkrv vprwarwpgl wewafdeldq papahvgtfl
      181 hrdfhlgnvl wtgerisgvv dwvetswgpa hldvahaaty lamlhgaapa aaftdaycrr
      241 aggrpaddel rywnvldivg ylpdpakvvq pwrdrgltig ddlarirleq rleavlahti
      301 rrp
//
LOCUS       WP_357526112             267 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357526112
VERSION     WP_357526112.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 267)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..267
                     /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]"
                     /calculated_mol_wt=28844
     Region          47..161
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mttthgdite idygamirsl nqahyagets fydtaplrtc eealyhglgt earildvgcg
       61 agrvtraita lggnvvgvdi neaaltaarv acphgtfvhg smsalplpta sfdqvwclrf
      121 sfnalateae rletlhelwr vcapggrvlv etfnwhyagr fglvrianvl dmtaravrwq
      181 gqrragsrpl pardiiylan kasgaapgya hlttatelyl lasacgirqh aivtseagvl
      241 stpsppirsr hrrysmwlvl skspeqp
//
LOCUS       WP_357526208             468 aa            linear   BCT 28-DEC-2024
DEFINITION  TldD/PmbA family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357526208
VERSION     WP_357526208.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..468
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /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=47917
     Region          8..464
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 msarsepela gqvvelvrrl ggpaaqaevv vtradlaltr fansaihqnv aestvgvrlr
       61 vhvdgrtaag sgsvvtadgl salvertlva arlcppdpgw pglapptptp dapevdeata
      121 haepdqradr vgafvaaagg lssagycrta lrssafansa ghtaygrsae aamdgiarld
      181 gadgvarrha hrlsdldgae lgaqaaakar aaadpvelpp ghyevvfepa avadllqnls
      241 wygfngkrya erqsfaepgv aqfdravtlv ddplgasglp fdaegtgrra ltlveagttq
      301 avahdrrtaa vagvestgha vaggatwgpm arnlrlsgaa agpasatgrs ttgaaagavv
      361 dadtaalvtg vrrgllvtdl wytrvldpks lvvtgltrng vwliedgtvv ravrdlrfte
      421 sypralgpga vlglgaravr qpdrvdgaww aapslrlasw hftggasg
//
LOCUS       WP_357526315             337 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357526315
VERSION     WP_357526315.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,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..337
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..337
                     /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=37296
     Region          1..332
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtenilevrd lvkhypvtqg vvfkktvgqv kavdgvsfgl ragetlgvvg esgcgkstla
       61 rvlmnlekpt sgsvmykdqd tsklsggalr rlrrqiqlvm qdpytslnpr mtvgdllgep
      121 feihpevapk gsrrakvrel ldlvglnpeh inryphqfsg gqrqrigiar alalrpeiiv
      181 cdepvsaldv siqaqvmnll eklqsefgls yvfiahdlsv vrhlsdrvav mylgkvveig
      241 tedeiyerpt hpytqallsa vpvpdptqrn nktiirltgd vpspisppsg crfrtrcwka
      301 qdicaeqvpl leirrdsdhp sachfaerre ivathea
//
LOCUS       WP_357526330             252 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Polymorphospora rubra].
ACCESSION   WP_357526330
VERSION     WP_357526330.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..252
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..252
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=27682
     Region          11..243
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mtvywaddtv tlhhgdmrdi lpalvnaglr adcalvdppy netkltwdrw pdgwpafvaa
       61 atssmwcfgs mrmfltrhae fagwqmsqdi vwekhngsgf hadrfrrvhe halhwyrgpw
      121 agihhqaptt adatartvrr ktrpphmget kdsaytsvdg gprlmrsvin vrsmhgrain
      181 gtekpvgvlt plieyacpsg glvldpmags gstaeaarat grrtvliegd eeaceaiarr
      241 lsqgvltagw pa
//
LOCUS       WP_357526340             131 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357526340
VERSION     WP_357526340.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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 131)
  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..131
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..131
                     /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=14891
     Region          4..123
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mqvidklawv hviegkilst rsygkdawyi pggkreaget dhealkreir eelcvelise
       61 siepmkvfea qahgksegvi vrmtcyrady qgdltpgsei eemswldysd reksspvdgl
      121 ifdwlrdrge l
//
LOCUS       WP_357526438             410 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora sp. NPDC049171].
ACCESSION   WP_357526438
VERSION     WP_357526438.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..410
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..410
                     /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=41992
     Region          7..319
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 msrdrtvdal rayaiggvvl ghwlvtglvl tddgglrqas pltaipglap vtwvlqtlgl
       61 ffftagfgsa rslagyrgrp ggwlvrrlrg lllptvallg vgaavllaat vagtpddtla
      121 valrlaispl wfllplvfli amtgplraav rrwglgrcvv pavavvaaad lavrllpags
      181 hlppvtvvaa wsvpyllgva hadgrlagrr aagtlaagga aalaallalg ypvsavgvpg
      241 agvsnlnpps llavalavaq vglgllarps lerllsrpvp gravtevnrc afriylshqp
      301 vlvavtalta rgglalpglh tgpddagwvl arfcwlplla avlvtvvrtg qsrsprhpag
      361 ggvadrsaec vssapqvydh rrsgppdlqe viavrdsdpp srgradgqpr
//
LOCUS       WP_357526452             273 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357526452
VERSION     WP_357526452.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=29466
     Region          6..251
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mpvheitdpd ddriadyral tdvelrtrwe pphglfiaeg elvlrralra gyparsylvd
       61 akridqladl dtgdapvyaa tqdvlqratg fhvhrgvlas fhrrplptaa evlaaarrvv
      121 iledinnhtn lgaifrgaaa lgidgvllsp tcadplyrrs vrvsmgevfa vpyakfsrwp
      181 agleevreag ftvlaltpaa dalpmqrlsp dqraraallf gaegpgltga aqsasdvrvr
      241 lpmrrgvdsl nvaaaaavaf welsrddpgf dge
//
LOCUS       WP_357526454             614 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357526454
VERSION     WP_357526454.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 614)
  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..614
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..614
                     /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=65300
     Region          7..129
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          255..609
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mfptvrevla lgpvrhgapr vvagdagldq pvrwvhvaev pdiatllggg elvlttgigl
       61 pgddaglraf igdladvgvs glvvelgrry vsgvprvmva aaerrglplv elrratpfvr
      121 iteavhaliv daqltelrat eeihqrfndl sveggdaaev irqaaelsgc pvvlenlsrq
      181 vlgydpages aellldgweq hsrrvrptgr taydpdngwl vtavgargqd wgrlllrwpa
      241 sgdvpsaqps gptagpptrl tilieraast lalgrlirrd aeglerqihr tlltalldhs
      301 rpvdevalra kalgvvldrr hlvgvmvrhr aedpvgetgp eaaqarlrdl seavgqalre
      361 akltaltsav ddnsvgalla ltdpaaedra lsafasalrr vrldagtgrp glgveparat
      421 pgsdasrsas gaessraapd adpsrppfgv eavrvgvera rgvgpgaviv aagsgvgtlr
      481 earrslvear qiaeaatrdr rdlavfrlph vglagllhll rdeprlqtfv erelgalley
      541 darhprerll dtlrtyleqg rnksagaaaa hlsrpafyer lariarildv dldsveasls
      601 lhvallalqa vrtp
//
LOCUS       WP_357526504             359 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357526504
VERSION     WP_357526504.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 359)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..359
                     /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=39189
     Region          76..357
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mefadeapkl lmllyglvaf vvvvggllll ldaipnhlar rreqrlvaas takggpggdr
       61 pagdrptraa rprrgealfa aiflfpaial lliglvvpav rttllsfmdg gsvnwvglrn
      121 ygwmfsqpei ldvlintlmw vvlvpllatg mgllyavmvd karfeaiaks lifmpmaisf
      181 vgagiiwkfv yayrseeqeq igllnqiavs lggepkqwll nsplntllli avmvwiqagf
      241 amvvlsaaik aipaeiveaa rldgvnawqm frrvtlpsir palivvvvti siatlkvfdi
      301 vrtmtngnfn tsvianemyn qafrfgqvgq gsalavflfv lvipiviyqi rnlrqqreg
//
LOCUS       WP_357526513             116 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357526513
VERSION     WP_357526513.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     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=12673
     Region          1..99
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mstvvddelw saigdptrrt midlllsdgp gtatslsrrl pvtrqavakh lavldrvgli
       61 haepagrerh yqvdeaqlar avaqlsavgs swdarlrrik riaeaiersr htnegd
//
LOCUS       WP_357526533             473 aa            linear   BCT 28-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Micromonospora sp.
            NPDC049171].
ACCESSION   WP_357526533
VERSION     WP_357526533.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 473)
  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 473)
  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..473
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..473
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48742
     Region          1..413
                     /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 mavhrlvtst aanllipvsg llvspflsre lgpegrglya altlpivicg wlgtfglqda
       61 ltfhlrqrrl srrdaarvsl vaalplglva vlllgvlgfl vfdraevdrq qflvlallap
      121 lhimanlaig altgdsdigg vnlmkvvpag lrtillviac vtvdlsafwa aalfltatas
      181 gvlvglprlr rrakppsrtg ptepaesadr sgptdraept draepipvrs lirysltclp
      241 gvlaatssar ldqviglpll garelgfyav avsvaelptv iataartvlm ggaggddnes
      301 vlrvarvavp vaalgcavla asagllvprf fgaafapatl ptvilcaatv vftcvqifsa
      361 lllvndkaar ssvalvvgsl tgvlllvvla pqgavgaala sligyavaag iaarsvrrlp
      421 avpslravtv pyaadlrhlh awlrrwwrar ragppeagda aqaqsagtgg gvr
//
LOCUS       WP_357526627             328 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Polymorphospora rubra].
ACCESSION   WP_357526627
VERSION     WP_357526627.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 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   5  (residues 1 to 328)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..328
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..328
                     /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=35090
     Region          4..240
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          255..318
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlrihftvad lnrtrvatap dplwelalsm hqlrrrgspp llagwksdla drlrpdttlr
       61 revalalaln pptgyfpdfl tpaeaaggfe aglqallntp rhrlraeial ldtaahrldp
      121 dalrvgdgdp galrvlgral rryhdvavap vwdrirasfd adralrartv ldggavalln
      181 glhpavrftd gvleianyra trdlyldgrg lvlvpsffka asrpmalvdp dlppvlvypv
      241 ersarivtev grtslaallg rtraavlela adnpstgtva grlgisapaa sehltvlrda
      301 glvvstrhgn tvrhtlaplg rtligggs
//
LOCUS       WP_357526630             577 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049171].
ACCESSION   WP_357526630
VERSION     WP_357526630.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049171
  ORGANISM  Micromonospora sp. NPDC049171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 577)
  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 577)
  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 577)
  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 577)
  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 577)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 577)
  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..577
                     /organism="Micromonospora sp. NPDC049171"
                     /db_xref="taxon:3155770"
     Protein         1..577
                     /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=62730
     Region          15..515
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mkpviggwsl rrrvitlltv vglllialaa aeatmaarnr tqidavlnet gplrvqsqel
       61 lnalldqeta irgyavsgdq ddlnpyregl aqeksvvvsm rallddypqi sqelriveer
      121 taqwrqsvae pvitttersg tsagqalvte rarqqfdevr tavndlqeev laareqtadn
      181 vrtssnvlvv llivaalvvv vagavlllsl drmvvrpltg latqvrevae gdyqhriatt
      241 gppefiqlgd dvdamrqkia adlaevraar eriewvnsql qkqaeeltrs nrdleqfayv
      301 ashdlqeplr kvasfcqllq rryagqlder adqyiafavd gaqrmqrlin dllafsrigr
      361 lttgfvevdl nkvmgdvagq teaarqyada eltwtdlpvi sgeeplltnl lanlvsnaik
      421 frradvapav hvsarlvgse weiscrdngi giepefadki fvifqrlhsk daypgtgigl
      481 aivkkiveyh ggrvwvdtsv pegtairftl palpgdleaa aaadsseqqs altagdatps
      541 neapaapteq sggsdrpdra dgspeggrtg dmretvg
//
LOCUS       WP_357526703            1522 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Polymorphospora rubra].
ACCESSION   WP_357526703
VERSION     WP_357526703.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13483049
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1522
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..1522
                     /product="non-ribosomal peptide synthetase"
                     /calculated_mol_wt=160298
     Region          35..>1113
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          1174..1422
                     /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 mtastdqlla vllarrgiev aatqairpgd rtgdlplspa qqriwfldrl gvgdstylmg
       61 tahrltgpvd pdalagalrl lvrrheplrt rftdrdghpv qrivdaddpr vavrlpvvdl
      121 gdlpaatret rlrrlarhel grpfdlrtpp lvraalvrla addhvllltf hhivcddvsa
      181 rllaaeltrt yaalaagrpa dlpplpvqya dyvrwlgerd pgvvagqeay wrerlagapa
      241 hldlptdrpr perprspags hpfrlsgrlt aavealrqre dcttftvllt afkivlarhs
      301 gqddlvvgvp aanrslpele smvgmfvntl alrtdlrgdp tlrevlrrvr qtslgglghr
      361 dvplervael vrpdrgagrq plfqvmfvln sgddrpgsgp aatgadpapg gtgggltvtp
      421 aglaggtarf dltllvvdga gplagqldyd aelftpatva rlaahlelal taladtpdlr
      481 lrdlalhtpg dlellrsglr paagpepttp tgyvddliaa qaartphapa vagdgpelty
      541 gelvgradrl arrlraagvg adtpvgmalr agpdgvvall aiiraggayl pldpghpvdr
      601 igalladaga tilvtdaagr drlaglpatv vdvagtadrg gdpdgvparr pdqlayvvyt
      661 sgstgrpkgv mvshrtltal atsfrdvhgf gpgqrilmip pltfdasvgd vfpalisgaa
      721 llvhpdpaal tgpalldlcv aqritavdap aalwqrwvdd lagdprqvpa dlpltlmmvg
      781 gervsadkle twhrltggrt afynhygpte atvcatvlrs egpadgyvpg ghlpvgrplp
      841 hvrayvldrr mrpapygaag elylggdcla rgylgrpdls atafvadpfa aapgarlyrt
      901 gdlarvgsdg qleflgrvdr qlkirghrie paeieavldg hpavarsvvv argqrlaafv
      961 vpggavpggp apggtvpgga vpggavptad dlraflrarl peylvpatft aldrlpltah
     1021 gkvdherlpv evadtppfva prtpaevava gvwsralgrd rvgvadgffd lgghsllaap
     1081 vlsevnrrfg trlplralfe aprldafaal vdaavaeagg vdaggagtgg vaaapaaapa
     1141 apvrrrgglr aeaelpddvr pagaytpaad pagvlltgat gflgaylldd alrhttadvy
     1201 clvraasdga avarieanlr rygrwrpaya arivpvtgdl aeprlgldpg gfdaladrvd
     1261 vvlhnggvvh fvqpygrlap anvagtvevl rlasrgrpka vhhvstlgvy lcpayasrtv
     1321 teavppdepd glyggynesk wvadrlvrta rerglpvsvh rparitgdsr tgagndddwf
     1381 srllrtfvev aavpelgyde dmapvdlvaa tigglsrrpe alagdrhyyt pglsypaiae
     1441 vlrdlgrpvr llpyrdwrae vvragagval gpfvptlpet dgprdhpvfd cadtrrsaaa
     1501 agiptpptpd tllrtylntl ls
//
LOCUS       WP_357526706             245 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357526706
VERSION     WP_357526706.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   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 245)
  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..245
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..245
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24912
     Region          9..241
                     /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 mvdevgdrdg drvllllhgm gatgavwegw rtplasgwpg rwlapdlpgh graaplagyp
       61 ypavaaqvaa glgpgdrvvv lghsyggvvg lalaasgvgv eavvtlgvkv twtpdelarm
      121 aalagrpatw fpsraeaaar ylrvsglagl vdeadpvvda glvardgrwr lamdpaafav
      181 dapdmpglla gcrapvllar gehdpmvgda elaalgvpta slaglghnah vedpaavldl
      241 ltpyr
//
LOCUS       WP_357526741             319 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357526741
VERSION     WP_357526741.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..319
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..319
                     /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=34356
     Region          23..315
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msistapvak tdptsatpgp sgraairtar mrqwwlaaal vfpavalavt fkfvplgrgv
       61 atslesssgf dgtsfagadn ytrmlddpmv ltsfrnallv vatlpvwvvl plvlallihq
      121 rtpgwklfra vyfipytiap ivvgimfrqi lapegplnag lravgldpla tewlngrysa
      181 lfslvavalw sffglgvmty laglatipge vleaayldga gfwrrlvsvv vpmlrptvay
      241 wtvlcasgvl iwlfpliyal tqggpgdatm lpeylvfltt fqfldrgygs aigvalfvfv
      301 alisvfsvrh mfkegtrka
//
LOCUS       WP_357526822             445 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Polymorphospora rubra].
ACCESSION   WP_357526822
VERSION     WP_357526822.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 445)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..445
                     /product="phosphotransferase 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=46331
     Region          <187..356
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mprtvnlvlv dpggrplgal apfdapdpww qdvadvvaaa rdrhrvevtv lrlltadrpa
       61 ppggtvtyla qvdtvpdgll pvpdtvdlap hprrapwaep ggpgrtlrwa rgrldrlgrg
      121 ayrpvqrraw nlsaiwrldp igtdpigtar tgtdrtgtdr tgtdrgdgag gyvgdpvwlk
      181 qvpdffahea vvlrwlggaa prlapvllga dgagrillgh vpgedrygag paerdaiaad
      241 hheiqtravp dlaalvaagl pdrrgtalaa wttgvlaahg adltpvagll dglagrlaev
      301 agcgipdtlv hgdlhpgnvr aggaagaggt ggdqrviidw gdacaghpaf dimrltegtg
      361 pataaaltrs waarwrasmp gcdpgraldl lrpvaalrma avyadflari epaehpfhtg
      421 dvphylalaa eaaglprkgr gntid
//
LOCUS       WP_357526838            1032 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Polymorphospora rubra].
ACCESSION   WP_357526838
VERSION     WP_357526838.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 1032)
  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 1032)
  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 1032)
  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 1032)
  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..1032
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..1032
                     /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=108117
     Region          8..>1031
                     /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 mttaeatyaq havwfteqag vagtayhmal gihfdgalde qalteactav tarheglsta
       61 vetdadgvph lvpatekitl aggpltddri raeiarpfdp rrgplarftl ltgaadrhll
      121 lvtahhlvfd gmskdvlard lahaydaava grpadlgpaa dhsghaaaer drvaaalpaa
      181 rdywasrwtp pgdvvlpgls rqpvaagpga tvefdldadl vagtarlatd lgvsrfelll
      241 aavhallhry gnealpvgvg lstrtaetag qiglfvnelp vpapapdatf rayacalrae
      301 lrqlyrhrdv plaqavsglr pataltpvsv gyrrrapepa ftgvattidw tvfggtarna
      361 lhvqvvdsgt gltvglqhsp dviptdavar igahlrtlla gavadpdrav delpilpdre
      421 ldlvleifng tardyaadsl parfaeqvrq rptdialvdg nreltyagld avsgrlaaal
      481 rdrgigagsl vavglhrswt avatllavlr sgaaylpvdp dlpaarqaai ladaapalvv
      541 ttattttadv aaelaggpav lpvddldtmp epagpevaad pagtdlayvl ytsgstgrpk
      601 gvrvphaala nllcamgdvl dsrptdrwla ltsmsfdisl vemflplvtg grvvvasgis
      661 aadgaavvrl veaygvtnvq atpsgwrvll aagiggddrg lvalaggevl ptalarelhd
      721 rvarvvngyg pteatiyatt eevtrgrevt igrpvanara yvldprqrpl pigvpgelvl
      781 ggagvadgyl grpeltaerf lddpydapdg rlyrtgdlar wttdgrlefl gradhqvkir
      841 ghrvelgeie trllehagva gcavtlrdgd egdsrlvgyv vpagaepdpa alrahlaqtl
      901 pavmvpatwv fldtlplnps gkldraalpv pareraepat agpgaavgag pdddapvvde
      961 vveeirtiwq dvlqiddigl dedlfdlggh sltitrissr ihqrlgvels levffempti
     1021 aeiaevvrea rg
//
LOCUS       WP_357526850             260 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357526850
VERSION     WP_357526850.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26157
     Region          1..253
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mstdndpvav vtgaaggiga avvrclardg frlalvdrpg paldalaael gsaghptlav
       61 aadvrdpaat eataervtah fggfdalvtc agigridpig ettdevwtdt latnltgtfw
      121 wcrsavprlk argggvivav ssttalvglp grtayaaaka gvlglartla vecaadrirv
      181 vavcpgatrt dlvrqgyara ddpaaaerah aalqpigrls epdeiaetia facspraati
      241 tgatlvvdgg ytaggqswnt
//
LOCUS       WP_357526885             953 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357526885
VERSION     WP_357526885.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 953)
  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 953)
  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 953)
  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 953)
  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..953
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..953
                     /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=101827
     Region          2..251
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          133..953
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mriqfrvlgp ltaeldgepv dlggrrprmv lasliaaqgr vlstdrlveq vwndgppptt
       61 atlfsyvaal rralepdraa rtparvlvre gtgyairvpp etidaerftg lvtagdrqld
      121 rgdpngales lsdalalwrg qaygdfvdap ftvpevarle slravareqr laamlavgeh
      181 staigeleal vidhplrerg wellavalyr agrqgdalav lrqarerlaa dlgsdpgpgl
      241 lrvqaailnq deslgqpvgd vaaprrhtgv alpasrnvsa ahssfvgrta dlatlsglla
      301 ahrlttvtgp ggigktrlvl evcreradad gpwvvelagl reptlvaqtv adtigipghp
      361 spaelatvla erdmvlvldn aehllpavae lartllgrcp airllvttrq plavageavf
      421 evlplpseea vellvqrias vvpgtrsagv drttarqvcr eldglplaie laaaqsrals
      481 lreiafqldd rftlldtghg dghrhstlen tigwsynllt eaeqclfrql svfdggfdld
      541 avrlvgadpr vpqvvpalig lvrkslvtsd tetvprryrm lesvrlyaat llrdgelraa
      601 qerhrnwllg ivetgeqrlp tadgaswlir lglerdnira avasaldagn alcaaricga
      661 lawfwyrtgq ideglrwsrr tlaalddgsp padadqgewt lararllmav ggvsylageh
      721 aaairalrts adlcqrvgar dahttaviyl asvtaisgdi vsalpladqa vqlaeevnrp
      781 walaealtvr aqlsractdl praraelara neiarscghr walmsadwvd skvsvdlgmp
      841 grardtltar llesdpaadr sswlatahsl agalgrtgrp evgavllgav aslgtpigyf
      901 permdpfdsp gdtaavraal ddrafeagla rgrqlgwgel veligsiagp arr
//
LOCUS       WP_357526887             308 aa            linear   BCT 28-DEC-2024
DEFINITION  1-phosphofructokinase family hexose kinase [Polymorphospora rubra].
ACCESSION   WP_357526887
VERSION     WP_357526887.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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..308
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..308
                     /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=31633
     Region          24..301
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mtghvmvfap aplltvtieq qadavelhlh pggqgvwqar miaalgvpat lcvavggevg
       61 avlravlaae nvevravtrq agsgwsvhdr rdgnrtgiae hpgepmvrhd idelysvtla
      121 eglrapvsvl sgpadptvvd pdvyrrlaad ltangskvva dlsgpylaav ldggvafvkv
      181 sheelvadgr agddsvdelv aaahqlrkdg agtvlvsrad apalalldde vtevhvprlq
      241 vvdhrgagds msagvaavla rggdleqavr tgaaagalnv trhglgtgra etieeligrv
      301 rlapldrg
//
LOCUS       WP_357526937             412 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Polymorphospora rubra].
ACCESSION   WP_357526937
VERSION     WP_357526937.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=44001
     Region          1..405
                     /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 mayllgvvlf alailvsvsl heaghmltak kfgmkvsryf vgfgptifsf rrgeteyglk
       61 aiplggfcki vgmtpqdddv epgdehrvmw rypvwqrtiv maagsathfm laivalwlaa
      121 mfmglpnkal agplpahvki tdcvvvanes reclpsdpag parqaglldd dkitsingtp
      181 vatytdlvnv vralppgqat igyerngvsg qvtadlaavq rtpldnpega avtvsalgva
      241 gpvpppgvpl mvtygpieai gatadytgdm aigtvqamqr ipekipalwa aitgdqrdrd
      301 tpisvvgasr lggeavenda weifvllfis lnffvgvfnl lpllpldggh iaiawfervr
      361 swffarlgkp dpgrvdyfkl mpvtyvvilv ggaftlltvt advinpitlf sr
//
LOCUS       WP_357526959             366 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357526959
VERSION     WP_357526959.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 366)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..366
                     /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=40310
     Region          12..351
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpdvsgtkrr errrpgsgir gneavagwlf vapvvvilgl flllpilmal wvsltdwngq
       61 gspfragvpf vgvdnytrlf aedglarrdf mtairnnlyy vaivvpvqtv lalflalvvn
      121 rrmlkgrsff rtafyfpsvt ssvaisvvfl flfansgavn gllallgidg pawfsdargv
      181 lhillggfgv dsapaaltgg gpfgltwwdw lsgpsvamca iialvvwtts gtfmlmflaa
      241 lqgvpealee astldgagrw qrlryvtlpm ikptlflvlt lgligtwqvf dqiyvmsqgn
      301 pakttltpay lsyrtafrdf eygsgaaisf vlfliiivlt lvqrrvlrer dgdrprwfrr
      361 raerrs
//
LOCUS       WP_357527015             288 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Polymorphospora
            rubra].
ACCESSION   WP_357527015
VERSION     WP_357527015.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..288
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..288
                     /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=29833
     Region          4..280
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mdpvarsyly vpadreklla kahgrgadal vldledavtp ankdtaraaa aaylaappag
       61 rfwvrinsdr veqdvaavag paltgvwvpk aepellatvd aalsaaerrl gladrtfgvv
      121 alietargvl rleeitsapr vlrlglgead lageigvqpg pdgaelapir sqvvvasaaa
      181 gitapvgpve tvlrdpdrla gttrallrqg frartavhpd qlatinevft psaaeiaaar
      241 evvdalaaae rqgtgiatqa sgqmldravv raarevlrra vpegpard
//
LOCUS       WP_357527029             292 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357527029
VERSION     WP_357527029.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   2  (residues 1 to 292)
  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..292
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..292
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30871
     Region          26..292
                     /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 mtitipdfey rrvpvapgvs lntavggsgs pvvllhgfpq thlmwrhvaa alaadhtvic
       61 pdlrgygdsd kpagddpaty akrtmaadvv alaatlgydr falaghdrga lvafragldh
      121 paavshlacl dvvptldtwq vlhgvsasva fhlylmaqpp glpetmians adaffghfld
      181 awgtgsdavp advraeylra saaavpsiva dyrasatvdi dddradldag nrlrmpvtvv
      241 qqdwgarlgy dagavwrawa pdlehrttta ghfmaeeapd diakaisell ar
//
LOCUS       WP_357527032             544 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357527032
VERSION     WP_357527032.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 544)
  AUTHORS   ter Beek,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 544)
  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 544)
  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 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..544
                     /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=53373
     Region          2..543
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 msaltgtgrl arlalrrdri vlpvwivgvp avglavaasv adlyggeadr layagttavs
       61 vvarafngpt sgaslgavvv aetftslavl valmttftvv rhtrqneetg rfeltgsamv
      121 grhaplaaal gvavgadlli gagvaaalvg iglpvtgala ygtalagvga afaavaavta
      181 qvfstsraan saaavavgva fglravgdal gtvdagglrv tsawpswlsp lgwanqvrpf
      241 dadhwavlal paafsvaava vaavlverrd agtglvaprp gparagvglr taaglawrlh
      301 rggllgwaig lavlgvamga vadevdalvg dnagladaia qlggtgglvd aflatimsiv
      361 almvagyavq avlrahaees agrleavaag avsrfrwlag hlvcaaggvl lllaltgatv
      421 gfaygatvad tagiagetar mtgaalaqap avfvlagavv avfgllprws aavawaalal
      481 calagqfgav ldlptavvna spfshvpavp addvtagpll allavaagll avgmvafrrr
      541 dlal
//
LOCUS       WP_357527099             242 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Polymorphospora rubra].
ACCESSION   WP_357527099
VERSION     WP_357527099.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..242
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25765
     Region          3..235
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mriqvdhlsk rhrgkyaird vsftaepgrv tgflgpngag ksstlrillg ldradagral
       61 fdgveyrrlr nplctvgsll dgsgahrsrt arahlswvar sngipkrrvd evlettglae
      121 aarrpvglfs lgmgqrlgla aallgepevl vldepvngld pdgirwvrtf lrryaadgrt
      181 vllsshlmge madtaddlvv isagrivtrg pletvtagha sledaffalt dagaahrsgr
      241 gg
//
LOCUS       WP_357527187             342 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Polymorphospora rubra].
ACCESSION   WP_357527187
VERSION     WP_357527187.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..342
                     /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=36275
     Region          1..337
                     /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 mkalvlqddr slrlthrrqp qvtapddvvv rvaqtgfcgt drgvllgrfp avpgvvmghe
       61 avgevvevga gvttlrpgdr vaanptlycg lcswcrrgal nfclhkagne igidrdgafa
      121 eylrleerfl hplpsgmsyd ravlveplac vmnnleaarl rtadevvvlg ggpigvlval
      181 ladhagarar laepdpyrra aaqtyfagip gcavtvtepd riaarsaslv vdtvgalldr
      241 acdiadnlgr vvvmgfhdka tatlrpldvl qrgltvigag dynslifvra velarhlple
      301 givthhvrld dftdaldtlg iapgaprpyt gmkvvittgg gr
//
LOCUS       WP_357527201             455 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Polymorphospora rubra].
ACCESSION   WP_357527201
VERSION     WP_357527201.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..455
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..455
                     /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=48804
     Region          27..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 mgkgilerls lvpfggrlpt ladrfdsran sigalrlvla favlvahcwp lvlgrsmlgs
       61 aesmrqtdvg klavygffvl sgflitgsal rfslprylwh ralrvlpglw vcllatalvm
      121 apavayyerg nldgfwnhpd gplqylwanw tlamdqwtis giladvpygr glegggpvng
      181 slwslryevl cyimlaalva asvlarapga vvllllgtyw vivedfgrgd glivrppkhg
      241 elgpypvvgt fdkqlviyla flfllgavak lyahrvpmtg wlaavaligl agtlrfgafy
      301 vvglpllayl llylavglpr slhpigrkrd ysygiyiyaf pvqqvlamli gvqygfvtyl
      361 aattagtlll aalswhlver pamllkdmal plparwrrpg ggspttgpdv taakaaalrp
      421 dptapipvta psaavtmsaa svievpvgev tglpr
//
LOCUS       WP_357527253             289 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357527253
VERSION     WP_357527253.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   2  (residues 1 to 289)
  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..289
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..289
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31514
     Region          11..289
                     /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 mggeripgsf teqtaqvgdv ainyvrggrg rtvvllhgyp qtwymwrkvl pelaehytvi
       61 apdlrgaggs dapaggydkk tlagdvygll aqlglddevs vvghdigtmv ayayaaahrd
      121 hvrrlvltea pipdqslyqa psltpngpgf wnfgffslpn glpeqivdgr ealwvdrftd
      181 smevqktgid dddvreyarh lqddahlras fdyfralpqd vadnaehgkt kltmpvlalg
      241 araslgeavp tqvaqyattv tggviedsgh wifeeqptel taqlmeflq
//
LOCUS       WP_357527258             456 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Polymorphospora rubra].
ACCESSION   WP_357527258
VERSION     WP_357527258.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 456)
  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 456)
  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..456
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..456
                     /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=50444
     Region          35..380
                     /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 mptdiplvap sdahpvvivg agpaglaaar avltrgipyi hlerhvdvgg iwdldnpgtp
       61 myksahfiss rdksgffdtp mpshfgdypt raqileytrg fadtyglrdr irfgtavtgv
      121 lqdeatgvwt vstdtedlka savicctgvt wdprlpevpg dfsgevrhsv tyvdpdefag
      181 krvltvglgn sgadiasdaa anadrafist rrgyhfvpkh lfgrpadsse mlpiwlkrll
      241 yrvfapivig dvrrwglpra dhrlfeshpl intqllhhlq hgditarpgi arfddsevvf
      301 tdgtreefdl vlfatgynms ipylpseyle wvggrpkmyl nafaarpglf gisyievnss
      361 aytlfdriah lvaehlddir sgpararrlr riidtetpdl sggvrfvgsd rhatyvevra
      421 yrralrrlas rmgwddleqg rfagharsdt rakats
//
LOCUS       WP_357527288             255 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357527288
VERSION     WP_357527288.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26560
     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 mtmvegplqg kvawvtgagq gvgaaiaegl aeagasvilq arrldtlqav rdrivanggt
       61 adivtgdvvd eaaadavvtl arqrwsrldi lvnnagispa lhrseqlgta twqqvintnl
      121 sgvficsraa gafmieqgtg sivnmssvhg qvgfprlaay saskggveql trtlalewaa
      181 agvrvnavap gyletqmteg lrshdqwskr lreripmgrf glprevvgav aflasdaasy
      241 vtgsvlhvdg gwtaq
//
LOCUS       WP_357527299             385 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Polymorphospora rubra].
ACCESSION   WP_357527299
VERSION     WP_357527299.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..385
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40016
     Region          1..379
                     /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 msgplagvrv lefagigpgp faamlladlg advvrvdrpe pgalsagdpr ldllnrgkrs
       61 vvvdlkhpdg aevilgladr aaiviegwrp gvaerlgigp qtvlernpgl vygrmtgwgq
      121 qgplaraagh digyiavaga lhpigrpdgp pqiplnlvgd fgggalylvv gclaalhvar
      181 ttgrgqvvda aivdgtahlt tmfagllagg awqpergrnl ldggapfydv yatadgghma
      241 vgalepqfya ellrllglad adlpaqhdva gwpvlrarla avfaertrde wtelfegtda
      301 cvapvlslae aqrhphlvar atfeehfgvr qpavaprlsr tpgvvgggpp vpgadtetvl
      361 tewglgahll rwlgsgavsr tqear
//
LOCUS       WP_357527321             400 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptidase [Polymorphospora rubra].
ACCESSION   WP_357527321
VERSION     WP_357527321.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..400
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44106
     Region          61..400
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mlqepaaryk ghrsysylep hsdyrvfela eevgrvpehd lgltgdqrar vtrlltehaa
       61 islhehpvil padvrelrty nrtarqrtgy eglarsglta vfdnfmagas cvtsengwkw
      121 ndlvyalgmr msdlykqdhv flatsladir aakqdgrlal vagleccspi eneldridil
      181 ygfgvrqlgi aysqanmlgg glserhdggl thfgrravdr mnklgiaidi shsgdqtsld
      241 vieasrvpvf ithagarsvw ntsrmkpdev iracaerggv igieaaphtt lsethkhhsi
      301 esvmdhftyc vdlvgidhvt fgpdtmfgdh vgvhntyaan yahdagnrpe hprveyvagl
      361 enpgeafgni vgwlvkhgys ddeiakvigg ntirvleqvw
//
LOCUS       WP_357527376             285 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Polymorphospora rubra].
ACCESSION   WP_357527376
VERSION     WP_357527376.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 285)
  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..285
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..285
                     /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=32466
     Region          9..252
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 maatgggslv aisdlhvvhp dnrtvvealr pgheddwliv agdvgefvad iewalrllsn
       61 rfakvvwapg nhelwtprdd pvqlrgeary rhlvelcrgl gvvtpedpyp vwdpdgdpvl
      121 vaplfllydy tfrppgtytk eqalarahet gvvctdeill hpdpyptrda wcharvreta
      181 qrltteragl ptvlinhwpl vreptrilrf pefaqwcgte rtadwhvrfe arvavyghlh
      241 iprttwydgv rfeevsvgyp rewrrrvtpp gqlrtilrsp ahqpv
//
LOCUS       WP_357527370            3649 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Polymorphospora rubra].
ACCESSION   WP_357527370
VERSION     WP_357527370.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13759389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3649
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..3649
                     /product="type I polyketide synthase"
                     /calculated_mol_wt=377262
     Region          2..30
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          32..1421
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1231..1683
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(1436..1437,1439,1460..1463,1488..1491,1515..1517,
                     1538..1539,1561..1562,1576,1603..1604)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(1539,1563,1576,1580)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          1697..1782
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1800..3204
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          3002..3464
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(3217..3218,3220,3241..3244,3269..3272,3296..3298,
                     3319..3320,3342..3343,3357,3384..3385)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(3320,3344,3357,3361)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          <3469..3647
                     /region_name="PRK06060"
                     /note="p-hydroxybenzoic acid--AMP ligase FadD22"
                     /db_xref="CDD:180374"
     Region          3483..3564
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 madeaklldy lkrvtadlhq vrqrlrevea gehepiaivs mscrfpggvr tpedlwdvva
       61 ggrdvmtpfp edrgwdldsl ydsdpdqpgt sytrhggfvh dladfdpgff aisprealam
      121 dpqqrwllet swevferagi dplslrgsrt gvfagstgqd yggvlmgaaq gleghlmtgn
      181 agsvvsgria ytfglegpav tvdtacsssl valhlagqal rqrectlavv agvtamctpa
      241 afvefarqrg lagdgrckaf aaaadgtgws egvgvlller lsdarrnghp vlavvrgsav
      301 nqdgasngls apngpsqqrv iqqalaaagl asggvdvvea hgtgtrlgdp ieaqallaty
      361 gqdrgdaapl llgsvksnig haqaaagvag vikmvmamrh gvvpptlhvd aptpevdwsa
      421 gavslvteat pwpaverarr agvssfgvsg tnahtiieqa pepeavapag prdrlpvlpv
      481 llsaraanav pgqaerwaaw lagdadlrpv dvgwssvtar svlehravvl aegrddllag
      541 lralaagsps gavvtgsgvr rgslavlfsg qgaqragmgr elyaafpvfa saldevcrhl
      601 dgllpqglre vlfaeagspq aelldqtvft qaglfaveva lfrlvesfgv vpdfvgghsi
      661 gevtaahvag vlsladacal vaargrlmqa lptgggmlav gadeaavres laglagigva
      721 avngpsavvv sgdvttlddl eafwsgkgvr trrlrvshaf hsplmepmla efravldglt
      781 faapllpvvs nvtgaladpd eirtpdywvr hvreavryad gitalqaagv gtfleigprs
      841 vltamngell tgddtvavat lrkdrpeaha llhalaelhv hgvpvtwqnw yadtgatrvd
      901 lptyafahqr ywpeggagwt gdvtavglrp arhpllgaav gvahaegflf tgrlarrthp
      961 wisdhvvfdt vllpgtgfve lalqagahvg adhvreltle aplilpetgg vdiqlwigpa
     1021 detgcrsvsl hsatdpgtdd geqawtrnas gmlastpatp gavpgwsdlt awpppdatpv
     1081 dtgdlylnla aqgydygpsf ialraawrrg edlfaelalp espaaeagay glhpvlldaa
     1141 lhtlglptpv apaggpapag ygrlpfswnd valhaagaaa arvrvthtgt dsisllladv
     1201 agapvvsvgs lvlrpvsadq lrvagggade slyrvdwvpa pvpaelpgvv savidpagsg
     1261 laaavgatga ypdlatlira mgdgtpapdv vvaslmdlad asdvpgavta athralavlq
     1321 qfladdrfag arlvlvtrga vaagpdpdvt dlagaavvgl vrsaqsenpg rfvlvdvddp
     1381 tdaaeamvrg mlgdepqlai ragvpyaarl trvpaqpepa vspfdadgtv litgatgtlg
     1441 qlmsrhlvtd hgvrhlilts rrgdaaegva elraeladlg atvtvaacdv tdraavadll
     1501 agipaahplt vvihaagvrd dgtiptltpe qvdsvlrpkv daawnlhelt aglglrafis
     1561 yssmaatagg pgqgnyaaan afldglaqhr earglaaltl awglwadrsg mttelddvhl
     1621 nrisrsgvva meaeeglalf daacrtsqaa vvparldlaa mraqfaggvv palyrglvrm
     1681 paraaavttg aslvqqlagl geadlhnall eivrgqaaav lgypdpaaie aprafselgf
     1741 dsltavemrn rlnvafgmrl patlvfdypt plalaaflat evagdpapvr ptpvtvtvdd
     1801 deplaivgma crlpggvwsp ddlwqlvagg vdaitdlptd rgwaldtlys pdpdqsgtfy
     1861 argggfltgv drfdpdffgi sprealamdp qqrlllettw etfesagldp armrgsstgv
     1921 fvgtsgqdya sllayapegt egyaltglts svisgrvayt fglegpavsl dtacssslva
     1981 lhwagqalrr gecdlalagg vmvmatptaf iefsrqrgla adgrcksfaa aadgtgwseg
     2041 vgmlllerls darrnghrvl avvrgsavnq dgasngltap ngpaqqrvir qalasarlas
     2101 gdvdvveahg tgttlgdpie ahallatygq drpaerplll gsiksnigha qaaagvagvi
     2161 kmvlamrhgl vpaslhvdep sphidwsaga vslvtearpw pavdrprraa vssfgisgtn
     2221 ahviieqade papdtgdrpt seagavangp vvwsvsarsr galagqaarl aefvqdraad
     2281 vdpaevawtl astrsvfdhr avvvggdvge laaglrglae gspvgnvvsg vagglgagpv
     2341 fvfpgqgaqs vgmasglvgt cavfdavlad cqrvlapwld vdlvsvltgd deswlervev
     2401 vqpvlfavgv alaavwkhag vtpravvghs qgeiaaacva gilsledaar vvalrsrala
     2461 vlagsgamas vdlsveqvta rldqfpgvgv aavngpstvv vsgppgpvag lvaacqadgv
     2521 rariipvdya shspavqqva eqlrtdlagv tpraggvrlv stltgdwvdp gsmgadywye
     2581 nlrrpvlfdt avrvavgagh stfvevsphp vlgmpvtail ddldtaghvl gtlrrgeddp
     2641 arlltslaaa ytiglpvdlt avlapaavte lptyafdhrr ywidmpayqv qdvaaaglhd
     2701 pghpllsaal tfpdsermvf tgrlsvrthp wlgehrvmda illpgtafve latyageqag
     2761 cprldeltll aplvlpepga lqiqltvgdr dadgrrtvql hsrpsrddad ealadaswtc
     2821 hatglvaptg pdrpvatfdl gvwpppgava vesddfysgi eatvfgygpa frglraawir
     2881 gdevfaevel pgdyrsdagr fgvhpalldg alqamsiggf lsrmgdggdt nvprlpfawt
     2941 gvslhaagat alrvrvaaag dvgvsfqigd atgapvmevd slimrrvagd tlgaarsgrh
     3001 eslfqldwpv lpvpvgpvpa agrwvalgad dlalgaacea agvrvrtdvd ldslaellag
     3061 dgeapelviv pvgpaepdrp dddatvaeqa ratthrtlaa lrawladerf aasrlalvtr
     3121 havavaaqst vdlrqapvwg llrsaqlehp grcqlidldd hpdtaavvaa alasgepqla
     3181 vragqvrtar lvrmpaevep lpggidpdgt vlvtggtgtl grilarhlvt thgvrhllla
     3241 grrgptadgv telvaeltda gaevtvaacd aanpaelaal lagvpaahpl tavvhaagvl
     3301 ddgvleamtp qridavarpk idaawhlhrl tagadlaafv lfssgaatlg sagqanyaaa
     3361 nafldalaah rrarglagis lawglwqqas gmtghlaead vrrmaeqgas glgtvqalnl
     3421 fdaawrldta tavpmrldva alraqaetgt lapmlrslvr vplrrsvdag gagtggvqlt
     3481 qrlaglagpd rmrvvldvvr sniaavlgha tadaidpgrl ftelgfdslt avdlrnrlna
     3541 lsglrlpatl vfdyptptal aeklaaevaa daapstqpif qgidavenll aaipldaqar
     3601 drftarvrdl lakasdlaag pgeapdrpdl esasddeifd fiskefgis
//
LOCUS       WP_357527402             396 aa            linear   BCT 28-DEC-2024
DEFINITION  LOG family protein [Polymorphospora rubra].
ACCESSION   WP_357527402
VERSION     WP_357527402.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..396
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42204
     Region          174..394
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 magvstpppi dvllphdnsp deiesraeld lhlragslag ltvqglrlde epvpdlapvd
       61 ltdtlfigcr fasraveadv vlrgahvvpp fralpyaihp srlytppdly agfdaagftg
      121 mydtvvydhf rahggalpei realaqrlhd havdnalahv tdawlathgp asvvgvmggh
      181 avprgtttyr laaaigwrla radrlvvtgg gpgvmeaanl gaylatrtad eltaaidlla
      241 gapdfhdhdp ytaaalavhe rftpadpldw arcgglaipt wlyghepanl fagqiakyfs
      301 nairedtilr larggivfaa gragtvqevf qaatktfyrt dgdsgpyifl drafwtetlp
      361 veallrplla lspdgdlakt vhladdvedv vqlltg
//
LOCUS       WP_357527444             194 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357527444
VERSION     WP_357527444.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..194
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20263
     Region          21..84
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
ORIGIN      
        1 mddaaqnpvp paatageyvg llrdvrrrsg ltyreisrra saaghwlpps tlatmlgrtt
       61 lprertvval ltacgtpaaa ieqwvglrrd idarvgerar rvseptipdp asldasspdp
      121 arpgarlpav epvpprppat tyratrpgpr rlrlaaivla galaggaygm llsgangsav
      181 vttdgcplvl rqsr
//
LOCUS       WP_357527433             509 aa            linear   BCT 28-DEC-2024
DEFINITION  rhamnulokinase [Polymorphospora rubra].
ACCESSION   WP_357527433
VERSION     WP_357527433.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 509)
  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 509)
  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 509)
  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..509
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..509
                     /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=53222
     Region          39..483
                     /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 mprrsdpgng ggsdlradsp aparsgpaph pggttpagva avdlgassgr vvlgqvgpdt
       61 lrltvahrfa nepvrvggtl hwdilalfre altglraagp vasigvdswa vdyglvdasg
      121 allgnpvhyr dtrtdgvleq vtrrlgaerl yattglaqlp fntlyqltaa vatpqfgaah
      181 rllmipdlia ywltgqvgae itnasttqly dvhtrtwadg lmadagiprh lfpplrepgt
      241 rigptlpgld lpgtpevvav gshdtasavv avpasgehfa yiscgtwslv gveldrpvlt
      301 easrranftn eggvdgtiry lrnvmglwpl qeclrgwggp dlaallaaaa repafrsvvd
      361 iddpaflppg dmpdriagac rrtgqptprs saavvrcivd slalahrrav hqvqelsgrh
      421 vdavhivggg arnallcqlt adacglpvla gpveataign vlvqaraaga vggdlaalrr
      481 lvrqtqrivr yepergsgaa raderrmev
//
LOCUS       WP_357527458             246 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Polymorphospora
            rubra].
ACCESSION   WP_357527458
VERSION     WP_357527458.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=26809
     Region          11..>144
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mhdadgyfgr dvaakyddpt semsdpavvg etvdvlaeia gggralelgi gtgrialpla
       61 grgvpvhgid lsramvdqmr tkpggaaidv tigdfattkv dgtfslaflv fntimnlttq
      121 eaqvacfrnv adhlepggcf iievmvpelr rlphgqnivp yeasptgway dvydvatqst
      181 tsnyvrivdg vgsyrsipfr yvwpseldlm aqlaglrlrd rwdgwnrqpf thesrqhvsv
      241 wekpia
//
LOCUS       WP_357527477             422 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357527477
VERSION     WP_357527477.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=44057
     Region          4..360
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkqralwsaa lvvglvtmag cgsaggpgns sggsadklvv wdwksgeasa aqyldkakad
       61 farkhpgvsv efvaqpfdqy ytllgaaiqa gkgpdvmlfn gggqirdrvd alvpldeqva
      121 edkqrlagwd aftadgktya apvtlqghpi yynkalytka gldpatpatt wdrfladcaa
      181 itragakcfa lgnkegagiq fwlsalgsgi ltaqeyddwi agkrdwnspn vkrvfalwqe
      241 agaaglnndg anstamfnds faifqsgkaa hiiglmsdvg hwkdfneflt pdnlgvmsap
      301 vvtegttpsl aydggigyav akwtkdpeva adlvrsltst ealkafyada gaiaadttid
      361 vsqggpavag ivaelrggkp alhvalsskt idlmgrlsqq llsgsitvde vvkqlaasdq
      421 ag
//
LOCUS       WP_357527516             161 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC047134].
ACCESSION   WP_357527516
VERSION     WP_357527516.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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..161
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..161
                     /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=17823
     Region          1..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpeeprwltd herdawlala klmfnlpgal daqllrdnhl tlfdyfvlsv lsmtpgrtmr
       61 lsdlanhlsc slsrlsnvvk rleqrgllrr apdpdspryt iaaltdagwd lvvaaapghv
      121 aavrhyvidg ltpsqidalr evachvtrqi sqtsetgprp h
//
LOCUS       WP_357527518             213 aa            linear   BCT 28-DEC-2024
DEFINITION  FMN-dependent NADH-azoreductase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357527518
VERSION     WP_357527518.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 213)
  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..213
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..213
                     /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=22568
     Region          1..208
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mtlfrldasi rshgsasrei adlveqewla thpgdtvtrr higvdtlpst lwaaalsagm
       61 tpteehtaeq reavalaaal vdellaadal lfavplynyg vsqhfktyvd vvfadprvtg
      121 qsflagkpav latvrggayg agtpregwdh stpylrriia dcwgadltvi ereftlvgvn
      181 paldsftdta aqmhagalqs arevgkalga gra
//
LOCUS       WP_357527568             289 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357527568
VERSION     WP_357527568.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 289)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..289
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30054
     Region          26..285
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mttsttflgl gamgsalaaa aldaghpttv wnrtphrara lgergatvad avekavagdg
       61 vivvclfdrp svhdvldpva dglrgrtvin lttttpdear eiaawaeerg vtyldgaima
      121 vpemiggpgs eifysgagtv feehrplldl wgastyfgpd aglaalydva mlagmytvfa
      181 gfvhgaalvg aegvsatrfa erqmpfltam vgqlaglaat vdaadytgag qqslrfteta
      241 ldtlmrastd qgvdpavlkp vhdivrrqia agfgghgtar mfeelrstr
//
LOCUS       WP_357527571             133 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Polymorphospora
            rubra].
ACCESSION   WP_357527571
VERSION     WP_357527571.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..133
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14561
     Region          10..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maskarrgpy icgidaamdv vsgkwkslil welhnhgtrr fgelrrglpg vsekmliqhl
       61 remeedglis revyrevppr veyaltghgr slnaalralg dwgterrerl aaegdlgsar
      121 paadallqsg gns
//
LOCUS       WP_357527613             270 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Polymorphospora
            rubra].
ACCESSION   WP_357527613
VERSION     WP_357527613.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=28814
     Region          10..244
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtgpdpssst ilvtcaagri gtllrhafag rhtvrchdtv apayrlagee wthgdvadad
       61 rlaaaadgvd sivhlaadad peapwdrlhg pnvagvravy etavrtgvrs vvfasshhas
      121 ggydrdrtpg veatwpprpc crygvtkvfg ealgrhhadv dglsvtclri gefagrptde
      181 lslriwvspd dlvrafraal ttdqrygvhl issantrslw rtadsnrqlg yaprddaeay
      241 aadvgpggpr hpcfrrpadp pttpdgagrr
//
LOCUS       WP_357527646             193 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357527646
VERSION     WP_357527646.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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..193
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..193
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20286
     Region          7..183
                     /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 mtatlgalaw lavvvlfgav vpvvptgaav sgaaalaayq dplivllvvl agaigaylgd
       61 lavylalrwg geriarrlrw lrgpqrldrv sarvreagvs lflvsrlipg grlpvllaaa
      121 vsgvtwrrfa vlnlpasllw salyaaigvl gravfpepwq sviaaivlvl lvsqvlgwwg
      181 rrrpvpvqpp atp
//
LOCUS       WP_357527701             134 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357527701
VERSION     WP_357527701.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..134
                     /product="PadR 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=14177
     Region          1..100
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mstplreptf liltalargp mhgygiigev aelsggrlam rpgtlygald rltdeglvaa
       61 dreevvdgrl rryyrltdag getlateter lrrnveaata rlrdraaadr atgdraaghr
      121 papgrnplaa ggia
//
LOCUS       WP_357527704             255 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357527704
VERSION     WP_357527704.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 255)
  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..255
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..255
                     /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=26743
     Region          4..248
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mtdtataqaa kllgrarrvv vftgagmsae sgvptfrdal tglwqrydpq elatpeafea
       61 dpalvwgwye wrraivaraq phpghlavaa ieahvphtll vtqnvddlhe ragstdplhl
      121 hgslfasrcs acahpaptpp addptegrrl ppprcdrcsa pvrpgvvwfg eglpqsalea
      181 aaeaaascev lltvgtsglv ypaaeiphva arsgatviqi npeptpldpv ceinlrgpaa
      241 rvlpalveaa wgdag
//
LOCUS       WP_357527714             275 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357527714
VERSION     WP_357527714.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..275
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..275
                     /product="YybH family protein"
                     /calculated_mol_wt=30372
     Region          1..127
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
     Region          135..263
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 matdeeqirt lierwvaavh rgdldavlad haedivmfdv pppqqgvrgl aayrqswppf
       61 frwqaqgasf eieslevtag gevafayall rcgtaadlaa apdrrlrltl glrrqdgrwv
      121 vthehhsfpl dtavrdpaad erelrelhqr wfaataaqdl dalmepiapd ivsyehdgpl
      181 qyvgapavre vcqagldaaa dgkvtweipn qtiliagdla vswglnrirv tppdgestet
      241 wsrgtriftr ragtwrlthq hlshplpppp parng
//
LOCUS       WP_357527719             137 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Polymorphospora rubra].
ACCESSION   WP_357527719
VERSION     WP_357527719.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=15189
     Region          10..129
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mgteagpavi dklawlrved grilstrsyg kdtyylpggk reagetdhea lsrevaeelr
       61 velvdgtief agifeapahg hpdgvtvrmt cyradyrgdl epgaeieeir wldhsgrels
      121 stvdklifdw lrgrgel
//
LOCUS       WP_357527728             176 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357527728
VERSION     WP_357527728.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 176)
  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..176
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..176
                     /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=19257
     Region          4..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrvdkarnrd mvlaaaarlf heathpdevs mdavaaaagv gkgtifrgfg drrglllaly
       61 qehidrelta pvaeetpaqt alelltrtwr fkqrhriltl aleregsgsp yqnsgytqlh
      121 aqltdlvgqa rgtdnaafla haliaavrsd liehlrnhpe idaeaglrel vydvlg
//
LOCUS       WP_357527788             301 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Polymorphospora rubra].
ACCESSION   WP_357527788
VERSION     WP_357527788.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..301
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..301
                     /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=31929
     Region          6..298
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mgataqprrv avvahakktl dggldelrrl iaaedvdell wyevpksrka pkkarkavra
       61 gaelvfvwgg dgtvqrcvda lagtgttvai vpagtanlla snldiprdla eavrigfhgd
      121 rraldagrvn gehfavmaga gfdaamigea drdlkdrvgr layvwtglrh mrdgavgvri
      181 rtdgadwfdg rascvllgnv stitggieaf deaepddgwl evgvatadga vqwartlgrm
      241 aagrsdrspf vritrarkid vrfaepvtye ldggergttr rlkakvrpga vtvcvpapgp
      301 a
//
LOCUS       WP_357527795             279 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357527795
VERSION     WP_357527795.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30274
     Region          10..71
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          98..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 masptarrkl gielkglrea aglnieqaat aagisdshls riergrvgvr pltlkallqs
       61 ygadaevter larsaadttr rgdrgwwqpy aasisdkyas liafeseais irafgpmivp
      121 gllqtedyar avlqrgpvrl kadeidtrve vrthrqaild qpdspnlwfi ldegvirrmv
      181 ggpevmrrql lhlvdvatrs nadlqvvpys sgahagtlgp lvilgfaege dvvycetyag
      241 dlypeavasy gdvfnrlaqd alsadrsiem lrsaaegmk
//
LOCUS       WP_357527792             261 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Polymorphospora rubra].
ACCESSION   WP_357527792
VERSION     WP_357527792.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 261)
  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 261)
  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 261)
  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 261)
  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..261
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..261
                     /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=26071
     Region          42..260
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mkapvllarl llaagvvaag laapatasaa patptyaate aasgpqgdvg ilvvngrpas
       61 enysfmvyvs gctgslikan wavtakhcps pstvrvgsin rssggvvvsv irvvnhptid
      121 vklfqlgssv syapapipts sgavgtatri igwgqtcpqp gcggaplvaq eldtsirads
      181 aclgingpye ictnntngna gacygdsggp qvrlinnrwn ligatsragn nnsvcatgps
      241 iygdlssirp wintqvgglp a
//
LOCUS       WP_357527809             810 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Polymorphospora rubra].
ACCESSION   WP_357527809
VERSION     WP_357527809.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 810)
  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 810)
  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 810)
  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 810)
  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..810
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..810
                     /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=85731
     Region          77..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 mprtasppds paastlparl yvaggllaai lyvadvsqll sgltfivvav agvvalvvgp
       61 rwhrtelrnp wtllaaaivv ftagallrpw asvqtgvael aadmftvpgy llmllsltgl
      121 lrarraiekh avidglivcv gmaivsillf avpaasisdr savvsalagv yplfdtvlvl
      181 lvvnlaftta arrpsylllv atmtgvligd vayaiigrtg hltgsplldl pflfsfafig
      241 aaalhpsmve lgratplpvq awswprlmli vpalavpfll tvllpdknvv hrvviaiggv
      301 amvvlllara vsavqayaaa qrlyqhqath daltqlpnrt tlpeqvgkll rapaapgamv
      361 wvffldldgf krvndswgha agdqliveva rrlrtvvpap atvarvggde fvmvdvgsrd
      421 aavalaervl dcfgaplsmp faqvvitasv giagrpvdag tqvtaddlmr eadtamyqak
      481 segpgkwtmf dssmhqrvre rvdievdlrk alpaetsdgs avspqlhlay qpivelrtgg
      541 llgaealirw nhpargaipp gafipiaedt gliakigrwv lresvrqlae wrrtgtvtdd
      601 fwisvnvspr qlrdphlpdv lastltdygv pprvvvleit esvmidasav tdevlrqmre
      661 lgvrivvddf gtgysalgyl rrhpvtgvki drafvrglgv daedeeivra vtamssalgl
      721 tvvaegvetp tqqgvlaelg vvmgqgmlws apigpvrfge rwsalrslpa lppgspvvps
      781 raagapatvp sgpptpaawr gqgqdgvgas
//
LOCUS       WP_357527864             500 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora rubra].
ACCESSION   WP_357527864
VERSION     WP_357527864.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 500)
  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 500)
  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..500
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..500
                     /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=53904
     Region          144..489
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtttpttrtt rttgttptep pvpppgrrtw qptvglrmrl lgwalvlltv aslssvlvvr
       61 qvllnqlenr isaylsqevs efrrlatgln patgqpfgad lhaiadtyll rnepqegevv
      121 lifvegrfhr ssvdppydlt rdtaltarwa altastygev dgppadarwl avpveigddv
      181 rghfvvaqfs gepraeidra vrtmvlacal vivvvaaggy lamgralrpl qsmtetardi
      241 eetdlsqriv vtgsdevadl grtfngmlgr lqgafaaqra fisdaghelr tpitivrghl
      301 elmgddpver retvalvtde ldrmnrmvdd llmlaraeqp dflrpeevpv apmmaevysk
      361 aaalgdrdwr lgpvaevtlw adrqrltqal mqlaqnavqf tapgdrvels araehgrvll
      421 avedtgigia pedrerifqr faraepgrqr aegaglglai vsaiaaahgg tvavdsipda
      481 gstftlvlpg gtlvlpgvga
//
LOCUS       WP_357527885             165 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357527885
VERSION     WP_357527885.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 165)
  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 165)
  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..165
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..165
                     /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=17574
     Region          3..160
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 maevmlrpmt aadadrvlai yqagldggqa sfetvapswa afdagrlpah rlvavddagt
       61 llgwiavspt strlvyagvv ehsvyvdpaa qgrgvarlll dgliasteaa giwtiqsavf
      121 pentaslalh rragfrvvgv rervarhhgr wrdvvllerr spvvd
//
LOCUS       WP_357527948             230 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Polymorphospora
            rubra].
ACCESSION   WP_357527948
VERSION     WP_357527948.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=24502
     Region          <59..191
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtvqdrpapc rqpagapwhg ppvlrfdvtp gvevavahqt rlvdlapstv dlaasadlpp
       61 drraewlavr tllrtllvae lgeragtvai gahpggqphl prrpdlfvsl shddgfvaaa
      121 vglgvpvgvd vqvpvpappa llrrccrpdv raaldrlpqp ardlefawlw tvqeacvkat
      181 gaglagepwt ipvpygrhrg rwrelcwvsl rgrvdvpvsv ayrdggsgat
//
LOCUS       WP_357527951             410 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            sp. NPDC047134].
ACCESSION   WP_357527951
VERSION     WP_357527951.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=42621
     Region          85..331
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mklralvtvf vvlatlvapv tpgaaaates avpavppcpk akapkvvrsp rptppptvaq
       61 hrvvggeala tpglvvppqa ppppkvtats wlvadldtgq vlggcgphey atpasvqkll
      121 laatmlprld ptqvvtvtre dldiapgssa vgllpggryr vetlwlglll qsgneaanal
      181 arlgggpegv aggvramney arhlgalqth avtasgldgp gqftsaydla liaracfads
      241 tfnryvrter aripaqkalg akgfqiqnnn qliyrypgal ggktgftdya rhtyvgaaer
      301 dgrrlvvtll gaepqplrgw eqgaalldwg fglppeatvg rlvdpgewea eptptptpps
      361 qdlppaqvtt saglddtpgg gryvplavga vlivlavvlv wrmrgsarrr
//
LOCUS       WP_357527967             389 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357527967
VERSION     WP_357527967.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 389)
  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 389)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 389)
  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..389
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..389
                     /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=41188
     Region          159..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtsgtlqsit paagtgspaa gqvrraravv vtrtvayvft vamlafgllp ivtavtgdrp
       61 wwvviagaag ftvvatafir lvthamrqpw sdrrghdall itgivlllpv lvdrdwqvig
      121 flalaavavt frprygllla agvlvlitve rilldtpgva fltvqdvltg aalagiivlv
      181 afieelfaar aevarlavda ervrfardlh dtlghnlsai alkselalrl ldqhpvrart
      241 elndvygiar eslrdvrtvv kgyrrdslqr elegvqsvlv aagvrcevat laaalpapve
      301 evlawavreg atnllrhssa srchismart dtevrldvvn dgaatpaptd eiggsgltgl
      361 aerlaplggt ltaehragge fvltvlipc
//
LOCUS       WP_357527969             388 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Micromonospora].
ACCESSION   WP_357527969
VERSION     WP_357527969.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  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 388)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 388)
  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..388
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41139
     Region          147..375
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvdagtapdp dnattgvavr taqtlvflls iaylsipasr vlttqpvpqa glallaligv
       61 allqfrhtwh glraqppltw swtlllqail syapaplagd awlgvpsfla asllitlrap
      121 lsyvaylgvv aaeipfallv hedpsdiaya tlgvaltgav vfgfvkmatl vwevhrlrat
      181 lahravdver lrfardlhdv lghqlcaial kgelasavlr trpetaerei aeliglarea
      241 hrdirevvag yrtvslagem tgvtsvltsa gircevdtvp letlppetat glafalrega
      301 tnvlrhstar hcsitlraqd eglrlrivnd gvppgpfhgg gngleglrer lheldghlna
      361 gpvgagsfel vvyvpspvte aamveatr
//
LOCUS       WP_357527970             311 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357527970
VERSION     WP_357527970.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 311)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..311
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..311
                     /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=33594
     Region          26..277
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtqtirpapa parkkppapp arggardrli rrapllpalv faivvtqipf lvtiylstls
       61 wnalrpgehd fvglanyadv ltddrlraal lntvvltasa vvlsvllglg lavlldrkfp
      121 grgvvrtlli tpflvmpmaa allwkhafyn payglvngvl ggstdwvssy pmasvvatlv
      181 wqwspfmmli ilaglqsqsq etveaarvdg agpwqvftrl tlphlrpyle lgallgsiyl
      241 vqtfdavfti tqggpgtatt nlpyeiyltt frkfeygeaa aagvvvvigt iivatfalrv
      301 isglfrmedh r
//
LOCUS       WP_357528000             258 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357528000
VERSION     WP_357528000.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=26355
     Region          3..256
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msdglagkva vvtgagagig lavsrslaga gcrvvmadld psacadvtea gvpvavdlgt
       61 pdgvatlvet attrfggvdv lvnnvalapy rdtftavdda awqrswdvnv mscvrlcrav
      121 iplmaarggg svvnigseaa rhpkpylvdy svtkaallsl akalsieygp kgvrvntvap
      181 gptrtstmds flagladrls idvdaaadhf vnemrklplg rmnrpedvaq vvlflagdrs
      241 rqvtgaeyav naggtasv
//
LOCUS       WP_357528009             178 aa            linear   BCT 28-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357528009
VERSION     WP_357528009.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 178)
  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 178)
  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 178)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..178
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..178
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19856
     Region          6..177
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mgrnaiifhg tggkptycwy pwlaerlatr gyavevphhp giniepittl lpkllsshtf
       61 dedtvlvghs ggaalllall ehlevtvaqa ilvagyctpp hteeepvlqp sydwaairdh
      121 vrdiyfinsr tdpygcddrq gramferlgg tqivrddghf gdhdqpyerf dlldrlip
//
LOCUS       WP_357528012             413 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polymorphospora rubra].
ACCESSION   WP_357528012
VERSION     WP_357528012.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..413
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44338
     Region          1..411
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mdrhvedllr elaprvlgvl trrfgdfaaa edavqealla afaqwpadgv pdnprgwliq
       61 vahrrlveqi rgeqarrrre dlvarqepvd rlaapaadae patdrddtlv llflcchpal
      121 saasaialtl ravgglttae iarafmvpea tmaqrisrak qriktsgvpf rqpdtedrgr
      181 rlgavlhvly lifneghtrs agpqlrqvel saeairltra lhtllpddse vtgllalmll
      241 tearspartg pagelislad qdrgrwdaaa iaegialvth alprgpvgqy qvqaaiaalh
      301 deaptadatd wpqilalyev leritdspvv alnravagam vngpaaglda lavladdsrl
      361 aghhrlfaar ahllemagdr saaaeayraa agrtaslper hylllraarl atg
//
LOCUS       WP_357528020             334 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357528020
VERSION     WP_357528020.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..334
                     /product="phosphotransferase 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=36720
     Region          11..277
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msplsptqqv ltptevadyi aasfsgarqv adcgpltggg fatvwwvrld dgaqvvlkvg
       61 pppqvpllry eagmlaaear yfrlvaarap qvpvppvlhh ghdprlgewl vtgrlpgral
      121 pdldgadega rydfgaamat lhritgdrfg yddgrtgget wstaftaiie dlladaadwe
      181 vtlpappqrf rellarhadl ldqvrrpall hydgwdgnvl aapdehgtyr mcglvdgerf
      241 lygdpmldlv splqlrraed epehpflrgy adttgtplvf degvrrrlal yrmhlhllmt
      301 vempsrgitv dndpgrhtll aelldrdltd lsrp
//
LOCUS       WP_357528070             320 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357528070
VERSION     WP_357528070.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  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 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   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..320
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..320
                     /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=34323
     Region          4..302
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 miemdlrrlr flrefeergt laavaaalgy spstvsqqlt llekevgarl laragrgvrl
       61 tdagrllvqh arvllsaaea aaadlaalgd qvrgtvragg lqsaarrllv palvrlradh
      121 pqirveifel eleqslpglr lgavdlvigd eydghprprp aglrftllle eplkivlpad
      181 hplarpegpv avaelrtaiw tasaegtghh amvvgtcral ggyepdlrhr asdadvqlel
      241 vrtagvvslm paltlpdgdp tlairdiaet tlnrrlvavt rdtppppalt tllaavidqv
      301 hrlqprwspl sartglpqgr
//
LOCUS       WP_357528082             531 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Polymorphospora rubra].
ACCESSION   WP_357528082
VERSION     WP_357528082.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 531)
  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..531
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..531
                     /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=55743
     Region          17..489
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mpegttyffv gpseepdkyr llrqvgggge aelwqadval gaerekvavk vlrsahedra
       61 awrsrwieqt dllrlirhpg vvgvhaafeg armhhagaad ptetalylvm nwiegtdlrd
      121 wparqsgppa avftcltqva dvldwlhsgk atpsqrpvvh gdispanviv nrdgqavlvd
      181 fglfrmsshv tnlpagtqgy lapevlrdga yspasdryaf gglayflltg ahppatadar
      241 aaglhavfgp tplldhalri faddpaarpp agewvrnlra qtsttnvsqs glppirpgsa
      301 pygfpgagpv pagvgsgndr rprpwwlava gaalalvlva gtvgvvglls dssagrpdar
      361 gaanptasad gtpdatvgsp neqapqtepg gdsaggsdpa gqpgkvllis lparygpdtg
      421 pvdidgtqyp ssiyeecdld teyhlgrgys llesgiglsd vsdtgasatf tvyvdqvera
      481 svtvrlseik tikvdvtngv rlrlyaeipd ayrnyigcga tpafadptls r
//
LOCUS       WP_357528089             171 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357528089
VERSION     WP_357528089.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 171)
  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..171
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..171
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=19316
     Region          <58..165
                     /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 misqngnaye egfvtefwep vwayadnpgp dtepalreal slaairwqyl hgvdrpelvd
       61 pdtwtfdhrd vnrpgndlaq falfrdyatn pplyprvhey frdsqvplla lwgaedlifg
      121 aqgaraftrd lpqaeirlip ggghfllesh ldtavehlrd fltrtlepat a
//
LOCUS       WP_357528246             950 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357528246
VERSION     WP_357528246.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 950)
  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 950)
  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 950)
  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 950)
  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..950
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..950
                     /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=103595
     Region          1..249
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          125..936
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          734..761
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(735,738..739,742..743,745,774,777..778,781..782,
                     784..785,814,817..818,821..822,825)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          772..802
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          813..841
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          851..881
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfevlgplr vwcderrldl gpvqrqvvla vlllhadkvv erdrlitgiw gstppayavn
       61 llqkhisalr rvldptpqkr gpstfltwtg sgyrlavapg gldlvdfere vaaartards
      121 gdtsaaatal hsalrrwrgp fcagltspal daertllder rlaaleerie ldlnlgrhla
      181 vvgelrqlva dhpyrerlwc llmvalyrsg rqaeaimtfh dvrrhtldgl gvepgadlhr
      241 lhqqilaadp tlvihepgps vgtaapltgl rlpvpaqlph pvpgfvgrqa dlarldglls
      301 qgcetatrts pvaviagmag vgktalavhw ahrvrgrfpd gqlyvnlrgy dqfgavaepa
      361 avlqtllhgl gvppeqvpag ldarsamfrt llstrrllil ldnardaeqv rqllpgscgc
      421 lvlvtsrnrm tglmatdaat lidldlmtaq esrkllvgrl gagrlsaept atdqliqqca
      481 glplalsiaa araanqtrfp lsalvarldt ardgldafsv qerqvdvrav fshsyqvldp
      541 atagmfrllg lhpgpevtvp aaaslvgvpr ahadrliatl vnssliseqa pgrhvlhdll
      601 rayavelthr hegeaarraa vrrlldhlvl sahgadrlls psrepitpvp atagvsperm
      661 tdrqaalrwf teeqtvllaa lepaagqgfd thvwqlawam ttyldrrgrw hdsaaiqtra
      721 laaarrlgde ralalahrgl graavrlqrp earshltaal tlftrvgdrq gqartrlnfa
      781 wlceqqgrhq ealphvrqav elfqrcddri gladalnalg wfhaklggyr aaltycaeal
      841 alaretgded geahirdslg yihqlgdqpr qalanyrdav rlwrelgdrh yeaealhqlg
      901 dlhhavaepa aaraawtaal tifdefhhpd aaqvrgklgk ldkvparsrc
//
LOCUS       WP_357528263             255 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357528263
VERSION     WP_357528263.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 255)
  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..255
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..255
                     /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=28178
     Region          20..240
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mivpssgvap aqaapveagl hgrvldylgt aicggelaag avlnidelvd ryavsrsvir
       61 evlrvlasmg fietrrrvgv mirsaehwnv fdpqvirwrl asagriaqir sitelrtaie
      121 phaawlaaqr vghddaselv glaakmwaag kagdeerflr ldiefhqrvl rasgnemfvk
      181 lqdlvaevli grhhhhlmph hpheqalqlh aevaqgiqrh dgdsarramv qimehafeem
      241 ssiweqtlhv etdpa
//
LOCUS       WP_357528273             207 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Polymorphospora rubra].
ACCESSION   WP_357528273
VERSION     WP_357528273.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 207)
  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..207
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..207
                     /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=21603
     Region          7..185
                     /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 mastdsrrlv lasasparlr tlqaagiepe vlvsgvdest vdstnpdtls ltlgrlkaea
       61 vaerlrrdgr vgsgalvlgc dsvlafdgei fgkpadadda tkrwaqmrgr sgvlhtghcl
      121 idldsgghae avaatvvhfa vvdddeiaay vatgeplhva gaftldgigg pfveriegdp
      181 gtviglslpl lrrllaqlgv rifdlwr
//
LOCUS       WP_357528301             123 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Polymorphospora rubra].
ACCESSION   WP_357528301
VERSION     WP_357528301.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=13782
     Region          3..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhafdilgdp vrrrilella dgeqtsgait eviraefgis qpgvsqhlrv lrengfttvr
       61 aqgarrlyav nseplrevdr wlarfrgiwe qhldalatel argrrerrrr ggtdggtgrq
      121 pgr
//
LOCUS       WP_357528332             128 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Polymorphospora
            rubra].
ACCESSION   WP_357528332
VERSION     WP_357528332.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..128
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13654
     Region          25..119
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtgahvpaav ddpagvrsra eatarevfaa igtkwaldav dalgpgtlrf telqrelpgi
       61 shkmltqtlr alerdgivdr tvhptvpprv dyrltaaghg lrdivngmcd wsgryldeil
      121 aartragg
//
LOCUS       WP_357528321            2546 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Polymorphospora rubra].
ACCESSION   WP_357528321
VERSION     WP_357528321.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13483049
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2546
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..2546
                     /product="non-ribosomal peptide synthetase"
                     /calculated_mol_wt=274794
     Region          36..>2151
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2190..2452
                     /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 mnaeitdpar ndadarreal irqrlaggrg grrdtiphvd rggrlpvsfg qqrlwfltml
       61 dprspeylvp lvlrvtgdld vaalgeawrr llvrhevlrt ryqladaepi qvvdpapdsa
      121 airftdltgl paadrdrral dlatadaaep idiglehpvr vhairlapdr hllavvfhhi
      181 acdgwsmgvf indlftlylh aidapdapal peptvqyadf aawqrgrlag aeldrqlghw
      241 rdrltgltpl elptdrprpa krdwagdrvl ftvpadlagr lrdlgrrhda tlftvgataf
      301 qvllsrysgq rdisvgsava grgrpevrnl igfflntvvl ratwsgdpsf adllrdnrrt
      361 vldalehqea pvqflvddvd rkrdrsrtpl fqvmfdlaea apsaftmpgl dveavdlvga
      421 vakhdlrlel seqgdgalrg vleyptalfd ratverfagh lltlfdsvct apeltlsale
      481 ildpaerell lgagpapatr paprpvtaav aeharhrphe tavvagpdrt tyaqlheran
      541 riahhlrgrg vgpgsvvgvc lgrgpdllpt llgvwragaa yvpvdpgdpa ervgyvlrda
      601 gaalvvtqta yagitathsg avllvdadra aidaepatdp agepdpdava yliytsgstg
      661 rpkgvlvshr glanyltwaa dayltaagrg aplfsstafd lvvttlylpl lagqpvhllp
      721 adlavgdlgr alteaaadgp fsfvkltpgh ldvlthqlta dqaarlaghl vvggegfasr
      781 ladrwwdlaa ggktrivney gptentvanv ayfadgppad psaaaellpi grsmpgttay
      841 cldaelrpqp vgvvgdlylg ggqlahgyrn lpavtaerfv pdpygppgar lyrtgdrarv
      901 laggdieflg rvddqikvrg yrvetgeiva alrrhpgvrd avvtlrgtgs agrtlvgyvv
      961 ttnpdalpia dlrellaatl pdymvpthlv pltelpltsn gktdlaalpd pdraatstds
     1021 alvaprtave eqvaavlrtv lgitevgvdd dffdlggdsl savalvgdlr dagldiavdd
     1081 vfahptvakl aelaaerpav agartgvapf alisdadrqk lpadvedafp vsmlqagmvf
     1141 emmgggevny yhnattyqir ddaefsvpaf eaavrllver qevlrtgfdl igysqplqli
     1201 hrtahlptsa adlrhlsvae qdeqirqrma aeradlfdla tpallrlhav vrtdtdwali
     1261 itechpimeg wsyhmllmel ltyyrqirdg qppqpaqelg irfadfiaae qeslrseddr
     1321 gywrrtvega arlalppgwa tgdgprgplr vevmfadled glralaktae vpikavlhaa
     1381 hlkvmsmltd eprffgglvc dtrpevagad rlyglflntv pfpfeltapt wrqlvrdvfa
     1441 qeielwphrr ypmpamqrel sanrrlvdvm fnyldfrtvd mdlvdfaasi ddsqiefkls
     1501 ttvfrqglin lrmhpdavsr pagerlaamy rqvltemaad pdgdalatyl paderrrlvt
     1561 ewndtavprp atdlatlfeq qvaadpaata avladgstls yaeldaranq lahhlrglgv
     1621 gpeqfvgica epgpemlvav lgvvkadaay lpldpshpte rlayvlrdag vsvlltqerl
     1681 addlppfmgq vvnvdtdwpe iagadastpa rsagpdslvy aiytsgstgr pkgvmithgg
     1741 lanyltwavg aytgpdgtga pmlgsiafdl avtnllvplv agrpvtllpp ggeveavagm
     1801 lagggrfdlv kltpghldvl rgllpadttv davgtfvvgg eqlpletvla wqelapatri
     1861 vneygptetv vgcvvhdvpa dvdrtqpvai grpidntrly vldrhlqpvp vgatgelfig
     1921 gagvargyhg rpeltaerfv pdpyapqpgg rlyrtgdlar yradgnlefl grvddqikir
     1981 gyriepgeie arllahpsvd eavvvahtga dgdrrlvaya agtgaqpsga vlrdflretl
     2041 pdylvpatfv lldalprsaa gkidrkalps pdgaradlgt efvaprtate rrlceiwerv
     2101 lgverigihd dlldlgadsl sglrvvaaat dlgltmspmd aiafptiaql arhllgggte
     2161 eldrilrads eldpairpag ppadpagpll ltgatgfvga fllrelldrt tnrvvclvrg
     2221 tsdeharerl vaalhrwsay hpqvesrvdv vagdlgaphl glsadrfael agtvgaiyhn
     2281 gadvnavhpy qamrrtnvdg treiirlact gpttplhhvs tmsifkvdaf drwidessiq
     2341 aeppssmsng ygqskwvaen lvrevsrrgl pttihrmakv swdtvtgtsn sadqfnrlia
     2401 aavevgaapd fdysmtltpv drvaagivdi aarpdavggc yhlisphqvt wrqmrgwlat
     2461 aghplaetdy akwrealvdr srqpggerln pllmllprer dnfevdaldd dyvpptptww
     2521 arhggeippi hqedftrflt hlrass
//
LOCUS       WP_357528405             212 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357528405
VERSION     WP_357528405.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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..212
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..212
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=22948
     Region          80..164
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mqqrrtpggq rparrpvrpg tgrgavrdsg vraqsrtagr apsaargaeg vrsakrpaar
       61 rsavggvtrl aaprprgltg ratvliavli alalaytypv rvyldqqadi ermeaaqaaq
      121 reliaeltse aekwqddayi etkarerffm hrpgekmvil ledpvgaard agrsgepevp
      181 vepdpwydtl wssvraadaa qldpttdsql de
//
LOCUS       WP_357528447             469 aa            linear   BCT 28-DEC-2024
DEFINITION  amidase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357528447
VERSION     WP_357528447.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..469
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..469
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48682
     Region          7..456
                     /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 mavqdimptw vgatakqiar gvrrgdvsat qvladhldhi akadtdlaaf rtvrggeavt
       61 eaekvdeqed lanlplagvp vavkentpva gmptwngsaa vrtavaeadh evvrrlrgag
      121 avilgvtrmp elglwavtdd dsavtrnpwd lartpggssg gaaaavaagl vpiahgndgl
      181 gsiripaacc glvglkpgrg vvpcqlgaed wfgltehgml sttvadaavg fqvlagraqq
      241 klvppqrlrv gvslrspvrg vspdapnrea vaaagrllaa aghdtlpadp vyptalglqg
      301 iatwfaaaaa dvraaavdrr slqprsrrhv algewawrrg yvreadraaw rersigfftd
      361 hsvdllltpa laaapppaas wsarswqtnm ltsiryapya apwnvaglpa lvvpvgrrpd
      421 glplavqlvg ppgsellllg vagqfemeap wprhapgypr vgtgaaasa
//
LOCUS       WP_357528458             475 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357528458
VERSION     WP_357528458.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=50948
     Region          27..475
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mtipypttqp msafaavtpp sgaprprvtf lgtgylgaty aicyaelgye vlgydvdpdk
       61 iaklnagevp ihepgldell rrnlaagrlr fstdiaetad fgdvhficvg tpqradgmga
      121 dlsyveasvt nlarhltrka livgkstvpv gtadwveqlv dkhasadlgi evawspeflq
      181 egfavddvlr pnrivvgvks ewansmlyaa hkgvfdlaat edrevplvvt dfataelvkv
      241 aanaflatki sfinamaevc evaggdvtql araigydpri gnrflqaglg fggaclpkdi
      301 rafqaraqel gagealrflh evdlinlrrr trvlhlaael ldrrygpagp dlsgtriavl
      361 gatfkpntdd vrdapalava allhkagadv hvydpqgvdn arraapelty eagmaeavtd
      421 adlvcvltew adfrnadpna lgelvtgrrv idarncldst lwtqagweyr glgrp
//
LOCUS       WP_357528501             472 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357528501
VERSION     WP_357528501.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..472
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..472
                     /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=51001
     Region          36..417
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mngpppdral aeavrapywl drperpdplp plagptsadl lvigggyggl wsallakqad
       61 pgrdvllvea gtcgwaasgr nggfcaaslt hglangvqrf pdeidelerl grenldaiaa
      121 tvagygidcd fertgelsva vepyqvdgla edvalarryg hdisvldade vraevnspty
      181 lgglwdrdrv amldparlaw glrracldlg vrihehtrvt glrraggall arttgadglp
      241 gavcadrvvl atnafppllr rlrawvvpvy dyalmteplt taqrdaigwr nrqgladtgn
      301 qfhyyritgd grilfggyda vyhygnrvap aleqreatft alashffttf pqlaevrfsh
      361 rwggvidtct rfcaffgtay dgrlafaagy tglgvgatrf garvlldlva gadtpltrla
      421 lvrdkplpfp peparaigig ltrwslarad arqghrnlwl rtldrvglgf ds
//
LOCUS       WP_357528570             302 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357528570
VERSION     WP_357528570.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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 302)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..302
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..302
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32104
     Region          2..283
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mhlhqlaqqi maikpvpvpt tgrdfdlavk vtapvsghdl pvlvfshgna wsmdayeplv
       61 drwaatgfvv vqpthldsrr hglgfddprf gtiwrvriad lhavldnldd ilgraglagr
      121 tdrervaavg hswggqsvgt llgarvldad gtpgedfshp lvkagallta tgtgdsltpf
      181 avehlpfmrp dfstmttpal vvaggkdqsa mstrgpdwft dayhlsptpk slftitdgeh
      241 tlggvageqv aetsdedpar valvaeavsa ylldtfdldg ttwkaltega aasdcayhve
      301 hr
//
LOCUS       WP_357528571             429 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357528571
VERSION     WP_357528571.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 429)
  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 429)
  AUTHORS   Rosinski,J.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 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..429
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48985
     Region          131..>184
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          222..387
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpykqppssl ralwlgeqmr rlrrdrritl kaaashlrvg hsalarferg qwpflagrva
       61 tlldvyqvtd pkrrgmllrl daevdrrnaw eadpddlhhp epdhepepad qennrmpfqe
      121 rhqptvrgqw laeqlrqlrl drsltlqqva erlpldwssl grfergeikp kyddvaalld
      181 vyhvfddrqr dvllslaldv rhgshwdvdf gdelpyrpyv nlawletrat tiryyatgri
      241 pdllqtpeya arfiqtqmgi hqptpehraa vaalnarkqa frdgtnplsa vitetalrnq
      301 vgdshlmdqq inhlhklarh prytinvlpd gheitarydt pftvfdmpdp yppvavtqsl
      361 agrlylehpr slrftvahdh lqtaaqphts hqldiihqqt taeaapsgsr tgsgrvptpt
      421 arqsssakp
//
LOCUS       WP_357528711            1326 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Polymorphospora rubra].
ACCESSION   WP_357528711
VERSION     WP_357528711.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 1326)
  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 1326)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10286316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1326
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..1326
                     /product="type I polyketide synthase"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=139559
     Region          <2..152
                     /region_name="Acyl_transf_1"
                     /note="Acyl transferase domain; cl08282"
                     /db_xref="CDD:471802"
     Region          221..384
                     /region_name="PKS_DH"
                     /note="Dehydratase domain in polyketide synthase (PKS)
                     enzymes; smart00826"
                     /db_xref="CDD:214837"
     Region          498..922
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(670..671,673,700..703,728..731,756..758,779..780,
                     800..801,815,842..843)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(780,802,815,819)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          940..1025
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1104..1315
                     /region_name="PKS_TE"
                     /note="Thioesterase; smart00824"
                     /db_xref="CDD:214835"
ORIGIN      
        1 mcdregirtr llpvdyashg rhvdpirdrl ltnltdpttd atdstgtdtt dstgttdnsg
       61 ttdpssgvtg vvmystvtgg lldpttqpld adywwhnlrr qvrfdtavha aaadghhtfi
      121 eisahpvltt aveeilhdhd tppatvatlh rdhgdlhrmv talteahnhg ipvdwntfyq
      181 qtghrphrvd lptyafqrer fwlsssvvgd vsrwglvgag hpllgvvvas avsggvvlsg
      241 rlsvgvqswl adhvvwgrvv vpgtavlemv vragdevgcd rvaeltlhvp lvlpeqggvq
      301 vqvvvggpnd dggrvvdvya rvdgsgtewt hhatglltaa rmdsvddgal gawpppgave
      361 vdvaglyerm sevgldygpv fqgltgawrv gesvwaevev plegagfavh palldaalha
      421 aaltsvgrdg amvpfsfsga rvlasgasrv rvrvrpcgdd alsvlmvdhg nlpvvvvdev
      481 avrpvarlqv sagvggdalf avewtpvdvv vgqtpsygaw eavrhlqhvp dvvvwecpgg
      541 vepgavraav agvldvvqrw vrqdrfgsst lvvltrgavd ggdvagggvw glvraaqaeh
      601 pgrivlldad ryadvadlva svsasgqpqv lardgglwvp rlskvapgit pdpgtdsada
      661 vggvwgggtv lvtggtgllg glvarhlvrv hgvrslvlls rrgvaavgvd vlvgeltglg
      721 arvevvacdv adrvalaavv egvvaggsrv sgvvhaagvl ddgvvesltv srldavlrak
      781 vdaawnlhev vgrvdafvmf ssaagvlgap gqanyaaana acdalafyrr glglpahsla
      841 wglwaetsgm tghldqndlt rlqgtgllpl ptdealsvfd salttehgml laakvdiqml
      901 qkrtasagip lllqslvsvp trrtvrddra aetetlekrl nglggkareq llldairrha
      961 atvlgypnad avdplrsfge lgtdsltave lrnrlnwetg ltlpstlifd hptpvelarh
     1021 lasgltgfge avvpeqeqsp danasgdvie mlyrranelg ryedgfdllr aaarlrpgfp
     1081 tggdatdvps pvvlsrgdrg pglvcftspl adqsphqysr laaairgvrd lcvvqapgft
     1141 aderlpdslm avvaaqaaai rqwqadvpav lvghssggwf ahavarhlee tgtpaagvvl
     1201 ldtllpgdgv mvslrslwaq tvverpesaa rldyirlsam aayadffvpw tpekvatptl
     1261 flvaeeavsa esvvdpdavr eqwqlegepv vvagnhwsmm eehavstarv ieewitrvca
     1321 vetgse
//
LOCUS       WP_357528729             212 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Polymorphospora
            rubra].
ACCESSION   WP_357528729
VERSION     WP_357528729.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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 212)
  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..212
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..212
                     /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=23179
     Region          <45..186
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mtattrrrsw rrrspghsia ggrcparlrs rrraggrrpg gpvvkvarah arvadtrrdw
       61 qhklstalir enqavhvedl cvvglgrtrl aksvhdagwa sftgmleyka arygrtfarv
      121 drffpstrmc sacgrinekm alnvrswncp cgaahdrdvn aalnvlaagq adngndrgar
      181 vrpervpapr geavthpdaa rstrsvegis vl
//
LOCUS       WP_357528734             272 aa            linear   BCT 28-DEC-2024
DEFINITION  MOSC domain-containing protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357528734
VERSION     WP_357528734.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..272
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29864
     Region          1..268
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mrvseintyp vkgcrglnhs eaevrpwgld gdrrwmlvdp egvgitqret talvrvhahp
       61 etgglwlraa drpdlwvpqp sevtpvqvrt frrralrvaa lpagpaadtw lsqlldrpvr
      121 lvwlaeparh ieagrkkhdp gdqvsfaday pvlltstasl aalgdwltea gadpvpmsrf
      181 rpnlviegap awaeddwegr smriggvafr aagpsarclv tttdqqtgvr greplrtlar
      241 hrnvdrqllf glnlvplesg rvrlgdpvla fa
//
LOCUS       WP_357528760             393 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357528760
VERSION     WP_357528760.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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..393
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..393
                     /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=42309
     Region          14..385
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mrlpdsfyts vrtrlseald ergldgylat sppevaflsg ffyiaterpv ylwmprvgep
       61 llviprldee yaaqqgvtlp tvsyfeypgv vsaeetlaaa lsrpggagrr igvsagvsva
      121 afralsgaig gaelvttdav aklrlckfpe eipfheaaar icdemlaagr alieealasg
      181 gplpredeia rhvigygtdq myanydlvvy ttklagglvy agpnsalphg lptrrrvqpg
      241 dtlilslgaa vasrfveser tfiigeptae qvryyeadrl aqevgtqamv agrtcaevnk
      301 icldvlrdqg lgdyirhrqg hgiglqnhea pwvedgdhtv lapgmllsse pgvyvpghag
      361 yrisdtvlvq qdgprrltgy prdlasniie gvr
//
LOCUS       WP_357528787             165 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Polymorphospora rubra].
ACCESSION   WP_357528787
VERSION     WP_357528787.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..165
                     /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=18485
     Region          14..137
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mpaatsavtl rigarvllld padrvllvha ldptepghhw welpggglde gedlrdaarr
       61 elaeesgiml atlgrelwvr esrfrykgrd hhriehvflg rtptttpqva lkptenekag
      121 lierrwwsah elrqcrdkll patlpalldd lladrlshpp ltlad
//
LOCUS       WP_357528821            1096 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357528821
VERSION     WP_357528821.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1096)
  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 1096)
  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..1096
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..1096
                     /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=120887
     Region          103..944
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mtepaatgpr dgplppalpe adftrvplqv aystgeqplt rfyvpllara ieykrlvgyf
       61 saqvlaraaa gfapfaarra rmqlvvgaql sdedvdavlr gepldqvvae rlcleplteg
      121 vsivqkehlr llawllregl lelrvgvpvd sdgkplrpeq arryfhskyg lftdalgrqv
      181 afsgsdnetv agwtgnhetf hvywswndav wplygadvir rleqhwdgtp dtgwavlpvp
      241 talrqglini vpagwappaq dpdlrlrdfd vpdnplgggp apgwtptpae dskadenave
      301 adrvrlleml raplsrtmvg vasaaalplp hqqliavrav etyprgylla devglgktie
      361 aglilrelll sgraetalll vpasvmsqwq eelhekisld vpryeggvfl drhnrevpse
      421 ptanpwtafp vvlasshlar radrraqvla gswdvvlvde ahharrrglk angtpntllg
      481 llqtmkaqqs wkalylasat pmqmapheaw dliellglpg ewsesadkfv ryfaelrrph
      541 adrdwallsr mlrdeldapd aaadeplrnr vvselgpvvs rsilrlhqpp ppsrqrvlgw
      601 kirqcelade wlrahtpmrd rvfrhtrgtm rryqeqgllp adliiprrti rdefiglspa
      661 ewtlyerida yisryynaym aagpgnsaar algfimtvyr rrltssfqav rlslkrrrea
      721 laagralais elldpddkta teddesgvdl tgvadpisad llaaeiaeld sfiadiealg
      781 gqdtkaeqly gdlneallsg ydsvvlftqy tdtldylrdr lagpyqrvac ysgrggerwd
      841 patstwtkit knelkqlfre geirillgtd smseglnlqt sgrlfnydmp wnlmrveqri
      901 grvdrigash evvtisnyfy adtveqaiys sikddfgdft eivgdaqpvl aateaaikaa
      961 amaaspaqrd aaaaqatrdi rdrvqeatsg dvrlsdaeqq tlsipelhps asladiatam
     1021 vgnkaiapwl rpdpaengvw elalpgaapq lvsfdravad askrdvslft wgtaeakala
     1081 klleeavpan pngets
//
LOCUS       WP_357528870             248 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Polymorphospora rubra].
ACCESSION   WP_357528870
VERSION     WP_357528870.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=26909
     Region          6..114
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mdlppsftir erdhrihdpf teekfailgr aiglwpgttv ldlasgsgem lcqwardhgv
       61 tgagvdistv fvaaararav elgvadrvtf rhgdaaghva atpvdvaacv gatwigggvt
      121 gtiallersl lpgglllvge pywrmdppdq atvegchats rddfrdlpgl vtlfgdlgwd
      181 lvemvladed swdryvaaqw ftvrkwldan pghelagafr aeldtaplqy vrygrpylgw
      241 gvfvlkrr
//
LOCUS       WP_357528876             246 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Polymorphospora
            rubra].
ACCESSION   WP_357528876
VERSION     WP_357528876.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     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=26508
     Region          <40..>144
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mddpdgyfge dvaatyddpa semfraevvg atvdvladla gggralelai gtgrialpla
       61 drgvpvhgid msramvarlr akpggdavgv tigdfattrv dgtfsvaylv fntimnlttq
      121 eaqvacfrtv adhlepggcf vvevmvpdlr klpagqnvvp frtsatgway drydvatqem
      181 ssnyvevvdg rgsfwsvpfr yvwpaeldlm aqlaglrlre rwagwgrepf tsesgqhvsv
      241 wekpaa
//
LOCUS       WP_357528934             162 aa            linear   BCT 28-DEC-2024
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Micromonospora
            sp. NPDC047134].
ACCESSION   WP_357528934
VERSION     WP_357528934.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 162)
  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..162
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..162
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16976
     Region          24..122
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mstrqptggp pdasthggag iryltvlyda hcpicrtare wlasqaqlvp lefvpagsae
       61 arqrfpgldh eatlrditvv addgalyigd gawiaclwal aeyrataerl srphllplar
      121 gvvaaasavr emvrepgsvp pggstgyggp ddrpvcaddr cg
//
LOCUS       WP_357528935             490 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Polymorphospora rubra].
ACCESSION   WP_357528935
VERSION     WP_357528935.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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..490
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..490
                     /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=54735
     Region          129..460
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkgttfkrcg crdttgrrlg qscpqlrrvg gawsrnhgnw hwqieipara dgtrrplrqg
       61 phpsqadaea vldriraalt vpdptdtyat sktgdlieta vktgapiptp dqirralhld
      121 itptelptme aylhswlagr kgikqgtvrt yeahirlylv pylghlridr lrpghidamy
      181 daiderntti dtlraspdpa kreqvkgqrt vvpatmhrir atlrkalnda irrhrlidin
      241 patmielpra rapkptiwtd qriktwrdtg ktpsrvmiwt pehtgrfldh thdagdrlya
      301 lyhlvtftgl rrgeacglhw ddldldnrtl tvrwqlvqhg wataidtpkt adsegavald
      361 aetitvlrah rtrqhrerla agetwtksgl vfttptgnpl hpadvtdhfh hlatqaglpp
      421 irlhdlrhga aamglaagvq mkvisnrlrh ssphftakyy gdvlpelsha aaeataavvp
      481 rrrgqgekta
//
LOCUS       WP_357528938             483 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357528938
VERSION     WP_357528938.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 483)
  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 483)
  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 483)
  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 483)
  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 483)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..483
                     /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=49526
     Region          28..467
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mrrdpglrrl algtllaayp gpvppdwave lvaeglaght lfgtnidtpa qvaastaalr
       61 tgraevlvai deeggdvtrl ahatgspypg naalgaidde gltrevyrai ggelaavgvt
      121 vnlapavdvn steenpvigt rsfgtdpvrv aahcaaavgg lqaagvaaca khfpghgatv
      181 tdshhelptv evspqvlrrr dlppfaaaia agaravmtah irvpaltgtq patfsravlv
      241 dllrreygft gavitdalem kgaalaaggi apgavralaa gadllcigak vdaalvegvv
      301 aevvaavgdg rlarerveqa agraaelaew trhtgptpvp spdlgyaaar ralrvegvpt
      361 rsvdplvvqv harstivqgr vpwglgphld gpelvevvaa eadpdelrrr agdrpivlvg
      421 rrlhrlpggp elvdaltaah pvtvvemgwp sgwrpvgsra fvltygasha ngraaaevlg
      481 lir
//
LOCUS       WP_357529092             183 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA cytosine methyltransferase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357529092
VERSION     WP_357529092.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 183)
  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 183)
  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..183
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..183
                     /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=19901
     Region          10..>183
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 msvahttvtr igslctgygg ldlavelvlg gqltwyaetd rhaatvlahh wphvanlgdi
       61 rtvdwstvtp vdivtagfpc qdisnagkra gitgehsslw nhiaaavrvl rprllfvenv
      121 aallrrgfdv vhrdlaeigy dtrwlclras digaahrrdr lfllatptpp drrgtdvadt
      181 lrp
//
LOCUS       WP_357529207             317 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora rubra].
ACCESSION   WP_357529207
VERSION     WP_357529207.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 317)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..317
                     /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=34149
     Region          22..314
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mstptlapav ppapaatavp trkrryrpae iaisvafllp stavylifvf yplartlwls
       61 vhgtdifgat tdfvgldryv effteprlrr vlfttalfst vtvlptlllg lllalslqak
      121 vrgisffrtf matpfafsaa aaavvfdify spsvgvfngl lsslglpvve wltnpttalp
      181 slavvsvwrd lgyamlvfsa glqaipdevl eaaridgagr wtllrrivlp lltptmffll
      241 vvstisslqt fgeiniltgg gpdgatttlv yslyqsafaf ggsdyglasv qavvllglvm
      301 litviqfrvl qrrvhyg
//
LOCUS       WP_357529211             213 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DUF47 domain-containing protein [Polymorphospora].
ACCESSION   WP_357529211
VERSION     WP_357529211.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..213
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=22381
     Region          24..>142
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mvadsriaal vrdlsgrtdq alaslvveql aataagvrla rsaaagelap avarqrmgav
       61 ehegdagral lvkrlrrsvs spidredlfr lsravddvld alrdfvrefd lfqaapspay
      121 apvldalaas vdhlseavrl lpaaprraad eallakkpgv rpryqhavad llggpvdadt
      181 lrdtlllgrl dqagtslaaa vdaladgvvk rfq
//
LOCUS       WP_357529228             963 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Polymorphospora rubra].
ACCESSION   WP_357529228
VERSION     WP_357529228.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 963)
  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 963)
  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 963)
  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 963)
  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..963
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..963
                     /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=103721
     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          147..960
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          742..770
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          775..811
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          822..850
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(823,826..827,830..831,833,863,866..867,870..871,
                     873..874,903,906..907,910..911,914)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          855..891
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          902..930
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrwrilgpve vtvdgkvldf rrpqqravla rllldadrvv spaqltealw adepprssrt
       61 qvqvcvsqir aalrgagltd vlltqaggyr ivvgpdeldl avftsavara rtavaagqpa
      121 tavellrtgl alwrgpalag aagafvesaa arldeqrlsa yeqlataelt lgrhadviev
      181 lrpvvdahpl reslisryll alagtgqqar alqvyagtrr rlveelgvep atelaaahlr
      241 vlrhdmpdpd papdpapdpg pgpepgpspd alpspaapvp aqlptdvpgf tgrqaelral
      301 dalldgadga ggravvisai ggtagvgkta lavhwahrta hrfpdgqlyv nlrgfdpggr
      361 avgpaeallg flealqvprh hvptelsrqa alyrtllagr rvlvlldnar daeqvrdllp
      421 gapgclvvvt srnrltglvi aegarpltld llsatesrel lrqrigwdrt ttdlaaveei
      481 irrcaglpla lavvaarast rphlplaala telrdvrggd ltafdtgdpa tdvravlsws
      541 yralepdaar lfrllglhpg pdagqpalas lagipparvr pllarlteah lltehapgry
      601 vqhdllasya aelchtidsa aeravashrl fdhylhttha adrlldpyrl avsvvpadpq
      661 pdvtsddpgd hpaamawfta eqgtllavve ragragsddh awqlaavltt yldrrghwhd
      721 liavqrtald aarrgadrlg qahahrglai actwlgrntd ahvhyqrvld lyreladpvg
      781 qahthvgvsw ilaregrhee aldqtgqals lyratgylvg qakalnnlsw lharldhhel
      841 alncsrralt lheenedrhg aalawdnlgy ahhrlgrpde alccyrrald lhralgdryd
      901 eaevlanlge tyqltgdpea arsawqdala ifdeldhpda dglriklaal prrswrirga
      961 isg
//
LOCUS       WP_357529257             150 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357529257
VERSION     WP_357529257.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 150)
  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 150)
  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 150)
  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 150)
  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 150)
  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..150
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..150
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15970
     Region          1..147
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mesttkvvlv tgassgigea valrlaaegh dvvagarrre rlaalaerhd nirvrrldvt
       61 drgdvaafvd savaefgrvd vlvnnaitpg vveseladti sdpvareamr eyrknsispd
      121 avaraisfav dqpadvdvne iiirptrqrg
//
LOCUS       WP_357529273             289 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357529273
VERSION     WP_357529273.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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..289
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..289
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31625
     Region          15..>128
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mnrpldtgsh adfraqrlld vliptkdrpt elavtlsgla aqqgvpgfgv vvsdqsddqp
       61 gyahpaaatm vralrhrghp vlltrrlprr glaehrafll aasaaryvlc ldddvwlepg
      121 tlhrlvtaie elgcgfvgng vhglsylhdv rpqthrhyqe wsgrpvperi gpdtpewdra
      181 qihsaanllh vtealalppg swrayriswi ggcvlydrak lvdcggfdfw rrvpprhqge
      241 dvaaqlavla rhggagvlps gayhlesptt vtdrdveawe fvlaeepgc
//
LOCUS       WP_357529301             743 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF1800 domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357529301
VERSION     WP_357529301.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10555974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..743
                     /product="DUF1800 domain-containing protein"
                     /calculated_mol_wt=80262
     Region          30..>127
                     /region_name="dnaA"
                     /note="chromosomal replication initiator protein DnaA;
                     cl42516"
                     /db_xref="CDD:455861"
     Region          275..738
                     /region_name="DUF1800"
                     /note="Protein of unknown function (DUF1800); pfam08811"
                     /db_xref="CDD:430230"
ORIGIN      
        1 mpdqnvpphr arddgrraer prsgahsdge rphapppysd gydrhaggrh gadpygghra
       61 gdghatgghr aggqrpdprp taghpadryp ddgyvtdryp tggyaadghp dpygdsrrgp
      121 rwvgpqggad vqpgrsasev lpdldddedd drrrtgrrra lialtgtaav vaggtalals
      181 pqgaglidal lgtgggdata pavtdgsaar psgqqpstvr tyteqnesym gsragevlkk
      241 nspvtgkshs gpasaaaetk vtvktvlakd pvrhlaqrat fgatpkvlad iekmgidawl
      301 rdqldpdkia ptpaelrlae lrtlkmsipq lreqrealda ngvhaddetv watiarqiws
      361 drqlfevmvd fwtdflhvaa yfegsriqra sfetevirkh algnyadmlv aanrhpallt
      421 ylnqaqsskd kvnenlaren lelysvgvdg gyteadvrqa allqtgrgvr edqyvyrper
      481 hyvgevrimg fqhannsaeg geaaadayfr ylalhestar yvatnlatrf vsdtppkslv
      541 drlakaytts kgaikpvlms lfsasefwas vgqkvrrpme ylvatyrvlg vspetpagyq
      601 hsnanrtafa eglrqikgkl eelgqfpagq ptpngypdvy vawtsagtmv ngwneagnil
      661 tgnrkmftyr rpeelvpapp atagayldal aqrlvfqklt gdqqkiilei agvqagtkvd
      721 atfdgaivpv arailaspmh hlr
//
LOCUS       WP_357529303             280 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF4190 domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357529303
VERSION     WP_357529303.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10619566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..280
                     /product="DUF4190 domain-containing protein"
                     /calculated_mol_wt=29278
     Region          93..147
                     /region_name="DUF4190"
                     /note="Domain of unknown function (DUF4190); pfam13828"
                     /db_xref="CDD:433508"
     Region          <175..266
                     /region_name="Septum_form"
                     /note="Septum formation; pfam13845"
                     /db_xref="CDD:433522"
ORIGIN      
        1 mtqpppppag pvaepgdtpa agpfdpyhas pqpvmttggw pappapphpv ypgasypapa
       61 spvypgapyp apagpggyep sgvprprppv nglaiaslvl alvtllpvsi vtgvialvqi
      121 rrrgqrgtgl aiagivisaa aslslvvagv vgalarmgdq ptqdeparpf yssgwvpghc
      181 iemvdesvgl ewpptkctep hqgevfavfd msgadypgdd avwryattgc dqrlpsyaps
      241 adldeeymiy fptaetwrdg drwiicvayh eeprtgsird
//
LOCUS       WP_357529359             243 aa            linear   BCT 28-DEC-2024
DEFINITION  dienelactone hydrolase family protein [Polymorphospora rubra].
ACCESSION   WP_357529359
VERSION     WP_357529359.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..243
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25447
     Region          20..224
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mrftsetssd gvreqlfilg eipgvlwtpd gatgtrplvl mghgggqhkk apgivararr
       61 fvagcgfavv avdvpahgdr pkeqeydria tdnqarvaag aevapliasf qelvarrtvp
      121 ewravldavq dldhvgagsv gywgvslgcg lgvpfvaaep rvraavlglg galasagsaa
      181 ritvpvrflv qwddervpra qslalfdafg saektlhanp gghgevpafe ldgdvrffar
      241 hlg
//
LOCUS       WP_357529360             200 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357529360
VERSION     WP_357529360.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 200)
  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..200
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..200
                     /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=20867
     Region          18..199
                     /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 mrtgatgrvl hdpkggsfwf dagavcldfa htggegpyav fetlhepadl aewlarpplv
       61 avltvpattg eltaartlrq avweaahara agrplptgav dvinraaaap plapelaadg
      121 ttagwappvl agqalstlar emigllsgpl serirvcagd ncplvfvdss rpgarrwcam
      181 ercgnrhklr alrarratgp
//
LOCUS       WP_357529367             931 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Polymorphospora rubra].
ACCESSION   WP_357529367
VERSION     WP_357529367.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 931)
  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 931)
  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..931
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..931
                     /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=97794
     Region          235..909
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mwrrcavvfe padppragrl afwapdgrpl pddvpdggsd ggsdgkltva vpdgggvavs
       61 tvaarrlpvg aalpllatag pdahpaaafw aaaarealhl vtrgrllpgv spagfdawrv
      121 gpldaddavr igalsaampa waravplpad gavrlpdayp llrafldava ddlprdvdad
      181 gtayagrapv rldglrdwaa elaagvdagv rvslrletpg gdpaagpwra vvqvhgladp
      241 glvadvapvw agsaagfdar apqdvvlavr raarvweplr rllsgpvpdr mvlgddevad
      301 lvdgaagrla vagvavhwpr evdrdvsvra lvgaagagpg gggavfgaga llsfdwqval
      361 ggepltaael evlaaarrpv vrlrdrwvla apevvararq rslpavtavd glaavlsgat
      421 vvdgepvevv addwlarlre rlatpgddrs apdrsgadvg ipaglaatlr dyqvrglrwl
      481 vrmtslglga claddmglgk tvtlialhlh rqadpatagp tlvvcpasll gnwerevrrf
      541 apgvtvsrfh gpdrslpava ggfvlttyat mrldaqrlag ggwalvvade aqhvknpdsr
      601 saralrlvag vaparvaltg tpvennldel waildwttpg llggrttfrr rwadpvqsgd
      661 eaagrrlarl vgpfllrrrk sdpdvvpelp aktqtdqpva ltveqtalye avvrealarl
      721 pgtagmarrg avvslltalk qicnhpaqyl redepvlagr sgklelldel vdaivaggga
      781 vlvftqyvam grllrrhlra rghgcellhg gtslprrqem vdrfqagavp vfvlslkaag
      841 tglnltradh vvhfdrwwnp avedqatdra yrigqtrpvq vhrlvaegtv edriaamlsa
      901 kreladtvlh sgaaaltels daelaelvvl r
//
LOCUS       WP_357529429             403 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Polymorphospora rubra].
ACCESSION   WP_357529429
VERSION     WP_357529429.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..403
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..403
                     /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=43128
     Region          16..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 mmmriaiagg glggltlari lhrhgidavv yereasrsar sqggmldlhp esgqqalada
       61 glaarfrsaa rpegeehril dptgrtlvhh rpqpgsfsgr peidrrvlrd llldslpadt
      121 vawqhrlvaa tprtdggfgl tfhgghsadc dvligadgar svvrslltdt tlsyvatlve
      181 ltisdadrrh pdlaelvgpg nlwcigvnri laaqrlgdgs irvgislpad drhldayrsk
      241 ralldmfdgw npgltaliea gdspptprri eamptgtrwa hqpgitllgd aahlmppvge
      301 ganqamldaa elaaelaanp tdpdsairty eqamftrirp iaemsarvqa mmlsptaadd
      361 iirfftprpt epapasgrpd erarrstrpp gkpvaggrhr msg
//
LOCUS       WP_357529458             231 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357529458
VERSION     WP_357529458.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  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..231
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..231
                     /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=24478
     Region          12..222
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mppavdsapa pprgrriqqt itqlrerila gewpvgsrip tepqlvealg vgrntvreav
       61 ralahagvle crqgsgtyvi stdelapvva rrltddrmte vievrrafev eaarlaarrr
      121 tpedlaalde alaareaawr ggrvaefvea daelhtavva aahngmlael yasigavlrs
      181 tvtqamggal tpdrhvdhar lvvairagdp dlaareagaf leprsggigc p
//
LOCUS       WP_357529431             284 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome c biogenesis CcdA family protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357529431
VERSION     WP_357529431.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..284
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=29045
     Region          28..243
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mgetfgqlav sgplllavga aalaglvsfl spcvlplmpg ylsyvtglag adlegrgtss
       61 tpaaaqgsaa arsggvgtvv rdeqprvraa vkgrvlagtl lfvlgftvvf vstailfsti
      121 grvffdykrp leivigalvv llglgylgvl pglqrelrin rlpsagllga pvlgavfalt
      181 wvpctgptla avlgmaatsg qtdravvlav ayclglgipf vvfglgfnrl lgvfqairrn
      241 srwvtrigga lliliglalv tggwtnvviw lqttigvgdf qvsi
//
LOCUS       WP_357529501             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357529501
VERSION     WP_357529501.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32573
     Region          16..77
                     /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          103..283
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 melsarrqpp tvrlrrlaae lrslrtaagl trdevseqtg inpatlyrie takvrpqrrt
       61 lmamldkygv tdedkrreli alsrqaaqlg wlqayeselp elyttyisfe aearsvrnye
      121 slfvpgllqt enyacavirg vlplatdadv qarvearmqr qeslrktepl rlwaildeav
      181 lhrltggpav maeqldalvt aagqphvtlq vipfttgaha gmpgsfvvmd fpdpadpalv
      241 yvdsmagdlf lereadvrry tstfehlrat aldptssikl iqehaaaisq kggtg
//
LOCUS       WP_357529528             253 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Polymorphospora rubra].
ACCESSION   WP_357529528
VERSION     WP_357529528.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..253
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27152
     Region          17..251
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtapnnddgl wvrrfhpapa grprlvclph aggsasfyfp vsralspave vlsiqypgrq
       61 drrhepcvdn ipelarqvla elgpwrdqpl alfghsmgas lgfeiarlie adqgscahlf
      121 asgrrapsmp rhetvhlldd eglladvrkl sgtnpavlgd pemlraalpa irndyraaet
      181 yayvpgpalr cpvtaftgds dpkttveear awgthttgsf dlqvlpgghf flaqhqaail
      241 raisaaltpt tvg
//
LOCUS       WP_357529549             403 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Polymorphospora rubra].
ACCESSION   WP_357529549
VERSION     WP_357529549.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..403
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..403
                     /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=42722
     Region          6..>61
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          42..388
                     /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(58,60,225,245,318)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mlkrtvfagg tvfdgastsr vdvavsgdri vdvgtsldgd dvvdcsemsi vpglfdchvh
       61 vmvrdlnisr aeqepfslqy yealrnlsll ldqgitsard aagadlgvkr aieqkliegp
      121 rlqiaivmls qtgghsdlhl psggsrsmsm mmphpgrpra vrdgvddvrr gvrevlraga
      181 dtikiattgg imspgddprh thfrddelev iaaeaaaagt dffahaqgte gikaalrhga
      241 rsiehgyhld deaidlmlra dawlvptlsa traivdaadr gvpipagsla larealeahr
      301 asfaravdag vkiamgtdsp pyahpsasnl delqlmteas smtpqdawra atssaaallr
      361 qdglgaitsg mladlvvvdg rlddlrglrd rirhvslggq rvr
//
LOCUS       WP_357529564             511 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357529564
VERSION     WP_357529564.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 511)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..511
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56049
     Region          84..483
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvssdp rrqppgatsi applppangr hhtappvpvs avsataepap rarvdfqvvr
       61 elrrqlseel trwqrgrefs vdeedterar lavllvaeya dsvrragtpm pageerllld
      121 qvtaelaglg rlqtllvddt ieevhilgcd qvritrhggg vdwvepiads ddelveilqa
      181 aarragater slstskptld lqlpdgsrla avflvshrpy avirkhntle vtlddlagsr
      241 adldemidpl vrdflrasmr aglnimvagl agagkttvir almseippde pyvlleesre
      301 llparrtgrh ravmsfeare ghgergpdgr pageisiadl ipvslrmgvl riivgevrsr
      361 eivpmlqamt tsrgsmctih artpggvser iielalahgr emtvdqarrm agnaldlivy
      421 vtvedetgig grkhrfvshi eevigvgdgn ritttkvfap gpdgravprh lpervrdqll
      481 rvgydarlls rwieagqgaw rrpkqtrlgr r
//
LOCUS       WP_357529589              67 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora rubra].
ACCESSION   WP_357529589
VERSION     WP_357529589.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..67
                     /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=6934
     Region          <23..61
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdsaalpaar ggrpagdgrr panwsevaad lgyfdqshfi rdfaaavgmt paayadacrr
       61 rvqpvsa
//
LOCUS       WP_357529551             263 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora rubra].
ACCESSION   WP_357529551
VERSION     WP_357529551.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora rubra
  ORGANISM  Polymorphospora rubra
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 263)
  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..263
                     /organism="Polymorphospora rubra"
                     /db_xref="taxon:338584"
     Protein         1..263
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27218
     Region          8..248
                     /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 mtggeasrvs tgdgvtsfrv egagpplvlv hglqvgqelf aelrphlvsa ftvitydqrd
       61 rgetafapvp yttddltddl aalitalgfs rahvlgtsfg gmvaqafalr hphlldtlvl
      121 gatsqapfrp ervagpvagl lgaleagdde karallarma ptvasvtgdg glrsaparnd
      181 almrrfaatr afdtrgrlaa ivartlvvhg rddamvpiqd alsmageiah advlvlagag
      241 hawendqpar aasaiaafla dar
//
LOCUS       WP_357529698             509 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357529698
VERSION     WP_357529698.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..509
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..509
                     /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=54182
     Region          18..395
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrrlaalaar tpadreryld llralailmv vlghwaiati sydrhgqpdg hsalpslpwa
       61 ypltwlvqvm pvfflvggya naaaltahrn rggevsswll grsarllrpt talvlvlags
      121 aliarlvgae aslvrtviwf atiplwflaa ylavvpltpl myalhrrfgl vvpvalaalv
      181 algdagrafg paelalanyl lgwlavhqlg fawydarhgd crpsspgrep paaaadrspp
      241 rrglrtrclp mspraalvml aagltvavll tgpgpypvsm inlpgqrldn aappsvalla
      301 vataqlglil llrepaerwl rrsrpwqavi avnavvltvf lwhlsavill vggldglgll
      361 ptpaagtraw fawrlpwllm lsavlavlvt ifgpieartg rstasrhhst dqpatdrqhp
      421 adrpaagqrq pdhrqggvdr prgdgrptpw wtvalavagy gavvyamaan svapkaapep
      481 lglpvtalva ylvgagtlrl lrsgwgtpg
//
LOCUS       WP_357529694             313 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357529694
VERSION     WP_357529694.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 313)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..313
                     /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=35006
     Region          12..310
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrhgvgrfvt gflalpvgly lfyvvwpflq aagysltdwg gysdrqqfvg lenylrlfsd
       61 elirkafwhn vfflvtvplf tialalflaf llnvggredk agirgvfgsg lykvifffpq
      121 vlslvviavm wqqiyradgq glingvlmki glvdendpit fvydpepflg vpavlwwllv
      181 iavwsgagfy mvlfsaamqs ipkdiyeaal ldgagrfhtf fritlpllrd tvsvawvylg
      241 fialdmfalv yimtpsqggp nhaseifasv infnafqrgq fgyacaiava laiftillaa
      301 lqlritrrer iey
//
LOCUS       WP_357529711             400 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357529711
VERSION     WP_357529711.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..400
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=42523
     Region          20..359
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mthrivvlga gyagaiaagr larrlhpdqt eitvvnaaad fvervrlhql avgadlavrp
       61 lrdlytgtgv rvrlarvtgv dvdrrivtla eadtsseigy dtlvyalgst aaehpggadh
      121 aydvagaqsa qrlrerlavl eaggrvlvvg ggltgleaat eiaetrpdlq valatrgglg
      181 dwldegarrh lrkvcdrlgi tvhehtdite vratgavtgt dgvipaqvtv wcagfavpsl
      241 vagmavrtap tgqilvdatm rsvshpevya igdaacaegp ggrplrmsca sgvpmawqaa
      301 daiaarltgr pvrstpiryy nqcislgrrd giiqwvtadd qargvhfrgw waarykeivc
      361 rgaawgvshp tlmlptrrrr lspaieprha rppaleakei
//
LOCUS       WP_357529859             129 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357529859
VERSION     WP_357529859.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 129)
  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..129
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..129
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14005
     Region          14..>73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mfphppdpls gppltrlrla rgwsqsrlaa elcaaagvpt lsrheisrwe rqrrtpgrfw
       61 hgwlaavlgv psdppadpge aggpaaaagd rerrrrpcrp asarpptrip rrvatrrnvg
      121 gsarrdpth
//
LOCUS       WP_357529898             449 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357529898
VERSION     WP_357529898.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 449)
  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..449
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..449
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47149
     Region          8..429
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtliaerpgp gaarpyrfpq vvrrtvaggq viaahlpgqn lavavlllda gagrepvgke
       61 glggvlskal eegtsqrdat ayalaiealg telvtgldwd sfqvsvqvpv erlgaavell
      121 aeavrtprld pddvrrvrdd eatalrmdwa npgpradavl radlfgidnr lgrplygdpd
      181 svaaldvedv tvfhsewfir pgtlvvagdl dridldalaa tafagtgggp vdrggpievp
      241 vrtgrriilv drpgsvqstl rlghpgphrg hpdhvpivla gtvlggafts rlnhlirevr
      301 gytygirgdf assrrygrfa vssgvqtavt apalvesvge iartqaggvt edelavarsw
      361 ragqlsvelq spraiagalt tlavhdlpdd yharlrqall dadvaqvsaa aathlypeal
      421 tlvvegdaal irdelvatgl gevidhasa
//
LOCUS       WP_357529982             554 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora sp. NPDC047134].
ACCESSION   WP_357529982
VERSION     WP_357529982.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 554)
  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 554)
  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 554)
  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 554)
  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 554)
  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..554
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..554
                     /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=55210
     Region          <6..213
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          280..553
                     /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 mteyesdprr pantdaepsh pelpraeyar sdslfaapag tgadsggeap tipvravets
       61 dpngqdaept mvglpvagsp ppphsgppay sgppapqapg qqpqspgqps qtpgqqqgpg
      121 qqpqgpgqqh wgpaapqqyq pgarypagpw ypsqpgwaaq aqqspsggyp gyqsgqpgtp
      181 gyqsgqpgvp gypgqqppwa apqsggprpg riakfvgagv avfalmlgsg vaggtlalal
      241 sdggsitrtf saapvidgad lpriaasvqd svvsistgsg egsgvvltad gyvltnnhvi
      301 agggdtvrvi fangtnaqaq iigtdprtdl avvkangvtd lkaatfgdsd amqvgdqvla
      361 lgsplglqgs vtagilsard rtiqagsger lpgqavssis gllqtdapin pgnsggalvn
      421 trgevigint aiatagqgnt gnigvgfaip snkakdiadk lqrrekishp slgvsvtgtt
      481 eggalinava pgsaaeragl ergdviirfg dkvindsndl vgavqagkvg dqvevtfqrn
      541 gaestatvtl aeas
//
LOCUS       WP_357529983             310 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357529983
VERSION     WP_357529983.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 310)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..310
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32422
     Region          13..229
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msdgqsrpnd aqivvsgltk qyrnvlavnn lsftvqpgrv tgflgpngag ktttlrmlln
       61 lvtptagtat iggrrypelt eplrhvgavl eassahkgrt ginhlrvica aaglppqrad
      121 ealalvgltp aakrkfkgys lgmkqrlgia aamlgdprvl ildepangld pegirwmrgf
      181 lkglaaegrt vlvsshllse mqlladdvvi iaagqlvrqg pveqvigsma qgvrvrvrtp
      241 qaealtsala egpatvqtde hgalliggvd aptvgraalt agvelheltt erpdlervfl
      301 eltagkagir
//
LOCUS       WP_357529988             302 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357529988
VERSION     WP_357529988.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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 302)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..302
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..302
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31695
     Region          11..277
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mgirrrfaas tvalllvwlt gcaasggppa rgtspgaapq vqyavgvrtf vldpgsarpl
       61 pvtlwypteg srvaegrfpv vlyshglasl pelhagltsr waaagfvvaa payphtrrga
      121 pefsradvrh qpadgwrvir hlvrldrraa dplaghldvq riaaaghsag gfttsgmfts
      181 grparlragi viagggmags fagppapmlf vhgtadpvva lsvgraayrr ttgpasflsl
      241 lgqghgeylt pgrpgftqfl gtttdflrwt lygdqqaarr lpthahpptl atletrplst
      301 pr
//
LOCUS       WP_357530040             370 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530040
VERSION     WP_357530040.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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 370)
  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 370)
  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 370)
  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 370)
  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..370
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..370
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40680
     Region          79..220
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 msemlrapae vkyadeldyl esvdtgpkpy swrlsprmvr lfvlgserad gldrdipqkw
       61 fgdrsfvers ivtlasdrgl lligdpgtgk swlaellsaa icrnstlvvq gtagttedhi
      121 kyswnvsmvi akgqsresmi pspimtameq gvigrfeelt rstsdvqdal isilsekyvs
      181 ipelnddniv fakpgfsiia tansrdrgvn dlssalkrrf nfvripvitn krseaeivrf
      241 rteellrrhq velevpptll dillqsfadl raaaasatsd deklesalst aeqigvleda
      301 ilhsqffgdr tlragtlags lvgslarrsp edlailnkyl havveprakq dggewndfld
      361 ggrqsiaals
//
LOCUS       WP_357530071             180 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530071
VERSION     WP_357530071.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 180)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 180)
  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..180
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..180
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19258
     Region          21..84
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
ORIGIN      
        1 mheaardpvp qtatageyvg llrdirrrsg ltyreisrra saaghwlpps tlatmlgrtt
       61 lpreqavval ltacgmppat ieqwvglrhe idvrlnepnr pvggpmsaec cgvrhpsrep
      121 lppvtsypag rrlhpaviav agallgaygm rlahrrdaap rpvhgpdgep pltaiddsrs
//
LOCUS       WP_357530089             141 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC047134].
ACCESSION   WP_357530089
VERSION     WP_357530089.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..141
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15318
     Region          25..120
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtsllgtela qrgvapdciq tielvrdvla rvgdkwtllt itvlasgplr ftalheqvtg
       61 isqrmlsqtl rgltrdglvt rtaypevppr veyaltplgr slseavdgla hwvrghqsdi
      121 lhnrhefdqa paenpaalph a
//
LOCUS       WP_357530087             108 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530087
VERSION     WP_357530087.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..108
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11678
     Region          3..108
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mvrdellrlr araeaeavtl aqdlealfla srdsnaddeh dpegatigfe raqltallag
       61 areriadvdd alrrvdaaty gvcercgqpi gderlaarpf arycmaca
//
LOCUS       WP_357530102             984 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530102
VERSION     WP_357530102.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 984)
  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 984)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 984)
  AUTHORS   Rosinski,J.A. 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 984)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..984
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..984
                     /product="helix-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=102410
     Region          <4..916
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          927..981
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mqievlrgrq gecreirsll aapaggalll hgepgagrta llayahrhra grrllaaagl
       61 adeatlpyag lqrlldpvld haealperqr qvlcralage gcpeedrlil stavlgllas
      121 aahagpllct mddldagdvp taqvltfvar rlahlpvvll ltsatdtaaq aipghrllpl
      181 drtdslalla arcpgppppe pvlaamggla cgnpqalvdl adsltpgqwc gaeplptmpp
      241 adgvlgrtyr avlarlprdt rgalllaaia aadpanptpt graaavdplt lgralraags
      301 gvealapaea aglirittpg gadfprrlar smieatasva arrdahllla avldgpgsrl
      361 rralhqatvt aghdpalate leqaaaahqd rsvaataltr aaelsddpal atarqvtaar
      421 yawqagqper aqallhrvad atgapppqpi gcrtaglpmt paaptgrsav glpiprpast
      481 gcsvpglpia apastgrsai dppvtaatgg laellrgemh lrcgrastal stlltaatal
      541 adidresalv alvrageavc fsgdhyryae varrvqalhr dgdppwvdll ttlvagvaat
      601 lrgehahggp llrravalgg rltgaavtpt altgaaaagl lvavdaaayr laedavdlat
      661 drgevsllpr alelramsey wlgrhdaaak screglrvar aagqhatagv hlgllavlsa
      721 vradhdaclg hvaelgdtaa pgsrpyalaq walgvldlvd gryadavdrl atlarpgtgr
      781 gqvlvqvmat phlveaaahd grtararaal avfdrwagst asplrralsa rchallaprg
      841 saeaeehfer alclhpadaa aferartell ygrelrrnrr prdardhlhr arqtfvllga
      901 dvwarqttve lraagesvgt pdrqavrllt gqqlriaqlv aagatnreva mqmflstrti
      961 dhhlrniyhr lgirsrtela ralg
//
LOCUS       WP_357530114             473 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530114
VERSION     WP_357530114.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 473)
  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 473)
  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 473)
  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 473)
  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..473
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..473
                     /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=49397
     Region          5..471
                     /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 mteweydvvv igagpvgenv adrvvqgglt aaiverelvg gecsywacmp tkallrsgsa
       61 lraarqvpga reavtgdlds aavlarrdsv aahwrddgqv swlesagivl hrghgrissa
      121 kvvevtgadg attrltarha vvvatgsssr madlpglaaa apwssreaas arsvprrlai
      181 igggvvatem atayaalgss vtvlarsgvl psmerfaadr vveslreagv tvqldaeava
      241 vhrddsgtvh iettrgerve adevliaigr tpntgdigld tvgltpgdwl pvddtmrvld
      301 gggwlyaggd vnrrvllthq gkyqaravgd vivarakgek vedgrwgrhv atadegavpq
      361 vvftdpevaa vgltaaaaea aglrirvvdy dlgrvagatl hadgyqgqar mvvdedrkvi
      421 vgvtlvgpdv aelihaatva vvgevpldrl whavpayptv sevwlrllea ygr
//
LOCUS       WP_357530144             234 aa            linear   BCT 28-DEC-2024
DEFINITION  PIG-L deacetylase family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530144
VERSION     WP_357530144.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..234
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25540
     Region          5..219
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mtrrllisph pddavwscgg vmgewaaadq sltvvtvfdg dpsapgpaar gatepalrrr
       61 edaaalarwp ltrislglpe alfrhdpdgr alypgplavr rrvhpadesl tvrvaqalrp
      121 llmrcdevll plaaashvdh viareaaefa lgdlappavr yyaefpyptr lpqgltahrq
      181 padfdawlra alvyrsqveg mfgsaprlar alfrhayeag tpvwrswtps aary
//
LOCUS       WP_357530155             334 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530155
VERSION     WP_357530155.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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 334)
  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 334)
  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..334
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..334
                     /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=35632
     Region          10..254
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtttahtppp vrigllgcad fairrmlpai drcpdtllta vasrdrstar ntaqrfgaca
       61 aesyeavlaa pdveavyvpv paalhaswve rallagkhvl aekplttays dtlrlaalar
      121 eaglvlaenv lfvhhgqhah vrrlladgai gelraasatf tvparpaddi rlrpeldgga
      181 lwdvgvyplr aamhllgndl evigatlthh peyevdlgga allrradgvt aqltfgldhq
      241 yessyrlvgs tgrielthaf tppaehrpti rlttsagvre itldaqdqct ramasfaaai
      301 regrpgteda vvaqarlldd lrrrattspa peap
//
LOCUS       WP_357530168             372 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530168
VERSION     WP_357530168.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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..372
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..372
                     /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=38615
     Region          3..346
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgdphgvgiv glgfisrayl etlvghpavr ivavadldpa raaaaaaaip gaeavsvegl
       61 lrhpevttvl nltipaahae isgaaieagr nvygekplta tfpqgrsiid raaaagvrvg
      121 capdtvlgig tqtaraaieg gligrplaas avmvtpgher whpepdfyya pgggplldmg
      181 pyylsalvhl lgpvraviga asrlrdvrii gsgprqgqri pvevpthvtg vlehadgalt
      241 tlttsfdgvg ttaapievhg eagtlavpdp nhfdgtvrrr alsdpewrpl epragyvaaa
      301 rgvglidlvr addtrppras gelalhvldi mtallrsaee grrielttta erpapvpltp
      361 aeewrsaltv rr
//
LOCUS       WP_357530204             273 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530204
VERSION     WP_357530204.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 273)
  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..273
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..273
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28211
     Region          1..269
                     /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 mtelrtitve gspvhlmesg tgpavlmlhg sgpgttgsga waataqalgt swhliapdha
       61 gfgrtpvpag argglrlwte qaaglmdalg iehyavvghs mggavalala aarpqqvtrv
      121 vavstmgapg aplsadleai waapagppga rdmlsrlvyd qrlvtdaava araaamraga
      181 aayaslfppp rarwvedltl spqtlaaira pvllvhgaed rvvpltaatq pllehladvr
      241 lqvfsrcghv paiehphefr hllsgflsqe srh
//
LOCUS       WP_357530263             442 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530263
VERSION     WP_357530263.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 442)
  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..442
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..442
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47423
     Region          23..437
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrsaggatra vtrtlsedpl ggtvrrtvlp sglrvlteai pamrsvsfgi wvavgsrdet
       61 gstagaahfl ehllfkgthk rgameisssi eavggetnaf ttkeytcyya rvldedlpla
      121 idvmcdlvad svlepadvet ergvileeia mhddepgdev hdlfaravyg dhplgrlisg
      181 tsdtvtpmtr rqiqtfyrrr yvapqiviaa agnldhaavv rlvrqalrgt pldtdpappa
      241 phrpaspavr trsartvvev keteqahivl gcpaidrldd rrfalnvlnn vlgggmssrl
      301 fqeireqrgl aysvysyasq yadsgvfgvy agcapgrvde vlaltraela rtaahgitea
      361 elargkgmsk gafvlgledt gsrmsrlakg ellygnlmpv nellarvdav tledvntlaa
      421 dllarpmsla vvgpfadrdf pa
//
LOCUS       WP_357530316             161 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530316
VERSION     WP_357530316.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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 161)
  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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..161
                     /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=18040
     Region          8..146
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mtlytprraa rvllvdradr lllfrgfdpa rpedgrwwft pgggldpges ypegaarela
       61 eetglrlamt qfgepvhaev tefsfdgvwy rqeqrfflvr vaahevdttg fsevernsvd
      121 ghrwwsaqel rstaercypl dlpevliral astatapgap c
//
LOCUS       WP_357530373              80 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: type II toxin-antitoxin system RelE family toxin
            [unclassified Micromonospora].
ACCESSION   WP_357530373
VERSION     WP_357530373.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 80)
  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 80)
  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..80
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..80
                     /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=9169
     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 mkvqidrdvl vwlhkqprnv fltvlsailg lvsdpvpqns temrdgsgrr lrvgdyrily
       61 rldrdeltih avghrkdvyt
//
LOCUS       WP_357530388             307 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530388
VERSION     WP_357530388.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=32139
     Region          43..244
                     /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"
ORIGIN      
        1 magstvepth gggepapaag rpvapsgaga gyrpsrtlpf aaefrrqasr rrtqlalgfm
       61 vllpliilia fqfdtgdddn grgefgslvs fatsgglnft lftifvsasf llvvvvalfc
      121 gdtvaseasw gslryllaip vprarlltik llvaltysgl alvllagtal ligtlrygws
      181 plrstvaaql epgegllrll avlgylavvl lvvaglafll svitdaalga vggavllwil
      241 ssildqital gairsflpth ystawlglls tpvqtddivr gavsaicyat afwglafwrf
      301 trkdvvs
//
LOCUS       WP_357530449             925 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530449
VERSION     WP_357530449.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 925)
  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..925
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..925
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=99331
     Region          44..924
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          694..722
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(695,698..699,702..703,705,735,738..739,742..743,
                     745..746,777,782..783,786)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          733..771
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          776..802
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mssrihlpag wvtfvftdie gstrlaqllg pgyrpvlaeh rrllrrtiaa tegaellteg
       61 dsfflafdda saaitaclta qralrehewp tpesaprvrm glhtgwaepr dgeyaspevh
      121 raarvaaaah ggqvlcsaat arhadplptg aslldlglhr lrgfddrerl fqlvapgler
      181 qfprprtada eahnlpvqvt sfvgrqaera dlrelvvrhr lvtvlgaggg gktrlaveva
      241 tdlvdeypdg vwfvdiasvt dsglvafaia avlglrpepg rpmidtlvey aanrrmlivl
      301 dtcdaqpsac adavtrllag gsgvrvlatt replalpgel vwripplsvd ppadgsesda
      361 vallldrtaa arggrqpdpa esadlrrvvr rldglplaie laaarlrvls vgqlaerldd
      421 vlgtldagrd dppqpstadt prssggstgd eqpelsvrta aerhltmqat vtwsyrtlgp
      481 raarllrwla vfagpvdlet vewllgddpl dplsvlvdks lvlaephasg ytyrmldpir
      541 ayaarrlaea geerdarnrh vawsahaleq ahlgpdgepv tlslyaldpl agevraalrw
      601 catggsarig lrlaggleqw wrerglareg rlwlfrlygr laetgevvpe gelaaayhlh
      661 slhagadgey aeelrysqra eaaarqagdv gllarvlagr aaplvdlgqf aeaericrev
      721 idwahdqgvd sealfavfrl aellwlrgel deaaellgaa rpveaarpve rgrrsvdmll
      781 gmvalargdl vaahehllaa lrsrmhhgfh gracdtlnai avrcavggap ltaarlfgaa
      841 qvtratlrst pgiydaywmq eqaalrrilg dtafdeayge gaelgldeav alalgvehpd
      901 laadsdrfaa egcrsgpcqs aatad
//
LOCUS       WP_357530457             445 aa            linear   BCT 28-DEC-2024
DEFINITION  TrkH family potassium uptake protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530457
VERSION     WP_357530457.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 445)
  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 445)
  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..445
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..445
                     /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=47319
     Region          8..440
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mhrffrhpvr lvplaflvai gigtgllmlp pmtaprhepa plltalftat saisvtglts
       61 vdtptfwsat glvvimvltq igglgiltga alvvltvsrr lglhnrmlvq aetleygign
      121 lgrlllriga tvlaceaamt aivtvrlwlg ydyplgralw sagfhaiqaf nnsgfslyph
      181 gllslardpw vclplalgsi igglgfpalf eavrewrhpi rwavttklti wgslalvllg
      241 flvllliews nartigpyav gdkilaaftq ialsrtggie vvpiaglree typlltglmf
      301 igggsastag gikvttffll afiiwaemrg epdvtvghrr vatasqrqal tvallsvaiv
      361 avgtllliam thqvpfdaal feitsafstt glsvgvtsal sdaglllltv lmyigrvgpl
      421 tlgsaialnt rrrlyrypee qpivg
//
LOCUS       WP_357530462             248 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Micromonospora].
ACCESSION   WP_357530462
VERSION     WP_357530462.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  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 248)
  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 248)
  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 248)
  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..248
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..248
                     /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=25516
     Region          1..246
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 maerlavvsg ggtgigaava rtlvadgcsv lvlgrraevl aatadrirae tgrpeavrpv
       61 pvdltdpeqv grvleavgdr pvdvlvnnag afhspqqdsl tgiadywrat ldtnvltavl
      121 ltealrprlr rpggrvilis siaaqrggde ayaaakaalh gwayslaaql gpeqitvnvv
      181 spgyvaetel fvgrmtpegh akrvaatlvg ragtpddiae sirylaspaa gyvtgqilgv
      241 nggsvlgr
//
LOCUS       WP_357530492             993 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530492
VERSION     WP_357530492.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 993)
  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 993)
  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 993)
  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 993)
  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..993
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..993
                     /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=108407
     Region          1..244
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          110..993
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(866,869..870,873..874,876,906,909..910,913..914,
                     916..917,944,947,950,953..954,957)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          866..894
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          904..938
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          943..972
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfrilgplc vgegdttita prdrvvlavl llranrvvsv ddlvdaiwee hppatsraql
       61 qtcvsrlrqr ladlglspdt iatdpagyai rirpgeldse ifarrveagr aalasgwlid
      121 arrqfrsale lwrgpalagi pqrsvrrraq aldeqrlavl eecvevelrl ghagalldel
      181 teqleqhplr erlrgqlmla lstvgrqada lalyragrrl yaeelgiepg palqelhqrv
      241 lagdlavagp eprsnvpvra lpraitdftg rmetvtrlvk eieegearih lidgmagsgk
      301 ttlavhvath ladqypdaql fidlhghsdr apltpgaala tllrqlgvpt eripvdlddr
      361 laiwrtelad rralvlldna asaeqvapll psgagcltli tsrrrlvgld egrpsslpvl
      421 atdeavellg rvagvervaa epeaavevvr rcghlplair laggrlvhrp rwrladladr
      481 lagsrdtlae lavgqrsvad afalsyvqas paaqrtfrll glhpgvrvdt ataaaiagvp
      541 laevqdalde lvdahlmdep epgryrlhdl vreyartlla dpanaterha algrllghhl
      601 hvlvaiatpy etpssrltlp rdlpdppcpd avagcidrgm awfdenrcnl vplatmates
      661 fphhawqlar aswrllylgg hleelleihh vglcaaealg neqaqvlmln ylasahvrra
      721 rfgqanallr ravelcrrag pphllrrlla niaignciig eprrgievfn eaaaaigggn
      781 vaercdllnn lthatcalgr yeealrlsrr hlllarevgd prhlatalgh vgivrhrmgh
      841 tgpagrllrm alvlqrqlrn rfdegevlne igmmareagr peeaaalhrq ayiaisdggd
      901 ligecrsrnl laralldqgd vrsaqdlfgr vlldatkinh ryerahaldg larclrdtdp
      961 agarsywfra lsllrevesp daeeieglla ela
//
LOCUS       WP_357530495             328 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530495
VERSION     WP_357530495.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 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   5  (residues 1 to 328)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..328
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..328
                     /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=35224
     Region          247..320
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrievtpadl aasryaispl getvsalrlh agqrstdglg pwvtrtrpay drlrrevpav
       61 gallallhrg gynadfiqpp pdgsardfhg elaavratpl aqardelarn lagpratppa
      121 yarqiyaspk mvdliadaie aawqalvepd wprlrailer dlvrragrll aygwgaaiad
      181 ldprlrwipg evgvieisgd dpethslagr gllfvptvfg tlityveqpw pyaivyratg
      241 vaellgppdp trpddaldrl vgrsraavlr alalpattsq lvaqlglslg gvgdhltvlr
      301 eaglvsrira gravryrrtp lgdalaad
//
LOCUS       WP_357530546             237 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530546
VERSION     WP_357530546.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 237)
  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 237)
  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..237
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..237
                     /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=25519
     Region          43..197
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mthrvetadt rhspawlqpl lvrlgtarte dftqlrtpeq garesavlvl lgeaetgpdv
       61 lvlqrsatlr nhagqpafpg gaadpedada aatalreane evgldtssvt lltelprlwi
      121 pvsdfvvtpv lawwhaphpv harepaevah varlpiaelv dpdnrmrvrh ssgwigpafs
      181 vrgmlvwgft agvlsalldm ggwsrpwpqd rvvelppmgq tpapsagtdq adesamr
//
LOCUS       WP_357530484             334 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530484
VERSION     WP_357530484.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..334
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..334
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=35842
     Region          39..334
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mpvrrrshrt liallaavmm lfglgavpay aepneggskk lrdtleatak ahieakrkld
       61 gskkrqkkma kelseleerl aelslmvgev aaqsyrigrl saaaalldsg tpeafvqraa
      121 sldmmaqrdg rrvrelaear eqarqaklai naevreqtkq laviakkkke teaalaavss
      181 gssggfsggn stsakpaprn angswpsesc svndpttsgc itprtlhalq qtqaagykry
      241 vscyrsggsg ehpkgracdf saatngfedr tatggdkayg dslaawhvrn adrlgvlyvi
      301 wyrqiwhpgt gwrsyggsgs paadhtnhvh lsmy
//
LOCUS       WP_357530585             548 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP and VCBS repeat-containing protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530585
VERSION     WP_357530585.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10608369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..548
                     /product="FG-GAP and VCBS repeat-containing protein"
                     /calculated_mol_wt=54894
     Region          116..198
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          179..217
                     /region_name="FG-GAP"
                     /note="FG-GAP repeat; pfam01839"
                     /db_xref="CDD:460357"
     Region          393..431
                     /region_name="FG-GAP"
                     /note="FG-GAP repeat; pfam01839"
                     /db_xref="CDD:460357"
ORIGIN      
        1 mstlaigvgl avsvpapaaa ndyrtvtrdg ivlqhyrvak attpvkgtgp trsdfdgdgi
       61 ddiaasadps eyrfpqapmg lavvryssap yvdyfatavt pgagepafge vlaagdfngd
      121 gyddlavgdy geydlsakan aggvwvipgs gtglrldgak hftqstpgvp gaseqgdwfg
      181 salaagding dgrddlavga ygeaigklty agavtvlygg asgltgtgaq qlhqnqaavp
      241 gsaerndhfg wtlaigkvnd nkyadlviga pgenedsspt gsgmltlmwg sangvklsga
      301 tsvtgaalrk atgrddsyvr slgmalaigd vnsdklgevi agapytqspk gnegmvavft
      361 grtggaglss savklfsqrt pgvpgsaevg dlfgatlavg dvtgdgradv lvgapgeaig
      421 tkkragtval lkgsasgltg tgaqgfdqdh pvvpggaesn dlfggevail nldgkgplda
      481 ivtspgelvs adperpasgs valfhggsgg lvpqsaswsg asmrtdfvwp kwygrrlata
      541 qsgalmyh
//
LOCUS       WP_357530678             193 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530678
VERSION     WP_357530678.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 193)
  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..193
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..193
                     /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=20598
     Region          4..190
                     /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 mtvatvrrps aqpglkivlt gplgvgkttl vgavseivpl ttevgmsagg ddvshcpgkv
       61 tttvamdfgr lavddvtvyv fgtpgqtrfw fmwdaivrga vgavvlvdtr rlqdsfrhld
      121 yiercrlpfv vavnqfpdar vysptqvrda ltlagdvpiv evdardrdsv rrllialveh
      181 viaatrtpag vas
//
LOCUS       WP_357530681             600 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530681
VERSION     WP_357530681.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..600
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..600
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=63914
     Region          <207..334
                     /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          357..594
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msladriaav svadavrasv sydqlrsydg slywletrpn aggaatltqw rrdegtrdis
       61 pagfdvtndv haygggsyav adgelwcvga gglyrsrrrd gefvlvspvs vgdltvgdge
      121 llavreterg delvampltg slrlrtvtgr ggflsaprpa agllawsawg erdmpwdace
      181 lwvgsyssqg higspvkvag grdesavepr wgpdgslyfv sdrdgwwnlf rwdgreveav
      241 apiagecaae pwemgyasya flddgrivva vqegsrhrlv lidlqgsvrp vdlpytsikp
      301 ylaahgttva migssptaap qialvhladd dpqvevlaks ehpelfgtqv stptelrvqa
      361 aggrevsalv ypptgstaew rapvivrahp gptascllrl dwqaqfftsr gfavvdvdyl
      421 gstgygrafr eslygrwgld dvddcaavaa hllaagrasp grifirgasa ggytalhava
      481 rngpfaaata vsaivdpdrw aetvprfqra halrlrggag rvrasavqrp vlfihgtadd
      541 vavvedvral adqlaardvs hrllllpdvg hyvatsaeag taleaelahy ravmmaavts
//
LOCUS       WP_357530674             266 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530674
VERSION     WP_357530674.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..266
                     /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=28748
     Region          29..257
                     /region_name="LivG"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivG [Amino acid transport and
                     metabolism]; COG0411"
                     /db_xref="CDD:440180"
ORIGIN      
        1 mrsvhrvdpd qppaprsrrd pdhahrtglv atglrhaygp ltvldldtft iapgdrhavi
       61 gpngagkstl lnvlagtlra hsgqltyngh pitrwtptwr aragigrtfq hptlwpdltc
      121 ldcvrvggwh hrrnpdhtpi evlnqvglad hadqpanals hghrrmldla valagqpril
      181 lldepaaglt dtdtgrlldi lhalpswmai viiehhmdvv aafadwitvl hhgrrhtdgp
      241 ahlvradpav atvylgttgg sdaahp
//
LOCUS       WP_357530673             243 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530673
VERSION     WP_357530673.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,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 11417798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..243
                     /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=25514
     Region          1..>186
                     /region_name="LivF"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivF [Amino acid transport and
                     metabolism]; COG0410"
                     /db_xref="CDD:440179"
ORIGIN      
        1 mlhtrdltva ypdgpsvlhd vtldlrppgv halvgpngag kttllhtlag hlqpisgtvh
       61 ldgrdvtgwh ptaaahagva lapqdrrlwp sltvaehfaa trpaasrden wtveelldif
      121 pplaarmghr ahqlsggeqq mltiaralrt aprllladep teglapivad qittvlrnvp
      181 trgvtvlaal phaaaaatva dtlhviasgr llgdthtsaa atsalrrhlt ltrpgdepak
      241 pdq
//
LOCUS       WP_357530698             103 aa            linear   BCT 28-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530698
VERSION     WP_357530698.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 103)
  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 103)
  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..103
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..103
                     /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=10513
     Region          2..>98
                     /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 mtvlaiivgg gigatlryll glglapatpp hfpwvtfvin mvgafalgav mtllaahklr
       61 gpwgkpflst gviggfttws hlivesdqli gagavgwass tws
//
LOCUS       WP_357530704             390 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530704
VERSION     WP_357530704.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=40333
     Region          1..390
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 msdavivgav rtpvgrrkgs lstvhpvdls ahvlqalaer tgidpaqvdd viwgcvsqvg
       61 eqswnvarna vlaagwpesv pgttldrqcg ssqqalhfaa atvlsgqadl vvaggvesmt
      121 rvpmgasvag aqpfserila ryrgvegvae daplpfnqgv gaeliarrwr lsraqldefa
      181 lashekaaaa qdagaftdei apvtladggt faadegvrrd tsleklgelp tpfrpdgvvt
      241 agsasqisdg aaalavttse wasrhglrpl arihtavvaa ddpvamltap ipatakalrr
      301 aglgieeigv yevneafapv plawlaetea dperlnprgg aialghplgg sgarimttml
      361 ahmrdngiry glqtmceggg manativell
//
LOCUS       WP_357530716             408 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530716
VERSION     WP_357530716.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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 11461692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..408
                     /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=42902
     Region          <172..399
                     /region_name="LytS"
                     /note="Sensor histidine kinase, LytS/YehU family [Signal
                     transduction mechanisms]; COG3275"
                     /db_xref="CDD:442506"
ORIGIN      
        1 mggnlsaivg vlslvavlaa alfgvarsra rraiatpgqr atyevlhtag laaeplragl
       61 npanaakaar hlrslvgaeg laltdtedll aldglgthhg rqlwaaaqrv iaaerstvlg
      121 eaelfcdrld cpvrgavvap lvgaegrvvg alvavtdgvp apglvqasle tahwagsqla
      181 laeldssrer laraevralr aqisphfiyn altaigsfvr tdperareli lefaeftrys
      241 frahgefttl aeelrsidry ltierarfgd rlqvrlqiap evlpvtlpfl clqplvenav
      301 rhglsrkpgm gmvsieaqda gaechitved dgvgmdpgtl tagiaelags ggdpgddpgq
      361 hvglsnvder lrsvfgdgfg lvvetdlgtg tkvsmrvpkf hpgvrana
//
LOCUS       WP_357530730             413 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530730
VERSION     WP_357530730.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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..413
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..413
                     /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=44561
     Region          191..413
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpdstdysal iaghtaiiem insgdaglpv ltrllrmaep tlgaagmafv efapnggrvi
       61 aatgaaewtl gwplpandpa tacllagprv rcvrtdhltn dlarqladrg lrrmvvsrae
      121 lgghtvgslh alyqagreep steqrgviay lgsciahlyg dqnglpvhgd apavtdgpav
      181 ddpddqedpe kerdlfvavt shelrtpvtv ikgyadtlsd hwdslseadr rqaarvirqr
      241 anelarlldr llssaaevwp gdgpptpfdf getlraaiad lptdlrrras vevptelpra
      301 vghrqslatv ltelvtnagk ysppgspiei sasadartvn lrvsdrgigv rpehverafd
      361 rfwqgdsgdr rrypgtglgl ylvrriveqq ngwvflqprt gggtvaevrl prr
//
LOCUS       WP_357530735             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530735
VERSION     WP_357530735.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..265
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28042
     Region          30..258
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msldpravlt rpapepdltv sygehpdqia dlrrplgegp prplvivvhg gfwrveydrr
       61 htdaladala rlgfpvaqle yrrtgqpggg wpgtlmdara gvaalpelaa ealpgrvapv
      121 ppilvghsag ghlalhtair spqtvggvla lapvtdlaea yrldldsgav aallgggpad
      181 fperyevadp ritaplpirt vvihgtldqq vpvemsrkyv aaaqalgaem hlvelpeceh
      241 fglidplspa wpqvtaafrs lhtdh
//
LOCUS       WP_357530778             237 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530778
VERSION     WP_357530778.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 237)
  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 237)
  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..237
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..237
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=26103
     Region          18..213
                     /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 mlspvtnlal gpdwldpewl istfgligil vivfaesgll igfflpgdsl lfttgllvad
       61 gqylkyplwl vcllitiaai agdqvgylfg rkvgpalfrr pnsrlfkqen llkaheffek
      121 ygarsivlar fvpivrtftp ivagvsrmny rtfviynvvg gilwgtgvtv lgyflgqipf
      181 vkaniefili givgisvlpi avellrawla arrgvtpqer aaaeeairet rehygkh
//
LOCUS       WP_357530815             396 aa            linear   BCT 28-DEC-2024
DEFINITION  mechanosensitive ion channel family protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530815
VERSION     WP_357530815.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 396)
  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 396)
  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 396)
  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 396)
  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..396
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..396
                     /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=43220
     Region          88..345
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mhsylvtvva alaaaatavv vvevvhrlik rwgrrsvllt elaehahraa qvaatvlavq
       61 fairfstgya vgtawrqvll hllvlaviaa tawlvtsllv vvedtalarf rvdvpdnrqa
      121 rrvrtqvvml rrvtivvivi ltvgvmlmtf pavrgigagv ltsagvvgiv aalaaqsllg
      181 nlfaglqlaf sdavrlddvv vvegewgrie eltltyvvvq iwddrrlilp tsyfistpfq
      241 nwtrteaavl gtaefevdws vpvqamreel rrlvegtelw dgrvcvlqvt datggmikir
      301 alvsagsaga lwdlrclvre hlvawvrdhr ptamprlrae vgdgagtlpw qwvrparapr
      361 rhaevpddar lfggsddgea rseafvgpee paqtrh
//
LOCUS       WP_357530846             447 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530846
VERSION     WP_357530846.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..447
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..447
                     /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=48455
     Region          6..>179
                     /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 maasgravvi gaslggllaa ralvdsfaev illdrdvppa epvhrrgvpq grhvhvllar
       61 grqalecllp elgaelyrlg atpvdlhgqv hwyndghrmr sarsdltgfg msrplleqav
      121 rqrilalpgv rlvpdcevtg llatadgrrv tgvrlapreg paatltadlv vdaggrasrs
      181 piwlaelgyp tveqervevg vtyvtrryrr edgqledklg vlsnampgra rygvvapqeg
      241 grlavtvagi lgeappvdea gfiryatsla apqvgelvrq aqpldepvlm rfpasvrrry
      301 erlsrfpdgl lifadalcsl npvygqgitv aavqalllrs llargrhrla rrffrraarv
      361 idgpwsiavg tdlrfpgvtg rrtwkvrfvn aylarlhvaa ardavlgaaf lrvvnlidpp
      421 arllgpdvml rvllgrrqrp sassmar
//
LOCUS       WP_357530864             697 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-1,4-glucan--maltose-1-phosphate maltosyltransferase
            [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530864
VERSION     WP_357530864.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 697)
  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 697)
  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 697)
  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 10571012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..697
                     /product="alpha-1,4-glucan--maltose-1-phosphate
                     maltosyltransferase"
                     /EC_number="2.4.99.16"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009313 - oligosaccharide catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0030979 - alpha-glucan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76860
     Region          3..188
                     /region_name="GlgE_dom_N_S"
                     /note="Alpha-1,4-glucan:maltose-1-phosphate
                     maltosyltransferase, domain N/S; pfam11896"
                     /db_xref="CDD:463388"
     Region          193..553
                     /region_name="AmyAc_GlgE_like"
                     /note="Alpha amylase catalytic domain found in GlgE-like
                     proteins; cd11344"
                     /db_xref="CDD:200482"
     Site            order(252,256,267,269,312,344..345,347..348,380,382..383,
                     411,467,520..521)
                     /site_type="active"
                     /db_xref="CDD:200482"
     Site            order(330..332,339..341,354,385..388,390,393,415,417..418,
                     421,425)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200482"
     Site            order(382,411,467)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200482"
     Site            order(414..416,433,436..437)
                     /site_type="other"
                     /note="acceptor binding site [chemical binding]"
                     /db_xref="CDD:200482"
     Region          <541..591
                     /region_name="PRK12313"
                     /note="1,4-alpha-glucan branching protein GlgB"
                     /db_xref="CDD:237052"
ORIGIN      
        1 mtgrfpiedv spvvscgryp aravvgelvp vsatayregh dalgcnvvwl gpdgrarpft
       61 rmrpgepghd rwhatitpdt vgewvftvea fsdpyltwhn avtkkiaagq gaedlandla
      121 egvrvlgaaa vpkaeqarle ravaalrdtd lplkdrvgpa ldlaellwah pvrelvttge
      181 ayriwvdrer alysawyeff prsegavlat aetparsgtf ataterlpgv aamgfdvlyl
      241 ppihpigrvn rkgpnnslva gpedvgspwa igaaegghda ihpdlgtpqd frdfvaaaae
      301 hglevamdla lqcapdhpwv tehpewfttr adgsiayaen ppkkyqdiyp lnfdndpegi
      361 raeilrvvrh wvgegvkifr vdnphtkpvd fwhwliwevk rvdpevlfla eaftrpammh
      421 glakvgftqs ytyftwrtsp admreycael vaaadymrpn fwpntpdilp enlqhggppm
      481 fkiravlaal lspswgmyag felfehvarp gaeeyldnek yelrprdwaq aqaqgrslap
      541 fiatlnrvrr enpalhrlrn lvfhdidnpa llcwskrdps tgntvlvvcs fdshtvqwgn
      601 ttldmpalgl dwhdrftvhd eltgahydwg qhnavrldpy lqpahvftlr ptdaaapspa
      661 paatatpapi tttvpataag lsggtasatk ddarwts
//
LOCUS       WP_357530881             170 aa            linear   BCT 28-DEC-2024
DEFINITION  HIT family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530881
VERSION     WP_357530881.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..170
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18555
     Region          33..159
                     /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(58,60..61,68,70,116,124,126,130,132)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(128,130,132..134)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            130
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 madgldrlwt phrmtyisge drpeggyekp sgcpfclapg rsqeeslvva rgehvfvvln
       61 lypynpghll vcpyrhvady tdldgpetie lasftqtamr virkvsnahg fnlgmnqggv
      121 agagiaahlh qhvvprwggd anfmpvigrt kvlpqllgdt rdlllrawps
//
LOCUS       WP_357530877             247 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530877
VERSION     WP_357530877.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   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 247)
  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..247
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..247
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=25366
     Region          4..245
                     /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 miiesggrdg spmllllhgm gasgavwlps apllserwpg rwmapdlagh ggspplagys
       61 fagladqvaa dlhpgdrviv lghslggvvg lalaaasrav tveavvglgi kavwspaela
      121 raadlaarpv twfdsraeaa rrylrvagla dllspddpav aaglrqvddr wrlaldpaaf
      181 gvgepdlttl lagieapvll argehdpmvs etqlkqygvp vvtlpglghn ahvedpaavl
      241 alldavr
//
LOCUS       WP_357530921             239 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530921
VERSION     WP_357530921.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..239
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25616
     Region          78..236
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mkptragsgk trppirraag wlgpvvviai vavlaiiarp sdqpagpaaa geqeespfas
       61 larrtpgdpl algapdapvv vieyadfqcp fcgkharett prlirdyvdq glvriewrdl
      121 pylgeesraa ataaraaaaq grfwefhdal yasqrrvnsg alndaalrdi atrigldltr
      181 fdadrafpgi reaidrdqre atsmgltgtp afsigdtlii gaqpyeafkq aideqldtp
//
LOCUS       WP_357530952             672 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357530952
VERSION     WP_357530952.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..672
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..672
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=71573
     Region          <513..665
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpthpsladc psspvswgdl tldrerrgpv sgrgrplavr lgrvgdptwa lpvdaaapel
       61 awhphrplva glavagrrhy pwvadhasgi ithyrdisaa asltahggrq vvplawigrs
      121 glalltvpeq eeppsewppa ptileatgpg finftpsgda lhaavsvhls lldvdtrnlr
      181 pltpplvvgr lvaspsgrli lldhlggepp gcdshrlpwq vsivdptrps riaapagsrw
      241 aygdsdviaw rdrsagattv wfrevdggaa acvrqppeas gswlplwhrg gpallveevt
      301 gavrlampde nlvvtaaagp irigrnepag dpsrpgrvaf glatlnrvgl gvvdldrldf
      361 taawleasri vvgpprgmws vldgdtdqlv idrdgalvrc hrqggdlvvs etllptasss
      421 rvreqprldg plvriearag tgilripvav gerddapvfl wlraasgees apppsapatv
      481 igaghpvatl dlalewpeda tvaslhgqiv givrqalavl tadaqvpvvv gghsfgatlt
      541 lyalaeipel aaavvhsgcy nrtltwggfq herrsywqap diyrefsall fadrlrrpvl
      601 iahgtddanp atppeqavdl yrgivaaggt arlvllpkeg htfhyrenlv llteehrawl
      661 grhlptpqgs sr
//
LOCUS       WP_357530998             184 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530998
VERSION     WP_357530998.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18102377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..184
                     /product="GNAT family N-acetyltransferase"
                     /calculated_mol_wt=20923
     Region          3..157
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          <106..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 miivparpcd vdiimswrre rvawlaarge eqwsiplprs avastvsagq twmvwdgeep
       61 iatitltayv dvdglwkpdr dpealwhped dpadalyaak mmiplrhanq nlggemldwa
      121 ggrayeaglt wlrldawttn qrlhdyyrhq gfrhvrtves rvsgacfqrp sqpynghrlk
      181 nett
//
LOCUS       WP_357530972             196 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357530972
VERSION     WP_357530972.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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 196)
  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 196)
  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..196
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..196
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21175
     Region          10..178
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mmlplptgdf qaylfdcdgt ivdsmpqhyt awrqaldewg chfpeelfya wagrptadiv
       61 valneqqrln mpleaviarr ealyqqllpt aagipgvlhh iddahgripf avvsgstrea
      121 vtaslgalgi ldrfevlvca gdytrpkpdp epflraaell gvppqaclvf edadlgieaa
      181 taagmaavrv pqprqg
//
LOCUS       WP_357531033             297 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531033
VERSION     WP_357531033.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=32980
     Region          13..273
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          189..270
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvpsdhlspa pfdptgeiet itlgslapdp rwrrpvlldr elivlttsgh gytevdfrpl
       61 pcrpgtllrv rpgqvlrcal peldatvvrw hpealrglev aldegpawfq lagededavi
      121 nevtqltvds rrhrdtpagr sllrhqltvl llrltmlpsd grrpesrpee vtfrrfcrev
      181 elgfqhsrrv edyadrlgcs vrtltracla vtgrsakqvv dervalqasr llaatdepia
      241 qigrqlgfse atnfgrfftr evgvspgsfr aardrpgpgp virprspvdt qtdihqg
//
LOCUS       WP_357531001            1057 aa            linear   BCT 28-DEC-2024
DEFINITION  type I restriction endonuclease subunit R [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531001
VERSION     WP_357531001.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1057)
  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 1057)
  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 1057)
  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 1057)
  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 1057)
  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 1057)
  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 1057)
  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..1057
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..1057
                     /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=116952
     Region          1..881
                     /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 madhnevvfe aeicaylesh gwlysandtg ydreralfpe dlfawleetq kpaytkalka
       61 agsqakfldv lttaldkple hgggtlnilr ngvlyigggr lkmaqfrpdt slnattneqy
      121 aamrvrvmrq vhfstadrrs idlvffvngl pvatvelktd ftqsldeain qyrknrhplt
      181 ngrpepllsf ghralvhfav sndlaamttk legekthflp fdmghdsgag nppaeggrsa
      241 taylwervwe kdawltiigr lmivetkeew dvatgtsvrr tsmlfprfhq weavtkivaa
      301 vreegvghry liehsagsgk tntiawtahr larlhvndek vfdsvivvvd rnvldgqlqd
      361 airqidgsgk ivatisredv rkagaksksg llatalknge liiavtvqtf phalheiqad
      421 tslkgrrfav iadeahssqs gkvssklrav ltaeeikeie eggevdveai lasemterae
      481 senisyfaft atpknktlel fgrkgpdgkp vefhlysmrq aieegyildv lrgyqsydta
      541 lkiagraesa dgelveeata rkglmrwvkl hptnisqkvq iivehfhinv ahllegkaka
      601 mvvtdsrkaa vkykkaiday iakraaedas ynyrtlvafs nsvkmdedee wtsdwgprps
      661 kdeefteakl npgagadlaa afkgttykvm lvankfqtgf dqpllsamyv dkklsgvtav
      721 qtlsrlnrth rtaggeqkqk tfvidfvnkp edirtafepy ftnatletet dpyvvvhlsn
      781 klaqagiytp eqvrevaelw vtrkgnnals aaispakndf arryaaaiea ddkvtlntld
      841 lfrkdvstyv rlydfmsqiv dygdpyleml siflrllekv itdsswsaev dlsdvvlvgv
      901 khtkatavdi sltgdgqlkg igaagtgtrk epkyvalqvv idkmndlfga esfsasqvre
      961 fvqglvqrll aypdlvnqak vnskkqfmes qdfqaavida vvdnqeahnt madyffsdgp
     1021 ginavivala dafheaaidq rtdvwqpgpe mgsraap
//
LOCUS       WP_357531123             309 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531123
VERSION     WP_357531123.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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..309
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..309
                     /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=30614
     Region          16..308
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mpsdparpdp agqggrilvv gdvitdvvam lagplasgsd taaeirftgg gqaantaawl
       61 aaqgvpvtlv aavgddaagr drvaeliaag vdcavariag cptgtvivla agdertmite
      121 rganlrltpe hveqalagap eathlhlsgy vlldpgsrpa glhalalarq qglttsvdaa
      181 saaplraara aaflswvrgv dvllvntdea avlaggldpv aqgralaasa rrvvvkqgaa
      241 gatwvdrqpt ivaiparrva vtdvtgagda faaglltawl agapphaale ratrlgaaav
      301 sqvgarpsd
//
LOCUS       WP_357531134             740 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531134
VERSION     WP_357531134.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=81225
     Region          1..740
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mlyqrlddlr eqasqrltee lrvtggtlqa rsqrdsavrm yadqveqfsa venglcfgrl
       61 dtdegerhyi grigifdteg dydpllmdwr apaarafyla taanpqgirr rrhlrtrqrk
      121 viglndevld lntasptahe eltgeaslla alnagrtgrm rdivetiqae qdriiradlp
      181 gvmvvqggpg tgktavalhr aayllythrr elstrgvllv gpnltflryi sqvlpalaet
      241 gvllrtqadl fpgvyarrve ppttaavkgr pvmvevltna vrdrqrvpee pleielpqre
      301 ilvldpatvr eardrarrsg rphnlaravf dieiihalad qvaerigadp lggenlleea
      361 dlaelrrelr eepevratld elwpvltpqr lladlyadpd riataapmlt aderaalhre
      421 pggwtpadvp lldeaaellg eddraagarr erlralqrey aegvleiarg srsidvedea
      481 eggeilgvtd lldadqller qeeadrltta qraaadrswa fghvivdeaq elspmawrll
      541 mrrcpsrsmt ivgdvaqtga lagtpswaqa lepyvadrwr lteltvsyrt paeimavaan
      601 vlaqidpalr ppravrssgr tpvsrrtpad rlaaelvevv taeaaaltdg rlgvivpatr
      661 veelgtvvta alpeaaigeq pdlesrvvil tvaeakglef dsvivvdpdq ivaesprgps
      721 dlyvaltrat qhlttltptp
//
LOCUS       WP_357531173             703 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531173
VERSION     WP_357531173.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 703)
  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 703)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 703)
  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..703
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..703
                     /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=74882
     Region          93..314
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
     Region          459..699
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 malvfqiahs tlepltwsvr trvltlvaqa avtllpflwv gplagalagf lagslllavs
       61 ggwrwwlfga vvlavllgqw veglsaidig ygvyftaltg lmiyavsslv vlvglvhati
      121 gqmvamvvar erlrvardlh dllgfnvsam mlkselayrl lpmtlerarq elgevlqiad
      181 ralsdirvva ggdqrmsmai eaeaartalt cagmrvtvep glsvlpepve svlgvvlrea
      241 atnvlrhska eecvievsvr dhearlsvrn dgveadsrsd ggfgldnlid rlavvggrlv
      301 astdegwfrl eatiplpvgp lppgassadr slgepaavpw hrrvaraftv lvlagygllm
      361 vinvlpgdpn vlhllglglc laavvglqvl qalrypyrwp rwsqaavlva qavlsalpll
      421 wiempwgsmg gflagslllv fggvwrwvsy glvgvavllt svaygatveq vayltistll
      481 tglvvygvss lsglvqqidq arvklageav tqerlevaeq lrtrlgelfs ailfrgrtai
      541 rllpdapeqa raevaemlgi ariaasnirt vatgyrhmsl raelesaatv lntagvevei
      601 diaegelare idallavvlr eavtnivrhs eahtclisvr seggrlrllv tndgasprak
      661 tgtslenlte rlraaggdlt aaatgdtfrl vaelpifpaa srg
//
LOCUS       WP_357531235             330 aa            linear   BCT 28-DEC-2024
DEFINITION  hemolysin family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531235
VERSION     WP_357531235.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..330
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35475
     Region          <41..307
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mraarrrgsr rwrptqprre pgrlargvar vvvravdggl rlvtallgtg ptagrerise
       61 aelrdlvaan tvldpvgrri idevlvagas lvrevmmprt evvflsaalt laeaeplvra
      121 gthtrypvvd gthddvvgfv hlrdvlwhpd rvpstkvgel vrevkrlpas krvlaaltem
      181 rreghhlavv ideyggtagi vtcedlieel vgeihdesae lpeptlaglp avvegrlnla
      241 dfaertsvvl pvgpyetvgg fvmaalgrlp rpgdevpvpd pagagggwll rvlslegrrv
      301 arlavtvgrl peqrrsvdrp adrtgpasps
//
LOCUS       WP_357531280             406 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531280
VERSION     WP_357531280.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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..406
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..406
                     /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=46346
     Region          76..387
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpvddlwyln krgpdgkrlp srrhgqgkrw rvrfadatgd prtrfferka daeafdarar
       61 agvaeetkvq qserlltlrd ygdrwrlsre vgwaletrkr vesnlrchly pafgdrplra
      121 inltsvlewl trrlaegtps tslklyfell dtvlnaavtd kiipdnpcdg vklsqvlrgy
      181 srapkwvpte revlalldvv paryraaiwl gagqgyrlge algvedgprc idqehselhv
      241 vqqlryaprq hdgfylsepk agssgtldld pvvgqvlaeh vrefppvpve lvdltpgnpv
      301 rrsvpllftt trgnpftdrt wsrewadwra aagwpkehgt fhalrhffat tlitnhaepq
      361 evqrmlrhkt lritletyvh wwpkrdrsrg ivgsvlrsal anqdhn
//
LOCUS       WP_357531393             329 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531393
VERSION     WP_357531393.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 329)
  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 329)
  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..329
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..329
                     /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=33429
     Region          3..301
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mydllvlggl gvdirvrvpa lplpvvdslt vepidlrign tgagvalaah alglrvavid
       61 tlgadpagev vraalsrtev qtvlaeapgg trrsvnlvdp vgrrmslydp rpseetapfa
      121 maqvaelirq srhvhlsimn wvrdllpdlg illgeggrss tdlhdwdghn pyhrpfaeva
      181 elvlvsgval gdrttalpaa lspsapavpv paggpartqp vtaggpavav pgragdsata
      241 vagrpvlvtw gadgadlhld gditripaat ppgpvvdtng agdafaagvi aarlrgatwa
      301 eaagyaarva aaacthdgme yppgllppp
//
LOCUS       WP_357531482             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531482
VERSION     WP_357531482.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=20150
     Region          1..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 marlgltpqr laaegaelad evgfdrvtas alaqrfgvkv aslyshirst qdlkvrialf
       61 aldeladraa eavagragkd alvalgdvyr dyarehpgry aasrlrldpq taaasagprh
      121 aqlaravlrc yelgepeqth avrllgsvfh gfaslelaga fshslpdseq swawaldsld
      181 allsarstgg
//
LOCUS       WP_357531512             579 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC047134].
ACCESSION   WP_357531512
VERSION     WP_357531512.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 579)
  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 579)
  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 579)
  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..579
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..579
                     /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=61136
     Region          135..550
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtgadvrdid pgdgrftpna pqepawrtdl saaalpaidp slsaadwpvv vehlreglvl
       61 cgpdgmvwqv spvaarllpe ivvggscaef ealpgpvaei trhgrrlrvr rvslsagrsc
      121 wyvedlseht gpvdalaaer arsaflamvg eklgnplhpd raaaavvrla vptlaetavl
      181 ilaprsgrar wwrasqaddg qsildrgalh tgempaavae slhgvqphtv dwlaeqavga
      241 gwlpghnaae vcarlvslpg rdapagvllv arpaprwyte ddldllrafa dragaaltta
      301 llyrnqaeva dtlqasllpv epaqapgvqw gtayrpaqag lriggdfyga hrlpdggsvf
      361 flgdvsgkgv eaavftgqlr qclhalhrie sqparllrll ndallettla hgqgrfatmv
      421 lgvvrphrdg glsltlaggg hlpplvvras geveqlplsg mligvvadpr vdqvstrlap
      481 getcllysdg vtearggrrg veqlgtdrlm qaltgcqrmp apalaerieq vtcdwlaqrd
      541 hddiavlalr aagvggrphr hlhavptptg varegattp
//
LOCUS       WP_357531530             485 aa            linear   BCT 28-DEC-2024
DEFINITION  LVIVD repeat-containing protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531530
VERSION     WP_357531530.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..485
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=52553
     Region          58..460
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          85..119
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          126..181
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 mdvstpprgr wlrltsavat glllaslata tpgsaqpvtq vatdstsave aplgvdeiss
       61 spnlrlianl pkqspfnttn algtdiafqg kyafvgnydg fviydvsrps qpkivsqvlc
      121 pgaqndisiy gdllflstda srsddscgsv sqpasikesw egikifdvrd kkqprylksv
      181 etacgshtht lvpaknnkav ylyvssyspq dafpdckpph dsisivkvpl kkptdaavva
      241 tpnlfpdggy egrtgasatt gchditayps kdlaagacmg dgvlldiskr eaprvlhrvr
      301 dttnfafwhs atfnnrgtkv vftdelgggg gatcnetvgp erganaiydl tgrgdkrkle
      361 frsyykiprt ngdtencvah ngslipvlgk dimvqawyqg gisvwdftds rrpteigfwe
      421 rgplsdtqmi vggswsayyy nghiyssdiq kgldvlaled wrtwtaklvh frelnvqtqp
      481 sylsw
//
LOCUS       WP_357531562             562 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531562
VERSION     WP_357531562.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..562
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61229
     Region          16..550
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mgyvdvaavg hhlpdgrelf advsfrvgeg akvalvgpng agkttllrmv agdlpvrtgt
       61 iaragglgvm rqfigmigde stladlalsl appplreagr rlaeteaamr aaelrgkyss
      121 aagkaqlaya ealaawgeig gydaevlfdt vativldlpw etarqrpvrt lsggqqkrfa
      181 lelllrgpde vllldepdnf ldvpgkrwle arlresgksv lyvshdrell ahtadrvvav
      241 eggsawvhpg gfaswhtarv arhdrldelr krwdeehekl relmlmykqk aaynsgmasr
      301 yqsaqtrlrk feeagpppvp pkdqdirmrl tggrtgkral iceqleldgl typfdlevwy
      361 gdrvavlgan gtgkshflrl larggtdpdp anppvdgaaa lapvahggla rlgarvrpgh
      421 fsqthdrpel maktlveilw rgdehrdgmd rhaamaalsr yelagqgdqr fgilsggqqa
      481 rflvlllels gatlllldep tdnldlasae aleaglaafs gtvlavthdr wftrtfdrfl
      541 lfqgdgevve tdepvwevss rr
//
LOCUS       WP_357531593             201 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531593
VERSION     WP_357531593.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=21523
     Region          10..201
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mtgdhyftta psasakprev qfavagrdft lasaagvfsa nrldpgtavl lrkadlppas
       61 tegalldlgc gfgpiscvla tvaptakvwa vdvnerarel taanadglgl adrvrvaape
      121 evpadltfaq iwsnppirpg kdelhdlllh wlprltpegv awlvvgrhlg gdslhrwlve
      181 qgwqverhas qkgfrvlrvt r
//
LOCUS       WP_357531621             325 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: phosphotransferase family protein [unclassified
            Micromonospora].
ACCESSION   WP_357531621
VERSION     WP_357531621.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 325)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..325
                     /product="phosphotransferase 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=34152
     Region          <80..249
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msnppvpyha taqrpgwaal paavraavsa rlgapvvear vatagftrgf aavlrtaegd
       61 safvkaaara eqphlvdwya reaailarlp aglpvpglrw tlweagwyal cldpveghtp
      121 rlpwdpaeld atltgyvdia aaladpptel aglglphlad laredilwwg evaagreptp
      181 plpasavgrl telvaleskl pgyaaeatgl thgdlrvdnv ligadrtawf cdwtwlchgp
      241 awfdlvglli tgyasglevd arfathpaaa dapadaldvt laalagyhlt aaaaapptas
      301 aqlpahqrwt geqalawlar rqgws
//
LOCUS       WP_357531712             219 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531712
VERSION     WP_357531712.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 219)
  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..219
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..219
                     /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=23514
     Region          13..190
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msvdgggavv tgrstsdlva aaangdesgw velvrrytpl vysvirvhdl taadaadvnq
       61 tvwlrlverl dqvrepeala swlavttrre cyrisrlgrr tqpfdpsdga fqgchrsgae
      121 aatpdedllr aerhqalreg faelpprcqv llslltadpp lsyrqiaerl gtpvgsigpt
      181 qarclrrlre sgalaayleg hrsaastgge rdgavaagr
//
LOCUS       WP_357531713             435 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531713
VERSION     WP_357531713.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 435)
  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 435)
  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..435
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..435
                     /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=45228
     Region          84..>408
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mhsdhprpgg wlprrrllva svlaaaatpl gagwrpgpal adqdaddaay qlafdrlvna
       61 drnvrrhtva greilyrprq lltaaedtgr vaawlrksgh qvligdafag vtrllfsaea
      121 dipaivtllr dprqwpgqri plvqphhvll glgnimgnpg gppraiaala ppdparaaeg
      181 agvtvgicdt giwryaggqh pdwlggaylp epddedplyl htdvlapqgg hgtfvagvvr
      241 qaapgvrvdp etalestgig destvvaals rlasqvsvvn lslggftldd qpslplanav
      301 aalppttavv aaagnagtnr plwpaaldrv vavaavrmgs aglvpadysg fgpwvdacal
      361 gqhdstfvpg ilplpgrptl vfhryarwsg tsfataqvsg rlaammsagg lsadaarlal
      421 lamprwhpdy gvlvg
//
LOCUS       WP_357531718             445 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531718
VERSION     WP_357531718.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=47912
     Region          31..356
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mhpathptsa pdgrtyrtpl lrrrllrgll aavvalplvg aaaacggdda adgktkisif
       61 wwggdarnal tvqaldlytk knpdvvfett wqanqgyfdk latltaggnp pdifqiddny
      121 lteyaarnat ldlkkyqdag dldttkfpps llqygvvdgk laglaagent qglvynktll
      181 tknglpeptt gmsweehiaw aeqvskktgv pgtqdpsady kafwvwlrqq gkdlysgsdl
      241 gftaedvtkw felwkgards gatptpdvih egnatditkq lvvtgksats wvwvnqmpel
      301 kkntadelgv iaypgdpsaq warasmywsv frgsknadia vdvinflvnd peavkllgtd
      361 rglpsnldlr rvvsddttdp amkqsievet klaetfgaap qvpikghskv raeltkaaen
      421 aqygratpae aaaqfvaagk aaias
//
LOCUS       WP_357531755             127 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531755
VERSION     WP_357531755.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   4  (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   5  (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 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..127
                     /product="PadR 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=13891
     Region          14..102
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrstsrpalr epsyfvlaal lggplhgyav ikrvtelsde rvtlaagsly svidrllgeg
       61 litadgeeiv ngrarryyrl tdegyrvlae eadrlaraar vvmdrlphrg fplgsadqps
      121 ivrtrpa
//
LOCUS       WP_357531766             331 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Micromonospora
            sp. NPDC047134].
ACCESSION   WP_357531766
VERSION     WP_357531766.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=35474
     Region          3..327
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mdvfltggsg saggvlirrl vadghtvhal arsataekav aaagarpvrg dltgalrsha
       61 gapawldtlh gvdavvhaaa fmefwgpdel fvernllptr alyqaavaag vkrfvllsaa
      121 svstgtrhln ivnetsdtgr aniaysrvkl rteqellalp haettlvilr ppflwghgta
      181 gnlqgfvdsv eagrfawidg gqhtvdfchf dnlahavala mtrgnhglvc yvtdgnprpa
      241 rtfftpllat qghdvsssrs ypraiasaia timetvakar rsttpppltq wivtfmgrdr
      301 vyditrarth leyqptisvd eglrrmatlg r
//
LOCUS       WP_357531805             249 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531805
VERSION     WP_357531805.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 249)
  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 249)
  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..249
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..249
                     /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=25190
     Region          18..248
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mttsqaviit gggtgigrat arrfaasgag vlivgrsadt laeaasghhn irtltadvta
       61 pdapriivdr allefgavdv lvnnaavgaf aaladldads vtaqldtnll apilltqcal
      121 qalgesggtv vnvgtaaalg lrsflqnsvy gatkaaldfl trswavelap qgirvvgvap
      181 gviatgvgvr agmpqeaydg flehmstrip agrvgtpddi awwihrltqp eaayvngtvl
      241 avdgalsit
//
LOCUS       WP_357531807             306 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Micromonospora
            sp. NPDC047134].
ACCESSION   WP_357531807
VERSION     WP_357531807.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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 306)
  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 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
REFERENCE   5  (residues 1 to 306)
  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..306
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..306
                     /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=32737
     Region          6..302
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 magvnrvavm gasgsvgrqv caafsrsgqs vlavarrpad hlsayrfrsv dlgaetpehi
       61 aeilvaesad vvvnatggwg tteqemeyah vvltgrlvea valvprrprl vhvgtiheyg
      121 pvpegtlide kiepapqtpy artklagsea vlhaardgri dgvvlravnl cgphpappsf
      181 lgylhrrlre atdgatlels iadarrdyld vrdaaeavvl aatapvtgqv inigrneavd
      241 lrelvalfia aagfpqdrlr vldrqvlskg gdwtradirl aqqvlgwrpr islaesmgam
      301 wesest
//
LOCUS       WP_357531817             362 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531817
VERSION     WP_357531817.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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 362)
  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 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..362
                     /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=41113
     Region          280..362
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtrathrfer vtsrrtlref laltdrlyag epryvptprq qirrwwregv slyvlrdatg
       61 tvvgrttlht daafdtklgr rcqlfgltef tepaarplfd aitahaepdr dllfgpvall
      121 pnqaggvits gyaergfvds awnpphyvta yeaygfhrrf eadtwicpvt apgqpkpsay
      181 iksdgvglev hrgdlrrldd qlellremln asfaqlgyyt piserqlrrq tdglgyllde
      241 slllyltrdg vpvafvlcvp diseflvavr gnlhvvnqlr lvtsarryrr eavliikgvl
      301 pqyqgrgyqr llsahlhhnl hiagyttlrs tyverdnpas aaqyrrlggr plhgytfyak
      361 er
//
LOCUS       WP_357531823             652 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531823
VERSION     WP_357531823.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 652)
  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 652)
  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 652)
  AUTHORS   ter Beek,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 652)
  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 652)
  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..652
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..652
                     /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=70353
     Region          <217..634
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 msitedgarr sesprqdsvl pelrelwwet gvraraqasl favfselprl vwaaivvswr
       61 adrlrtsiva vttvgagvms afgllaaqrv lvelfaggpt pdkviaalpa lialaavivl
      121 rasmatamgy aqngltpkvd reverglfem ttavrleafd adafaddmer atrgsasttd
      181 lvqasmnlla glagviavai avvvihplll pallmatvps gwaslraghl ryrtyaagsv
      241 rrrrmwllhr lmaerdsape lrsyglrgfl ldqydrvmgv etdiqlalar rvtttttiga
      301 miggiatavv yvllglllid gqiplaaaat cviaiqsaqr slsvvtfqtd rvytegqhfr
      361 dytgfmtraa dylpppaapg aeapdrlrei vveavslryp dretaavdrv slrirdgqtv
      421 afvgengsgk stlatmiall rtptggtirf ngrpaadwdt dalrariavv tqeyhkwpft
      481 aatniaigdi ttvpeqarie taaaravahd mitdlpygye tlldrtfagg qdlsggqwqr
      541 itaargflrd adllimdeps saldpraeda lfqairdrqg qgitilithr lanvrhadci
      601 yvlhhgrlve tgthdqlmaa ggryaelftl qsagyrataa tsslprqpta sa
//
LOCUS       WP_357531826             942 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357531826
VERSION     WP_357531826.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 942)
  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 942)
  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 942)
  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 942)
  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..942
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..942
                     /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=102413
     Region          2..249
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          124..939
                     /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..816,843,848..849,852..853,856)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          803..837
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          842..872
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mplrfdllgp lsvvhhgrtl dlgsvkqrlv lacllfrpce avaaerlvaa lwgdqppvsa
       61 nanirtyirg lrralqdgvd dkprivtthg gyllrvepde rdldrfdaat argrealtng
      121 dparaeaela galalwrgqa laelplapql srwveqlaer rllaeedhae aklalgahae
      181 aiprlralld ryplrqrawt hlmsalyasg dvagalaafr qvrralaeet gmdpgpelir
      241 lhddilhhrr hrngssatgg rgvtamarvr paqlpfvppg fvgrelqltr ldaaiddrvd
      301 gpttvvisai cgmagigksa lalhwahrva drfpdgqlhv nlrgyddgev vapadallgf
      361 lealgvplar ipssldarig lyrsllasrq mlivldnard aeqvrpllpg tgrsvvvvts
      421 reqlhslvaa egarllaldv ltatesthll rsriggdrld vepdavadmi eaagrlplal
      481 sivaarvatr ptftleaiaa elrppearle vladgdvrrv fswsyralsp vaarlfrlig
      541 lhpgpeltsa aaaallgcpt pavgpvlkel trlhlltehl tdryachdll rsyaaeltrg
      601 adrsaerhea rhrlydhylh saypaarlvq pqwtpitpvp alpdvihlpm adqdaaldwf
      661 sterrvllrv irqaattgfe ayawqlawal ttflaprglw hdqlaaqqta laaaeclgdl
      721 naqatasrll graaarlgqq dtagdhlqra iklyeqldde dglaqtlhny tehcfvlgrv
      781 dealthghea lrlyrrtgnr agqgralnav gyihavrgdh lqaivdctaa ltqqrliddr
      841 ngqaatldsl gfayqglgdh aravscyeqs velfhasadr yhqaetlvrl geaqaamgka
      901 eaaaeawrla aaiyddlgdp tvdearrrla elgqaaagrk st
//
LOCUS       WP_357531835             291 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Micromonospora].
ACCESSION   WP_357531835
VERSION     WP_357531835.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..291
                     /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=31912
     Region          3..288
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtrprrpltg waflapyaia vallvavpal lnvgyaftdh tgltrdpqfi gldnirrmfg
       61 drflldslea slfhvalavp vrfiaavglg lllaaprpgg rwfrtavylp tvipdvalav
      121 lflwvlnply gplnqllglf ghegynwlad pttarigvvl mlafpigegf vvvlaarrll
      181 dgrlyeaatl egcgpfgqlr rltlpllapv lvllavrdii ltlqvnfvpa yvltdgrpan
      241 atlylpvyif dqvfefsgfa ygslvtillm litaviiivl llvvrrwrvl r
//
LOCUS       WP_357531937             301 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531937
VERSION     WP_357531937.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  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 301)
  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 301)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..301
                     /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=31943
     Region          1..135
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
     Region          158..298
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 meqmrrvgay gvlrdpegrv llvrgserad fpgvwslpgg glehaehpaq avlrevaeet
       61 glavevaglr avvadvvpyp dlgvalhtdr vlfeltavgg tlraerdgtt dlarwltpqe
      121 aaglpllpft aealalpvvp lpsgalrrre pfaapqaarr qrfgayglvt dpagrvllal
      181 iaegypgagq whlpgggtdh geqpvsallr elveesgqlg rvseligvdn lhnpaalgpe
      241 gypidwhgir vvyrvqvdrp tepavtelag gstaraawft psqlrelplt eiaaealraa
      301 r
//
LOCUS       WP_357531979             271 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357531979
VERSION     WP_357531979.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..271
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28965
     Region          32..264
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 msrqprmvrg wewarpvrpv rrevlsvvpe leqghppllf vpgfghgawa yaehwlghta
       61 argfpayavs lrghggsgpa pdadlrayah dvvqaaaglp rqavlvghga galvvahala
      121 ryparaavlv apvlggwasl gaalrhnpvg tlpavfgagl rlsrsqlfsr elpeaearrh
      181 tarlgraarr aqwqlltggd pepavgrppv lvlgspddrv vpaaaltraa rrygsapllf
      241 pgmghdlmld arwrepidai ldwllkqpnr p
//
LOCUS       WP_357532019              88 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357532019
VERSION     WP_357532019.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 88)
  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..88
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9142
     Region          <29..>74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvrqpltaeq iaagqrlgra lraaragrsl vevalaagis petlrkieag rlpapafgtv
       61 vclsqaldvp lddladvwla dmpirqas
//
LOCUS       WP_357532011             138 aa            linear   BCT 28-DEC-2024
DEFINITION  cold-shock protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532011
VERSION     WP_357532011.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 138)
  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 138)
  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..138
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..138
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15004
     Region          5..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 masvgkiirf devrgygfia psaggedvfv handfgehrh qvrvgmpvef eavdsdrglk
       61 aasvrliepe spavtgerrl rpriegdeel cdvlspaeft gavtelllrc spsltgaqii
      121 avrerfiefs rahgwvdg
//
LOCUS       WP_357532078             471 aa            linear   BCT 28-DEC-2024
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532078
VERSION     WP_357532078.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 471)
  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 471)
  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..471
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..471
                     /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=50042
     Region          16..470
                     /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 mrdaaprret drrgpraprp amdrpryaay qavaavnrdd ayanlvlpai lrdeglygrd
       61 aafateltyg tlrhsgtlda iltaaagrdv eridppvrda lrigayqllh trvpphaavs
      121 stvdlvrmvg qgatgfanav lrevsasdid kwvarlapsm etdpighlal ahshpqwivr
      181 sfaealggdl gettrllien nerppvhlca rpgladpvel adasggapga fspyavylag
      241 gapgdlaavv dgrahvqdeg sqlvaaalvq apvegpdgrw ldlcagpggk sgllgalaaq
      301 rearltavev aehrarlven atrglpvtvl htdgrlvgae pklpeghfdr vlvdapctgl
      361 gslrrrpesr wrrqpsdlpa ltrlqrellt agiravrpgg vvayvtcsph tvethvtvte
      421 aarrsgtpvd fidarpllpa gmpglgdgpt vqlwphrhgt damflamlrr s
//
LOCUS       WP_357532049            1090 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532049
VERSION     WP_357532049.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1090)
  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 1090)
  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 1090)
  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 1090)
  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..1090
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..1090
                     /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=120531
     Region          8..1086
                     /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 mverdniesi aglaamqkgm lfshavdtgs dayveqfdfv itgevdvehm raalagvsrt
       61 ysvlrtifsy rntdqpyqiv lkewapqldv rdyrdrpdrd rdveefkvad rvkgfdlsad
      121 vllratlirl adrrwrlvft fhhiildgws lgplfgtlmg yyeeltrsgs fqsrpealpy
      181 rdyvtwyerq hdedarrywa ealegyetea vlpasprpgg yrgathrfal paelydglkg
      241 faqkagvtqs avfqaawgvv lqkftyaddv vfgsvvsgrg temagigeav glfcntqpvr
      301 vtttqdqhft glcrevqqsy lrasafehya lheiqgltpl rnkllnhvva fenyplseql
      361 rdfagdtgdg lafdgvevfe rtsydlhivv npgrdfaitf aynenhyapg liqalehslr
      421 nvltaavrnp rvrvadialw dsraadvavp qpahsamlds svvdvfadva athaektalv
      481 wrgrefsyae vdrwsdavaw elksrgvipg vavgvladrr pelivailgl lkngnfyvpi
      541 dtkdakprve yvvadagvrd lctvaefadr apaatrvllv dppigdvppf prqrnlngat
      601 aylmytsgst gnpkgckith rnilrlvadq effdfddrqv lmftgspafd astfeiwgtm
      661 lfgatlvlad eldvldgdlm reaikrnevt gmwltaplfn qlcdhdpaif drlghlivgg
      721 salsvqhltk vrsacpslri tngygptent tfsttyqird edllreripi ghplahssah
      781 vldrglnllp pgavgelcvg gdgvstgyhn rpdldlaafv tvpalssrrl yrtgdlvrel
      841 pdgsldylgr addqvkisgf rvelgevesv lrsvehveda avicvevdge kslrgyyvag
      901 kriapevvrq gmaqqaapym ipaglvqldr iplnksgkvd rtrlaeirpe pearpeaphl
      961 gpvsdmtril fdiiadlvpa etidvdrnff dlginslnll tinnrlrkvl drnvplvqlf
     1021 qhtsiaslaa flavadsgdd ptadpddaea daedafaeqe eehtfsatal lreiadeiae
     1081 elaadlekel
//
LOCUS       WP_357532143             307 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357532143
VERSION     WP_357532143.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..307
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33394
     Region          7..293
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 melivdagdv slpatldvps dgpthgavvv lhgsgepqrs yflyehlara fpaagvavlr
       61 fdrrprergd vpytvqadda laavaevrrr igevpvglwa wsqgawpasa vaarrpelis
      121 flvlvagsgv spaaqmrygt aqqlllhgyg raeladlarl realekvvrg hidrrtaqtv
      181 idryadrpwf placvprdld dhpgtwedmd ydpepviarv rcptllfyge adewtpadds
      241 iavwrraaat sdltihrlad cthlptiggt etlesissdy rsamlawvqe rvgrgesrip
      301 aggsdag
//
LOCUS       WP_357532171             236 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532171
VERSION     WP_357532171.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..236
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=25272
     Region          1..229
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mriyclghag gsagsfasvv drhaegltmv pverpgrgnr wreppcrgwp dlladlsdri
       61 lgeldgtpyg lfghslgalv gyelahalrd aghpadllvl sgrnppwmap gsalwhavdl
      121 pdeelfarlv alggadaraa gpltyrtflp mlradlrlaq ayrpgprrpr latpvvvlhg
      181 iadpltspaa ltrwadittg dfllravpgg hffpmrepae varvlgqavp dpvrsr
//
LOCUS       WP_357532189             686 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532189
VERSION     WP_357532189.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10196129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..686
                     /product="serine/threonine-protein kinase"
                     /calculated_mol_wt=72065
     Region          29..289
                     /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..54,87,92,97..100,112)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(36..37,39..42,44,57,59,95,111..114,118,120,157,159,
                     161..162,164,174..175,178,195..198)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(36..37,39..42,44,57,59,95,111..114,118,159,161..162,
                     164,174..175)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(40,118,120,157,159,161,178,195..198)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(174..182,191..198)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <337..>495
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          <568..680
                     /region_name="PsbP"
                     /note="cl03356"
                     /db_xref="CDD:446075"
ORIGIN      
        1 mtqiptwsgg pvstptngra tpgtligdry slrsavgngg mgtvwratdt llrrdvavke
       61 vvlppglaps drdamyertl rearaaaaia hpavvqvydv vteagrpwiv melldarsla
      121 dmviedgpia qrvvakigia llgalevaha igvlhrdvkp anvlicsdgr cvltdfgvar
      181 mptdvqlttp gmvlgsphfi speramgqef gppsdlfslg vtlytavegr ppfdrgdpie
      241 tmhavvedpp appqrsgplt rvlmgllekd parrldvhta ramlrellag plssnaaavn
      301 smtdpysvmq mpqpaaisap ptpakdkpsg qiggsamlap gesltdrlaa lrrgerpgqv
      361 tpisatasea tsadalarpa phglmspppv grtyggadat qhfgaaeatq rfggadatqr
      421 igadatqqvg pmafgyggga peatqrvggd yggqwpaaps qpygarptpa ggspmdkaka
      481 agtqlvgtvk gwprkmqlaa agglalilli givalsgged sspttpvadp spsvdagpgi
      541 emqehsgrgv qvlvpkgwkk atgglyvdyt dpedsgrrvr ilneewrgds trwaevaeng
      601 lktrstscak pynqismeqk elagkpsaef eytcgkgdsm rhgiwqgvah egrmysfylt
      661 atdsrfeesk piyeemvksf qltnag
//
LOCUS       WP_357532211             718 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532211
VERSION     WP_357532211.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 718)
  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..718
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..718
                     /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=75440
     Region          13..269
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,37..38,71,76,81..84,96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,79,95..98,102,104,141,143,
                     145..146,148,158..159,162,179..182)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,79,95..98,102,143,145..146,
                     148,158..159)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,102,104,141,143,145,162,179..182)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(158..166,175..182)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <188..586
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 msdasasqlv adryrlispl gqggmgrvwk ardevlhrdv aikelvpppg ltnderremr
       61 erslrearai arlnnvnvvr ifdvlrtdgd pwivmeyvas rslqdtlaed gpvspaqaae
      121 iglgvlnalk aahragimhr dvkpgnvllg tdgrvvltdf glatipgdpn vtrtgmvlgs
      181 payiaperar dgtagpeadl wslgatlyaa vegkspfarp saiatlaala tepmphprna
      241 gplksvlngl lrkdpqerit adsaermlrk asgrrvrtis lldgvrrpgp ngpreprppl
      301 vpaprpsgeq psapvsppap rtplaagstg vdaaatarmd agdtgsdrge stssdaapta
      361 liasgpgssa qvegrdsaag eeaveptgsq ategsgsege tsveagptdr vgagratatp
      421 dptpsnddsa aaadaeptrr vtsgstgdpt rvvpqgtvqv psapadsepa rgavftsgfl
      481 rsernrrgll vgalvallvv glvvavpllt gddgkdggtp qgstgsptas apassepaap
      541 pptsdappts aappspsvsp staeptsggl pagwtmrndp vgfkvpvpeg wrrssgstwv
      601 kyrdpngvse ltidrtdrpg rdaaatwrel epgrrnvrgv qnyrlidiws fdckwrtcgd
      661 wdwyqtrngv elrvrnrgfv tasnrgfalr wevpnsewea qlpnfetafr efvpdrqd
//
LOCUS       WP_357532248             349 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357532248
VERSION     WP_357532248.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 349)
  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 349)
  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 349)
  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 349)
  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 349)
  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..349
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..349
                     /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=36163
     Region          11..325
                     /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 meahpadeqs mrallltgdr qsvvrqvprp vpaddevlvr vtvsavcgsd lphyrksaqd
       61 lghrlhtvpg heavgviara aasgdgpaeg arvivyqhsg cgdctfcrsg epmfcadrrt
      121 lgnhrsgada eyltapatgv lpvpedvsda maaliacnfg taysafrksg vavgdrvavf
      181 glgpvgccvv alaaaagaev favdpiegrr dlaktlgaat lidpigqdpv aavaavtegr
      241 gpevafecsa npaaqtqvmk larphgtvvl lgannsmeid pgvdvirkel rvigswvftq
      301 pefpavlraa rslpalqhli tdpfpaqrap ealaaadagh igkvlidws
//
LOCUS       WP_357532388             215 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532388
VERSION     WP_357532388.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22374
     Region          2..166
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlfdmdgtlv dserlwdval aelaetyggs lsaearraiv gtgmadsmri lhedlgqphr
       61 dpaasaawid rrilelfrag lqwrpgalal leavraaqvp talvtssgra lveialdtlg
      121 rssfdvvvcg deveatkphp epyltaarll gvpidrcvai edsvtgvasa vaagaavlav
      181 paevplaprd gvhqveslla adlellaall arsaa
//
LOCUS       WP_357532394             320 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357532394
VERSION     WP_357532394.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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 320)
  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 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   5  (residues 1 to 320)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..320
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..320
                     /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=35034
     Region          237..>304
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msiwrvpvdl larsrfivsp mtdtvaalra lhhparpwqh awrqphlgay rqmlarratl
       61 ravlaaafqp rwtadfltla pataapdfae elavvaergd dqiradlrat rpgplpeils
      121 adgltaevvf lldwvwghtv rpewpnrrrr lqadivarta rlsaegwagv lagfnpgmrw
      181 lgdgclrvnd ypaaplpldr aeelvfvpah cvrgwvlwdq ptrfgmvypa tgilaettpp
      241 vpegldrlig anraailvrl tsplstsqla svtglslgsv gdhlrvllds glvtkrrsgr
      301 evlywqtsrg atlcgpatge
//
LOCUS       WP_357532426             485 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357532426
VERSION     WP_357532426.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 485)
  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..485
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..485
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=53283
     Region          55..>117
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtpancprcg grlardnhsg rcapcqaaer drltappavp ppfwdhqpvr aalarrhlgh
       61 lirayrhhpy hgrlpltqsv vagwlgitqa qlsrietgpa pihldrlthw atllripekl
      121 lwfrllrlpp idmsdrgaha dsptsvetap vegggttnrr rfnalaalag lggsnlidal
      181 laaddraenl gmehvrlags lvkrfrqada avgadelcda amtvhtrlsa wtgkarvsrn
      241 leatlqaala dlanqaawla idaerrpqar pylndaitra risdnpreev ralaclsllt
      301 redqptesvh caeaalraaq gwstprlrtl lrlrmahaya nlgdasgfnr emasafrefd
      361 rgpqdddlpf lqfvtshelt giqglaflal drparavksl avssttrteh rrnrvlstvr
      421 laeaeyrlgd vnqaartalr vlpevkqlns grttrnlaqv gahlsrentt aardfvdayr
      481 aefrp
//
LOCUS       WP_357532420             319 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532420
VERSION     WP_357532420.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     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=35916
     Region          30..319
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msgpasaapp stglpraarr rtwrralrrd wqlyslailp llfflvfryl pmlgnviafr
       61 rfqpggslfg eywvglryfk mflsdptfwn vftntltlga ltllfcfplp ivlalllnev
      121 rarrlkrfvq svsylphfls ivivaamvmq llsmdgtinq lvragggeai pflqrpewfr
      181 tiyvssevwq tvgwgtilyl aalttidddl yeaaridgan rwrqtwhvtl pgirptmvtl
      241 lilnigtfma vgfekillly npltyptadv istylfrvgf tssnfsyaaa iglfeavigl
      301 ilvlsanlia rrtvgtslw
//
LOCUS       WP_357532502             281 aa            linear   BCT 28-DEC-2024
DEFINITION  amino acid ABC transporter permease [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357532502
VERSION     WP_357532502.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..281
                     /product="amino acid 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:0006865 - amino acid transport [Evidence
                     IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=29939
     Region          57..278
                     /region_name="HisM"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG0765"
                     /db_xref="CDD:440528"
ORIGIN      
        1 msttrhvpsp aqrareeyrr rqttlsvlia aastaaigtl laiavtgapg wervrasfld
       61 pqiardalpa vltglwlnlr llvccalgal llgliiailr tlrgpvffpi ralatgytya
      121 frglpliivl yvltlgvpgl rlqgmpsvlv lgglalvlty sgylaevfra giesvhpsql
      181 aaarslglty rqtmrhvvlp qavrrvappl lndvvalqkd vglvslagpi davraaqiet
      241 aqtfnytpyi lagvlfvlla ipliavtdrv tlraarrqsg g
//
LOCUS       WP_357532515             441 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532515
VERSION     WP_357532515.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 441)
  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..441
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..441
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46265
     Region          6..394
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 msvralpplg ptrrlklpsq aertldnglt viavrraavp lvelrlwmpf srahlargqm
       61 laatllsgte tmssvqiaae lqkiggglsa gldpdrlmls gnglatgldr lleilaevlt
      121 gadypaewva terdrlvdgi qvarsqpghl vhtallkriy grhpyavqtp epeqvravrp
      181 aalrtlhaqr vrpagavlvl vgdvrperal daaekalggw sgaghsaapp papplapgpl
      241 llvdrpgsvq sslrmalpav prthpdhaal qlanlifggy fssrwvenir edkgytygph
      301 ssvehsvags llvaaaevat evtapallet hyelgrlatv ppgaeeleqa rqyalgtlql
      361 gvstqaglas misayagsgl rldflaehaa rlakasaedv aaaaarylap aravtvvlgd
      421 aeriadslgt ltpvetapvp v
//
LOCUS       WP_357532580             853 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532580
VERSION     WP_357532580.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 853)
  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 853)
  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 853)
  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 853)
  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..853
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..853
                     /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=87961
     Region          10..838
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mstdtvtrpv tpgglssaea aqrlrrdgpn steapprrhl tvrvlrqltd plvalllaaa
       61 vvttvlrdyp dtavillvva vntiigvvqe vradraiaal dqlaaptarv lrdgrdlvlp
      121 aadlvrgdlv rieagdvvpa dllleetsrl rldesaltge smpvardige easagtvvtv
      181 gratgtvvrt gaasalgria slaattrpgp tplqrrlsal grvlglvavl lsglvfalgv
      241 lggrpvvema vtavslvvaa vpeslpavvt lalalgarrm ataraiprrl haveslgsvt
      301 viasdktgtl tegrmavqqa rtadggrfev tgtgyaphgv iqrdgervav tdelrrlara
      361 gllcndatla apdeqrpdwg avgdpleaal vtfaarcgle pqttrrawpr vaehpfdqel
      421 rrmttvhrsc dnrylvvckg apesvlaapl vdadaeelae laaaaaelag aglrvlalaa
      481 alvdtpptdp ahpvglqvvg lvgvgdplra gapeiagsft eagvrlvlit gdhpataaai
      541 agqlgvwdpg dpvvrgddgd paeadpaarv fartrpeqkl divaamqarg hvvamtgdgv
      601 ndapalrrad igvamgggte varqaadlvl vdddlstvat aigegrriyd nirrflryal
      661 sggvaeivvm llgplfglav pllpaqilwi nllthglpgv algaepaepg tlgraprspq
      721 esvlgaglgr hilvagalis avtlgagvla ahwerpwqsv vfvvlglaql gvalavrapr
      781 ppgarrgnpa lplavavsal lqvagvlvap lrdllgtrpl gavdllacav vsvlpglllr
      841 ltmmtrrgrg rgr
//
LOCUS       WP_357532586             248 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532586
VERSION     WP_357532586.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..248
                     /product="phosphotransferase 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=27018
     Region          7..226
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 magveevtvv vahneratlr vgdvflkvds dqtridveve amrlapvptp evlwrkppvl
       61 aiaavpgqal grlgepspas paawaaagaa irklhdappp rwagkklvgl daelerecaw
      121 lvdngvlptd lvdrnreiaq aairpwtpvf mhgdlqithi ftdgdevtgv idwseaapgd
      181 plfdlavltl gheerlddll agygtdvdrd virawwslrs llasrwlieh gfdpsvpgce
      241 fdvlrsrm
//
LOCUS       WP_357532575             408 aa            linear   BCT 28-DEC-2024
DEFINITION  NRAMP family divalent metal transporter [Micromonospora sp.
            NPDC047134].
ACCESSION   WP_357532575
VERSION     WP_357532575.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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 408)
  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 408)
  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..408
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..408
                     /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=42595
     Region          10..383
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mkkllaatlg ilsavggfvd igdlvaagqa garfgmshaw vlllgviaic ayaemagria
       61 avtgravfdl vrerlgarma lvnlvasylv tvitlaaelg gvalalqlas gvpyllwvpv
      121 agaavwlvlw rvrfpvmerl fglagltlvv favalfwlpt dwaalgrgav siddggqgwg
      181 aywfvavalf astvspyevf ffssggveer wssadladar fsvlvgfpig gflalsliat
      241 atvvlrpagl tvsdlgevah pvvlafggvg laiaalaffa vtfgaaletg lsaayaaaqy
      301 fgwqwgkrvn preaarfhtv llvsvllgvl llltridpvt lteymliisa valpltylpi
      361 lvvandrtyl gdrvngrwln algavlllii vaaaiaaipv avgtrmgq
//
LOCUS       WP_357532626             270 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora sp. NPDC047134].
ACCESSION   WP_357532626
VERSION     WP_357532626.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047134
  ORGANISM  Micromonospora sp. NPDC047134
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 270)
  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..270
                     /organism="Micromonospora sp. NPDC047134"
                     /db_xref="taxon:3154340"
     Protein         1..270
                     /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=28288
     Region          2..270
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mrvlvvggsg flgrevcrrg vgagwsvigt chcgavrvpg vavrrldvtd rlavrtlvaq
       61 vrpevvvnts yryddwtvta dgaayvaraa aevgarlvhi ssdalhagrs epyadddppt
      121 pifpygaaka aaetavraid pgavlvrtsl ivgegspqir lcrealagrg alfteelrcp
      181 vdvtdlaaav lelatsdyag plnvagpdpv sraelgrlla hrdgldtgal ttttaaergl
      241 vrpaeirldt trattllhtr lrgitellar
//
LOCUS       WP_357532723             311 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357532723
VERSION     WP_357532723.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 311)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..311
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..311
                     /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=34667
     Region          1..305
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mttqphgwrn rllrfdlryt pylliapffl lfgvfgifpi vfngvvalrh wrlddptltg
       61 wagwanferl laddafwnal lntfgiflls tvpqltlali vagllnrglr aqtwfrvgvl
      121 lpyvtpltas tlifavvfar dtgaanwvls vlgmaepidw raakwsswia iatmvnwkwi
      181 gynallylaa mqsiprdvye aaavdgagpw rqlwritvpm irpvviftvi lstigglqlf
      241 tepmlfqqnt aaatgganre wqtialliyq vgwkdlnlgy aaamswalfl iiivvavlna
      301 vvtnrlgggr r
//
LOCUS       WP_357532745             706 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357532745
VERSION     WP_357532745.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 706)
  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 706)
  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 706)
  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 706)
  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..706
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..706
                     /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=75818
     Region          1..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 meaaaqrnsv pperalpfft fvtaivtlag avtavslval pseipalpvg fwlmaglavv
       61 cdarpftppg rrqssavfps icftfaimll wgeapaiavq aaavvvaswr mrhtvwrtvf
      121 niaqyalalt aaytvirlap glpyvvtvva aaatwfavky gtvtvairll tgghwwrsvs
      181 hglafellst gsllllgpil asaartnaal iplvvvplya vyrmarlste heqvgrldpl
      241 tglanrkall gevadrlpah aeraarhaae rhlallvldl drfkhvndal ghavgdrllv
      301 evagrltaav rpqdvvarlg gdefailsgr ladpaeatdl aarivevlae pvpidglpld
      361 vggsigvavy pehgedfetl mrhadvamyd akhrgdavav yapdsdhssp erlslladlr
      421 rvlettgpqh sgggpatgre tatagragat agreaggage itmyyqpqie iatgevvgve
      481 allrwrhprr gmvdpeelir vaeqsavmrl ltrrvvddvv eqvakwaaag lplraalnvs
      541 vrdlhtgeia dqiddrltry gvppdrlqle itegalmadp rrvlatiarl drigvaiald
      601 dfgtgyssmq hlrrlplsev kvdrsfvlgm tgdaddaaiv rsiielagal glrvvaegve
      661 dertwrmlhe agchvaqgwf yarpmpadel aawlaryhpl rphltt
//
LOCUS       WP_357532727             881 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357532727
VERSION     WP_357532727.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 881)
  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 881)
  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 881)
  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 881)
  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..881
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..881
                     /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=92236
     Region          252..878
                     /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 msvepllrap arpvpirlvt llapavvapf aiaaalsgav svlvavaaav vpvaavctar
       61 lirlalsfra iekrtsgcrg agllglgvla tgltaaalpl vpagrlpsva laglaaatvl
      121 svlgllllpg aavtisvrlr rgfdglsmga sfafagwllh pagaapkaal aaglvaaagl
      181 siivitalra arfrraalls gagasatvlg mtiltwllay dappatllaa gavlagapll
      241 twigasrtev ggrplahgea egnfsaypll tvpaviatla aayhlvtvgs fdvtsivlgl
      301 aviptlvvre vlsaldvrry arrlaeqeah frslvsgand ltlvvgedll irwqspaaar
      361 lfglsdadvl grafpelmhp ddaadvtaal tgvltrraad ggrpplvtar lvdghgvlrd
      421 testisdqrg vpevgalvvh vrdvgerrhl ertlhemaft dqltglanrr elmrtivtqr
      481 svsghtgall vidlhgmagi ndvrgrevgd avlievgrrl ratidrddva arlagdefai
      541 vtvegpmlay tlgtrllaal tepyqlpgav vhlhlsigla elaggdgvdd vlrradlarr
      601 rarqlgrnri ewydayleeq lvrrmdlere lsgaagrgel dlvyqpvlgl hdgqpvgvea
      661 llrwrspalg tvlpaellpv aedlaiavei grwvldracr qlatwshpsr plwmavnvtp
      721 helaapdfvs tvaatlaahh lapeqlvvev aearvasdvp tvvtqlaglr algvrtaldd
      781 fgagqaslaq lrrlpvdilk idralvadsg rgtqskplid vvvslgrrlg leivaeglet
      841 dgqvdqaraa gcrygqgfal srpapaerme aflesfrsps l
//
LOCUS       WP_357532780             228 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [Actinomycetes].
ACCESSION   WP_357532780
VERSION     WP_357532780.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 228)
  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 228)
  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 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 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..228
                     /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=24796
     Region          40..216
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mtdyppfavt vdlvvltvra dalhlllvrr gippdegrwa lpggfvgide dlpdaavrel
       61 teetglpepa ghleqlgtyg rpdrdprgrv vtvawlallp dlptpvagsd aasaewvpvd
      121 rltlgqlafd hdrivadgle rarakleytp lasafcppef tvaqlravye tvwgtrldpr
      181 nfhrkvtgtp gfvspagrat egdrgrpaql frrgpatrlh ppmlrpep
//
LOCUS       WP_357532820             217 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357532820
VERSION     WP_357532820.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   ter Beek,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 217)
  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 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..217
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /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=22158
     Region          1..211
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msrtvvasrv tvgyggepvl revsamavpg rvlavtgpsg agkttllwtl agllrpvage
       61 vsvaghplrd pdhavaekiv lvpqgnglaa iltaaenvrv allaggvaad eagrrtttal
      121 drlglagqad qlveelsggq qqrtaiargl amhgdvllad evtseldaan rgrvldllhg
      181 earrgaavvf athdpeaaat cdaelhlvdg raetvrr
//
LOCUS       WP_357532838             279 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357532838
VERSION     WP_357532838.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30159
     Region          60..>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 mtgeprlgdv fgellrdaya vhtgigprpl vggrlprpvi eiierddglv ngapaahyld
       61 gpehwqpydh ravdrtrgat ldvgvgggri alvlqergvp vtgldtspga lrvsrhrgvr
      121 dlvlgtvdeh vadgrrydtf lllgnnlgli egrerapafl aalaalarpg aqviahgtdp
      181 ygttdpvhtg yhewnrqrgr lggqlrlrlr yrelgtewfd ylvcsaeela elvrgtpwrl
      241 tdvddrdapy ylatlrlagp gggergrqav igargaggr
//
LOCUS       WP_357532845             391 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357532845
VERSION     WP_357532845.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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 10280671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..391
                     /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=42621
     Region          6..>56
                     /region_name="Methyltransf_13"
                     /note="Putative zinc binding domain; pfam08421"
                     /db_xref="CDD:429987"
     Region          91..237
                     /region_name="Methyltransf_23"
                     /note="Methyltransferase domain; pfam13489"
                     /db_xref="CDD:404385"
     Region          <279..380
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
ORIGIN      
        1 mtgqachacg aaelvpfadl gtipvfcgvh wasrdealas plgemrlayc pscayvrnva
       61 fdpaalvydt tmdtnlhhsp afqtfsaelv rhladryplk gatvldvgcg qgeflrelch
      121 vsgarghgyd amfagpvged psgavfhsth aplddstpaf dfvtsrhwfe hlddpygflv
      181 rlrelaggrt vhgyievpda cydlatagwe viyphvsyfd ayalrsiver agwrveatgp
      241 lfsgmfrfve fsvnadgppr sdaplpdtad rdrqltsiag fadrhhaerd hwrttidrli
      301 aegdrpvlwg agsrgvqflh ladpdhrlaa vvdvnprkwg rylpvtghev tdpatlaelg
      361 tgsviitnpa yrkeitatlr qlgvtaqllv a
//
LOCUS       WP_357532873             545 aa            linear   BCT 28-DEC-2024
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357532873
VERSION     WP_357532873.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..545
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=57113
     Region          4..285
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
     Region          <340..537
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mareihtvgv vglgtmgagi vevfarngvd vvaveitdaa ldrgrdnltg stdravargk
       61 lapadrdall srvtfavgld alrevdlvve avperldikr rlfadldrtc kpatilatnt
      121 sslsvteiaa atgrpeqvvg vhffnpapvm rlvevirtvv tapevvadve alcarlgktg
      181 vtvddragfi vnallltyln qaagmlesgh vgredldtam rlggglpmgp lalldligld
      241 tayeiletmy rrggrdrrha pvpllrqmvt agwlgrksgr gfysyekpgs avvvpdgwap
      301 spapagaaaq vatvgvvgsg epaerlaelf tgagydvvav tgeldrlaga dlvvtagpgd
      361 pdadralfta ldgickpgav laasttrlpv idlamatgrp advlglhfld papdralvei
      421 vhtvrtaptt tataravcer lgraavvcad ragyvvdall lpylndavrm leasystadd
      481 idhamrlgcg ypvgpfelld rigldvalat lrdlyrqsre pglapaplle qlvtagrgfr
      541 vhpgd
//
LOCUS       WP_357532996             175 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357532996
VERSION     WP_357532996.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..175
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..175
                     /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=18257
     Region          <8..126
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mgtqsvperl qwtvdrlglk pgddvleigc grgvavalva dlldggtita idrsdkaidg
       61 arqrnrehvd tgrvvlhtaa ledvelgaat fdvifavnvn lfwvrradae agllkrllrp
      121 ggrlhlvwep pgggkatqia dtvggllsdn gfevtvgtgt tgtgaalvdv rgtvr
//
LOCUS       WP_357533008             250 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357533008
VERSION     WP_357533008.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   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 250)
  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..250
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..250
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=26875
     Region          5..102
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkeqrerrty gqqcglayal divgerwtll ivremllrpr ryrelldalp gigtnllaer
       61 lnfltqagvi eptdpdrrtg gyaltelgek lrepvlamar fglavmsgqs epspatvtra
      121 swavlaieam cqaeratade tyefdvagev fhviasdgkv atrsgpatdp vlrigtdtqt
      181 ffdlgsglie pveavlsgsv tiegppaavp rclyllglgs epaersllgp arrtprrpat
      241 gadpaltsar
//
LOCUS       WP_357533014             233 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: anti-sigma factor family protein [unclassified
            Micromonospora].
ACCESSION   WP_357533014
VERSION     WP_357533014.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 233)
  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..233
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..233
                     /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=24769
     Region          1..>67
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtrcefahdd gayvlgalap adraayerhl sgcaacreav aevavlpgll grldpttlee
       61 flppppeisr vpdliavard rrrrertrnr rryaltalva aafalvlgfg gaaalrpagp
      121 papttqavrm vsmapvspkt palhaeigls gtkwgtevim hcgydatagy gkantfrlva
      181 rgpddateqi aswlaapgdd vnlrgatrft dadlvrlell radgtlvlsy dvr
//
LOCUS       WP_357533027             431 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533027
VERSION     WP_357533027.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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..431
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..431
                     /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=47254
     Region          4..425
                     /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 maeprwrqlg lrtvqlagiv tghavasvpa vvrvaprgrk avrealwtrl rglltamgas
       61 yikgaqllst rqdlldpalc eslsklqdrv pamsdrqvre tvekayaggd wpfaefdwep
      121 lasgsiacvy rarlldgtdv avkvrrpgla wrmtadfglm atgagviqri pgfarlpavt
      181 mvrqireavl gqldfaaead alnllranlg dltylrvpap vadasregvl vmefvpglrr
      241 frrdelapev aelavrrvlq cvyrmlfidg vvhcdlhpgn lyldeegevv lldagfvvhl
      301 tprvrklfae fffnmsrgng rqcasivers arneagtadl erfragiidl vegahakpag
      361 efqlapfaat lfdlqrrcgl faapefvfpl lsllvlegmi nefdadvdfq aeakpvlira
      421 lltaipkeka a
//
LOCUS       WP_357533082             261 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533082
VERSION     WP_357533082.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 261)
  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..261
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..261
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27013
     Region          1..249
                     /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 mqslhladag galryhdlpg tgpagvyipg lacsasadfp etaahpaird rrwilvdpfg
       61 vgfsdrpadf sytieahaat vaalldhlgl tscavvgssm ggavaitlat arpdlvgyll
      121 laepaldrgr gmlspyladl deaefvergh relvemlaka aadghtgagn faaavraaap
      181 hamhrsgrsl rqprdpgfrd qlyrlpmgra vvvgarsgvd vgafaahgip ayevpdaghs
      241 mmdenptgfa talaaglagw r
//
LOCUS       WP_357533102             286 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357533102
VERSION     WP_357533102.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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..286
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..286
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29493
     Region          20..270
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 maddrtlggd raagrpglgl dvaggtatir idnpakrnam tvrmwrelpv lldrlaadpr
       61 vrvlvltgag dtfcagadig sldellgvgg dggdgqiaav vaetalaafp kptiaeirgh
      121 cvgggcqlav acdlriaadg trfgipparl gvvyplpttr rlvelvgpaa akyllysael
      181 vdtahaarig lvdevvpadr ladrvralaa tlaerslltq saakeyvala saarhggadp
      241 gagrvaywer emrtagdlae gvaafherra prftwnppgp gqtpag
//
LOCUS       WP_357533182             311 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357533182
VERSION     WP_357533182.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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   3  (residues 1 to 311)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..311
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32932
     Region          14..230
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msdghtgpta ggeiivsslt kqyrnvkavd nlsfrvqpgr vtgflgpnga gktttlrmll
       61 nlvtptsgta tidgrrypdl keplrtvgal leassahkgr tginhlrvic aasglpkqra
      121 detlamvgls paakrkfkgy slgmkqrlgi aaamlgdpkv lvldepangl dpegirwmrg
      181 flkglasegr tvlvsshlls emqlladdvv iiaagklvrq gtvdevlgsm ttgarirvrt
      241 phadqlakal aeqnakvqrg edglllvegs daafvgrval aaqvelhelt perpdlervf
      301 leltsgkavi r
//
LOCUS       WP_357533255             195 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533255
VERSION     WP_357533255.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..195
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..195
                     /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=20515
     Region          <32..133
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mknpdewdra yaaaglafdv ephpelarav gdlqpgrave fgcgegrpai wlatrgwrvt
       61 avdfsqvavd rgrqvadrhg vevdwqvada rayepvgsid lavvlylhig saeiatvlrr
      121 aaaalapggt lfvlgwdrsn avagtggprp adllydaael travaglrvr raeavpqlgs
      181 adaadlvlta yrppa
//
LOCUS       WP_357533296             445 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533296
VERSION     WP_357533296.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 445)
  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..445
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..445
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48432
     Region          1..430
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 maarraripa tkypverltl dnglrvvlap drtapvvgva vvydvgirse pegrtgfahl
       61 fehlmfqgsa nleklahfrh vqgaggtfng sthfdytdyf etlpsnaler tlfleadrmr
      121 gprlteenlr nqvdvvkeei rvnvlnrpyg gfpwlklppv lfdtfpnahd gygsftdleg
      181 atvadaadff eryyacgnav lavagdfdva eatalverhf gdvparpape rpsfaepdlt
      241 aerrqsytdp laplpafasa wrvpdpigdf daylpyvvla evltdgeasr lverlvqrdr
      301 svtsvgsylg fmgeafevrd ptalllqahl ppsgdvdkvl rtvdeeldrl atdglapgel
      361 artqarmath llrdndavlg ralgvavleq qrgapeline lprlvgavte eqvraaaatl
      421 rperratvev iagaaapagk gkanq
//
LOCUS       WP_357533386             491 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora sp. NPDC048894].
ACCESSION   WP_357533386
VERSION     WP_357533386.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     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=53616
     Region          1..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 matehvdvli vgaglsgvga achlrrdcpd ktyavfeard aiggtwdlfr ypgirsdsdm
       61 ftlgysfqpw tdpkaiadgd sirryvrdta rrygvdehir frhrvvragw dsgtarwtvh
      121 arrddtaeev vltcdflftc tgyyrydagy tpdfpgvery agrlvhpqhw pgdldhtgrr
      181 vvvigsgata vtlvpalarr aghvtmlqrs ptyvialptr drvadllrrg lparlayplv
      241 rgknvllgtv nyqlsrrapk avrafllraa rgrlpagydv drhfsprydp wdqrlcvapd
      301 gdlfaavasg rasvvtdtvd tftpggvrlg sgvelpadvv vtatglqlla lggmaltvdg
      361 vdvdlgatva ykgmmlsglp nfaltigytn aswtlkadlv atyvcrllrh ldatgqqvvt
      421 pvapadgpls piidlrsgyv lrsvdglprq gprtpwrlhq nyvrdvllmk hgrlvdegvr
      481 fsraaadtpv g
//
LOCUS       WP_357533338             781 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357533338
VERSION     WP_357533338.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (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   3  (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   4  (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   5  (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   6  (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 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..781
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85655
     Region          2..760
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mdetwqirrt atdldrlset esvfalsngw vgwrgtldeg qpygmpgsyl nglherrrqs
       61 ypedgyafpq esdtvisapn aalirlwvag epldlrtgtv rahertldlr agvvrrhtew
      121 ispaghgvrv rstrlvslpr havaavdyqv eplddrpvei rvcsdvlane pvperaddpr
      181 aasivpdpld aelhrpdghr gvlvhrtdrs aqrvavavth atdvpagftd gddhtpdrlr
      241 ttlegrlapg qrlrltkyaa yectpvdggt pdeladlvta eadaahrhgf dalladqrat
      301 lderwrtadv eidgdpelqq avrfsvfhll qagrvdgdrt iaakgltgng ydghvlwdte
      361 syvlpvltyl lpgvargalr wrhdhlpqar draaelrltg atfpwrtigg recsgywpag
      421 taalhvnadi adavlryvtv tgdqefladt glellvetar lwagyghwsd dgafhvtgit
      481 gpdeyaalvd dnvftnlmvr rnlrgaadaa grhperatal gvdpaeiagw raaadavhlp
      541 ydhkrgvhqq aagftgqpew dfaamtdddy plllhypyle lyrrqvvkqa dlvlamqrfp
      601 geftaeekar nfayyqartv rdsslsagsq avlaaelghl dlaydlfaea alhdladlgd
      661 ktgdglhlaa lagawtavve gfgglrddtg vlsfdprlpa ridrlafhlr whghrlrvtl
      721 trdgaryelp dadpettvdl rhagepvtvt gaaavtrplp qvpdpgpepp sphgrrparr
      781 a
//
LOCUS       WP_357533402             146 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Polymorphospora].
ACCESSION   WP_357533402
VERSION     WP_357533402.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
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   Wintjens,R. and Rooman,M.
  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 146)
  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..146
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..146
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16245
     Region          18..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 mpetahgrki afaafvrkal ddarttrawt gsevsrrtgv srqtinrwvr gewasdpeae
       61 rvvafceglg inptvafgvl gwdrqtsarp apaappmdpd veallrrlvd pnvseaekfh
      121 iretirylay rppipseprk grrras
//
LOCUS       WP_357533419             777 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533419
VERSION     WP_357533419.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 777)
  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 777)
  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 777)
  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 777)
  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..777
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..777
                     /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=82975
     Region          45..713
                     /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 mlvwsarrhs gasrrarlvl aagagvaaas lvvglvglva mvpdwsayre qrvtlagvvs
       61 igvvlsgvlf svgllrmpgl agdtrtvarh lldavvvgaa lwfvgwvlls eptrvlgaat
      121 pttctailla svavaivvgv avvavlrtar prrgliltga givttavggl gvaagvcqpg
      181 tamvlastva vpvgvlvlvw avrfpdtpge phgdvirrgt ayaflpmlgm aasavyhlll
      241 egrftapgia agiaegfalv arqyvalldv rayahrlaes eahyrdlaht daltglanrr
      301 gllkelrrvh qrdvpvvlla ldldgfkyvn dmrghdvgda vlgdvgarlr qnlrpgdlaa
      361 rlggdefavl mrtgpaeaqr aadrllgvlc rpyeqgdgiv flsvsigiar rtggsdvptl
      421 lrnadlalry akqrgknrve qydiaydqll rrrttlehel rgavergelh lvfqpvaeip
      481 avrpvgaeal lrwthprlgk vrpdefipla eecgmiatlg swvlhqachq lalwraaghd
      541 vwvsvnvspr elhapeyveq vaealrahrv psqrlvlevt ehtvatdlde likrlralra
      601 igvrialddf gagysslgql rhlpidilki dhslvaeqks pvdgrpdrvf apyvdvvmrl
      661 ghqlglqvia egvtnqtema avveagcrfg qgqlfgwgvp aehlealles atspgaravp
      721 avprqiggra dggvgapvnr tpdvdpaqss hevdqrnptr gdqdvrsvds aremrqa
//
LOCUS       WP_357533441             315 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048894].
ACCESSION   WP_357533441
VERSION     WP_357533441.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   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 315)
  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..315
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..315
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33708
     Region          18..299
                     /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 mdyvrsgdry gagmltgeek fvrrghvrlw terfghpdhp tvllimgtst qgigwpdelv
       61 ealvdsgrqv irfdhrdtgr sdsvdftahp yaladlaada agvldghgvt aahvvgtslg
      121 aaigqwlalh qasrvrtlta masspmgnnp gpawaramag qppaadelpp ptawflghlm
      181 daakaprata rqrvdadvrt wrvlngsvlp fdepaarrfv ehchqradnl aaaanhdlag
      241 rrwdhdrraa lsgitaatlv lhgsddplfp pahgeavaaq iptarleivp gmghhpffsp
      301 glteriagsi irhts
//
LOCUS       WP_357533486             379 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Micromonospora].
ACCESSION   WP_357533486
VERSION     WP_357533486.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..379
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39806
     Region          7..348
                     /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 mpsdrrpdat gplagvrvve laslapapfg cmvladlgad vvrvdrpggp apgrlaaptt
       61 gplhrgrrvt tldlktpagv adllrlvera dvlveayrpg vaerlgfgpr tcrdrnprlv
      121 yarltgwgqd gplaaraghd idyialsgal eplgrpgerp haplnllgdf agggmllatg
      181 vlaallerer sglgqvvdaa mvdgsallta flhgmlgdgr wsaprganll dggapfydty
      241 rtaddrfvav galepafyaa lltglgladd ptlpaqhdpd gwpelrrrft arfaertrde
      301 wtavfadlda cvapvlapte ahrhphnaar gtfvavggev qpapaprfar tpaaaprpap
      361 dpadpldvat vlddwadrp
//
LOCUS       WP_357533506             414 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357533506
VERSION     WP_357533506.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..414
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43406
     Region          160..401
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msdalldiep glaglapsvg dhlrglrgpl herilatvra amaaqgrslt ggqgqglalg
       61 vqtavdtfvd avadparelt gtrevfhalg rteyreghrv dalrtvltlg ardiwaflve
      121 hatapatpgw patapagpap adlyviagal fgyvdalaga aaegflaeqr dtaqdwattr
      181 rrlvtllvqp dpptgavlha aadaarwplp atvavcsvdg tdaehvargi gagalaavvg
      241 dairvvlpdp gtpgrldrar qalvgrraal gptvqrqrar lsyrlsrral alhqqgalgp
      301 dpvvscddhl ltlltawepg laghlagtvl aplaglrptt rralaetlhg wlrrqgqvva
      361 vaedlhthpq tvryrmrqlr glfgpalddp darllltlal hqhptgepnr sgdg
//
LOCUS       WP_357533523             198 aa            linear   BCT 28-DEC-2024
DEFINITION  chloramphenicol phosphotransferase CPT family protein
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533523
VERSION     WP_357533523.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008105
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..198
                     /product="chloramphenicol phosphotransferase CPT family
                     protein"
                     /calculated_mol_wt=21313
     Region          1..184
                     /region_name="COG3896"
                     /note="Chloramphenicol 3-O-phosphotransferase [Defense
                     mechanisms]"
                     /db_xref="CDD:443103"
ORIGIN      
        1 msppgqivll ngtsssgkts lagqlltvld gprfrrpyfh lsvdafgamr aarpttqlsp
       61 aevtdvltrt ragfhravag maragndvva dhvlsepwrl rdclevmagl dvvlvgvhcs
      121 aeelarrerv rgdrqigqaa aqvervhahg vydvecdttt ttpydcavri rdfllarppg
      181 ptafdrlraa aagrpygr
//
LOCUS       WP_357533542             516 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora sp. NPDC048894].
ACCESSION   WP_357533542
VERSION     WP_357533542.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 516)
  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 516)
  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..516
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..516
                     /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=55476
     Region          32..499
                     /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 mslpgstvea pvtgtyplpp rahllnagtv adyrravaqg iervaarvte vdrpatgvtp
       61 delapriagi dldrplgdtt aaldelhdvy lrdavyfhhp rylahlncpv vipallgeav
      121 lsavnssldt wdqsaggtli errlidwtae riglgpaadg vftsggtqsn lhalllaree
      181 ayarivgggt drpsrpevls rlriitstag hfsvqkaakl lglgadavlt vatdagrrmr
      241 tdelaetldr crrdgqtvla vvatagttdf gtidpldria eictaagvwl hvdaaygcgl
      301 lvsptrrhll agieradsvt vdyhksffqp vsssallvrd rrvlrhatwh adylnparma
      361 erripnqvdk slqttrrfda lklwltlrim gadavgalfd evvdlaaaaw rlladdprfe
      421 vvtrsqlstv vfrylppgag rdvvddanly arealaasgt alvagtkvdg ahhlkitlln
      481 pettlddiah vldliaehag wyartratae lsspvg
//
LOCUS       WP_357533567              95 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HesB/IscA family protein [Polymorphospora].
ACCESSION   WP_357533567
VERSION     WP_357533567.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 95)
  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..95
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..95
                     /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=9622
     Region          1..>71
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mltltdnavt virdlttqqe vpegaglria tdtsagaltl gladqpaqgd qvvddsgari
       61 fldpeaaqil ddkaldasvd aqggvqfgit eqqag
//
LOCUS       WP_357533590             650 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533590
VERSION     WP_357533590.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 650)
  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 650)
  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..650
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..650
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=71785
     Region          293..641
                     /region_name="COG4867"
                     /note="Uncharacterized conserved protein, contains von
                     Willebrand factor type A (vWFA) domain [Function unknown]"
                     /db_xref="CDD:443895"
ORIGIN      
        1 mtggnryryg swrggpdpla ppydvraavd qvgaevlagg slrqalrdll rrgpqgrggl
       61 ddltararrl rreamrrgnl dgavtraqal ldqalaaerd elagrdddda rfaqarldnl
      121 prstaravee ladyrwssde arglyqqild glrgdvleqr fagirdalrd pdpaarrrle
      181 emltdlnall drhargadtt daftefmrrh gdffpekpgs vdelvdalar raaagerlmr
      241 slspqqreel srlmdqafgd galadrmrdl tanlrtlrpd lgwdraervr gredlgygaa
      301 agaleeigel ddlldqlgqe hpgatlddid veavqrslgr eaaddvrrlr elerelrrqg
      361 wvtrdgdglt lspkalrrlg gtalrrvfnd lsgrrrgqhd lrdagaagev tgasrpwayg
      421 deqpldvvrt vsnalrrgaa vpvrlevddf evveterras aavalcvdls fsmisegrwg
      481 pmkqtalals hlvatrfpqd alqivgfgrh alplsreqla avepdlvqgt nlqhalklag
      541 rhlrrhpgae pvvlvvtdge ptahledgea vfswpptlet vqatvvevde ltrfgatlnl
      601 fmlgedpglr rfveavarrs ggrvftpdad dlgryvvsdy lrarrgrrar
//
LOCUS       WP_357533596             338 aa            linear   BCT 28-DEC-2024
DEFINITION  mechanosensitive ion channel family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357533596
VERSION     WP_357533596.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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 338)
  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 338)
  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..338
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..338
                     /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=37980
     Region          75..323
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mkaflvvata iagaclvawl tgmavrwiar rryepflmkf hracfwpwat mlvfgtlyyv
       61 lpatgissgk lagyrhgvqi gliaatgwll ikylfvaedv afrrlpvnva nnrrvrrart
      121 qiglmrrmta lvitiltigt aamtfgplra fgasvlasag vagvilgfaa httlgnavag
      181 lqlaftdalr iddvvvvece wgrveeiklt hvvvrlwder rlmlptsyft nkpfqnwtrh
      241 earvlaavtl hldftahide iraethrlle qtplwdqsew vlqvvdgsdt sicirvlasa
      301 sdgpsawdlr celrekliqy lrekhpewlp rlrsefkp
//
LOCUS       WP_357533624             304 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357533624
VERSION     WP_357533624.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  AUTHORS   ter Beek,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..304
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..304
                     /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=33900
     Region          24..303
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtsisarrrp satrrrwant ngmwagilfv lpmlvlfvvf rfvpsfgaig msftdyrlng
       61 dfevigfeny srlvsdpifr nalvttliya afyvplivvv smftavvldk lvwgvgffrg
      121 alflpyvtsf vlagviwywi ysadglvngl lqrwgidaip flsgdqwqvl gslsvvsvwr
      181 gfgysmlill aglktiptel teaakldgan avqrffrvtl pllrpvvffv vvietiaafq
      241 vfdtvyvmtg ggparasysl vyalydegfk ffdfgyaati gvaifalvfv isiiqrrfld
      301 rdet
//
LOCUS       WP_357533689             417 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC048894].
ACCESSION   WP_357533689
VERSION     WP_357533689.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..417
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45305
     Region          5..408
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mgpstvedll rvlapqvlga vvrryghfdt aedavqeall aaatrwpveg lpehprgwli
       61 tvaarrltdl lragqarrrr eddegraqrw iapaadhrep vddslillfl cchpalppaa
      121 qialtlravg glstaevara flvpeatmtr ritrakqrir dsglpfalpd aderparlda
      181 vrqvlylvfn egyastagph lrrvdlstea irlarllhrl lpddpevtgl lalmlltdar
      241 gparvgpage lvpmaeqdrr rwrgdqiaeg valisavlpr gdvgpyqlqa aiaavhdeap
      301 sadetdwaqi valyevlmri sdnpvvalnh avavamargp vdglrlldvl aadprigddp
      361 rrhaarahll ercgslaear aayahaarls tnlprqryly grlarltdag dgehgng
//
LOCUS       WP_357533737             330 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533737
VERSION     WP_357533737.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=35056
     Region          23..317
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtrpagpadr saipaddara alhrlraeva kavvgqdavv tglviallcr ghillegvpg
       61 vaktllvrtf aaaldldakr lqftpdlmpg dvtgslvfdp rtaeftfreg pvftnlllad
      121 eanrtppktq sallevmeer qvsvegtprp lpqpfivvat qnpveyegty plpeaqldrf
      181 llkltvplpt rdeelgvlra hhagfdprdl aaagvrrvat atdlaigrea vgavgvaepv
      241 lgyivdlcra trvspslelg asprgatall ltakawawla grdhvtpddv kavaraalrh
      301 rvrlrpeael egvtadavld avlgtvptpr
//
LOCUS       WP_357533762             341 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified
            Micromonospora].
ACCESSION   WP_357533762
VERSION     WP_357533762.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 341)
  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 341)
  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 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   5  (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
REFERENCE   6  (residues 1 to 341)
  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 341)
  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..341
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..341
                     /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=37780
     Region          41..339
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mttrdttvaa gsdrtrpdgp tgtprgrrpa rrrrvplrtr lardwqllvm vtpgflvllv
       61 fsylpilgni iafqdynpyl gdnplqafar snwigfgqfq llfedsafwe alrntlaita
      121 fqlvfffplp iflaimlhnl lssrwrgfvq tvvylphffs wvlvvsffva mlggagllaq
      181 tmrdagmqpw nvmtnpdtfi ilvtaeavwk dvgwgtivfl aalstidtsl yeaaaadgag
      241 rwrrlwhitl pglrpvivll lilrlgdals vgfeqfllqr davgrqaaev ldtfvyhfsi
      301 atgnygygaa aglfkaaigl glilaanrva hllgergiys k
//
LOCUS       WP_357533757             170 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Micromonospora].
ACCESSION   WP_357533757
VERSION     WP_357533757.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 170)
  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..170
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..170
                     /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=18710
     Region          3..159
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrdaeefdaf yassaqrvlg qvyamlgsrt eaedavaeay arawsrwatv recdspeawv
       61 rkvayrvavs awrkavnrvt ahrreatgqq vepvsvdhvv lvdalrhips eqrraivlhh
      121 lvglsvaeia aetranpntv ktrlargrqa larylsddgh qtaagrshga
//
LOCUS       WP_357533889             212 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533889
VERSION     WP_357533889.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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..212
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..212
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=22611
     Region          85..176
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 maqrrtpsgq gparrpgqpg rgttrrtgrp aardfgvrvd arggsgrtpg tgrttdgprs
       61 asrpaaarra aaggaakrtt aqqprritgr atvliavlva lalaytypvr lylsqqsdia
      121 rieaaqaaqr ehidelaera elwqdpeyvk tearkrfymv mpgevpmvvl tdpegaarda
      181 gvepagppad papwydtlwa siqaandegq hp
//
LOCUS       WP_357533867             340 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533867
VERSION     WP_357533867.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 340)
  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 340)
  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 340)
  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 340)
  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 340)
  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..340
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..340
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36423
     Region          25..314
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtggdavsgg rqaggiavpd vgrmaravld svgtvvvgkq dalelvlagi lagghvlled
       61 lpglgktlta rsfaqalgld frrlqftpdl lpadvtgsfl ydqskadftf ragpvftnll
      121 ladeinrtpp ktqaalleam qekqvsvegv tyrldapfhv latanpieye gtyplpeaql
      181 drfllrvsfg ypdreqewdi lrrrmsrqre eadlepvvda aallamqaal etvvvedsig
      241 ryivdltaat rehasvlvga sprgslalll larakaalag rdyvipedvk evavpalahr
      301 itlrpemwlr rvdpsfvvde vlsstpapas galptyaagf
//
LOCUS       WP_357533925             588 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [unclassified Micromonospora].
ACCESSION   WP_357533925
VERSION     WP_357533925.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 588)
  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 588)
  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
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..588
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=61580
     Region          6..532
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 msagnlagil egrcadradl pglygedgrs wtfdqidlla ggvaaalrae gvgpgdrvac
       61 yltngpeivf llfgawkiga vpvtvsslyn aaelaesvak taprlllvdd rrpdvvaafl
      121 aaraaagdaa raapgnddad gtgagdvaag ppvrsvtasl agvpalpwrr evrvtgvevg
      181 peaeacilft ggttgrpkav svthggtres lmrlarvttg tgaegtaapd arpnlialpl
      241 fhsggqhall fayfvgrpav vwerfgvdrl adlmarfgfd nlfllptmvf divhadrdlp
      301 fagvksvlva gqaiswpvrr afeeryrvpi lvnygsteag hiagwtgrdm kagrwkpgsa
      361 grvypgvele irddagtalp sgaqgevvvr saltrgyvdd aaasaelvrd gwvhtgdmgy
      421 vdadgvlflv grkrdmikcg gfqvwpeeie delrahplvr dvrvlgrpdd rlgeipvalv
      481 vratdgtvdd tdlsarlvay arerlahfkt prriefvpal ersatgkisr vadpaaqpag
      541 agaaapspdp tdadhaaaaa paadsvasva vsrphdgrts rptargsr
//
LOCUS       WP_357533926             496 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357533926
VERSION     WP_357533926.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 496)
  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..496
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..496
                     /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=52448
     Region          238..470
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtvvapaagp grppdreapp gdapghppma gyavgpvagg khraagpppv lpawpvtgll
       61 llyplwwalg lgvlifpila vpmayallra hlggrpvrlp pgfwlwavfl avlvvsmaal
      121 gseptgavpg pasgrmvgvl frlveylamt vllihagnlt erelpvrrlv rllgwlfvvt
      181 vaggllgvfa gtfeftspve mllppeirgr gfvqslvhpy aaqihdiigd qrprpaapwg
      241 ytntwgnnfc llvvwfvvaa wgqvtrrrtr llalaclavs vvpvvislnr glwiglglaa
      301 gyvalrlala grvwvigala aaavalaaal vvtplgnvvt arldngksng vrsyligrav
      361 agvaespvig ygstrttigg rhsitvgesa dcercgnfti ggngqlwqll iahgltgtfa
      421 ylgflgygvw rfrrdrspvg iagscailgs faamlwynal vtplafmfla yallwrnegr
      481 qadesghhrt gtpdrr
//
LOCUS       WP_357534015             418 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357534015
VERSION     WP_357534015.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 418)
  AUTHORS   ter Beek,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 418)
  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 418)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..418
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42396
     Region          28..414
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mttttaavqk esapapaptl gdhvrgylar vrggdigalp avlglvvlcv vfsimrpsfl
       61 sagnfanlft qgaavtliam glvfvlllge idlsagfasg vcaavlavlv teqglpwyva
      121 llaalgtgvl iglvlgllva kigipsfvvt lagflafqgi vlllikggnn vsvrdsvlva
      181 ianrnmppvl gwvlagvava gyaavqllrh rnraarglvt dplavvaari gglalilgva
      241 vyilnqersr vlvtslkgvp ivvpiiavll ivwtfvlqrt aygrhiyavg gnkeaarrag
      301 invdririsv fvicsamaai ggivaasran svdantggsd vllyavgaav iggtslfggk
      361 grvldavlgg avvavinngm glmgyssgvk yvvtgsvlll aagvdalsrr ratatgnr
//
LOCUS       WP_357534022             412 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357534022
VERSION     WP_357534022.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 412)
  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..412
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..412
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43801
     Region          5..75
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maiptvgdrl aeirrearlt qeqlaersgi svevirkleq gsrgaarldt lhalaralgv
       61 stsallgdas qaaargepgh rqlslaeirr vvapvrgidg aplvvpadep pgldtlrrnl
      121 haadhvyhag dyavalrvvp pllvnvraav glvgsdrqhe aydllaraqh lagglliqlr
      181 addlaqtals aaldaaqrsa nrvvaatvir tmcwllmrqg rigesaglav vtadeveprl
      241 sraapeelaa wgwlllsaaa ahardnrpde vadligvaaa aaarigervp asdhlmlvgg
      301 fddakvqmqr veaaavagda grvlelsalv ppvptisasa wrrhrldlaw ayaqlrrygk
      361 atavltqlrd taptwlrqqr yagdivdtiv tgrrramtde laelaeltgg ar
//
LOCUS       WP_357534028             594 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: type IV secretory system conjugative DNA transfer
            family protein [unclassified Micromonospora].
ACCESSION   WP_357534028
VERSION     WP_357534028.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..594
                     /product="type IV secretory system conjugative DNA
                     transfer 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]"
                     /calculated_mol_wt=63015
     Region          170..556
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mssgsprgad lffwafclvv lanaalftva wlggtlgagv tghgwqtppf tlgayfmvis
       61 gaagalwpga spyalysgml vvallvvvpa vlvgrrlldl rgrgvglarv rdlapltpag
      121 iaararelrp slagvrqlap ddtgnllgdl spngpelrss fedveldlma pragkstgia
      181 vprvlrarga vlltsnksdv yavtraerer vgtvwtfdpq giahvprqmw wdiladcvti
      241 egarrlaghf vasvnddtak kdfwisaaqn tltalflaaa rgrapvaell gwladpadrt
      301 pidllrdagm aamaeqlqgt vrgavetrdg iyetarqcva clldpeilaw vspdpylpqf
      361 rpdrhvlgrd tlfllskdgg gsaagviagl adatlragvv aaermggrld ppmtavldea
      421 anvcrisdlp dlyshlgsrg invvtllqsy rqgsrvwgea gmdalwgaat ikllgagldd
      481 adfvekvskl vgqhdvstvs vsrsrdgssr stsyrqehvl ppdriralpk gtalllatgi
      541 rpavitlrpw ykepdagris aqarqevaai teraagkata tpwqanwret ptag
//
LOCUS       WP_357534032             374 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357534032
VERSION     WP_357534032.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 374)
  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..374
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..374
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=40170
     Region          63..372
                     /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 maadngrtka krragifgav vgvaaaglaa giaaeraivr rskrgvgdiy aeerfgalpy
       61 detctvttad gtdihveive padgveidag fitgvaagpa eptivfvhgf cldmgtfhfq
      121 rseltrrgdy rmvfydqpgh grsgrlesge yelpalgetl ravidetvpe gplvlvghsm
      181 ggmtimalae lypqmferrv vgavliatsg glveqakfgl ptiisrfgsp llplvnnatr
      241 ltggvidrar taasdlawlm trrygfgttr pspalvsyve kmnsgttaet varylrtlyt
      301 harypalatl retptlvivg dkdmitpvah seeilrrlpd aefikiadsg hvvmlehade
      361 vnavlidflg kler
//
LOCUS       WP_357534136             341 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534136
VERSION     WP_357534136.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..341
                     /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=37251
     Region          15..339
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mvkkpadepa gekqsdrepl lvvkdltkhf pvrgglisrk eyvravdgvs fsvapgetlg
       61 lvgesgcgkt ttgrmlvrll eptsgsivfe gkdithakrg glralrqdmq iifqdpyasl
      121 nprhtvgnii smplevngin ppggvkkrvq ellelvglnp ehfnryphef sggqrqrigi
      181 aralalkpki iiadepvsal dvsiqaqvin llrelqrelg lafvfiahdl avvrhfsqri
      241 gvmylgklve lgdreqiyer pshpytrall savpdvtkfg tggrirlegd vptplnppsg
      301 crfrtrcwka qdicateepp lsvkpsgsla achfpesgel t
//
LOCUS       WP_357534156             547 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [unclassified Micromonospora].
ACCESSION   WP_357534156
VERSION     WP_357534156.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 547)
  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 547)
  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
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..547
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=57090
     Region          88..542
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpaehhndgr raaehqhadh ratehhndgr raaehqhadr ratepghhgg hdragrgsad
       61 rdragsgtva agderwpqpv lrllttggdr pvfedgdriv gaaeladlvr rtasglraag
      121 igpgravalr igvtpealag vlaaftvgar vsgirpeltp aqldrllasd dallvddtrl
      181 aalartpddg splvaagrpa diaritwtsg stgnpkgcaq tyaamgaawa ayperwpaai
      241 adlaprlgry lvfgslssqv mleygiltla aggtlvaarp pgfpgmitrh ratasvitvg
      301 klhqlvrdqr tdpvdlsslr alvvsgsplt asrlaealdv lgpvvfhgyg qtetgmiamv
      361 tptelladpg rlasvgrapd vvdlsirdat grpaaegelf vrtpaqasay wadpaetaev
      421 ftdgwvrtrd larldadgyl hlsgrvrdvi ivnanlvyag piervlaadp avaeayvvsr
      481 pddvtgeavh ayvvpatgcp ldvgrlrdrv aatlgaaavp ttvevidrvp vgpsgkpdkr
      541 algvgtg
//
LOCUS       WP_357534171             438 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357534171
VERSION     WP_357534171.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..438
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..438
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45191
     Region          <217..422
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msrsgelaaa rprlavaaap apaafaqwla elafggagwp ellaavaert gaacrlvaes
       61 gellaasdga dgprcaatpd dvrralvtgr agtgvptlvr cvdgwtgrav avgagsrrlg
      121 alllaepvaa gqlalagaat tallieavrh espppavrda atvlralrdg lgdptgspag
      181 pagggagllr ageaglpqag etgpsaagga gplrpgeael lragaahgwr ldqphavagi
      241 aytgaqqrrw asalswldrp vlaegrrawt llhgdverev trlrvrldqi vgagqvrvva
      301 galvtgpart aesfrdadrl lrlllrapde rvelpfgqag laqvllavpd erlrwfvhrh
      361 lgpiahrddl lrtldcwlat ggsrqavser lhlhrnsvgy rvglikrllg vdpldpqtva
      421 vlrtalaare llaaseag
//
LOCUS       WP_357534177             314 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified
            Micromonospora].
ACCESSION   WP_357534177
VERSION     WP_357534177.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 314)
  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..314
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..314
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33048
     Region          43..311
                     /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 mrkpvrvvlt tlgvlvavpv lllattavvn vvatkseass itrygqlvpv dgkqmnvvva
       61 gsgaetvvll pglgtaapgl dfqplitelr styrvvavep fgtglsdpad tdrtaanitr
      121 evhealrhlg idryvlmghs iagiyaltys asyadelvaf vgidssvpdq pggdepiptg
      181 vivglsklgi tralaaiadd pyaglpyder trkqlrllsa kntaaptmvn emehvsanfa
      241 avsgktfpkg lpvllfvrsd dpdvagwval heqqaasvdt grvvllagdh ylhhtlsaei
      301 aqetraflaa rslr
//
LOCUS       WP_357534265             455 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357534265
VERSION     WP_357534265.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 455)
  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 455)
  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..455
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..455
                     /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=46603
     Region          3..454
                     /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 medlgrlfrl aadhaagyre slpdrpvgas inqgalaeaf tgplpsvpcp peqvladlla
       61 aaepglvasa gpryfgfvvg galpaataad ilaagwdqla tnavtspaai aaeaaagvwl
      121 kellgipasa svgfvtgaqa antaglaaar hhlladagwd vdrrgllgap pirviagaer
      181 hatidrslrl lglgtdlvep vpagpngaid lgllrevlqg gpsgptivcl qagnvntgac
      241 dplreacelv rrhggwvhvd gafglwaaas patrhlvdgl eladswacdg hkwlnipyds
      301 gfafcarpdv haaamsfaas ylvgsggvpa ggdftaessr rargfavwag lrelgrdgvt
      361 alvdrccala rrfaagltsa gfevanevvl nqvlvgfgdd artdrvvaav qadgtcwagg
      421 ttwrgrrlmr isvsnattte edvdrsiaai vrlat
//
LOCUS       WP_357534361             192 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TlpA family protein disulfide reductase [unclassified
            Micromonospora].
ACCESSION   WP_357534361
VERSION     WP_357534361.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..192
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19886
     Region          59..187
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrrllaalla vlvlagcsag ptaetapvla ggastlpgpv padlalrppp gtapaapaft
       61 galtdgtplt aaglwadrpv vftffsswct tcvarqdals elarrhrdrv vfvgvagadq
      121 adelqdylrt hrveypvvvd eqqtvwrsya vreppavvlv akggallrgw pggldaaale
      181 qrleelvlag sg
//
LOCUS       WP_357534325             692 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357534325
VERSION     WP_357534325.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 692)
  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 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   3  (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   4  (residues 1 to 692)
  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 692)
  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..692
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..692
                     /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=72639
     Region          1..628
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
     Region          <632..>691
                     /region_name="PHA03377"
                     /note="EBNA-3C; Provisional"
                     /db_xref="CDD:177614"
ORIGIN      
        1 mtadathpdt vagvlrrtae drwrivrllp raggpavcaa vvvnlllaaa pvlfvvatsr
       61 migwlpqavr dgvdapafgh lvtafvvaag alsaqqllaq lqvatgllvq rridgwvade
      121 lmtaalssvs ttpledqall eqlteasrev ehgiqspgaa gagmlallar ygqllgyavi
      181 vgaafawsag lgllvavlaf rhgqrgglrr yaaiygsvva rirrltyfrg vamgrpaake
      241 irifgllpwl reqyreayld wmrpvwaqrr rvylkpyfly tavgltvlva vlaalglagg
      301 ggqlgltrla lviqavlaav qlgefypead vqtqfgmnay ravgefragm rdrtatgdva
      361 agpavepasg ragdrpagpv dirfeavsfr yphrstpvft dldltlpaga ctaivglnga
      421 gkttlvklls rlalpdagri tvgatpvddl ppahwrrhla vifqdflrye tsaadnialg
      481 aiahaddreg iraaadaagi ldtldalplg ldtpltgqlr dgvdlsggqw qrvaiaralf
      541 avrhgasvlv ldeptasldv raearffdei iaattgvttv lishrfatvr radhivvleq
      601 grvveqgshe ellsrggrya rlfslqaqrf aahpdpvtsd atdagpptag pptagpptag
      661 pvdggavdgd ldggpldagg aaadvgspgs tr
//
LOCUS       WP_357534371             303 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Micromonospora sp. NPDC048894].
ACCESSION   WP_357534371
VERSION     WP_357534371.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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..303
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..303
                     /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=34636
     Region          4..257
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mlavvvgtgr cgstlvqell srhpgvgfvs gvddklsrln lagrfngply rrsaprpagm
       61 tslrhsrrll ekgrlrvaps eaydlldrhv vagfsrpcrd ltaddltpyl rrrlraffda
      121 rierqgcrll lhhvtgwpra gflragypql rvvnvvrdgr avtnswlqmg wwdgwrgpdn
      181 wflgplptdl rqeweeydrs fpvlaalgwk mlmdsfaear aahpegqwld vryedlladp
      241 rgevarmldf ldldwspafe rgfgryrfha grqaayheel gdaqlaaver vldkplrqwg
      301 yrd
//
LOCUS       WP_357534402             417 aa            linear   BCT 28-DEC-2024
DEFINITION  RCC1 domain-containing protein [Micromonospora sp. NPDC048894].
ACCESSION   WP_357534402
VERSION     WP_357534402.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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..417
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..417
                     /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=42895
     Region          65..410
                     /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 mgtgndfhpt paatsahrrr seflatvval avvlmigdal gatagravaf amppnpgtqq
       61 vpaklggvra iaagdahsia llsdgtvvtw genffgqlgd gtnarrttav rvcavgqsap
      121 csrsltgvia iaanrndnla llrdhtvvaw ghnssgqlgd gtwtnrttpv rvcavgqvap
      181 cgkflsgvrs iaagwghsla vvgnalavaw grnyegqlgd gttvgrttpv rvcavgqvap
      241 cdqflyavka iaggelhsms lrgdggpvgw ganyvnqlgd gtvvnraipv rvcamgeiap
      301 chrflygirh itvgashsma qlssggvlgw gfngygqlgn gtwdtrlqat rvcavgeaap
      361 cdrflsgirs iaagtahsla lqpdytvaaw gynaqrqlgd gtttwrptpv qvlapqt
//
LOCUS       WP_357534428             443 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534428
VERSION     WP_357534428.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 443)
  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..443
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..443
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46311
     Region          9..81
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mstevavpdr dpatlglrlh alrtargltq relaepryta ayvssvesgr rmpsgdalth
       61 fadrlgvpat elatgrspae avradlalte adrtaasdpa gaehvyrraa tgaddpgqva
      121 rgwlglgrla llqgdpqtae rhferaeppe gsppwlrada tagraaalrq rgehryaayl
      181 lantrddlvr aglpdpiall vlhtelavch gelgdedaaa saaetalsla gspdpdhvta
      241 lhltvartll ddgqltaaai aaeqarqair qallrvelaf chrargrgrw tagdpvggva
      301 dltiahdilt saaatepald tgvelaevyr avglpdqatp lldaaltagg dgprvaraar
      361 vlgmlaadag dadsahrhlr aavahyhrtg prhelaattl llanllekqg radetldilr
      421 talarveqla aetgtgtttt sar
//
LOCUS       WP_357534439             142 aa            linear   BCT 28-DEC-2024
DEFINITION  YkvA family protein [Micromonospora sp. NPDC048894].
ACCESSION   WP_357534439
VERSION     WP_357534439.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..142
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..142
                     /product="YkvA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15104
     Region          <57..124
                     /region_name="YkvA"
                     /note="Uncharacterized membrane protein YkvA, DUF1232
                     family [Function unknown]; COG3339"
                     /db_xref="CDD:442568"
ORIGIN      
        1 mlrdvllgva vaalatwaal lvgllivrpr galltealrl lpdllrllrr lagdatlprg
       61 vrvrlgllma ylavpidlip dfvpviryad daiivaavlr avvrragvda vrrhwpgted
      121 gfaalcrltg irppdgdrpa ag
//
LOCUS       WP_357534445             342 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534445
VERSION     WP_357534445.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..342
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37425
     Region          10..338
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mtahqtpapr vaedlnralh eamsrdervv llgqdildpy ggafkitkgl ssrfpdrvig
       61 mpiseqatvg iagglalcgn rpiieimfad fvtlaydqil nfltksvsmy grrvpmpvli
      121 rcpvggdrgy gpthsqylhk qllgiphltl felspfhpcg plleeilsgd epamlfenkl
      181 lygrrvhtdg ivddlfqydy ldprgrvari sigapadgdv vviapgglce rvlsaarrlf
      241 ltreircqil vpvqlypldl tallptlaga arvcvveedv agatwgadva ravyerlwrt
      301 lrhpvtvvss rhgvipaarv lekqvvvqad dvyraiaedi ha
//
LOCUS       WP_357534495             537 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534495
VERSION     WP_357534495.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 537)
  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..537
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..537
                     /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=56810
     Region          7..124
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          222..505
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtvtiaqvla lpdlnlrvva gdaglgnevr wvhvsetvdp tpwlrggell lttglkieqp
       61 eqfepyvhrl adaglaglgf giglghaqvp epliraaaqr glpvlevpvd apyvaiseav
      121 snllaaeryd tiarafdaqq altaaavesg rggivaatar avggwavltd laanvvrafp
      181 pqaadrlpal lpdvmrarer girssgsvvg ptesvaihtl gargrmrgfl vagvpgrssd
      241 ysrmvlagav allslemers qaatrqvrrl radplaqilr gavtdqvagq hataweldpt
      301 avrvavylca adragrvcdd vnelmseagl pgavvaqdag rqtrvavltd atdrataala
      361 elasvrpmvp lglgdvvpve qvglsyraat haaevgraer ravtrfddle alhmlfraqs
      421 pqalagfvrr vlgplqqhdr gregallasl rsflahnghw netaaelgih rhtlraridr
      481 ieqvtgrdln saygrmelwl alladsaadt ddfagpapdr pagpvpdrsg grgqdrk
//
LOCUS       WP_357534511             123 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534511
VERSION     WP_357534511.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=13105
     Region          23..111
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mqyvgsakit tpaisplage pikradaerl agvlkafadp arlrlisliq sspsgeasvt
       61 dltaplglsq ptvshhlril teagllerdk rgvwvyyrlv psaiagvadl ltpprkramk
      121 kvr
//
LOCUS       WP_357534514             321 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [unclassified Micromonospora].
ACCESSION   WP_357534514
VERSION     WP_357534514.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..321
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35761
     Region          3..321
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mtraqfsaet sgggafvrqp nrftgrvtph stspegggpd dqgrwpleag ryrliwcrac
       61 pwahramivr gllgldgvis lgtvdpirde rgwrftldpd gfdpalgigl lseaylttdp
      121 dytgrvtvpa lvdtltgrvv tndypqltld lstewrrlha pdapdlypva lrpeldalma
      181 eihtdvnngv yrcgfatsqq aydeayaalf arldvlsrrl adrrylmgda iteadvrlft
      241 tlvrfdvayh ghfkcnrqkl tempvlwaya rdlfqtpgfg etvdfdhikr hyyathrein
      301 ptgvvpvgpd tsgwltphgr a
//
LOCUS       WP_357534536             566 aa            linear   BCT 28-DEC-2024
DEFINITION  murein biosynthesis integral membrane protein MurJ [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357534536
VERSION     WP_357534536.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Kuk,A.C.Y., Hao,A. and Lee,S.Y.
  TITLE     Structure and Mechanism of the Lipid Flippase MurJ
  JOURNAL   Annu Rev Biochem 91, 705-729 (2022)
   PUBMED   35320686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     gene            1..566
                     /gene="murJ"
     Protein         1..566
                     /product="murein biosynthesis integral membrane protein
                     MurJ"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=56060
     Region          19..>406
                     /region_name="MurJ"
                     /note="Lipid II flippase MurJ/MviN (peptidoglycan
                     biosynthesis) [Cell wall/membrane/envelope biogenesis];
                     COG0728"
                     /db_xref="CDD:440492"
ORIGIN      
        1 mgtpgtvtga griagaaali avltvasrla gfartgvftw vvggtdlggv yliantvpni
       61 ifeivaggal aslvvpllag aiaagdraav aattgalltw tvtllvplav vvavfagpiv
      121 aaiandptpa evavgarmlr ifapqlplyg igivltgvlq ahrrfawpvi apllssvtvm
      181 aaylvfagtq grgvdiagvd lagelilavg ttagvvvlsl slliplralr lrpaptyafd
      241 adarrriggl avagavtvvg qqvallvsln lvsggatgvg avvpynlaqt iyllpwsvla
      301 vplavaaypt laaahttgde dgyratlapt vrrvlllsal gaaaltavar pvaqffftgv
      361 aaeqaaagiv gfapgllgyg lfavlsraly argdtraaav atglgwlavp aaavllaaav
      421 pddqrvpavt gansvgmvvl gavlvvavar ragpgtvagl praagvalla gglaalagtv
      481 vgnwlagagl slwpaadagg gtpahtvall qgmlagavva lvfagvaypl drhdlrpmva
      541 avgrrlrggr rdgpdrhdda egtdpr
//
LOCUS       WP_357534574             205 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC048894].
ACCESSION   WP_357534574
VERSION     WP_357534574.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..205
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21955
     Region          6..187
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 marerptall ldfdgvlrhw dpavaagier eyglsagvlg eiamhwgrlq pvltgqvsha
       61 dwvssvadal tesvgpdrar aavqqwqryr gevdadvlaf vrevraagvr vglgtnatdl
      121 ldtdlaelgl vgeldvvvns svvgvhkpak eyfqaaceal etpparvlfv ddedwavrga
      181 raaglsayrw sgpeglrylr aalgl
//
LOCUS       WP_357534586             252 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534586
VERSION     WP_357534586.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26555
     Region          2..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mriaivtgas sgigqsaaiq iakrgtgvil tyrdnhagas dtvatiekng gtavalrldi
       61 grsetfpafr dsvvvalrdt wqrdtfdylv nnagssrmal fedtteemfd almrvllkgp
      121 yfltqtlrpl ladggaivnv tsnaasssgl epgysaygtm kgglvvltry lakefsrrgi
      181 rvnsvspgst rtriadnafe rhpevvpgla aktalgrlge pddigvaiaa llgedgswit
      241 aqnievsggy nl
//
LOCUS       WP_357534608             151 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357534608
VERSION     WP_357534608.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=16693
     Region          9..139
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtidiaegvv trqrvylddl dgfgvlhhag yavlfdravi dywleagwap npresvqvvr
       61 eltityhapi vgmcdvdvhf wveragrtsv tyrfevlstt ravryaegsr vlvnldpvsl
      121 rpvpltdgmw eiagpllgrg vsrpdtgepv s
//
LOCUS       WP_357534646             803 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [unclassified Micromonospora].
ACCESSION   WP_357534646
VERSION     WP_357534646.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 803)
  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 803)
  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 803)
  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 803)
  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..803
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..803
                     /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=84555
     Region          60..737
                     /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 mrlppgmvav avlsgllaaa atalladsar rrggphrqah llfalaaava latlvaggva
       61 llgatehgah qrgrhpgwas viaggtaltg lafcagllrl pgamvaraaa arllldglvv
      121 atsiwfvgwv llseptrllg patpsacpai llasvtaait agltgmvvar adgprtrlav
      181 lgtgitatat gglvvaagvc qggsamavtg mallavglla gafavhrvda pgqvdidlir
      241 rdgeyafipm vamagsamyh lmqggrfdal givagslegf alvtrqyltl ndvrryagrl
      301 aereahfrel ahtdplttla nrrgllremq rcaaeggdcv llgldldgfk nvndmrghdv
      361 gdmvlaevgr rlrsnlrpgd laarlggdef avlmrgrpad advvaerllg vlgrpydqag
      421 gavflsvsig vagqggdpdv vgllrhadla lryakqrgkn rierydgsyd rlltrrtrle
      481 hemrgaierd elrlafqpva slpsvrpvga eallrwhhpe lgnirpdefi plaeecgmia
      541 klgawvlhqa cwqlsrwlad ghdvwvsvnv sprelhapey vvqvaealra hhvppqrlvl
      601 evtehavatd ldelirrlta lrltgvrial ddfgagyssl gqlrrlpidi lkidhslvae
      661 hepvrpvgrd gpafapmvdi vmrlghqlgm eviaegvttp telaavvaag crfgqgalfg
      721 wgvpaehlea mleaatspga rpasappapp paprrptpsp llprlrshpp atppvpaprp
      781 ayeesaqagp vdetptgdgv prs
//
LOCUS       WP_357534696             377 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534696
VERSION     WP_357534696.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=38658
     Region          5..375
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtapdvlvig agvvgaacaw yatraglrvt vvdrgpvagg ttgagegnil vsdkppgael
       61 rlaqlssglw rdlgeqvggf eyepkggvvv asaaetldql gtladdqrga gvevtmigpd
      121 glsdyephln palaggayyp qdaqvqpala aarllraara egarlrsgve vrgllrdgdr
      181 vtgvrtgdgd laagavinaa gtwggeiarl agidlpvlpr rgfilvtepl privrhkvya
      241 aeyvsdvasg dadlqtspvv egtpagpvli gssrervgyd rtlsvpalra vaakaiglfp
      301 vlagvsvmra yrgfrpycpd hlpvigpdpr apgllhacgh egagiglsaa tglllsqvlt
      361 grdteldlap frperfa
//
LOCUS       WP_357534712             406 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RCC1 domain-containing protein [unclassified
            Micromonospora].
ACCESSION   WP_357534712
VERSION     WP_357534712.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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..406
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..406
                     /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=41182
     Region          62..401
                     /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 meqrqnsrlw arwrraarst vtaaavslgv aalavgfsag aavagvggva tnaafaaapv
       61 aqvtagdlht cairtdgtlw cwgdnyggkl gdgtttnrtg pvqvgtattw srvdagtshn
      121 cairtdgtlw cwggnysgql gdgtttsrst pvqvgtattw agvsaganht cavqttgtlw
      181 cwglnrnaql gvgtspsrat spvqvgtgtt wasvttgyah scavqtggtl wcwgdstdgq
      241 lgvgilgyra tpaqvgtast wtgvtaghah tcavqsggtl wcwgengygq vgggtgvqts
      301 piqvgtattw tgvvasvdss calrtdgglw cwgnngfgql gdgttthrsa pvrvgtattw
      361 tqnlgvsyhs cgvrtdgglw cwgnnmsgql gdgttthrst paqlvl
//
LOCUS       WP_357534714             217 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534714
VERSION     WP_357534714.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 217)
  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..217
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..217
                     /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=24109
     Region          33..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhavetgqia ndagrprqac dapagpdgqg lrdrkkaats lalhqaamrl aiahglsevt
       61 veaiadeanv srrtfsnyfa nkedallyed rvrvrrllde arsrpeheta wqalrqvaas
      121 ryadwdeldp wwaaqtrlir lhpslraqqm avhanterel aqeisrrtgd plaarlmvaa
      181 flsaqriave twlegqgarp laevmeqald lvgrnfe
//
LOCUS       WP_357534733             514 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357534733
VERSION     WP_357534733.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   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
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..514
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=53647
     Region          16..508
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 masttvtpar raartvpdll awraeahpdr vaievhgvat lsfaawesaa gavaaalhrr
       61 gvrpgdrvgl vfgardwvdf avaycgvqra gavsvplsdr lapgqlrhal ehcaaaavlh
      121 agaagtgpdg adglpaypva elsgepagda pvvdhrvrpg dlaqilytsg ttgrpkgvga
      181 thanltvhap nhprrlalgh serflhafai gtnaaqtmlf nalsakptal tpaqftpgrf
      241 arliatpgtg tvflvpsmai elldsgaldg rdlshvhlig staaalapav aarlsaafps
      301 aavvnyysst eaapaqttmi fdparrdavg kavggtlmia dddgeplpag etghvwlrcd
      361 hprayyrdae asaatfrgew vrmgdvgrmd adgylyltdr hqdviksgaf kissleveaa
      421 lhehpavaea avvpvphpvl gsaiaavvva rpdtppadle lpalrgflag rltdyqlptr
      481 vlvvedlprn eggkvvkrel itrfetqaet qegp
//
LOCUS       WP_357534777             581 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357534777
VERSION     WP_357534777.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 581)
  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 581)
  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 581)
  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 581)
  AUTHORS   ter Beek,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 581)
  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 581)
  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..581
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..581
                     /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=62084
     Region          42..566
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mssttlgara avltgrlrgg ssagwfpyll vlplalvlwg yvvqpmlatf gesvaedgag
       61 nylsflgsag varaslftsl aisaasvllc givgvgmafl lkrftfpgrr lieaiilvpa
      121 alppligais fqllysetgi lprglqqlfg taspllafdg iagvlvvhtf tmypffylaa
      181 saalagmdps veeaaynlga srvrvwrtvl lpmltpalvs gsllvfmtsl asytapllfg
      241 vdqtmtmqiy inrtngdlpm astyasvlgi vsivfllgmr wyegrrsyrs mskgiaahrr
      301 eitnpfgrwl alvgsllatv vllapvatia lvafsqdgsw ttevipsvyt tenfvaifte
      361 prsfqpilns lqmsalatvg civigvltay avrrlkffgr glldvavmia walpgtvvai
      421 nlisafstgn afslgqvlvg tfwivplayf vrflplvfrs ssaalaqldp smeeaarnlg
      481 atwwrafrtv tlrlmlpgvf agallafvhg vgefvasvli ytssttpisv ainnrmysfe
      541 mgtaaaygml qvalifvvml vagrlenggr rtsreatqwv n
//
LOCUS       WP_357534806             311 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: S1C family serine protease [unclassified
            Micromonospora].
ACCESSION   WP_357534806
VERSION     WP_357534806.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 311)
  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 311)
  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 311)
  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 311)
  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 311)
  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..311
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..311
                     /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=30107
     Region          142..>308
                     /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 msdtmlrpap tnpvppavpv seppsssppp psaapsptsp psppvspspp sppvspsspa
       61 psspsrwrrg llaggaavvl mlagggtgal vvdrfagqgs svtattaaap vstatidsla
      121 tvvavvspsi vtvevtgare sslgsgvild tdglvltnqh vvdsggqvdv aladgrtapa
      181 tvvaqdarad iallratglt gltpatlgsd stltvgdtvl afgsplglvg tvtsgivsal
      241 hrsvddlsgl vqtdaainhg nsggalvdta grvvginvai attgedegsv glgfaipmdt
      301 vrqvvarlta s
//
LOCUS       WP_357534815             338 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Micromonospora].
ACCESSION   WP_357534815
VERSION     WP_357534815.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..338
                     /product="GlxA 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=36259
     Region          6..326
                     /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 mtlvphrigv laldgvvgld lgtpaqvfga actadrqply tvdtctpggh pvrsssgfrv
       61 lpdhgldllt tvatvvvpgl hggppmtdgt vdpavtvalr qahdrgvrim sictgafala
      121 aaglldghra tthwahvepf rrlypqvdld pdvlfidsgq vltsagvaag idlclhvirs
      181 dhgsevanra arrcvvppwr dggqaqyier pvprspasgt aatrewarqq lhepvtlrel
      241 aaharmsvrt ftrhfrsetg lspaqwllqq rtdharllle ttdltvdqva rragfgttaa
      301 lrqhlhtrig vspstyrrtf rrpppsvdhp vvgsatta
//
LOCUS       WP_357534875             274 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534875
VERSION     WP_357534875.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 274)
  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..274
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..274
                     /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=31957
     Region          2..244
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 maisdlhigy qenrdhvagl rpespadwll iagdiaeqva dvewtltvla rryakvvwvp
       61 gnhelwtpre dpvqargvqr yehlvelcrr lgvvtpedpy piwngpggsv livpmfllyd
      121 ytwrpehtrd kreslayaye tgivctdevm lhpdpyptrd dwcrarvdet lrrlderehp
      181 dlpivfvnhy plvreptril rypefaqwcg tdltadwhtr yrtaamvygh lhiprttwhd
      241 gvrfqevsvg yprewkhrgp tppaprqilp yegq
//
LOCUS       WP_357534901             317 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357534901
VERSION     WP_357534901.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 317)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..317
                     /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=34839
     Region          14..300
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavvtapska psdasvmpdt pgwarwandh rkwlfaapam afvvaliifp lgwtiylslt
       61 dssgsvraes efiglrnyid vlgdtdrfwp avgrtaaftg vallfevvlg maialllwrp
      121 frgekwvrva illplvatpv avgmmwrlif dpniglanqa lgwigigpqp wlagqhtalp
      181 ttifidiwqw tpmvvlilla gltslsdepq eaamidgasp wqrfrhvtlp llmptvivav
      241 llrgidalkt fdilyatkgr gggsfnevet lnvyayglsf dyneyglsst vlilffliii
      301 gsmwaltyrk kkqeagr
//
LOCUS       WP_357535015             192 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357535015
VERSION     WP_357535015.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 192)
  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..192
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..192
                     /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=20154
     Region          3..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mirrtprthg eilaaaarrf avtgykgtsl qdiarevgcs kaavlyhfag keallaelma
       61 gpisvlceld eriaaltgaa aqqaaaegfv dlavrfrgei allrgefpel laqpafahih
      121 liserlieam tgpdggqdar vaalvllagi aegcgtfadi pdeelrpall avaqrvlvta
      181 appptpdhqh hd
//
LOCUS       WP_357535186             268 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357535186
VERSION     WP_357535186.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 268)
  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..268
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..268
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29137
     Region          1..264
                     /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 mpvsyldrge griayevtgt gplvvclpgm gdlrsvyrft vpalvdagyr vatvdlrghg
       61 dsddgfsrhd dvalgtdlla lieelggpav vlgnsmgaga avwaaaeapd ritglvllgp
      121 fvrdpdlgpa mnlafrllla kpwgpaawhw yyqkfypgrp padltehrar ireslrrgdh
      181 wrsfvkttrt shrpaeqrld svhaptlvvm gtkdpdfpdp vaearfvaer lsgelllvpd
      241 aghypmaeyp elvnpelvrf lgtvhada
//
LOCUS       WP_357535205             209 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Polymorphospora].
ACCESSION   WP_357535205
VERSION     WP_357535205.1
KEYWORDS    RefSeq.
SOURCE      unclassified Polymorphospora
  ORGANISM  unclassified Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 209)
  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..209
                     /organism="unclassified Polymorphospora"
                     /db_xref="taxon:2685497"
     Protein         1..209
                     /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=22185
     Region          19..177
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtsagaadaa rageaaqpaa rrrsrrdeil diavglfaar gyhgvsmddi gsaagvtgpa
       61 lyhhfagkea mlvaalipvs eslleggrqr vaehpddpda alqslvnfhv dfalanpavi
      121 alhlheldrl pdeprrqirr lqrlyveewv tvltglhpgl vaaesrvlah aafglmnstp
      181 flggevdrqr rasllraatl aalraasds
//
LOCUS       WP_357535228             342 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Micromonospora].
ACCESSION   WP_357535228
VERSION     WP_357535228.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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 342)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..342
                     /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=35111
     Region          1..138
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
     Region          202..331
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mqerrriaay gwcaddtgrv llvrgaaadp apglwrlpgg gvahaehpad tvvrrftget
       61 glgvavgglr aavadlstrr lgavevpvht drlvfhvtvl dgqpshgdqt tadgpaelaw
      121 ctpqqaatlp lmpftaelfg lparpaagpp gppgpppppp aagpptgpap sdspagsesa
      181 eeagsaevts agveptadrr qrfaayglvt dpdgrvlltm iapgypgagl whlpgggtdh
      241 geqpvdgllr elveesgqrg ridrlmladn lhnpvalgpe grpldwhgvr viyrvlvdep
      301 tdpvvteaag gstqaaawft saqlsglamt dvaelatgrt vg
//
LOCUS       WP_357535239             622 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: S8 family peptidase [Polymorphospora].
ACCESSION   WP_357535239
VERSION     WP_357535239.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 622)
  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 622)
  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 18791949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..622
                     /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=62087
     Region          36..622
                     /region_name="COG4935"
                     /note="Regulatory P domain of the subtilisin-like
                     proprotein convertases and other proteases
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:443962"
     Region          125..379
                     /region_name="Peptidases_S8_PCSK9_ProteinaseK_like"
                     /note="Peptidase S8 family domain in ProteinaseK-like
                     proteins; cd04077"
                     /db_xref="CDD:173790"
     Site            order(128,131..132)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173790"
     Site            order(156,187,246..247,274,341,344)
                     /site_type="active"
                     /db_xref="CDD:173790"
     Site            order(156,187,344)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173790"
     Site            order(293,295,318)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173790"
ORIGIN      
        1 mnlprrtvlv gvaaltaiaa atpalaaept gtirnaggat avadsyivvl kdsavsrasv
       61 dttasslagq yggsiartys salrgfearl darsaarlaa hpsvafveqn htvslagtqp
      121 nppswgldri dqpnlplnss ytypnegsgv rayvidtgvr tshndfnqas sgydavdggt
      181 addcnghgth vagtvggtsy gvakdvqivg vrvldcsgng tyagvidgid wvtanavlpa
      241 vanmslggpa dssvdlavqn sidegityvv aagngnifgq rqnacnyspa rvpaaitvga
      301 tqsndaaasf snfgtcvdil apgvsipsaw htndsatnsi sgtsmasphv agaaalvlsq
      361 nptwtpqqvr delvntstpn vvtnvgtgtp nrllfvggtt ppptnnfsvs vaptsgsvva
      421 ggsvtatvst attagspqav slsasglpsg atasfspasv tsggsstlti attastaagt
      481 ytvsvngsga agtrtatytl tvtgtgggcs gtngtdvaip dggsavtssi visgcnrnas
      541 atsrvavniv htyrgdlvvd llapdgtsyr lknssasdsa dnvnttytvn lsseaangtw
      601 rlqvrdvyla dtgyintwtl tl
//
LOCUS       WP_357535235             293 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357535235
VERSION     WP_357535235.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   Wintjens,R. and Rooman,M.
  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 293)
  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..293
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32456
     Region          14..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          99..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mterrsptvr rrrlgaelrr rredagvtie mvaerlrcss skisrietgh tsatprdvad
       61 mlgiygvvgp egeelvqiar earqkgwwhp ystvltgayv gleaaarsvr ayeqqvvpgl
      121 lqtgdyakam irsarpdita eeverrvrvr lqrqslltqd dpievwvvld eavvsrpvgg
      181 devmraqlar lveaadlpnv tlqilpfevg ahagmdgtft ildfaealdp gvvyaenatg
      241 glflekaeel rkyvfifdhi raaalrpees vaaiaklaee plwrsrpkss gwt
//
LOCUS       WP_357535311             409 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357535311
VERSION     WP_357535311.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..409
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41743
     Region          62..406
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mtdlppagtt lppaavpvdr aagpvpaadp lavvsprygg gsladvlpsa lavlgvpgav
       61 dllglapgla gvrrvavllv dglgwyqlpt aaryaptltg laatvgrplt cgfpsttpts
      121 lvtlgagaap gthgvlgftv rvpgtdrvln hidwhgdpdp lhwqpvrtqw qraraagvav
      181 svvsrpeyag sgltlaanrg gdyrgaagvd algrtmlaal sagagptlvs gyhpdldrhg
      241 hlsgvdsapw riaaaevdgl larlvdglpa daallvtadh gqldvpaahr fdldtdlrlr
      301 agirvvagep rvrylhvepg avddvvatws avlgpaarvc traelvaegw fgpvaeehls
      361 rvgdvvvtcr dtyavlatrs eppaasrlva yhgadsaaem tvpllvvrg
//
LOCUS       WP_357535326             240 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Polymorphospora].
ACCESSION   WP_357535326
VERSION     WP_357535326.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 240)
  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 240)
  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 240)
  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 240)
  AUTHORS   ter Beek,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 240)
  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 240)
  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..240
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..240
                     /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=25223
     Region          29..236
                     /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 msfrglsslt vlagerfaye gpgnpwfswr yvrdnsetil aalrehatlt aqavviaavv
       61 alplavvayw frpltgpila lsgvlytips lallafvapy vgttnpasvl ialvlyalll
      121 mvrntlagln qvpeeardaa lgmgygrlgr llridlplal pgiitgvrla tvstvalvtv
      181 gsligfgglg dlilggfrnn fykaeiltgt ilcvglalvl dlllagigrl ltpwargsvr
//
LOCUS       WP_357535329             662 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Stk1 family PASTA domain-containing Ser/Thr kinase
            [unclassified Micromonospora].
ACCESSION   WP_357535329
VERSION     WP_357535329.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15774046
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..662
                     /product="Stk1 family PASTA domain-containing Ser/Thr
                     kinase"
                     /calculated_mol_wt=70093
     Region          11..600
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          406..464
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          472..532
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          540..599
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          607..659
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          607..659
                     /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 mdiqvadtll gslldgryri rgrvarggma tvytatderl ertvavkiih psqaaearsr
       61 lagfpdrftd eakaiarlth pnvvavydqg thqglpylvm eyvrgrtlre vlaerrrlnp
      121 dealaimeqm laaiaaahra glvhrdvkpe nvlvaeaptg gvanlvdsvv kvadfglara
      181 veasaeegdg nqlmatvayv apelvtdgra dprtdvysag ivlfemltgr vpydgdrpvd
      241 vawqhvdrdv papsvlvpgl prvldelvar atrrdpgarp adagallaev qvarddlgnp
      301 nahtavlgrv aeelpavaqp tmvvaavtpv trptwarlpe patpqrphrr raaesaglgs
      361 rlaelrtrvm gtprgrlsva aavvvvglla amggwwvgvg rytvapqlvn lsradaqaqa
      421 dragfqldfa aprydekipr dgvvaqdpgs aakilkggti tvtlslgper fplpdvvgke
      481 fglaeadltg aklvvakgsp ryddnlpagv vvdtnpkvgt evkpgtkvtv ilsrgrapit
      541 vpdlvgksln darsalsrlg lvvaettyke sdkprdevlg qspadgagve kgtkvklevs
      601 kgppqvtvpr vvdlpcqqak qqlegagftv nvqfnpngtv rfqnpgensq vppgtpvtlg
      661 cl
//
LOCUS       WP_357535343             116 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: histone-like nucleoid-structuring protein Lsr2
            [unclassified Polymorphospora].
ACCESSION   WP_357535343
VERSION     WP_357535343.1
KEYWORDS    RefSeq.
SOURCE      unclassified Polymorphospora
  ORGANISM  unclassified Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 116)
  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 116)
  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 116)
  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..116
                     /organism="unclassified Polymorphospora"
                     /db_xref="taxon:2685497"
     Protein         1..116
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12442
     Region          1..112
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 makhiihklv ddldggdade tvkfsldgvq yeidlsnkna gklrdlfapy vtagskigrg
       61 gvvvggraar grggaaadre qnkairswak kegkeisdrg ripqeivdey hqkagr
//
LOCUS       WP_357535402             326 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357535402
VERSION     WP_357535402.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=35784
     Region          18..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 malttapqpt srtkdpvrts akrgsgrvrr reglagyvfl spwliglmai taipmllsly
       61 lsftnydils swselewvgf anyermftad psywhavqvt lsfaliavpl klaaalaval
      121 llnrawrgvg lfrglfylps llggsvalai vwvnmfnreg afnsflsifg iegkpwvndp
      181 dwaletlmvl aiwqfgapmv iflaglkqvp telyeaasvd gagpvrqfln itlpmlspvi
      241 ffnlvletin gfqgftaafv lsngtggpvd stlmytlnly itgftelemg yasamawvfl
      301 laiaaitivl fstgrfwvhy sdgedr
//
LOCUS       WP_357535413             391 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357535413
VERSION     WP_357535413.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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 391)
  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 391)
  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..391
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..391
                     /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=40126
     Region          1..268
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mttptvalig asghglwhrr alaplhesgr lrlvalvdvr pveaapdapv pegvgvftdh
       61 remlrvarpd vvvictpaht hlpialdcva agadlllekp pvltlaehat ladalaaagr
      121 tcqvgfqalg saaltelrqa vgsgalgtvt gvaavaswrr ddayyarssw agrrsvdgrp
      181 vldgalanpl ahavmqslvi aggcasgrpv svdveryrtr pievddtatm rvtldggppv
      241 vvavtlaged fipgevivhg tagravleyp tdrlrlpger varevpgrvg llenllahra
      301 dpagvpliap laateaftav veaigtapep tlvdavsvga gparvrvieg idgalrlagd
      361 rmallselgv awarppfrae lagaagvgqg g
//
LOCUS       WP_357535418             363 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357535418
VERSION     WP_357535418.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   3  (residues 1 to 363)
  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..363
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..363
                     /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=39607
     Region          1..363
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvtyakas riypgterpa vneldleigd geflvlvgps gcgkstslrm lagledvdkg
       61 siyidsrdvt hlppkardia mvfqnyalyp hmsvydnmaf alklrktska eidrrvkeaa
      121 allqleefls rkpkalsggq rqrvamgrai vrepqvflmd eplsnldakl rvqtrtqias
      181 lqaklgvttv yvthdqveam tmghrvavml dgvlqqvdtp rtlydtpanv fvagfmgspa
      241 mniktvslse kgavfadllv pltreqvata qadggnkkvt vgfrpedcdl vsptegglpv
      301 vvelvedlgs danvyghatl dgvserfvvr tdrrhmpnmg dtvfvkprtd rhhtfhaatg
      361 vrl
//
LOCUS       WP_357535457             258 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357535457
VERSION     WP_357535457.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  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 258)
  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..258
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..258
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27371
     Region          7..219
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 menltqlvsv itpvhapsie ylagayasla kqemppgwdw qwlvqedgqt galadvlpdd
       61 prislgtgrp ggpgvartla lsrvdgdlik vldaddqltp galgrdiaaf dahpqigwtt
      121 srvldllpdg stagwdkdpa ggvidrgavl afwqandyra svhpatlclr rdlvfalggw
      181 malpasedtg lllaanavta gyftreygll yrkwpgqvts qaahrepaey qarmkiiear
      241 analtsmipn fggggaka
//
LOCUS       WP_357535491             262 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048894].
ACCESSION   WP_357535491
VERSION     WP_357535491.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 262)
  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..262
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..262
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28857
     Region          1..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 msyadvnglr lwyeehgdgp plvllhggyg stetfapilp alaerrrvia vdlqghgrta
       61 dvdrplryes maydvaallr hldlpgaevl gyslgggval rtaiqhpelv rrlvlistpc
      121 rrrgwypevl tmmagqdera geqmrgtpph qlyqriaprp qdwpqlwaks gallrheydw
      181 spevaalavp tllvfadads ipvthmaefy rllggghrhp gadgtgrpts rlavlpglth
      241 hdilttpllp qlvvpflahq lr
//
LOCUS       WP_357535507             208 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DUF47 domain-containing protein [Polymorphospora].
ACCESSION   WP_357535507
VERSION     WP_357535507.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..208
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=23766
     Region          5..208
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mkfsfrpteg afyelftraa enlvrgtell nelalpdvdv qsvserltev ehdsdqithq
       61 lykkinsafi tpfdrediyq lgsqlddvmd hleavgnlly lygltklpsl premhelvdv
      121 ldqqakltae amprlrsmkd ledywiecnr lenegdrayr mllvrlfsge ydaltvlkmk
      181 evadeleaac dafehvantv etiavkes
//
LOCUS       WP_357535532             705 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC048894].
ACCESSION   WP_357535532
VERSION     WP_357535532.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 705)
  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 705)
  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 705)
  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..705
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..705
                     /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=77127
     Region          5..701
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mtdqttleqe iaaeqrhldr vyarlaelrr aaaraerdgy rmagvgtfga lverdamvfh
       61 aaqrrhllda eheglvfgrl dlrdrqvlhv grlgvrgdda etlvvdwrap aaaafyratp
      121 aeplgvvrrr tisssdekvt rieddlldpe aappdmpvvg dgallatlsr atgrgmrdii
      181 atiqreqdea irspgsgvti vsggpgtgkt avalhraayl lyadrsrygg ggilvvgpsa
      241 vfveyiasvl pslgeetatl hslgslfpgm satrtdgpev aavkgslrmr rvleraarda
      301 vpdgpqelrl lyrgtllrle rreldgirdr alhrgarrne vrrvgfdgvl aalyaqarrs
      361 avsglpeqra fedeiierpe freflkawwp rlhprhvlgw larpdrlhry aagilsraev
      421 gllvaayrsl dvegltvadi alldeldall grpvrpkkan rdpfqlaggv relstfgerq
      481 raaraaarer pedyrdyahv vvdesqdvsp mqwrmvgrrg rlaswtvvgd paqtawtgdq
      541 qeldrardqa lgrrrrhrft lstnyrnsae ifavaaaeir rlypdlelps avrstgvepv
      601 alhvpaaela patvdavdav laevagtvgv itpvprrdev agwlgdrgga rlqvvtslqa
      661 kgmeydgvvl vcpgeiradp gsgvrtlyva lsratqrltt idptg
//
LOCUS       WP_357535545             393 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: saccharopine dehydrogenase family protein
            [unclassified Micromonospora].
ACCESSION   WP_357535545
VERSION     WP_357535545.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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..393
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..393
                     /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=41604
     Region          3..391
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mshdrpydiv lfgatgftgg ltaeylarha pvglrwalag rnpaklaavr drlaaidpal
       61 aglplltadv tdagslrvva eatrvlattv gpyvhhgepl vaacaavgtd ylditgepef
      121 vdlmyvrhha eavrtgarlv hacgfdsiph dlgvwytvrq lpsdgpimvd gfvraggkfs
      181 agtyhsalta fsrtaqtkqa ararravepr pdgrrarava gklgrsaatg mwavplptid
      241 pqvvrrsaaa cpeygpdfry rhfaavkrlp tvllagvgma gvvglvklpp trrwllgrla
      301 sgqgpsaaqr arswfrvrfv gegggrtvrt evsggdpgyd etakmlaesa lclaydelpa
      361 tsgqltpvta mgdalldrlv ragmtfrvlp ars
//
LOCUS       WP_357535557             254 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357535557
VERSION     WP_357535557.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..254
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..254
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26174
     Region          3..243
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtpvaivtga ssgigaatar rlaaegfhvv laarrtdrle sllaeiatag grattvacdv
       61 tsdesvagla eavgdlpgpv tllvnnagga rgldqiedad vgdwqwmydv nvlgtlrvtk
      121 allpilersg aatvvvvsst aglgvyeggg gytaakhaqt alagtlrlel ngrpirvvei
      181 dpgmvrtdef alvrfdgdae raaavyagva eplvaddvad cvawcatrph hvnidrlvvr
      241 plaqaaqhkv hrvs
//
LOCUS       WP_357535563             722 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Micromonospora].
ACCESSION   WP_357535563
VERSION     WP_357535563.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 722)
  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..722
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..722
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=79783
     Region          65..712
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          501..527
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(503..504,507..508,510,534,537,544,547..548,550..551,
                     574,583..584,587..588,591)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          532..568
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          573..606
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msddrgrvdn dfsgrsgavi qagliqgnvn lravtetplp sprqlppatk gfidrevhiq
       61 qldslldeve litdksrlpv vtistisgsa gvgktalavh wahrvrerfp dgdlyinlrg
      121 ydavppltph ealdgflram dvpaekvprd lhdrtalyrs lttgrrmlil ldnaataeqv
      181 rpllpaapsc mviitsrsrl sgltvrdgai ravldvlssh datrllrvtv gadrvdrqpe
      241 mvdrlielcs hlplalriva drarldeerp laelveelta eesrldalav eeddlsavrt
      301 vfswsyqala aetarvfrlv glhpgadial daavrltgla psvtrrhlds lvglhlltrs
      361 gphrfrlhdl lrlyamerat ldespeavha arerllrwyl hhtyaayrai lpqgrplpdv
      421 dvppdatldd alrwceherl nlldviraap ewghhrlgwq ialasmaffe rrsywkawid
      481 shlagldcar hlgdrraegw lllslgdaww drgdldeagr cyagslhaar evgdawttgy
      541 alrgcglvde drgdfpeatr yarealrtfr qlgeergtgl almslgnaqr gagrfaealv
      601 syddamtvfe rlgnrwsqgl valhrgqtll htgepapala avtsaaalfr elgdrrhaal
      661 arayegdahl qlhqphaare aladalltll elddplaadv rrrlaaldhh davpeqqgeq
      721 dg
//
LOCUS       WP_357535568             461 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357535568
VERSION     WP_357535568.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 461)
  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 461)
  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 461)
  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 461)
  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..461
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..461
                     /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=47987
     Region          20..393
                     /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(29..30,33,36,69,119..120,122..124,127,147,150..151,
                     154,229,232..233,236..238,241,268,272,321..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 mrsvrgwvrd tagglprtfw ylwagtlinr lgsfvlifla vyltsergfs elqagvvlgl
       61 wgaggtvgtl aggtladrwg rrptlltahl gaatmmlglg larelwaiav gafllgmfae
      121 aarpafsamm vdvvperdrl rafslnywal nlgfacaail agfaaqadyl llfvvnavtt
      181 tataviifrk vresaparta vkltgtpaap gglrtaltdr vflvfaglnl llalifmqhi
      241 smlpiamgqd glspatygsv ialngvlivv gqlfvprlir grsrshvlal aalitgigfg
      301 ltafaevawf yaltvliwtl gemlnspsns tliaelspst lrgryagvfs lswslasfaa
      361 piaggwvqqn lgnsvlwlgc galagfvaia qllsgparer raaalraasa paaqpdtpaa
      421 sstgtpddaa pateplvapl ppaqvtaaai tptrkgvstt g
//
LOCUS       WP_357535598             300 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357535598
VERSION     WP_357535598.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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 300)
  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 300)
  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..300
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..300
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32253
     Region          43..267
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 marirparrg rapvsrtvst daqghttgwa ttglgtgvvd rpdptaaaff didntmmqga
       61 siywfargla arryfttgdl trfawqqmrf rvlarehagd msqareaala fvegwrvddi
      121 erlteeifde lmapriwags ralaaahlta gqrvwlvsaa pveigrviar rlgltgaigt
      181 vaeirdgayt grlagelmhg pakaeavgql asvegldlsr ctaysdsand ipmlsavgha
      241 aavnpdsalr aeartrgwei hdfrtgrraa riaipstvaa glligavtag ravhrrwrgr
//
LOCUS       WP_357535616             480 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357535616
VERSION     WP_357535616.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..480
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51298
     Region          3..341
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 msrrlvvldv vgltprllah mprlravaeq gfsaelgtvl pavtcsaqat lltgeqpsgh
       61 givgngwyfr dlgevllwrq hhalvggekv wqaarrvepg ytvanvcwwy amgadvdwtv
      121 tprpiyyadg rkepdcwtdp pelhdtltaa lgtfplftyw gpgaglpssr wicqaaeril
      181 adqapdltlv yvphldydlq rfgpsspraa aaaaeldavl aplldaaraa datvvalsey
      241 gitdvsrpvd vnrllraegl lrvytqdgme yldpwtsraf avadhqiahv yvkdpadvaa
      301 vaklcaglpg vaevldaegk aaagldhera gelvlvaepd swftyyywld darapdfarn
      361 veihrkpgyd paelffdpaa pgaakrragv alarkklgmr ylmsvvglda garavrgshg
      421 rlpadpadgp vllcsdpsla rdsfaatevk allldlaglg agadgastap tgppgtgdrr
//
LOCUS       WP_357535676             199 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357535676
VERSION     WP_357535676.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 199)
  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..199
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..199
                     /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=21020
     Region          8..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 mgtaappagg hrasppipvk iiiaggfgvg ktttvgaise idpltteaem tsagigvddp
       61 gsrsaktttt vamdfgcvti dhslklylfg tpgqarfgfm wddlvrgalg alvvvdssrl
      121 ddcypavdyf erarlpfvva vnafdgrvah dleqvrwala igrhvplltf dardrlsvrd
      181 allvvldral dravqegks
//
LOCUS       WP_357535764             310 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357535764
VERSION     WP_357535764.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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   6  (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   7  (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 10001941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     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=34539
     Region          <37..98
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          124..256
                     /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(125,127,129,138..140,142..143,148,156,163,165,167,
                     169,178,180..181,183,186,192,194..195,209..210,212,214,
                     224,226,228,230,236..243,245..247,250)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 myvrggreas tpclcfcplp afadptrrrl ldslrredgq tlgqlcaqla mtrqsvtqhi
       61 gvlqeanlvn avrrgrekwh ylnpvpihel pqrwiaafee prlrvldgir rqaeepqmnv
      121 trptfvyvty ihatpervwe altdadltgt ywghrnvsdw rpgsrwehqr tdgsgiadgg
      181 gtileatppt rlvmtfgnvd aeagpdastv tfliephrdi vrltvthvnl psdddfeavs
      241 agwpavmanl kslletgrvl pqapwempaa qqnghdgter tdstrptptl ppvtdepgqp
      301 rvrghrqstd
//
LOCUS       WP_357535778             536 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357535778
VERSION     WP_357535778.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..536
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..536
                     /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=55774
     Region          11..535
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mnerssaqlp sradvvvvga ghnglvsavl laragldvvv leaaqvvgga arterpfakv
       61 pglghstgsy llglmppeli telgveipvl rrdphyflpt pggagspyll fgsdraatre
      121 qmaaffspad iaaddamqae laalredlap awlaepsave etaqryvrpa lrqvfvdlvr
      181 gsvadylarf efrsellvam yavtdglsgl nagpddpgtg hnflvhnmcr lpgadgtwmi
      241 arggmgtvsr tfadaaraag aqiftgtpvr svtvdggaas gvvladgrtv sarvvlgacd
      301 pyrlidlvpd nalpaeltar maaarrpgst lkinlalsgl prfaclpdda pspfgstihl
      361 lpgsaslvgd gagespmaal ramwadvqag rlpeeptmew ylhttvdpsl qdpaghhssa
      421 lfvqsvpyel adgtwadalp syvdkllavc eryapgtgel vadmmpltpp gieehfgitg
      481 ghihhvdntv sftdrmpyat gldglyagsa gchpagsvig aaghnaakri ladlat
//
LOCUS       WP_357535851             459 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357535851
VERSION     WP_357535851.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=49292
     Region          39..455
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrptllpaqr lggrpddraa trsrsggggr avtralggtv rrtvlpsglr ilteaipttr
       61 svsfgvwvav gsrdetrpqc gvshflehll fkgthkrdal qisaeieavg getnayttke
      121 ytcyyarvld edlplaidvv vdavadsilt padvetergv ileeiamhdd epgdevhdll
      181 aravfgdhpl grlisgteet ispmtraqiq gfyrrrytap sivvaaagnl ehtevvrlvr
      241 aalrggpldt gpaapaprrs avrpvrtrra dtvvehkdte qahlvlgcag fgrlderrfa
      301 ldvlnnilgg gmssrlfqqi rekrglaysv ysyfsqyada gifgvyagca pgkvdevlel
      361 iraelaemaa hgvteaelar gkgmtrggyv lgledtgsrm sriakgellf gdlmtveell
      421 arveavttad vnavaadlls rpmslavvgp fddgdftta
//
LOCUS       WP_357535860             366 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357535860
VERSION     WP_357535860.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 366)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..366
                     /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=40127
     Region          9..349
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpdvsgtrak agrrpgsgir gneavagwlf vapvvvilgl flllpilmal wvsltgwngq
       61 gspfragvpf vgvdnytrlf aedglarrdf mtairnnlyy vaivvpvqtv lalflalvvn
      121 rrmlkgrsff rtafyfpsvt ssvaisvvfl flfansgavn gllallgidg pawfsdargv
      181 lhivfgvfgv dsapaalagg gpfgltwwdw lsgpsvamca iialvvwtts gtfmlmflaa
      241 lqnvpealee astldgagrw qrlwyvtlpm irptlflvlt lgligtwqvf dqiyvmsqgn
      301 pakttltpay lsyrtafrdf eygsgaaisf vlfliiivlt lvqrrvlrer dgdrprrfrr
      361 raerrs
//
LOCUS       WP_357535920             459 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357535920
VERSION     WP_357535920.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..459
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..459
                     /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=49715
     Region          13..400
                     /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 mtdgqnpfsr qervvvigag lsgslaavyl arrgyqvdvy errpdprtap aglggrsinl
       61 glsargmral devglltdvl krsvpmrgrv vhspdgavrf qpygvrehei lhsvlrdeli
      121 allvdaaets agvrfhfgwr ltrldrdtat vevlpeaggd pvevtadlvv gadgihsvvr
      181 qhlqrglrad ysqeflewgy keltipvgdd gdprvrleal hvwpgdsamm vahpnvdgsl
      241 tcslfmpheg pvsfatldtp eavlgffran fadaeelmpn lveeiaghpv ghlvtvrtap
      301 wrhgdrvvli gdaahavvpf ygqgmnsafe dclvldgcla rhpdraaala afeaarkpht
      361 dvladlsian fvdlrdrvhk paytahavad rllsrllpdr wtplytmvah tttpyadala
      421 rarrqdrilr gataaagala algavttiga alrrrsrgr
//
LOCUS       WP_357535890             185 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357535890
VERSION     WP_357535890.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 185)
  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..185
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..185
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19409
     Region          1..75
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvllrrvigd alrarrqgqh rtlrevstaa nvslgylsei ergqkeasse llasicdalg
       61 ahlsdllrev shtvalaeqm qgvlvpvqda pgadsaagre vrpagaarpa rtavgadara
      121 praaevrpta dagrlpvgea kvrqvtsdgk vsvsvrqegp lkatlrttrt vrsgkkhdld
      181 vvyaa
//
LOCUS       WP_357535992             503 aa            linear   BCT 28-DEC-2024
DEFINITION  deoxyguanosinetriphosphate triphosphohydrolase family protein
            [Micromonospora sp. NPDC048894].
ACCESSION   WP_357535992
VERSION     WP_357535992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..503
                     /product="deoxyguanosinetriphosphate triphosphohydrolase
                     family protein"
                     /calculated_mol_wt=54872
     Region          26..485
                     /region_name="Dgt"
                     /note="dGTP triphosphohydrolase [Nucleotide transport and
                     metabolism]; COG0232"
                     /db_xref="CDD:440002"
ORIGIN      
        1 meqpadprar rlfggsaral gdlaaspfra drdrivaspf farlggvtqv ispvgsgllv
       61 hnrlthslkv aqvaraiaer ltadptqrdl leklggcdpd vveaaalahd lghppfghlg
      121 ervldrlarq rlgladgfeg naqsyrivts teirgaattg ldltaavraa mlkypwtrld
      181 hpdphprhlr paprgaaapp ddpdsgsakf gaygteladl rqarapftgr iaqwqqtvea
      241 svmdtaddia yaihdvedfy rvgvlqqgtv aaelmawqre gghlravtdp alagaarrpg
      301 taiealrrql hrkdawiadd dafaaavehv reelvdglla lpfdgsieae qyvarfsvrw
      361 ttrlvdaitv tatpdvrsgh vqlapaqwhe vqvlkfvhhr fvlarpdlal hqrgqarlld
      421 tlvdalwqwl ldpeeesrlp rrlpdlvela eaelhprtpd rigrargrai vdfvaqltdg
      481 qavamldvls grsgalwtda fvl
//
LOCUS       WP_357536003             220 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357536003
VERSION     WP_357536003.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 220)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..220
                     /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=23936
     Region          8..190
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 msdhaflatt rdsydsmavd yaewlrsdld erpldralla ifaervratg nlsvadvgcg
       61 pgrvtilldr lgldasgidl spgmialarr typglrfevg smlaldlpda slggllayys
      121 iihvpwelrp aifaefrrvl apggqlmlaf qvgddrshht eafgrpvdla fhrqrpeeva
      181 dllrdagfep wattvkereg tektpqglvi ahkrgagspg
//
LOCUS       WP_357536034             411 aa            linear   BCT 28-DEC-2024
DEFINITION  YeiH family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357536034
VERSION     WP_357536034.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..411
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..411
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42611
     Region          64..406
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 mtadatrpaa pdatrpadpd attpttapet tapettapet glpttpktgp gvrdgafwaw
       61 tagglvvvfa laaltryleq gvpewfagts vedlaaavey pvyaillgll gnvvvtvtgi
      121 rdriaaafrt effiktglvl lgasinlsvi asaagpaiaq aillisavfl ftwwlagrfg
      181 lddrlralla savsicgvsa aiaaagavra rreqlaytas lvilfalpsi filpwladvf
      241 glspavagaw iggnidttaa vtaagalage etlqiasivk vtqnalmgvv avaltayfay
      301 kvdrtagsar pgagelwrrf pkfvlgfiaa sviatiylqn agsdgravig vvndlrtwfl
      361 ilafvsigle frvsslreag wrpiavfasa tvfnlvvala lasllfrdfa g
//
LOCUS       WP_357536040             402 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357536040
VERSION     WP_357536040.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (residues 1 to 402)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 402)
  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..402
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=42340
     Region          166..399
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrsltgwwrg rgqperfdly trlsmysvvc feplvvlavl spvrdagril pilvlsvaht
       61 avclllnrag ldnylgrrpp pvglavagga ltlagtglal lllptldesp aktaaflvfa
      121 gyfyaalsta vpprvsllal lagvpctfvv gradglasqr avgitialva vfvagyvsfr
      181 lsawmlgvvw qldqsrqvqa rlavaeerlr fardlhdvlg rnlsvvalks elaakfaerg
      241 raeavtemle vrriaqeslt evrevvrgyr spdlvaelag arsvlsaagv dcqvlvdgtg
      301 lppdaqatlg wvvregttnv lrhtdanecv islrtdgrkt gtvtltmdnd gvpagrtaef
      361 gsglqglaer laavggtmsa gpaapgrfrl tarlplgaav ap
//
LOCUS       WP_357536088             572 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357536088
VERSION     WP_357536088.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 572)
  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 572)
  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 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..572
                     /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=62020
     Region          14..547
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mvsqpvstqs fpalrswqrk alveylrrrs pdfmavatpg agkttfalri aaeliadgtv
       61 eavtvvapte hlksqwaqaa arvgiqldas frnadvhssr dfhgavvtya qvgiapqvhr
      121 rrtmtrrtmv ildevhhagd srswgdgvka afepavrrlm ltgtpfrsdd npipfvtyer
      181 ggdglqrsra dsvygyadal rdgvvrpvif laysgetrwr tsagdelaar lgepmtqdli
      241 aqawrtaldp agdwmpqvlr aadarlqvlr eggmadaggl viasdqqsar ayarlierlt
      301 gqkavvvlsd dvgasariaa faasedrwlv avrmvsegvd iprlavgvya tsastplffa
      361 qaigrfvrar lpgetasvfv psvphllgla semeaerdhi lggpkkegfd delleraqrd
      421 ekaggelekr fealsatael dqvifdgasf gtgaqagtpe eedylglpgl ltadqvalll
      481 nkrqaeqlaa qrrrkadpap eprepvvapp taaerrirlr rqlnalvaar hhrtglphgk
      541 ihaelrrlcg gppsaqatie qleeriatmq sl
//
LOCUS       WP_357536119             408 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Polymorphospora].
ACCESSION   WP_357536119
VERSION     WP_357536119.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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..408
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..408
                     /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=42955
     Region          26..387
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtvyltgrrs rlrptlrlrl tllngvllvg agavlmvlaw llvddalhpa dqllpgttvv
       61 ladgqtldar vwqehvvdav sgellakglv allaisivgv agayvvagra lrplhqvtat
      121 aqrlreetle erirytgadd evaelaatfd amldrigeaf eaqkrfvana shelrtplav
      181 mrteidvtla ddeadvaefr rmatvvrdas eranglvdal lvlarseaqs grrlsrkvpt
      241 dlacgvsaal satsaeaqrl klrvtatlgp aqvvgdpsll erlagnlven avrynhlhge
      301 lwvrtgsadg hvylvvgntg fevdpadvpg lfepfrrggr ertgargsgl glsivravcd
      361 ahrgtvgava qpggglevtv tlpaadttpv vtasavvspp ttspadpv
//
LOCUS       WP_357536120             363 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PseG/SpsG family protein [unclassified
            Micromonospora].
ACCESSION   WP_357536120
VERSION     WP_357536120.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..363
                     /product="PseG/SpsG family protein"
                     /calculated_mol_wt=36978
     Region          5..351
                     /region_name="SpsG"
                     /note="Spore coat polysaccharide biosynthesis protein
                     SpsG, predicted glycosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG3980"
                     /db_xref="CDD:443179"
ORIGIN      
        1 mkppriglrc dagprtgvgh lvrclalgee flargarvel fgtvervgwa adrltargip
       61 vhpgpgtpag lveaarahal dalvldsyel dpagagalra agvvtlaivd gdtrgqdadl
      121 yldqnfgadt agthgtggtg tgggrllagv ryallrdavt avrppapppa tptdrprvla
      181 ffggtdavga apvlarvllg tghpmeltvv vgrpeieael trvatgrgqs lhllaptdtl
      241 paligaadlv vsaagtstwe lcclgapaal vcvvdnqrda yrrvvahrla aglgelpdlv
      301 apglagraar adagrtlral laspqrraal aarawatvdg rgrarvadav ltriadrtgv
      361 lnp
//
LOCUS       WP_357536152             306 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357536152
VERSION     WP_357536152.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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..306
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..306
                     /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=32491
     Region          40..284
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mdgtgpavsr vlrppagyhl agsvgalamg hhdpcarfvd gtfwwtartp dgpgtlalrr
       61 sgtelvaegf gpgadrvvdr adavaglrdd ltgfaevaat hpvverlara hrglrlpatg
      121 qvfprllrav leqkvtgkea yrayaatvrr fgtpapgpva nlwippepaa iaaqpywvfh
      181 pfgveqrrad tlrraaaaad rlercadpae atarltaipg igpwtaaevv riaygdadav
      241 svgdyhipnt vawalagepr gddarmlall aqftghrgrv calldaaglh aprfgprmpl
      301 rsfary
//
LOCUS       WP_357536174             101 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357536174
VERSION     WP_357536174.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=10970
     Region          2..82
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mevldvlgdp vrrriveals sgsltsgaia arfeisrpai sqhlrallaa gvvtvrpegt
       61 rrvytlnpda ldtatdwleq qrvrwnrgld alehaldtgq i
//
LOCUS       WP_357536157             281 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357536157
VERSION     WP_357536157.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 281)
  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 281)
  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..281
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..281
                     /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=29761
     Region          32..226
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mgrkrggqrl gvridsglae lapdpdrpas ftllvdgtpq shvdlddpth lefeyvrria
       61 mvvdlmapag rplrvlhlgg galtlpryvs rtrpgstqrv veidaalvdl vrehlpwppd
      121 rnlrvrvgda rdavttgrdg sydlviadvf agartparlt svefagevar vlapgglyva
      181 nladggalky argqvatvga vlphaclvad tavlrgrryg nlvlvagrve ppvagltrra
      241 agdwfpgrvv hgdelerftg gaavvldata rpsdpppvgf f
//
LOCUS       WP_357536186             435 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357536186
VERSION     WP_357536186.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 435)
  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 435)
  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 435)
  AUTHORS   ter Beek,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..435
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..435
                     /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=45786
     Region          24..369
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mivtprrrri aaaalasvav faatacgsds dsadpnepit livdvfgdqg fgyealyeqy
       61 qadnpnikiq ergkglglgd yntrltqqit agagagdvva ieegtivqfy aqadkfvnla
      121 dhgandlkan flpwkweqgs tpdgkvlglg tdvgsmaicy rtdlfqaagl ptdreevakl
      181 wptwdefiat gtkfaaadkk nkfvdaatnf fnvvlsqvag agtgytyydk snnlvlesnp
      241 dvrtsfnltt kmiqaglsnn lqsfsnewna gfknatfati acpawmtgvi kgqagdaaag
      301 kwdiakapgn ggnwggsflg vpksskhqke avelakflss akgqveafkk vgnlpsspqa
      361 ltdaavasat ndyfnnaptg tifaagatel kpvylgpknq avrtavenal raveqgqapd
      421 aawqdavkng aaagk
//
LOCUS       WP_357536274             228 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357536274
VERSION     WP_357536274.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 228)
  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 228)
  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..228
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..228
                     /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=24165
     Region          10..196
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mpptpdkpli aedlllllfd pasgsiageg tlfyvlggal ltelaldrqi didertglrg
       61 rlvhvvgstv ptdpllrsar dhvaqkprdv qailaaigpr lrapvldrlv rgghvrrerr
      121 kvlglftrta lrdggtphrp ellarvravl vdgaapdprt aaicalisas gtlptfhrdi
      181 pwstpvitra kelergdwga eaaaaavart maatvanalv aanvlpkn
//
LOCUS       WP_357536351             713 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC048894].
ACCESSION   WP_357536351
VERSION     WP_357536351.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   3  (residues 1 to 713)
  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 12993645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..713
                     /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=73935
     Region          28..288
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(28,52..53,86,91,96..99,111)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(35..36,38..41,43,56,58,94,110..113,117,119,156,158,
                     160..161,163,173..174,177,194..197)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(35..36,38..41,43,56,58,94,110..113,117,158,160..161,
                     163,173..174)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(39,117,119,156,158,160,177,194..197)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(173..181,190..197)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <360..575
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mtqiptwsgg pvsppngraa pgtiiggrye lrssvgnggm gtvwratdtl lrrdvavkev
       61 vlppglapsd rdamyertlr earaaaaiqh pavvqvydvv teggrpwivm elldarslad
      121 mviedgpvag ravakigial lgalevahan gvlhrdvkpa nvlictdgrc vltdfgvarm
      181 ptdvqlttpg mvlgsphfis peramgqdfg ppsdlfslgv tlytavegrp pfdkgdpiet
      241 mhavvedppa tpqrsgpltr vlmgllekdp arrldvhtar amlrellagp ltstatavns
      301 itdpysvvpv qrpsgppavt appaeskpsg qiggramlaa gesltdrlak lrrgerpepv
      361 atsaaalddt sadafagplh tptdampasg gptvdplptr ptagtygrpe atqritpsaa
      421 peatqriggg ttdatqrigg gpeparagyg taeptqaiyg gggnseqtqa vyggqwsipg
      481 tgqswtsppa ppggadggal grakgaggrl vgtvkgwprk lqlaaaggla vvlligaval
      541 fsggdpestp ppqagpsapa agggelppmq ehsargirvn vpkgwqratg gvyidyvdpq
      601 dkgrkvrilt ekfggsssrw vevaadglrk rtsscarpye qlamgeknla gksaaefeyt
      661 cgdggdkrhg vwrgvvhegk vysfyltand akfaeskpif demvksfqlt gss
//
LOCUS       WP_357536341             260 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357536341
VERSION     WP_357536341.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26386
     Region          3..258
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msdglagkva vvtgagsgig lavarslaga gcrvvmadld psacvdvgpa gsgvpvavdl
       61 gtpdgvatvv etattrfggv dvlvnnvala pyrdtftaid daawqrswdv nvmscvrlcr
      121 aviplmaarg ggsvvnigse aarhpkpylv dyavtkaall glakalsiey gsrgvrvntv
      181 apgptrtstm dsfltalagk leidvdaaad rfvnqmrglp lgrmnepedv aevvlflagd
      241 rsrqvtgsey pvnaggtasv
//
LOCUS       WP_357536395             286 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357536395
VERSION     WP_357536395.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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 286)
  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 286)
  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 286)
  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..286
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..286
                     /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=29520
     Region          7..280
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtsaprrvlv tgaagrlgra vldllaardv pataldlrdp gdlpadrvvv ggagdpvavr
       61 aaladvdavv hcaalaaptm gspeevfagn aratfvtlee saragvrraa iassiavlgl
      121 sfaprplspa ylpvdeavpa qvadpyalsk qadeataamm srrygmtvva lrfpllggpr
      181 dtlpeiaary vddpgfgaah lwgyldtrda atvvwlavtr pitgchvlfv aapdtlapqp
      241 tgellgrfyp gvprrlplpg raapidvgaa arvlgftaeh ryplgs
//
LOCUS       WP_357536377             313 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048894].
ACCESSION   WP_357536377
VERSION     WP_357536377.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 313)
  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 313)
  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 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   5  (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
REFERENCE   6  (residues 1 to 313)
  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 313)
  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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..313
                     /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=32124
     Region          48..250
                     /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"
ORIGIN      
        1 magsaagsps ggaaargaap dgtatgafgp ggaavgyrpg atlpfgaefr rqasrrrtql
       61 algfmvllpl iilvafqfes gdddgsgrge fssladlats gglnftlfsi lvsasfllvv
      121 vvalfcgdtv aseaswgslr yllavpvpra rlltvkllva laysglalll lagtallagt
      181 lrygwsplts qvaaeltpte glvrllavlg ylavvllvva glafllsvit daalgavgga
      241 vllwilssil dqitalgalr dflpthyssa wlgllstpmq tddvvrgais aisyatlfwg
      301 lafwrftrkd vts
//
LOCUS       WP_357536449             353 aa            linear   BCT 28-DEC-2024
DEFINITION  type III polyketide synthase [Micromonospora sp. NPDC048894].
ACCESSION   WP_357536449
VERSION     WP_357536449.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..353
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37235
     Region          4..352
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mavpliaglg aahppgarqd elwagyfaeh fsgptralae rifansgvsh rqaavnplle
       61 dvsdwptdrr mrryqvealp lgkeaigral taaglaagdl glfvvcsctg yatpgldill
      121 ardlgmaaet qrmfvghmgc yaalpglgaa gdfvtargrp alllcaelts lhiqpasarm
      181 dtqqivshal fsdaavatvl vpgtettdrg yalrevasvt dtstadhmtw dvtdtgfrmg
      241 lspkvpqvls ahvrglvdgl ltrhgttiae vdgwavhpgg prilnvvere lalpadalaa
      301 sravldehgn cssptvllil drllravvpp rwvvllafgp gltlyaalle rrp
//
LOCUS       WP_357536511             500 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357536511
VERSION     WP_357536511.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 500)
  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 500)
  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..500
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..500
                     /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=51540
     Region          3..373
                     /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 mserddrvaw alpargvpad qvldeiralr sadrpthggr lfayvydpav pglddlamsa
       61 yalsahvngl dptafpslla menilvgaaa svlgggpgta apdvvgsvtg ggteslilav
      121 kaardarpev atprlvipvs ahaafakaah ylgvaldlvp vsattlrpdp advaaaigpd
      181 tvlvacsaps yahgvvdpvt eiaavaaaag vrchvdacfg gwtlpylrrl gvdgpafdfs
      241 vpgvtsisvd lhkyaycpkg vsvllhrdaa lrapqyfafa dwpgytminp visstrsggp
      301 iaaayatlrh igddgylala grtldavrgl aaavtkvdgl rlmaepestv vaftsddpal
      361 dlfvladelt vrgwhtqpqm aygdlpasih ltvtaavapr vaefgpalea aataardhgp
      421 vrlpdevaal lgalapeqlt selveglagg lglgfgdpqa gaalpdrsav vntvlnvapp
      481 rmrerllief vgllqrptyr
//
LOCUS       WP_357536613             297 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357536613
VERSION     WP_357536613.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 297)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..297
                     /product="phosphotransferase 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=31309
     Region          11..226
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mlnrdlenia rtalaahlpg thlgrleplg egednvayev dgelilrvrk eadpapater
       61 earllatvad lsplpvptpl faapelgcla yrkvpgvpll dlpdrlayaa pvaaaigrll
      121 galhavpver maevaepdhq plpdwlaeav enhaalagrl paehgaaiga flaapppdgg
      181 yvpvfshndl gvehvlvdpa trtvtgvvdw sdaaivdpay dfglllrdlg paaletalda
      241 agrtgpdrdg lrnralfyar cgvfedlvyg feapdrsayv dkslaalhwl fpapggd
//
LOCUS       WP_357536650             355 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357536650
VERSION     WP_357536650.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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 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   4  (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
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..355
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..355
                     /product="helix-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=37567
     Region          16..319
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpttsarlla llsllqtrrd wsgtvlaerl gislrtvrrd vdrlrelgyp vaaakgpdgg
       61 yrldagtelp pllfddeqav altvalqvaa tgaddalada aaralqtvrq vlptrlrqrv
      121 galsvtavar pattptppvd ggvllalsaa vqtreilrfd ygpdsterpa rhaephhvvt
      181 wggrwylvaw dldragwrtf ridritpcpp hgprftprpl pggnvatylt gvfrgsaggs
      241 adwpcrgtvl ldlpaatvar ytrdglveev tpdrcrltlg swswvslaaa varydaeitv
      301 vgpppltdaf allagrftrt atggvaagks agsaagtrsg qqgergegvv ppqqp
//
LOCUS       WP_357536632             539 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357536632
VERSION     WP_357536632.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 539)
  AUTHORS   ter Beek,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 539)
  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 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..539
                     /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=56557
     Region          3..502
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mtiqftdvtv tyadapapal ravtlsieeg elclvagrtg agkstllrav nglvphftgg
       61 rlagrvtvag ldtrehppre fahlvgvvgq dplagfttdt veeelaygme qlavpppvmr
      121 krveetldll giaelrnrpl rtlsggqqqr vaigavltaq prvlvldept saldptaaed
      181 vlaaitrlvh dlgvtvvvae hrlervvqya drmlylpgdg tvvsgtpadv latadvappv
      241 velgrlagwq plplsvrdar rrapalrerl rdrplpprtt aagpvaltar rvvvrygevy
      301 avrgvdldlr ageitalmgr ngsgkssllw avqgsgprqg grvdvggtdp kqlsagkarr
      361 lvglvpqtpa dllyldtvda ecaqadqesg spagtcrall drlvpglpga shprdlsegq
      421 rlalvlavql vaappvvlld eptrgldypa krhfaavvre laeagravvf athdvefvaa
      481 aadrvvvmae geivadgptp dvvvaspafa pqvakvldpl pwltvaqvaa slagqdvpa
//
LOCUS       WP_357536662             355 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357536662
VERSION     WP_357536662.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..355
                     /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=35670
     Region          12..352
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mafletstaa grttfrlarp avsgvlalrp iavgtllaav tfaafcvsva dgriqipltd
       61 vvpalfghgd pgtllvvrel rlpraltgll vgaafglsga vfqamtgnpl aspdmigvia
      121 gaqtavvagi vlglgaglgt qtlgvvgali aalvvyllaw grgttgyrlv lvgvgvawmc
      181 tsatdylvar ampyearaav gwlvgslner gwhhvrplal amavlvpavl llgrwlgtlh
      241 lgdpvatalg tpvgyarial lvtgvglaaf gtaaagpilf valvspqiaq rlagratppp
      301 lisavtgali vlagdlvsri vladarlpig vvtgvlgapv llwllvranr tgsgg
//
LOCUS       WP_357536670             261 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Micromonospora].
ACCESSION   WP_357536670
VERSION     WP_357536670.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..261
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28760
     Region          3..255
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 malmrcefds ealgmntsmt vilpqpdpar ptptgpadag ppvlyllhgl sdddtawtrh
       61 tsieryvapl glavvmpqvg rsfytdethg nrywtfltee lpevcrsffr lsdrredtfv
      121 aglsmggyga vkwalrqper faaaaslsga lnvahrrysp drpldpdvwh tvwgdaptag
      181 pdddtvalvg ragpdtpply vacgtedfly ddnerfvaaa rdrgvpvtvd fspgdhdwpy
      241 wdatirdvla wlplrtrppv s
//
LOCUS       WP_357536692             479 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357536692
VERSION     WP_357536692.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..479
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..479
                     /product="ATP-binding protein"
                     /calculated_mol_wt=52448
     Region          8..338
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
     Region          326..418
                     /region_name="DUF4143"
                     /note="Domain of unknown function (DUF4143); cl24018"
                     /db_xref="CDD:474127"
ORIGIN      
        1 mgdiltafvg rdaelallst elgrvlpgtd rpgrcllirg rrrvgksrlv ekfvedtava
       61 dffftaagss pgeeirrfca daaestlpdr ellatanprd wdaafrllat tlpdeapsvv
      121 videvpylmd servfegllq rawdrqlsrk pvlliligsd lsmmealndy rrpfhqrgre
      181 mvvgplnpad lavmmnlpaa eaidaalvtg glplictewp pgtdlwdfla aatadptsal
      241 ivsaerslaa efpsqvqart vlsaigsger tfgniarasg elaatslqrs lsaltdkrlv
      301 vgelplstap skerryritd pylrfwlrfi apnmpeierg rgdltlerir rgwtswrgra
      361 veplirdala rilpdgqlpv agtiggywtr tndveidivg adrgpvarel lfvgsikwld
      421 rdtfdvrdlt alqrqrdrlt seplplvavs rggvscpgvd asygpeqlia awrptgsar
//
LOCUS       WP_357536702             468 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [unclassified
            Micromonospora].
ACCESSION   WP_357536702
VERSION     WP_357536702.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 468)
  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..468
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..468
                     /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=47502
     Region          13..262
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,37..38,67,72,77..80,97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,75,96..99,103,105,142,144,
                     146..147,149,159..160,163,180..183)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,75,96..99,103,144,146..147,
                     149,159..160)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,103,105,142,144,146,163,180..183)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(159..167,176..183)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgvlssevvl sgryrlderv atggmgdvwr atdlvlgrqv avkvllpalv sdpdfiarfr
       61 searimaalr npgivqvfdc gedrladgtr adylvmefve geplsrries aghldvtetm
      121 svvaqvaqal haahaggivh rdvkpsnllv qedgtvvlvd fgvarstnvt sitstnavpg
      181 talymapeqa sgrpvsaatd iyalgavahc cltgqppftg dnplqvavrh lddeppelpa
      241 dipapvralv aralekdpad rfatgaemaa aaraasgdgt atamtalvtp plrdpsgant
      301 prlvgaqtpr tvvgagsgrt rrgslvgala avlvaltalg aalgaaksld ngvpnirstg
      361 pavapteqse lpavveqtgp qeterpnrpg nqtakpspsa svsptplpng ssqslptksa
      421 patpvetttp agttpapttp agptppettp ptpdaggggg dgmppadn
//
LOCUS       WP_357536759             997 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357536759
VERSION     WP_357536759.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 997)
  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 997)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 997)
  AUTHORS   Rosinski,J.A. 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 997)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..997
                     /product="helix-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=105984
     Region          <7..916
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <937..995
                     /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 masevdsapl vgradqlatl raalhddigp gqtaavfvtg esgvgktrll teaaarlrda
       61 gavvltgscl digdasplhp vlqalrrfda dltaaqarts savrgllrtf aedssgadsa
      121 gallervsrg lsliaegrpl vlvlddlqwv drttrqllly llaglgdlql svlaavraes
      181 lqgahplrrv ltelrrlrsv rvldlapldr adtdrlagei vgtplapeaa dqvwqrsggn
      241 pfvveelard lrdgrdglsd tlreiflsrv dvlprqahaa vhavaagvep vehwllaevl
      301 glpepeliea lreavahrll vgaddgyrlr hrlvaevlah ellpaeragl hrryaealtq
      361 apaelhqarl ahhwrlagep aralpaamaa areaqrlhgf aeahrhwsaa lqlaatptsg
      421 pggvppevdr avllehaaet ahqsgehara lsllaelagg epldpscgvr irrarylaaa
      481 grsapaeaey rgvlesvact ageraaaaaq lahllvlqgr yadagqrare alelaatvdg
      541 stnsvvlasa algfseafle dpdsglavvr raletaersg gpedvacayl hlaelltgpl
      601 nileegvvva rrgaervael glgrtyetrl laiatnglfr vgqwaeaekv vaaalrhrps
      661 gadavellla rcrlsvgygd veasdrdlea vatmlaggga prhvlpmlil raglamwqgr
      721 hdvarqavqr gmtesrsddv vllgtlawhg lraeaeahas rtvavdptav rrlrdavdrv
      781 taksataagp vrvvadgfla lctaeltrld grgdpdawar saaewdkrnh pypaaysrlr
      841 qaeallarrg rssaagtllr qahemalslg avpltseirt lagrarvelt draqptgvdr
      901 rqgrprstgv ghrrpagsgs gsvtvvagpv vdelttltar erevlaavae gltnkeigqr
      961 lfisertigv hvshifdklq vrtrvqasai hlrnrge
//
LOCUS       WP_357536796             178 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NuoI/complex I 23 kDa subunit family protein
            [Polymorphospora].
ACCESSION   WP_357536796
VERSION     WP_357536796.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 178)
  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 178)
  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 178)
  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..178
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..178
                     /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=19522
     Region          1..133
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
     Region          126..>169
                     /region_name="PHA03201"
                     /note="uracil DNA glycosylase; Provisional"
                     /db_xref="CDD:165468"
ORIGIN      
        1 mtrragtqqy pdvepdlppr srgviallee nctvcmlcar ecpdwciyid shkeevvvpg
       61 aararqrnvl drfdidfslc mycgicvevc pfdalywspe feyaeydird llhdkdhlge
      121 wmatvppppa hdpngepske eataarkaag gpapgraagg patprvrpqr ptgtadps
//
LOCUS       WP_357536822             441 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357536822
VERSION     WP_357536822.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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 441)
  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..441
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..441
                     /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=49211
     Region          5..380
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 msrtvkrafk yrfypsteqa aelartfgcv rlvynmalra rteawtlrqe ranynatsal
       61 ltgwkkteel aflnevscvp lqqalrhlqt aftnfwakra gypsfksrkr srrsaeytts
      121 afrfrdgqlr lakmsapldi vwsrplpaga spstvtvsqd aagrwfvsll cedviepgsa
      181 pgmgsvgida gldslltlst gekivnprhe rvdrqrlara qrnlarkekg sanrakarlk
      241 varvharigd rrrdhlhkls trlvrenqtl viedltvrnm vqnrslarai sdagwrqfrt
      301 mleykadwyg rnlvvvdrwf pssklcstcg aladrmplnt rswtcrcgtv hdrdlnaarn
      361 ilaeglsvaa cgagvrpqre ssrtgrsavk qetpgatqgi pflqrgedvn ctmftmtmat
      421 sasprsasss emrrpagapa r
//
LOCUS       WP_357536901             289 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357536901
VERSION     WP_357536901.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=30621
     Region          14..281
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtersegstv giprsilytp alsldrvvka wnydadvhli dledsvppae kpaartvcrd
       61 alekapkpan iavrmnelrg vaavqdlvml tesrvrpgiv mmtmvtdaae ievvrrilas
      121 adahpeiyvt vetveavvdi dpiaraadgl vlgsadlaat lgveitweam laarqamala
      181 carygiacid tanfrltepa vlaeetarir tlgfhgkatv hpselavinq alrpnpddlr
      241 larrvtqavg aagggiavld gnmvgppfar mardtvargd awtarfgag
//
LOCUS       WP_357536945             396 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FAD-dependent oxidoreductase [unclassified
            Micromonospora].
ACCESSION   WP_357536945
VERSION     WP_357536945.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..396
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..396
                     /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=41400
     Region          1..372
                     /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 mrsavvvgag lgglsvagal arsgwqvtll eradrvrpep tavvlwpngv ralrvlglga
       61 gldaiatplp dggirrpdgh wlaqprptpa drmpvvvhre dlhdaliagl gdrvelrtgv
      121 vvdsvranpd erpgvglngq fveadlvvaa dgtdsvlrrq lapeasvvss gcaawravip
      181 wyrvpvpadq pvggevlgag yrfvaaslge rgssgasrrg gvywvataag aprpespqtq
      241 lallkrwyag wpapigdlla atepadlvqq evrelrplpr aygfpagpgg vvllgdaaha
      301 mpphlgqgac lafedaatls sllresrlpd avlaydrlrr praatvvrqt rrmsavlqtr
      361 grlalrarda algtisprll sgaaaaaaaw rppptp
//
LOCUS       WP_357536977             786 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Micromonospora sp. NPDC048894].
ACCESSION   WP_357536977
VERSION     WP_357536977.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 786)
  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 786)
  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 786)
  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 786)
  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..786
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..786
                     /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=82980
     Region          2..>117
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Region          219..772
                     /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 mpprsdeprr datgsrrgsv rggtarggep rppeprtpep rtpqsrtgep paagpragep
       61 rgqgragdar tgqpragdgg gisdaraytp rgrtiressd erggqrrtpr agrsgdpfrp
      121 alqvldggra aanragrrea aptgrtgvir tvpataapdd defadppapr rrpgrttprr
      181 tdapgrgapr rteaprrtdr pagrrpvrkp rrppklaepr rrlrlgtalv lavfavigir
      241 lvvlqavdtp ayagggvgnr lsrvelpapr gsiedrngap larsvearyv fvdptlvkdr
      301 tetakllspl lgipvselae kmkrqgglqf rylargvdia qakqiealel agigthrder
      361 revpggdlaa nlvgftspdm dglegleary ddvlrgqdgr wvyeagagdl dapipggysq
      421 ttaprpgssl vlttdrdlqf qvqqilsrqm aqtrgaigaa vvldvktgev laqasnptyn
      481 aaspdqsrpt dredaatsfv vdpgsvhkai tygaalqegv itpdsawpva ntitrggvtf
      541 rdthpaegkk lsvagmlays snvgtieigd rlgpdrlidy qkrfglgqpt gegmpgeasg
      601 rllpadqwsg ssygsvpigh svdatplqma aayatiandg tyvqphlike vvgadgkrtp
      661 aaapvtrsvl spsnaaalrt lleavttvdg atglaaavpg yriagktgtg lryvngkqqp
      721 gevgsfigma paeapryvva vfvwnpeggg gavvapafre mmgftlrhyr vppsrgkspn
      781 fevfpr
//
LOCUS       WP_357536983             212 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Micromonospora].
ACCESSION   WP_357536983
VERSION     WP_357536983.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..212
                     /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=22527
     Region          16..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 mdapgdgldr lrlvptpfvp evrlhlaeda ivwwarmeaa agralpppfw asawaggqal
       61 arhlldhpdl vagrrvldla agsglvaiaa alggatqvva ndvdpyavaa vtvnaranrv
      121 rvqarsgdll dddgtqaell vagdvlydre laervlpylr raaqggtqvl vgdpdrghlp
      181 wdvlevvasy pvpttepsvd spvrrvqvlr pr
//
LOCUS       WP_357536988             521 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357536988
VERSION     WP_357536988.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=55652
     Region          6..513
                     /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(171,174..179,181..182)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(174,289..290,311..316,398,410,413,424,506)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(174,215..216,263,265..266,269,289..290,311..316,398,
                     410,413,421..424,487)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(215,265..266,269,289,421..423,481,487)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mtslslatvl aesarrhpak vavvdgdtrv tyarlwhear tyaaglrelg vrpgdtvall
       61 apnvvdfpra yygalaagav vvpvhlllta deaayvlrds radllvchas qlamgaaaae
      121 ragiplvtvg avapvpaqrp appvrrledl caglepvlsy vsrgaedpav ilytsgttge
      181 pkgavlthln lvmnamvnvf dandarptdv vlgclplfht fgqtvamngt friggtlvll
      241 arftgpaald lmvrervdvf hgvptmyial leaaagrdel prprlcvsgg aslpvavler
      301 fntafgttif egyglsetap tattnqphfg tragtvghpi wgveveiarp evpdrvellg
      361 vgelgeivir ghnvfagylg rpeataeavv dgwfrtgdlg trdadgfvti vdrtkdvvir
      421 ggfnvyprev eevlarhpav aqvavigvpd pvhgeeicav vvpdpaadpp pdgeeliawa
      481 rerlgrhkyp rrirflerlp lgpshkvlkr qlrrtfaaeh r
//
LOCUS       WP_357537107             366 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC048894].
ACCESSION   WP_357537107
VERSION     WP_357537107.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 366)
  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 366)
  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 366)
  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 366)
  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 366)
  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..366
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..366
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39659
     Region          63..>306
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msswlvfrgs gephngiddl ppppnwrrfd ggppmpvpgn sadptigrrl grrrpalagh
       61 tnpnavhmvn aalylrrpll vtgkpgvgks alayevahel glgpvltwpi ssrstlaegl
      121 yqydpigrlr eenlrqlreg qprtdsvaad aspptggvsr pdlngtdade asigryltlg
      181 plgtallpyd rprvllidei dksdidlpnd llnvfeegey vipelrrltk taprvnvlta
      241 dedvsatvsa grvrcrafpf vvltsngere fphaflrrcl rltltepepd qiaamveahl
      301 gadvaakare mieafvtnrn gtgvyatdqi lsaiylrfsr sdtdsdaamm qtvravlsdl
      361 smsgpg
//
LOCUS       WP_357537119             332 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC048894].
ACCESSION   WP_357537119
VERSION     WP_357537119.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     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=35504
     Region          20..309
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mndtpaplsq pevqgfaala arlaenvnav vlgkpevvrl altalfaqgh vlledvpgvg
       61 kttlaravaa tvqgqwrriq ftpdllpsdv sgvtifnqat rgfefhpgpv faniviadei
      121 nraspktqsa llevmeertv tvdgvrhpvp qpflvvatqn pvemdgtyrl peaqldrflv
      181 klsvgypdea vevevlrgat vrspdslqpv tdtatvgemv rmarrvhiae plygyavrla
      241 tatrqhpqvr vgvsprgvia ltraacayal idgrgwimpe dlkalvepvf ahrllltada
      301 qvrgvtaadv lrqavasvpv plpsgqstpt hg
//
LOCUS       WP_357537233             346 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357537233
VERSION     WP_357537233.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     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=34894
     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 mtgattsgpd vallrrpart rltwllvvla altlaliasv afgsrivgwa ditaalggth
       61 dtldqaavvk rlprtvlaal vgaalalsga vmqgvtrnpl adpgilgvnm gamlaiavam
      121 ttvglytatm yiwvaiagaa vsalfvyavg slgrggatpl kialagaats aalaslvvav
      181 vlprgdiaen fqswqvggvg ganwdsigqv lpfllaglas cllcaralns lalgdelaag
      241 lgervalvrg iaaagavvlc gaatavagpi afvglivphl crllvgldhr wllpfatlvg
      301 avlltvadva grvvnrpdei eagiitalig apffiyivrr qkvrel
//
LOCUS       WP_357537240             118 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357537240
VERSION     WP_357537240.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=12883
     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 myardnaata ndghqeptea qfeaaatafr mladptrlrl mwllrkgehd vatltaalgv
       61 arpavsqhla klrlaglvas rrdgrrvlyr trgghvravi aealfqadhq lanhpdhd
//
LOCUS       WP_357537258             298 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357537258
VERSION     WP_357537258.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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..298
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..298
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=30227
     Region          <4..>43
                     /region_name="PRK15313"
                     /note="intestinal colonization autotransporter adhesin
                     MisL"
                     /db_xref="CDD:237940"
     Region          90..289
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 magdpvlaap aapvpgnadp vrpvpgnadp alpvpgaadp vgpvlveqrg evrwlrlnrp
       61 rrrnaidpal lsaldtavaa aaadpdtavv vlagtgpsfc agadlrhlrs vaatgadpld
      121 flgrvsasld riervgkpvv aavhghvvag glelalvcdv vvaregtlig dghvrngllp
      181 aagssvrlpr rvgeplarwl altgellpae vftasgfvha vapadrfdel vaatagrlar
      241 aagpaqtgfk nllydvrdpp agpalaaeld afgahwaatd mtaaldrflg tatgegrr
//
LOCUS       WP_357537282             272 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified
            Micromonospora].
ACCESSION   WP_357537282
VERSION     WP_357537282.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 272)
  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..272
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..272
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28017
     Region          1..268
                     /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 mttprtvtvd gspvhvfdsg vgpavlmlhg sgpgttgsga waataqalgp swrvlapdqa
       61 gfggtpvpag srgglrlwtr qaaglmdalg iehyavvghs mggavalala aayprqvtrv
      121 vavstmgapg aplsadldal waaptgpvga rdmlsrlfld qtlvtdaava aradamraga
      181 aayaalfppp rarwvddltl gartlaaira pvllvhgadd rvtplatatr plldhltdvr
      241 lhvfdrcghv paiehphefr hllscflnpd rt
//
LOCUS       WP_357537424             270 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357537424
VERSION     WP_357537424.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 270)
  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..270
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..270
                     /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=29318
     Region          20..238
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mapgphrgpd agvrlkrdrr ppkasvmlaa dirahilgha lpagsvlpse aqlvsdsglg
       61 ratvrealrl leaegliaik rgpqggvtvq rpdlsrlsrs lapfltlsea plrdlfvfrk
      121 aveptaasla avhatdeqrd rllrladhdp hsgysneiaf helvaesagn elmrvlllvp
      181 ydllrlhldv editaddvge anaahkaiat fiadgdqqra gramlkhves feemmqrhnr
      241 ldqpivprer wlrewrtasg glgdggdlgd
//
LOCUS       WP_357537436             325 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Micromonospora].
ACCESSION   WP_357537436
VERSION     WP_357537436.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 325)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..325
                     /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=35207
     Region          24..298
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavpdtvagt ppaatptptp tpasrrrprg rdaaywlyll pgavlfilvi gvplvgtgyl
       61 sltrwsgvgd ptfvgldnyq rllhdevfwa sfrntvamiv amvvvptlvg lllasvlfdv
      121 vgrrfrprta aalraafylp qvlpvvvagi vwgwilrpdg afnstldaig lgalrhdwlg
      181 dpdtalpavm avmiwvqigy pvvvfmaalq rvdpelyeaa evdganwlhr fraitlaqir
      241 petfvvaltc tiaalkvfgp iyaltrggpe natnvpsyfa yytffkklqv gygsaistvl
      301 tviivvvavv figvqarser rdrgi
//
LOCUS       WP_357537531             540 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357537531
VERSION     WP_357537531.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 540)
  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..540
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..540
                     /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=55924
     Region          96..462
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mtgerppdgd eavpavdrtg pqragqpggs pgagqsaagp eragqpaggp rragppagpp
       61 grgvdlsggl aalrgllarp lasyylllss agllliiglt mvysatsvra fadegsatat
      121 fanqavfali glvafwvcqr lpartfqala ipvlgvaltl lvildallal aalgllkdsv
      181 lgpleadrlw lfigpvglqp sevakfgmvl wgsdviarkg aalgwwrela mplfpvvgll
      241 fvlvgyndlg tmlcllavvv gllwaagvrl rifatlsvlg lagvglliaa asqggeggny
      301 rldrltlffn ppddckldlc yqmiqsrnal dtggwfgvgl gkgslkwdwl paadndfifa
      361 ilanelgvvg cfvvlalfgv laysgmriar rvegdfrrla aasattwlvs qaliniggvv
      421 glipltgvpl pfisrggsal lvtlaavgml asfaraepda aralharppa rwvrllwapl
      481 pplpagrrad rssaptarst gsgarrgadp gatkrrdgda rpkqggtarp ragsgserrr
//
LOCUS       WP_357537504             437 aa            linear   BCT 28-DEC-2024
DEFINITION  phenylacetate--CoA ligase family protein [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357537504
VERSION     WP_357537504.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 437)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..437
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=47558
     Region          24..421
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 msgglavavr elrhlpavwr aphrapertr alalegvnal lrhcrervpa fadyptgpla
       61 sldelaglpi ltkravldag aesfhtrgla agayrtdvts gttgtrlhir hdvdaygyhg
      121 atvlrrflls gyrpwwriah ikpfprpvrw fqrlglfprv vvpagqsdaa maravlavrp
      181 qlimgypvvl rgllraldpg dlarlrrglk lvmtdsellt devaalfter fgvpvydeys
      241 ayevltvssg caagrmhvde drvwleivde agtpvpegvt gsvvvthfre ramplpryql
      301 gdrayvlpag cpcgsrfrrm rlvdgrtndf vtlpggrrvy sgvflalamh tpgvaecmir
      361 qdeagqvtvh lvpeapgeaa faaacvafeq algeavdapv vprfvraeri altpggkgrf
      421 vesayrpgvt gpraerg
//
LOCUS       WP_357537547             351 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357537547
VERSION     WP_357537547.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=38202
     Region          22..312
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtqqtrdelg dilpadefrt aseaivanie qviegktatv rlalavllae ghlliedvpg
       61 vgktklakal artidcsvrr iqftpdllps dvtgvsvynq ethdfefkpg avfanlvvgd
      121 einraspktq sallecmeer qvtvdgttye lqspfmviat qnpiemegty plpeaqrdrf
      181 tariamgypd agaelamldv hggadplhal rpaadavtvr rliatvrdvh vadavkqyav
      241 dlvtatreap dlrlgaspra tlqllrtara vaaldgrdyv lpddlqtlav pvlahrimpt
      301 adaqlarrtt daivadlvhr lplphdrrsp ydtrstgndd nsrshyeprg r
//
LOCUS       WP_357537673             383 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine desulfurase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357537673
VERSION     WP_357537673.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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 10003004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..383
                     /product="cysteine desulfurase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38900
     Region          6..376
                     /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 mgvtgvylda ataapphpva reallaalad gwadparlyt qarrarqlld aaraataetl
       61 gvrpdevsft asgttaahaa vlgglagrrr sgtvlvhsav ehsavlhaag rhvaaggsav
      121 pvpvdrlgrl dldawsaava gpgvalaali sashevgtvq pvaaaaraca dagvplyvda
      181 aqsvgrvplp dgwsvltasa hkwggppgvg vlvvrkgtrw espypedere sgrtpgvvnl
      241 pavvaaaaal ravaaeatae aarlaalvdr irstvaatvp dvevvgdpvd rlphlvtfsc
      301 lyvdgeallh aldrrgfavs sgssctsstl rpshvleamg vlshgnvrvs lhrgtteaev
      361 trflaelpev vaalraeagv tdl
//
LOCUS       WP_357537695             275 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357537695
VERSION     WP_357537695.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   5  (residues 1 to 275)
  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 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=29045
     Region          14..275
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 madasrvaeg gagraylall rgqvraqasy rvsfvvdlls nvgatvfdvl svlvlfrvtr
       61 dlagfglaea mvmvglsaaa fatadlavgn iervkhyvrt glfdavlvrp lgslpqlllm
      121 dlplrkvsrv lfgvvvlvva lvaadvdwtp grvalavvap lagavffgsi fvigasvafw
      181 wiesgeiana ftyggrdfts ypvtvysgwf rrlfayglgf afvayypala llgrtdplgl
      241 pvwvgwaapg vavvaatvaa vvwrvgvrhy rstgs
//
LOCUS       WP_357537691             185 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Polymorphospora].
ACCESSION   WP_357537691
VERSION     WP_357537691.1
KEYWORDS    RefSeq.
SOURCE      unclassified Polymorphospora
  ORGANISM  unclassified Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 185)
  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 185)
  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 185)
  AUTHORS   Rosinski,J.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..185
                     /organism="unclassified Polymorphospora"
                     /db_xref="taxon:2685497"
     Protein         1..185
                     /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=19251
     Region          5..84
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          96..172
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(97,112,114,124,127,133,167,169)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mtshasplat iavalrrerd raglsltela rragiakstl sqleagngnp svetlwslgv
       61 algipfsrlv eppgpavrvv ragegpavrs ehadltatll aagspharrd iyrlavepgs
      121 grhaephipg svehillaag rlrtgpvsdp velgpgdyat fagdvphhye alepgtfgil
      181 vmehp
//
LOCUS       WP_357537697             228 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357537697
VERSION     WP_357537697.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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
REFERENCE   5  (residues 1 to 228)
  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..228
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..228
                     /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=24444
     Region          1..228
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mllavatgtg tglaagysre qlatfvwagq gllavigiwg wteladrirt gdvasdllrp
       61 vdpvtsylag dlgragyavl trfvppvltg plffdvhlpa rwqtvplfav smllavvvcf
      121 gcrylvnata ywlhdargvt tlwtlgsgvl aglyfplrfl pdwlwgtiwl atplpsvmqa
      181 pldvlverdp apvqlgivgv qlgwavavla gcrvvqhrae rrlvvqgg
//
LOCUS       WP_357537765             390 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357537765
VERSION     WP_357537765.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   3  (residues 1 to 390)
  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..390
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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]"
                     /calculated_mol_wt=41091
     Region          147..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mglrrltsrg vrliraddpe tgwlvrivvs alliwsllfl tppspavrlv lvvalacwvv
       61 flvtdtrwpr varaglalgt vlpatvagvp esasaplfly amlftfvllp rtpmwailal
      121 tgativvllt gmwlagrgpt amltqpalia vlvlfslhrr eyrlraeqta lllkqtgrtq
      181 eaqaraaals ertriarelh dvlahslgal gvqlevaeae ltekgdaaaa aarirrarrl
      241 avdglaears avaalrtdvp plaralgdlv adhradhtat itlrtggsph dlppgaeval
      301 lrttrealtn aakhapgapv avtldysdsa vrltvrnpap drpgpadddd gggggryglt
      361 garervalvg gtleagvvdg awrvsvevpg
//
LOCUS       WP_357537803             439 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional pyridoxamine 5'-phosphate oxidase family protein/GNAT
            family N-acetyltransferase [Micromonospora sp. NPDC048894].
ACCESSION   WP_357537803
VERSION     WP_357537803.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 439)
  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 12124336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..439
                     /product="bifunctional pyridoxamine 5'-phosphate oxidase
                     family protein/GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /calculated_mol_wt=47132
     Region          20..165
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
     Region          <182..>292
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          243..418
                     /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 mypptartta srtrdrmsyd raaahavlde ayhcvlgfvv dgeprllptl hvrvgdtlyl
       61 hgstgsrpll aargeaglpv cvtvtlldgl iyarsqfhhs anyrsvvahg tahlvtsedd
      121 kraamtalve kvgagraads rpptrrelae tavlalplre vsvrartggv rdepadldlp
      181 hwagvvplrl tagppepdag vvapvpgylp ttgsptpgst gspapvvslp gpdsgaapww
      241 epvplhgahv llepltpaha delfaataep evwahlghpl padpaamrtv vaaalaarqd
      301 gervpwvqrc artgavvgtt sfyeidpqrr svaigytwlg rpwwrsgint eakllllgra
      361 fdtlgavrvv whtdirntrs qaaiarlgat regvlrmhrq rpdgswrdtv qyamtvdewp
      421 naqamlrerl rgttpvgrg
//
LOCUS       WP_357537833             131 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357537833
VERSION     WP_357537833.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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 131)
  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..131
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..131
                     /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=14626
     Region          4..123
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mgvidklawi rvtggrilst rsygrdtyyl pggkreages dhealkreva eelrvelvdg
       61 tiepagvfea qahghpdgvt vrmtcyrady rgtltpgaei eeirwltyag rerssmvdkl
      121 ifdwlrgrge l
//
LOCUS       WP_357537842             207 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GTP-binding protein [unclassified Micromonospora].
ACCESSION   WP_357537842
VERSION     WP_357537842.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  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..207
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..207
                     /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=22281
     Region          19..200
                     /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 mdfagydpvg srqsrgivsa kivvaggfgv gkttlvgais eitpltteal mtaagvgidd
       61 pskvpgkett tvamdfgrit maqdlilylf gtpgqtrfwf mwdeiirgav gaavlvdtrr
      121 itdafapldy fenrklpyvv alnrfdgsdl yepdevreal aisadvplvm cdardresvk
      181 qvlvtvveha mirlqaehgr gfptpvg
//
LOCUS       WP_357537830             568 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357537830
VERSION     WP_357537830.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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]"
                     /calculated_mol_wt=61550
     Region          5..555
                     /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 mtqteleayl ggltdrlaet lraepfhpra gyqigidlva ahiaapegig rtvevidlrl
       61 lrdlgmsged ardrlsrllg tvvtgytral rdrtldeqes irraamvarq qaetalrese
      121 arfrhqathd pltglpnrtl ftqcldavfa gphldrrlgv cfldldgfkv vndalghqig
      181 drllvsvadr lsrsvgrhlv arlggdefvi lvedstcved vvrvadaala aiagpaivdg
      241 heltvsasag iverpvggtt agdvmraadv tlhwakaagk grwslfdpvr nelemtryal
      301 saampaaidh gqfyldyqpl vsladerilg vealvrwrhp esgtlrpdsf ielaeetgli
      361 vrlggwalae achearrwld ldpgapfvsv nlavrqvhdp glvdevlall dhtglpperl
      421 qleitesalm gnsagpvral rtlydrgiri aiddfgtgys nlaylrtlpv helkiagsfv
      481 eglrrpypdl atatderilt tlvslahtlg ltvtaegvet awqaerlrai gcdtaqgylf
      541 grpgppekit arlgrpvgtt vagrqptp
//
LOCUS       WP_357537917             482 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent decarboxylase family
            protein [unclassified Micromonospora].
ACCESSION   WP_357537917
VERSION     WP_357537917.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 482)
  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 482)
  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..482
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..482
                     /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=49531
     Region          2..363
                     /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 midkngvpae rvldeirqlr agdrpvhggr lfayvydpgv ggldalgaaa haesahvngl
       61 dptafpslla menwlvgaag gllgggpgsa apdvvgsvts ggteslilav kaardahpel
      121 taprivvpas ghaafakaah llrvtldtvp vdpvtlrpsv advatairpe tvlvacsaps
      181 yahgvidpva giaqvaaaag vrchvdacfg gwtlpylrrl gvpvppfdft vdgvtsisvd
      241 lhkyayapkg vsvllhrdat lrspqffaya gwpgytmvnp vlastrsggp iaaayatlrh
      301 lgddgylrla attrdavdtl aaavrgvdgl rlmaepestv vcftstdpal dlfilvdelt
      361 argwhtqpql ryadlpasvh ltvtasvapr vaefgpdlaa avaaarqagp velpaelval
      421 agsltpqtlt peligglaag lglgagppdr mamvntllda apaalrecll vefvgllqrp
      481 tw
//
LOCUS       WP_357537944             222 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Micromonospora].
ACCESSION   WP_357537944
VERSION     WP_357537944.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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: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=23453
     Region          5..217
                     /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 mselsaafvr lharlapvaf vpevllhqad epiglwelte gefrsaqppp fwafawaggq
       61 glaryvtdhp evvagrrvld lasgsglvai aaaragaatv raveiderav aavalnaaan
      121 gvrvdaelad vldgnagdaq vllagdvfys eamarrvlrf llraarsgar vlvgdpgraf
      181 lprerfhela gydvpvpeal esvrvkhttv weldpappga ar
//
LOCUS       WP_357537951             835 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357537951
VERSION     WP_357537951.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 835)
  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 835)
  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..835
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..835
                     /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=92328
     Region          8..819
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtlttripaa pdpdtlfdaf agwadsrgfa lyphqeeali eivsganvil ntptgsgksl
       61 vaagahfaal addrvsfyta pikalvsekf fdlcevfgae nvgmltgdas vnedapiicc
      121 taeilanial rdgeradvgl vvmdefhfya epdrgwawqv plielpqaqf vlmsatlgdv
      181 trfeddltrr tgratavvks aerpvplmfs yamtplhetl eellstkqsp vyvvhftqaa
      241 aleraqalms vnvatraekd miaeaignfr ftagfgrtls rlvrhgigvh hagmlpkyrr
      301 lvetlaqagl lkvicgtdtl gvginvpirt vlftglskyd gvrtrllkar efhqiagrag
      361 ragfdtigtv vvqapehvie nekalakagd dpkkrrkvvr rkppegaigw aqptferlva
      421 aepepltssf qvshsmllnv iarpgdafva mrhlltenhe drpaqrrhir raiaiyrall
      481 aggvverldt pdeegrsvrl tvdlqfdfal nqplspfala aielldaesp syaldvlsvi
      541 esildnprqv lsaqqfkarg eavaamkseg ieyearmell eevthpkpla elldaayemy
      601 rrghpwvady evspksvvrd myeramtfve yvgfyslsrs eglvlrylad ayktlrqtvp
      661 edakteelvd liewlgelvr qvdsslidew erlrnpadev ekvlderppa vtrnlrafrv
      721 lvrnalfrrv elaalrrwdd lgeldaadgw nadawadave pyfdeheslg igpdargpal
      781 llieqgrerw tvrqifddpe gdhdwgisae vdlaasdeag aaviritdvg plqtv
//
LOCUS       WP_357537972             254 aa            linear   BCT 28-DEC-2024
DEFINITION  bleomycin resistance protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357537972
VERSION     WP_357537972.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 254)
  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..254
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..254
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=27348
     Region          6..125
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(6..8,38,45..47,49,64..69,74..75,78,123)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(29..30,38,49,51..52,66,105,112,114,118..120,122)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 maektipllt caqispvsdf ytalgfevty lqkapypylv vergdielqf fgmrdfdpat
       61 slggcyvltd dvetlyetfr sglkgfygri ptrgiprigp lrdtsygvrq flmtdpggns
      121 irvgqpdggg peirpaprdp yekalhtatl fadskedlpg aarvldrvla rpdgkptagq
      181 lvrllvlrad iaqrsgdpga aaelldraag tpltddqrgs lrdelrrmae lgdllrddgw
      241 rvagsgagep ahgg
//
LOCUS       WP_357538078             202 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357538078
VERSION     WP_357538078.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..202
                     /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=21607
     Region          7..199
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 mtstktdgsl flreflrapt rtaavapsgt aladqmalpi pergepvvve lgpgtgaftr
       61 aieqrlagrg rqlavelnpt madhlaarfp gvevargrag dlpqilagyg idradvivsg
      121 lpwfayeads dgpplvhtla svlttqgvlt qfaytwtrwa pparrllhgl ragfeevvsg
      181 rtvwanlppa tvyfarrprs lp
//
LOCUS       WP_357538185             266 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Polymorphospora].
ACCESSION   WP_357538185
VERSION     WP_357538185.1
KEYWORDS    RefSeq.
SOURCE      unclassified Polymorphospora
  ORGANISM  unclassified Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 266)
  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 266)
  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..266
                     /organism="unclassified Polymorphospora"
                     /db_xref="taxon:2685497"
     Protein         1..266
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28986
     Region          1..222
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mgrsaaffdl dktviakssa lafgrpfyrd glitrrdvvk sayaqlmfrl ggtdeqtmar
       61 trdylatlck gwqvdqvrqi vaetlhelin pyvyaeaaal ieehqaagrd vvlvsasgee
      121 mvrpigellg vpdviatrmm isegrytgev efyaagpakv davgelakar gydlaecfay
      181 sdsssdipll ecvghptavn pdrtlrklas enswpvlefr hpiplhrrlr erpavpvaaa
      241 aigvgvgvai giawygrhrr trtasa
//
LOCUS       WP_357538228             309 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357538228
VERSION     WP_357538228.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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..309
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..309
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32827
     Region          19..>128
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mtrpidpgep aafragrlld vliptrnrpa elattlsgla gqpgpagfgv lvsdqsdgep
       61 swahpaaaam arvlrhrghp vllarhlpar gmaeqrafll agsaaryvlf ldddvwlepg
      121 avdrlvtaig rlgcgfvgna vqglsylddl rtaeqatyee wpgrpeperi rsggpgwdrw
      181 rlhsaanllh iadrlglgpg qwraykvawi ggcvlfdrak lvraggfdfw prvpadhqge
      241 dvaaqlrvme rdgaagvlps gafhlesptt ltdrgvecwq vvlgdgtgad yppttglpat
      301 gpgvpsrag
//
LOCUS       WP_357538284             314 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357538284
VERSION     WP_357538284.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 314)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..314
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..314
                     /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=34310
     Region          1..>78
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          99..265
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mnhlgaalra wrdrlepatv glvhhaprrv vglrrgelam lagvsaeyva qleqgraktp
       61 saqvcsalar alqlndeeqa hllrlaghta npdriprlip isvrrvtdql sasplavyda
      121 awqllhwnll faatwgdpcr asvedrnami tqferrnarv rqtaaervwf eqslvadlrt
      181 ttgrypddpd vaslidrlsr tarfrelwas ptvaahesah ktavhpevge ialdanilpt
      241 qdsdlrvvvl tarpgtdars kldllatigv qemalrpdqp gtpgrapaan psavaacges
      301 wpprqgergh trsr
//
LOCUS       WP_357538249             583 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine/threonine protein kinase [unclassified
            Micromonospora].
ACCESSION   WP_357538249
VERSION     WP_357538249.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 583)
  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..583
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..583
                     /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=59024
     Region          10..476
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mndglrpgdp arlggyelld rlgeggmgsv flarspqgrr vavkvvrpel shddefrgrf
       61 rsevnrarqv ppfctaevld adpdhdppyl vveyvegpsl aqvirdggpl gsaqlhgiav
      121 gvataltaih gagvihrdlk panvlvapgg ikvidfgiar afeatsqhtr thqmvgtvsy
      181 maperfdtas gravgpaadi fawgavvaya atgrnpfggd satatamril tqppdltglr
      241 gplrelvsra lekdpdvrpt arelldgllt vtapagdpap agdpasagvp apagvpapgg
      301 vpalpvapss agadrpsags papvaatgvp gdgpgdpasa sggsgepsaa gvdvagrrvs
      361 srrrllvgvg aavavvavlv svavfgprlv gdrstpdptg aaaggpttgg ptttasgsgt
      421 ppaspsaasp sapdrtrail agqrqillhv veidrdlslp fdgvvgvgdg ttpdarfvld
      481 pvgvdfmirs lnpqiahrpc lgvkldaqgy aslvgtdcep taatlfgisr egkddkgrla
      541 yaivseqygv vqwspsqkki yvevlgdapv gttfslvdrg avg
//
LOCUS       WP_357538301             557 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 27 protein [unclassified
            Micromonospora].
ACCESSION   WP_357538301
VERSION     WP_357538301.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 557)
  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 557)
  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 557)
  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 557)
  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..557
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..557
                     /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=58380
     Region          46..308
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(53,88..89,130,164,166,199,218,222)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          320..395
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          433..556
                     /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(444..447,457,459,462,466..467)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(453,486..489,499,501,504,506,508..509)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(472,476,478,482,486..488,499,501,504,508)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(529..533,542,544,551..552)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mfrrrvalls pvllaatlgt avvtgaavlg sappaqalen glartpqmgw ndwnsfgcnv
       61 netlirqtad tlvtsgmaaa gyeyvniddc wstrqrnasg dlvadpakfp sgmkaladyv
      121 hgkglklgiy ssagtttcag ypasinyeqr danlwaswgv dylkydncgd hlgrsgqqry
      181 tamrdalaat grqilyslcn wgqdsvwtwg asvgnswrnt gdiggnwnsi mgildqqvgk
      241 dsyarpgawn dpdmlevgng ptetesrahf slwallnapl lagndlrtms aatrtiltnt
      301 dviavnqdwg grqgykisds gdlevwrkpm ssggvatvll nrgggtatvt ttasalglgs
      361 assyavrdlw ahssststgt isasvpahga amflvtgggt pppttppptt pppttppptt
      421 pppttpppgt tsavrsvsag rcldvngatq tngataivwd chgqtnqswt stgsqelrvy
      481 gtkcldvnna gtangtsvii wdcngqsnqk wrfnadgtvt avgsgrcldl vgngtangtr
      541 tqiwdcngat sqrwsrg
//
LOCUS       WP_357538355             317 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Micromonospora].
ACCESSION   WP_357538355
VERSION     WP_357538355.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 317)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..317
                     /product="GlxA 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=33224
     Region          2..316
                     /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 mhtvlvlalp gtiafdlatp ievlgrvrlp ggragyrvlv cgsepvvdag plrlavdhgl
       61 daladadtvi vpgrydpaap lpaavldalr aaaaagvria sicvgaftla aaglldgrra
      121 tthwaaaerf qamfpavrvd pavlyvdtgq fvtsagatag vdmclhlvrr dhgaavaada
      181 srqavaplhr dggqaqfivr pgadpagvgl gpvlewlesh aderltladv aaraglsvrt
      241 lnrrfheetg ltpmqwvaav rvrraqelle rtdhgvdria hlvgfaspah frvqfkrrsg
      301 vspqayrrtf vagsvpg
//
LOCUS       WP_357538378             125 aa            linear   BCT 28-DEC-2024
DEFINITION  YidH family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357538378
VERSION     WP_357538378.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..125
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..125
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=12993
     Region          1..96
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 mrepawyrag depdyrfsla nertflawir talallagsv avvqflppsa lsgmrdllaa
       61 vlaaagsalp aaaylrwvrv qkamrlgrgl pftpllavma vgaavvgvgv illavlpwas
      121 apaap
//
LOCUS       WP_357538414             195 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357538414
VERSION     WP_357538414.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 195)
  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..195
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..195
                     /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=21656
     Region          10..169
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msaggpater tarerrfral htetypdllr fverrvpsse aedivstvfl vawrrldeip
       61 ddtrpwlfgv arrtianqtr gwlrrrvldl rlasepehaq adgstaaavr ldlvrawrtl
      121 sagdrevlal vafdgltaeq aatvlgcrrs tfamrlgrar qrlrkalepg apaaapgrtt
      181 rnslgderlw tgasr
//
LOCUS       WP_357538423             360 aa            linear   BCT 28-DEC-2024
DEFINITION  segregation and condensation protein A [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357538423
VERSION     WP_357538423.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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..360
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..360
                     /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=37568
     Region          39..283
                     /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 mtappldppt tpqqppvlaa evaadlatdp agvpqagqsa gftvrlanft gpfdlllqli
       61 skhkldvtev alhtvtdefi ayiramgdew dldetsefll iaatlldlka arllpsaeve
      121 deedlallea rdllfarllq ykaykeaaah iaeleavggr rypravtlea ryadalpdlv
      181 lgvgperllr lavramtpkp vpevsiahvh lvrvsvreha tilaerlrra giatftllca
      241 dceitlevva rflallelyr eglvafvqee aleeltvrwt gpadgdadlh vdeyagtpad
      301 addtgpapgg paapaaapdg padpgsagpg sagpgsagpg sagpgsagpa geaattqetr
//
LOCUS       WP_357538511             476 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357538511
VERSION     WP_357538511.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 476)
  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..476
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..476
                     /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=49662
     Region          23..474
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtmaeasdva davtsdprap ltrlaqlvdp gslrlfgpdd avkagnarig gspvvvfctd
       61 atrvggslga eesmqivtai dlavrdrvpv iglwhsggar ltegvqsmdg vgrifaaiir
      121 asgrvpqisv vlgpaagaaa ygpaltdvvv madggrmfvt gpdvvrsvtg eqidmeglgg
      181 leahgrksgv vhvsagsete aysaarhlvg ifarpgwfdl ssvkddegla evlpasarra
      241 ydvhplisrl ldepgdegpa flelqprwar nvvvgfgrla graigvvann plrrggclds
      301 lsaekaarfv rkcdsfgipl lvlvdvpgyl pgvnqewggv irrgakllya fgeavvprvt
      361 lvvrksygga yiamnsrslg attvlawpda evdvmgpeaa vgilhrrals aapaadrerl
      421 rreltaehrr isggtqrgvg lgmidevidp tvsrrriaea latapagrgs hgnipl
//
LOCUS       WP_357538521             944 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357538521
VERSION     WP_357538521.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 944)
  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 944)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 944)
  AUTHORS   Rosinski,J.A. 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 944)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..944
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..944
                     /product="helix-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=101606
     Region          <3..878
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          858..909
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mefversrel dilrdlysgs vtgrgrvali sgpgatgkte llrafadhvg aagglvlraa
       61 csraerllpa avmgqlfhsv plpdevmrri gafvdiegvt tggdaeirav hamcvelidi
      121 ararplvllv ddvefadett lhtllylqrr ltaaqilvvl tespqpqpfh pefraeisrq
      181 asfcniqlsp lseagvaell rgwvddetaa alapayhgvs ggnplllhal gqdrrvagst
      241 evaevvvgdq frqavlaclr rwdptileta hglallgdla tpallarlld tkparvqwvl
      301 naltmsgllh agrfrhpaar aavlhdltpe alaemharaa ellhaegapa paigghllaa
      361 gglaepwait vlqdsathal aedrvddave slklahdmcd dvprraalta tlaacqwrin
      421 paavsqhlqs qrdalraghl serhaaallr yqlwhghrad aqetlrhlrd trqqldatta
      481 aelegcaewl rlhfpvafae ldadagpavt pagtparsdg slgsatpslt avltdgvtde
      541 viaraeqvlg shllvdvgle salcalqtlv yadrmdravh wcdvlgaeag argattwhai
      601 lsdvrshial rqgdlplser farealdams phnwgvaigs plsnmllami gmdkldeaea
      661 qlkhvipdam rdtwfwplyl rarghlhlag grvhaaladf etcgqlatqw gmdlpallpw
      721 rgdlaqvylr sgrperaram vteqlsrpga enartrgvsl rllgsaldvk qrvntlrqaa
      781 nllqesgdry qlflalaals sahygrgefn tsrvvarsal qlakdiqaqa lcrrllpggd
      841 aaggddpdap peheemsrls daeqrvatla alghtnreig kklyitvstv eqhltrvyrk
      901 lnvrrrtels lglpmdaaga gllavgsggs erswpqwesa vqas
//
LOCUS       WP_357538528             248 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357538528
VERSION     WP_357538528.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..248
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27464
     Region          15..248
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mteeeslwir rfhqsteakv rlfclphagg sasyffpmsr tltpavevlp vqypgrqdrr
       61 fepcvedlhe ladlvfeair gladrpvaff ghsmgaalaf evslrmeakl gisprhlivs
      121 grrapstsrv eqvhlrddsg ivaelrdlsg ttddmlgdtd ilrmilpair adyraietyq
      181 grpddavrap itvltgdadp rvslaeahrw rshttgtsev lvfpgghfyl ndcrndvngi
      241 varilaea
//
LOCUS       WP_357538568            1037 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase, partial [Micromonospora sp.
            NPDC048894].
ACCESSION   WP_357538568
VERSION     WP_357538568.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048894
  ORGANISM  Micromonospora sp. NPDC048894
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1037)
  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 1037)
  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 1037)
  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 1037)
  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 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Micromonospora sp. NPDC048894"
                     /db_xref="taxon:3155493"
     Protein         1..>1037
                     /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          9..>995
                     /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 mgstapayqd aiavigmscr fpgaaspdef wdllvrgeea ireaptdrws gdpgtvrrgg
       61 flddvagfda pffgvsprea aamdpqqrlm lelawealeh agadptplrg sstgvfigti
      121 qddyatltrr gggdpgphtl tglhrsvian rvsyrlglag psmvvdtgqs salvavhrai
      181 eslhagectm vlaggvnlil tgestdavrg fgglsptgrt hlfdahadgy vrgeggglvv
      241 lkrladavad gdrifcvihg gavnndgggd glttpsqagq eqvvqlahtr agtdpadtgy
      301 velhgtgtpv gdpieaaalg avvgtalapg drllvgsakt nvghlegaag vvgliktala
      361 lrhglipasl hhetpnpaid faatrltvqt tlavwpvnrp lagvssfgmg gtnchlvlgp
      421 wpappaavda ptsvdgpgtp sgtqvaapav arvvwplsgr tpaalraqah rlhrhltdrp
      481 tvpigavgrs lagrsgfdhr avvvgrdree llagladlad grrraglvtg radtgtlgfl
      541 ftgqgaqrpg mgrdlydasp vfaeafdevc aeldrhldrp lrevvwddpt aldqtgytqp
      601 alfalqtalh qltvsfgvrp dyllghsige lsagyaagvw slpdacllva argrlmqaap
      661 aggamlaiaa pedvvtahla dfaarldlaa vngpnavvvs gdadavtdla arfdqlavkt
      721 rrlrvshafh sahmdpalde ftrvaagipa rtpqvpvvsn vsgklvqaey tdptywaaqi
      781 rrpvrfldgl rtlrsagvta flelgpdpvl tglaeaehda gsgssddtay avllrrdrde
      841 pttaltalar lhshgvpvnw splwpdadra dlptyafqrr pywidtaass agtastatat
      901 astagsavpv dvppstapea patgaaevdp aswagrllal peherrpaae llvrrlvaet
      961 ldyadladvd gsltfkelgi tsltavelrn lvtaetgqsf sasmvfdfpt pvlvaerlvg
     1021 lvvggvsgvg vagvgvg
//
LOCUS       WP_357538606             207 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357538606
VERSION     WP_357538606.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 207)
  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 207)
  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..207
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..207
                     /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=22503
     Region          7..199
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mavphslpqr ifllaynpdk grvdlgtnlg amlraaalad llrgghltde rgraaidvrh
       61 pchdpvlgal leeiagskph twqswighrq ratvratrqq lndggwvhlq phkvlglfpt
      121 trvtvrdprv rkklldrvnt alrkpigsid padaalvaii aaadlnlvld rktrrankqr
      181 iqeltklsgp igpalhksiq aaaigev
//
LOCUS       WP_357538707             381 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357538707
VERSION     WP_357538707.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 381)
  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 381)
  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 381)
  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 381)
  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..381
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..381
                     /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=40241
     Region          67..377
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnrltirarl tlvfgglffv aggvllavny alvagrlqqn rlslwiggsg dtsgldtaai
       61 gamvgdyqrv vrdsaldsll tqgglalvav svvavaigwl vagralqplq eitgtarria
      121 gadgagrglh erialggpkd evrelagtfn emlerlnraf dgqrrfvana shelrtplal
      181 nralvelamt rpgapaevrq lgeslltvne rherlidgll tladsenevt drtpvdlaev
      241 arhvadqvag padvrveldl aaaptagdpv llerltqnlv enavrhnvpe dgwlsvetav
      301 vdgratltvs nsgptvpgye veslfqpfrr lnrdrigggr gfglglsivr aiarahngsv
      361 eatprpqggl tvtvslpsrs a
//
LOCUS       WP_357538758             314 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357538758
VERSION     WP_357538758.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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 314)
  AUTHORS   ter Beek,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..314
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..314
                     /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=33944
     Region          18..314
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtavdvksaa aprkvgdrpa krpprwrrav tgwafatpft alflvfmalp vvaslamsvt
       61 dlrstdlrnp lavnfvgldn yarlfgdelf vrsavntlvf vvvgvpltmv lalaaasaln
      121 sglirfralf rvgfylpvvt sivaiavvwr flldpeaglv nnllrlvgvd gpawlgdtst
      181 alpslivmaa wrnfgflmvi flaglqgipq hlyeaatldg agrwqqfrnv tvpllrptll
      241 fgavvtgigf lqvfeepfvm tqggplsstl svsyhiynqf gfgnygyaaa asyvlfvaiv
      301 alsvlqfrll gerd
//
LOCUS       WP_357538633             311 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357538633
VERSION     WP_357538633.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 10582168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..311
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34152
     Region          228..274
                     /region_name="HTH_20"
                     /note="Helix-turn-helix domain; pfam12840"
                     /db_xref="CDD:432824"
ORIGIN      
        1 msalaetias lhvlrgrgaa pgrpahtpaq taayrarlaa dpvvtlfvkt vlqpnwmpdf
       61 isppphpqdr tfneelrrvr qtpaavalae lttafggpvp aglavpdlpd rvadllhwvw
      121 shtvrpdwln rrrifeadiv srtqqistgg waaalsgmrp gmrwlgdgrl qintyeyppr
      181 dlagvqllfi pstarrgwva weqphryavv ypcsgvlaea ehagvpyalr allgpvraev
      241 lsqldtpkst tqlvalggyg lgtvgrhlki lldarlirrr rsgrsvlyyr tpagdhlvra
      301 qtetepplpd r
//
LOCUS       WP_357538839             225 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GOLPH3/VPS74 family protein [Polymorphospora].
ACCESSION   WP_357538839
VERSION     WP_357538839.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
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="Polymorphospora"
                     /db_xref="taxon:338583"
     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=23161
     Region          15..190
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtsvalaeel lllayddesg katgsrigld lgmaaavlvd lalagrlays dgsmvvidet
       61 ptgspladev lariaadtpn spaawvqrlr hglrdrvlag lvargivqdv detalgfihv
      121 hrypmtdata etdardrlak altgdgtpde rtaalatlia avrmeptlgl sgsaiddahr
      181 rlqeiagsag fggtvsldes tvrpsvalvi atltraidaa lgara
//
LOCUS       WP_357538840             160 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357538840
VERSION     WP_357538840.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=17945
     Region          5..158
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd18886"
                     /db_xref="CDD:467596"
ORIGIN      
        1 mqaiiatlgy vlspdrrqvl mlrrdarpdd lhygyynglg gklepgedvv agmrreihee
       61 sglecetvel agtvswpgfg rsgenwfgfv fripswtgep kqdcpegtll wtdladilag
      121 rvpmwesdhh flplvfapep rvfhgvmpfk dgkaqswsws
//
LOCUS       WP_357538852             113 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357538852
VERSION     WP_357538852.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   4  (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
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..113
                     /product="PadR 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=12013
     Region          <24..101
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mkaqalhghl dalllavlag galhgyaiie alrarsggvl dlptgtvypa lrrleraglv
       61 esewstvsgr qrrtyrltra ghgalrtert gwqefsatvg rflgvdeppp aat
//
LOCUS       WP_357538948             188 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357538948
VERSION     WP_357538948.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 188)
  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..188
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..188
                     /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=20271
     Region          13..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msressavrr dgrvtdtrer vravalrlfv tkgfsatslk diadalgvtk aalyyhfpak
       61 adlarsifqp fiddvdallt rldradrppr eiltayvetl iphreafaai mrdptaaadl
      121 dvegasqrwl drltellatg dtpevrirvt vavggltrvl vlpdadadai rgtaidaava
      181 algpaahr
//
LOCUS       WP_357538953             546 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357538953
VERSION     WP_357538953.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 546)
  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 546)
  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..546
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..546
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=57510
     Region          45..308
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          268..543
                     /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 mrrtpqlvla aallalatac tadpapttpa sgsedpylrg sgtlrvlags eladlrpild
       61 eareatgvtv qlteigtldg iervasgaaa rdhdaiwfss nrylelhpda gdkigvdakv
      121 anspvvlglr tstaqrlgwd knrptwseia taagegefty gmtspatsns gysalvgvaa
      181 alagtgralt tdeitaltpr lqsfftghal tsgssgwlad ayvhrqtagv pldglinyes
      241 vllslnaggr lsepltviyp adgvvtadyp ltllagageq aranhaaiad flrrpstqak
      301 imerthrrpa vtgislasdf gptdgglvel pfptryevan klvssfgdtl rkpartiyll
      361 dlsgsmrggr leglqsallg lsgadtslsg eltrfngreq vilvpfsttv qeprrfdvps
      421 ddprptldri radvqgfsan gdtaiydala rglelareld tadpgrftsv vlltdgertv
      481 grsldafrsl haglpatirs vpvftllfge gnvgemteia tltggrtfda rtgslgavfk
      541 eirgyq
//
LOCUS       WP_357539001             109 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539001
VERSION     WP_357539001.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 109)
  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 109)
  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 109)
  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 109)
  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 109)
  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 109)
  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 109)
  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..109
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..109
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11695
     Region          11..107
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mstdlhdvsg rdwlgdlrtn ltgefdaqtt rltqltadtg dpaqeptraa liaatrqsle
       61 qisaalgrid agtygrcvhc gkqipaerlq ilpharfcvp cqekhgrag
//
LOCUS       WP_357539031             393 aa            linear   BCT 28-DEC-2024
DEFINITION  NRAMP family divalent metal transporter [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539031
VERSION     WP_357539031.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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 393)
  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..393
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..393
                     /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=40300
     Region          3..388
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msgaadtdpt tvatlvvvga asgyglawlt llaipalavv qvlatrvgal tgrnlqravq
       61 dgygrlvssl llvsvlvvnv vtvgadiaag aaaigllvgl esrwlvpvfa vavltllflg
      121 gydevervlk wimigllayg gavvlarpew savargsllp plsvtaahvt galailgtll
      181 ttymylwqtv eqveekaagk slrirefdav vgatlacvig wsilvasgat lgvhhekvdt
      241 aqqaaqalrp lagslaself avgllaaavi aapvimaagg yaaasafgwr rglsyrprqa
      301 pgfyalialq avvgsvlamg vvspirllff aslvagvatp fglvllvlca gnprlvgerp
      361 isrglraagw fvaagtaavs llflaqqfhl vrl
//
LOCUS       WP_357539060             198 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539060
VERSION     WP_357539060.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 198)
  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..198
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..198
                     /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=21188
     Region          5..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mahvhrqqvd egildraaal faqhgydhts lktvadsvgl skagllhhyp tkealylatq
       61 qsvraqgqrv fdqvadlppg pardrralel ltdvaldrpg lvaqafsslt tppsdgepdh
      121 lddiatlvfa tfavdaaqps erlvrvigal salavlslsv nraagektmw rphilatcld
      181 alghhrrtls sdptqvea
//
LOCUS       WP_357539089             266 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539089
VERSION     WP_357539089.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 266)
  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..266
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..266
                     /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=27562
     Region          8..257
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mesvlpgaaa llgqarrvvv ftgagisaes gvptfrddlt glwarydaeq latpeafhad
       61 pdlvwgwyew rrarvrrarp npghlataai edlvpgtvvv tqnvddlher agsrapihlh
      121 gslfaprcvg raahpvafvd paddaadhda adpgegsrla pprcghcgal vrpgvvwfge
      181 alpeaaltaa aeaaatcdvl ltvgtsgvvy paaeipriaa rsgatvvqvn plptpldaic
      241 dvnlrgsaar ilpalveaaw gaagrt
//
LOCUS       WP_357539107             241 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539107
VERSION     WP_357539107.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 241)
  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..241
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..241
                     /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=25792
     Region          8..234
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtveqlfspv vgarpheail gqveqllsag llrpgdrlps erslaerlgv srptvreamr
       61 tlealgvarp adtagrgsaa viagradtal gavlrlaiat sdlsvpdvvd trvllerdav
      121 srlartpepa ltaaevllre mdepgltper fhaadvrfhi alaeaagnra valmmsslry
      181 aiegyvldlv aglddwpgvs rrlrvehrdi laaiadrdad eaarrverhi rafhgtatas
      241 r
//
LOCUS       WP_357539108             280 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease
            [Polymorphospora].
ACCESSION   WP_357539108
VERSION     WP_357539108.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
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="Polymorphospora"
                     /db_xref="taxon:338583"
     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=30807
     Region          17..277
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavlllpfvv lfllfylvpi gyaihqsffk vrregtfgrp etvfggfeqy vrvfeneafr
       61 esvgrvllfg vvqvpvmlgl allfalllds gllplkrffr layfapyavp gviaaiiwgf
      121 lyspslspfs wvtervpfms gslvlwslan vttwmftgyn mliiyaalka vpqelyeaar
      181 ldgagniria lsikvpmvrp alvltgvfsi igtlqlftep qvfrslttav tgsytpnlvv
      241 fstsvipnfn laaafsvvla latfalsftf lriaqrgssl
//
LOCUS       WP_357539119             432 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539119
VERSION     WP_357539119.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 432)
  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 432)
  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 432)
  AUTHORS   ter Beek,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..432
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..432
                     /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=45215
     Region          52..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"
ORIGIN      
        1 mrrtlgrrta lrslagalva alaisvgact gddssgpsva eagpngiddg seltlwtrap
       61 lekqakllvd aynashqnkv kltvvpnddy vakvgaaags dslpdlfaad ivyvpnwvnq
      121 glfqdlsanv dglgfkdsin kghlsagtld gkehvlpfvl dlsmlfwnkq lfrdagldpe
      181 kapanlteya aaakavqalk regvygtaag lncggclvft wfpaiwadgg evlsddgtea
      241 kladdtaqkv ystwqdlwks gavlpasage tgptwtaaft egnvglmlyp atllsstpfd
      301 vgvagipgps ggastfvggd gigvskdskk aaqawnflsw mmseeaqvev laknkdvvsr
      361 sdlannkyaa edprlvtine vagkgdtpva lnfqqafnap nspwltlvrn qvlngsgnlq
      421 qdngeitavl kq
//
LOCUS       WP_357539208             307 aa            linear   BCT 28-DEC-2024
DEFINITION  sortase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539208
VERSION     WP_357539208.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..307
                     /product="sortase"
                     /calculated_mol_wt=32179
     Region          97..224
                     /region_name="SrtA"
                     /note="Sortase (surface protein transpeptidase) [Cell
                     wall/membrane/envelope biogenesis]; COG3764"
                     /db_xref="CDD:442978"
ORIGIN      
        1 mttatpttpp gaapsrtgrl gfylpgtalt ilamltlgfv vhltlvshlq yargqqtlys
       61 dyraelargt apvgqtrlef tdgiagderi vetgspvavl ripaiglrav vlegsdaevl
      121 rdgpghrrdt vlpgqpgtsv vmgrqaaygg pfrdldllip gdlvtvvtgq gehsyrvtgt
      181 rrpgdptppr lpsgagrltl itadgdrylp qdllrvdadl vspaqpapar rfgaaslpaa
      241 eqpmatdpda wtplmlwsqa lllatlavay lrgrwggwpa wtvgvplvaa lggaaadqva
      301 rllpnll
//
LOCUS       WP_357539219             234 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539219
VERSION     WP_357539219.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..234
                     /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=24191
     Region          1..194
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 mtsdaptfla qfvrhpfttg avlpsgsgla aditaavprt ghplvvelgp gtgvftraiq
       61 rrlagrgrhv avevnpafaa glarrhpave vvradaatlg rvlldhrlpa vdvvvsglpw
      121 aafaagrqra ildavvgald aggvfttfay rhalparpar rfrrlldgaf eevtvgrtvw
      181 gnlppalvyh crrptgagnp ppapaetpac agtgrapaat grgagtrsdp pvrr
//
LOCUS       WP_357539218             392 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539218
VERSION     WP_357539218.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=40712
     Region          <192..390
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtearrrwwp dvllglvtag lglagtwivq pgaargdwag ivvavltgla liavrrrpwp
       61 vlvvesalll vavaatpagg gtsllaaava lgyvayrsgr astaaayalf lgvalanvlf
      121 qgdaavrfsv tgvlslimla gvaaapvafg rylrgvrlaa aaaeerarem rerraaetra
      181 arlaeraaia rdlhdivahh iaaialraga aryavqhtgr tepavaalge lretagqvld
      241 elrellevlr dpetverdgp qveleqmigd aarrvgeagv tvrvsvpetl srvplsvgtt
      301 aarvvqealt ntlkhagpga tatvdirvad gtlllevvds gavrerpvlp asgyglagmr
      361 ervgllggtl taaaadrggw rvsarlpire na
//
LOCUS       WP_357539276             245 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539276
VERSION     WP_357539276.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 245)
  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..245
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..245
                     /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=26300
     Region          16..244
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 maeashdaar aaapvmhgav ldalgleitg gqhapgtalt lehlqqrfgv srtvmrevmr
       61 ileslnlvas rrrvglvvqp mhrwrvldpr virwrldgpg radqlrtltd lrvaveplaa
      121 agaarhatad vrerlctlat rmrqlgeage ldaflaadve fhalllqacl nemftaltgv
      181 iaevlagrte hglmpkcprp valdlhdrva dcvaagdawg aetamrelve evrdaisttp
      241 kaaag
//
LOCUS       WP_357539319             351 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539319
VERSION     WP_357539319.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..351
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..351
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=36717
     Region          50..>188
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mrlrekglla allavavafg aapataapvg svparqalap gdtddeggtk klrdqldaat
       61 kgyvdakaal dnstkrqrel darlktigee ltvrgqavge lasrayrtgr igpiaallnt
      121 sspegfldrt talgnlaase drqlrllqet qeqetraraa vdneireqkk qlatmdqrkk
      181 qaeralaeag sgqsssgvqg sgsgsgsgsa sakpaprnan gswpsegcti ndpttsgcit
      241 prtlhalnqa kaagftryvs cyrsggsgeh pkgracdfaa qkggfggvat ggdrtygnnl
      301 aayyvnnasr lgvlyviwfk qiwlpgsgwk ayrgggdpss dhtnhvhlsv y
//
LOCUS       WP_357539314             710 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539314
VERSION     WP_357539314.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 710)
  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 710)
  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 710)
  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..710
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..710
                     /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=77740
     Region          5..709
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mtdvstvqqe iateqrhvdr vyarltqlra saaraekegy rlagvgnfga lverdamvfh
       61 aarrrhvlda eheglvfgrl dlragtvlhv grlgirgeng epllidwrap aaaafyqata
      121 adprgvvrrr miqssgervt gveddlldpq aappdmrvvg dgallatlar akgtgmrdiv
      181 atiqreqdea irspgsgvtv vsggpgtgkt avalhraayl lysdrgryag ggilvvgpsa
      241 vfvdyigsvl pslgedaatl rslgslvvgv tatradptpv aavkgslrmr rvleravrdg
      301 vpdrptelrl lyrgellhld aarldriwdr alprgarrne vrragidglf dalwpqarag
      361 klitriefed dlaereefrs flrawwprll prhvlawfad parlrryatg ilsnaeirll
      421 adsyrtlatd gptiadvall deldelmgrp pkpkrrgqdp yhvrdgvrev ttyadrqraa
      481 raaaverpdd yrdyahlvvd eaqdvspmqw rmlgrrgrla swtvvgdpaq tawtgdpael
      541 arardralgs rrrheftlst nyrnpaeifa eaaaviravl pdlplpkavr stgvppvtlt
      601 vadaelrtav hdattrllte vegtvgvitp aprhpqvttw laelltttpr lqvvtslqsk
      661 gmeydgvlll apdeitaeag artlyvalsr atqrltkihv indpqrlsgs
//
LOCUS       WP_357539320             185 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539320
VERSION     WP_357539320.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 185)
  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 185)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..185
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..185
                     /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=19921
     Region          1..185
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpsrqdqlld aaievlgtgg prnlthravd araglpagsa snhfrtreal lsgivtrlve
       61 ldrvdwqgla atvrprdaee lagaladfvr yatgpgrhrt laryalglea avrpalqtel
      121 rrgqevivgw gvvwlrdlgs tdpardtrlv mdhldgtmlh qlsmpvadfd prpgiravla
      181 gvlgr
//
LOCUS       WP_357539355             326 aa            linear   BCT 28-DEC-2024
DEFINITION  1-phosphofructokinase family hexose kinase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539355
VERSION     WP_357539355.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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..326
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..326
                     /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=33356
     Region          9..284
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 msgftlhvvc pnpaldrlqv vdrfhpyevn rvttvrslpg gkgmivcrga rrldatvsah
       61 gfvggftgqv irrgcadlgv ldrhievegd trvtpvviee stgrstvlne rgpdiapgep
      121 ekllaglaad vvpgdvvvst gslppgcppd lhariarlal aagatvivda hgeplarvid
      181 dvrsappagr lvvkpnvhel agvlgrdlpd latataamrd lhaetgatfv vtlgtdgalw
      241 idgaerlavd tpkvetrnat gsgdsflagl avalgrgasp aaalvlasam gaanaasltp
      301 dvdpdlvtkl rdqvtvtttp vtpvtp
//
LOCUS       WP_357539339             187 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539339
VERSION     WP_357539339.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 187)
  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 187)
  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 187)
  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 187)
  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 187)
  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..187
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..187
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20337
     Region          33..185
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mtaagitplq vtvsrlraav tdedhtqgpm dapatvvvyg dfqcphcaaa ypnlrelrrq
       61 rpgtvrlvfr hfplanvhpy aeiaaetaea agvrgqfwam hdwlfthqdq ldpvhlalgt
      121 qhvglpveev aaevndhvhl drirrdfvsg vrsgvdgtps ifvngmrheg tyalsdllta
      181 vdgaahh
//
LOCUS       WP_357538781             230 aa            linear   BCT 28-DEC-2024
DEFINITION  gamma carbonic anhydrase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357538781
VERSION     WP_357538781.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 230)
  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
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..230
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23520
     Region          35..180
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mpnprdslag qvghvdrpep paevngdltt gvfrrslrgr spqvsagafv aptavlagdv
       61 hvadgavvld gavvtaesap vvlgeecivm enavirgagr hpvdiggrtl igpgahvtga
      121 rigaecmvat rasvfngari adgvlvavga ivhvgtvlpe gavvpmqhia vgdpyqvfpp
      181 qeanaahdlv drigftavaf dhdtsgldlr qcmswlcgvy apalrrthat
//
LOCUS       WP_357539393             569 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539393
VERSION     WP_357539393.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 569)
  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..569
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..569
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60170
     Region          1..352
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mitqtevdgv ptllapnpng pliagltfrv gqadetlara githllehla lhqfgltdyh
       61 yngstgtvvt hfhtqgspek vtafvngvca algnlpmdrl dmekgilrte rgsrvpgyge
      121 plavwrhgav gyglpghpef glrsvgpddl rawaaryftr dnvvlwiagd avpaglrldl
      181 pggtrqpvpp awsalpetpa yfcggasriv afdavvrrsv aagiytavle relfralrqe
      241 dglsymatat ysprgddham vtaaadalpd khgavlggfv dvlaklrvgr ieqadldtvc
      301 aateetysra dfdaarlpga alnhltgqpn lstdemrael kavtladiha vaveaagtal
      361 lmvpgsrgae wagfaaapth stsavtgrra asrtagdetg lvigpygvtl dqpgapvtve
      421 yancaallvw pdggrqliga dalfvpvept mygvtaadva aidnivpadr hvpmpardpe
      481 sipvppaeqa vvpkglrlpr wyealgllff gilalplllf ivvqgilivt gdaddpdswl
      541 fmgvllglta gvawpivall rrlrrplrr
//
LOCUS       WP_357539417             279 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539417
VERSION     WP_357539417.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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..279
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..279
                     /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=31076
     Region          38..229
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mtarrglvdl arrgvrgara yaraavpgav galpdflvig gqrcgttsly hylaahprir
       61 tgtgkelqyf tlhhrrgtrw yrahfprtgp gertfeaspy ylfhpevpar vaaalpearf
      121 vallrdpver ayshylhtrs ygaepldfaa alaaepdrla aalragpdsr tahaalrnhs
      181 yaargryaeq lerwfaavpr ervlvlrsed lyaepvrvya dvlrfldldp ytpdgfarht
      241 rrvdrgesgl tdavraelag hfaphnarla dllgwsstw
//
LOCUS       WP_357539442             179 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC048999].
ACCESSION   WP_357539442
VERSION     WP_357539442.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 179)
  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..179
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..179
                     /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=19910
     Region          9..155
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkpvgersed wftslyathy pdivryglrr lpdadaaael aqdvfivawr rrsevperpl
       61 pwlyavarnt vvnrwrrgrg aptlvpltea dqvpaglvgp damapvldlh ralrelpead
      121 qeilrlvgwe dlsvsdaaat lgctrsaaav rlfrarrrlr salaarpqlp dprpasiyv
//
LOCUS       WP_357539468             197 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357539468
VERSION     WP_357539468.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 197)
  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..197
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..197
                     /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=21383
     Region          5..195
                     /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 mshrppvpsg rvtsakivia ggfgvgkttl vgsvseitpl tteaimtsag vgvddtrqvp
       61 gkttttvamd fgrisidrdl ilylfgtpgq trfwfmwdel vrgaigavvl vdtrrladcf
      121 aaidffehrr lpylvaincf dgmqyhnpqd vrdalaissd vpvvacdarn restkhvlis
      181 lveyvltmrr sravapa
//
LOCUS       WP_357539429             467 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539429
VERSION     WP_357539429.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..467
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50282
     Region          1..340
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mkpllvldvv gltprlldhm prlsavadag fraslgtvlp avtcsvqstf ltgeppsghg
       61 ivgngwyfrd lgevflwrqh nalvggdklw haarrvepgy tvanvcwwya mgadvnwtvt
      121 prpvyhadgr kdpdcytdpp elhdaltgrl gtfplfsywg anagitstaw itkatmqima
      181 dhspdltlay lphldydlqr fgpsapqaaa aaaeldatvg plldaatarg atvvalseyg
      241 itdasrpvdv nrllraegll rvytqagmey ldpwtsrafa vvdhqvahvy vrdpadvpvv
      301 akllgglagv aevldrdgqk tygldhersg elvlvaepda wftyyywldd arapdfarlv
      361 eihrkpgydp aelffdpanp gaakgraala llrkktgmry lmnvvgldag aravrgshgr
      421 lpadpldgpv llcsdpaaar dhfaatdvkg lllhlaglgd ppavgtr
//
LOCUS       WP_357539517             311 aa            linear   BCT 28-DEC-2024
DEFINITION  YihY/virulence factor BrkB family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357539517
VERSION     WP_357539517.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..311
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33227
     Region          19..255
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mnlfgrveaa fdrridvard rlpafdhlwr agtlytdvla grlaaaiayy gffaafalal
       61 vgyaafgail kdndeasraa akfleknlpf lepqqiaess ktvgvvglii liftgvawve
      121 airssqrlmy glnqqpgnlv vrrlvdlgvl vavfvllgis vaavdalesl lrfllrstgs
      181 iglttvsavl svlvnvvlag allvavprlr msrrrlrpvv lvvavgitll ntvgryyvvr
      241 ternpayavv atavglllyl yllnqlvlfg aalaatsryg rvvdlaegrt arevdveade
      301 vtepgtpgga g
//
LOCUS       WP_357539535             296 aa            linear   BCT 28-DEC-2024
DEFINITION  sortase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357539535
VERSION     WP_357539535.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..296
                     /product="sortase"
                     /calculated_mol_wt=30860
     Region          86..212
                     /region_name="SrtA"
                     /note="Sortase (surface protein transpeptidase) [Cell
                     wall/membrane/envelope biogenesis]; COG3764"
                     /db_xref="CDD:442978"
ORIGIN      
        1 mptpapastr paprpaggpq vvataltlla vlllgfvahl tlisrlqyar dqqtayadlr
       61 selanatapt gqvdqdgrll apgtpvavlr ierlklrqvv fegtsggvlt agpghrrdtv
      121 lpgqpgtsvl lgrraayggp fadldllstg diitvatgqg qhtyrvqsvr rtgdlapppl
      181 apgagrltli tadgqpylpq dllrvdaeli sppqqvgsrp ltaaslpaae kpmatdpaaw
      241 tplllwcqal aaaalgfawl rtrwgrwqsw vvgvpvlaal gaaaadqiar llpnll
//
LOCUS       WP_357539681             318 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357539681
VERSION     WP_357539681.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..318
                     /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=34095
     Region          6..309
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 maavgrprrs clavpgssvk mlgkaqglpa dqvfldleda vaplakpdar knivaalneg
       61 dwagktrvvr vndlttpwty rdvievvega ganldcimlp kvqnaaqvqw ldltltqiek
      121 tlglevgrig ieaqienaag lvnvdaiaaa sprvetiifg padfmasinm kslvvgalip
      181 dypgdpyhyi lmrilmaarm hdqqaidgpf lqirdvdgfr evakrsaalg fdgkwvlhpg
      241 qieaanevys paqadydhae lildaydwyt seaggklgav mlgdemidea srkmalviaa
      301 kgraagmtrt ssftppar
//
LOCUS       WP_357539686             293 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539686
VERSION     WP_357539686.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 293)
  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 293)
  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 293)
  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..293
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..293
                     /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=31540
     Region          30..273
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 meavrtstah pvparsavvr qnrrvpveli tdpdderigd yraltdvelr trwepphglf
       61 iaegelvlrr alragyrprs ylvdakrveq lgdtgdapvy aasqdvlera tgfhvhrgml
      121 asfhrrelpt aaellavarr vailedvnnh tnlgavfrga aalgvdgvll spscadplyr
      181 rsvrvsmgev favpyatltp wpdgleqvra agftvlamtp aadavpiqrl taeqrgraal
      241 llgaegpgls rqalaasdvr vgipmrrgvd slnvaaaaav afwelgrddp lpt
//
LOCUS       WP_357539699             431 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora sp. NPDC048999].
ACCESSION   WP_357539699
VERSION     WP_357539699.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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 431)
  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 431)
  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 431)
  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..431
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..431
                     /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=42837
     Region          158..428
                     /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 mtdgwdwrrp ggtptaaeap vpgspsqgtg gdapapwwsd aladpwrdpy apaavvvsaa
       61 padggsepep vsdpdapvrp wlrqvvlasl itallagslg saltyallrg gpgvpslgaq
      121 saqapalaqr kpeslagvae kvlpsvvtvr vaslggiseg sgfvvstegh ivtndhvvsg
      181 gtgkvtvifn dgssasgtvv gqdpesdlav ikaarsglrp vefgdsdala vgdpvlaigs
      241 plslantvta givsaldrtm qasepggptr yyaaiqtdaa vnhgnsggpl vdgagrvvgv
      301 nstikslvad gqeagnigla faipinqakr vaqdiigsgk arrtvigvqv ggtgvtgggv
      361 rlgtvdpsgp aaaaglrtgd vvlrlnghpm adptdlvalv rkyapgsvva veyqrgttrq
      421 ntsvtlaada k
//
LOCUS       WP_357539821             254 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357539821
VERSION     WP_357539821.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25301
     Region          4..243
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrcdglvavv tgggsgigra cveallaaga rvgvldldpa gaptdprvhp vradvadras
       61 laaavasvad ayggidilvn nagisavgtv ednddaqwar vldvnvtgia rttavtlphl
      121 rrsraaaivn mssiaagagl prrvlysask gavhamtlal aadlvgegir vncvapgtvd
      181 tpwvarllad addpvaekir laarqptgrl vtapevaaav vylaspdsga vtgtslavdc
      241 glyglrlaps ppps
//
LOCUS       WP_357539829             485 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539829
VERSION     WP_357539829.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 485)
  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..485
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..485
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51320
     Region          36..420
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msltsarsag paeappppaa pagsgagrrt yglgplllrl hfyagvlvap flvlaavtgl
       61 aytvtpqldp ivygtelrad pagrtalpvs eqvaaaraah pdgtltyvap gadgtttqvv
      121 ftspelgedq hsvyvdpyta qvkgqlttwf gytpvrtwid dlhrnlhlgt vgrhyselaa
      181 swlwvvalgg lalwwrrqrg srgrlrrlll pdlaarkgvr rtrgwhastg vwlvvgllfl
      241 satgltwsry aganfgagld aldartpvls talggadgpa aggghhggap taappvdpaa
      301 iddvlriara dgltgpvevv ppadvssawt veqvdnvwpv rldrvavdpa agtvvdrsdf
      361 adwpllakls slgisahmgl lfgpvnqill aalavgllcv ifwgyrmwwq rrptradrra
      421 vvgappvarg awwqlptwai viglpavfll gwvlplfgip llafivvdlv vaawrrrrsg
      481 aavsa
//
LOCUS       WP_357539908             289 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539908
VERSION     WP_357539908.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 289)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..289
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30004
     Region          26..285
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mttsttflgl gamgsalaaa aldaghravv wnrtphraqa lgergatvad gveeavagdg
       61 vivvclfdhr svhdvldpva pglsgrtvvn lttttpdear eladwaarhg ityldgaima
      121 vppmigrpgs eifysgsaaa fethrdlldl wgassffgpd aglaalydva mlagmytvfa
      181 gfmhgaalvg aegvsatrfa erqmpfltam vgqlaglaat vdstdytgeg qqslrfteta
      241 latlvrasae qgvdaavlkp vhdivrrqia agfgghgtar mfeelrstr
//
LOCUS       WP_357539910             303 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357539910
VERSION     WP_357539910.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 303)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..303
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31049
     Region          8..298
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mngtgspapv tvvglgpmgr amaaallrag hpvmvwnrtp graaglvaeg atlaptpaaa
       61 vagvdliils ltdyqamydi lgpvvtdrrh adalagkvlv nlssdtpdas reaatwaagh
      121 ratfvtggvm vpapmvgnpg syvfysgpqe afrghepvlg llgeprylgp dpglaqlfyq
      181 anlavfltal ssllhatslv taagvpaaef lpgavgmltg ipamvgdgle lareleagky
      241 pgdlstalmm gataehivrt sekagvdvel pkavrshyer aiaagygtrn wtalyevvra
      301 tdg
//
LOCUS       WP_357539951             217 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357539951
VERSION     WP_357539951.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22896
     Region          1..189
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mvdavlfdld gvivdsepvw eevrrayvaa hggtwqpdsq rrlmgmstge waaylsgelg
       61 vdrsaeqvat evvaemtrry aqrvplidda dtvvrrmatr wplglasssp trliaaalda
      121 tgladcfgat lsteetargk papdvwlava arlgveparc vaiedssngv rsaaaagmrv
      181 vavphrsypl dpdaealaaa llptidalts elvaqlv
//
LOCUS       WP_357540127             191 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357540127
VERSION     WP_357540127.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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 191)
  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 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 191)
  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 191)
  AUTHORS   Rosinski,J.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..191
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..191
                     /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=21121
     Region          17..>84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtearpeqrr vtisdpqvmr alahparmai mehlstvegg atatecaeia glspsatsyh
       61 lrelakfgli eeapsrgdar ervwfspsyy vesgpdadse araaelalvd ahlardsqrv
      121 rdwirrapde pgewyeaawf adsvllltae eltglnnaih ellgpyrrrv rtnppegars
      181 vavqyrslpl d
//
LOCUS       WP_357540167             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357540167
VERSION     WP_357540167.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31675
     Region          11..289
                     /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 msdgrvptgf teqraqvgdl minyvrggag palvllhgyp qcwrmwrhll selarsydvv
       61 apdlrgfggs dapptgydkk tvaadlhgll aglglttdir lvghdlgtmv ayayaaahpd
      121 qvsrlvltea pipdesiyti paltaagpav wnfgffnvpn glpehlvagr ealwvdrftd
      181 siminkgslg pddieeyagh lrdeahlras fgyfrafgqd iadnaayrat klsmpvlaig
      241 aqaslggqva eqahryadtd tgevvdncgh wlfeerpakl talllpflgd qssta
//
LOCUS       WP_357540175             493 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357540175
VERSION     WP_357540175.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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 493)
  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 493)
  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 493)
  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 493)
  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 493)
  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..493
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..493
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54005
     Region          10..339
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 mtqlakpkgi fdrdvewael trfaaderpg atlgvvsgrr rqgktlllye laratdgfyf
       61 gateataaes lrrlgealga ytgalgpvql adwgaavdal lalarerpvt vvidefpylv
      121 rvardlpsii qhaltpgrpe rtqsqtrlll cgsalsfmgg llagsaplrg raglelpvqp
      181 ldyraaaafw giqdpllavk vfsivggtpa yrreyvqdda pdgpedfdsw vvravlnpar
      241 plfrearyll vedpdlrdta lyhsvlaava egnasrggia gyigrkandl qhpltvleda
      301 gllvrepdpl rsgrssyrit eplitfyqav mrpawtaleq rrggdvwrrs krrytsavlg
      361 prfeeivrqw airfadldvf dgivaeasaa tvtdpstrts heldlvalge pplgdgprtl
      421 laigevkwgr rlgqadlerl rrvrellvhr pgidasrtrl llasgegftd dlrraaayrp
      481 divlvdaarl ysd
//
LOCUS       WP_357540194             168 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357540194
VERSION     WP_357540194.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 168)
  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 168)
  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 168)
  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 168)
  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 168)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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
REFERENCE   7  (residues 1 to 168)
  AUTHORS   Rosinski,J.A. 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 168)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..168
                     /product="GbsR/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=18607
     Region          11..157
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mpddhrptrn eeeihlfver mamafadvgf prmagralft vmsaddplta aeigerlgvs
       61 aaavsgavry ltqfgmlvre pvkgsrrdry rmpdnpwyea titktglykn fidianggvd
      121 allgrdtpag ervsemrdff lfvqeeidal gerwrarraa tghggras
//
LOCUS       WP_357540219             165 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357540219
VERSION     WP_357540219.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..165
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18266
     Region          1..105
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 meehrsgcpi nlslevfgdr wslivirdim fgnrrhfrel ltnnnegias niladrlhrl
       61 vglgmvsrap dpghkqkivy rltepsiqlv pvlaqlgawg vrhlpvspel avrarlladg
      121 gpplwddfma elrelhlgip rpagvesvfd rltaayqael aragn
//
LOCUS       WP_357540225             589 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357540225
VERSION     WP_357540225.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 589)
  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 589)
  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 589)
  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 589)
  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 589)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..589
                     /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=62717
     Region          24..547
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mdgppyrdar lpvavrvedl lrrmtlpdka gllfhtmvgi gpggslapad pdagllsaae
       61 mvrdrrmnhf nllgtaapad lahwhnrlqe laaatpfgip vtlssdprha ystnpntaal
      121 agafsvwpep lgmaatrdaa lvrgwadvvr qeygavgirv alhpqadlat eprwprtlgt
      181 fgedaglaae lvrayvgglq gpmlgpdgva amvkhfpggg aahdgedphf rygreqvypg
      241 grfadhlrpf vaaldagcsq vmlgygmprg tgyaevgfsf nrdvvggllr rrmgfggivc
      301 tdwgvltgav frgqvrpara wglehlspgq rahrvldaga dqiggeavpg lvvdlvragr
      361 vgvarldasv rrvlrekftl glfdrpyvdp draaavvgca rfraaglaaq racvtllsna
      421 apdraarlpl rrglrvwcdg vapevvardw rvvdrladad vallrlqapy dhrpgqfeaf
      481 fhagslefaa gemarvlaia etvptvvdvy ldrpavlsrl aarvaaltvs fgvcdealtd
      541 vlagraapgg rlpfdlprsa aavragrpdv afdtvdplfr fghgltyrd
//
LOCUS       WP_357540238             239 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357540238
VERSION     WP_357540238.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 239)
  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 239)
  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 239)
  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 239)
  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 239)
  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..239
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..239
                     /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=24658
     Region          5..239
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtlilrsair ndvglvrtnn edcalagdrl vavadgmggl pagevaseiv irildeltpp
       61 tvpdeaadal ravvstanqr iraaitvdpa rdgmgttlta gllagdalvl aqvgdsrcyl
      121 lragaltqlt rddtfvqalv dqgalspdqa rhhpqrslvt ravqgsdtpp aigmltvfpg
      181 drlllcsdgl sdyvadaaia svlgtysdrq lcgeqlvkla hqagapdnvt vvvsdvtaa
//
LOCUS       WP_357540286             508 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357540286
VERSION     WP_357540286.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 508)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..508
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55558
     Region          81..480
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvshdp rgqqpgatst applappngr hhppaaavap pappppprpr vdfavvrelr
       61 relserltlw qrgrefdada eeverarlav avvsayadsv rrsgtpmaad eerllldqvt
      121 aelvglgrlq tllvdetiee vhilgcdqvr itrhgggvdw sepiadsdde lveilqaaar
      181 ragatersls tskptldlql pdgsrlaavf lvshrpyavi rkhntlavsl ediaggrpdl
      241 demidpllrd flrasmragl nimvaglaga gkttviralm deipadepyv lleesrellp
      301 arrghrhrav msfeareghg ergldgrpag evniadlipv slrmgvlrii vgevrsreiv
      361 pmlqamttsr gsmctihart pagvseriie lalshgremt vdqarrmagn aldlivyvnv
      421 edetaiggrk hrfvshveev igvgegnrit tttvfgpgpd gravprhlpe riraqllrvg
      481 ydarlltrfi eagtgawrrp lrtrlgrr
//
LOCUS       WP_357540337             360 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357540337
VERSION     WP_357540337.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..360
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..360
                     /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=38056
     Region          15..355
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mgvfattddp gstgheqvvf cqdkqsglka iigiystalg palggtrfyp yaseeaalad
       61 vldlsrgmay knalagldlg ggkaviwgdp eriksepllr aygrfvetlg gryytacdvg
      121 tyvadmdvia retryvtgrs vehggagdss vltawgvfqg mraaaehvwg aptlagrrvg
      181 vaglgkvgky ltghlvgdga evvatdvnpk alewvrathp qvelvddtaa lvasdidvya
      241 pcalggalnd dtvavlqakv vtgaannqla hpgiekvlad rgilytpdyv vnaggviqva
      301 deiegfnfer aklratriyd ttreilrlad eegvppavaa drlaerrmae vgrlrtirlr
//
LOCUS       WP_357540399             459 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357540399
VERSION     WP_357540399.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   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 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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..459
                     /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=49063
     Region          75..187
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mttptdlvvv lpgilgstlk lddrlvwaps agsalraikt fggsikrlql pdgigdehpd
       61 ddvqpvglmp dlhvlpgvwt pvkgydklla rlrslgyhes agtdappgnl lpvaydwrls
      121 nrynsrrlag ivgpalerwr aqggryadar vtfvchsmgg lvarwyiehc dgheitnkli
      181 tlgtpyrgaa kaldqlvnga hkgvgplgvd ltdlirslps myqllpeyac ierdgdlvet
      241 vetglpeldd rrvadgahlh rqladaelar pdslarthai vgirqptstt arlnggkiel
      301 vddyrgddlf gdatvplvaa cradvpmdsp llrripdrhg slqrnraald evegiltarp
      361 ivvraptavd lrvdlrdlii agedlevrva tadgsrhavr itvtdesgrm vdarmprpat
      421 agtvttipgl apgaytvdva gvgpgspvsp vggdvlvwg
//
LOCUS       WP_357540375             486 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357540375
VERSION     WP_357540375.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 486)
  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 486)
  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..486
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..486
                     /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=54720
     Region          128..449
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpdgsltkrc scrdtngkli gvtcpklrrt ngtwsadhgh whyqielppt tdkrrrqlrr
       61 ggfrtrtdaa deldqartli slanrdrerg teigdmlqti ahnrqalpdp deirrrlrag
      121 gsladaptva eyltqwltgl qvdentirsy esharnhhip hlghipldkl rphhiknmft
      181 aieqraneiq aaktspdpki rasvkgirpc gpatrqrira slrkaindal aeeiivgvan
      241 patlvktrgh rahpivwepe rvahwkttgh ipgpvmvwtd ellarfldya aehdpdlhpl
      301 fhflayrgpr rgeacglrds evrldkrevt innqiatygh larqkppksk agnrdltlda
      361 dttavmtayr arrntqrlka gpdwpdtglf fvrpnghpwh pnlvtqrfrk ltrkaglppi
      421 rlhdlrhgaa tialdagidi kvvseqlght tttltrdtyq svtkelhhqa adkvaeriak
      481 krgkia
//
LOCUS       WP_357540416             269 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357540416
VERSION     WP_357540416.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=29053
     Region          6..258
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mteetspspr ralitgatlg igeafarrla adgwdlvlva rdagrldata telirrydcr
       61 ieimsadlst ddgcavverr lgdeppvgll vnnagmslnt pfvrspigde arlirlnvla
      121 vlrlthaalg pmvkrrkgtv invssvagfg vpmpgstysa skawvtnfse sigqsvapfg
      181 vrvmalcpgy trtgyherag inmsripawl wlrpddvvde glrdlrkgrl vsvpswkykl
      241 avaglrhapr rllrgvsrdt rgriapgad
//
LOCUS       WP_357540464             414 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357540464
VERSION     WP_357540464.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..414
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45013
     Region          4..412
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mtgptveqai irvhheewar lvaslarrfg dldvaeeata eafvaaaerw phegvppnpg
       61 gwlattatrk aidqlrresq rdakhqaari vyddtppept gpveddrlrl lftcchpala
      121 mearvaltlr llggltvsei araflvqeta marritraka kikaahipyr vpsaddirdr
      181 lagvlavvyl vfnegylase gddptrvdlt deairlgrll rallpdngev agllalmllt
      241 darrlarvsr tgelvtldeq drgawnrtli aegnalvrer ieavaaggdp pgryqlqaai
      301 navhtnapta rdtdwsaiva lygrmvlldp spivrlnrav avaevdgpgv glaeidrlae
      361 vldgyhafha aradllrrlg rggesraayd raiglagnpa erayltrrrd qlvg
//
LOCUS       WP_357540468             245 aa            linear   BCT 28-DEC-2024
DEFINITION  aminoglycoside phosphotransferase family protein [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357540468
VERSION     WP_357540468.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 245)
  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 10007009
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..245
                     /product="aminoglycoside phosphotransferase 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=26470
     Region          2..223
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
     Region          <122..200
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
ORIGIN      
        1 meevevvvah hgcatlrvgd vflkidadqt rtdveveama lapiptpqil wrkppvlala
       61 alpgralgrl gepsaassea waaagaavrm lhdaplppwp grsldeltsr ldgecewlvr
      121 ngvlpadlvt rnrevaeaal rpykpvfmhg dlqvahvfvd gdeitgvidw seaaqgdalh
      181 dlailtlghe ehlgdvvagy gtdvdldvir awwslrslla vrwlvehgfd psspgcevdv
      241 lrsrm
//
LOCUS       WP_357540474             307 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357540474
VERSION     WP_357540474.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..307
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32417
     Region          8..216
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtgdrltiev srltkrygdv tavrdlsfti epgvvtgflg pngagktttm rmmtglvspt
       61 sgtatiggqr ydrlaspsrt vgavfdtnaf hpghsardhl rvyaamggyp dsritelldl
      121 lglaeaadrr trgfstgmrq rlnlatallg dprvllldep gngldpegls wlrgllrqla
      181 dqgrtvliss hvlseiqqlv ddvvvirrge lvatgpwsrl agppavlits pdadvlavtl
      241 atspasggta psveavgpgr lrvrgldaps iadlaaahrl rvhelvtenp sleqlflhlt
      301 tgkaatr
//
LOCUS       WP_357540517             501 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357540517
VERSION     WP_357540517.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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 501)
  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 501)
  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..501
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..501
                     /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=52701
     Region          5..495
                     /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 mnaplrrvgv vvmvlfgllf anlnwiqayk adeyrnsdyn drvqvaeydr krgnievggt
       61 avaiskdtgg klkfqrtypg geayahvlgy kpvnladtgi erleneflag tsdqligdri
      121 kdmftgeeta ggnvlltlsk raqdtafkql qdnqvgatrg aaiaidprtg avqalvsmps
      181 fdpnpltshd teaakkaydk ldedpdrpla nralsetlpp gstfkivvaa aalengigqq
      241 tqipagrswt pptagtpikn aadsicpqak vtlkqavtds cntgfaqlgv qlgsdkikek
      301 aqqfgfeqdd ltvgqlgkgg lpvaasrtgd mqnpdgstdp aalaqssigq nnvrmtplqg
      361 aliaatvang ggqmrpylvk qllapdrtts yynadprelr qpvsgqvasd lrdmmvnvvh
      421 ngtgrkaaid gytvggktgt aesgpdtpdh gwfigfvldk tgtpisavcv eleragsggs
      481 aeaariagri maaviadagg r
//
LOCUS       WP_357540519             491 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357540519
VERSION     WP_357540519.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 491)
  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 491)
  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 491)
  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 491)
  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 491)
  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..491
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..491
                     /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=51038
     Region          5..240
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtltlryaah sdrglirdgn qdsvyagprl lavadgmggm aagdvasniv igamaplded
       61 vpgdalvdal rsavgtanqq lrdtvdanpq legmgttlta tlfsgsklgm vhigdsrayl
      121 lrngefaqit kddtyvqmlv degrisaeea sshpqrsllt raldgrdidp eysvrqvlpg
      181 drylicsdgl sgvvsadtig dtmrqyadpq qcverlvqla lrgggpdnit viiadatdqd
      241 iveatpivgg aaardrgmat sadvstpaar asalsaprap vpeepmdahd depergrhrp
      301 vrtaamllal lvilgggvfg gwsytqrqyy vgatedgqla vfrgvpgria gldlssvhar
      361 seaklddltl aaqeqvkqgi qaksepdaer rlaelisddp tnpnlkplcp psptataasl
      421 tptttadaaa ptptasaevl ppatvtpept gtpestgtpe stgtpepttt pdavvsdtvp
      481 pvdpagcrsp e
//
LOCUS       WP_357540697             705 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357540697
VERSION     WP_357540697.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..705
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..705
                     /product="PhoX family protein"
                     /calculated_mol_wt=75298
     Region          45..699
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msdrrrllpl lgqavhgsrs amtclyrcgn acdhpvpnes dnpyftdvvn sgmsrrgvvr
       61 asavgalvlg vggaaggall gaapaaatpp gpdlaaltps rpksgngalt fkpippnrld
      121 tfvvpngydh svvirwgdpv vpgapafdvn dqtaakqsvq fgynndfvai lplhqhnkha
      181 llvvnheytn enlmfpgftt fdamtleqir vaiaahgmtv ielarveqtg ewevatkgkr
      241 pynrrltale tpfaftgpaa gsdllktaad pkgrtaigtl nncaggvtpw gtvlsgeenf
      301 nqyfvggdgv adevkpklar ygisttaryp gdsrkwervd erfdltrhpn eanrfgwive
      361 vdpydlkggq rkhtalgrfk heganvivak nghvvaymgd derfdylykf vsdkkfiddn
      421 stvarkhnlt llesgtlyva kldstsadei dgsgklpsdg afngtgtwik lvrgntsyvp
      481 gmtaaevltf trlagdavga tkmdrpedve pslltgkiyv altnntnrgv gsnpkadean
      541 prnanrhghi vemvedrgdn tsetftwsip ivcgdpadps tyfagydksk vspiscpdnv
      601 afdgagnlwi stdgnalgsn dglfataieg perghlkqfl tvplgaetcg pfittdnqsv
      661 fvavqhpgei sgasleepas nwpdgdyakp gvvvtwrldg gpigs
//
LOCUS       WP_357540699             229 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357540699
VERSION     WP_357540699.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 229)
  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..229
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..229
                     /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=24283
     Region          1..150
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mscefahddg ayvlgamapa ereryehhla dcpacreavg eiavlpgllg rldqagldrv
       61 agppstgpqv tdllagaatm rrrdrlrrrw ryagvalvag clalfvglgv gslrtvgpdg
      121 tdfeirtvtm apvagsvpvt aeiglngatw gtevimrcsy aetedyakay tfrlvaygpd
      181 gaseqvgswk aapgddvtft gatrfsaeel vrieltrydg tpllaydvp
//
LOCUS       WP_357540720             180 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357540720
VERSION     WP_357540720.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 180)
  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 180)
  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 180)
  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 180)
  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 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..180
                     /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=19253
     Region          6..157
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mttlrlrped padeapvarv lagafarpdv atppevglvd elrrsedwip elamvaeygg
       61 evvgyalltr vrvraddsay salalgpvav aphrqrighg tavvqaalda ateldeqlvv
      121 vlgdpnfyrr fgfsradrmg ltspwsglge pwqalvlppv geepappqge vvfpppwskv
//
LOCUS       WP_357540763             273 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357540763
VERSION     WP_357540763.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 273)
  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 273)
  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..273
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..273
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29122
     Region          7..270
                     /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 mtrpglpkli atdldgtlvr sdetvsayth qvldrvraag ipvvgatgrg prlteltrnd
       61 iraadflvma gggrvvdqsd pegplvlrde rlsgevlagl lvdleaavgp ltvmveasde
      121 hdaplwgdfh aswpyqdrfe artraeclsg dvikafarta dhhvdellav arqivppala
      181 tltqaglgfi eicppgvdks tglsvvaerl gvdpaevlvf gdqpndlpmf gwagwsrvav
      241 anahpevraa adeitlrndd dgvaiyldrl lsr
//
LOCUS       WP_357540764             402 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357540764
VERSION     WP_357540764.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..402
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..402
                     /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=41922
     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 mrtavvvgag igglatagal arsgwqvtll eradrlradh tamvlwpngi ralhalglga
       61 gldaiatplp dlgvrrpdgq wlvqprkpap ppgagravvv hredlhdalv aglgdrvdir
      121 tgvavralrs aagerpavdd grqtfeadlv vaadgidstl rrrlapeaav vssgcaawra
      181 vipwyraprl padgpvggef lgagyrfvaa slgergssgg strggiywia taagaprpes
      241 patqltllrr wlagwpapvg ellaatepdd lvqqevrelr plpktyafpv gtggfallgd
      301 aahgmphhlg qgaclafeda atlaavlrsa lpgpgaraal styqrlrhtr tvtvvrqtrr
      361 msavlrtrgr lalrardaal gtisprlmgr aaaaatgwqp pd
//
LOCUS       WP_357540807             185 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357540807
VERSION     WP_357540807.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..185
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19572
     Region          1..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..178
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 mprarlstag vvevalavid eqgleqltla avaahagvat pslykhvasl aqlrnlvgvr
       61 vmedmaeqlt lavvgrsgdd avaslmrasr ayvvrhptry aampadplhd patqaagykl
      121 lqvflgalra yrlddaatih atrclraith gftsieaagg fglpeglddt yeqliqmfia
      181 slprp
//
LOCUS       WP_357540821             405 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357540821
VERSION     WP_357540821.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11461692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=42812
     Region          <171..396
                     /region_name="LytS"
                     /note="Sensor histidine kinase, LytS/YehU family [Signal
                     transduction mechanisms]; COG3275"
                     /db_xref="CDD:442506"
ORIGIN      
        1 mggnlsavfg vvslatalaa alwavlrlra rrgiatatqr atyevlhtag laaeplragl
       61 nragaakavr hlralvgaag laltdreall aldgrgahhg dqllaaarrv vgtgrstvlr
      121 dselrcdlvd cpvrgavlap lsadgrvvga lvavadeqpa pglvqatlet ahwagdqlal
      181 aeldssrerl araevralra qisphfiyna ltaigsfvrt dperarelil efaeftrysf
      241 rahgefttla eelrsidryl tierarfger lqvrlqiape vlpvtlpflc lqplvenavr
      301 hglsrkpgtg mvsieardag aechitvedd gvgmdpttla agiaelagsd ptadpgqhvg
      361 lsnvderlrs afgdrfglvv etglgsgtkv smrvpkfhpg vrags
//
LOCUS       WP_357540824             286 aa            linear   BCT 28-DEC-2024
DEFINITION  Fpg/Nei family DNA glycosylase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357540824
VERSION     WP_357540824.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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..286
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..286
                     /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=30410
     Region          2..270
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpelpeveal agylreravg rcvervevaa isalktydpp psavsgravv gagrhgkfld
       61 vrfegglhlv vhlaragwlh yreafssavp lrpgkglval rvrlddgsgf dlteagtqkk
      121 laaylvtdpa qvpgvaklgp daldadlptf aervrsrrgq vkgvltdqav lagvgnaysd
      181 eilhaarlsp faitdrltdd qlaelhgatr avlgdavrrs lgqraaelkg ekrsglkvha
      241 rtglpcpvcg dtvrevsfad sslqycptcq tggkpladrr lsrlvr
//
LOCUS       WP_357540887             184 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357540887
VERSION     WP_357540887.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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..184
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..184
                     /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=20392
     Region          6..149
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 myrprdtrre altadiavdl rrltidsehv ghafaslhgl gatdlqalia imdaereenp
       61 itpgrlgehl nlssgsvtal idrleraghi rrdrdtvdrr kvflryadrg arvamdffrp
      121 lgwrtegvms gytddeltvv hrfmrdmaam mrqhrddvra grptgpapgg daadraapag
      181 rppd
//
LOCUS       WP_357540975             276 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357540975
VERSION     WP_357540975.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 276)
  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..276
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..276
                     /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=30483
     Region          60..>213
                     /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 mqayeaqrat qaaissaswl gltahdaavl hnsntltlrl qpcdvlarva paahqcaqle
       61 vdvaqrlaev gspvaalesp qvfvrgdyvv tfwtyyepvt thslsnaeya galerlhagm
      121 rkvdlptphf tdrvseaqtl vadhartpel adlnrvflas tldrlrravs esgrpeqllh
      181 gephpgnlll trtgplfidf etccrgpief dlahapdkvg dhypnvdhrl lrdcrtlvla
      241 mitawrwdrd dqfpdglqlg iewlnqlrgk vtaqsg
//
LOCUS       WP_357540986             351 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357540986
VERSION     WP_357540986.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=35600
     Region          28..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 mpparpaglr krwlaagiga vlvalvagvs lgpvslppgs vaaellnllp gvhldsglte
       61 reiaivtelr lprvvlgllv gallalaggc yqgvfrnpla dpyllgvaag aglavtavia
      121 lgvgaggavs gmplaiplaa fvgslgaval tyllgaaggr drspaalila gvavsaflaa
      181 gqtyllqrha eslqqvyswl lgrlatagwh dvrlvlpyfl ftsvvvllhr reldvlsvgd
      241 deatglglhp qrsrylliaa aslgtaaavs asgligfvgi ivphtvrlla gssyrvilpl
      301 smlfggafla ltdvvartaa apaeipigvv tallggpffv lvlrtarrvf t
//
LOCUS       WP_357541058             133 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357541058
VERSION     WP_357541058.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..133
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14132
     Region          31..122
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mterdvagpa gdgtdptgvr aaaeatarev favigtkwal davnalapgt lrfaelrrel
       61 pgishkvltq tlralerdgi vtrtvhptvp prvdyrltaa grglrdvvng mcdwsrrhla
      121 eilaartrsg ptg
//
LOCUS       WP_357541125             168 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357541125
VERSION     WP_357541125.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 168)
  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..168
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..168
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18215
     Region          37..89
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
ORIGIN      
        1 mlgvimdgar repgldtfqg rldhlfqtvr pvgkdrytvr qvsesirknq gveisagyis
       61 mlctgerdnp glqqvealak ffgvppafls ghgdtdavar dlrtlrdaie lkeklqaade
      121 amndpeirtv alkarglsad nlklvnalld qarklegltq tgdttapn
//
LOCUS       WP_357541138             293 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357541138
VERSION     WP_357541138.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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..293
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..293
                     /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=31838
     Region          3..263
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 milprfgnvm isavlpmtvg rwvadltnrv gasqvrqayr llsqimasav dnglipvtpc
       61 rgvklprlpe pnptiltaeh vdrlvaelsp pddvlvlvla ygglrigeal clrrrhvdva
      121 dgrmtvaesv aqlpggpvid tpkshqrrel alpafvvdrl rqhlaelped pdaflfpgrq
      181 qrtagrpqsy ngwkyrfdra veragltdli phdlrathgs wvadshgvlv aarrlghsna
      241 svttrhyara vdgrdaevaa fldrarksgh rsegarngha gesgassgde krp
//
LOCUS       WP_357541144             842 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357541144
VERSION     WP_357541144.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 842)
  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 842)
  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 842)
  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 842)
  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..842
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..842
                     /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=91105
     Region          157..824
                     /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 magrdrsrrr ptdhawlitg plalfavvca titglvsdep sgqwplaaal lvvmvavgvp
       61 vlnfvvrrqs lgvtlteipl vvalfllppl tvvviytias mvtqtrhrlp pakfwfnvak
      121 aaagtalagl vlqalppmrg vgpgtwmilf tavgsvivvs laavvgvhal lqgwqagrda
      181 lrtappallt aaintsmglm iliaikttww svllvavlaa alvlvyrsyv effrqhrtla
      241 qmydltrata khgqdgtlad allgrvralm qaeyatlwlp aqgrhpevll tarvddhgll
      301 dvvrtpgvlr eraaadgrtv avgrafgteq dtlrvttdak vkdvivvplr sgqavigtle
      361 vanrlsdvgh ftqsdvpvfe tvaahaaval ensrlvdrlr hdadhdaltk lpnrrrltaa
      421 vaeavkirap gevvalllfd vdrlrqvnet lghaagdkvl vevaqrlrac tpssalvgra
      481 ggdeflvtlr lesveaalel agqlreqird emvfdaltld vdtavgvavh pdhgsdavtl
      541 lqrvdlaata aksvpgsvql yspalesrsl rrlglagdlc ralddnelev yfqpkvtlrd
      601 rrlvgvecla rwehpahgtv epedfvavae htgqlgrlte fvlreslrrs rdwshgeqpl
      661 svsvnlaart ltdrhfpalv relldeydvp pqrltleite sgvldgterp iptlrrlrdl
      721 gvrlsvddfg tgnsslaqlr rlpvnevkvd rsfvqgmatd pgdlaivnav vtlsqqfgla
      781 vvaegvesel tlellqdigc qigqgflfsr plpyerletw fgaqlepegv vagelprlra
      841 vp
//
LOCUS       WP_357541234             107 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357541234
VERSION     WP_357541234.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..107
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11738
     Region          9..74
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mikkmgyewh lrqlmagrgm fqtsdlvpll aergislsre qvfrlvtqpp qrlsmdvlaa
       61 lcdildcapn dlievkvvnt nvrkaasgvp aaappvrrts irrpgte
//
LOCUS       WP_357541197             245 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357541197
VERSION     WP_357541197.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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..245
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..245
                     /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=26162
     Region          34..118
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mlgclseild eettgllggl plvptgrywv paagngsvar wlartlgpta evvasdidpr
       61 hilqvdglrv vqrddvadgp lpggwdaipi rlfaahtsar rdlihqyaga lrpggvlvdq
      121 ewglwsgfvq hspyadahdv yqhyqealra vfdaqgndan wsveaaevfe aaglvdvrtt
      181 vatrswpggs pgcrlpvvva aelreqlidh gadpalldrl peimhdsetv vignatwttv
      241 gfapa
//
LOCUS       WP_357541241             279 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357541241
VERSION     WP_357541241.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 279)
  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 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..279
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [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]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30120
     Region          1..250
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mirlsgvsrt fdgrsgrvea vrgidldvae gefvailgrs gcgkstllrm iagllpvtgg
       61 eitvggtpit kprrdiamlf qrpallpwrs vldnvllpve ifgwsrakhr drarallema
      121 glggfekrlp helsggmqqr vslcrslige prvmlmdepf saldaltree lsgelqrvhm
      181 etrativfvt hsideavlla drvvvlsprp grirkvvevd vprprtlgrn ahladvaris
      241 adlhellmer nppdvpapag pggavnptqt paragsggr
//
LOCUS       WP_357541254             207 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357541254
VERSION     WP_357541254.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  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..207
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..207
                     /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=22498
     Region          9..200
                     /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 mdfanydpdg anrsreiisa kiviaggfgv gkttlvgais eitplkteal mtaagvgidd
       61 pskvpgkett tvamdfgrit maqdlilylf gtpgqtrfwf mwdeiirgav gaavlvdtrr
      121 itdafapldy fenrnlpyvv alnrfdgapl yeveevreal aispdvplvl cdarqresvk
      181 qvlvtvveha mlrlqaeher gypapvg
//
LOCUS       WP_357541263             369 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357541263
VERSION     WP_357541263.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=39520
     Region          18..305
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mtdayadrlr rvtaqrgcdt vlsgvrpasv heqlatlrsa atedllpdcy geggpveele
       61 rrvaellgte avaffptgtm aqqvalryga eltgrdtvgl hplnhplvhe rdayavlsgl
      121 ravlttgapr nptaeeigal depigtllle lplrdagfvl pgwdelvavv daarqqgvri
      181 hldgarlwes tahlgrsate iaaladstyv sfykslgghs gaalagstel vryarawrhr
      241 yggnlfqqwp aalaalagla helprlsdyv thakviaaal atlpgarvhp apphthqfrl
      301 wlphpaealn aanlalaeee kawfvggwrd tevpgialae vtvagpalel dadqvvdlad
      361 rflrrvsrs
//
LOCUS       WP_357541281             363 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357541281
VERSION     WP_357541281.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   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 363)
  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..363
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..363
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=38780
     Region          74..363
                     /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 msrrsrvprp rtaagrvaga igaavgvaaa glaagvvger llvrrlksdp adpythedfg
       61 aqrydeafql empdgtdihv evveptrpva ghptvvlvhg fcldmgtfhf qrellaargd
      121 yrivaydqpg hgrsgrletg dydlaalgrt lrrvldevap egplvlvghs mggmtimala
      181 elcpelfgdr vvgtvlmats ggalaetrlv apallgrvaa pmlymmsnaa ryggtmidka
      241 rkstsnvawl ltrrygfgte kpspalvsyv eamnsrtsad tvtrylrtla tharypalaa
      301 lagtpvlviv gdkdmitpvt hseeivrrlp haefvkihds ghvvmlehad evnaalagfl
      361 egl
//
LOCUS       WP_357541345             601 aa            linear   BCT 28-DEC-2024
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357541345
VERSION     WP_357541345.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..601
                     /product="type IV secretory system conjugative DNA
                     transfer 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]"
                     /calculated_mol_wt=64259
     Region          167..569
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 msrpvgprgg hddagllvgg iaitalvvas tvwlpitltd apgytgggpi aaatgllrge
       61 irwttactlv avaeaavlvl lvavvllarr airrrrtrvd gaarkmarra elahlgpagv
      121 tesarrlrps lngvdqpgpd etgvligytv aegmplrqsw edmavgiwgp rtgkttslai
      181 paivaapgpt lvtstkgdiv eatydiraar gqvrvfdlqd ifghgqhmww nplrgintit
      241 darrlaehfa agerppnasr dsffdpaaer lvanlllaaa vsgrdilapy rwsvdprdde
      301 palllrehgy dlpaasvtgs lnlpdrtrgg vyagaqglle cltepavsrw vtppsrldke
      361 vlefdpaafv dstdtlylls eggagspapl vaaltdavmh agvlrarksa grrldpplla
      421 vldeaanicr lrqlpsqysy fgshglvvit ilqsypqgid vwgregmekl wsaanvrtyg
      481 ggvaddafle klsrligdhd vttrststsg tgwgqrsvsh sprrqrildl adlhalprgr
      541 mviyvsgarp alartapwkt gpyadavras iarwdptget yqrllddvve pddqtdpeps
      601 p
//
LOCUS       WP_357541379             166 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF4190 domain-containing protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357541379
VERSION     WP_357541379.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10619540
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..166
                     /product="DUF4190 domain-containing protein"
                     /calculated_mol_wt=16970
     Region          <1..>81
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          84..150
                     /region_name="DUF4190"
                     /note="Domain of unknown function (DUF4190); pfam13828"
                     /db_xref="CDD:433508"
ORIGIN      
        1 mqpgypgqdp ygqqppqdpt apqqpqdpya qppaapqygq qptagqpygq qpyqdpyaqq
       61 qpaygaptyp nagypqpqgq qntlglvsmi lgiasiplic clyigipigi agavtgylgr
      121 qkaaqglann dgqakaglic gsigaglgiv lfilgmvanv alptsp
//
LOCUS       WP_357541450             263 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357541450
VERSION     WP_357541450.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 263)
  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..263
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..263
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=26989
     Region          2..263
                     /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 maetitsrdg tilvvdtigq gapvilvgga fndrstvagl gaelasgftv vtydrrgrga
       61 sddrsedyav anevddlaav iahvggrasv fghssgavlv legamrglpi drvavyepsy
      121 qadeslpmps advydrlkal vaagdrdgav elflggvvgv pagavagmra getwpflvdk
      181 apslpydvll stpwqlmpfd rlarigvpvl avygdqtapg laaetkavaa tvpgaalevm
      241 agedhavlqr pavlatilak ffs
//
LOCUS       WP_357541551             318 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357541551
VERSION     WP_357541551.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=34773
     Region          3..309
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mantstrmlq llsllqthry wpgselagrl svsertlrrd vdrlrelgyp vdaargvagg
       61 yqlqagaalp plllddeeav aiavglrtaa ggavagiaet svralakvvq vmpprlrrrv
      121 dalhtytepa ltgggptvda ttltliaqac rdderlafdy tsrdgapttr lvephrlvsy
      181 grrwylvafd verhdwrtfr vdrlsaartt garfrprdlp aadaaefvrt glssiptrhr
      241 vrirveagtd hvarvvgrwa eveadgegsv vtmhvdefdw pvlllaaiga efevlepaef
      301 rehlgrigrl figaagra
//
LOCUS       WP_357541562             199 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357541562
VERSION     WP_357541562.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=21945
     Region          22..>88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mslrspaeqg npygdleltd pkamralshp vrlailsrlq rhgaatatel sehvgatpsv
       61 tswhlrhlag fglvqdsgtg gdarkrywea strgfrfqfp ddeegraasq vlsralfaqy
      121 adapqrwmae ieprlapewr reagvsntgv rltvaelaav naaieqvlap yvtrdaadqp
      181 pdgrhvrfmr yvmpeaeer
//
LOCUS       WP_357541571             232 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357541571
VERSION     WP_357541571.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 232)
  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 232)
  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 232)
  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 232)
  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..232
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..232
                     /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=24797
     Region          2..209
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mklvifgang ptgrlataqa lteghtvtai trqpeafpls dpalevvkad alnpaavdhv
       61 vaghdavist lgvhygstat ttfsesatni vaamtthhir rlvcvtstgv pmkpppgetl
      121 vyrkvivpml lrmgrplyed agrmedtvar sdldwtvirp sglfngpavt dytvgppqmv
      181 grftsrrdla daliretvdn rnvrsivevi ttqgtpgvyr vflkealrig na
//
LOCUS       WP_357541718            1051 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357541718
VERSION     WP_357541718.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 1051)
  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 1051)
  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 1051)
  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 1051)
  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..1051
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..1051
                     /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=113443
     Region          3..1045
                     /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 mielplspaq erlwfldrfd pgqpnnvafa rrlhgpldpd llaralavvt trhealratf
       61 verdgapvql iadpgefdle rvdlsaepeq lredrareig wdyfdtrfdl aagpliraal
      121 lrfaaddhll vivvhhvvfd gasqailiad lgiaygallt gtepaftplp vgwgdyvreq
      181 adqppgkteq dlaywrerla dapaltlptd lprplfktpr tervhhriag dlagqvqrla
      241 rsqrctpymv lltawqlllg rhagqsdvsv gsasagrsrt eleplvgcfv htlvmrgdls
      301 gdptvaellr rtrttaleay ahqqilferl vgeldvardv srtplfetmf ilhtqdspem
      361 dilpgikgap fsigitqvlf dlvldawigp gmlalslryd tglftpdtvr aflqryevll
      421 ramiatpdar lselpmddva gqrqvlawgq gprrrysgtv pglfaaraaa hpdapavddq
      481 tygdldaran ritrhlaglg agpgtvvgic ldrgpdlvat llavwrcgaa ylpldpnlpa
      541 arlswlrada gathlvtrrg vtpdldpagy ahvvdladdp aagepadave prydpqglay
      601 vlhtsgstgr pkgvevshaa ltnlllsmrd tlgsgpsdvw lgitslsfdi sglelylplv
      661 tgarlvlvpe dslrdgvavv riahdnavth vqatpsgwrm lldagfntpt vtaltggeal
      721 pprlarelrp rvrrlvnvyg ptettiwsta geiadaasei tlggplantq lyvvdaalrp
      781 vpvgvpgell iggagvalgy rgrpeltaqr fvpdpygppg arlyrtgdrv rwlrggklef
      841 lgrvdhqvki rghrielgev earlsghpdv hlaavltage ghdarlvgyv taapgaepss
      901 rqlrahlaee lpaymvpgqi vvldamplnt agkidrrnlp aaeagdlevr eyvaprtele
      961 emvtatwgev lgreqvgvld dffdigghsl latrvvarlg aalglevpir vlflhstaet
     1021 faaaveellv adveqlsdde veslldggva r
//
LOCUS       WP_357541725             181 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357541725
VERSION     WP_357541725.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 181)
  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..181
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..181
                     /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=19233
     Region          2..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marsvpethd eilaaaarrf avtgykgtsl qdiagevgcs katvlyhfan kealltelma
       61 paiavleald ariaghagad aqrvaaegfv dlavrfrrei allrgefpdl lqqpafahiq
      121 qiserligaf aghsdrpsar iaalvvlagi aetcaefidi pdeelrpall avvrralept
      181 t
//
LOCUS       WP_357541778             669 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357541778
VERSION     WP_357541778.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 669)
  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 669)
  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 669)
  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 669)
  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..669
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..669
                     /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=72157
     Region          116..658
                     /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 mpaalppgvp davlqvmgsa lltttdgavd wcneaavrlg qaigtdlrtl platvtpdgp
       61 srelpcpvpd gkphylrvtc rqlprrddvg pellyevadv taaradrara dnyewrlkhi
      121 eelskvgtwe wdlatndviw sptllsmfgl pagstldypa yramlypddv tmiestlaaa
      181 lerpapfsyt hrmyladgrt lrvfecygev ftdaggapar vlgtahdvte vqrvqdelty
      241 ladhdpltgl pnrraltaai sgaaaqgrag gtlllidvdn fkdindlrgh gvgdevmrll
      301 arlltshlpa gavvgrlggd efavlldgyd paaamavagr lcdlvartpf avrgeplrvt
      361 lsigaapfep gddhdlllah adlalyqakd egrnrarlfa peqhrqaaqr vgvvsrvrra
      421 ldtgrlelda qpiidlsdlg vhsyellvrv rdghlpelep adflpalerg dmvceldrwv
      481 vetairalar ataagvalrf dvnissrsle dpsfgdwvvh alrsagvpat rlgleitett
      541 aianlhdarr lastitsagc gfslddfgag ygsfvylkhl pfttvkiage fvrhadhggp
      601 dpilvdavvr aahglgmytv aehidrpelv gvlkmlgvdr gqgfhlgrpq rlddlmrrti
      661 pldaatgvp
//
LOCUS       WP_357541800             304 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357541800
VERSION     WP_357541800.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..304
                     /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=31644
     Region          1..134
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
     Region          164..293
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 meerrrigay gvlrdewgrv llargaagcp ypgvwqlpgg viehaehpet avvrefaegt
       61 gldvevttir aavadvavvr dagvalhtdr lifdieargg alrpepaggs delgwctpdd
      121 aagrplmpft aellgipvsp lpadlpralp papaaaptad rrqrfaaygl vtdpagrvll
      181 tmiadgypga gswhlpgggt dhgeqpaagl lrelveeagq lgrvvdllav dnlhnpaalg
      241 pegrpldwhg vrviyrvrvd aptdavvtel aggstaaaaw fapeeidglp mtdvavlatg
      301 hrsg
//
LOCUS       WP_357541827             332 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357541827
VERSION     WP_357541827.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=35234
     Region          20..309
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mpptpqplap hevqgfaala trlagnvgsv vlgkpdvvrl altalfaqgh vlledvpgvg
       61 kttlaravaa svhgqwrriq ftpdllpsdv tgvtifnqgt rgfefhpgpv faniviadei
      121 nraspktqsa llevmeertv tvdgvrhpvp rpflvvatqn pvemdgtyrl peaqldrflv
      181 klsvgypdea veievlrgat trspealepv tdttavgemi rmaqrvhiad plyayavrla
      241 aatrdhprvr vgvsprgvia ltraacayal vdgrgyvlpe dlkallgpvf ahrillsada
      301 qlhggtatei lddvvrsvpv plpagqlaas ga
//
LOCUS       WP_357541918             516 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357541918
VERSION     WP_357541918.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 516)
  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 516)
  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 516)
  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..516
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..516
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54154
     Region          33..>239
                     /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 maesvadlar psheepgpag appapgpray gpwlvaggvi vtllilsnry gyhrdelyfl
       61 iagrnldwgy vdqgplvpal arladtvapg nlvalrtpsa fiaggcvllv aalarefgag
      121 rgaqtfaafl agssglvlas ghllstttvd mlvwlaaalc aarllrtgdt rwalgiglvl
      181 gagmlnkllp allgvgllag vaiagprrll rdrwvlagfg valllaapsl vwqathgfpq
      241 lsvaasisgg dssysgrlda lalqfviisp yavpiwiagl vallrrpqwr ayralawawl
      301 vvvavvllag gkgyydapll lvltaagaiv taawatrras vlrrtllvag allfvapngv
      361 lllptlpadr lpgfvvdvny dagetigwpa fadslatvhq alpaeqrqra viltanygea
      421 gavarygptr glppaysghn smadfgrppa dadvviavgw nrpdqlrewf ttvslagrvd
      481 qrvdvdnden ggpiwlcvgl rrpwadiwqa evrhag
//
LOCUS       WP_357541942             232 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357541942
VERSION     WP_357541942.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 232)
  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..232
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..232
                     /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=25342
     Region          1..225
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mptlvghrga ptrrlentvg slllardqga eavefdvrat rdghpvllhd rtlerfwgrp
       61 elvgeltlae lrelraaeep earlptlgev adavdlrlvv dgkdpdlvpt ivevlrrhda
      121 larscfigep gvlgevrrvl pdaeiilswa gerppppell dtirpaalnl rwaglsdety
      181 ravrelghqi wtycvddatq arralrlgid avitndlpav apvlagvaev gr
//
LOCUS       WP_357541943             400 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357541943
VERSION     WP_357541943.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 400)
  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 400)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..400
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43149
     Region          26..399
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrillvgagg vgsaavaiaa rrsffetmvv adhdparasr aiagrdsrfv aaqvdasste
       61 avaalcrehr ithvfnavdp rfvmsifdga faagadyldm amslshphpt apyaetgvkl
      121 gddqfaaasa wvkagrlalc gigvepglsd ifaryaadel fteideigvr dganltvdgy
      181 dfapsfsiwt tieeclnppv iweadrgwyt tppfsepevf efpegigpve cvnveheevl
      241 liprwvkakr vtfkyglgde fievlktlhk lgldavspvr vrgvevsprd vvaaclpdpa
      301 tlgdrmrgkt cagtyvtgig vdgrprkvyl yhvvdnewsm reyghqavvw qtavnpvval
      361 ellatgawsg agvigpealp pvpfldlltd ygspwgmeer
//
LOCUS       WP_357542053             424 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542053
VERSION     WP_357542053.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=43706
     Region          197..420
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrvggmlgpl vqgstwrrav flllggvlal pyallaaafa qilavddvpr avvfglllva
       61 vvlaavpvfl sgsraleiaa arallavdlp epaaghridr etrvraalwi alhlftgglv
      121 lfaaisafpm alvflagpfg vdpgavpddg fgalianpvg atltgvvllv glgyavaglg
      181 alaasmapvl lgpsqgeria aleartvrla ernrlarelh dsvghaltva tlqagaarel
      241 ldadpefarr alraieetsr hamddldhvl gllresedag rpaptapqpt ltrldrlvad
      301 traaglavdv rvsgavgelp aavsregyri vqegltnaar hgegavtvrv avpaqaaaps
      361 escrgleiel vnglrggtgp grggrgldgm rervlllggr ltagpegerw rvraflpvpr
      421 geag
//
LOCUS       WP_357542054             261 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357542054
VERSION     WP_357542054.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 261)
  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..261
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..261
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27010
     Region          1..259
                     /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 mtefvtsadg triasdiegd gppviligga mqfrafdpdt vqlahrlaar gftvvnydrr
       61 grgesgagsv galeseiddv aalvarvggr aalygsssga vialwaaqag vgvtrlalwe
      121 aplalegqgd ggetlrglre riaagdhega veffmrdmpp ewlagakagp awpvmvgiap
      181 slvadaaalt raqeapwarq wsavdvpvla ivgertlplf ppaadalvta lpharrvtvp
      241 gtdhgwelda mtdtlagflt n
//
LOCUS       WP_357542066             478 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357542066
VERSION     WP_357542066.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 478)
  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   2  (residues 1 to 478)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..478
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=50006
     Region          19..473
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mtdvmaspra grvrgvrrdg iasfrgipya aapagplrfr ppvpvpawgg vrdagsfgva
       61 ppqlppgpga psawrpadgl dclslnvwtp dpgagglpvm vwlyggafkh gsagrpdfda
      121 tvlasagvvv vtlnyrigfe gfghipgvpd nrglrdqiaa lewvrdnvta fggdpanvtl
      181 fgqsagaast allmtapaar glfrraiaqs ipdaclspae arratavlag aagvaatwed
      241 laglspeeil rhqdaplpep atggsaftpv vdgdlvggpp wrrlrdgagr didlicgfth
      301 dearlytsav paaaidlpaa aaalrlpera vadyrtaypd rtdpelltvm msdalfrmpt
      361 trvaeahtaa ggrtwlydlt wqsprlgach ildvplafgn aasplaarll gtppppgfae
      421 lsaqirtawt sfaatgdpgw prfdrergtt rswnvpateg ayplpasrri wldvvpte
//
LOCUS       WP_357542097             773 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542097
VERSION     WP_357542097.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 773)
  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 773)
  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 773)
  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 773)
  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..773
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..773
                     /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=82073
     Region          103..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 msgrepeqsf vpqqdasrav tavarrplsg rvgpvaaalv vlgeaswlia glpgaalvsd
       61 lgamavsswa afacaraarr hppplrlfwt lltvtmalag vgrilwtvar lggpglpntp
      121 lvggiftagi vtgtaallcs laaprslvgq artlldgviv glalipigwv vvfrdiaaad
      181 ladplrtfgl lypmfdlmql tilvavaapa rprwralali gvslgirata daiyvslvah
      241 gsyapghpid vwwplsylli gaatgypppp gweeteette splppwwrva mpylpvggai
      301 vavvlarqpt gqsphlifva mmallgvlal rqglaanenl rlaarlrrla ytdqltglan
      361 rltfnrrlrr alraggpvav llldldgfkq vndrfghaag drllttiaer mrdavgddgs
      421 iarlggdefa vlidgdrvsp eqlaqrllva leplpgeedl gahpsasigi aeygpqhash
      481 tdllrdadia myaakaagks ayqtctpglr esavsraeli adlrravdeg qllmefqpiv
      541 dlatgtvrsa ealvrwrhpr lgvlpparfl plaeetglil aidrwvirqa craaatwrph
      601 apevtvavni aaahlqrpdl iatvtgatsa aglapraltl eltesalieg sevvlerlhq
      661 lrelgvriai ddfgtgyssl sylhripate lkidrsfvsr ldagdpraya tvemvnrlag
      721 afdlavvaeg vetgtqheav taigclhgqg wrygrpatls ellamlapid aar
//
LOCUS       WP_357542108             248 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357542108
VERSION     WP_357542108.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 248)
  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..248
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..248
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=25197
     Region          3..245
                     /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 mvhevrvrgg gsghrvllll hgmgatgavw egwrtplasg wpgrwlapdl pghgraapls
       61 gypypavaae vaaalgpgdr vvvlghsygg vvglalagag vgveavvalg vkvtwtpdel
      121 armtaladrp vtwfpsraea aarylrvsgl aglvdeagpa vdaglverdg rwrlamdpaa
      181 favdapdmpa llagcrapvv largehdpmv gdaelaalga ptatlaglgh nahvedpaav
      241 ldllapyr
//
LOCUS       WP_357542154             280 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357542154
VERSION     WP_357542154.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27160
     Region          40..258
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mttatgpgaa dgdpnaaaga gaapagnada rpgpaetgll agrrvvvvgg asgiglattr
       61 aaaaagaava vldldgdgar aaaaqagpea ygyqlditde aavaatldra aadlrgidtv
      121 lhvagimrgq gldvrevtvd lwarviaanl tgpflvakha aghleaaggg vlvfvaskag
      181 ivtgsgsvpy gaskgglhgl altlarqlrp rgirvhtlcp gdidtplmrr sldeaarnga
      241 daagvarvra glgrpedvaa vltllaapaa daldgtvyts
//
LOCUS       WP_357542239             227 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357542239
VERSION     WP_357542239.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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 227)
  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 227)
  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..227
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..227
                     /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=22821
     Region          17..227
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrarlalatl atalvgvvaa psvataapvg pdpiigggtv ssapwaaavf sngsftcsgs
       61 viaanwvlta rhcvsgtmsv rigsvnrtsg gvtrnvtasy gqydlallrl nspvtsgavt
      121 lsnsyppvns tntifgwgmt cysgcsastv lktasvrvts tsvtdayggr airstringn
      181 awrgdsggpq fyngaqvgva stadgvniqn ygsvaynraw itsvagv
//
LOCUS       WP_357542204             205 aa            linear   BCT 28-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357542204
VERSION     WP_357542204.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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 205)
  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..205
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..205
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=22340
     Region          1..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 mslrvlayge rallievadh healalyddi rreppvgvvd lvsaaasvlv vfadeesaqa
       61 asstlrtrsv prvdravgdl vevpahydga dlgevaeslg msveevvrrh eiaeylvafv
      121 gfapgfaylt gldpalhmpr rsvprtrvpa gsiamageyt avyprespgg wrllghttld
      181 mwdldreppa llqpgmrvrf rrvtr
//
LOCUS       WP_357542266             362 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357542266
VERSION     WP_357542266.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..362
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36533
     Region          53..358
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mnepnlrrgr tplvvaaavv vaaaagvaia vgadghpggt aasgglppgt aqvtrqtlvd
       61 tesfdgtlgy gathtatari pgtvtsvaat gsqvsrgkpl fsvdnekvvl lygrlpayrt
      121 lgpgmsgadv rqlernleal gytgftvdne ytsatatavr swqkdlglpe tgrvelgrvv
      181 yadgavrvns qqadrgdpaq pgqavltytg tarvvtvdlk vdderlakrg akvsvtlpng
      241 kqvpgtitdt etvidtgsgg gpgggsdpet kievtvtvad pkaltgfdqa sakvaftaae
      301 rpdvltvpva allalaeggy gvqlvegdst riiavetglf aagrvevsga glaegatvgm
      361 pt
//
LOCUS       WP_357542272             415 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542272
VERSION     WP_357542272.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  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 415)
  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 415)
  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 415)
  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..415
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..415
                     /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=44211
     Region          70..395
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkrltirarl tlvhggllll agtillgvty vlvdqrlrqp lngifaraqv vpttpygqlp
       61 spggaaeqvr vliqetqdea krtalesllt qgglalllis avalgfgwli agralqplhq
      121 itgtarriaa vgaagrglhe rialhgpqde vkeladtfdl mlerldrsfd gqrrfvanas
      181 helrtplaln rsllevamsr pgapaelrql getllavner herlidgllt ladseqqvvd
      241 rtpvdlaeia ghvldqaagt aeptvrrwla paptagdpvl lerlthnlve navrhnlpag
      301 geievstgtv dgrvvlvvvn tgpvvptydi etifqpfrrl rhervavrrp ddragaargf
      361 glglsivrav aqahggavha qprnggglvv tvtlpslgam vpaqparvlp aatyg
//
LOCUS       WP_357542310             213 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542310
VERSION     WP_357542310.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 213)
  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 213)
  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 213)
  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 213)
  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..213
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..213
                     /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=22708
     Region          4..213
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mssivvfgag gtagsriaae averghrvta avrrpeatsy lpagvrtvtg datsarsvre
       61 laedadvfvv aigggerelw rdaartlvdt lrelpdpprv ihigggatll tskgtpylde
      121 pdfpeeyrda algqadalav yrssadgvtw tyvsppplef hpgertghyr tgtdhpvtda
      181 qgrsvltyed lavaivdeie nprfdnarft aay
//
LOCUS       WP_357542376             393 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542376
VERSION     WP_357542376.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..393
                     /product="phosphotransferase 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=41934
     Region          <151..330
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mitlvlvdda gaplgalppf evpepwwqqv gaivggvrhh hgvdvavlrl laadrpeppg
       61 ghltylgqvt tppavplepv svdlsphplr apwaqpggpa rslawaagel hrlgrpvtat
      121 aqhrtwnlsa iwrldgehgs awlkqvpgff rheaavlrwl attvpgtapa llaaddtgri
      181 lldhvpgedr yaaddaeraa iaadhhvlql ravdhadalv aagvpdlrgp alaawirrwl
      241 aphdvsvvad lladlderld qvrdcglpdt lvhgdlhpgn vrgdgrrqav idwadsfvgh
      301 pafdilrlte tlapsaaapl ldawaarwra dlpgsdpera vdllrpvapl rlaavyamfl
      361 agiepsehpy haadvpaclg raaaeadrvc lpd
//
LOCUS       WP_357542363             276 aa            linear   BCT 28-DEC-2024
DEFINITION  PhzF family phenazine biosynthesis protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357542363
VERSION     WP_357542363.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..276
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=29254
     Region          3..275
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 madvftevpl egnpvavfvd padlspermq qiaqemhlse tvfvlpaedd gdvrvriftp
       61 vnelpfaghp tlgtaivlge snpaprirme tamgtvafdl eragggragt asmwqpiptw
      121 epydradell aglglaasac tlpvevyrng prhvfvglgs vatlsavepd qrilarlpdm
      181 aancfagsgt rwrlrmfspa ygvvedaatg saagslavhl arhglipfge wieirqgvei
      241 grpstmrara tgtperiesv qvagsavvva rgtlya
//
LOCUS       WP_357542393             401 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357542393
VERSION     WP_357542393.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 401)
  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 401)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 401)
  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..401
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..401
                     /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=42946
     Region          145..401
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mepfalapaa erlqtvfrtr pwlldtavav lvvvvgaisr ptlsfitwsq tvytlivvgc
       61 aaalvfrrlf prpgltviai lllghlvaai epglcvalic liaayttqtq ltppwrwvfl
      121 aaiyggtvaa imtspipavd vrgrlivtgv vltlltlaal tgvirrqrrt rytlaveran
      181 mleaqqdadr rlaaveertr iaremhdilg hslnaiaaqa egvryvlrsd adradqalad
      241 igwlsrravd dvrdlidvlt tdaaqtsvlp tpslgdmpel iaslrytkaa irlqfdgdvd
      301 avpghvglaa yrivqesltn alkhadgvpi tvrvtvqdrh vevavlnpra pavplpgtaa
      361 ggrgiigmre raralggave agpdpatggw rvratlprsr a
//
LOCUS       WP_357542427             698 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357542427
VERSION     WP_357542427.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 698)
  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 698)
  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 698)
  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..698
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..698
                     /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=74829
     Region          12..688
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mrvggggter vdrqvrlerr lvdamyarld savadglaar drvlaapved aqdlyvrdve
       61 iarltrtvhe lraaerslcf gridsaagts ahigriglrs qdgalllldw raeaarpfya
      121 ataasplglr rrrhlrldgr kvvdvsdeil dgssptpvdv vgdgpliatl gsartgrmre
      181 avatlqaeqd aivrsphsgv svvdggpgtg ktivalhraa yvlhafpala krgvllfgpn
      241 rrfldyisdv lpslgendvq matiadltgv epssiesdaa alvigqaqva valarwvrnh
      301 qprgvpldir vgqetlvldp etvddahrha tqgglahnpa relfkehlvd dlvnllerrt
      361 tetltemddd vatslgidld ravaedlrai glddtvattg daeidwegvr dgllddpgvd
      421 lavervwprl raadalqgll gdraaltall palsgdeiav larsraggnt ssdlalldea
      481 ralidgppeq lyghivvdea qelsemqwrm lmrrcptrsm tvvgdfaqag sattirswte
      541 avgpfigerf ahhtltvnyr ttaeilhatt allariapeq qpsrsirhge hprtllvtda
      601 rldaalrelv eqaaaahpge ligiigpsdr varlttaldg tgavtvaaae arglefdtvf
      661 vidpaaieda rtggardlyv artratkrvm tielssdp
//
LOCUS       WP_357542436             412 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542436
VERSION     WP_357542436.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=44455
     Region          1..405
                     /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 manllgmvlf alailisvsl heaghlltak afgmkvtryf vgfgptlwsf rrgeteyglk
       61 giplggfcki vgmtpqdddv epadqhramw rypvwkrtiv msagsithfg laliaiwlaa
      121 mfmglpnkal egpvaayvkv tscvvpsedq recqagdpvs paklaglrdd dqilaingta
      181 vatnmdlikq iralppgpat iryerdgvsg evhadlapvq rrpldnpkgd pttvsalgve
      241 implppgvpm ivkhgpvdai gattdytgkl avgtyesmkr ipqkvpalwt aitggeravd
      301 tpisvvgatr lggeavqhna welfvslfig lnffigvfnl lpllpldggh iaiswfervr
      361 swiyarlrrp dpgrvdylkl mpityavili ggaftlltvt advvnpitlf sr
//
LOCUS       WP_357542466             374 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357542466
VERSION     WP_357542466.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 374)
  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 374)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 374)
  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..374
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..374
                     /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=39011
     Region          127..373
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mssarigard wlvaagvavi llaigvsghr dttggqgved llgllllaag glalawrrra
       61 pvavlaatgl calgyqaagf dvfavaylia vyaavragrr tvtvavsvam laalpavtmi
      121 tgpydtaaaf arsrgvlela wliaagaage alrqaerrad eaertreena lrrageerlh
      181 iarelhdslt hqisviklqa evavhlarkr gepvpealla irdagreaar elratlealr
      241 ddstaapgmd hvpqlvqrar tagldatlti agdradipaa vdrtayrivq ealtniarha
      301 aaatasvrid clpgkvvvqv dddgtatpds apapgvgllg mrervtalgg rlraeprdsg
      361 gftihaelpv ertp
//
LOCUS       WP_357542486             238 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357542486
VERSION     WP_357542486.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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 238)
  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 238)
  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 238)
  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..238
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..238
                     /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=25348
     Region          1..222
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mnfdglrvav tgavrdtgrl laeafadrga yvclsarnla aaeqaasvin qrgpgradaf
       61 rcdlaepdsv rafaaavadr teridvlinn gaayiegddl thapddkien vmaaggtgtl
      121 lltkhllpll rasarpdivn misacgetgh rrsgahpafy aakhahagla eilshrlrpe
      181 girvislfpp dfvqdgprqa sgdltarsvv dcvlfavgqp rdcfirefhf eqvqpsrg
//
LOCUS       WP_357542522             145 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542522
VERSION     WP_357542522.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 145)
  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 145)
  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..145
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..145
                     /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=16485
     Region          1..144
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mddhvpealr avedeltall rrgralswev arevhpnlep ntyglllwlr rsgsirltdl
       61 atrlgvgkgt lsrqiagleg lglvhrdpdp tdrraaqisl teegsrrfda artarfeqir
      121 htmgnwperd vedfarllhr fnehf
//
LOCUS       WP_357542594             236 aa            linear   BCT 28-DEC-2024
DEFINITION  sirohydrochlorin chelatase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357542594
VERSION     WP_357542594.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..236
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=24014
     Region          1..221
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 msrplvavsh gtrdprgqaa iralvgavrr rrpdldvrea fvdvqapdlg avldragpaa
       61 vvvplllapg yhvhvdvara vaaagavaap alapddgiaa vlvdrlrgcg agtddtvvla
      121 aagssdvrar paveetacrv aalwgapvev gclggtgepl havlarsrrp rrrvvcaaml
      181 mapgffhdrl rsagadlvtg plldgrrpdp rlvglvvery eaalaatlag sgvisg
//
LOCUS       WP_357542617             197 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542617
VERSION     WP_357542617.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=21602
     Region          9..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 mpadfsvkpt ltgdrvvlrp fvdddiaafq aiasdpevar ftgsppgeaf dlgrlrawyg
       61 trnsqtdrld lavvdratga cvgevvlnew dghnrscnfr tligpagrdr glgteavrli
      121 vgygfeqldl hrislevfaf nprarrvyek vgfvaegtlr qvlrdgdhwv dasvmsilaa
      181 ewaahrghpe sgkrdrg
//
LOCUS       WP_357542659             204 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357542659
VERSION     WP_357542659.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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: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=21135
     Region          4..203
                     /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 mhlvevplvp eirlhlaeda ivwwarmeae agrslaapyw asawaggqav aryvldhpet
       61 aagcrvldla sgsglvaiaa alagasavta tdidpyaiav ialnaaangv avdvsgrdvl
      121 dtdgdgadlv lagdvfydps madrmlpfld rvvarggrvl vgdpgrgtlp weslevvasy
      181 papteaafad aelartyvlr lsrs
//
LOCUS       WP_357542628             349 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542628
VERSION     WP_357542628.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 349)
  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 349)
  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 349)
  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 349)
  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 349)
  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..349
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..349
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37436
     Region          25..321
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtdisdtlts vpspadadag gveleqtlfe vkrvivgqdr lverlltali adghcllegv
       61 pgvaktlaaq tlatvvggtf sriqftpdlv psdivgtriy rassesfdve lgpvmanlll
      121 adeinrapak vqsalleama erqvsiggrs wpvpepflvl atqnpieseg vyqlpeaqrd
      181 rflmkvvvdy psdadelail yrmscdrptp rpvldparlr elqrrasqvf vhhalaeyvv
      241 rlilasrdpg rfgladiapl ltygasprat lglvaaaraq alirgrdhvl pedvrdlavd
      301 vlshrlvlsf davadgvsad avvrrlveav plprvvagrp etasdlaaa
//
LOCUS       WP_357542669             439 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542669
VERSION     WP_357542669.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 439)
  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 439)
  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 439)
  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 439)
  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 439)
  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 439)
  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 439)
  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..439
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..439
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49116
     Region          2..419
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 msfrfanhrs frdeqqlnlt payrsdehep avrvvgifga nasgksnclh alafmrrfvi
       61 fsdrevepgl gvarepyrmt pdsleapsqy vvdldlsgvr htygytldnd gvleewlyhy
      121 prkrkrrvfe rtgdsytwge dsgqrvgler iaevtaptal flstiarfdh rhtapggtep
      181 eplrdtyqwf qkmhsrsqph lgnrlngiyg agwpesdasr rtlvellraa dvgivnvvev
      241 tsavtdeqpi lfrpsdlepg nertmtrnrr rerkrlrfah qgpagevqfe laeestgtqq
      301 llglaieaad vlsgggtmcv deidaslhpl ltakliglfq siasnprhsq liftshdaal
      361 lgtidteeil hrdeiwftek gadgastlyp ltdfkprreg enrqrrylng nygavpdlst
      421 hlfeqalaar ggaddaaar
//
LOCUS       WP_357542677             427 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357542677
VERSION     WP_357542677.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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 427)
  AUTHORS   ter Beek,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..427
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..427
                     /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=46053
     Region          1..337
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkrswthwar aatvgavslv mvaacsgkst tggsdsgdgq itlkinfwgd fglqdlktky
       61 eaehknikiq lnsgeynaqh edlqkklvag sgaadiaaid egfvvqfrsq adkfvnlldk
      121 gagsyeskyl pwkwkqtlsa dgktqiglgt dvgglamcyr tdlfqaaglp tdrdqvsalw
      181 ptwdkfievg qqytaktkkk fvdsatnmfn pilgqqpvgf yndqeqlqmd ggpkvafdya
      241 vkgieaglsa nlasfqadwd kgftsgsfav lacpawmlgh ikdtapgtag kwdiaavpgg
      301 ggnwggsflt ipkqgkhvde aykllewlvq peqqieifkt vgnlpsqpal ysdpaiadfk
      361 npffndapvg qifpkmaagl tpqylgkkng ptrvevenvi grvqnkslkp daawaeavka
      421 aekvans
//
LOCUS       WP_357542706             278 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357542706
VERSION     WP_357542706.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=29095
     Region          3..259
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrrilvtgag grignylrer lprpdralrl ldvgpqappa pgepvevlra dltdagavaa
       61 acagvdavvh laalrgedtw enilrvnvdg trtlleaari agvprvvlas sihaagfyrr
      121 agaapepsgv papagpdgvp sgsvprpdsy ygwskaaaes lgslyadrfg mtvfalriga
      181 ctttpaawnr dawlspddca rlvdvclttd atgfrvlwgv srnrdrwwsl aegaaigydp
      241 vddaeaytag mtpmddahap tvgllggtfc tlplgkpr
//
LOCUS       WP_357542735             257 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357542735
VERSION     WP_357542735.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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..257
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..257
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26842
     Region          5..251
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mgefvrlevk dgigtirler ppmnalnvqv qeelraaata atadaevrav ivyggekvfa
       61 agadikemad msyvdmvdra ggissslgai agipkpvvaa itgyalgggc elalacdwrv
      121 vaedaklgqp eiklgvipga ggtqrlarlv gparakelim tgrmidaqea lrigladrvv
      181 paaevyeaav alvkpfltgp aqalraakla idgglemdln sglawesqhf aalfatddrr
      241 egmaafvekr kpdftgr
//
LOCUS       WP_357542742              99 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor
            [Polymorphospora].
ACCESSION   WP_357542742
VERSION     WP_357542742.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 99)
  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 99)
  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 99)
  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 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   5  (residues 1 to 99)
  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 99)
  AUTHORS   Rosinski,J.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..99
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..99
                     /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=10418
     Region          15..88
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(17..18,20,23,26..27,30..31,34,64,83..84,86..88,
                     90..91)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(18..19,23..25,38..40,49..52,54..55,58..59,61..62,
                     68..70,75..77)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(38,41,83)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mttgngyeay egagellral sapirvaivt elaggercvh elvetlgapq plvsqhlrvl
       61 rgagvvrgsr rgreiayalv dehvahivad avsharear
//
LOCUS       WP_357542801             257 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542801
VERSION     WP_357542801.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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..257
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..257
                     /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=27472
     Region          11..239
                     /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 migdvhppas ldvrgvryay pdghvalhgv dlsvargdrv allgpngagk ttlvlhlngi
       61 ltptegtvsv ggltisrdrd tlaeirrrvg ivfqdpddql flptvaedva fgpanlglrg
      121 aelaarvdea laavgmsehr draphhlsfg qrrrvavatv lamrpeilvl depssnldpa
      181 arrelaeilr alpvtllmvt hdlpyaaelc drsvildagr ivadaptpdi ltdesllakh
      241 rlelpygfdp rtaarpc
//
LOCUS       WP_357542747             332 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357542747
VERSION     WP_357542747.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 332)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..332
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35783
     Region          5..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msavieisgl rktfhtlrqg rhvavdgfdl lveagqvhgf lgpngsgktt tlrallglvr
       61 adggrmsvlg adsperlpev agrvgaives pqffgnftar rtlrllavag gvptsrvdev
      121 leqvglrdrg eervkgyslg mkqrlavasa llkqpellil depangldpa giremrdlmr
      181 slseagvtvl lsshilaeiq licdhvtiis rgrrvahgrv devlagfdqh ewqvrvaepe
      241 ravellgqag lsvtaqpdhl lvagvdepel isrtlgeqgl wvrelvplrp dlesvflelt
      301 gstphpsvpr qldgpddvvi dldvrenrev ga
//
LOCUS       WP_357542821              98 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor
            [Polymorphospora].
ACCESSION   WP_357542821
VERSION     WP_357542821.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 98)
  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 98)
  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 98)
  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 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   5  (residues 1 to 98)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..98
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..98
                     /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=11008
     Region          6..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 meanpdlfka lgdatrriil deladrdgqt lfeicgrltm khglassrqa isqhlavleq
       61 aglvhtrrqg rfkfhhidts plrsivarwp idreepnp
//
LOCUS       WP_357542831             900 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357542831
VERSION     WP_357542831.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 900)
  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..900
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..900
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=97691
     Region          9..900
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          562..589
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          602..629
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          643..669
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(645..646,649..650,652,682,685..686,689..690,
                     692..693,716,725..726,729..730,733)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          680..710
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          715..749
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          761..789
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          794..830
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          841..869
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mavspggdgr pdpaaastaa efvealrrlk swsgvgfrrl esraaaagrm lprstvtaal
       61 ardtlpredl vvalvrtcgg ddeevhrwvt arrrlaalrp apvaepapgp aparctlpad
      121 qavfvgrdke ieqivstvad atragevvsi haidgmagvg kttlavhvah rlkdrfgdrq
      181 lflslhayts grhpadpadl ladllaadgv darflpptld graalwrdrm ngrrlllvld
      241 daastnqvlp llpgtpgclv lvtsrrilad lpapvpigld vlspdeaatm farlaardag
      301 revaelvhac ghlplaisim aslyrrhrsw tiaelrremr qpagglltlt aehrtvaavf
      361 dlsyqhlpag rqrlfrllgl hpgvefdgya vaalaglpvh eaglhldelq rdhlleepay
      421 rryrmhdlvr shavhlttaa dppetraaat grllayyrda aalavsvtdp herrrrrttp
      481 adsplpdlpd aghagrwlkn elanlltaaa hsgpdrpepa wemsvllhrh lrthgqyqea
      541 eslhqhsldl arlagnqeae tdalidlgyv hraqgrhela eehyglalri aqrrgdrsge
      601 lyaqhglghv nwmrgnners aihygrslai aaeigdrgge laalnglghv gmllgqyeqa
      661 enhyrralri agdlgdrsge lqaltglgvi rlklgeleqa lrhygealri aqdsgnrage
      721 lyalhglghv rwllgqhepa aghqtralri aqeigdrtge lqalvglgha hlaqcrfapa
      781 decyeqalrk grelgsanwq fealqglgrl rqamgqpava lvqhrqalrh atglgqlpdq
      841 arahdglaha ylaigdrela gkhwqvaldl laklgtdhtd daqttgprir aqlaelrggr
//
LOCUS       WP_357542913             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542913
VERSION     WP_357542913.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30858
     Region          36..295
                     /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 mrsfrwpppp dggprtwgpg pgaprtgrpa lpepetelva tphgvglerl vtgvgapvtv
       61 fahglgsgia ttrpfgsavt grkiffqfrg hgrsdsppgp wtyldlardl raiadlggat
      121 rafgvslgag alcrllaesp erfeklvffl pavldtprge tararlsnll davadgdaaa
      181 ladavslelp pdvrdtpagw aylrqrldql lrdglapgla slpeqaplrd agalaavtap
      241 alvigcagdd lhpvavaeql aaalphatlh vydrpgvlwt eradlreris tflng
//
LOCUS       WP_357542917             188 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357542917
VERSION     WP_357542917.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  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..188
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..188
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19360
     Region          4..>65
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 matskdlpdv ggfirdlrrn akislrqlae qagvsnpyls qierglrkps aevlqqlasa
       61 lrvstpamyl raglldakeg qgvlaaiavd peltmaqkqs ltqiyetfrr enarlaeata
      121 aaqaatepta rasapseapq apatvtpaat gpttpggspt eavlesvavt eagatpaptt
      181 avpdeees
//
LOCUS       WP_357542919             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542919
VERSION     WP_357542919.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   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 265)
  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..265
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..265
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28116
     Region          4..264
                     /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 makievngal laydeagsgs pvllvhagia drrmwqaqlp alaarhrvia vdlrgygdse
       61 lppapfahhd dviglldalg igqaalvgcs fggrvaadta laypervsal alfgapvsgn
      121 ewseeteelw eelvgevdpe dfaataagev rfwvvgptrr pedvdpelir faeemdrral
      181 aaelalsavd ageldppaie rlaelrmpvl vavgaddlgd irrladriaa etpqgvrlpd
      241 vpdaahllpl erpepvnaal ldflp
//
LOCUS       WP_357542978             115 aa            linear   BCT 28-DEC-2024
DEFINITION  GroES family chaperonin [Micromonospora sp. NPDC048999].
ACCESSION   WP_357542978
VERSION     WP_357542978.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 115)
  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 115)
  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 115)
  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 115)
  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..115
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..115
                     /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=12324
     Region          12..98
                     /region_name="Cpn10"
                     /note="Chaperonin 10 Kd subunit; smart00883"
                     /db_xref="CDD:197951"
     Site            order(12,14,16,19,50..51,63,73,78,80,96..98)
                     /site_type="other"
                     /note="oligomerisation interface [polypeptide binding]"
                     /db_xref="CDD:238197"
     Site            30..43
                     /site_type="active"
                     /note="mobile loop [active]"
                     /db_xref="CDD:238197"
ORIGIN      
        1 mtadqnldsg lpirllhdrv lvrtengege rrstagivip ataavgkrla watavgvgpn
       61 vrsivsgdrv lfdpddrsev elhgrayvll rerdvhavaa ervekeptgs tglyl
//
LOCUS       WP_357543021             237 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357543021
VERSION     WP_357543021.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 237)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..237
                     /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=25674
     Region          9..136
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          75..225
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 maeqaetlrr tplsrdrvlr aavaladeag ieslsmrnla qelgvvpmal ykhvankdel
       61 ldgmidvvvg eidppvagad wkptirgril sarqvllrhp wavlaiearn matpailayl
      121 damvatlrtg lsadlahhvm hamgsrmlgf sqelfdasrn agrsgatdpe ppasmppeva
      181 arfphlaeia taashddesv vgqgcddqfe fefaldllld gierlqqqgw rsshqtr
//
LOCUS       WP_357543101             173 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543101
VERSION     WP_357543101.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 173)
  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..173
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..173
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17604
     Region          6..170
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtersivllr hskaeqpdgi adverpltdr ghadaaaaga wltgsdnlpd lvlcspakrt
       61 rqtwhgvava iagtagesgp gagapevrye qalytgsvgd llavlrdagd ayetvlvvgh
      121 npaisdlsal ldpssgadeg lrtsgiavhr ftgswgdlaa dsaavtdsht arg
//
LOCUS       WP_357543204             319 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357543204
VERSION     WP_357543204.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..319
                     /product="GlxA 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=34451
     Region          3..316
                     /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 mlrsvavial devaafelgv laevfgtdrt adgfpgyrfd lcttdgrpvr srsgflltph
       61 adlapveead lvavpahtpg apvpapvlea lrraadreaw vlsvcsgafv lgaaglldgr
      121 nctthwrhvd dlqrrypaar vrcdslyvad grlltsagta agidaclhlv rqehgsttat
      181 rlarrmvvpp hrdggqsqyv etpipktpea ptlapvlawl mghldrtvtv delaaragma
      241 prtfarrfra etgttphgwl tnqrvllarr lleetglsve siadhagfgd aaalrhhftr
      301 rvgttphayr atfrdrvea
//
LOCUS       WP_357543285             214 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543285
VERSION     WP_357543285.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   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 214)
  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..214
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..214
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=23408
     Region          3..212
                     /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 matfvlihgg ggsawdwhll vpelvgrghd vvvpelpied rsagfaefce tvvdaigdrd
       61 dlvvvghsyg aftapliadr lpvrlivllt pmvpvpgerp gdwwdntghr saegfseeqq
      121 fhngvpaevv aeaakhgreq vsaewnepwp ldawpdvptk vliahedrff panfqrrvaa
      181 drlgvtpdei dgchavalsh pkqladrlta ylpr
//
LOCUS       WP_357543312             150 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357543312
VERSION     WP_357543312.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 150)
  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..150
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..150
                     /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=16404
     Region          12..150
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mshatvdrpa vefghvehvp vhfddldamg ilhnaryavl leraltpywa ergiafqggr
       61 stapdvfhav refnityhap isgtgpvavh fwldhfgtss aryayefrsv dgatlhadgt
      121 rsivrldpat mrptawtdaa ravaatllrp
//
LOCUS       WP_357543332             208 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent F420 reductase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357543332
VERSION     WP_357543332.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..208
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21716
     Region          14..193
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mkigiigsgh iggtltrrlr alghdvtvtn srgpqsltel aaetgatagt leetvqgsel
       61 vviavpvrav pdlpaalfdg klvadadnyy perdgeipdl vdrsltssrw taehlkgarv
      121 vkvfntiraa hlmdngrpag apdrialpva gddpaakqvv melvdelgfd pvdggtldas
      181 wrqqpgtpvy gadrdadgvr qglaaarp
//
LOCUS       WP_357543338             338 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357543338
VERSION     WP_357543338.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..338
                     /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=35666
     Region          6..338
                     /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 mpdngmralv krsrsprdva vidwrrpvps agevlvrtda vglcgsdvha wnqdigyewv
       61 arsvvlghea vgvvtevgsd vdpgwigqrv vpisidgcge cdvcatgrrh icprrqvlgl
      121 sfhgaaadcf tvaaqrlvvv pddlpvqalv lteplaiamh avsklqdaaq graseivvtg
      181 pgpiglmaal lldsfghrvt lvgiardqpv rlaaaaklgl qtsqgedlpl apdmwleasg
      241 sgealdravr qtaiggavvv pavfariptv dinvvtrhel hllgsygasr edyeraavil
      301 qrdpgrwdgl ttsfpldqgv dalraveqgs vvkaillp
//
LOCUS       WP_357543460             198 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543460
VERSION     WP_357543460.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 198)
  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..198
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..198
                     /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=22327
     Region          1..183
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 maqgrqrpga lsapedqefd affranwdrm ikhvsrkawg atiedvedat syamtqlyer
       61 wstqerptln pqgwvfkvam nklaeisrrr sdgwqrhvta aladaapape verrvilqde
      121 tshvmhlisr lpegqrtvma flydgyapte iatmarrpva tvrsnlrhar arltrelrty
      181 qkeplaaagg syaaghpl
//
LOCUS       WP_357543497             200 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543497
VERSION     WP_357543497.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 200)
  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..200
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..200
                     /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=21599
     Region          1..199
                     /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 mdsvrsdrrg tgpriplalk iliaggfgvg kttlvgsvse irplqteevl tdagidtddl
       61 tgveaknttt vamdfgriti nsdlqvylfg tpgqdrfwfl wdelsfgalg avvladtrrl
      121 adcfpsvdyf eqrgtpfvvg vncfegaqrf spdsvrtald ldpevpvvlc dardrqsgka
      181 vlvslveyva srrghpvpay
//
LOCUS       WP_357543507             159 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543507
VERSION     WP_357543507.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=16950
     Region          <40..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maehhgpdgp epsiaaevda aaeallsvwd sareratsrl sgsqlravii veqydginlr
       61 glaesmgmil ssasrlcdrl vaagvlervp gradrreisl hltpvgqall aelrrdrrer
      121 laavldamsa gsqqallrgl refesaarae taedearsa
//
LOCUS       WP_357543521             354 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357543521
VERSION     WP_357543521.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 354)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..354
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..354
                     /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=38682
     Region          60..352
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mefadeapkl lmllyglvaf vvvvggllll ldaipnyfar rreqrliaas takggpggds
       61 papvarprrg eglfaafflf paivllligl vvpavrttll slmdggsdnw vglrnygwmf
      121 sqpeiidvli ntlmwvvlvp llatgmglly avlvdkarfe aiakslifmp maisfvgagi
      181 iwkfvyayrs eeqeqiglln qiavsfggep kqwllnspln tllliavmvw iqagfamvvl
      241 saaikaipae iveaarldgv nawqmfrrvt lpsirpaliv vvvtisiatl kvfdivrtmt
      301 ngnfntsvia nemynqafrf gqvgqgsala vflfvlvipi viyqirnlrq qreg
//
LOCUS       WP_357543527             259 aa            linear   BCT 28-DEC-2024
DEFINITION  M23 family metallopeptidase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543527
VERSION     WP_357543527.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..259
                     /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=26760
     Region          <56..148
                     /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"
     Region          188..>244
                     /region_name="sporang_Gsm"
                     /note="sporangiospore maturation cell wall hydrolase GsmA;
                     NF038016"
                     /db_xref="CDD:411609"
ORIGIN      
        1 mfrrlltlsa aalmaaaavi ipaapaaaap tfkvpfpcgq twsgqtrtnh sppnsidfnr
       61 tndvgdpvva saagtvdrvt nlgntsygky vrinhgggyh tyyahlnafr vsvgqtvrhg
      121 tvigtvgstg gstgphlhye qrlngadiki rfngtlalyw gtrnytsdng csggstaagt
      181 vrtagtpltv rsgpgtgyas vgtlatgtnv tihcqttgts vtgtygtsni wnrigsgrfi
      241 adaytytghs gfipgvprc
//
LOCUS       WP_357543608             309 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357543608
VERSION     WP_357543608.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 309)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..309
                     /product="GlxA 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=32767
     Region          2..307
                     /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 mhqvvvlayd gvipfdlsvp vevfgrarra dgspayevrv cavtdevrag avnirvphdl
       61 savagadtvv vpgvadldla vpaavldava ttparlvsic tgafvlaasg rldgrratth
      121 waaapelarr hptvtvdpdv lfvadgpvlt sagaaagldl clhvvrgdhg vavaadtars
      181 cvmpleragg qaqfiayepp apagdglqpl lawlaenlhr pltladiaah ammstrslsr
      241 hfrdqvgttp mrwlnrqrir raqqllerth qpvervgelv gfasptafre sfrhivgipp
      301 rayraafpl
//
LOCUS       WP_357543623             309 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543623
VERSION     WP_357543623.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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..309
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..309
                     /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=32873
     Region          93..271
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mraarpaeqv rgskesapgk dfggtrvpgg trvpgelrge pvvipparpa ttpvpagaat
       61 gavatagavg avgttaigpf rpryavghpv artigkmfft hmgeglvcsa givnsasksl
      121 vwtaghcvay dghfaqnwif vpnynmdhsw pqspapygyw yarylsapge wtdhrhfhsd
      181 wgaavvwpng sgtriqdylg aqgisfslpy fpfsyaygyp adppydggyl ylaiaqahda
      241 gasvmymens mtggssggyw ltnfdgefgv vnghnslglp hqpqytyspy yglstvnfyn
      301 lvqainama
//
LOCUS       WP_357543649             380 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543649
VERSION     WP_357543649.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 380)
  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 380)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 380)
  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..380
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..380
                     /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=39979
     Region          139..379
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mmwasrrlpp wavdallgag vtlvvsvais anqggrhgpd avaylwavgl galmfarrry
       61 pvvvlavtal glfayyaagy pavglgvpva aalfsaaefg rlvhavvtgv vvvavsvffr
      121 lvegqafsfv vnyelaghil lmaaaialgd svrsrrsvqe garriaelta qryrqesdar
      181 vhadrlaiar elhdsightt svislhadva realgrdeaq traaldliks tatrtmselr
      241 rtvallrapd essrsvvsls nvgtlresas aagidlefdv rvgaelpatv dasafrivqe
      301 avtnvvkhsr gsraqvtayd dgsvlhlrva ddgagsgmtg rghgitgmre raealggtlt
      361 agreepgfvv ravlpleeps
//
LOCUS       WP_357543707             230 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357543707
VERSION     WP_357543707.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 230)
  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 230)
  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 230)
  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..230
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..230
                     /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=24489
     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 mriaiagagn vgrsiaqeli dnghqvmlie rqpkmlrpdr vpaaewvlad acelasleea
       61 niagcevvva atgddkvnlv vsllaktefa vprvvarvnr aenewlfteq wgvdvavskp
      121 rvmaalveea vtvgdlvrlm tfrqgeanlv eitlpptapy vgqpihavpi prdaalvail
      181 rgkrvlvpsp ddpieagdel ifvctaaved evravilgpa saergnqdqg
//
LOCUS       WP_357543710             116 aa            linear   BCT 28-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357543710
VERSION     WP_357543710.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 116)
  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 116)
  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 116)
  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..116
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..116
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12615
     Region          1..114
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 marqvittli ddldgkpadr tvefgvdgvk ytvdlseana gklrtaldpf ieggrrlgrg
       61 gpasptsrpa srsaaapnrr qenreirdwa aqngfevser gripqevlda yrtahr
//
LOCUS       WP_357543713             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357543713
VERSION     WP_357543713.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=34890
     Region          32..311
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mvipkappap aaagtggmpr prrsrrrtrs plaaygfltp alglflilvg ipmlgafalv
       61 fldyriigqp rfigldnlrr ffddpmvpqv fgntlkmllp lvaahcilgl glayatfrva
      121 artasiyrai iyfptivttv svavawgfml dtdngvvnyy laklgaphip wlvsptwsip
      181 aiivfsvwkf vgtpylffli glqniphsyl eaadvdgana wqrfryiilp lltpttflvv
      241 vlsfinylql fdepfvltdg gpgtsstsvt myiyqnfeag rygyastisa vlfvcilait
      301 lvqflaskrw vrydne
//
LOCUS       WP_357543715             424 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357543715
VERSION     WP_357543715.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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 424)
  AUTHORS   ter Beek,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..424
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..424
                     /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=46144
     Region          34..418
                     /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(153,155,278,280,309..311,351)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mfrkilaiaa tailaagvag cgvgdssesd gkvtltlayp sdpnaqakld alvreyqksn
       61 pdvsvkyvfi pftswseyit kvktmvaggd apdllrlave girqfvdddl ampfddyaaq
      121 hgdyvtslgl dqihpniqap lqidsktygy afdwnnvvmh intklfeeag vplpaenwtk
      181 ddflkaaqal tktvdgqkqy gfmipndyfl ttaflygnna svlnedmtka tvnqpnavev
      241 vqfmhdlvyt hgvspvpgpn vdagrlfmag klamypagrw pvasyqqndf sdfdvqylpt
      301 fqsqtaafgs gtfpvlktse hpqeaqkfam wlsaseysqt nflavdsips rqdvmtsvtt
      361 aappanggif kesadsvkai qapvrytdvs tifvkalsev ysnqksaqea ldhaakdinr
      421 alds
//
LOCUS       WP_357543898             504 aa            linear   BCT 28-DEC-2024
DEFINITION  LVIVD repeat-containing protein [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543898
VERSION     WP_357543898.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..504
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=54632
     Region          80..479
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          104..138
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          145..200
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 mnkpslpgar qfkflavgaa allfvnlvaa vpgnaqapvd qcaplvgsgd dfaelclteq
       61 eltamdttga dlgvdeiass rnmrqianvp kqapfntqaa lgtdiafqgr yafvgnydgf
      121 viydiknprs pkitsqvlcp gaqndvsvhg dllflstdss rsddscssvs qtasnaaswe
      181 gikifdvkdk rnpryiksve tncgshthtl vpgkdhrnvy lyvssygpna sfpdcqpphd
      241 lisivkvpvr tptdahvlsa pvlfpdggnp ggngssttsg chditvfpkk dlaagacmgd
      301 gvlfdianre aprvihtvrd ttnfafwhsa tftndgskiv ftdelgggga ptcnptigpt
      361 rganaiyhle grgdnrklvf knywkiprtn gptencvahn gslipvlgrd imvqawyqgg
      421 isvwdftdst rpfeigywer gpvdanrivt ggawstyyyn gyiyssdiqk gldvleindw
      481 rtwtaklqwf pelnvqtqpg ywdf
//
LOCUS       WP_357543932             356 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357543932
VERSION     WP_357543932.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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
REFERENCE   3  (residues 1 to 356)
  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..356
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=37365
     Region          130..354
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnasmglrpv eapfllvacg avvfrrrapl pallvavval gvgvvvcgli geappwayla
       61 vwillfhvgl rgtrvlvpaa flagaaalva figaaefgem aldarwtaml pvaamsaaal
      121 lagsqmrgar edakrhreea treavaaers riaremhdli ghdlsviasl saggqaaars
      181 apddaerafv aigevsrasv gqlrhvlrll rtteddfvhp ltpqpglaql galiesvrra
      241 gfridderhg dlaalppghq lavfrlvqea ltntmrhsga gsaasvriai daeevvvsia
      301 drsavpeidr pgvssdghgi igmrervdal ggtleagptv vgwrvratip regrdr
//
LOCUS       WP_357543938             403 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357543938
VERSION     WP_357543938.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..403
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..403
                     /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=42718
     Region          6..>61
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          42..388
                     /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(58,60,225,245,318)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mlkrtvfagg tvfdgastsr vdvavsgdri vdvgtgldgd dvvdcsemsi vpglfdchvh
       61 vmvrdlnisr aeqepfslqy yealrnlsll ldqgitsard aagadlgvkr aieqkliegp
      121 rlqialvmls qtgghsdlhl psggsrsmsm mmphpgrpra vrdgvddvrr gvrevlraga
      181 dtikiattgg vmspgddprh thfrddelev iateaaaagt dffahaqgte gikaalrhga
      241 rsiehgyhld deaidlmlra dawlvptlsa traivdaadr gvpipagsla larealeahr
      301 asfaravdag vkiamgtdsp pyahpsasnl delqlmteas smtpqdawra atssaaallr
      361 qdglgaitpg mladlvvvdg rlddlrglrd rirhvslggq rvr
//
LOCUS       WP_357543989             287 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357543989
VERSION     WP_357543989.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   Wintjens,R. and Rooman,M.
  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 287)
  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..287
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33411
     Region          15..76
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          104..282
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpfkepvrkt lraqwlgylm relrrergvt lkeateylnr dhsalaryer aewpfkrddv
       61 malldiygvd dpdrrarilk lseecwrtge wdldyaderh nrgyvdhdwl eehatsiniy
      121 athllpdllq tpaytahviq lrertkkrte hqgrlvdklt arqrafeart nrlnvvidea
      181 alhvktpdpd lmreqlahva alaqrtrini qvirsdvnta arawgpfelf lmpdpypevg
      241 yldnlagriy vetphskrfv layeqlqqaa lnpndsikai qqaaeha
//
LOCUS       WP_357544000              88 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Polymorphospora].
ACCESSION   WP_357544000
VERSION     WP_357544000.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora
  ORGANISM  Polymorphospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 88)
  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..88
                     /organism="Polymorphospora"
                     /db_xref="taxon:338583"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9228
     Region          15..>73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvrnpltpeq ieagrrlgsl lrrargaagl nevalaagis petlrkietg rlpspafgti
       61 aalsevlgls ldevaavwrd rsplrlts
//
LOCUS       WP_357544084             179 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357544084
VERSION     WP_357544084.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 179)
  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..179
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..179
                     /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=19208
     Region          3..136
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgtrdlwlge gvvvladegp agvridrlaa rlgltkgsfh hhftgvadyh aallthiehg
       61 qvalldglsd elaavdpvda lrtlpsrlde lfdaeldral rawaigndga rgvvervdna
      121 rltfletlwn ravpdptrar aaallphlll iganairppl daagrravfd llpdliphv
//
LOCUS       WP_357544093             928 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357544093
VERSION     WP_357544093.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     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=99987
     Region          3..236
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          122..925
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          755..785
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          796..824
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          829..865
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 myrdgqpvsl gsvkqrllla tlllrpneiv gtnelaamlw gddqpasaaa nlrtyvrglr
       61 qslgggaswe gitaaaggyl lrvepgerdl dlfdaaaarg rdalaasdat raeaelsaal
      121 glwrgdplsd lplpaalarr vaqleerrll aeedytgall algapadvih rlralldrhp
      181 lrqrawgqlm vglyrigdva galdtfrqar qvlaeetgld papeltklyd dilhhrpgla
      241 acppprpdgp apetppgpli qrpeqlprav pefvgrgvel asldalldsr aqgpttvvis
      301 vvsgmagvgk talalhwahr vadrfpdgql yvnlrgydea gvvsppdals gflealgvpq
      361 aripsdlear tglyrsllas rrmlvvldna rdsaqvrall pgaggcmvvv tsrdrlggli
      421 aaesaapltl svltaeests llasrlgtgr lasepaavad iveatgrlpl alsivaarva
      481 thptfplgai aaelhsaear ldaladgdvr rvfswsylal gqdaarlfal lglhpgpdlt
      541 paaaaalagv saadvtprlr eltrlhllae hapgryafhd llrvyaaela esperadehe
      601 aararlydhy lhdaypaall lqpqwppiep vpplpvpgrr pvtghdgala wftvehrvlm
      661 rvvqqaaeng feayawqiaw alntflaprg lwqdqlatql valaaaekid dlagqaaanr
      721 llaraltrlg dhdtaehrlk ralelherlg dptgqaqtlh nycelcyldg rldealthgr
      781 ealrlyrlvg nrsgeartln aigwllaatg dyvqaiesct ealaqqrrsd drngqaatld
      841 slgfaydrlg drdraadcye qaiqlfrdsv dryheaetli rlgdtrdgmg draaasaawr
      901 qavriyedvg dpaaeetrrr leryeseg
//
LOCUS       WP_357544204             141 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357544204
VERSION     WP_357544204.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..141
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15321
     Region          18..131
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mattnaaekr nqaksaynaf lavcpsrqll drlsdkwvvl vlcalggdga gnagppasmr
       61 yselsrliag vsqkmltqtl rslerdglit rtvtptvpvt vdyaltdlgl slhqttrqlr
      121 twaqdhmdav qahrdhydad n
//
LOCUS       WP_357544237             271 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357544237
VERSION     WP_357544237.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 271)
  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 271)
  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..271
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..271
                     /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=28383
     Region          7..235
                     /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 mtgpvslevr gldytypdgq valrgvdlrv prgarvallg pngagkttlv lhlngvlhgg
       61 agtvtvggla vgrdratlae irrrvgivfq dpddqlflpt vaedvgfgpa nlglrgaela
      121 arvdealaav gmsayrdrtp hhlsygqrrr vavatvlamr peilvldeps snldpasrre
      181 laailralpv tllmvthdlp yamelcgrsv ildagrvvad gatvdvlada ellarhrlel
      241 pygfdpalaa aqlaardrpp agpasaqeal a
//
LOCUS       WP_357544247             449 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357544247
VERSION     WP_357544247.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 449)
  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..449
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..449
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47193
     Region          8..429
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtliserpap geprsyrfpp vvrravagge vvaahlpgqs lavatlllda gagreplgre
       61 glagvvakal eegttdrdaa ayalaleglg telstsvdwd sfrttvqvpv drlapavtll
      121 aeavrtprld padvervrdd evtslrmywa npgpradaal radlfgaevr hgrpmdgdpe
      181 svaaltvddi tgfhagwlrr pgtllvagdl dridldvlaa aafagtggdp veagapidvq
      241 vrtqrriilv drpgsvqssl rlghtapprs hpdyvptqla gtvlggafts rlnhlirevr
      301 gytygiradf gmsrrfgrft vsssvqtavt apalveavge iartqadgvt eeelavarsw
      361 ragqlsvelq tpaaiasala tlvvyglpdd yhahlreaml sapldvvsaa aaahlhphgl
      421 tlvvegdval irdelvasgl gevvddgpr
//
LOCUS       WP_357544263             287 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357544263
VERSION     WP_357544263.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
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   Wintjens,R. and Rooman,M.
  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 287)
  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..287
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31359
     Region          23..71
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(29..30,41,44,48..49)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          103..281
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtalhgatig rrrlrsalra aregagltqe qvadamdwsl skvirieaga vsvstndvka
       61 lishyrltds eqvaelvala rvsrrrawws ryrdglpapy lsyiglevea ssllvfqsvg
      121 ipgllqtday arastvaslr favepfdldi vddvrarrrh evldradpps ievvldesvl
      181 hrqtggalcl reqlrhlvea grrsnitiqv lpfqvpdyav rspfivvrfp gtgdtdvvfv
      241 gsplsqdltd tsdtvepyva afrtlqgmsl epaaslaria riaddlg
//
LOCUS       WP_357544288             116 aa            linear   BCT 28-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357544288
VERSION     WP_357544288.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 116)
  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 116)
  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 116)
  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..116
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..116
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12736
     Region          1..114
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 marqvittli ddldgkpadr tvefgidgvn htidlseana gklrtaldpy ieagrrlgrg
       61 gpasfmnrpa srsatapnrr qenreirdwa aqnglevser gripqevlda yrtahr
//
LOCUS       WP_357544295             390 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Polymorphospora
            sp. NPDC050346].
ACCESSION   WP_357544295
VERSION     WP_357544295.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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 390)
  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..390
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..390
                     /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=41446
     Region          1..385
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 meavvdasls qmevghmlte lldrvrrilq vdvatilqld ahaqqlvqva vsgsvhgggv
       61 dvrvpvgqgt agrvlrdrlp vvveqaepge lpgpafasal rsllavpmia gtdvigvlqv
      121 ggsrprkfss ddigllqlaa dratqatqar lshldraaal alqrsllppr lptvpgvdla
      181 arylpghdtg vggdwydifs lpsgwlgvvi gdvaghglha avvmgrlrsa lrayalecad
      241 paevltrldr kirhfeaghl ataiyamlpp grdcvhlsva ghpppvlvsr drpaellslp
      301 vdhplgfdgg rsrrtrvidf pdgavllcyt dglverrgel idagldrlra avepgpaetv
      361 cstvmtklvd repiddiall tihrqeeqad
//
LOCUS       WP_357544320             534 aa            linear   BCT 28-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357544320
VERSION     WP_357544320.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 534)
  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 534)
  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 534)
  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..534
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..534
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=57935
     Region          22..231
                     /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 matttahepq aadvlpgsyk llelaaievn thnvrddaqa lpgivqnlqt dgvaglvspi
       61 vvtpigdnry rlidgeqryw saveanqtvi qaivradlfg treqiinmlr qvhrtdpnat
      121 qlahgiqqla lagmdaaeia rstgyrpeqv taaravasld natagrakel gldltqmavl
      181 adfagdtevv dalteaaeeg pfafaraaeh aratrathea ltaridelrr agvkvltdrl
      241 fyhdpkakei tdlrdnngqr itpdahatcp gravalydry gvpteaeccm dwrthghtay
      301 tydytsnarr gpmteedkae rrkviennkq mdaanavrrd wlagllaakt ppkgtsklia
      361 qvltdghtld twirngrpml ddllnpskrk gtkrvpakls darytvislt avaaafesai
      421 drttwrtpte tlatwlqwcv lngfqigpve qliidtveqr kapsrptlnl vttddrgsvd
      481 dqattpapdg gheltdislp anqdgtddrg svddqattpa pdggheltdi slaa
//
LOCUS       WP_357544336             321 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357544336
VERSION     WP_357544336.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 321)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..321
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..321
                     /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=34704
     Region          40..298
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpsvstpqam rqastmtdps svpaarqpaa rrpsarrrsw sallwvapaf gmyavfvlfp
       61 mlqsvqysfy dwdgigpatp agldnwkaif tqpellqsvl nafvlvifyt vlpvglglva
      121 asfirelkpg afsttarvll fvpqvlplva agiawtwmys sdglvnqilr avgldqytra
      181 wlgdftfalp avgvigvwvm lgfctvllla gigkidpaly eaarldgagp vreffavtlp
      241 glrrelvvca tftiiaalas fdvvqiatqg gpgyqtmvpg vqiyrltflq qhvgqasala
      301 vfltvvvllv iwpiqrlgrq k
//
LOCUS       WP_357544379             328 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357544379
VERSION     WP_357544379.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 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   5  (residues 1 to 328)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..328
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..328
                     /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=35063
     Region          4..240
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          255..318
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlrihftvad lnrtrvatap dplweltlsm hqlrrrgspp llagwkadla hrlrpdttlr
       61 heispalaln pptgyfpdfl tpaeaadgfe aglqalldtp rdrlraeial lgtdrhrldp
      121 aalrigdgdp aalrtlgral rryhdvavap mwdrirasfd adralrartv ldggavalln
      181 glhpaarfta gvleianyra drdlhldgrg lvlvpsyfka asrpmalvdp nlppvlvypv
      241 ersarvasea graslsallg rtraavlela adgpstgtva grlgisapaa sehltvlrda
      301 glvvstrqgn tvrhtlaplg htlldggp
//
LOCUS       WP_357544384             268 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Polymorphospora sp. NPDC050346].
ACCESSION   WP_357544384
VERSION     WP_357544384.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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 268)
  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..268
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..268
                     /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=28687
     Region          21..>79
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          51..247
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mteeeflaay dprayppvav tvdvvaftir dgrlhlllvr raappyaghw alpggfvhpd
       61 edlptgagre laeetgvqag glgrvhleql gtygapgrdp rmrivsvayl afapdlpdpa
      121 agsdadeaaw vavdslglpd aaalpgrpvr qrpgttrkla fdharivadg ldrarskley
      181 tplatrfvgp eftiaelrav yetvwgdtlh agnfhrkvls vpgfldsvga ttdrggargg
      241 prarlyragd arllhpallr psreeavr
//
LOCUS       WP_357544398             424 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Polymorphospora sp.
            NPDC050346].
ACCESSION   WP_357544398
VERSION     WP_357544398.1
KEYWORDS    RefSeq.
SOURCE      Polymorphospora sp. NPDC050346
  ORGANISM  Polymorphospora sp. NPDC050346
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Polymorphospora.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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 424)
  AUTHORS   ter Beek,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..424
                     /organism="Polymorphospora sp. NPDC050346"
                     /db_xref="taxon:3155780"
     Protein         1..424
                     /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=44995
     Region          1..340
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrarltaavt laallgltac gggdagdsdg pvslrmttws aneahlalfn eiaeeykkan
       61 pnvteikfdp ipfenytttl ttqiaggnpp dlawifensa pdfvssgalv alddtlkgtd
      121 gyvfdeltpa atklwqdegk lyaypfstsp fgvfvntdlf ekagretpae liaagrwtwd
      181 tavaaasavn aetgkaglvi rdfdykgwdn lstvwtgwga qawsedgktc gfdqqpmvda
      241 mtflhkaift dkalpapgtt adffagdagm titqisrasl ladqkfgwdl vplpagpngd
      301 yavigqggmg vlrkgdnakv aadflafltn ptnsaklaqf fppprqsqlt aetlaktnpl
      361 lkpeqlqsvv idgissgvvk pshtgqaeis qavraaldpl wqpgadvrtv ltgvctqikp
      421 lldr
//
LOCUS       WP_357544534             113 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Pseudonocardia alni].
ACCESSION   WP_357544534
VERSION     WP_357544534.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 113)
  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 113)
  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 113)
  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 113)
  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 113)
  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 113)
  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 113)
  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..113
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..113
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11907
     Region          15..109
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mdptalaaar aharewvasl rreldaladq qaltshddeh dpegvtiavq raqlqgllaa
       61 aerecgdldr aadrmadgdy grcsvcggpi aperlealpa adtciscasd prr
//
LOCUS       WP_357544576             465 aa            linear   BCT 28-DEC-2024
DEFINITION  amidase [Pseudonocardia alni].
ACCESSION   WP_357544576
VERSION     WP_357544576.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..465
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..465
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48165
     Region          1..461
                     /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 mtvtvastar eqvaalrare isarelmdlh lariearnpe lnavvsldee raragaaaad
       61 erlasgapvg plhglpfafk dthavagwrt tygsplfadh vpdtddlive riraagvvpi
      121 gktnvpefaa gshtfnrvfg ttvnphdptr saggssggaa calaagmvpl aegsdmggsl
      181 rnpasfcgvv glrpswgrvp ewpssnmwet tstggpmart addaalllsv lagpdpraph
      241 algdpgetfa pplrpvplag lrvalsadlg gaftvdrsva avvgaagdal agagaavsgt
      301 apdltgadec frtlrawhfq arfgmqlavh pqefkaslaa niragealtg advavayqrr
      361 ttlaqrmref ftehdvlvlp vsqvppfpad qefpatvdgv ptasyldwmr saylitvtgc
      421 pavsvpfgrt pdglpvgvql varhgadral leiaaaverl arpaa
//
LOCUS       WP_357544588             104 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Pseudonocardia alni].
ACCESSION   WP_357544588
VERSION     WP_357544588.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=10344
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawiylvvsg vletvwaaal sqsrglsrlg psllfagala lsmgglalal rdlpvgtaya
       61 vwvgigavgt alygmaalge pattarllcl laivagvvgl kvlh
//
LOCUS       WP_357544605             288 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudonocardia alni].
ACCESSION   WP_357544605
VERSION     WP_357544605.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32572
     Region          13..74
                     /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          102..282
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtaahgplvi rkrlgwalkq lrvarhrqls eiakllevsa sklsrletgq vepkfrdvrd
       61 lleiygasdt erdrilgwah dakapgwwep lgpapsgvdl nmlisleaes rakstfsipi
      121 sgllqtedya rllltevfag qdhveiermm kirmgrqnvi epdrteappl elhvlldeva
      181 lhrcadeevl raqigelirr gdqpnitlqi lpfragwtsa tstfsvftpr hpetdwpmvn
      241 vegtendvfi dtpqavadyq qiwqrlldqa mspddsrrml drrfagrs
//
LOCUS       WP_357544611             256 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Pseudonocardia alni].
ACCESSION   WP_357544611
VERSION     WP_357544611.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 256)
  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..256
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..256
                     /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=26599
     Region          6..234
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mplvtarrgg lvdqvidqlr saitggewpv garippesel asslevgrnt vreavralah
       61 ggllevrqgd gtyvrattel sgalrtlcgp elrevlevrr tleveaarma aarrtdadlt
      121 vlraalagrd ravaavaayg rrgeepdaad veraaradtd fhvavvrcag ngllvelyrg
      181 vveavadsvk ttmpgtagte ddishtgive aiadgdvdra areagdfldr liaarpvtpq
      241 gpagergpda gagpta
//
LOCUS       WP_357544665             284 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Pseudonocardia alni].
ACCESSION   WP_357544665
VERSION     WP_357544665.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   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 284)
  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..284
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..284
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29481
     Region          48..277
                     /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 mrtghftdta ardrfralyd davaglgpts srdittthgv vrvltcdgpp gipfvllpga
       61 gspgvgwapn vpalrrlatv hlvdplggpg astqdvpvrs vgdqvrwlrg vldalgpchl
      121 vgtsmggrla fevarrspag irtltlldpa ltftripagt vaaslgalpg apswlrrrfv
      181 arvggdadvv ddpvarliea glsgyasavp hpslpsvrdv aavevrtlvl lggrstmldp
      241 vrargraall prgtvevwpd aghalpgefp ervaerlwsl vaas
//
LOCUS       WP_357544688             225 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Pseudonocardia alni].
ACCESSION   WP_357544688
VERSION     WP_357544688.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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..225
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..225
                     /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=23900
     Region          2..222
                     /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 miefsgvghr ygertvldgv tltlaeprva lvgangsgks tlartvnglv apsagsvrvd
       61 grdpardgaa vrrrvgfvfs dpdsqivmpt agedvafslr rtvrdrtera rraaetltgf
      121 glgdhvehpa hqlsggqkql lalaavlvld pdvlvcdept tlldlrnkra fadrlaglrq
      181 qvllathdld lltgfdrvvv ldggrvvadd epgpavayyr rlcgs
//
LOCUS       WP_357544707             602 aa            linear   BCT 28-DEC-2024
DEFINITION  gamma-glutamyltransferase family protein [Pseudonocardia alni].
ACCESSION   WP_357544707
VERSION     WP_357544707.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..602
                     /product="gamma-glutamyltransferase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=61441
     Region          14..594
                     /region_name="Ggt"
                     /note="Gamma-glutamyltranspeptidase [Amino acid transport
                     and metabolism]; COG0405"
                     /db_xref="CDD:440174"
ORIGIN      
        1 maprghdrig phgavssthh lgtaaaatvl arggnafdaa vacgfvlqvv ephlcgpgge
       61 lpavfvtatd pvprvlcaqg vapaaatadr lrdlgctivp gtgllpatvp gawegwltll
      121 rdhgtwelad vlapalgyaa ggfplvprvp aaigtvadhf rthwpssaat wlpdgrvpaa
      181 gelvrlpvla atwrrlldea vgpsrearid aardawyrgf vaeeigrfaa tpvrdetgrd
      241 htglltaddl agwsahyeda lvadagsgws vakcgpwsqg pvllqqlrll agldlelpgg
      301 vatldtvhaa aeaaklafad reawygdgat pdllddllsd aytddrrgli gpasdgglrp
      361 gspggrtpri gdyagtpgag rgsgtegpgt geptvsrdgv argdtvhvdv vdaagnmisv
      421 tpsggwlqss ptipalgfcl gtrgqmfwle eglastlapg rmprttlsps lalrdgepal
      481 afgtpggdqq dqwqlaflla lmhggldlqa aidaptwhst afpasfaprg wephglvves
      541 rlgaatlagl trrghvvdda gawalgrmca vgtgaavpgg ggpgtlhaav dprsgvgaai
      601 al
//
LOCUS       WP_357544719             333 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Pseudonocardia alni].
ACCESSION   WP_357544719
VERSION     WP_357544719.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 333)
  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 333)
  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 333)
  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 333)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..333
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..333
                     /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=34708
     Region          61..164
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 marttrstll alavtaaclt gvagvaaasp erdpdpgpal taagldeslt chgdlagsag
       61 tpvllvpgtt ldpdvnfdwn yarafaqegr ahclvqlpah atgdiqvaae hvvhairtmh
      121 deaggrisvv gfsqggmvpr walkywpdtr gmvtdmigid psnhgtlday pvcgpgcvpa
      181 fwqqqtgsrf ltalndgret fagidytvvy tvtdevvvpn lppaasselr rdgagrvani
      241 pvqsicpvhv aehltmgstd pvgyavvada lehdgpadag ridravclad vmpavdrtql
      301 panearllgq vatsiatepr vaaepplrey arg
//
LOCUS       WP_357544743             225 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Pseudonocardia alni].
ACCESSION   WP_357544743
VERSION     WP_357544743.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=24362
     Region          43..202
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 maddvvvpep vqrqlrerve aalttlppae rraapeadra gkraaavtlt llpvpgatgd
       61 grladevafv ltrrarslra hsgqwalpgg rldpgetaeq agrrevseei glelgpdrvl
      121 gllddyptrs gyvitpvvlw aggageptpn pdevaelhrp plaeidhepr fltipesdap
      181 viqvplfdry vhaptgavlh qfrevvlhgr atrvahleqp vfawr
//
LOCUS       WP_357544755             437 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudonocardia alni].
ACCESSION   WP_357544755
VERSION     WP_357544755.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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
REFERENCE   3  (residues 1 to 437)
  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..437
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44726
     Region          160..425
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mhphpepppr tgaerldarl talglagprr rdaalavlva agtlavvtpv vlapgpaael
       61 glapgtaala lgvvtvqnll lalrrtapav claltvglel vnvvllpvga alrgpatava
      121 agtcgsrlpt rragglvgaa avvettvvlt giavrpadga llgaaglvva qvlsavlvyg
      181 gplllgvylr trrryaeldr vhtagvvaay reradaavar erarmarelh dvaahhlsam
      241 vvqaavverl vdrdpdearr tasrlreqgr rtlhdlrlvv galrepgvgg aeadapvpgl
      301 aeldglveqa relggpvelv rrgdpdepsp vadvtcyrvv qealanareh aagapvrvtv
      361 thadgrvave vvngpargtp pesgsapgtr gfglagmrer allvggefea grtgddgwrv
      421 rlvvphdpgp etgggra
//
LOCUS       WP_357544764             263 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudonocardia alni].
ACCESSION   WP_357544764
VERSION     WP_357544764.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27699
     Region          4..258
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mhldltgrta lvtgstqgig laiavdlara garvavngrt aervdaavar vrdesggevv
       61 gvaadvttdd gtatlaaelp evdvlvnnlg vfgaqealti tdddwrryfe vnvltaarli
      121 rtylpgmrdr gwgriqnias dsavvipaem ihygvsktal lalsrgfake aagsgvtvns
      181 viagpthtag vedfvyqlvd palpwdeaqr efmrahrpqs liqrliepee iahmvtylas
      241 plasattgaa vrvdggyvds ilp
//
LOCUS       WP_357544768             317 aa            linear   BCT 28-DEC-2024
DEFINITION  ketopantoate reductase family protein [Pseudonocardia alni].
ACCESSION   WP_357544768
VERSION     WP_357544768.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 317)
  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 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   3  (residues 1 to 317)
  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 317)
  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 317)
  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..317
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..317
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32417
     Region          1..303
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mryvvigaga vggtiaarlh aagrevvvva rgahldaire rglrldtpdg stthpveavg
       61 tvgearptpd dvailavksq dtppplaall eaapgitvac aqngvanerl aarrtdrvqa
      121 mlvilpaehy epgvvvasss pvpgvldvgr fpsgvdaite aivadltaag fssradpdvm
      181 aakygklltn lanavdaicg lddpdaprlv davtaegrav ldaagitart gdddrvrreg
      241 titerpvaga trrgssswqs lqrgtgsiea rhlngeival gaahriatpv ntelmrvaee
      301 maaageqpas rsgadll
//
LOCUS       WP_357544914             277 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Pseudonocardia alni].
ACCESSION   WP_357544914
VERSION     WP_357544914.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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
REFERENCE   2  (residues 1 to 277)
  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..277
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..277
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28540
     Region          5..268
                     /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 mrssdgvela vtvfggtgap vvllhglmsc arswrprvaa lrpygrvlap darghgrsgr
       61 pagradadaa wspqrladdv velletleap aalvghsmgg vsallaaaar pdlvsavvae
      121 dppldltatp plrlddaraw faavagphpt rvaleqalag pdpevgrhmg rcavrradgw
      181 wlacavddal avarhwvrap lldracavrv pslvleagas vappgqlaql agrirgarhv
      241 rvpgtghlvh daapqtwaae vtallratgr taaappg
//
LOCUS       WP_357544953             280 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Pseudonocardia alni].
ACCESSION   WP_357544953
VERSION     WP_357544953.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   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 280)
  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..280
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..280
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28898
     Region          5..>148
                     /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 mtvvttdlld rpdaritfdv rgagpllvlv gspmgaegfg pladamaadh tvvtfdprgt
       61 grspaadpea dstvavraad laallervgg apatlfgssg gavvslalaq erpelvgvvv
      121 aheppleell pdaaehraat eqiigtyreq gaaaawamfl asaglpgaap ddaaqsaadd
      181 aglpatdgda taqqaaderh fflhemretv rwrpdpqrlr grrvvvgigs asagqicdrt
      241 sralaaelgr dpepfpgghv gwledpagfv arlrevlart
//
LOCUS       WP_357544980             272 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Pseudonocardia alni].
ACCESSION   WP_357544980
VERSION     WP_357544980.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..272
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..272
                     /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=28527
     Region          5..272
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 miplafdyar pdtlddaial laekgedasv lagghslipv mkvrlgapef lidigrlpel
       61 syirvegdel avgaatkhrd vvdsaevate vpllgavart vgdpqirarg tlggtvahad
      121 paadlpaall aldatvvlqg prgkrtvpig efytgvfttv repdelivei riprcgdkgw
      181 ayekftrrsn dwaivavavs ddriglvnmg stalrasate ralaegksia eaaalaaega
      241 eppadthgsv ayrthlvqvl trraletarg qg
//
LOCUS       WP_357544989             221 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Pseudonocardia alni].
ACCESSION   WP_357544989
VERSION     WP_357544989.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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 221)
  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 221)
  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..221
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..221
                     /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=24421
     Region          8..166
                     /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 mpeklcslrw peesdyelve qwlkplspta altgdanelv fardvreane sgrvrylmvd
       61 tpdgvtigvv nhrrvgsags havggavgdp alwgagagae aftllvdllf hqlnahrvef
      121 ttasfnrhtm smltrggfvl egvlrdyyyl dgeyhdrtiw silreefvag anehselmpv
      181 adlvperdkv rartllakyl aadpptslrg vegraarrrp y
//
LOCUS       WP_357545065             440 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudonocardia alni].
ACCESSION   WP_357545065
VERSION     WP_357545065.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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..440
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..440
                     /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=45148
     Region          211..440
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 maadpvrsre apivtahage lpertreerq avvlricvvl gavgllvarp dlagarpvva
       61 avliglsavy aaalgvvsvl rgrlpvppav ltgidgllal lacgltggva spmvaalplv
      121 viaialrggh rlgqlvalgl gvgytvaall gsdrgvtvga avvaglwwtg flfatavltg
      181 vlvrllerql adiattrara eseherylse ralrdrivsq srarldgarv vlhefrtpva
      241 sltalsadla agrlggdaar rasrlladha ahlqdmldgl adlavadgsp lgrdrprrva
      301 laeladavld aagiaahrrh pvvepagaav hcdpqrlrrm ltnlaenaar hsgdevvelh
      361 lahdgavlta evrdrgpglp agqegvvtak gvalgerrgt aglglwiaea lasamdgels
      421 llpreggglv arltlplaga
//
LOCUS       WP_357545108             168 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Pseudonocardia alni].
ACCESSION   WP_357545108
VERSION     WP_357545108.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 168)
  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 168)
  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..168
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..168
                     /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=17889
     Region          34..165
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mvsaspdegd trdgdsgdad atdgdtggdl lrldrqvcfa lavaarnvia lyrpllepmg
       61 lthpqylvml alweraprsq gelaralald pgtlspllkr leaaglvdrr rvpgdertma
      121 vsltaagral raraesippa vverlgmpla eleelravld rvidasrs
//
LOCUS       WP_357545112             387 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357545112
VERSION     WP_357545112.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..387
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39840
     Region          40..384
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mtgpavgpld qvaprygggs ladilpsala algvpgavdl lglgprlagv rriavllvdg
       61 lgwyqiptaa pyaptlagla atagtvltsg fpsttptslv slgtgtpsga hgvlgfkvrv
      121 pdtdrvlshi ewagdpeplr wqpvptwyer araagvavtv vsrpeyggsg ltlaanrggd
      181 yrgaagvdal agqmltalaa gagptlvsgy hpdldrhghl sgvdsvpwrl aaaevdrlla
      241 rlvdglppda allvtadhgq lnvpdehrid ldtdprlrag vrvvageprv rylhvepgat
      301 advvaawsav ldgaarvttr deavatgwfg pvpeehlrri gdvvvvcrgt yavvatrset
      361 piesrlvayh gadtaaemti pllvvrg
//
LOCUS       WP_357545119             535 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Pseudonocardia alni].
ACCESSION   WP_357545119
VERSION     WP_357545119.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..535
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..535
                     /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=55213
     Region          3..521
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mhatydavvv ggginglvaa arlaragwsv alvdehdrlg gfiaseqrdg ytrdtwsswh
       61 plfvtgpaya afgadlhrhg ltyantdgpl tatvaddgsv afahrsvaat vagfaeprdr
      121 eayramidrf gahaagiggl lgaelhapss lgpvatlara agvsgmetya rdaltsgrsw
      181 mrarftgpet drlwapwllh aglapdsasg glmvpifaat mhgaglpvvt ggagnfltaw
      241 erlldelgva vhtgrrverv avvsgratgv agegfalqar ravlatvtpt alygsllppg
      301 vvpapvadaa aryrpgraam qvhvrlsgpv pwadgrlagv plvhvsdgsa staiacaeae
      361 agllprrptv vvgqqhvldp trvpegaaal wlqlqelpfa pvgdaageld tadgwnrtla
      421 egyaervldr vaahapglre lvrgvdvldp taitahnpna lcgdpyagsa eldqnfwwrp
      481 lptsgghatp vpglwqigas thpgpglgga sgflvadrla apgpvarlrg rltgr
//
LOCUS       WP_357545123             374 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudonocardia alni].
ACCESSION   WP_357545123
VERSION     WP_357545123.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 374)
  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 374)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 374)
  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..374
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..374
                     /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=38380
     Region          135..374
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrridpnvva glimtvlcgi lavpvaleqa agvasplgpp wlwwatyaaf llalvvggwl
       61 devvgvvavr allalmvlas atlvllgaqf gwlpillvvt asvstyhlrg pvtaaivvgn
      121 vgvaaaaalv agssvqvaav tgaiylllqs asvllivalh reeesrrrla aahaelaaag
      181 aalaetsraq erlrisrelh dlvghqltal aleleiatht gddpgghvar aralagdlla
      241 dvrttvgqlr srapdlaatl erigeqlprp vvhvhvadgv aadeertlav vrcvqeiltn
      301 airhgdadtv widlspvpgg glrltarddg rgaaagavpg nglrglaera gafggsvdwg
      361 pavprgfavt aelp
//
LOCUS       WP_357545177             235 aa            linear   BCT 28-DEC-2024
DEFINITION  TVP38/TMEM64 family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357545177
VERSION     WP_357545177.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..235
                     /product="TVP38/TMEM64 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24153
     Region          33..231
                     /region_name="TVP38"
                     /note="Uncharacterized membrane protein YdjX, related to
                     fungal oxalate transporter, TVP38/TMEM64 family [Function
                     unknown]; COG0398"
                     /db_xref="CDD:440167"
ORIGIN      
        1 mnsatrrpsa hrlarllrqp sarrfgllll llagfgvall laprpdpael prladalggy
       61 apiaavggga llmaalvprt fvtlatgaif gpvaggaysl gaallaaglg faigrllgrd
      121 fvaervrgrl arldgwftrq slfgvitvrl lpiaafglvs ygygttgarp lpylagsvia
      181 aaptavgyaa lgaaatspdp vnwyaaapas lgliasvviv hrwwqaerqr rlgps
//
LOCUS       WP_357545184             402 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Pseudonocardia alni].
ACCESSION   WP_357545184
VERSION     WP_357545184.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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 402)
  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..402
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..402
                     /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=44056
     Region          22..397
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(58,65,87..88,95,99,106,232..233,236,240..241,244,
                     277,282..283,286..287,289,312,339..341,344..345,347..349,
                     353)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(65,86,88..89,171..172,180,231..232,235..236,240,283,
                     286..288,388)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 maltttgtet hdlfsgdfwt dphpayaalr teepvrelal pdgkawlisr yadvraafvd
       61 prlskdwrwt lpadqregqp aapipmmilm dppdhtrlrk lvgrsftvrr mndlqprvee
      121 itqelldalp aegpvdlmrq yaflvpvlvi cellgvpaed rdmfsawssv mvddspqeek
      181 faamgslngy laelierkrt epddallsgl lavsdadgdr lsseelvama tllliaghet
      241 tvnligngvl allthpeqra rlqadpslit saveeflrfe spvsnapmrf asedveysgv
      301 tipagstvml glaaanrdpe wledperldi trdsssgvff ghgihfclga qlartegrva
      361 igrliaqrpd lalavdpsel vyrestlvrg lsrlpvtpge pa
//
LOCUS       WP_357545199             496 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Pseudonocardia alni].
ACCESSION   WP_357545199
VERSION     WP_357545199.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13740664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..496
                     /product="PucR family transcriptional regulator"
                     /calculated_mol_wt=49906
     Region          7..128
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          257..491
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mhptiadvla rpevragapa vragraalgt pvrwvhvsev adpagtlppg vlvlsvgvpv
       61 adpttvpary vdalraagav glvveigrql pslpaglvqa araagfplve lrrtvrfaei
      121 vagvlgqvah rdddpgppgv eavfrslalh rvppgrvvge larridapvv cedlahrvll
      181 taggpdlrdw aarsrlagpa gpegwatapv grpgarwgrl avpsrptpgt adrvrallda
      241 aadavslldp spegllrsar dalvadlava vpsdtgrlav raraagldtg gplsvvalrp
      301 agddapgrav dpeqavdaal avaapgatvv spapgelvvl vpgdggplla alpatvaaat
      361 agpgpfaava dllrrarddv aahaatggrg lvrvpalrgl vhrlgddpal lgfaadvlgp
      421 vaalpaaahg dardtlwalv eaggvvadva rrlgvgrpaa yarlrrlsgl lgldltdpev
      481 rtalhlallv daraar
//
LOCUS       WP_357545227             162 aa            linear   BCT 28-DEC-2024
DEFINITION  ester cyclase [Pseudonocardia alni].
ACCESSION   WP_357545227
VERSION     WP_357545227.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..162
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17883
     Region          21..155
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mttapppdtt rcdpdaalrw yqawidawns hdpdrvrplv tddflletpt trnsgwdvrg
       61 pdaaadyvry vltaypdltw ertgppllap daprvaftwr gtghftgtlt ppgipgtglp
      121 fdfvgvevfd fhdgrahrlh asydlmgllr rtgvlrggag rr
//
LOCUS       WP_357545231             262 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pseudonocardia
            alni].
ACCESSION   WP_357545231
VERSION     WP_357545231.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=27380
     Region          4..252
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mlllglasvt frersvpdvv rlavdagsev vewagdrhvr pgdraaasaa rgacagaglr
       61 igtygsyhka gpsdpgefda vvataaelga prvrvwagta asaevspagr aatvdalrrc
      121 adavaergmg llvehhvesl tdgldtalrl raevghpalv thwqprelpd tdvclaevra
      181 lrpatvhafs wgadgyterl slgdradlwa pvlaeltaqs rddgtdtevl lefvpgdtaa
      241 slrrdaaalr dlragrdlag ar
//
LOCUS       WP_357545255             757 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357545255
VERSION     WP_357545255.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 757)
  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 757)
  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 757)
  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 757)
  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..757
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..757
                     /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=80021
     Region          191..742
                     /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 mpprsedprr datgsrrdss rggrddvprs gepriggisd araytprgrt iregggatrt
       61 gagggaqqrr tprsgrsgdp frpalqvldg gqagttrtgr retaaaperg ragaaragrr
      121 eagaggraga vrsvsarpvr epfdddepap srrspgprrp aarrpsrkpr rppkladprr
      181 rlrlgtllvl alfttigirl vilqtltppa fadggldkrv vsvelpaprg aiydrtgapl
      241 ahsvearyvy adptlieeke rlttakqlsp llgvpasela drmkrrtlpg tttqsqfvyl
      301 argvdidkak qimaldlagi gvhrderrev gdlaanllgf vspdmvgleg leakyddlle
      361 gqpgkktyev gqgdlaapip ggysetteak pggsleltvd rdlqfrfqri msakmaqard
      421 gvgaavaiei psgevlaqas ypgydaaapg kvnspadrad aatsfvvdpg sihkaityga
      481 alqegvitpd ttfpvantit rggvlfedth pangrqmsip gmlafssnvg tieiaerlgr
      541 drlidyqkrf glgratgegm pgeaagrllp adewsessyg svpighsvda tplqmaaaya
      601 aiandgtyvq phliknvidp dgkrtpaatp vtrpvlspqn aaalrrmlea vttvdgpdgq
      661 atglaaavpg yrvagktgtg lryvdgkkqt gevhsfigma padkpryvva vfvwspggea
      721 agvsapafre mmgftlahyr vppsatdrsp kfevfph
//
LOCUS       WP_357545352             164 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Pseudonocardia alni].
ACCESSION   WP_357545352
VERSION     WP_357545352.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 164)
  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 164)
  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..164
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..164
                     /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=17318
     Region          2..134
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mnrlalqlrd livatdeyrr aeaaalgigv aeaavlgeih hrgplppsal vvrlgiasas
       61 vtalldrltv aglvqrephp tdrrsvlvtl tprgraaipa mfamftedil aavhaaqpey
      121 vrmftdvlgr iaaslrerlv detaiaeela artgaadgyp vgpv
//
LOCUS       WP_357545507             209 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudonocardia alni].
ACCESSION   WP_357545507
VERSION     WP_357545507.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 209)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..209
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..209
                     /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=22028
     Region          25..184
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mdgrhtrsar traalldaai aiictrgvta vtqravaara gtslasttyh frtaddllva
       61 afeatssrti admrrtarea aergagivda amavvarapy gdrlppdgvi qltlsaihnp
      121 rlrpiaeafv eelaalftpl tttpdtartl arslsglilh emargadapt ptmradvtrl
      181 faafgvpdhp ttgrpqadpa hhhedpepg
//
LOCUS       WP_357545509             731 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Pseudonocardia alni].
ACCESSION   WP_357545509
VERSION     WP_357545509.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=76687
     Region          18..717
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mstdtagpda tvlsdaagri rfavpalrgr talavavede ldhvggvrqv hayprtgnvv
       61 vwyrpgcdrv elveaigkgl gaepeataar tprsadqhng elarlvvggv alaalgfrry
      121 alrrppllgp asrtvatgvt iftgypflrg alrslaggkg agtdalvsaa tvaslvlren
      181 vvaltvlwll nigeylqdlt lrrsrraise lltgattrtw trladgteie idiadlsvgd
      241 evvvherivl pvdgevvgge gvvdqaaitg eqlpvavapg avlhagsvll rgrivvrata
      301 vgqdtaigri idrveqaqgd rapiqtvgen fsrrfvpasf llsaltlvvt rdvrramtml
      361 liacpcavgl stptaisaai gngarrgili kggahleaag rvdavvfdkt gtltqgrpvv
      421 tnvisfhddw apeqvlayaa sseihsrhpl aqavirstee rrieipphee cevllgqgmr
      481 vqadgrvlli gsrdllraqg vtvprkaadw vrrlqkaset plllavdgal vglvslrdtv
      541 rteargvler lradgvtriv mltgdhpqta kavaeelgit eyraevmpeq kqdvvralqa
      601 eghtvamigd gtndapalal adigiamgva gtdvavetad valaaddlna lldlrdlgrr
      661 sitlirqnyg msiavnaagl lvsaggamsp vvaailhnas svavvanssr liryripaga
      721 attvvegevv r
//
LOCUS       WP_357545515             383 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudonocardia alni].
ACCESSION   WP_357545515
VERSION     WP_357545515.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..383
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40269
     Region          4..381
                     /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 maepgtggpl dgvlvadfsr ilagpyatml ladmgadvik vegpagddtr twtpperdge
       61 atyylginrg krsialdlrd pgdlaaarel arradvvien lrpggmarfg ldhasvaagn
      121 pgvvyasisg fgsgagahvp gydlmvqams glmsltgdpd gppyragisv fdvmagnhaa
      181 igvlaalrhr drtgagqhve vnllssaltg lvnhssawva ggtvpyrmgn ahpsvfpyep
      241 mptadddliv aagndaqfrk lcgvlevpgl addprfarna drtvnreelr plleerlatr
      301 gavewfellt aagvpsgpiq tidggfamae rfgldpvvtv gegdravptt rhpvrfsatp
      361 avyrlppprl dehgadlrkw lds
//
LOCUS       WP_357545526             359 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Pseudonocardia alni].
ACCESSION   WP_357545526
VERSION     WP_357545526.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=36737
     Region          8..359
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mphparrdal rallpaagld allvtdlldv rhltgftgsn aaaviaadpg ddllctdgry
       61 rvqaaeqcpg levlvdrpsa paaaaripag ltlgydsatl tvdglaavrd avpgrrlrra
      121 pglagrlrav kdageveria aacaladtal rallddggvr pgrteadval dlddrmrrlg
      181 adgpafdtil aagphsavph hrptgtelrr gdlikidfga aldgyhsdtt rtfclgpaad
      241 wqrelhalvd gaaaagraal vagasvtavd aaardvitaa ghgerfphgl ghgvglavhe
      301 ppwlgttatg ridagnvvtv epgvyldgkg gvriedtlhv vaggpavplt glpreliei
//
LOCUS       WP_357545550             275 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Pseudonocardia alni].
ACCESSION   WP_357545550
VERSION     WP_357545550.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 275)
  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 275)
  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 275)
  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 275)
  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..275
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..275
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29811
     Region          11..261
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mtstvttsaa aylellgvdr atpdralldr vvtahnatip fenldpftgv eppttsdgva
       61 aklvhgrrgg wcfehnrlly dvlaavgyqv tplvgrvrlg lapadpptsr thrltlvdtt
      121 egrftvdagf gstvpttalr lvagleqptp qatyryardd hgawvlqrrg sgdwadqyvf
      181 dlvpapdvdf amgswylthh pashfrtglv aarttpehrt tldgtrltvr aadgdvarde
      241 ltsparvrda leerlgvdtg avagledrlr evyfp
//
LOCUS       WP_357545571             255 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudonocardia alni].
ACCESSION   WP_357545571
VERSION     WP_357545571.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25788
     Region          1..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 mtgfpaertv iltgagsprg igryaadhla aagwhvglid idgdaaaata aaiaerhgvr
       61 aagvgadvad revavaavda leqqlpqlva lvafagvasp vpyldvdeqe wrrivavnld
      121 gthwvtqrva rslvahgvgr ivgissvsaq rgggtysktp ysaakagiqg lirsvarelg
      181 phgitanvia pgpidtdimg gtlsperkaa maadgvvsri gtphdvaaaa ayligpdsgf
      241 vtgqtlnvdg glymh
//
LOCUS       WP_357545587             383 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudonocardia alni].
ACCESSION   WP_357545587
VERSION     WP_357545587.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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
REFERENCE   3  (residues 1 to 383)
  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..383
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=40134
     Region          124..383
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtdvaayrrw vvdglvvlvt aligllmarl rvvsspggpe lllgvdvaag mlacvalwwr
       61 rrcplpvavg vvvlctfsev asvpglvalf avaarcparv saavflgsfa sfavyyswrp
      121 apeaplwllv galvaghaav fgwgllvrsr rllveslrer aamaesaaal raertahear
      181 ealaremhdv lghrlsllsv hagalafhrg apaeetaraa evvrenahra lqdlrevigv
      241 lrapvgelpl pgitdvgell eetrrtgtav vlhdgpgvtt gehpvpetag rtayrlvqea
      301 ltnartyapg apvtvtvtgg agdglvveva npaparpara drpgagqglr glaeratlvg
      361 grldhgptpd ggwrtgmrlp wps
//
LOCUS       WP_357545597             539 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Pseudonocardia alni].
ACCESSION   WP_357545597
VERSION     WP_357545597.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 539)
  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 539)
  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..539
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..539
                     /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=59160
     Region          3..485
                     /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 mttsttpdvd avvvgagfgg iymlhtlrdr lglsvrafek gdgvggtwyf nrypgaksdt
       61 egfvyrysfd rdllqewnws tryldqpdvl aylehvvdry glgrditlgt evtaavydee
      121 aglwrvrtsg getvrcrylv nalgllarsn ipalpgldtf agrtvhtnaw pddlditgrr
      181 vgvvgtgstg aqfivaaapr aahltvfqrs pqynvpsgnr pvtqdevdrt kehfpeiwdq
      241 vrgsvvafgf eesaveamsv saqerervfq enwdagngfr fmfgtfcdia tdpeanaaaa
      301 afirrkisei vvdpetarkl tptdlyakrp icnegyyetf nrddvelvsi renpiaevvp
      361 agvrtadgvv heldvlvlat gfdavdgnyr amdlrgrggr hiddhwtdgp ssylgvskag
      421 fpnmfmilgp ngpftnlpps ieaqvewige lighaersgi gtieptaeae qgwsrlcrei
      481 adatlfpkad swifganipg kpnavmfyma ghrayreels tvardgyrgf amhgsggsr
//
LOCUS       WP_357545650             290 aa            linear   BCT 28-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Pseudonocardia alni].
ACCESSION   WP_357545650
VERSION     WP_357545650.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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 290)
  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..290
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..290
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=32536
     Region          1..255
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 msaryswggd efvfvelaed mslqanfkav aitnllrser pdgileicpa nasyqvrydp
       61 dvldphalma qlteletrvg dalgvtldcr vveipvlyqd pwttetlmrf rdrhqdpeat
      121 dieyaaring yagvdefiaa hsgspwftsm vgfvaglpfk yqmvprdrqi vvpkylrprt
      181 dtpkqtvgyg gcfsciysvr gaggyqmfgi tpapiydptq tkpdftehmv fmrpgdmvkf
      241 rgidrdeydq lqaaaeagey ritarpvafd lqpflddpdg yntrllevla
//
LOCUS       WP_357545675             714 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudonocardia alni].
ACCESSION   WP_357545675
VERSION     WP_357545675.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=77890
     Region          36..708
                     /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 mqqadvaaar adhgralvpa alpdpadlaa pwaselarhs vlpatelrpv ldrvttqlre
       61 aalaerydpa lpaaaggdlv rarihqpgcl eigmellgah lepaadtaar vrriaavlaa
      121 fargfteatr slvlaeheqv traalearrv aeearrhsdl rlrtvvdsaa vgivifepdg
      181 rlvevnetaa vmtgytpaql lrmrvtdfvp resapevwae rprlldgsld rlrvvrpvrr
      241 addsdvwidv avtllggvgg eeqllvavvs dvtdqllmqe nlahqashdp ltglpnrslf
      301 ferlaaaida gssgarpgic yldldgfkvv ndtlghqagd rllqvladrl rgalepgghl
      361 varmggdefv vlvprtadra eleevatral gtvrrpvrvd grdivisasv gvvrhdgelg
      421 tdeliaaadt tlysakragr gryvlydrdr hrddvarfel ssqmpealrr ddfvvvyqpl
      481 vrladertig vealvrwqrp dgqllgpdrf iplaeetglv vplgrrvlde acrqgrvwad
      541 aypdrpltis vnvaarqvte sdlvadvaat lerhdwppel lqveltesdl mgspgrplat
      601 lreldrlgvk iaiddfgtgy snlaylrhlp vhrlklaghf lagtaerddv ilrtlislas
      661 aldlevtaea vetreqaarl reygcanaqg wyyapavvae rvpdlirdpf lral
//
LOCUS       WP_357545681             246 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Pseudonocardia alni].
ACCESSION   WP_357545681
VERSION     WP_357545681.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 246)
  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..246
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..246
                     /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=24883
     Region          11..231
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mtpdplftgd avggwlqlps pavaeiagsv gfdlvcvdtq hgligddtvl gmlqalsatg
       61 tpslvrvpgh saesigrald rgadgvivpl vdsaeqaaaa vaacryppdg vrsfgpvrps
      121 wqgrdlfapp rtvvmvetva avanladiva vdgvaavfvg psdlalahgl plaaqgdggp
      181 esdrhaelvs gitavcaeag vpvgiycdsp ahvrrfralg ctftilaaeq airrsalaek
      241 ladarp
//
LOCUS       WP_357545692             331 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pseudonocardia alni].
ACCESSION   WP_357545692
VERSION     WP_357545692.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=32875
     Region          16..323
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtaalavlla valvgslafg aedlpvakvv davlhdrpgp vstivrdlrm prsllaaivg
       61 aglalagagv qtlvrnplad pyllgvssga svgatavitt gvlgalgtwa lftgallgal
      121 aagalvgaia vaqggltpir liltgtvlgs afsatasylv frsgdpataq svlfwllgsl
      181 sgaqwdrvav pavtvalllv llvtfsgwld altagpdtaa algvpvtaar talftvcava
      241 vgvlvavsga igfvglvvph larllvgsrh rvllpvtalg galfllvvdv varvavrpte
      301 mplsvvtgli gapvflvlmg rrryrtagsm a
//
LOCUS       WP_357545746             216 aa            linear   BCT 28-DEC-2024
DEFINITION  FMN-dependent NADH-azoreductase [Pseudonocardia alni].
ACCESSION   WP_357545746
VERSION     WP_357545746.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 216)
  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..216
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..216
                     /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=22784
     Region          1..211
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 msllrldasi rtegsvsrei adeverayld arpgaevvrr dlgtaplpad lwttavaagy
       61 vaeadrtpeq rgalariael adevlaadav vigsplynfg iaahlktwvd alitdprfap
      121 gttplagrpv vlvvsrgggy gpgtpregwd hgsgwitril rdvwgadvtv veteltladv
      181 vpamselrsl aaekrerarv dartagerva avtpaa
//
LOCUS       WP_357545768             463 aa            linear   BCT 28-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Pseudonocardia alni].
ACCESSION   WP_357545768
VERSION     WP_357545768.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=51013
     Region          4..459
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mapstavvwf rrdlrvadqp tflaaadaad ralalfvldp alltpsgaar anflfgclre
       61 ldealggkll vvkgdpadvv priamavgaq tvhvaadygp ygrerdeqve kalaeddvel
      121 vrtgspyava pgrvekgtgg pfkvftpfsr awadhgwrap adtdastctw mdpsdsdggp
      181 ravkvpddep veaelpeage saalarwkdf ldegvedygs ardlpaergt sgmspylkyg
      241 cvhprtllad lakrkgdsvk tyrteiawrd fyadvlyrrp dsargnydaa fdhlplrtgk
      301 aadadferwc egrtgfpivd agmrqlrgea wmhnrvrmiv asflvkdlhi pwwrgarhfm
      361 allvdgdlas nqhgwqwtag sgtdaspyfr vfnpitqger fdpdgdyvrr wvpeladveg
      421 kavhqpwklk ggipegypep mvdhkaered alarydqvka ars
//
LOCUS       WP_357545771             642 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Pseudonocardia alni].
ACCESSION   WP_357545771
VERSION     WP_357545771.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 642)
  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 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..642
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific 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=68970
     Region          59..631
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mrplpdgaqg atpagrptph prhpgdgrdv satgtaptpa trtttsaaae riaaardafl
       61 hheqlredav rppilaswir srdsdvapds idlpeidret dsplmraatp ivselcdqfa
      121 tepvslilcd gdgvvldrrt gdsalrqhld rvwlvpgfsy aeqhvgtngi gtalegrrpt
      181 evfghehfve hledlacaga pirhpvtgki lgvvdltcwr seanalmvat aattarriee
      241 allaasgrhe ltllhdylta vqrggdsavl avgddlvmmn drareliapg dqvpllagat
      301 dalragrnrq lvvdlpsgat arvqcrpswn eagsaggilq vslthretvg rgsatptitt
      361 alptavgsga lwtkcaqavd rhfrtnewlv lqgehgsgrt tlarathhlh spaghvrvld
      421 aadvgprwls evsdelgggg gtlvlrevdr lppaaaaala dvlephrest dperawvvat
      481 rsssrttdsp elaslldcfp rtievpplrh hvedvaelvp yllarltrga dltcapealr
      541 vlmrhrwpgn veqlyqvlrk vvsrrrtgvi rledlppetr vlarrvltpl esiecdaivd
      601 alldadgnka eaarrlgmsr atiyrkirgy giatpegagm sr
//
LOCUS       WP_357545777             243 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudonocardia alni].
ACCESSION   WP_357545777
VERSION     WP_357545777.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 243)
  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 243)
  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 243)
  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 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   5  (residues 1 to 243)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..243
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..243
                     /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=24930
     Region          <32..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtggpgtdgv gsggpidpad laaraallad rtraafclal idgrawtage larhagvaps
       61 tasahldrlv dagllvaerq grhrylrlgg pdvartietl aagtapappa ptlrasraaa
      121 rlasartcyd hlagalgval fdglvaddll atgdglaltp agrlwfagla gpdaltrrgr
      181 pvvracldwt errhhlagta gavlcralfd rgwvergrdr rsvrltvsgr talpalvgva
      241 lpd
//
LOCUS       WP_357545804             490 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Pseudonocardia alni].
ACCESSION   WP_357545804
VERSION     WP_357545804.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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..490
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..490
                     /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=55151
     Region          3..436
                     /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 maatttehvd vlivgagvsg igaahrlree fpersfvlle aqdapggtww thrfpgarsd
       61 sdlftygyrh kpwtgpsiaa ggeilaylre videddlagh iryhhrvtal swsseenlwt
      121 advtrtdtge tlrmtasflw mcqgyynhde pytpewpgie rfagtvvhpq swpsdldvtg
      181 kkvlvigsga taatvvpata ataehvtmlq rspsywfpap tvhelatmle pldlpaewth
      241 eilrrtyvqq ldwlattgrd dpdalheflv esirpllpeg tdverhfvpr yrpwqqriaf
      301 vpdgdffaam regkasvvtd tiseftekgv qvssgeviea dvvvtatgfd lavfgdipft
      361 vdgepvdftr hvtwrglmis dipnmayafg yfrhswtlri dlvndligri larmdergdr
      421 vvvptlraqd admprlpwvs ednfnpgyig rsqhrmfgqg drepwthmhe hdvdrvelpk
      481 adlddglqyr
//
LOCUS       WP_357545810             425 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Pseudonocardia alni].
ACCESSION   WP_357545810
VERSION     WP_357545810.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 425)
  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 425)
  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 425)
  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..425
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..425
                     /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=45515
     Region          24..418
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(65,72,105..106,113,117,124,253..254,257,261..262,
                     265,298,303..304,307..308,310,333,363..365,368..369,
                     371..373,377)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(72,99,101,104,106..107,193..194,201,252..253,
                     256..257,261,304,307..309,409)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 maedttitpa aatsgpdtvd psdpvaafsg mrevaavvei pleipgrptq qglmvtrhae
       61 vramltddrf rhdaaavpea enylrnaqtg liglpedldl lrrpmlgrdg edharlrrlv
      121 sraftvrrvn glrprvgaiv dgllddvaaa gadgtpvdlv ealaypvpia vicelvgvpe
      181 gdrdrwrefa rlliqpdper mpdvargmva hvrdliearr repaddllsg lvaahdedgd
      241 rlseqelvdm tvnltvagfe ttahvlakgt lallsrpdel aalradpqlw ptavhelvrt
      301 cgpipagapr yaaedleiag tpvpagtavl pgvlpanfdp rvvdrpdeld vrrdpgrgeg
      361 hlgfghgahy clgaalarqe vevvlsalvt rfpglrlaep adgpsrlgfe rlpalpvhvd
      421 rppeg
//
LOCUS       WP_357545828             176 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Pseudonocardia alni].
ACCESSION   WP_357545828
VERSION     WP_357545828.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 176)
  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..176
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..176
                     /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=18689
     Region          2..172
                     /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 msgsaaldlv gtvtwrradp telltgpadl arwldacadl pdgvtvtpei lgrardlrea
       61 vhrlatdrla grafdpaala lvngtargpg ltvqlddhgt rrtgdadavl aelardavav
      121 ladrdtplke cgrpactrly ldrsrgarrt wcgmdecgnr vkaaayrark ktitgs
//
LOCUS       WP_357545879             180 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Pseudonocardia alni].
ACCESSION   WP_357545879
VERSION     WP_357545879.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 180)
  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 180)
  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 180)
  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 180)
  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..180
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..180
                     /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=19239
     Region          8..173
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 madptastvr aavpadapgi advctrayra tyrdllpeaf vddvvarfyd etrvrsetvp
       61 apphwlgyvv aeeagsvvga aggaitgagv gelyvlyldp drrgegigtr lldhvtaqlr
      121 dhgatgmwvs vaegndlgvp fyrargfvec drvpmhisaa ddglwslrmh rviarssrqs
//
LOCUS       WP_357545890             520 aa            linear   BCT 28-DEC-2024
DEFINITION  SLC13 family permease [Pseudonocardia alni].
ACCESSION   WP_357545890
VERSION     WP_357545890.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=52946
     Region          112..496
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mavqsgprag steapdaera agssrfdsvr ariglplgpl gflavlllad glvwpqrala
       61 avfvlvmvww vtealplavt avfavllcvf lgvadeetvl gafgtdtifv flggfviara
      121 msvhgldrri alralsvpgi agspvrtmia fgvlaavisa fvsntatvam llpigigivr
      181 svstvstreg gpdlsrsrwa tsvmlmiayg asigglitpv gaphqligrd lveaqtgrti
      241 glvewvtmfl pivlvmfaal avlllllnrp evtrlegaae fvaeqraalg gvtrgekntv
      301 vaflvavvlw ttpgvlgavi gedtapvrwl tehvtegvaa vfaatllfll parsatgggl
      361 aptltwaeav kidwgvillf gagtvlgsms setglartfg dgiasglgvs slvavtvlaa
      421 vmallvsett sntasagivv pivvpiaaai gvdplipglv ataaagygfm lpvstppnai
      481 vygsglvplt tmirsgvvfd vvgvavlvvg vllmaplvgl
//
LOCUS       WP_357545896              94 aa            linear   BCT 28-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Pseudonocardia alni].
ACCESSION   WP_357545896
VERSION     WP_357545896.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 94)
  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..94
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..94
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9805
     Region          1..>51
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 malyvyrcga dgpveerhpi gsapatarcp tcgersprvi tapmlgladr grmalidrtt
       61 atahepqvvs appprplrpg gpplhpatrg lprp
//
LOCUS       WP_357545911             199 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Pseudonocardia alni].
ACCESSION   WP_357545911
VERSION     WP_357545911.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 199)
  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 199)
  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..199
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..199
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=20938
     Region          85..171
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 madrrgrgrd ararttgtgr graaakprtt tarsarapas tggsgarsrp agpqgarprl
       61 trarsragev varttgllgl sstkraaila ivvcalaltv avplhnfvaq rqeladvsdr
      121 qqaleadvar lssdrarlsd paeveaqars rlgmvrpget pyvvqfpapp apvvedgqae
      181 pgvpwfhtlw ndvtgdprr
//
LOCUS       WP_357545939             295 aa            linear   BCT 28-DEC-2024
DEFINITION  RCC1 domain-containing protein [Pseudonocardia alni].
ACCESSION   WP_357545939
VERSION     WP_357545939.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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..295
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..295
                     /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=28845
     Region          9..268
                     /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 mhpgdmgvla agrrhsagvr adgsvvaagd gragecavdg wtgvvavavg nvhtarntgr
       61 thtvglradg tvlatgrddd gecavagwrg vvavaagwrr tlglradgtv laagraaega
      121 cavdgwrgvr glscgdwhsv glcddgtava tgndrydqca vggwhdlvav sagylhtvgl
      181 radgtvvttg rgggdvagwh dvvavsagsg htvglradgt avaagddglg qcavgtwrdv
      241 vavaagsaht lglradgtvv avgegsggrc dvdgwtlavt apdgssgarp srrgg
//
LOCUS       WP_357545961             525 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Pseudonocardia alni].
ACCESSION   WP_357545961
VERSION     WP_357545961.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 525)
  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 525)
  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 525)
  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 525)
  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 525)
  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..525
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..525
                     /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=51590
     Region          <2..156
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          246..525
                     /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 msddrgtrpd gaadpaahgs apprlrprpl drpatdpgeq aafgrpdgvg ssfappsshl
       61 gangslptvp pptaavaraf grpdrtpdgd pagglqrppg asgdalrgge qsaeqdpfwp
      121 ggstgdpwrd pgtpvvaapp pgdgddsreg prpdgprlsv revlfgkrvq pralallgvl
      181 alvvgaaggl vghwtataas altspgavls ateparerpr gsvsevasrv lpavvslevt
      241 vgnqagngsg vvidpagyvl tndhvvapat gpgqgtieal fsdgsrvpat vvgadpmtdl
      301 avvkvpvanp tvaaigrsge lavgdaviai gspfglagtv ttgivsavdr pvrldpegsa
      361 gdavidavqt daainpgnsg gplvdatgav vgintairsa gsaesgaqgg siglgfaipi
      421 ddaraiaeel irtgrvahad lgvnarsvtd gatdgaqvqn vvaggpaaaa giadgdvvvd
      481 vagrpiasad elvvavreha pgeqvpvglv rqgrpltvtv tlgqr
//
LOCUS       WP_357545967             418 aa            linear   BCT 28-DEC-2024
DEFINITION  aspartate aminotransferase family protein [Pseudonocardia alni].
ACCESSION   WP_357545967
VERSION     WP_357545967.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..418
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43144
     Region          4..415
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 maqlspllkq atpvqaarge gvylydtdgr rhldftagig vtstghchpt vvaaaqeqva
       61 tlihgqyttv mhqplltlve rmgdvlpegi dsvfftnsgs eaveasvrla rqatgrqliv
      121 afdggfhgrt mgaaalttsg akiragigpm mggvafapfp yayrygwsee qavafalsel
      181 drqlastapa sdvaafivep vlgeggyvpt ppaflhglre radrhgilli adevqtgygr
      241 tgkfwghqha egltpdiivt akglasgfpl saiaapkalm ekawpgsqgg tyggnavaca
      301 aalatlevvq geglvenarv qgekllagvr daaqgiaaig dvrgrglmvg iefvdadgkp
      361 dgataakvha aaaaqgllll tcgvhgnvvr mipalvvtae qvdeglalwt kalndals
//
LOCUS       WP_357545995             464 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Pseudonocardia alni].
ACCESSION   WP_357545995
VERSION     WP_357545995.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=48538
     Region          23..417
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 msaarthrsa eeigrtergp rplpalgrtk evplpdvlte tlpngltvla arrpgvplve
       61 tvlripaasp epiadaarta gtevlaetil tgtagrdrig iddalasvgg elgvavdpey
      121 lqaggsalat glptvldvla dvltaathsd aevarersrl aeriavaraq prtvarealm
      181 rrrfgdhpiv semptaeava avtpervrel hadlvvpdga slvlvgdidp eaaiaevarr
      241 lggwtgdhpa rwlsappvpq agdlelvhrp gsvqsqlrlt apgldrtder ytafqlanlv
      301 fggyfssrwm eniredkgyt ygahsgqefv pggavlglda dvasdvtaaa lletryelgr
      361 mvavppteqe vtsarryaig sllisldsqs alagtlsalh aagldvdwlr drprrleavt
      421 vdevaaaava lfaptrftgv vvgdadvvgp plaalggvvr gggr
//
LOCUS       WP_357546043             249 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357546043
VERSION     WP_357546043.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 249)
  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 249)
  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..249
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..249
                     /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=25475
     Region          1..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 mnnaqrravi vtgagtgigr atarafcadg vhvlavgrra aplaetaagh plitpltvdi
       61 tapdgpdrlv gaaldrygrl dvlvnnagia gggplaelde kaarhqldtn llapvrlaha
      121 avaaladtrg mivnvttsvg qrawpgssvy aagkaaldsl trswavelap rgirvvavap
      181 gaidtpigeh qgltpeqraa vrrwqlahtp larigrredv awairqlcdp aagfvtgvvl
      241 pvdggavva
//
LOCUS       WP_357546053             448 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Pseudonocardia alni].
ACCESSION   WP_357546053
VERSION     WP_357546053.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..448
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..448
                     /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=45802
     Region          6..439
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mfsgqdeler fllsrpatgr rngaapdapr ertrevlagl gdpqeavrtv hvagtagkgs
       61 vcafvasllt rhgfrvgvqa sphvygirer frtgdlpvra dvlddrlaav arsvaavear
      121 rgercsffev vtalgfaava gradyavvet giggrldptn vvarpdklav ltaigldhvd
      181 mlgstlgeia tqkagilpvg gravlargvp esdaavarea vrrdtlvdvv dvaaaaalar
      241 tgpsgttvdl agwsdvplgl hgrhqagnav lalhavsvla rrdgwrldpl avrrglalas
      301 lpgrferrtv agtpvvldga hdalklsala ttvaethpgr pvtwvlalar dkdlgeavra
      361 vagagarvva tglpggehas rhwspseiaa aagaagvpav avadpgdavd halttgggdp
      421 vvvtgsfrlp gavtsrldrp avpegqpa
//
LOCUS       WP_357546115             350 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pseudonocardia alni].
ACCESSION   WP_357546115
VERSION     WP_357546115.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=33981
     Region          44..348
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mttaappgdd ptavlrrira rsrrrratag lavtaaalaa fvaslsvgaq glgpgdvlaa
       61 laglgtprte lvvlqlrmpr altallvgaa lglagalfqr vlrntlaspd vigvgagaav
      121 gavtasvvlg lsatgtsaga vlgavaaall itvlarrdgl ggtrfvlvgv gigsaamavv
      181 sylmitaslt taqqtlvwlt gsvtetgwst avplalacav lvpaglllar alprlelgdd
      241 tatalglpvg rvraallava vllvaaavaa agpvsfvalv sgplaarlag pgraslphas
      301 gvgaalvlla dvvartliae valpagvvtg aigapyllwl larsrtggtp
//
LOCUS       WP_357546117             352 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pseudonocardia alni].
ACCESSION   WP_357546117
VERSION     WP_357546117.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=34698
     Region          48..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 mtapattapv ppppgapatv rrrrwpaavg laaallavaa lgllvgarpl apgfvldvlt
       61 gavdrtspda lvvtevrlpr tvlavlagaa lgvagvlaqg mtrnpiaepg ilglntgaal
      121 avvlgiallg vdtltgyvwf gfagaavaav vvagvagigr rgsvspatla lagaalaagl
      181 qsittlfllt dpqafddhrf wqvgsvagrd lgiaaqaapf vvaglalalt cgprlnalal
      241 gddvarsfgr avgtdravcg valvvlagaa taaagpiafl glavphlvrr lagtdhrvvl
      301 plaalagpvl llaadvlgrv vtppgevqag vvtavvgapl fvalvrrrrf lr
//
LOCUS       WP_357546157             495 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Pseudonocardia alni].
ACCESSION   WP_357546157
VERSION     WP_357546157.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..495
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51025
     Region          53..493
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mpdrataaap vvvepegrpf ggstapaeld asgpdaagra vlaelaaald adrvltdpdv
       61 vrpyvhdeae waeygtplcv vrarttadva atvracaahr vpvvargagt glsgganavd
      121 gcvlvslerm taireisage rlavvepgvv nddlrsacae qglwyppdpa sapwstiggn
      181 vatnagglcc vkygvtrdyv lalevvtatg evvrvgrrta kgvvgydlag lmvgsegtlg
      241 iiteitvklr parpaaprtv vgffdsladc gaavaavteq glqpavfelv dreclaavna
      301 wrnaglptga aalliaqtdl pepaaqaead ailaaftahg atdamastde tesealfaar
      361 rmaypaleql gmgmltedvc vprprmaeml ariedigrrr gvriatvaha gdgnlhplml
      421 tphddpdard rtraafdeii gaavelggtv tgehgvgllk rdgmerelgp evlalqravk
      481 aaldpdgiln pgkav
//
LOCUS       WP_357546183             155 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Pseudonocardia alni].
ACCESSION   WP_357546183
VERSION     WP_357546183.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 155)
  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 155)
  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 155)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..155
                     /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=17527
     Region          20..144
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 martdhfhdp dapkatsivi avsafvtder drllmirrtd nnlyalpggr helgetmtet
       61 avretheetg irievtslvg iysnpdhvma ytdgevrqef sicfrarpvg geprtsdess
      121 evlwverael dsidvhpsir lriehgfsrr dpyyt
//
LOCUS       WP_357546296             518 aa            linear   BCT 28-DEC-2024
DEFINITION  APC family permease [Pseudonocardia alni].
ACCESSION   WP_357546296
VERSION     WP_357546296.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 518)
  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 518)
  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 518)
  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 518)
  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..518
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..518
                     /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=54354
     Region          26..483
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtvpeptrrd pspdadgdgg glaefgysqt ldrsigkfas faagisyisi ltgtfqlfyf
       61 gfgtggaayw wswpmvfagq fmvalsfael agrypvagsv ynwskqlagp tvswlagwmm
      121 ftasvvslaa valaaqltfp qiwsgfqlvg dasdagdaav ngvllgaili vlttvinavg
      181 vklmarinst gvfieliaav vivvalllsi rnpvsvlfet papaaggggy fgtflvaala
      241 sayvmygfdt asslgeetvd prrtapaail raviasfvlg glillgiila apdladprlg
      301 skdgggqlvl levaggtigr iflitisiav ivcllavhta airlmfamar dnalpagsvl
      361 aridpkhktp vvpaivvgvv aililvanvg vpevftavts vaiimiyiay llvtvpmlvr
      421 rlrghwpdeg qkgyfslgrl glpvnvlavl wgasmainla wpreevygtg wlrfiaflfi
      481 gvvalagltw frlrgrhglg clpehrakei eqgmgeta
//
LOCUS       WP_357546289             213 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Pseudonocardia alni].
ACCESSION   WP_357546289
VERSION     WP_357546289.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 213)
  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..213
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..213
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=23035
     Region          4..110
                     /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 mtfeirreia lpaspdevwr aiatpegqag wfmtvdaasg dvveepprrl eqrfgtqave
       61 yvveaagggn avlrfvhsgi reedwgdewe tmtglgwdly lftlgeylrh fagrpavyae
      121 aeaparrdvw pdvlaalgdp legdrvdtpv gsgvvdirtg thlgirtgsa lvrvhdrsli
      181 gmgtavghhe tgpadrhala atwsawleav aqp
//
LOCUS       WP_357546317             452 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Pseudonocardia alni].
ACCESSION   WP_357546317
VERSION     WP_357546317.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=48932
     Region          12..452
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtesrtvree fhevvvigag maglmaatal adrdvvvlea sdrpggrvdt vrkgdywinm
       61 gtqftegtgp lidalhrhhi slgtlegksv alslggkqvd tsnpfsvmfr ssmtwrdrlg
      121 laavgtrila nvpflemspe nrlakrvrar lddrradfvl rgvrselard mvrswsgqwm
      181 gcepeetaat qfvfsmgill tdpekvdnlt lpeggnqtlt diladdlggr irlgtpvrtv
      241 ewtddgvvvd yedasgpari rarraivavp advavtimpg lpatyraafe sirygryvvv
      301 gfftheegpq qwddflavst pelsfqavfn haaalrrggv rtpggalacf aggaeadalf
      361 elgddeivsr ftadllrlyp elegkvepgi lrrhprvvpf wapggrasla tlrdplgpvh
      421 lagdyqldvp sladaaasge qaarrvletl sa
//
LOCUS       WP_357546370             844 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Pseudonocardia alni].
ACCESSION   WP_357546370
VERSION     WP_357546370.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 844)
  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 844)
  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 844)
  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 844)
  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..844
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..844
                     /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=85541
     Region          59..824
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mspvagdvsp vapplhpwaq davavaeqlg tdpdeglgga avagravada drpspgldrs
       61 laasvlaqlr etmilvllga aalsvavgda gdaavivlvv vlnttvgvaq erratgavaa
      121 lraraaprat vvrdghrhev paaevvvgdl lvlgrgdvva adarlltahd lqvdesaltg
      181 esqpsdrrag pacaedtpva drstvvhagt lvvrghgrav vtavglrtel gtvdvllqrr
      241 rppptplqrr larlgraisl gvvvacalvg vtglargepw plvvltalsl avaaipeslp
      301 avvalalaga trrmarlgvi vrtlpaveal gsvtvlavdk tgtlttgrit ctavwhpgtg
      361 tteltgplpa gparsvleaa vlggdaeegt pgtegavara aaragldlra vrarrprtav
      421 rpfdarrrct vsrhdgpdgp levvvgapev vlpgradaaa vvdawaraga rvlavragpq
      481 etgllrlddp vrddaaaavg aartagvrtm mitgdhpata aavaaavgld tgerdglpav
      541 haradpgtkl alveslraag eivamtgdgv ndapalrvad vgvamgergt evakeaadvv
      601 lgddglgriv aavaegrrva dnvrrfvryg lagglaellv mvagpflalg lpllpaqilw
      661 vnlvthglpg vamgseaaea dvlsrppqpp rqgiltrrtv vetavlgvvv agcslvvatt
      721 aaatgrpwqt mlfvtlalsq lglalttrsd stplwrlpvr snpflyvaaa tsvlatfavv
      781 ylpgagllfh tvalgpaela iavgaaavps vlveaeelrr srrrahpgqd qsrtsgassp
      841 vssa
//
LOCUS       WP_357546382             914 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Pseudonocardia alni].
ACCESSION   WP_357546382
VERSION     WP_357546382.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 914)
  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 914)
  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 914)
  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 914)
  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..914
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..914
                     /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=93465
     Region          31..898
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mtdtrhrpag papgtggpad hppaggvpdp repaarllrd lrsgpaglsg rdaarrlarf
       61 gpntparaea rstwralrrq lthplavlll vaavlavaag taqlgtailv vvvlnagfaf
      121 lqerhagrav ealgrylpph arvrrdatvr svpaaelvpg dvlllaegdr vpadarllsg
      181 glqidasalt gesvpvvrda sapdtaaral dspvllfsgt gcvagaaeav vhatgahtei
      241 griaalagtr ptdesplerq vrrvarliaa vavgvgvafv plgvvaglsl tealvlavgl
      301 ivanvpegll ptitlalavg vramadrgal vkrlsavetl gsttvictdk tgtlttgtmr
      361 vvdvrgpgpe tsppgpafwt alarcstadp rtgagdptel allegaaaag agvdagvrda
      421 erlvlhafdp hrmlmstldp gpdgpvlhvk gapgavlarc vlpadrraav edavaamagr
      481 glrvlavarr dpaadpaaah paaadpgard aaesgltllg lvglldpprp eapaavasch
      541 hagirvhvvs gddgrtaaei arrvgigadr vvdgavldam tepelerffa gcgevvvara
      601 apeaklriad alrargevva mtgdgvndap alrhadigva mgrsgtevar eaatlvltdd
      661 dvatvvagve egrrvydnvr kfvvyifghl lpelvpflaf alsggliplp igvlqilaid
      721 lgtdllpala lsrepaepgl mdrpprprse nvitgemllr awglmgpvaa vlatglflav
      781 lvrggwspga atgpgsplht tyrqattatf aaivacqvgt afaartrrvs lrsvgittnr
      841 lllgalaael vfaaaaiflp vansllgttp ppawvfacll pmpllvwgtd eayrgvrrar
      901 eparlhpapp gagr
//
LOCUS       WP_357546416             477 aa            linear   BCT 28-DEC-2024
DEFINITION  amidase [Pseudonocardia alni].
ACCESSION   WP_357546416
VERSION     WP_357546416.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..477
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..477
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49054
     Region          5..451
                     /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 mepgeyaeld atalaalird gevtaeevar aatealaavq pavnglvdgp faspldhaad
       61 gpfagvpfgl kdliahaagv ptrsgtrllg dgvpmptdth lvarfrragf atlgltatpe
      121 lgfnanteav atgsvrnpwd lsrspggssg gsaalvaara lpvahandgg gsiripaaac
      181 glvglkpsqg rtspgpdyad pllgmgvefv ltrtvrdcaa vldavhghep gdryalpdpv
      241 rpyadeahag srplrialht apfsgdgpvd ascveateaa grvleelghh veraapqldg
      301 avfddanfia wtafladgvd glaealgltp gpehleattl acvehgrtlr aadlfaadrv
      361 fnatrrtvae fhrtydlilt ptmnvpntaa gyldaddasl gargwydrif stagftalsn
      421 mtgnpaislp lgtstegwpv gvqlvapymg eatllalaad leralpwadr rpgtvvg
//
LOCUS       WP_357546449             435 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudonocardia alni].
ACCESSION   WP_357546449
VERSION     WP_357546449.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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
REFERENCE   3  (residues 1 to 435)
  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..435
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=46192
     Region          <70..>201
                     /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          170..430
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msittrmrds lrrlpalrss pseaptlver avalgrrnpv vldavlaall iwvavswtle
       61 gkgvrsdmri ealvvsvlaa lpvplrrvhp mpaaiatavv alvcsfalpg tmaafllpsl
      121 vmgysavayg prwagwlalv vltvgvfgpf vargpaalfa spdmtplval allgamatvp
      181 llvwllgslr raahrrtldl rernrllees rrqevrlell aersrisrev hdvvahslsg
      241 iiaqadggqf aaqrdpakav evlsgiastg rsalsdvrgl lsmlrdtgpd ddtdtdparp
      301 qpgagdvpal veqvrtgglp vdlrtigtpr elptgpgltv yrivqesltn vikhagpgvp
      361 thvdlrwttd eltvrvhdeg argpiptppr gghgltgmre raalhggsve agphadggwt
      421 vrlrlpltpp arger
//
LOCUS       WP_357546453             116 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudonocardia alni].
ACCESSION   WP_357546453
VERSION     WP_357546453.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=12306
     Region          <30..97
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 metapedpqp ldpelladaa aafgmlaats rlqivwllad gprdvgtlat tlgqpvatvs
       61 qhlaklklag lvrarregrh qiyviadagm vevvrtvvaa qhrrrepdav rgrgiv
//
LOCUS       WP_357546459             608 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Pseudonocardia alni].
ACCESSION   WP_357546459
VERSION     WP_357546459.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 608)
  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 608)
  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 608)
  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 608)
  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..608
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..608
                     /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=63367
     Region          46..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 mvyapprprp rgqgprggrr rsaaddprfr lrlawvalaa lllvsgaklv vvqtvqagtl
       61 tadaekqras rivipaerga isdrngavla fsteskalvt nprlinstkg adavayknrm
      121 adavaavthg dpeelkraln sdrgyvvmat avdpgpardl rtrfpeiaee srearqypng
      181 tlasniigaa twsadaqkli griglessdd gllagrdgfq iadtaegsgt vipgsvrseq
      241 aavsgsdvql tidsdlqfqv qrmladyagr sgarsgsavv ldratgqvla ladntsfdpa
      301 qllsadpnsl gnkgvttpfe pgsvnkvvtm aaaleagvak pddvldvpgs ievadrtikd
      361 awehgvdhyt ltgvlakssn vgtlmtaqkv gedrfsdmla kmgigqktgv glpgesggrv
      421 paratwsgst fgnlpigqgl smtvlqmagm yqaiandgvr vppriiaatt gpdgvrvpte
      481 apepvqvmsp qtaqtlrtml tavtqkahgq sgtgpaaavp gyevagktgt aqqvdpatga
      541 ysrsqywitf agmlpaqdpr fvigimldap kggtsaaplf hdiasylaqr davpvqtvpq
      601 pvqtlqir
//
LOCUS       WP_357546463             339 aa            linear   BCT 28-DEC-2024
DEFINITION  cell division protein FtsQ/DivIB [Pseudonocardia alni].
ACCESSION   WP_357546463
VERSION     WP_357546463.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..339
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..339
                     /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=35781
     Region          130..339
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mssdeqdtgd drardgarsp grrdpeqerr aaerarrire rraaerraag apaadghdep
       61 depgaagdra adtdevagpa grgsgrgaaa avrertaara aersrsrdpr yrrrrlvavl
      121 ataavvllgv saagwwalgr ygppvatvrv dgtrqipvrd veaatgdqtg vplaavdtdg
      181 vaarvsaipg vaavevdrsw pdtlvvvvte rtpaalldtp dgpklvdvtg fvyrdappdv
      241 rlprlqlprv apddpatlaa vgvlqalpvp vrdqvqtlsl ggggstfelg ltedrrvlwg
      301 pwsdtdrtaa rarvlgpvlq regavydvss pslvtvrqr
//
LOCUS       WP_357546540             165 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudonocardia alni].
ACCESSION   WP_357546540
VERSION     WP_357546540.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 165)
  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..165
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..165
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17377
     Region          43..107
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msrageapth ggrrprsage taadelreng rraaedawsa qvnalggfir aqrqmaklsl
       61 remaamtkvs naylsqverg lhqpslkvlr siadalhlnt dqmlsragws vgdpdtagda
      121 aaaeeaapva asppgveaai esdarlsdeq kaallgvyrs fvqrd
//
LOCUS       WP_357546553             437 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Pseudonocardia alni].
ACCESSION   WP_357546553
VERSION     WP_357546553.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=46715
     Region          1..370
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrphritaav vtvlalllag cgagsrtpaa tatlvpcafp ppaqsldvrv laynssavdp
       61 ftntmvrscs rdgvtlrhep idfagqtqkt iatlsgrygt ydivetyglv vpqfastgkl
      121 rplddlvary reeygldrls pemlaalsyd gklyglptma qpftlvyrrd vfdrlglapp
      181 rtfaelreva arvqrdggir yplalpllas adiataydaa lgslgtdyvd rgtgrpnftt
      241 paaaraftel rsllpfmdpq vttfaqpavq qqmyngsaai aimysgrmfd lvqernsrfs
      301 qefafappps vaggdvlyns lsvdgwaipa ntevdpdllf rflaasvgpe saraavpaaf
      361 psrlgsvtpa sspfapaqle algkapppep fpwtsrisva trpvvadvla grvpveqgqq
      421 rmqdiataiv aeyravg
//
LOCUS       WP_357546604             217 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Pseudonocardia alni].
ACCESSION   WP_357546604
VERSION     WP_357546604.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=22961
     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 mgvaiagaga vgrsialelv esdhrvmlie relthidpna vpeaewvhad acelssleda
       61 giegcdvvia atgddkvnlv vsllaktefg vrrvvarvnd prnewlfgen wgvdvavstp
      121 rllaalveea vavgdlvrll tlrqgqanlv evtlpedtpl agrpvrvlel ptdsalvtil
      181 rggrvivpqp ddaleggdel lfvattavee diraalm
//
LOCUS       WP_357546562             351 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Pseudonocardia alni].
ACCESSION   WP_357546562
VERSION     WP_357546562.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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   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..351
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..351
                     /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=37407
     Region          1..350
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 magvtydavt rrypgstraa vdaldleiad geflvlvgps gcgkttslrm lagledvdgg
       61 ririgerdvt gvapkerdia mvfqnyalyp hmsvaenmgf alrmagtaka eiahrvaeaa
      121 rildleayle rkpkalsggq rqrvamgrai vrqpqvflmd eplsnldakl rvqtrtqias
      181 lqrrlgvttv yvthdqveam tmgdrvavlk dgllqqcaap gelyarpana fvagfigspa
      241 mnllslpvta dgvrlggvdv avprgagdti tlgvrpedlh laddgiplei dlveelgada
      301 yvygrtrldg vehpmvarvd grrppsrgtg vhlapdpart hlfaadgarl g
//
LOCUS       WP_357546699             432 aa            linear   BCT 28-DEC-2024
DEFINITION  cupin domain-containing protein [Pseudonocardia alni].
ACCESSION   WP_357546699
VERSION     WP_357546699.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..432
                     /product="cupin domain-containing protein"
                     /EC_number="1.14.11.47"
                     /GO_process="GO:0043687 - post-translational protein
                     modification [Evidence IEA]"
                     /calculated_mol_wt=45093
     Region          41..331
                     /region_name="RoxA"
                     /note="Ribosomal protein L16 Arg81 hydroxylase, contains
                     JmjC domain [Translation, ribosomal structure and
                     biogenesis]; COG2850"
                     /db_xref="CDD:442098"
ORIGIN      
        1 mrtelsepta gagtpatgap apsgaraasg ngalarlvgs dtdtfgarhw gttallrpga
       61 dtgafrdlld ldgvdellsr rglrtpflrl arngsvvgsg dftgpggvga eigdqvrddr
      121 vaalfgdgst vvlqalhrvw pgvidfctal aedlghpvqa nayitppqsq gfsahydvhd
      181 vfvlqlagqk hwrvhapvht dplrsqpwsd hgdavaarar ddepvidrvl epgdvlylpr
      241 gwlhsatalg dvsahltvgv hvvtryalve sllalvasdq rlraslplgv dladpeqlap
      301 hlgavraalt galaavpaed vsrrvrgrvw sggrpepvrp vasaafardl apgdtvrrrl
      361 gvhhrlvpgd drvvlelaek tltlpavvap alvallgggt htvgglpgld addqvvlvrr
      421 llregvlvpa ta
//
LOCUS       WP_357546702             332 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357546702
VERSION     WP_357546702.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..332
                     /product="phosphotransferase 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=36445
     Region          6..274
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msptqrrldp dqirryvaas lgpaprvvec gpltgggfaa vwwvtlddgq avvlkvgppp
       61 svpllryerd migaearylr lvaerapavp appllhhgsd pvlgdwlltg llagrtlwdl
      121 teagvdtavv eaefgvalat lhgitgdryg ydggrasadt wrgaylamvd dmladaadwr
      181 vplpapagri relvdrhahv ldavrrpall hfdcwagnvl atdgpdgtpr lsglvdgery
      241 lwgdplmdlv spllfrrted epehpvvray qaispfpfda dvrrrlglyr lylyllmtve
      301 mpsrgitaes epwrvtrlpe lldeelsdld kp
//
LOCUS       WP_357546760             480 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Pseudonocardia
            alni].
ACCESSION   WP_357546760
VERSION     WP_357546760.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 480)
  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 480)
  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
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..480
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=49880
     Region          3..475
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mhiavlprer artapgapcl adehrtldnt gfaaavdaaa galhvagtgp gdvvavvlpn
       61 rvelvvtlfa awrlgaavtp vnpaltadea ghqitdsgav vvvgeraasp lvtldvaela
      121 gdpavapdpv tddgatalli ytsgttgrpk gvvldhanva amcgmviagi glgaddhsll
      181 vlplfhvngi tvsvlsplla ggrttiagrf raetfldtva rvrptyfsav paiyamltal
      241 pareadtssl rrvicgaapm pvelvarfee rfrvplvegy glsegtcast inpwdglrkp
      301 gtvglplpgq rvalmdpegr fvdhgpgevv isgpnvmrgy lnlpeataet irdgwlhtgd
      361 vgrfdddgyl vlvdrikdmi irggenlypq eienalyahp avheaavvga pdpvlgeipv
      421 ahvvlrpgaa atpedltahc aqrlarikvp triglvdtlp rnavgkvdkp alrrapvpag
//
LOCUS       WP_357546809             708 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Pseudonocardia alni].
ACCESSION   WP_357546809
VERSION     WP_357546809.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..708
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..708
                     /product="PhoX family protein"
                     /calculated_mol_wt=76051
     Region          56..697
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mahscpgdap qagprralpl ldrvrhgrqg ltcryrcgda csrpepnpss nayfgdvmqa
       61 vldrrgmlra gaviglgaga gvalagtasa aeptpaapah plgadvaapa qarpprglqy
      121 etvapnldda irvpvdyasn vvirwgdpmf pdapefdfen qtaaaqarqf gynndfcgil
      181 pidgpgrryv mfsnheytle plmfrgyded aptpeqirig maahgggvve vtrdlrtgel
      241 rydragrlnr ritadtemvl dgpaagaevl rtkadptgrs vrgmigncag gttpwgtfls
      301 geenfdgyfa sgpvtderak rygfsegpse rrwetvdprw dlaqepnean rfgyiveidp
      361 hdprskpvkh talgrfkheg atvaltrdgr pvvymgdder fdyvykfvsd krmrrghsra
      421 arehnatlls sgtlyvatft gdspaaeitg tgalprdgrf dgsgqwkpla stttsyvdgm
      481 svadvfvftr laadkvgatk mdrpedvepn prtgkvyiac tnnsdrgkvg akagpdeanp
      541 rnanqhghvi eltetrddpa attfawnill vcgnpddpst yfggfdksqv spitspdnva
      601 fdpygnlwvs tdssqalein dglygvvleg pqrgstrlfa svpvgseccg pvvtenfvlv
      661 svqhpgdvdd aspekpashw pdggaaqprp avaairhlkd grpakigv
//
LOCUS       WP_357546812             235 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Pseudonocardia alni].
ACCESSION   WP_357546812
VERSION     WP_357546812.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 235)
  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 235)
  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 235)
  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 235)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..235
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..235
                     /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=23825
     Region          5..93
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mtsyllvpgf widatawsav addlrarghd vaaldlghep gataetrvde vltalgdagd
       61 pvvlvahsga gpvcaavaer argrlahlvf vdtgplpdgv aqidftppdg qaairatlae
      121 hgalpmpara eldaagssta gipdavfddv rarsvaeppg vvltgarrgt pdpslpktvv
      181 acsfapdevr glidagvpaf aemsdpewti ialptghwpm lsepsglagv ldglg
//
LOCUS       WP_357546908             151 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357546908
VERSION     WP_357546908.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 151)
  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 151)
  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..151
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..151
                     /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=17390
     Region          2..141
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mkrpedepqi gallrmawea lhvevygqlh aagfddlrev hrpllryppi dgmrptelaa
       61 qlrlskqatn dllrdlekln yvrldrdpsd grarvirytd rgwrlfrtgs qlsrdvgrrw
      121 aqaigqkryd qfsatlrtiv elgrpaeqtp s
//
LOCUS       WP_357546909             336 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Pseudonocardia alni].
ACCESSION   WP_357546909
VERSION     WP_357546909.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..336
                     /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=33761
     Region          13..332
                     /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 mttapavpat tvavrltapg rldptpvatp apgpgevlvr vtavglcgtd lavrsgarpv
       61 palpwtvghe gggrvvavgd gvdpgrvgev vavepniacg rcrfcaagrt sacpdrrslg
      121 vnapgllagl vavpagyahp lpagldpdla ervvacvepr vvtraalrra apepgsrclv
      181 vgagsqgtll catllaaghv pvvaephdgr rrraldlgae elvpgevfat vfetsgapaa
      241 watataavdr agtllligqh dgpstvnthd lvqrqvtvtg sliydhphdf aaaladlpav
      301 adtlvglmep epfgpgraga afdavagadr kvwlap
//
LOCUS       WP_357547006             435 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudonocardia alni].
ACCESSION   WP_357547006
VERSION     WP_357547006.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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
REFERENCE   3  (residues 1 to 435)
  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..435
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=45086
     Region          199..435
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msapgtagpd vsagperrll artlarhavv taaavvlvca lvaagvwwla haeaerraee
       61 vsrrvatavv vgladrdlat agpagrerll adlapfratg mvsrvkvwlv egptarlvfs
      121 deariegltr rfdpvlaarl dggaavvlpv pddgehryeh gdglrevflg ftdgagrpar
      181 levyvpvdvd gatahavgll lppavagmll vaaavlplsv alarrrerer terrdaalyg
      241 laagelarrd larrlhddvl ptlagaglml dlaparpell draratvgdg vvrirsvlda
      301 lhpadvdaag lpaalaalaa ggdppaavvt tgdpagaldd rgavllhrva sellrnarth
      361 arartvevgl hvaagrarlt vtddgtgfdp grgpepghig lllvrravad aggtlevrsa
      421 pdrgstvtvv lprrg
//
LOCUS       WP_357546925             260 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein, partial [Pseudonocardia alni].
ACCESSION   WP_357546925
VERSION     WP_357546925.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,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 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         <1..260
                     /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]"
     Region          <3..126
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
     Region          <27..>232
                     /region_name="MRP_assoc_pro"
                     /note="multi drug resistance-associated protein (MRP);
                     TIGR00957"
                     /db_xref="CDD:188098"
ORIGIN      
        1 sairdivmek idmvglvgae gklpgeisgg mrkraglara lvldpkiilf depdsgldpv
       61 rtaylnqlii dlnamtdstf livthdinsa qtvpdnigll yrkhlamfgp revlltsdep
      121 vvaqflngrr egpigmseek daaqaareme eagelegrpp mkpqlvastg mpdrqavhrr
      181 rerveammhe lppsaqeair eqhadsdaqa gggpsqdgtt rqmarsgatv sddrptdihp
      241 ritddtpdpg grhqlsggdr
//
LOCUS       WP_357547009             529 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Pseudonocardia alni].
ACCESSION   WP_357547009
VERSION     WP_357547009.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=53063
     Region          43..492
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mllrrspprt apagppapvr lrrrpprall gaavvvaaca alplvwlvvr vagadpgrva
       61 allarertlt lalnsavlva vvgagslllg latatalvrv rlprpglwwv laalplavps
      121 yllafavlav rpearglgpl avvlvlactp yvtlpaaaal raadtgpeda artlglgpvs
      181 afcrvtlpqa lpaalagtll aalytladfg apallryesf twavqaayeg tvdrtgaavt
      241 alvlaaatlg lvaaeravrr rftgaragta ptaaapvrlr paagaavvag lvavaavtlv
      301 gppavlvgrv vaaggvdadl prlavaagwt lllsgaaall avamalpvgv laaryrsrav
      361 aatesvaylg qglpgvvvgl alvflslvlv palyqtaavl vfgyailflp kalgatraav
      421 ervpveaeev artlgrtpws twwsvtapqa apgvaaggll vavtamkelp atlmlrptgi
      481 dtlatrlwaq tslgafgaaa paalalllla cvpaallvra ttggpgger
//
LOCUS       WP_357547025             517 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Pseudonocardia alni].
ACCESSION   WP_357547025
VERSION     WP_357547025.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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
REFERENCE   2  (residues 1 to 517)
  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..517
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..517
                     /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=52165
     Region          5..122
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          242..515
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mllselvarp elrlrvlhgs aadldrsvrw vyptdlpdps rylgggelvv sglvwrrtpa
       61 dserfvaava rsgaaalvag eavfgdipad vvdacrrhdl vlvavpvdvs fgavteavig
      121 alsaargdrl ahtlgrhrrl laafaggael adlagavsag tglvcrvlta aggllagpal
      181 peaerdavva gfltagrlpv tvpagpagaa hlvvpaapgt aratgwlvaa qlppgtaqag
      241 tdavdavgel aaiaaldrsr rregaavarp iaddalaria adtgdrpetr vrlrqagvep
      301 dgtlavvvlr asgvadpadt ahtvlldalv gtgpaavgvq ggdavavvav pgardapdpv
      361 eqvlaavhrl gpglaggrls agvsrpsaad alsgalaeag haaglaaars gpvtsvrage
      421 itshvallag vpddvrrgfa aqvlgpvldh darsgtglle tlevfldesg swnrtaarlh
      481 lhvntvryri grvaeltgrd pssfadrvdl ylalrsr
//
LOCUS       WP_357547022             225 aa            linear   BCT 28-DEC-2024
DEFINITION  urease accessory protein UreF [Pseudonocardia alni].
ACCESSION   WP_357547022
VERSION     WP_357547022.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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..225
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..225
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22653
     Region          4..225
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 maglaslvla darfpggghv hsggleeaae rglvtdvasl haflrgrlrt agrvaacaaa
       61 aaahpagrer laaldaalda rtpslaqrea srvqgkaalr aaraawpspe ldtlvavdrr
      121 phhpllvgvv vgvagespsa aarcvgylav sgpasaavrl lgldpfavna alvaldddla
      181 vvvdeaaala agdpadlpap gapvldlmae shvhhhrerv rlfas
//
LOCUS       WP_357547169             272 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Pseudonocardia alni].
ACCESSION   WP_357547169
VERSION     WP_357547169.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 272)
  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 272)
  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..272
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..272
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28033
     Region          18..266
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtspatgtdp avlvtrdetd psvavvtlnr pakynaltve lkeallaaav evagdesvra
       61 ivltgagkaf cvgqdlgeha aaldadpvda lgtvrrhynp liralneapk pvvaaingpc
      121 vgaglgiala adlriaaegl kfataftgig lstdsglaas lahavgvsra telvllneqf
      181 taedarnwgl vrdvvpagev lgtalelarr laagptraya evkgalrfga vnelpavley
      241 eadaqvrlst trdhqqavsd flakkkpvfe gr
//
LOCUS       WP_357547195             460 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Pseudonocardia alni].
ACCESSION   WP_357547195
VERSION     WP_357547195.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..460
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..460
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48004
     Region          152..419
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mlpdvhrhpv adatlrrlel assrlaaacl aemerrcpwf aglpadqrag valvtqtgva
       61 nfvswlrepd rttpltaeaf riaprdlarr islrqtvelv riaadvfeeh lppladdgte
      121 rhelteavlr fgreiafaaa tvyagaaesr gawdarleal vvdavlrgdt dgalvsraaa
      181 lgwdpaapvh clvgsapgsg pespqlivel rrvaarlghd vlvgvqgrrl vvllhltgrp
      241 arrvadrlae ttsaraaptg pgpapgasav tarvlaevaa hfgpgpvvsg ppstdlatag
      301 aavaealagl aaapghpdap rpvdaadllp eralhgdpaa rrrlaedvla plhdtggell
      361 rtlaaylegg aslegcaral yvhpntvryr lrrigelvgr sptdpreafv lraalvadrt
      421 arasdgpava ahtpltpldp tgehdqevdg vrvpvggals
//
LOCUS       WP_357547297             544 aa            linear   BCT 28-DEC-2024
DEFINITION  (2,3-dihydroxybenzoyl)adenylate synthase [Pseudonocardia alni].
ACCESSION   WP_357547297
VERSION     WP_357547297.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..544
                     /product="(2,3-dihydroxybenzoyl)adenylate synthase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0008668 -
                     2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
                     [Evidence IEA]"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58747
     Region          4..538
                     /region_name="EntE"
                     /note="2,3-dihydroxybenzoate-AMP synthase component of
                     non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1021"
                     /db_xref="CDD:440644"
ORIGIN      
        1 mtlvpypeda vsryrgtglw ggdtiatefh rialrhpgrd avvamegrlt faeldrrtdl
       61 laaglaglgl rpgdpvlfqv tnrldavvaw ygvlkaglvp vatlaahrgy eigeisrrvg
      121 avahlveagl rgfdlvgfae eqrrdhptlr hvlvlgddpr gvsltvlgrd retaaarslv
      181 ervqadidpd avaafqlsgg ttgvpkvipr lhaeywynga eyarswgwta qtrvahlipi
      241 ihnagivcav hgphsvgacl vlgtpdldes lplmaresat hvllghghyr avahpefdaa
      301 travtqvvls gskvppalfe alearglwsg qlfgmgeglf lttrpgapre arlttvgtpl
      361 saldearile pgsegdvaeg evgelcargp ytlpgyfdap ehnaraftsd gfyrtgdlas
      421 fvridgeryv siegrlkdli nrggekinae evellllrhp ritavavvpm pdlrlgertc
      481 ayvvvdgpel tlsevqehfa alqvakfkwp erlehlpdip rtlvgktdkk rlaadiarkv
      541 savp
//
LOCUS       WP_357547326             387 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudonocardia alni].
ACCESSION   WP_357547326
VERSION     WP_357547326.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..387
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39739
     Region          8..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 mdevergrgp lagrtvvela gigpgpfacm aladlgadvi ridrpaagpl ttapppadvl
       61 nrgkrsvvld lkrpeaveav ltlagradvl vegnrpgvae rlgvgpdavw arnprlvygr
      121 mtgwgqdgpl ahtaghdigy ialtgalham geaggppqip lnlvgdfggg ttylvigvla
      181 alleaertgr gqvvdaaivd gashllaaih amlgsgrwed rrgvnmldgg tpfyavyata
      241 dgghmavgsl epkfyaellr lleiprevaa penqqdrsrw palraalaar fatrtrdewt
      301 avfdgtdacv apvlglreaa ahphvaargs vadtggvlqp gpaprfsghp vaapaappar
      361 grdtravlag agldvdalla cgaaqea
//
LOCUS       WP_357547345             441 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Pseudonocardia alni].
ACCESSION   WP_357547345
VERSION     WP_357547345.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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..441
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..441
                     /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=48343
     Region          3..392
                     /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 mttpdhpapr ycvigagaag latvralrda gvefdcfers ehvgghwntd yealhlisar
       61 dvsafrghpm pgdypyypsr lqvvdylndf adaydlrrhi mfgvevvrae pvdpdgrtgw
      121 tvtlgdgter hyagvvvang hlwdprtpev ageftgtvlh ssdyhdvgdv tgdrvlvvgt
      181 gnsgcdiavd vaqdrrhayv vmrsgqlfqp ksffgrpran lpiaklppll aelatvaltr
      241 ivnggaaeyg mpaprswrlk dsppivntql lhwiqhgrie ivptierfdd dkvvltdgrv
      301 lavdtviwct gfhvslpfld eslvprrdgi plrhaatvlp ptveglfyig lcaprggqfp
      361 fydvqaellv dmialrergd valsrefaar eepewrldvm phlwfaqver trkhlaalaa
      421 alptragspa gttpsskvng s
//
LOCUS       WP_357547379             437 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Pseudonocardia alni].
ACCESSION   WP_357547379
VERSION     WP_357547379.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     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=46566
     Region          28..338
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mspvlksqls rrrflglaag aaasvpilaa cggsssggsg gefkfwdmpw gtpeyndisk
       61 qitssfaapa gvspvtyqii qwdnfnqtfa savasrtnpa vstgggfqaf qfadqgaiay
      121 adglvekfrs nglyddflpg aidgmktdkg ivaipwhldp hvwwynktll eqagakvpts
      181 wdevvttgqa lkrigvfgfa tgagsgngha yetpltlmvn ngggifapdg sldvlnprni
      241 eaiefmkqlq gegiidpasv sytndnqmeq wrnrkfglgi dqagqaenvg sdagkelvva
      301 dpipgphgdn ktlvvennim myadtpsqea seafvehfik ssgvfwknnl ingipvlksi
      361 vatpefqkkt nfvtmvekyq pigisysarg etvgvsqaki dgnsamfqfg qavltqgtda
      421 rtaltdlsng ltsllrk
//
LOCUS       WP_357547405             400 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Pseudonocardia alni].
ACCESSION   WP_357547405
VERSION     WP_357547405.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..400
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40623
     Region          55..399
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mttttesatg aapdtarrdp rtllhysrta eattmrmlal vavivlvavv fnvvtdgvfi
       61 sprnltnlsv qvsvtalvsi gvtwlliarq idlssgalia liavliaqse vvhqwpfaaa
      121 vgialglglv cglvngllva kwgipafivt lgafsylrga aylvsdgntv agfgptmfal
      181 gndgvpplls vllvllvtga gvaltvrrla aerarggirl stalslvail fagavatwvf
      241 gsyqgvpwav viagvaiava ilvstqtpfg rhlyavggnp asarragidi trlmiilfvv
      301 aglltaigal vqaarldsgp pttanlmels aisaavvggt slfggkgtig gsmlgavlma
      361 aianglslag vntfwqlvat gvllvvavat drrarkesal
//
LOCUS       WP_357547472             247 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudonocardia alni].
ACCESSION   WP_357547472
VERSION     WP_357547472.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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   Wintjens,R. and Rooman,M.
  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 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 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..247
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27792
     Region          5..61
                     /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..38)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mttnerlrgs ivaarlhptg laerigvdpk tverwitkgr lphrthrvav agalevdeay
       61 lwpeilgqqv tqsasvaell elhptrasvp hdtwrqlygs areamdilty agsflfeqhe
      121 itevlrtksr egvrcrflig detseavrlr aeeegtsggl egriqlhrry lrdvvglpgi
      181 evrthgttly nslfrfdqdl lvnghaygap aghspvmhlr rvpggrmweh fmrsfeevwd
      241 sgtpiek
//
LOCUS       WP_357547600             217 aa            linear   BCT 28-DEC-2024
DEFINITION  response regulator transcription factor [Pseudonocardia alni].
ACCESSION   WP_357547600
VERSION     WP_357547600.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 217)
  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 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   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 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..217
                     /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=23611
     Region          29..214
                     /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"
ORIGIN      
        1 mtsgrdtdra gtadpvdpvv hvvdddddlr qslrfllgsv giqaldypda atflaefdpa
       61 epavvvvdvr mpgmsgfqlq eelldreypa pvvfcsahgd ipmsvralrg gavdflekpy
      121 dtqrilevvq hqqgrarelf aahaaraavr ervetltpre revlalvieg masqavahrl
      181 gtsvktvdvh rarikaktga eslgtlvrdi lthrvdv
//
LOCUS       WP_357547678            1094 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Pseudonocardia alni].
ACCESSION   WP_357547678
VERSION     WP_357547678.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia alni
  ORGANISM  Pseudonocardia alni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 1094)
  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 1094)
  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 1094)
  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 1094)
  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 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Pseudonocardia alni"
                     /db_xref="taxon:33907"
     Protein         1..1094
                     /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]"
                     /calculated_mol_wt=111756
     Region          7..>1085
                     /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 mtaghgtdpv vvvgmacryp ggvrdadglw dllcsdreta tgfpddrgwd lgalhgdgpg
       61 rcatrtagfl dgagdfdaaf fgmspreavs tdpqqrlvle taweaveqag idptslrgtr
      121 tgvfvgaggq dyagvvqnsp ddlaghaltg lipgltsgrl ahllglegpa ltvdttssss
      181 lvalhlairs leagectaal aggvcvmstp aalvghsrqg glapdgrakv faddadgttw
      241 aegvgvvvlk rlsgaradgd pvlavlrgsa ltadgatdgl tapsgaaqer mirdaladag
      301 ltaadvdave ahgtgtpvgd pvearallat ygqgrdpdrp lwvgslksvl ghaqaaagva
      361 gliatvlalr hellpatrha atpstrvdws agavalrtap vpwprgdrpr ragvssfgis
      421 gtnahvivee apatdlsgag drgaapapvt pwpvsaatah dldaqverlr ahttgpgapd
      481 prdigwslat graalrhrav llpgehgpve vardraaerr vallfsgqgs qrlgtgrala
      541 arfpvfaral ddvtaaldah ldrplrdvaw gsgdpaaall detgwtqpal favevalfrl
      601 vtalgqapaa vgghsigeit aahvagvlsl edaarmvaar atlmqalpag gamvavease
      661 devapllgdr valaavngpa avvlagddda vsalaadlag rgrrtsrlav shafhsprmd
      721 pmleefrgvv egltfsepri plvsnvtgel ggaaatdpgy wvrhvrgtvr fadgvrslaa
      781 dgvdvlvelg pggvlsamar dtlgpdsaah avpllrrdrp eetsfavalg rlhalgvpvd
      841 whafhagtga rrvplptyaf ravrywpapp tpgnpgcspg llpawgatep ghdaragtrp
      901 aaaaarpdpa ptpttagdpg edrpgtgpgg ryaamapavr eralldlvrt htaavlghpd
      961 paevgvrsvf kelgfdslag velcdrlsrd tglrlpttlv fgfptpelaa revsallgpg
     1021 pqepcgpela gleaalaglp gegpdrrava erlevlaagl rrpaaqpggp pdedldsvsv
     1081 drlldiidee fdta
//
LOCUS       WP_357547734             583 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357547734
VERSION     WP_357547734.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 583)
  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 583)
  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 16985460
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..583
                     /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=62147
     Region          49..120
                     /region_name="Inhibitor_I9"
                     /note="Peptidase inhibitor I9; pfam05922"
                     /db_xref="CDD:428674"
     Region          129..381
                     /region_name="Peptidases_S8_PCSK9_ProteinaseK_like"
                     /note="Peptidase S8 family domain in ProteinaseK-like
                     proteins; cd04077"
                     /db_xref="CDD:173790"
     Site            order(132,135..136)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173790"
     Site            order(160,193,252..253,281,343,346)
                     /site_type="active"
                     /db_xref="CDD:173790"
     Site            order(160,193,346)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173790"
     Site            order(295,297,320)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173790"
ORIGIN      
        1 mttrsyryrl aavgllatal alsatgpaaa aqpegeivqa ggptavkdsy ivvlkkdmvt
       61 raqvadkard marthggkag fvydaalrgf evslsqsaar rlaanpavdw vqqnhtvsvq
      121 gvqhnppswg ldridqrklp ldsvyhypnk astvnvyvid sgirlrhtdf dnravtgfda
      181 itpggdandc dghgthvagt iggtnhgvak evtlhavrvf dcagngtvag viagvdwvtk
      241 khvspavanm slrvlggslt ldtavtnsin sgvtyvvaag ndyreacdvs parvnevitv
      301 aattnkdarp sfsnygkcvd ifapgsdits awatsdtatn tisgtsmasp hvagaaamll
      361 hshpswtpaq vkdqlikdat pdvvtnagpe spnrllyipg lqikfeipfv fvrdfldkdp
      421 lwrlkeyvdl gfgpivicpr cfgpvlgvpk vdlpldrerm lygmvmagmq nlgrahttes
      481 peearryqea aqasfrkave ltekqslrfs pvgyysdeke evvraenqpl anlashlteg
      541 lavlqeanag gspelvdkam qllntayadf vnaaelggln idr
//
LOCUS       WP_357547728             284 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome c biogenesis CcdA family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357547728
VERSION     WP_357547728.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..284
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=29280
     Region          18..157
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 melgllgall ggvltllspc svmllpaffs yafaspatlv nrtgvfylgl ittlvplgvl
       61 agtlgafvnq hrdmfvtvaa tvvivlglim lanipipgls rsglegtssa svyalgtiyg
      121 lagvcagpll gavltvaavg gnafyggivl lvfaagmalp llvlallwgr lpfvrqlvrp
      181 rgisvgrwrn twtgitsgtl tvligillla tdgttslggl laasdqarle nwvrqktesv
      241 pdflvaaivi ggaigarili riwrkrhaaa apphrveage sprp
//
LOCUS       WP_357547779             304 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357547779
VERSION     WP_357547779.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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..304
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..304
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33107
     Region          6..272
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 msdtlrcsvv iptydratll ghtlaalarq slprtqfevl vaddgstdnt advvagfrdr
       61 ldvtylrqeh dgvgagrarn mgigaargdv cvmidsgvlp hsgclaahva ahdaapgpva
      121 vigyvygfsl dgddaeleql idvhdadati ermaaeplhg dvrdlfyrry dddfadlpap
      181 wvmfwtcnvs artaqlrdvg mfdehfrtwg gedldlayrl hcadarfvld raassvhvph
      241 kknfeaslas ahgnyqymit kyqsplmpll latptinpfn indvipvldl ppdagksdrk
      301 qada
//
LOCUS       WP_357547784             198 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357547784
VERSION     WP_357547784.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=21811
     Region          6..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          91..177
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(94,107,109,120,125,129,163,165,177)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mddelertld avgprlkqlr trrditltdl aeetgisvst lsrleaglrr ptleqllpla
       61 raygvtldel vdapptgdpr inlrpvaagd gstilpltrr pggiqaykfi lpagnddrep
      121 dlrthegydw vyvlngtlrl vlgehdlilq pgdaaefdtr tphwfgatss gpveylslfg
      181 rqgerahvrv aprsnqnr
//
LOCUS       WP_357547830             125 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357547830
VERSION     WP_357547830.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 125)
  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 125)
  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..125
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..125
                     /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=12771
     Region          29..>119
                     /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 mltppgallt pfvafradef dglrlvrlpf vpgirlylad daivlpgqvg earvgpgrtp
       61 fwanawaggq alaryvldhp qvvagrrvid vasgsglvai aaakagaaev tandiapyap
      121 ggrgd
//
LOCUS       WP_357547846             118 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357547846
VERSION     WP_357547846.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=12930
     Region          3..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mvddslsatf aaladptrrs ilarlaegea tvkelaapha mslpsvsrhl svlekaglvv
       61 ksrnaqwrhc rleigpllel dkwmepyraf qarldrleeh lktmmrdrea ggpagadg
//
LOCUS       WP_357547855             443 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357547855
VERSION     WP_357547855.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..443
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..443
                     /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=48845
     Region          8..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 mtsrvgdral vlgsgiagll aartladffg evlvldrdel pdsagyrrgv phgrhahgim
       61 akgqqileqq fpgltdemia agvkagdfng gnrwyidgkr lapsisgllc vpatrpvleh
      121 hvrervrkla nvtildrhdi lgfeatpdrr rvvgvrvrsr aegdaektip adlllditgr
      181 gsrtprwlwe lgydrppedk vkiglayttr hyrlrtdplg ddlaiipapt ptsprgafly
      241 rlpgdpgrye lsltgmlgdh pptdpegfva fakslpvpdi yqairdaepl ddpvsfsypa
      301 svrrryerlt rfperllvmg dalcsfnpiy aqgmtvaaie svvlrrqler gmpdpqtffr
      361 emapevdlaw dfsagadlgf pgvegnrtlk irmanayvar lqkaavrdpa ltnafiraag
      421 mvdppqalmr pgtvlrvlrh sir
//
LOCUS       WP_357547889             596 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding and vWA domain-containing protein [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357547889
VERSION     WP_357547889.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 596)
  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 596)
  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 20696117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..596
                     /product="substrate-binding and vWA domain-containing
                     protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=64520
     Region          52..360
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          315..589
                     /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 mapaptrtrq wlpytaavia gllviagafa lvrqrdagtg rpradctisl evnsstekaa
       61 llvelaeryn gsdrsldggg carvhvsalt sgkateelaa gwsgtglpkp qvwlptsslw
      121 tgqlrrldqa agrvpqtpdr ypsiansplv iampqpkgdl vrqrgplgwg eilglsgrag
      181 wadfgkpewg rftfgkdnpn lstsglaati atyyaavnrs sdltrsdlan pavtqfvrri
      241 eanvshysdd vvdllrdlae adlagrgssr ddmsaivmqe elvhlynegr lsprqdgqeq
      301 grrpnvplva vhpkegtfnl dhpfvvlpsa derqraaavd flafltedvq qesfarlgfr
      361 nherrasaqm lasvgaeptg gltyfeppdp qvveamlrgw gtlrkkanil ialdtsgsme
      421 aavgnrtrlq vaaaaagkgl allnaedrvg lwsfssetpq rpngpyreev rlgdfdqkri
      481 nsriaalhag ggtalyatvr aahhyvldry dpqrinavvv ltdgkneysr dtdlarllad
      541 veldpqrpvk vfciafdres dfatldriak assgkafdat dparideafv klvssf
//
LOCUS       WP_357547901             378 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357547901
VERSION     WP_357547901.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=43306
     Region          5..377
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mgevvkrayk yrfypspeqa ellnrtfgcv rkvynralea rtrawvvdrq rstyvqssgw
       61 ltewkrtdel aflnevssvp lqqtlrhlqa ayvafwdkrs ryprfkskrk srasaeftrs
      121 afrwrdgqlt lakmntpldi vwsrplpega epstvtvsrd pagrwfvsil vedptvkplp
      181 pvtaevgvda gitslltlth pipgmsdeqg kvanprfgqa drrklakaqr dlarkqkdsa
      241 nrakarlrva riqariadrr rdhlhklttr lvreiqtvvi edlsvrnmlr nrrlarvisd
      301 aswgqfrsml eykagwygre vipvdrwyps sktcstcgri nttlalndrt wtcpgcqteh
      361 drdinaarni laaglaer
//
LOCUS       WP_357548186             523 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548186
VERSION     WP_357548186.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..523
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=56067
     Region          18..499
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtdqpnyvhq alnllagfgd realvgggrr ltypqvatev rglagallrh gvrpggavlv
       61 mlgntvespl lqlalhllgc rsmwiapvts rreidefval arpdafvhdp ratdslgaei
      121 aaglsgvpvl clgpggvgpn ltargpapve lpaevpapes flqtsgttgt pklvhhresf
      181 yrqilalaad frtagfpllr hlshspmwla sgqittlfnl ftggvlflre rwdpaafirt
      241 vdaerltstf vtppmlyevl dhpalagadf samfmfnvga gpaaparlrq aiarfgpclr
      301 ivyglseavv icalpgltdd pehperllsc grpygdvtvq irdadgrvlp pgsdgevwar
      361 tklsfagyhg qpeltaetlv dgwvrtrdig hldadgylyl vdrlqdrilt rqrswpiysr
      421 piedalaahp qvraaavigv pdpvagelpy ayvvpapgat vtgdelitlv trelsetwap
      481 gavefvdalp lnrsakvdkr alraryaaar padtdattig tra
//
LOCUS       WP_357548250             978 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548250
VERSION     WP_357548250.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 978)
  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 978)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 978)
  AUTHORS   Rosinski,J.A. 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 978)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..978
                     /product="helix-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=104921
     Region          <2..881
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <918..977
                     /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 mgsdvdtapl vgradilaml rsallggvap ghtaavfltg esgvgktrll aevndglras
       61 galvltgscl digdasplhp lrqalrrlda epteartssa vrgllqvfde etpgpdgaga
      121 llervsqglh avaggrplvl vlddlqwvdr strqlllyll aglsdlqlsv laairaealq
      181 gahplrrvlt elrrlrsvrv ldlapldrag tdelaaaiag aplppdaadq mwrrsggnpf
      241 vveelardlr dgrdglsdtl revflarvda lpqhahavvh avaagvepve hwllaevvrl
      301 seaelieavr aavahrllig addgyrlrhr lvaevlahel lpaeraalhr ryaevltsat
      361 aelhqarlah hwrlagepgr alpasmaaar eaerlhgyae ahrhwsaalq lasvpaadpr
      421 gvdrpaevav graellkhta etahqcgeha ralalleela gepdgpracv lhirraryla
      481 aagrsalaea eyrqaltddd ctprerataa ahlaelllhl gryaeagdqa realelagav
      541 dgttsevvla saalgyseaf ledpdgglav mrqaletaer sgrpedvaca ylhlaelltg
      601 plnileegvv varrgaerva elglgrtwet rllaiatngl frvgqwteae kvvaaalrhr
      661 psgadavell larcrlsvgy gdieasdrdl eavatmlagg garhvlpmli lraglamwqg
      721 rhdlarqavq rgltesrsdd vivlatlawh glraeaeaya srtiavdptv vrrlrevvdr
      781 vagrsekapa pvryvadafl alcdaeisrl ddgrgdpelw grsatewdrr nhpypaaysr
      841 lrqaeallar rsrvatagkl lrqayqmaqa lgavplssei rtlagrarvt leeapaarpa
      901 prpraavpaa ppsadelavl tarerevlaa vaegltnrei gqrlfisert igvhvshifd
      961 klqvrtrvqa saiflrnh
//
LOCUS       WP_357548256             159 aa            linear   BCT 28-DEC-2024
DEFINITION  FluC/FEX family fluoride channel [Micromonospora sp. NPDC048999].
ACCESSION   WP_357548256
VERSION     WP_357548256.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 159)
  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 159)
  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 159)
  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..159
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..159
                     /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=15695
     Region          34..142
                     /region_name="CRCB"
                     /note="CrcB-like protein, Camphor Resistance (CrcB);
                     pfam02537"
                     /db_xref="CDD:460582"
ORIGIN      
        1 mnrppefpvd pdvdlrvpad rgelnahpaa vlgaiaaggv lgalaraglq aafphpptgf
       61 pwatfginvv gslligalma vltvrpagpl vrpflgvgvl ggfttfstyv vdtqraaaag
      121 apgtalayla atlvgallav wagdavagrl lsraagaar
//
LOCUS       WP_357548260            1034 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548260
VERSION     WP_357548260.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1034)
  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 1034)
  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 1034)
  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 1034)
  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..1034
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..1034
                     /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=111636
     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          108..1031
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          707..735
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          750..775
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(751..752,755..756,758,788,791..792,795..796,
                     798..799,828,831..832,835..836,839)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          786..816
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          827..855
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          866..896
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          907..935
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mefrilgave vwsdgarvdv ggrqprlvla alllepdrvi pvdrlidllw pqsppssara
       61 tvqalvsrlr avfrrhdapv eivsrgggyl vrvhpdlvda hrftaltara rsaedetavd
      121 lldralelwr gepladvade evrhrlgagl rearwtaved raeallrlgr arqvvgeltd
      181 qvarcpgrqr lvgqlmlalh regradqala tyqrvrvrla desgldpape lrrleqlilr
      241 adptldppes tdqrgsvrpa elpheipgft graadlarld atlddrvggt riwvltgtag
      301 vgktalavrw ahrvrdafpd gqlfvdlrgf daerepvppa aalthllggl gvdpraipde
      361 vdaraalfrs llagrdvllv ldnarevgqv lplipsagtv lvtsrhrlge lvvragarml
      421 pldvltpads agllatllgd dtvraeadaa arlarlcghl plalriaaan iqaagepeia
      481 glaqelaegd plagltidga desavtkafa lsyralsaeq rqmfrrlglv pgtsfgagva
      541 galvgaspat agrllralaa ahlverlagd ryrfhdllrr yavdrvttee dvaqrdllrq
      601 rlfdhylvta daagrrliph fvrlprpvpv dpfpsteaal awldaewtnl tvaveqaarq
      661 gprryawqlt dalrayfhqr grraewlaaa tvalaaaqae edpraqaamh qsialvhvts
      721 geyegarrhl ldglridagd gwpegrtgml nnlsavhqrl gdpqaaiaca rrslelnrql
      781 gndggevmsl anlgfaywql galaqayehv qaalergeqt garynvavll vdlanvrrdl
      841 gdhrvaeely tralaanrdl gyrygeatal agravlwcat graaaahpda eravtltgei
      901 gdtgteawal dalgrvllal grpaeaaqeh rralelarrt rfswgeatal aglaearlva
      961 gepvvarehg raasalavra gyrlieirat rvlaraarms gevaeaarld driahlvret
     1021 gyaapaseag rcvr
//
LOCUS       WP_357548272             231 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357548272
VERSION     WP_357548272.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  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 231)
  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 231)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..231
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23894
     Region          55..230
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtepapphrq peeghrhgrl sarpatvaap gptgltsvpd peggppalry vpadgagpyr
       61 lvvllhgagg sarqgldlll pladarrlll lappaaastw dliaealgpd vrridallga
      121 alaeypvagv tlggfsdgas yalslgltng dlvdavvafs pgfaaplvth grprvfvshg
      181 addrvlpvdv csrrlvprlh tlgypveyae fpgghevpae irrravdwla g
//
LOCUS       WP_357548317             335 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548317
VERSION     WP_357548317.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=36357
     Region          14..309
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrpaarggr asadrlarll nlvpyllarp gieiaeaard lgtterqlre dlellwvcgl
       61 pgygpgdlid mafdgdrvti tydagidrpl rltpdealal vvalrmlaet pgvanreave
      121 ralakiesaa gdlagapvev rlpadtarvr elraavergr alrityytaa rdettertvd
      181 plrmlmvagr ayveawcrra eavrlfradr idavtelaep avvppqarpq dlsdgvfrpa
      241 pdlplitlri grgerwitey ypcerveadg eqwlvslrvt dlgwarrfvl glgpevtvia
      301 paelaeqvra qaaaaldaya tpvdragpap agatq
//
LOCUS       WP_357548506             536 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548506
VERSION     WP_357548506.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..536
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..536
                     /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=56436
     Region          79..535
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mgsrgrtplt srlratlaah aesertgipv deviemhaag lsrrkllgga avvgaaavas
       61 aaglprpaaa aaaptpppsv tivgaglagi raahwlykvk giraavyegn sriggrcysl
      121 rgffddgvvv ehggafintd hntirslans lglslrtvng gnqppggdky widgaeytyk
      181 dasadwrqvy qafkaaqqaa pypqrydsyt aaglaldnqt vnewldanmp gglasrfakl
      241 mqsdalaeyg ldpdqqsaln liyllgsngp nslspiagdd ekytivggnd qlltamvgql
      301 pagtvtldrk lvavkanang satctfqagn kytdvtsdkv ilalpftmlr ecdlskagfs
      361 tvkmrsinef dlgsnaklhv qftsrpwvaq gyggstytna tgfqcawddt vnqptstgvl
      421 cefpggsqtk awtgaafgaa paaqvtalln qlepiypgit aayngkayrd awplnpwskg
      481 aysaqkpgqy trffgieaar egnvhfageh tsidyfgyln gavesgeraa kevagp
//
LOCUS       WP_357548467             332 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548467
VERSION     WP_357548467.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..332
                     /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=36507
     Region          26..322
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtstnptlnp aggasappag lrpagrssar aagtrrkwye iiglttpavv vyvmfvlvpm
       61 gfavyyslyr wrgvgpptey vgfnnyklaf qdpifldalr nnaiivfgsl liqgpvalgi
      121 alllnrrfrg ravfrllvfv pyvlaevtvg imwklilttd gtvdqllrsl glgsmvqawl
      181 adldvviwtl lfvltwkyvg faiilllagl snvpdeltea aaidgaswwq iqrhitlpll
      241 gptiriwmfl smigslqifd miwvtsvpav rslgasatma tymvdngffa rlwgygnava
      301 vilfvisfva allfqrfllr rdiegaltrk vn
//
LOCUS       WP_357548595             194 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548595
VERSION     WP_357548595.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=20415
     Region          18..>87
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mfdiaviedp aaaeasldpm rarllaalae pasatmlaar vglprqkvny hlraleqhgl
       61 ielveerrkg tvtervmrat aasyvispva lgavrpnpsd apdrlsarwl lavaarlvqd
      121 vgalitgadr agkpvatfgv datvrfasaa draafaeela savsalvgky hdekapggre
      181 hrvvlalhpt lksd
//
LOCUS       WP_357548598             252 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357548598
VERSION     WP_357548598.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 252)
  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..252
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..252
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=26921
     Region          6..133
                     /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(7,9,11,20..22,24..25,30,46,48,50,52,56,58..59,61,64,
                     70,72..73,84..85,87,89,100,102,104,106,114..122,124..126,
                     129)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mghhfelhkd ieltatpeqv waaiatgpgi dswfmgrsev epreggrssl tmgghteqat
       61 vtawepgkrl alrsepgpeg aftaieylie greqgattlr lvqsgilgdn weteyeamqa
      121 gwdmylgtla aylvhfpgra gapvaafrpg agtpeqvwaa vadalgitgp vtvgqrarlt
      181 vdglppidgv vdlaglptyl gvrtddalyr flhsgtergn vlvlghhvfa pgqdptraeq
      241 awqhwvnalp ig
//
LOCUS       WP_357548601             857 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357548601
VERSION     WP_357548601.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..857
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=91075
     Region          48..850
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(653..654,656,686,689..690,693..694,696..697,720,
                     729..730,733..734,737)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          684..714
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          719..753
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtapdfgvdp ttascpeqyv allrrlrdqs glayrtiarr aqrngdvlpa stlatmlgrs
       61 tlprrdlvva llracdvpdd raaawlttwa rlsaartadr gaalgsgaad sgrssaappd
      121 pmdpvldtpr gspvlrlvpg tgglrvapgr pgaarvaeag gpdaerertv shapswpipd
      181 qvrandrppv pfqlppappf lvgrdaesng liaatahdga icvvdgaggv gksalalhva
      241 hqiaarydgg clyadlhgts tgiapaepad vlarflralg apaapasmee atallrtwaa
      301 drrvlvvldn aasaaqirpl lvsgpgcatl ltsrwgladl datvrirldp lpddaalalf
      361 erlggarrvv aepdaaaqvv rhcgglplal riigarasar pdaplrglae rmndeerrld
      421 vlevgdlsvr aslhlgyqaf gdapqeerrr vaqlfrlaal pdwadatayg caaladlpvp
      481 vaertlealv dahllesagd gryrfhdivr lyarerahei davsdreaal grltgwlfat
      541 taaaarllyp qerlpvaals dpaghpgqpl tgttdawawf erehtnlltv arqqvaagqt
      601 lasvrdlaav lvkfidysgy vseqqqfgql aveaaqrlgd rsgtalasni vavallrqgr
      661 ldeavpller nlavqrelgd rareaaclnn lgnalrdkgd leaalrhlra alairrelgd
      721 rhkegsvldn lalvhqrrge frqavahhea glaiaadgad plwqaqalvn faetlhlagg
      781 heaaitraae sleicqryrh qrgiglaqrv lgdayaslgr paearrhwre alvrldgldr
      841 eantklraal gddgstg
//
LOCUS       WP_357548620             280 aa            linear   BCT 28-DEC-2024
DEFINITION  RICIN domain-containing protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357548620
VERSION     WP_357548620.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19228254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..280
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29597
     Region          152..279
                     /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(167..170,180,182,185,189..190)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(176,209..212,222,224,227,229,231..232)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(195,199,201,205,209..211,222,224,227,231)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(252..256,265,267,274..275)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mpksrifvsg tgyndnvttv cadsrlsgtf lslhfygfwk ptessywtwa ndlrnrigsc
       61 asrtvldewg apmttglnyn gpingnayia yvqatsdtlr llgmgsvywp glrtgdsysm
      121 ttlggsgtsl tltnnnasgv srlqwawgvg sataapirgv gsnrcldvpg ssttwgtklq
      181 iwecngggnq swlltpsktl vvygklcldv pggsvtagtr vdtwdcsgsg sqqwsvngdg
      241 titnvqsglc ldvtgagtan gaavelwycn sasnqrwtrs
//
LOCUS       WP_357548626             145 aa            linear   BCT 28-DEC-2024
DEFINITION  Fur family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548626
VERSION     WP_357548626.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 145)
  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 145)
  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..145
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..145
                     /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=15803
     Region          21..145
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mdagtsgngg tvtqaipnvt rntrqraevl allrevegfh taqqlhqmlv arkarvgltt
       61 vyrtlqllvd ageidstrlp ggeqlfrrcs qsrhhhhlvc recgrtveva gpaverwadq
      121 vasqhgftdv shtmeifgtc vscae
//
LOCUS       WP_357548659             503 aa            linear   BCT 28-DEC-2024
DEFINITION  deoxyguanosinetriphosphate triphosphohydrolase family protein
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357548659
VERSION     WP_357548659.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..503
                     /product="deoxyguanosinetriphosphate triphosphohydrolase
                     family protein"
                     /calculated_mol_wt=55280
     Region          26..490
                     /region_name="Dgt"
                     /note="dGTP triphosphohydrolase [Nucleotide transport and
                     metabolism]; COG0232"
                     /db_xref="CDD:440002"
ORIGIN      
        1 meqpadsrar rlfggsarsl gdlaaspfra drdrivaspf farlvgvtqv ispggsgllv
       61 hnrlthslkv aqvaraiaer ltadeaprel leklggcdpd vveaaalahd lghppfghlg
      121 ervldrlarq rlglpdgfeg naqsyrivts teirgaattg ldltaavraa mlkypwtrld
      181 hpdphprhld paprgaavpp ddpesgsakf gayrtevddl rqarepfadr ipdwqqtpea
      241 simdtaddia yaihdvedfy rvgvlqqgav aaelmawqre sghlrsitda alaaagrrpg
      301 aaierlrrql hrkdawiadd eafaaavehv reelveglla lpfdgsieae qyvarfsarw
      361 strfveaitv tpepdvrsgh vllaeaqwhe vqvlkfvhhr fvlarpdlal hqrgqarllg
      421 tlvealwewl ldpeeesrlp rrlhdlvela eaelhprtpd rigrargrai vdfvaqltdg
      481 qavamldsls grsgalwtda fvl
//
LOCUS       WP_357548668             348 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548668
VERSION     WP_357548668.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=34686
     Region          44..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 mttvavrpaq agtpsrrgvr rrlavtlaaa llltvallas lalgsrplpv davwgaltap
       61 dggdastivr elrmprtalg lvvglalava gvlfqavtrn plaeprilgv sagasvgvvl
      121 aiavfgvstl tgyvwfgvag allagllvft vanrtrdgas pvtlalvgaa ldaslgaivy
      181 allsidartf eeyrfwvvgg ltgrdvgvag rvlpfvlagv alaalvargl dalalgddva
      241 rglghrialv rlgagiagvl ltgaavaaag piafvglavp hlarslvgad hrwtllvagl
      301 lgpalllgad ivgrlvappg evpagivtal igapllaflv rrarvvta
//
LOCUS       WP_357548684             306 aa            linear   BCT 28-DEC-2024
DEFINITION  proteasome assembly chaperone family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548684
VERSION     WP_357548684.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..306
                     /product="proteasome assembly chaperone family protein"
                     /calculated_mol_wt=33578
     Region          15..262
                     /region_name="COG1938"
                     /note="Predicted ATP-dependent carboligase, ATP-grasp
                     superfamily [General function prediction only]"
                     /db_xref="CDD:441541"
ORIGIN      
        1 mldphelyel tddlpdlgqp vliqaltgfv dagsatrlar eqlltsiear lvarfdvdql
       61 fdyrsrrpvm tfaedhwady daptldlhll hdddetpfll ltgpepdlqw erfvaavagl
      121 atrlgvrltv glnsipmavp htrpsgvtah atrrelisgh epwlqrvqvp gsvghlleyr
      181 lgergrdalg faahvphyva qaeypaaaea llaavsrstg lllprdglrs aaeavrveid
      241 rqvaqteeav tlvqaleeqy dtfargrgek nllatetgpl ptadelgael erflaeqthp
      301 gdtper
//
LOCUS       WP_357548728             211 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548728
VERSION     WP_357548728.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 211)
  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..211
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..211
                     /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=21632
     Region          17..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maprraaalg ggeqslrehl iaaagrlvar rgvagltvrd iareaevadg vlynhfadke
       61 ellayalhah vrtveaaqeg pppqpgegav eanlraylrr alalhaailp afaglatqpk
      121 llarlgdlpt plgggqglra elagyvraeq glgrvgatas peavatlvvg vchdlvlgrl
      181 ldptgpppep spelvdalvt tllhgiapvd s
//
LOCUS       WP_357548769             390 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357548769
VERSION     WP_357548769.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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 390)
  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..390
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..390
                     /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=43340
     Region          7..373
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 meeavrytyr lrlgatavaa ltaewhrcrw lwneavhqqt qgnrptattl halltearac
       61 sawlregsvv aqqqvlrdya qaltasfkvk grgrpvrkar kktrpslnyt qrgfsirngr
      121 lclpgkvvvp vvwsrdlpad ptsvrvyqds lghwyasfvt rreparlpda dggigidwgv
      181 ktvanttdpg fdlphpeygr raaralataq rrmarrapkp gqkasrgyrr arleaakvya
      241 kttrqrqdta rkwakrvven haviavedfk pkfltktsma rkaadgaiga tkrelidrgk
      301 ragrkvvpvp payttmtcan charakqrlv lserifrces cdhvadrdrn aarvilasag
      361 lnragadgvr rvldsfgvda vlpepgiprl
//
LOCUS       WP_357548878             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357548878
VERSION     WP_357548878.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32573
     Region          21..75
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          107..287
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mttvsaeqgp asgptvlrml lgaqlrrlre gagvsretag weirsseski srmelgrvgf
       61 kerdvadllt lygvtavqer gtllklarda nspgwwhryg dvlptwfqsy lgleaaaali
      121 rtyevqfvpg llqtpeyara villghrgaa agevdrrvsl rmerqrvlrr sdppqlwavl
      181 deavlrrpig gvevmrdqld alieataaph vrlqivpfda gghaaasgaf silrfgdedl
      241 pdivyieqlt saiyldkrdd ldyyalamar lcveaapper trelltrird eltag
//
LOCUS       WP_357549030             132 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357549030
VERSION     WP_357549030.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 132)
  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 132)
  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 132)
  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 132)
  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 132)
  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 132)
  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 132)
  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..132
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..132
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14559
     Region          12..130
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mlvhdttvqg rspaevdqir qslrsrydel taeyeqavlq sqvlrlveig dtagddqads
       61 gtktaerdta qsllrsildr raqfehaltr ldegtygfce gcsapipver leifpsatsc
      121 vsckqtrerr aa
//
LOCUS       WP_357549094             443 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357549094
VERSION     WP_357549094.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..443
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..443
                     /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=47851
     Region          7..390
                     /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 msereeiavv gaglagclla cylarrgypv alyerrpdpr igkvergrsi nlalsergld
       61 alrriglerq vmadalpmrg rmihpvegeq qfqsysgtge wainsisrga lnnalltaaa
      121 glpnvrvafd hrlvglepat gemtfetpqg kvtatasvvl gadgagsavr gqllghgalt
      181 esldfldygy keltipplgg dfaldpgalh iwprgtsmmi alpnpdrsft ctlfwpthgt
      241 asfaslgspa aieryfaahy pdliplapnl vddyqhnpvg vlgtvrctpw qvngkvgllg
      301 daahaivpfy gqgancafed vveldrclde cgddwsaalp lfqqrrqana eaiaqmaltn
      361 fvemrdkvas pvfqtrrrie haleralpgr yvsqyelvsf stmpyaqvrr rvrrqyqvvg
      421 alaagalaal agatlaigrr rrg
//
LOCUS       WP_357549129             286 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357549129
VERSION     WP_357549129.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   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 286)
  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..286
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..286
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29871
     Region          1..275
                     /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 mvtetdlrlg dgrtlhvydt ggagrlavfw hhgtpnigap paplftaadr lqlrwvsydr
       61 pgyggstpvp grdiasaatd vaavadalgi arfvvmghsg ggphalacga llpdrvvavv
      121 sgaglapyda egldwfagmv psgvaslraa aagraamvah etsgieydpq ftpadltslh
      181 gdwswfdsvv gpatksgqgg lvdddlayas pwgfrpaqvt ppvlllhgdr dgivpaahge
      241 wlarhcpaae lrrypedghi svlrhaesal ewlreradvd adidrg
//
LOCUS       WP_357549142             448 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357549142
VERSION     WP_357549142.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 448)
  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..448
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..448
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47219
     Region          8..397
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtlittrpgp glarpyrfpq vvrrsvaggq vvaahlpgqn lavalllldg gagrepvgke
       61 glggvlakal eegtaqrdat ayalaiealg telvtgldwd sfqvsvqvpa drlsaavell
      121 aeavrtpkla padvlrvrdd eatalrmdwa npgpradavl rgdifgtdnr wgrpmygdpd
      181 svaaldvddv tvfhsewfir pgtlvvagdl drldldalga aafagtaggp vekggpfevp
      241 rhdrrriilv drpgsvqstl rlghpsphra hpdhvpmala gtvlggafts rlnhlirevh
      301 gytygirgdf assrrfgrfa issgvqtavt apalvesvge vsrtqltgvt edelavarsw
      361 ragqlsvelq tpraiasalt tlvvhdlpdd yharlresll aadvaevsaa aaahlhpesl
      421 tlvvegdsav irdelvatgl gevvdhtp
//
LOCUS       WP_357549229             381 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357549229
VERSION     WP_357549229.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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..381
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..381
                     /product="LolA family protein"
                     /calculated_mol_wt=39651
     Region          44..260
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mpvfknravl rwlvpvtagv avigggaavg tfaagaepal pprtaadlln dlrtsrldgl
       61 sgtvvqradl glppiadlag aatgnelatl ltgthtlrvw yagpdrqrla lidtlgeqdl
      121 lhngrdvwtw ssrtntashr tlpageatlp sapatpadaa dralaaidpt tevtvgrsar
      181 vagrdayelv lsprdadslv hqvrialdak khvplrfevl angtdrpafe vaftqvdfrt
      241 pdadqfrfnp ppgvtvteep gvkagedlag vergpaakhd pdtdrrpdgq dlrtvgtgwt
      301 tvlvarldaa gltggpkgda ksaapgadav aqvlgglpkv sgdwgsgrll tgklfsvllt
      361 ddgrvlagmv tperlyqvar g
//
LOCUS       WP_357549232             398 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357549232
VERSION     WP_357549232.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..398
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=41719
     Region          3..>287
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mqhriivlga gytgaiaagr lakrlrredv aitlvnaepd fvervrmhql aagqdlkprp
       61 lremfagtgv elrlakvtgv dvdrrtvavl dangaeelay dtlvyalgsg wnaqgvpgta
      121 ehayeiasrp galrlrerla rieagqtvlv vgggltgvea ateiaearpd ldvalaardg
      181 lgdwlspkgr ehlrkvfgkl gitgyehtav tgveadrvvt adgraipaav tvwttgfavh
      241 piaeattlev tgtgqivvdg tmrsvshpdv yavgdaasam gpgdkplrms casgtpaawq
      301 aadaiaarlt ggklphvsir yfnqcislgr kegliqyvta ddravqavlt grlaagykel
      361 vckgaawgva nptlglptrr rhvtperava gsaiksla
//
LOCUS       WP_357549242             236 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357549242
VERSION     WP_357549242.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 236)
  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 236)
  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 236)
  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 236)
  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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..236
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25147
     Region          5..217
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mprpvifdly htlihgadee rdrvvgemav mvgvapaalv aayhatwrdr mvrwdveeti
       61 rilagrlggt ptneqvtrag ehrralgrrv ldsvstatld vldalrddgh plalisnats
      121 dtseawpqsw lahrfdvavf scdvglskpd paiyhltaeg lgvgpaecif vgdgsdgela
      181 gaaavgmtvf rttehndtdp swggpaiatl adlpailrep fkvmepsgah tghkta
//
LOCUS       WP_357549334             251 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357549334
VERSION     WP_357549334.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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 251)
  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 251)
  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..251
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..251
                     /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=24702
     Region          1..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 mseltgrvav vtggtrgigl ataralaegg atvvitgrda tnaetvakef gghglgldva
       61 dfdavgaavk rvvaehggld ilvanagime ngllgmlrgd dvrrtldvnv sgavaavqaa
      121 gramarrrkg adgaerrggs ivllasvvgt ygaagqsvya askaavaala rsaarelggr
      181 girvnavapg virtdltasl paevldkqag aaalgrlgea devadvirfl agdgaryvtg
      241 qvlgvdgglv a
//
LOCUS       WP_357549394             450 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357549394
VERSION     WP_357549394.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=48536
     Region          83..446
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnrlglrarv taafaigall laaamalfsy dltrrsllde reraairaan fdaavvragl
       61 dtdtpdvaev lrsldtgsar rpllqrdgrw fartaeigas svppelqrmv rsgepavqri
      121 rtdgqpalvv gvplspttsy yeltslreve qtfqlvgltl tavaimvags gaalgwyatr
      181 hslrpltava daaeriaagd lstrldpatd pdltrlstsf nrmveqlvrh ierdrrfaad
      241 vshelrsplq tlaaaasvld rrrehhdert ataaglvade iarfqrlvdd lielarteqp
      301 vhrervdvea lardacrthg lpdglvrsap agsewlvdrr rvaqillnlv enavryaggp
      361 vevrlacdge gtgiievddd gpgvpepdre vifarfvrgr aaharagtdg tglglalvae
      421 haamhggrat vtdrpeggar frvelpgclp
//
LOCUS       WP_357549562              69 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357549562
VERSION     WP_357549562.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=7778
     Region          11..69
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mngptgpewr pdplltigdl aawlgkpknt lyawhsrgkg prairvgntl ryrrseverw
       61 ldahtdaer
//
LOCUS       WP_357549840              95 aa            linear   BCT 28-DEC-2024
DEFINITION  Lrp/AsnC family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357549840
VERSION     WP_357549840.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..95
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=9986
     Region          <2..75
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mitaivlidc atdsipevae tlanlpgvse vysvaghvdl iamvrvrefe qiaqviaghi
       61 skvpgvinte shiafraysq hdleeafaig lasad
//
LOCUS       WP_357549841             177 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357549841
VERSION     WP_357549841.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..177
                     /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=19258
     Region          38..142
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
ORIGIN      
        1 mlpraratgr algyqlfyrl pvplrrrlvr ltvpkyivga vtlvrdteda grilllrqpp
       61 gyswslpagl lqrgeapvvg aarelheesg irlspdrlrp avpnalvhdk gwvdvvfete
      121 vpastteltv dgaevfeaaw hplddlprls ratanllghy gigprtgevp ravppat
//
LOCUS       WP_357549857            1194 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357549857
VERSION     WP_357549857.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1194
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..1194
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=128215
     Region          28..1183
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 megvisaqcd rcgrtaaegd rfcggcgael gavcphclrp latdvafcts cgaprsgarp
       61 paatpqedrr rvsvlfvdli dftpyverad peqvrsmqtg ffsaakrvvg qyggvvekyi
      121 gdavmalfga pvatetdalr cvraglelqr vltrfaptgr delrfrvgva tgealvdvaa
      181 ardggqaiva gdvvntasrm qsvappggvl vcgathaltk dairyeeqpp vtlrgrstpt
      241 evwlalapvr rqptdrepdt tplidrehel gllvnalhrs lrdrlpqvvt vfgragigks
      301 rlvrelyrha lrlvdepltw rigrcppfge nvtfaaladi vkteagildt dpastaaqrl
      361 taavtelvgp aerdrivgal rplvglagaa lpaeeaesaw rrfllalatr rptvlvfedl
      421 hwadeamlrf vellgtaare vpllllctar pelvdrdpsw agtitgsvti tlpplrdagi
      481 aslyahmfgq aafpaemltp lvevaggnpl yaheyvrmli eqgalrqsgr gwslekhldl
      541 pmpesvhavi anrvdlldak dravllaasv vgvqfwpgav aaalgqsves veralrrleq
      601 rdfvheqaas tmagqpelrf rhvlvrdvcy qrlprterva rhertadwld alsqsrdtdl
      661 aevlahhrwa aheiartlgm dthryagpar aalhraarra yalhgldaaa ahvaralsla
      721 ddsdpvgrlq lellsteisf yrdgnaflsg ggpeqlhtla drllahrdea caarawtllg
      781 qaawlradrg aavaclgrav tlfeplpdsa qkadayaelg rlhmlnyerd atvvaaetaa
      841 gigarlglae vnvnaritaa tarfqagdrs gldelhelve ssraqqllal pralqnlaya
      901 vreegdwlrs dallsatpta tgggqtlats ysgeamrayf dgdfarliaa adafvdtptg
      961 gwdmqvrglr scllvlrgrp vplaprpapa qrddaapevp rhrddvaaal dsarrsgfhr
     1021 prwtmlgmaa lcravqgrad eaaelvdela dswsavpala sgewiaaaay aaalasrdaa
     1081 vrvramldrl ghrtpwseaa lrtvtaalaa adgdhrrage lhlagaeiyg ripdvtdrml
     1141 alalavaeld rvgeraalav plaevrafae rneapgllal arrpvpdtgp avac
//
LOCUS       WP_357550029             190 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550029
VERSION     WP_357550029.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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 190)
  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 190)
  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..190
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..190
                     /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=21412
     Region          6..179
                     /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 mslptptlht arlrlrpfdd adatdlfalh ssayvlrywd appwsehvrs erfiaacrqm
       61 aeggtgarla vdrvsdgafi gwcslnrwnp dyrsaslgyc fneaawghgy ateaarvllr
      121 wafdtldlnr vqaetdtrnv asarvleklg fvregtlred cvvngevsds wvyglirrew
      181 rpssepypar
//
LOCUS       WP_357550087            1078 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550087
VERSION     WP_357550087.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1078)
  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 1078)
  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..1078
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..1078
                     /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=112063
     Region          97..550
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrssrstrav laggivvtll tgapgtaaar paaapkavkp vaatggsktv tlitgdrvtv
       61 agdgrlgivp rkgvtfhsyr tgkhqyvips davpllradr ldqrlfdlte lvaaqaarps
      121 smplivsgat avpgltvqrr lpavrgfaae tpveslasrw ratrtgvtag kiwldavrep
      181 aldqsvplig aptawsagfd gtgvrvavld tgidathpdl agkvsarqnf tegmeddrdq
      241 vghgthvast iagsgagsgg kykgvapgas lldgkvcvqf gcmeswivag mqwaaesgas
      301 vvnlslggpn gpevdpleqa vndltaqhgt lfviaagndg edetvgspat aeaalavaaf
      361 tksdeladfs srgpsadgwa vkpeiaapgv divaargkdg flgepgqlym plsgtsmatp
      421 hvagsaalls qahpgwsaaq lkaslmasak pstgigvfaq gagrvdvara itqqvttspt
      481 svtfglqewp hdndelrsst vtyhnsasaa vtlslglttd apagifslsa dtvtvpaggq
      541 asvtlsadtr qggnvtgglg gqltataagv svqtpfgvvr eelkypvkvt aterdgdpae
      601 daftvivskd ryrnymafga sndlrlppge yfafswvhqe dgdnystsql vypkltingp
      661 ktvsmdarga kgfdvtvpdp tampllagfd avyheagfgy dvallgddfg sifakligpk
      721 pakglssllt gtlvkadeqg dlagtpyvyn vgwhskndll gglvkhlkpr dfatvrasha
      781 avvpgtngmk msflsppegg gwavgwdtpl pftrtefyag dapwqnefmv elpaegddwp
      841 etltdhgsla tykagrtyqe qwnkgvfgps vapffpgdvp alreddvmyv apallgdgqg
      901 ragfgqitsg hgalyrngkl iaesnqypta yaedvapgaa tfrfdgsler darlttklsv
      961 swtfrsahak kpqslpltav sfapplddhn vgkagstavy pvtitqtegs gpvakltvqv
     1021 syddgktwkn asvrkhaglw elevahpkaa gfvslkasga dakgntfdqt virayelr
//
LOCUS       WP_357550108             590 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550108
VERSION     WP_357550108.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 590)
  AUTHORS   ter Beek,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 590)
  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 590)
  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..590
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..590
                     /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=64308
     Region          44..589
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 mlpvrktsgr vgrrlsmlpa rlpwirtqvg wadvvvaatv lvvfyvairv gagvavsftp
       61 srplhidtdp tklpyyavrs llrmfaalav svvftlvygy aaarsrrler vlipaldilq
      121 svpilgflti avttlvglfp hsllglelaa vfaiftsqaw nmtfsfyhsl itlpreldel
      181 srnlrltrwm rfwrievpha aiglvwngmm sfgggwfflv aseaitvanh eytlpgvgay
      241 agtaiangnl agigyaiatm timvvavnfm fwrpltawve kfkqeqseav dvprslvldl
      301 lrrshwpqfi apakraaaea lgrigrvfgt ddqalsarpv rrragdvafn vamlgllawg
      361 vvevvrylhg sgeglgvfte plllglltlt rvvvlmlvat vvwvpigvri glsprlarva
      421 qpvvqvlasf panflfplvt wllvhtgisl diggvllmal gaqwyilfnt iagaqaiptd
      481 lreamtdlgv rgrqrwrrli ipavfpyyvt ggitasggaw nasivaevvt fggttltahg
      541 lgayiaeatn agnypkvlag iavmslyvvg lnrlfwrrly tlavtryalt
//
LOCUS       WP_357550121             332 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357550121
VERSION     WP_357550121.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 332)
  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 332)
  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 332)
  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 332)
  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..332
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..332
                     /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=33528
     Region          90..322
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 migcpdhgpp sepdhrfcev cgrnlltgep apqsepapqs vsptwlssra aepacascgt
       61 ayvgdeaycd hcgrrrpvgr ehadldlgav agvtdrgmrr rrnedaiavg rtgdvtaavv
      121 cdgvststhp dtaayaaaea giaallaafa htadptratl dgaqaaaaaa ratagpdagd
      181 sppsctyvsg ivtadtvtvg wigdsraywl gadpacltvd dsvagqlaag rplppgldad
      241 pesralirwl gadsdateaq vvslrpagpg rlllctdglh dylsdprala aaasgqlidv
      301 arrlttiald ggghdnvtva vlshaasggs vq
//
LOCUS       WP_357550165             427 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357550165
VERSION     WP_357550165.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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 427)
  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..427
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..427
                     /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=47877
     Region          8..403
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkadagrryr lyptegqaer ltgwghtcrw lyntaleqrq fvwrqrkttl gvtaqcahlt
       61 earkdfdwva dlpaqsgqqv lrnldqayrn wwnpqhpaga ptckrksarl svpfpgqaie
      121 vrrlnrrwgv vslpkvgevk frwsrrlgga vrnavvsfdg vawhvgfgih tgvttpeaha
      181 rpdtvvgvdr gvkvalamsd grmwnrtftt pgqerklarl kstagrqeta rrkhgattsn
      241 rarkiraqva raeakvrnrr rdfvmwaanr lcaqhavvki erldiqamta takgtnekpg
      301 tkvrqkagln raildkgwgl fhtaldnkar ttgtriarvp aaytslrcsr crytdrdnre
      361 sqavfrcgsc gyeanadvna ainvrdaaev aspltgravr drnrkascrp ptqrrprtal
      421 etgvsrr
//
LOCUS       WP_357550186             351 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550186
VERSION     WP_357550186.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..351
                     /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=38267
     Region          3..330
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mnllqvrdlk vhfpirggtl qrrqhgsvka vdgvdldvaa gttfglvges gcgkstlara
       61 imrlieptsg tvhidgedll algerrlrsa rrnfqmvfqd pmasldprqs vesllteplr
      121 ahripggaae harrirhlle vvglpatalh ryphefsggq rqrigiaral vlspklvvad
      181 epvsaldvsv qaqvinllke lqerfsltyl viahdlavvr hisdtvavmy lgsiieqaps
      241 ellyrkpthp ytralmgavp vpdpaveagr nrillrgdlp spanppagcr fhtrcpwrqp
      301 trcaderppl rtlapgqqva chyaediesg riqptvtaap kakpaaphaq r
//
LOCUS       WP_357550218             429 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357550218
VERSION     WP_357550218.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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 429)
  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..429
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..429
                     /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=44273
     Region          62..369
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mldaatnqvl epvpprsrgr hrarrprrli sgllalilaa avlvaiaplr hplpaptvtr
       61 tvpasmvipg tapaipwpkt gqaalsvegv gsfgtsggrk pvpiasvtkv mtayviltgh
      121 plnrgqhgpk ltvsaqqaaa ypaelarees lvpvvagavf terqalqavl lpsannmari
      181 laawdagsie afvakmndta atlgmtnthy tdpsgydpgt vstavdqvil areamklpaf
      241 aeivaqkeat lpvagtvkny nslvgqdgvv giktgstdea ggclvfaavv kvagrkftvv
      301 gavlgqpgad tpvqldrvfr atrplvrtaa aaigvhpvvr agdqiatvqg plgagtalna
      361 aqdltvvgwp gmrvrldidi ptvparlpae aehgrvtava gggapvaael rtdvglepps
      421 twdrirrhr
//
LOCUS       WP_357550294             225 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550294
VERSION     WP_357550294.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=24316
     Region          8..198
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mslpqlplrd elfllghddd tghphihrqa lalglagavl idlylagriv ldptgdtqpv
       61 gdrwlrphsg qpvgdliadt alaairhgqa appvktflrw faedlyertr aglvaagilr
      121 httrrrlggl artdtylatd skwvvvarar lrylaagreq pdnhtaalag lvatlglaeh
      181 lylgddtttl ttrlneiagq hhrsvrdita tvdatvgdla tatyr
//
LOCUS       WP_357550308             259 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550308
VERSION     WP_357550308.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 259)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..259
                     /product="phosphotransferase 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=28171
     Region          12..205
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mvaidgrvsd varelttgqa nrvwyvngst pyvlkhygia araaneaaal tllaahrapa
       61 prllaadpra appwaaqtav hgppvtpdqf ldriaeplav ihripgphag rlagarryra
      121 wraylhnrlh tytdaaphlv pvaaaiqrel dttdldiepr llhhdlqvgh llhipgglll
      181 dwelaaygdp lsdlarlavr lqlpdptdll sltyrphptd ahrlvlywrv hqladaalnt
      241 dplihsqant qlaamtapg
//
LOCUS       WP_357550356             328 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550356
VERSION     WP_357550356.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=35114
     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 mrpfryrrpa evaeavalld aepeaaylag gtnlvdlmkl gvqrpnllvd vtrlpldtve
       61 plpgggvrig anvrnsdlaa hpvirrdypv ltrallaaas gqlrnmattg gnllqrtrcg
      121 yfqdtskacn krepgtgcaa rhgqnrdlav lgwsehcvat hpsdmavalv aldavveaha
      181 adgpreiplt hlhrepgdrp eqettlprga litavrlpps plarrsayhk ardrasfafa
      241 tgsvaaaldl sggvvrdvrl aygavahrpw rayraeetlr gqpftpelaa raadvelaaa
      301 rplahnafkv plirnltvra ltelagqp
//
LOCUS       WP_357550385             432 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550385
VERSION     WP_357550385.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..432
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..432
                     /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=47078
     Region          18..428
                     /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 mstsplrvii agggigglcl aqglhaagis vvvyerdaap darlqgyrln iepvgsralh
       61 dclpahlwei lvatagdpgp gmgvfterlr llmreddppa glsrsertha vsritlrrll
      121 lagldgivhf gkeftryrqn adgtvtaffa dgtcatgdll vgadgarsrv rrqllphakq
      181 rnapgvgigg klrlddrtaw lpeemtstkn milpkrdflf tavfrrregg daiearvgdq
      241 lraagldpdl vvqdtkdddy vmwayvahrr alpaeatgkh gqrlrdlvvs rlagwhpdlr
      301 elisqtppdt verfdfaaaa rvkpwattnv tllgdaihym ppvgglggna alydanalrr
      361 alitvsrgew ellpaiaeye ramlkhgfga vraatmylhl atlrshvira tarmffqlcg
      421 kvpslrravf ae
//
LOCUS       WP_357550409             187 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550409
VERSION     WP_357550409.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..187
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19648
     Region          51..185
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mftamaaavt tavvgceatd gnvtqggggs dkggvivpkv afsvgkrpag phlagrlldd
       61 taldpatlng kvtvinfwas wcspcraetd dleavyqatr ddqvmflgin tgdskdaats
      121 fvqgrvtyps lfdppgrmal qfrevppavi patvildrqg riavvfrkai vqtelepvvm
      181 qlateqi
//
LOCUS       WP_357550433             754 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550433
VERSION     WP_357550433.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 754)
  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..754
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..754
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80778
     Region          23..749
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          503..531
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          536..570
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          581..609
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          649..685
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          690..724
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msspqerlva qlarikelsg lslralarea glsssslsry ltgqlvppwe avvalsravg
       61 rdprplraaw aeaakagaap aprrndlpad lfdftgreae salveellgt agavaidgma
      121 gvgktslavr vahrlaptyp dgglyldlhg ftpgqeplpp haalgrllga ldvthppagg
      181 aeraalwrse lsrrralvvl dnavdadqvr pllpgagksa vlltsrhrlv sldgvppvsl
      241 epladadaah lfgraaglap tdeeavgqvl rqcgglplal rmagarlrhr pgwtvavlae
      301 rlgatpnrfd safgmslrql davqrrmfrl lgvlpgadfd aavagaltdm padqvgtale
      361 elvdahlvqe pspgryrthd lirqyaadla adeepqaeaa lrrvlrhyla qavahdqtlp
      421 sphrkepapg dpakamawfd heyvnlvagf daavrlgmde vvaelpqamr vwffrhrgtd
      481 dqarlleaaa aaaarlgrdq qraslladlg yaraaagrvt ealsayelae qagpdddgla
      541 aalalrigla rrdlgdlkaa qtqfrrarel fekignhagq aqalafdgwv alhlgqhgea
      601 velarasval angpaqitgl vtlgvalash dpaeslrtlq dalrlseqnn lqhnqawchn
      661 ylgvalrimg speealehhr rafellepla evqleidfrh tyaetcratg rydealalld
      721 rtievarelg rphdekrara aretvraarv dstg
//
LOCUS       WP_357550438             457 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550438
VERSION     WP_357550438.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=47046
     Region          3..455
                     /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 meelsrlfhl aadhaadyrr slpdrpvgvp idqatlakaf sgplpaapsp peqvladlva
       61 aaepglvasa gpryfgfvvg galpaataad ilaagwdqva fnavmspaai aaeaaagtwl
      121 kellgipasa svgfvtggqa antaglaaar hqvladvgwd verrgllgap pirviageer
      181 hatidrslrl lglgvdvvep vsagpngaid lgslrevlra gpagptivcl qagnvntgac
      241 delrkacelv hrhggwvhvd gafglwagas patrhlvdgl eladswacdg hkwlnlpyds
      301 afafcsrpev qaaamsytaa ylvgsgglpa gadltaessr rargfavwag lrelgrdgva
      361 alvdrccala rrfaeglsaa gfevanevvl nqvligcgdd artdrviaav qadgtcwagg
      421 ttwrgrrlmr isvsnattte advdrsiati trladlp
//
LOCUS       WP_357550435             414 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550435
VERSION     WP_357550435.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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 414)
  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 414)
  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 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 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..414
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43896
     Region          36..265
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mpttrtsint lptpqldvaa ellallsdtt tearpdpqle altltvaadl pvllwgepgi
       61 gktaaltqla asldlplttv iasvhepsdf sglpvvgddp atqgvpmapp dwavrlvrvg
      121 rgllfldels tappavqaal lrlvlerrig nlhlpagvri vaaanprssa adgwelsppl
      181 anrfvhlqwt hdqevvvrgl ggtwpratlp rldpqrlpea valarravcg llsarpglvh
      241 rlptgeagrs gpwpsprswe mtlrliafat aadasrevls mlvrgtvgdg pglellasld
      301 rmdlpdpeal ladpaaavlp ergdlrqavl dgvveavrrr perprwdaaw allvraletg
      361 apdlvvvpas tlarlrqedw dvpasieqla gavslsrrad etaarvaava gtrr
//
LOCUS       WP_357550514             409 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550514
VERSION     WP_357550514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..409
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..409
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45315
     Region          87..401
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrmelqrivd riaarvkrpa liedrrqrvv vysehsgvid gvrrssilrr httpemiawa
       61 rdlgimearq pvrtpaspel dllarvcvpi rhqdlllgfv wfideaegmt dddisvvtea
      121 mpdlslalyr enllgeltsq reaeatrtll vespearrea vrslltdgll gsdgqvtalv
      181 ahlvpapdda lddtarlale halvaarqwv gsretlhlvr hdhgvlllcg rhagrgpaee
      241 aaahldqalr gavrglasva rtvlgvgdar prlyeslrsy qeafqaarvg vqlpalgsiv
      301 ywsdlgiyrl lsgvdarhld varvhpglgr llgdeahqvl letletyldl agnahataer
      361 lrlhrttlyy rlqrvellad tdlkdgnerl clhlalklgr ltgqyqhgr
//
LOCUS       WP_357550506             287 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550506
VERSION     WP_357550506.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..287
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..287
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31252
     Region          138..204
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          218..282
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 msahlaptlr vlreeinarw phrdrtsdgw igdaahqarg srsdhnpdsd dgsvnaidvd
       61 vdgidpllvv recithpsce yviynrviws rtrgfaaary tgdnphdkhl hvsvshqral
      121 edsqrpwgia tasetrlgdr ilrngsqgsd vrelqtlvnr lgaalavdga fgprttawvr
      181 afqqaqkltv daivgpatla alrratappp atagnppgsr tvrhgstgdd vafvkrfigt
      241 rrcgppgtdf devteagvrw yqrmrgltgd givgrltwaq mgvrvty
//
LOCUS       WP_357550483             378 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550483
VERSION     WP_357550483.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 378)
  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..378
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..378
                     /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=42831
     Region          24..363
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtaiqnkadn piahlsaedi eiigkeldai rdrviadrge rdaryirkvi ktqrtleiss
       61 ravllfslfp pawilgtagl avakildnme ighnvlhgqw dwmrdpkihs ttwdwdhvsp
      121 adqwkhshne lhhrytnvlg kdndlgygim rvdedqpwsk ghlgqpfynl lnacffeygi
      181 aaydlelgqn lkdgghkspe frararavgr kirrqvlkdy vaypllsgps flttlaanft
      241 anlirnvwsh svimcghfps gvetfektsi egetkgewyl rqmlgsanis gsrllhimag
      301 nlshqiehhl fpdlpsnryr eiapevralf dryglryttg slpkqvasaw wkvirlsfpn
      361 rrrknaepva palvsasv
//
LOCUS       WP_357550532             257 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550532
VERSION     WP_357550532.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..257
                     /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=27386
     Region          4..206
                     /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 msapilvtgg tgtlgrlvtp llreaghpvr vlsrrggqta sgiehvtadl ltgdrvdaav
       61 rgtdivlhla ggqkgddqat rnlvraarrg gvrhlvyisv igadrvplaw lrtkldaera
      121 iaesdlpwtt lraaqfhdlv ltvtekmakl pvipvpgglr fqpvdahdva arlvdlalge
      181 paglvpdlag stvygmdeli rgylravgkr rlllpvrlpg kagrayrngd nltldgadtg
      241 arswetflae rfatrra
//
LOCUS       WP_357550537             332 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550537
VERSION     WP_357550537.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 332)
  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..332
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..332
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34721
     Region          2..185
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mnplvsvvip cynrartvel cvrsvrqqty paieiivvdd assdgsaala asagasvlql
       61 ktnsgpgaar nagaeharge ilffldadva lepgsvaaav aelrstaalg avcgvlrpes
      121 llshnliaey ralqmyhwwl ahegpmtglh talcamraev fheigpfnpd lrhteapeyg
      181 hrirqrydvr staaiagvhd hdttlrvllp kvflrarasa aevrpgevlg gatsrvlasg
      241 lvlaaaltlp aplvagvagv avplafaaga valdagiyrr vladrgipfg lrfaavhlly
      301 qltsavgavl gtgqrllhra vwraapsvga sr
//
LOCUS       WP_357550539              78 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein, partial [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550539
VERSION     WP_357550539.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 78)
  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 78)
  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..78
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..>78
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
     Region          7..>68
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 msapdavavv vpnfnkaktl raclesiyaq thqptevivv ddhstdtspt iardfpctli
       61 ttptnqgpaa arntgaaa
//
LOCUS       WP_357550584             592 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550584
VERSION     WP_357550584.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 592)
  AUTHORS   ter Beek,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 592)
  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 592)
  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..592
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..592
                     /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=61121
     Region          126..386
                     /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          <462..557
                     /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 magrlllvcr lmvrdlrrrr tetvllllai saatatltlg lalnnalaqp yertraatag
       61 pdvvampgat gpealaalap latapgvtay sgpypmaylt ltahgktvpa vvqgrdnspa
      121 aldrpavttg twvrpggvvi eptfasalgv rtgdtvding qplrvvgtav taaravypra
      181 dwrygpgspl vqyaglvwvd rsqlgalaga rplsytlnlr yadphagtsf rhmntggiey
      241 tswqeiayqd grlvefahea lligswllta lavasvaniv agrvvdqrrr vgllkavgag
      301 pamiaavhla eylviglaaa gaglaagwla apwltrpgag llgsvgvhpp alravlattv
      361 lalaiagaat lapvlraast dtvhaladaa tpprrrgwrv wlsrrmptal ligvrinarr
      421 prraglvvvn tlitttalaa llmglmqnrq vklgeselan pqstrtlqam flvivvlcvl
      481 alinavvstw tavldarhpl avartlgatp aqvtvgmava qllpaipgva lgvpagigly
      541 lvatagdpqy apaswmlama lavlfavaal aaipalaaar rpvadalqps pt
//
LOCUS       WP_357550606             902 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550606
VERSION     WP_357550606.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 902)
  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 902)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 902)
  AUTHORS   Rosinski,J.A. 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 902)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19885634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..902
                     /product="helix-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=95966
     Region          14..>388
                     /region_name="PRK04841"
                     /note="HTH-type transcriptional regulator MalT"
                     /db_xref="CDD:235315"
     Region          <325..838
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <842..902
                     /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 mpeqadrvev aetpllasrl apatlpepvl vrprlldrld qgvtgpvtlv capagwgktt
       61 llaswaradr aepspawvav eegdtghrlw sylaaalrat segvpdegpr ppvpdtpprp
      121 dqlellaaal aardrpvrlv lddlhrihdp aaltglefll rhtegrlrll agartdppla
      181 lhrwrlagel teigpdelaf tpdevadllv ahgvplpaaa vprlrertgg wpaglrfaal
      241 alraqpdpar gverfggdrs dvaaylrdev lapldpdard vlrrsavaav vcadladavt
      301 gradagqlla dlartggflr pdggtppwyr chplladllr delgrlpgee lrdlhlraag
      361 wyagndrpae alrhalagge wnqatellia rwpelapyer dgsagppppe ppaeavrrdp
      421 elalacaaer ayagdaagad hhlrraaeqa rdlpaprrdr frrlatalel tlarlggdha
      481 eirraaarll atctaagpad dpragageda dvravagtal glvllaegel paaaerfaea
      541 rtearragrp rtelvdasrs allnaarggl raaertarea letpacqgws arldcgyayl
      601 alalvachrd epaetaahla lagpaaaqpg aavlaalcra ellaadgqpa aalravaaar
      661 egapggesaa wltaaevrlr advgdvdtar vqvtdalrnc dagsaeaaal gvalsrvelr
      721 agdpraagra lpdwagpgvq swplavrlta glldavlard sgddrragri leqvldlaep
      781 eghrrvftra epgvrdllaa hldsgtahwa tvsdllrgvd errvdesaer pgapqrtlne
      841 pltereltil rylqsilsnv eiaselslsv ntvkthvrni yrkldatrrr eavqrardlr
      901 li
//
LOCUS       WP_357550652             158 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550652
VERSION     WP_357550652.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..158
                     /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=17120
     Region          19..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtadrtegtq deatlgriet evallmrlge atrrasgtae hrvldraayv ilryldsvgp
       61 qnvsglaarl nldgstvtrq vsamqrdgli trtpdpadgr gtvvsptqag lqrmaavqaa
      121 rtrlygdila awspddrdtl adllhrlnea ldarnrrr
//
LOCUS       WP_357550657             253 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550657
VERSION     WP_357550657.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Rosinski,J.A. 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 253)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..253
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..253
                     /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=27760
     Region          51..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkpllrhpdf rvaivrcrdd htgwsapepn etyglvltrr ggfrrvgrgg eefvdptvay
       61 ltvpgeaerf ahpvggddct svrlserlwq elfadrpvpa vvhvdahvdl ahrlllrtas
      121 dpdhaaaerl vrlvgaatgp avggsgrhrr lveraraalh dghpdaagll plarafgvsp
      181 yrlsrefqal vgvpltryrn rlrvgrvldr leegvpslse laaelgfadq ahltrtvraq
      241 lghtpgqlrr llr
//
LOCUS       WP_357550756             287 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550756
VERSION     WP_357550756.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..287
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..287
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30418
     Region          60..130
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mrrpwfiagl aalcmavgvp ahawaatpgt taqrtvttaa lpvvdmeavi laaqidprra
       61 dntltpgakn svlaveqalq arnllnaqwv dgyfgtttit ayaayqrslg ysgldanglp
      121 gttsltklge nrytvvntis pgakvqrdgy vvntrtqaml aeaqrllgyt lvldqgsynp
      181 ggdptsagth dgggvvdiav tgmtaakrtd varalrqvgf aawvrnpsqg dwpwhihava
      241 isdtdlssqa qhqagdyylg mnglanrgpd dgpripiktw eqyqrgq
//
LOCUS       WP_357550670             361 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357550670
VERSION     WP_357550670.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=36458
     Region          44..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 mtavqarpep atdtvrpkgl rgpallaglg vtlllvvlla agrgqvdisp aevigsvlhr
       61 lgldigplps avqgenalwi vrfprvllaa ivgaalgcag tvmqgvfgnp laepgvigvs
      121 agaavgaala ivtgvtvlgg wtvplaafag glattylvyv larsggrtev vtlvltgvav
      181 navagsvigl lmfvtdqsgv qaiafwnlgs laqanwsavs laapcllvgl avahadarrl
      241 dllalgepaa rhlgvhverl rirmivital lgaaavaftg iisfvglvip hlirmiagpg
      301 hrvlliasal ggaivvitad laartlvehq elplgvltav iggpaffwll rrtrnraggw
      361 g
//
LOCUS       WP_357550916             335 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357550916
VERSION     WP_357550916.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=36360
     Region          17..306
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mndvdrsllp aevgrlartv ldavgtvvvg krdalelvla gilagghvll edlpglgktl
       61 tarsfaqalg ldfrrlqftp dllpadvtgs flydqrsgdf sfragpvftn llladeinrt
      121 ppktqsalle amqekqvsve gvtyrldepf hvlatanpie hegtyplpea qldrfllrvs
      181 fgypdhdeew evlrrriarr reeaeikpvv dagtlramqa aledvvveds igryvvalta
      241 atrehpsvlv gasprgslal lllsrvravl anrdyvvped vkavavpala hritlrpemw
      301 lrrvdpsfvv gevlestpap asgalpsyaa glagr
//
LOCUS       WP_357551024             239 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551024
VERSION     WP_357551024.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   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 239)
  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..239
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..239
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=25182
     Region          2..229
                     /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 mngrpnivlv hgawadgscw sgvierlqaa gyqvtapqfp ltstaddvar lrqvlalqdg
       61 ptivaghsyg gqimtalgtd apnavglvyi aafgldqges lgallsqgpt ppalehlftd
      121 kqgfmwqpqd qfvqhfaadv dpvqakvlha vqqptasstf seamgmpawk slpswylvas
      181 qdqaippdaq rmfasrmgat ttevpashla mvshpdeaaq liktaaeart pmpagragr
//
LOCUS       WP_357551041             464 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551041
VERSION     WP_357551041.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 464)
  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 464)
  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..464
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..464
                     /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=48855
     Region          120..458
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 madgslarwv rrrlgvrlrs alaaalavaf afavgaaafv ylaradlvan vdatarqraa
       61 evasavaggg qgaidqtlkp spgeqtlvqv lapsgkveaa saalagaapl splrpqpgev
      121 lreqrllpfa dedpyrvvae gvttgtgtrt vlvaqslrpv nesteavaai lavglppmll
      181 vigaavfvfv grslhaveai rgrvagitar dlharvpvpe ahdevaalae tmngmldrle
      241 tsaagqrrfv adashelrsp latlqagldr laiaplpgdn aelvgllrre sqrlgrlvad
      301 llllarider gptrrhddvd lddlayterd rittrrpdlt vraqlapvrv rgdahdlgra
      361 lrnladnaar harsevilrv avrdgwgcvd vtddgpgvpe eqrerifdrf vrlddsrsra
      421 dggsglglpi tkeivaahgg tvqvlpgpgt tvrillpldg appg
//
LOCUS       WP_357551082             222 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551082
VERSION     WP_357551082.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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]"
                     /calculated_mol_wt=24249
     Region          20..>140
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 medivdtqdn ptakvlraae kmaprydrdi rflekvqfag grewigarve grvlevavgt
       61 grsfdfyppa vritgielsp amlaiakqha adlgldvelr qadaqalpfd ddsfdtvvca
      121 lslcsipdpa aaiaemkrvl rpggrlllld hirstwppvy acqwllerit iraagehftr
      181 rplplvkaag feiaetqrlk agtvervaar kpviacpaat pe
//
LOCUS       WP_357551107             253 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551107
VERSION     WP_357551107.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..253
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27721
     Region          14..245
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtgsswirrp rvvpearirl fcvphagagp sfyarwltel apavevclvh lpgresrfge
       61 rpvddldlia trvaeaaqpl ldrpyalfgh smgatiayev ahrlpreper lfvsgapaph
      121 rptdeppiah lpdadflaev rhgyggipds lwadpdllrl llpvlradfa acegyrwsar
      181 pplrcdihac sgagdhyvpe hsladwgelt tgrctadvig hghfnlvsdr aavlrlvreh
      241 lglvaamegt rhd
//
LOCUS       WP_357551148             337 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551148
VERSION     WP_357551148.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 337)
  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 337)
  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 337)
  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 337)
  AUTHORS   ter Beek,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 337)
  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 337)
  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..337
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..337
                     /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=36626
     Region          39..334
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mttqgtagvv etpaaapaap pgrtrrkarr tlrarlardw pllamtapaa alllvfhyvp
       61 tlgnviafqd ynpfvgndpi daflhsewig fgnfealfrd plfwgavrnt laitafqlvf
      121 ffplpillai llnslvsgrl rglvqsvvyl phffswvlvv tffvqmlgga gllaqqmrqa
      181 glqpwnvmtn pdgfivlvta eavwkdigwg aivflaalaa idpnlyeaaa adgagrwrrl
      241 whitlpglrp vivlllimrl gdalsvgfeq filqrdavgr naaevldtfv yyqaiatqqw
      301 glgaaaglfk avvglalilt anhvahrlge qgvysks
//
LOCUS       WP_357551170             468 aa            linear   BCT 28-DEC-2024
DEFINITION  KamA family radical SAM protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551170
VERSION     WP_357551170.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..468
                     /product="KamA family radical SAM protein"
                     /calculated_mol_wt=53308
     Region          46..416
                     /region_name="EpmB"
                     /note="L-lysine 2,3-aminomutase (EF-P beta-lysylation
                     pathway) [Amino acid transport and metabolism]; COG1509"
                     /db_xref="CDD:441118"
ORIGIN      
        1 mtqtqpveti paprpapvav ptagqpyeyr rsplvepdwt rfpgwrhvtr eqwenaqwqr
       61 vncvknikql rtvlgdlvde tfyadleadq kalatmsmlv ppqmvntmvp fepmtteafl
      121 adpvrrymip vasdrrtdwp shpyasrdsl hehdmwvaeg lthryptkvl aellstcpqy
      181 cghctrmdlv gnstpavdkl kltlkpvdry dahiaylkah pgvrdvvvsg gdvanvpwkn
      241 lesylmrlle ietirdirla tkalmglpqh wlqpdvvegl ervartaarr gvnlaihthv
      301 nhrqsitplv akaaqtaiav gvrdvrnqgv lmrgvnattp dlldlcfalq geagilpyyf
      361 ymcdmipnae hwrvpvwhaq qlqhdimgyl pgyatprivc dvpfvgkrwv hmlteydrer
      421 gvsywtknyr tsiestdlea ldkryayydp idtlpeagqa wwaahrnd
//
LOCUS       WP_357551208             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551208
VERSION     WP_357551208.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31737
     Region          51..278
                     /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 mkiavslvgs alnaasllsp rtagkaalal wrrpmrrgtv rtierethda avaerlavng
       61 kdvvtyrwgd gekpvlmvhg wqsrgsryag fvpvlrdlgf spitfdapgh gdsggtsmti
      121 leyeevirhl qgrygcfeav iahsfgvpcv fhalrngvga grlvavsgva efgflvdefs
      181 rqlglsgrvq qelrrrieed lfpheteiwe rfssvyrpts ldipvlvvhd egddwvpleh
      241 ahritaahka rlvvtrdlgh rgilgqpevi naavefirpg avtpsrvtga g
//
LOCUS       WP_357551242             458 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551242
VERSION     WP_357551242.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..458
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..458
                     /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=49066
     Region          18..>217
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrrlrqlaer tppsreryad llralaitmv vlghwlitvi gydragrptg qsalgylpwa
       61 wpitwvaqvm pvfflvggya naaaltswrn rggnatgwli drssrlirpt tallviltig
      121 aaiawlrgan pseirtvvwf atiplwflva ylvmvpltpa myalhrrvgl vvplvllglv
      181 algdlgrilg panlatanyl fgwlavhqlg fawydargps ptvpgqgtdr pglrrrrlpt
      241 srragavlll aglvalvllt rvgpypvaml nvpgerlnnt appsvallaa ataqlglill
      301 lqnparrwlr rsgpwqtvia vnavvltvfl whltaavlli gllnalgvlp tppvgsatww
      361 awrvpwllal tvvlaglvav fgpieartrr hgrastggpv rtalvaigya gvaigllins
      421 ltpknaadpl glpaptlvay lvgagvlrll rsgwgnrg
//
LOCUS       WP_357551287             286 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551287
VERSION     WP_357551287.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=30675
     Region          19..264
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mrggpgparq nrpvpvheit dpdddriady raltdvelrt rwepphglfi aegelvlrra
       61 lragyparsy lvdakrvdql adldtgdapv yaatpevlek atgfhvhrgv lgsfhrkplp
      121 taaevldtar rvviledvnn htnlgaifrg aaalgidavl lsptcadply rrsvrvsmge
      181 vfavpyakle rwpagldqvr eagftvlamt papdavplqr ltpaqreraa lllgaegpgl
      241 taaaqsasdv rvvipmrrgv dslnvaaaaa vafwelgrdd ppfgig
//
LOCUS       WP_357551511             265 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551511
VERSION     WP_357551511.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=29280
     Region          37..139
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtmslfhgtv gfyrqyrpgi patvadvlda avptgmprrl ldvgtgtglv veallgrfdd
       61 iiaidndpdm laaaedalrp qlpadaqlrl qevtaeeftp pagwqaelvt icrafhwldq
      121 aailtrldaq vspdgavaif gdnsfwtats dwkaairavi qdflgeqrra gertfqhhdr
      181 pyseimresp fsqveehsvp vnrtwtadsi lgylhstsfa apqlfgdrlg efdsavraal
      241 arysdtdtfa edneflirig rrera
//
LOCUS       WP_357551545             231 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551545
VERSION     WP_357551545.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  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 231)
  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 231)
  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 231)
  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 231)
  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 231)
  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..231
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..231
                     /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=24839
     Region          4..219
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mgartfmvvg gtsglglava rllveehrvg vlgdqpdeva avaddlecag ivcdvssyeq
       61 vrdafaevve rygtidgvav casvwaggdl adlspqrirr avevnalgtt yvfkealrql
      121 drqgfgnvvy vgamavtkpr pgipvyratk sygsslvesl aegrhsnrik vmqlhpgpmp
      181 trlqervgde fldevyagpe qvavevvrll rlapddlyvs gahmlradgr w
//
LOCUS       WP_357551581             309 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551581
VERSION     WP_357551581.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  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..309
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..309
                     /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=33960
     Region          3..297
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mglvlgclgv agvvlvrlgp swwqtvvaav lavvfaqagf ighdaghrqi frsrrandvv
       61 glvfgdllig lsygwwvdkh nrhhahpntq ghdpdivvap lsftpgqaev rrglgavfvr
      121 hqatlffpll lleglhlhvn svkavlgrgr lkhrpaeagl lalhiggylt avfllldipq
      181 aivfilvnqg lfglylgcsf apnhkgmpil dqagsldylr rqvltsrnvr ggwlidvllg
      241 glnyqiehhl fpsmprpnlr raqplirrfc tehgvsyhet tltrswaqal qhlrtvgtrp
      301 tqplsadrn
//
LOCUS       WP_357551608             304 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551608
VERSION     WP_357551608.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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..304
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..304
                     /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=33872
     Region          3..294
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mptfdeyidr vseavtvgtr rvygtywkrv rdvwgsrrln epspleigql aermkeqlvv
       61 rrnsrggrta aehlisslrc lysyavadgl iaeagnpakr vpkprrlast rralserqla
      121 sinevaattg ndpdldtlll rlhietacrr ggglalrgad ldteqcmvql hekggtvrwq
      181 pisptlagrl aelaedrggg dpsdkllryr tgkpitsrry dhlwqrlgrh lpwvaaqqis
      241 thwlrhttlt wverkfgyav arayaghngr sdagttstyv radayevara lmaltgephp
      301 llst
//
LOCUS       WP_357551639             427 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551639
VERSION     WP_357551639.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=44883
     Region          <104..407
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mewavaveva valvaglvag tllsrpvrkw rrsassesgs srqstgrpgi pderqgglsg
       61 lgrktidslr agvvvldped vpvlvnpaar amgllragtt pgsiaahplv rtlagqvrrt
      121 gvrreieldl prgrdsagdn plgvhlramg lgagyisvea advteshrla rvrrdfvanv
      181 shelktpiga lqllaealvd atepagggap dlsedliaar rfaeriqhes trlgrlvqel
      241 leltrlqgae pqpapepvav dwviaevidr trtaatarrv eiavdgqrgl tvygsdsqla
      301 tavanlvena inysgedtav rvtaratdeh veiavtdqgi giapnevdri ferfyradqa
      361 rsratggtgl glaivkhias nhggrvdvss tlgggstftl rlparppddl eatlssagie
      421 agpaelr
//
LOCUS       WP_357551675             269 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551675
VERSION     WP_357551675.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..269
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28751
     Region          3..266
                     /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 mpdpllqevg allreiaadv vvpmfrrlda aeisekapge vvtvadrrae elitarlrrl
       61 rpgsvvvgee avadhpdllr hlrgtgdvwl vdpvdgtanf aagrrpfalm valltdgvpv
      121 aswvydpmag tmaacragag twldgtpvrt twpvpkigal hgtamtrflp patrqrvvtg
      181 ggrigellpg qhcagreyld mltgaqqfvl fwhtlpwdha pgtllvreag gvarrfdgtd
      241 yhpaddgpgl lvassaevwd evhtalldg
//
LOCUS       WP_357551690             269 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551690
VERSION     WP_357551690.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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]"
                     /calculated_mol_wt=29630
     Region          36..163
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 maaaphvyth ghhetvlrsh rwrtaensaa yllphlrpgm slldvgcgpg titvdlatrv
       61 aagrvtaaei tepalqlara easarrqeni dfvvadvhsl dlpddtfdvv hahqvlqhva
      121 dpvraltemr rvcrpggiia ardsdyaaft wfphvpalnd wltlyrqaar nnggepdagr
      181 rllswarkag ftdvtatast wcfaaptdrq wwgqmwadri lhsdlaqqvl asglatgddl
      241 hrisqgwrew adatdawftv lhgeiicra
//
LOCUS       WP_357551705             304 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551705
VERSION     WP_357551705.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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..304
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..304
                     /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=34405
     Region          5..257
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mlslvvgtgr cgstlvqell srhpavgfvs glddklprln lsgrfngply rrsaprppgm
       61 tslrhsrril ergrlrvaps eayqlldryv fagfsqpcrd lvaddltphi arrlrgffda
      121 rigrqgcrll vhhvtgwprt gflhaaypdl rvvnvirdgr avanswlqmg wwdgwrgpdq
      181 wlygplppdl reeweeagrs fpvlaalgwk mlmtafadar aahpadrwld vryedviaap
      241 reqvgrmldf lgldwspaye kgfsryefpa areaayrdel taaqlaamdr vlekplvewg
      301 ypvd
//
LOCUS       WP_357551706             331 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551706
VERSION     WP_357551706.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 331)
  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 331)
  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..331
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..331
                     /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=36084
     Region          <138..241
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 msgvrvlyla gsgrsgstlv ttilgqldgv faagelrylw qrgavdnrpc gcgrpfrecp
       61 lwtsvtaalp padpariaag lrrrlrlrgl prllrrdrhg rppvaghpdd dtiaalytai
      121 athagsgptd tlivdssklp pygallgtlp gldlrvlhvv rdpratafsw rrrrgldgdg
      181 darlmnrppv wkaallwlvw ntatvrlwer rhpdrylrir yedfvaapqe tiraiarfag
      241 lnptdlpfta tgavrltpth svagnpsrhr vgavpitgdt ewigglsraa yavvtaltap
      301 alrrfryplr rppvppaptp vavpsvkhqe d
//
LOCUS       WP_357551738             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551738
VERSION     WP_357551738.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  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..191
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..191
                     /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=21134
     Region          3..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhaiqerald lfdergfsav tieeiaaaae vspssvyryf gtkegllvad efdhmsrqml
       61 edlldpadpv gsllravray esapepalhs advardsraa rspwrrvryf ftepsvrmaa
      121 caaldraaqr iapllaatgd lsqtqarvta nalvfgyfaa leqwyldgge rpiadyveeg
      181 mrplrriwsr a
//
LOCUS       WP_357551793             223 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551793
VERSION     WP_357551793.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=23709
     Region          <10..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 mnkrdasegv vviglgrlgg qvaesltklg healgidddl eivqklsdvl phvvradstd
       61 edalrqvgvg efsravvstd iqasvltvla ltglgveeic aktisakhgr ilerigarhv
      121 vypeadmggr vahlvtgqll dfielddgya iakvyppdei fgsalsrlnl rtrhgitvva
      181 vkraggeaet alpetmiedg dtlivsgptk kveqigerqg frr
//
LOCUS       WP_357551814             182 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551814
VERSION     WP_357551814.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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 182)
  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..182
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..>182
                     /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..>182
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mgevvkrayk yrfypspeqa ellgrtfgcv rlvynralea rtrawvvdrq rtsyvqssgw
       61 ltewkrtdel aflnevssvp lqqtlrhlqa gfvafwdkrs ryprfkskrk srvsaeftrs
      121 afrwrdgrlt lakmsspldi vwsrplpega epstvtvsrd aagrwfvsil vedpavaplp
      181 pv
//
LOCUS       WP_357551803             247 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551803
VERSION     WP_357551803.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=26037
     Region          2..235
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrtvvisgas sgigrataar faaagdrvvn ldvrppdpad vrggiswrev dvadwvevgr
       61 avdeihaehg amdvvvanag isvrrgvldi dertarrvme vnllgvlrlw qaaarhmvar
      121 rhgvllatas vngmrgyply adynatkagv aslcrtfale lsphvrvacv spgavltpmq
      181 qaeyteemla avnhqipagr haapeeiaaa fvylasdear fctgqelvid ggetagatta
      241 mhgtaya
//
LOCUS       WP_357551817             440 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551817
VERSION     WP_357551817.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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 440)
  AUTHORS   ter Beek,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..440
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..440
                     /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=46044
     Region          21..351
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mnatraslaa alaatialpl tacdsntaan apktlsvlvs ansiypkeqk qwfadvsakf
       61 qqqtgakisf etfaspndel tkiqtsmlsg qgpdvyslgt tftptafstg afvnlsaddw
      121 tkiggrdrfv patlgisgpd gtqevgipft srpfvmaynk ellaaagidq pattwdglrq
      181 qakqltkdgk ygmavayadg fdpwkfiwam siqagnplve ggtarltdpt tvkayqtylg
      241 wlatdkivdp aatgwknaqa iaafgegkaa flpmvsatsk vtldqsavag kyayaimptv
      301 ppgasnlptg gvgatsilsg dnlviakysk nkdlalrlvn mltsaeaqgn yyrtfgelpt
      361 naemaqrlva dpalaafvds askahgtpfh ggwskvqlal vnvvvqsvpn laagkvddka
      421 lndliakaqs eaqaaldkak
//
LOCUS       WP_357551818             326 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551818
VERSION     WP_357551818.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=34627
     Region          42..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 maatgsvtad apgtgnprrp gaarparsrr rrrgatagga alwllapggl ltlavivvpf
       61 tvalivslld ldqytfrqwl sapfigagny aealnstslp haiwvsgsaa viatllalpl
      121 gvaaaltthl pfrgrslirs lylipyvlpa fvvgtvwrii lqpdgianhs latlgvdggl
      181 wlngpksyla lilvqawsgw plvyllalsg lqsiddslhe aaaldgaqwr aklrhvvfpl
      241 lrpsvslaai isllhmvnsf tlpfvlfgvp sphdvevlpv ltyvesfqnl rfglsaamav
      301 islvlilipl lvylrtvrld rpeata
//
LOCUS       WP_357551820             277 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357551820
VERSION     WP_357551820.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=29461
     Region          1..265
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mttwtlsgfg deidpepavq lavlsalgar hievrsawgt nvvelsdtql dglaeavsar
       61 gmavsaiasp vgkvdvttdd ggeldrlraa vaaahrlssr yirifsfyrp agvapadird
      121 avlarmrafa glaedsgvvl lhenekdiyg dvpqrvadii esvdspalrv awdnanfvqv
      181 gvrpyddgye llrphleylq vkdalmatae vvpaghgdgq llrtltalrd dgyagfasle
      241 phlanqhhlg gfsgpaefgr aaraftnlta sigvhlq
//
LOCUS       WP_357551825             280 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551825
VERSION     WP_357551825.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..280
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..280
                     /product="YybH family protein"
                     /calculated_mol_wt=31371
     Region          1..130
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
     Region          138..264
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mdvhkddetl isdlverwaa airagdlagl ladhaddivm fdvpppqdgv rgidayrdtw
       61 ppffrwldss alfeivrlev tagtdvafah allrcgmpqh lsrhpdqrlr vtlglrkedg
      121 rwvvahehhs fplaeaadta aveeeirelh erwfdrtaak dldglmahia ddvvsyehet
      181 plqyvglaqv rqvcqrglda gsgevtwrvp dltvaaredl avawglnqvr veapdgqvde
      241 fwsrgtrvfr rtgdgwsmvh qhlsfpfdph tgaarldlqp
//
LOCUS       WP_357551835             378 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357551835
VERSION     WP_357551835.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=42950
     Region          5..377
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mgevvkrayk yrfypspeqa ellgrtfgcv rvvynralea rtrawvvdrq rstyvqssaw
       61 ltewkrtdel aflnevssvp lqqtlrhlqa gfvafwdkrs ryprfkskrk srasaeftrs
      121 afrwrdgrlt lakmtspldi vwsrplpegv epstvtvsrd pagrwfvsll vedpavgplp
      181 pvtgevgvda gitslltlsr pipgvsderg kvanprfgqa drrklaraqr dlarkqkgsa
      241 nrakarlrva rihariadrr rdhlhklttr lvretqtvvi gdlsvrnmlr nrrlarvisd
      301 aawsefrrml eykaawygre vipvdrwyps sktcsacglv nttlalndrv wtcpgcqtgh
      361 drdinaarni laaglaer
//
LOCUS       WP_357551878             310 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357551878
VERSION     WP_357551878.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=31224
     Region          5..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(35,249,252)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(189,220,247,250..251,254)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mgyavvlgea lvdlldaeyd gqpvyrqaig ggplnvavav arlggdvefv gslgddalae
       61 rirallaeag vglagavtvp aptalavatf tgpepdfrfy geprsygllt addlsvplie
      121 gaqvlycgsv vllhppvlaa arrawsiaga lrvfdpnvrt rlldgsgala alrevvaefa
      181 asahlvklsa adaavlypre pvegvaaylr elgagtvvvt lgadgalvaa addvvrvpap
      241 kvgavdatga gdsvmgalia ellaagepvd pvgwrdrvaf alrvaalvce spggatsmpt
      301 raavaarfps
//
LOCUS       WP_357551928              91 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551928
VERSION     WP_357551928.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 91)
  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..91
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..91
                     /product="helix-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=9660
     Region          <15..80
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mstqlapvaa dttsaatprl tieqryllwl laegethasi grrigvttpt armrlsrtyr
       61 qigarnacha vaiacragll papeqpgdgh r
//
LOCUS       WP_357551887             189 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357551887
VERSION     WP_357551887.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..189
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=20744
     Region          1..188
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mtdrpgprer lltaardlty regvhvgvda ilkeadvarr slyqhfggkd glvaealrts
       61 gvperyream rragdnprdr ilavfdelea vttrptfrgc rytsaelalp dpthpahaev
      121 raykeglhrl lvdelvrygh pdpagaadql lvlidgvlvh altrpdahpa raarrlakll
      181 ldaarpaae
//
LOCUS       WP_357552045             266 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC048999].
ACCESSION   WP_357552045
VERSION     WP_357552045.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 266)
  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 266)
  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 266)
  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..266
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..266
                     /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=28445
     Region          24..260
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mfrrrspdqp vdpahrlvvg rltleiaggs vvghhysenf dvlhvdpalp lavvidgmgd
       61 gegsrvagat amrtfvaqvr agwpavgahe lhaataqtql rvrqagaela gltgcaltal
      121 vadpdggqgw lvqlgdsray rlrdgllelm tvdhtmawlg vlhgwwpats peadraryql
      181 lryvghpdkp epdvlavplr tgdtwllctd gvsdqlgyhr lrdllaarre partvgalls
      241 atldeggddn atavvvrvhp tvptpr
//
LOCUS       WP_357552068             222 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357552068
VERSION     WP_357552068.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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: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=23618
     Region          5..217
                     /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 msnlsaafir lharlapvaf vpevrlhqad epiglwelte gefrstqppp fwafawaggq
       61 alaryvtdhp elvagrrvld lasgsglvai aaarvgaaav ravevderav aavalnaean
      121 gvrvdaelgd ildgdagdae vvlagdvfys eamarrmlrf qlkaarsgar vlvgdpgray
      181 lprerfhela gydvpvpeal egvrvkhttv weldptppga ar
//
LOCUS       WP_357552272             601 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357552272
VERSION     WP_357552272.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 601)
  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 601)
  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..601
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..601
                     /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=64433
     Region          46..577
                     /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 mtsssgasrr qvlavaaaaa tapllasapa qaaasngngv ptttwdltil gtsdmhgnvy
       61 nwdyyldaey ddsqhndvgv aklatlvnqi raerkgkatl vldagdtiqg tplatyyakq
      121 epitvtgeth pmanamnvln ydavtlgnhe fnyglpllak wieqlgfpal aanalnakdg
      181 kpafvpyvik pvnlgghgap alnvgilglt npgvaiwdkg hvegklvfad miataakwvp
      241 imrdrgadlv iisahggdsg tssygpelpi enpvrmiaeq vpgidailfg hahseirerf
      301 vtntktgerv ltsepskfgq rltrmdftlt rekgdwkvia kgatmlntnt vvedpkvlaa
      361 vrsqhtktvn yvnqvvarst velkaaesry kdtpildfin kvqtdvvtta lagtayaglp
      421 vlsiaapfsr tavfpagdvr irdvaglyvy dntleavvmt gaevkayley sakyfrtlpv
      481 gatvnpgsis dssvpdynyd tlsgvdydid iskpvgqrit rlvmpgtdtp vpadaqfvva
      541 vnnyrrsggg nfpgivktqv yneqkeirdl lidwakakga idpadffvpn wklvregvpv
      601 f
//
LOCUS       WP_357552425             159 aa            linear   BCT 28-DEC-2024
DEFINITION  phasin family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552425
VERSION     WP_357552425.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..159
                     /product="phasin family protein"
                     /calculated_mol_wt=16615
     Region          1..98
                     /region_name="PhaF"
                     /note="Polyhydroxyalkanoate synthesis regulator phasin
                     [Secondary metabolites biosynthesis, transport and
                     catabolism, Signal transduction mechanisms]; COG3937"
                     /db_xref="CDD:443138"
ORIGIN      
        1 mqdawrayle lamglteapr kkaqdavrrv vdqggttaaq lqslaeelvs tsmanrealt
       61 klirfevdra lgavglatad evaeltrrvr elerqlreat atpadaavpi gpvpastkav
      121 vkkavakaar tsaeeasaap arpakkaaar krttggaes
//
LOCUS       WP_357552480             265 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552480
VERSION     WP_357552480.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..265
                     /product="phosphotransferase 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=28964
     Region          5..243
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 migaklgagr eadvyewdds tvvklyragf lghraealal akldgrgvap klvdavecdg
       61 rtglvlerlg gadmlsllqr qpwrvlglar aladahlavh eapapgdlpe lrqvlasria
      121 davlpshlrd yalrvldalp dgdrlchgdy hpgnvlvaad rvavidwpna argvpeadha
      181 rtllllrwtd pqpgtplvsr plitagrsmf ahryarayrd rslrrlrqpa swlvvqaaar
      241 laegieveqn tligfldrth qrper
//
LOCUS       WP_357552640             636 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357552640
VERSION     WP_357552640.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 636)
  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 636)
  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 636)
  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 636)
  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..636
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..636
                     /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=65107
     Region          34..633
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msdacgcgdd kpraegveee heperlwqvs evraaavagv fllagfiagl agaprlfgvs
       61 lytvallvga atfvpntlrr lvkgkigvgt lmtiaavgav vlgevaeaat laflysiseg
      121 leeyagartr rglrallslv pakatvlrdg aqvaidpahl rvgdllllrp gerlatdgvi
      181 rtgstaldvs altgesmpie anpgdaiyag singtgavev qvtatasdns larivrivea
      241 eqsrkgaaqr ladriakplv pgimllaaai avagalagep rtwieralvv lvaaspcala
      301 isvpvtvvaa igaatrfgtl ikggaalerl griravaldk tgtltrnkpt vvdvavstad
      361 reqvlrvaaa lesrsehpla qailaaapeh tlasdvdavp gagltgvvdg rparlgrpgw
      421 idpgplgehi tamqtagatv vlvehhgtll gaisvrdelr peaveavarl hadgytvaml
      481 tgdntrtata laaqagidev hadlrpadks rivagmrtar ptamvgdgvn dapalatadv
      541 giamgamgtd vaietadval mgedlrhlph tlaharrsrh imlqnvglsl glitalipla
      601 atgvlglatv vlihelaeii vigngvragr arplqe
//
LOCUS       WP_357552674             128 aa            linear   BCT 28-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552674
VERSION     WP_357552674.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 128)
  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 128)
  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 128)
  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..128
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..128
                     /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=13820
     Region          <40..>122
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 midartvlgs vperyyvhne hrgetlhrsa aqaihrdvia ldvhdgarvl eigtgtgysg
       61 avlaaragtt grvtsidisd hlvgwanrlh qqrglttirc hvadgmagyp phapyqrlva
      121 wctfsglr
//
LOCUS       WP_357552754             184 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552754
VERSION     WP_357552754.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 184)
  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..184
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..184
                     /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=19451
     Region          16..155
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 maapertehd agrqpvvils gnprpgsrtm daatrlaqrv pasgtrhvvd laqlaghvye
       61 pghariedal aavrsaevli vatpvykasf tgllksfldl lpadslasat aipvvvsasv
      121 shrlltelhl rivlrelgat lpstavllde ghladldpvl dawaeqqipv lqtaravlgr
      181 prvr
//
LOCUS       WP_357552734             215 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552734
VERSION     WP_357552734.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22414
     Region          2..165
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlfdmdgtlv dseklwdval qelaavyggt lsdtarrami gtsmaasmri lhddlvqper
       61 dpqasaewin arilelfrig lrwrpgalal lravraagip talvtssgrp lvevaldtlg
      121 rdsfdavvcg devgaakphp epyltaarll dvpiercvai edsptgvasa laagaavlav
      181 paevplpptd gvhqlesltg adlellaall gdppa
//
LOCUS       WP_357552766             127 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357552766
VERSION     WP_357552766.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 127)
  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 127)
  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 127)
  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 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   5  (residues 1 to 127)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..127
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..127
                     /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=13689
     Region          36..117
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mskqqtsppv vdlngdvpcc ppltqrrvpa etaavlapaf kalgdpvrlq lmsmiasaed
       61 gevcvcdltp afdltgptis hhlktlreag lvdaerrgtw vyyrarpqil rqlaallsie
      121 ptpayrp
//
LOCUS       WP_357552770             109 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357552770
VERSION     WP_357552770.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=11720
     Region          7..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgddlldrdt aqtyaswfra ladptrvqiv eylarhnrpm svgelvaavg laqstvsqhl
       61 kiltevrfvl vepvgtarhy rindacvgcf psaadvvmgr papipkgac
//
LOCUS       WP_357552782             292 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552782
VERSION     WP_357552782.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 292)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..292
                     /product="phosphotransferase 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=32452
     Region          6..251
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mttavldhaa vrrllpgtat fyarplpqgr fntcwhlasa grsyllklnd regeahlrqm
       61 atamsdaaag gvavprvlhv gtdpglgpfl lqewldgctf aeareddaie tdlwprlghq
      121 iallhscppt paltatpasr trqlgdlvdt lrrhrlvsaa laeathrrgl plaqqlgdle
      181 cvnthqdihp dnilirpggq ialldfdhat taeyasefvk ldrwcqpsvh nreqlldayw
      241 qqrgelvdpl feqrlafhrl vitlsyflyw hgrdatqipg ctaalrtele rt
//
LOCUS       WP_357552771             165 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552771
VERSION     WP_357552771.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 165)
  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 165)
  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..165
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..165
                     /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=17471
     Region          3..160
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 maditvrpmn pddagrvlai yqagldggna sfetvaptwa afdagkladh rfvavdtdga
       61 lvgwvavspt saravyagvv ehsvyidpaa qgrgagrlll daliasteaa giwtiqsgvf
      121 pentaslalh qrvgfrmiga rervgrhhgr wrdvillerr sptit
//
LOCUS       WP_357552805             510 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552805
VERSION     WP_357552805.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=55919
     Region          1..423
                     /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 madhvdvliv gaglsgvgaa vhlqrdcpgk tyavleardd vggtwdlfry pgvrsdsdmf
       61 tlgysfkpwt dpkaiadgqa ireyvreaar ehgvrehirf hhrvlraewd sgtarwtvha
      121 hrddtgedvv ltcaflftca gyyrydsgyt pefpgvdryt grlvhpqhwp edldwtgkrv
      181 vvigsgatav tlvpalaqra ghvtmlqrsp tyvialssrd pladalrrwl pakaaypvvr
      241 wknvlmgvat fqlsrrapgl vkrflrraaq grlpvgydid rhfvprydpw dqrmcvvpdg
      301 dlftavsqgr asvvtdaidt fteqgirlgs geelpadiiv tatgldllal ggmavtvdgv
      361 evdlartvay kgmmlsgvpn famtigysna swtlkadlva tyvcrllrhl datgqqivtp
      421 lapdsgelap iidlksgyvl ravdrlpkqg prapwrlhqn yprdvllmrh grltdagvrf
      481 sragasatgv vdaarptapv argernspya
//
LOCUS       WP_357552786             459 aa            linear   BCT 28-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357552786
VERSION     WP_357552786.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 459)
  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..459
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..459
                     /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=50039
     Region          2..439
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mvilgagpcg lacahelqrl ghrdwvllea aprvgglgss vvdeagftwd lgghvvfskm
       61 ksfdallael fepqellrhq rssfvrhggs wvpypfqqhl hhltqararr clddltaaqa
      121 rgralaetdf aswleatygh alveeffapy nkkiwatsls emsaswiaer vapadisalr
      181 lalktgftgt qvwgpnaqfa fpasggtgai wrrlaarldg dvrtgqrvvy vdeaaksllt
      241 adgtvlaydh lvatgalngl vammagaped vrlaatalrh ttvamaglgy rspttdrrsw
      301 lyfpgceapf yratnfsrya panvpdsdpg rysawmtets lpagtlldra glveecdlal
      361 rrcglvpesa ervsghveli pyaypvptvg rdaalaliqp wlerqsiysr grfgtwryei
      421 gnmdhavtmg qdiarrlvrg taeriytarp ptvgsadvr
//
LOCUS       WP_357552808             330 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357552808
VERSION     WP_357552808.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..330
                     /product="helix-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=36375
     Region          14..309
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrllsil lllqahgrlt aaelarrlev svrtiyrdve slhaagiply geaghaggyq
       61 lvdgwrtrlt gltaeeadrl lfaglpgpaa elgyqsvvaa vqlklraalp ppladraarl
      121 eqrfhldtpg wysdgdpspy laptadavwr qhrvrvryrs wtgevtrile pyglvlkggr
      181 wyvvaarpdr aepatfrvnq ildltpldep ferpefdlpg wwrahvadfr arlhrdeati
      241 rlsprgrerl reiatdpvva avdatagppd qagwvyavip ieslthahgd llrlgaevev
      301 lspaplrdrl attaaalaal yrphpapscr
//
LOCUS       WP_357552814             221 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552814
VERSION     WP_357552814.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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 221)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..221
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..221
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23541
     Region          4..212
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 msfaaagthm ivlpgggyae haaheaepva rwlgdigvqv nvfryplnvr hpeplnalra
       61 eiarrrargv qrigligfsa gghlaglaal apgaapdetv nfavlgyait smetetyrpa
      121 rlillgedas pelrrstsld slvrpqsppf fvwhtaedps vppehtyrla salaanrvph
      181 avhvfahgph slglaqsage taiwttlake wileqaaapp r
//
LOCUS       WP_357552934             308 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357552934
VERSION     WP_357552934.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..308
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32409
     Region          2..218
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 miearqltkr ygektavdrl dfevkpgmvt gflgpngagk sttmrliigl daatsgsvtv
       61 ngrryarhva plqevgalle arsihpgrta fdhlmvlsht hgiprrrvde mieltglqsv
      121 arkragsfsl gmgqrlgiaa allgdpatvm ldepvngldp egvlwirnll aglaaegrtv
      181 fvsshlmaev alvaehlivv grgrlladtt vqdlvrqagg dtvtvatadp arlraalagp
      241 gveitgrags eqlqvsglsa rqiglvaaeh gialfeltpk hvsleeafmd ltrdaveyhg
      301 avtsgvma
//
LOCUS       WP_357552888             266 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552888
VERSION     WP_357552888.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     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=28903
     Region          7..250
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mrdiltvypa lvrsatlvav tyrgrivlsv ltaffplltm avwltvvaeg gppagwttgd
       61 flsyyaaatl lwnlagdrvv wqwdadlrsg dlsvrllrpv hpfhqyasdd lghrllfltv
      121 lapalvlaal lvpgldypvt pgrlvavaaa lvlayalsll mastfaligf wstqasnvwl
      181 lwwglgsfas gwvaplalmp dwlrtaglvl pfrtamgfpi ellmgrldgr eaaygfavgl
      241 gwlavfglly rvgwrrgvrr yqavag
//
LOCUS       WP_357552991             129 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF732 domain-containing protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357552991
VERSION     WP_357552991.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10526342
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..129
                     /product="DUF732 domain-containing protein"
                     /calculated_mol_wt=14459
     Region          17..111
                     /region_name="DUF732"
                     /note="Protein of unknown function (DUF732); pfam05305"
                     /db_xref="CDD:461618"
ORIGIN      
        1 mavpvtvlgv hvthprdedg yltylkqygd phsdgpvlvl ppaadllaeg daacdwmreq
       61 pyalwrtdsq yhfpavyery eqhvanrsps wgndppemgs vtagawaylc padwelrqpr
      121 rrpfapnpd
//
LOCUS       WP_357552998             281 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357552998
VERSION     WP_357552998.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 281)
  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..281
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30514
     Region          1..62
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(6,10,35)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(9,34)
                     /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"
     Region          87..262
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maaelkrire glgvsgeeva aalgwsqpkv srienariav strdlatllh yygvpeevra
       61 ellaitadde gtggawlvra ggvtrrqgev aaietrvrsi qqyyplivpg qlqspeyama
      121 ytrsggwpnp eaivarrmsr qallrsddap aysalldara flawpgsrdv ilsqlaylrt
      181 raelpnvtir iiplgvdrta samvpftlyd fraessprvv fvesqtadly lsapadveiy
      241 sgvfdalaad alspdesieh lallaphied lkdprstdgr p
//
LOCUS       WP_357553114             313 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC048999].
ACCESSION   WP_357553114
VERSION     WP_357553114.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 313)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..313
                     /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=33011
     Region          56..310
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msaptsttaa gpsaparvrr grrygravdr rtalaipaga lllalavwpl aqlgsmslht
       61 vsaatlnstw dfvgldnyaa mlrepdfgqv vvntvafvli vttigmvggf mvavavlsst
      121 rggsfllglm vfvwalppvv ngsiwkflla dqglvnqalr alggqglgfl ydskfalwsv
      181 alvnawavvp fnalvlraal lgvdpqalea aeldgarpwq rawhvlvpag rtaatvltil
      241 tivyafrsfd fiyvmtsggp gtasttlpfl ayseafltld ygrgaatali allvvvvltl
      301 iyardvrrte gea
//
LOCUS       WP_357553164             270 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC048999].
ACCESSION   WP_357553164
VERSION     WP_357553164.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..270
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28793
     Region          53..264
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mahtltrrrl lavgagtaav avvgglaare lsrprsgpap dlpdapagde rliriassar
       61 grevdfwtav pdgygdgrgl pvclvlhgas atprdygrfg larfltdavr rgtppfvlag
      121 atggrlawrr sgdddpqrml reevpnwcar rgfdtdraaa wgwsmggfga lllaeaypgw
      181 lravaafspa vrpgdavfad vdklrgtpvg lwcgrqdnfl rdvralakal peppvraewt
      241 dgrhnfaywg tvipdafall gtalttprtg
//
LOCUS       WP_357553193             408 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Micromonospora sp. NPDC048999].
ACCESSION   WP_357553193
VERSION     WP_357553193.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048999
  ORGANISM  Micromonospora sp. NPDC048999
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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 408)
  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..408
                     /organism="Micromonospora sp. NPDC048999"
                     /db_xref="taxon:3155391"
     Protein         1..408
                     /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=45041
     Region          20..406
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(56,63,87..88,95,99,106,239..240,243,247..248,251,
                     284,289..290,293..294,296,319,346..348,351..352,354..356,
                     360)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(63,81,83,86,88..89,171..172,188,238..239,242..243,
                     247,290,293..295,396)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtdhvvrgsd iytdefaadp yptfarlrad rpvcpisspr fdsylitrfd daraalndpr
       61 lskdlygpgq hylrifgpns eglnknmlns dppehtrlrr ivsqafaprr iealrprvaq
      121 ivddlldkvv pqgrielmhd faiplpmtvi cellgvpvad heqvlgwtqv irtsgssrrs
      181 pqeeraavqe aqlrlhhyla dlvrakrtrp addmisalid acdqdgalae pelvtttfll
      241 lfaghqttad fignamlall thpdqlellr ttprllpsai eellrfdgpl pvasprittd
      301 dveyqgvcip rgsvvgvvln sanhdpahfa dpdqldvrrv rgphlgfghg vhyclgvsla
      361 rmeaqlgiaa llrrlpglrl avpltevrrl paaspfrgll elpvtfaa
//
LOCUS       WP_357553381             314 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553381
VERSION     WP_357553381.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 314)
  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 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   3  (residues 1 to 314)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..314
                     /product="GlxA 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=33310
     Region          8..312
                     /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 mhkqsathrv avlalppvva fdltiathvf ghegqgrytt tvcspdggav ptttaglalt
       61 vdatidalah adtvlvpgfr rgpapapald alraayrrga riasictgaf alaqsglldg
      121 rratthwmha ealarehpdv rvdanalyvd egqvltsagl aagldlclyl vgrdhgqdva
      181 ierarlmvtp lhraggqaqf vpaqasgeda elaavttwat anlhlpitva dlaraglqst
      241 rtlhrnfrhr fgmspqawlt eqrlraacgl lesddstidd varrtglgta tnlrahfrra
      301 fattptayrr aftp
//
LOCUS       WP_357553359             282 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553359
VERSION     WP_357553359.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31165
     Region          15..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(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..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mprftpatpr srrlgrelrk lreakdltge aaaaivdcsp srisriesge irprvgdvme
       61 llvaygvkid eepgtslldq arglredgww qrlggkyaty iayeieavel knfepmlvpg
      121 llqtesyare vnvigretdq atvdqrvsar mtrqgvlrrq ptplrmhail seasvrtevg
      181 gpdvlreqld hlvalsrlpn vtiqvlrfga gahlaissgf allsferdep plgyietlag
      241 elflessrdl arlsaaydnl rtlamspaes itfvkelskh gt
//
LOCUS       WP_357553495             246 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553495
VERSION     WP_357553495.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 246)
  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 246)
  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..246
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..246
                     /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=25021
     Region          1..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 mmtlndrval vtggsrgiga gialrlaqdg advaltyrqd aeraatvvkq iealgrrala
       61 vradaadpsa vrgavdrvaa dlgrldilvn naavfpvgtm delgpaemeq tiavnirapy
      121 vavqaalrhl geggriisig snvgeravfp gltlycmskt alvgltrgla relgprditv
      181 nlvnpgptdt danpadgpna aaisgftavg ryarpadiaa tvahlaspea gyvtgavinv
      241 dggfts
//
LOCUS       WP_357553472             421 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553472
VERSION     WP_357553472.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..421
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44174
     Region          153..388
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mstpgggela atlrriersa galatssvar mdetlpwfra lpadqrswvm lvaqagarsl
       61 vqwlsegggt adstqevsde vfaaapqala rsitlqqtva likvtidvve eqvshlaaeg
      121 eeqqlreavl rfsreiafaa arvyaraaes rgawdarlqa llvdallrgd spdvlasraa
      181 algwadappv avavgrspgg evsavlhvvy rqarrigvev iggvhgdrlv ivlggaadpl
      241 tatakllsaf gdgpvvvgpa vpsldeates araalsgfra apawpnaprp vpaadllper
      301 alagdaearr rlrhdvyatl vraggellat ldaflaaggt lesaaralfv hpntvryrlr
      361 riaevtgfsp lsprdafalq valtvgrldp vvpitstvss qtmtpnarkt aqteddprrf
      421 l
//
LOCUS       WP_357553459             704 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357553459
VERSION     WP_357553459.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 704)
  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 704)
  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 704)
  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..704
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..704
                     /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=77008
     Region          1..700
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mtdqtgleqe iaveqrhldr vyarlaelrq savraerdgy rmarvgtygs lverdamvfh
       61 aaqrrhvlda eyeglvfgrl dlrdrqvlhv grlgirdedt ttlvvdwrap aaaafyqatp
      121 aqpldvvrrr tiqsraekvt rieddlldpn aapegmtvvg dgallatlsk atgrgmrdiv
      181 atiqreqdea irspgsgvti vaggpgtgkt avalhraafl lysdrsryag ggilvvgpsg
      241 vfveyiasvl pslgedtatl hslgtlfpgm satrtdppev aavkgslrmr rvleraarda
      301 vpggpgelrl lyrgtllrld raaldrvrdr alhrgarrne vrragfdgif aalwaqarev
      361 gvrlpeqrtf eaeiaersef reflkawwpr lhprhvlgwl arpdrlrrya ggilsgaeir
      421 lltaayrnle sdgltiadia lldeldallg kpaqpakarr dpfqlaggvr elstasdrqr
      481 aaraaarerp edyrdyahvv vdeaqdvspm qwrmvgrrgr laswtvvgdp aqtawtgdpd
      541 eldrareqal grrkrhdftl ttnyrnssei favaaaeirr lypdlplpta vrstgvdpve
      601 lvvpatglet atvqaaagll tevegtvgvi tpvprrdeva gwlaaldapr lqvvtsleak
      661 gmeydgvvlv apseiradpg agvrtlyval sratqrltti dptg
//
LOCUS       WP_357553587             186 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553587
VERSION     WP_357553587.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 186)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..186
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19386
     Region          17..79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          100..182
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mppepaapla tiaaalrrer ervgisltel arragvakst lsqlesgtgn psvetlwalg
       61 valgvpfsrl veplddavrv iragdgsrvr seqadfagtl lsagaahlrr dvylielepg
      121 aaraadghtp rsvehvvvaa grlrvgpeta pveldpgdya afpgdaphry ealapgtfav
      181 lilehp
//
LOCUS       WP_357553593             383 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine desulfurase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553593
VERSION     WP_357553593.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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 10003004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..383
                     /product="cysteine desulfurase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39031
     Region          3..376
                     /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 msaspvylda asaapthpva rqallaaldd gwadpgklyt qarrarqlld aareatavtl
       61 gvradevsft psgttaahga vlgglaarhr vgsalvhsai ehsavlhaae rhvarggtat
      121 gvpvdrlgrl dltawsaavr apgvalaali tashevgtvq pvaeaaadca dvgvplyvda
      181 aqsvgrvplp agwsvltasa hkwggppgvg vlvvrkgtrw espwpadere ggrtpgvvnl
      241 pavvaaaasl raaaadaaae atrlaalvdr irarvaadvp dvevvgdpvl rlphlvtfsc
      301 lyvdgeallh aldrrgfavs sgssctsstl rpshvleamg vlshgnvrvs lhretteadv
      361 erflaelpgi vaglraeagv agl
//
LOCUS       WP_357553650             388 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553650
VERSION     WP_357553650.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..388
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39452
     Region          42..385
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 msesptpapl ailgpehggg rlaevlpsal avlgvpgsad plglapalag vrriavllvd
       61 glgwyqlpta apyaptlagl aatvgrplia gfpsttptsl vslgtgvpag ahgvlgftvr
      121 vpgtdrvlth tdwagdpspl swqpvttqle raraagvttt vvsrpefggs gltvaanrgg
      181 dfrgaaggaa vaaamlaala agsgptlvsg yhadldrhgh lsgvdsvpwr daatevdalv
      241 arlvdglppd aallvtadhg qldipathrf dldtdprlrd girvvagear vrylhvapga
      301 lddvvaawst vlgdaarvrt rdevvatgwf gpvpeehlar igdvvvtcnd tyavmasrte
      361 rpmasklvay hgsdtaaelt vpllvvrg
//
LOCUS       WP_357553858             284 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora sp. NPDC049230].
ACCESSION   WP_357553858
VERSION     WP_357553858.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 284)
  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 284)
  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 284)
  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 284)
  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 284)
  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..284
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..284
                     /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=27930
     Region          109..>283
                     /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 mavqtglgep rgpwfispql dpdgrgwwdt perdpgerrp rrllaalavv alsavsgava
       61 ggvvaardgg ggpaaasaap vsaelvtaae rtvpgvvsvl aggtsagsat gsgfavddqq
      121 hlitndhila kggggpvtve lpdgrrfaaa vvgreprsdl avlkvpaaag ltplplakpg
      181 atrvgepvla vgsplglagt vtagivsald rqvrlgnnrh ravqtdasin pgnsggplvn
      241 argevvgvnt aiatidgngs igigfaipid qvqqtadtii gkgg
//
LOCUS       WP_357553930             225 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357553930
VERSION     WP_357553930.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..225
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23885
     Region          2..207
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtikalifdf dgllmdtett lleswrwewr rhglrldptg ffadhggdan earyvaleaa
       61 igpaydrtss halrmayrae lnaaltpapg ipqwldraae sglrlavass spsrhvgall
      121 dqaglrgrfe vlatgeevta hkpdpavyll aldrlglpad qvvafedtah gvaaaqaagl
      181 rcvavpnrha dharftaadl vlpsaadlpl dallarlalg agglr
//
LOCUS       WP_357553772             293 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553772
VERSION     WP_357553772.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 293)
  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..293
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33225
     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..283
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mddsgstvpr rqlgrylrel renayvtvta aakelewsap riwryetgqv pmhpndveam
       61 crvygaspet iermralare tkahgwwhsy geaikdwfkl yvgleaaatr irhyeanlvp
      121 gllqtveymt eviatdhpql geaerkarvd irlrrqrlla ravpraphld vilnesvlrr
      181 plrdrsamir qldalvvtse rhnislrvlp laaglfrwas agtftmldfp sevrapeptt
      241 iymdgpcgav yldkaheiev yenvwrslge ralpptesre liaaiakemt dga
//
LOCUS       WP_357553984             188 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553984
VERSION     WP_357553984.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  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 188)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..188
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..188
                     /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=20122
     Region          2..187
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkkvdhrer rtliadalmr iaaeqgleav slrhvaaaag vsagmvqhyf rtkdemmafa
       61 lsvvrersql riteavarlg esppprlllr tmlaallpld drtrddgrva laflaytavr
      121 psaeprlhed taqftgfiag vlpeghgaaa aagllalmeg lgvyllggqy taeqalgald
      181 ahldllfd
//
LOCUS       WP_357553996             238 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357553996
VERSION     WP_357553996.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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 238)
  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..238
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..238
                     /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=24535
     Region          1..234
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mstsqgqkvv vitgasqgig adlvaayrkl gygvvatsrs igasddpeiv tvrgdiaead
       61 taervvaaal drfgridtlv nnagvfvakp ftdytdeefd lvtgvnlagf fhltrrvlph
      121 llavgaghiv sittsfvdqp sshvpsvlas ltkgglssat kslaieyagr gvrvnavapg
      181 viktpmhpve thqalaglhp vgrmgetsdv vdavvylesa pfvtgeilhv dggqnagh
//
LOCUS       WP_357554081             539 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554081
VERSION     WP_357554081.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 539)
  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 539)
  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 539)
  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..539
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..539
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58579
     Region          22..>235
                     /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 mshpeqhrgr rrprldrpal vallfglagv gyrlvltlft vpvsnsdeat fglaalhigq
       61 grerpvflyg qhymgmlesy laaplvavag pswpvlrlpm lvlyalflyl ihrltrrlct
      121 qwfatvvvgl lalggervvr dqltvvggrp evkpavllml litvglaagt vrrrrlavgl
      181 fgllvglaaw sdwlilpyla vaglalvwav rrellgwsgl llvagvvvgi apmvldnlra
      241 gpgedsltvf revstkagps ppwsdrirgg llegvplahg lcpvegcgrw qqwfgvlypv
      301 llvvgaalat layrradagp rgervapvvq lalvagaalt llsyvrspla atspldnary
      361 lsvlqlslpa vlwplwvaal tvwrgtssvl griigalsaa vlvaltvtml vitvlfattg
      421 taasrteerq arelaaalra ngphevygdy wtcnrlvfnt detvicavld gdlspgqnry
      481 rpywrqvgra erpgyvveid spmdrrlrrl ladradttav revggyrvyh pdtpvrpwr
//
LOCUS       WP_357554084             730 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-1,4-glucan--maltose-1-phosphate maltosyltransferase
            [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554084
VERSION     WP_357554084.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 730)
  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 730)
  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 730)
  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 10571012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..730
                     /product="alpha-1,4-glucan--maltose-1-phosphate
                     maltosyltransferase"
                     /EC_number="2.4.99.16"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009313 - oligosaccharide catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0030979 - alpha-glucan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=79849
     Region          3..190
                     /region_name="GlgE_dom_N_S"
                     /note="Alpha-1,4-glucan:maltose-1-phosphate
                     maltosyltransferase, domain N/S; pfam11896"
                     /db_xref="CDD:463388"
     Region          195..549
                     /region_name="AmyAc_GlgE_like"
                     /note="Alpha amylase catalytic domain found in GlgE-like
                     proteins; cd11344"
                     /db_xref="CDD:200482"
     Site            order(248,252,263,265,308,340..341,343..344,376,378..379,
                     407,463,516..517)
                     /site_type="active"
                     /db_xref="CDD:200482"
     Site            order(326..328,335..337,350,381..384,386,389,411,413..414,
                     417,421)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200482"
     Site            order(378,407,463)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200482"
     Site            order(410..412,429,432..433)
                     /site_type="other"
                     /note="acceptor binding site [chemical binding]"
                     /db_xref="CDD:200482"
     Region          <537..635
                     /region_name="PRK12313"
                     /note="1,4-alpha-glucan branching protein GlgB"
                     /db_xref="CDD:237052"
ORIGIN      
        1 mtgrfpiedv spvvscgryp akavvdepvp vsarayregh dalgcnvvwa gpggasrpft
       61 rmrpgepgqd rwhatiapda vgewtfavea fqdpyltwqn avtkkiaagq gpedlandla
      121 egarvltaaq glvptadqpr vaaaltalvd tdlplpqrvg palaladllw ehpvrelvtv
      181 gdrysiwvdr kralysawye ffprsegatq drsgtfatat erlpgvaamg fdvlylppih
      241 pigrvnrkgr nnaltagptd vgspwaigaa egghdtihpd lgtpadfraf vqaaaaqgle
      301 vamdlalqca pdhpwvtehp ewfttradgs iayaenppkk yqdiypvnfd ndpegiraev
      361 lrvvlhwvge girifrvdnp htkpfdfwhw liaevksvep dvlflaeaft rpaimhglgk
      421 igftqsytyf twrttaaqmr eyceelvasa dhmrpnfwpn tpdilheslq hggppmfkir
      481 avlaallsps wglyagyelf ehvarpgaee yldnekyelr prdwagaeaq grslapflat
      541 lnrvrrdnpa lhqlrnlvfh eidnpallcw skhdpatgnt vivicsfdpr ivqwgnttld
      601 mpalgfdwhe rftvhdeltg tsydwgqrna vrldpylqpa hvltvrrpva paapepvgve
      661 padltvtdvp ddlsggtapt tpatttpatt tpaattpatv asrlsaarsa aahsrtapta
      721 aapkddrwts
//
LOCUS       WP_357554136             837 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554136
VERSION     WP_357554136.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=92379
     Region          1..824
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtltaalpts adpdtlfdaf agwakergld lyphqeeavi eivsganlim ntptgsgksl
       61 vaiaahfaal adsrttfyta pikalvsekf falcevfgae nvgmltgdas vnadapiicc
      121 taeilanlal regtkadvgq vimdefhfya epdrgwawqv piielpqaqf ilmsatlgdt
      181 trfvddltrr tgratavvrt aerpvplifs yamtplhetl eelletkqap vyvvhftqaa
      241 aleraqalms vnvcsraekd miaqaiggfr ftsgfgktls rlvrhgigvh hagmlpkyrr
      301 lvetlaqagl lkvicgtdtl gvginvpirt vlftglskyd gvrtrllknr efhqiagrag
      361 ragydtigrv vvqapehvid nekalakagd dpkkrrkvvr kkppegsigw gqptfdrlvd
      421 aepepltssf qvshsmllnv igrpgdafta mrhlltdnhe epaaqrrhir raiaiyralr
      481 aggvveelpe pdetgrrirl tvdlqldfal nqplsplala tielldaesp syaldvlsvi
      541 esilddprqi lsaqqfkarg eavaamkaeg ieyearlell ddvthpkpla elleaayemy
      601 rqghpwvadh qlspkavvrd myeramtfte yvqfygltrs eglvlrylad ayktlrqtvp
      661 edakteelid liewlgelvr qvdsslidew erlrnpadva evaqahaslt drppavtrna
      721 rafrvlvrna lfrrvelaal rrwdllaeld aadgwdydaw adalapyfee ydsigvgpda
      781 rgpallmieq grerwtvrqs fddpngdhdw gisaeidlva sdevgaavvr itdvgql
//
LOCUS       WP_357554152             336 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357554152
VERSION     WP_357554152.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 336)
  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..336
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..336
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37424
     Region          69..119
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(74..75,86,89,93..94)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          144..328
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mqghpittpg ntvprmiair nmrkpvlraa clrkevrysa wqdgdmsqrq sptvrrrrla
       61 ltlrqlrdra gitsadaarr vdhdaswlsr ietaevrphp ndvrallaly gvegdqaeav
      121 iavarqakqr gwwqrysdvl pdwfaayvgm eseasvirty ecqmvpgllq teeyaraafq
      181 gapvkmrdde verqvalrme rqailrgddp pmlrvvideg avrrvvggpe vlhgqlnrli
      241 eesarsnvqi lllpysagvg fdgsfvildf ppmpepypda aeerlvyvdt ltgalylerp
      301 gevaayaaah eqlqalalap kptrdtlrai aanlit
//
LOCUS       WP_357554184             248 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357554184
VERSION     WP_357554184.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  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 248)
  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..248
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..248
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26034
     Region          <26..245
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpsrsswsta rwnavlttgl vagavpgdtf ryssvglmva gkivervtgq rldqalnsnl
       61 agplglrdtg fnpdtwlsgt arasrlvatd arssrgllrg tvhddvanhl ggvaghagvf
      121 atatdlavig qllldggthq gqrilaaata rrmlanhnag kpavdperph rtaahglgvv
      181 ldqswfmgrl ssartfghtg fagpsllvdp rrrlvlallt nrahpnwsws npdpvraavg
      241 dllakevn
//
LOCUS       WP_357554200             305 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357554200
VERSION     WP_357554200.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 305)
  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 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   3  (residues 1 to 305)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..305
                     /product="GlxA 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=32514
     Region          2..305
                     /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 mhrvvalvrp vqstfelgca vevfgtkrag vpqhyefevc tetpglvpts agyamsvsrd
       61 laaleragtv iipgwapvea plsdrvhdal lrahargarl vticsgvfal artglldgrs
      121 atthpgraeq lrrefprvrv eqdrlyvdhg dvatsagaga gidlclhlvq qdhgaahaal
      181 laqhmampph reappasagd aldglldwag arlgtslsvq dmaayvgvsp rtlarrfarh
      241 lgtspggwll srrvaeartl lehtdlsvev iaarvglssa vnlrrrfhar lgmtpsayrr
      301 aarvp
//
LOCUS       WP_357554228            1138 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554228
VERSION     WP_357554228.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1138)
  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 1138)
  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 1138)
  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 1138)
  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 1138)
  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 1138)
  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 1138)
  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 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1138
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..1138
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=119989
     Region          712..1114
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 misddqrgal eavslnpavt pddvwrpsph nvpelhekvv aeilrgvara rtddtsmplg
       61 vamqgragag kthllgavre riqreggyff lvdmvsgktf wesvalalve gmgrthvgwg
      121 tqlktflrrl tpqlglpvev rdavagatpv traqldafvr alrerhrevg rdtqdtaral
      181 vlhgavdfea qdvgyahlis epgdpaaraa wglsaatrtp qqivqdisrl malaldptvi
      241 avdqldtlfa qtstsmlhqh egledgqakv lgpiadgllk lrditrrtlv vvsclpdtwv
      301 lltrtaptpv gdrfrtatlp driptpqigq aivakrlaaa fagprfvpph ptwpiapaaf
      361 adaptltpra llrrvdrhva wcrdrdevve ldrlidgsds tpttpivraa pgdpttderr
      421 lreldarfae lveaadvsaa vdparedehm pallaaglaa wiaeqaptga tykydpppgr
      481 kpalhgrlie vldeatenea hwcfraiahp naiavtarvk aactlagldr dlpqrrlill
      541 rngpwptgrr ttevlagfda agglrravpe adlrvfaalr vmatepstal qewlvarrpa
      601 sgtelfravl pgperprdgg ppappddgvp ppgdagtpph dagttsdevg tassgtgtts
      661 dnagtppqda rtssdgvgta ssdaeapagg aeagstggpa pdgagglstg haavavpade
      721 vdsvagaggr aiglgrtvdg ghpftvples lrrhtvvfag sgsgktvlir rlveecareg
      781 vsaivldpnn dlarlgdpwp appsgwgpgd aeraadylah tevvvwtprv tagrplsfqp
      841 lpdftslrdw pdefdqavrs avealaprag vdrssrlaqq gkavltealq ayarsgmvgl
      901 pgftefladl pegvsrlara gklaeelaea lkaamvtdpl fggvgapadp gllltpspgr
      961 rarvsvisfv gltsehqrqs fvnqlqmalf awikrhpagd rplgglfvmd eaqtlapstg
     1021 ttactassia lasqarkygl glvfatqapk glhnqisgna ttqffgllna paqidaarql
     1081 aeakggrlad igllnsgefy aagegfsfvk vrtplclthh pkapltpeev vararpag
//
LOCUS       WP_357554245             551 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357554245
VERSION     WP_357554245.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 551)
  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   2  (residues 1 to 551)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..551
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58783
     Region          60..550
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mlvppgtvtw fdrpvtwfdr pvgdadvege hvrqllpaav aalsvvlavt payagsqrla
       61 spaadtpara lartenglie gasgagyrvf ngvpyaappt gpnrwrvpqp atdwhgvrda
      121 ttlpaecaqn piggggpitg aedclhvnvt tppnrtgrhp vlvflhggsf tagsanqydp
      181 rrlaadgnlv vvtvnyrlgv fgyfglpglp gsgtfglqdq qaalrwvqrn iaafggdprh
      241 vtlagessgg msvcaqltap savglfdkai iqsgscltdw pdglflpgik agsqfsslaa
      301 vqnqgaqlrd rfgcatvacl raasytdllh qtqgaglaaf atpaygtpll parpadalrs
      361 gryqhmpvle ggnldehraf lgftelypvp kpytpgdyra alrtafgdra gqvearypva
      421 awgtpglawa avatdriwac ptleqtrlla ernrvygyef aerdgpvldp rypwgaahgl
      481 elaylfdmdf ltdqtqpelr srfvtawsrf astgtpgwpr mpyvqtfadd rsgnvdlaae
      541 hqcgfwssvp r
//
LOCUS       WP_357554339             362 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357554339
VERSION     WP_357554339.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 362)
  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..362
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..362
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38150
     Region          2..342
                     /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 melaslapap fgcmvladlg advvrvdrpg gpgagrlaap tggplqrgrr vtaldlkssa
       61 gvadllrlvd radvlveayr pgvaerlgfg pevcqarnpr lvyarmtgwg qdgplaarag
      121 hdidyiavag aleplgrvge rpyapmnlla dfagggmlla vgvlaaller ersgvgqvvd
      181 aamvdgsall tsflhgllgs glwsaprgrn lfdggapfyd tyatadggfm avgamepafy
      241 avllsgldla ddpdlpaqyd psgwdelrrr fterfaertr dewtavftdl dacvapvlap
      301 geahghphna argtfvevgg eiqpapaprf drtptdqptp apdperdirp aaeildtwpr
      361 rt
//
LOCUS       WP_357554355              69 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357554355
VERSION     WP_357554355.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 69)
  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 69)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..69
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6963
     Region          1..69
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mvnttfqvqg mtcghcvsav saevgaiagv rdvqvdlatg qvsvsseqpl dvrvvraavd
       61 eagydlvda
//
LOCUS       WP_357554351             115 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Micromonospora].
ACCESSION   WP_357554351
VERSION     WP_357554351.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=12085
     Region          9..115
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mssapspigd dlvrvlasla nphrlrivaa larerayvsg larqlgisra llqvhlrkla
       61 aaglvtasle lsedgkamny yevqpfvltl tpeiiaaave tltvpdsaeq pgadr
//
LOCUS       WP_357554481             245 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554481
VERSION     WP_357554481.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..245
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=26789
     Region          22..245
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 msaqpdrwfq rtvecrelrq vlvafphagg sagffrdwat hlpgadvlav rypgraerid
       61 epppadmvrl grdiadalge lladtdvplt lfghsmgavv aletaralee lgvrpahliv
      121 sgsragplpe vapptelead elalrlaalg gtdaamlddp ffrelvlpyi rsdgemfhay
      181 rhrrepvlhc pvtavvgadd tdadqrpwpe lttagfrehv vaghhfylvd eppyellrna
      241 lavtr
//
LOCUS       WP_357554392             268 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554392
VERSION     WP_357554392.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..268
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27629
     Region          10..243
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlglpahvta clfdldgvlt qtarvhnaaw tqtfdeflrq raaasgepfq pfdpgpdynr
       61 yvdgrpradg vrsflasrgi vlpegtpddp pdadtvngvg nrknvlllqr lrdsgvevyp
      121 gsvrylkaav taglrravvt asanggevva aaglepllea rvdglvaraq glrgkpqpdt
      181 flagarllgv dptqaavfed alsgvaagra ggfgyvvgvd rvgqadella hgadivvrdl
      241 adlldtadpa apartaaaph pgteggla
//
LOCUS       WP_357554483             980 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554483
VERSION     WP_357554483.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 980)
  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 980)
  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 980)
  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 980)
  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 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..980
                     /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]"
                     /calculated_mol_wt=100319
     Region          5..>980
                     /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 msrdrsldia vtgvhalfpg aadlddwwea mlagrvlttr ldradllsag vppeladdpd
       61 yvpvrghldd adrfdhvlfr isardaelmd pqhrlmlesa waaledaagr sadlttavya
      121 sdsgsgylra mlaagpldpl tldqalhgte pdfiasliay klgltgtalg vrtacssslv
      181 svhlavqali ngecdqavvv aagidypqag hlhvpggiqs vsghcrpfda radgvvagsg
      241 vacvvlrrla dvtdgpplyg vllgtatnnd gsakagyyap saegqeaviv aalaaadvga
      301 dsigyleaha tgthvgdpie wsaasaalsa ggarpgqvav galkstighl dsasglagli
      361 ramrvlregv vppvtgftel nplldvagcp lyvptaagpw agpeprragv ssfgiggtna
      421 hviveqpppa pvvpprpere rlvvlstasa dvldraadrl ashlrraepd ladvaytlat
      481 ardplnsrla vtgrtaaeia erlehaagva rgacptegpa pvvfllpgqg tqrpgmaigp
      541 aavlpgfade ldaclrgyga alaaqlrhal ydpkfpaedl aatalaqpal fameyaigra
      601 liglgvapaa lvghslgelt aaclagaidl pdaarfvaar geamhacprg smlalgcdpg
      661 tarslladag adlelateng aescavagpd eeierfrawl gdrvltrvlp tshafhssli
      721 epalpalaqa ltgvtlrppa vpyasnlsgr liepgepisa ddlvaqarrp vlfagglaav
      781 aerlpgclai evgpgrvlsg laaaaglaav pllpmrderp arevvdalgt lwtrgqplap
      841 ellgadggrp vhlpsypfad rrwsapevap vaaatatrap vagagpaagp apadqvpaaa
      901 pavvlpklwa evlghgdldd dsdffalggd sllitqlarr iheefglrvp lrellagrtl
      961 grqtalvrdt lrsaaagtts
//
LOCUS       WP_357554519             385 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554519
VERSION     WP_357554519.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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 385)
  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 385)
  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 385)
  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 385)
  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..385
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..385
                     /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=41527
     Region          63..385
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkrltirarl tliygglfll agvvllavty vlvdqrmpqp fgvslrdlpk tspttpsgqn
       61 vdnlrtliqq aqdeakrnal eslltqggia lilvsavaia fgwllagral qplhqvtdta
      121 rriagadtag rglherialt gprdevrela dtfdemlerl drsfdgqrrf vanashelrt
      181 plalnralve lavsrpeasa etrrlgesll ainerherli dglltladse neltertpid
      241 laevcahvld qtgrqapdvl vrrslapapv sgdpvlverl tvnlvenavr hnlpadgwve
      301 vrtglsddgr atltvtntgp aiagydietm fqpfrrlsre rvagargfgl glsivravar
      361 ahggtvdaqp rpagglivtv tlpva
//
LOCUS       WP_357554527             535 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357554527
VERSION     WP_357554527.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 535)
  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   2  (residues 1 to 535)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..535
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56773
     Region          39..535
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mtripyprwa vvlgvvalla pamavgpaaa addrrgaavv rtdqgtvrgs vsadhlsfqg
       61 ipyarpplga lrwappqpgp vwagvrdatk pgaacaqlqg lpmdhaadse dclhlnvttp
      121 rtaartprpv mvwlhggdfr fgradvydgq rlaaggdvvv vtvnyrlgal gflahpalag
      181 pgggtgnfgl qdqqaalrwv rrnaaafggd pgnvtafgqs agatsvcahl aapgsaglfh
      241 railqsnscv npvqtrveaa raaeefarni gcadvgtvaa clrgrdpaql vetagypgag
      301 vdlgpvvdgr tlpvdpahal atgklhqvpv ltgmnrdesr lvvwgmehsg lncpepqpgd
      361 eaescpltdd qyrdrvramf gdraeqvlar yprndeqvas etlgavwtds dyaepiysaa
      421 lafarrvpty lyefadddap fftkgpepsf ptgayhcael pylftvdyae aftpaqqrls
      481 demvrvwsdf artgraswpr lrgaapyvrv fagggesgtt afaaahsydf wrslr
//
LOCUS       WP_357554648             388 aa            linear   BCT 28-DEC-2024
DEFINITION  homogentisate 1,2-dioxygenase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554648
VERSION     WP_357554648.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..388
                     /product="homogentisate 1,2-dioxygenase"
                     /calculated_mol_wt=43358
     Region          1..385
                     /region_name="HmgA"
                     /note="Homogentisate 1,2-dioxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3508"
                     /db_xref="CDD:442731"
ORIGIN      
        1 mpyyrsvgev prkrhtqfrq pdgslyaeel mgqegfssds sllyhrhapt ailaaeefap
       61 paftrapnlp lkprhlrthk ldtggadpil grqyllandd vrigyvladr psplfrdatg
      121 dhclyvesgt lrvespfgal davagdyvvi ptstihrlvp tgdepvrlla veasghigpp
      181 krylsvrgqf lehspycerd vrgpdapllv dgeevevlvr hrrgwtryvy anhpfdvvgw
      241 dghlypwafs ihdfepitgr ihqpppvhqt fqgpnfvics fvprkvdyhp dsipvpynhh
      301 nvdsdemlfy tggnyearrg sgieqgsisl hpsgfthgpq pgaaersiga dyfdelavmv
      361 dtfrpldlcd aantcedeay awtwarqr
//
LOCUS       WP_357554708             247 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554708
VERSION     WP_357554708.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 247)
  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..247
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..247
                     /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=25563
     Region          60..247
                     /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 mdsvrspewp vaplggvvgn saagryavpg tgpiigragp ppppyqppsg agapppvgkp
       61 aappipvkil vaggfgvgkt ttvgaiseia pltteaemts agigvddpgv rstkttttva
      121 mdfgcvtidr slklylfgtp gqarfgfmwd dlargalgal vvvdsarldd cfpaidffer
      181 aglpfvvgvn afdgrlalel geirwalaig dhvplvqfda rdrlsvrdal lvvldraler
      241 atrerqa
//
LOCUS       WP_357554737             322 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554737
VERSION     WP_357554737.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  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 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   3  (residues 1 to 322)
  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 322)
  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..322
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..322
                     /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=33874
     Region          1..273
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtrwgilatg hiasrfaedl rlvpdaelva vgsraadsar rfadtygakr aygswvelaa
       61 dpevdaiyva tphsahyeaa mtcltagrav llekpftldl atstelvdta raagvflmea
      121 mwmrtnplil rvveliaega igtvtgvrad fgvagpfppe hrmrnaalgg galldlgiyp
      181 islahlllgv pqhirswaql gpegtdentg llfgydtgal atlscgivgl sgltasitgt
      241 tgridlpepf frpgsvllhr agaepetiva dgagngyqye aievqrclaa gltesplvph
      301 aatlevmall dtvreqigvr ya
//
LOCUS       WP_357554787             316 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357554787
VERSION     WP_357554787.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..316
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..316
                     /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=34594
     Region          1..316
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mravlvvnpk atttsersrd vlvralrsev dlsvrytrrr ghamalarea aaegvdlvvt
       61 lggdgtvnev vnglmtadpp traddapmae rlpalatvpg gstnvfaral glprewpeat
      121 smileglrlg rsrtvglgra ddryftfcag fgldaavihr veqarrkgrv stptlylrsi
      181 mnqyflasdr rhpaislerp geqaeaelat viiqntapwt ylgdrevnpn paasfdlgld
      241 vlalrqlrva sttrtvtqfl srqpdprgrq vlrlhdtpef tlvsshpqaf qldgdylger
      301 ekvrftsvpa alrvic
//
LOCUS       WP_357554841             300 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554841
VERSION     WP_357554841.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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 300)
  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 300)
  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..300
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..300
                     /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=31655
     Region          1..300
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mlrfglfgtg hwaiethgka lhahpdaelv gvwgrnpera salaerygvp ayadvdalie
       61 qceavavalp pdiqadiatr aatagrhlll dkplalsvad adrvvaaaee sgvasvvfft
      121 qrfqpnvtaf laataaaggw qhcrttafas ifqdgspygg slwrrehgal wdiaphalsi
      181 llpvlgrvtk vaamdgpsgm vhlllthegg atssaslsld aptesmaref vfygengiet
      241 vpfgendaat afgvaidqli eqvragtrdh rcdvrfgrev vgilaaaeta rtesrtvllp
//
LOCUS       WP_357554891             596 aa            linear   BCT 28-DEC-2024
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357554891
VERSION     WP_357554891.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..596
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=63490
     Region          4..285
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
     Region          313..592
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 marefstvgv vglgtmgagi vevfarngvd vvaveisepa lergratltr stdravakgk
       61 lavadrdalh ervhfavgld alhsvdlvie avpehldlkq rifaeldrvc rpetilatnt
      121 sslsvteisv attrpnqvig ihffnpapvm klvevvrtvv tapevvadve alctrlgkvd
      181 vtindragfi anallfgyln havamveshy aaredidaam klgcglpmgp lalmdligld
      241 tayeildtmy rrggrdrrha pvpllkqmvt agllgrksgr gfytyerpgs pvvvpdeatp
      301 latdaaladg araiakvgvv gsgtmatgiv evfakagyev vsvargqeks atlreavrts
      361 lnkgvvrgrl aeadrdaalg riswsatldr ladvdlvvea vveelsvkka lfasldeick
      421 pgvvlattts slpvidvama shrpadvvgl hffnpapvmp lvevvrtirt speatatara
      481 vcatlgktgv vcgdrsgfiv nallfpylnd avkmleasys taddidhamk lgcgypmgpf
      541 elldvvgldv alaiqrelyl elrepgfapa pllehlvtag ylgrkarrgf rdhshr
//
LOCUS       WP_357554811             564 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora sp. NPDC049230].
ACCESSION   WP_357554811
VERSION     WP_357554811.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 564)
  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 564)
  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 564)
  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 564)
  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 564)
  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..564
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..564
                     /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=56575
     Region          <36..>214
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          286..562
                     /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 mteyesdpqr rpaptdaeps hptaelprde raqsdspttp isvvsttgda qptgdaattr
       61 dtettavtqp vagsegapay geqpastppa vmqptgyepp taaqptgyep paatpsappy
      121 pvsgypapsq pgypqpnagr ypgapwyagq qsgwagggqp gmaypphqqh gqhpqhpgqh
      181 aqqaqhfgqh pqhpgqpipp wgpqvappgs gprpgriakf agagvavfal mlgsgvagga
      241 lalaldgdgg gvtrtytaap vlnsadlpki aasvqdsvvs ittgsgegsg vvltndgyvl
      301 tnnhvvasag gdtvqvvfad gtkapakiig tdpktdlavv kadgvtdlkp akfgdsdamq
      361 vgdqvlalgs plglqgsvts gilsardrti ragdgqqqdp sqqsqpvssi sgllqtdapi
      421 npgnsggalv ntrgevigvn taiatsgqst gnigvgfaip snkakdvagk lqrgekvshp
      481 slgvgvnqae gggalvasvs pgspaekagl qrgdvvtkfg dkpvndsddl vgavqagkvg
      541 drvevqykrn gveksatvtl aets
//
LOCUS       WP_357555067             293 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555067
VERSION     WP_357555067.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 293)
  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..293
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32647
     Region          14..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..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mserrsptir rrrlgaelrr qresagitie vvaeqlecsa skvsrietgh ttatprdvrd
       61 mlriygvvga esdelvqiar earqkgwwhp ystvlvgayv gleaaassir ayeqqvvpgl
      121 leteeyasam iraarpdfta dqvhqrvrvr lgrqslltqd dpvdlwvvld eavvrrpvgg
      181 devmrgqlkr lvevaelpnv tlqvlpfevg ahagmdgtft ilsfpepgdp dvvyaenatg
      241 glfleksdel qkysfifdhi raaairpees vahiaklaee plwkwrpkgs pwt
//
LOCUS       WP_357555070             518 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555070
VERSION     WP_357555070.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 518)
  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 518)
  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 18791949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..518
                     /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=51875
     Region          1..518
                     /region_name="COG4935"
                     /note="Regulatory P domain of the subtilisin-like
                     proprotein convertases and other proteases
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:443962"
     Region          125..376
                     /region_name="Peptidases_S8_PCSK9_ProteinaseK_like"
                     /note="Peptidase S8 family domain in ProteinaseK-like
                     proteins; cd04077"
                     /db_xref="CDD:173790"
     Site            order(128,131..132)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173790"
     Site            order(156,188,247..248,275,338,341)
                     /site_type="active"
                     /db_xref="CDD:173790"
     Site            order(156,188,341)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173790"
     Site            order(290,292,315)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173790"
ORIGIN      
        1 mglprrsvlv gvatatvlav gtpalaaepa gevraaggat avpdsyivvl kdsavardrv
       61 gdtakrlsgr hggtvartyg aalrgfevkv sasaaariaa dpavayveqn htvsisgtqa
      121 nppswgldri dqrnlpldss ytypntasnv hayiidtgir fshndfggra tsgydsvdgg
      181 aaddcnghgt hvagtvggss ygvakavqlv gvrvlncsgs gtnagviagv dwvtanaikp
      241 avanmslggg anssldnavr nsiasgvtyg laagndngan acntspartt eaitvgstts
      301 sdarssfsnv gtcldifapg ssitsawyns ntatntisgt smatphvvga aalvasanps
      361 wtpaqvrnql vanatpnvvs npgsgspnll lyvgtgttpp pptgctgtng tdvsipdaga
      421 avtssitisg cgrnassast vavnivhtyr gdlvidllap dgsayrlkns stsdsadnvn
      481 ttytanvsge aadgtwrlqv rdtysadtgy intwtltv
//
LOCUS       WP_357555073             489 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357555073
VERSION     WP_357555073.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 489)
  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 489)
  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 489)
  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 489)
  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 489)
  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..489
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..489
                     /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=50319
     Region          5..240
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtltlryaah sdrglirdgn qdsvyagprl lavadgmggm aagdvasniv igamaplded
       61 vpgdalvdal rsavgtanqq lrdtvdanpq legmgttlta tlftgsklgm vhigdsrayl
      121 lrngdfaqit kddtyvqmlv degrisaeea sshpqrsllt raldgrdidp eysvrqvlpg
      181 drylicsdgl sgvvsaetig etlreytdpq qcverlvqla lrgggpdnit viiadatdqd
      241 iveaspivgg aaardrgmat saddstpaar asalaaprpa vpeepaasdd epdrpkrrpv
      301 rtaamalall vivgggafgg wtytqrqyyv gateegqvav frgvqgeiag mdlstvhrrs
      361 gtrlddltva aqdtvrvgir aksepdaerq laeltsdsps npnlkplcpl dpsaaaggtp
      421 tpasaspspn gspspngsps tiasptsngv vsasptvgat aigssttpdv tpsdsatpal
      481 dpaacrspe
//
LOCUS       WP_357555342             158 aa            linear   BCT 28-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555342
VERSION     WP_357555342.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..158
                     /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=15572
     Region          52..152
                     /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 mseppdqrtd pdvdlrvdad rgelstrpat vlasiaaggv ggalgraalq haaphaaagf
       61 pwatfavnls gclligvlma ilthlggghp larpflgvgv lggfttfsty avdvqqalva
      121 gapgtalayl agtvlgalva vglgdavtaa llrrwvag
//
LOCUS       WP_357555403             445 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555403
VERSION     WP_357555403.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=48510
     Region          42..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 mhpttdapvg ridrtplsrr rllrgllalt vaapllagaa acgdddggaa dpnapvklsa
       61 fwwggdarak ltedalalyt kkhpnvtfet twqanqgyfd klatltaggn ppdlfqiddn
      121 ylaeyaarnt tldltsyqks gkldtsrfpe slwqygvvdg klaglaagen tqglvynktl
      181 ltkhnlpept tgmtweqhia waeqvtattk vpgtqdpsad ykafwvwlrq qskdlykgke
      241 lgftaedvtk wfdlwkgard rkatptadvi hegnssdvtk qlvvtgksat swvwanqmpd
      301 lkkntkdelg viaypgdpsa qwarasmyws vfrgsknrdv avdvinflyn dqeavtllgt
      361 drglpsnldl rrlvsegttd pamkqsiave teltqkfgps pqvpikghsk vkselikaae
      421 naqygrasta eaaaqfleac ksaia
//
LOCUS       WP_357555431             330 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555431
VERSION     WP_357555431.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 330)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..330
                     /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=36675
     Region          45..326
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matsttapda drrepragsp argparrprg prrsllpyll lapaivlela ihvvpmvvgv
       61 wmslleltqf hirnwstapf vglenyratl dlnsaagkel lhsfwvtlay svlsvgfawl
      121 lgisaavvlq kpfrgrailr alfltpyalp vyaavitwsf llqrdtglvn hvlvdqlgll
      181 gerpfwligd nsfwsllvvs vwrnwpfafl clmaglqnvp gelyeaaaid gagfwrrlrs
      241 vtlpmlrpvn lvlllvlflw tfndfntpfv lfggsapeqa dlisihiyrs sfktwdfgsg
      301 samsvalllf lmvvsaayll itnrrrddha
//
LOCUS       WP_357555455             959 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555455
VERSION     WP_357555455.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..959
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..959
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=101523
     Region          <12..954
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mttglenask dprfvgrrpq larieraqat vlsrgrqmvc evvgepgigk trfvhealrq
       61 saptvgwaig tcspdergvp fhvfrhalte gqslrrglra grslgetwae saaavppapa
      121 rasdarrfrt yqlarrligl aardglvlvl ddlhwadass aglithllry pvpaplllvl
      181 vyrprqmatp mpfgppdpge hadatptshd rielrplgla evallhpyvd qvelrarydv
      241 sggnpgylaa lpgdptsnga epvraapgar lsdaavavlr rewaglppve laclragaiv
      301 dvpfaadlla evaqvpvala aeagwrlarl dlirrvpgsg rfafrhpvlr mavaqdtdpa
      361 wqveacaral galvdlgapp adlaryaerl lalpngrwad rcvnvlcraa qevrretpdl
      421 airwlrlalr alrptaglaq rrqdvslala qitgeagdla esrallqeiv plfpadpqgr
      481 raqavalwar verllgnyae aaaisrrela alpaaagpag gyrlateigv agimagrpva
      541 glpdglngdl ggsgadragl lavrglaaah dgalddargl ldagarivda lpdtdvrdhp
      601 dcltalglte lylerqadav rhldrgvtlv rashrddglc qlllgrsqva yhggqlnsai
      661 alateagiva rrigshdlls falafeaeat awrggprddd ravalarsaa giatdlatwc
      721 grtaatalat aallsgdpat caelvrsagg dsrlsrlqtt lrprwfellc aaalaagela
      781 daerqarlam aeaeqvglpg qrgfaesayg evllargeaa aalphletaa dlfraggmvl
      841 rrslalasla raaeaadqtg paararrral elagwcgter valrlarpvg prevaaltdr
      901 ewhiarlaat gatsrligrq lsisprtvea hltriyrkag vasrsalvaw varlddtdr
//
LOCUS       WP_357555439             121 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555439
VERSION     WP_357555439.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=13635
     Region          3..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhafdvlgdp vrrrilella dgeqsagavs avirdefgis qpavsqhlkv lrdngfatvr
       61 pegtrrlyav dprplrevdg wlehfrrfwt pplaalatel argrrerrlr epadspderd
      121 t
//
LOCUS       WP_357555466             707 aa            linear   BCT 28-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357555466
VERSION     WP_357555466.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 707)
  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 707)
  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 707)
  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..707
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..707
                     /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=79715
     Region          190..522
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 msgtvkaali yppltdptsg yhslnyldsy araqghrpae iidanieafh hsytpsayew
       61 lrrelsrlst ddlsgpdalm aranqlglpd pdperlrrsi gvlqdpslfy dyrhyqdavd
      121 gviswmdalg avgfpgqfha gfrlhpppmi sigsvaaltd eallarlnrp flpyyedvli
      181 prlvaggnqv igisvtyqwq lpfalwiarl vrracpdvfl iaggteisdv wkcaskpeyv
      241 fqvladfdai vvgegesayt eildavqtgt lpaghpnvrl hpkygrqrql plryerlaqi
      301 pvpdfsglpw dlylsperfv yysptrgcyw nkctfcdygl ntdgptspwr qdtvdtmiad
      361 vtelskfakf iyfsvdvlap atilrfaekv vergldfrwg aeirlekyws dercellrrs
      421 gcvaisvgfe sgnqrvldli dkgtkpeqar rtmmamtkan igvqmmgftg fptetreeal
      481 dsvnflrdnp dlwtlgglgd fmltpgaiva kepdrfgitn vrpvegsdiv rmlkfdepvt
      541 eaaqaevaqa kaglnpghyh rpwlgatdtp htffyhdryg tavrgvlahd rvrhdtddqt
      601 eflangsfvd rddeqvweay rrirsdeqeg vpgdlpanrh lfrrvdgqvf alnrssrlfl
      661 dlfsapltla eaqrrlwive ptvadrvwrt figqrlirrh rlpapae
//
LOCUS       WP_357555483             338 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555483
VERSION     WP_357555483.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=36126
     Region          101..335
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrdlllifai algaavgigl agavllralr rssitvhlnv lltttvvavv vgvmavaeam
       61 flsahdlevv litvaaaavv slavgghfgr rlaraavwrd qarererrle kgrrdlvawv
      121 shdlrtplag lramaealed rvvrdpdtvd eyhrrirlet drmtrlvddl felsrinaga
      181 lrlslravpl gevvsdalas tiplaearri kliasesgwp tvaasepela rvvanlllna
      241 vrytpedgtv rieagheedh awlsvadtcg gippadlprl fdiafrgepa rtpragdgga
      301 sgglglaivh glveahggrv evrntpegcq flvrlata
//
LOCUS       WP_357555539             929 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555539
VERSION     WP_357555539.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=100459
     Region          9..230
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          105..916
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          709..737
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          789..817
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(790,793..794,797..798,800,830,833..834,837..838,
                     840..841,870,873..874,877..878,881)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          828..858
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          869..897
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mttettaqpi sglrrkgvla vlalhpgviv ssdrlidviw gdrapatapn slqshvsylr
       61 ralggraaiv grppgyvldl pgeatdveva erliragtrs idhgqartll agalalwrgr
      121 slvdvasidw lhaqaerleh lrlvavralv dnrlalgeha alvpelella qqhpldehih
      181 eqlmvalyra grqsdalaty rrlrrtlrdd lgiepsralr dregailaqd palawsapag
      241 evvvarasap aqlppavraf agrhvelrwl derlgrpgap dpqtmviaal sgtpgvgktt
      301 lavhwahqva drfpdgqlyv nlrgfdagga vldpadairg fldalgvpve rvpaglpaqa
      361 alyrsvltgr rtlvlldnar daeqvrpllp gsagclavvt srnqltslva gegahplald
      421 llpageardl larrlgsdrv aneptavnqi iascarlpla lavatsraat rpgfplaala
      481 gelreaadal dafdggdptt dvravfswsy ralspaagrm frllglhpgp diavpaaasl
      541 agtplrears llteltrthl liehtpgrya fhdllrvyas elthdldsdd erqravrral
      601 dsylhvayag arllqpfrdp idlgiahpgv tavapadaeq amawfvaehp vllnvisraa
      661 ddglyahawr lawtmadffd rkghwqdwva thetaltaad lladswaaas vrrglgrara
      721 qlgqfteaha qlrqaarlya rlgdvtgqah varsiawvca rqgrhregls haqhalrlce
      781 aigdralrar alnsvgwqya qlrdhraalr hcrralhllr avgdrfgean twdsigyahh
      841 hlgdypqata cyqravelfr dlgdryyead tlthagesyq aagdpeaarl awlraldila
      901 alghpdadrl ratlrhhpsv rptapstca
//
LOCUS       WP_357555558             223 aa            linear   BCT 28-DEC-2024
DEFINITION  VOC family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555558
VERSION     WP_357555558.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..223
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23342
     Region          <64..139
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mkklgrrivr gmpdscnsas esawsrplrv gascaapiae srtmcgwpag sacsvqfgpg
       61 ltsaapglam aylvvsdiea thdtlvaagv evgdvfhvsp dgpvdgpdpq rrsyfsratl
      121 rdpdgntwll qeitarlpgr ieggltsfgs asdlagalrr aaaahgehek rtgqhddnwp
      181 dwyaaylvse qsgakprpre prlgpmpvgq hddspasssp tag
//
LOCUS       WP_357555562             293 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555562
VERSION     WP_357555562.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=32383
     Region          8..281
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mtdtllnltl dplgphfgae vrgldlhrat dddlaavraa lvdrkvlffa dqrldddgqv
       61 rlgrrlgelt ashpvvggvd erhpevyald sadngfadvw htdvtfvarp plgsilravt
      121 lppsggdttw adsqlaydsl aepvrrlvdt lvavhdgnre fgyylaqrrg grgsvwdgev
      181 vtrldpvehp vvrvhpetgr rgifvnpgft shivgvseae sraildllya hltkpehlvr
      241 hrwrpgdvam wdnrstahya nrdyggarrv vhritlrgdr pqgpadpwrg ppr
//
LOCUS       WP_357555634             697 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555634
VERSION     WP_357555634.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10196129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..697
                     /product="serine/threonine-protein kinase"
                     /calculated_mol_wt=72642
     Region          28..288
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(28,52..53,86,91,96..99,111)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(35..36,38..41,43,56,58,94,110..113,117,119,156,158,
                     160..161,163,173..174,177,194..197)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(35..36,38..41,43,56,58,94,110..113,117,158,160..161,
                     163,173..174)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(39,117,119,156,158,160,177,194..197)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(173..181,190..197)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <291..602
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          560..691
                     /region_name="PsbP"
                     /note="cl03356"
                     /db_xref="CDD:446075"
ORIGIN      
        1 mtqiptwsgg pvspangraa pgttigdrya lrssvgnggm gtvwratdtl lrrdvavkev
       61 vlppglapsd rdamyertlr earaaaaiqh pavvqvydvv teagrpwivm elldarslad
      121 mviedgpvap ravakigial lgalevahai gvlhrdvkpa nvlictdgrc vltdfgvarm
      181 ptdvqlttpg mvlgsphfis peramgqefg ppsdlfslgv tlytavegrp pfdkgdpiet
      241 mhavvedppa ppqrsgpltr vlmgllekdp arrldvhtsr amlrellagp lgstatavhs
      301 vtdpyavvpv qqrpvpvlpp aqpepkpdnq iggpamlapn esltdrlaal rrgerpkpvt
      361 pvggsgfdet sadalagplh tptgampgpd qqpsgrtygg ssdatqrvda gahpdatqrv
      421 sygnpadatq qvgyggapea tqrigggapq aaqrggtygg gnqwsvpgtg qpwatppaas
      481 ggggalgkvr atggqlvstv kgwprkvqla aagglavvll ltvvalssgd dpppntpaaq
      541 ptasapaapt vemqehaarg iqvsvpqgwt katgasyfdy vdpgdegrkl riltekwsgs
      601 ptrwaesaqn flrtksttck kpykqvsise kesagspgve feytcgeggd mrhgvwhavv
      661 nngkaysfyl taseaafaes kpifdemvkt fqltgeg
//
LOCUS       WP_357555648             582 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555648
VERSION     WP_357555648.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 582)
  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 582)
  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..582
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..582
                     /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=61123
     Region          1..445
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          515..581
                     /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(538,547..549,556)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            548
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvirac rdaglgsvav yadsdrealh ttladeayal ggdsatetyl
       61 ridklldvaa ragadavhpg ygflsenadf aqavidaglt wigptpqair dlgdkvtarh
      121 iaqragaplv pgtpdpvasp devmafavdh glpvaikaaf ggggrglkva rtmeeipqlf
      181 esatreavaa fgrgecfver yldqprhvea qvladqhgnv ivvgtrdcsl qrrhqklvee
      241 apapfltdaq raqihdsaka icreagyhga gtveylvgkd gtisflevnt rlqvehpvte
      301 etagidlvre qfriadgakl rstedptprg hsiefringe dpgrnflpap gtvtalrlpt
      361 gpgvrvdtgi sagdviggnf dsllakliit getraealer arraldemiv dgmatalpfh
      421 rlvvrdkaft aepftvhtrw ietefhntvp pfaaagaaea paeretvvve vggkrlevsl
      481 pagfggsttt aapasrkpar rggaakagap vsgdaltspm qgtivkiava dgdtvaegdl
      541 vvvleamkme qplhahragt vsgltaevga vltagapict ia
//
LOCUS       WP_357555659             327 aa            linear   BCT 28-DEC-2024
DEFINITION  ketopantoate reductase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555659
VERSION     WP_357555659.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 327)
  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..327
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..327
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33960
     Region          1..297
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mryviigaga vggtigvrla qadrdvtvva rgahlaaira rgltlrqpdg evtarldavd
       61 gpgeqplpad tvliltvksq dtagalaawv dapvvgggta gerlplvtaq ngvaneraal
      121 rlfvdvhpvc vwlpathldp gvvvangyph pgmlhigryp agvddtdrai aadlsaagfa
      181 apvredvlrw kygkllsnlg nglqallgqd ipdalvervr aegvaalaaa githtspqee
      241 kaergdlvrq rpvdgearsg gstwqslarg tgstevdhln geiallgrlh gvhtpvnvav
      301 qravrravre rvaagafpla elekmip
//
LOCUS       WP_357555820             304 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555820
VERSION     WP_357555820.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 304)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..304
                     /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]"
                     /calculated_mol_wt=31206
     Region          22..156
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 madtaslrar gaafwagaaa gwirhadrqd eagrplgaaa tdrlaarpge rildvgsgcg
       61 gttaeiaaav gvtgaaigvd ideamvaaar rrfptddypg iqfhvadiet ldvvpgapfd
      121 aaysrmtlml ladptagcra irrslrpggr laatvfrdsg vnpwlsaaml gaaphlgplp
      181 plpvgdepgp fafadparlv rilttagfta vtvtpcdval etpddadava ewlvevgpag
      241 apyraaapsa rasaragaar llrrfrapgv gyrlptglwl vaansagadn ptathpqprq
      301 detr
//
LOCUS       WP_357555793             437 aa            linear   BCT 28-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555793
VERSION     WP_357555793.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=48704
     Region          5..426
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mtagtaivll trdlrvhdhp alattcaafd rvvplyvldp eladrsanrt rflhqaladl
       61 raelrerggd lvvrhgdpva etirlagevg atavalsadv shyarrrerr lraecerhrl
      121 hlrlfpgltv vepgalrpgg ggdhyrvfsp yhrawagsrw reelapprrv tlpggvrvgs
      181 lpkppagdsp daavggerva rqrltdwlpd ldryadqhdd magddtsrls pylrfgcvsp
      241 lavanragdr sgpfvrqicw rdfyyqvtaa fpeistaayq rgaterwryd ddalaawaeg
      301 rtgvpivdag mrqlrtqgwm hnrarlitag fltkslgqdw rggvgvffrw lldgdvanns
      361 gnwqwvagtg ndtkpyrrfn pvrqaerydp agdyvrrwvp elagvrgkai hqpwklpeap
      421 dyppplsvpg tepvwlr
//
LOCUS       WP_357555823             146 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555823
VERSION     WP_357555823.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 146)
  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 146)
  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..146
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..146
                     /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=15987
     Region          21..141
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msdaasadvg vlsahllsnf eeqlfsrlta aghdrlrrrh gavmayldlt gtraselaer
       61 ssthkqvigt lvdelealgy vtrqpdpddr raklivpter grqqialadt lvadieraya
      121 ervgakrfaa fkevfaeiag hpyirs
//
LOCUS       WP_357555859             426 aa            linear   BCT 28-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555859
VERSION     WP_357555859.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=43327
     Region          41..419
                     /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(51..52,55..56,59,91,141..142,144..146,149,168,
                     171..172,175,251,254..255,258..260,263,290,294,343..344,
                     347,351,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 mtppptaapa ppapvlvdpp strdpgtgrr thpatggalv lvgmllvaln lravvtslga
       61 lldeirdglg lsgtmaglvt tlptiafagl galtpwlvrr vaparvlvva mlalavgqvl
      121 raatdsawvf vltsalalag iavanillpm lvkqhfphrt glvtgaytma ltlgttvaaa
      181 savpiahafg swraglgvwa amaavavlpw vplalrtrag arrstptaag tapvrvrpar
      241 trlgwamavy fgaqslsgya imgwlaqlfr dagyqpesag lllagvtalg vpialvmptv
      301 agrmtslrpl vlgmttastl aylglalaph gaallwvill aigqgafpmi ltaiglrart
      361 aegtvalsaf aqstgyviaa lgpllvgily evtggwtapi gfllgalavq tvagmaisrp
      421 ryvede
//
LOCUS       WP_357555828             416 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555828
VERSION     WP_357555828.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=47346
     Region          4..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 msspkermpr vesltglrwf aafavflfha nqiislptvy gikpgdffrf gdagvtffyv
       61 lsgfvltwsf spkvntatfy wrrfarvwpa llvstviawv slnqvwehsw krtllslslt
      121 eswfrpaefl vanpvawsvs ceaffyllfp fvirpllrlr lpalaiiaaa glfvewaywf
      181 fvqdlidpkq ywiqlswflr fppirfiefl lgmiaaaall rgwrprinlw lalsavpasv
      241 lvlwwgaeqg wwgahwsqqg lvpacvlvvl aasirdlsgr psifrskplv algawsyafy
      301 lvhlsvihwl mgpvtpsagt wanlkvlliw tvmgialawa cyrwvehpve rflrnlyprr
      361 vppapptppa pqapeepqel vavseprtev vltghgvltq emepglyrst gsfdvr
//
LOCUS       WP_357555901             783 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555901
VERSION     WP_357555901.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 783)
  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   3  (residues 1 to 783)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 783)
  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   5  (residues 1 to 783)
  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 783)
  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 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..783
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=85875
     Region          6..757
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mddrawrirr tkadldrlde tesifavgng wvgwrgvlde gvpcgmpgsc vnglherrel
       61 sypeegyafp pasdtvisap naalirlwvd depldirtgt lrhheqvldl rsgvlrrete
      121 wtspagrgvr irstrlvslp rrpvaavrye vepldapvev rvcsdllane tvpqrsddpr
      181 aasvpdnplt aeayraagrd gvlvhrters gqrvavavsh lvdgpttvtt tgdgtpdrvr
      241 ltvagrlhqg erlrltkfaa yewaavdats adelaalava eadaaradgf dalltdqraa
      301 ldaawqvadv qldgdpelqq avrfamfhli qagrpdadrt ipakgltgng ydghvlwdte
      361 tyvlpvltyl apavarsalr wrhhhlpear eraaelrltg atfpwrtigg recsgywpag
      421 taalhvnadi adavlrylaa tddklflaea glellvetar lwhgfghwsd eghfhlhgvt
      481 gpdeyaalvd dnvftnlmar rnlrgaadaa erhpeladrl gvdrdeiagw raaadaafvp
      541 ydhargvhqq aagftdqpew dfantgdddy plllhfpyle lyrkqvvkqa dlvlamqlcp
      601 gefsadekar nlayyeartv rdsslsaapq avlaaevghl dlaydlfaes vlqdladlgd
      661 ktadglhlas lagawlalvq gfgglrddrg vlsfdprlpr ridrlafslr wrghrlrvtl
      721 tptearyelp gagpdaevel whhgeplrvt gaepvtrpmp pvpdpgpepp sppgrrptrr
      781 ssd
//
LOCUS       WP_357555928             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555928
VERSION     WP_357555928.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,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 265)
  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 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..265
                     /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=28357
     Region          <1..243
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mlevdrvtag ygdiltvved vtlrvaagei vglvgdsgcg kttlarvitg lhrprggtvr
       61 vagvdvhalr gralrahrrq vqmvfqdpfl tlsprqtirq aiaeplqihr igdsrsrsar
      121 vdelldlvgl dptvgdrrpg qlsggqqqrv aiaralalgp qllicdepvt aldvsvqakv
      181 lnllcdlrdr lefgclfith dlavvaqlad riavmsggri veqgptgqii nqpahpytqa
      241 llavgihdgh rltgtirpah styss
//
LOCUS       WP_357555933             320 aa            linear   BCT 28-DEC-2024
DEFINITION  epimerase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555933
VERSION     WP_357555933.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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 11437757
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..320
                     /product="epimerase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016854 - racemase and epimerase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=35099
     Region          2..300
                     /region_name="YfcH"
                     /note="NAD dependent epimerase/dehydratase family enzyme
                     [General function prediction only]; COG1090"
                     /db_xref="CDD:440707"
ORIGIN      
        1 mkivipggtg qvgtildral taeghdvvll trspkgerqv hwdgrtlgdw arqingsdvv
       61 inlagrsvsc rytaenleam mssrveparv vgeaiaeagr ppkvwmqmst atiyahrfda
      121 andeygglig gaergvpgyw aysvkiaqnw evaqeqaatt pdtrkvalrs amvmspdrgg
      181 vfdvlswlar lglggpvagg rqyvswihdq dfvravrfli erddltgavn laapgplpqr
      241 dfmrelrsaw rmpvglpatr smaevgafam rsdtelllks rrvtpgrlsd agfafdyprw
      301 rtaaadlaar rrrgwrlrar
//
LOCUS       WP_357555974             472 aa            linear   BCT 28-DEC-2024
DEFINITION  xylulokinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357555974
VERSION     WP_357555974.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 472)
  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 472)
  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 472)
  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 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..472
                     /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=47552
     Region          3..432
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 mplvagvdss tqsckvvird aetgelvreg raphpsgtav ppavweaals davaqaggld
       61 dvaavsvagq qqgmvcldae gavvrdallw ndtrsagaat dlisdlggge tgrrawaqav
      121 glvpvasftv sklrwlasve penaartaav clphdwltwr lagapgldal rtdrsdasgt
      181 gywsaaagay rpdlirlafg rdglllpqvl gptgraghlr tgaplgpgag dcaaaalgvg
      241 aesgdvivsi gtsgivstvs dvpaadasgi vagfadttgr flpvvctlna arvldaaatm
      301 lgvdhaqlsa lalsappgad glvlvpyleg ertpnrphat gavhgltlrt stpahlaraa
      361 vegilcalad glaamiaqgt tvnrvilvgg garseavrri aptvfgcpvl vppplgeyva
      421 dgaarqaawv lsggqrppaw tigqvevyda eavpavrery aaaranvsdh ad
//
LOCUS       WP_357556000             282 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556000
VERSION     WP_357556000.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 282)
  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 282)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 282)
  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..282
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..282
                     /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=29336
     Region          37..277
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnahprpsgr srtvpvvavv isvlvmamct vgtqgplavi lpslivggav taalwavrrt
       61 radraayesr ltawaaseav laerlriard lhdivshglg litvraaatr hlpkpaevqv
      121 altdiedasr hataelrrml tvlrepaaag rrapvdsldd lpdivhgasl agirarltve
      181 plgpvsqgvq vavcktvrea lsnaarhagp tdvrvsvyrd gthvvvtvad tgpsvdgwra
      241 spgaghglag lrervgslgg tlsaervgag frlsarirde aa
//
LOCUS       WP_357555992             198 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357555992
VERSION     WP_357555992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=21806
     Region          6..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          102..179
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(107,109,122,125,129,163,165,177)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mdtspertld avgprlkhlr qrrhitltdl aaatgistst lsrleaglrr ptleqllpla
       61 rfygvtldel vdapptgdpr vnmrplptsd gstvlpltrr pggiqaykfv lptgrddaqp
      121 dlrthqgydw afvlngrlrl vlgehdlile pgevaefdtr tphwfgatss gpveflslvg
      181 kqgerahira apqrhesr
//
LOCUS       WP_357556062             107 aa            linear   BCT 28-DEC-2024
DEFINITION  divalent-cation tolerance protein CutA [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556062
VERSION     WP_357556062.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003543
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     gene            1..107
                     /gene="cutA"
     Protein         1..107
                     /product="divalent-cation tolerance protein CutA"
                     /GO_process="GO:0010038 - response to metal ion [Evidence
                     IEA]"
                     /calculated_mol_wt=11510
     Region          2..104
                     /region_name="CutA1"
                     /note="Divalent cation tolerance protein CutA [Inorganic
                     ion transport and metabolism]; COG1324"
                     /db_xref="CDD:440935"
ORIGIN      
        1 msdyvqvsta aptreaavrl aegataarla agaqvagpvl svywhlgeqg tseewqvllf
       61 tttdryprle aylidahpwe npqvtatavv hasadylawi rrtvega
//
LOCUS       WP_357556121             222 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556121
VERSION     WP_357556121.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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: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=23522
     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 mselsstfvr lharlapvaf vpevrlhqad epiglwelte gefstdrppp fwafawaggq
       61 alaryvtdhp elvagrrvld lasgsglvai aaaragaasv ravevdelav aavalnaean
      121 gvrvdaefgd ildsdagdae vvlagdvfys gamarrvlrf llraartgap alvgdpgraf
      181 lprdrfdela vydvpvpeal esvrvkrttv wqlraglpga ar
//
LOCUS       WP_357556125             193 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556125
VERSION     WP_357556125.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 193)
  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..193
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..193
                     /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=20808
     Region          2..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 martrefdld aavnaamdvf rrkgyegtsm rdlaeatglg sgsiyaafgs kdglylavld
       61 lyrqryaapm vdllrsgnda revirevfvg avdditgdgr hlaclivgas merahqdlrv
      121 aerlrsttqs lelalhdlla eaqlrgqvts drsatdlagf lvtslqglrv mgainpdraa
      181 ltryaevalt cln
//
LOCUS       WP_357556154             318 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556154
VERSION     WP_357556154.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..318
                     /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=34717
     Region          54..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msdlpliqad havpppaatt stggrrrrlr llsrtdrvvv tlmvlvplll vtgfvwlpaa
       61 atvllsgtnw dgigpldeie fvgarnysdv vniyppfvpa iqhnllwlaa lfvvatpfgm
      121 flavlldkel rgsrfyqtal ylpvvlslal igfvwqllys rdqglinavf gssvdwygds
      181 svniwavlva sgwrhvgyim llylaglkgv dpslreaaav dgasesrtff rvvfpvlrpi
      241 niivlvvtvi eslrafdlvw vvnkgrngle lisalvtqnv vgeasrigfg salatimliv
      301 slvfitiyla tvlredrq
//
LOCUS       WP_357556161             287 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556161
VERSION     WP_357556161.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 287)
  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..287
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32699
     Region          14..77
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(20,24,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(23,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(30..31,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          102..280
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mphkpfirtl raqwlgqqlr alreergmtl klvaehlqrd msalgryera dwpirkgdvi
       61 allalygfhq aaerarllal aeevwrtdrw dedygdvvda sfieypwleg raeqvccfhl
      121 tlvpgllqir eyaeavirna aepgvseati nrwvelrmtr qevlrrrrpl tisavideaa
      181 lrrvvggpev lrrqlhhlaq aqrlgnvair vmpfgvalhq gldgtfwifr lpepypavay
      241 veslggrlyl espkaerfvr afgrlldsal sesestklit siaeels
//
LOCUS       WP_357556177             375 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556177
VERSION     WP_357556177.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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..375
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..375
                     /product="LolA family protein"
                     /calculated_mol_wt=39369
     Region          11..262
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 msvlrsrpvl rwlvpataav avigggaaig tfaaeaepsl pprtaaqllv dlqtsrlegv
       61 sgtvvqradl glpplvglap gneltsmltg thtlrvwysg perqrvalld tlgeqdvirn
      121 grdvwtwesr tntarhralg dteagkaape arpnlpatpq qaadlalaai dpstevnvgr
      181 satvagqday elvlqprdkd slvhqlriai dakqhvplrf evlakgsdqp afemaftqid
      241 yrrpaddqft fnpppgvtvt eekaerpgpg kpghvkpaad pqvravgtgw ttvlvarldg
      301 alggkpadak pavppagaap dmdlskllgg laavkgdwgs grlltsklfs vlltddgrvl
      361 agavtperly qaarg
//
LOCUS       WP_357556189             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357556189
VERSION     WP_357556189.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..416
                     /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=43894
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..379
                     /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(349,351..353,355,366..367,371..372,375,379)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 midelaraes avatcadasa walsehdlia aldathrlqq rlaavqvavv reldgrgtav
       61 aqgassttvw lrhrlrldva aarrlvglaa sldvappavr aalargavtv eqarviaeav
      121 atvsahagve vadkavgvlv dwaaqfdptl lrrlgsrild hvapeiadaa aaaaleaeaa
      181 raardrhvtv seraggrlrl sgtldaetaa lvraaidpls ppcgpddtrt pgqrrhdala
      241 evcrlalrtg elperggdpa qlvvttdfdg ltrrlgagtl dtgphltpaa vrrlacdaai
      301 lpavlggagq vldvgrqrrl vtgplrralv lrdggcafpg cdrpprwcaa hhirhwadgg
      361 ptsldnavll cghhhrhlhq aewavrlggd gkpefvppaw ldpgqiprrn hyhrrt
//
LOCUS       WP_357556201             420 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556201
VERSION     WP_357556201.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..420
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45009
     Region          1..414
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mttdsrvegl lrelapqvlg vlarrfgdfa taedavqeal laaatqwpve glpanprgwl
       61 vqvgyrrmie lvrgeqarrr redlvarrnp ddrryapaad eeltaerddt lvllmlcchp
      121 alaptsaval tlravgglnt aeiaraflvp eatmaqrisr akqrirasgl pfrmpeeaer
      181 aerlaavrqv lylifteght stagpalrri dlaaeairla ralhallped setagllalm
      241 llteargpar tgpsgelisl adqdrtrwda aaiaegvalv tgalprgpvg pyqvqaaiaa
      301 vhdeapstsq tdwpqilaly evlgrlvdsp vvtlnravat amvhgpaagl aalaalagdp
      361 rlgghhrlpa arahlhemag dreraivdyr aaaaltsslp eqryltmraa rlaaepvdls
//
LOCUS       WP_357556204             743 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556204
VERSION     WP_357556204.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 743)
  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 743)
  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 743)
  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..743
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..743
                     /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=81383
     Region          1..742
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mlydrldglr eqaaqrltae lrntggtlqd rsqrdssvam yadqveqfsa venglcfgrl
       61 dgdddsrhyi grigifdtsg dydpllmdwr apaarafyla taanpqgvrr rrhlrtrqrk
      121 vtglndevld idtaspgghe eltgeaslla alnagrtgrm rdivetiqae qdeiiraelp
      181 gvmvvqggpg tgktavalhr aayllythrr elssrgvllv gpnatflryi sqvlptlaet
      241 gvllrtqgdl fpgvsaqrte paqtaalkgr avlaevlala vrdrqwvpde pleidveret
      301 ltldpeivra ardrvrrvdr phnlartlfd tevvhaladq vaerigadpl ggdnlldead
      361 raeirrelre eteiqaaldr lwpvltpqrl ladlyadpdr iaaaapmlte eerallrrep
      421 ggwtpadvpl ldeaaellge deraaaarrd rirmmereya egvleiargs rsidvedeae
      481 ggeilgvtdl idadrllerq eeadrlttaq raaadrrwaf ghvivdeaqe lspmawrllm
      541 rrcpsrsmti vgdvaqtgal sgtpswadal apyvaqrwrl teltvsyrtp aeimtvaadv
      601 laqidpalrp prsvresgvp pwdrtvpder laaelvaaat reaaaltegr lgvlvpagrv
      661 gelgaaltga lpeaavgehp elesrvvvlt vaqakglefd svlvvdpdrm vaesprgrsd
      721 lyvaltratq rlgvlrptpi aah
//
LOCUS       WP_357556205             447 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556205
VERSION     WP_357556205.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=47255
     Region          72..446
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 maigvfglti glalggvvll galgfvlqrt vdteafrtad avallaaeda lpdplpvagg
       61 qvrvqvvdgq griraasida drlvpmvrpe rldhdgrqrl evpaervglv gpvrvvavpa
      121 gtaadpltvl varsmadvrh sahavrvill vafpllvavl agvawrvvga tlrpvealrr
      181 gaeeitgrag tgrlpvpasa deihrlavtl ngmldrlesg rvrqrafvsd aahelrsplt
      241 nirtelevaq rladrtdwta vtanlladtd rlsrlvddll llarldeapp argtgpvelg
      301 alltevaary psppvrvtmp pgplwttgna delrrvlanl vdnavrhayg tvvlaaeaap
      361 vtrrtdgayh lvtvtddgpg ipaadrervf drftrlddgr arddggaglg laivresvrr
      421 aggsitltda peqhglrvrl llpadpv
//
LOCUS       WP_357556235             385 aa            linear   BCT 28-DEC-2024
DEFINITION  branched-chain amino acid ABC transporter permease [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357556235
VERSION     WP_357556235.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   ter Beek,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 385)
  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 385)
  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 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..385
                     /product="branched-chain amino acid 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:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41796
     Region          64..370
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 midkirsadr rrvgaltsvg drwralpkwq qaiglaafva ilyylpllgi pgltwlrtds
       61 ieggnnwagv lfvcaiyvlv aiglnvvvgl aglldlgyig ffaigaysva lfgsvnspvv
      121 kwiqqefnlp ptwavtwaic lfiaivltmi sgvllgwptl rlrgdylaiv tlgfgeiiri
      181 varnatgltn gpvgisaipg pegapsadnk vfglidakpw ywlaitfvlv mvflvrrleh
      241 srvgrawlav rededaaavm gvypfkfklw afaigaalgg lsgflfgsrn afidptqfna
      301 nlsilfvamv vvggsgnmig vslgavllay lperfrdfad yrwlvfglam vlvmilrpqg
      361 lvpsrrrare lkdraaeaee vparv
//
LOCUS       WP_357556266              88 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556266
VERSION     WP_357556266.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 88)
  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..88
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9033
     Region          15..>74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvrppltpaq iaagqrlgaa lrvargarpl vevalaagis petlrkievg rlpapafgtv
       61 vclsevlgva lsdlaevwla dlrireas
//
LOCUS       WP_357556322             735 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556322
VERSION     WP_357556322.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 735)
  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 735)
  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 735)
  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 735)
  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..735
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..735
                     /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=77382
     Region          163..720
                     /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 mprrsdeprr dptgtrrgss rdatpadsep rtgepgiggi sgaraytprg rtvrdergtp
       61 prgvgaeqrr tprstrsgdp frpalqvldg graaaragrr dapaagrggv vrtvaprtpr
      121 gpgvdepppr rrttpraprr adrpaarrps rkpprppkla dsrlrlrlgt alaltlfvti
      181 girliflqav dapayagggv adrtikvelp aprgaiydtt gaplarsvea ryvfadptev
      241 kdpaatakal spllgipask lvtlmkprkl engnlskfay largveipta krvqalelrg
      301 igvhrderre vpggdlaanl igftsqdmvg leglearynd vlagqdgqrr yeaglgdlga
      361 pipggfsqtt pakpgsslgl tidgdlqfrt qqilsegmak qrggtgaavi meipsgavla
      421 qasdptysaa kpadsdpver edaatsfivd pgsihkaity gaalqegvit pdttlpians
      481 ikmgdtwfsd thpaggkrms ipgmlayssn vgaitvadkl grdrlidyqk rfglgrptge
      541 gmpgeatgrl lpaeewsgss ygsvpighsv datplqmtaa yaaianngty vqphlvkevi
      601 gpngkrtpap apvtrsvlsp qnaaalrtml eavttvedat gttaavpgyr vagktgtgwr
      661 lvngkkqrge vssfigmapa dnpryviavf vyapdgggaa ianpafrdmm qftlrhyrvp
      721 pstggsapkf vvypr
//
LOCUS       WP_357556356             434 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556356
VERSION     WP_357556356.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  AUTHORS   ter Beek,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..434
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..434
                     /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=47133
     Region          38..345
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mqrfrrlvaa ialaatattt vaacgggdng ddsdakvlkl whyesensam gvgwnraiei
       61 fknehpgvev rferkafeqi qqnagmiins segpdimeyn kgnataglls tqgllsdlsa
      121 eadkrgwagk lspslqttar ysdkgvmgsg kwfgvpnyge yvtvyynkdl fqrngvkvpt
      181 smaemtaamd tfvgkgvtpl gmagaeypag qlfyqlalsk gdrqfvdnyq lyknpvdfka
      241 dplkygadtf aewvrkgyva knsaslkaed mgtafiagkt pmivsgswwy grfktemkan
      301 wdtflfpgnt lnagssgnlw vvpenskaks laydfiditl rpeiqdlign nggvpvaada
      361 skisdpkdrk liedfntvsk sdglafypdw pvpgyydvlv sgfqglings kspdqvldai
      421 akpyadgvke itsk
//
LOCUS       WP_357556394             344 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556394
VERSION     WP_357556394.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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..344
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..344
                     /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=37507
     Region          40..329
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqattmsddr riadaqrlla elgvsvddlr daqrpqvpti aeylprvvaa agpgasrtyg
       61 sywariaaqw gdrrldsiva tdveallrqa aavalprrng rggrhagehv iaavraiynr
      121 avadglmdas dspahrvskp rrlpstrral tpeeleeine varssgndvv ldaillrlht
      181 etacrrggal alrlmdldrd rglvrltekg gtlrwqpitl dlaaslydha rqrgavlptd
      241 allrfrhgga itsrrydhlw krigerlpwv aaqgisthwl rhttltwver hfgygvaray
      301 aghtdstgaa tttyikadln avatalsamt gqphplarpt dasa
//
LOCUS       WP_357556445             273 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556445
VERSION     WP_357556445.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 273)
  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..273
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..273
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28081
     Region          1..269
                     /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 mttlrtvavd gspvhvlesg tgpavlmlhg sgpgttgsga wattaqalgt swhlvapdqa
       61 gfgrtpvpag argglrlwte qaaglmdalg vehyavvghs mggavalala aarpervtrv
      121 vavstmgapg aplsadldal waapagrpga rdmlsrlvld qalvtdsavd araaamrage
      181 aafaslfppp rarwvddltl saqtlaavrv pvllvhgaed rvtplgtaaq pllehladvr
      241 lhvfgrcghv paiehphefr qllscflhqd rgh
//
LOCUS       WP_357556409             539 aa            linear   BCT 28-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556409
VERSION     WP_357556409.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 539)
  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 539)
  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 539)
  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..539
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..539
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=58036
     Region          287..530
                     /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 mqaelrwqld hhfdsktivi adrrlgnpaa arraiddark alggqdvllv claghavtft
       61 rrdgditala lpgsvpgrpn smlridelsa vvlpeagkpv ivcadlvsar dtvgavapaf
      121 agafvlasps aadttpestc hdglaavlgd laasgtqqav phlldlarqr vvaaggsphl
      181 avsasqaait sryvseqlpd yvredltspd pgsrldavte laalaastpf arasllrlaa
      241 sdraeavrsy adtmsrqdrq pslrqlladg viprevheaa lkepavpdll phtggevilg
      301 vdaphgqddc rprhtvrlqp yrlartvvtn rqylaflaae ggpcpdhwqa hdslwrddlp
      361 vvmvswldal rycawltrhl hhtralapdq rivlpseaqw easagndrgg rhpwgdvpdp
      421 rraniratgi gtvvapgqfs pdgdneagcq dlignvwewt rslwghsghq ptfgypyrhd
      481 dgremastrp geryvirgga fyyatecans ftrnrmlatd rhpaggfrva stnaretts
//
LOCUS       WP_357556467             991 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556467
VERSION     WP_357556467.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 991)
  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 991)
  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 991)
  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 991)
  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..991
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..991
                     /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=106286
     Region          27..276
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          157..956
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          811..838
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(812,815..816,819..820,822,845,848..849,852..853,
                     855..856,885,888..889,892..893,896)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          843..873
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          884..912
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          924..950
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 meqeielsks agarhaddgp rpvsgslrfq ilgplriwrd dvelsagprq qghllallla
       61 ragrpisvsn liellwgeda ptsatnvihk yvgtlrrlme pslplratgs ylrrhgggyl
      121 fapgpgtldl vrfreltsaa raslalrdrd raldsyveal elwrgpagdt yasgsaatsi
      181 faaldrefld vcvsatelav slnrsgrvlq plrlaasmaa lnepvqasli salgaaghqa
      241 ealkvfrtvr srlredlgid pgktleaahr hvltqataea dagqgqtvdr lppeplvrpa
      301 qlppdlptfv grteelatls alrsglggtg rtgplivald gmggvgkstl aahfahlvsg
      361 dftdgqlyld lrgdqtsdes vsagdavgsl lssqgvhvss ipetlaarvg tfrsltasks
      421 ilvlldnasd caqvrsllpn speslvlvts rkplvelaai dgahllhldp pdmrtarelv
      481 rrrlvsapnr amagfsspad ildeiielcg rlplalaila grlsarprla ladvaaelrd
      541 gtqrlaafss shsvrdpraa fawsyrqlsp daarlfrlss aamapglsaa asaslseqsp
      601 gvaraslrel adaalldedd kgrftshvlv kayaqelflt hepaadraaa ttrllqhylh
      661 sayraaivla perpivapsp apagvapeqp taydeamrwf eehrevlpea vrraaegdfg
      721 iagwqlalsm qqwlrrsgrf hdwqdvmhva lasasdrgdq vgaahvmcsl adssshlgah
      781 eealdlissa qqifaehgll aeqgvvhstl hrihtqlgqh rraleenera lalnraagie
      841 hceiwasaaq grslvrlgal daamscleea ltrseksest tdeadirism aeclsamgdq
      901 hravehlera vdmaaeaqdr igvfeasill ceahlcldev pgacrawrqa cdamhamqng
      961 gtrnmrdkvc dmgdkltevt efcprsedtq r
//
LOCUS       WP_357556474             334 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556474
VERSION     WP_357556474.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  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..334
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..334
                     /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=36557
     Region          15..191
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mllpisgpas agdveqvvra aqqgdprsft llyelhyagm laaahqilga vpdaedacqd
       61 aaitafgrig elrdpaavrp wlhaivrnnc rkllrsrrpv pvgvagetlh aselddpvar
      121 idrsalrdwi whglhqlspa aqtvamlryf tennsyeqia dlcgvpigtv rsrlsearrq
      181 laevlprvhd erhhetaalr aerreeattv lsavangapm srvaarwaed mtfcwpsgkr
      241 ttgreavfaa mrrdydsgva hqitgvvaga gitiwenafi nppedpfhcp pggtwllrek
      301 kglvcevrlm htprpthpei appanrtsvr rtgs
//
LOCUS       WP_357556476             307 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556476
VERSION     WP_357556476.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 307)
  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..307
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..307
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33553
     Region          8..282
                     /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 mntgsektht irvgdlslic hirgrgplcf vhpggpglsg dylrmpller rltmvylepv
       61 gtgdssrlpa gatydletya dhldaviadl sdvpalvlgh ghggfvaqsl alrhpdrtag
      121 lilyatapva dahtraaare klrryalaha drtdaeamia afdrpagrwv hestarlwqi
      181 lpayfadywr rrtefahllg alpcwprstt dfdfrgalps isaptivvag vhdfafgpep
      241 aemlrsaipd avlaefsdsg hfahleeaer fshvvlefal rvsggvpgrp rrademaltg
      301 rhdarww
//
LOCUS       WP_357556496             539 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556496
VERSION     WP_357556496.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..539
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=57437
     Region          60..532
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mttisrrgll vgaaaatgav tagvgaapal adeqtdptvp aarivtpgda rypdvvvgnn
       61 qrfvatpeav ffagstqqvl davqkavrag krisvrsggh cyadfvyhsa akviidmsam
      121 nsigydntrn afaiqpgall gqvyetlkkg wnvtlpggvc ptvgigghva gggygllsrr
      181 ygvvadhlea vemvvvdkyg varvvvasrn sadvnrdlww aaagggggnf givtkywfrs
      241 igatgttpgq qlpqppaevl vsslpvgwpt ltqeafttlv rnfgtwyern adpsspytal
      301 sgaafithrs aggfglvtqi daavpdaarm ldeylaaitq gtgivapypp rrlrwlaatr
      361 ligtsnpatm ldptmrstvk saymrkgftd sqiaalwrgl trtdyanpna tvqltgvagg
      421 kvnslsesat ayphrnasfl tlfenfwmdp sqdaahvgwl rdiyhqtfad tggypvpnlq
      481 tdgcyinspd mdirdpainr sgvpwstlyy kgnyaglqra karwdplntf rhsqsielp
//
LOCUS       WP_357556595             252 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LytR/AlgR family response regulator transcription
            factor [unclassified Micromonospora].
ACCESSION   WP_357556595
VERSION     WP_357556595.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=27905
     Region          6..241
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mtaaflrvla vddeppalde layhlradpr varlhtagda tealrllrdg dvdvvfldir
       61 mpgldgmela rvlrrfarpp aivfvtaydd gavdafdlga tdyvrkpvra drlaeslrrv
      121 igsrvvpshp aalaraeedp tipielagtt rmlprsavrw veaqgdyarl htaegshlvr
      181 vslatlaerw adagfvrvhr sylvqlklia elrlvnsgyv vvidatelpv srrhtrelkd
      241 klvraakqdw gr
//
LOCUS       WP_357556557             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556557
VERSION     WP_357556557.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..265
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27522
     Region          30..256
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpvdpravlt rpapepdrtv aygdhpdqva dlrrpagvgp arplvvvlhg gfwrveydrr
       61 htdplaaala adgypvaqle yrrtgqpggg wpgtltdvlt gvaelpglaa ealpdrvtqv
      121 apilvghsag ghlalyvaat apatvggvla lapvadlgea yrrdldsgav aallgggpae
      181 vpdryaatdp rllvptrtrt vvvhgsedqq vpvemsrgfv aaataagsdi slvelpgceh
      241 fglidpesta wprvvaelrs lrvdh
//
LOCUS       WP_357556627             303 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556627
VERSION     WP_357556627.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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 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   4  (residues 1 to 303)
  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..303
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..303
                     /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=34510
     Region          57..158
                     /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(58..60,74,91..93)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:206648"
     Region          181..298
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mdsknaldqr krwsraflca vslvplcgcs awltltlrqp ltfvshrrve gvvevdwsih
       61 diarmagtts rtlrhygdvg llrpsrfgrn gyryydqekl lrlqrilllr elglglptia
      121 evldgsqhtv ealrthlkll eqererigrq iesvrttlrk teggeplmpe emfdgfdhtq
      181 yeqevterwg reayakgdrw wrslspaeki afqqrqveig rdfgaahhag aaadsdqvqa
      241 itqrlydwls gtsttptrey figlgelyvs dpryaaafdn aentagtatl irdamhvyae
      301 rnl
//
LOCUS       WP_357556707             527 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556707
VERSION     WP_357556707.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 527)
  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..527
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..527
                     /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=54570
     Region          9..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(9,33..34,63,68,73..76,89)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,71,88..91,95,97,133,135,
                     137..138,140,157,159,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,71,88..91,95,135,137..138,
                     140,157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(20,95,97,133,135,137,159,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157,158..163,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <172..515
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mtapqrigpy aierllgvgs fatvwlgydp aldahvaikv laenwshdlr vrerfrdear
       61 llrrleherl vrvhtvgelp dgrpyavlaw adggslrdrl atgeipapaa lrllgeicag
      121 vavlhrhgvv hrdltpgnil fhsagpddpd aervliadlg lakalaaasg ltaragtpgy
      181 mapeqddpga vvdtradvyg lgrlgirllg adppgahptg pgpqgrapdp pgyaaradpp
      241 rhapeirlra gvppavaavl aqatahhpad rypdaatlha alarasgrvg rpvsgptvrp
      301 vaptrasgpv grpvalaras gqvgmaaasg pvrqrpaprr rgrrpyrlrm agaavvavaa
      361 vgavgaepgg agsarpvggt yttgpltvvl pagwsatgat wagqygadge pepalvmspq
      421 prrwaadprl pgafvglsat taarttpagf laerthgdct paparltrqa gaewtvvayr
      481 cdrgrprive saaahpgrpa lvyvqiappa dsgpefvdtl lagvrlr
//
LOCUS       WP_357556788             208 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556788
VERSION     WP_357556788.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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..208
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..208
                     /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=22133
     Region          3..176
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mliadeffli ahndsrgkak lhpaatglgl aggllgelli yghihvaagr vtvidrrppa
       61 dalahtvldq ligesqhqel rtwlsflaqs atasvgerla ragvlrrqes rrllrtsvny
      121 lpidlnavaw patrlralld rpdppsvpda lllglvvaag ltrevlwsag prahhrlnvl
      181 lpalpaplke lvghteaavg aavlrgvl
//
LOCUS       WP_357556807             479 aa            linear   BCT 28-DEC-2024
DEFINITION  rhamnulokinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556807
VERSION     WP_357556807.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 479)
  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 479)
  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 479)
  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..479
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..479
                     /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=50917
     Region          8..455
                     /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 magdrearfa avdlgasngr vmlgrvgpgs lhltqahrfg nepvrvggtl hwdilhlyrn
       61 ildglraagd vtsigvdswa vdyglldatg allgnpvhyr drrtdgvadr iagrlgeerl
      121 yattglqhlp fntlyqlvas agtpqydaad rlllipdlva ywltgqpgae itnasttqly
      181 dlrrrawavd lmaaagirgd lfpplrepgt rigpvrpdvg lpgrpevvav ashdtasavv
      241 gvpsqgtrfa yvscgtwslv gveldapvlt easrlanfsn esgvdgtiry lrnvmglwll
      301 qesvrwwgpv dlpdllrqaa aepalrsvvd pddpvflppg dmparladac rrtgaavpes
      361 paatvrcivd slalahrrav hqaqrlsgrd vdvvhmvggg arndllcqlt adacglpvia
      421 gpveatalgn vlvqaraagt iggdlsalra llretqhlvr yeprghqaaw raaearlgg
//
LOCUS       WP_357556847             138 aa            linear   BCT 28-DEC-2024
DEFINITION  Fur family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556847
VERSION     WP_357556847.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 138)
  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 138)
  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..138
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..138
                     /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=15123
     Region          14..136
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 maatvnqamp nvtrntrqra evlallreve gfhsaqqlhq mllarkagvg lttvyrtlql
       61 lvdageidst rlpggeqlfr rcsqskhhhh lvcrdcgrtv evagpaverw adqvatqhgf
      121 vdvghtleif gtcaecvq
//
LOCUS       WP_357556860             256 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556860
VERSION     WP_357556860.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..256
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27069
     Region          14..248
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 maswldqrta phvgtatlic ipsagngdfq fdrwpdtvgp wcvvrppvvg dlgggapgtr
       61 saaqppsglp eraaelvadl krrgiekfal fghegaallg yqvaveldrq gapaplrlfi
      121 sgcpapqfls ryageahtep tddeltervl atavamgtip lpsivaagar alraelaalr
      181 ayqmphpapl rcpltairwl dqgieaevva gwsaygdtdl vqlpgsglsy atepadllrv
      241 igdrmpaadr rrpaew
//
LOCUS       WP_357556862             200 aa            linear   BCT 28-DEC-2024
DEFINITION  response regulator transcription factor [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556862
VERSION     WP_357556862.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 200)
  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 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   3  (residues 1 to 200)
  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 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
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13297827
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..200
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [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=21248
     Region          <83..171
                     /region_name="PRK10360"
                     /note="transcriptional regulator UhpA"
                     /db_xref="CDD:182408"
     Region          <141..200
                     /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 mgepmwvnvm atdpvleagv tsamlgcpdi vvvttrekaa vtvlvvdhlg qdaldsvrav
       61 rtgahrpevv lvvpevepad alraiaagar gllrrreata erltrtvlaa gegdctvspd
      121 mldrllaapa vpagtlasni sdreravlrl iaegretgei akelcystrt vtsvvhditr
      181 rfrlrnraha vafalragml
//
LOCUS       WP_357556924             939 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556924
VERSION     WP_357556924.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 939)
  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 939)
  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 939)
  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 939)
  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..939
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..939
                     /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=101611
     Region          4..254
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          141..939
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          770..804
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(771,774..775,778..779,781,811,814..815,818..819,
                     821..822,850,853..854,858..859,862)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          809..839
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          849..878
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          890..916
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnpevrftvl gpvrawrqdv eidlrppqlr smlglllvra pdpvapeefs allwgedppa
       61 ragnivhrhi galrkllepe lanraqgrwl tragsgyrle vapseldllh freqaeaatl
      121 aaeggdhpta laqraaalrl whgrcaagid pgaalapefa avdqervava caavddalrg
      181 gdpgdlvpli qaaadqnpld evvharliil lsasgrqaaa gavyhairlr lteqlgvdpg
      241 rdlvaaydrv lrqdslvqpa papdprrsvp sqlppgsnlf tgrdaeldql salaaevgrd
      301 rsatvigvvd glpgmgktsl vvhwahrmsh lfpdgrlfin lqgfdpsgsv vdtgkalehl
      361 ltaldvpyse mpadiatrtn lyrsrmaerr tllvldnard eehvrpllpa ssnslvlvts
      421 rnrltglvtr egatpvslga mtlaesravv rkrvgddrqs gdeqhldeii ascgglplal
      481 avvcaralay ecplrevade lrhavtldpf dgdeprsdvr nvfswsyhml sdqaaqlfrl
      541 lplhlgtdfg vasaaslagv pfhtarkllg elnrtrllte vrlgryamhd lirvyagelg
      601 agedldehrr aavarlldhl rqtayaagsa lmpssrlsep prslagvtpq svadaqsams
      661 wfttelttie gslavrdvpe frpwqlaeal mpyyqrramv prwlstatla lrvavdagdl
      721 egqavmhrmm agaevfgsha aaatrfaaat rhleralelf daagrpldma faycnfgtvh
      781 dsqgrhreal tdyeramsvf esldhergla lalfgrgwql velgdleagl enlaraeala
      841 iagnddsnag scagtmaevl rrlgrldeav aclqrarelf ltsgnhvesa klekrlgdvf
      901 aatgrpaeal sawrmardry adlgqeeava qiekamaar
//
LOCUS       WP_357556945             336 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357556945
VERSION     WP_357556945.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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..336
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..336
                     /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=36396
     Region          3..332
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtstplrvgl lgasriapaa virparktpg vtiaavaard drrgrryatk ydiptvhddy
       61 qslisdpaid avyvplpngl hgqwtiaamr qgkhvlcekp ltanaaearv veaeahesgs
      121 vmmeavhyry hpvalrmiei vrsgeigalr hveaalcapy arfsdiryrl dlaggalmdp
      181 gcyavhmvrt vagaepevvs araelrpsgi dravtaelaf pggvtgrivt slwssdlfrl
      241 svravgerge mrvfnpllpq lghrivtrvh rrarrvehlt rrpsyafqld afaaavrdgt
      301 pvltnatdav rtmsvidavy daaglprrqp vpvpas
//
LOCUS       WP_357556950             117 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357556950
VERSION     WP_357556950.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..117
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13037
     Region          11..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtglpltagt plspaldmlf srwtphilwl ldcsgplrfa dllrrlrplg tamltlrlre
       61 leaaglishe lymlhpprve ysltefgrsv rpvlqaievw tetqlrpaqv sshkava
//
LOCUS       WP_357556995             257 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357556995
VERSION     WP_357556995.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26700
     Region          9..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 mneglpihpl agrtalitgg grgvgasvar lfatagarla ltgrseeslr evadslqdga
       61 viipsdlsrd geterlfdaa larlgqldil vnnvgalnft qsqklteaea ddlwrlnars
      121 plilagraae hmasrgggsi vnlssvigse raianqtlyg atkaavdgmt lamaaewgpk
      181 gvrvnavrpa vtntdmsapi fanpewkktl taqyalgrlg epediaqavl ffaspassfv
      241 tgqllsvdgg wistlvh
//
LOCUS       WP_357557017             286 aa            linear   BCT 28-DEC-2024
DEFINITION  ester cyclase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557017
VERSION     WP_357557017.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..286
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31857
     Region          20..131
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
     Region          162..284
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 miptqdppls ggdagttaal verlfrevyn gqafdlaeql faddyvnhqp gaapgisglr
       61 qwastmltmf pdltgtiehm vvqndramvf vawhghmagt gkelnsqtan lyrvrdgria
      121 ehwsvfdysa lvpfgitppd qeqpasepdw taspaeqenl rlvlrvweev mqkqnleyad
      181 ehyradyiqh nrfaaqsggg lagmkqffag lfvaapdltg tidhilvqdd fvalfsrwrg
      241 reatsgrelk lhtadllrie dgriaehwdv fdysavsqfg iipppr
//
LOCUS       WP_357557035             260 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357557035
VERSION     WP_357557035.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..260
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..260
                     /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=28638
     Region          14..>150
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtdhsefgpe sygerlagiy ddwvvqlqdd teqtvtflad lakqtaadae tgdllelgvg
       61 tgrvalplaa rglsvtgvda svqmldllaa kpggqqvqrv lgdftdmrid rrfgvvyivf
      121 ntllslptqe dqvrclrnaa ehlvnggvlv vqafvpdvar feagrssgqa mevarkests
      181 lllsvsnhdp vtqrmwpryg lkgedgvqey plqfryvwps eldlmarlag lrpegrwggw
      241 egqeftgesp whvsvyrrvn
//
LOCUS       WP_357557049             289 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557049
VERSION     WP_357557049.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 289)
  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..289
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..289
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31393
     Region          12..271
                     /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 mtaarwsrdp apapapvtta hhpvrvhrlr parglscqrl lllnglagsp siwrpfaqrv
       61 paeielwgae lpwasggdph wqaaggptte avegalaavp rgadaivahs faanavlell
      121 srrvpdrlqa vilvspfyra taerfdwsdi syylndfhri laegirvsaa hplapevver
      181 malrlrervg pygwmrffda ylrtpfldlt rvlvpvlvvg grrdlavpia dvealaealp
      241 agrlarvaas ghfamaehps wftsvvqdfl avnappsplp ivdvplell
//
LOCUS       WP_357557050             323 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557050
VERSION     WP_357557050.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 323)
  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..323
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..323
                     /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=36148
     Region          189..303
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mttthiagpt ldavlregtr trlrpryega nictwigfkh vnylveeavl ehlragglap
       61 gglyeryglg vdlvdldtri lhafhvddva vaevtpldpv ggelvfsvvl lvdgdqpira
      121 atarvrvvlr qdsdnapdvp pelrpvttta irraerassa apggnefhws wripyfychf
      181 terlqmsgyl rlmeeavdlf leqrgisirt lldeqdwipv vprsritild evrmeqdlel
      241 vftvenvfkg ltydarldwy vqdqdgrrhv avgrithgya lienrrdwrl vefdermlsa
      301 lsappagaga vrgrggmage prg
//
LOCUS       WP_357557068             157 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557068
VERSION     WP_357557068.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=17509
     Region          10..149
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msnpaaeplq plnpdeealv ralgqvmhvl praidtdmvg dhqlplteyt almnlsevpg
       61 rrmrmnelas achlslsgmt rtiirletqg lvrrerceed argwnavltd sgfarltesw
      121 pshlaavrrr flqhfegfdl dqlarafqra gtaettd
//
LOCUS       WP_357557073             338 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557073
VERSION     WP_357557073.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 338)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..338
                     /product="phosphotransferase 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=36871
     Region          9..282
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtgssptqra ltrddvahlv rasfgphtrv rdagplaggg yatvwwarld ddrrvvlkla
       61 ppagtpllry erglcaaear yfrlvaehap qvpvppvlrh gadpaygewl vtallpgrsl
      121 sdlaadgvav ddgparydlg valaavhrvt gdrfgydgdr aggptwpvaf tamldallad
      181 atdwdvrlpv tpgrlhtlvg rhaevldevd rpallhfdcw dgnvlaapds qgrfrlrglv
      241 dgerflygdp lldlvspllf rriedepehp llrgyrdaag tplvldasar rrlglyrlhl
      301 yllmtvemps rgmtpsshpq rharlatlld aeldalar
//
LOCUS       WP_357557095             178 aa            linear   BCT 28-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357557095
VERSION     WP_357557095.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 178)
  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 178)
  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 178)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..178
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..178
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19602
     Region          6..178
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mgrraiifhg tggnpdvcwy rwlagrlaar gyavevphlp dlnvepiatf lpkvldahrf
       61 dedtvlvghs ggaalllall ehvevtvaqa ilvagyctpp ntseepvlqq sydwaairah
      121 vrdisfinsr kdpygcddsq gramfdrlgg tqivrddghf gdydqpydqf dlldrlia
//
LOCUS       WP_357557098             190 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557098
VERSION     WP_357557098.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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 190)
  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 190)
  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..190
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..190
                     /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=21340
     Region          7..177
                     /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 mfalpltedv elrpldpwra eeflahldra rehirpwvsp sfvatdlpsa ravlqryadr
       61 wasdtggiwg lwwrgtlvgg vmfvsfdvtr gvcevgcwve paaqgrgiva pairrivdwa
      121 vrergiqrve wrttadnmrs ralarrlglr ldgtlrqvsp gphgridlev wsvladewpa
      181 ahspstgdre
//
LOCUS       WP_357557128             251 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557128
VERSION     WP_357557128.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 251)
  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 251)
  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..251
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..251
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=27202
     Region          25..210
                     /region_name="TerY"
                     /note="Uncharacterized conserved protein YegL, contains
                     vWA domain of TerY type [Function unknown]; COG4245"
                     /db_xref="CDD:443387"
ORIGIN      
        1 mnpfalfeed tdgpdevafi tdthrrrfva llidtswsma atqsngvrai dalneelarw
       61 lpavraegrg slrdveflvv tfgaggvsvv sgngtpsaed dgafvpaarl elptlvagga
      121 tpmvaavdla ltlveqrrqh vqtvhaqqtg gprlilvsdg tptdeegnpt ddwqplarrl
      181 eqwrstrrlq lfafgvpgvd devmralatp sgyfplddld lrklldlilv atsdhvdfer
      241 vrsqvygadl p
//
LOCUS       WP_357557164             900 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357557164
VERSION     WP_357557164.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 20189366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=92951
     Region          <50..727
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          711..888
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          835..888
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mprprtarpg viprrrmivg rtaqldalda araaaatggr falvrgpags grtslldaaa
       61 gawrtagvvv lrvapaapgd taagfaalln avrdkyella dpplagplsa lgalcdepag
      121 ahagrgiala qqaaaafali grraptvlia ddagpalapa laaavragcl vvaagtpgdg
      181 rlgtladvvv dlpplsadav rgmlarryav plddavpsal stalgplagh pgtvleiahe
      241 ltragrlavv rghlclldph apialptdhs llaalrargp vavrlatmaa vtrfgiddlp
      301 lfadatrgrl sdygwmidel iddgllvagp qgeivpqspa ltarlitdag pdavarlhra
      361 caaamfrraa sgrpadgaal adqvtsagia lpvdrrtavt laatadentd sapdraahwl
      421 raalwhsggg ragddilarl lrllvrtgqv arlgevvdta ihrghgassr haadlvaaaa
      481 lvavhtgepv patvrsalrg apaapatvvf adwwrtgvpp apsmppaaha dtgsllhpte
      541 lgvladavgh gladagpate elllagetgd laallelvlg phrygvpkdg llsayhrlht
      601 cqadgdlsgv lsaareldlt gaeaplprcl arlwaaealg llgrateaps wlrsvpddpp
      661 yaalrwwagn gpageaqtaq eagrrlgdgr rayeshlhhg srigvehllv raaglaarfg
      721 lgeqmawlta vvdadaaepr rrlssqttll iqalcrgden aavrgvdlvr aggnrlalay
      781 aclalgrvae dprpwlveaq avaktmtsgw lrsavaavmr erdvrqprtr tprtgfspve
      841 ariielighg rtnrqiaaqv risektvenh ltrlfartgc rsrvelaavs lttdilgpas
//
LOCUS       WP_357557175             434 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357557175
VERSION     WP_357557175.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  AUTHORS   ter Beek,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..434
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..434
                     /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=45815
     Region          1..364
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkraipavis aataltlvla gcgggdepvd pnapvtitla gwslsstpef ktladgfkat
       61 hpnvtvelke yapgndydtq mitdlaagta pdvyvmknlk nfytyqsggq lldvsdaasg
      121 lgsapglasy qvdgkayavp yrqdswvlfy nkdlfakakv tppdgswtwd dytdaakrlh
      181 tglkgagsna tgayqhtfqs tvqgfalaqt pnadllsgnf gylkpyyers ldlqaagaqp
      241 tfgtaktnkl tyqaqfgkqq samllmgtwy vatllnqrks gdadkfqwgi apapqfdkst
      301 tgtsatpvtf gdptglginp kisksktaaa kdflkyaagp eagkalagig itpaqvtdav
      361 tatlfgldgv pqdelskfay skhtikpenp vskhtaglqn llnethsail sdskgvdael
      421 skaqtrakne vlnq
//
LOCUS       WP_357557181             590 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557181
VERSION     WP_357557181.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 590)
  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 590)
  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..590
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..590
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=63796
     Region          45..353
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          308..583
                     /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 mpptatrkrq wlpytaavta glvviagafv ivrqrdadct ttlevnsste kaallvdlae
       61 rynrsdrsid ggrcaqvhvs alnsgkatea laagwantgl pqpqvwlpts slwtgqlrll
      121 dqaagrepqt paqypsians plviampqpk aelirqrgal gwgeilglsg rdgwagfgkp
      181 ewgrftfgkd npnlstsgla atiatyyaav qrssdltrsd lanpavtqfv rrieanvshy
      241 sddsvdllrs laeadltgdp gstgdmsavv lqeelvdlyn tgalsprqeg qergrrpnvp
      301 lvavhpkegt fnldhpfvvl psadgrqraa aadfrkflte ddqqksfarl gfrdhegras
      361 aellasvgae ptgglryfkp pdpqvigaml dgwrtlrkka nilialdtsg smeakvgttg
      421 trfqvasaaa gkglallnse drvglwsfss eipsrpktpy rrevplgefd ekqinskiag
      481 lhvegataly atvraahrel rdrydpqrin aivvltdgkn eyskdndlar llddvaldpq
      541 rpvkvfciaf drdsdfatld riakassgka fdatdpakid eafvklvssf
//
LOCUS       WP_357557284             304 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357557284
VERSION     WP_357557284.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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..304
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..304
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33156
     Region          1..244
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 maqtltivtv lyrssdmlae tlptwvraae glpvtfifad nwpedecakv iadalddery
       61 eylpdssnpg faagcnrava avrtshvlll npdvwlpeda lvrlfasiaa dpqspiavgl
      121 amhggefvgi dlhpvslfid raatvprgpl gpsggaavfp talfhrfggf yehlfawged
      181 adlafrmyae glrtrrldfm lphagghsve gdnklqgfra fllarnrllv aartftwplm
      241 lvaipvlala hlalaarrar qgllrpflrg vgrglvegpa arrqwkgrrf gfaslisylr
      301 vrsa
//
LOCUS       WP_357557382             143 aa            linear   BCT 28-DEC-2024
DEFINITION  cold-shock protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557382
VERSION     WP_357557382.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 143)
  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 143)
  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..143
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..143
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15568
     Region          5..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mwaagkiirf detrgygfia pskggedifv handfgelrh lvhpgmrvey eveagdrglk
       61 vaslrvvdpv gvlrpervpd aaptrtgqtg dddgmcdvls preftyevte lligrvptlt
      121 aaqvssirqa lvdharshgw ves
//
LOCUS       WP_357557478             570 aa            linear   BCT 28-DEC-2024
DEFINITION  amylo-alpha-1,6-glucosidase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557478
VERSION     WP_357557478.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..570
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..570
                     /product="amylo-alpha-1,6-glucosidase"
                     /calculated_mol_wt=62861
     Region          215..559
                     /region_name="GDB1"
                     /note="Glycogen debranching enzyme (alpha-1,6-glucosidase)
                     [Carbohydrate transport and metabolism]; COG3408"
                     /db_xref="CDD:442634"
ORIGIN      
        1 mtvvpsgpef pvqdipfsyr gswfnispvv aektyaddlh lvshqtglha vlrlspavad
       61 ttvvatpall twrngtdrie avydgpdtlr irgrrlglrv aaaaatltpf sgtylyhdpv
      121 dgshvftsye tgrryritvl sgalertdgv ealgtadrsv dlpgdqpwei aieeyatarr
      181 pyvgsvtfdq lcrdraaeft afvdavapwr gaetpaaela ayvlwsatvg pagfvtrpav
      241 lmskhwmdkv wswdhcfnai alaagepela whqfqlpfdh qdeagalpds vthsevlhny
      301 vkppihgwal hhlrrrlpqp ldraalaqty drlarwtrfw ldarrapgqe lphyqhgnds
      361 gwdnattfdg nrvlqtadla gflvsqlrcl aalatelgep adtwsreadr vhgamlrdlw
      421 dgerfaarnp htgqrrtsrs lldlmpvalg adlpapvava largvethlt thglatepvd
      481 sahyladgyw rgpiwapstv lvedglrrag qtrvadeisr rflalceksg faenfdaetg
      541 aglrdraytw tassylilaa gqeerrvtrg
//
LOCUS       WP_357557492             314 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357557492
VERSION     WP_357557492.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 314)
  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 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   3  (residues 1 to 314)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..314
                     /product="GlxA 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=33253
     Region          2..310
                     /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 mydgvtlldv agpaevfkea nrfgadyriv llsptgadvt sslgvrlavd gavssepald
       61 tllvagsdhy psahvpaela daarlpaaaa grvasictga fvlaaagvld gkratthwqv
      121 ahelaarcpt crvepdaiyv rdgttytsag vtagidlala lveedhgpdl trdvaralvv
      181 ymqraggqsq fsaplqgppp rspalrritd vvtadpradh slgalakhln vstrqltrlf
      241 hdelsttpar yvenirfdla ramldqghta tqaatlagfp syesmrrvfa rklslspaay
      301 qrrfstarra revg
//
LOCUS       WP_357557515             473 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357557515
VERSION     WP_357557515.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 473)
  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 473)
  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 473)
  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 473)
  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..473
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..473
                     /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=49315
     Region          3..471
                     /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 mttteydvvv igagpvgenv adrvvrgglt aaiverelvg gecsywacmp tkallrsasl
       61 mrtarqlpgv retvtkdldv aavlarrdsf ashwqddgqv swlasagial hrgqgrirsa
      121 rvvdvtgadg vvtrltarha vvvatgssal lpdvpglrea apwssreaas agsvprrlai
      181 igggvvaaem atafaalgss vtvlardgvl psvepfagel vkeslrdagv avlvgaqals
      241 vrrddsgtvh irtadgdlle adevlvaigr tpntqdigld svglvpgawl tvddtlrvvg
      301 ggewlyaage vnrrvllthq gkyqaravgd vivarakgak vddgrwgrha ataderavpq
      361 vvftdpeias vgltaasata aglrirvvdy dlgavagasl hldgyrghar mvvdedrkvi
      421 vgvtlagpdv aelihaatva ivgevpldrl whavpaypti sevwlrllea ygr
//
LOCUS       WP_357557551             309 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557551
VERSION     WP_357557551.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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 309)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..309
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..309
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33160
     Region          5..262
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mrevdmtava ddglplvgtl tlpvgpgphp avlllhgsgr ldrdsntarl rmelgpplak
       61 rladagiatm rydrrgvgat ggdwlatgfa agrhdaaavl ralavrpdir adavavlghs
      121 egavhamslg arpevaavvl lagfarpged alrwqaamia rdlpapvrpl lpilralanr
      181 qlarikttst dvvrilgrpt narwlrelld hdprsdlani kapvlaitgd kdiqvdpadl
      241 deirrlvpgd ttvhripdlt hvlrrdlgrp svrsyrrllr qpvdpdllaq vagwlarrlh
      301 gtpetvrag
//
LOCUS       WP_357557556             174 aa            linear   BCT 28-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357557556
VERSION     WP_357557556.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 174)
  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 174)
  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 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 10007544
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..174
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18858
     Region          5..173
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 mtrhllvpgr giaraehwlr rwaethpeyr wapeppgppl ilrdrvaalh tavgesdepa
       61 vliahsagci tvalwaaths gpvraamlvt ppritgaepd dpsdipwvvp rarlpfrtiv
      121 vasrsdpytt faqfeqfaed wgaelvdagd vghldtasgf gpwpegerlv selg
//
LOCUS       WP_357557598             214 aa            linear   BCT 28-DEC-2024
DEFINITION  FMN-dependent NADH-azoreductase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557598
VERSION     WP_357557598.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 214)
  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..214
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..214
                     /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=23044
     Region          1..206
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mhllhidssi rgdwsvsrrl taravatwra ahpdgtvtyr dlgadplphl daagglarmt
       61 padqhtpaqr eswelserlv devkqadvvl lglplynyga pssvkswvdh livpglafdp
      121 ttqegllggr efvvlatrgg gygegtprng wdhaepwlph glsmtgmqpr fisaeltlap
      181 svpamaelvp lheaslaaae keidnlwtpa saqr
//
LOCUS       WP_357557719             403 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557719
VERSION     WP_357557719.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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 403)
  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 403)
  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 403)
  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 403)
  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..403
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..403
                     /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=43058
     Region          92..394
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msfedtmlrr trarvsllvg ltmtallalg aaisyaallr yqheqierel nygavhgtia
       61 gppgcswiil ydgnrtdsgr nppppgfplq saidavaldh qvrsdkvdrn gttyyvrtqp
      121 rgtgvvqavf darfqlsdrr hllaafllaa vvglaaavft givvgrrava plaealgrqr
      181 rfvadashel rtpiaqvhtr aqilarraga eradydrlie ttrrlgeivd elllsarlaa
      241 tpadrhpsep vnlallaaqa vdceadraae qgvhlhlsvp dtpvlvpgia salrrmvgel
      301 lanalthtpt ggridvalrt srrgadlvvk dsgtgfdpad aehlfdrfhr gagakdrrfg
      361 lglallrevv tshggtistd srpgagatft vrlptippra aag
//
LOCUS       WP_357557026             141 aa            linear   BCT 28-DEC-2024
DEFINITION  SCP2 sterol-binding domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357557026
VERSION     WP_357557026.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Burgardt,N.I., Gianotti,A.R., Ferreyra,R.G. and Ermacora,M.R.
  TITLE     A structural appraisal of sterol carrier protein 2
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (5), 565-577 (2017)
   PUBMED   28284963
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Dyer,D.H., Wessely,V., Forest,K.T. and Lan,Q.
  TITLE     Three-dimensional structure/function analysis of SCP-2-like2
            reveals differences among SCP-2 family members
  JOURNAL   J Lipid Res 49 (3), 644-653 (2008)
   PUBMED   18084051
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Bun-ya,M., Muro,Y., Niki,T., Kondo,J. and Kamiryo,T.
  TITLE     New aspects of sterol carrier protein 2 (nonspecific lipid-transfer
            protein) in fusion proteins and in peroxisomes
  JOURNAL   Cell Biochem Biophys 32 Spring, 107-116 (2000)
   PUBMED   11330036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007129
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..141
                     /product="SCP2 sterol-binding domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=15677
     Region          9..125
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
ORIGIN      
        1 mpvfpsakwl dgyverinss eefedaartf eadiafvfea epengvpadi wclatfadgk
       61 cqqadydveq eraagatfvi rapysrwkdv iesrldpieg mldgdlvvtg hlptllryvr
      121 atdelvnlaa kvsssfvder r
//
LOCUS       WP_357557854             294 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557854
VERSION     WP_357557854.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   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 294)
  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..294
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..294
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31634
     Region          13..294
                     /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 mgsthhdvsa lapgahtfll dgvrqvyhva gsgpvcvahs ggpgiewayl rtpsleehft
       61 mvyvepvgtg asgrlddpad yrldtyvrfl davvehlgep rvyllghshg gfviqryala
      121 hpdrvaglal ydtspvtgae fwaeamaela aypqrhpdrp eaaavpaafg qigaatddes
      181 latalraalp vyfadfwgrq defaplqaav rvsfapataq dpapfdvren laeiiapavv
      241 ivgaydficp prraeelhag lkdsrlvlle hsghfahieq pvefteavve lltr
//
LOCUS       WP_357557804             367 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557804
VERSION     WP_357557804.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   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 367)
  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..367
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..367
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=39485
     Region          72..361
                     /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 msyriprprt avgrvagivg aavgvaaagl aagvatertl vrrlkadpad ryaheafgeq
       61 rydeafrlal pdgtdihvev veptrpvpgq ptvvlvhgfc ldmgtfhfqr qmlaargdyr
      121 ivaydqpghg rsgrletgey dltvlgrtlr qvidrtapdg plvlvghsmg gmtimafael
      181 fpelfgdrvv gtvlmatsgg liaetklvap allgrvggpv lymvsnatry ggpvidkark
      241 stsnvawllt rkygfgtrkp spalvsyvet mnsrtsadtv trylrtlath srfpalaala
      301 atpvlvvvgd kdmitpvvhs eeivrrlpha efvkikdsgh vvmlehadev naalarfles
      361 lgkpeel
//
LOCUS       WP_357557866             397 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557866
VERSION     WP_357557866.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 397)
  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 397)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 397)
  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..397
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..397
                     /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=41249
     Region          170..394
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstpdlrhww vrlaqaagll algllalfdl rfgapgslag lllllvrmgl avatvplwlp
       61 vhrlgsrllp laalglavvs lavtagvlll sngiylfsgs wglaesagli gvvfvvtrwg
      121 asrlapwaav avglavaalp lragtenllv ifgllqvlaa agaagvglyl rimaagrera
      181 ialvraeqra efardlhdfi ahhvtgivvq aqgarfvaeq dpqrvivale qieragaetm
      241 asmrrmvgil rnpdappdap laplagvtel pplvagftgt antpahlhvd gdlhglpvev
      301 stsayrvvme gltntrqhap darsvhvavr rtpdwllvrv addgasprta parghgfgli
      361 gltervralg gtitagpgva ggwvldaafp lrgavar
//
LOCUS       WP_357557928             119 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357557928
VERSION     WP_357557928.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..119
                     /product="YybH family protein"
                     /calculated_mol_wt=13227
     Region          3..119
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mseaqilrtv ldlwksavda hepdrvascf tddaifqglr pytvgragva ayyaaqplgl
       61 tasydireir rladdvilgy levefgftdr pplpahlgvl lrrvddnwqi ghyqisqlp
//
LOCUS       WP_357558028             291 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558028
VERSION     WP_357558028.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  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 291)
  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 291)
  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 291)
  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..291
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..291
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31052
     Region          40..258
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 marsrkvtvs tdaaghttgw aetdlspava papdptaaaf fdvdntmmqg asiywfargl
       61 asrnyfttad larfawqqlr frllarehag dmsvakeaal afvegwrvdd verlaeeifd
      121 emmapriwag thqlaqrhld vgqrvwlvsa apveigrvia trlgltgaig tvaevvdgay
      181 tgrlvgelmh gpakaeavtq lavvegldla rcaaysdsan dlpllsavgr avavnpdgtl
      241 lrqarqhgwe vrdfrtgrra vkiavpstaa aglvvgavta glalqrrrra g
//
LOCUS       WP_357558062             412 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558062
VERSION     WP_357558062.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 412)
  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..412
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..412
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43549
     Region          1..77
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtnpttgdnl arlrraaklt qeqlaeraal svetvrkleq nkpgsarlet lhafaralgv
       61 pttaligdas gaaardephh rplslaeirr avapvhgltg aalaapvgdp ppadtlrtrl
      121 ravdrayqan dyataltalp pllldvraav slaadddepa afallartlh ltgnlliqlr
      181 agdlaqtalt daltaarrsg dqvvaatviq glcwlltrqg rlaeaaelgv stadqveprf
      241 sratpgelaa wgwllmgaaa ahardnrpdd aaelvnaaaa aavrigerdp ggehlmmvgg
      301 fnagrvqmar veaaavagdp grvltlaeav ppgptpvgss wqrhrldvaw ahatrrqfve
      361 seailidlgr lapawlrhqr yardivqtid egrrramtdd laaladlvgy kn
//
LOCUS       WP_357558072             222 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558072
VERSION     WP_357558072.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=23788
     Region          <11..207
                     /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 msarradsgg ivviglgrfg chlagsltrm nrevlaidhd paqvqrwsaq ldrvvqadst
       61 eegalrqlgi tgfgqavvai gasveasvlt vlalvelglp qiwaratsqk hakilssvga
      121 hhvifpeaet gdrvahlivs rllnfiefdd dfaiatvrvp etlvgrtlrd lrpeehygir
      181 vvgaklpger frytsddtal paggvliveg gidqvqrfag qr
//
LOCUS       WP_357558080             248 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558080
VERSION     WP_357558080.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  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 248)
  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 248)
  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 248)
  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..248
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..248
                     /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=24793
     Region          4..246
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mgsriavvsg ggtgigaava gslardgydv livgrradvv taaagrisse cgrpdsvtav
       61 aadltepeqv drvlaavdgr pvdvvvnnag sylagdtgtl agiaahwran ldanvltavl
      121 ltealrpvlr rpggrvilvs sisaqrgggg pysagkaalh gwaydlaaql gpdqitvnvv
      181 spgyvaetdf fgdrmtaegh akrvaatlvg ragvpddiae avrylaspaa gyvtgqvlgv
      241 nggsvlgr
//
LOCUS       WP_357558102             448 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558102
VERSION     WP_357558102.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 448)
  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 448)
  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..448
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..448
                     /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=48333
     Region          1..445
                     /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 mtdiprravs rtaklaalpl gfagrtvlgm gkrvtglasd visaeiqqrt aeqlfsvlgq
       61 lkggamkfgq alsvfeaalp eeiaapyrqa ltklqeaapp lpvasvhkvl aeqlgpdwrd
      121 lfvefndtpa aaasigqvhr arwrepgvde sgapngrdva vkiqypgage allsdlkqls
      181 rlggmfraiq pgldvkpllv elreriteel dyeleaesqr afaeayaddp eiyipkvvna
      241 aprvlvtewv tgtpladiir egteeerdea grlmatlhls apqragllha dphpgnfrll
      301 pdgrlgvidf gavarmpegt pepigriaal alrgdadevv aglrsegfig saeeidaegv
      361 ldfirpmlep iaadgfrftr awlrgeagrl asprsptyql srqlnlppsy llihrvtlgs
      421 igvlcqleak apyrgilerw lpgfapva
//
LOCUS       WP_357558142             204 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558142
VERSION     WP_357558142.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..204
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22401
     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(8..12,110..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 madtvlfdlf gviarqqaps gqellaatag vsaptfwety walripydrg eltgseywrq
       61 vaaaldttfd dhqiacliaa diaswsavdn dmvalveqta asgrrialls nipeelavhy
      121 eehhrwlkyf davafscrtg hakpepdayr wccralalap grilfvddsa eniqaaeaig
      181 mhahlfvgpt qarqaiaeld tmpr
//
LOCUS       WP_357558152             173 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558152
VERSION     WP_357558152.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 173)
  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..173
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..173
                     /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=19083
     Region          2..142
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 melfrrhyga vmryaarrvg pdrapdvvse aflvawrrls evpvteplpw lyattrhlig
       61 neirgrsrqa rlasrlgevg emvspdhadv vvdqvrvrra laelpegdqe alrlaawegl
      121 dasaaatvmg csrtaykvrl yrarrrlaaa leptrnrtst daalsplahe ggs
//
LOCUS       WP_357558155             127 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357558155
VERSION     WP_357558155.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..127
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14025
     Region          13..113
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mshtdgdcvd fvadcrlrmg tdlfthvwdp vilaalaagp qrrralraki ggisdkvlte
       61 alhrlvtngl ierrsyaesp prvdyaltpl grtfadgpmr alaewvtrhg delfeaqeqm
      121 rlaqpcp
//
LOCUS       WP_357558228             158 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558228
VERSION     WP_357558228.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..158
                     /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=16914
     Region          1..139
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtsctpadgp pdllfllswa shalqtehaa glaelgispr ahyvlaqaht geltqreige
       61 rcgvdkttmv vtldqlerag laerrpaptd rrarlvvvtp ageqvlqrar qvvrriqddl
      121 latlpaqdre aflrallalv ngplahtspy apgarsgc
//
LOCUS       WP_357558241             264 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558241
VERSION     WP_357558241.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26741
     Region          16..261
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtdnthiads rpgglltgkv ilitgasrgi gaaagrlfaa egaavvlasr stsalgviva
       61 eiragggvad avaldladra siraavdrvd qlhgrldgaf nnggvvqrqv gplhttsded
      121 ieeqfavnfl ahwtamnaea almrrnggga ivntssigsr ranpvlpayg amkralnsit
      181 etaavtwapd girvngitpg gtltemmqew eatspgviea ssaatplgrm aeprevaeaa
      241 awllsdrasm vtgaivpvdg gaga
//
LOCUS       WP_357558269             319 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558269
VERSION     WP_357558269.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=34253
     Region          21..317
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mvetsvrllr lltllqvrre wsgaeladrl avttrtvrtd verlrvlgyq ieshpgvagg
       61 yrlgagsalp pllldddeav avavglraaa ggsvtgieet slralakleq slparlrhrv
      121 dalraatvsa agggptvdad titaistavh raerlrfdya ghdgtatvrd vepyrlvytg
      181 rrwyllgwdt dradwrtfra driqprvptg prfapreppg gdavahvlrg vgsaawphpa
      241 rvrlhasadq maqripstag lleaidertc llhtggeslg nlaafistle vdfdvldppe
      301 lhavvravaa rfgraaqvs
//
LOCUS       WP_357558313             508 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558313
VERSION     WP_357558313.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 508)
  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 508)
  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 508)
  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 508)
  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..508
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..508
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=55351
     Region          47..490
                     /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 mparrpvvrv ligvlvgvll lgaglavgaw tltrptdtvg avsfvrplav pplaesrldd
       61 rgqrvfdlva qegrrdfrgd grttatagfn gaflgptlra rrgeqvrvnv antlgqetnv
      121 hwhgmhlpar mdggphqlvr pgatwsptwr vdqpaatlwy hphphgated hvyrglagmf
      181 ilddereaal plprtygvdd vpvivqdrsf sgsgqfdktr nafagvgvlg dtllvngtvg
      241 pyldvrtqrv rlrllnasta rtydfglsdn rqfaligtdg gllartarlt rvrlspgera
      301 eivvdvrpge rvslrstppd lgigglsrrs aggadrfdvl qlraadtlap appvpddlvp
      361 varldagaav ttrrlelrgr gingqsmrmd ridfavtrds tevwevlnad gtphnfhvhd
      421 vqfqlltvdg aapppeltgw kdtiflpphr pmrivlrftd hsdpnlpymy hchllwheda
      481 gmmgqfvvvd pgqapgrppt htghgkhd
//
LOCUS       WP_357558377             244 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558377
VERSION     WP_357558377.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 244)
  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..244
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..244
                     /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=26493
     Region          14..>71
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          44..219
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 msddrwvtpr vllavdlvil tlrravlqvl liergvephr galalpggfi ghdeeellaa
       61 ahrelaeetg fgadrphleq lgvygtpgrd prgrvisvay laiapalpep vagtdassay
      121 wrpvdeslag dvrlafdhrr iladgverar eklertalat afcgptftia elrtvyeavw
      181 gapldprnfy rkvrsvdgfi vpvqatrrtd ggrpaqlfrp gphttlhppm vrpsgpgpad
      241 keta
//
LOCUS       WP_357558456             272 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558456
VERSION     WP_357558456.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=27918
     Region          100..271
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <211..271
                     /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 mrtvlvcvrt plaaqhltsa aarlglsaiv rtavsdpevm lrlaerpadv vladtaltrp
       61 dsagfvrrvl arapqaavll lgteeseaaa atisagargl iqnvdhdlts avakallllt
      121 apgrasrqri tdpardaaav ggsgrsgptp rgsaepgwtg tpgegqagvp svpvqrgdde
      181 aeaatgesta dqtdparpga ntrptrasig lterelqvll gmaegksnae igrelfvsed
      241 tvktharrlf rklgardrah avaagfragl va
//
LOCUS       WP_357558460             275 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase, partial [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558460
VERSION     WP_357558460.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..>275
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
     Region          8..271
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mdtrhdlpvs vlglgamgsa ltaalaragc tptvwnrsad rasalvaqga ipastaaeav
       61 ragqlvvvcl ldhasvhevl dplagdlagr tlvnvttttp eqarelaawa aasgvtyldg
      121 gimavpamig qpgssilysg saaafdthrp lldrwgtsty fgadpglasl ydlallagmy
      181 vmfagffhgv amvapsgvsa tefatlaapw lsamtgafpr faavvdggdy tvpgqqslef
      241 sdlgqagggn vdsarilagv davvadavqt mraet
//
LOCUS       WP_357558509             470 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558509
VERSION     WP_357558509.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 470)
  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 470)
  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 470)
  AUTHORS   ter Beek,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..470
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..470
                     /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=51501
     Region          1..400
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkrngrvart alavvtvlfa gvavngqaaa ptdeltvlgp wtdeeevafr avlekfrkss
       61 giharyqghr dvsqvlqvai erdrppdvav lprvndlqry vnagqlvple gpittdpgad
      121 pqlvklapka gqagdtlpya vaitthlksv vwyapteldk fgqsppstwg elvaltqrri
      181 gdkqvrwclg msaqpvsgwp gtdwiedill hqsgedsyeq wtrgdlhwds pqvkgawetw
      241 gallgvsseq taraslyttf qtaanglfpg kvkevvippr chlnhqgsfv vrkypqpkps
      301 sqtdadppft ffstppigpk atqslhevsd dvavmfrhsr tsrdakdsnd terarelmsy
      361 lastqaqtaw reatsgvafs rrgdapapqd rvlaavaerl rtgtlcwdas dlmpaamata
      421 ferailvyle aperlgsllg eleklrdkvv pkaewldltc vppdergser
//
LOCUS       WP_357558550             871 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558550
VERSION     WP_357558550.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 871)
  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..871
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..871
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=94089
     Region          2..871
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          612..640
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          645..681
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          695..720
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(696..697,700..701,703,731,736..737,740..741,
                     743..744,772,775..776,779..780,783)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          729..760
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          771..795
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mefvgalrql rlwsgltyrq laakaaasgd alpfgtiasv lsrtslprre fvvtfaracg
       61 lddasiarwv rqrnalavna tqvvgggard egadlataep awpspamlpp diadftgraa
      121 evaalthrlt aerndtrasa alpvttiagm ggvgktalat hvahlvraay pdgqlwanlt
      181 nvdaspvdpa evlarflral gmpyraipad paeraeayrt rtanrrilvv ldnavsegqv
      241 rsllpgaapc avlitsrarm taiegsrrid ldvlsateav eflarladde rvvgeptaaa
      301 dlvklcgylp lavriagarl aarpawqlah lveqlddeqr rldwlvtgdl tvraslaisy
      361 rgltpeaqrl frllglfdvp dfsatlaaal lgcppersie haealvdaql lvvdgldvag
      421 qtryrfhdlt rlfaarcael evepderaqa vqrglggwla larrmarwip gpcyapisgg
      481 aphtaldwad dyaervaaad wfdaecaalq agvrqacrlg lddlafdlag clekyfdlrg
      541 rytewtslnt eamavcriag nrlgeavmlr glldvstwit ddrdgdamar ssiqarnlle
      601 mftalghdag asdaavmysw alsaggaype atamatralr laersdhlgg qarsnlalam
      661 ayyeqqhvdl aighaltsle naralgnmrw vatglqylgi ayrqlgdhet sermldesla
      721 israhrdhyp evltvlalar lylergdgta retaetalll srryhmrhhl aeayailgei
      781 elrdgrpaha irhleasvai wrtrgwhsfq aaslttlgka ylhvdayaah qafvdaqaly
      841 aqlgntdkva elglladsaa dpsghadrsr a
//
LOCUS       WP_357558516             225 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558516
VERSION     WP_357558516.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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 225)
  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 225)
  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..225
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..225
                     /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=23441
     Region          4..223
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 msgiaifgag gragravtae ararghrvta vvrnpattgd igtdgvtvvr gdvtdprsts
       61 tisrghdavv stvspasgpe alaalgrldd qfyvktvdal lhglteagvg rlvliglfan
      121 lrdehgrlil ddpaafpshl rpfalshtag ldrlraadta vdwlmltppa mldaagprlg
      181 ryqlggdsvp psgrsttlsy adlavavide ietprhhrtr vsvfd
//
LOCUS       WP_357558512             763 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558512
VERSION     WP_357558512.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 763)
  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 763)
  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 763)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   5  (residues 1 to 763)
  AUTHORS   Kannan,N., Taylor,S.S., Zhai,Y., Venter,J.C. and Manning,G.
  TITLE     Structural and functional diversity of the microbial kinome
  JOURNAL   PLoS Biol 5 (3), e17 (2007)
   PUBMED   17355172
REFERENCE   6  (residues 1 to 763)
  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 15505478
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..763
                     /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:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=82399
     Region          7..128
                     /region_name="PknG_rubred"
                     /note="Protein kinase G rubredoxin domain; pfam16919"
                     /db_xref="CDD:435653"
     Region          129..378
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(129,153..154,182,187,192..195,212)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(136..137,139..142,144,158,160,190,211..214,218,220,
                     264,266,268..269,271,280..281,284,305..308)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(136..137,139..142,144,158,160,190,211..214,218,266,
                     268..269,271,280..281)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(140,218,220,264,266,268,284,305..308)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(280..288,297,302..308)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          439..761
                     /region_name="PknG_TPR"
                     /note="Protein kinase G tetratricopeptide repeat;
                     pfam16918"
                     /db_xref="CDD:435652"
     Region          525..548
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          588..615
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 mtpqcdrpgc tgtvdetgfc dvcglaplpt dtasdtdapa aapsrpaard twtvaglvsl
       61 pvltfpsdtv tthlrrvpee frfcpnghqv grsrgarpgr dkgfcpycpt rtpfnfavsl
      121 rpgdlvadry rvvrcvthgg qgllylaqdt hkdqvnvalk gvlhaadeas ldvavkerkf
      181 lnaldhpniv rstdfatvdd pdagptsyiv meyldgmslr rlqgaakdpr qpdvslpidh
      241 ilaygheila alhylhrrgl lytdmkpdnv mrtadrikvi dlggvrkads grkrvvhsdd
      301 fsvgdtefqt lgptvrsdlf avgrtleely ryrtpgpdtp gagpdalgie sfrrlvarav
      361 rsdwdrrfas atemseqllg vlreilagqp drrqpepisl fqpsarllda glglavplrt
      421 widggdsial ddglpasvdv alglavprpd psdpavdvlr tvdasdpqal lrelamveqt
      481 sveielsrcr ahlaladpgl aaaaltaaet vpdiqpdvdw riawhrglla laadrvdeag
      541 qrfdevysdi pgevapklal gycaeragdh vraaryyaav wqrdpfqasa afglarlhla
      601 atdrtgavav ldevpalsrh hdaarvaavr vlssrlpggp ptavelnqav hrlaaltldg
      661 eardrlttai remaldlars gdaakltggp vlgapptqra irellemsyr algqqaqhad
      721 lpapviarlg rtrragppld aarraahdll vdranavrpr trw
//
LOCUS       WP_357558557             994 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558557
VERSION     WP_357558557.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13307259
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..994
                     /product="glycoside hydrolase family 3 protein"
                     /calculated_mol_wt=106913
     Region          27..854
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
     Region          873..985
                     /region_name="CBM6_xylanase-like"
                     /note="Carbohydrate Binding Module 6 (CBM6); many are
                     appended to glycoside hydrolase (GH) family 11 and GH43
                     xylanase domains; cd04084"
                     /db_xref="CDD:271150"
     Site            order(890,900..901,960)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:271150"
ORIGIN      
        1 mgykrlrrgi avlalvllal pavpgtalae ptypfrdphl pvnarvddll grltldekis
       61 wlhqyqpavp rlgiglfktg tealhgvaws tdidnngavv kargtsfpqp vgmastwntd
      121 linrvgsavg deargyhaqn prvwglnlwa pvvnllrdpr wgrneegyse dptltaaist
      181 aygsgmtggd pnhlksaptl khylaynnei rrdvtssnvp arvlneyera afkpalaada
      241 atgvmaaynl ingrpatvdp dlatvvrgwt dqplmnvtda wapnnlvasq gyyatqaean
      301 aaiikaglns fitddtnaqp tvtaikqala tgllteadid arireilnvr frlgefdpgg
      361 gryggitpdv inspehqrla rqaageamvl lknsrqalpl dpartrkvav lgpladtlyt
      421 dwyggdlpye vtafdgirer lgnsasvnal dgadrvalkd patgryvtat gttdadpvaa
      481 tgttaspeaq fdvvdwgqdv vtlrnaangr ylgynwgpfv trdaqpngwy vqqqfklepq
      541 ddgsvvlryv gyetkeswfa pekyvtvgdd galklgastp aaathfsrel issgidrava
      601 aakaadtavl vvgsnpfing reahdrtsta lstgqealvk avvranprtv lvlqtsypvt
      661 ttweqehvpa ivwtthagae tghavadvlf gdrnpsgrlt qtwyrsdgql ppdlleydii
      721 ssgqtylynt akplypfghg lsysrfrygq artgdrpvaa dgtitvsvdv tntgsragae
      781 vvqlythqrt srvktpnral kafqrvhlap gqtrtvtlrv pvadlahwdv trsrwvvess
      841 thdlmvgasa ddirartavr vrgetvpard lsrttraenf dryagvrlvd etkaqgtavg
      901 ataagqwisf agsalrpgah tftatvaras adagtiqvrl gsptgrllgt atvpstgddy
      961 ryvsvsaela raagthdvyl vfdsplrlad fsir
//
LOCUS       WP_357558605             953 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558605
VERSION     WP_357558605.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 953)
  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 953)
  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 953)
  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 953)
  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..953
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..953
                     /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=103885
     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          146..931
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          739..767
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          772..808
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          818..846
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(819,822..823,826..827,829,860,863..864,867..868,
                     870..871,900,903..904,907..908,911)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          858..888
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          899..927
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 melrvlgpve vwnrgvslqf arrqqrvllg ilaleanqlv tgdrlvdllw gerpprrara
       61 vlqtrlsevr aildlaeqpd pavllettgg gyllrvspeq vdaqlfkalv sdqrtrgsdd
      121 earsilrsal alwrgpvlgg wlpdegqadl trgldalrlt atedlfdvel rlgnhrdivd
      181 evvelagrhp trerlagqmm raltrsgrgp ealtsfdrwr rwlrdelgtd psaelqaihl
      241 avlrgvadqp dtdgsgtavv stqpphppdg qqrgspagfq lstprhlpad iadfsgrqpe
      301 lariekillr pgtgariavv sgpagvgkta fsihvahrla gsfpdgqlyv nlrgadsdrg
      361 ltpyevlgrf lralgvdglh lpatldertd lyrdlladrr llvlldnaaa ddqlsalipg
      421 gtscgvlvts rarlgailga qtvalavmda tdaalllsri agpgavldea satallsrca
      481 ylplairivg aklaakphwt vdrlvqlldd errrldrlsh ghldvrasla lsyqvlspaa
      541 rtllrrlgdi eiaevsdwla aalldttadr aqelleqlid aqlldfsghy pagqpryrlh
      601 dlvrlfgrer alseaspgel gaargrafga alsiierllh alyggrtltm rggtprwevd
      661 ellvgssatd llgwfdverp tivslvkraa rdglgetawd lacaasplfp mrrqyddwqh
      721 vldvawesal atndirgqaa isyrlgmvtv drqefdrade hfqrarrifd kmddpygvav
      781 vdaylamvsr frgqpgaalr ryssaltvlr dtdvggaafv lrgmgqahld lgdqegakah
      841 ldesialydt igsppmgrgq alfwqgmrll aagrhdqaap lfdhvltita vlgdrhgqaq
      901 alrglgicqh ragripqara tldealrlvr qptptivesf vrrtvrdlfg ddc
//
LOCUS       WP_357558645             268 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357558645
VERSION     WP_357558645.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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..268
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..268
                     /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=28585
     Region          30..260
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtsrvpvlls sssvfpepta aafqlaaalg ydgvevmvwt dvvsqdagal rglsahygvp
       61 vlsvhapcll vtqrvwspdp werlrraael aetleaptvv vhppfswqrd yarnfaegla
      121 tvadrfsglr favenmypvr magrqfvpyv pgwdptdtgy psytldlshc aashsdplem
      181 adrmgaglah vhlgdgtgeg rdehlvpgrg tqpcgellss lagrgftgav avevatrgak
      241 sravreadlr aalefarqhl tapspvda
//
LOCUS       WP_357558669             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558669
VERSION     WP_357558669.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   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 265)
  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..265
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..265
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27759
     Region          1..265
                     /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 mhkitvngas iaydeagtgs pvvllhagia drrmwrgqlp alaarhrviv pdlrgygdse
       61 lpptpfahhd dvaglldald lpraalvgcs fggsvaidta lahpdrvsal alfdtavsgn
      121 ewseeandlw dslvgevdpd dfvagaagev rfwvvgparr pedvdpella faqemdqral
      181 aaelalgave vgeltppaig rlgelripvl vtagaadvpd isrladriaa evpgavrmpd
      241 vpdaahllpl erpepvnaal ldfls
//
LOCUS       WP_357558767             148 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558767
VERSION     WP_357558767.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=16766
     Region          1..144
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msdrfvyhca lrwsdldayg hinnarfltl yeearvalmf aggrawgvgs fadgvvirrh
       61 evdylrpvdy algrataeaa ptvrielwve eirhawftva yelydgevla srarsvlvpf
      121 dltrqvprrl tdqerdflst yapqggla
//
LOCUS       WP_357558836             315 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357558836
VERSION     WP_357558836.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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 315)
  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 315)
  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 315)
  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..315
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..315
                     /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=33645
     Region          2..234
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilvvggsg ligahvvdvl rerghatttv artaqpgvdh lldlgsasie dlrpllaghd
       61 gvvyatrtde qrplpkpiyp qfrrdnvdpv vrlctaarle gltrgvvmgs yytyfdrlhp
      121 rwrlaerhty ircrveqare graaagpdlp vavlelpfvf gragdrlpnw agpldrwars
      181 rtplavptgg saavsarsva eiaadaleqa sgadipvade nltwddmigr iaeavgrrrr
      241 vgrlpagaak aafrlggalq algrkesgin lshladlllv dlfvepttgr sldsalretf
      301 pttaptgaat avdpg
//
LOCUS       WP_357558963             190 aa            linear   BCT 28-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357558963
VERSION     WP_357558963.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..190
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21533
     Region          8..181
                     /region_name="YdeN"
                     /note="Predicted esterase of the alpha/beta hydrolase fold
                     [General function prediction only]; COG3545"
                     /db_xref="CDD:442766"
ORIGIN      
        1 msdavrvvlv hgnagatidg iwfpylkrel elrghnvvaq tfpdpikgrm rywlpyltdv
       61 irpddrtviv ghssgaltal ryaesapllg tfvvaghhtd cgfelerrsg ffdrpwdwaa
      121 irrnqrfivq fhstddpwvp vevarelhrl tgsrltlmeg mghfgsydqk ldtfpellea
      181 vcqqletadr
//
LOCUS       WP_357558987             251 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357558987
VERSION     WP_357558987.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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..251
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..251
                     /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=28052
     Region          15..189
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mhadpgarlv eepafilsai rsgstllrci lnthsqicap helhlphtrv dtttwytela
       61 lrtagfpdee lnfllwdril hrlleaskks vlvektpgns lswrrlsqcw praryifllr
      121 dpadivrsal rvgpdpestv ipivldmidg vedarrelsg ltiryedlls dpvastkavc
      181 ayldvdwept mleygqadhg pfepgigdfg dairsgqvqp rpetttaqpv pdylgercar
      241 wgyapearda r
//
LOCUS       WP_357559016              80 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559016
VERSION     WP_357559016.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 80)
  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..80
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..80
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8810
     Region          12..78
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mperndgelr aqrlrfgqrv rdlrqarrls qeelaelagv hrtyvssler gqrnvglnni
       61 laiaaalgvp asalfteetp
//
LOCUS       WP_357559007             205 aa            linear   BCT 28-DEC-2024
DEFINITION  NuoI/complex I 23 kDa subunit family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559007
VERSION     WP_357559007.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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 205)
  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..205
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..205
                     /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=22179
     Region          19..170
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
ORIGIN      
        1 mvdmtdpseh gdppgatsar glpgaglvkg lavtlktmts rsttqqypdv apdlpprsrg
       61 vialseenct vcmlcarecp dwciyidshk eevvvpgaar prqrnvldkf didfslcmyc
      121 gicievcpfd alywspefey aeydikdllh dkdhlgqwma tvpappahdp ngepakeeta
      181 aarkaaaarp appavrpdad qdpts
//
LOCUS       WP_357559066             390 aa            linear   BCT 28-DEC-2024
DEFINITION  lactonase family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357559066
VERSION     WP_357559066.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..390
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..390
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40431
     Region          51..369
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mkrsvalaaa llaglssvgs npgtaladgg gpgyhddrkg gdnhhgdega vfvqtnkaeg
       61 ntikvydrde dgrltkagey etgglggfti gapldalasq gsliyhkgll favnagsntv
      121 tvfgvegtkl hklqviwsgg llpvsiaarg dlvyvlnagg egsvqgfelr kghlsrieda
      181 nrslglhngn ppafgtapaq vkidpdsefv lvstkgnnvm fsyeigrhge lardpavsda
      241 gntpfgftfd sedsllvtes ganavsrfel eddgtldqvg psvpngqqap cwiqrvgdyf
      301 fvanagssti ssyrvdddgk leivknvaad tnggsidmtt sdgflyvqna tagnvqgyev
      361 nddgslrlvt tveglpkfen gigmegiaas
//
LOCUS       WP_357559135             215 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357559135
VERSION     WP_357559135.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 215)
  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 215)
  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 215)
  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 215)
  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..215
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..215
                     /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=22124
     Region          3..215
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 msritviggt gyagsaivae aatrghqvts lsrsapttpv pnatyrhgda tdeatlsaav
       61 egadvvvaal aprgplaatf rdvyravarl adaagvplfv vggysslrpa pgadrfvadl
      121 sqvpaelhde iragaaliie dlpatpatld wvfvspalrf gawmpserlg ryrlgddvai
      181 apedggaisa adyalgfvdl iekgdhhraq vnlgn
//
LOCUS       WP_357559136             139 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357559136
VERSION     WP_357559136.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..139
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15396
     Region          14..117
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvttpgaesv lrgspyradc ptrhildrig drwtvlvvga lwdgsvrfse vrrrvegvsq
       61 kmltqtlrgl erdglvrrtv ypevpvrvey alteagrtlr gplraleews ithlgdvsaa
      121 qaaydranlp asdstdrdh
//
LOCUS       WP_357559317             240 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559317
VERSION     WP_357559317.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Rosinski,J.A. 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 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 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=24741
     Region          7..224
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mtasaaptgg taaesstrdr vtqlllerga ttaaqlgval glspaairrh ldamladgdv
       61 yareqavqgs rgrgrpakvf mlteagrvrc gthhydnmat aalrwiarrg gsdaveafaa
      121 eqvsalesrc raamedagdd plaraealaa altgegyaan attiasggql cqhhcpvahv
      181 aaefpqlcea etavisrlvg thvqrlatia hgdgvctthi ptqpgraqsg npvttvrtar
//
LOCUS       WP_357559405             158 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357559405
VERSION     WP_357559405.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..158
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17918
     Region          7..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrpaaldwsv enctiarame ilgerwtlvv lrevftgvrr fddmrvrtgi prqvltnrla
       61 alvgqgvlrr epyrepgsrp rheyrltekg ldlwpvlvav lgwgdrylad aegspltvth
      121 rdcdapvrve lrcaeghdvr rmrdvlsrpg pgarrrsp
//
LOCUS       WP_357559436             464 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559436
VERSION     WP_357559436.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=49093
     Region          6..461
                     /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 mtdrpeefdl lvvgggkagk tlsmdvarag qrvamvergm iggscinvac iptkalvtsa
       61 raarllrgas alglsvqggr vdvdllrahk qdvvegmvaa nrqqfldsgl hlvigearfv
      121 sprtvrvsla dggerllrgd dvvintgtrp hlpsvpgmae agvltsdell rldrlparlv
      181 vlgggtvgve faqmfasfgs avtlveggpr llpredpdvs davlrvfldd gvdvrvgiav
      241 arvdrdvdgt lrvtlddgsl vtgddvlvaa grepvtdglg ldvagvrlde rgfvqvdehl
      301 rtsaertwaa gdvagspqft hvslddyrii ranlvggers tadrlipytv fttpelarvg
      361 ltetearrag ydievahlpv aaiprartlr qtqgiwkavi dtstdrilga allgaeagev
      421 itsvqlamla gmpwtalrda vithptmteg lnllfaslkp rpvr
//
LOCUS       WP_357559488             208 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559488
VERSION     WP_357559488.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 18527488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..208
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22622
     Region          12..90
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          85..192
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mtesgadrvg avtaavarqv relrarrgws fdelagrsgv skgmlvqieg artnpsvgtl
       61 crvadafgvn iaqllepaee ravkitsade apvlwqgehg gaarllsglg epdlvelwdw
      121 rllpgeahls ldhprgtrev lhildgtviv rvggqdhpvr agetieihad rehgyrndsd
      181 epallvmvvv tpsgewdrrt rsrrprqe
//
LOCUS       WP_357559498             328 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559498
VERSION     WP_357559498.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=36513
     Region          38..325
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mttltevpea aaaretparr rrrvdrlpyl lllpalliig vlllwplgqv vvmsfyrlns
       61 vrqlrgdrew pwvglgnyad ilsdpffltv lrntvlfaaa nvlltmvlgt lvglllnrlg
      121 rkmatfvasc vmlawatpal tgtivwkwif ddtsglvtwl fnalpdglss slfgrsdwtg
      181 ygwfnspllf failtlvvvw hsfpfiavsv laglksvpse lheaarvdga spwrvfwkit
      241 fpllrpvfgi livlstiwdf kvftqqfvla ggtqdrptfm laiysyaeaf spppkyglga
      301 aiaviltlil lvvtgfyvrm vlrqedes
//
LOCUS       WP_357559545             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559545
VERSION     WP_357559545.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32715
     Region          21..83
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(26,30,55)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(29,54)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(36..37,48,51,55..56)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          107..287
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msmvpteggp ttgptvlrml lgaqlrrlre ssgvtregag weirsseski srmelgrvgf
       61 kerdvsdllt lygvteeher dallklarda nspgwwhryg dvlptwfqsy lgleaaaali
      121 rsyevqfvpg llqtreyara vvllghgaag pdeidrrval rmqrqqllrr dsppqlwavv
      181 deaalrrpig gpevmrgqlt alieatktph irlqvipfaa gghaaaggaf tilrfgdqel
      241 pdivyieqlt saiyldkrdd ldyyavamer lcveaepper taeilgrlld dlypa
//
LOCUS       WP_357559554             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357559554
VERSION     WP_357559554.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30293
     Region          4..>154
                     /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 mtttqthtla vpgvdlvydv rgplppsdgr pvllmigqpm aaegftalap lftdrtvvty
       61 dprglgrsvr tdgrtdhtpq qqaadlhhli ealgagpvdl fassggavta lelvaaypgd
      121 vvtlvahepp inavlpdaga aeraradfyq ayqtkgagag maafiamtsw qgeftdayfa
      181 rpaadpatfg lsteddgsrd dpllsdlswa isdyrpdasr laaaptrivi avgeestgty
      241 tartalglaa llgqeavvfp shhggflgge fgyagkpeef aarlrevlda a
//
LOCUS       WP_357559619             359 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559619
VERSION     WP_357559619.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=36966
     Region          52..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 mehvltsgtg trpeprtvpp ekvprdslsr tgrrwaglvv gvvalaaava lsiavgsrsl
       61 glgtvwqvlw hddgsaaaei vhrlrvprti lgfavgaalg lagtmmqalt rnplaepgll
      121 gvslgastgv vlaiallgvt sangyvwfai agagltsaav falggagrap tperqvlagv
      181 sltsvlgagi wailvthrea fdryrhwdvg sladretgti tqlapflvvg vllalvlgrq
      241 lnalsmgdda atsvgahpgr irvlgmitit llcgaataac gpiwfvglav pyaarmftgs
      301 dhrwilaysl vlgptlllvs dvlgrvlvap aelpvgvvta flgaplfial crrrrlstl
//
LOCUS       WP_357559626             411 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357559626
VERSION     WP_357559626.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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 411)
  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..411
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..411
                     /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=44999
     Region          25..408
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(62,69,98..99,106,110,117,244..245,248,252..253,256,
                     289,294..295,298..299,301,324,350..352,355..356,358..360,
                     364)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(69,92,94,97,99..100,187..188,197,243..244,247..248,
                     252,295,298..300,399)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mteaapldat vddhlvldad qlaqphefyk vlreqrpvvr ivvpsgiraw lvtrhrdvra
       61 vladprlakn sasvvrlmer htdpdkfhnv vksaahhmln sdppdhtrlr rlvgrafttr
      121 giahyrprie qiadelldav eagaagtgge fdlldsfasp lpiavitell gvpleqrdaf
      181 rewsngilsg rpsptrrygd laaflrtlid dkrrhpgpdv lsmfvatdga dalsdqeald
      241 mvlllliagh ettvnligng vlallrhpeq maalradptr tpqaveellr ydgpfnmatl
      301 ryttepvvls gttipadefv lvaltsanrd adqypdpdrl digreggnla fghgihyclg
      361 aplarlegei alnallarfp rltlarapee lgwrsgtlvr glltlplrig a
//
LOCUS       WP_357559673             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559673
VERSION     WP_357559673.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=35880
     Region          4..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msrtrterlv nlvicllstr rfltaaqiaa tvpgyehdpd dardheafqr kferdkaelr
       61 elgvpletgt asafdaepgy riahreyalp dillepdeaa avgiaarlwq haglaaaass
      121 glaklraagv dvdpqatlgl epmvtvdpaf apltaaardr revgfdyrvp drdapsrrrl
      181 qpwgvvcwrg rwyvvghdld raatrcfrls rvvgavrvag aagayeppan vdlishvarw
      241 sgpvertgra tvlaapgraa glrrwavevt tgpdgdrlvl pyadpdglag hlvgygpdvr
      301 vldppevrea viqrlkeiav rhdelavagg ar
//
LOCUS       WP_357559699             332 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC049230].
ACCESSION   WP_357559699
VERSION     WP_357559699.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..332
                     /product="phosphotransferase 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=36432
     Region          13..283
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtrdesvagr gflraddvrd lvaeqfgsar rltavdrltg gskkgvyrlr lddrttvily
       61 vwaaaenfwp asptvpddpf tdasgadlfa ishaaltaan vrvprllmld rdgrylpsdi
      121 alvedvgdlt leallardpv aaatplsalg dclrrmhttl gahygklati thgatsqtrs
      181 aedvvadral ghldavatrd arladahdri aahvrhlrga vtarrayglv hgelgpdhvf
      241 vtpdnepali diegltyfdv ewehawlqmr fgdaypalrp veldphrlel yryaqvlsli
      301 egplriaatd fpnrrwmldl aewniakala pl
//
LOCUS       WP_357559801             392 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049230].
ACCESSION   WP_357559801
VERSION     WP_357559801.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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=40284
     Region          164..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpavaaptap pptldnpagg alvlifttip allrltcgvi ggavalsvre ppvdpavllp
       61 avaaltgwsi wyayramrhg itpwlvtadv tvtalaclli pvlvapgvlp gegswiavla
      121 sttvinaqat aparwsipag llvtvtyatg aqaagnptea rahattllvq tactammaav
      181 mrrrigradr sfvehqrltr qalvaraard aerqqnrdlh dtvlgtltmv glgavagssa
      241 tfrdrcgsdl rtlvaltdvg pvagdgpvpl dgrlravagr lpelsaeltl tpctvpagva
      301 daigesayaa lsnvarhapg arvtlrlsrh avgvvvevad dgpgfdpatv pphryglres
      361 ihgrmatvgg raevrsaiga gtrirlewpg vg
//
LOCUS       WP_357559873             436 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559873
VERSION     WP_357559873.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 436)
  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..436
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..436
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46885
     Region          1..>60
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msesaspfae rlrtliksrg vsyralagkt fysksylhdl acgrktptln tahrldaale
       61 aggmlaalal apgaeegsav tyglrcdaeq ladllvtqtp npenaaelah qwliaeppqr
      121 yelsagrrvg detvarvegr vrqlrrlddh vggaetytmv saelaatadl lregsyreav
      181 nrrllvaiad lcqlagfvae dsgrvtearr hyltgmraah aggdtasaan clsslsylea
      241 nlgdrrsait larsayvggr haaeatgqal llervawaha rlgeatlaer algdvqqiye
      301 hsdlddapsw aywlthdeve vmagrvwtel rrplravpil egaivryged spretslyls
      361 wlteallqag elehavvaag rsmdlarsar sqravdriae lrrmmaaaed rtgaadkfpk
      421 vsadlsaaag gqvggq
//
LOCUS       WP_357559905             231 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559905
VERSION     WP_357559905.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     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: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=24446
     Region          29..229
                     /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 mlapmrgaaa daltelerei dapgngldrl rlmptpfvpe vrlhlaedai vwwarmeaav
       61 ghplpapywa sawaggqala rhlldhpela agrrvldlas gsglvaiaaa lagatqvvan
      121 didpyavaav tlnaranrvt vdvfgddlld dtgseadlvv agdvfydram adrmlpylqr
      181 aaargadvlv gdpdrghlpa drltvladyp vpttepsvds sirqvrvlrp v
//
LOCUS       WP_357559910             171 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC049230].
ACCESSION   WP_357559910
VERSION     WP_357559910.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 171)
  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 171)
  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..171
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..171
                     /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=19063
     Region          6..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 myrrrdtrre qlaaeitnnl rryavdaqhv ghafatlhgl nptdlqalia vmdaellgdp
       61 itpgrlgeql nlssgsvtal vdrleraghi rrdrdtadrr kvllhyadqg aalameffqp
      121 lgartdtvma rfgedelevv hrfmaemses lrghrdavra arpesprrpt g
//
LOCUS       WP_357559945             302 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Micromonospora
            sp. NPDC049230].
ACCESSION   WP_357559945
VERSION     WP_357559945.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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 302)
  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 302)
  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 302)
  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..302
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..302
                     /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=32797
     Region          9..294
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msnsalprrv vvtgatgklg ravvahlrav gvdvlavdra ggrdprdvdg efllvdltdy
       61 gqvveaftgg adehaggvda ivhlaavpap glmsnattfa nnsaatynvf aaaraagikr
      121 vvwassetvl glpfdtpppy apvdeeyapr pestyslnkv leeemarhfc rwdpelvmvg
      181 lrfsnvmdve dyapfpsfda dprarrwnlw gyidardgaq averalahdr pgadvfiian
      241 adtvmsrssa sllaevypgv evrkelgehe tllsidkarr vlgyeprhsw rdhvhpvqra
      301 aw
//
LOCUS       WP_357559956             383 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049230].
ACCESSION   WP_357559956
VERSION     WP_357559956.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049230
  ORGANISM  Micromonospora sp. NPDC049230
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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 383)
  AUTHORS   ter Beek,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..383
                     /organism="Micromonospora sp. NPDC049230"
                     /db_xref="taxon:3155502"
     Protein         1..383
                     /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=40926
     Region          26..321
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mwdwksgeaf aksyldkaka dfkkkhpkve vefvaqpfdq yytllgaaiq sgkgpdvmlf
       61 ngggqirdrv dalvpitdyv aedkqrlagw daftkdgkvy gapvtlqgyp iyynkeiyrk
      121 agldpatpaa twdkfvadca aiakagakcf algnkegvgi qfwlssmgsv tltaaeydaw
      181 itgkrdwnsa nvkrifqlwk etgdkkmnsd ganstamfnd sfalfqsgka ahvmglmsdv
      241 ghwqdfnefl tpeklgvmka pvvtagttps lpydggigya vakwtkdpkv aadlvrslss
      301 adalkafyad agaiaadtti dvsaggpavs tivgdlktgk palhvalssk tldlmgrlsq
      361 qllsgsitvd evvkqlaasd qag
//
LOCUS       WP_357560134             289 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome c biogenesis CcdA family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357560134
VERSION     WP_357560134.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..289
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=29587
     Region          27..250
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mgetfeqlaq sgplllaiga aalaglvsfl spcvlplvpg ylsyvtglag adletrrpqv
       61 rkgpppsdpv aegalpdteg gsggvavrer aepaaasvkg rvlagtllfi ggfsvvftat
      121 ailfasvgrv ffeygralei vvgvlivvlg lsylglvpgl qrefriqrlp aaglwgapvf
      181 gavfalswvp cagptlgavm gmaavggqtd ravvlalayc lglgvpfvvf glgferllgv
      241 fravrrnsrw vtgvggalli liglalvtgg wtdfviwlrg mvgvgevsi
//
LOCUS       WP_357560135             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357560135
VERSION     WP_357560135.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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..191
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..191
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20200
     Region          45..183
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mtarrwtagl laavaavala gcssrdreed cgnrdgiiec apdqrsaapk lagelltggs
       61 hdvasdrgqv vvvnfwgswc apcraeaddl entyqatkas gvtflginvq derdkalafe
      121 ksfgvtypsl fdppsrlala ldiapntvpa tvvldrdgri avviraavkq eglqpiveri
      181 aaeqpapnrs r
//
LOCUS       WP_357560252             360 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357560252
VERSION     WP_357560252.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..360
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..360
                     /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=37968
     Region          15..355
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mgvfasnddp gssgheqvvf cqdkqsglka iigiystalg palggtrfyp yasesdalad
       61 vldlsrgmay knalagldlg ggkaviwgdp erikseallr aygrfvesla gryytacdvg
      121 tyvadmdvia retsyvtgrs vehggagdss iltawgvfqg mraaaehvwg aptlagrrvg
      181 vaglgkvgky lvghllddga evvatdvspr alewvrdnhp qvalvddtaa lvasdidvya
      241 pcalggaldd dtvpvlrarv vagaannqla hsgiekilad rgilyapdyv vnaggviqva
      301 deiegfnfer aklratriyd ttreilrlad aegvppavaa drlaerrmad vgrlrtihlr
//
LOCUS       WP_357560298             269 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357560298
VERSION     WP_357560298.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=29261
     Region          1..258
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtldrpdser ralitgatag igaafarrla adgwhlvlva rdaarladta adltgrhgre
       61 vetipadlst ddgcetverr laegppiell vnnagislnt pflrssaede arllrlnvha
      121 vmrltlaalr pmterrhgav invssvagfg pvmpgstysa skawvtnfse svgqsarpfg
      181 vrvmalcpgy trtefhdrag inmsktpawm wlraddvvde slrdlrkgkl vsvpawkykl
      241 avaglrhvpr rllevafrdt rgrvdrtdg
//
LOCUS       WP_357560453            1501 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357560453
VERSION     WP_357560453.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1501)
  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 1501)
  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 1501)
  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 1501)
  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 1501)
  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 1501)
  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 20187797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1501
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..1501
                     /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=153410
     Region          <71..774
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          616..1466
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mtplgraaar llppvavpqv vgeasrsvga aanrlarmag ltrrrvwsrp grhhievhgv
       61 cqdggdalar qveaaleqvp gvewarvnap sgrvvvavgt pqpelrhlia tvaraervcp
      121 hqpdpdippp hppeegprtp rtlgalasda lgltisaatr ilpftpvpge vagllgavdl
      181 hprlhalanr glradpradv lfplaeavvq glsggwtgiv ldgaqrvvqw gearaqlrtw
      241 aqaeprltgd pdravarapk ldrprpkpdg paeryvtrml tagaaaaaaa tpvvgrkraa
      301 alglsalpka pgsgregyaa qlgrilarrg viamdrsvlr eldridtlvl daavlgsdrg
      361 vladlaplag adtgrvatha ftlfdpaapg elrqsdgwrl gpldaldadd pgdtpdsrrl
      421 regggsllgl aegdtlaavl rvepepapgv dalptaarqa glrlvvagdd drrygfadah
      481 lpggdrlaes vralqadgav vmvvsgdraa lgvadcglgf sapedlppwg ahllvgadlr
      541 vvtlvieatg varsttrqni glalagtglg algaftaapa qlpgrtlaav ngaaalafah
      601 gvvrahrlpd rmdapaptit awhlmpsstv ldqlgtgpdg lasdearrrr iaspdgpsgp
      661 tgllrafvde lanpltpvla agavlsatfg slvdaalvgg vvggsallga vhqhntersl
      721 aellsrsavt arvrrdgaea vlpadelvpg dvilleagda vpadcrvles agletdessl
      781 tgeslpvgks dqpvvaaava drrsmlyegt tvaaghgtav vvatgadtea grslamarqa
      841 ppasgvearl grltrgaipl aagsavavag agllrgvpla etaataanla vasvpeglpf
      901 lvsaaqlaaa rrlaehgalv rnprtiealg rvdvlcfdkt gtltegqlml agvgddgryv
      961 pmdrvddslr pvlavalrat ppaadphdla qqtdravrsg aqaagvteqt gaqgwepvgg
     1021 lpfepsrgyh atvgrtgdrl llsvkgapes vlprcsawrt pggrdepldd agrdglhatl
     1081 aararaghri lavaecrtss pgvtddqvdd ltfvgflala dgvresaapa vrrirqagvh
     1141 timitgdhpa taeaiaatis dhdeqrvvta aeldqlddda laarlaatdv varctpahkv
     1201 riiqalqkcg rtvamtgdga ndapairlad vgialgqrgt paakaaadlv vtddrletii
     1261 atlvegramw ssvrhalsil vggnlgeiaf svltaaatgr saltgrqlll vnlltdlapa
     1321 laiavrppga dhadgllreg pdtslgetmt reiglraaat tlgatagwtl arytgrrrra
     1381 gtvalvslvg tqlgqtvlag gtspavlast vasagvlavv vqtpgvsqff gctplgpvgw
     1441 tiatgsalga tfangaltrl verlprsesg padrpdadgp dadrsdvgds tdttgdqatr
     1501 p
//
LOCUS       WP_357560476             433 aa            linear   BCT 28-DEC-2024
DEFINITION  ParA family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357560476
VERSION     WP_357560476.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 433)
  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 433)
  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 433)
  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 433)
  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..433
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..433
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46323
     Region          <8..154
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          172..423
                     /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 mhddgryddp rvtgsrdpvs retdypswsp depsrgpsiq pqdwepaarp saaepdapar
       61 aavdgpypgg aaggrvipir rnassparfe savpqqptpd avpdaspdpv svtdtsgppa
      121 gsyepaaaea ayvsretptr eeddpplame amravqilnp sgevmmprpe rtrvmcvanq
      181 kggvgktttt vnlavalalh gnrvlvvdld pqgnastgln vphhtgvpdv ydclinsvpl
      241 aevaqgvegi pnlwcvpati dlagaeielv svvaresrls raieaypghf dyvfidcpps
      301 lglltvnalv aaqevlipiq ceyyalegln qlinninlvr qhlnprldvs tilltmydrr
      361 trladaveqd vrnhfgdkvl qaviprnvrv seapsygqsv mtydpgsrga tsyfeaaqei
      421 aergikepvg rng
//
LOCUS       WP_357560547             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357560547
VERSION     WP_357560547.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..265
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27266
     Region          30..258
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpadpravls rpapapdltv sygdhpdqva dlrlpagagp arrlvvvvhg gfwraeydrr
       61 htdplavala alghpvaqve yrrtgqpggg wpgtpadllt gvtelprlaa galpgrvaag
      121 ppllvghsag ghlalyaaat apaavggvla lapvsnlaea yrldldegav aallgggpad
      181 fperyaatdp ralvpvssrt vvihgacdrq vpiemsrefv aagraaggei rlvelpeceh
      241 fglidpespa wpqvtaafrs llkdh
//
LOCUS       WP_357560629             522 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC047074].
ACCESSION   WP_357560629
VERSION     WP_357560629.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 522)
  AUTHORS   ter Beek,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 522)
  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 522)
  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 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..522
                     /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=52800
     Region          4..522
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mtwlavrqmr rgativiiiv ggmsamvatt yastvgdamd aaalaalaen pairtlfgqp
       61 valdtaggft vwrtgtilav lvgawallta tritrgaeda ghwdlllagt vplstvvmrh
      121 atvivtaall vglgtatalt aagtppagaa lhgagvalvg vffatagtla aqifpsraaa
      181 sgatvallga glllrmigdg vdalgwlrwl spfglaalsr pyhdnrvlpl lvlalatsvl
      241 laaipaatgr rdvrggwltp rtgraprlrl lgsvpafalr rllrplagwt agvgayylli
      301 gllavsmtdf ladnprfadl aaqagfaglg svegyaaamf allaipagif tavhvatiaa
      361 aeadrrltli yagpitrlrl ltaeattaat gvvaltttag latwigatsm gaplrlaaal
      421 agtmnvlpia alclgaaila lgwlpraval vgalpaaggf llqviadstn aphwvgtlsp
      481 fthlaavpda apdwpgvigm litasvltla gaigyqhrdl rt
//
LOCUS       WP_357560686            1328 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357560686
VERSION     WP_357560686.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1328)
  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 1328)
  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 1328)
  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 1328)
  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..1328
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..1328
                     /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=142473
     Region          2..1322
                     /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 miplshaqqr lwfldrlhgf dptyhlpvvl rlqgpldrta laaavgdvva rheslrtvfp
       61 dtdgvphqkv laaaaagpel tvtacpaael dariqaaasa pfslaqappl radlfvcsaa
      121 esvllltlhh iiadgwsigv llrdlaaayr trsaglgapg waelpvqytd ytlwqrellg
      181 drgdpesiag rqlaywrdal egvpaalplp adrprpsaag qrgagiaidw dasrhrelsn
      241 larrhnctvf mvvqaalcgl lcrmgagtdi plgsvtagrt dealddlvgl fvntlvlrtd
      301 lsgdpsftel lrrvrdvdlq ayahqdlpfd llveelnppr sadghpffqv mlafetrveq
      361 eldfgsvrvs rpevdipaak aelnlqlteh vdaagglkgi sgvleyatdv frrgtaqlla
      421 drlsrfldaa vaapempise ltlltpdere qilrtwndtt rqlpvttlpe afrrqtaltp
      481 hataliwgss sltyaeldle tdrlarglrq lgagpgavva valprsaelv vsllavvkag
      541 gaylpldpgy pderirmmlh darpvcvlsd pelrtrladg efcvatpgel madaatgvad
      601 plrtgpvlrp qhpayviyts gstgrpkgvv vshaaidnrl rwmqaayplt pddrilqktp
      661 sgfdvsvwef fwpmqvgaal vlagpdehrd paalvrtiva hrvttvhfvp smlnlfitgp
      721 taarcgglrr vfcsgealpr dtatafhqil pgvaltnlyg pteaavdvtc hdcvpgeqgp
      781 vpigrpvwnt qvrvlddrla pcpaglagel yisgvqladg ylaraaltst rfvadpygpp
      841 gsrmyrtgdr vrwtpegelv ylgrtddqvk lrgqriepge veaallaeet vaaacvvvre
      901 dtpgdqrlva yvtpaaagpq vrasvdpqal lgnladvlpg alvptavvvl dtlplspngk
      961 ldrralpppp vsvaqgrepr srlertlvrl yaellgvadv gveddffqlg ghsmlavrla
     1021 rrihtelavt vpvqsifrhp tpaalarqlp rtgateeafg pvlelrsega geplflvhpg
     1081 tglswcyfrl lehldparpv halqargfae taaggvlpal prtvaemaad yltqvrkiqp
     1141 tgpyhlagws fgglvahsma trleregeqv aslvvldgyp evpgqetagr llgealhnll
     1201 gvppgdaagd aqdpgelvas vldevrrrfp pladadddgl haalrigmnn lrlqygfvpe
     1261 llqsdmtlvv arsgdpsewq ryvagrltvl hldaehhdlc saaaedsgrl lagvlaktga
     1321 aagqgsek
//
LOCUS       WP_357560634             148 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357560634
VERSION     WP_357560634.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 148)
  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 148)
  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 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   4  (residues 1 to 148)
  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 148)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (residues 1 to 148)
  AUTHORS   Rosinski,J.A. 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 148)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..148
                     /product="GbsR/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=16249
     Region          8..147
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 maalrdpaeh lalaltqggm qrmtarvlaa llfteqdtlt ageiteslti ssgsvstalk
       61 sltsvgliek vpapgsrreh frfregawat lmseqnqlvk vmreaaeqgi tatgedsvag
      121 rrlgemrdfy dylwrelpal idrwkaqr
//
LOCUS       WP_357560695             126 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC047074].
ACCESSION   WP_357560695
VERSION     WP_357560695.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14200
     Region          22..116
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maepfpdtpt athvaqvhlv arevfdvvgt kwavpvieai gsdtrrfgel hrqvagishr
       61 lltatlrqle rngvvdrtlh ptvppraeyr ltpagrelhd tingfcrwsr hhldeilasr
      121 rrfeqa
//
LOCUS       WP_357560711             387 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357560711
VERSION     WP_357560711.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 387)
  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..387
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..387
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=39188
     Region          53..121
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          110..165
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          154..216
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          206..270
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          260..323
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          312..375
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mdrrfhagla tvlavtvvva vpagaraasg gtfapaqyla tgstatnava vadvtgdgrr
       61 divvgvdaad gtqtssvlvf aqrtdgshga ptritahggy nsdvrlavad idrdgrtdva
      121 lsssagvdll fqrngglaap vlvpgtagdv avtdvtgdgr pdlvvsawhg qvriypqtat
      181 gtfpsytpiv gpfadgapgh qvfaadlngd gridvaqfyg hgtwvrlrqa dgsygpaaty
      241 rtppdagghr rvsngaavgd vtgdgrvdlv mtvngnmpds avqvfaqgsg gltatpvrhp
      301 ayesaaglai gdltgdgrad lvvahsnwaa vsvhlqrsdg tlggyttnsv davgwqedal
      361 aigdvtgdgk pdlvvvsydk vavlrql
//
LOCUS       WP_357560814             184 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357560814
VERSION     WP_357560814.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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 184)
  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 184)
  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 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..184
                     /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=19491
     Region          9..160
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mprvttlrlr pedpadtgav rrvlasafar pdvstppevg lveelrdsda wlpelamvae
       61 yggeivgyal ltrvrvrsdd haapalalgp vavaphrqri glgtavvqaa ieaatelger
      121 lvvvlgdpay yhrfgfgrad rmgltspwsg lgdpwqalal pptvsgegpp phgevlfppp
      181 wskv
//
LOCUS       WP_357560960             318 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357560960
VERSION     WP_357560960.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..318
                     /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=34063
     Region          6..309
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 maavgrprrs clavpgssvk mlgkaqglpa dqvfldleda vaplakpdar knivaalneg
       61 dwsgktrvvr vndlttpwty rdvidvvega ganldcvmlp kvqnaaqvqw ldltltqlek
      121 tlglevgrig ieaqienaag lvnvdaiaaa sprvetiifg padfmasinm kslvvgalip
      181 dypgdpyhyi lmrilmaarm hdkqaidgpf lqirdvdafr evarrsaalg fdgkwvlhpg
      241 qidaanevys paqadydhae lildayehyt seaggrlgav mlgdemidea srkmalvvaa
      301 kgraagmtrt ssftppae
//
LOCUS       WP_357560974             189 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357560974
VERSION     WP_357560974.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  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..189
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..189
                     /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=20621
     Region          4..165
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mpcltvivas trpgrvgrri gdwftgiatr hdtfddvrlv dlaevglpfh dephhpsegr
       61 ylhrhtrews atvaagdafv lvmpeynygf saplknaidy lytewqykpv gfvsygmtsg
      121 glravqmikq vvttlkmapa neavtvflre sldgagelvp dpardaaaev mldelgrlaa
      181 alaplrvpa
//
LOCUS       WP_357561223             189 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357561223
VERSION     WP_357561223.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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..189
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..189
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=18167
     Region          60..188
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 miknirrraa lglgagalgl vavagvavna saagpatvak pavpvaaakp aaasnvvanp
       61 sldidaalra aqatlkaaek dgqrvtvvvl drsgavqvql kgdgagpqta dsatrkafta
      121 vsfgqptsal agrvtgsgat lrdipgtlfl aggvpvsvdq qvvgaigvgg apsgdldery
      181 adagaatlr
//
LOCUS       WP_357561009             155 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561009
VERSION     WP_357561009.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 155)
  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 155)
  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..155
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..155
                     /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=16708
     Region          5..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdlitlrdap lgrllvvagh ltgqrwnryl aeehgltqag mvtlmtlaqh gelphrtvae
       61 hgfvrpatlt givdtlerdg lvarqrdetd rrsvrlaitp agrarldalt avlhsghplt
      121 pvdadpakaa vireflvqvi argegdhrtp egvac
//
LOCUS       WP_357561235             486 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357561235
VERSION     WP_357561235.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 486)
  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..486
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..486
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=52899
     Region          56..>121
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mthancprcg grlardndsg rcapcqaaer drlsappvvp asfwehrpvr ralaerhlgr
       61 virayrchpy hgraalpqtv vagwlgitqa qlsrvetgpp imhmdrlthw akvlriplah
      121 lwfalpgqth ragnnavhvt plpnqqssgp degrrallag iaavaagagl vggaglvqpr
      181 rigaadvarl navlelyrsv dyecgggllh qevarfaesv yrmldwshpa gltprlvaav
      241 aaarqlagwt aldagrhhda qrhfvagera altagdvlla amirysqakq lqhlrhnrda
      301 latlqlahtq lgahatpaik allwgaeaas vaalgdhrta vttlgkasdq ferisserep
      361 gwlgfydrge lfaqygrvyr dkarqdsrha peavrwvesa iatfgpanvr stvlnevglc
      421 salfladepe qalvvgarvm eqvrtmsstr vidrvvnlrr dlgrhrrlpq vaeferhltp
      481 halaak
//
LOCUS       WP_357561392             313 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357561392
VERSION     WP_357561392.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 313)
  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 313)
  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..313
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..313
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34769
     Region          1..269
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mkasvvvptf nssalldrcl rtlraqklav sdslevlivd dgstdptaet vqyhmtadsr
       61 frylhlprsa tssrsaarnr gaeeatgdil ifvdgdqlvp ptfadrhlrh yrvmpekkav
      121 igfrkylrap eafddrfmed gaeeflggli kgdirldllg rlsdlggdlk tswhlfftcn
      181 vsvpsvdykr vggfneefrg wgledselgy rlgrsgtqiv fdeesfayhq gpplspnkpv
      241 yegwlknlsl fialhkeape vilqamlapi fnpavganwt dtyeqfemca rstpaaftgs
      301 rvqveddfpa pva
//
LOCUS       WP_357561350             238 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561350
VERSION     WP_357561350.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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 238)
  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 238)
  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..238
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..238
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25121
     Region          76..236
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mssrkgqkss arvvreqlar eqrrkrtlwv svaavavlvi agligwsvys sqrsddftap
       61 tganeagtgv vagsgpvtvd vyedflcpac kqfeqlsgpt ldqlisegkv rvvhhpvayl
      121 nrfstteyst rssaasgcaa eggryreyak alferqppeg gaglsdsela diaagagidr
      181 dgfasclreg tfkpwtehvt eeaskanits tptilidgkp vadrspegik aaveaagk
//
LOCUS       WP_357561403             301 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357561403
VERSION     WP_357561403.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  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..301
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..301
                     /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=32628
     Region          51..298
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mrnivrvgia vlaaavsavv vavpggatvp taetamaapa hsrkgpavvd yahrgasgsa
       61 pentiaaarf avtqgatfve tdvrrtadge lvvmhddkls rttnveevfp drapywvhdf
      121 tlaeirqlda gswfapeftg ervptlrefv dalkrrsgll leikgsllyp gieadivael
      181 ksipgylpwa latgklviqs fwvpavrdih tllpdvpvgl lfetrptddv lveasrwadq
      241 inpgnaftdq alvdrvhelg msinpyvvnn grdmrrfvnl gvdgiitdyp avmrdivrit
      301 r
//
LOCUS       WP_357561540             140 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561540
VERSION     WP_357561540.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 140)
  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 140)
  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..140
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..140
                     /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=14976
     Region          4..137
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 malpsgpvtt sseaeaalfd lvdvydraye aaaaelslsp aqacvlgrld errgmgalae
       61 elgcdasnit qivvrlealg lvtrepnprd rrarlvartp rgdeinhrfa taftfartav
      121 grlspeeqdq ltallrkalg
//
LOCUS       WP_357561463             129 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561463
VERSION     WP_357561463.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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..129
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..129
                     /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=13798
     Region          2..123
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mlrraasqra gsvalpdaqv evlrlverrp gigvreaaer lgtapntvst lvgelttsgl
       61 lhrerdpadr rtvrldltda areriaaygr hrhdlltaal galegpdrea lltaapalrr
      121 ladglaeql
//
LOCUS       WP_357561592             401 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357561592
VERSION     WP_357561592.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   ter Beek,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 401)
  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..401
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..401
                     /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=43818
     Region          1..388
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 madivldrvs kkfpdgtvav advdleiadg efvilvgpsg cgksttlnmi agledissge
       61 lriggqrvnd kaprdrdiam vfqsyalypn mtvrenmafp lrlakldket ihrkveeaak
      121 vlelsalldr kpanlsggqr qrvamgraiv rqpkaflmde plsnldaklr vqmrtvvsrl
      181 qkklgtttvy vthdqteamt lgdrvvimrg gavqqvgppq elydhprnlf vagfigspsm
      241 nflhaavedg tlrtalgdvp igerirrele gadaprelil girpehfeda alidddtrrr
      301 gmefeapvdi vesmgsdkyv yfsvegeras aaeleelaad agadfsgega nlvtrlsaes
      361 pveegqtrrv wfnlekihlf dptngrnltl hegraagala d
//
LOCUS       WP_357561715             220 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF47 domain-containing protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561715
VERSION     WP_357561715.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..220
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=24217
     Region          29..219
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mrlpgrrlrr rtrrlvddls grshhrmvei llrqidaakt gadlavsvas gvvpsalgra
       61 rmaeiehagd rhrgelvsel stvlttpidr edlfrlsrsv ddvldnlrdy vretdlfavt
      121 aapgsvaale svneglgllr latarlpatp rgvaelalat rkrssrvrrh yqiaiadlms
      181 epigpdtlkr rellrrvdvi glrlgecvna lndamlkrsv
//
LOCUS       WP_357561717             351 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561717
VERSION     WP_357561717.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..351
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..351
                     /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=37796
     Region          7..>167
                     /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"
     Region          <286..320
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
ORIGIN      
        1 midghwdvvv vggriagast awalapyaer vlvvdasrat afwpqqstwd rsgnlawsel
       61 glletvlacg apptygdtqr vgedvtervy predaysfrm svprevldpa llaaagsrgn
      121 vtvlrparvr dltieagrvr gatvrhgavd sevtcdllvl adgrlsrnae rvgasayrvv
      181 espwfallay yedlplptdr syfslqdrsv listpcggkq wcvavdlhqs lidqtgrhpa
      241 rsyermvrdd pclgpavaag rratsiggag rlrmlrrpms gpgwclvgda gyhldpvtaq
      301 gtraalvtar ilrdriagag rvagadltgl tderdaalda dwayteqivr g
//
LOCUS       WP_357561423             252 aa            linear   BCT 28-DEC-2024
DEFINITION  leucyl/phenylalanyl-tRNA--protein transferase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357561423
VERSION     WP_357561423.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 252)
  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   2  (residues 1 to 252)
  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
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Abramochkin,G. and Shrader,T.E.
  TITLE     The leucyl/phenylalanyl-tRNA-protein transferase. Overexpression
            and characterization of substrate recognition, domain structure,
            and secondary structure
  JOURNAL   J Biol Chem 270 (35), 20621-20628 (1995)
   PUBMED   7657641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..252
                     /product="leucyl/phenylalanyl-tRNA--protein transferase"
                     /EC_number="2.3.2.6"
                     /GO_function="GO:0008914 - leucyl-tRNA--protein
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0030163 - protein catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27030
     Region          14..233
                     /region_name="Aat"
                     /note="Leu/Phe-tRNA-protein transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG2360"
                     /db_xref="CDD:441927"
ORIGIN      
        1 mgwetldlda apgegpvafg ddlspatllg ayrrglfpfp adteerkivs eftyagdvaa
       61 griavlagsv dpyavawcsp dprpvilvdr ariqrslrrq lrnkvewttt ldvcfdrvvq
      121 hcrvgreprw ltdrlvsalr elhaaghahs vevwegdelv ggtfgvrvgg vfsadsqfal
      181 rsgaakvava clvrrvadsg gvavdvqhdg ehakligavp vprseylall rehadddcam
      241 aadqlparsl aa
//
LOCUS       WP_357561800             286 aa            linear   BCT 28-DEC-2024
DEFINITION  CoA transferase subunit A [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561800
VERSION     WP_357561800.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..286
                     /product="CoA transferase subunit A"
                     /GO_function="GO:0008410 - CoA-transferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30954
     Region          1..231
                     /region_name="AtoD"
                     /note="Acyl CoA:acetate/3-ketoacid CoA transferase, alpha
                     subunit [Lipid transport and metabolism]; COG1788"
                     /db_xref="CDD:441394"
ORIGIN      
        1 madktltard avsrlepgmt igiggwgsrr kpmalvreil rsdlrdltiv syggpdvgll
       61 caagkvrkvv fgfvsldsia ldphfraarq rgavevaeyd egmlqwglya agirlpflpt
      121 raglgsdvlk hnpdlklvqd pygteqlvam pplrldaalv hmnradaqgn gqflgpdpyf
      181 ddlyclaadq afmscerivp taelsaaghs atikinrqlv agvvetpnga hftscapdye
      241 rdeafqreyv kaagdpqawa kfekrylsgt eddyqaavaa raeeva
//
LOCUS       WP_357561802             371 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357561802
VERSION     WP_357561802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 371)
  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..371
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..371
                     /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=38560
     Region          19..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 msgaegphpr lrtratdlfg vrypivqtgm gyvsdvrltt atanagglgi laagllsyde
       61 lvvaieqiqa gtdapfgvni radqpdvvkr idllisagvk vasfalapkr ellarckdag
      121 lvvvpsigar rhaekvaawg adavivqgge ggghtggvpt slllpqvvda vdipvigagg
      181 ffdgrglvaa laygaegiam gtrflltsds pvqpsvkdvy laktvndtvl tlqvdgvpqr
      241 vlragtverl ertsasgrll ravrnavafq klsgtpwgdm vreglamrka hdltwsqvvm
      301 aanapmlyrs allegrtdvg vmatgqvvgl iddvpsvael idriideatr tldrlgvpap
      361 vasapaapee d
//
LOCUS       WP_357561865             365 aa            linear   BCT 28-DEC-2024
DEFINITION  PLP-dependent cysteine synthase family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357561865
VERSION     WP_357561865.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..365
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..365
                     /product="PLP-dependent cysteine synthase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38611
     Region          1..299
                     /region_name="CysK"
                     /note="Cysteine synthase [Amino acid transport and
                     metabolism]; COG0031"
                     /db_xref="CDD:439802"
ORIGIN      
        1 msaphllalv grtpvtyvqa alpgrhggfw akvecaspgg mkaraavaml taarargelr
       61 pgapvvests gtlgvglafa gqalghpvhl vvdrelepsm rallraygar levvdtpdav
      121 ggwqrarldr lavvraglpg swwpdqyrnp dnaagyvsla deiagqvdav dvlvcsvgtg
      181 ghsagvaral rrhwprlrlv gvdtvgstvf gqparprlmr glgssihpgn vdhaafdevh
      241 wvgpgeaves crllarhafv tggwstgaaa rvaawvarte pgarvlavfp dgphryldsi
      301 yddgwcarhg lpgptrghpv eiphpwaaev trwsrcrtvv dparvdparv dparvgpard
      361 ervpa
//
LOCUS       WP_357561872             539 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357561872
VERSION     WP_357561872.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 539)
  AUTHORS   ter Beek,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 539)
  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 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..539
                     /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=56959
     Region          3..523
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mtatvvrvag lraeagsrpl ldgvsftlaa gqvlavlgas gsgkttlgra llgeagpgvr
       61 ltgqvevagr dvtptrpprp gtvgyvpqqp saalnpvrrv gpvlheiarr hlphscsprw
      121 pgttvgdlra rrerarqavr aalhrvslpa drdllrrfpd qlsggqqqrl vvahslltga
      181 hllvadeptt gqdnltrrdv ateltalarg gmavvllshd lrlvrevade llvlhqgrpv
      241 eagtaaevfd aprhdwtrrl laarpagtrv gagarppvlg vgglaaehsg ggrrrrpvle
      301 gvdltlaage clalvgrsgs gkttlarcva glhrpragtv elagrplaat vdrrdradla
      361 avqyvfqdar asfdpwrpvl dqvarpavrl hgrpahvars aaraaldrvg laghlvtrna
      421 gelsggelhr aalarallae prvlicdeit agldavtrdr ilalvdelrr addlallvis
      481 hdrdvvarla drvavlhdgr viedgpaatl ltsarqslsr sllhedvvvp dragksqle
//
LOCUS       WP_357561880             345 aa            linear   BCT 28-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561880
VERSION     WP_357561880.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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 345)
  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..345
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..345
                     /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=37162
     Region          <40..143
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mtaadplhan vpeqfyvhnp drgetlhrsa aeaihrdvta lnvhegnhvl eigtgtgysg
       61 allasrvgat grvtsidisd dlvdwadrlh rqrgvttitc htadgvtgyp phapyqriaa
      121 wctpprlpra wvnqlapngr ivaclpiaaq psttlvttit ltagqphvea vtfggyaqst
      181 atpvvdaltl pgrwvdhhtd qpdpawisig wrdqddpqht gartalnllr npghtetyhr
      241 aplnwpswta ysviaggpqr siaalddgkr gighttptta aviltdgtil adstrspslt
      301 alrswlhrwe ragrpdagwf rprlvpndgk dlpgwdlrvt agval
//
LOCUS       WP_357561892             288 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561892
VERSION     WP_357561892.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 288)
  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..288
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..288
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31564
     Region          1..282
                     /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 msaaeiemdd gaqlrtwttg sldhadiplv ilhggpglpd ylgpvagmve dlclvhrydq
       61 rgtggsgweg hhtiarhvrd lallldawgh dravlvghsf gtnlacyfal ahpervagli
      121 qiagpfldpw rdaygaaqrt rrtdeqqdrl deleanasrt daeeieyltl swftdhadra
      181 rawdwalasa ralrpvnyvm nsqlnaakka dpleshvnel rerlpagtvi iggtddsrpa
      241 dalrrlgahl gcevvlipna ghhpwleapd qftaairtav arqtrrha
//
LOCUS       WP_357561991              89 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl carrier protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561991
VERSION     WP_357561991.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 89)
  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 89)
  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 89)
  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..89
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..89
                     /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=9554
     Region          5..82
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mdapdratva relhdfiapa lsgpigpded yfalgllnsl faielvvfve qrfdleveva
       61 dldlghfrti srltdfvlak lagraglaa
//
LOCUS       WP_357562000             252 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562000
VERSION     WP_357562000.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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]"
                     /calculated_mol_wt=28273
     Region          50..155
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mrtfsdlvde aaavdvsgwd fdwlegrate erppwgysrl iasrlphvts aldidtggge
       61 iiaevshlpp rmvvtegwrp nverarrtls prgvevvpve qgqplpfada sfdlvtsrhp
      121 vdpdwseiar vltddgtyla qhvgpasafe liefflgplp rerlgrhpdh eaaaaraaal
      181 eivdlrtarc rmeffdigav vyilrkcvww vpdftveryw dtlkqldahi rhhgafvahs
      241 trslvdarra pr
//
LOCUS       WP_357561966             256 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357561966
VERSION     WP_357561966.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..256
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..256
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27029
     Region          26..246
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mtgaagappa raaderpfyf ragaehifgv lteptaadsg vgvlllsggv yvlstnrnrl
       61 yvrmarqlaa qghrslridy rgvgestgmi gdyplddpnv pdveaaigql vaagarrivl
      121 vgscygaraa mhvaaghpal asmvllappl gdrgrgaaat pdevgkvfqd rlstlwrrri
      181 ptlllygqed nyyhdfaras aepwlsglfg dgsalvlrtl pgkahglqri dlqdvfvdtv
      241 ldwvasvtgg drapav
//
LOCUS       WP_357562015             264 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562015
VERSION     WP_357562015.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=27592
     Region          6..264
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 mvllmmirvy lrllgahlra vleyrydall tigatvlgqg aglvfvgavf aqvpelagwt
       61 rwevvcvyam vllaegvgsl ffegtwqlag minggdldyl lvrpypvtlq vtgsalgvng
      121 lgnvllggvl lvgavgqvdv dwqpvtigwa vvllvsalat kvainlatns vafwllspss
      181 slaagvhvlg dlarypitvy gvglrvlltl lpvtfvgyfp aaallgkgvs atvglltpvv
      241 avlcliiarq ifkaglrrye sags
//
LOCUS       WP_357562053            1126 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562053
VERSION     WP_357562053.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1126)
  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 1126)
  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..1126
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..1126
                     /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=117630
     Region          120..601
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mslltaltlv igpasasaap ppadaapsad rsptasapta ttvtlltgdr vtvrtqpdgm
       61 lagdvqpgpg rsdvlfvqqs gpgsltvvpa dahpliasgk ldkrlfdvay lvehgyadgv
      121 raglpliaty rpgtraastn aaqalstlae prrslpsidg gafevpkaea atfwgtltgs
      181 gargaatrtt aaaqpldgvr klwldakvta slevsvpyig apaawqaght asgvtvavld
      241 tgydpahpdl agvvttavdf tgtsptaadr hghgthvasi iagrgtasgg khvgvargak
      301 lvvgkvlgdt geglfsqama amewaaretp akvinmsfga mdtpevdpve elvnrltaet
      361 gklfvvaagn hgprpftlgt pstadaalsv anvstgdala egssrgprlg dravkpdiaa
      421 pgtaivaars agvhpngsdv iddwylragg tsmasphvag aaaivagqhp ewdaatlkaa
      481 ltsttaalpe qspyevgagr vdvaravset fvatrssvsf gflrwpytdp qplseeitfr
      541 ndgaspvtvd lridataqdg tpaapgtftv spqqltvpah atgsvvvtfe rgaadpgtyg
      601 gvliaessdg ahrarvalgg tkepesyevt fqaldrtgql ppegalfdyl avfnhdtgdv
      661 leidngdtvr lpvgrygvys ylttnragtw vpsvsiqayp evkidrtttv tldarqaqrv
      721 sytvddrpda klrhqyqhai frhpatsahs ysswttslag dlfdevyvgg andsdgfgfa
      781 ssarltdsag naynltfpse rrvpdvdfhv taaglgrvdg tyrglggqsq vrvgflpvyf
      841 drylfnltqn ltvpsthtey fspgipfhqt veplvwtplr smkpgerrse tflagvigps
      901 faaappaifq nygpsrphwa yrsgdtidvh lpmlvdsgag hvpamltgtp iggtvklfrd
      961 gtlvggnssq pagwyrvpad paeyrleasl tcdvvycqpt spaassvwtf rsshtgttap
     1021 lplmavryap vldelnrapa gtfsfpvyve hqpgsvknrt vreltmeasf ddgatwtpvs
     1081 vrrhgndwta qlanpgsgtv slravavdry gnsvrqtvlr aygvss
//
LOCUS       WP_357562125             528 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562125
VERSION     WP_357562125.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 528)
  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 528)
  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..528
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..528
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58779
     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 mrfdgesgrt sapdvsvvva vyntmpyltt cltslveqti grdrlqvvav ddgstdgsge
       61 eldrfaaryp etfvvlhqan sggpavpsnr aleratgryv ffigsddhlg pealerlvta
      121 adrwesdvvl grmvgtnkry vhqaiyasse pdvdlfdsel pwslsntklf rrdlverhrl
      181 rfredmpmgs dqpftleacf rarrisvlad ydyyyavrre naqnityrsr heerlrcaee
      241 ivdfvaglie pgerrdavlv rhftwevakl lrkdfldlpe evqqqvhtri rkladqhlta
      301 girgrlpvdv lrrlsvaqhg dlshllelvr qeadkelppv tiedgrwyar yvgfrdpqls
      361 lpddlydvta rvgeimarlt atdltwkqda agervltvta rppwtgpgtd tygplrvvvg
      421 eltvdgavsg gahgtvvrad lpagelvrav gsgrqvvrat aegsgsgpvp vraerrlaap
      481 rvvvrqgvrl ylvtpavnhk gqvivavtpv tprrliarlr riwpsggk
//
LOCUS       WP_357562115             346 aa            linear   BCT 28-DEC-2024
DEFINITION  App1 family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562115
VERSION     WP_357562115.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..346
                     /product="App1 family protein"
                     /calculated_mol_wt=37759
     Region          14..346
                     /region_name="App1"
                     /note="Phosphatidate phosphatase APP1 [Lipid transport and
                     metabolism]; COG4850"
                     /db_xref="CDD:443878"
ORIGIN      
        1 mpptpagqla vpnlhraari edavhslver rlrrtgwrtn ivaytgygap gwvrvmcrvl
       61 lgrldtrqrg rlekvrgwrs fttlpakhvt vhieaggvah earadrsgfv dvvvaadlpp
      121 gwgsvrislp daepveapvr ildpevrfgv lsdiddtvmv talprpllaa wntfvldeha
      181 rnavpgmavl yerlvtahpg apvfylstga wnvaptltrf lsrhlypagp llltdwgpta
      241 drwfrsgreh krvtlarlar efpgvkwllv gddgqhdqei yrefaaahpq nvagvairrl
      301 sptqavlags lpapagessa gpvgqkwlsa pdgaglwkll rdarlv
//
LOCUS       WP_357562257             319 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562257
VERSION     WP_357562257.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..319
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..319
                     /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=34496
     Region          59..317
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msdlplvqpd ravpppaatt vptggrgrrv rllsrtdrvv valmvavpll lvvglvwlpa
       61 satvalsgtd wdgigplgdi ewvggrnyad vvqnyppfvp avrnnllwla alfvvatpfg
      121 mflavlldke lrgtrfyqta lylpvvlsla ligfvwqlly srdqglvnal lgtdvdwygd
      181 pdvniwavlv aagwrhvgyi mllylaglkg vdpslreaaa vdgaseartf frvvfpvlrp
      241 vnvivlvvtv ieslrafdlv wvinkgrngl elisalvtqn vvgeasrigf gsalatvmlv
      301 vslvfitvyl atvlregrr
//
LOCUS       WP_357562439             208 aa            linear   BCT 28-DEC-2024
DEFINITION  NuoI/complex I 23 kDa subunit family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562439
VERSION     WP_357562439.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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 208)
  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..208
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..208
                     /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=22552
     Region          20..170
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
ORIGIN      
        1 mvgmtdrser sepggtdpdr glpgaglvkg lavtlktmtr rsttqqypdv apelpprsrg
       61 vialleenct vcmlcarecp dwciyidshk eevavpgaar prqrnvldkf didfslcmyc
      121 gicvevcpfd alywspefey aeydikdllh dkdhlgqwma tvppppahdp hgepakeeta
      181 aarkaavpaa paarpaapav rpepeaga
//
LOCUS       WP_357562300             537 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562300
VERSION     WP_357562300.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 537)
  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..537
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=56043
     Region          131..387
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mekwwsartg grwprqavrr rladlllwga taapigyagv tpphsrhaia ltlgalllla
       61 vavavsrrwp vaalivtvlg sllngnflfa ipvfsylagr rgatavpaav afaaiaaggt
      121 vlnlgllgtg aatwfllast llfagvlpwl vgryrrqqaa ltdagrrhve ardrerrgda
      181 ervrlrerar iaqemhdslg hdlslialra aalevaadlt prhraaatel rasvaaater
      241 lhgiigvlre pdgtattrpa desvtelvdg areagmavrl dgadalaqlp pmaayavhrv
      301 vrealtnaar yapgapvtvv laadgdrvea avvnapppag plpgpassgs gllalaervr
      361 laggaltagp rtgggfavra rlpvagrpet dglpppgadp psagdpwpva tadevgrpgt
      421 geglgeaerr lrdarrqvrr sllvalgapa glalvlllvy ypvattgtvl rdeafarlpv
      481 gaaraelagl prrqldppag arpgcehytd gnfplaqptw rlcfvegrlv skeridg
//
LOCUS       WP_357562442             320 aa            linear   BCT 28-DEC-2024
DEFINITION  complex I subunit 1/NuoH family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562442
VERSION     WP_357562442.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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 320)
  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..320
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..320
                     /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=34659
     Region          4..320
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 mplwlelvir vggvlvaflt lpllvgqaeh kvmahmqgrl gpmyaggfhg waqlvadgvk
       61 fvqkedvtpr eadravfrla pavalvpyll vllviplgpn dlvgqpldvg lffvlavvgv
      121 gvvavlmsaw asankysllg girgaaqllg yelplvlaaa svamaagtls lsgiveawqp
      181 wwllwqapam vvfflaglae irrppfdmpv adselvfgym teytglrfaf fllaeyvgiv
      241 viaalttvlf lggwqgpfad aqlgwlwtll kvfavsflii wlrvsyprlr edqlqrlcwl
      301 vlvpvslgql vltaavrval
//
LOCUS       WP_357562467             728 aa            linear   BCT 28-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562467
VERSION     WP_357562467.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 728)
  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 728)
  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 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   4  (residues 1 to 728)
  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 728)
  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..728
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..728
                     /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=77752
     Region          9..580
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
     Region          <664..720
                     /region_name="PRK00934"
                     /note="ribose-phosphate pyrophosphokinase; Provisional;
                     cl46892"
                     /db_xref="CDD:481232"
ORIGIN      
        1 msqdrtavre raeavlrrla geharlredq wraiealvvd rrrvlcvqrt gwgksavyfv
       61 atallrerdq gaatvpgeeg rvpgeegrpg ggvagptviv spllalmrnq vesaaragir
      121 artinsanld ewdeitaeih agavdvllis perlnnpdfr dtvlpklagt tgllvvdeah
      181 cvsdwghdfr pdyrrlrtfl gnlpertpvl attatanarv tadvaeqlgd alvlrgsldr
      241 eslrlgvldl pspahrlawl adhldrlpgs givytltvaa agetaeflrs rgyavasytg
      301 qaedadrraa eqdlldnkik alvatsalgm gfdkpdlgfv vhlgappspi ayyqqvgrag
      361 ravahaevll lpgaedaaiw ryfaslafpp eeqvravlaa lhpdrplstq alepivdlrr
      421 arlelmlkvl dvdgavrrvr ggwlatgepw vydearlrrv aqartaeqqa mreyattpdc
      481 rlrylrecld dagaadcgrc drcagplfta dvsdvaltaa qtflgrpgve iapkklwptg
      541 leavgvplkg riapaeqalp gravgrlsdl gwggrlrdlv gpeaadvavp ddvaaavvev
      601 lkawahgder wprrpvgvva vgsrrrprlv gslaeriatv grlpllgqvt pggaaaggsr
      661 gnsaqrvral hgaltvpddl agalagldgp vllvddlvds gwtmtmaare lrragapdvl
      721 plalavag
//
LOCUS       WP_357562479             399 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC047074].
ACCESSION   WP_357562479
VERSION     WP_357562479.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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 399)
  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..399
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..399
                     /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=42545
     Region          18..395
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpyphgglgr hpnlppgerl rvllveddeg daflvgella etnsmidlvv atslsaarqr
       61 vtgvdcvlld lglpdaqgld glrqvlemas gaavcvltgr sdehlgivav aegaqdylvk
      121 gqvdgvlltr alryaverkr adenarrlre velrqaesar lergllpqpl mttdavavht
      181 fyrpgrhaal iggdffdvvq trpdrleliv gdvcghgvde aalgvelrva wralilagvp
      241 ddevlpaleq vlmserraqe ifatvatarl dldanratvr laghppplll aggkvlpvpa
      301 psglllgvrp rrpvaydlef dtddwsllmy tdgliegrig egderldvpg lsglladpat
      361 lavplaelpa wlvgraeqin ggpladdvam llvsrgggr
//
LOCUS       WP_357562473             452 aa            linear   BCT 28-DEC-2024
DEFINITION  TrkH family potassium uptake protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562473
VERSION     WP_357562473.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 452)
  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 452)
  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..452
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..452
                     /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=48794
     Region          16..447
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mvekedclvr rffrhpvrlv pigflvtill gtgllmlpwa tseyrytpfl talftatsav
       61 svtgmavvdt pnywnefglv mitvltqvgg lgivtgatlv ivvvarrlgl rsrllvqaet
      121 aefgigdvrr lllriaglal aceavitail tarlwiaydh pfgdalwgsv fhavqafnng
      181 gfalytdnli gfstdawvtl plaigtivgg lgfpalfeav rewrqpsrwa vatkltvwgs
      241 ltllvvgflg llvvewanpr tlgsyswpek llvafaqdaf irtggfnvvd vehledesfp
      301 liialmfigg gsastaggik vatffllafv mwaelrgepd vtvghrrvat asqrqaitva
      361 llsvalvvcg tvllifltdg vryyqalfev tsaftttgls vgvaatlpen gqlalivlmf
      421 vgrvgpltlg saialntrrr lyrypeeqpi vg
//
LOCUS       WP_357562474             222 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562474
VERSION     WP_357562474.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=23459
     Region          <11..207
                     /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 msarktdggs vvviglgrfg chlagsltal dhevlaidrs peqvqrwsaq ldrvvqadat
       61 eegamrqlgv adfgravvai gasveasvls vlalaelgvp qiwaratstk hakildsvga
      121 hhvifpeaet gervahlivs rmldfiefgd dfaiakvcap evmvgrplae ltpterhgvr
      181 vvgvklpger fryatdttvi asgsmliveg digqvqrfaa ls
//
LOCUS       WP_357562509             291 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562509
VERSION     WP_357562509.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  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 291)
  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 291)
  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 291)
  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..291
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..291
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31124
     Region          40..258
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 marsrkvtvs tdahghtagw aetgltppap pepdptaaaf fdvdntmmrg asiywfargl
       61 aarnyfttad larfgwqqlr frllatehag dmsqakaaal afvegwrvdd verlaeeifd
      121 elmapriwgg trqlaqrhld tgervwlvsa apveigrvia arlgltgaig tvaeivdgay
      181 tgrlvgdlmh gpakaeavtq laavegldlg rctaysdsyn dlpllslvgr gvavnpdgal
      241 lkearrrgwd vrdfrtgrra vkialpstaa aglvagavta glalhrrrrd g
//
LOCUS       WP_357562521             428 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562521
VERSION     WP_357562521.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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..428
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..428
                     /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=44936
     Region          <103..406
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mewavtvava vglavgviag vllprfvpal agratragsr sgfpytwgrp piaedpqsgt
       61 grrtidslra gvvvldpddl pvlvnpaara mgllrtgptp gsivphplir tlagqvrrtg
      121 vrreieldlp rgrdnagvnp lgvhlramgi gggyiaveaa dvteshrlar vrrdfvanvs
      181 helktpigal qllaeallda tepagagapd lsedlvaarr faeriqhest rlgrlvqell
      241 eltrlqgaep qpppepvaid wviaevidrt rtsaaarrid vtadverglt vhgsdtqlat
      301 avsnlvenai nysgadtvvr iaaraagehv eisvadqgig iaptdvdrif erfyradqar
      361 srstggtglg laivkhiagn hggrvevsst lgggstftlr lparppeeil atlpsagiea
      421 gpaelrqv
//
LOCUS       WP_357562543             329 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562543
VERSION     WP_357562543.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=36016
     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 mraarlislv lllqaretmt agelarelev sertvyrdvl alsaagvpvy adrgraggyr
       61 lvggyrtrlt gltrdeaeal flaglpgpag dmgladavas aelkvlaalp ptlrdapart
      121 gqrfhldvpg wfrevgpppw ltelagavwr drvvelryrr gdrevartlr pyglvlksgv
      181 wylvgrvgdd vrtyrvdrvt gvevsdetfd rdegfdlegh wraraeafqr gmlreratvr
      241 lspaglrrlr hladapfayd eavagadgpd gqgwvvtrlp vesvdvayeq llglgpevev
      301 ldppelrarl aeaaartarr yagagpdqr
//
LOCUS       WP_357562552             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562552
VERSION     WP_357562552.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   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 265)
  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..265
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..265
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27732
     Region          4..264
                     /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 mnkievngts layddtgsgt pvvllhagia drrmwreqig plaarhrvia vdlrgygdse
       61 lppapfahhd dvaglldald ipsaalvgcs fggavavdva lahpqrvtal allgtavsgh
      121 ewseeanelw erlvgevdpe dfvasaagev rfwvvgpgrd pedvdpelia fatemdqral
      181 aaelalsavd vaeldppaig rlaelrmpvl vtagaadvpd isrladqiaa eapyatrlpd
      241 vpaaghllpl erpapvnaal ldflp
//
LOCUS       WP_357562577             208 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF47 domain-containing protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562577
VERSION     WP_357562577.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..208
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=23670
     Region          5..208
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mkfsfrpneg afyelftraa qnlvkgtell nelslpgvev qsvserltev ehdsdqithe
       61 lykkinstfi tpfdrediyr lgsllddvmd hleavgnlly lygltklpsl premhemvnv
      121 ldaqakltad amprlksmkd ledywiecnr lendgdqvyr mllvrlfsge ydaltvlkmk
      181 evadeleaac dafehvantv etiavkes
//
LOCUS       WP_357562580             112 aa            linear   BCT 28-DEC-2024
DEFINITION  GroES family chaperonin [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562580
VERSION     WP_357562580.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 112)
  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 112)
  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 112)
  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 112)
  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..112
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..112
                     /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=12058
     Region          12..98
                     /region_name="Cpn10"
                     /note="Chaperonin 10 Kd subunit; smart00883"
                     /db_xref="CDD:197951"
     Site            order(12,14,16,19,50..51,63,73,78,80,96..98)
                     /site_type="other"
                     /note="oligomerisation interface [polypeptide binding]"
                     /db_xref="CDD:238197"
     Site            30..43
                     /site_type="active"
                     /note="mobile loop [active]"
                     /db_xref="CDD:238197"
ORIGIN      
        1 mtvdqnldsg lpirllhdrv lvrmegsege rrstagivip ataavgkrla watavgvgpn
       61 vrsivsgdrv lfdpddrsev elhgrgyvll rerdvhavaa ervendstgl yl
//
LOCUS       WP_357562598             339 aa            linear   BCT 28-DEC-2024
DEFINITION  glutathione S-transferase family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562598
VERSION     WP_357562598.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..339
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38076
     Region          11..313
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mrtggryvep ggeftrdqry iatritadgr dgwpvqpgry rlavsracpw anrliivrrl
       61 lgledaisma vagpthdkrs wtfdldpggr dpvlgierla dayfarfpgy ergitvpaiv
      121 dvptgqvvtn dfgrmsldls tewtayhreg apdlyperlr deidevsavl frdvnngvyr
      181 cgfagdqaay erayrrlfdr ldllggrlag qrylvgdtit eadirlfttl vrfdpvyhgh
      241 fkcnrsklte mpvlwayard lfqtpgfgdt vdfdhikrhy yevhrdinpt gvvplgpdla
      301 nwltphgret lggrpfgdgt pppppppter vtpthtplp
//
LOCUS       WP_357562614             207 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562614
VERSION     WP_357562614.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  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 207)
  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 207)
  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 207)
  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 207)
  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..207
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..207
                     /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=23138
     Region          59..197
                     /region_name="SpoU-like"
                     /note="SAM-dependent rRNA or tRNA methylase related to
                     SpoU; cd18096"
                     /db_xref="CDD:349969"
     Site            order(132,134,154..157,160,174..175,177,183..184,186,189)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349969"
ORIGIN      
        1 mtgdqldvgv gpwpgdppdd prydpellae gdrrnvvdry rywrheavva dldrrrhdfh
       61 vaienwqhdf nigtvvrnan aflaaevhiv grrrwnrrga mvtdryqhvr hhetieefvs
      121 waaarelpvv gidnlpgsrp metttlprrc vllfgqegpg lseparaacd qlfsiaqygs
      181 trsinagvas giamhawira hagpppg
//
LOCUS       WP_357562687             136 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system VapC family toxin [Micromonospora
            sp. NPDC047074].
ACCESSION   WP_357562687
VERSION     WP_357562687.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..136
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=14238
     Region          5..130
                     /region_name="VapC"
                     /note="Ribonuclease/mRNA interferase VapC, contains PIN
                     domain [Defense mechanisms]; COG1487"
                     /db_xref="CDD:441096"
ORIGIN      
        1 mnglvldtsa llayasgtsv epgamltlae edpdqevwip alclgqaqle lagtpaasml
       61 dlllvaerdi qvavydaats rrvariaaaf tvsldvahai atailyrcyl vtrdrkaiea
      121 aappgldvld igetwd
//
LOCUS       WP_357562714             574 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562714
VERSION     WP_357562714.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 574)
  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 574)
  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 574)
  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 574)
  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 574)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..574
                     /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=57504
     Region          68..566
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mgrvsttprr agvalavlta llvsgcsgpm drrpdpapts pavaatptpd asdpaaraaa
       61 lvgtladedl vgqvlmpyay gdaatrvtpg saagnralag vdtpaqmvek yrlgglilvg
      121 fsaddptkgn qettnvdnpk qvraltdglr gaagrlpagq apfligtdqe ygvvtritdg
      181 vtllpsalaa gaagkpglte aawrvagael aamginldfa pvadvlatrs tvigsrsyga
      241 dpkatagqva gavrglqaag vaatvkhfpg hghsaadshe glpvlgqprr tletgawppf
      301 sagidagama vmsahldars vdpgtaatfs hklltgvlrg qlgfqgvvit dgmnmppakr
      361 wspgeaavra lkagndlilm ppnvgqaydg llaalrdgsl prtrlveaat rvltmklkla
      421 drptpelstl gapahrkave elaaaavtml rgacgkgvkg pvtvtssggr dhtraaltea
      481 ltaagvkvvp aggtvvhlvg ygdgtgdlra daavtvamdt pyvlakaksp tllatysssr
      541 asmtalagvl agkarpggrs pvpvtglpat tcga
//
LOCUS       WP_357562742             163 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562742
VERSION     WP_357562742.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 163)
  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 163)
  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 163)
  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 163)
  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..163
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..163
                     /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=17373
     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 meltlapmta defarlreph vrsyaeavvt argltpadal eraetqlres lpdgvatvga
       61 llrvarvgdv evgwiwvglp rdsggpagpd tawiynvevh pghrgqghgr rmiqlieael
      121 aalgvpelgl nvfgsntvai hlyrglgfqv aaqqmtkriv ppg
//
LOCUS       WP_357562793             231 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562793
VERSION     WP_357562793.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=25328
     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 mnrtdrlyal veelravspr prsarwlagr fevstrtier digalqesgv piwaepgrtg
       61 gyaldrartl ppvnltpvea vamavalhrm rgtpfaaaag talrklisvm paadaaeahr
      121 latrvhligd gpvtpvpaav adavrarrvl riryadraga gslrdveplg ylgnprhwyl
      181 lgwcrlrdgi rafrtdrits vtvlaerape relaaddidi prervrrlsl v
//
LOCUS       WP_357562861             106 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562861
VERSION     WP_357562861.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=10493
     Region          2..86
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 maylflvlai aaevagtsll katngftrlw ptvaliaayi tafvllsqav kgipvavaya
       61 mwsglgtaai vaigaaflge pltvtkvvgv glviggvvvl nlggah
//
LOCUS       WP_357562875             375 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562875
VERSION     WP_357562875.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 375)
  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..375
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..375
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41263
     Region          13..>52
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mtgrgrsaph rgevtgylfk liresipltq eqlavdlgvd rvtvqswesg rrpfsavplg
       61 qaiavrhrlg rlgantvlla alddaaeadl vlaavldeqv drcdiaeqpl gwsvlthrlt
      121 dlilwavlgq aptfarglsi arprrgpvas gpalpvderr vffmnlhvla eraaagrnrn
      181 vllhrqacfv agmdptkaaa gwltqttard rrlntfrtws plwpearsvv tslanqgdpe
      241 plrdfiarah pddaceraal nysaywvgei pyrhrddsfm pealadwhgs illrhlvqrl
      301 epghpfvdln ihniwallta rrgltvdspa aaralldrsv plldsdrisa qsrqeltsiv
      361 yslradgltg rgtgr
//
LOCUS       WP_357562901             674 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562901
VERSION     WP_357562901.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 674)
  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 674)
  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..674
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..674
                     /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=69849
     Region          1..456
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          606..671
                     /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(628,637..639,646)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            638
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mitrllvanr geiarrvlat cralgvetva vhsdadadap fvaeadqavr lpgntpaety
       61 lrielildaa rragadavhp gygflaenae faaavtdagl twvgppakai aamgdkmaak
      121 allaeagvpm lptwtdadei tafpvlvkas aggggrgmrv vrdaaalaea vasarreatg
      181 afgdgtvfie ryvergrhve vqifgdthgt vvalgvrdcs iqrrhqkvve eapgvlphev
      241 rmalheaava agravdyvga gtvefllasd geiyflemnt rlqvehpvte lttgldlvrl
      301 qllvaegepl pvaatppaqg haievrlcae dpaqgyrpat ghlhrfavpg vvaefgplag
      361 pglrldsgvv dgsvvgvhyd smlakviawa ptraeaaral agalaraelh gvttnrdllv
      421 rvlrspefga vdvdtgfldr hpevfapllp adelplvala aalataaarr adapvlagip
      481 sgwrnvpafp qvtrfaapdg eievryrldr sgglaewaal pdagstalad esapdaaspa
      541 daptsvvslv gaapdrvvld vdgvrrayrv hrassevfvd gpdgatslte lprfpeptae
      601 laagslvapl pgavtrvhve vgqrvaagdl lltleamkle hpvlapadgv vaelpvaagg
      661 qvdtgavlav vnpe
//
LOCUS       WP_357562902             533 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Micromonospora sp. NPDC047074].
ACCESSION   WP_357562902
VERSION     WP_357562902.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 533)
  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..533
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..533
                     /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=57047
     Region          21..531
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mttlrsvvda aspghranre allerlaeld aeldrarsgg gekyvtrhhk rgkllpreri
       61 ellldrdspf lelspvaayg tdfpvgasvv tgigvvegve clivandptv rggavnpwsl
      121 aktrrageia ltnrlpmvnl vesagadlpt qaeifipggr vfrdltrlsa akiptvsvvf
      181 gnataggayv pgmsdhvimi rdrsqvylag pplvkmatge vtddeslgga amhastsgla
      241 dflasderdg irlarqcvrr lnwrkqgpap rnprpaqpry dpeellgias adlkvpfdpr
      301 evlarvldgs efdefkpayg talvtgwgel hgypvgvlan argvlfseea qkaaqfiqla
      361 naadtplifl qnttgymvgt eyeqrgiikh galminavsn stvphltvnl gasygagnyg
      421 mcgrayeprf lftwpnaksa vmgpaqlagv lsivarqaaa argrdydeds daamrmmveq
      481 qiesqsgalf lsgrlyddgv idprdtrtvl glclsaihng pvrgadgfgv frm
//
LOCUS       WP_357562911             209 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562911
VERSION     WP_357562911.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 209)
  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 209)
  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..209
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..209
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21695
     Region          72..204
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msanrrlaal lvpvllavgg ctagteekdp gpsarqkaaa srpspfqdcs algtpppsaa
       61 pavpagggga alpelslecf tggasfalre lrgpavinvw aswcppcqee lpafqrlser
      121 aagrlhvigv nnqdsreaak gigedfglrf pvlfdqgesf kralerkaip vtvfvdgqgr
      181 vrhvdtsgal ddarladlvr qhlgltvpa
//
LOCUS       WP_357562922             318 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562922
VERSION     WP_357562922.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (residues 1 to 318)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..318
                     /product="GlxA 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=34339
     Region          3..318
                     /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 mlrsvavlal dpvatfelgv vtevfgtdrt adgfpgydfs lcspdggpvr tssgfhlipn
       61 adlgpveead lvavpahhhs tvpatvltal rraadrgayv lslcsgafvl gaaglldgre
      121 ctthwryvde lerrhptarv rcnslyvqdg rlitsagtaa gidaclhlvr qehgsatatr
      181 larrmvvpph rdggqsqyie apipktpeap tlepvlewlm ghldrpvtvd elaaragmap
      241 rtfarrfrae tgttphdwlt nqrvllarrl leetgltvea vadragfgds aalrhhfarr
      301 vgatphryra afrdrvga
//
LOCUS       WP_357562977             198 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357562977
VERSION     WP_357562977.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=21591
     Region          6..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          90..176
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(93,106,108,119,124,128,162,164,176)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mengfdqalg avgprlralr rqrettladl saatgisvst lsrlesgsrr ptlelllpla
       61 rahgvtldel vdapptgdpr ihlrpvtrhg mtmlpltrrp ggiqayklvi pgggrraepd
      121 pqthegyewl yvlngrlrlv lgdqdmvlvp geaaefdtrv phwfgaagae pveflslfgr
      181 qgerahlrar prnprppg
//
LOCUS       WP_357563002             408 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563002
VERSION     WP_357563002.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 408)
  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 408)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 408)
  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..408
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..408
                     /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=42786
     Region          131..399
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtvnrtilgr plrsvafdvf vvamvmlfgl vtavsqpggw ratlvgaama vallfrrshp
       61 savaavvaal glvqlaagwg plafdvavlv alysvvkyad rlrdgilagv gagvgvvlaa
      121 lqtrgdvaww ataiyfglvt gavwlvglnv rtrhlyvlsl eeraatlere reaearaava
      181 gertriarel hdvvahgmav mivqadgarf mldrdpetar qamkvvgdtg rqaleemrrl
      241 vgvlrepspf daagepdgag vaadpahrrl altelptlld rfraaglrar htvtgqpppm
      301 ppgleltvyr vvqegltnal khagvgarve vtlvhaddav vvrvvddgrg qtpvapapsg
      361 ghglvgmrer vgvydgslta gprlaggwqv earlplpsts gatevaaa
//
LOCUS       WP_357563075             253 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563075
VERSION     WP_357563075.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..253
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27894
     Region          12..236
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtwflsaggw hpapvqlfcl pyagggasvf rrwqdelgpd vevlpvqlpg renrisenpv
       61 fqvgdvadav herirgpyai yghsmggrvg fevvrelrra grplplrlyv ggaraphvtg
      121 qshfdglsrl dddqllrrlq eggglpagll ehrelvelll pllradfgrv dgyryvpdep
      181 lpmpivafng rddhsvtseq sdgwrehtaa gftlheidgg hfflnerlpd llatiradla
      241 aalaeesarr hha
//
LOCUS       WP_357563128             285 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563128
VERSION     WP_357563128.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 285)
  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..285
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..285
                     /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=32445
     Region          8..252
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mvgtgggrlv aisdlhvvhp dnravvealr pgheddwliv agdvgefvnd iewalrllsr
       61 rfakviwspg nhelwtprdd pnqlrgeary rhlvqlcrgl gvvtpedpyp iwdpegdpvl
      121 vaplfllydy tfrpagtytk eqalarahet gvvctdeill hpdpyptrda wcrarvreta
      181 erltaeragl ptvlinhwpl vreptrilrf pefaqwcgte ktadwhvrye arvavyghlh
      241 iprttwydgv rfeevsvgyp rewrrratpp gqlrtilpap agrpa
//
LOCUS       WP_357563148             139 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563148
VERSION     WP_357563148.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 139)
  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 139)
  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 139)
  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 139)
  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 139)
  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 139)
  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 139)
  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..139
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..139
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15404
     Region          21..139
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 makpadtrta grkpvakatr saaetekiha alaarrdelr aeydrtlsei telqrdrltd
       61 sagddqadtg tktfereqei slansileri tqveralerl deggygwcer cgnpipverl
      121 aafpsatlcv tckqleerr
//
LOCUS       WP_357563182             209 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563182
VERSION     WP_357563182.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 209)
  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 209)
  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 209)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..209
                     /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=21315
     Region          7..133
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
     Region          114..>196
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
ORIGIN      
        1 mgaftwavaa vvtddagrvl lcrqgrgerr halpggrlrp aespvhaaar hiraetgwev
       61 evvdlvgiyh ltgtcgpppa ghagplpdvl vhvfrararg tgpagdpmgg crlswhhpga
      121 lpealtpttr aaltdaladr sgvlrhatpt spaplpptpd epapgdpatv ppatggpatg
      181 lsttgdpapt tnhppgqrtt pptthmthp
//
LOCUS       WP_357563204             294 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563204
VERSION     WP_357563204.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..294
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32065
     Region          12..292
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msqagvavgq aavdqllevl dlehtggmtf rgmsppvgpq rvyggqvagq alvaagrtvd
       61 parfvhslhg yfvrpgdpae pityevenir dgrsfsvrrs valqhdkpif fmsasfqrae
      121 egldhqaptp pdvpgpdevp tmsdrlaryp erlgiwaqip rpidvryvge pgwvrpgdrp
      181 aephqrvwmr idgklpddpl lhacaltyas dltlldsvls vhgevwgpgg vvgasldhal
      241 wfhrpfrade wflydcwsps asgarglatg rmftadgrhi asvvqegllr rvgd
//
LOCUS       WP_357563239             171 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563239
VERSION     WP_357563239.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 171)
  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 171)
  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..171
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..171
                     /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=19032
     Region          1..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 myrrrdtpra rliaeisael rrysvdaqhi ghafaglhgl natdlqalia vmdaelfgqp
       61 itpgrlgeql nlssgsvtal idrleraghi rrdrdtadrr kvflhyaerg allakdffrp
      121 lgrrtdevma gfsddelavv hrfmvamtts mgehrdavra ardeparran g
//
LOCUS       WP_357563304             203 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563304
VERSION     WP_357563304.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 203)
  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..203
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..203
                     /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=21874
     Region          16..199
                     /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 mdyghserpa gatplptaik ilvaggfgvg kttmvgavse trplrteevl tesgvgiddl
       61 sgvesktttt vamdfgriti sddlvlylfg tpgqdrfwfv wdelalgalg avvladtrrl
      121 adcfpsidyf egrgtpfvva vncfegsrqy rldevqsaln ldpgvpvllc darkresske
      181 vlitlmeham ktrearrrag ttg
//
LOCUS       WP_357563342             240 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563342
VERSION     WP_357563342.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=23466
     Region          7..238
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdfafpaget vvvtgagsgi gratallaaa aglrvaawdv aaravagtad eivagggaav
       61 altvdvadsa avraalaasg parylvnnag passadldfd ralaltvgsv rtvtdawlag
      121 rtgagaavvn vasvagnlvg tdsawycagk aaiagytrhl atrrapavra navapgliet
      181 prtagfaatd lgrdlvarnp mgragqpaev ahavlfllsp lagylngvll pvdggwtvtq
//
LOCUS       WP_357563357             396 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563357
VERSION     WP_357563357.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 396)
  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 396)
  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 396)
  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 396)
  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 396)
  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 396)
  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 396)
  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..396
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..396
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42267
     Region          108..251
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mtvtehvrps aapetaaqvl saeqryagel aflaayddga rppgwaltpr avvtfiqgsn
       61 gealklpadr rtgpggtelp asmtippkfv gerslvercv vtlagergll lvgepgtaks
      121 mlsellaaav cgtsaltvqg tagttedafr ygwnyallla qgptpqalvd spvltamrtg
      181 rvvrieevtr clpevqdalv silsdrrmnv pelsgtedgl iravpgftvi atanlrdrgv
      241 semssalkrr fnfetihpis dadtetnlvr qqataavqra gaayavddav ldalvtvfrd
      301 lrsgrstegw dverpgtvms taeavqvavs lglsaaylpg gdaldlvpgh llgvvrkddq
      361 ndharllgyw dgpvrrraed gsamwrrlwd lreslr
//
LOCUS       WP_357563362             268 aa            linear   BCT 28-DEC-2024
DEFINITION  M23 family metallopeptidase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563362
VERSION     WP_357563362.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 268)
  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..268
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..268
                     /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=28287
     Region          11..182
                     /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 mqtfdetspg egtasrgidr rhllglvtat laagiipeaw laeaaygatp rwnrpfdkwv
       61 pitssygmrt dpitgvsrmh ngtdysasgi lgypirsiaa gtvtgvsysa sglghnatit
      121 hadgwrsvyg hmreaprvgt gvqvaagqhi gnvgstghst gphlhleifq pngqrinpes
      181 vltgapyaga pgtppeivtk dglmyliwst ggtgylvtpn rviglrsmah ynlfkriins
      241 nqaaaqpevf naleidqina ylngtvpa
//
LOCUS       WP_357563374             402 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563374
VERSION     WP_357563374.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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 16985460
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..402
                     /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=40919
     Region          62..118
                     /region_name="Inhibitor_I9"
                     /note="Peptidase inhibitor I9; pfam05922"
                     /db_xref="CDD:428674"
     Region          135..381
                     /region_name="Peptidases_S8_PCSK9_ProteinaseK_like"
                     /note="Peptidase S8 family domain in ProteinaseK-like
                     proteins; cd04077"
                     /db_xref="CDD:173790"
     Site            order(138,141..142)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173790"
     Site            order(166,197,256..257,284,344,347)
                     /site_type="active"
                     /db_xref="CDD:173790"
     Site            order(166,197,347)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173790"
     Site            order(298,300,323)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173790"
ORIGIN      
        1 mtlgrswrtr llaltattaa glatvvaips palaagapfr akpvpitapa vdenttlipg
       61 aylvtfrega dpnvalralk agarvsfgea vngfaanlss aqvtelqhss dvvrierdaw
      121 hsnvldatqt nppawgidri dqttlplsas ytytatgagv hayvidsgid ashpnfggra
      181 qfnynaidtn ntdcnghgth vagtigstsy gvakqatlhg vkwlncaggg stsgavaavn
      241 wvtnnhvkpa vantswnaay satlataltn mmnagvflat sagntggnsc drlprnltas
      301 lvvaattstd arasyssigt cvdiygpgsa ivstvpgnat asyngtsmat phaagiavly
      361 katygdasqa tvhtwivnna ttgvvtgsls gtpnrllnkk tl
//
LOCUS       WP_357563366             493 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563366
VERSION     WP_357563366.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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 493)
  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 493)
  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 493)
  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 493)
  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..493
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..493
                     /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=51623
     Region          143..477
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mhrrllvvlv plavllvaal gvplgitvae remqetyvdr lndvgrfasl adtalqtgrt
       61 eaihqdltry helygdpvav idtsgrvllg pvgayqeaar sepalpqivt aalagarsep
      121 sgewapwhds hlvvaepmgr dsevvgavva iadlsktrqh ilvrwarlag igllplfalv
      181 avawpvsawv lrpvreldaa tsrisqgdlt iradaeagpg elrrlaesfn tmmdavenav
      241 qrqrafvsda shqlrnplts lrlaveslap hlaptgqgaq myavavdelk amqrmlnslq
      301 asarmeslrt aspvdldavl atrvdrwral tatagqtlsv dvspglrlme ppgglgsvld
      361 elisnalrls gaqvvavtar avpgggagtg padgpagelv miavrddgqg ideserakal
      421 rrfwrsprhq nvagtglgla icadlvgaag gvlrledglp rpdgsghgfa avltlpivap
      481 vasppaavps tpg
//
LOCUS       WP_357563384             844 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563384
VERSION     WP_357563384.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 844)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 844)
  AUTHORS   ter Beek,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 844)
  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 844)
  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..844
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..844
                     /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=87674
     Region          1..841
                     /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          144..389
                     /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 mawrslrsrw faalgsvvai algaalvtga milqqsssaa tpggvstpwq lrdvevvvrm
       61 pneatdgkgr tilltdrrrl tdaqlatira tagvaavtae tpspayvvvd grkigdaekr
      121 swahpwstav vepfalaqgr ppnqadelvl drstaeeagv gvgdrvtlst trgastyrlt
      181 gvgdwpgsqf ehavfvadrq aaqlggdpll alvdvtgdpa avarnlrrsl peaevtldra
      241 halfldrrqa elsggsgqfm avmatsalsi aalviastls vsvmqrrrei allrtvgatp
      301 grirrlvige aafmglvagt agavagvglg avairffaaq gmvsrstelv vgltplvvsv
      361 gvalvtavla gslpawkasr vapaeamrav dvqpaqsgra rviwgvlmlt vaagfvtaga
      421 vtartggfta vdvagvlflm sapflvlaav llgrallagi lavvrpllar sfggflatrq
      481 irsdlsravg vttplmlmva facllifqee gtfeararny erqlridlav rgseqlglps
      541 elagrvseld gvraatgmin triglpdgam svtsldvvav dpatvptlfa leahagdwsa
      601 fgddgiaver giaeaqgwqa gekakvllpd gtpsqatvat vfeadsatfs vfvprsmvlg
      661 hmlepydagv lvalepgaeq aavaaridal rtvdpdvral tkaeymsflr aqssgdtwii
      721 ylfviliggy agiaainvlv tsamarrgqf allrlagaqp ghvvravvwe taiivlggll
      781 lgtavaavpl lgygyiftht lwlpfaagqy alicaaalli gvvggvvpar lvlraralda
      841 lnap
//
LOCUS       WP_357563396             288 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563396
VERSION     WP_357563396.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..288
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..288
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29674
     Region          41..260
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mshrsrpvpr lsasacaavl avaailspga pasarsaaed spstsadgaw dspgpyatav
       61 qvgavntlyy prdiaastrr hpvivwgngt gaaplvyrdl llrwashgfi vsaantptsn
      121 lgismrlgid alteadrnpa svfhgrvdla higasghsqg gaaaivvgad pridtvlpiq
      181 pgpladidav gvpaflmagq kdsivfpilv ksfyddadhi paiygevrga dhftvvgdpg
      241 pfaapttawf rfhlmgdaaa gaefhgpscg ictdtqtwsd vrrnalvp
//
LOCUS       WP_357563410             249 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563410
VERSION     WP_357563410.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  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..249
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..249
                     /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=27271
     Region          61..210
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 martasanas spgpsqaghd ghtaepllsa lgaasgsesl lerafteale raddndevat
       61 rildaayeqf crmgirrstm edvarragvs ritayrrfat kdrlveqvvr refrryfdqf
      121 lldiqqaptv ddrvvlgfvs alqafrrnpl igglmtaepd vlvpsmisdg grtlatvqrf
      181 vagqlrreqr agnipatadv evvaelmtrl scsflvtpsh vvdlddaeql ravarrflvp
      241 mleygsqse
//
LOCUS       WP_357563425             398 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563425
VERSION     WP_357563425.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 398)
  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..398
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..398
                     /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=42902
     Region          13..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          215..369
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrpaangtsp vatkrpkdrk drialagael fcergyhrvs vdeiaavvgi sgpavyrhfp
       61 nkyailvhat revvgallaa tadpqtgtte gvldellgtl agvavskrrv aglyqwegry
      121 ltpehrrefa atmttlvgrl aaplrelrpe ltagqaellv naalsafgsv atyraaatgt
      181 dteqlltrva wtllradapq vppqpraapg taplrpasrr elllseairl fhrhgyhava
      241 vedigraagm qassvyryfp skadllaaay yratdrltga ttaaiaeasd ppdalrrvvq
      301 ayvafafgqs dlvavylaen nnlpdedrhq lrgaqrshve ewvrlvgtvr pdlpaadarv
      361 lvhaalnvvt digrlgrfdr tegydaqtvr lalavlrs
//
LOCUS       WP_357563431             622 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563431
VERSION     WP_357563431.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 622)
  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 622)
  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..622
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..622
                     /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=66188
     Region          15..613
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mdpaetlaer caktaadltv pallhrnate fadlpalttf drddtrtwae lrdevaelsg
       61 glaeiglepg rhmlimmssr pehwlvdlaa vhlgavpsti yptlstdqmr ylalhsgaqv
      121 lvlegpaala rwrsilpdlp hlrrvvlvde adpgdttpet vplsqvrslg raahqadpda
      181 ferrwrevrp eqpvtllyts gttgepkgvv lshhnviyqa vsleanvsvp dhapsvaylp
      241 lahiaerflg iynaiyragh vticpdatql vaalravgpp sffgvpriwe kmaagvqahl
      301 agaepavqaa fsaasatale ayglraagqp vpdelaarla qveaavlrpi qstlgmhnmv
      361 wagsgaapip vevlrflagl gvdvlevwgl tettgtatin tpdrfrtgtv grphigmevr
      421 laddgeilvr gplvcsgylr gdgsvepvvd adgwlatgdv gtidddgflt vtdrkkelii
      481 tssgknispa hiegllrahp ligqavaigd rrpyvtaliv lddevapqwa rargiseaql
      541 pglasdplll aeiqaavdaa naslarpeqv ktfqvlpssw tpesgeltpt lklrrrvivd
      601 rygesidaly gsagvavesa tg
//
LOCUS       WP_357563440             391 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563440
VERSION     WP_357563440.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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 391)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..391
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..391
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42259
     Region          41..373
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mtstltrrhl laaalatgva vplgdagrgw aaapggparl tlppptgphr vgtvslhlvd
       61 rsrpdpvagp ghcrelmasv wypaardarr hpvvpwmpaa plrallgsag fdadaaaapl
      121 taghegapal rtpgrlpviv fshgndghra eativvqela shgyvvvtvd htydgfsefp
      181 dgrltvpldl sftpwdsthd irfvldried laagrnpdae rrplpaglga aldlrrigmf
      241 gwskgatata lvmnqdrrvr aglgfdgpmq sqppvtdldr pfmlmtaeft raaepsverf
      301 wshlrgwrln vqadgaahss ycdhqwlipq lariigmsde dlagwigtld paravriqqa
      361 yplaffdlhl rhrghllnrp npafpevqfi v
//
LOCUS       WP_357563444             259 aa            linear   BCT 28-DEC-2024
DEFINITION  M23 family metallopeptidase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563444
VERSION     WP_357563444.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..259
                     /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=26623
     Region          <66..149
                     /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"
     Region          188..>245
                     /region_name="sporang_Gsm"
                     /note="sporangiospore maturation cell wall hydrolase GsmA;
                     NF038016"
                     /db_xref="CDD:411609"
ORIGIN      
        1 mkarslrlla vallttlggl vapstpalaa ptfkvpfpcg qawtgqtrtg hspayavdfn
       61 rtddlgdpvv asapgtvdvv tnlgdtsygr yvrinhgggy ttyyahlnaf nvsvgqtvgy
      121 gqvigsvgnt gnssgahlhy eqrlngndiq vrfngtlaly wgtrtytsdn gcsagtatgt
      181 vntagspltv rsgpgtghta vgtvadgttv tiscqttgtt vtgtygtssi wdrigtgrfv
      241 sdayvytghd gfipgvprc
//
LOCUS       WP_357563476             519 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563476
VERSION     WP_357563476.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=55524
     Region          149..513
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkpldqgkaq lrgvplrvkl vaavlalvaa allvisslta vflrgyliek vdgelhgtts
       61 svealvnlyr qgrtgqtmlp tdfmvvladr sgvgqpiydd rnlrleqlpq lpatreefaa
      121 mtgeprtvda adhrtrwril ytelkggevv avgqhltdvd lavrrlvwid llfggavlvl
      181 lasigaaivr tslkplveie rtaaaiaggd ltrrvpdpee gqsvptselg rlsralnaml
      241 nqievaftar aaselaarsa eaaardaaga aqaseararr seermrqfva dashelrtpl
      301 ttirgfsely rqgaarapeq tadllrrieq eaarmgllve dllllarldr erplslapve
      361 lpvlaseave aaravaperr ielevvpgsg plvvygddar lrqvignlmt navthtppda
      421 svtlrlraep gnlavvevad tgpgltpeqa ervferfyrv daartrragg ntgtglglai
      481 vaalvrahhg tveavetpgg gatfrvrlpl vpdadgdge
//
LOCUS       WP_357563507             181 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563507
VERSION     WP_357563507.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 181)
  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 181)
  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 181)
  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 181)
  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 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..181
                     /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=18693
     Region          6..153
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mtglsvrrag padfaavarl tvaayeadgq lkdehgyava ladvatraeh gevlvavdda
       61 tgavlgsvtf vlpgtryael srpgetefrm lavdpaaqgr gvgaalveac vsraaelgcs
      121 avvicirdgf ataaqrlyrr rgfvrtperd wtpvagvdll glrldlrpgg estvgqvvta
      181 g
//
LOCUS       WP_357563526             439 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563526
VERSION     WP_357563526.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=47224
     Region          17..343
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mpaarfpllr agadpgrrrv laallgapvl aagctedrta pvetepvels vfwyggakra
       61 eltervlrly tdrnprvgfr vtwqgadgyy grlatqaagg nvpdliqldd smlteyarre
      121 ivldlggyva dhrldlrtlp sglvrygqvd grtvgvaaaq taaavvydrt llrrlrvpep
      181 ttgmswaeyi awaqrvtrag egrvagtmda sgdarafwlw lrgqggelyq grqlgfdadv
      241 liewfelwrr arsgratpsa alikradgde parqlvvtga taasfawshq fpelqrltra
      301 dlglaalpgp peaqwhrasm ywaafrgtrh pavvadvinf ltgngeagta lgherglsps
      361 lavrsyvdas itdpaqrraa algvaladrl gpapgpppqg hprvrvllre aaesirrgta
      421 gpraatsrfm aqanaalag
//
LOCUS       WP_357563547             149 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563547
VERSION     WP_357563547.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 149)
  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..149
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..149
                     /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=15122
     Region          3..134
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 myvsarsdya lramlavaae dpvgggvlvk agalagsqdi plsflqgilv dlrragllls
       61 hrgteggyal arpaaeisvg dvlravggsl ttvrglpaeh adyegvasgl revwlavhga
      121 ialvvdrttl adllgvgqwp agaeespar
//
LOCUS       WP_357563584             411 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563584
VERSION     WP_357563584.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..411
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43558
     Region          10..411
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 madgptdrla vadavatast gsyarivasl irvtgdwtla edcaqeastl altrwpaegv
       61 panpggwlmt varnravdvl rrasverrkl relaalalte pepepgpage geivddrlrl
      121 vftcchpals pearvaltlr tvcgvstadi araflvtest mtrrltraka kiaaagipyr
      181 vptgpalaer lpgvlavlyl lftrgydadg epafadeair larlldrlip aqpevaalla
      241 lfllqhsrrd arrdrdgnll tldrqdrarw dhaaiaegva vlarvradgp yalqariaac
      301 hataasaeat dwgviagayd rlagwhpspv velnravahg yahgpaagla llaaaragga
      361 lngyplavaa eaeltarqgd reraaalfrr aadahhgaer ralldradql s
//
LOCUS       WP_357563721             487 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydroorotase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563721
VERSION     WP_357563721.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 487)
  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 487)
  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..487
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..487
                     /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=53785
     Region          7..484
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
ORIGIN      
        1 mtsfdlllrn vrvvrhdrpe pelldvgvkd griariapai eageaatvvd gggrlafpgv
       61 vdahqhwgiy nplgedtate sracaqggvt saitymrtgq yylnkggeya dffpevlets
      121 agrsyvdyaf hlapmmrrhi deipalvrdh gvtsfkvfmf ygshglhgrs adqnsflmip
      181 egerydyahf efvmrgvqaa reqfpeladq islslhceta eimtaytklv eeagelsgle
      241 ayhasrpphs eglavsiaay lahetglpti nllhltsrka vdaalrmara fphidfrrev
      301 tvghlladih tahgiggkvn pplrpredvd alweylldgk idwvvsdhac crdeqkfgep
      361 rddvflaksg fggaeyllpg mvtegtkrgl plrriaelta ynparrfglh dkgaievgyd
      421 adialvdpgv twtvraedse stqeytpfeg feltakvtdt flrgehvlvd gkvvgdpqgr
      481 yvhrarr
//
LOCUS       WP_357563770             223 aa            linear   BCT 28-DEC-2024
DEFINITION  NuoB/complex I 20 kDa subunit family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563770
VERSION     WP_357563770.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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 223)
  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 223)
  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 223)
  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..223
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..223
                     /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=24690
     Region          1..169
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 mgieeklpag vlltsveklv nwsrkssvwg atfglaccai emmaaggphy dmgrwgmevf
       61 rasprqadlm ivagrvsqkm apvlrqiydq maeprwvism gvcassggmf nnyaivqgvd
      121 hivpvdmylp gcpprpemli davlklreki gheplgpngr kmlearkarg dvpvvpygsm
      181 pssyrsdkar raewtkavre greeqlrien wmkaqnhlhg svk
//
LOCUS       WP_357563784             260 aa            linear   BCT 28-DEC-2024
DEFINITION  IclR family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563784
VERSION     WP_357563784.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..260
                     /product="IclR 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=28131
     Region          8..257
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrdplaepsd lirsvsralr vlesvgrapk gltvkqiarr celtvattyh lvrtlayegy
       61 virredgtyi vglevadryr elvtafrgpp vvgeslrraa mdtgyshylg rfvggqvalt
      121 alaegprspy ledlvpgfde gahatalgka llatltadqr frylreygmr pftsatltsp
      181 eafevdlaag drrgmqlelg qfrqgvacaa vlvspdkdme rrvvlacalp agemmtsarv
      241 vraklltaar aiadglatds
//
LOCUS       WP_357563935             307 aa            linear   BCT 28-DEC-2024
DEFINITION  ParA family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563935
VERSION     WP_357563935.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 307)
  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 307)
  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 307)
  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 307)
  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..307
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..307
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33256
     Region          52..302
                     /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 magngdraet wtselreqqa algtdlgpad paaytmrkpi pepmptdrhg pariiamanq
       61 kggvgktttt inlgaalaey grkvllvdfd pqgalsvglg vnphnldlsv ynllmqddvt
      121 aedvliktdv aglhllpani dlsaaeiqlv nevaremala rvlrsirkey dyilidcqps
      181 lgllainalt vahgvliple ceffslrgva llldtidkvr erlnfdlele gilatmydsr
      241 tthcrqvlqr vveafgdkvy qtvitktvkf pestvagapi ttldpassga rnyrqlarev
      301 iaaqser
//
LOCUS       WP_357563963             587 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC047074].
ACCESSION   WP_357563963
VERSION     WP_357563963.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 587)
  AUTHORS   ter Beek,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 587)
  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 587)
  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..587
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..587
                     /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=61159
     Region          126..381
                     /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          <464..582
                     /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 msgrlllvcr llmrdlrrrr tetvlllaai taatatltlg lalneiahrs yqqtrtatag
       61 pdvivtprat sqaaldelas mttaagvtdh sgpfpiaylt mtahgrsahv vvegrddapv
      121 svdrpavtdg twvrpggvvv erffadalgi rtgdtvsvdg hplrvigtav taaratypya
      181 rwhypnsvlv ergglvwvdr sdiatlagsq plsytlnlkl adpaasstyt vgphlttwqe
      241 ighlngrlys darmvllvgs wllnglalag vagivagrii gqrrrvgllk aagagpamia
      301 avhlaeylvi gltaavtgla agwfaapvli rpsagligsv naqppglrta iavtalalti
      361 avaatlvpvv raattstvha ladaatpprr rrwriwlsrr lptalligvr inarrprrar
      421 lvtvntlitt talvailtvn tqvvqfdlgy telanprver geqatlvlav vlcilalina
      481 vvstwtavld arqplavara lgatpaqagv glalaqllpa ipgvavgipa giglvasvst
      541 gevqylpgsw llatalgvll aiaalttipa mvatrrpvvd tlqsvpt
//
LOCUS       WP_357563969             152 aa            linear   BCT 28-DEC-2024
DEFINITION  Fur family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357563969
VERSION     WP_357563969.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 152)
  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 152)
  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..152
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..152
                     /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=15738
     Region          7..148
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mstsgadrvd aalrrsrrag lrntaarrai ldelaravgd qghltatrlh hallargltv
       61 elstvhrvla qlvelgiaht vpvgrtvtfg laddahhhav cagcgdirql paaavaasva
      121 aaraagiead psghptgvvv ygrcrrcrtt th
//
LOCUS       WP_357564001             111 aa            linear   BCT 28-DEC-2024
DEFINITION  YidH family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564001
VERSION     WP_357564001.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..111
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..111
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=11341
     Region          9..>84
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 mnserldvdv rfllanertl lawlrtaltm laggvallhl sdtrpvatat algifalgiv
       61 taiigylryr aageairagd lppsgrggvl vtvgvvviat vivavhlagl g
//
LOCUS       WP_357564025             357 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564025
VERSION     WP_357564025.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 357)
  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 357)
  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..357
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..357
                     /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=37602
     Region          2..350
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mirrltarsq ltlvytglvl aagslltavt ylllfrslql hideamskll tqaapallvv
       61 talagltgwl vagrilrpir tisgtanqls aenlsdripv rqptdelatl aatinsmldr
      121 iqhgiaerdr vlnsqrlfva naahelrtpl ttmrtaidvt ldgepdrael vamagdiata
      181 vetsqrtldg llvlarsqag pprrtpvdla avaaaavada adwaangavt lqadlrpapa
      241 sgepvllerm agnllenalr ynhasghvtv tsgtakghaf lrvvntgppv tpeeerrlfe
      301 pfvrgtgndn rgaglglsiv ravviahdge ifstarptgg mditvqlppa matptsm
//
LOCUS       WP_357564039            1417 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357564039
VERSION     WP_357564039.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1417)
  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..1417
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..1417
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=147627
     Region          131..188
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          177..246
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          235..292
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          281..354
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          343..403
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          <879..1201
                     /region_name="myxo_dep_M36"
                     /note="myxosortase-dependent M36 family metallopeptidase;
                     NF038112"
                     /db_xref="CDD:468355"
ORIGIN      
        1 mrsgrfgpwa gatvaalava llgpgagvpg aaapvraagp pgaglaagcd tfgftampva
       61 agiagprdve avdtnqngfd dllvasargd gdvhqliavg ngtfrtsvnp ggrpevypts
      121 gapgriavgy fnrdakadfa aattegvsiw agngdttfgp agllldgrsv advavadfdr
      181 dllpdlaavd pqiqsnpgdd rvrvfrnlng gafderfllg dqpsyvqpef laagdltgng
      241 vpdlllssrl qstvsmirdg rnspeprieg lgeafspaia dfdldgrlda avaiigedri
      301 rlwsdfrdpp aggtspapre lpsldlgplt peregpydvd vadlnrdgrp dlvvvayasr
      361 avyvfpgngd gtfgspavlp agsrpvyaav grfdnnqsld vavldevdis lrvylntcta
      421 pgpnlrvsgl eatqviqdlt nsvdlvadrr tvvrayvgtd aatpavtaal hgfrpdgtsl
      481 gppvapanpg rllvpdrtvr rgqlaggflf elptqwtseg evrlrvevnp drrvtepdyl
      541 dnviertvrf qaakpvrvkl irlgyqrngq tvlpaesdld raesllrrtl ptsrlevtra
      601 dyrddqpfrw inddshyldg sdarsvltsy rnatagvrep gvyhlvmvnr pqmggiadai
      661 pgwvavggsh dptiilhelg hllgaqhvec tddpgdehgr rpypyprgti ggpdlanpsf
      721 agydigdasv gaprrvvwap dtsppvadlm sycrnkwisd dlwrlwrdgv qnppaqqgat
      781 gdllalsgav gdgdatltgq rlartthrpa ttpgpyalrl ldaagatlae hpftpaaase
      841 haatrpfhev vdfvpgtrrv tlvdtragrd latlpvsanr pvvaltgdap pspvpatgpv
      901 tlrwsagdad ggpvtasiqy spdgaddwrv laggltgtsy tvdaaqlagt ggaatgrlrv
      961 rvtdgvntad atsgpltvag kaptvritap ltgtffatgq tvtlaatvtd peqgdldgsa
     1021 vrwtsdrdgd lgvgatrtpg qlsegrhvvt vtatdadgar taartevtvg rvlpaggppt
     1081 adagpdrtat egdtvtldtt rttdpdgdpv tlswavlaqp dggglggglr legpartpsf
     1141 radragtyrl eltatdarhg tttdtvtvtv anrpvevspi aldqelrvag pvtvratftd
     1201 pgvpdthrca vdwdgdgpaa atpgvvtear negvcvatgd lrpgvhvarl tvtgddggtg
     1261 qqtvrivvyd psdvtvagag aivspagals advaatgpge fafvaglvkg sptpfgattf
     1321 rlpereftft gtaherltva gsvgqyrgeg tvngrpgyay qltiydapdg rdvdrfriri
     1381 wesdggrvvy dsgrgapddl dpahlqplnq grvvvvg
//
LOCUS       WP_357564061             894 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564061
VERSION     WP_357564061.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..894
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..894
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93221
     Region          <1..894
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mlygraeeqa eidrlvdgar egrsgalvfr gpagigksal leyaalratg mqvvrgvgie
       61 seaalpfaal hlllrtgldr ihalpdaqar algaalglrn appesrflvg latlsllsel
      121 agdggllclv ddaqwcdeas vdalvfaarr lgaegvamif aarpdlpvtg lpahrlagld
      181 dtaaaallpa dlppqvrerl vqesagnpla lielpaaltp eqrtgrlspv gampvavrvq
      241 eaflsqlaal peaartallv aaadgsgela tlvaggasld gleaaersrl igingtavgf
      301 rhpliraavy qsasvsrrla vhraladali sstspdaadr riwhlaaaal gpdedvarql
      361 eeaagrartr gghaavaaay qraaeltvdp vrrsarlata alaasdaglt draaalagsa
      421 tpdvdepami valtqvrahr evelgtplaa griildaapr vaardpeqat wllveavrca
      481 wfagdaplag qaatalhelp aigsplvnqa vglarllagd lagglpftgd aldpsglagl
      541 gvpgltftag aalatgraal ceeltgrvva dcrrsgmigw lafalqdqgf aqglqgrygd
      601 aratldaglr latdlghehr vihltcclaw vlahqkdvag craraedgvr raddrklvla
      661 atlgrwalgr lelglgnada aleqleripl sgfgalaaad lveaavrsgr perageplec
      721 yltwarhvrq pasdavalrc ralmdqdeah fvaavrahdg adqpyeqart rlaygewlrr
      781 arrradartq lraalevfdr lgaeswarra raelratgdv paaprragdp lsvltaqere
      841 vvrlaaagas nrdiaaqlfl sprtvgyhly kafpklgits raqlatlagv aaae
//
LOCUS       WP_357564111             355 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564111
VERSION     WP_357564111.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   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 355)
  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..355
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..355
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=36074
     Region          3..>131
                     /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 metgqrqvsa ngitqavrva gppdgvpvll ihgncssaaf weplvrrlpa tlrvvapdlr
       61 gygltdtapv datrgltdfa ddvaalldep slfapgarpv vvghslgggv amrllvdhpd
      121 rvgalllaap vspygyggtr dlagtpttad fagtgggtan gdfvkrlaag drgadgpssp
      181 ravlratyva dpaalgddee llldsvlsta tgddnypgta lpsanwpgta pgrrgvlnal
      241 spayfrvade lvavagkppi twihgdadvi vsdaalmdla hlgslgvlpg wpgqdacpaq
      301 pmvgqtravl eryaaaggay revllpgcgh sphlerpaef vaellrltgg taasa
//
LOCUS       WP_357564062              94 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564062
VERSION     WP_357564062.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 94)
  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 94)
  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..94
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..94
                     /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=9889
     Region          <6..92
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mhhnvpdgkv evatrlaagq allavtntgp vvppeevdrl fepfqrmrrv addahhglgl
       61 sivraiavah gavltaharp rggftveisf pamp
//
LOCUS       WP_357564169             301 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564169
VERSION     WP_357564169.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  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 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   3  (residues 1 to 301)
  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 301)
  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..301
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..301
                     /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=30977
     Region          1..263
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mvrfglfgtg hwaakthgaa lhahpgttla gvwgrdpgka aalaerygvp afddvdalid
       61 acdavavalp pdvqagialr aatagrhlll dkplalsvad adrvvdaaqa agvasvvfft
      121 gryqpdiagf lastaavggw htaravrfas ifqpggpyga sawrrehgal wdigphalsi
      181 ilpvlgrvtr vaatdgprgl vhlllthdgg atstisltld appeaasref vfygengvea
      241 vpagegdsvt afgvaidqll eeiasgtrdh rcdvrfgrev vavlaaaeaa raegrivdvp
      301 r
//
LOCUS       WP_357564298             381 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564298
VERSION     WP_357564298.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 381)
  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 381)
  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..381
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..381
                     /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=39608
     Region          5..291
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msgptkriri avaglgiiah tahlpllrrr adlfdivala dlspsrlaga gehygvgpqr
       61 ryadaarmvt dggcdavlla tsgshgdlaa lalragvpvl cekplavtla ettrlaelga
      121 gdaalmvgym kqydpavaea arllaelggp ervhavevtv lhaggdrqls fanlspapad
      181 vppdeaarls gagarlldaa vgadpgartl yqilinsish dlsllrlftg apatvehvat
      241 wplapdgpve psveisgrlp ggtrygirwl nlpeypayre tvtlhhargs lelafpspyl
      301 mnapttltvv dyhaggerra ayrsvteafe qelvafhamv tegaapltgi aggatdlrts
      361 qqvvrrygel tgavvggeaa g
//
LOCUS       WP_357564303             315 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357564303
VERSION     WP_357564303.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 315)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..315
                     /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=34004
     Region          38..312
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mvqatsspde vvegarpvtg aspapdaagl graraagflv pamvlilvfl vvpaawtlyl
       61 gvtnyrltgl aaahpeivgl dnytralgde rfrtslvltl qfvlgsavig qaglgfaiaf
      121 alrdrrgplr rlvegfvlls wilpssvvaf lwialldrdg gtlnamlgip gmawlldypm
      181 lsiiifntwr gtafsmmlya aalenvprsh letarlagas twqqlrdvvf prirghvltn
      241 lllislwtfn dfapflitag gpeqrseilp vyvykvalsg gelgfgaais fimllinlvi
      301 alvylrmlgr rkepa
//
LOCUS       WP_357564321             173 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564321
VERSION     WP_357564321.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 173)
  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 173)
  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 173)
  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 173)
  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 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..173
                     /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=18303
     Region          3..153
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mlirretpad tdairavhla afadpakpda vpveaglvda lraddgwlpa fslvavdggq
       61 vvghvvatra rvagepvalg lgplgvlpdr qrrgvgcalm havlgaadar deplvvllgh
      121 pdyyprfgfr pavdlgvtpp qpwgpqyfma rpltawqpsi rggftyarpf del
//
LOCUS       WP_357564338             429 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357564338
VERSION     WP_357564338.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=45785
     Region          34..407
                     /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(146,148,272,274,309..311,354)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrrrsvigts lamvvalgls acggggddag ssntvrvtlv nhvwtenikk alpefekqsg
       61 lkvevtqlge dqlsdqynvk lnagstdldv mmyrplqegk lfaknkylad ltdksksdsa
      121 feigdfqsgp vqattyedkl vgvpiiteqe vlyyrkdlle ksgftappkt ldelkaqaak
      181 veadnpgvag fvsrtgkaaa vtqfssflys fggdfvdang kasvnteqak qayayyggll
      241 rehgpenist dmswseamai ftqgkaafyt eanslyknat dpakskvset vgfaafpagp
      301 agskpynips walgvnessk nqdnawkfiq waagkeqala qqkagvpsar tsvwenpega
      361 atypkdlaea ttvstangvg hdrplvvkva eareivgqpi vdaitgkdaa asadaanerf
      421 qkflddeak
//
LOCUS       WP_357564437             105 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357564437
VERSION     WP_357564437.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 105)
  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 105)
  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 105)
  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 105)
  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 105)
  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 105)
  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 105)
  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..105
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..105
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11606
     Region          10..104
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mttptqsseq kwlddlrttl ttdfeaqtar ltqltadtgd pgeahtqsal iaatrrsleq
       61 isgalrriae grygtcerct apiprerlev lpharfcvpc qqkqh
//
LOCUS       WP_357564564             171 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357564564
VERSION     WP_357564564.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 171)
  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..171
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..171
                     /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=18419
     Region          2..164
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrlvitadth vpkragdlpe rlwaaidaad vvlhagdwvd ealldalaar arrlvgvygn
       61 ndgpalrarl peiarvelgg lrvavvhetg pkggresrca arfpdvdllv fghshipwdt
      121 vapgglrlln pgsptdrraq pyatyltarv aagrldevel hrlpprrppg h
//
LOCUS       WP_357564616             263 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564616
VERSION     WP_357564616.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..263
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28761
     Region          13..247
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtdtelwvrr fhpaddaatr llclphaggs asyflpaaka lapevdvlav qypgrqdrlr
       61 epgltsvhei adqlvaallp lvdrpiavfg hslgatigfe valrlrragl apsalfvsgr
      121 raphrrkmer ihlrddagli aevralagtd dtllddedvv rmvlpairad ytaaetyeyr
      181 peprldcpiv aligdrdprv tveeaqawqe htgaefelav hpgghfylnd hmpavlrrir
      241 ahtrslrpap rgdttlapaa qpg
//
LOCUS       WP_357564621             416 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564621
VERSION     WP_357564621.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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 416)
  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 416)
  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..416
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..416
                     /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=44572
     Region          1..409
                     /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 mayllgvvlf alailisvsl heaghmltak afgmkvtryf vgfgptlwsf krgeteygik
       61 giplggfcki vgmtpqdddv dpadepramw rfpvwkrtiv msagsithfa lavialwiia
      121 vsaglpnpqf psteaeirke pavialsecv vpentlrect aadpaspaaq aqlrdgdrit
      181 avngtpindy gqllttlrtl kpgetaqiay vrdgqpgtgs avlaqtqrpp lddpkgqvaa
      241 vaalgvglvp stptritygp vgafgatadf tgdmavntye amkripekvp alwtaitgge
      301 rdidtpisvv gasrlggeav eneawllffm lfvslnffig vfnllpllpl dgghiaiawf
      361 erarswlyar igradpgrvd ylklmpltya viliggvftl ltitadvvnp itlfsr
//
LOCUS       WP_357564652             164 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564652
VERSION     WP_357564652.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 164)
  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 164)
  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 164)
  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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..164
                     /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=17820
     Region          8..146
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mtvytprraa rvllvdaagr lllfsgadpa rpehgrwwft pgggldpges ypecaarela
       61 eeiglrlpas afgppvhrdv tefpfdgvwy rqeqefflvr vtghevdtag fseieratva
      121 ahrwwspdel agtgeryypt dlpavlaral tsaqapvage gapc
//
LOCUS       WP_357564723             378 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564723
VERSION     WP_357564723.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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 378)
  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 378)
  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..378
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..378
                     /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=39427
     Region          12..287
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtglppaaat drpvrvavag lgwagreiwl prlaahpgya vtavvdpaag vrekvrdthg
       61 ipagyadvde lpagsvdlvv vavpnhlhat vaarllrrgv pvflekpvcl tsaeatllad
      121 aerdggavll agsaaryrad vralaaaaae lgpirhvdva wvrargvpda ggwftrrdls
      181 gggalvdlgw hlldtvlpll gpttrvvhai gsvsddfvnd gaanaawrgd tgagdrapgd
      241 vedtargfll tadgasvalh acwashesld rttvtvhgaa gsatlrctfg fspnreptpv
      301 ltrtrdgesv rlplpeepig teygrqldel pglladpasr gaavaearrt idvieriyhs
      361 arptepareh alaghrdr
//
LOCUS       WP_357564779             549 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 27 protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357564779
VERSION     WP_357564779.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 549)
  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 549)
  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 549)
  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 549)
  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..549
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..549
                     /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=58749
     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          427..548
                     /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(438..441,451,453,456,460..461)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(447,478..481,490,492,495,497,499..500)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(465,469,471,478..480,490,492,495,499)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(521..525,534,536,543..544)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mrrtrqwlaa lgvlvvalaa tvadgavapr paqalnngva rtppmgwntw ntfgcdinet
       61 lirqmadaiv vnglrdlgyr yvvvddcwfn pnrdaqgnlq ahpqrfpsgm kalgdhlhsr
      121 gllfglyqap ldqtcaqyfd afpgstgslg heyqdarqfa awgvdylkyd wcsptgtidd
      181 qvarfgimrd alaatgrpiv ysinpnsihe ktgpqrnwsd vanlwrtted itnawntgqt
      241 ngypmgiqni vdvnvplagy aapggftdpd mlevgnggmt dtemrshfal wsimaaplmm
      301 gndlrsasaa tltilrnqnl vainqdglgr qavqvshdgt rrvlakrlan gdvavalfnq
      361 gssattvstt ataigksgas ftlrdawtna tstttgaisa svpahgtvvy rvsgggttdp
      421 pppttfrlrs esagrcldvd nsntangtgt liwdchadpn qqitqsgqtl rvlgkcldvp
      481 ttaangtrvq lwdcnggtnq qwtfngngtv gnvrfpslcl dvnnggtang ttvilwschg
      541 ntnqrwsra
//
LOCUS       WP_357564810              95 aa            linear   BCT 28-DEC-2024
DEFINITION  Lrp/AsnC family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357564810
VERSION     WP_357564810.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..95
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=9971
     Region          <2..75
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mitaivlidc atdsipevae tlanlpgvse vysvaghvdl iamvrvrefe qiaqviaghi
       61 skvpgvlnte shiafraysq hdlesafaig lanad
//
LOCUS       WP_357564820             603 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564820
VERSION     WP_357564820.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=64298
     Region          1..603
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrefsvppii tigdaanltd pvwdnaavap devqfvrpga tngtattwvd vtcrqfrdev
       61 vaaarglvaa gvqagdrvgl msrtryewtl ldyaiwaaga itvpiyetss adqaawilad
      121 sgavgcvvet gahatlvagv rdrlpdlrhv wqidldavdq lvrsgdtvdp aeidrrrsal
      181 gaddvatiiy tsgttgrpkg cvlthrnmya dianavpvlp nlfgpgastl lflplahafa
      241 rliqigvvqa ratmrhcadt knlvgelqef rptfvlsvpr vfekvyngak qkaeadgkgk
      301 ifaraeqvai aysealetag gpglalraqh alfdklvyrk lraalggrcr daisggaplg
      361 arlghffrgi gvnvcegygl tetspaaaan lpdatrigsv grplpgvtir ieddgeilia
      421 gdlifqgywr neaataeals adgwfrtgdl gqldndgyls itgrkkeiiv taggknvapa
      481 vledqvrahp lvsqcvvvgd rapfiaalvt ideealpqwl asaglpadtp veklrehegl
      541 raeiqgavdt anravskaea ikvfrilphd fteatgeltp slkvkrqvvh ksyaaeiadi
      601 yqr
//
LOCUS       WP_357564825             469 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564825
VERSION     WP_357564825.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 469)
  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 469)
  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..469
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..469
                     /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=52243
     Region          33..435
                     /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 mststdhgrp dpeastlalt rdgrpvsdrg dtvcvigaga sgltaiknlk ehgfgvdcye
       61 retgvggawn wrhdrspvya sthlissrpf tqfpdfpmpd dwpdyphhsq llsyferyad
      121 hfdlrghiwf gtevvrvepv agdrwdvttr stggygpert sryaavlvan ghnwspklpr
      181 yegleeyrge vmhassykdp aqlrgkrvlv vgagntgcdi aveaaqqasr cwhstrrgyw
      241 yapkyvlgrp adqvndalla lrvplrvrqw lyhwtlrltv gdltrfglpk pdhrvyethp
      301 iansqlvyhv ghgaitpvpd varfrpyave lsdgreidpe lvvfatgylp rfefldpgvl
      361 gddagtgrpk lwlnafvpgh ptlavaglvq pdsgifplsh wqavlfarll rlrvtrpdra
      421 aafaarvsak ageryagpvk dssrhwfevg hadylravqr alralesar
//
LOCUS       WP_357564873             351 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564873
VERSION     WP_357564873.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=38290
     Region          22..312
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtqqtrdevg gllphdefra aseaivsnie qviegktatv rlalavllae ghlliedvpg
       61 vgktklakam arsidcsvrr iqftpdllps dvtgvsvynq ethdfefrpg avfanlvvgd
      121 einraspktq sallecmeer qvtvdgvtyh lqtpfmvvat qnpiemegty plpeaqrdrf
      181 tariamgypd pnaelamldg hgatdpldel rpvsdantvr qliahvrqvh vadavkqyai
      241 dlvtatreas dlrlgaspra tlqllrtara vaalegrdyv lpddlqalav pvlahriipt
      301 adaqlarrtt daivsdlvhr lplphdrgrs pydtrpageg ngrasyeprr r
//
LOCUS       WP_357564928             350 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357564928
VERSION     WP_357564928.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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 350)
  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 350)
  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 350)
  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..350
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..350
                     /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=36078
     Region          5..345
                     /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 msadrylava gprelrengi svaapgpgrv tvditytgic gtdvhgytdg hmlppavfgh
       61 ewtgsisavg dgvtglrvgq rvvggvgpac grcpqcvagh trncdtvfae angvdadapa
      121 yggfatrvqv aarrvlpvpd sisnveaalv epatvtfhav rrvaaelgat tvvqgagpig
      181 lltaqnarna gagpmivsep sparralaak lgfahvvepa dlraaldelt rglgadlvye
      241 ctgvpslfqp saelvrrggt lallgyplen stvsygdwqs reltvigsla yhhedfvaam
      301 qaiaagrldv aslhtgtfgl sslgdileel dsgrsehtkv lidpsrdars
//
LOCUS       WP_357564830             398 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357564830
VERSION     WP_357564830.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 398)
  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..398
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=41766
     Region          148..396
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgvdeaqrsa gpraagfgrl sretvrdllv gaavsivvsa aitanlggdr grdlpaylfa
       61 lglgaltlar rrapvavlla saaglvayym adyppvglal plaaalysaa eagrlrwavl
      121 vglgllvvst afrtaqgesv aylvgfelas svatmaaaia lgdgvrsrrl rrreqrwrlr
      181 qmerdharea trrveeerlr iardlhdvia hhisvislha gvadealddd ppaaraalgh
      241 vraattevar elrttlgllr dptgtdprqp vaglagldal vagarstglr iavhrrgelt
      301 glpaavdsta yrliqealtn alrhadattv eidlvrdsra vglavrddgr gqredvprgh
      361 glggmrerta llggtvtagn rtgggfevra elplggvp
//
LOCUS       WP_357564994             188 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357564994
VERSION     WP_357564994.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  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 188)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..188
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..188
                     /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=20899
     Region          1..188
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mrrnderraa lidaaievla eqgargltfr avdaaarvpt gtasnyfanr ddlfthigar
       61 vyerlqpdee tvvrhlegaq drekltavmr etvrrvagfr tgylallelr leatrrpelr
      121 avltrsvrad vdaniashqa sglpgdatsv rllhmalnwl iverltlpev yseqesddlv
      181 araverla
//
LOCUS       WP_357565061             816 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357565061
VERSION     WP_357565061.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 816)
  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 816)
  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 816)
  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 816)
  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..816
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..816
                     /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=90135
     Region          9..>638
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtrqalhegw tlravegpqv pvgiagrrvp atvpgcvhtd llaaglipdp ylddnekgaa
       61 wigrtdwvye ttfahqpgde qridlvcagl dtvatltlng tevgrtenmh rgyrfdvrsl
      121 lvagsntlav rfdsaygyae aqrdrlgdrp naypepfpfi rkmacnfgwd wgptlvtagi
      181 wqeiglhawg tarlaavrpl vtvengdgrv elhveverag dapltvratv agaaaeatia
      241 agqrtavlal tvrdpalwwp rgygdqplhp levtlhhadd rpldtwsrri gfrsvrldtt
      301 pdahgtpfal hvndtpvfvr gvnwipddaf ptritrdrla hrfrqaadan vnllrvwggg
      361 ryesddfydl adelgllvqq dflfacaayp eeeplgaeva aeaaeqvvrl aphpslvlwt
      421 gnneniwgwh dwdwqeplag rswgrgyyle llprivgeld ptrpywpgsp wsgseeihpn
      481 dpahgtthiw dvwntddytr yrdyvprfva efgyqappay atlrralsde plapdspgma
      541 hhqkaidgda klrrgldahl papadfddwh wltqlnqara iqlgvehfrs hrdvcagtiv
      601 wqlndcwpvt swsavdgdgr rkplwyalrr ayadrlltvq pregglavva vndgaapwra
      661 tasvtrltla gaprakttle ldvpaygrle lalpaelarp dearrellva eagdtaeral
      721 wffaedrdad wpaagwdatv epvdggqrir vtartvlrdl tlfpdrldpa aevdealvtl
      781 lpgesatftv raagpldpaa ltarpvlrcv ndtaag
//
LOCUS       WP_357565195             393 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565195
VERSION     WP_357565195.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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..393
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..393
                     /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=42492
     Region          14..385
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mrlpesfyts vrsrlnetld ergldgflat spadvaflsg ffyiaterpv ylwmpregep
       61 llviprldee yaaqqgvtvp lvsyfefpgv vtaeqtlaaa lsrpggavrr igvgagvsvg
      121 afralsraia gatlettdav aklrlrkfpe eipfheaaar icdemlgagr alieealasg
      181 gplpredeia rhvigygtdr myaeydlvvy ttklagglvy agpnsalphg lptrrriqpg
      241 dtlilslgaa vasrfveser tfiigeptae qvryyeadre aqevgtqami agrtcaevnk
      301 icldvlrehg lgdhirhrqg hgiglqnhea pwvedgddtv lapgmllsse pgvyvpghag
      361 yrisdtvlvq eagprrltgy prdlasnvie gvr
//
LOCUS       WP_357565198             329 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357565198
VERSION     WP_357565198.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..329
                     /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=36217
     Region          2..329
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mppsddvvlr vdnlvkhfpv kgrvplrsgg vvkavdgvsf dlrrgetlgv vgesgcgkst
       61 larmlvgler ptagevrfgd avvhrargre lralrrriqi vlqdpytsln prrtvreill
      121 qpyeihpdvl pkarrldrir elldlvglda slhldryphq fsggqrqrig iaralalqpd
      181 vivcdepvsa ldvsvqaqvv nllerlqeel gvayvfiahd lsvvrhisdr vavmylgklv
      241 etgpgaplyd qprhpytkal lsavpvpepa rrverqrill agdppspvdp psgcrfrtrc
      301 wqatdtcatt eppltgpehp vachyplaa
//
LOCUS       WP_357565221             263 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357565221
VERSION     WP_357565221.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 263)
  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..263
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..263
                     /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=27014
     Region          6..260
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mteiggatrl yallgdpiaq vrapgllnpv larrgtdavl vpvhvapadl dqvvrglrqm
       61 anldgmlvtv phkaaalala draserahla gsanalrrep dgtwtadtfd gdgfvrglaa
      121 aghqlsdrra cvvgaggags aiavalldag vaelrlsdtd pgrletlrcr lsaaypgrvt
      181 atarprlada dlavnatplg lrpddpppfp vtdlpthavv adiimkpaet allagargrg
      241 laahpgepml ahqldgylaf fgl
//
LOCUS       WP_357565231             915 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357565231
VERSION     WP_357565231.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 915)
  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 915)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 915)
  AUTHORS   Rosinski,J.A. 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 915)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..915
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..915
                     /product="helix-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=95552
     Region          <10..883
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          857..912
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mvnastvqia vlrgrseeca airrllgdlp gdggalllqg epgsgrtalv dhahrhaegc
       61 tvlagtglae eaglpyaglq rlldpvldra gmlpvqqrrv llralagagc pahrrlalsl
      121 avlglltaaa rdrpllctmd dvdrgdqpta dtlafvarrl rrsrvavllt aatdapdgip
      181 rhrlrplddr dsaalladrv agapptppva aalgavaggn pqalvdlaev lspgqcrgee
      241 plpeavpfdg glgrayrtrl drlpadtrrv lllaaldedg dlatlvraar vagaaveala
      301 paelaglvrv gpgrvtfpqp lvravvrgaa plaarraahl rlagvldrae hrlrraghla
      361 aaaqgpdpal aveleqaaag cgggvavsaa lqraaelsdd pvhaaarlva aarcawsagq
      421 ahrarlllgr lpavrdaavt gragllggei elrvgrprta ltmllaaada lagvdralal
      481 galvrageaa cfagdqyrya evarraeplr rpddppatel lsaylagtaa tlrgdherag
      541 palrravvlg grltgpaltp aaltcaaaag llvavdgagh rlaeravala rdrgelsalp
      601 ralelraaae ywlgrhdaaa dssreglria rdtgqdnwag vhlgmlavla avradrddsl
      661 rrireigeep gahsrprala qwalavldlv dnrpaaatar laalarpgtc rgqvlvqvma
      721 tpylveaaaa vadgpaagva lavfdrwass taspsrrals archgllapr gsaeaerefr
      781 aalrlhptda gaferartel llgrelrrnr rpraarehlh aareaftllg aavwaeqatt
      841 elraagesvg ppeepaarll tgqqlriaql vaegatnrei aarmflstrt vdhhlrnifh
      901 rlgirsrtel arals
//
LOCUS       WP_357565270             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357565270
VERSION     WP_357565270.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=35762
     Region          4..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msrtrterlv nlvicllstr rfltaaqiaa tvpgyehdpd dardheafqr kferdkaelr
       61 elgvpletgt asvfdaepgy riahreyalp diplepdeaa avgiaarlwq haglaaaass
      121 glaklraagv dvdpqatlgl epmvtvdpaf apltaaardr revsfdyrvp drddptrrrl
      181 qpwgvvcwrg rwyvvghdld reatrcfrls rvvgavratg apggyeppag vdlishvars
      241 tgpaertgra tvlvaagraa glrrwaagvt agpegdrlvl pyadadqlag qlvgygpdvr
      301 vldppevrda viqrlkeiaa rhdelavagg ar
//
LOCUS       WP_357565413             223 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357565413
VERSION     WP_357565413.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 223)
  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..223
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..223
                     /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=23609
     Region          14..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marrtqgvsa gldreriaav avalvdrdgl erfgvrrlae elgvdpmsiy hhlkgkaall
       61 daiseavlae vaggeddtsg sweeitrata rryremayrh prvfpllatr aqtspvaltg
      121 lermvsamra aglpdqvvad aplmlfgfln gyllavlsge pdgigavpai daaayptmat
      181 lmplqagfgs paefdrmldt vldgirnraa rpdgpgpaqr vss
//
LOCUS       WP_357565421             176 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565421
VERSION     WP_357565421.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 176)
  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 176)
  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 176)
  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 176)
  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..176
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..176
                     /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=19457
     Region          11..176
                     /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 mlrapatstl pelllrpwrd ddadalvaay rdpvllrwtr apvtttadar rfvaaarrdw
       61 ddghrfafav veprpagetl vaqlvlknvt egaehaevgy wtaapargrg vaphalgavt
      121 dwafarfagl rrldllhqid npascrvaek agyrfqevlp arppfprdgh rharwa
//
LOCUS       WP_357565426             345 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565426
VERSION     WP_357565426.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 345)
  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 345)
  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 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   5  (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   6  (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   7  (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 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..345
                     /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=37873
     Region          27..342
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msgpgtagav dapadprptr pgrrgraagr tppvrprrtl wdrlrrdwpl lamtapaacl
       61 llvfhyvptl gnviafqdyn pfvgddplea flysewigfg nfealfgdpl fwdavrntlt
      121 itafqlvfff plpimlaill nslvsgrvrg fvqsvvylph ffswvlvvtf fvqmlggagl
      181 laqemreagm qpwdvmtnpd tfivlvtaes vwkdvgwgai vflaalsaid pnlyeaaaad
      241 gagrwrrlwh itlpglrpvi vlllimrlgd alsvgfeqfi lqreavgrea aevldtfvyy
      301 qaistqqwgl gaaaglfkav vglililtan kvahrlgeqg vyaks
//
LOCUS       WP_357565434             441 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565434
VERSION     WP_357565434.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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..441
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..441
                     /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=47220
     Region          1..414
                     /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 mgaqprvavi gagaaglatl kaladagvpa vgfeagdrvg glwvygapgs payrtlhlnt
       61 srtrtefadh pmpahwpdyp dharvagwlt dyadrfdlhq avrlrhtvdr vtaapvgrwt
      121 vhadgpdgpv svtvdavvva nghnrvpkpp apdhtgtcta tqlhshayrg pdqltgrrvl
      181 vvgggnsamd iavdasyaar rtllslrrgv wvvpkhllgr psdalngala rrlpwrlrqr
      241 itermlaatv gsptryglpa pahgflqdhp tlsdgllsrl thgeieprpg iagfdgdrvt
      301 ftdgrtdeid lviwctgyrv eipfldpall gdgadtlply rhvfhldapg lafvglmqst
      361 gsafplveaq aklvaaqlsg ryalpdpqqq ravcraelra atarwgqrrp amrvdfdayl
      421 aeltrelaag trrahaagat a
//
LOCUS       WP_357565454             148 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565454
VERSION     WP_357565454.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=16503
     Region          1..144
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msdrfvyhct lrwsdldayg hvnnsrfltl yeearvalmf aggkawgvgs fadgvvisrh
       61 eidylrpvey algrataeaa ptvrielwve eirgasftva yelfdgevla srarsvlvpf
      121 dltrqrprri tpeertfllt yapsggaa
//
LOCUS       WP_357565484             448 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565484
VERSION     WP_357565484.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 448)
  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..448
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..448
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47223
     Region          54..429
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtliadrpgp gaarpyrfpq vvrrtvaggq vvaahlpgqn lavallllda gagreptgke
       61 glgavlakal eegtaqrdat ayalaieglg telvtgldwd afqvsvqvpv qrlsaavell
      121 aeavrtpkld pddvrrvrdd eatalrmdwa npgpradaal radlfgaanr wgrpmygdpe
      181 svaaldvedv tvfhsewfir pgtlvvagdl drldldalga tafagtaggp adrggpievp
      241 srpgrriilv drpgsvqstl rlghpsphra hpdhvpmtla gtvlggafts rlnhlirevr
      301 gytygirgdf assrrfgrfg vssgvqtavt apalveavge itrtretgvt edelavarsw
      361 ragqlsvelq spraiaaalt tlvvhdlpdd yharlrdsll aaevaevsaa aathlrpeel
      421 tlvvegdaav irdelvttgl gelvdyag
//
LOCUS       WP_357565515             593 aa            linear   BCT 28-DEC-2024
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565515
VERSION     WP_357565515.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..593
                     /product="type IV secretory system conjugative DNA
                     transfer 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]"
                     /calculated_mol_wt=63301
     Region          167..556
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 msrpagprgg hddaglivgg iaagvlvlas gawlpvvlar ppgytgggpv qvaaavlrgd
       61 itwtttctli avaevtvlll lavggittwr wtrrrrtrvd paarrmasrk dlahlgprgv
      121 adsgrrlrps ladvdrpdpd qlgvliahtv aggmplrqsw edmavdiwgp rtgkttcrai
      181 paivaapgpt lvtsvkgdiv datrdiraar gqvwafdpqh ilgpkqgmww nplrtvatit
      241 darrlaehfa saerepgvsr daffdpssee lvanlllaaa vsgrdilaay rwavsprdde
      301 paellrergy elpadavagv vnmpdktrgg iyagaqkmlm cltepavtaw vtppprggvl
      361 efdpavfvas tdvlyllsqg gpgspaplva altdavlrag elqarasagr rldppllsvl
      421 deaanicrlr qlpalysfyg shglpiitil qsypqgidvw gregmrklws aanirtyggg
      481 vadpdwleel skligehdvt trstsssgsg wgqrsvshat rrqrildvad lhalprgrmv
      541 vyasgappal artapwqtgp yaaairasia rwdphertdw tltpddtppe ptp
//
LOCUS       WP_357565548             242 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC047074].
ACCESSION   WP_357565548
VERSION     WP_357565548.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 242)
  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 242)
  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 242)
  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 242)
  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 242)
  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..242
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..242
                     /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=25209
     Region          10..242
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtsalhldqa ggshlgyvrr rnedaiylgc sliavadglg ghvagdvass tvietlrqyd
       61 qevdqqalat tlgkavgaan dalraritse pelagmgttl vamlingtsa alanigdsra
      121 yrlrrstght tqitedhvyg qlvadaadvp nlperlarfl dgrldgrspd itllaltpgd
      181 rfllcsdgls syvpehllht altdastprq avdhliaaal ehggpdnitv avldvlagan
      241 sd
//
LOCUS       WP_357565594             141 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565594
VERSION     WP_357565594.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 141)
  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 141)
  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..141
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..141
                     /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=15233
     Region          1..141
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maaaaedaed glaeafwavt rrlrhrtrea lapwdvtpgq sralgvlirh galrlsalae
       61 hlriaprsat evvddlearg lvrrrpdpad rratlvtptd ggvragaaih aarrtatadl
      121 fgrlapadre qlarilrtlr d
//
LOCUS       WP_357565597             381 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565597
VERSION     WP_357565597.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..381
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41214
     Region          3..377
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mdeallrslt pavlgvlvrr gadfvaaeda vqdalveavr awpadpprdp kgwlvtvawh
       61 rfldaarada srrrredrvd eepapgpvpa vddtlqlyfl cahpsltpss avaltlravg
      121 glttrqiaqa ylvpeatmaq risrakrtvs gvrfdqpgdv atvlrvlylv fnegysgdvd
      181 laaeairltr qlaavidhpe vagllalmll hharratrra pdgslvplaa qdrgrwdtts
      241 iaegvdvlqa alardrlgef qaqaaiaalh adapaaeetd wvqivewyde larltdspvv
      301 rlnravavge adgpraglaa laaldgslpr yaavaaylhe rdgdlptaar wyaeaahrap
      361 nlaerdhltr qaarlnarmr r
//
LOCUS       WP_357565643             449 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565643
VERSION     WP_357565643.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..449
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..449
                     /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=49226
     Region          3..395
                     /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 msprpphvli igagtgglcl ahglrragis vavyeryrtr gegllgyrvg igptgsralr
       61 eclppalfdv ylatcarspr yfnvitqrmg rtasftlrpd tdpvntersv armtlrqvll
      121 tgmedvvhfd rtfthyeqrd dgtvtahfad gstatgdllv aadgtgsavr rqylphavtr
      181 dagtiniatr ipltahtrgl lperlekgis lifgtggmmg vlhvmefkwd rdgtlkpgvd
      241 padaellrdw pglrhdntrd ninlviwsta rrfppdvmqr rgedlillal rltrnwhphl
      301 rellargdpg salpirvats epvppwksst vtllgdaiht mtpgrgvgan talrdaallc
      361 rqlrlaatgd ktllqavady eaamvpygfa rvadslnrsg tngedrmykp vvgrlallga
      421 rgyfgvtsrv prlarrfvdd fysyrgeed
//
LOCUS       WP_357565716             255 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357565716
VERSION     WP_357565716.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26027
     Region          18..247
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mscvvtgggr gvgravverl ldagdsvvvi eydpdavawl tahpaadrla avvgdaader
       61 vaaraadlae rtgpltgwvn naavfrdasl haapvgevld ligrnlrpav vgaatavrrf
      121 laadtggaiv nvsshqarrp vpgclpyata kaavegltra laveygprgv rtnavalgsi
      181 aterhtafla gqepataewi daeltrlhpv grigrpeeaa aavayllspa asfvngvtlp
      241 vdggrsvfgp dpear
//
LOCUS       WP_357565761             113 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565761
VERSION     WP_357565761.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 113)
  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..113
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..113
                     /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=12011
     Region          1..>63
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mlvtnrfvvd vdvadefter ahaaltalaa rpgylrgqlv ralddprhwc lvtewesvgt
       61 yrralggfdv kitavpllae svdepsayea lataapggdv vlaasdraag pyr
//
LOCUS       WP_357565748             266 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565748
VERSION     WP_357565748.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..266
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27633
     Region          1..237
                     /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..34,69,73..74,77..78,112,116,123,
                     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..215,221,223)
                     /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..222,226,228)
                     /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 misfepvarp eaplarrnpv aklvaalvfs fvlvatldpv apaiaiavel avlplfgvry
       61 rvlarrawpl lvgavgivvt lvlfaaersg rvlveagpav vtsgvlltal glvlrmfava
      121 lpgvivfatt dptdladali qnakaparfa igalaafrlv pllgqewqmi smarrargve
      181 aghnplaklr lftstaftll vgairrgtrl avamdargfd agtprtvarr qrfvaadgll
      241 iagaaalaga altvsvllgt frplig
//
LOCUS       WP_357565858             241 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357565858
VERSION     WP_357565858.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 241)
  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..241
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..241
                     /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=25354
     Region          4..211
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mafapvpras vsdhvfgqir daivsgdyrp dealpgerel aavfgvnrha vrealrrlqq
       61 lglvrvsqgd atrvldwrvh agldlalslt rghdalpvgt lvrdmlemra cigvdaarlc
      121 aergdpavra ailraveaya glapdlagmg eativlwrhi vagsgntayl lafnslvaga
      181 lavgevpper raaelldvag hrrladaivt graadaahea ralltapltt ptaaprrear
      241 a
//
LOCUS       WP_357565860             393 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565860
VERSION     WP_357565860.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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 393)
  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 393)
  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..393
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..393
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40682
     Region          31..261
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtaairalaa addlvaatra wrtepaadpk vealalavsa nlpvllwgep gigksatlqq
       61 ladglglple tviasvheps dfaglpivgd spatdgvpma ppdwavrlar tgsgllffde
      121 lssappavqa allrvvlerr vgslslppsv rivaaanppt saadgwhlap planrfvhlh
      181 wthdartvar glagtwpavt vpevragrta talarargai agfltarpgl thhlpadaea
      241 rggawpsprt wemvlrlltv hyaagsgaea lalavigavg dgaglefvty lenldlpdpe
      301 rvladpgafr lpergdrqla fltavisavq akvdrsrwea gwvvlgkave agvpdvaara
      361 amdlaalrdt swpvppaiha faevlglsgr lsg
//
LOCUS       WP_357565906             214 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565906
VERSION     WP_357565906.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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 214)
  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 214)
  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..214
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..214
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22608
     Region          55..212
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mstnlkvtlg vlavalavla gvvlvnrggd ttptaaaeav vrpdshrlst aadgkttvve
       61 fldfecescl aaypgveklr aeygdrityv vryfpiashp naynaahaae aaarqgkfep
      121 mykklfdtat awghqqqsqa avfegyaqel gldmtrfkad vasaevaarv kadatdgeal
      181 gvqgtptffi ngekfdgrpd ydglkaaida slns
//
LOCUS       WP_357565913             461 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357565913
VERSION     WP_357565913.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..461
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=46809
     Region          3..459
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 malsatvlae lrgivgpshv hdgagdlvay ardatplfsh rpdavvfpad taevaavlal
       61 atrhgvpvvp rgagsnlcaa tvplrggivl vltrltsile vsadellarv qpgvtsaala
      121 daaaargllw apdpgsrtva tvggtiatca gglrglkygv trnyvlglea vlptgevirt
      181 ggrlwkdvag ydltrlltgs egtlavitea tvallpapas tntgvayfpt ladageavar
      241 viragvvpat lefldraciv avedfahlgl radagalllf gddgppdlva ahldrigaac
      301 veagavevtt arevaqaeal laarrcalpa lsrrggvtil edatvprpri aemvdridai
      361 aarhgvaiat fghagdgnlh ptcvldsaed hdavrraeaa fadvfaaald lggtitgehg
      421 vgaaklpfla arlgddqlal lrriktafdp agilnpgklg s
//
LOCUS       WP_357566037             363 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357566037
VERSION     WP_357566037.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 363)
  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..363
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..363
                     /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=39623
     Region          1..363
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvtyakas riypgterpa vnqldleigd geflvlvgps gcgkstslrm lagledvdqg
       61 sihiddrdvt hlppkardia mvfqnyalyp hmtvyenmaf alklrktska eidrrvkeaa
      121 allqleeyls rkpkalsggq rqrvamgrai vrepqvflmd eplsnldakl rvqtrtqias
      181 lqaklgvttv yvthdqveam tmghrvavml dgvlqqvdtp ralydtpanv fvagfmgspa
      241 mniktvplge rgatfadlqi pltreqveaa rsdggdgkvt vgfrpedcdl vspteggmpv
      301 vvelvedlgs daniyghaal egnnerfvvr tdrrnmpnmg dtvfvkpreg rshvfnastg
      361 nri
//
LOCUS       WP_357566128             874 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566128
VERSION     WP_357566128.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 874)
  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 874)
  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 874)
  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 874)
  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..874
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..874
                     /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=89078
     Region          10..849
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mpadtstrpv arldpaeggl ssaeaaarlr adgpnaavap prrrlggrvl hqltdplval
       61 llaaavvttv lgdypdtavi vlvvlvntai gvvqelradr aiaaldqlaa ptarvvrdgr
      121 dvvlpaaelv rgdlvrveag dvvpadlvla esarlsvdes altgesvpvt raageeasag
      181 tvvttgratg tvvrtgdasa lgritalvas trpaatplqr rlaglgrilg faavvlsglv
      241 fvigvvggrp vvdmavtavs lvvaavpesl pavvtlalal garrmagara iprrlhavet
      301 lgsvtviasd ktgtltegrm avqhavtpdg srygvtgtgy apqgavrhgg atvavpddlr
      361 rlaragllcn datlapptde rpewtavgdp leaalvafaa rcgldpehtr vawprvaehp
      421 fdqdlrrmtt vhrscdrryl vvckgapenv ltaplveasv eeiaelsaaa hrlaaeglrv
      481 lavasdvvds ppddlarptg lrpaglvavg dplragaadi agsfddagvr lvlitgdhpa
      541 taaaiggqlg lwregdpvvr gddgdpaqah prarvfartq peqkldiiag lqsrghvvam
      601 tgdgvndapa lrradigvam gggtevarqa adlvlvdddl stvataigeg rriydnirrf
      661 lryalaggva eiavmllgpl fglavpllpa qilwvnllth gvpgvalgae paepgtlrra
      721 prspsesvlg aglgrdvlvt galiaavvlg agvlaahwdr pwqsvvfatl glaqlgvala
      781 vraprpagar rgnlalpvav avsallqvag vllaplrell gteplgavel lacaavsvlp
      841 alvlrlvrrp agggtpgagr dlgpvpagtt apdr
//
LOCUS       WP_357566081             232 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566081
VERSION     WP_357566081.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 232)
  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..232
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..232
                     /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=25153
     Region          40..180
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mrvdpgrpgp ltlrlarlld gawtagsrvr ravrgwatvh rfavrggrvv fdpdgvytye
       61 tielganvdl gyrpvlmaar sririgdnvm fgpevtirgg nhrvdrvgvp miavrkqpgd
      121 eqhdrgvtig ddvwvgtrai ilqgvtvgrg avigagavvt rsvppyaiva gnparvirlr
      181 wpvetiaehe ralyppsqrl ddeelaalve fpapvarpas vtnrltanlq dr
//
LOCUS       WP_357566147             457 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357566147
VERSION     WP_357566147.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=47881
     Region          21..341
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msnltrrrca aalaavtalt mlaacgesep eaekakeitf wtpqttpqrv aaqekvaarf
       61 tektgiavkv vplseadqkq alatgaasgd vpdvmlhsst ttaawrsqgl lntgaaeevv
      121 kdlgaetfna nalkafsldd kvgavpsdgw vhllvyrkdl fqaanvavpt nleelakaat
      181 tmkatgvsgi algtqsgtps gteavysmfq sagcqlvqdg kvtidspect raaeqfkvlr
      241 dsstqgdfdv tsaraaylag kssmllfsth ildelaglds anpptceqck adpaflskns
      301 gfitvldrnh paqygatlgy gipegantag akefikfmle egysdtlasa tegriplrng
      361 tkaepnayld awgklgvgpe akssvaelyg pemvtqirdg vnavslwgmg tkdsplagav
      421 taenvlaqfl erlyggqspa ditkamaeev kkvqael
//
LOCUS       WP_357566148             318 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357566148
VERSION     WP_357566148.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..318
                     /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=34996
     Region          <71..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mstptvrssr werlsrsqre nlngqlltgp tllllalvvl lpfvlvvifg fsdtrlidip
       61 rlspstiewt feniadawrs dafwgalwtt viyatlttlg sigvgmalal amrrpfrgrg
      121 ivralllvpy vlpviaaami wrtmlnpqyg ivnaigmeyl gwqspigfls ttstdvaglp
      181 vpvsllvvva feiwksfpla flfvtarlqn vpggieeaaa ldgasrwqnl rhiilpqlrg
      241 vvlllmllrf iwsfqnfndv ylltegaggt qvmaikvyte lvtrsdigsa aaygllmsli
      301 lcvllagyvl lsrrketl
//
LOCUS       WP_357566210             290 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566210
VERSION     WP_357566210.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 290)
  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 290)
  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 290)
  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 290)
  AUTHORS   ter Beek,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 290)
  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 290)
  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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..290
                     /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=30570
     Region          26..227
                     /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"
ORIGIN      
        1 mmagtsptvg aaagyrpsat lpfgaefrrq asrrrtqlal gfmvllplii liafqfdtgd
       61 ddngrgefgs lvefatsggl nftlftifvs asfllvvvva lfcgdtvase aswgslryll
      121 avpvprarll tvkllvalay salallllag talligtary gweplrstva aqlepgegll
      181 rllgvlgyla vvllvvagla fllsvvtdaa lgavggavll wilssildqi talgalrafl
      241 pthystawlg llstpvqtdd vvrgtisais yatlfwglaf wrftrkdvvs
//
LOCUS       WP_357566292             511 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566292
VERSION     WP_357566292.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 511)
  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 511)
  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 511)
  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 511)
  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..511
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..511
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=55824
     Region          50..493
                     /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 mtvrrrsplr vltgvlvval vlccggvavg gwvlarggtd tvgrvdfvrp lavpplatsr
       61 vdgqgrrvfd llardgrrdf hgdgrltrta gfdgdflgpt lrarrgervv vnvvnrltee
      121 tsvhwhgmhl parmdggphq pvrpgatwsp twtvdqpaat lwyhphphga teehvyrgla
      181 gmfildddre salplprryg vddvpvivqd rnfsrdgefa rtrnsiasig vlgdtllvng
      241 tvgpyldvst ervrlrllng startydfgl addrpfalig sdggllprtv rvnrvqlspg
      301 eraeivvavr pgervilrst ppdlgagala drfaggadrf dvlelraadk lepsppvpda
      361 lvpldrldpa savgtrrftl tgrsingrsm rmdridfavt rgateiwelv nqdgtphnfh
      421 vhdaqfqvlt vggrtpppal tgwkdtvyla pgrpirailr ftdhsdpdvp ymyhchllyh
      481 edagmmgqfv vvepgqragt pprpgthahh d
//
LOCUS       WP_357566306             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357566306
VERSION     WP_357566306.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=35795
     Region          14..310
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrllsll lllqtqgrmt aaqlaerlev strtvyrdve slhaagiply geaghaggyq
       61 lvegwrtrlt gltaqeaerf flaglpgpaa elgygaavaa lqlklhaalp peladraari
      121 qerfhldapg wfadgdasph laevaeavwr qrrvavryrs wtdeadrvld pyglvlkggr
      181 wylvagrprh dgpaayrvnq ilslvtlgee farptgfdlp awwrayvvrf raglhrgdat
      241 irlspggrer lreivsplvv tavdetagpp ddagwvtavv pieslthahg ellrlgadve
      301 vlapaalrdr laataaalaa lygprpagig ts
//
LOCUS       WP_357566319             494 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566319
VERSION     WP_357566319.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 494)
  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 494)
  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..494
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..494
                     /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=54062
     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 matdhvdvli vgaglsgvga achlrrecpe ktyavleard aiggtwdlfr ypgvrsdsdm
       61 ftlgysftpw tapkaiadgd tirdyvrrta deygvtdhvr frhrvvradw dsgtarwtvq
      121 ahrddtgaav tltcsflfvc agyyrydagy tprfagtdrf agrivhpqhw padldhagkr
      181 vvvigsgata vtlvpamaer aahvtmlqrs ptyvmalpsr dvladalrrw lpaaaaypvv
      241 rwknillata nfqlsrrapa lvrklllraa rgrlpvgydv drhfsprydp wdqrlcvvpd
      301 gdlfaavarg sasvvtdtid tftergirla sgeelaadvv vtatglnlla lggmtltvdg
      361 aevelpgtva ykgmmlsgvp nlamtigytn aswtlkadlv atyvcrllrh ldrtgqqvvt
      421 plppadgelv plidltagyv lrsvdalprq garapwrlhq nyprdvllmr rgrltdpgvr
      481 fsragtperr tvra
//
LOCUS       WP_357566320             322 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357566320
VERSION     WP_357566320.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=33971
     Region          6..269
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mrryvfaggt avvtgaasgi gealahslar rgsdlvlldr dagrldtvva elraaypdrq
       61 lttylvdlad aaatartaea lrrrhpairl lvnnagvalg grfdqvtlde fdwvvdvnfr
      121 avvqlthall ptlraepgah lvnvsslfgi iapagqtays askfavrgft ealgqelagd
      181 gigvtcvhpg girtriaqna rvgagvpaee fetgrrqfer lltidpataa evilrgvqrr
      241 rgrvligwsa klpdllarva pasyqrvlaf glnriagest rqlttgqpap tqrqpaptqp
      301 qpapaqrqpe aapaadpage pa
//
LOCUS       WP_357566349             248 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566349
VERSION     WP_357566349.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=27102
     Region          <24..141
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mdlpriftir esshrlhnpf tpgklatlgq alhlapgarv ldlasgsgem lctwardhhi
       61 tgtgvdistv fteqararaa elgvadrvtf vhgdasghva depvdlaacv gatwigggva
      121 gtvellgksl rpgglmlige pywrqevpdq etaeaclags kddflalpel ieqfgdlgyd
      181 vvemvladqd swdryqaaqw lnlrrwlden pddelaaevr aelttepary tryqreylgw
      241 gvfalmsr
//
LOCUS       WP_357566426             269 aa            linear   BCT 28-DEC-2024
DEFINITION  Fpg/Nei family DNA glycosylase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566426
VERSION     WP_357566426.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 269)
  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 269)
  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..269
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..269
                     /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=28914
     Region          2..268
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpeghtihrl aarhadlfag dkvhaaspqg rfaegaarls gtvleateay gkhllhhhag
       61 eltlhvhlgl ygkftdgdge ppepvgqvrl rltsdrhwld lrgptacell tppevaalra
      121 rlgpdplrad adperayari srsptplaal lldqsvvagt glifvtealf raglpptlpg
      181 rrltragwda lwadlvglmr lavtrgridt vrdahlpeam graarvdrhg gevyvyrrpg
      241 dpchvcggpv srgglagrnl ywcptcqps
//
LOCUS       WP_357566498             438 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566498
VERSION     WP_357566498.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..438
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..438
                     /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=47214
     Region          1..>226
                     /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 matgsavvig asmgglltac alteaydrvt lvdrdvlper aesrrgvpqg rqlhvllarg
       61 rraleellpg isaeltacgv ptvdlheqvh wyndgyrmrr apsplialgv srplleqvvr
      121 ervaalpgvr ivagcevagl tttadrarvt gvrlrprdge pgtvaadlvv daggrgtrsp
      181 vwlaelgypp apedrvkvgv tyvtrtyrre lhhlegllga ltnavpgqpr ggivavqeqg
      241 rfavafsgml geeppvddeg mtafaeslva pqiadllrta rpesppatmk fpasvrrrye
      301 rlrrfpagyl vvadavcsfn pvygqgitva alealllrrl lrrppdrlar rffrgaarli
      361 dgpwsiavgt dlrfpevpgr rsprvrlvna yvhrlhaaat rdpalgaafl rvvnlvdppa
      421 rllsppvllr vlrgasas
//
LOCUS       WP_357566548             362 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357566548
VERSION     WP_357566548.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     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=38492
     Region          65..360
                     /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(66,68..69,72,136,141,174..179,198..199,203,220,
                     245..246,248,268..269,295..297)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mrdrvvvvsg pgrvdlveqd aaeltdgtfr vetlfsgvsa gtelsyvkgt npylnvtwna
       61 glglfqpgsa stpypvtrlg ymqvgrvves rtpavavgav gamtyghrtg wvadpvaerf
      121 vplpadldpl lgvyvahmgp icangvlhaa adlygadvrs lgdgvrgrrv avvgsgvval
      181 ltalfarrhg aasvvvldpt pqrravaeal gletldsead dpavvlktrw ahgpgdrgad
      241 vvfqcrgqaw alqlalrllr pqgtvvdlaf yqagadavrf geefhhngls lrcaqigrvp
      301 rglaptwdre rlsaetvdll raygdvireh lvsavvpfdq apavltdlaq rrrqelqvvl
      361 tg
//
LOCUS       WP_357566559             444 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566559
VERSION     WP_357566559.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..444
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..444
                     /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=46676
     Region          5..444
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mtdrtefaav daeltgrgft rmafeldkie slldllgspq raypsihltg tngktstarm
       61 idsllrafgl htgrytsphl etvrerisld gepvgeerfv atyrevepla rlvdersaep
      121 ltyfdmttal afatfadapv dvavvevglg gaedstnvlq agvavitpig ldhtewlgdt
      181 iedialhkag ivhkgatvis aaqeedaarp ilercaevga tiaregsefg vlrravavgg
      241 qvlslqglgg vyeeifiplh gahqaqnaav alaaveaflg agakrqldie avregfaaas
      301 spgrlervrs aptilldgah nphgmaatva alqeefafsk lvavvgvlgd kdaasllell
      361 epvadqvvvt rnssprampa relaalaaev fgpervevae empdaieaav amaeedvpge
      421 lsgvgvlvtg svvtvadarr llkr
//
LOCUS       WP_357566582             384 aa            linear   BCT 28-DEC-2024
DEFINITION  thioester domain-containing protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357566582
VERSION     WP_357566582.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10551059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..384
                     /product="thioester domain-containing protein"
                     /calculated_mol_wt=38771
     Region          71..185
                     /region_name="TED"
                     /note="Thioester domain; pfam08341"
                     /db_xref="CDD:462437"
     Region          <309..>355
                     /region_name="PLN02983"
                     /note="biotin carboxyl carrier protein of acetyl-CoA
                     carboxylase"
                     /db_xref="CDD:215533"
ORIGIN      
        1 mfgqrgrrwa rialatvagg alafgaaapa vaapatgvak svkgsqvrlm lngepkstsa
       61 lalkiggklv pafcidyrtn vaidgeykeg twsesqvknl gkvqwvlthg ypnadsgkll
      121 aaagaavpae adaknllyfg tqtaiwhfsd gvqlgawadg qkllgkkqyd vvkkvhdylv
      181 anatdqpepe aalsvdpasa katvgekagp ftvkgpagei avtvrggsav daegkpvtkt
      241 tnggqfwlta dgagevkvav saegsvsfgr vflftgeraa qklilgdttg ktvtakakaa
      301 faaapaesps psapaespsp sapaespspt tpgdspapst spagndlplt gspiatalaa
      361 gvallaagav avlmfrrrkl rfta
//
LOCUS       WP_357566606             363 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566606
VERSION     WP_357566606.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   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 363)
  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..363
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..363
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=39252
     Region          74..363
                     /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 mtsrsriplp rsgparaavg alaavgvaaa glaagvater alirklksdp tdryagevfd
       61 eqrydesfrl empdgtdihv evveptrprp gaptvvlvhg fcldmgtfhf qrkllaerge
      121 hrivaydqpg hgrsgrletg eydltalgrt lrevidraap egplvlvghs mggmtimafa
      181 elfpelfgdr vvgtvlmats ggllaetklv apamlgrvgt pvlymvgnvt ryggpvidra
      241 rrsttnvawl ltrkygfgtr hpspalvsyv etmnsrtsad tvtrylrtla thsrfpalaa
      301 ladtpvlvvv gdkdmitpvt hseeivrrlp haefvkisds ghvvmlehad evnealirfl
      361 eal
//
LOCUS       WP_357566688             252 aa            linear   BCT 28-DEC-2024
DEFINITION  M23 family metallopeptidase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566688
VERSION     WP_357566688.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 252)
  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..252
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..252
                     /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=25914
     Region          51..245
                     /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 mqediqnent adaparhrrt wasgrtrmvi aaaalaglgl ggvalavtgn deppvpaavd
       61 ldararaeaa eradrsdret tapatpsasa vpsptkasps akpspkatta kpkptskpkp
      121 swvipmrgaa itscygprwg tqhagidfal pagtpvraaf ggtvtkagdv gdgygisvfi
      181 dhgngylthy ahlstakvsv gqkvttgqti glegstgdst gphlhfevhq gqmwnqidpa
      241 pflrargidv ac
//
LOCUS       WP_357566706             158 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC047074].
ACCESSION   WP_357566706
VERSION     WP_357566706.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..158
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18030
     Region          7..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrpaaldwsv enctiarame ilgerwtlvv lrevfngvrr fddmrvrtgv prqvlanrla
       61 mlvergvlrr epyrepgsre rheyrltemg ldlwpvlvav lgwgdrylad pegspltvah
      121 rdcgaevrve lrcergheva rprdvvprpg pgarrrad
//
LOCUS       WP_357566777             294 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora sp. NPDC047074].
ACCESSION   WP_357566777
VERSION     WP_357566777.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 294)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..294
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29771
     Region          8..289
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mtdrdlspvt vlglgpmgra lagallaagh pttvwnrtad radplvarga rraptvaaav
       61 rasplvlacv idyaavravv epaadalagr tlvnltadtp qrartmaawa agqgvdyldg
      121 aimtpaptig gagalvlysg pervwhahrg tlaslggsad wlgpdpsraa aydvalldvf
      181 wtamsgitha falaraegit aselmpyakg isgllpdlvg dlagrvdvgn htadvstias
      241 aaatmshive aaeghgihag tlraagevva ravraghgde dfsrlvqvya kasg
//
LOCUS       WP_357566809             597 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357566809
VERSION     WP_357566809.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 597)
  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 597)
  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..597
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..597
                     /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=64160
     Region          43..573
                     /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 mtstsgpsrr tvlaaaataa asvpliaaap aqaagparsr twdltilgts dthgnvynwd
       61 yysdaeydds khndvgvakl aalvkqirae rrgkatlvld agdtiqgtpl atfyakqepi
      121 tatgethpma hamnvldyda vtlgnhefny glpllakwis qlgfpalaan avnvatgkpa
      181 flpfvikkvd vgfaapplrv gilgltnpgs aiwdkanveg klrfddmiat aakyvpimre
      241 rgadivlisa hggdsgtssy gpelpnenpt aliaqqvpgi dailfghaha evaekfvane
      301 rtgeqvllte pskwgqrlsr mdftlarekg rwkivkktaa llntntvted pkvlaavraq
      361 hqktvayvnq vvarstvels aaesryrdtp ildfinhvqt evvgqalagt syadlpvlsi
      421 aapfsrtavf pagdvkirdv aglyvfdntl eavvlsgaev rayleysaky frtlapgapv
      481 dpaaisdpav pdynydvisg ldydidisrp vgqrvtrlvl pgtdtpvadn aqfvvavnny
      541 rrsgggnfpg ivktqvyneq qeirqllidw aqargvidpa dfyqpnwklv regvpvf
//
LOCUS       WP_357566788             318 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC047074].
ACCESSION   WP_357566788
VERSION     WP_357566788.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC047074
  ORGANISM  Micromonospora sp. NPDC047074
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (residues 1 to 318)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Micromonospora sp. NPDC047074"
                     /db_xref="taxon:3154339"
     Protein         1..318
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33473
     Region          5..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mgqvielqsl trrygrttav ddltltvrpg yvtgflgpng agksttlrmi lgltaptsgt
       61 atvsgvrfag rprglrhaga lldagdvhgg rsavahlsal arsngiprgr vdevlrevgl
      121 agaarrrigg fslgmrqrlg iaaallgdpp vllfdepfng ldpegvrwvr dlfrrlaaeg
      181 rtvfvsshlm semehcadrl vvigrgrlia eqslaefaar stragvavrt pdaagmaaal
      241 eaagatlere dhdtllvtgl taarigdlal ahriavhglt artasleeaf meltadsaey
      301 rgdrrpqpaa hlageetr
//
LOCUS       WP_357566895             262 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357566895
VERSION     WP_357566895.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 262)
  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..262
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..262
                     /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=28501
     Region          4..262
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mggplvfahr gasfdlpeht laaylralde gadglecdvr ltrdghlvcv hdrrldrtsn
       61 grglvsartl aeldaldfgs whpgsapdgd lppdeshtrl ltlarlldav laagrpvrll
      121 vetkhpsryg snverrlvsl lrrygladpa pddrvqvtvm sfsplavrrv relaptlptv
      181 lllevlprwl rlgrlpfgtr iagpgiglvr arpqllpalr aagnqvyvwt vneptdlelv
      241 laagvdgiit drpayalarl dr
//
LOCUS       WP_357566915             416 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein, partial [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357566915
VERSION     WP_357566915.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 416)
  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 416)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         <1..416
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
     Region          16..394
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 grapvskgvl rgvdraafav alagrlrrag vpaglttvdd fvralaaspp dsmsslywta
       61 rislvrrhtd vpafdrvfaa ifadppplpr pqrsapptdg pddvyvrvpa dtddagpggg
      121 lpwatlpptv aetpehdsel rlperrpsah trladrpfde ldaaqvtqlg dalraavadw
      181 ptrrtrrhtv gssgarialr atiararrtg wepvevvrar pvrrprrvvl lcdvsesmra
      241 qataylhlmr afavvadaev fafattltrl tvvlrhtsaa eavaqasaav tdryggtria
      301 tnlrallash haeavrgavv vigsdgwdsd ppvdlaavma rlsrrayriv wlnpragapg
      361 faprvggmaa alpycdrmlp agtfqdllvv arqlqsvtct dgrkwptltp apriia
//
LOCUS       WP_357566979             270 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357566979
VERSION     WP_357566979.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 270)
  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..270
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..270
                     /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=27671
     Region          2..269
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mrvlvvggsg llgrsvcrrg lgagwsvvgt fhsgeiavpg vaarrldvtd raavrglvae
       61 vrpdavvgtp yrygdwavta dgaahvalaa aevgarlvhv ssdalhagrp vpyaddeppt
      121 pvhaygaaka aaetavraid pgaalvrtsl ivgegskqiq lcrealagra tlfsdelrcp
      181 idvtdladav lelvasmyag vlnvagpdav sraelgllva erygldpagl rtttsaatgl
      241 vrpldvrlds araaallrtr lrgvrevlap
//
LOCUS       WP_357567117             959 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567117
VERSION     WP_357567117.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..959
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..959
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=102358
     Region          <7..952
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mltsvnspgf ligrgpelte lwdavqrlrl gaggvvwieg epgigksslm aaaahvgrel
       61 gcqvsegvad qlahppllgv lldcleirpr stdphraria ellsdrrsvl dladaghaaa
      121 avemvvalvd elctagpmml lvddvqwadd asidvcrrla svaaylplll vlsyrpgahr
      181 stvrrlrava rrravlrvpl gsltpesvrd llaalvgvpp gdglvrlaaq aagnplflre
      241 lveslvredl ldigaqaevr dsaagvvprs laaalegrls svpagtvelm raaallggef
      301 avtelaallg rpaidfsadl qeavtagilv eagprlrfrh pllrqalydg mpaalraalh
      361 ldvaralest svepqrvaqh llasgvvgnr warrwlagag pvlagwaphl aaellrrevd
      421 hdpgdedvrv vlrmnlarvl iaageheeaa qrvrqtlglv vdpddrgqlh wmlaralcsg
      481 ghndaavanl hralagadlp dawrarllas lamfqragsg dlaaadatar dalrtaavag
      541 dafatayalt glwashsvrr qhrlalhsae aaiealsfva dhvdlrafal hgrifslqnl
      601 srwtdaeaal ceardflraa nrmddttagv taavllfwlg rwddalaeld avaqdtstst
      661 yrglrdggpg rlwhgvsali aghrgervra aahlragldr pvvtvadren ldfllvarsl
      721 aaeqdgdlrm aldhlaalld rrpgemtlth qwlprfvrla lavddrsaae agvraclaea
      781 aaeqvparaa asadrcrglr sgdpatirsa vahyrasgvp velagtledl avvlaqrgdi
      841 aqartalnea idlygtfgat wdirraearl rgrgirrgvr garsrrpghg wdaltpterk
      901 vallvaagrs tpdiaqnlfl trrtaqthis rilaklnmhs rveiagavlr rasegvveh
//
LOCUS       WP_357567155             409 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567155
VERSION     WP_357567155.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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..409
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..409
                     /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=43329
     Region          210..393
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkhalrrlrt gavalaactl glsllsvpaa eaysvaplap qserapesnq fsaegvttig
       61 elrtvdssls yatnggtqii qhpgatyvkv hfsalrlaeg dhvtvssrdg kesyrydrhl
      121 nratgsdytt dgqpgfwams vegdtavvtl hssrpsrgsa atidrfwrgy drteiaahnf
      181 saqsvcstda rrdvvcyqns hpteyargra varllisggg lcttwrvgdt nrmltnkhcf
      241 stqsavsgse mqfnyqcatc gganpgagtr vsgatlyrvs sggsnqldya lfsvnnfaai
      301 qgfgtlylat tatsngtriy vpghgdgsak rlsiyedtqn gatcavrnan yntwnisysc
      361 dtsggnsgsp vlnashrvia lhhlggcpsn qgakahliyn eiaslidng
//
LOCUS       WP_357567182             886 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567182
VERSION     WP_357567182.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 886)
  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..886
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..886
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93153
     Region          4..885
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtpdhdwsrs pagrttlpel lrghrraagl tqaelasrar vgvrtvrdle rgrsirpqrt
       61 tvellagala ltgtsraafl aaargagvep aspdatsttf avggnatsaa apadpsvalp
      121 ppvaligrer dltelagmlt aergprlvsl vglagvgkta latsvahlva aahpagvagv
      181 lvgegadgpd vlaasmsvlg varlpelval lagrptllvm daverapgpv aatlhrllga
      241 lpslrvlvtg rhpvglpger vwpvapldvp ppeaehsgle swpavalfta rlaqvrrepp
      301 tpaelpalaa lvrrlgglpl aielmaargr lldltelldr ygdrvldlat padasahpvw
      361 dapealgsrt sgpdtraavs vavtlrdava fsyrllasde qaalrqlavf gnrwsvelae
      421 emladeadrd gtvaidpvpl ldrfvelgll svrgsgsfrf rlldavrdya veqaagagel
      481 tcirrrhaev iarlvartas dltgprlpda vhrldemssd issslahatt ddpltalrla
      541 acltrwwrfr grdvvgrqwl rrlladplta dadpllrgwa algvarlaae hgagaeelst
      601 araalntfqq agdvtgelea rnvlgtllis vgrqdeareq aeallrlaar ngrtrdlava
      661 qnslawheir agdlaaarrr laavdrlaae sgeqrlrvlg wanraevarl egwyadaidr
      721 grraivalse lgdpgrrrrv lgtvglalaq dgraaeatev ltelraggve alparptvpr
      781 prprsddaal awggpeaglc aliegnlalh rgdrelaaew faaaadhagq drrdavealv
      841 glaastadps vldrldrvca eggirllpqe sgllyallaa rggpaq
//
LOCUS       WP_357567197             378 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567197
VERSION     WP_357567197.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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..378
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..378
                     /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=39253
     Region          131..169
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <136..260
                     /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          174..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <225..>315
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
     Region          225..255
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mnsgpfthtt rpasvrrsga lagtaallll afgaaacgta dpktapapae sataaapang
       61 dtsaagtggt ggtpgappsg gsstntpsvr igklfygpar npvgengnlr swrpgespvr
      121 lmelphtaai lnvnvspdgr rvawsgedae dsgdlyianv dgsnkqkmrs evdpycvtpa
      181 wspdgrqllf rvdlpggghg rfglldtrse krtvrwwrte psachavwsa dgktiamttd
      241 vgvtvdagvv lygtdgtkkr aipgfsrdgw hsndiaslsp dgsriallrm klgeddgnla
      301 rdlranvvld trtgkqvslp lggrtlhqvy fqsdgsmvvr veagsgyavl lvdgdgkkvs
      361 etaepaslkd eqilavvd
//
LOCUS       WP_357567227             257 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357567227
VERSION     WP_357567227.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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..257
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..257
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26869
     Region          5..251
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mgefvrlett dgigtirler ppmnalntqv qeelraaata atadpevrav ivyggekvfa
       61 agadikqmad msyvdmadra anlssalgai aripkpvvaa itgyalgggc elalacdwrv
      121 vaedaklgqp eiklgiipga ggtqrlarlv gparakdlim sgrmvdaqea lrigladrva
      181 paaevydtav amitpyltgp vqalraakla vdggldmdln sglawesqlf aalfatddrr
      241 egmaafvekr kpgftgr
//
LOCUS       WP_357567244             817 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357567244
VERSION     WP_357567244.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 817)
  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 817)
  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 817)
  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 817)
  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..817
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..817
                     /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=90721
     Region          9..>639
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mvsrqalydg wtvraapgaq vpeeiagrsv patvpgcvht dlldagligd pylddneral
       61 awigrtdwvy qttvvhragd dervdlvcag ldtvatltvn gvevgrtanm hrgyrfdvrp
      121 llrdgnndlv vtfdsayrya ealqerlgdr pnaypepfhf irkmacnfgw dwgptlvtag
      181 iwqeislhaw starlaevrp latmdgrdgr vevhveverv advpltvraa vagvraevvv
      241 pagertavlt ltvrepalww prgygeqtrh pievtlhapd gdkldtwshr igfrsvrldt
      301 tpdehgtpfa lsvndvpvfv rgvnwipdda fptritrerl aerfdqalaa nvnllrvwgg
      361 gryesadfyd ladergllvq qdflfacaay peeepfgtev aaeaaeqvtr lapypslvlw
      421 tgnneniwgw hdwdwqqala grtwgrgyyl dvlprivgel dptrpywpgs pwsgteaihp
      481 ndpahgtthi wdvwntddyt kyreyvprfv aefgyqappa yatlrralsd vplahdspgm
      541 ahhqkaaggd aklqrgldah lpapadfddw hyltqlnqar aiqlgvehfr shrdvcagti
      601 vwqlndcwpv tswsavdgdg rrkplwyalr hayadrlltv qprdgglalv avnetaeawt
      661 vpamvtrfti agepraktsv nldvpayssv vlalpadlar pedarrevlv aeaggtaqra
      721 lwffaedrev dwpaaawdat vepvdggqrv qvtartvlrd ltlfpdrldg sasvdtalvt
      781 llpgestaft vhadglldea altsrpvlrc vndierr
//
LOCUS       WP_357567268             202 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357567268
VERSION     WP_357567268.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 202)
  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..202
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..202
                     /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=22005
     Region          7..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 masaeptarp searlkllrt atrifyaegi havgvdriia eakvtratfy rhfpskddli
       61 laylrevhql ergmvdeala anrspvdpll aiatsiaqni qspgfrgcaf lnaaaeypdt
      121 nhpvhqelma hrqwfldtit tlmaqvhegt adpaarhfvm lrdgamaagc lsdptlvset
      181 flrgvegllr vnserqsaes ag
//
LOCUS       WP_357567270             479 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357567270
VERSION     WP_357567270.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 479)
  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 479)
  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 479)
  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 479)
  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..479
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..479
                     /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=49983
     Region          5..477
                     /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 menatydviv igagpvgenv adrvvqgglt aaiverelvg gecsywacmp tkallrsqta
       61 lraarqlpga reavtgelda aavlrrrdsf ashwqddgqv swlnsagial yrgqgrigsh
      121 rivevtgadg vttsltarha vviatgssal vpdiaglrea apwtsreasa asevpgrlai
      181 igggvvatem atayaglgsa vtvlvrdgvl tqaepfvger vtqslreagv avqlgaeats
      241 virdgdgtvh itltdgdqve adeilvaigr tpnthdvgld ridlkpgawl tvddtlrvvd
      301 dagaligdgw lyaagdvnrr vllthqgkyq aravgdviva ratgeaaddr qwgrhvatad
      361 elavpqvvft dpevasvglt aaaaeaaglr irvvdydlaa vagaalhadg yqgqarmvvd
      421 edrrvivglt lvgpdvaeli haatiaivge vplerlwhav payptvsevw lrlleaygr
//
LOCUS       WP_357567278             273 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567278
VERSION     WP_357567278.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 273)
  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..273
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..273
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28117
     Region          1..268
                     /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 mtalrtvtvd gcpvhvldsg sghavlmlhg sgpgttgsga wattaqalgt swhlvapdqa
       61 gfgrtplpag sraglrlwte qaaglmdalg ieyydvvghs mggavalala aarpeqvtrv
      121 vavstmgapg aplsaeldav waapagpiga rdmlgrlvld qalvtdsavd araaamraga
      181 aafaslfppp rarwvdeltl saqtlaavra pvllvhgaed rvtpletaaq plldhladvr
      241 lhvfgrcghv psiehpqefr qllscflrpd rgh
//
LOCUS       WP_357567370             533 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567370
VERSION     WP_357567370.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 533)
  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..533
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..533
                     /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=56444
     Region          21..531
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mttldsavdp sapsylanra allerlteld aaldqaragg gdkyvtrhha rgkllpreri
       61 ellvdadspf lelspvaayg sdfpvgasvv tgigvvegve clivandptv rggavnpwsl
      121 aktrrageia lanrlpmvnl vesagadlpt qaeifipggr vfrdltrlsa agiptvsvvf
      181 gnataggayv pgmsdhvimi rdrsqvylag pplvkmatge vtddeslgga amhagtsgla
      241 dylaaderdg irlarqcvrr lnwrkqgpsp rtavpqppky dpeellgits adlkvpfdpr
      301 evlarildgs dfdefkpayg dalvtgwgel hgypvgvlan argvlfsaea qkaaqfiqla
      361 nasntplifl qnttgymvgt eyeqrgiikh galminavsn stvphltvnl gasygagnyg
      421 mcgrayeprf lftwpnaksa vmgpaqlagv lsivarqaaa argrdydeds daamrlmveq
      481 qiesqsgalf lsgrlyddgv idprdtrtvl glclsaihng pvkgadgfgv frm
//
LOCUS       WP_357567376             805 aa            linear   BCT 28-DEC-2024
DEFINITION  penicillin-binding protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567376
VERSION     WP_357567376.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..805
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..805
                     /product="penicillin-binding protein"
                     /calculated_mol_wt=85813
     Region          38..708
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
     Region          720..778
                     /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"
     Region          720..777
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
ORIGIN      
        1 mrkrdhnvlt naasllvcgl lagvvvaaaa fpavamsgla akagaetfga lpteltvara
       61 pqisyllasd gktplatmyd enrrdvklpd islpmqkaii aaedhdfykh ngvdingvar
      121 afvnnqsegs grqgastltm qyvrlaiays athpadvvaa tedtsarklr emrlalqvdk
      181 efskdeiltr ylnlasfgng aygiyaasqv yfgkppsklk ieeaallagm vkapttndpt
      241 telgyplald rrnyviqnmv dikaitqqea daakatklvv kdkrtpngcv aanvnewgff
      301 cdyfyrwwmd qetfgstryd rerrlksggy nvvtsidiqa qraadkavrk aksvnskeaa
      361 mvavvepgtg rvralavnrq fklddpknpk nkissdpaks kkkirgnypa tvnplltggd
      421 gitgyqagst fkmftivaal ekgiplghti napkqfrsey iiqpgpaacp gtnlycptns
      481 tesmagvhnm wsafgrsvnt yfvplqqqvg aenvvkaakr lginfrsqed ldlekgahqw
      541 gaftlgvsqt tpldlanaya tlaadgkyce pipvqeirdp egnkldianp rcekrfstev
      601 araavdaarc pvgdkssssr ctgatagnvr gdvgypvagk sgttdsekta alvamtkqys
      661 vagimadpdw pqtnvkmkhk eqdginppvw etlrdamkgk pkfdfeapgq kislgdqrsi
      721 pdvkcvsveq aksrlkgagf epvvsstkvp ssckagdaag tspdgrtikg gvvtievssg
      781 ggtpgntngt pggqpggrpg grpgg
//
LOCUS       WP_357567445             843 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567445
VERSION     WP_357567445.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 843)
  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 843)
  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 843)
  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 843)
  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..843
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..843
                     /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=89565
     Region          150..825
                     /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 mtsdpaddpf drlgvrgtpg rllvltaavt ltalaaaavg ltlpvrlpad dplggparfg
       61 iavavlalaq farlrfrsaa gmvsitwgea alivclyltp agwlpsatll gtglawtlls
      121 lhndrrpale ivriaaslaa asalavsvtt algrpllspp tpilalavia gsvtyllvta
      181 wlggvtlglr hglpigppll aalrgkllmf vgnvavglvv valleldprw llllppllwl
      241 lqqtyryrlr sdqerrtwra faeataalnq ldergvasaa vtgaltlfna elvdvdvara
      301 dgrwhlyrgd aggqlvdret gppdqsepdk helsralsvg atpvgrlrvr fprsapptar
      361 erdavaafgd alaaalhdaa thhelrlvta rssyeavhdp ltglanraam lskgdqslrq
      421 lshdhpvall lldinqfkev ndtlghaagd qllrltanrl nslvragdll grlggdefal
      481 lltavpvlgd raapmahalr qareiaerla aptevagvrm sievsvgvvv aaagtadlte
      541 llrradiamy qakegggnva aydgsrdaas tdqlallael realkvddql vlalqpavdl
      601 atgaptgvea lirwqhprrg wlnpadfirp venseqlgtf tryvlnkals vaaswaregl
      661 dvpisvnlsa rslldprlpa eiaealrrhq vpphrlvlei tetvvmsele videvlatlr
      721 smgvqlavdd fgtgfssltf ltriavdelk vdrsfvirma dspeaaaivr ttvglahelg
      781 lrvvaegvet aeqrmalael gctsaqgyhf fkpmpadkig avlgslrdsa esnvfrlrad
      841 gas
//
LOCUS       WP_357567499             165 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567499
VERSION     WP_357567499.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=18142
     Region          4..144
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 matpdyivgl rkhvghdllw lpsvsavvrn dagelllgqr addgrwsvis gfvepgeqpa
       61 talvrevree tglevtpvrm ssavshphty pngdrceyln lgflcrlvag tarvnddesl
      121 avrwfpldrl peldkhallv iayalrenkv agylepgttw ddvpd
//
LOCUS       WP_357567506             283 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567506
VERSION     WP_357567506.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 283)
  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..283
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..283
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30596
     Region          14..277
                     /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 mpfitvgten staidiyyed hgsgqpvvli hgfpfngatm eklanpllna ghrvitydrr
       61 gfgassqpdt gydydtlaad ldtlmteldl rdtilaghsm gtgevtryls rygservsrg
      121 vllsplapfl rktsdnpegv dgsvfdgfkq aiaadrfayl tafctsffny dktkgkqvse
      181 eafqahwaig rlasasamyq cidaiatdfr advprvdvpi livqgdqdav lpypvtgqrl
      241 apmlpngklv tlkgaphgip wthadevnka imdfigapam ara
//
LOCUS       WP_357567575             387 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567575
VERSION     WP_357567575.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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..387
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..387
                     /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=38779
     Region          3..387
                     /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 mttdvmvtgi gavschgtga dalwkamtga aarrpdrpad ppavmdrpli hlapggdltg
       61 aratrfavaa areawrdagl gpaeagagva vvvgscmgep ginesdrrgd vapeqgwlpp
      121 frlaagvaga lgvlgtaqdi anacaaggya lgaaadmira geasvvvagg adaysrvalg
      181 cfnrlgavdp qrcrpfdrnr ggtvfaegaa mlvlesreha eargaavpgr glrlagtaws
      241 cdaghptape peaeqivram seaiaeagga egigcvvphg tgtrlndale sralhrvlga
      301 raarvplysl kallghagga sgalgavaga qilrhgsvpp nvrldeqdee cdvslpqdgp
      361 vpldggrvlv naygfggnnm slvleaa
//
LOCUS       WP_357567587             388 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357567587
VERSION     WP_357567587.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..388
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..388
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41608
     Region          159..367
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mgglfslwrq rvadnahrav dayqeelley rnlaamprvr semldfavfl rqrtvdlaad
       61 sapfhvqdld lmaamgrqrg ekgltltaqr qvllvhtrlt lrevyeaagp ndiaatmhtl
      121 awlapaglaa qgaytrgwie gqrrtlataa qvrlltvmll agddsatdla rglhmpvpdh
      181 vvatvvrvag gspgpdqaar defagallkt hwmplswpep hevvalipss pggrqpaver
      241 glalardvas mtgrpcaagt apgrvrafgd avalarqvse vapvravprh aytvtdvfae
      301 lgaarlaevg qwlqvvgaql dagpdlvatl dayyqhdmnr ldtaaalcih prtldyrltr
      361 vrdltgleag strgvrvlst avarilag
//
LOCUS       WP_357567611             466 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567611
VERSION     WP_357567611.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..466
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=47560
     Region          1..466
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 maptallddl raalgddavl tdpdllrmhq rdeadlcaag vplvvtrprd teqvvaviqa
       61 aarhgvpvvp qgartglaga anavdgavvl stvamneire idpvsriavv qpgvvnaala
      121 gavakqglwy ppdpgswqss tiggnvatna ggmccvkygv tteyvlglev vlasgevlrt
      181 grrtakgvag ydltrlfvgs egtlgvitev tvalrpapad sltlvavfps tatagaavae
      241 iaargltpsl lelldqthll aieayqpmgl rtdaqallla aadtgsraad dlavlaevce
      301 avgadevyaa tdaveaaall qarrlahpam ekfaadaypg gngglviddv avprgalaal
      361 ldgvariave cevpigvvgh agdgnmhpni vvdradpasv ergrrafdei mrlgldlggt
      421 ctgehgvgll krdwlareig pvgvrvhqai ksaldpagll npgkvl
//
LOCUS       WP_357567675             228 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Micromonospora
            sp. NPDC048843].
ACCESSION   WP_357567675
VERSION     WP_357567675.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 228)
  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..228
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..228
                     /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=24085
     Region          <29..143
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 maqltvsgrd tvyvwvdrda ggqpdpaavl vrragalllg rpetelvlth dregrpvvrv
       61 devtgsvela vsvsrtpglv vvaarradav gvdverirpl palalarrwf ppaelawlgd
      121 rpeadrtadf lrlwtakeav gkalgrglrg gglrrlmppp glplrqvpga eplrvghprl
      181 gggvvlavaa rasaqvdvev vqrpghgvta ersasverts lpvvvrgn
//
LOCUS       WP_357567652             289 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567652
VERSION     WP_357567652.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 289)
  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 289)
  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 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   5  (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   6  (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   7  (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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..289
                     /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=30658
     Region          24..226
                     /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"
ORIGIN      
        1 maavtdagea rgyrpsatmp faaefrrqas rrrtqlalgf mvllpliili afqfdsggdd
       61 dngrnefasl velatsggln ftlfsifvsa sfllvvvval fcgdtvasea swgslrylla
      121 ipvprarllt vklvvalays glallllagt allagtlryg wsplrstvaa eleptegllr
      181 llavlgylav vllvvaglaf llsvitdaal gavggavllw ilssildqit algalrdflp
      241 thfstawlgl lstpvqtddv vrgcisaisy atlfwglafw rftrkdits
//
LOCUS       WP_357567693             161 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567693
VERSION     WP_357567693.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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 161)
  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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..161
                     /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=17951
     Region          8..145
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mtvytprraa rvllvdaagr vllfegfdpa rpghrywftp gggldqsesp aagaarelae
       61 etglrldpaq lgepvwsdat efsfdgiwyr qeqdfflfrv dswrvdttgf ndierrsiad
      121 hrwwvpdela asgdrfyppe lpalltrlgq sttagqdeas c
//
LOCUS       WP_357567765             799 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357567765
VERSION     WP_357567765.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 799)
  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   3  (residues 1 to 799)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 799)
  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   5  (residues 1 to 799)
  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 799)
  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 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..799
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87308
     Region          19..775
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mqtgsatdqq qsttaladde twrirrtead vdrlgetesi falgngwigw rgvldegapc
       61 gmpgsyvsgf herrelsype egygfpqasd tvisapnaal irlwvddepl dlrtgtlrsh
      121 ervldlrtgv lrretewisp agrgvrirst rlvslprrpv aavryevepl daavevrvcs
      181 dllanekvpe rsddpraasv ptdpltaety ratgldgvlv hrtersgqrv avavshlleg
      241 pdtatisgdc tpdrvrltvt grlhpgerlr ltkfaayewa avdatpadel aalvaaeada
      301 aradgfdall sdqraaldaa wqvadvrldg dpelqqavrf amfhliqagr pesdrtisak
      361 gltgngydgh vlwdtesyvl pvltylapav arsalrwrha hlpeareraa elrltgatfp
      421 wrtiggress gywpagtaal hvnadiadav lrylaatddq gflaeaglel lvetarlwhg
      481 fghwsdegdf hlhgvtgpde yaalvddnvf tnlmakrnlc gaadaaeahp elagrlgvdr
      541 devagwraaa dtmavpydse rgvhqqaagf teqpewdfan tgdddyplll hfpylelyrk
      601 qvvkqadlvl amqlcpgeft adekarnlay yqartvrdss lsaapqavla aevghldlay
      661 dlfaesvlqd ladlgdktad glhlaslaga wlalvqgfgg lrddrrvlsf dprlprridr
      721 lafslrwrgh rlrvtltpae aryelpdaaa daevelwhhg eslrvtgaep vtrsmppvpd
      781 pgpeppsppg rrptrrsad
//
LOCUS       WP_357567766             300 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357567766
VERSION     WP_357567766.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 300)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..300
                     /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]"
                     /calculated_mol_wt=31016
     Region          38..156
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 madtaslrar gtafwaeaaa gwirhadrqd etgrplgaaa mdrlaalpae rildvgcgcg
       61 gttaeiaaav getgaaigvd ideamvtaar rrfptdghpg iqfhvadvet ldavpgapfd
      121 aafsrmtlml ladpvagcrt irrslrpggr laatvfrdsg vnpwlsaaml gaaphlgplp
      181 plpvgdepgp fafadperla rilttagfta vtitqcdvvl etpddadava ewlievgpag
      241 aayrtappag qasaragaar llgrfrkpgv gyrlptglwl vtanaagtpt hhepredkiq
//
LOCUS       WP_357567794             506 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357567794
VERSION     WP_357567794.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 506)
  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..506
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..506
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=54763
     Region          17..78
                     /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 mivsvapppe laqsraalgr rlaearksag ytqetlaplt hygrstianv ergrqsigrd
       61 fwvrcdeilh tggvlaaeyd rlrvlvtrst aghldggrar gatfatrtet pvptalslla
      121 pqaangdlap qtyvvdlwap agrffpglai payvhpavae dgrvlaavpa gycddrllrt
      181 prrslvvgri etdqgaqlfg ldarharqrl apaapdarlv ipqayqldel vlallwavan
      241 ldealladda rieqataela syeqmsrsav shdlaadlsd vgrmwlgsvf caghihrhad
      301 altstpaywt reqrgeeast wllfahkqry ldltaarags hriirafcip raavdasprg
      361 erillllavt lmesygievv itdepeyagt pgfvtdsdrh avlanwvgaq giwhvdvtdd
      421 hrtvrqygaa inhasgrsvi aaaspparlr vlaeyldlnw etlasrcrdl adqgcaavvq
      481 prsrhlstag idracrylad aaaltd
//
LOCUS       WP_357567896             249 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567896
VERSION     WP_357567896.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..249
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=25619
     Region          15..247
                     /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 mnaasdkpaq dagmptvvlv hgafadsssw ngvianlkrr gypviavanp lrgvqkdaay
       61 aravvdsvsg pvvmaahsyg gcvmteaadg apnvkalvyv asvspdvges vadlitkfpg
      121 salltsvkmv ptplddggtt maqyihqnqf pavfaadvdp daaelmavtq rppteaaqte
      181 svtkaawkti pswtlittqd kgippdlqrf lakragsttv eidashavav sqpgpvadli
      241 dtaarataq
//
LOCUS       WP_357567985             405 aa            linear   BCT 28-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357567985
VERSION     WP_357567985.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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..405
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..405
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40213
     Region          1..303
                     /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 maylvpvlaa rrldpadlst laaalglvai vgvpglglql avavhrarhg asdtrrltav
       61 tatvcavtlv aatpllvtal dlpvempall avttaaivls srslgelqgg qrfvrlaigm
      121 avlaagrygg viaglllgag ptgalavgal taaltpavla rlarepqlss taprltvaqv
      181 vagcgatlam lvvsyadlll srqllsasds gaysvgtvls kgalwapqva avlalprlar
      241 gdrrsrtval avtggcgavl vlastlaggl afrfaggpdy dhlgryapvf aavgalyavt
      301 fvllndrlaa garwaaaplw vgvaglvavt atlrphtipg lllaavgtai vttalmavta
      361 rrpapvpate ptspprasps avggrssppd raddprtpgp aappg
//
LOCUS       WP_357567986             267 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357567986
VERSION     WP_357567986.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 267)
  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 267)
  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 267)
  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 267)
  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..267
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..267
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27661
     Region          10..243
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlglpahvta clfdldgvlt qtarvhnaaw tqtfdeflrq ratvsgepfq pfdpgpdynr
       61 yvdgrpradg vrsflasrgi vlpeggpddp peaetvnglg nrknvlllqr lrtagvevyp
      121 gsvrylkaaa aaglrravvt asanggevva sagfepllea rvdglvaraq glrgkphpdt
      181 flagarvlgv dptqaavfed alsgvaagra ggfgyvvgvd rvgqadella hgadivvtdl
      241 adlldsadpp aphrtatdpl aaergsg
//
LOCUS       WP_357568113             604 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568113
VERSION     WP_357568113.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=64644
     Region          1..604
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrefsvppiv tvgdaanltd pvwdnaevap dtvqfarptp radgtvtewt evtclqfrde
       61 vaavarglia agiepgvrvg lmsrtryewt lldyaiwavg avtvpiyets saeqaawile
      121 dsnavavvve seahaaliag vrhrlpelgq vwqidsggvd elvttgatve laeverrrka
      181 vragdlatii ytsgttgrpk gcvlthrnmy adianavpvl pnlfnagast llflplahaf
      241 arliqigvvq aratmahcad tknlvaelqa frptfvlsvp rvfekvynaa kqkaeadgkg
      301 gifaraeqva iaysealetp ggpglalraq hvvfdrlvyr klraalggrc rdaisggapl
      361 garlghffrg vgvtvlegyg ltetspaaaa nlpsgtrmgs vgrplpgvtv rieddgeili
      421 sgelvfrgyw rnetataeti sadgwfrtgd lgqldsdgyl sitgrkkeli vtaggknvap
      481 avledlvrah plisqcvvvg drkpfiaalv tvdeealptw lekagmplda tieqlreheg
      541 lrkeiqaaid aanqavskae aikvfrvlph dfteatgelt pslkvkrqvv hktyaaeiad
      601 iyrg
//
LOCUS       WP_357568124             401 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568124
VERSION     WP_357568124.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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 401)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..401
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..401
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42946
     Region          49..382
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mptvrpvgar gitrrglvga alavgagvpv giagrataai adsgpvrltl prptgpyrvg
       61 vvplhlvdrs rpeplagpgr yrelmvsvwy parnerrypr spwmtaasmr mllesagfdp
      121 haalapltag hegapvrhpg rrlpvvlysh gagshrsdtt ivvqelashg yavvtvdhty
      181 dgfgefpdgr vtvqeedvds tpwtytrdvr fvldqiadla aggnpdvdha plptglgaal
      241 dlsrigmfgw skggtatalt mgtdrrvrag lsldapmlsq plpsadlsrp fmlmtaefsr
      301 aaepavaeff thlrgwrlnv qaadaihssy gdnqwlvpql arligmsdee lagwvgaldp
      361 aravrigqay plaffdlhlr hrgghllngp srsfpevafi p
//
LOCUS       WP_357568136             378 aa            linear   BCT 28-DEC-2024
DEFINITION  epoxide hydrolase family protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568136
VERSION     WP_357568136.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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 378)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 378)
  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   5  (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 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..378
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41483
     Region          6..111
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          77..>219
                     /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 msdtairpfr vevpqtaldd laarldrtlw padlpgaggs ygmsndrvrt lvdrwrgefd
       61 wravearlna npqfvteidg eqihflhvrs srpdatalvl thgwpgsvle yldviaplte
      121 ptdrdapafh vvvpslpgfg fsgptraagw nrfriarawa elmnrlgyds ygavgndags
      181 mvapelgrvd pgrvlgvhvt qlfsfpsgdp aefaglsead qaalghlqwf yenkfsfnqv
      241 hsqqpqtlaf aladspvgll awnaqlfdes ldadfilanv alywftgtaa sairlyweda
      301 hagepptept taptalamfp gdfqsirrfa erdhanivrw tayetdvdgr gdvgghyaah
      361 qatevlvadi reffaslr
//
LOCUS       WP_357568143             130 aa            linear   BCT 28-DEC-2024
DEFINITION  cytidine deaminase family protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568143
VERSION     WP_357568143.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Navaratnam,N. and Sarwar,R.
  TITLE     An overview of cytidine deaminases
  JOURNAL   Int J Hematol 83 (3), 195-200 (2006)
   PUBMED   16720547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..130
                     /product="cytidine deaminase family protein"
                     /EC_number="3.5.4.5"
                     /GO_function="GO:0004126 - cytidine deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009972 - cytidine deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=13311
     Region          5..120
                     /region_name="Cdd"
                     /note="Cytidine deaminase [Nucleotide transport and
                     metabolism]; COG0295"
                     /db_xref="CDD:440064"
ORIGIN      
        1 memrdtdral vqaatavskl rcrsqhhtva saartadgrv ftgvnvqhat ggacaelvvi
       61 gtaatqgvta letivtvadr grevvapcag cqqvlrdyfp qllvvvgpmd alrviplsel
      121 paetgsgsag
//
LOCUS       WP_357568165             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568165
VERSION     WP_357568165.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30369
     Region          6..>154
                     /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 mqdiqthtlv ipgvdlvydv rgplpptgah rallmigqpm aaegftalap hltdrtvlty
       61 dprglgrsvr kdgrsdhtpq qqaadlhalv qaldvgpvdv fassggavta lelvashpdd
      121 vatlvahepp inavlpdata aeraragfye ayqakgsgag maafiamtsw qgeftdayfa
      181 qpapdpamfg maadddgrrd dpllsqnswa itdyrpdasv ltaaptrivv avgeesagty
      241 tartalglaa llgqeavvfp shhggflgge fgyagkpeef aarlrevlda g
//
LOCUS       WP_357568199             221 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568199
VERSION     WP_357568199.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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 221)
  AUTHORS   ter Beek,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..221
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..221
                     /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=24268
     Region          <3..218
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpavqhnllw laalfvvatp fgmflavlld kelrgsrfyq talylpvvls laligfvwql
       61 lysrdqglin avfgssidwy gdssvniwav mvasgwrhvg yimllylagl kgvdpslrea
      121 aavdgasesr tffrvvfpvm rpiniivlvv tvieslrafd lvwvvnkgrn glelisalvt
      181 qnvvgeasri gfgsalatim lvvslvfiti ylatvmrenr e
//
LOCUS       WP_357568211             362 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568211
VERSION     WP_357568211.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=38560
     Region          65..360
                     /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(66,68..69,72,136,141,174..179,198..199,203,220,
                     245..246,248,268..269,295..297)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mrdkvvvvtg pgrvdlveqd aaplrpgtfr vetlfsgvsa gtelsyvkgt npylnvtwna
       61 dlglfqpgaa stpypvtrlg ymqvgrvves etpavavgtv gamtyghrtg wladpvaerf
      121 valpddldpl lgvyvahmgp icangllhaa adlhgtdvra lgdgvrgrrv avvgagvval
      181 ltalfarrng aasvvvldpt pqrrqvaeal gletldtead dpavvlktrw ahtagdrgad
      241 vvfqcrgqaw alhlalrllr pqgtvidlaf yqggadavrl geefhhngls lrcaqigrvp
      301 rglaptwdre rlsaetvdll raygdairkh lvsavvpfde apalltdlad rrrqelqvvl
      361 as
//
LOCUS       WP_357568384             451 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568384
VERSION     WP_357568384.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=47995
     Region          107..447
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrlglrtrv taafavgall lsasmalisy eltrrslldd rerialraay fdaavvhagl
       61 dtdtpdvvev lrsldtggsr rpvlhlngew yaraadpgtt aaipdellrv vsagepavqr
      121 vrvdgqpvlv vgvplsasat yfevnslrel eqtfrvlala ltsvavlvag agatlawyat
      181 rhglrpltav adaaekiaag dftarldpat dsdltrlsss fnqmvdrlal rierdrrfaa
      241 dvshelrspl qtlaaaasvl arrrehqder tataaglvad eidrfqrlvn dlidlarsdq
      301 pahrapvdvv elaretcday dlpgalvrla pdvpptwqve rrriaqilan lldnavtygg
      361 gpvavhlgrd ggsgvievdd dgpgvpvedr eaifdrfvrg raahtrgagd gtglglalva
      421 qhaaahagqv tvadrpggga cfrvtlpesl s
//
LOCUS       WP_357568391             431 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568391
VERSION     WP_357568391.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 431)
  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..431
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=45759
     Region          162..420
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrdhtdtdfg trrltkwlda rltrlgvtkv fprdcllaav ltvltfvllt slfwfvaped
       61 gvsfdraraw llvaiccaqa mllclrrvrp llclalvvgl qlpiigfslp eatirglapf
      121 vvaytvgsll pvrrallavs avvvvesiga avvvtpdllt avayvsasal tyasatfvgg
      181 yvatyrryve lvrvradeav reqrtkvqaa igaersrmar elhdvaahhl sgmvvqaaav
      241 erlidrdpaa akagvawirs qgketldnlr lvvgvlrgrp gheggdgaap vpglgmlddl
      301 vrtagnlagp vefvregeqr evppiadval yriaqeslsn arqhapgaaa rvtlrfeprs
      361 vslevvnepa tprrvpaart ggvglvgmre raqligatft agptaaggws vaatlptsgp
      421 aafrpkeeap a
//
LOCUS       WP_357568415             522 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568415
VERSION     WP_357568415.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 522)
  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..522
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55883
     Region          125..380
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdeltritgr lraagpwavv ravlltvama spliidsvge dgpgwiapls lvvivvafal
       61 srshpgstal galavsaidw rlfvavlvls ylagrrraln latlgglagv lvlgtvvqll
      121 qnlelytwlv wtagvivfgl fpalvgsfrr lqadlvrtgw dqaaqlereq rvvaeqarlr
      181 erariaqdmh dslghelsli alragalela sglapehraa aselragvtt aaerlseiig
      241 llrdeedkap lrpvhehiee lvaravdsgi pvvlcasgey advapmqyra ayrvvqealt
      301 navkhvgatp vevrldrhdd eivvavrnep prqapaappp qggrgltglq ervglaggvl
      361 ragplpdggf qvvarlpvrp gpvfeeagpe pappttaagf rrarsrarrg lvlaftlppv
      421 lvgaltgtlm alyahdslts rlpperfral pigasrddva srlperqvpe rrdeggplpp
      481 egstceyyrs aagfvptpfd vyrlcfrdgr lvtkdvlppp ir
//
LOCUS       WP_357568460             370 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568460
VERSION     WP_357568460.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=38723
     Region          3..346
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgdphrvgvi glgvisrayl dtlaahpevd ivavadldaa rssevaatip gaeamsverl
       61 larpdvqtvl nltipaahad islgaidagk nvygekplav tfsdgrsiie raasagvrvg
      121 capdtvlgtg tqtarsaidg gligrpmsas avmvtpgher whpnpdfyya pgggplldmg
      181 pyyisalihl lgpvravtga asrlraervi gsgprtgqri pvgvdthltg vlehtngals
      241 tittsfdgvr ttaapievhg eagtlavpdp nyfdgevrlf algdtewral dpragyaeas
      301 rgiglidlvr addqrpprag gdvalhvlet mtsllrsaae grrielttvv erpvpvpltq
      361 iedwtayraw
//
LOCUS       WP_357568464             529 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D family protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568464
VERSION     WP_357568464.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..529
                     /product="phospholipase D family protein"
                     /calculated_mol_wt=59147
     Region          13..410
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
     Region          270..410
                     /region_name="PLDc_vPLD1_2_like_2"
                     /note="Catalytic domain, repeat 2, of vertebrate
                     phospholipases, PLD1 and PLD2, and similar proteins;
                     cd09105"
                     /db_xref="CDD:197204"
     Site            order(375,377,390,392,403)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197204"
     Site            375
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:197204"
ORIGIN      
        1 mllqdwflta eeranpvsgi pvwttgnlae plihgaayfd rlvdevealg pgdhlfftdw
       61 rgdpdhrlrp dgptvaqlfa qaaqrgvvvk gliwrshldv layseaenrd lsetisaagg
      121 evlldqrvrr ggshhqklvv lrhqgaperd vafaggidlc hsrrddaahh gdpqpvqmsp
      181 rygpnppwhd vqlavrgpvv galdtlfrer wtdpmpldse npmaylrdrl rgsdlrpdpl
      241 peqpadpppc gphqiqvlrt ypavrprysf apdgertvar gytkavrrar rliyledqyl
      301 wsaevadlfa halrdnpdlh liavvprhpd vdgklalppn mvgreqalsl ceraapdrvh
      361 vfdvenhagd pvyvhakvcv vddvwasvgs dnfnrrswth dselscavld dtpdqreptd
      421 pagrgdgars fardlrlrlw rehldrdpdg addtdlldpa davaavtaaa dalqqwyddg
      481 qvgerppgrl rphrperlpw ytrawalpvy rlvydpdgrp lrarlagtw
//
LOCUS       WP_357568528             240 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568528
VERSION     WP_357568528.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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
REFERENCE   4  (residues 1 to 240)
  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..240
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..240
                     /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=24740
     Region          27..235
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          151..231
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtgvphaagn adtgwsgtll lkpgllaftg rigaaaahth aclqilavta gvvhvhdrhg
       61 dssriaptav ipagtthtit adpaakglia yldpaspaar talnriagag psdrvatwtg
      121 vgiggagpda pplhlalrra mdigrhhadg ppdlvalaea iglsasrlgh lfhdqlglpy
      181 plwrrwtrlr haidhvrnga tltdaahavg fadsahltrt cramfgitpt ealratgwrt
//
LOCUS       WP_357568531             315 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568531
VERSION     WP_357568531.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   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 315)
  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..315
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..315
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32190
     Region          67..309
                     /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 mttqkisgfh raalalvlpv aviaavagca dsaapkaapa assvaaapst stgaagpasa
       61 apaaglhmia nnghqlafhv tpgssptivl dagggedssy wdalvpqlsq atgsqiityd
      121 ragmgaseev kgpwdpkaaa sdlqaglrel gvtqnvvlag hsqagevahy fvlanpgvvs
      181 gavlidanvp qfftdtqtqr lvalttpqie elkeapstka nrqliatadn fgpthqayhk
      241 vswpdgvpvi yivsdktpfd gspqdaqawr daaaaftkag pdrtlviaeg sshdvpqdkp
      301 alvlkeieqm taivk
//
LOCUS       WP_357568601             439 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568601
VERSION     WP_357568601.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 439)
  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..439
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..439
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47135
     Region          1..>60
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpasaalfae qlralmrkrg vsyrtlaaqt fysksylhdl asgrkpptpk taerldaale
       61 aggklavlaa epgtdeswav ggaarwsrrd aerladllta qapdpdnaaa lahqwliaep
      121 pqryelsagr rvgvstvtri esrirqlrrl ddhvggaeth alvaaelvat aellregsys
      181 eavnrrllhv vadlcqlagf vaedsgriae arqhylsgmr aahagedtas aanclsslsy
      241 leagvgdrre avtlarsayv ggrhaaeatg qalllervaw aharlgeasl aervlgqvqe
      301 iyprcdleqa pswaywltqd evevmagrvw telrrplrav pilesaiary gddspretsl
      361 ylswlaeall qagefeqvav taerslslar raqspraver vaelrrmvaa aageagavae
      421 flelsadlsa vggghpggq
//
LOCUS       WP_357568582             394 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568582
VERSION     WP_357568582.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=41085
     Region          138..392
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrappwldsg tlgrdlvlag aslagglvlh algwqpqvrp dgnvpsalfl pplvavcvav
       61 glrrvapras lavgtgalvv dtalgsslgt vlvytqvlyd acvygpprlw rwllritval
      121 slvgvvvgvl gygqwrgaal gvlvvlagvl pvltgisvrq yrdqaaaera raeqtarlve
      181 ldrrqavsae rarmarelhd vvanhlsava ihatavlsvp gldrgqvesa lrviressvq
      241 glaemrqmie vlrepgtsvd paapevvtar laeadglver vraaglavrv rtdgtpgplp
      301 vavdlaayri vqesltnalk hgtgeadlti aygsaevvlt venpvrrhgv glpgagagli
      361 gmrerttlla gritagpqdg rwlvraalpt gevg
//
LOCUS       WP_357568611              70 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Micromonospora
            sp. NPDC048843].
ACCESSION   WP_357568611
VERSION     WP_357568611.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 70)
  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..70
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..>70
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <1..56
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtqqmladrl rrskswvdkv ergvraldry sviqelahvl rvdpevllgq qrptpagtpd
       61 gvddiraala
//
LOCUS       WP_357568651             424 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568651
VERSION     WP_357568651.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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 424)
  AUTHORS   ter Beek,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..424
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..424
                     /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=44354
     Region          3..340
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrkrltavva laamlglgac gggdsagsdg pvslrmttws aneahlklfn eiaaeyqssh
       61 pnvakitfdp ipfesytttl ttqiaggnpp dlawvlenaa pdfvssgall pldetlrktd
      121 gyafdelapa atklwqadgk lygypfstsp fgifvntdlv taagakspae liaanawtwe
      181 navttasava artgkaglvv rdfdykgwdn lstiwtgwga qawsadgktc gfnasemvda
      241 mtflhqaift akalpgpgta adffageagm titqisrasl lekqkfgwdl vplpagpkgn
      301 ysvigqggmg vlkkgkhaav aadflafltn pansaklaqf fppprtpllt aatlaktnpl
      361 lkpeqlqsvv idgiangvvk pnhtgqaels qavrsaldpm wkadadvrav ldgvcsainp
      421 llak
//
LOCUS       WP_357568710             174 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568710
VERSION     WP_357568710.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 174)
  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 174)
  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..174
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..174
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17888
     Region          48..163
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mlflstavai laalvlvdla lsaavirrlr eteakliemn sppasglsvg ttlpefvspd
       61 gqvssadlag sptligffsa gcrhcpaqae kladraeefg gtgvrvvsfl tvgegmtdel
      121 gptlrkagll vmddspsavm aafqvqgtps fvlfdadgrl aarghdlsev lgsr
//
LOCUS       WP_357568713             255 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein, partial [Micromonospora
            sp. NPDC048843].
ACCESSION   WP_357568713
VERSION     WP_357568713.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 255)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..>255
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
     Region          1..>254
                     /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 mtaplhgvtv vdlatlfagp laaaflgdfg advikvehpa kpdpsrghgp ardgvglwwk
       61 vlgrnkrtvt lnlsdpdgae llrrlladad vlvenfrpgt lerwglgpae lhavnprlvi
      121 trisgfgqvg pyarrpgfgt laeamsgfaa atgepdgppt lppfgladsv salaaayavm
      181 lalrardvtg vgqvvdlaii epimamlgpq itwydqlgyv qprlgnrsnn naprntyrca
      241 dgrwvavsts aqsia
//
LOCUS       WP_357568736             992 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568736
VERSION     WP_357568736.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 992)
  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 992)
  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 992)
  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 992)
  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..992
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..992
                     /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=109182
     Region          1..244
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          110..972
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(672..673,675,703,708..709,712..713,715..716,745,
                     748..749,752..753,756)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          701..739
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          744..770
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfgilgplr vgggestvta grdrivlaml llragrlvpv delvdavwed rppataraql
       61 qtcvsrlrrr ftelelapdl ivtdpagygv rtaptdldae vftrgveaar saatagrlvd
      121 araefraala lwrgpalggi psrsvrrraq aldeqrltal eecvdvelrl gqaaelieel
      181 aesvdrhplr erlrgqlmla lsavgrqada lavyregrrf yadelgiepg aelqelhqrv
      241 lagdlalagr earpiapvrs lpraigdftg rqqtlarlvk eveagariql idgmagsgkt
      301 tlavhlatal addypdaqly ldlhghsert pltpaaavat llrqlgvpde rvpanqddrl
      361 alwrselsgr rallvldnaa tadqvtpllp ngsrclilit srrrlvgvde grpsslpvld
      421 tdegvellgr vvgmnrvaae peaatevvrr cghlplairl agarlahrpr wriadlaerl
      481 strpdplaef eagersvgra falsyaqvsp aaqrafrllg lhpgvrfdnl vaavlvelpl
      541 pevqdlldel idahlveeae psryrlhdlv reyartlvae peragerrda ierlldhhlh
      601 vataiarere lsstqplilv tvpvradlvt ivteqgrtwl nenlalwpal vrlaetegll
      661 qkcwqlarac whaqfesgrl deliethsag lraaeelgdd ravatmlnyl asahyrlgaf
      721 pesirvmers leifrrlglr refrntlgnl gtsyaanfef rrarecydaa ralatrlrdk
      781 ealanelnnl tmtlllwgrf dealrtarrh lgiareigdp rrignalghl gmtrhrmgdv
      841 vpaerllrva lrvkrevgtr fgegevlnei gmmereagrp eqaadlhraa lvamteagdr
      901 iaqcgsrnll araildqgdv tsaldlhrrv lvdatglgsp reqglalegi arcvratdpa
      961 aarahleqal alfrqiespd qheverllte lg
//
LOCUS       WP_357568785             963 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568785
VERSION     WP_357568785.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 963)
  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 963)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 963)
  AUTHORS   Rosinski,J.A. 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 963)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..963
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..963
                     /product="helix-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=101708
     Region          <4..899
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          897..957
                     /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 mtvraassvl vgrhretaal rdalgrarag epttvlvgge agvgktrlle efagwatdga
       61 srvlvgqcle lgeaglpfap faaalravlr adgpevfagy eaefapllpe lgrasaaltt
      121 pravplsdap rgylfdlvae lfqrladarp lvliiedlhw adrstrdlig flvraarpgr
      181 lllvctyrtd elqrghplrp flaeldrarg vervelarld rdgtaailad llgaeplara
      241 vddvhdrtqg npffieelav agdpigcaal petlrdllla rvdrlpepaq rvlriaaagg
      301 trfahdllae vaglpetele dalraavaaq lvvadrdgdy efrhalvrea vhdellpgeh
      361 arlharfaaa ieaqphlvaa grapaeiahh whaahdhpra lvaaraaaca aadryayaeq
      421 rrlleralel welvpdaadl lgmdhlalle qtldaavtag dfsraitltr aglaevdada
      481 aplraarlld qrgrlmallg ksdgsrelde ayrlaaggpp ggervrllad iathlvkidp
      541 qkaarvaaea atdaealgeh vallstrial lchgerdltg glaelgraaa aaraagdapt
      601 lvlamvfesd mlcelgryae saqaaeagva earrvgisrs tgayllsnra ealialgrwd
      661 eaeavcaeaa ridlsgvtgl hwlqlgaglr larahpgade lvdraltfln rpylwpnhrl
      721 plhelaieaa laaddkveav raarvavvde slpqlaregw pvlsaaarta arvgdremaa
      781 avaalatalp arhpaaraha aqvtallavg dqalpawraa vdawradgqp yplgrallal
      841 aeataaager deaaaavtea teigrrlgat plveaaatla rrvglraggg agadlltare
      901 revlrlvaeg hsnsriaerl fispktasvh vsriiaklgv tnrveaaala hrlgllteta
      961 apr
//
LOCUS       WP_357568791             331 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568791
VERSION     WP_357568791.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   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 331)
  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..331
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..331
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=35515
     Region          111..331
                     /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 mvvnvvrrmg rflsahrrll iraaavlavi tvaiayalrd papvgyftsa esqdrfvsay
       61 aeamadlpap drtldvrtgy gvvrlyhfsg gtdpaaapll llpgrasasp vwadnlpsll
      121 rsrnvytvdl lgepgmsiqq rpikdttaha hwlhevllal peptihlvgv sfggwtamnl
      181 avhlpqkvgs vvlldpvlvf adlsaevvlr sipvsvrwap rswrdsfasw tangapvedv
      241 pvarmieagm qayvmklsap trpsedqlaa vdvpvlvlma gksrlhdage aaklaersls
      301 hgtvktypda shaingeypd eiaadisafl n
//
LOCUS       WP_357568757             321 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568757
VERSION     WP_357568757.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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 321)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..321
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..321
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33187
     Region          58..301
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mprrvtpall asavlmaglv gcsadarkte sqqapveppp aatptpqvpa gkapqrafav
       61 gvrqlklnrd gralpttlwy paagqsggaa krsataaqgr fpvvmfshgl ggrpddyatl
      121 mtrwaaagfv vaaptfphts rgadnnvldv lnqpadvsya ldqvlaldgk agdalrgrld
      181 gervaaaghs aggvttiglf tasrderlda gvvfagtalg vgtafagaaa pqlfvhgeld
      241 evveyaagra aydkvpwpka mlslpkgdhg rallsdgatl rvvsdtsvef lrwslygdad
      301 akkriptdat rgdiatfddh l
//
LOCUS       WP_357568796             551 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568796
VERSION     WP_357568796.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..551
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59438
     Region          21..>213
                     /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 mshpehhrgr rrprldrpal vallfglagv vyrlvltlft vpvsnsdeat fglaalhigq
       61 grehpvflyg qhymgmlesy laaplvavag pswpvlrlpm lalyaiflyl ihrltrrlgt
      121 pwfaafvvgl lalgpervvr dqltvvggrp evkpavllml litvglaagt vhrrglaigl
      181 fgllvglavw sdwlilpyla vaglalvwav rrellgwsgl lllvgvvvgv apmivdnlra
      241 gpgedslsvf revstkagpq pqwsdrvrgg llegvplahg lcpvdgcgrw qqwfgvlypl
      301 lllagaalav layrraagap rgervgraag vlrgervgpv vqlaliagaa ltllsyvrsp
      361 laatspldna rylsvlqlsl pavlwplwva altawrgtss vvgrftgals aavlaaltvt
      421 tlvitvlfaa tgtapsrtee rqarelaaal radgphevyg dywtcnrlif ntdesvvcgv
      481 ldgdlspgqn ryrpywrqvg raerpgyvva vdspmdrrlr alladradas pvrevggyrv
      541 yhpdtpvrpw r
//
LOCUS       WP_357568816             312 aa            linear   BCT 28-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568816
VERSION     WP_357568816.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=33510
     Region          1..311
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mrdiavfsgt ahpdlaaeic ahlgvplhpv rvsrfandcl evqlqancre rdvfliqplv
       61 ppvqehlvel llmidaarga sagritvvlp hyayarsdkk daprisigar lvadlltsag
      121 adrvlamtlh spqvhgffsv pvdhlhalre lathfrrydl sntvvvspdl gnakeaaafa
      181 rllgtpvaag akqrfsddlv kisavigdva drdvivldde iakgstvvel mehlrglkvr
      241 sirlacthgl fsgdalqrls dqdgvleivc tntvpipadk rvpklqvlsv apalaeatrr
      301 ihngesvsal fa
//
LOCUS       WP_357568861             329 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048843].
ACCESSION   WP_357568861
VERSION     WP_357568861.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 329)
  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 329)
  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 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   5  (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
REFERENCE   6  (residues 1 to 329)
  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 329)
  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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..329
                     /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=35726
     Region          68..206
                     /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"
ORIGIN      
        1 miwltwrqhr kqalytvlgf avlaavlvpi glsmrntfad lgltdcvnql aradvaqttr
       61 etcdagfhrf tnqygnlnll avllitlpvl vglfwgaplv areveqgthr fvwtqgvgrn
      121 rwalvkfglv gagvlvlavg yglgmswwve pltqtaregr fglivfdlqg vvpigytlfa
      181 valgifagtv wkrmlpamgi tlagfigvra aiavlarphy qpartqtfpi dgggipegnr
      241 gdwvlsvgir nadgamvaed triqcppggk gpdgrvcgae lglkpgaynw elyqpadrfw
      301 lfqgietgif valalllvyl avrrvrria
//
LOCUS       WP_357568934            1364 aa            linear   BCT 28-DEC-2024
DEFINITION  RHS repeat domain-containing protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568934
VERSION     WP_357568934.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1364)
  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..1364
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..1364
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=145041
     Region          49..1104
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 msknnnstvv nltdsaggth edidelagke lettqylgeg gridsstits ywvsaatatr
       61 srsglsamta hrvepaktya rqsvtaggav twrytatdns ydantasatf gllkntytyt
      121 vpidaaynqc ttytyaptnt aknlaglvsq tetvsvacgg ftqgspasep gsvntlttps
      181 svnrpaqvvk aertfydvtd fsttfpqaaa pskgdvtmtq vakdytsgay vwqttgrsty
      241 dsygrvtdsy dgngnktvta ftmnavrltv gtsttnalgq vasatvnprr glplgatdan
      301 gvvvtqhfda lgravsvwln sratsspahr kftyvisktg tsgtmtetln nssgyqksll
      361 iydallrprq tqattpqagr litdtyydtg gwtrasyngw wddstaptlg apvsaadlgk
      421 qvpnqtlnty dglgrpvvvv aakngvtvss tttvyqgdrt tsvppaggvv qttltdplgr
      481 tkelheytal ptvttpndvf tgsfavtggt atiskyghdg hgnqssftda lnnawtaefd
      541 lmgratkksd pdtgaitgll ydgngnllqs tdsrgkstsv rfdklnrrig qyaapvseqs
      601 ssnqvnawvy dnsnnavanm typigqltts inykggkayi kqqkgfnvfg kslgetvtip
      661 dsegalagsy vfghtfssvl glpltdsypa kgtlpsetvl hgysgvldlp ttlggsagys
      721 ngvsydawgr vsqatvgsgs nlayitntyd ahtsqllnql vtrstgtptt vdeqsykydl
      781 tgnvtkqvsk rlgatapaes qcylydklrr mteawtatdd catapstsnk amvgnnvggg
      841 saywtswsvd pignrtnqie rgiggamdkv ttysyggtvg gqphaltstt ttggaassts
      901 ygydsagnmt trnaekgaqs ldwnelgqlt avtgtagqss fiydadgnvl lqkdpgkvil
      961 ylpgqqlald tatqvvtgnr yfnlpgggta irsgsgsnys feigdshgsp slyldntaql
     1021 akwrqytpfg aprgpadvyp dnrgflnkvv nnatgliqvg arsydalvgr fisrdaaldm
     1081 gnpqqmngya yssnnpvnfs dpsgniqvgd drgllvavpn adgtetivdn rpkkcrtryc
     1141 fgapknpykp eatrypyspk akatakdywn wnlyrwlrmg aaavsnplls pvdltdgvat
     1201 ynhyrdasgt dfeidyekay gqdavirrnv daeiaeaqgf aesllaecac dslsmtgedk
     1261 giegypesen wqkalgdhnv wgsakvarkg ekvtmtitvh aedfydfnpk nkdvrsglsd
     1321 ddngrfatlg wakpfltqgs ltrtvtwvpg gspsdstitg garr
//
LOCUS       WP_357568939             200 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568939
VERSION     WP_357568939.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=21163
     Region          1..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 mprvglnqqi vvreaarlad evgfqqltla alasrlgval pslykhvkga dalvqklaal
       61 ataelatamt taavgrsggd alramadayr dyalrhpgry patqrvpdpa daehveager
      121 avgaifavlr gygltgddav datralrsal hgfvsleaag gfglprdvdr syhqlvasmd
      181 isfrswpgtr qvadqeergw
//
LOCUS       WP_357568949             441 aa            linear   BCT 28-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357568949
VERSION     WP_357568949.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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 441)
  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 441)
  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..441
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..441
                     /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=49252
     Region          4..430
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mtastaivll trdlrvhdhp alattcaafd qvvplyvldp aladlsanrt rflhqaladl
       61 rdqlrerggd lvvrhgdpva etiriagevg asavalsadv shyavrrerr lraecerhrl
      121 hlrvfpgltv vepgalrpgg ggdhyrvfsp yhrawaanrw reelaaprri alpdrvrvgr
      181 lpalpagdsp daaiggeria rqrltdwlpd ltrygdqhdd magddtsrls pylrfgcvsp
      241 lavanragdr sgpfvrqlcw rdfyyqvtaa fpaistaayr rgateqwryd ddalaawteg
      301 rtgmpivdag mrqmlaqgwm hnrarlitag yltkhlgqdw rsgvavffrw lldgdvanns
      361 gnwqwvagtg ndtkpyrgfn pvrqaerydp dgdyvrrwvp elagvqgkai hqpwrlpeal
      421 rqtldypppl svpgtdpvwl r
//
LOCUS       WP_357569023             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            sp. NPDC048843].
ACCESSION   WP_357569023
VERSION     WP_357569023.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..416
                     /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=44797
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..371
                     /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"
ORIGIN      
        1 mveelaladd avaacldaaa walpepelia aldaahrleq rlaavkltlv reldgrgtpr
       61 ahgasstavw lrerlrltip aarrlidlat aldtgnpgir qaladghisv dqarvitdta
      121 ttvqatagtq aadkavgvlv gwasqfdpth lrklgtrild hvapdiadaa tqaaldaear
      181 raardrhltl seqtdgrlrl tgtldtetag llraaidplt apsgpddtrs pgqrrhdala
      241 dvcrlalrsd elpdsggdsa qivvtttyda ltrqlgggal diglqltpdt vrrlacdati
      301 lptvlggtgq vldvgrqrrl itgplrralv lrdrgcafpg cdrpprwcha hhihhwadgg
      361 ttnldnavll cghhhrhlhh sdwiiqlghd ghpefvppaw ldpeqlprrn hyhrrt
//
LOCUS       WP_357569037             384 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357569037
VERSION     WP_357569037.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 384)
  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..384
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=40806
     Region          155..384
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 maseavtpra drrlrrvrwv tlvslatgvw asvllpavgl trepdpgrvt lgavgilafv
       61 iaqtvvlyaa vtpwldprwr rraelslvgv avltvplvgp vaagswptwa wlgaaligmt
      121 pllvrwraal tvaagvlava vavawwtggs vprhlavtgg igaavaavng lqvwfwdllv
      181 earqgqaaqa rlaaaeerlr fardvhdvlg hsltvialka elaarlapvd peragreaae
      241 vqrlaasals evretvhgyr vvdldeqlta vvgvlrscgv rctvlplpad lpqpaaiela
      301 avlreastnv lrhsradwcr iridreddva rmtvandgad drspdahshg lrgladrlaa
      361 aggelrvrre daiftleatv paps
//
LOCUS       WP_357569043             411 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357569043
VERSION     WP_357569043.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..411
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..411
                     /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=45543
     Region          12..355
                     /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 mtsvaatsaa rpapavprlp sltglrwiaa llvfgfhagt mriiaepdyk avidalftlg
       61 lsgvqfffil sgfvlvwsar egdsrrtfwr rriakiypnh lvlfaatlvv awwfadpvlp
      121 aaalenllll qawdprpgwf ysintvswsl scefffylcl plalpllrra rpkllwalvv
      181 alpllilalw paqelvpevs rwwftqifpp vrslefwlga vaaelmrrgl wrgpgltvas
      241 giflvtwvaa aqwiraelwt tllavayllv itaaadadvr grrspwrsrp lvwlgevsfa
      301 fylvhvlvmt svlrwsgtwg igfagwrgpa vvlgflaanl vlagllhrfv etpmmrrlap
      361 rraarpapvp rqraagddda repgssarge vdgpadevgq aggrstyvdl r
//
LOCUS       WP_357569063             358 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357569063
VERSION     WP_357569063.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 358)
  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..358
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..358
                     /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=38041
     Region          42..293
                     /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 mvfrmvqdva rqvaeqvrag fglrlstmes vtsgadqhar lwlardadgs ryavklsggg
       61 tsaglvvtay laeqgvpgia aplraddgrl sidndgrrls vvpwvsdrra ldgpmtgahw
      121 raygevlaav hevpvtvels rllpaggaay psivtatram aarlrdpdpv dladplvmel
      181 agvwsaaadr lgvlireveh ravdkrdrpg anvvchgdph lgnlllgadg rvwlidwdda
      241 vlappecdlm fvlggvlafa pitaeqqqav lagygrtdvd pvrlawflav ralddlsdwt
      301 rqaldldaea adrdraariv rglvspvglv tladaalrgl drrrvagpas vqgghhae
//
LOCUS       WP_357569226             727 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC048843].
ACCESSION   WP_357569226
VERSION     WP_357569226.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 727)
  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 727)
  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 727)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..727
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..727
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=78578
     Region          135..375
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
     Region          427..727
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mtteqyhgrl rrlgvrrrls aaftagviat aavliapqaa aadtpwldvs adryatfavp
       61 aayvqenlgt vsqvvvegnf gpsaswaefg ltrrgdvwsg vlgalepgly nyqltaddtl
      121 tikdptnsts vaskpllstf lvagdsarwl ldapagtggk ietltyrttn aqrsalvwtp
      181 pgyaakgpkg ypalflqsgd gvaatdwldl grskqildnl saagsirpmv vvindvdgsd
      241 hkglkdlrka vadryrvlrd pehqaiagvs dgatdalraa ltkpgqfgyv gsfsgtsape
      301 idrkdakain rgvkllrlyt gnvtdpaynt tyrltkalgr advrfefdgv npdggatwtt
      361 wqenlvdfvp rlfrhvadhg pspghqplkr eftpppagtt ptpfvtedgf vtfetttdft
      421 daqhvtvwan vapggswlrl pltrdgdrwr atvgplkpwf yyyrlivdrv avkdtsnptt
      481 vttepmwstf fipgpgarll sdvpagrggk vesmtytstv agqdrtalvw tppgydpnrt
      541 qpypvlylqh gggqnytdwv emgrakqild nqfldgdltp mvvvmgngns snfnselren
      601 ivptararyh issdpsqqal aglsmgggqa fgvlkaypge fayvaafsag fgsgtgvdva
      661 ainngtkmlr lyvgdqtdfv ypsfmasltt lnnlgiryef dgvtpgphgw dvwqknlidl
      721 aprlfkr
//
LOCUS       WP_357569380            1848 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase, partial [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357569380
VERSION     WP_357569380.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1848)
  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 1848)
  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 1848)
  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 1848)
  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 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..1848
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..>1848
                     /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          2..1366
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1074..>1705
                     /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 mrdldsfgai lagpdslvtd vpadrwgpef sdptrsrpgt tsshvgtfld gidrfdpayf
       61 giapreagal dpqqrmilqv aweamsdsgr prdaweatrt atyvgiland yallhsktlg
      121 iagigphyap gtefsfaagr lahafdlrga aaavdtacss slfavqmacq slrsgdsdva
      181 laggvnlmia pelsvfmsrv gaisptgrcr pfhpgadgvi rgegcgfvvl krlsdavadr
      241 driyatlrgw avnqdghslg vtapnaaaqi dlhlaalrha glgpddidfv eahgtgtplg
      301 dqmellalae ayqtrartap pvlvgsskav fghtdaaagv tgllkalwiv naarvpgqpd
      361 ldqltsavdw esariavptv gvdlsdllrp vragvssfgl sgtnvhvive aapnhervat
      421 ppmgpyvlla satheqglve qialtrqrvp dnrddladlq asaatrrthe thrfaavaag
      481 ptemlaalgd prqlpegayt gtvdpgnvpp pvfvysgqgs qwagmatdly dtvplirdtl
      541 decdalirdh vswslveelr rtsdtaldrt ditqpaifav qvaltrwlaq lgvrpvavlg
      601 hsvgevaaah tagcltlada valivhrgqi lhetagagrm lavdaaradv eevltniggg
      661 vvvaavngpa svvvagpvea idaahavlmq rgvrckrlel dyafhspvva dcgpqlaaai
      721 stlasspaal rmlstvqpdt dleqadatyw grnishpvlm wpaidrllss sdhtlveiga
      781 hpvltrplte avrhrgrkgr vlatlrrgep gplglrkala qlhvagvpvd wekatgrpnr
      841 yrslpvpswa gepywlpgvp rgrqdggaap aqvrlsllda sggvitemla qptpaaapat
      901 tlgaapapav psvlastaal paptaaaipp vapatvappa aaaeaatpsr gvvddvdaiv
      961 rivlglpdse llprrrglfe qgmdsltave lrtrleaafd ltlpatvvfe hptvgalaay
     1021 lsellaarpa paltttpgsv eaigdddana raaagyieds rpdadavavv gvacrlpgaa
     1081 dpeqlwrllt egrhaigdlp adrrndpiwa eagpnvptrg gylpdvtgfd adffrispre
     1141 arsldpqqrl mlevaweale daghpavalh dqpvgvylgl ntadyqqllt rdmrqvdhfy
     1201 gtgtsfaata grlsyflglr gpsiavdtac sasltavhla cqglrdgdcd iavvgganvi
     1261 vaptvsvsms aaaalapdgr cktfdddadg ygrgegaval ilkplsaatr dgdrvyavlr
     1321 gsavnqdgas ggmtvpsaaa qtavvrqalr ragwephevd yveahgtgtp lgdpievral
     1381 aaalgpgrsp atpllvgsak anlghleaaa gaagllkvil alhhgeipph pinkpstrid
     1441 wnslpitlaa rrqdwpqrhr paragvsafg fsgsnahvlv eqvpqpatpa pgpgpgrtmp
     1501 yvlpvtaatp talaaaagrm anqlragsdd lddlvytaaf rrsrlshrla avgqtaadla
     1561 avlqmaadga tdprvrvghv vddeptpvaf wygpdlppta lrirllgsge yrtaldtcaq
     1621 tlstitgtsh dlnteppvel raaylfcyhv aatmlwttvg vhahaviglg agqvsaawaa
     1681 gqitttdalr ilthrdsgmq lrpgripvlp vehvqpattt deltrrltpd pnppvsgtal
     1741 qsltdrlada dldrvidtll gelprplgnq vdiavnaddp llrlaltaae lfvtggiraa
     1801 asgsgrrpvt lpaypwehrp ywyrehvsgf lsltpwvlag psraavrg
//
LOCUS       WP_357569458             187 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein, partial
            [Micromonospora sp. NPDC048843].
ACCESSION   WP_357569458
VERSION     WP_357569458.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 187)
  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 187)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         <1..187
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
     Region          <1..184
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 gadigqlrer grtdalaain saafariral pmptvaavdg palgggaela yacdlrvcta
       61 ravfgqpevr lgilagagat hrlpaligeg rakellftgr rvdaaealri glvnrvvdep
      121 gelltvahal ldeialgspl avrltklavd apaaahphld lvsqavlfed dekhrrmtef
      181 lerrrpr
//
LOCUS       WP_357569464             238 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357569464
VERSION     WP_357569464.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Rosinski,J.A. 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 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 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     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=24536
     Region          1..222
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 msaglagpaa aevstrdrvt qllleqgait aaqlgaalgl spaairrhld amladgdvya
       61 reqtvqgsrg rgrpakvfll teaarvrcgt hhydnmataa lrwiarsggs gaveafateq
      121 vsalesrcrt amedagddpl araealaaal taegyaanat tiasggqlcq hhcpvahvaa
      181 efpqlceaet avisrlvgth vqrlatiahg dgvctthipt qpgraqsgnp vttvrtdr
//
LOCUS       WP_357569493             948 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357569493
VERSION     WP_357569493.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 948)
  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 948)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 948)
  AUTHORS   Rosinski,J.A. 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 948)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19885644
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..948
                     /product="helix-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=99881
     Region          17..>399
                     /region_name="PRK04841"
                     /note="HTH-type transcriptional regulator MalT"
                     /db_xref="CDD:235315"
     Region          <419..897
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          771..933
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          885..933
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mpeqdhvrve papgpallas rltpavppep vvarprllrr ldegsagpvt lvaapagwgk
       61 ttllaswmrl ggappdvepg alvpdsgdls vssaddpvsa wmsveagddp arlwaylaaa
      121 llsatgatdg gpvpdrpprp dqlealaatl aaadrpvlli lddlhrvadp aaltglefll
      181 rhaggrlrlv igaraglhlp lhrlrlagel teigpdelaf tddevadllt ahaaalpata
      241 vhrlrertgg wpaalriaal avreqpdper wvgqfggdqp eiagylheev latldpaeed
      301 llrrtavvdt vcadlaealt gradagqvla dlagtggllh redtrppwyr ydslladllr
      361 adlarlpaee lrelhvraad wyagdgrpad alrhalaagr wdlagdlfva hwpeltrfdr
      421 dpvhapaptp ppadviradp evalacaaer ayagdlpaat ghlraaagha aglpvprrdr
      481 flrlvtalel tvarladdrs evraaaarll rtrpaeatpt rlparvtgsa ptaggggaad
      541 dldlraftgt alglveladg alptarfvra raaareagrp rtelvaasra alllavrgel
      601 raaeraarda lgmppcrgws crldcghayl alavvallrd qpeeatanla lalpaldvtg
      661 gwagdpevrg dwlaaapdep vaaavaalcr aqlrrdsgdp atgqrllvra realadrpsa
      721 geltgllraa eaelraargd ldsarellad aadegadpvl avtlakvqls agdaataqrt
      781 lpdwqapaat awplpvrlda glldavlaqr agdarragri leqtldlagp qgcrraftra
      841 ephvrdllaa hldagtahft lvsdlvrgag qgadgpaaga rgaldeplte reltilrylq
      901 silsnveias elslsvntvk thvrniyrkl datrrreavr rarelrli
//
LOCUS       WP_357569495             534 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357569495
VERSION     WP_357569495.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..534
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..534
                     /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=57706
     Region          <8..>99
                     /region_name="mnmC"
                     /note="bifunctional tRNA
                     (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase
                     MnmD/FAD-dependent
                     5-carboxymethylaminomethyl-2-thiouridine(34)
                     oxidoreductase MnmC; cl40718"
                     /db_xref="CDD:424349"
     Region          61..533
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 msdqtqsmvs rrgflrtvgi sggagamlat mgamglapsa aasvtpafrp persdftltg
       61 rsgasvvvlg ggiaglttay elgkagyhct ilearhrvgg rnltirggdv etdldgrtqr
      121 agfsdgvyfn agpgriaqwm vtmdycrelg vpievftnqn adawiynesa gmtepvryrt
      181 akadvygyvs ellakatdqg aldarltted rdrllsflqs fgaiggrtsd waytgtnrrg
      241 ysaypgagnd vgsllgappa lsnvfasnvg ryfsfefgyd qamlmfqpvg gmdqitrala
      301 ravgphrirl naevtgvtdr gsrvevtyrq ggrqsqitad ycvaalpphl marvphnlgt
      361 pvtaaladfp vtasgkigle yrsrwwetdq riyggitetd ldlshiwyps ygfhgkrglv
      421 vgyyntgana raysgltpeq rseraisqgv kihgdkyrse lvtsyshawd rtryiegawt
      481 sprygtagyn lllqpagrvy fagdwlshev awqhgafvaa rsavsalhqr vmag
//
LOCUS       WP_357569543             426 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Micromonospora sp. NPDC048843].
ACCESSION   WP_357569543
VERSION     WP_357569543.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..426
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..426
                     /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=44763
     Region          20..389
                     /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(29..30,33..34,37,69,119..120,122..124,127,147,
                     150..151,154,229,232..233,236..238,241,268,272,321..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 mrtmrswfrd ttgglpttfw ylwsgtlinr lgsfvlvfla iyltqergfs asqaglvigl
       61 wgvggafgtt aggtladrwg rrptlltahv gaaammlglg lardlwaval galllgmfae
      121 aarpafgamm idvvpakdrl rafslnywai nlgfacaavl aglaaqadyl llfvvdaatm
      181 litaliifsk vpetrqagpa tavtaaaapr galrtiltdr vylgfvalnl faalvflqhi
      241 smlpiamgdd glspatygsv ialngilivv gqlfvprlir grsrshvlal asvvmgvgfg
      301 ltafagtpwf ygltvliwtv gemlnspsns tliaelspae lrgryqgvfs lswqiagasa
      361 pilgglvreh agndtlwygc aalglltava hlvsgparer ratalrrsge alaptttsra
      421 pqpaea
//
LOCUS       WP_357569579             201 aa            linear   BCT 28-DEC-2024
DEFINITION  phasin family protein [Micromonospora sp. NPDC048843].
ACCESSION   WP_357569579
VERSION     WP_357569579.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..201
                     /product="phasin family protein"
                     /calculated_mol_wt=20682
     Region          1..98
                     /region_name="PhaF"
                     /note="Polyhydroxyalkanoate synthesis regulator phasin
                     [Secondary metabolites biosynthesis, transport and
                     catabolism, Signal transduction mechanisms]; COG3937"
                     /db_xref="CDD:443138"
ORIGIN      
        1 mqdawrayle lamglaeapr kkaqdvarrl vgsggataaq lqalgeelvt tgaanrealt
       61 klvrfevdra lgavglatad evaeltrrvh dlerqlrear stesadappa gprpqpdptv
      121 aarpgaglvp sdasagapvs apvakkavak kavakkavak kaiatkppat isptadedvp
      181 tpavmpakka airrqrpdda e
//
LOCUS       WP_357569602             521 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein, partial
            [Micromonospora sp. NPDC048843].
ACCESSION   WP_357569602
VERSION     WP_357569602.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 521)
  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..521
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..>521
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          29..420
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msltelsgtp tpepattiek parparrasp fgalllrlhf yagilvapfl vvaaltglaf
       61 tttpqldtil ygdqltvaqv gdrqlplaeq igaarnahpd gsittvqpgd gdrttkvvfs
      121 lpelgenqht vyinpytges qgqlttwfgs tpvttwlddl hrhlhlgtvg ehyselaasw
      181 lwvmalggvi lwwrrrgaak aaarhllvpn lstakgvrrt rgwhattgiw ltvgllflsv
      241 tgltwsryag anfaagldal sartpeists ltagppapae tggghehgaa gaggvvesaa
      301 fdrvlavarg aglsgpveis papepgsawt vtqvdntwpv kkdriavdpa sdtvtarsdf
      361 adwpllakls glgiqahmgi lfglvnqill aalalgllcv ifwgyrmwwq rrptradrra
      421 iagtppargg vrglplwall igvpvtvaig wtlplfgltl laflvidvvv gavsrrrrpa
      481 avptspapag gvyrrtstta pkpvdpgsmr rarptmyfrp v
//
LOCUS       WP_357569608             235 aa            linear   BCT 28-DEC-2024
DEFINITION  urease accessory protein UreF [Micromonospora sp. NPDC048843].
ACCESSION   WP_357569608
VERSION     WP_357569608.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 235)
  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 235)
  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..235
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..235
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23264
     Region          7..235
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 matpslllll adgrfpagah ahsggleaav aagrvtdlas leaflagrla taglvgaafa
       61 aaahraavae tadpaesvar sgalarldae ldartaapal ravsrrqgra llragraiws
      121 dapfadlpat pggahqplvl gllcaaagls raetatiaay gtltgtasag vrllgldpyq
      181 vqallvglad acdgtaadaa raaddpperl paaaapladi haeihatwev rlfas
//
LOCUS       WP_357569640             291 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357569640
VERSION     WP_357569640.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..291
                     /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=32031
     Region          3..281
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mglttpavli yvmfvlvpmg favyyslfrw rgvgpptefv glrnytlafq dpifldalrn
       61 naiivfgsll iqgpialgva lllnrrfrgr avfrllvfvp yvlaevtvgi mwkllltgdg
      121 tvdallrslg mgglvqawla dldvviwtll ailtwkyvgf aiilllagls nvpdelteaa
      181 aidgaswwqi qrhvtipllg ptiriwmfls migslqifdm iwvtsvpavr slgasatmat
      241 ymvdngffar lwgygnavav ilfvisfvaa llfqrfllrr diegaitgra k
//
LOCUS       WP_357569689             589 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase,
            partial [Micromonospora sp. NPDC048843].
ACCESSION   WP_357569689
VERSION     WP_357569689.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 589)
  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 589)
  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 589)
  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 589)
  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..589
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         <1..589
                     /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..589
                     /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 aeladpartl gllfpmfdlm qltilvavsg parpmwrpmt vlaasltlrv vadvvyvslv
       61 aradytaghp idlcwplsyl liglaarnpp ppdcdgtddt aesplppwwr valpylpvgg
      121 aiiavvlarr ptgqtpqlvf vtmmvllaal avrqglaane nlrlvarlrr laygdqltgl
      181 pnrllfnrrl rlalrdgrpv avllldldgf kqvndrfgha tgdtlltgla armhtavngd
      241 gtiarlggde favlvdgerp vsperlaerl ldalrpsdde edvgvhpsas igiaeygpqh
      301 ashtdllrda diamyaakaa gksayrtcta alresavsra eliadlrrav dedqlhlefq
      361 pivdlttgav rsaealvrwr hprlgmlppa kflplaeetg lilpidrwvi heacraaatw
      421 rgrapdatva vniaaahlrr pdliatvtaa tsaaglapra ltleltesal iegteavler
      481 lhqlrelgir iaiddfgtgy sslsylhrip atelkidrsf varlgtddra yatvemvtrl
      541 agafdlavva egveterqhe avtaigcprg qgylygrpdv pamvgqnrs
//
LOCUS       WP_357569663             376 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase, partial [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357569663
VERSION     WP_357569663.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 376)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..>376
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          9..376
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpdsgypwpi qtsrldnglr vvvsedrtap avavnlwydv gsrhepagqt gfahlfehlm
       61 fegsvnvakt ehmkliqgsg gslnattnpd rtnyfetvpa ehlelalwle adrmgglvpa
      121 ltqetldnqr dvvknerrqr yenvpygdaw lrllpllypp ghpyhhatig smadlnaadl
      181 atfqafhqty yapnnavltv vgdatasdvf aladkyfgal parddippap egrnvpatgq
      241 tavesvsadv paprvyiahr sypfgspgyn vitvlatilg sgrgsrlyqr ladgeriaqp
      301 dlvgaygvdl ahapapliat atarpgvsae rlaeglaevv delatvpvta aeldrakall
      361 stgwwrqlst vdgrad
//
LOCUS       WP_357569748             170 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048843].
ACCESSION   WP_357569748
VERSION     WP_357569748.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 170)
  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..170
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..170
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18874
     Region          <1..51
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(3..4,15,18,22..23)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          78..>106
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtivevakka elststiqrf erglfpaklr trdiralcev fgaddnltaa leglarqanv
       61 qswwheyddv iprsfnvymg leasvermyt yspdavvgll qtpdyappcs adghraprgv
      121 tmrprgwpia rpriaippcm prsrpksgcs tgesgpmqrr cnvsarrlrv
//
LOCUS       WP_357569709             235 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Micromonospora
            sp. NPDC048843].
ACCESSION   WP_357569709
VERSION     WP_357569709.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048843
  ORGANISM  Micromonospora sp. NPDC048843
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Micromonospora sp. NPDC048843"
                     /db_xref="taxon:3155389"
     Protein         1..>235
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          12..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(16,20,45)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,44)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,38,41,45..46)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          96..>212
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mispyvrrrr laselvrlre ehgysaerlc retkiakqkl srlenarvrp dqdeimrvld
       61 hfrvdekrwe eimaiaresq engwwekfrv emgprqalya dleagaehia eyhitllpgl
      121 lqipaytevr avadraaypr rftveralea raarqrvldr pggptyevii delairrhaa
      181 ppevvraqld hlinvgheqq kttirvlrlt ariagnavpr ssyfsyrypd psdpv
//
LOCUS       WP_357569824             244 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Micromonospora].
ACCESSION   WP_357569824
VERSION     WP_357569824.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 244)
  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..244
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..244
                     /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=26334
     Region          14..>70
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          44..219
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 msddrwvapr vllavdlvil tlrgavlqvl liergvephr galalpggfl ghdeeellaa
       61 ahrelaeetg fgagrphleq lgvygapgrd prgrvisvay laiapalpep vagtdassay
      121 wrpvneslag dvrlafdhrr iladgverar eklertalat afcgptftia elrtvyeavw
      181 gapldprnfy rkvrsvdgfi vpveatrrtd ggrpaqlfrp gphttlhppm vrpsgpdpad
      241 keta
//
LOCUS       WP_357569830             283 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357569830
VERSION     WP_357569830.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 283)
  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 283)
  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 283)
  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 283)
  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 283)
  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..283
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..283
                     /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=29153
     Region          23..283
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 msappsggrl nraggthima ftprtprvva arrlqrrrdr datgrflaeg pqavrealar
       61 pgvvtelfgt paaldrhpel aataaradvp vseitddala altetvapqg lvavcqhldv
      121 sleqalanap rlvavlaeir dpgnagtvlr tadaagagav ifagdavdpy ngkcvrasag
      181 slfhvdvvra pdpvtvvdal raaglsifat tgygdsdldd ladygrlvgp tawlfgseah
      241 glpeeltaaa darvrvplyg raeslnlaaa aavclyasar aqr
//
LOCUS       WP_357569873             403 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357569873
VERSION     WP_357569873.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 403)
  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..403
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..403
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44014
     Region          1..83
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mdslpeptfg qrlkvyrers gktravlggl vgrsaewvka vetdrilppr vhmldriara
       61 lkvdlsvlvg elsdrsaivn gpehpalasv rdavnrytfs gdatpeplgr lgnrlaaawr
      121 arhqapdhrt vlgallpdll rdvqraalty egderrraqa llgealglaq mflayqpaae
      181 ilwrvadram vaaqesgdpe alacagwflc qvhrdagdwd tamavtldvl salearasda
      241 ntnllalfga lhfeaaytaa rageegrawr ywdhadriaq rlpqgfyqpq tsfsrvimga
      301 havtvavelq ksgeavrqar rhdaaaipsr prrarhlvev arahygkgds dtamanlrqa
      361 hesapetvrf ngyarqitld llsgppssre dardlalkvg lvs
//
LOCUS       WP_357569898             496 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 3 protein [unclassified
            Micromonospora].
ACCESSION   WP_357569898
VERSION     WP_357569898.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 496)
  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 496)
  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 496)
  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 496)
  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 496)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..496
                     /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=51180
     Region          36..480
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mttptghlpa laaavlqpgf vgitpppwvc rwlgeglgsv vlfarnvvdp eqvatltatl
       61 raerpdviva ideeagdvtr lesvqgssrp gnfalgvvdd pelteavard lgvelaaagv
      121 tlnyapdadv nsnpanpvig vrsfgadpal varhtaawvr glqaggvaac akhfpghgdt
      181 rvdshhdlpr itadrerldt celvpfraav aagvqavmtg hllvpaldpr lpatlsqril
      241 ggllrdemgf sgvvvtdave mravadrygf agatvralaa gadaicvgge rsdeqaarel
      301 rdaivaavvs gelpeerlae aakrvgqlaa wtmaarttgl agardaadvg lvaarravri
      361 tatgtapdal pltraahvve fepmrniaig aetpwgigap lgellpgtst vryaepdvpa
      421 dpaagagtrp lvlvvrdlhr hewmrsavqr alaarpdavv velgvpevvt gavhlathga
      481 trasgraaae vltgar
//
LOCUS       WP_357569958             691 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha-1,4-glucan--maltose-1-phosphate
            maltosyltransferase [unclassified Micromonospora].
ACCESSION   WP_357569958
VERSION     WP_357569958.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 691)
  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 691)
  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 691)
  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 10571012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..691
                     /product="alpha-1,4-glucan--maltose-1-phosphate
                     maltosyltransferase"
                     /EC_number="2.4.99.16"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009313 - oligosaccharide catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0030979 - alpha-glucan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76610
     Region          3..190
                     /region_name="GlgE_dom_N_S"
                     /note="Alpha-1,4-glucan:maltose-1-phosphate
                     maltosyltransferase, domain N/S; pfam11896"
                     /db_xref="CDD:463388"
     Region          195..549
                     /region_name="AmyAc_GlgE_like"
                     /note="Alpha amylase catalytic domain found in GlgE-like
                     proteins; cd11344"
                     /db_xref="CDD:200482"
     Site            order(248,252,263,265,308,340..341,343..344,376,378..379,
                     407,463,516..517)
                     /site_type="active"
                     /db_xref="CDD:200482"
     Site            order(326..328,335..337,350,381..384,386,389,411,413..414,
                     417,421)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200482"
     Site            order(378,407,463)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200482"
     Site            order(410..412,429,432..433)
                     /site_type="other"
                     /note="acceptor binding site [chemical binding]"
                     /db_xref="CDD:200482"
     Region          <537..612
                     /region_name="PRK12313"
                     /note="1,4-alpha-glucan branching protein GlgB"
                     /db_xref="CDD:237052"
ORIGIN      
        1 mtgrfpiedv spvvscgryp akavvdepvp vsarayregh dalgcnvvwm gpdgvtrpft
       61 rmrpgepgqd rwhatirpda vgswafavea fqdpyltwqn avtkkiaagq gsedlandla
      121 egarvlaaar dlvptaerpr iadaltalve tdlplpqrvg palaladllw ehpvrelvts
      181 gdtysiwvdr kralysawye ffprsegatq drsgtfatat erlpgvaamg fdvlylppih
      241 pigrvnrkgr nnaltagptd vgspwaigaa egghdtihpd lgtpadfraf veaaaaqgle
      301 vamdlalqca pdhpwvtehp ewfttradgs iayaenppkk yqdiypvnfd ndpegiraev
      361 lrvvlhwvge girifrvdnp htkpfdfwrw liaevkkvdp dvlflaeaft rpaimhglgk
      421 igftqsytyf twrttaaqmr eyceelvasa dhmrpnfwpn tpdilheslq hggppmfkir
      481 avlaallsps wgmyagfelf ehvarpgaee yldnekyelr prdwagaeaq grslapflat
      541 lnrvrrdnpa lhqlrnlrfh eidnpsllcw skhdpdtgnt vivicsfdsr vvqwgnttld
      601 mpelgfdwhe rftvydeltg tsydwgqrna vrldpylqpa hvltvrrpaa psapepagve
      661 padltvtdvp telsggtapt apapkddrwt s
//
LOCUS       WP_357570013             327 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570013
VERSION     WP_357570013.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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..327
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..327
                     /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=34079
     Region          <233..>324
                     /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 mtamstraki gvvvasavll gsvaagyvam aaepaptppp asgdqavtlt pgprllaitd
       61 rhlstvatad ptgprtvsgl eclrvyaaag tgvclkpeta wsyqvvvlda alrqtrtvgv
      121 pglpnrarvs asgrmvswtt fvggdsytas gfstrtgild tttgatvtsl eefavtrdgr
      181 syrspdvnyw gvtftaddnr fyatmstagk rylvrgdvaa rtvetvkenv ecpslspdgt
      241 riafkeavda dpakgwrlsv ldlasmrvta taetssvddq aawldgrtla ytrrqsdgqp
      301 dvwsvpadgs gtpkltipga espapls
//
LOCUS       WP_357570016             556 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 27 protein [unclassified
            Micromonospora].
ACCESSION   WP_357570016
VERSION     WP_357570016.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 556)
  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 556)
  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 556)
  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 556)
  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..556
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..556
                     /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=58500
     Region          43..326
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(50,85..86,127,168,170,205,226,230)
                     /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          442..554
                     /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(446..449,459,461,464,468..469)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(455,486..487,488,498,500,503,505,507..508)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(476,478,482,486..487,498,500,503,507)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(528..532,541,543,550..551)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mnritrgrrw gsvlaagvlv agalvglrap aaqaldngva rtppmgwnsw nsfgcninea
       61 lirqtadaiv ssgmrdlgyn yvvvddcwfn pnrdssgniq gdptrfpsgm kalgdylhar
      121 dlkfgiyqvp vdktcaqyfg aypgatgsrg hevqdarqfa awgvdflkyd wcspegsind
      181 qvatfakmrd alaatgrpiv ysinsnsiha ktgpqrnwgd vanmwrtted itnawdtgqt
      241 ngypmgiqni invtvplasy arpggfndpd mmevgrggmn dtemrshfam waimasplia
      301 gndvrnmnsa tqtilknanl iainqdslgl qgtqvsfdgt rrvlakrlan gdvavalfnq
      361 ggstttistt aaavgksgss ftlveawsga ttsssgtisa svpahgtvvy rvsgggttpp
      421 tttppttppp gtssalasaa sgrcldvpns nttngtqpvi wdcngaanqr wtvngqtlqa
      481 lgkcldaptn aaagskvqiw dcngganqrw tinangtisg aqsglcldvn gngtangttv
      541 ilwnctaaan qrwtqr
//
LOCUS       WP_357570049             418 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Micromonospora].
ACCESSION   WP_357570049
VERSION     WP_357570049.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..418
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46064
     Region          3..408
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mndtvvaava qahrrdwaqv fsttaqltrd ldlaeectqd afaqaletwa esgipdrpga
       61 wlttiarnra rdvlrresvf rrkmpllvad ettpgpedgl vddrlrlift cvhpalsrqa
      121 qvaltlrlvc glstpevara flvppttmaa ritrakrkia taripyrvpg pdqlgervsa
      181 vlevvhlift tghtapvgah lvrqdlvdca iglarmlhll mptdaeisal lalllltaar
      241 qdtrvsvdgr lvllseqdrt rwnwqlideg rslltdalrr rpptryalea aiaavhadap
      301 twpdtdwnqi vglydtllrl wpspvvglnr avaiglrdgp eagldaltpm ladpalstyg
      361 ylsasradfl rqlrrwpqav tayeealtlt dndveraflt erltdvrrhl pgsappap
//
LOCUS       WP_357570071             249 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: phosphotransferase enzyme family protein
            [unclassified Micromonospora].
ACCESSION   WP_357570071
VERSION     WP_357570071.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  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..249
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..249
                     /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=27488
     Region          37..214
                     /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 msnreevlqg nvtsgvvrvg dtvrrpvgpw temvdllldh lhavgftacp rplgrdeqgr
       61 qvleyvpgem gaesgtypat elrsigrlla hlhealasfv ppaggswnqv ippdreemic
      121 hndvapwnlv rsdrgwvlid wdgaapgsrl wdlayaaqsm aglradrpvp qsaarlrafv
      181 dgyglddasr palavllgrr aramydllre garhqrqpwa riwtedgpyw latadyldah
      241 rdawlagle
//
LOCUS       WP_357570114             334 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357570114
VERSION     WP_357570114.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=35930
     Region          17..307
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mdagqdrrps ggdgglrsav vvnpvkvddl delrrtvnda lsaagwpepq wyettvddpg
       61 rgqaeqavka gvdlvfacgg dgtvmscvsa lvgtdvalav lpqgtgnlla anlglstdla
      121 aglqvaverg rrlldvgave dkyftvmagm gfdaqmleat nettkarigw payvmgaarh
      181 lrdrpmrvqi riddrppvrr rarsvlianv grlqggvtll teaepddgwl dvavltprsl
      241 rhwlalgwav vrrsgqvprm evfrgkrvvv ssnraqprel dgdlispgrr lqaevrpeal
      301 wlcvpqpeda pdlavdaqga gergeqlied arre
//
LOCUS       WP_357570130             519 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570130
VERSION     WP_357570130.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 519)
  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..519
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=54931
     Region          129..383
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrildfslpg pldrrrrllv dallwavvaa pvgyagvspp ypryalpllv gkllllgaav
       61 vesrrrplva lvlvvlgsvv dgnfvfavpv fsyltgrrsv sarpvagvfv liaaggtaln
      121 lgllgtgeat wfllasvllf aavfpwlvgr yrrqqqelaa aghrhveali reergaaeri
      181 rlrerariag emhdslghdl slialraaal evaadldgrh raaagelras vsaaterlhe
      241 iigvlreegg esvrpsgetv adlvdnarea glavrleaas avaelpamtg haahrvvrea
      301 ltnaaryapg apvdvrlird gervevsvvn gapsgdplpa ppsqgsglla laervrlagg
      361 tldagpradg gfavvaalpa tappveaies dlagpsggwp gpverpvdae rrlhdarrrv
      421 rrsllvalla pagfalvlsl vyypvatagt vldratfdqm rvgtarsele glprrqvenp
      481 vgvdragcey ytdgnfplae ptwrlcftdg rlaskewia
//
LOCUS       WP_357570132             168 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570132
VERSION     WP_357570132.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=18537
     Region          1..154
                     /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 mlrgravtlr patvedvpal aairatpevr rwwrgdddla aavrddladd dlalyaiehd
       61 grvigaiqwh aepdpdyrha smdifldpav rgaglgvdai rtlarhlide yghhrftidp
      121 aaansaaira yakvgfrpvg vlrryergdd grwhdgllmd lladdlve
//
LOCUS       WP_357570219             146 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357570219
VERSION     WP_357570219.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 146)
  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..146
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..146
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15709
     Region          1..75
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 millrrvigd alrarrqgqq rtlrevstaa nvslgylsei erghkepsse llaaicdalg
       61 arlsellrev sdtvalaeqm pevlvsmqde padagavsks tsrsvrqvts dgkvsvsvrq
      121 dsplkatlrs arvrpterdr dvvcaa
//
LOCUS       WP_357570256             407 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent RNA methyltransferase [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357570256
VERSION     WP_357570256.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=42964
     Region          10..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 mlerglaeae rveltvdava pgghcvarvd gqvvfvrhal pgerviaevt evhrgfvrad
       61 avsvleaspd rveppcpyak pgacggcdlq hvapeaqlaw ktavvreqlt rlggltdael
      121 dqlgvrveal pggllgwrsr vryavdaadr agllkhrshe vvpidrcria hpaiqrlpvl
      181 aerwtaaeav etvastggdv tvtavrdgvp tpvsgptevr evaagrdwal pasgfwqvhp
      241 aaadtlctav lelldprpge tawdlyggag lfaaalagrv gaaritlves srdgvdaara
      301 nladlpqvev vaarvetalt rrritgpvdv vvldpprsga gaqvvrdvva agpravayva
      361 cdpaafardv rtftelgwrl aalrgfdlfp mtqhvecvgl llppver
//
LOCUS       WP_357570265             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570265
VERSION     WP_357570265.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30346
     Region          4..>154
                     /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 mtttqthtla vpgvdlvydv rgplppsggh pvllmigqpm taegftalap hftdrtvvty
       61 dprglgrsvr tdgrtdhtpq qqaadlhhli evlgvgpvdl fassggavta lelvaaypgd
      121 vvtlvahepp inavlpdaga aeraradfyq ayqtkgagag maafiamtsw qgeftdayfa
      181 qsapdpamfg lsteddgsrd dpllsdlswa isdyrpdasr ltsaptrivv avgeesagty
      241 tartalalaa llgqeavvfp shhggflgge fgyagkpeef aarlrevlda g
//
LOCUS       WP_357570267             347 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357570267
VERSION     WP_357570267.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 347)
  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..347
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..347
                     /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=36474
     Region          38..318
                     /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 mtedvprqva eqvraafglp lstmgqvthg adeharlwla stvdgaryav klsgggtaag
       61 lavtaylarq gvpgiaaplr thdgqlsvdh gghrlsvvpw vsdqraldga mteahwyayg
      121 evlaavhavp vtdelsrllp pggaaypsiv aatramaerl rdpdrsdpag pvladlaavw
      181 stvadrvrtl tggvermaad lrdrpapvvc hgdphlgnll lgadgqvwli dwddavlapp
      241 ecdlmfvrgg vlafapvtpg qqravlagyg padidparla wflavraldd lsdwtrqald
      301 pgadpaerdr aavivrglvs pvglvtlada amrdlappsr tprwtda
//
LOCUS       WP_357570272             132 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570272
VERSION     WP_357570272.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 132)
  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 132)
  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 132)
  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..132
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..132
                     /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=14744
     Region          4..125
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mreidkvawi liedgrvlst rsagkdvwyl pggkrepget dletlrreid eelsvevdvr
       61 havhlgtfta qahghaggvt vrmtcyragy qgqlrpasei aemawlgyvd rhrtspvdhl
      121 ifdhllaegl lr
//
LOCUS       WP_357570291             117 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TraR/DksA family transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357570291
VERSION     WP_357570291.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..117
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12675
     Region          9..117
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mtsdpsttre allrlreqtd sqaaalegdl rslfeasrss naddehdpeg stiaferaql
       61 tavldatrrr laeldvalrg iddgsygice rcsrpipaer llarpsartc vacasrr
//
LOCUS       WP_357570372             725 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570372
VERSION     WP_357570372.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=78758
     Region          31..716
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mrqdsalhhg tagegegtpe gesptatddv arrsavaeeq afldlatarr dgladhlrve
       61 lsaealdave qarqrmlgqr yeelrqareg lvfgrldgld gtvrhvgrig lrddgeddep
      121 llvdwraaaa rpfytatavd pqgqarrrhi rtsgstvvgv ddepldgtls aelvgegall
      181 aaldqrrtgr mstaiatlqr eqddiiraea tgplivqggp gtgktvvalh rvayllfarr
      241 tiadqavlvl gpsprfleyi aqvlpalget avvsatcdtl lpgiqvgrde srqlaeikgr
      301 alwqstlesy vtsllprpre lklrwqgefy aipaetvaqa lasavqgrpy hraravfaeq
      361 lhhlladavv eqretlmdem eegfedilar vdrgmarehh sgrastgsdv dgvfseeeve
      421 dlrsriagsa siarfveaww ptldpetllg tlltdrtlla rfapqlspae itavsaeptp
      481 wapsdialld aladllgeva apqpqgefva erarrqrgwv yghvvideaq elsemqwqmv
      541 vrrcpsrsit avgdidqaea ahrhrswaea vqavfgdrwt aatlticyrt prevmdltgp
      601 vltkagshna ppravrssgi apweltttpa eladtaveav relrqrwrgg tvgviapadr
      661 vnellavlnd vpvltatqak glewdatllv dpqgiaaepr gwnglyvalt rctqelgqvi
      721 lappt
//
LOCUS       WP_357570390             860 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570390
VERSION     WP_357570390.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 860)
  AUTHORS   ter Beek,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 860)
  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 860)
  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..860
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..860
                     /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=87572
     Region          9..856
                     /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          153..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 msrrvlsqrs lalawstirg rkggfvaafv avlcgsavit acgillesse rsgvpteryq
       61 aadlvvgarq alpvaddvdp rfgeratlpa drvgdvarvp gvraaiadvt vpvslvtada
      121 evlagpdgtp tlghgwssaa lgpfttgagr aptgpddvvl dsalaeragv tvgasvrlav
      181 gstvstyrvv gigglpgrql arqsavfftd drareltgqp drvdavgvla apgvdadela
      241 saieaavadv vvyadrdrse aefldigstr sfisemslaf ggsmvlvimi vvastlalsv
      301 rqrlrelall raigatpkqv lgmigaetmv vgtlgavlgv ipgiglslll reafilagav
      361 pddfelsisp lpvlgamvlc lvgarlggwi aarraarlkp vdalgeaave pptlgwirlt
      421 vgvllvpagl amafvlplvl pgegaaesaa fsafllifav allgprllgg avtvlgpwsn
      481 rrpgvsgfla tanahansrr laaattplim gitlaagqlf sattasaaaq dqaadglrad
      541 ytvtstsagv spevadvlrg vsgvsavtpv vrtrtlavfg peespqirty aaqgvigdrl
      601 vetmdlavld gdvanlrgnt valsriaadt lgaalgdtvd lrlgdgtpir ptvvarydrg
      661 lglgdvtlph dlvlehttdh ldfamlvaaa sgtdvgalgd alraavhhlp tvqvndresf
      721 vaaqsaaaag esatglilna vllgylaiav vntlvmataa rfrefallql vgatrgqvfa
      781 mmrgetriiv vaavligtla aappvvgtsi altrtpipsv pplvylgiva vaallgsaai
      841 mistrlamrs qpvvaigare
//
LOCUS       WP_357570394             479 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357570394
VERSION     WP_357570394.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 479)
  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 479)
  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 479)
  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 479)
  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..479
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..479
                     /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=49738
     Region          5..477
                     /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 menatydvvv igagpvgenv adrivrgglt aaiverelvg gecsywacmp tkallrsqta
       61 lraarqlpga reavtgelda aavlrrrdaf aahwkddgqv swlnsagial yrgqgrissd
      121 rivevtgagg attsltarha vviatgtsal vpdiaglrev apwtsraaaa asevpgrlai
      181 igggvvaaem atayaglgsa vtvlardgvl tqaepfvger vtrslrdagv avrlgveats
      241 vsrdgdgtvr itltdgapvd adeilvaigr tpntqdvgld rvglepgawl avddtlrvvd
      301 gagaligdgw lyaagdvnrr vllthqgkyq aravgdviva rargeaaddr pwgrhvatad
      361 eravpqvvft dpevasvglt aaaaetaglr irvvdydlaa vagsalhadg yqgharmvvd
      421 edrrvivglt lvgpdvaeli haatiaivge vplerlwhav payptvsevw lrlleaygr
//
LOCUS       WP_357570400             287 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Micromonospora].
ACCESSION   WP_357570400
VERSION     WP_357570400.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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 287)
  AUTHORS   ter Beek,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..287
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..287
                     /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=31804
     Region          3..285
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msrntvagws filpnflgfa altllpvvvl fyvaftnwnv fgvaewtgta nfrrmwddts
       61 fwtalrntvy yavfhipltl gaalglalll nrklrgvgff rtiaffpyit sivaiavvwn
      121 qlfspeygpi nallgavgvd dppgwtasat wsmpaviivg twrymgyyml lflaglqtip
      181 aqlyeaaetd gaspwqrfvh vtlpglrttt ffvtvlltie sfkvfdlilv mtgggpgqst
      241 lvlsqyiyqk gfeenqfgya savsivlfai cfgitviqfm vnkrrns
//
LOCUS       WP_357570408             144 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570408
VERSION     WP_357570408.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 144)
  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 144)
  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 144)
  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 10140345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..144
                     /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=16064
     Region          8..142
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04663"
                     /db_xref="CDD:467548"
ORIGIN      
        1 mpekavtqka lcyivrnggl lvfrhtdhsy eevgvqvpgg tirpgeaped aalreareet
       61 gltdfrvvrk lgeaeydisp lrfeiqrrhi flmelleptp lrwssqeghd gtqpptpfec
      121 fwvpltaghi lqsgqgallg rifd
//
LOCUS       WP_357570458             189 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357570458
VERSION     WP_357570458.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..189
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=20367
     Region          1..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 merlgltpar ltragaelad evgfdevtvs alarrfgvkv pslyshlkns qdlririalf
       61 aleeladrva davagragrd alaafahayr eyarehpgry aaarlrlgpe taaasaggrh
      121 aqmarailrg ydvdepdath avrmlgsvfh gyvslelagg fehsapaaqe swdwivdsld
      181 sllrnrsst
//
LOCUS       WP_357570462             275 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570462
VERSION     WP_357570462.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  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 275)
  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 275)
  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 275)
  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 275)
  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 275)
  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 275)
  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..275
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..275
                     /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=29158
     Region          2..204
                     /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 mtilvtgagg rigatvlrql yeqgrpvraa grtkpadlpg gvewadldla aptsaarava
       61 gveqiflyar pegaeqllka aadaglrhiv llsslaidhd aeqpgpialq hllveraiea
      121 agigatvlrp gafasnalqw aaqiraegrv alpyprtyse pvhpddlaev avrafddgra
      181 gavhritgpq slsareqvra igeatnrpie vreidpqrya qqlsahvpat fvrslldyqr
      241 erdgqpgpvy dvaallgrpa rpfatwaaen aasfs
//
LOCUS       WP_357570516             263 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570516
VERSION     WP_357570516.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 263)
  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 263)
  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 263)
  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 263)
  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 263)
  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 263)
  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 263)
  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 10588955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..263
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27329
     Region          4..162
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
     Region          <184..>262
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mtdlfgrahe igvldaliag arqgggsvll rgdagvgksa llhaataiad rhghlvltav
       61 gidgdaspyv slrrmlppqm idaadlppaq raallaatrt ddpaavpepf lvgmaaltvl
      121 tdapedrpit livddahwld aqsraviafl grrlaadpvl livatrpvdd pappstrprp
      181 spcrrcpptp rphcstrspp awtrssaars ctppaatrwh wpnypapgpa whpprrpsps
      241 attsgpaspa ataachrsaa tsc
//
LOCUS       WP_357570489            1823 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570489
VERSION     WP_357570489.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1823)
  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 1823)
  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 1823)
  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 1823)
  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 11463197
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1823
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..1823
                     /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]"
                     /calculated_mol_wt=189952
     Region          22..1362
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1370..1642
                     /region_name="hot_dog"
                     /note="The hotdog fold was initially identified in the E.
                     coli FabA (beta-hydroxydecanoyl-acyl carrier protein
                     (ACP)-dehydratase) structure and subsequently in 4HBT
                     (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A
                     number of other seemingly unrelated...; cl00509"
                     /db_xref="CDD:469797"
     Region          <1726..>1822
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
ORIGIN      
        1 msnptaadqs ddvtespehg iepiaivgla arlpgaadvh efwrnlvdgv estteltree
       61 qlargatpte vddpgwvnra plvdgydefd atlfgmtare aeltdpqhrl fleschtale
      121 dagydparyd gaigvyagtg gntylhryvl rnqrvggnph gtvsiatgns pnyvatnvsy
      181 rldlrgpslt vhtacstslv afhlaceslr ngecdmalag gvnielphvg ylgmegftsp
      241 dgrcrpfdaa angtvwgsgv gvtllkrlsd aiadgdhira vvrgnainnd gagkvgftap
      301 svdgqvaaia qavdmadidp rtisyveahg tgtamgdpie vaalsavygr dtdergwcgi
      361 gsvksnighl sqpsgivsvi ktvlamehgl ipptinyetp npavefadtp fyvantlakw
      421 dtdggprrag vssfgiggtn ahvvleeapa ayrtdrrvrp ahllqvsaat pgaldaavqr
      481 laahldgaad agpayladva htlragrrph phrravvasd lpgavtalra pkrgaqpstg
      541 gpapkvallf sgqgsqyagm gaqlhaeqpr faavvdecae lllpdlgidl rdlilgrdpm
      601 agerltetry tqpalftvey alaalwqatg vrpaamighs igeyvaatva gvlslpdalr
      661 vvaargrlmq slptgsmlav sldesavadv lpdglsvatv ngpgtcvvag etaaveafaa
      721 tltakskmlr tshafhspmm epilaeftal mgtvslrppt apflsnvtgt witaeqatdp
      781 aywaahlrqp vrfgdcvatl laagtwqlve cgpgrqlasl armqvakaap eqhpliplgs
      841 lpaagettgd laallgtaga lwcaglpvrf dvdsaarrvp lpsypferrr ywidpdpeqq
      901 vaaapvetgp rplpewfavp vwrqaaplpp tgslgrclvl tagargdalv aglraagadp
      961 ilvrpgdaft adggyrlrpg vrsdhealva altadgglpt rlvhaftldg aptgtdiaat
     1021 waaqelgffs alhlvqalag agltgedgdv vldlvtagtg dvrgddlrrp ehatlaglar
     1081 vlpaelpgla vrlvdadpad ddvtalvael rrprepeval rggrrwvadv eqvtldaege
     1141 pgalrdggry litgglggig itlaedfatr araklvllar sglpererwd dhlavhgddr
     1201 agraiaairr meaagaevlv laadvtdpad lrrvrdaaqa ayggidgivh aaglpgggmv
     1261 evkeraeaer vlapklagtl alaqvfgdlp ldfvvlcssi tavvggfgqv dycaanafld
     1321 aharsgagwr apvlsqnwgg waevgmavet aapagfraag rdtvtstvdh pvlttkvsgp
     1381 metvlhglvs asthwlldeh riagvpvvpg tahlesvraa vaaampapdg eaavelrdvv
     1441 flepfavpdg tiaqyrvelt paddggtdfa vrslasgllr thvrgaagwt deptpparrv
     1501 eptgrrvddd asfgrgrtsm ltfgprwaal sehhladvte lavieapaaa lgdlpawglh
     1561 palldvataf grgqgsgayl plsygrivvr gplparftse lrhrpghtde vvaadlslrd
     1621 pdgrelvais dfvlrrvdqg avtggltets tvdapslvst edirpvdgae afrrsltagl
     1681 gaqvviatrt vadirhragr vtagdlagdd tvtgstrsgl gdggaapgte lekiiarvwe
     1741 dglgvaevgv dddffalggn slvavqliaa mrkatgvrlp mrslfetptv aglaarieel
     1801 raadtddpaa paptsaiprl pra
//
LOCUS       WP_357570600             577 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570600
VERSION     WP_357570600.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 577)
  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 577)
  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 577)
  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 577)
  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..577
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..577
                     /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=61630
     Region          1..438
                     /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 mqirrviarn frgirhadws lprqrfvclv gpgdstkttl ldaialvlsp rwtvqftdad
       61 fhrcdvsqpi vlqlligdld dtmladsafg ldlcglaesg qllhdpvdga eecvllqlrv
      121 dedleaewtv mrpgstettq pltaskrkal glfridervd thlrwgrgsa ltrltetsga
      181 sqavtlagra arnavfdash talqaaadtv alaassigga aytglrpgwd plavastgal
      241 llhegavplt haglgtrrlt siavqegaal nghvmlvdei eqglephrll hvlhrvkqra
      301 igsrgqviit thspsavqal etadicvvrs tagettvrqv pdvvhdaqss lracpsavla
      361 rkvivgegkt evgmvrhlmr awdteqidad qpthaalgva ladgggktap vrakvfqdlg
      421 fstlllvdnd dpnfdadiat athagvavir wqaghsteae itsaldidgl sdllqlaael
      481 sgedpvrdav iakldrvpap gqlspaswle aghalpelqr avaaaagkka wfkredtger
      541 lgafvldhwd qfkgvalghr ladlhsfiyg dshyysq
//
LOCUS       WP_357570816             309 aa            linear   BCT 28-DEC-2024
DEFINITION  SIS domain-containing protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570816
VERSION     WP_357570816.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Bateman,A.
  TITLE     The SIS domain: a phosphosugar-binding domain
  JOURNAL   Trends Biochem Sci 24 (3), 94-95 (1999)
   PUBMED   10203754
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454870
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..309
                     /product="SIS domain-containing protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32565
     Region          5..308
                     /region_name="AgaS"
                     /note="Fructoselysine-6-P-deglycase FrlB or related
                     protein, duplicated sugar isomerase (SIS) domain [Cell
                     wall/membrane/envelope biogenesis]; COG2222"
                     /db_xref="CDD:441824"
ORIGIN      
        1 mayvdaeias qpdcwreaaa lagvvhgdlp rpgervavvg cgtswfmama yagrreqagq
       61 getdafqase fptgrrydrl iaitrsgttt evlellaalr gqtpttvivg dpaspavela
      121 taavtmpfad ersvvqtrfa ttalallrah lgdpvtalaa daevavrspl pidpatieqv
      181 tflgrgwtig laqeaalkcr eaatfwaeay pamdyrhgpi svgapgrlvw afgelpdglp
      241 edvaatgaaf vhsrthgwrt vlgswsagrt pvdpmadlil aqrfavalat srgldpdapr
      301 hlsrsvvla
//
LOCUS       WP_357570738             328 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357570738
VERSION     WP_357570738.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 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   5  (residues 1 to 328)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..328
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..328
                     /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=35592
     Region          10..237
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          <259..324
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mselrfslad vagvrlavsp vnetvmsmwa lanpvryavh lpwidrarvt lrrpevadrv
       61 rplvglvvpg rwlpdfltpa arpnvemaeq ldqiaatppa vvaqdllatt wqrplspfgr
      121 alladpggll pqvvdavrvw ydeaiapdwp rmralldadv ayraaqlaes gaggffeqlh
      181 pslrwhgdrv vsddtferdf dlrgrglaln ptvfteqhvl wnlledslpa gaypvravgt
      241 lweatgpppg dplarvigpg raallhllet altttdlarl tgmsagnvsq hltalhaagl
      301 vsrsrqgrhv ryrntevaav llrasgge
//
LOCUS       WP_357570845             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570845
VERSION     WP_357570845.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31200
     Region          36..295
                     /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 mrgfrwpppp dsgprtwgpg pggprtgrpa lpepetelvt tphgvrlerl vtgtgdpvtv
       61 fahglgngia ttrpfgsgvt grkvffqfrg hgrsdapdgs wdyldlardl raiadlggas
      121 rafgaslgag alcrllaesp erfeklvffl pavldeprgp vaheritdll aavqsgeasa
      181 vadvvalelp aavrntpagw aylrqrldql lrdglaeglg tlaeqtslrq igdlaavtap
      241 alvigcagdd lhpvevaerl avalpqatlh vydrpgvlwt eradlrdria gflne
//
LOCUS       WP_357570860             189 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Micromonospora].
ACCESSION   WP_357570860
VERSION     WP_357570860.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  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..189
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..189
                     /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=20313
     Region          12..173
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msspspggdd laaigtdpaa ferfyrrhve tigrfvarrv ddphtaadlt aevflavids
       61 aagfqpergn elawlfgvar nviaaehrra trhlrasgrl agrrlldadd iarieerida
      121 eslarrtyra lgglpehtra llelvavdgl sltdaaaalg ispvaarvrv hrarravrla
      181 laqsesalv
//
LOCUS       WP_357570843             204 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357570843
VERSION     WP_357570843.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..204
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20896
     Region          4..>65
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 matpkdlpdv ggfirdlrrn akislrqlae qagvsnpyls qierglrkps aevlqqlasa
       61 lrvstpamyl ragllddkeg hgvlaaiavd tdltmaqkqs lsqiyetfrr entrlaeata
      121 eaegagttga ttptdvadqp advanlaatg pttaggtpte avlesvavte agtapapgst
      181 stpekkaagp aareaatvae eets
//
LOCUS       WP_357570687             559 aa            linear   BCT 28-DEC-2024
DEFINITION  murein biosynthesis integral membrane protein MurJ [Micromonospora
            sp. NPDC048905].
ACCESSION   WP_357570687
VERSION     WP_357570687.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Kuk,A.C.Y., Hao,A. and Lee,S.Y.
  TITLE     Structure and Mechanism of the Lipid Flippase MurJ
  JOURNAL   Annu Rev Biochem 91, 705-729 (2022)
   PUBMED   35320686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     gene            1..559
                     /gene="murJ"
     Protein         1..559
                     /product="murein biosynthesis integral membrane protein
                     MurJ"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=56272
     Region          20..520
                     /region_name="MurJ"
                     /note="Lipid II flippase MurJ/MviN (peptidoglycan
                     biosynthesis) [Cell wall/membrane/envelope biogenesis];
                     COG0728"
                     /db_xref="CDD:440492"
ORIGIN      
        1 msrpaplvga grlagaaali avltvasrla gfgrtavftw vveqsdlggm yviantvpni
       61 vfeivaggal aslvvpllag avaaddrrtv aattgalltw tvsllvplav lvvlfadpii
      121 slisegrsaa elaagarmlr vfapqlplyg igivltgvlq ahrrfawpvi apllssltvv
      181 vvyvafgaaq grgmsvaqvg rsgelllsgg ttlgvvvlsl slliplrrlr vrprfgyaft
      241 pdarervggl atagavtvaa qqiallvvln rvsggptgsp qvfnlaqaiy llpwavlavp
      301 lavasyptla tasaagdedg yrrtlsgavr gvllfsclgv aalvgtaqpi aalfypdnpa
      361 staaaisgfa pgllgyglfa vlsralyarg dtrsatvait lgwlvvpava lpltallpta
      421 drvlavtsan svgmlvlgal lllavgrsag rpalagaara gaagglagvl aalaglgltr
      481 wldtpgggtp ttaaalgqgm lsgvlvgavf lavvwfvdrr dvqpllagvl rrlgrrgprg
      541 ggptpvspqr gdgketaar
//
LOCUS       WP_357570965             329 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048905].
ACCESSION   WP_357570965
VERSION     WP_357570965.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 329)
  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 329)
  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 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   5  (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
REFERENCE   6  (residues 1 to 329)
  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 329)
  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..329
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..329
                     /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=37141
     Region          33..329
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mtstlrpppp apprspaeaa spapraprrr rswrqalrrd wqlyslailp llfflifryl
       61 pmlgniiafr rfkpggsifg eywvglryfr mflsdptfwe vftntlvlgt ltllfcfplp
      121 ivlalmlnev rarrfkrfvq svsylphfls ivivaamvmq ltsvggaanq lvglfggepv
      181 aflqkpewfr tiyvssevwq tvgwgtilyl aalttvdedl yeaaridgas rwrqtwhvtl
      241 pgirptmmtl lilnignfla vgfekillly npltyptadv vstylfrmgf qssnfsyaaa
      301 vglfeavigl ilvltanlis rrtvgtslw
//
LOCUS       WP_357570999             272 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Micromonospora].
ACCESSION   WP_357570999
VERSION     WP_357570999.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..272
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29379
     Region          5..>68
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          95..264
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mttrtrpgra vgellrdwrr arglsqldls igagvsarhl sfvetgrsrp spdlilrlae
       61 qlnmplaern tvllaggyap aypsqelsdp elaplraavr qmldghspyp avlvdrhwql
      121 veanpavalf tdgaaphllt ppinvlrlsl hpdgmasrii nlpewrahll arlrqqaamt
      181 tdpvlsdlle elrgypsgdd vvaptsders rvviplryrh gerelsfist ttlfgtpldv
      241 tvaglaveaf fpadpvtaaa lhalgtpgag tr
//
LOCUS       WP_357571047             332 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571047
VERSION     WP_357571047.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..332
                     /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=36082
     Region          26..320
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mttpstvsdt rrgdtatdpp apgpgtarqr grqprpgrgg vlaifltpal vlflllviap
       61 ilvagygsly kwngfglpen figldnytra fqdptfrgdl wrgfvlvlls lavqlpaala
      121 lamllnqplr gravyrliff apyvlsevtt avlftlvfsp nrglgealsg wlsadagavf
      181 adpdtvlfav flvvswkyfg lymmlflaar qgipkelsea avtdgatawq afrhvtlpll
      241 gptirisvfl svigtiqlfd mvwvltgggp ihssetmavt myeygfrrfe vgyasaisii
      301 mfllslvfal fyqrtvlrrd tagaitnqgg qr
//
LOCUS       WP_357571179             841 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571179
VERSION     WP_357571179.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 841)
  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 841)
  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 841)
  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 841)
  AUTHORS   ter Beek,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 841)
  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 841)
  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..841
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..841
                     /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=88224
     Region          1..838
                     /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 miaklavrnl lahrarfllt amavtlgvaf vagtmifrdt asqsfgplfe kraqaetvtv
       61 rgvetvsgag appstvpsgl lttlnekvtd aevygqiegy salvrdngsi igedvnanlg
      121 gaftprpgvt ltllsgrept gadeivvetr tategqvkvg dsytvvaqrd trrmkvvgif
      181 elqdedvgrv vtyvgyspaa ahdlltgpgn ysaillkprq gvsqeevlgq vrpllsqqye
      241 attpaeqaeq feaelkdlfa llsrfllafa gvsvvvgsfi ifntftmlia qrtrelallr
      301 algagraqvt ravlaeglgv gilgatlgli agvgvsfllr llftqfagtq lpirapvias
      361 atvfwsylvg vlvtvvaayv parrasripp maalrddvve arrarlvrli lgltvallgg
      421 aglaggvgdr gadgaalvvi sgvilllaaa mvspylgrpv irvlgwpiar ltgavgrmsr
      481 enarreprrs aatasalmvg lalvsvatvl asslsasaea dvdrqfgady tieprgltgf
      541 krevvdrvaa vpgvhsvtpl qigsleigre emaavvadaq alsvpanlti legsatlgtd
      601 dilaqrtlae skgwqvgstv agkypdgkaa tfrvggifad nrmvgrsimi hpdgytshtp
      661 ttliqkafid iddaraatal agvrdtlray pnvdlqdred akaaarqgid qiltivvvll
      721 vlsiaiatlg ivntlglsvi ertreigllr avgmarsqva amityeavmi alfgavlgvg
      781 lgtavgwalq ramadevgtl hipldrlgly llaaiaiavv aatwparras kmnilraihh
      841 s
//
LOCUS       WP_357571224             243 aa            linear   BCT 28-DEC-2024
DEFINITION  GAF domain-containing protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571224
VERSION     WP_357571224.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 243)
  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 243)
  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 243)
  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..243
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..243
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25531
     Region          <11..>238
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 mayshpieps nafaelgrim pgktslrdvf qrvvdltgls ipevteasvs lvqgkeahtp
       61 actgglalal desqyelghg pclqaaaatt iesitnmate srwpdwtara lragahssls
      121 iglpihatig galnlyatep hafddhtiav aqtfasyasl aiandhldna rttlsrhida
      181 amdsgavieq akgiimgdrr ctadeafavl tttarnttrt vrdvartlvd rtavsraqvt
      241 ggp
//
LOCUS       WP_357571235             420 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571235
VERSION     WP_357571235.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..420
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..420
                     /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=45230
     Region          1..415
                     /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 mvtpsvmiig agigglclaq glrragvsvt vhertkartd wlqgyrihin pngsralhac
       61 lppatwqafl dtvsidtggf gftterlddl lrftpeeitp agapegrhyg vsrislrevl
      121 lsgmddvvrl dhefthyeat tdgrvtayft dggtatadvl igadgansrv rrqllpharr
      181 vdtgvvavag khrladaalp rvltqdvnlv ipksrgsfft avwhpgpqvi appdqflldn
      241 ttayllwgyt daatafpaeg veslpgtdlq rlvlnrtdgw apalreviag sdpqtinair
      301 vrsatpvkaw etgrvtllgd aihnmtpmag igantalrda allcvkltev hagttamvpa
      361 lhdyerqmld ygfaavrqsl rnarqasttn rlartafraa lrtasavppl rrrmatqlgq
//
LOCUS       WP_357571248             362 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [unclassified
            Micromonospora].
ACCESSION   WP_357571248
VERSION     WP_357571248.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=37320
     Region          14..356
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msgpllqlrp sgrttrlvvr srggrlslrv hlralvagta llltalgval vnlssgdfpi
       61 pvpdvlrslv gqgdpgtdfi vhelrlprvl itllvgtalg asgtifqglt rnplgspdfv
      121 gltvgaatga livlllfngt gfqvaagaiv gclatsvaiy llafrrgvqp frlvlmgvgv
      181 aalldsfnsf liyrsrldea iaaqvwligs vngpgwtevt lvavavavll pvalyhgrhl
      241 dmlalgdeta mlhgvpvers rmvlalagvg laagataaag piafvalaap plaarltrsp
      301 nagilpaalm gaallaasdw vaqrllpddd vpvglvtaal ggiyltwllf herrnrgqga
      361 qr
//
LOCUS       WP_357571252             226 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571252
VERSION     WP_357571252.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=24007
     Region          12..202
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtteprsnap tivedlllll fqpssgtiag entlfyvlgg avladlalge nlstadrgrl
       61 rgvpdhppsd gllrpawdyl aekprgvqta laaigpalrq pvlerliarg dideesrkvl
      121 glfrttalre grterrsrll advrqvlvdg aepqarvaal aallsasgtl pqfhreipwt
      181 ssvisrakel ergdwgadaa aeavtrtvta tvvnsavaai ivlprg
//
LOCUS       WP_357571292             382 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571292
VERSION     WP_357571292.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 382)
  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 382)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 382)
  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..382
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..382
                     /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=40436
     Region          160..380
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlgysalmrt glsdvwnrik swiiavgvaa allitalage hsttglkllg yalvvtsgla
       61 laainrapip vliftglcvv gynaigfavp avayliavya avrsghridt lvvsvvvmtv
      121 lplaimtspe gaakepiaqa rgvlelawli aaaaagealr qaerradeae htreetarlr
      181 atqerlhiar elhdslthqi siikvqaeva vhlarkrgeq vsesllaiqe agreatrelr
      241 atletlrdvs kspshgldhl pellagahgi glsttltieg erqdvpdavd rtvyrivqes
      301 ltntarhaaa anasiridyl pdaiairidd dgtakpssap vhgvgllgmr ervtalggsl
      361 raeprteggf tvqaelpvar is
//
LOCUS       WP_357571332             143 aa            linear   BCT 28-DEC-2024
DEFINITION  cold-shock protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571332
VERSION     WP_357571332.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 143)
  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 143)
  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..143
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..143
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15659
     Region          5..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mwavgkvirf deargygfia pakggedifv handfgeqrh lvhpgmrvey eveagdrglk
       61 vaalrivepv agarpervpd vvptrtgqtg eddgmcdvls preftyevte lliervptlt
      121 aaqisairqp lvdharshgw ves
//
LOCUS       WP_357571372             307 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: cytochrome c biogenesis CcdA family protein
            [unclassified Micromonospora].
ACCESSION   WP_357571372
VERSION     WP_357571372.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..307
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=31430
     Region          12..169
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mtaalllalt agmlgavnpc gfallpayls llvagasdar gavgraltaa agltlgyvlv
       61 fgafglalap lagwlrprlp wltvvlgvll vtagcwllag rrlpapgwsa raprltrtwp
      121 smalfgaaya laslgcaiap flaivvtslr agstgqglal fgayalgmgl vvavaalava
      181 llrdglvarl rvagalvprl sglvlllagg yvawygwyel rlsagrrdal rdpvirvaae
      241 vqrtladald avgpapllat latllllatl arrphprrph prdlavsvat ktaehhvsat
      301 etarsat
//
LOCUS       WP_357571352             282 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571352
VERSION     WP_357571352.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31432
     Region          13..71
                     /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..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mprftpatpr srrlgrelrk lreakeltge aaaaivdcsp srisriesge irprvgdvme
       61 llvaygvkid eepgtslldq arglredgww qrlggkyaty iayeieavel knfepmlvpg
      121 llqtesyare vnvigretdp etidqrvsar mtrqevlrrq ptplrmhail seaslrtevg
      181 gpdvlreqld hlvtlsrlpn vtiqvlrfea gahlaissgf allsferdep plgyietlag
      241 elflessrdl arlsaaydnl ktlarspaes ikfvkelskh gt
//
LOCUS       WP_357571379             577 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571379
VERSION     WP_357571379.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 577)
  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 577)
  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 577)
  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 577)
  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 577)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..577
                     /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=57151
     Region          68..>422
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mggvsnrpwr atvavaalta llvsgcsgaa erptptaspv gasaapsapa atpasdpaar
       61 aaalvatlsd edlvgqvlmp yaygdsatkv sagsaagnqa lagvdtpadm itkyrlggli
      121 lvgfsaddpt kgnqettnvd npkqvhelts glraaagrla agpapllvgt dqeygvvtrv
      181 tdgvtvlpsa laagaagdpk lteaawraag aelaamginv dfapvadvla trstvigsrs
      241 fgadpkqaaa qvggavrglq aegvaatlkh fpghghsadd shqdlpvltq saaalqsgaw
      301 ppftagidag amavmsghld araidpgtpa tfshklltdv lrgqlgfkgv vitdgmnmpp
      361 akrwapgeaa vralnagndl ilmtpnvgqa ydgllaalrg gslprtrlve avtrvltmkf
      421 rlaetpaaqm stlnapahra aadalaaaav tvlrgtcgap vrgpvtvtss ggrdgtraal
      481 taaltaagvq vkpsggtivh lvgygdgakd lradaavtva mdtpyvlsga tsptllatys
      541 ssrasmtgla avlagkarpg grspvtvpgl pattcgt
//
LOCUS       WP_357571399             152 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Micromonospora].
ACCESSION   WP_357571399
VERSION     WP_357571399.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=16518
     Region          14..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msddhdettl gqietevall mrfgeatrra tgtaehrvld raayvilrhl adagpqnvsa
       61 ladrlnldgs tvtrqvsalq rdglitrtpd psdgrgtvis ptpaglqrma vvqaartrly
      121 gdmladwtte dratlaslls rlnqalinrn rr
//
LOCUS       WP_357571417             110 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571417
VERSION     WP_357571417.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   4  (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
REFERENCE   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..110
                     /product="PadR 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=11772
     Region          10..90
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mritipiakv laallaepde qrygldlmrl tglpsgtlyp vlhrlqgagw laadweaidp
       61 vaagrparry yrltadgvaq arqaladlra aipdgrrswg gteptgapaw
//
LOCUS       WP_357571432             963 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571432
VERSION     WP_357571432.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 963)
  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 963)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 963)
  AUTHORS   Rosinski,J.A. 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 963)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..963
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..963
                     /product="helix-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=101595
     Region          <4..920
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          894..956
                     /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 mtvraassvi vgrqrelatl realaragag epttvlvgge agvgktrlle efsagttdgg
       61 arvlvgqcle lgeaglpfap faaalravlr vdgpevfagy eaefarllpe lgraplaaps
      121 aapvgdaprg ylfdlvaelf qrlaevrplv lmiedlhwad rstrdligfl vraarpgrll
      181 lvctyrtdel qrghplrpfl aeldrvrgvh rvelgrldrd gtgavladll gvepstravd
      241 dvhgrtqgnp ffieelavag dplgcaalpe tlrdlllarv drlpepsqrv lriaaaggtr
      301 fahdllaeva glpdteleda lraavaaqlv vadpdgdyef rhalvreavh dellpgehar
      361 lharfaaaie aqphlvavgr apaeiahhwy aahhhpralv aalsaardaa dryayaeqrr
      421 lleralelwe lvpdaadllg idhlglleqt ldaaitagdf sraitltrag laevdadaap
      481 lraarlldqr grlmallgks dgsreldeay rlaaggpigv ervrlladia thlakiapqr
      541 aaqvaaeaga aaaalgeela llptriamlc hgerdledgl aglatveaaa rtagdtptlv
      601 lakvfqsdml celgryaesa qaaeagvaea rrvgisrstg ayllsnraea lialgrwdea
      661 egvcaeaari dlsgvtglhw lqvgaglrla rahpgaeelv dralaflgrp ylwpnhrlpl
      721 helaieaala addkieavra arvavadahl pqlpregwpv lsavartaar vgdrdlaaav
      781 salaadlpvr hpaarahaaq vtallaigdq alpawraavd awradgqpyp lgrallalae
      841 taaaggerde vsaavteate iarrlgatpl aeaaatlarr vglrgtgqgg agadlltare
      901 revlrlvaeg hsnsriaeql fispktasvh vsriiakldv tnrgeaaala hrlgllaepa
      961 ppr
//
LOCUS       WP_357571457              95 aa            linear   BCT 28-DEC-2024
DEFINITION  Lrp/AsnC family transcriptional regulator [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571457
VERSION     WP_357571457.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..95
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=9866
     Region          <2..75
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mitaivlidc atdaipevae tlaslsgvse vysvaghvdl iaivrvrefd qiaqviagsi
       61 skvpgvlntk shiafraysq hdleeafaig lssad
//
LOCUS       WP_357571502             395 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571502
VERSION     WP_357571502.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=41654
     Region          22..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 mrsavvvgag vgglavagal arsgwqvtvl eraerirpep tavvlwpngv ralqalglga
       61 gltaiatpls dggvrrpdgh wlvqprpipa drmpvvvhre dlhdaliagl gervelrtgv
      121 tvrhvrvepg erpgvsdgrq tieadlvvaa dgtdsgirrq lapesrvvss gcaawravip
      181 wyqaprlpdd qplvgeilga gyrfvaaslg ergssggstr ggiywvataa gaprpeppet
      241 qlallrrwya gwpapigall datdpadlvq qevrelrplp raygfpvgpg gvvllgdaah
      301 ampphlgqga clafedavtl asllrearlp davqaydrir rprattvvrq trrmsavlqa
      361 rgrlalrard aalgtintrl lssaaasaaq wrppa
//
LOCUS       WP_357571518             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571518
VERSION     WP_357571518.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  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..191
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..191
                     /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=20919
     Region          17..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtsagqapev faqrpkrada rrnydaliaa areafaehga aasledvarr agvgigtlyr
       61 nfpsrrhlfe avyveevral srsaedlgel ppwdalvawl hrfvayvatk ralaeqllhd
      121 seiftscrte iyaageplmr raqdagvvra dvgfddvvrl isgltmaqfp speqrdrvlg
      181 valdglratv r
//
LOCUS       WP_357571540             191 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571540
VERSION     WP_357571540.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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 191)
  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 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 191)
  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 191)
  AUTHORS   Rosinski,J.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..191
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..191
                     /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=21183
     Region          12..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 metpdvrhvt dsrvlaamah plrrrlmdvl kvhgpstvgl laertgqapa nvshhlkvla
       61 aadlvteape lardrrerww rlvtrgvrws nrdfdadpaa ravadaatsl nldrhvalar
      121 awhaaddaaq aawhdgpfsl nkwlhltpde laelsremva lldrwadrsv padgherqpv
      181 fvfahgipar p
//
LOCUS       WP_357571615             260 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571615
VERSION     WP_357571615.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..260
                     /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=27170
     Region          2..209
                     /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 mrvlvtgagg rlgravlarl hsagvgvrat srrpharsea ewvvadlatg rglpealsgm
       61 davlhlasap kggqtyqvdv lgtrrlvvaa gaagvghlvy asivgvdrvp ipyyrhklaa
      121 eevvaagpvp wsvlratqfp qflddllass arlgpvigdr avlaqpvdpg evaarlaarl
      181 vagplgavee yggpqvlrfd eaarawrear gsrrpllpvr ipgrlgrelr agglvtealp
      241 rgartwadhl adtyggtgrk
//
LOCUS       WP_357571630             880 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571630
VERSION     WP_357571630.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 880)
  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..880
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..880
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=92552
     Region          11..879
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtpdhegsrs pagrtplpel lrghrraagl tqaelasrag vgvrtvrdle rgrsvrpqrt
       61 tvellatala ltgtsraafl aaarghsgte spgpdatpta lgtgdrttsq slstnppatl
      121 pppialvgrd rdlaelaeml taergprlvs lvglagvgkt alatavahlv avdhpggvag
      181 vlvaegsdgp dvfaaamavl gaarlpdllt rlagqpallv ldavehapdp vaatlhrlig
      241 avpslrvlvt grhpvglpge rvwpvapldv pppgdgraga apleswpava lfttrlaqvr
      301 reppspdelp alvalvrrlg glplaielma argrlldlte lldrygdhvl dlatpadpvv
      361 hpgaaaavsv tlrdavatsy rllapderaa lrqlavfgdr wsvelaeeml gdradrdgav
      421 aidpvplldr lvelgllgvr gtgpfrfrll davrdyaieq aaaageltci rrrhaeviar
      481 lvariasdlv gprlpdavhr ldemssdiss slahattddp ltalrlaacl trwwrfrgrd
      541 vagrqwlrrl ladprtadad pilrgwaalg vaqlaaehga gaeelstart algifrqagd
      601 vtgelearni lgillssvgg qdeareqaet alrlaarngr trdlavaqns lawheirtgd
      661 laaarrrlaa vdrlaaesge qrlrvlawan raevarlegw yadavdqgrr alaalselgd
      721 prrrrrvlgk iglalaqdgr aveatevlte lragtaeava aespraparr avaprqrsge
      781 salsaggpev glgaliegnl alhrgdrela aewfaaavda kgqerrdvve alvglaasta
      841 dpavlerler vceesgirll pqesgllyal tatrsgpeap
//
LOCUS       WP_357571699             799 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571699
VERSION     WP_357571699.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 799)
  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   3  (residues 1 to 799)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 799)
  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   5  (residues 1 to 799)
  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 799)
  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 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..799
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87398
     Region          19..776
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mqtssatdqp ppasgtvdde awrirrtkad ldrlgetesi favgngwvgw rgvldegapc
       61 gmpgsyvngf herrelsype egyafpqasd tvisapnaal irlwvddepl dirtgtlrgh
      121 eqvldlragv lrretewisp ggrgvrirst rlvslprrpv aavqyevepl dapvevrvcs
      181 dllanetvpe rsddpraasv pdnpltaeay raadldgvlv hrtersgqrv avavshlvdg
      241 pdtvtvtgdc tpdrvrltva drlhlgerlr ltkfaayewa midgtavdel aalvtaeada
      301 aradgfdall tdqraaldaa wqvadvqldg dpelqqairf amfhliqagr pdsdrtiaak
      361 gltgngydgh vlwdtetyvl pvltylapav arsalrwrht hlpearerat elrltgaafp
      421 wrtiggrecs gywpagtaal hvnadiadav lrylaatdde rflaeaglel lvetarlwhg
      481 fghwsgedaf hlhgvtgpde yaalvddnvf tnlmarrnlr gaadaaerhp dvagrlgveh
      541 devagwraaa damvvpydhe rgvhqqaagf teqpewdfan tgdddyplll hfpylelyrk
      601 qvvkqadlvl amqlcpgeft aaekarnlay yeartvrdss lsaapqgvla aevghldlay
      661 dlfaesvlqd ladlgdktad glhlaslaga wlalvqgfgg lrddrgvlsf dprlprridr
      721 lafslhwrgh rlrvtvtpte aryelpgagp daevelwhhg eslriteaep vtrpmpavpd
      781 pgpephsppg rrparrsad
//
LOCUS       WP_357571746             263 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571746
VERSION     WP_357571746.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 263)
  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..263
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..263
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29099
     Region          <2..45
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          66..246
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvaeqlecsa skvsrietgh ttatprdvrd mlriygvvga esdelvqiar earqkgwwhp
       61 ystvlvgayv gleaaassir ayeqqvvpgl leteeyagam iraarpdfta dqvhqrvrvr
      121 lgrqslltqd dpvdlwvvld eavvrrpvgg devmrgqlkr lvevaelpnv tlqilpfevg
      181 ahagmdgtft ilsfpepgdp dvvyaenatg glfleksdel qkysfifdhi raaairpees
      241 vahiaklaee plwkwrpkgs pwt
//
LOCUS       WP_357571770             391 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571770
VERSION     WP_357571770.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 391)
  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..391
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=40050
     Region          163..388
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpavaaptvp ptldnpagga lvlifttipa ilrltcgvig gavalsvpap svepavllpg
       61 vaaltgwsiw yayramrqgi tpslvaadvt italvcllip vlvapgvlpg egswiavlas
      121 ttvinaqata parwsipagl lvtvtyatga qaagnatear ahattllvqt actammaavm
      181 rrrigradra fvehqrltrq alvaraarda erqqnrdlhd tvlgtltmvg lgavtgssat
      241 frdrcdadlr tlvaltdvgp vagdgpvpld grmravagrl pelstqldlt pcavpagvad
      301 aigesayaal snvvrhapga rvtlrlsrha vgvvvevadd gpgfdpatvp phryglresi
      361 hgrmatvggr advrsapgag trirlewpgv g
//
LOCUS       WP_357571776             348 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571776
VERSION     WP_357571776.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 348)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..348
                     /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=38310
     Region          88..346
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mkfdfadqqp kflmlmyglv afvvvvggll llldvvpawf arrreaqlva asvgggplpr
       61 rrkqreglfa fffllptlll lviglvvpai rttllslmdg sstnwvglrn ygwmfsddsi
      121 vrvlintlvw vllvplvatg fgllyavlvd karfeavaks liflpmaisf vgasiiwkfv
      181 yayrgdgdqi gllnqivvsl gggpkqwlle splntllliv imvwiqagfa mvvlsaaika
      241 ipgdiveaar ldgvspwqmf wqitmpsirp alivvvvtlt iatlkvfdiv rtstngnydt
      301 sviasemynq afrygqngqg salavflfil vipvviyqir nlrqqreg
//
LOCUS       WP_357571858             448 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC1 kinase family protein [unclassified
            Micromonospora].
ACCESSION   WP_357571858
VERSION     WP_357571858.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 448)
  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 448)
  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..448
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..448
                     /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=48514
     Region          1..445
                     /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 mtdiprravs rtaklaalpl gfagrtvlgm gkrvtglasd visaeiqqrt aeqlfsvlgq
       61 lkggamkfgq alsvfeaalp eeiaapyrqa ltklqeaapp lpvasvhkvl aeqlgpdwrd
      121 rfvefndvpa aaasigqvhr arwrepgfde sgapnsrdva vkiqypgage allsdlkqls
      181 rlggmfraiq pgldvkpllv elreriteel dyeleaesqr afaeayaddp eiyipkvina
      241 aprvlvtewv tgtpladiir egteeerdea grlmatlhls apqragllha dphpgnfrml
      301 pdgrlgvidf gavarmpegt pepigriaal alrgdadevv aglrsegfig ateeidaegv
      361 ldfvrpmlep iaadgfrftr awlrgeagrl asprsptyql srqlnlppsy llihrvtlgs
      421 igvlcqleak apyrsilerw lpgfapva
//
LOCUS       WP_357571844             303 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357571844
VERSION     WP_357571844.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 18123688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=32464
     Region          13..219
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          230..295
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mievrftpdd lsrvrfvhsp laelvasswa lrkpakywmh rpwreraerl lpgaglepll
       61 avlrssngyv pdfltpigva pnlaaelrav agtdpsrvrr qldragaprl apdelvaqlr
      121 ryftlliapd wprlralala dirrrtllaa dqggrtllre lhplirwdga alrvavgtsr
      181 paglddrpwt llptsfsgpt vhailegdag palcyppagl gglwasppps aalgallggt
      241 raaalsllda plstgelaam lglapatash hlttlrdngl ivgvregrvv ryartvlgdq
      301 lvd
//
LOCUS       WP_357571869             179 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571869
VERSION     WP_357571869.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=20013
     Region          1..176
                     /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 mfatdrvrlr pptpddaadm frlygdpelh litdgepflp rhvghirarl ekqvseppdg
       61 raavpllaet vadgtflggg alwgidafnq yahlgisllp eargqgygte virllcrygf
      121 rnrnlrrlel etvasntamr rtaetcgfth egtqrereyd gdgfvdmviy gllrrdwtp
//
LOCUS       WP_357571880             147 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357571880
VERSION     WP_357571880.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 147)
  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..147
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..147
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16154
     Region          3..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(4,6,8,17..19,21..22,27,37,43,45,47,49,59,62,68,
                     70..71,83..84,86,88,98,100,102,104,110..118,120..122,125)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mvdilhqvgv vaplddvyqa vaspegvagw wsvdttgkse vggrlavrfg ddpgfdleil
       61 eldpagrvrw rvtdgpaewi gtkigwrlde rgeftivqft hegwreptel mhqcstkwat
      121 fllslkafve tgrgrpapdd vqigdgh
//
LOCUS       WP_357571921             310 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified
            Micromonospora].
ACCESSION   WP_357571921
VERSION     WP_357571921.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   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 310)
  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..310
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..310
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33879
     Region          21..310
                     /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 mtdqrggvvd escvltegpw thrfvgangt rfhvveagtg pmvlflhgfp ehwwawhqml
       61 pavadagfra vavdlrgyga sdkpprgydg ytlaadiagl iralgersat ivgsgvggmv
      121 gwtvasfhpp lvrrlvvlga phplrlragi fadprgqfaa stpalkfqlp ryehvltrdg
      181 aaaiaeilrr wggsrwvagp dfeayaercr eamcipqaaf calegyrwaf rsllrlhgyr
      241 fvrlmqkpla tptlqlhgal dtaslprtal gsgryvvapy ewrlldgvgh fphleapelv
      301 lgeilrwaks
//
LOCUS       WP_357571992             111 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357571992
VERSION     WP_357571992.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..111
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..111
                     /product="helix-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=11802
     Region          15..81
                     /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 mastatgatg ggrnwtfltn hghvllaiar dptarlrdva aevgvteraa qaivadleae
       61 gylhrtrvgr rneytlnpag rfrhpaeadr qvgdllalfa etpttevape v
//
LOCUS       WP_357572026             431 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572026
VERSION     WP_357572026.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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 431)
  AUTHORS   ter Beek,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..431
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..431
                     /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=46517
     Region          29..348
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msdfdpgrrr flghlglagl galgassfls acassasgpt tsngsgavti qsnlsspqak
       61 aameklietf naqgkgtasl ntiasetfrt qlptyltsan ppdlytwyag svandyaskd
      121 llldvsdvwk slgdypqslr tlstdasgkq vfvpmnnyww gffyrksnfa kwgvqepktw
      181 teflalcetl kskgvppigi glgdtpwvas awfdylniri ngapfhrell agkqrfddpk
      241 vkavftrwre alpyfdpkgk aypfqeatta llagktgmfl igtffadaap kdalgdldff
      301 rfpiidpavp laeeaptdgf fasaktanpt gtrallsyls gveaqeayvk assgivlpan
      361 pkakasdspl vvkgkamlde akeltqffnr dssdalqpta dtaltkfidk pdqidailre
      421 wqagaekvfk g
//
LOCUS       WP_357572031             301 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572031
VERSION     WP_357572031.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  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 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   3  (residues 1 to 301)
  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..301
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..301
                     /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=31770
     Region          1..295
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mqlnalqvfr avaehgslta aarslrytqs avsrqiaale aetgsplldr lprgvalteq
       61 grcllghaea vldrldtarr dlaalrdlsa grlrvgafpt avaalvpral asfksahpev
      121 tlslvegltp gllerlvhgd advavvsaaa dqpldadqfd lhhlvdetll vavprthrla
      181 drrtirlrdl adesfiagsa taeetllrat lpagfrprid ivaaewtgkl gcvaaglgva
      241 lvpalavraa psdltllrlh pddasvrrif aatvagrsrp pavrrflthl draaglsead
      301 g
//
LOCUS       WP_357572133             316 aa            linear   BCT 28-DEC-2024
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572133
VERSION     WP_357572133.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 316)
  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..316
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..316
                     /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=32944
     Region          33..>230
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mhtflvlats vvvlagtsgt paraadaqpd tyvvsrepgv lpegiavtra gtmyvtslat
       61 gavyrgdvrh qrlrpflpag sdgrahaagv hvdragrlfv agydtatlfv ydpdgrllak
      121 rsavtgaaln dlvitdhaay vtdsaggtiw ratldgervg plepwlrpsd fptapgflng
      181 ivagaddrva lvadqgtgap gterlwridl adatasevav sggqlgadgl llegnrlygv
      241 vnfpdpadgy rfavnlavld gdlraarvvr qsrtagleqs pttlardrdr llwvnsqlna
      301 tapappftvt evpglg
//
LOCUS       WP_357572180             257 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572180
VERSION     WP_357572180.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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..257
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..257
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26906
     Region          5..251
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mgefvrlett dgigtirler ppmnalntqv qeelraaaaa atadpevrav ivyggekvfa
       61 agadikqmae msyvdmadra vnlssalgai aripkpvvaa itgyalgggc elalacdwrv
      121 vaedaklgqp eiklgiipga ggtqrlarli gparakdlim sgrmvdaqea lrigladrva
      181 paaevydtav alvtpylngp aqalraakla vdggldmdln sglawesqlf aalfatddrr
      241 egmaafvekr kpdftgr
//
LOCUS       WP_357572160             814 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572160
VERSION     WP_357572160.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 814)
  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 814)
  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 814)
  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 814)
  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..814
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..814
                     /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=90291
     Region          8..>638
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 msrqalydgw tlraasgaqv padiagravp atvpgcvhtd lldaglipdp ylddnelava
       61 wigrtdwhyr tsfrrptgdh drvdlvcagl dtvatltvng vevgrtanmh rgyrfdvral
      121 lrdgdndlsv afdsayryae aqrerlgdrp naypepfhfi rkmacnfgwd wgptlvtagi
      181 wqdislhaws tarlatvrpl vtmdgrdgrv elhvdierva dvpltvravv agahaetvvp
      241 agqrtavlil avrepalwwp rgygeqalhp ievtlhapdg dtldtwshri gfrsvrldtt
      301 pddhgtpftl svndvpvfvr gvnwipddaf ptritrdrla erfdqaaean vnllrvwggg
      361 ryesadfydl aderglliqq dflfacaayp eeepfaseva aeaaeqvtrl tphpslvlwt
      421 gnneniwawh dwdwqsalag rtwgrgyyld vlprivgnld ptrpywpgsp wsgteaihpn
      481 dpahgtthiw dvwntddytk yreyvprfva efgyqappay atlrralsde plahdspgma
      541 hhqkaangda klqrgldahl papadfddwh yltqlnqara iqlgvehfrs hrgicagtiv
      601 wqlndcwpvt swsavdgdgr rkplwyalrh ayadrlltvq prdgglalva vndggttwra
      661 sasvtrltld geprakisvd ldvpayssvv lalptdlvrs ddarrellla eagetaeral
      721 wffaedreve wpvaaweaav epfdggqrvr vtagtvlrdl tlfpdrldas atvdsglitl
      781 lpgesvtftv radlvladaa lttrpvlrcv ndig
//
LOCUS       WP_357572199             157 aa            linear   BCT 28-DEC-2024
DEFINITION  dTDP-glucose 4,6-dehydratase, partial [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572199
VERSION     WP_357572199.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Beis,K., Allard,S.T., Hegeman,A.D., Murshudov,G., Philp,D. and
            Naismith,J.H.
  TITLE     The structure of NADH in the enzyme dTDP-d-glucose dehydratase
            (RmlB)
  JOURNAL   J Am Chem Soc 125 (39), 11872-11878 (2003)
   PUBMED   14505409
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Allard,S.T., Beis,K., Giraud,M.F., Hegeman,A.D., Gross,J.W.,
            Wilmouth,R.C., Whitfield,C., Graninger,M., Messner,P., Allen,A.G.,
            Maskell,D.J. and Naismith,J.H.
  TITLE     Toward a structural understanding of the dehydratase mechanism
  JOURNAL   Structure 10 (1), 81-92 (2002)
   PUBMED   11796113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         <1..157
                     /product="dTDP-glucose 4,6-dehydratase"
                     /EC_number="4.2.1.46"
                     /GO_function="GO:0008460 - dTDP-glucose 4,6-dehydratase
                     activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
     Region          <1..152
                     /region_name="RfbB"
                     /note="dTDP-D-glucose 4,6-dehydratase [Cell
                     wall/membrane/envelope biogenesis]; COG1088"
                     /db_xref="CDD:440705"
ORIGIN      
        1 mdvvvtrcsn nygpyqfpek viplfvtnll dgatvplygd ggnirdwlhv hdhcrgialv
       61 qqkgragevy nigggteltn keltgrllda cdtgwdrvvp vtdrkghdrr yslditkihq
      121 elgytpsitl dqgladtvtw yrdnrtwwep lkttpta
//
LOCUS       WP_357572238             266 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Micromonospora].
ACCESSION   WP_357572238
VERSION     WP_357572238.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 266)
  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 266)
  AUTHORS   Rosinski,J.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 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..266
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29864
     Region          1..>55
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          82..259
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgnvtdyvle elrlfrtglg lsqddfgrgi gysgshvssv etggraptke ymraidthhp
       61 tagrfqrmle rlarldaepa wlrewiefer eattlrwfel ayvpgllqte ryaratlagg
      121 rfdaedvdri vasrlerqai lqrprppqli avldeavlrr pvldqpglmv eqcehlvqla
      181 taehiqvhvv pvdagmylgl agqfiiaemp dgervahadn qltaqfvdap tdvaklaktw
      241 eivrnealpr rqstelikev akswtc
//
LOCUS       WP_357572261             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572261
VERSION     WP_357572261.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,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 265)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..265
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28571
     Region          15..257
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msnspttaqa eqsaihvhgl eksfkdlkvl rgvdidvarg sifallgsng agkttvvkil
       61 stllradagt arvngfdvaa qaaevresis ltgqfaavde ilsgrenlvl vaklrhlkdp
      121 raiaddllrr fslteagsrr vatysggmrr rldiamslig nppvifldep ttgldpeari
      181 evwqavmdla kggttvlltt qyldeaehla driailhegr iivngtldel kqllppakie
      241 yvekqpsled vfltlvgart nkeqs
//
LOCUS       WP_357572285             356 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572285
VERSION     WP_357572285.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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..356
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..356
                     /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=38536
     Region          38..327
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtadpsavaa ahqvlahlgv tvadlqahps araalptvae ylprvlaaag pgarrtygty
       61 wermaatwpd rpldgvaasd iealkqvmia savsrrnsrn grhagehvva aarafytrai
      121 adglidasas pahrvakprr lpstrraltp heleeiniea rtggndvild alvlrlhtet
      181 acrrggalal rlvdldting lvrltekgat irwqpitldl aehlhehara rgavlltdal
      241 lrtragqpit srrydhlwkr lgerlpwvav hgvsthwlrh ttltwverhf gygiarayag
      301 htdspgsstt tyikadlhdv analsamtgq phplarladh tdrwsqasga vsptte
//
LOCUS       WP_357572300             464 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572300
VERSION     WP_357572300.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=49156
     Region          6..461
                     /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 mtdqpeefdl lvvgggkagk tlsmdvarsg qrvamvergm iggscinvac iptkalvtsa
       61 raarllrdas algltvdggr vdvdllrahk qdvvegmvaa nrqqfldsgl hlvigearfv
      121 gprtvrvsla dggerllrgd dvvintgtrp hlpsvpgmae agvltsdell hldrlparlv
      181 vlgggtvgve faqmfasfgs avtlieggpr llpredpdms davlrvfldd gidvrvgiav
      241 arvdrdvdgr lrvtlddgsl vtgddvlvaa grepvtdglg ldvagvrlne rgfvlvdeyl
      301 rtsaertwta gdvagspqft hvslddyrii ranlaggers tadrvipytv fttpelarvg
      361 lteteasrag ydiqvahlpv aaiprartlr qtqgmwkavi dtstdrilga allgaeagev
      421 itsvqlamla gmpwtalrda iithptmteg lnllfaslqs rpvr
//
LOCUS       WP_357572309             512 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572309
VERSION     WP_357572309.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=55129
     Region          32..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 mtvptypvet taprpapaaa rahllqdgsv eqyrrtiaeg vdrvarrvat vdrpltgitp
       61 aelaplvdrv nldrplgdas aaldeledvy lrdavwfhhp rylahlncpv aipallgeav
      121 ltavnssldt wdqsagatli errlidwtae riglgptadg vftsggsqsn lqalllaree
      181 acadaigpaa raellprlrv ltsaaghfsv qksakllgla pdaviavptd arrrirpaav
      241 reeiarcrqa glvvmavvat agttdfgsid plpelaeira atgvwlhvda aygcgllvsp
      301 trrhlldgie radsvtvdfh ksffqpvsss allvrdrqal rhatyhadyl nparmvqqri
      361 pnqvdkslqt trrfdalklw ltlrvmgpda lgalfdevid raadawqlvs edprfevvtr
      421 sdlstvvfry lptgagrgla daanlharea laasglavva gtrvdgrhfl kftllnpatt
      481 vddvgyvldl iathagryvh dhvaaeltch vg
//
LOCUS       WP_357572311             613 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: IucA/IucC family protein [unclassified
            Micromonospora].
ACCESSION   WP_357572311
VERSION     WP_357572311.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=67924
     Region          24..608
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtatavpaqt aaaydsigdp vghltpqrwa ranrllvrka laeftherll tpqpvpgpdd
       61 rqwyevrsdd gtvtyrfaar vlalahwqid adsitrhrdd ttlppdavdl ivelrgtlgl
      121 sarvlpvyle eitstlagta yklsqaapsa aeladadfqt ietsmteghp cfvanngrlg
      181 fgvdeyhrya peaaapvrle wlaahrdhst fssaadldyd tlieseldae trarfaatmt
      241 dlgldladyh lipahpwqww nklavtfage laarrlvhlg pgpdvylaqq sirtffnvta
      301 phrhyvktal svlnmgfmrg lsaaymaatp aindwlaeli asdevltgtg ltvireraav
      361 gyrhrqyeaa tdrtspyrkm laalwrespv pdlapgqrls tmaallhvdd eggslaaali
      421 arsglapevw lrryldaylt pllhsfyahd lafmphgenv ilvldehdtv qrvifkdiae
      481 eiavmsdeve lpaeverirv dvpddtkllt iftdvvdcfl rhlnavlvea gvlaeddfwr
      541 tvatcaadyf drvphlaerv rhydlfapef tlsclnrlql rdnqqmidls dpsaalqfvg
      601 tlvnplaaha ptr
//
LOCUS       WP_357572318             336 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572318
VERSION     WP_357572318.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..336
                     /product="phosphotransferase 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=36964
     Region          14..280
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtgvsptqrl ltgddvaylv rasfgphtrv rdagplaggg yatvwwarld ddrrvvlkla
       61 ppagtpllry erglcaaear yfrlvaehap qvpvppvlwh gtdppygewl vtallpgrsl
      121 selakadvav ddarydlgva laalhrvtgd rfgydgdrag aatwrvafta mldalladat
      181 dwhvrlpvtp drlhtlvgrh advldevrrp allhfdcwdg nvlaapdaqg rlrlcglvdg
      241 erflygdpll dlvspllfrr vedepehpll rgyrdaadtp lvldasarrr lglyrlhlyl
      301 lmtvempsrg mtpsshpqrh arlatlldae lralta
//
LOCUS       WP_357572348             327 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FAD binding domain-containing protein [unclassified
            Micromonospora].
ACCESSION   WP_357572348
VERSION     WP_357572348.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..327
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..327
                     /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=34955
     Region          1..326
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mrafryhrpv dvadavavlg aephaaylgg gtnlvdlmkl gvqrpdvlvd vtglpldtve
       61 elpdgglrig atvrnsdlaa hpvvrrdypv larallaaas gqlrnmattg gnllqrtrcv
      121 yfqdtgkacn krepgsgcaa lhgqnrdlav ldwseqcvat hpsdlavalt aldavvqvhe
      181 tdgprdlpit alyrapgthp erettlarga litavrlppl paarrstylk vrdrasfafa
      241 agsvaavldl dgdvvrdvrl aygavahrpw rayraeeelr grqfspelag raadaelaea
      301 rplrhngfkv pltraitvra lselaas
//
LOCUS       WP_357572437             469 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572437
VERSION     WP_357572437.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 469)
  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..469
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..469
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=51536
     Region          19..>84
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvpasfwehe pvrqalaerh lgrvirayrc hpyhgrvalp qsvvsgwlgi tqaqlsrven
       61 gpplvhldrl ahwaqllrvp pgslwfrlpd ehcwtvprsv gvktnsahcd dqvvergera
      121 akavnveqap sqgggatdrr rfnvlaalag laagghtyll pgppaevpgn igmeqvrlas
      181 slvddlrrad aavgadllcd vamqahtrls awaarasysr evgdalqsal adlsieaawl
      241 aidadrrpea rpylheaitr sriaddpqve vralthlsll iredqpgesl hcaeaalris
      301 agwttprlst llhlrrahay avfrdasgfs remtkarrel drgaheddqs fvhfvneqel
      361 ngieglsyla ldrperavqs lraitanpsp shrrnqvyya vrlseaayqq gdvneaaria
      421 ldvlpavrqi nskrvsqhla qvrghlaapr qattttrqfv daydqavsa
//
LOCUS       WP_357572448            1127 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Micromonospora].
ACCESSION   WP_357572448
VERSION     WP_357572448.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1127
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..1127
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=120885
     Region          <2..885
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mdvrrgdaii grdhpaallr aeldraatsh gglalvtgep gigkttlvts vawearqrga
       61 lvlgaacwds dsapgywpwv qvlrglrrsa ddwavarqaa epalaallge sgtskepadr
      121 ltswagvdsv pdvgdqeafa lydgvtaalv avsqhrpvvv ilddlhwadp aslrllsfaa
      181 qhtwferlll igtyrdaeve sgehplrpll mplvakatti tltglsrdev aalmtrtagr
      241 kpaaglvdev hrrtggnpff ieqtarlwha deaadtiapg vreavrrrla qlppavveal
      301 tvaavlgref hrqvlaacvt apvaqvdrll draltarlav srgggrfafa hdlvretlyd
      361 gltdddrqar hgtvvravdd lreltdllip adlarhayla gpaldrarva tllvaagrda
      421 farlatdeaa vhyrraleiv edrsqrvril vefgeaqyhh adreeaerll seagtlartl
      481 ddpallarva livnrarqvv tadsveaael vreayrrlig epdpdapvga liadlitate
      541 siarrgrdde altfslwarh dstwglgtaa aravltaeir dvarrtgdre telwatslrw
      601 vallelgdpr fndefttfis adrrgdlarh dmaatvdsai iaafrgdfae adksfaditd
      661 lshaefgfmg hhlrwsrlll qgrhaeadtl ldglapldyp yrellraita aergddettv
      721 rltagieatt iryprpvspl wlrlqaqaaa asgdprrcea araalaphrg ewtvglfgcd
      781 isgpvdhwla lvdaaqqrwd daiagftaac dsadrlgsrp wsliaraglv nalaarghpa
      841 daatlaalra ttareatalg mtqvldrlga tvdpaaptta tarqavtpgp avgptmaagp
      901 gqlsgpgqln glgqlaapgq sggpanagpg qasasgqaaa depagggyef rrdgpvwqlg
      961 yagsvvhlpd akglrdlhll lsrpgtdvpa velldpaagp eliaarrmga dpvlddeaka
     1021 ryrqhlarld eeidraaard ddrkvaaldn ergalldelr vaaglagrsr rlgdeaerar
     1081 ktvtarirdt lrklddrhpa lashlresvs tgnacrylpp eplpwrl
//
LOCUS       WP_357572614             218 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Micromonospora].
ACCESSION   WP_357572614
VERSION     WP_357572614.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 218)
  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 218)
  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 218)
  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 218)
  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..218
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..218
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22871
     Region          2..201
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlfdmdgtlv dseklwdval qelareygge lsedarrsii gtamaesmri lhddlgqper
       61 dpeisaawin arilelfrtg lpwrpgafel lravrsagip talvtsspra lveialdtlg
      121 rdtfdtvvag devvaakphp epyltaarql gvpiercvai edsptgvasa lasgaavlav
      181 paevalarta gvhqvesltg vdlgllaall tdraaatg
//
LOCUS       WP_357572653             173 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572653
VERSION     WP_357572653.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 173)
  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 173)
  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 173)
  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 173)
  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..173
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..173
                     /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=19047
     Region          12..172
                     /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 mrylrtggpa airrprptds defvaaarrs rdlhhpwlva psspqeydny lrrirrrdga
       61 gylicdrasg aiagyvnisg ivlgalrggy lgyaafqpys gtghasagva lvidhafhtv
      121 glhrleaniq pgnepsrrva rklgfrlegf spdylfvdga wrdherwait aph
//
LOCUS       WP_357572651             758 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572651
VERSION     WP_357572651.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 758)
  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 758)
  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 758)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   5  (residues 1 to 758)
  AUTHORS   Kannan,N., Taylor,S.S., Zhai,Y., Venter,J.C. and Manning,G.
  TITLE     Structural and functional diversity of the microbial kinome
  JOURNAL   PLoS Biol 5 (3), e17 (2007)
   PUBMED   17355172
REFERENCE   6  (residues 1 to 758)
  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 15505478
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..758
                     /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:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=81934
     Region          <72..123
                     /region_name="PknG_rubred"
                     /note="Protein kinase G rubredoxin domain; pfam16919"
                     /db_xref="CDD:435653"
     Region          124..373
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(124,148..149,177,182,187..190,207)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(131..132,134..137,139,153,155,185,206..209,213,215,
                     259,261,263..264,266,275..276,279,296..299)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(131..132,134..137,139,153,155,185,206..209,213,261,
                     263..264,266,275..276)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(135,213,215,259,261,263,279,296..299)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(275..283,292..299)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          418..756
                     /region_name="PknG_TPR"
                     /note="Protein kinase G tetratricopeptide repeat;
                     pfam16918"
                     /db_xref="CDD:435652"
     Region          520..543
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          583..610
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 mtpcnwpgct gtvdetgfcd vcglaplppd takptaapsr stgrdiwtva slvslpvltf
       61 spdgattqpl rvpeefrfcp kghpvgrsrg grpgrdsgfc pycptptpfn frpglqpgdl
      121 vadryevvrc varggqgwvy lahdthndhv dvalkgvlha adeaslraav eerrflnald
      181 hpnivrsidf athedpvagp tgyivmdyld gmslrrlqna akdlrqpdvs lpidhilayg
      241 heilaaldyl hrrgllytdm kpdnvmrtad rikvidlggv rkadsgsegi vhsvdfsvsr
      301 aeyqnrgpte rsdlfalgrt ledlyrhrtp gpdtpgaapd algiesfnrl varairldwd
      361 rrfasatems eqllgvlrei lagqpdrrqp epislfqpsa rlldaglglv lplrtwidag
      421 dstvlddgrp asvdvalgla vprpdpddpa vdvlrtvdas daqallgela mveqtsveie
      481 lsrcrahlal adpdsaavsl asaetligtr adadwriawh rgllalaadr iddagqrfda
      541 vysdipgeva pklalgycae rrgdhvsaar yyaavwqrdp fqasaafgla rlrlaatdra
      601 gavavldevp alsrhhdaar vaavrvlssr lpggppaage lnqavhrlaa ldvggeerdr
      661 litairemal elarsgdaak ltggpvlgep pterairtll ersyralgqq aqhaafpdlv
      721 avranrirra grtddagrra ahdllvdran avrprtrw
//
LOCUS       WP_357572678             275 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572678
VERSION     WP_357572678.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  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 275)
  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 275)
  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 275)
  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 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   6  (residues 1 to 275)
  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 275)
  AUTHORS   Rosinski,J.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..275
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..275
                     /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=30742
     Region          1..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          108..264
                     /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(109,111,113,122..124,126..127,132,141,148,150,152,
                     154,162,164..165,168,171,177,179..180,209..210,212,214,
                     225,227,229,231,237..241,248..251,253..255,258)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mddafralad psrrrlldrl ndrngqtlre lcdglatsrq avskhlavle aahlvtsirr
       61 grekvhylna apinaiadrw lsrydreraa aladlstale rqpmespafv yttyvrttpq
      121 rlwaaltepa ftrrywggva lasdwqvgsp vlwqdtpdge prdlgqrvlv aepyrrlsys
      181 whgfqpehae hfgwsaeela arlgerrstv tfeiephsgs tvrltvihdg fspdsemhra
      241 isgqldgsgg wpellaslkt lletgepmpd psqah
//
LOCUS       WP_357572732             225 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357572732
VERSION     WP_357572732.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  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..225
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..225
                     /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=23677
     Region          21..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtparrttpa rrrgapaaaa evrealltvg crllssdgpa alsarrlaae vgtstmaiyt
       61 hfggvpdlve aivqmgldrl aerlaavrpt ddpvtdlarl arvyrdsala dphlyavmlg
      121 gvaqahfglk prdleldslt lgaadvhvrr sieagrfrag phwdltvrvw ammhgwvmle
      181 iagygigasv ddyllhvlvg agdsladatr svrrsggvgp tagps
//
LOCUS       WP_357572798             167 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Micromonospora].
ACCESSION   WP_357572798
VERSION     WP_357572798.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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..167
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..167
                     /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=18453
     Region          32..158
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtttpdtvds hierwlpvvp hldadvegav trmikltrhl rsvkervlad fdlsvheydt
       61 lqalagrrgr aapsdlatdl amapasitar vdallrrgfv rripstvdrr rvdveltdag
      121 raawrgamei qgaeehrllg alttterrhl adllrrvllv aeqpaad
//
LOCUS       WP_357572801             516 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572801
VERSION     WP_357572801.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 516)
  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 516)
  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 516)
  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..516
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..516
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54459
     Region          33..309
                     /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 msesainidr phrpaptspp gapepgaptr gpglvalats vvllllagry gyhrdelyfl
       61 lagrhldwgy vdqgplvpal arlldtiapd nlvilrtpsa llaggavllv aaiarelgag
      121 rgaqtcaavl aalsgivlas ghllstttvd llvwlaaawc avrllrtgds rwalgiglal
      181 gvgmlskllp allavgliag vliggprrll rdrwvlaaag iavllaapnl iwqaahgfpq
      241 ldvaasiadg dssysgrrda ltlqfviisp yavpiwiagl vallrrpawr ayravgwarl
      301 vvfgivliag gkgyydapll lvltaagavv tvgwasrgsv rlrrallalg vvpfllpniv
      361 lllpvlpaer lpgfvvdvny dagetigwpa fadsvatvhr glppeerpra viltsnygea
      421 galarygpvr elpraysghn smvdfgqppa sadvviavgw erpepltawf dectlagrvd
      481 qrvevdnden ggpihvcrgl rrpwaqiwdt evrhtg
//
LOCUS       WP_357572806             633 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572806
VERSION     WP_357572806.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..633
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..633
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67789
     Region          10..>107
                     /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          398..632
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtgltaelvv dgrtpqrpal apngrrlcyv laptsrtgdh ldtelwlvdt dgavashrat
       61 adtatesvpr wsadsttlff lsdravrgtp qlhalnlsdg tlttvtswrt gvidhlplad
      121 ptlvallaed eptgpdarra rdrddaivvg ereprarlrl ldlrtgritt pnvfgdrhvv
      181 elrqrpdggp lavltrasad ndhgprggql hlldpttetv enlgpvgvda qslawwpged
      241 gwhlghlalt ppglqagtav fdlavdsrvl rnrtaglpmc ptelcqtdaa plvvcadgln
      301 ttlarldptg lttlsqhpgr ldnltttpag aviavltgtr yeppnvhvgp ptgalrritn
      361 trpeldgval gtqqplayra adgldldgll vlpvgrtaaq gpfplitivh ggpydryadr
      421 cqlfwfpsaq wlaaagyavl lpnprggqgh ghgfaasvag rvgqqewtdi ltgidllvae
      481 giadpdrlgi agwshggfms awavgqtdrf raavvgagvv dwgmlaatge ngqfeaalgg
      541 stgwsgtgph phdavspisf ashirtpvli lhgaedtnvp lgqavylhra lrhfdvehef
      601 viypreghsi rerhhqidvl rrtrawfdrw lrp
//
LOCUS       WP_357572844             351 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357572844
VERSION     WP_357572844.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=37672
     Region          15..305
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrpaarggs rtsadrlarl lnlvpyllar pgieiaeaag dlgvterqlr edlellwvcg
       61 lpgygpgdli dmafdgdrvt itydagidrp lrltpdeala lvvalrmlae tpgvanreav
      121 eralakieda gdlvgapvav rlpgdtrrve alraaveggr alrityytaa rdettdrvid
      181 plrmlmvggr ayveawcrra eavrlfradr idaitelpep atvppqavph dltegvfrps
      241 pdlplitlri grserwitey ypcerveagd gdqwlvslrv tdlgwarrfv lglgpdavvv
      301 apaelaeqvr aaaaaalday avpapaaelr vpevdatsap agdpavagrt q
//
LOCUS       WP_357572863             328 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572863
VERSION     WP_357572863.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=36497
     Region          37..325
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mssqtkppet aaareaparr rrrvdrlpyl lllpalviig vlllwplgqv vvmsfyrlns
       61 vrqlrgdrew pwvglgnyad ilsdpffltv lrntvlfaaa nvlltmvlgt lvglllnrlg
      121 rkmatfvasc vmlawatpal tgtivwkwif ddtsglvtwl fnalpdglsd slfgrsdwtg
      181 ygwfnspllf failtlvvvw hsfpfiavsv laglksvpse lheaarvdga spwrvfwkit
      241 fpllrpvfgi livlstiwdf kvftqqfvla ggtqdrptfm laiysyaeaf spppkyglga
      301 avaviltlil lvvtgfyvrm vlrqedes
//
LOCUS       WP_357572891             294 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified
            Micromonospora].
ACCESSION   WP_357572891
VERSION     WP_357572891.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   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 294)
  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..294
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..294
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31417
     Region          13..294
                     /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 mgstshdvsa lapgahtflv dgvrqvyhva gtgpvcvahs ggpgiewayl rtpsleehft
       61 mvyvepvgtg asgrlddpad yrldtyvrfl davvqhlgap rvyllghshg gfvvqryala
      121 hpdrvaglal ydtspvtgae fwaeamtgla aypqrhpdrp eaaavpaafg qigaatddes
      181 latalraalp vyfadfwgrq defapfqaav rislapasaq dptpfdvren laeiavpvvv
      241 ivgaydficp prraeelhag lkdsrlvlle qsghfahieq paeftaavve lltr
//
LOCUS       WP_357572905             410 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YeiH family protein [unclassified Micromonospora].
ACCESSION   WP_357572905
VERSION     WP_357572905.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..410
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..410
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42476
     Region          63..393
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 mttdatragd atragdatre gdatgavdav gpapasgppt tvdpagptht ardgrfwawt
       61 alglvivlgl aaltryleqn vpgwaegtav gdigaaieyp vyaillgllg nvavtllgwr
      121 drivaafrte ffiktglvll gasinlavia saagpaiaqa illisgvfff twwlagkfgl
      181 edklrallas avsicgvsaa iaaagavrar reqlaytasl viifalpsif ilpwladvfg
      241 lsdavagawi ggnidttaav taagaiagee alqiasivkv tqnalmgvva valtayftlr
      301 verrpgaerp glrelwtrfp kfvlgfiaas viatwyldga gadgkatiai vndlrvwfli
      361 lafvsiglev rvaslreagw rpvavfasat vfnlalalgl asllfrnfsa
//
LOCUS       WP_357572912             176 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572912
VERSION     WP_357572912.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..176
                     /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=19088
     Region          35..160
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mhiatdgeav diitaadhwq sswyppsnpp agtphgstgv cvvagqvilv sddgkhwqfp
       61 ggrpeadedw sgtlarevse eacatvlgcr llgfsrgvcr rgseqglvlv ralwraevrl
      121 dawmpehemv errlvppegv wdavtiptgw epifrrilve adipvgqspr ggpmhp
//
LOCUS       WP_357572908             156 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572908
VERSION     WP_357572908.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 156)
  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 156)
  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 156)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..156
                     /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=17412
     Region          20..144
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mariehfnnp sapkpnsivv avtvfvqddq grvlliqrsd ndlwalpgga qdfgeyitet
       61 avretreetg veievaglvg vysnpnhvvq ysdgevrqqf sicfrgryls gdpttsdess
      121 svrwvaqdhl dhlsihpsmr lrvdhgfqws pepylc
//
LOCUS       WP_357572910             410 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357572910
VERSION     WP_357572910.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 410)
  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..410
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..410
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44571
     Region          1..81
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtsddlpigr rvarwrvrrs mtqqqladri crskswvdkv ergvraldry sviqelaevl
       61 rvnpevllsq rpqrtpigtv egvddiraal arydtsqase rtteeanrqv gyawltyqha
      121 dyaqlvrtlp glldavqgsr spellvqayr itssllvklg aadlgwlaad raraaagddp
      181 llsaaavvsi aqalraqnrd hlalaallpa anralppsth sgdqevsgtf vdqisrkpld
      241 hrgqtdrrdq avggtllvqa alaaagcgeh rragelidra agiaanlrgy ddphrtsfgp
      301 vavelarvll aaqrddaaea vrrhstvvrr egwrrlpaey rdaylldvar tylrlgdlrg
      361 aaralvdadh vapaevrcrp lvrtviaeia raqptpagva rlaavvgltr
//
LOCUS       WP_357572982             259 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572982
VERSION     WP_357572982.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..259
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27281
     Region          1..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 mnlaydrspg tgpdvvclpm fsmsraatat afgpafagad lretyldlpg hgdtpatcap
       61 tsqavldsvc awlddhvdap vllagasyga ylaagiarqr pdlvrglllv cpgvtiardt
      121 rtlpdeppld aptgwlddap aalrahldaa lgqrtpavaa tvlaamesgg pgdatflqkl
      181 qsgpdyalpd etaevifdgp vtvltgrqdr vvgyadqfra mhryprgtft vvdaaghylp
      241 yeqasvlrsh tqewlrrap
//
LOCUS       WP_357572998             154 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC048905].
ACCESSION   WP_357572998
VERSION     WP_357572998.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=16327
     Region          2..120
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 merpedlaaa iaaaagtlia vldssasghq vpptqlrvlt lissraetnv nglaelldvv
       61 pssasrlcdr leatgllrrv adprdrrevr lvptpaalal lgdlaerrrr avqsvldrmp
      121 grtqhdlwla lvafgraatq svpekqtdpa aqta
//
LOCUS       WP_357573051             321 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC048905].
ACCESSION   WP_357573051
VERSION     WP_357573051.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     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=35628
     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 mnpdrffalm lllesrdgat tqelasalgv slrtitrdln wlrdaglpvt ahrgrlggvt
       61 mlpgsgldlt rltpgehdhl sligldeklr aelntsaesr ralaklaatq srrvdellpl
      121 sdvvhvdsrp whqtrasgtn paaligavrr grqlrieyds prepcprdlv vdsygllaka
      181 giwylvadca rvprmyrler ittwqevdqp rrlrenqtla tvaaalidqw ehshaievsa
      241 tidptqiera qrifglrlvr dddeesatgh kvtirflnle dvrallpfgn avtvhgptea
      301 rahlrdlatn lahhyapspm s
//
LOCUS       WP_357573053             419 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC048905].
ACCESSION   WP_357573053
VERSION     WP_357573053.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC048905
  ORGANISM  Micromonospora sp. NPDC048905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Micromonospora sp. NPDC048905"
                     /db_xref="taxon:3155494"
     Protein         1..419
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44854
     Region          31..419
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mstsqrrpvr iqapagaaaa eavaaagvea yprivatlir vtgdwalaed caqealaval
       61 erwpgdgvpt npggwlmtva rnraldvlrr asverrklhd lalltptdpq pepevgqdvv
      121 ddrlrliftc chpalaldar valtlrtvcg vptadiarll lvsestmtrr ltrartriaq
      181 agipyrvpsg palterlpgv lavlyllftr gyvadgepaf adeavrlarl ldrlmpeqse
      241 vaallalflf qhsrrdarrd aagalltler qdrdrwdrag iaeglaaldr vrrdgpyawq
      301 ariaachata vsaddtdwpa iaraydalad irpspvialn ravahgyayg pavgldllda
      361 ahagggldgn plavavradl varqgdrira atlfreaaaa vssaaerhal lkraaelar
//
LOCUS       WP_357573166             160 aa            linear   BCT 28-DEC-2024
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Micromonospora
            sp. NPDC049114].
ACCESSION   WP_357573166
VERSION     WP_357573166.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 160)
  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..160
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..160
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17044
     Region          24..121
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mtaapvggps dptalggggv rgftvlfdan cpicraarrw lasraqlvpl efvpagstea
       61 rrrfpgldhd atlrdltvva dtgevyagdg awfarlwala dhrsaaerls rphllplarq
      121 vvatasaire rvrdpwaept depagyrdpd dratdaddcg
//
LOCUS       WP_357573146             816 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573146
VERSION     WP_357573146.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 816)
  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 816)
  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 816)
  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 816)
  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..816
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..816
                     /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=90116
     Region          8..>638
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 msrqalhdgw tlraapgaqv paeiagrsvp atvpgcvhtd lldagliadp ylddnelsla
       61 wigrtdwhyr ttfgapagdh drvdlvcagl dtvatisvng vevgrtenmh rgyrfdvssl
      121 lrdgdndlav afgsayryae aqrdrlgdrp naypepfqfv rkmacnfgwd wgptlvtagi
      181 wqdialhaws tarlagvrpl vtlgggdgrv dvhveverva dvpltvratv adahaevvvp
      241 agqrtavltl tvrepalwwp rgygeqsrhl levtlhapdg dtldgwsrri gfrsvrldtt
      301 pdehgtpfvl svndvpvfvr gvnwipddaf ptritrdrla grfdqaigan vnllrvwggg
      361 ryesedfyel adergllvqq dflfacaayp eeepfaseva aeaaeqvtrl tphpslvlwt
      421 gnneniwgwh dwdwqeplag rtwgrgyyld vlprivgeld ptrpywpgsp wsgtdavhpn
      481 dpahgtthiw dvwntddytk yreyvprfva efgyqappay atlrrsisde plahdspgma
      541 hhqkaangda klqrgldahl papadfddwh yltqlnqara iqlgvehfrs hrdvcagtiv
      601 wqlndcwpvt swsavdgdgr rkplwyalrh ayadrlltvq prdgglalva vnetaeawta
      661 patvtrttla gepraktsvd ldvpayssvv lslpaelarp desrrellva eagdaveral
      721 wffaedrdve wpaaawdatv epveggqrvr vtartvlrdl tlfpdrldal atvdsalvtl
      781 lpgesttftv sagasldgaa ltrrpvlrcv ndiers
//
LOCUS       WP_357573253             414 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573253
VERSION     WP_357573253.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 414)
  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..414
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=43925
     Region          164..411
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtfraalapl vagstwrrgv flllggvlal pygvlavtfa qlltdstipr plvyalllia
       61 aliavvplll dgsraleiaa vrallgvdlp dpapghrgdr esrlrsalwi athliigalv
      121 mialfsalpm alafiaqqfg vgaeltsqer fgpldgrdgg wltltgvall vglgyavagl
      181 galavsmapv llgpaqaeri aalearatrl aernrlarel hdsvghaltv atlqagaare
      241 vldsdpefvr raltaieeag rtamdeldhv lgllrenggd rpsvapqrtl adldrlvadt
      301 raagltvhaq rvgdparlpa ivsregyriv qegltnavry ghgpvtlrld lrpdalelel
      361 vntmsspdra dtgrsgrgld gmrervlllg grltvgpdgd rwlirarlpy edvr
//
LOCUS       WP_357573275             400 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573275
VERSION     WP_357573275.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 400)
  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 400)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..400
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43125
     Region          1..>34
                     /region_name="ThiF"
                     /note="ThiF family; pfam00899"
                     /db_xref="CDD:459987"
     Region          26..399
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrvllvgagg vgsaavaiaa rrsffetivv adhdpdraar avaghgdrfv aaqvdassad
       61 avtalcrehr ithvlnavdp rfvmpifdga faagadyldm amslsrphps qphartgvkl
      121 gdeqfaaapa weeagrlalg gigiepglsd ifaryaadel fseideigvr dganltvdgy
      181 dfapsfsiwt tieeclnppv vweadrgwyt tepfsepevf dfpegigpve cvnveheevl
      241 liprwvkarr vtfkyglgde fidvlrtlhk lgldgvspvr vrgadvsprd vvaaclpdpa
      301 tlgermrgkt cagtwvrglg pdgkprevyl yhvvdnewsm reyghqavvw qtavnpvval
      361 ellatgawtg vgvlgpealp pvpfldllta ygspwgmres
//
LOCUS       WP_357573280             256 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573280
VERSION     WP_357573280.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 256)
  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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..256
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28038
     Region          4..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(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"
     Region          73..250
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manealrvam aeagetvesl aekvgvdpkt aarwlaagri phprtriava evlrrdaadl
       61 wpepfrrrdl pwfrpwaele qdatsirsyq pllvpgllqt egyaravlnt gglvpvsevd
      121 qivasridrq avlcrdappq lvavidevvl rrpvgdgsvm agqlrhlasa aewehgqvrv
      181 ipaespwhtg lagpfvlgrl pdgtelayld nqlrgqivtd pldvaslgrr wesvagealp
      241 qrrsielire vattwt
//
LOCUS       WP_357573403             384 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573403
VERSION     WP_357573403.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 384)
  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..384
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=40837
     Region          162..383
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 midlrmvpgs wrrwpvtvrd lplalllala svvpplrnhg tqlgdlpgrp fdaltvavia
       61 leclplavrr rwpalclalv svgfvidqlr ayhtvagsal aiallsagah vqrhrratmv
      121 lgsaayvala valdrqgste gvlgfatfyl llvlawgvga wlrearavea errrhvaata
      181 raaertrias elhdivthhv tamvvqaeaa ryltaaperl dttltaitdt grraitdlrh
      241 lldllnpdhs tdprtpavge lhalvaqtrq agqpvdfted gspaettgga evvayrvvqe
      301 altnalkyar gsrttvhvqh gemettvqvs tegsgsyseg pggsgrglag lrervdvlgg
      361 dfsagrqadg sfvvraript gsps
//
LOCUS       WP_357573445             172 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF421 domain-containing protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573445
VERSION     WP_357573445.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..172
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..172
                     /product="DUF421 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18960
     Region          9..164
                     /region_name="YcaP"
                     /note="Uncharacterized membrane protein YcaP, DUF421
                     family [Function unknown]; COG2323"
                     /db_xref="CDD:441897"
ORIGIN      
        1 madwqevfvp dtplleivvr gsvmylalfi llrvilkres gttgvtdllv ivlladaaqn
       61 gmsggyhsvt dgvllvgvii gwsyllnava yrwqaaarli rpgslvlvrd gevvranmrr
      121 elitneelht llrqqgvtdl shvrevrmep dgrfsvttrt pgrprddldg rg
//
LOCUS       WP_357573477             109 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573477
VERSION     WP_357573477.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..109
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..109
                     /product="helix-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=11554
     Region          4..79
                     /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 mtsaataggg rnwtfltnhg hvllaiardp tarlrdvaae vgvteraaqa ivadleaggy
       61 lhrtrvgrrn eytlnpaghf rhpaeadrqv gdllalfaet paddvssrp
//
LOCUS       WP_357573526             578 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573526
VERSION     WP_357573526.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 578)
  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..578
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..578
                     /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=63386
     Region          <153..321
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 msderddhqt pageqpdger aprrprstdp lelgftprkp vpwlapflli stgirtllai
       61 lfgayldkre lqnafgdgif rqagpdgglw ldyvadlgdg fhatysvayl laqpeltvdg
      121 hrlprgqtlv mggdqvypsa ayaeyenrck gpyqaalpat ppegptlfav pgnhdwydgl
      181 taflrlfvrs rdrnfagwrt gqsrsyfave lpagwwllgv ddqsgsyldd pqlayfdeva
      241 rrltpeskvi iaapsptwvk aadiptayds idyfirtiid ptgaqvrlll sgdlhhyary
      301 agpdrqlitc ggggaylypt hklpkrievp prdtltrras rtepydlvar ypdaarsrry
      361 gwgifarlpf rnpgfatllg tlhtllmlam agatanwads tnqrlfsvpl vlmvlvtvva
      421 avlfakppsa sgkrhvrhwi lgvshgvaqv alaaggtwvw lalpfydwpw plpavaaavl
      481 ygpviglvas qlvaayllva safgvnvnel fagqgiedsk sflrlridpd gtltvyplgv
      541 drvsrdwqvn pdqsptaswl tprapltphl teppivls
//
LOCUS       WP_357573542             709 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573542
VERSION     WP_357573542.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..709
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..709
                     /product="PhoX family protein"
                     /calculated_mol_wt=75490
     Region          47..703
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msdrprllpl ltgnrhgtrd amtclyrcgn acdhpvpnts dnayfgdvvn aevsrrgvvr
       61 agavgalvlg fggaaagala gaapaaaaap atpdvpenfg fgrpttgvgs galtfkpipp
      121 nkldtlvvpn gydhavvikw gdavlpgape fnlhhqtaaa qskqfgynnd fvgvlpldrq
      181 grrallvvnh eytnedlmfp gfpgldglsv eqlrtamaah gmsvvelerv agtgqwkpvd
      241 ngrrpynrrv talgttfdlt gpaagsawlk taadprgrtv vgtlnncsgg vtpwgtvlsg
      301 eenfnqyfvg adaapadlkp kldrygitta srypsgsrkw eraderfdla khpneahrfg
      361 wiveidpfdp esrprkhtam grfkheganv ivakdghvva ymgdderfdy lykfvsdkkf
      421 lkgnswaark hnltllesgt lyvaqldqts ageidgsgnv padgafngrg rwiklvsgnr
      481 sfvdgmtaad vltftrlagd kvgatkmdrp edvepslltg kvyvaltnnt drgkagkata
      541 deanprnank hgqilelved rndntsetfa wslpivcgdp tdpstffsgy dktkvspisc
      601 pdnvafdatg nlwistdgna lgsndglfat avegpekghl kqfltvplga etcgpfitgd
      661 nrsvfvavqh pgeitgasve npasnwpdgd yakpgvvvtw rldggpvgs
//
LOCUS       WP_357573557             775 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573557
VERSION     WP_357573557.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 775)
  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 775)
  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 775)
  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..775
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..775
                     /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=81609
     Region          8..756
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpapdldthp etdlvaerah latsraalrr mreraealfs tgdqvagdpy aaemlgrtla
       61 rrvaeladdp ttplffgrld fggttsddkt atgpttsatt tnadttnsaa ttsagtatss
      121 ttttsageas ggsgsggstg rsgsggsggs grgssgregs gsgsgdhygr ryhvgrrhvt
      181 dehgeplvld wrapvsrsfy rasardpqgv avrrrfgfsn gvltsfeder ldrgeelgta
      241 sriltseier prvgpmrdiv atiqpeqdel vradladsic vqgapgtgkt avglhraayl
      301 lylhrerlrr agvlivgpnr aflsyiaavl palgeveveq atveelisrv pvraveapav
      361 aalkhdarma svlrravqtr igtptdsitv sdgsfrwrig leplhrivee trreglpygt
      421 grervrarvv sllqrqaear raespsdawl rrmsrcrpvv dfldavwpal tpeglvhgll
      481 sdparlataa dgllsdaeqa qlvwakpart pkaarwtaad avlvdeaagl lerpsgfghv
      541 vvdeaqdlsp mqcraiarrs ehgsvtllgd laqgtapwaa tdwreslthl gkpdavvvpl
      601 tvgfrvpaav vafanlllpa lavdvppaes lrhdggldvr tvadltaatv aevrtalahd
      661 gsvgviaadd avdelraala aagvatatad dvtaaervtv vpatlvkgle ydhvvvvepa
      721 aivaaeprgl hrlyvvltra vsrlsvlhse plpaplltap pqtpaqaapl epapl
//
LOCUS       WP_357573612             513 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573612
VERSION     WP_357573612.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 513)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..513
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56311
     Region          86..485
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvstdp rqqppaatst applappngr hhqsaavpqp mptatpppev aprprmdfqv
       61 vrelrrelte rltlwqrgre ftvdeedter arlavtvvae yadavrragt pmaageerll
      121 ldqvtaelvg lgrlqtllvd dtieevhilg cdvvritrhg ggvdwaepia dsdaelveil
      181 qaaarragat erslstvkpt ldlqlpdgsr laavflvshr pyavirkhnt ldvslddvag
      241 argdldemid pllrdflraa mraglnimva glagagktti iralmneipp depyvllees
      301 rellparrre rhravmsfea reghgergfd grpagevtia dliplslrmg vlriivgevr
      361 sreivpmlqa mttsrgsmct ihartaagvg erivelalah gremtvdqar rmagnaldli
      421 vyvtvedesa iggrkhrfvs hveevigage agqittttvf gpgpdgravp rhlpervrdq
      481 llrvgydsrl ltrwieagtg awrrprqtrl arr
//
LOCUS       WP_357573675             322 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573675
VERSION     WP_357573675.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 322)
  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..322
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..322
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35671
     Region          156..218
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(157,161,198)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(160,197)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(167..168,191,194,198..199)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mtgrpekpld psagpvahfa fqlrrlrqea ggpsyrtmas rtfysisals iaagglrfps
       61 wkcveayira cgvadegiaq wkrrwtavrq qlqhdkraar eeakarakak srhlsleavq
      121 mhttmdsras lpvldvryvd adpaevtsie eflialdqmr vekglslrki adrsrlitlp
      181 gtevsggltr sqlhemlngr aplrprhvla yllacgvpqe raalwlsrlh rlrdqerrar
      241 aaltalkgqp nvarpvtpth ntrvftsgrp vtssgviqip ppgqppaaal rpatdrgkhr
      301 qrkpwtslln wlngpkdnev ia
//
LOCUS       WP_357573684             488 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC049114].
ACCESSION   WP_357573684
VERSION     WP_357573684.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 488)
  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 488)
  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 488)
  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 488)
  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 488)
  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..488
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..488
                     /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=50379
     Region          5..240
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
     Region          <211..>326
                     /region_name="PRK06975"
                     /note="bifunctional uroporphyrinogen-III
                     synthetase/uroporphyrin-III C-methyltransferase; Reviewed"
                     /db_xref="CDD:235899"
ORIGIN      
        1 mtltlryaah sdrglirdgn qdsvyagprl lavadgmggm aagdvasniv igamaplded
       61 vpgdalvdal rsavgtanqq lrdtvdanpq legmgttlta tlfsgsklgm vhigdsrayl
      121 lrngefaqit kddtyvqmlv degrisaeea sshpqrsllt raldgrdidp eysvrqvlpg
      181 drylicsdgl sgvvsaetig etlreytdpq qcverlvqla lrgggpdnit viiadatdhd
      241 iveatpivgg aaardrgmat saddstpaar asalsaprpa apeepnasdd eperpkrrpv
      301 rtaamalall vivggaafgg wtytqrqyyv gatdegqvav frgiqgqiag mdlstvhrts
      361 gtrlddltva aqdtvkvgir aknepdaerq laeltsdtpt npnlkpicps dtaavtgtpt
      421 ptppptppat sptpntspsp gasvngvvsa sptnaatagg tdpttapdat psdsatpald
      481 pagcrspe
//
LOCUS       WP_357573702             259 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573702
VERSION     WP_357573702.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..259
                     /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=27217
     Region          2..208
                     /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 mrvlvtgagg rlgshvlarl sddgmsvras srrprtgsdv ewvvadlasg agvaeavtgv
       61 davlhlassp rgrtyqvdvl gtrrlvvaag aagvghlvhi sivgvdhvpf pyyrhklaae
      121 qvvaagpvpw svlratqfpq flddllttsa rlgpvvgdra vlaqpvdpge vaarlaarla
      181 agplggieef ggpqvlrfde avrawrearg srrpllpvri pgrlgrelra gglvtealpr
      241 gvrtwadhla dtyggterr
//
LOCUS       WP_357573726            1030 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573726
VERSION     WP_357573726.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1030)
  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 1030)
  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 1030)
  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 1030)
  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..1030
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..1030
                     /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=112836
     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          126..1025
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          739..763
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          768..804
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          814..842
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(815,818..819,822..823,825,855,858..859,862..863,
                     865..866,895,898..899,902..903,906)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          847..883
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          934..962
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          974..1001
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 meinllggle vlladhklhl gtpkqrvifa mlavqpgqlv tlaslidelw adrppcsava
       61 nvrtyaanlr refetlalad atlvrqgdgy rlalrpdvid vfrfqdelca grdalgagdl
      121 srasellgra larwqgpmla gvplgpvlta rtvaaeeerl lavellaevh lrsgrddlai
      181 pslravtalh plreptylll mralhergdn aealvaydei rrhlmtelgv spgasleklr
      241 rrilaeapsp vpdvpgpskg avgrravsap apagdsttkq lppvvdhlpr svtdfvgrda
      301 vvarllaetr rveervpavh vidgmagsgk ttlavhlarr lsdrypdarl yvdlrghgek
      361 dlvgpasalv vllrqlgvpp ervpvdlddr telwrrelar rrsviildna assdqilpll
      421 pieptavvlv tsrrrlthpd lgasqslpvm ssregvdlla lsvgrervda epeaavevvr
      481 rcghlplair lagarlahrr gwrladlaaq magaasvllh lagenstvtg afaasyeplp
      541 estkrvfrfl glypgsrfsp tavaaltglt vaeahaaldd ltdrhlvedl nsrqyglhdl
      601 mrqysvelcl yvdsardrrs alaqlldftl aaalriaeii epvvigsqvs hlpfgrpell
      661 ealgepsvew leaeradlvt mvasahesgf yehawrlara lwrfcyirgy fediitthqq
      721 glaaaeatgn vestalmqny lasayvrtgd nrealkhltr avelskesrd vlntaryqan
      781 lapvhywsgn lseavalgme qlrdyrgygn agapnalpnv gialtslgry eealwihrrh
      841 lawartnsse fhvlnalshi gavrtrmgdl hqairilras lalrdrtghr ygeaevrldl
      901 giayrglgrl aeaqqehemg ralavgsger hieaaalnel grtlrargld reaaemhrea
      961 lrlatriahp heqgralagl aehfsavdpt earrhweral aifrrmgvpe rldverrlae
     1021 lgsalvdvgr
//
LOCUS       WP_357573749             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573749
VERSION     WP_357573749.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..265
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27026
     Region          30..256
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msadpravlt rpapepdltv aygdhpdqva dlrrpagvgp arplvvvvhg gfwraeydrr
       61 htgplaaala aegypvaqve yrrtgqpggg wpgtftdala giaalpglat ealpgrvsga
      121 apilighsag ghlalyaaat apstvsgvla lapvadlaaa hrldldsgav aallgggphd
      181 fpdryaagdp rslvpirtrt vvvhgsadlq vpvamsrdfv aaaraagsdi slvelpgceh
      241 fglidpesaa wprvlavlrs lhddh
//
LOCUS       WP_357573755             262 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573755
VERSION     WP_357573755.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 262)
  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..262
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..262
                     /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=28401
     Region          4..262
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mggplvfahr gasydlpeht laaylralde gadglecdvr ltrdghlvcv hdrrldrtsn
       61 gsglvsartl aeldaldfgs whpgsapsgd lppdgshtrl ltlarlldav laagrpvrll
      121 vetkhpsryg snverrlvdl lrrygladpa pddpvqvtvm sfsplavrrv relapalptv
      181 lllevlppwl rlgrlpfgtr iagpgiglvr arprllpalr aagnqvyvwt vnepadlelv
      241 laeevdgiit drpahvlarr dr
//
LOCUS       WP_357573761             458 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357573761
VERSION     WP_357573761.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..458
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..458
                     /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=48912
     Region          27..403
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mryedlsywl stldepltpr palpgdtdad vvivgagytg lwtayhlara dptlrvvvle
       61 reiagygasg rnggwcsalf ptsltglarr hgrdaavamq ralhdtvrav grvvaaegid
      121 cdwadggtvt lartgpqlar araavdeara fgfgaehlal ldadeaaarc gaegvrggty
      181 tphcatvhpa klvralarav erlgvriheq ttvtairaga artpsgtvra svvvrategy
      241 tpmlpglrrt vapvyslmva teplpaqtwe rigladretf sdhrhviiyg qrtadgrlaf
      301 ggrgapyhfg srvspgqdre prvfaalrrt lgelfpvlgp dvpvthawgg plgvardwaa
      361 svgfdrasgl awaggyvgdg vgasnlagrt ladlirgqrs eltglpwvnh rspgwepepl
      421 rwlamnaalr vmtsadaken rterpsrrar tlsrllgq
//
LOCUS       WP_357573762             826 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573762
VERSION     WP_357573762.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 826)
  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 826)
  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 826)
  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 826)
  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..826
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..826
                     /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=87682
     Region          133..808
                     /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 mparllvltt avtvtalaaa vvgltlpagl psddplggpa rfgiavavla vaqlarlrfr
       61 ssagmvsitw geaalivcly lapagwlpsa tllgtglawt alslhsdrrp pleivriaas
      121 ltaasalavs vttalghpll aaptpmlala viagsvtyll vtawlggvtl glrhglpigp
      181 pllaalrgkl lmfvgnvavg lvvialleld prwllllppl lwllqqtyry rlradqerrt
      241 wrafaeataa lnqldergva saavtgalal fnaelvdvdv aradgrwrry rgdaggqlhd
      301 revgppdrse pdeyelvrql svgaapvgql rvrfprsapp atrerdavaa fgdalaaalh
      361 daathrelrl vtarssyeav hdpltglanr tamlgkgdqs lrqlahdhpv alllldinqf
      421 kevndtlgha agdqllrlta nrlsalarpg dllgrlggde fallltsvpv lgdraapmah
      481 alrqareiae rlaaptevag vrmsievsvg vvvadagtad ltellrradi amyqakeggg
      541 svaaydstrd aastdqlall aelrealkvd dqlvlalqpa vdlatgaptg vealirwqhp
      601 rrgwlnpadf irpvenseql gtftryvldk algvaagwar egldvpisvn lsarslldpr
      661 lpaeiadalr rhqvpphrlv leitetvvms eleiidevla tlrsmgvqla vddfgtgfss
      721 ltfltriavd elkvdrsfvi rmadspeaaa ivrttvglah elglrvvaeg vetaeqrlal
      781 aelgctsaqg yhffkpmpad kigavlgslr dsaesnvfrl radgas
//
LOCUS       WP_357573772             448 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573772
VERSION     WP_357573772.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 448)
  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 448)
  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 448)
  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 448)
  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 448)
  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..448
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..448
                     /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=44035
     Region          174..445
                     /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 mggtdvtdgw dwrrggetpa pasppgagtp pagapttpgs daapaaaaga spwwsdalgd
       61 pwrdpatpaa vvvpgvvaag tepepvtdpd apgrptlrhl llipvitall agtlggalgy
      121 afavrggaag tvlgaqaaep pvlaqrkpes lagvaervlp svvtvrvssl ggtsegsgfi
      181 asadghvitn dhvvsgssgk asvifndgts apatvvgqdp esdiavikvn rtglrpvefg
      241 dsdalavgdp vlaigsplsl antvtagivs aldrtmqage pggpvryyaa iqtdaavnhg
      301 nsggplvdga grvvgvnsti kslvaegqea gniglafaip inqakrvtqd iigtgkarrt
      361 vigaqvggpg aganggvrla avepsgpaag aglkvgdvil klngrpmtep tdlialvrkf
      421 apgsvvtvef rrgaarqnts vtlaadak
//
LOCUS       WP_357573877             442 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573877
VERSION     WP_357573877.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 442)
  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 442)
  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 442)
  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 442)
  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..442
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..442
                     /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=48522
     Region          8..>227
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msprsdgrvr yavvgtgara emfvralvld hadttelvaf advnqarmda hnrwlaelgh
       61 rpvptypage framldkerv dvvlvtsvdv thdeyvvaal ragrdvvtek pmtvdaarcr
      121 rildavsetg grvtvafnyr ynplheqvrr lladgavgei gsvhfewlld vrhgadyfrr
      181 whrdkatsgg lmvhkashhf dlvnwwlgat pvevyaagrl ffygetgrrh gyardyeray
      241 gspaavddpf alrldahprl relyldaeae dgyqrdrnvf apgvsieddm avlarystga
      301 tmtyhltaya pwegyrvmvn gsrgrlelev tendfvdrgt agavkgaalh gveapaeggg
      361 atltlrpfwe pprqipvegr trhghggada rmtavllggq pdplgraata ddgalalltg
      421 laanrsfetg qpvrvadllt pr
//
LOCUS       WP_357573931             423 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573931
VERSION     WP_357573931.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..423
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44789
     Region          3..413
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mgtadveavw riesarivaa ltrftgdfgl aedaaqeava ealvswrras panpggwlma
       61 tarrraidai rrrhalqery allaadaagd aaaglvvded idpdridddv lalmfvschp
      121 vlspearval tlrvvgglss eeiaraflvs vptvqaritr akktiaaarv pfelppaaer
      181 rerlggvlsv lyviftegst atsgdrllrp dvayeairla rtlaalapde pevhgllalc
      241 eltaarfpar tgtdgspvll adqdrrlwnv sairrglasl arasarglgp yglqaaiaav
      301 hatapsveat dwerivvlye algrvapspv vdlnravava masgpahala ivdeliaanr
      361 lpgshlvptv rgellarlgr raearaelel aaqlcanqre rsvllrkase sadpgpaqra
      421 pid
//
LOCUS       WP_357573999             277 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC049114].
ACCESSION   WP_357573999
VERSION     WP_357573999.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 277)
  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..277
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..277
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29527
     Region          33..271
                     /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 msrtqlletp peaaaaappd prrprparrw rrlvspvvlv lgwelaartg vlapeklpap
       61 sdvlatgwrl srdgtlavhl vdsltragag lliggvlalv lgavagllrl gddlvdppvq
      121 marmlphlgl vplliiwvgi geslkislva lgaffpiyfn tyagirdide rlveaaracg
      181 lgpaarlrhv vlpgalpslf lglrlaigaa wlslvvgeqv naqtgigflm mearefsqtd
      241 vvvlgllvya llglisdlal rvaerrmltw rrglrat
//
LOCUS       WP_357574005             288 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357574005
VERSION     WP_357574005.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 288)
  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..288
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..288
                     /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=32945
     Region          6..250
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mspsprlrav sdlhisyaen rafvqelrpd hpgdwllvag dvaerfadie walgllsnrf
       61 arvvwapgnh elwtppgdpe hlrgetryre lvelcrrlrv vtpedpypvw dgeggpatia
      121 plfvlydytf rvpqastkqe slalayaagv vctdeallhp dpypsreawc dariteterr
      181 laerdpalpt vlvnhyplvr eptdvlwfpe faqwcgtvrt rdwhlrfgas tmvyghlhip
      241 rttfydgvrf eevslgypre wrrrgpvpdp vrtinpaedl rrresvsg
//
LOCUS       WP_357574006             298 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574006
VERSION     WP_357574006.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..298
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..298
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30462
     Region          69..296
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mpisrrrilq lvaagggvta lgaagialvd aevlpgrsvl dhalgrcdaa pptapqgtpq
       61 ppvtgsfcsa arrrevafai syppgyapga rlpvclalhg yaadarsavt aarypeflag
      121 alaagvppfa laapdggdgy whphatddpl gmlvdeflpl lagrglrtdr vavagwsmgg
      181 ygallaalth pdrfrtvvat spaifrsyad aervnagafd gpdewarydv taraaqfagl
      241 pvriaigaad pfagavetlr drlpdpevvt igvgchdgdy wasvapaqvr aigaalag
//
LOCUS       WP_357574011             302 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574011
VERSION     WP_357574011.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   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 302)
  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..302
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..302
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32571
     Region          1..299
                     /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 mpetfvdsgs vpiairdfdg pgqpllllhg aggnlaqmtt laehlrptyr vvtvdlrghg
       61 rsgdgpwrwd dvladlaavt dhlgltspav vgvslggmla tlwaqrhpec pgvvsfdgnp
      121 plnrpdqlag ldpeqaetel aklravfdgm aamlaeplta eqvaamragq ramaqrygaa
      181 pddwvaafer nlvpgddgrs qlrpapdltr qlrdamdsld lmpayrdarc plllvlated
      241 lpeqqpfhsl yeayrkvtad rlatvdnpsl rvrhlagash amvaerpqel atlitdflsp
      301 qd
//
LOCUS       WP_357574211             372 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574211
VERSION     WP_357574211.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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..372
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..372
                     /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=38325
     Region          3..346
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgephrvgiv glgvisrayl dtlanhpavs ivaladldas rsaaaaaaip gaesmgverl
       61 larpdvqtvl nltipaahae islgaieagr nvyvekplav tipdgrsiie rassagvhig
      121 capdtvlgtg tqtaraaidg gligrplsat avmvtpgher whphpdfyya pgggplldmg
      181 pyyisalihl lgpvravvga asrlraervi gsgprngqri paqvdthvtg vlehangals
      241 tittsfdgva ttaapievhg etgtlavpdp ntfdgdvrvf plggtgwrvl epragyvegs
      301 rgiglidlvs adgqrsprag gdvalhvlet mtsllasaae grrielttvv qrpapvpltp
      361 vhdwtesnay gr
//
LOCUS       WP_357574215            1087 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357574215
VERSION     WP_357574215.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1087)
  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 1087)
  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 1087)
  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 1087)
  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..1087
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..1087
                     /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=116511
     Region          7..251
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          127..1076
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          767..793
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(769..770,773..774,776,806,809..810,813..814,
                     816..817,846,849..850,853..854,857)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          804..834
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          845..873
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          885..913
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdqvedglqi rllgpvgvwh gsrllgpsaa qqrtvlamla lecgnivpin rlvtalwgta
       61 ppasarnavq gcvsrlrall nsvdqpsrta qlvgvgtgyr ltvdrsavdl hdfrdllrsa
      121 rtcepqrare lvdralrrwr gpaladvagp wldelvapql neerfaavel radldlrlgr
      181 ygdivddlsd liadnparer lalavlialh rcgrrvdalt lfrrvrenlv erlgiepgee
      241 lqrayramla gtepaaepav qlvreptgvv prqlpaatpg fvgrqrelav ldevrkerta
      301 pvavvcgpag agktslavrw ahdvhhhfpd ghlfvdmrgf hprprrtpge alpllldalg
      361 vpadripaep daqvalyrst lagrrvllvl dnvadadqvr plipgcpdcl vvvtsrdrls
      421 glvardgaar ltldvlpaad avellvgtag aerinadpaa arelaeicgh lplalriaga
      481 rladrahvsv rrhldeliar grvaqlrveg ddstavraaf elsyqalpap agrvfrllgl
      541 vpapaglaap aaaaltglpc ddleplidtl arlhliritr atrivshdll leygaqlaae
      601 hgdaadnaaa vhrllhfylh avarasaaln gpsrlrlppd ppptgvripe lddqaharew
      661 lvaetanlva alehaaadgr drmawqlahv lydflrmrtp lsqwrsiart glkaarrdgd
      721 lrgeavmrqs lgllnwrtgd lraaraeyea vaalaaradw qvgasaahcs igialaqlgr
      781 praaisrfeq alvidreigd rraeagtlan laaaceevge laaaarhgel amrllratgq
      841 hlgaavasen lalvarelgr ldeartaaee avrvgrsiga rheeaasltt lgrvhgdagr
      901 yaeaeevlhl gldivqglpd grlevvtqaa laevllrqnr laeassrldl vrdladrtgn
      961 erarvealml lsdlsaaake fdsahehatg aisaaraggy rlvagqarsr laaarlglgd
     1021 pegclvegrq alrvqrragq rlayartlmt vgsayaalgr psaaqtrwra ahelfreiga
     1081 aeaaplg
//
LOCUS       WP_357574230             415 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357574230
VERSION     WP_357574230.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  AUTHORS   ter Beek,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..415
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..415
                     /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=44489
     Region          39..410
                     /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 mgkqrarfgf araacalgla atfltgcgsd ggssdgvtkl tfaastfgdp grgpqltkwl
       61 defnqsqtki qvsaaavpyp tfgqtvltqm gsgkgpdlvr fdmpefeaas daglvapldk
      121 lvdaskydll kqpdqfmvhd gvrhgvifea snyamfynad liptppttye qfastakslt
      181 kgdvfglafr qteaeeagvw qdifnyvygf ggawsdgknl tinspenlkg lqafkdlyda
      241 nviprgadaa tfrrmfaegk vgmelnnggy vtatrgqnak lnfsvapipf pvrkqgtila
      301 pivineaseg kdeaatfikw alepqnqvkl qeilgassva tttqrsaetl katpflpvfd
      361 gltesslpqi vlgfeaktpd irkvvvqnvv aalqgktdlk saldraqqqa telvr
//
LOCUS       WP_357574274             272 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574274
VERSION     WP_357574274.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 272)
  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..272
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..272
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27875
     Region          1..269
                     /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 mtalrtvtvd gspvhvlesg tgpavlmlhg sgpgttgsga wattaqalgt swhlvapdqa
       61 gfgrtpvpag srgglrlwte qaaglmnalg idhyavvghs mggavalala aarpqqvtrv
      121 vavstmgapg aplsadldav waapagptga rdmlsrlvld qalvtdsavd araaamraga
      181 dafaslfppp rarwvddltl saqtlaaira pvllvhgaed rvtpletaaq pllehladvr
      241 lhvfgrcghv paiehphefr rllscflgrg hq
//
LOCUS       WP_357574318             326 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357574318
VERSION     WP_357574318.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=35287
     Region          29..314
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msvnatpaga qvsaeaerst tvptqrggrr kpplsenkka errlgwllca paalvmvavt
       61 aypiiysvwl slqrydlrfp dqrefiglen yatvltnefw wtafgvtali tvvtvavelv
      121 lgmglalimh rtlvgrglvr tsalipygiv tvvaafswry awtpgtgyla dlfsdgaplt
      181 erasslaiim laeiwkttpf malllmagla lvpedllkaa stdgatswqk ftkvmlpvmk
      241 pailvallfr tldafrvfdn ifvltaggne tssvsmlayn nlirglnlgi gstmsvlifi
      301 tvaiiafvfv klfgtaapgs ddserr
//
LOCUS       WP_357574338             481 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574338
VERSION     WP_357574338.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..481
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..481
                     /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=50844
     Region          18..>215
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mgrlrqlaer tpagreryvd llralaitmv vlghwgvvvi vrddgglptg hsalsdlpwa
       61 ypltwvaqvm pvfflvggya navslarlra rggdaaswll drsarlvrpt svlvlvlgga
      121 avvarllgtd ptrirevvwf atiplwflva ylavvaltpp myalhrrlgl avplvlvalv
      181 glgdlgrltg pvglsygnyl fgwlaihqlg fawydtrpaa gpkpasetap padtagrpal
      241 aeadpsaheh sgvrrrrlpt srraalvflv gglaallllt vpgpwpvaml nvpgerldna
      301 gppslallav aatqlglill lrgpaerllr rtgpwqvvia vnlvvltifl whltaaigli
      361 glldatgtlp tpevgstaww awrvpwllll aavltvlvai fgpvevhssg hrtgqragqg
      421 tttrtaltva gyaavvfalm lnsatpklta eplgmpapal laylagagvl rllrsgwgtr
      481 g
//
LOCUS       WP_357574466              69 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357574466
VERSION     WP_357574466.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=7564
     Region          1..63
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mahgpgelva agevlamlgv grsrfrqiqq sphfpapyar lsvgsiwlka dvekyiaehr
       61 rprpvdede
//
LOCUS       WP_357574513             246 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357574513
VERSION     WP_357574513.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 246)
  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 246)
  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..246
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..246
                     /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=25437
     Region          1..222
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msywsdrkvl vvgasrglgr gvteafvaag atvtalsrdt aplaaladah rtlslvdada
       61 tdpasldvlr rnppdvlalv agaapelrpl aeqtwetfst pwntdvriaf lwlrqvlrqp
      121 lapgsrvivt ssgaalkgsv lsggyaggka tvrfladyaa qeaaragldi tfhtvlpqlt
      181 petglgraav dayaeragvp petfvepmrp vltpeaagaa flrlggdpdp sgtvhlltga
      241 glarlp
//
LOCUS       WP_357574579             559 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574579
VERSION     WP_357574579.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..559
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60707
     Region          16..550
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mgyvdvaavg hilpdgrelf advsfrvgeg akvalvgpng agkttllrmv agdlavrtgt
       61 varagglgvm rqfigmigde ttladlalsl appplrdagr rlaetetamr aaevrgkfss
      121 aagkaqlaya dalgawgeag gydaevlfdt vativlnqpw davrdrpvrt lsggqqkrfa
      181 lelllrgpde vllldepdnf ldvpgkrwle arlrestksv lyvshdrell aqsadrvvav
      241 eggsawvhpg gfaswyearv arharldelr rrwdeehqkl relmlmykqk aayndglasr
      301 yqaaqtrlrk feeagpppvp pkdqdirmrl tggrtgkrav vceqleldgl tfpfdleiwy
      361 gdrvavlgan gtgkshflrl larggtdpdp angpvdgaga lapvahdgta rlgarvrpgh
      421 fsqthdrpel mgktlveilw rgdehrtgmd rhaamgvlsr yelagqgdqr fgtlsggqqa
      481 rflvlllels gatlllldep tdnldlasae aleaglnafe gtvvavthdr wftrsfdrfv
      541 lfrgdsevve tpepvwdvg
//
LOCUS       WP_357574578             201 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357574578
VERSION     WP_357574578.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=21469
     Region          9..201
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mtgdhyftaq pasdapardv efsvadrdyq lvsaggvfsa srldpgtavl lrkaelpaad
       61 tagalldlgc gfgpiacvla dvapaatvwa vdvnararel taanaariga adrirvsapd
      121 dvpadllfaq lwsnppirig kdelhelllr wlprlapdgv gwlvvarhlg gdslqrwivn
      181 qgwhverhas qkgfrvlrvt r
//
LOCUS       WP_357574600             420 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574600
VERSION     WP_357574600.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 420)
  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 420)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..420
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42908
     Region          24..416
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mtttavrkdg paavtppptv grharnyisr vrggdvgalp avlglivlct vfavmrpssf
       61 lsagnfanlf tqgaavtlia mglvfvlllg eidlsagfas gvcaavlanv vtvlgypwwv
      121 avlaaiatgl vigttlgmlv akvgipsfvv tlagflafqg ivlllvkegt nisvrdnvlv
      181 aianrnlspa lgwafailav agyaavqllr hrnrvargli tdpiavvalr iaglaiilgt
      241 avyvlnlers rnvlisslkg vpivvpiiav llviwafvlq rtsygrhiya vggnreaarr
      301 agigvdriri svfmicssma avggivaasr ansvdpntgg snvllyavga aviggtslfg
      361 gkgrvldail ggavvavien gmglmgysag vkyvvtgvvl llaasvdals rrraaatgtr
//
LOCUS       WP_357574655             436 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574655
VERSION     WP_357574655.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=47830
     Region          8..435
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 maarrsripa tkypverftl dnglrvvltp drsapvigva vvydvgirse pegrtgfahl
       61 fehlmfqgse nleklahfrh vqgaggtfng sthldytdyf etlpsnaler alfleadrmr
      121 gprlteetlr nqvdvvkeei rvnvlnrpyg gfpwltlppv mfdtfpnahd gygsfddles
      181 atvadaadff rryyasgnav lavsgdidva eatelvtrhf gdvpsrpapr rpdftepdlt
      241 aerrssytda laplpavaga wrvpdpvgdf agylpyvvla evltdgdasr lverlvqrdr
      301 tvtslggylg fmgdpfdvrd ptalllqahl ppggdvdkvl rtvdeeldrl atdgltdgel
      361 artqarmath llrdtdavlg ralrmavleq qrcepgllnd lprlvgdvte eqvraaaatl
      421 rperraavev ipggar
//
LOCUS       WP_357574685             296 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357574685
VERSION     WP_357574685.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..296
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30162
     Region          11..276
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mgvrrlvavl vtallagcap atavaggsag ppsarrapeg syvvgvrtlt ldprsarplp
       61 vtiwypagtd gvaagrfpvv iyshglhsrp elhaglttrw aaagfvvaap ayphtragaa
      121 nftradvrnq padgwrlirh lgrldgdpad plaghldlts iaaaghsagg fttsgmfteg
      181 hparlrggiv iaggglpgsf agptapvlfv hgtadpvvpv tvgraayart pgpavfvsvl
      241 gqdhgayltp gnpgfaavla tttdflrwtl ygdrtagarl ptdartpgtr yesrpa
//
LOCUS       WP_357574754             238 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574754
VERSION     WP_357574754.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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..238
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..238
                     /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=25274
     Region          23..207
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mslssvaeam eppwldrgev srcddlfllg hddtghphvh rqtlilglag avlidwylag
       61 rvtlypnidt haadhqrihp hidrpvgdli adataatirn ahpllsmwlr afsptrttap
      121 sptcslagsc asapdgasag lmradtylps dskwaviars rlrylaaghe qpndhsaala
      181 glvtdlgltd hlylddetpa mtsrlrataa qhyqpvrdit aavdaavdaa vgdlatat
//
LOCUS       WP_357574768             461 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574768
VERSION     WP_357574768.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=48778
     Region          115..453
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 maigwirrhl gvrlrsalaa atvvgaafav gaaafvylar tdlagnvdaa arqraaevia
       61 avgagdqdal aqtlrpspge qtlvqvldps grveaasaal gdaaplsplr prpgqllreq
      121 rllpfadedp friaaegvat dsgvrtvlva qslrpvnest eavaailaag lapmllvvga
      181 avfwfvgrsl rpveairrrv agitardlha rvpvpavrde vaalaetmnl mlerletaaa
      241 sqrrfvadas helrsplatl ragldrlaga ptpdnqhdlv allrreasrl gdlvadllll
      301 aridergatg rgddvdlddl ayterdrlaa hrpdltvrah ltpvrvagda hdlgralrnl
      361 adnaarhart svtlrvsvrd gwgcvevtdd gpgvpdadre rifdrfvrld dsrtrpeggt
      421 glglaitrev vaahgghvqa vpgpgmtvri llpsdvesdh r
//
LOCUS       WP_357574858             458 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357574858
VERSION     WP_357574858.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..458
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..458
                     /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=49500
     Region          27..>360
                     /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 mslspvrvfa alnavrppdq ptprlgkavv vggsvaglla arvlsdhaes vllldrddpq
       61 lsgarpgvpq gtqlhallpg gllqleqlfp gfrqqalahg aieappaarr syldgrrkvv
      121 vpddddslag srplleglir qqvlrlpnvk tvtaratglv fdgdavtgvr yevdqvpgve
      181 gadlvvdamg rssrlsewle qagwerpatr rmavhlnyat alfrrpepsp ettvvlalht
      241 prtmtdiaga affaiedgrw mammagygkd rpgrtaqdfv rrlreqfppe fgevagqeml
      301 gdvqtyhhad srrrdfhalr rfparlvsvg davasfnpvy gqgmtaaalh aaclsaylrs
      361 dpdlseparh flalqkvvvd aawststsad lalphvdgpy prgyrvsswv srqiltatvt
      421 dvatarrfne vvslrehpls latpgvilga lranrrsg
//
LOCUS       WP_357574887             342 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357574887
VERSION     WP_357574887.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..342
                     /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=35317
     Region          1..337
                     /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 mkavvyrgar dlgiedrape ppgpgqvria vaytgicgtd lhifhgdmda rvgasavigh
       61 emsgrvaalg dgvtgltvgq pvtvmptrac grcpacrrgn shichamdfl gidspgamqs
      121 swtvpaelvl alpddlpldh aalvepvava vhdvgraevt sgehvvvvgg gpvgvliaav
      181 arargaevll vepdgfrrgv asgigieavd pgptdvvalv nertggagad vafevsgsaa
      241 gvgtavdvlt trgrlvmvai hpqprpvnlh rffwrelell garlyqredv veairlvaag
      301 viparelisr vlpvagvtda ftaleggggv mkvlldwree gr
//
LOCUS       WP_357574908             491 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Micromonospora
            sp. NPDC049114].
ACCESSION   WP_357574908
VERSION     WP_357574908.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 491)
  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..491
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..491
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51505
     Region          29..420
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msltelsgap tpepttaadt parparrtsp fgalllrlhf yagilvapfl vvaaltglay
       61 tttpqldail ygdqltvaqv gdrplpladq igaarnahpd ggiatvqpgd gdqstrvtfs
      121 lpelgekqht vyvdpytaqv kgqlttwfgs tpattwlddl hrnlhlgvvg rhyselaasw
      181 lwvivlggvi lwwrrrsanr atarhllvpd lsagkgvrrt rgwhattgiw ltvgllflsa
      241 tgltwsryag anfgagldal sarapemsts ltadpaapae tggghehgas gagglvvsat
      301 fdqvstaara aglsgpveia paaepgsawt vtqvdntwsv akdrvavdpa tgtitarsdf
      361 adwpllaqls algiqahmgi lfgpinqill aalalgllcv ivwgyrmwwq rrptradrra
      421 fagtppargg vrglplwvll vgvpviaaig walplfgltl laflvidavv gvvsrrrrpa
      481 avptspapag s
//
LOCUS       WP_357575002             310 aa            linear   BCT 28-DEC-2024
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357575002
VERSION     WP_357575002.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 310)
  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..310
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..310
                     /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=31972
     Region          45..298
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mrrlltllvv plvaaatltt vgsaaaahpt psfpsrialp dgfspeglti grgttvyvgs
       61 vgngavwrgd vrtgrgsvli pgapgrekag lkldpqgrlw tadfssggas vhdggtgaql
      121 ahyqftdepg sivndlvvts ravyftdsar palyvvpllp ggrlpaagaa rvlplrgpaa
      181 tpdafnngiv alpdgdllva qmltgrlvrv dprtgasrvf dlggysvdra dglvlrghtl
      241 yvirnltnvi avvglnadyt agvvrreitg palrspatgd llgsalyvvn grfdvepgpd
      301 vdydivrlpa
//
LOCUS       WP_357575077             263 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357575077
VERSION     WP_357575077.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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]"
                     /calculated_mol_wt=28043
     Region          23..153
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mthpvwadad ayeayvgrws rlvaadfvrg lavapgrhwl dvgcgtgalt atvlaeadpa
       61 ritgidpsag fvaqararvq darasfhvgd aralpvpdra vdvvvsgltl nfvpeparav
      121 aefarvvrpa gavsayvwdy tegmammrhf waavahldpg aagrdeasrf smcrpeplrd
      181 lwvdaglrdv svrpvdvptv fadfddywrp flggqgsaps yvtslgepqr aalrdllaar
      241 lpiepdgsir ltarawavag tap
//
LOCUS       WP_357575191             383 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine desulfurase family protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357575191
VERSION     WP_357575191.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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 10003004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..383
                     /product="cysteine desulfurase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39132
     Region          6..376
                     /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 msassvylda ataaplhpva rqallaaled gwadpgklys qarrarqlld aareaaaqtl
       61 gvradelsft ssgttaahga vlgglagrhr agatlvhsai ehsavlhaae rhvaaggvah
      121 avpvdrvgrl dlaewstavr apgvalaali tashevgtvq pvaeaaavca dvgvplyvda
      181 aqsvgrvplp agwsmlsasa hkwggppgvg llavrkgtrw espwpadere ggrtpgvvnl
      241 pavvaaaasl raaaadaaae earlaplvdr irarvaaevp dvevvgdpvl rlphlvtfsc
      301 lyvdgetllh aldrrgfavs sgssctsstl rpshvleamg vlshgnvrvs lhrdttesdv
      361 erflaelpgi vaglradagv vgl
//
LOCUS       WP_357575121             314 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575121
VERSION     WP_357575121.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 314)
  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..314
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..314
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32934
     Region          11..296
                     /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 mperfevgmp dgvrlhvevt gpadapvtav llhgwtldgr swhrqvdalt tssgdavrvv
       61 aydarghgrs scmalptatl aqlgddlaav ldavapsgqv ilvghsmggm timeyahrhp
      121 dhfaartagl vfvsttaegh thtvyglspr iarlirlaet tgagvlarcg swrapralln
      181 alqpsirwml fgdrcdpsdi rlvtsavara slrsiggfra sigaqhrldt ltalahlpaa
      241 alvgdrdrlt pppcaesiaa alpateltvc pgaghmlmme rpdevnaalt gvlrrvlaap
      301 ardgldasat gtrr
//
LOCUS       WP_357575223             231 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575223
VERSION     WP_357575223.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   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 231)
  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..231
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..231
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24601
     Region          4..228
                     /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 madvvlvaga wlgswawdev vpglraaghr acpltlsgla errgvpagqq thvqdivgei
       61 errdlrdvvl vghsysgipv gqaagrigdr ltrvvyvdae vpvdglsfas gwwqgqaafe
      121 svladnggdw ppldvaefdg qgltdeqiar lvkgctphpg atltepavla rplgelptty
      181 vkclldgpep ndtvsallts eqwrlvtmat ghwpmfsqpd elarllveqi g
//
LOCUS       WP_357575297             179 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575297
VERSION     WP_357575297.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=19504
     Region          12..167
                     /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 mrylrsggpa airrprpadv defvaaarrs rdlhhpwlaa patpqeydny lrrirrrdsa
       61 gylicdrasg aiagyvnisg ivlgalrggy lgyaafepys gtghasagia lvidhaftta
      121 glhrleaniq pgnepsrrva rklgfrlegf spdylfidga wrdherwait aptptpppa
//
LOCUS       WP_357575468             391 aa            linear   BCT 28-DEC-2024
DEFINITION  lactonase family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575468
VERSION     WP_357575468.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..391
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..391
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40556
     Region          52..370
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mkrsvalaaa llvgltsvgt lpgaawadgg gptgnhddrg ggdyhhdseg avfvqtnkae
       61 gntikvydrd edgrlskage yetgglggft igapvdalas qgsltyhrgl lfavnagsnt
      121 ltvfrvdgtr lhkeqviwsg gllpvsvtvr gglvyvlnag gegsvqgfql hkgrlspihd
      181 snrslglhng nppafmtapa qveidpdgef vlvstkaanv mfsfeigrdg elsrrpvisd
      241 agsvpfgftf dtedsvlvte sgsnevgrfd ldedgaldqv gpsvpngqqa pcwiqrvgdy
      301 fyvanagsst isayrvdddg klqlvhavaa dtgggsidmt tsdgflyvqn aaagnvqgye
      361 vkddgslrlv ttveglptft dgigmegiaa s
//
LOCUS       WP_357575434             299 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357575434
VERSION     WP_357575434.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (residues 1 to 299)
  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..299
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..299
                     /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=33112
     Region          4..281
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdvdlrklry fvavaeelhf graaarlhia qpvlsrqira feqelraelf vrdrrstvlt
       61 eagrqlltda rpllasaeal hrrvqraahg rstftiafmp giivtaeara iaerhpdlsv
      121 dvvrtsprdq advvregrad vsyvrlpvdk rglslrplfs eprvvvlpre hrlagkesvd
      181 laelveerll qdpdvvpewr dlpnrpsdsd prprpvlssv eeklehvaaa agmvilplsi
      241 atfytrpdva hvavddlgpn qvclawaedn rsplvrefvd laarqaqaag rgsaggdgw
//
LOCUS       WP_357575316             373 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575316
VERSION     WP_357575316.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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 373)
  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 373)
  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 373)
  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 373)
  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 373)
  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 11471805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..373
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40454
     Region          2..366
                     /region_name="COG4938"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443965"
ORIGIN      
        1 miegvritnf krfreidlpl rqltvltgtn gagkssliqa lllvrqased erasvvqlng
       61 pygleigead dalcvaaedh virvslnigs irheyefsai ieerslhlpi irrpqplptl
      121 lsspgmsfty lnaerlgprd qlsvtsaevs nigvgvrgey vaqaitirer dvvaghlrhp
      181 dastvqtfra qveawmsdiv rpirieaqwp lgmttstirf qtpdiesqpl rpgnvgfgvs
      241 yalpivvagl aveqgilive npeahlhpag qsklgrflgr vagagaqviv ethsdhvlng
      301 irraavddrt vgasdivvhy fddsqsspav idigaggsms nwppgffdql dqdlgrlaha
      361 krearratki gdr
//
LOCUS       WP_357575479             441 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575479
VERSION     WP_357575479.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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..441
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..441
                     /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=47571
     Region          23..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 mqapprvavi gagaaglaav kalrdaavav vcfeatdqvg glwvygapds payrtlhlnt
       61 srgrtefadh pmpadwpdyp dhtrvagyla dyadrfglhd airlrhtver vtrqpdgtwt
      121 vaasgpdgpv evtveavvva nghnrvprlp dppypgasta eqlhshdyrg peqltgkrvl
      181 vvgggnsamd iavdasyaae rtllslrrgv wvvpkyllgr psdtlngala rrlpwrlrqr
      241 isqtmltatv gsparyglpa pthgflqdhp tlsdgllsrl thgdvearpg vaalhgdrve
      301 ftdgrtdevd livwctgyrv eigfldpell gggadtlaly rhvfhpdapg lmfvglmqst
      361 gsafplveaq akliaahlag ryvlpeperq rafsraelra atarwgqrrp amrvdfdayl
      421 aeltrelasg arrarpagag r
//
LOCUS       WP_357575587             764 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575587
VERSION     WP_357575587.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=83687
     Region          13..762
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msrhsggtge lplddeigre qeyvsmlydr ldglreqaah rltaelrntg gtlqdrsqrd
       61 ssvamyadqv eqfsavengl cfgrldgddd srryigrigi fdtsgdydpl lmdwrapaar
      121 pfylataanp qgvrrrrhlr trqrkvtgln devldidsas pggheeltge asllaalnag
      181 rtgrmrdive tiqaeqdqii radlpgvmvv qggpgtgkta valhraayll ythrrelssr
      241 gvllvgpnat flryisqvlp tlaetgvllr tqgdlfpgvs aqrvepaeta alkgravlae
      301 vlalavrdrq wvpdepleie verevltldp etvraardrv rrtdrphnla ralfdveivh
      361 aladqvaeri gadplggdnl ldeadraeir relreetgiq aaldrlwpvl tpqrlladly
      421 adpdriaaaa pmltdderar lhrepggwtp advplldeaa ellgederaa aarrdrirmm
      481 ereyaegvle iargsrsidv edeaeggeil gvtdlidadr llerqeeadr lttaqraaad
      541 rtwafghviv deaqelspma wrllmrrcps rsmtivgdva qtgalagtps wadalapyva
      601 rrwrlteltv syrtpaeima vaadvlaeid palrpprsvr esgvppwdra vpdeqlpael
      661 vsaatreaag ltdgrlgviv pasrvdalga altaalpeat vgehpelesr vvvltvaqak
      721 glefdsvlvv dpdrmvaesp rgrsdlyval tratqrlgvl rpcr
//
LOCUS       WP_357575598             421 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575598
VERSION     WP_357575598.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..421
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45382
     Region          1..414
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mttdphiedl lrelapqvlg vlarrfgdfa taedavqeal laaatqwpvd glpanprgwl
       61 iqvgyrrmie lirseqarrr redlvarrdp ddrqyapaad eeltaerddt lvllflcchp
      121 alapasaval tlravggltt aeiaraflvp eatmaqrisr akqrirasgl pfrmpeeaer
      181 aerlsavrqv lylifteght stagpalrrv dlaaeairla ralhmrlpdd setagllall
      241 lltearspar tgpsgelisl adqdrnrwda aaiaegvalv tralprgpvg pyqvqaaiaa
      301 lhdeapstda tdwpqilaly dvlerlagtp vvalnravat amvhgpaagl taldalgddp
      361 rlaghhrlaa arahlhemag dreraiadyr aaaartsslp eqryltmraa rlaagppttd
      421 d
//
LOCUS       WP_357575657             536 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575657
VERSION     WP_357575657.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..536
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..536
                     /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=55909
     Region          7..499
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mtttgaqsad avvvgaghng lvaanllada gwdvvvleat avpggavqsa evtapgylsd
       61 lyssfyplgy aspvlngldl gryglswrha pdvlahllpd graavinrdp dvtaasleqf
      121 apgdgkrwln aytdwldvae pmlttittpf ppvrgglgll rrlrvagalr larrlvvpvr
      181 klgdelfdgp ggpallagca lhtdlspeea gsgvygwlla mlgqqvgwpv pdggarqitn
      241 alvarlserg grilygarvd rvltargram gvrtsggalw rarravladv papalyldlv
      301 gpaalpsrlv edlahfrwdg stlkvdwals apvpwtnrev agagtvhlga dlngltryag
      361 elargelprd pfllvgqmsv adpshsppgt eslwsythlp frqdwraeei aghvqrmedv
      421 leaaapgfrq livgrhvagp aelekgdpsl vggalgggta aayqqlflrp ipglgradtp
      481 vdrlflasss ahpgggvhga pganaaraal ardraltgta yaaaiatahr avyppt
//
LOCUS       WP_357575669             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            sp. NPDC049114].
ACCESSION   WP_357575669
VERSION     WP_357575669.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..416
                     /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=44440
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..371
                     /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"
ORIGIN      
        1 mveeltqaea avaacvdapa waliepdlva aldtahrleq rlaavqlalv reldgrgtaq
       61 aqgasstavw lrdrlrltvs aarrlvglag sldagapgvr aalasgdisv eqarviddtv
      121 rtvhnaagae aadkavgvlv gwagqfeptv lrklgtrild hvapevadaa araaleaear
      181 rcdrdrhvtl selsdgrlrl sgtldaeagg llraaidplt apsgpddart pgqrrhdala
      241 dlcrltlrtg elpehggepa qivvttsfdt larqldagtl dtgprltpet vrrlacdaai
      301 lpavlsstsq tldvgrqrrl itgplrralv lrdrgcafpg cdrpprwcda hhihhwadgg
      361 ntslpnavll cghhhrhihh gdwtirpgnd ghpdfippaw ldpeqiprrn vyhqrt
//
LOCUS       WP_357575680             348 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357575680
VERSION     WP_357575680.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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=34685
     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 mttlvdrptp arnrsgtrtg rrvavtvgaa lvlllavlas falgsrplgv gavwhalvap
       61 dgsdastivr elriprtalg lavglalava gvlfqaltrn plaeprilgi sagasfgvvl
      121 aisvfgvgtl agyvwfgiag alvagllvfa iasraregas pvtlalvgaa ldaslasgvy
      181 allsidartf eeyrfwvvgg lagrdlgvta qvlpfvlvgl llavlvargl dalalgddva
      241 rglghriglv rlggglaavl ltgaavaaag pvafvglavp hlaralvgad hrwtlavsal
      301 lgpalllgad vvgrlvappg eipagiital igapllavlv rrarvvta
//
LOCUS       WP_357575693             166 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357575693
VERSION     WP_357575693.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 166)
  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..166
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..166
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17980
     Region          2..71
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtntltiger vnwyrrrrgl sqevlaglig rtadwlgkie nnrieldrls vikslaevld
       61 vslgdllgep sllawtgdsg tatvpalraa lmnyraiapi gggtdakpps vamlrkevga
      121 lwdayqdsrf gyvtgrlpdl lyraqaaadh hngddqdqar rllgla
//
LOCUS       WP_357575765             227 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575765
VERSION     WP_357575765.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 227)
  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..227
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..227
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24358
     Region          5..221
                     /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 mttyvlvpga wkgswsfeav vplleraght vhaltltglr pddddatvat anldthaddv
       61 vrlldrahva datlvghsya gmvvaaaadr adgrisrrvh ldayvpldge scwsatnehf
      121 rkvfaagaag tgysvrppeg gdprrrphpl asflqtirlt gaaarvprre fvycsgwadr
      181 tpfaqlrarv dadpewqvhd lptghdamhe apeavaalll deggssr
//
LOCUS       WP_357575764             258 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357575764
VERSION     WP_357575764.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  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 258)
  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 258)
  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 258)
  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 258)
  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 258)
  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 258)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..258
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..258
                     /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=28249
     Region          14..101
                     /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          <61..256
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtshlwpsgg rhlwpaggts aaqtharghl vyaasgilav htergasivp anrvawtpae
       61 fthdhrahga tdmrivflap sltrflperp avflasdlar evllaltgpg nyddttpgys
      121 raarsrllrv lvdelreape qplhlpeprd drlraiarll yetpadnatl aelgrtigas
      181 trtlsrlfhd elgmtfyewr tqlrvyhalv lladgrdttq tayacgwanp ssfiaafsai
      241 igttpgryra grtpsprr
//
LOCUS       WP_357575859             314 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575859
VERSION     WP_357575859.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..314
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..314
                     /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=31520
     Region          <139..249
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 msvspspdpl aaleasawal aaavgtmsda lsaplaevla asphrsavle aagllswdag
       61 vpvahpslla adgptgrsav qarlsslrqa vaaaaqepsg pggtgwaelg devllhqgra
      121 saatgralat rvvpelpgla rrlgstdgrv ldvgtgvaal avalaralpr asvvgidvlq
      181 raldlargel aaapdvadri slrrqdvaev aepggydlvw lpapflpqqt ltvalprlvq
      241 alrpggwlva gtnppaadpl raavgrwnav rnggnafdad rmaqvlagag lvdvrrfptv
      301 pggpvlvaah hpgg
//
LOCUS       WP_357575905             242 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357575905
VERSION     WP_357575905.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 242)
  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..242
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..242
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=26026
     Region          3..237
                     /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 matfvlvpgf wlgawawrev tgqlraqghd vhpmtltgla erhhlagpqv tlethttdiv
       61 rlievedlrd vllvghsggg mpvaqaadli pdriarvvyv esgplpdgta qfdtvppqeq
      121 qrlraaigdg hllppppwdp tadptnlagl deptlsllre rstaqplrta tdpvrrtggr
      181 pvptalvast fglavvrqmi deghpfftgl adgqlhelpt ghwpmlsepk aladvldlia
      241 rt
//
LOCUS       WP_357576004             414 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC049114].
ACCESSION   WP_357576004
VERSION     WP_357576004.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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 414)
  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..414
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..414
                     /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=44266
     Region          34..410
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtrphrgggl aaspvvpyph gglsrhgnvp pgerlrvllv eddegdaflv gellaetnsm
       61 idlvvatsls earqritgvd cvlldlglpd aqgldglrqv lemssgaavc vltgrsdehl
      121 givavaegaq dylvkgqvdg vlltralrya verkradvna rrlrevelrq aesarlergl
      181 lpqplmttdq vavhtfyrpg rhaaliggdf fdvvqtrpdr ldlivgdvcg hgvdeaalgv
      241 elrvawralv lagvpddevl paleqvlmse rrlqeifatv attrldldan ratvrlaghp
      301 pplllsggrv vpvpapggll lgvrprrpia ydlefdtddw sllmytdgli egrvgagner
      361 ldvpglsgll depanrevsl pelpawlvgr aeqinggpla ddvamllvsr gggr
//
LOCUS       WP_357576006             269 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357576006
VERSION     WP_357576006.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..269
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28551
     Region          13..266
                     /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 madtllddvg dllaeaadqv vlplfrkldd advsekapge vvtvadrrae elisaglrrl
       61 rpgstvvgee gvaddpgllr hlrdsgdvwl vdpvdgtanf aagrrpfalm valltdgrpt
      121 agwildplag tlaagrvdeg tllngqpvda adavpplgel rgaamtrflp aeardrvrag
      181 grrlgellpg qhcagreyld iltgeqqftl fwrtlpwdha pgvllvraag gvarrfdgvd
      241 yhpadegrgl lvaaneqvwt evhdallgs
//
LOCUS       WP_357576007             337 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357576007
VERSION     WP_357576007.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..337
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..337
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=35967
     Region          42..337
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mprtrlsqrr vrrvllplla avalvlaggl payaepgegg tkklqdalel takghieaka
       61 kldnskrrqt altgelkave vrlvgltaqv gevaaqsyra grltptamll ntatpqaflq
      121 raadldlmaq rdskrlrdlt eakqqaqqak iaidtevreq qkqlavmakk kkeaetalae
      181 vssgssngfs ggsstsakpa prnsdgswps escsvkdptt sgcitprtln alkqtqaagy
      241 kryvsckreg gggehpkgra cdfsaaaggf qdknatggdk aygdslaawh vrnadrlgvl
      301 yviwyrqiwh pgtgwrsysg sgspaashtn hvhlsmy
//
LOCUS       WP_357576046             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357576046
VERSION     WP_357576046.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,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 265)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..265
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28723
     Region          15..261
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msippttdqv eqtvihvqgl eksfkqlkvl rgvdidvarg sifallgsng agkttvvkil
       61 stllkadggt arvngfdvat qaaevresis ltgqfaavde iltgrenlvl varlrhlkdp
      121 gaiaddllrr fslteagtrr vatysggmrr rldiamslig nppvifldep ttgldpeari
      181 evwqavmdla eagttvlltt qyldeaehla driailhegr iivngtldel kqllppatie
      241 yvekqpsled vfltlvgart hkeqr
//
LOCUS       WP_357576052             253 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357576052
VERSION     WP_357576052.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26524
     Region          1..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 mtdravlvtg ssrgigravv eafaasgdrv aihhrdsgda aeklraglpg sghvvvradl
       61 tdpgavramv draaellggl dvlvnnagty gdrdvphpif gtsydewqqr wrqvletnlt
      121 gagnviwcaa qhlrerggri invssrgafr gepdqpayga skaglnalgq slavalapyg
      181 itvatvapgf vatdmttehl rgergaaira qspfdrvarp eeiaaavhwl aspeaewasg
      241 tivdlngasy lrs
//
LOCUS       WP_357576075             720 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC049114].
ACCESSION   WP_357576075
VERSION     WP_357576075.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 720)
  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 720)
  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 720)
  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 720)
  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..720
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..720
                     /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=78024
     Region          38..720
                     /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 maavpdptgv dvgrggaqgf aadwaravrr igfvplsaae terllllhtv rlaqvvraep
       61 fsarpaeevg ralveahlte pralewslra lgeafpdrvl atgdrppdlg eriaavqggl
      121 aagfaralrd rtftqqeria rsawqardev eqalrdsear fravftgaai gigiagvdgq
      181 iidvntafad mlgysieelc emnvaelfha ddaagmwely qeliegkqds vrvekryhrk
      241 dgsivwtdla vsliryddgr prftvamied iteryelqqr lrfqalhdpl tglpnrtlff
      301 etlgrvfdta gpaqrvgvcf ldldgfkain dslghdlgdr llvaigrrla ecvadhghlv
      361 armggdefvi lvdggddvdd avavaeaala avaapvhlgd qqlavsasvg ivdcpaaett
      421 aselmkaadt tlywakaagr grwavydper sardlarsal vaglpaaldr gefvlhyqpi
      481 vsllegtmla vealvrwehp elgligpdrf iglaeetgli vqlgewvlrr achdaerwrr
      541 efpearlvvs vnlaarqadd paivatvada latsglpael lqleltesav mgsageplrs
      601 lhrlaalgvr lavddfgtgy snlaylrrlp ihclklagpf vegiradgtd vvadhrderi
      661 vdalvrlaha lelwvtaeav etpvqaerlr alrcdtgqgr yfgapapaee itarlrrata
//
LOCUS       WP_357576151             460 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Micromonospora sp. NPDC049114].
ACCESSION   WP_357576151
VERSION     WP_357576151.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..460
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48264
     Region          37..447
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mssaatadva saaarlrall gdrlhepgep gfdtatrlwn aavdsqpalv ahcldadeva
       61 aavrvaarch lpvsvrsggh dwagralrdg glvldltglr avrvdpdrct vtvaggasaa
      121 dllaaaapyd lvvptgvvrd vgmagltlag gygplggrfg laldnllgae vvladgrrvt
      181 adprhdaely walrggggnv gvvtelryra hrlpavlagm imfalaeapa vlrgyatlla
      241 dapdeltvma gflpgpagep vvfvcpfysg pdldagrpwl drlralgtpl vdqvdplpya
      301 dalrmfdggm vdgnhyllrt rwlptladga vdalvdaarq vtspfsalal hhfhgaatrv
      361 rlgdtafglr aehllteiia awapggevap hlawaertse alaplalpgg ypnllaptet
      421 ervrlaygan warlrrakrh ydprdlltav ptlppsehpe
//
LOCUS       WP_357576189             339 aa            linear   BCT 28-DEC-2024
DEFINITION  glutathione S-transferase family protein [Micromonospora sp.
            NPDC049114].
ACCESSION   WP_357576189
VERSION     WP_357576189.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..339
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38372
     Region          13..315
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mgeetggkyv epggeftrdq ryiatritad grdgypvepg ryrlavsrac pwanrliivr
       61 rllgledais mavagpthda rswtfdldpg grdpvlgier lqeaffkrfp dydrgitvpa
      121 midvptgqvv tndyaqmsld lstqwtayhr dgapqlypeh lreqidevnd vvfrdvnngv
      181 yrcgfagsqe aydkayhrlf drldwlterl tdqrylvgdt iteadvrlft tlvrfdpvyh
      241 ghfkcnrqkl sempvlwaya rdlfqtpgfg dtidfdhikr hyyevhrdin ptgvvplgpd
      301 lsnwvtphgr ealggrpfgd gtpppppaep vdpahtplr
//
LOCUS       WP_357576192             202 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Micromonospora sp. NPDC049114].
ACCESSION   WP_357576192
VERSION     WP_357576192.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049114
  ORGANISM  Micromonospora sp. NPDC049114
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 202)
  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 202)
  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..202
                     /organism="Micromonospora sp. NPDC049114"
                     /db_xref="taxon:3155498"
     Protein         1..202
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20660
     Region          13..196
                     /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 mtqwlaqvge lpilvlmgal glvmlfdavp llgvlipgdv ailaavgvgr patglatfaa
       61 vlagclagws lsflvgrrya erlrhsrigs wigearwsaa egilnhgggr mmvvapflpv
      121 fnallplaag glrmsyrrfl gcatlgaaaw aglylalgta srslagllpg apspllvtmg
      181 vglalafvml vgarrrfsal ag
//
LOCUS       WP_357576266             283 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [unclassified
            Micromonospora].
ACCESSION   WP_357576266
VERSION     WP_357576266.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=31339
     Region          11..254
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 magedgeggs llaisdlhvg hrgnrevveg lrpaspqdwl lvagdvgdtv advewalgll
       61 srrfakvvwa pgnhelwtpp adpvalrgaa ryaylvdacr rlgvltpedp ypvwrgvggp
      121 vlvaplflly dhswrpdgfd tpeaaleeay rtgivctdef llhpdpypsr sawcaarvae
      181 aarrlaerep glptvlvnhw pllreptrvl rypifaqwcg teltadwhlr fdaaavvygh
      241 lhiprttwhd gvrfeevsvg yprewqpraa ppalrrilpa pqa
//
LOCUS       WP_357576383              86 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YciI family protein [unclassified Micromonospora].
ACCESSION   WP_357576383
VERSION     WP_357576383.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..86
                     /product="YciI family protein"
                     /calculated_mol_wt=9236
     Region          3..>86
                     /region_name="YCII"
                     /note="5-chloro-2-hydroxyhydroquinone dehydrochlorinase
                     TtfG, YCII superfamily [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG3795"
                     /db_xref="CDD:443009"
ORIGIN      
        1 mvpryllsvy gpaeptelgt hhsreavpra yadtgafder lrrdghlvft dglapattat
       61 tvdgqggrpv ltdgpyletr ehldgf
//
LOCUS       WP_357576370             461 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357576370
VERSION     WP_357576370.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..461
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=46937
     Region          3..459
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 malsatvlae lrgivgpshv hdaagdlvay ardatplfsh rpdavvfpad taevaavlal
       61 atrhrvpvvp rgagsnlcaa tvplrggivl vltrlnvile vsgdellart qpgvtsaala
      121 daaaaqgllw apdpgsrtva tvggtiatca gglrglkygv trnyvlglea vlptgevirt
      181 ggrlwkdvag ydltrlltgs egtlavitea tvallpapas antgvayfpt ladageavar
      241 viragvvpat lefldracid avedfahlgl rtdagalllf gddgppdlva ahlerigaac
      301 veagavevtt arevaqaeal laarrcalpa lsrrggvtil edatvprpri aemvdridai
      361 aarhgvaiat fghagdgnlh ptcvldsaed hdavrraeaa fadvfaaaid lggtitgehg
      421 vgaaklpfla arlgedqlal lrriksafdp agilnpgklg s
//
LOCUS       WP_357576390             341 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [unclassified
            Micromonospora].
ACCESSION   WP_357576390
VERSION     WP_357576390.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 341)
  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 341)
  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..341
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..341
                     /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=34541
     Region          3..339
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mitlrtggls lrlrpravav gvtcvllala lgmlaigsgd ypmspadvlr altgqgtpae
       61 efivtelrlp rvvtalcvga alalagavfq slvrnplgsp dmlgftqgaa tgalvvvvlg
      121 gssvalassa vvgglvtgal vyalswrrgv hgyrlilvgi gtmailtgvn gwlltraplm
      181 daaravlwlt gsldgrgwsn alpllialgv lvplmlagyg pamrlvemgd dtaaalgvrv
      241 erlrlvvlaa avllvslaaa aagpvnfval taphlarrlt rapgpnllps aavgavllva
      301 adqlalrafp ghqlpvgvvt gvlggaylvw llaterragr l
//
LOCUS       WP_357576424             334 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Micromonospora].
ACCESSION   WP_357576424
VERSION     WP_357576424.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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 334)
  AUTHORS   Rosinski,J.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..334
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..334
                     /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=35454
     Region          261..326
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlkiyfsaed ilrtrvapaa dpvwelvlsl hllpgrgrdp llagwrrsvt qglrevsdsa
       61 glrllltlnp prgyfpdflt pyesvsgfda gmeavrstpt allqrdlall aansalpvga
      121 galargepdi lrgltgamer yrglaidpyw triqaavead rarraralld ggvegllasm
      181 rpamrwedgv leirdyphsr elhlggrgll lvpsffcaat pvalldpalr pvlvypvdrl
      241 gglltasgeg ggpgasdpgr ealaallgrt raavlaasdd gcttgevarr lnisaaaasq
      301 httvlrnagl lvsqrdrntv lhtltplgra mlns
//
LOCUS       WP_357576514             631 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF262 domain-containing protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357576514
VERSION     WP_357576514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 631)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..631
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=70997
     Region          14..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"
ORIGIN      
        1 msltvsatev lrprllsipn yqrgyaweqe qvqdflddls llepgkthyt gtivllggge
       61 plvddesnal vradvvdgqq rlttlcllln elrralqvag redaaqglrr qfllisekgv
      121 prnklqvgpd svavwtalln dtpvpppetl sakrlqraal qirqhveela sksddhvdal
      181 fslrnlvvtg lhftlytlnq qaevgvifet lndrgkplte lekvknyllf laarlpigqq
      241 ealadrinaa wstiyrllle vamvspaged qflrahwlaa vdpvptrwrg tkslkahfpr
      301 qqylgkpell ireigdyvds laraarayad slrpkiqafa dfgplaskar saherlsrag
      361 tvavfqplml alrerspgdg qtylkvldlc erfavrtyli ggyradaaqt rlyrlahevy
      421 igkrtpssve talralaldy andtyvrqsl ldtefnwyrw galkfflyey elnllggatp
      481 einytffeks krektiehil pqaanssywq krfdrnerrq lthalgnlvl trdnsaysnk
      541 dfpnkrgaag pgiaatacya qaplaqeqel arladwtpee vlarqerlad walkrwaidf
      601 sdfdlgiele deedpsddpa dpkpadlimn e
//
LOCUS       WP_357576537             184 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357576537
VERSION     WP_357576537.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 184)
  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..184
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..184
                     /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=19925
     Region          4..140
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtplrlavii gstregragd rigrwfvdra rrrdevavtv vdladhdlpa scpaeptpai
       61 gsfvaqvara eafvvvtpey nhsfpgslkq aidhaydewq akpvgfvsyg cgsiglhave
      121 qlrtvftalh tvtmrdvvgv dlldgapspp tadrceraad vlldqlhwwg lalregraar
      181 pyvs
//
LOCUS       WP_357576555             474 aa            linear   BCT 28-DEC-2024
DEFINITION  argininosuccinate lyase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357576555
VERSION     WP_357576555.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Baruteau,J., Diez-Fernandez,C., Lerner,S., Ranucci,G., Gissen,P.,
            Dionisi-Vici,C., Nagamani,S., Erez,A. and Haberle,J.
  TITLE     Argininosuccinic aciduria: Recent pathophysiological insights and
            therapeutic prospects
  JOURNAL   J Inherit Metab Dis 42 (6), 1147-1161 (2019)
   PUBMED   30723942
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Erez,A., Nagamani,S.C. and Lee,B.
  TITLE     Argininosuccinate lyase deficiency-argininosuccinic aciduria and
            beyond
  JOURNAL   Am J Med Genet C Semin Med Genet 157C (1), 45-53 (2011)
   PUBMED   21312326
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415011
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..474
                     /product="argininosuccinate lyase"
                     /EC_number="4.3.2.1"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004056 - argininosuccinate lyase
                     activity [Evidence IEA]"
                     /GO_process="GO:0042450 - arginine biosynthetic process
                     via ornithine [Evidence IEA]"
                     /calculated_mol_wt=52246
     Region          1..455
                     /region_name="ArgH"
                     /note="Argininosuccinate lyase [Amino acid transport and
                     metabolism]; COG0165"
                     /db_xref="CDD:439935"
ORIGIN      
        1 mhdeilrpqf efdmthllph ylavevvlll eyermgvitg eqrrdiadrl gridestlsa
       61 dpatnmsdts maieqwvhgq ltepvpawhv drsrndsqat ahalaarewl ggaaedllgl
      121 geavhrlang ttdllmpgyt hlqaaqvitp gfylaalsqq ilhnlrrwla tydgndlspl
      181 gagsmagqql pwdrhrmahl lgfagpvpha ltavasrsla lemmaefsil gaelsrfvtd
      241 lmtwgsneya fidlpdelsg isaampqkkn fpilerirgk lahlgafgvd ivlaqrstpy
      301 snmvevskea tanlhvsvst trtalrlfst vvdnlrfrsd rmreacrrey lgafalandl
      361 tlndgipwrd aqivvgqyia aaissdipph pgdpgllvev agrhgyqvsd aarvladafd
      421 iekairgkrs tgsvnpqela dllasqadef rllrqqwddr rerrgsaral lgrr
//
LOCUS       WP_357576569             452 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576569
VERSION     WP_357576569.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 452)
  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 452)
  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..452
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..452
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50131
     Region          11..258
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mtartndave lsvviptyqd aqclaltlra ltrqtvsper fevviirdgg spagyadave
       61 aatgldlrll efprrrgrsa arneavrhtr aplllfldad syaspqller hlahhavagr
      121 pavlmgrrde lslehveaal dggemtdvpr rradragdlr fphgqppgpe wlragwalay
      181 thnislardl fdraggfder sglrwgledi elfyrvhrhl gvtelnfafd dearafhlph
      241 hrntdrnwsd faanrslltg qyhviewefy glldvydsle rivyyrsaat dcarrstcri
      301 gpafdrladr lpgprvlwvg tgsdqvdlpt galtfdyaap pgptnyhlvg vdppiapasl
      361 davvsvdfwr ylrwddlcrf vntsgrlare vhlvgtgdtg sapltpgpav ldylrrtlsa
      421 afatrlthvd glgevltlrp lpatarrspa rv
//
LOCUS       WP_357576575             259 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576575
VERSION     WP_357576575.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28301
     Region          57..180
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mpldpvahnr tawdrqveqg newsrpvsse ttararagdw svvligyqpv drswfpadla
       61 gtdilclasg ggqqgptlaa agarvtvfdn sprqleqdes varrdglelr tvlgdmrdls
      121 afpdssfdlv fhpvsnlfvp elapvwrecf rvlrpggtll sgflnpdvfl fdnealdqrg
      181 elvvrhrlpy sdlthvpaae rerlwgadap leyshtmtaq iggqlaagfv ivgfeeaphh
      241 sdatagwlpg yfatravkp
//
LOCUS       WP_357576620             165 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576620
VERSION     WP_357576620.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 165)
  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..165
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..165
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17374
     Region          <25..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msllrrvigg vlrrlrlrqg rtlrevadaa gvsvpylsev ergrkeasse vlaaicralg
       61 ihlsdlleea rddlrrvepr ipaapragla rleraevgrp davtpavrva praggpllhl
      121 aprpggttlr vgrpasavgg rsgprtrval gcgrtragar tltvv
//
LOCUS       WP_357576629             246 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576629
VERSION     WP_357576629.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 246)
  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 246)
  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..246
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..246
                     /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=25803
     Region          1..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 msplavvsgg trgigltfsr rlvklghrvv apyrgdavaa asaaaelgaa fhpvrldvgd
       61 aaavdaavet vlaehgpptv lvnnaginid rpflemsted wrrvldtnls gvfhltrafa
      121 pamlaagrdg vivnvgattg irprrngvny caskagllql tkclalelap rirvnclipg
      181 mtetdelvtr frlddpaara avvaeiprgr igtteeiada leflvgpasg yltgqklivd
      241 ggqfmw
//
LOCUS       WP_357576650             234 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357576650
VERSION     WP_357576650.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..234
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25050
     Region          6..223
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mvsgppkavl fdvgmtlvha dgeflvtels aegitglpie lataamvtsf parhlplprg
       61 rdyvdktglt laalldipqa eacralrrvf arpdlfrlld pdaipaltal rhagvrlgvi
      121 snsdggldee ldsygllgff emvldshdig tekpdpkife iglermgldg sdcwyvgdnl
      181 indiigakaa nfaetvmydr friyghipgt lhidalsqlt plvlegtsva agrp
//
LOCUS       WP_357576704             702 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357576704
VERSION     WP_357576704.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 702)
  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 702)
  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 702)
  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..702
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..702
                     /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=74954
     Region          15..701
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mtdldldlda dlaaerehla tsraalaqmr eraqalfstg dqvagdayaa etlgrtlarr
       61 vaeladdptt plffgrldfg attgappadd ppggpgdgpd gwhadhagrr yhvgrrhvtd
      121 drgeplvldw rapvsrsfyr asardpqgva vrrrfgfssg altsfederl drgeelgtts
      181 riltaeierp rvgpmrdiva tiqpeqdelv radladsicv qgapgtgkta vglhraayll
      241 ylhrerlrrs gvlivgpnra flsyiaavlp algeveveqa tvedlvgrvp vravedpava
      301 aikhdarmae vlrravdahi geptepimvs dgsfrwrigl dplhrvvqet rrerlpyatg
      361 rervrarvva llqrqaearr aespsdawlr rmgkatpvta fldavwpalt peglvhallg
      421 dpqrlaaaad glldaeeqar lcrlaapagt klgrtpkatk wtaadavlid eaaglierpg
      481 gfghvvvdea qdlspmqcrv iarrsehgsi tllgdlaqgt apwaaadwre slrhlgkpda
      541 vvvpltvgfr vpaavvafan rllpalavdv ppaeslrrdg aldvrtvddl aaatvaevra
      601 alafdgsvav iaaddavggl raaleaagvd tatvdepaaa arvtvvpatl vkgleydhvi
      661 vvepaaivaa eprglhrlyv vltravsrla vlhtrplpap lg
//
LOCUS       WP_357576795             289 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576795
VERSION     WP_357576795.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..289
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32018
     Region          9..75
                     /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 mterdgsiev gralralrrg adlsqrelar rsgvpkstva rieadpgadp klrtverlvr
       61 aaggelavrv rtadqgttdg gpgtgvalpp vpheerrdeg grrypahldi revrtlkdwp
      121 aawwghwyvs paqwpvrvpe rtydlyrgrr derrvrerar aavrfrrvte gvpdgcwrlv
      181 avlpggelvg elrahersed lllgedlgdq relvldgvlv apqlrflgig rrllgllgde
      241 ldragirtvr aiagisgvgg adflvacgyq veasrptalr fdrrpvhrr
//
LOCUS       WP_357576842             275 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576842
VERSION     WP_357576842.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  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 275)
  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 275)
  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 275)
  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 275)
  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 275)
  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..275
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..275
                     /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=28290
     Region          9..252
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtkpapgaav vtgaagglgr aiaaalhadg wpvlltdhdd qavaraaapl ggwsrrldvr
       61 dsdacaavaa eaagrgglgl wvnnagilvt gpswehdaat rrrvvevnal gamngtlaal
      121 avmreqghgh vvnvvslagl vaapgetvya askhalvafs igtladlrla ghrgvhvscl
      181 cpdgiwtpml hdrlddpgaa asftgtlltp ervarraarl arrprpvvsv prwrgaqvrl
      241 ldalpgvavr laplilaagr agqrrqrrri gagpr
//
LOCUS       WP_357576857             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576857
VERSION     WP_357576857.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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..191
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..191
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20053
     Region          45..183
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mnarrltagl laavvsvala gcssrdgeea cdnsggiiec apdqrsaapk lagelltggs
       61 hdvardrgqv vvvnfwgswc apcraeaddl entyqatkgs gvtflginiq dqrdkalafe
      121 esfkvtypsl fdppsrlala ldippntipa tvvldrdgri avviraavkq eglqpiveri
      181 aaekpapngs r
//
LOCUS       WP_357576866             405 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357576866
VERSION     WP_357576866.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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 405)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..405
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45029
     Region          24..>189
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
     Region          43..343
                     /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 mhftsedfav shksnldann gaviqlfvrw fkpdlppsrp rqpvlmvhgr sspglvsfdl
       61 eydageggys warelaedgf dvfvmdlqgm grstrpvqmn dpcninplqq hlllprepca
      121 arypkqltns asdwaelgtv vnwilgqpdm ppkvdligys agayavgpfa mtvdpakvas
      181 vlllapifav tgpstpptlp vsspcpvygf pmhivhkagl rkswdsevdv eprypgqrdd
      241 ahgivdvvwd aflandqlgr twgpgvsrfr ngfwwgwnqe rvtadhtnlg ekvpvlivyg
      301 qkdatannia lnfsvpelyr siqgrhklmy rldgtghlvv werqrtwlhk lsskwlrsar
      361 hpnrpynvdg nttgtfvvpw egdpvemdya sgrteqplaa plepm
//
LOCUS       WP_357576876             227 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576876
VERSION     WP_357576876.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 227)
  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..227
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..227
                     /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=23745
     Region          12..224
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mppsvdsaaa pprghrvrqt iaqlrerilg gewpvggrip tepqlvaalg vgrntvreav
       61 ralvhagvle crqgsgtyvv stdelapvva rrltadrmae vvevrrafev eaarlaalrr
      121 ttedlaaldg alaareaawr dgrfdefvaa daalhtavva aahngmlael yasvgaalhs
      181 tiaqsmggal epdryvdhsr lveairagdp graaieagaf lepspga
//
LOCUS       WP_357576888             353 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357576888
VERSION     WP_357576888.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 353)
  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 353)
  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 353)
  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 353)
  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..353
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..353
                     /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=37917
     Region          1..352
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msrlgvgvig vgsiaemhlg ayaanpdvhl vgvfdvnqer saqkaetfgv trvhptldsl
       61 ladpeidavs ictwndshae iataaldagk hvlvekplsr tageaealve aversgrhle
      121 vgfvrrfgan akvlksfvda gllgdvyhar atnirrlgnp ggwfadhkrs gggplidigv
      181 hvldlcwyfm gtpkavtvsa vthtrlgnra nvtslsrykv adydptqsdv edfatalirf
      241 dngasltlet syslhaledr levavfgerg gaelepklri atemhdtvln vgpqidhlsf
      301 dfaegfanei ahfvslclge aeqvapvshg tevmrmldgi yesaraghei rls
//
LOCUS       WP_357576914             510 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CpaF family protein [unclassified Micromonospora].
ACCESSION   WP_357576914
VERSION     WP_357576914.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 510)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..510
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55962
     Region          83..482
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvsgdp rrqppgatst applappngr hhplplpvpv taprpepppr prvdfqvvre
       61 lrrelserla lwqrgreftv deedterarl avtvvaeyad avrragtpma ageerllldq
      121 vtaelaglgr lqtllvddti eevhilgcdq vrvtrhgggv dwvepiadsd delveilqaa
      181 arragaters lstskptldl qlpdgsrlaa vflvshrpya virkhntldv slddlaggrg
      241 dldemidplv rdflrasmra glnimvagla gagkttvira lmdeipadep yvlleesrel
      301 lparrrlkhr avmsfeareg hgergadgrp agevsiadli pvslrmgvlr iivgevrsre
      361 ivpmlqamtt srgsmctiha rtpagvseri ielalahgre mtvdqarrma gnaldlivyv
      421 tvedetaigg rkhrfvshve evigvgdgnr itttqvfgpg pdgravprhl pervraqllr
      481 vgydarllsr wieagtgawr rprqtrlgrr
//
LOCUS       WP_357576904             239 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576904
VERSION     WP_357576904.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 239)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..239
                     /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=25867
     Region          9..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          75..226
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 maeqaetlrr aplsrdrilh aavaladgag ieslsmrnla qdlgvvpmal ykhvankdel
       61 ldgmidvvvg eidppvpdad wkhavrsril sarqvlrrhp waplaiesrn matpavlayl
      121 dsvvgtlrag gfsadlahhv mhamgsrilg fsqelfdasr ragrsgtass eppqafppev
      181 aarfphlaei staashddas vvgqgcddqf efefaldlll dgierlrqqn wtsprsvir
//
LOCUS       WP_357576948             227 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357576948
VERSION     WP_357576948.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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 227)
  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 227)
  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..227
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..227
                     /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=22982
     Region          24..227
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrirsmvavl ataaagllga ssgalaapag pqpiiggstv ssapwaaavl sngsftcsgt
       61 iiapqwvlta rhcvsgtmsv rvgsvyrssg gqtrtvsasy srydlallrl sssvstsyvt
      121 lansnpplns tnsiygwgmt cysgcsastq lktasvrvts nsatdayggq airstringn
      181 awrgdsggpq fyngaqvgva stadgqsiqn ygsvaynraw itqtagv
//
LOCUS       WP_357576975             882 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576975
VERSION     WP_357576975.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 882)
  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 882)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 882)
  AUTHORS   Rosinski,J.A. 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 882)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..882
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..882
                     /product="helix-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=94349
     Region          <17..880
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <813..873
                     /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 mpdamissta qigrrwplvg rdpdidrtid rllapegrav lvtgptgvgk srvleavlhr
       61 cvakghhvlp angtmtdqga plgvarhlap qvepldtapa galhrliesl prptgqhlvv
      121 lavdnvsgld eaaarlvgkl aseqrvrvll aaaetaigtg pvdvlrrtvr ldrvdlapld
      181 wqhtrqlisa afgtdvdglt adglwrltgg nplllrellr navendaltl hdhvvgwrqg
      241 tvvrawagda ltgpleslst eesaalryia ygdgapvdvi ehlapmsvie rleelglirl
      301 dpsdpstpvt vahpltartv rtrtgllrar rvhaelvaal eatgspdrvr dvlwrlaarf
      361 evpddevlra saeallghda ataeqlarqv hgpaaawhlg rallargshr saerwlaeay
      421 rnltdpaara naaalravnr cwgidepdsa lrmiaearaa lpadvhadll aadafvmafg
      481 gpaaeaadav dqlsqhpprd pllagvvppl rprllllggr peravaefpt dlsgkpsiwp
      541 amrallqath vqalimagav rqaadlvgrh yrdavehgtp dgvatialag gicayyqgna
      601 gqaarwlrea raltaervgf rfretllaig vgveaqlgqv ekaqellsrl rrgatartas
      661 dygafgevwa lvisgnrtga atllrrlaae aaragdllma teflhvevrl apsaaaasrv
      721 relaaktdgr lfallaehae alarrdarvl nrvsatfeel gyrgfaleaa angamfgggr
      781 vtnalarrtq rllgehqgtw pewlpeprta paltdrerqv selaatgmdt paiaraltis
      841 artaenhlhr aysklgihrr helaralaed gfvlptiarq vv
//
LOCUS       WP_357576965             771 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357576965
VERSION     WP_357576965.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 771)
  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   3  (residues 1 to 771)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 771)
  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   5  (residues 1 to 771)
  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 771)
  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 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..771
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=84330
     Region          2..746
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mdrlaetesi falgngwvgw rgnldegtpy gmpgtylngf herreldype dgyafpqfsd
       61 tvisapnaal irlwvdgepl dvrtgtlrth ervldlragv verhtewisp aghgvrvrsv
      121 rlvslprrpv aavrwsvepl dgtvevrvca dllanervpe raddpraasv itdpltaeyr
      181 hsdghdgvlv hrtghsgqrv avavahdvha pdgfapgvdc tpdrlrltlt gtlragerlr
      241 ltkfaayect pvdglppqel arlvvaeada araegfeall tgqraaldaa wqtadvqldg
      301 ddelqqairf svfhllqagr adgdrtipak gltgngydgh vlwdtegyvl pvltyldppl
      361 arsalrwrha hlpqareraa elrltgatfp wrtiggrecs gywpagtagl hlnadiadav
      421 lryaaatgde eflagpglel lvetarlwhg fghwsdtgtf hlhgvtgpde ysalvddnvf
      481 tnlmarrnlr gaadaaerhp eaaarlgvea aevsawraaa davfvpydrk rgvhqqsagf
      541 teqpewdfad tseddyplll hfpylelyrk qvvkqadlvl amqrcpgeft adekarnfay
      601 yeartvrdss lsaspqavla aevghldlay dlfaesvlqd ladlgdktgd glhlaslgga
      661 wlalvqgfgg lrddrgvlsf dprlpaaidr lafhlrwhgh rlrvtltsde aryelpdadp
      721 etgievwhhg eplrvtgagp vtrpmpevpd pgpeppsppg rrptrrsagd h
//
LOCUS       WP_357577014             619 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577014
VERSION     WP_357577014.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 619)
  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 619)
  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 18791949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..619
                     /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=61561
     Region          11..619
                     /region_name="COG4935"
                     /note="Regulatory P domain of the subtilisin-like
                     proprotein convertases and other proteases
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:443962"
     Region          124..375
                     /region_name="Peptidases_S8_PCSK9_ProteinaseK_like"
                     /note="Peptidase S8 family domain in ProteinaseK-like
                     proteins; cd04077"
                     /db_xref="CDD:173790"
     Site            order(127,130..131)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173790"
     Site            order(155,187,246..247,274,337,340)
                     /site_type="active"
                     /db_xref="CDD:173790"
     Site            order(155,187,340)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173790"
     Site            order(289,291,314)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173790"
ORIGIN      
        1 mglprrsvlv gvaalamvat atpamaaepv gtiraaggat avadsyivvf kdssvarssv
       61 gdtaqrlvgr hggavartyg aalrgfevrv daraaariaa dpavayveqn htvsiagtqt
      121 nptwgldrid qralplnssy typntasnvh ayiidtgirf shsdfggrav sgydavdggs
      181 addcnghgth vagtvggsay gvakgvqlvg vrvlncqgsg tnagviggvd wvtanavkpa
      241 vanmslggga nttldtavrn sinsgvsygl aagndsggna cntspartae gitvgsttnt
      301 darssfsnig tcldifapgs sitsawhtgd tatntisgts matphvvgva alvasanptw
      361 tpqqvrdylv nnatsnvvtn pgtgspnkll yvvngdtppp tndfsvsvsp tagstapggs
      421 vtatvatatt ngsaqsvsls asglpsgata sfspatvtsg gssaltists astpagtysv
      481 tvtgtaasgs rtatysltvt gtgggcsgtn gtdlaipdtn vavsssivia gcarnassas
      541 tvavnivhty rgdvvidlva pdgssyrlkn sswwdgadni nttytanlss eaangtwqlr
      601 vrdvysgdtg ylntwtltl
//
LOCUS       WP_357577045             258 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577045
VERSION     WP_357577045.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  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 258)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..258
                     /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=27382
     Region          2..199
                     /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 mrvlvtgagg rlgrvvlprl raegwdvrat grrartgswv vadlatgegv veavagvdav
       61 lhlasapnrg rqthrvdvlg trrlvvaagq agvrhlvyvs ivgvdrvpip yyrhklaaeq
      121 vvvagtvpwt vlratqfpef ldamlrgasr lgpvigdpav laqpvdpgev adrlvrrlta
      181 gplhgieeyg gpevlrfdda arawtaarrs rrpllpvrip gaigralrsg glvteatpkg
      241 vrtwvdhlad tyggtgar
//
LOCUS       WP_357577107             430 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577107
VERSION     WP_357577107.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..430
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46324
     Region          14..424
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mggapadtgg tdeapaavve avfreergrl laalvrrfgd ldlaeevtse aveaaltrwp
       61 vdgvpprpga wlmttarrra vdrlrrdqal aarlailqae adraepapdp mpggelpder
      121 lqlfftcahp alaaedhgal tlrylagltt pevaraflvp tatmakritr akkkiheari
      181 pfrvpgaqel pqrlpgvlqa vysiftegya asegprlqrl dlaeeairla rilhrllpag
      241 revagllalm lliharrdar tgpddelvll deqdrgrwdr rmiaegldlv pvalaggppg
      301 pygvqaaiaa lhveaadlat tdwpqivaly dvllalapsp vvalnraaav amrdgpeagl
      361 alldeladep llrghhpypa aradllhrlg rhadaaeayr eafglagtep erallrrrld
      421 aierlrapgt
//
LOCUS       WP_357577132             429 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577132
VERSION     WP_357577132.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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..429
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..429
                     /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=46628
     Region          73..393
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mtsspqapir vetadagsrp sltvlsgfwp aatfavartl laadpslllv rhdlagirdg
       61 vvrrvvrtgt givederial ahgcasctlr edvlptlvrl trdnpgqdlv lllpevvepe
      121 avaaacahhl vdgtpvtdli qvdsyvtvld aehlldglas tddlatlgiq aaeddhrgla
      181 dvvvrqieya dtlvlwgrsr egefdtgria vllqrmapwa ahfrvdgdlv dadaltrqlr
      241 hthrhrpetp gvlarglqgf algthepead cgvvsavfra rrpfhprrlh dvledvnadv
      301 irsrghlwla sqpdtvvawe faggglamgs lghwlvslpe pgwehvcdqr rlaaalewdp
      361 yygdrhqhlv figldvdpve lhrtladcll tdaeladgee fwrtyhdpfa gcfplgvaep
      421 tdtggarpa
//
LOCUS       WP_357577145             543 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357577145
VERSION     WP_357577145.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 543)
  AUTHORS   ter Beek,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 543)
  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 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..543
                     /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=57014
     Region          1..507
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 midfdrvtvr yaesdrptlr dvtlridege lclvvgrtgt gkstllrain glvphftggt
       61 lhgsvtvdgr dtrrhpprdl advvgvvgqd plsgfvtdtv eeelaygmeq lalpatvmrk
      121 rveetldllg iaelrdrplr tlsggqqqrv aigsvltahp rvlvldepts aldptaaedv
      181 lavvtrlvhd lgvtvvlaeh rlervvqyad rllylpgdgr vvdgepaavl advdiapplv
      241 elgrlagwtp lplsvrdarr raaalrhrlv daavpaaatv pagppvltar avvvrypgtv
      301 avagvdmels pgrivalmgr ngsgkssllw avqgsgprqg gtvavvgaqg tvdpkalppg
      361 rarrhvglvp qtpgdllyle tvegecdqad retgapagtc ramldqltpg lpadrhprdl
      421 segqrlalal avqltaappv vlldeptrgl dyrakrqfta vvrrlaadgr avliathdve
      481 lvaaladqvv vmaegeivaa gttaevmlas pafapqvakv lapapwltve qvtaalattg
      541 apg
//
LOCUS       WP_357577161             436 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577161
VERSION     WP_357577161.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 436)
  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 436)
  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..436
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..436
                     /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=44948
     Region          84..>410
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mpsddsfasr ppaglsrrqv mawstlvaaa aplglvgrga paaagespde tyqrvfleal
       61 aadpdlrrha vagreflyrp rqllvahpdv qrvvgrlrsy ghpvtegvgf ggvarllfat
      121 etdipsvvtr lrdpqqwpgq pvplvqphha llgfgnimgn pggpprvaaa lptpdparag
      181 egagvtvgic dtgiwrlags rhpqwlagsy lpevddedal yvgadvlalq gghgtfvagv
      241 vrqaapgvrl dpeaalnatg vgdeemlvaa lgrlgpqvsv vnlslgyftq ddqpplplvn
      301 alaglpgrav vasagnagts rrawpaaldr vlavgavsag atgpvpasys sygswvdaca
      361 lgdrtstyvr grlqlpgqpi ryfdgfaawt gtsfatghva grlaalmtsa glgaeaaraa
      421 lvagprwhpd ygvlva
//
LOCUS       WP_357577162             876 aa            linear   BCT 28-DEC-2024
DEFINITION  CHAT domain-containing protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577162
VERSION     WP_357577162.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 876)
  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 876)
  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 876)
  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 876)
  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 11419075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..876
                     /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=91893
     Site            order(49..50,53..54,56,81,84..85,90..91,93..94,119,
                     122..123,126..127,130)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          49..73
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          51..>231
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          79..112
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          117..146
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          158..181
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          198..853
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
ORIGIN      
        1 madstvpgav qaqaaldavq rypreaiaia rqvlaaghpd aderstaera iglalrelnd
       61 lpgalrhlrr avrvtdspra ralarmslgy vlanagrtga alravtlalp rltgadagra
      121 rmqrgvvlhy rgrfdeavrd ygiaveiaqr egdllleara rnnrgllnah rgtsrdaddd
      181 lfrsaaifsr lgldlaaada rwnigiaagq rgdvagalrs fatvgdeyrr lsvprpalll
      241 drfelllsvp lvdeavevat savtelrrrg masdlaeall araraallag dldtaaaaaa
      301 ssrarfrrqg rriwaafarh velraefarg trstallkam vrtagqldat gwpspalttr
      361 ieaarlaeam grpalaaell avaarahrrg taphraqgwy alalrrrldg dlrgaaralr
      421 rglgvldghr aslgatelra hsgayghela aegldiavrt gtpaqvlawa erwranalrm
      481 ravqppqdpe laaalaelrm vstaledall aghpgyalrr sqgrleqrir elargahgga
      541 rgadggdlva pptvaalaaa lgdavllelv ahgprlravl vrdgrtslhd lgpldealgr
      601 arlhrfglrr lvttgdsasa ragvefatta ldqqlfdpvr rllrdrplvi vpiaalhavp
      661 wsglptcagr pvtvapsatv wlravgrivp agppvlvagp rlpaaetevr qlgaalpgsr
      721 pltgcaatad avtdalngag lahiaahgaf radnplfstl eladgpltay elerltrppg
      781 cvvlsacdsg lsgvrpgdev mgftavllal gtrsliatvl pvpadlttal mldlhrrmra
      841 gappavalae aqrafgtagg gaahataaaf vcfgag
//
LOCUS       WP_357577170             532 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 64 protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357577170
VERSION     WP_357577170.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Wu,H.M., Liu,S.W., Hsu,M.T., Hung,C.L., Lai,C.C., Cheng,W.C.,
            Wang,H.J., Li,Y.K. and Wang,W.C.
  TITLE     Structure, mechanistic action, and essential residues of a GH-64
            enzyme, laminaripentaose-producing beta-1,3-glucanase
  JOURNAL   J Biol Chem 284 (39), 26708-26715 (2009)
   PUBMED   19640850
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Rutenber,E., Ready,M. and Robertus,J.D.
  TITLE     Structure and evolution of ricin B chain
  JOURNAL   Nature 326 (6113), 624-626 (1987)
   PUBMED   3561502
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19012040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..532
                     /product="glycoside hydrolase family 64 protein"
                     /EC_number="3.2.1.39"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55766
     Region          35..391
                     /region_name="GH64-LPHase-like"
                     /note="glycoside hydrolase family 64:
                     laminaripentaose-producing, beta-1,3-glucanase
                     (LPHase)-like; cd09216"
                     /db_xref="CDD:185755"
     Site            order(149..151,153,158..160,162,164..165,299..300,365,
                     368..369,378)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:185755"
     Site            order(149,165)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185755"
     Region          405..530
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cl49609"
                     /db_xref="CDD:483949"
     Site            order(420..422,433,435,442..443)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467330"
     Site            order(461..462,474,476,483..484)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467330"
     Site            order(504..506,517,519,526..527)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467330"
ORIGIN      
        1 mklrrrllaa vsalvaavpv tlaaapahav gpallpvtvt nstgrgeavh lyvigvqlss
       61 grlgyvnqgg tfvpwsggql ppspapdasi pgpgnggstt irfprgfsgr vyfsfgeklk
      121 ffltpdglvq papwaagdan rdilfdwsef tyndaglwln ssqvdmfavp havtvtgatg
      181 vtkrtgdvva ggrnaiiegv rsqpgwantv htrsdgtvlr vlapgkaaga glfsatylds
      241 yiasawnayt trtltvvpfa dqpntryfgr tsgnvmtftn sagqvvasfn rpssasvwgc
      301 dgdlpapndp vvgpisrtlc aalnrgtlgt idtqpstdaa qfyrnnptnh yarvihanmt
      361 dgrayafafd dvgafeslvh dgdpraagiv lspfgagsgg pgnpgtgvpv lsnwnnkcid
      421 vpssnfvdra qlqmwncngt aaqkwtftgd tlrsqndkcm dvdngatgng avvqlytcng
      481 tgaqrftlta agdlvniqag rcvdirdwns adgaklqlwd cagtanqkwr kg
//
LOCUS       WP_357577269             301 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [unclassified
            Micromonospora].
ACCESSION   WP_357577269
VERSION     WP_357577269.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  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 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   3  (residues 1 to 301)
  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 301)
  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..301
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..301
                     /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=31025
     Region          1..301
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mvrfglfgtg hwaaethaaa lhahpgvafa gvwgrdprka aalaerygvp afddadalid
       61 acdavavalp pdvqagiavr aatagrhlll dkplaltvad adrvvdaaqa agvasvvfft
      121 gryrpdvaaf lastaavggw htaralwfas ifqagspyga spwrrehgal wdigphalsf
      181 vlpvlgrvtr vaamdgpngl vnlllthdgg atstvsltld gpqeavaref vfygengvet
      241 apagqgdaat algvaidqll eeigsgtrdh rcdvrfgrdv vavlaaaeta raegrtvdlp
      301 s
//
LOCUS       WP_357577273             979 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577273
VERSION     WP_357577273.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..979
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..979
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=104958
     Region          <2..938
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mrfsspvvig rdaeiravda rltatrassg gtifligeag igktrlaehc ahaaaeagme
       61 llrgrssstg pivpfrplte aifslsrtgr lpdntelapy rpalarlvpe wrdpavperv
      121 ssivelaeav lrlvtavagg rgcvliledi hdadaethav leylvdnlad lpillvatmr
      181 pgsgpatela waaavrrsat vvelrpladq evhelaaacl ntdalpaelt drlvrdsegn
      241 pfvaeellns migaralvrd gdgwrftddp aialpntvtl svtrrlagld pqartllhta
      301 avlgrrfpva alraatglee ramlshlrsg vdvevvmpdr stpdwysfrh altadailat
      361 ltpaersala kraadalesa yaglpghwcq laaelrqtag dnhaagllfa eagrralgdg
      421 attsavtlld rayqlmsdpp dpearagile sllnalaeag hanrafalvd datwvnavtl
      481 gveqhvsirt rlawvavttg rwsdgasqvr iaravlgssp ppgpaarvdv veahlifgdg
      541 dgcgrttqae qlvlqalava ervpmaetac qalqllamia rsrsfdeaes yltrmlaiae
      601 ehrlplwrin alfrlgvnqs mrtgeqtllr qaeqaaqlsg aimigqsieg vyairavmqg
      661 dyptgdelaa rcaaatarlr niddqqfalv taaasaahrg rrrlmeqrle efravggges
      721 ghvplaygfc eavcalleed rpaairaldl araweddhpn tyymtgrfgl rplldalags
      781 ldrtgmeava lapgatlrwn rqflhlakav vygragqrer aatevalale aaapyrmsyh
      841 lglrlvaeaa ladgwgepva wlraaedhfh nvdapviaga crgllrqaga slgqrrsghd
      901 riparlravg vtvrehevlv llakghdnqd lasllhlspr tvekhvasll lktghanrrt
      961 lrdnvdellg pdsrsgsrr
//
LOCUS       WP_357577295             381 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577295
VERSION     WP_357577295.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..381
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41113
     Region          3..369
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mqeallrslt pgvlgilvrr gadfaaaeda vqdalveavr twpadpprdp kawlvtvawr
       61 rfldatrada arrrredlvd eepapgptpt vddtlqlyfl cahpsltpas avaltlravg
      121 glttrqiaqa ylvpeatmaq risrakrtvs gvrfnqpgdv atvlrvlylv fnegysgdvd
      181 laaeairltr qlavaiehpe vagllalmll hharraarta pdgslvplaa qdrgrwdtts
      241 iaegveilqa alardrlgef qaqaavaalh adaptaeetd wvqivewyde lvrltdspvv
      301 rlnravavge adgpraglaa laalddslpr haavaaylhe rdgdlataar lyaeaarkap
      361 nlaerdhltr qaarlnarrr a
//
LOCUS       WP_357577291             372 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD-IIIC family phosphatase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577291
VERSION     WP_357577291.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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..372
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..372
                     /product="HAD-IIIC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39408
     Region          68..371
                     /region_name="FkbH"
                     /note="Predicted enzyme involved in methoxymalonyl-ACP
                     biosynthesis [Lipid transport and metabolism]; COG3882"
                     /db_xref="CDD:443090"
ORIGIN      
        1 mtsgwegsav givdtaasra ladlvgglry dleqvahhtg ptagtaadpg prcahrlpag
       61 ssprhpehal drrgvlhava srgeraaata hlaahglldl ftrvevgwga kslavtriaa
      121 dlgigldtva fvdndpvera evaaalpvvr chpadavaal palpefaref vteesrqrrq
      181 lyrtderrra aeathagppa dflaslglvl evrragpadl araheltvrt hqlnttgvtf
      241 slaelralca sprhevlvar lrdrfgsygt vglavtelrp dasvlrlllm scrvlsrgag
      301 aalldhlvht alaagrrpva efvptavnrq mlvtlrfagf aveddagdrw tlaidparpp
      361 tarahpvrvv ta
//
LOCUS       WP_357577336             505 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 27 protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357577336
VERSION     WP_357577336.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 505)
  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 505)
  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 505)
  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 505)
  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..505
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..505
                     /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=54131
     Region          1..282
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(6,41..42,83,124,126,160,182,186)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          294..368
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          383..504
                     /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(394..397,407,409,412,416..417)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(403,434..437,446,448,451,453,455..456)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(421,425,427,434..436,446,448,451,455)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(477..481,490,492,499..500)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mgwntwntfg cninetlirq tadaivangl rdlgyryvvv ddcwfnpdrd aqgnlqahpq
       61 rfpsgmkalg dylhsrgllf glyqapldqt caqyfdafpg stgslgheyq darqfaawgv
      121 dylkydwcsp tgtindqiar fgimrdalaa agrpivysin pnsihektgp qrnwsdvanl
      181 wrtteditna wdtgqtngyp mgirnivdvn vplagyaapg gftdpdmlev gnggmndtem
      241 rshfalwsim aaplmmgndl rsasaatlti lrnqnlvain qdplglqavq vsndgtrral
      301 akrlangdva valfnqgsst ttisttaaai gksgtsftlr dawtngtsts tgtisasvpa
      361 hgtvvyrvsg ggttnppppt tfrlrsesag rcldvdnsnt angtgtliwd chgnanqqis
      421 qsgqalrvlg kcldvpstaa ngtrvqlwdc nggtnqqwtf ngngtvsnvr fpslcldvnn
      481 ggtangttvi lwschggtnq rwsrv
//
LOCUS       WP_357577370             144 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357577370
VERSION     WP_357577370.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 144)
  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..144
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..144
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15273
     Region          1..75
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvllrrvigd alrarrqgqh rtlrevssaa nvslgylsei ergqkepsse llaaicdalg
       61 arlsellrev sdtvalaeqm pgvlvpvqde paapvavrrs tgrgvhqvss dgavavqvrq
      121 dsplkatlrs srvrgserdv vcaa
//
LOCUS       WP_357577374             104 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577374
VERSION     WP_357577374.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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=10641
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawivlvisg lletawaial drsagftrlv pslafvvtlv lsmaglayal reipvgtgyv
       61 vwvgigavgt alvgmlalne paslpriacl llvvagvvgl kvfh
//
LOCUS       WP_357577376             816 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357577376
VERSION     WP_357577376.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..816
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..816
                     /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=87109
     Region          84..>188
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          198..807
                     /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 magrtsqasr rrgasprgtt nsrarqpakk taraaarrrp avrsgpgliv gqavrtlwmg
       61 mahglgwafr qagsargldp eqrrdgagll vfglallsav alwfsgagpv garladtfrl
      121 flgaisvvvp vllmigawrl mrepvdpehr grglvgwtsm lvataamlhi gqdpadagqr
      181 dfagglvgag vgslmeravt awvavpllil llvfgllvvt atpinkvper lgllfgtria
      241 ppvveeetde eparpaprkr aakraapppp dpaefdddld gvdlqetlvl prkppgrvpa
      301 trrpaeppeh spaptraeql altglagdyt lppanilgsg aapksrskan devivaltgv
      361 feqfgvdaav tgftrgptvt ryevelgpgv kveritqlsr niayavkspd vrilspipgk
      421 savgveipnt dpenvalgdv lrsraatsdh hpmvvalgkd ieggyvvanl akmphiliag
      481 atgagksscl nsllvsiltr atpdevrlll idpkrvemtg yegiphlvtp ivtnakkaad
      541 slewvvremd mryddlaang vrhiddfnrk vrngeikapp gseremrpyp yllvivdela
      601 dlmmvaprdv edsvvritql araagihlvl atqrpsvdvv tglikanvps rlafatssla
      661 dsrvildqpg aekllgrgdg lflpmgaskp iriqgawvte reiadvvkfc kdqrepefrp
      721 dvlvapdagk kkideeigdd ldllvqavel vvtsqfgsts mlqrklrvgf akagrlmdlm
      781 etrgvvgpse gskardvlvk pdeleevlvg lrgged
//
LOCUS       WP_357577417             724 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [unclassified Micromonospora].
ACCESSION   WP_357577417
VERSION     WP_357577417.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 724)
  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 724)
  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 724)
  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 724)
  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..724
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..724
                     /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=78577
     Region          38..720
                     /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 maavpepggd dlsrsgaqwy aaewaravrr lgfvplsaae terllhlhtv rlaqallaep
       61 fsplpaeevg ralveehlte prvldwsvra lgdrfaarvv pgradrdgtt qrvaalqggl
      121 aagfaralrd rtfaqqeria rsawqarddv eqalrdsear fravfvgaat gigiagvdgq
      181 iidvnqafad mlgysieelr etnvaalfha ddaagmwely qeliegkqdr arvekryyrk
      241 dgsvvwtdls vslirhddgr prftvamied iterhelqqr lrfqalhdpl tglpnrtlff
      301 etlgrvfdva daarrvgvcf ldldgfkain dslghdlgdr llvviakrla dcvagrghlv
      361 armggdefvi lvddgagidd avgvaelala avsapvrige qqlavsasvg ivecpvggts
      421 aselmkaadt tlywakaegr grwavydper gardiarsal aaglpaaldr gefvvhyqpi
      481 vslvegsmla vealvrwqhp elgligpdrf iglaeetgli vrlgewvlrq acrdaeawrr
      541 efpraqlvvs vnlaarqadd pgivdtvada lastglpadl lqleltesav mgtageplrs
      601 lhrlaalgvr maiddfgtgy snlaylrrlp ihclklagpf vegirgedve avpdhrderi
      661 vdalvrlaha lelwvtaeav etgvqaerlr alrcdtgqgr ffgppapaae itarlrdddr
      721 gata
//
LOCUS       WP_357577425             325 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577425
VERSION     WP_357577425.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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=34093
     Region          8..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 mrglppdgrv llichvnpdg dalgsmlgfg lglrrlgvrr mqatfpgppe vpepfrglpg
       61 ldllvpatea ypdpdlvicf daasesrlgd lvdrletaga alvldhhasn trfgrinlvd
      121 phaaatsvva egllarlgvp ldagiaecly valstdtgsf rfeattpavh qlaarllatg
      181 irpgdisrri fdtrpfgavr lfgevlgrar lepagaaghg lvwtyatqdd larhdqrpyv
      241 lealidsvrc taeadvscvv kqtptgdwav smrskgavdv srvavalggg ghrfaagftg
      301 sgtvdevvdr iraeldgalt gpgrl
//
LOCUS       WP_357577550             369 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577550
VERSION     WP_357577550.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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..369
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..369
                     /product="LolA family protein"
                     /calculated_mol_wt=38388
     Region          27..258
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 msvlksrpvl rwlvpvtavv tvigggaalg tfaaqaepsl pprtaaqllv dlqtsrlegl
       61 sgtvvqradl glpplaglva gdgpaalltg thtlrvwhsg pdrqrialvd tlgerdvirn
      121 grdvwawnsr sntathrtlp egaagaesre lpvtpgeaad ralaaispst evsvgrsatv
      181 agrdayelvl aprdaaslvh qvriaidarq hvplrfevfa dgsdkpafem aftqvsyarp
      241 daeqftfnpp pgvkvteeta grqpadvpgk rpahgerpdv rtvgeswatv vvarldgaga
      301 padragtapa gegstgdpaa llgrlpkvsg dwgsgrlltg klfsalltdd grliagavtp
      361 erlyevarg
//
LOCUS       WP_357577540             247 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Micromonospora].
ACCESSION   WP_357577540
VERSION     WP_357577540.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=24973
     Region          3..247
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mnnaldgkva lvtgggrgig aavalrlaed gadvaltfqq nqqraddvvd qikaagrrai
       61 avqadsadpa avvgavdrva gelgrldilv nnagafllgp leqltleefe qtvavnvrap
      121 fvasqaavrh msaggriini gsnvaeravf pgfalyamsk taligltkal grelggrait
      181 vnlvnpgatd telnpadgpn adtingftal ghyadpadva aavaflasad gryvtgatin
      241 vdggfti
//
LOCUS       WP_357577551             768 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577551
VERSION     WP_357577551.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 768)
  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 768)
  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 768)
  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..768
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..768
                     /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=83788
     Region          16..767
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mgdglsrhsa dsaelqsdde igreqeyvsm lyrrldelre qasrrlteel ratggtlqar
       61 sqrdsavrmy adqveqlsav esglcfgrld tddggphyig rigifdtggd ydpllmdwra
      121 paarafylat aansqgvrrr rhlrtrerkv ialndevldl dtasptahee ltgeasllaa
      181 lnagrtgrmr divetiqaeq driiradlpg vlvvqggpgt gktavalhra ayllythreq
      241 lstrgvlmvg pnatflryis qvlpalaetg vllrtqgdlf pgvsarraep aetaalkgra
      301 vlvevlaaav rdrqwvpdep leialpqqev llldpetvra ardrarrser phnlaralfd
      361 veivhalaaq vaerigadpl ggenlldead vaeirrelre epevraaldq lwpvltpqrl
      421 ladlyastdr iavaapmlte aeramlhrep ggwtpadvpl ldeaaellge deraaaarre
      481 riralqreya egvleiargs rsidvedead ggeilgvtdl idadrllerq eeadrlttaq
      541 raaadrgwaf ghvivdeaqe lspmawrllm rrcpsrsmti vgdvaqtgal sgtpswadal
      601 epyvaqrwrl eeltvsyrtp aeimavaadv lteidpalrp prsvrssgvp pwdhavaper
      661 laaelvaatt reaaglddgr lgvivptgrv delgaaltaa lpeaaigedp elesrvvvlt
      721 vgqakglefd svvlvdpdri vaesprgrsd lyvaltratq rlgilrpt
//
LOCUS       WP_357577592             276 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577592
VERSION     WP_357577592.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 276)
  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..276
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..276
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29270
     Region          1..270
                     /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 mrieargftf dvrvggpegg tpvlllhgfp qhggefddvv palhaaglrt yapdqrgysp
       61 garpeaveay rlpelvadav glldalgvda ahlvghdwga vvawavaahh pervrtltav
      121 svphpaamaw altedagqka rsaymtvfrk pgtaekallv lgatglrrml hgvgddarva
      181 ayadpmrepg altaalnwyr amsrrdlaai gpvavpttyv wsgrdiaigr taaeacaehv
      241 tadyrfvelp rvshwipdea paalaeaila rvhdpv
//
LOCUS       WP_357577669             608 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577669
VERSION     WP_357577669.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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=64802
     Region          5..603
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 maldvpyrsi pdmflkrvaa spdrdafahp apddsgpvwl tweqmarrak avaaglhglg
       61 vgledpvail antrldwvia dlgimcagga tttvypttep ddatyiiads gsrvlfaenp
      121 aqaakiagan lpalthvvlf dgaadpaaav pqltlaelee qgaralaaep dlidmlvagi
      181 gpehlatliy tsgttgrpkg vellhggwcw egvaqvevgl lrdddlqylw lplshsfgkt
      241 llcgaihvgl ptyvdgrvdk lvellsvirp tlmcgaprvf ekvynkavtt aqagggakak
      301 ifgwgvrvgk ekvaleqagr plptglklky tvaeklvfsk lqarlggrir vlvsgaapls
      361 peiatffaaa nlpisegygl tetsagnfvn ppdglrigtv gkamgdlecr idtdgeilvr
      421 grpvmrgyhn lpeetaaaft edgffrtgdi gtldsdgylk itdrkkdlvk tsggkyiaps
      481 hiegmfkatc pytsqavvig qarnyctmlv tldpeaikgw aagtplegrd yteivtspea
      541 kamvegyvae lnaklnrwet ikkvailprd ltiedgeitp slkikrrgve snfageiekm
      601 yagtlael
//
LOCUS       WP_357577778             485 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577778
VERSION     WP_357577778.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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   4  (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   5  (residues 1 to 485)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
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 18747083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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: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=51679
     Region          3..483
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          253..483
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpertdlsal iaghttviem insggtglpv lthllrvars algaagtafv efaptggrvi
       61 aatgaaewav ghpvpaddpa tvcllsgarv rqvrtdeltg rlsaelaerg llrmvvsrae
      121 iggltvgslh vlypdgddpp daeqhavagy lasciahmyg dqtglpvhgd gpvvaaladg
      181 lavvdrdnhv rlwnpaaarv tgrsvaqaln rplpfplpps gqvrdhrmpd grwltitsge
      241 lpgpgalrvv tfrditdqqr rdhdrdlfva vtshelrtpv tvikgyadtl tdhwesltet
      301 drrqaarvig qranelarlv drllssaaea gpgdqppapy dlgdalraaa vdlpaelrqr
      361 lvlrlpadlp kalghrlsla tvltelctna gkyseagsli eitadadgst vsfqvrdrgi
      421 girpehvera fdrfwqgesg drrryagagl glylvrrive qqngwvslrp ragggtvaev
      481 rlpcg
//
LOCUS       WP_357577749             896 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577749
VERSION     WP_357577749.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..896
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..896
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=95389
     Region          <1..893
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mlhgrseeta ridallrqar agrsgvlvlr geagigksal lgdaaaradd mrvlrtdgie
       61 seagfpfagl hlllgreidr idalpapqvr alrvalgqea ggdvdrylvg lavltllael
      121 aeerpllclv ddahwldpas aqallfavrr ldaepvaviv avrtdevspf dpaglpelpv
      181 gplgesaaae vlaqrsepvp ghlrpdllte aqgnplalle lpvdgmprrl pssryqrlhe
      241 vfaervrrlp eatrrllgvv adassadasv vfpaaerlgc trddlapaeq aqlvrlvdgr
      301 lvfrhplvfs alrdtveags rmaahealaa vhaargdvcs yawhrsamat gpdeeaaaal
      361 etaarsgsar gsavvsamye raagltadra rrgrrltvaa eaaadtgqld raatladqaa
      421 dhvtdpvqla dialvratvl dsrdrpreah rllsdaavav aaldlslagh llfragraaa
      481 hagdfdaldr taaraeelgv psahlvtals rafaaqnalt daaiaplrvl veettrcdrh
      541 lelldigwwh lmladldsad dvasrlaava rqqgaaglla svlpllaraq lmrgrhddae
      601 anateglria adtgqrrhav ylttvlagla airgeeqrcv elaaapiarg vtpgnvhaag
      661 alslldlglg ryeaafgrls gmlgarhrgg amaslpdlve aairvdrred glaaarqyae
      721 wagrvrqpwt ravalrcqal ldgnadgrya ravalhqegg tpferartel lygewlrrar
      781 risearivlh saleifdrlq ahpwsararg elraagesvr aadpgavqrl tpqehqvvql
      841 aarglsnrei gaqlflsprt vgyhlykayp klgvgsrsel aslvatrpdh strvgt
//
LOCUS       WP_357577831             511 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase 2 family protein [Micromonospora
            sp. NPDC049060].
ACCESSION   WP_357577831
VERSION     WP_357577831.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..511
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..511
                     /product="DNA-3-methyladenine glycosylase 2 family
                     protein"
                     /calculated_mol_wt=54606
     Region          1..345
                     /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          228..510
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 meldfercyr avdsrdqrfd gwfytgvtst giycrpscpa mtpkrqnvrf fpsaaaaqta
       61 glracrrcrp daapgspqwd vradvvgram rliadgvvdr dgipglaarl gyterhlhrm
      121 lraemgagpl alaraqraqt artliettgl gmaevafaag fgsvrqfndt vrevfgaaps
      181 elrtagrrcp apggagtitl rlayrpplha ealldflalr alpgveevrd gtyrrglrlp
      241 hgageaaltp adghvtatlr ltdmrdlapa varcrrlldl dadptavdgt laadpalagv
      301 vaaepgirlp rsvdgfemav raivgqqvsv rsarttltrl lahlrppapg ptpgpagvdq
      361 evstagersr epkpldqpae gawrawlsgf ptaeevlgvp devfgmpagr retirglara
      421 vadgsldlap ggdreetvrr llalpgigpw tagyvamral gdpdvllptd lavrrgaaal
      481 glpdapttld tyadrwrpwr syavirlwra a
//
LOCUS       WP_357577785             808 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC049060].
ACCESSION   WP_357577785
VERSION     WP_357577785.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 808)
  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 808)
  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 808)
  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 808)
  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..808
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..808
                     /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=86146
     Region          112..770
                     /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 mclreltrld wsrnhltlsl tlvclallam tikwririra tvhaiswset aiilslavap
       61 tplvilttgi gvaiaqylak lpplkaafgv aktmllavgg gaalhatggs ppitdlwpal
      121 gpigvayavt vvldevltlp vialatgtrl rqlfreglgl rltsalarfv livttlfilh
      181 gdprlllavp plvlslhlly snqvkarteq qawqrlartt dalnvvdldk vlttavtqaa
      241 elfsadevei elrdggrtvr ggavaitydg pageptavdg tvvpaalegh drtvdvgvlr
      301 lrfrgpvqls ereqytlrtf asalctavrn aqayaelarv adehayaath daltglanrr
      361 hlldqgteql dtrhadgvta lvlidlnhfk evndtlghaa gdhvlvqvae rlrdaaqegd
      421 lvarlggdef avllrglpap avaahraetl latlhepfdl dgmrisveas ggiaaapatg
      481 gmpellrrad vamyqakrag qrtstyaptr dtadlgrltl ggelpravad heftvnfqpi
      541 vdlgtgrvtg aealarwhhp thgmidplrf leaversgll pafaeaildq allaagswrd
      601 agfdvpvavn vsprslldar fpgsvlarlr ahdlppdrlv leltetltls qldvvdrvls
      661 rlrdegvrla lddfgtgyss lsllsripvh elkidrsfvt ametsaeaaa virstldlgr
      721 slgldvvaeg vesepqrral welgctagqg hlfarpvpag tllaafrrgs ggspgtlapp
      781 lhdagavirl apgrrpggrg rtdrhlpa
//
LOCUS       WP_357577948             533 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA carboxylase subunit beta [unclassified
            Micromonospora].
ACCESSION   WP_357577948
VERSION     WP_357577948.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 533)
  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..533
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..533
                     /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=56698
     Region          21..531
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mttlrsavda sspgyranre allerlaele taldqaragg gekyvarhhk rgkllpreri
       61 ellldpdspf lelspvaayg tdfpvgasvv tgigvvegve clivandptv rggavnpwsl
      121 aktrrageia lanrlpmvnl vesagadlpt qaeifipggr vfrdltrlsa akiptvsvvf
      181 gnataggayv pgmsdqvimi rdrsqvylag pplvkmatge vtddeslgga amhastsgla
      241 dflaedeadg irlarqcvrr lnrrkqgppp rnpvpappky dpeellgias adlkvpfdpr
      301 evlarvldgs efdefkpayg talvtgwgel hgypvgvlan argvlfseea qkaaqfiqla
      361 naadtplvfl qnttgymvgt eyeqrgiikh galminavsn stvphltvnl gasygagnyg
      421 mcgrayeprf lftwpnaksa vmgpaqlagv lsivarqaaa argrdydeds daamrmmveq
      481 qiesqsgalf lsgrlyddgv idprdtrtvl glclsaihng pvrgadgfgv frm
//
LOCUS       WP_357578016             938 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357578016
VERSION     WP_357578016.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 938)
  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 938)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 938)
  AUTHORS   Rosinski,J.A. 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 938)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..938
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..938
                     /product="helix-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=100333
     Region          <4..883
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          865..926
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mqqeeqttrl rhafqacedq qrghvalvtg avgsgktsll esfsewaaga ggqvmsaags
       61 raerglhlgv vgqlfhsarl tpeaaarvek lmrdatfavp lpepgaeaad gdrawapllh
      121 glfaalldlt aagplvlvvd dvhhadpasl hcllyvtrrl rharimvvla eastlrpphp
      181 lfraellsqp hfsriglppl tvdavarlvg geadnadarr taercvrmtg gnplltrall
      241 eeragaetnd eygppvgdaf dqavlgclyr hepgvrrvaq alavlnrpat tellghlldv
      301 vpestapavr vlrtsglmeg dqlrhprilr silgdmsade rrslhqraae vlhdhgaeps
      361 vvaehlvaag sasapwvvpv lqdaaghala sgrpdvaaac lrlvsrapvd aqqrtattem
      421 lvnarwqinp lavngqltel vetaraagws tdaglsavpy llwqgrvdea teavsafptd
      481 eehgsagtag rlrmmqllvs lshpehlatv retpsawsra asapttispl lqavtvlgta
      541 ltpaadndtv ataeqllqrh htddgalgll tapllallwa grsdraavwg dvllgrpaaq
      601 hapvwravir avraeaalrv gdlpgaehha raaledmpap awgvavagpl atlvacates
      661 grfseaerwl ahpvppgmfr tplglhylaa rarhhlavrr phaattdlrr cgelmrawgi
      721 daaglvpwrl elarvqlsvg nkaqatqllq eqlrvphgvd drtrgrtlrl lattaaqdhr
      781 rkllseavnl lqssgdrlel vralgdtgqt lqragdsara rllvrrayql aqdcgasvla
      841 qrlirrepgs glpaypaaae lqepddglsd aerrvaalaa qghtnrqiss klfitvstve
      901 qhltrvyrkl dvkrrtdlps rlvayaeala detqgaas
//
LOCUS       WP_357578017             950 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357578017
VERSION     WP_357578017.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 950)
  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 950)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 950)
  AUTHORS   Rosinski,J.A. 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 950)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..950
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..950
                     /product="helix-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=102212
     Region          <32..890
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          864..920
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 melterscll smlerrltdl fsseasptnr tvavltgpvg sgkttllqtf arracdsgar
       61 vlgasasrae rtvplevirq lvraaplsga gnpdlwarlg rlldagaltw tdaddtdhed
      121 talataaigg allemtaqgp lviavddvhh advpslrcld yvarrisglp vliilteapr
      181 trpwrpevha ellqparlqr irlpqltadg tfqllarrlg vpvartiaee shrisggnpl
      241 lvqalaedqa aaprpadrpv tgesfreavl sclyrcdqlv lnaarvlavt geplhgnllp
      301 hlvdarsraa lgaiddstsa gliteqglrh pavsqavldg mtaeerarlh leaacllhdd
      361 gaapariaph lvgidelaep wmaqtlldag eqalrdgeme talrylrrah rscageclra
      421 rirsalarae wrldpqaaip hlvgvvsair aghlgsqqaa gaihyllwhg eidkavdlvn
      481 hlseradsvd prsaaellvt tgwmstlypg vmvdrpapav aardpltmak vkrgiegatl
      541 lsavldrgda gaveqaeral sttglddepn mwtavcalia miyadrldla ddwcdrlgrn
      601 patpryptps atlaalraav agrlgdlpra eklanealsq lspkgwgvvi giplavrvra
      661 ltfmdqldaa aaslqvpvpp amfetpiglh ylqargmhal aaespeaala dfqlcgqlmn
      721 rwrldfsglv pwrtesaral lrmgrrqqag rlvreelarl rpvhvrhraa alrvlaated
      781 gpdriphlrs avrllrqcgd rmelahnlad lgqayqqvgd rrqarvaars arvlaeecgi
      841 pmlrpglsar sggaegagat avvrgltdae cnvatlaaqg htnreiaekl fltvsaieqr
      901 ltriyrkldv nsrselaarl rmnrpgatvl dppprgrddp ghrpagprpr
//
LOCUS       WP_357578077             291 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357578077
VERSION     WP_357578077.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  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..291
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..291
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=32097
     Region          10..76
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 msgnghcrsf ngdgrmdimv rddvtgellv fphsgsfrgs etfgepelis tgfhpnrnhg
       61 lvrpidvngn gyadvigism thmnethgif lypnrgglng ldtlgepiri sgarddkkwe
      121 tlgiadldld gcddmfgreq daghvdaffn krqvtqnety drtahrlvtv dvddfplama
      181 dftgtgradl lvrrangdld lyefahdtsg egpwwrgegr wftlahgwqk yeiiavtdid
      241 ldgrpdvlgl rpdgtlvvhl hhgtfdpdrp fatlsapevv atgwqkysvv s
//
LOCUS       WP_357578099             483 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 3 protein [unclassified
            Micromonospora].
ACCESSION   WP_357578099
VERSION     WP_357578099.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 483)
  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 483)
  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 483)
  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 483)
  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 483)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..483
                     /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=48778
     Region          25..>319
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mgldpglrrl algtllaayp gpvppgwavd lvaeglaght lfgtnvhdlg qvaastaalr
       61 agrpdvliai deeggdvtrl ahatgspypg naalgaidev altrrvyeai gaelaalgvt
      121 vnlaptvdvn tadenpvigt rsfgadparv aahsaaavtg lqaagvaaca khfpghgatv
      181 adshhelptv dvpldvlrrr dlppfaavve agaravmtah irvpaltgdg patfsravlv
      241 dllrgeygft gtvitdalem kgaavaaggv gpaavralaa gadllcigaq vdaelvervv
      301 aeivgalgdg rldrsrveea agraaalaaw trtagatpaa pdglgyaaar ravrvegelt
      361 gldrplvvql haastiaegr vpwglgphld gteelrvvat etgpaalrql agdrpivlvg
      421 rhlhrlpgga dlvtalaaeh pvtvvemgwp srwrpagvra fvttygasha cgraaaevlg
      481 lag
//
LOCUS       WP_357578101             336 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357578101
VERSION     WP_357578101.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 336)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..336
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35660
     Region          5..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msavieiegl rktfhsvrqg rrvavdgfdl lveagqihgf lgpngsgktt tlrallglvr
       61 adagrmtvlg vpspdglplv agrvgaives pqffgnftgh rtlrllarag gvpvarvdev
      121 leqvglsdrg dervkgyslg mkqrlavasa llkdpellil depangldpa giremrdlmr
      181 slaeagvtvl vsshilaeiq licdhvtiis rgrrvaagrv devlagfdrh ellvrvddpq
      241 ravelltaag laatghddhl vvggvddate vsrtlgeagl wvreltplrp dlesaflelt
      301 gtathptlpr qvddsvlpdg rasepvidld ergvda
//
LOCUS       WP_357578193             271 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified
            Micromonospora].
ACCESSION   WP_357578193
VERSION     WP_357578193.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   5  (residues 1 to 271)
  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 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..271
                     /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=28338
     Region          9..271
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 maetsggala ayrallgaqa raqtayrtsf vidvvgnvgs tvfdvltvlv ifgvtrelgg
       61 ftlretlvvv glstcafava dllvgnierl pryvrtglfd avlvrplgal pqlllmdlpl
      121 rkvsravfgl avlvvavgsa gvqwtparal lvvlaplagv vffgsvfvat atvsfwwvds
      181 gelansvtyg grdfasypvt vfegwfravf ayglgfafvs yhpalallgr adplglpawv
      241 gwtapavalv aavgaaaawr tgvrhyrstg s
//
LOCUS       WP_357578350             445 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357578350
VERSION     WP_357578350.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..445
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..445
                     /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=47925
     Region          4..391
                     /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 mtdqrdeiav vgaglagcll acflarrgyp valyerrpdp rtgtvergrs inlalsergl
       61 dalrriglde qvladglpmr grmihpvdge aqfqsysaag drainsisrg alnnalldaa
      121 tslpgvrvaf dhrlvgldpt sgemtfetpq gtvaatasvv lgadgagsam rgqllaygll
      181 tesvdfldyg ykeltipplg gdfaldpeal hiwprgtsmm ialpnpdrsf tctlfwpthg
      241 tasfaslgsp aaierhfaeh ypdlpplapg lvddyqhnpv gvlgtvrctp wqaygkfgll
      301 gdaahaivpf ygqgancafe dvveldrcld ecaddwseal plfqqrrqan aeaiaqmala
      361 nfvemrdkva splfqagrkv ehalervlpg ryvsryelvs fstspyaevr rrvrrqhrll
      421 gavaagaval lagavgltis rgrrr
//
LOCUS       WP_357578216             119 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357578216
VERSION     WP_357578216.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   4  (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
REFERENCE   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..119
                     /product="PadR 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=12743
     Region          9..100
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mdtplreptf liltalagep mhgygligev aalsdgrvsl rpgtlygald rltdaglvev
       61 dreevvdgrl rryyrlsptg datlsaeter lrrnveaata rlrtraarpl aprtaggla
//
LOCUS       WP_357578375             340 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357578375
VERSION     WP_357578375.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..340
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35672
     Region          8..339
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 maepgaervg eglnralatl laerpdlhli gedmadpygg afgvtrglst gypervlstp
       61 iseqaivgfa vglalrgrea vvevmfsdfa tlcfdqivnl askavtmyge pvrmplvirc
      121 ptggnrgygp thsqslqkhf vgvpnlavhe lspvhdahat larildsgap amyfedkvly
      181 grrrfgaaag delfhcerig gacdfavlgv rgvdradvvv iapggltdrv lggmrgayla
      241 deiavravvp srlypfdpap laalvagagr vvvvedatag gtwgaevaht ihqqmwdlls
      301 qpvrllhapp stipaaphle ravlvqaddi ravvtavagg
//
LOCUS       WP_357578415             471 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Micromonospora].
ACCESSION   WP_357578415
VERSION     WP_357578415.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=49177
     Region          237..461
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 maeptvappp rhrpgrtlts ravlvtcava lvsvlvtaiv avplavrgve rhdrealaaq
       61 arlaaevlrp rletgrttde erivrqlnaq gvdaylvrgg aaerpglppr vvrrvaegrn
      121 vstrrvidgr rtliegralp ggngvvltra rpaapwrqvv pslwlpllag laagvaagll
      181 larrlarpir raadaaarlr agdravrvpv eppdevadla yalnglaaal atsegrqref
      241 llsvshelrt pltairgyae aladgvigpa daagagrtvl aearhldrlv sdllalarle
      301 aadfplepvp vdlarlaada grtwadrcaa vgvpfraeip dapvpvhtdp grirqvvdgl
      361 lenalrvvpp gapivlavra agadplaggv vevrdggpgl tdddlavafe rgalhqryrg
      421 vrkvgsglgl alaaglvrrl ggdvaaghap eggaaftvrl ppdpyrtrts l
//
LOCUS       WP_357578445             166 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357578445
VERSION     WP_357578445.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 166)
  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 166)
  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 166)
  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 166)
  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..166
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..166
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18095
     Region          <13..156
                     /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            94
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mlldapglrl ssracrhael gttfdddrtt aliaadvasw asvdtdmirl ieraaaagvr
       61 lallsnipee lashyehhha qwlrhfelva fssrighakp epaaflwccd rlgvppgsvl
      121 fvddttvnih aaerlgmhth qftepagtaq aisrvqtgwp rsdarl
//
LOCUS       WP_357578490             697 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha-1,4-glucan--maltose-1-phosphate
            maltosyltransferase [unclassified Micromonospora].
ACCESSION   WP_357578490
VERSION     WP_357578490.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 697)
  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 697)
  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 697)
  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 10571012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..697
                     /product="alpha-1,4-glucan--maltose-1-phosphate
                     maltosyltransferase"
                     /EC_number="2.4.99.16"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009313 - oligosaccharide catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0030979 - alpha-glucan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76966
     Region          3..190
                     /region_name="GlgE_dom_N_S"
                     /note="Alpha-1,4-glucan:maltose-1-phosphate
                     maltosyltransferase, domain N/S; pfam11896"
                     /db_xref="CDD:463388"
     Region          195..555
                     /region_name="AmyAc_GlgE_like"
                     /note="Alpha amylase catalytic domain found in GlgE-like
                     proteins; cd11344"
                     /db_xref="CDD:200482"
     Site            order(254,258,269,271,314,346..347,349..350,382,384..385,
                     413,469,522..523)
                     /site_type="active"
                     /db_xref="CDD:200482"
     Site            order(332..334,341..343,356,387..390,392,395,417,419..420,
                     423,427)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200482"
     Site            order(384,413,469)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200482"
     Site            order(416..418,435,438..439)
                     /site_type="other"
                     /note="acceptor binding site [chemical binding]"
                     /db_xref="CDD:200482"
     Region          <543..658
                     /region_name="PRK12313"
                     /note="1,4-alpha-glucan branching protein GlgB"
                     /db_xref="CDD:237052"
ORIGIN      
        1 mtgrfpiedv spvvscgryp akavvdepvp vsarayregh dalgcnvvwr gpdgrarpft
       61 rmrpgepgqd rwhavirpda vgewvftvea fqdpyltwqn avtkkiaagq gpadlandla
      121 egarvltaav elvpagdagr vraavaalgd adrelprrva paleladllw ehpvrelvtt
      181 gaehrlwvdr rralfsawye ffprsegavp atadaparsg tfataverlp gvaamgfdvl
      241 ylppihpigr vnrkgpnnsl tagpddvgsp waigaaeggh dtihpdlgtp edfrdfvaaa
      301 aeqglevamd lalqcapdhp wvtehpewft tradgsiaya enppkkyqdi ypvnfdndpe
      361 giraevlrvv lhwigegiri frvdnphtkp fdfwhwliae vkkvdpdvlf laeaftrpai
      421 mhglgkvgft qsytyftwrt saaemrayce elveaadymr pnfwpntpdi lheslqhggp
      481 pmfkiravla allspswgmy agyelfehva rpgaeeyldn ekyelrprdw agaqaqgrsl
      541 apfvavlnrv rrenpalhql rnlvfheidn pallcwskhd petgntvlvv csfdsrevqw
      601 gnttldmpal gldwhdrftv rdeltgasyd wgqrnavrld pylqpahvlt vrrpapgagp
      661 vpaqaapdlt vedvpddlsg gtapttpaqk ddarwts
//
LOCUS       WP_357578510             382 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DegT/DnrJ/EryC1/StrS family aminotransferase
            [unclassified Micromonospora].
ACCESSION   WP_357578510
VERSION     WP_357578510.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=39742
     Region          4..373
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 msgtihlspp dvgpleesyv vaalrsgwva pvgpdldafe revatrvgtr gavavssgta
       61 alhlallgvg vgpgdavivp tltfvasana vryagarpvf vdcdphsgnl dvalvdelir
      121 alvlrgqrvg avvpvdlfgs cadhtalapv caaagvpvve daaealgath hgrpagsfgq
      181 vgilsfngnk imttsgggml vsddtallar arflstqare ptphyehret gynyrlsnll
      241 aalgraqlvr ldgmiarrrh lrdqyaklfa pipgvrllgv edpgsncwlt tiavdpqrag
      301 wraadlaahl agrdietrpv wkpmhlqpay adaeclvtgv aerlfadgla lpsgsamner
      361 qvglvlaavd eflaartggs ta
//
LOCUS       WP_357578536             132 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YidH family protein [unclassified Micromonospora].
ACCESSION   WP_357578536
VERSION     WP_357578536.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..132
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..132
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13916
     Region          16..>104
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 mvvdtddets srtpgrrrwp grvfdrgvdp dprfslaner tflawirtsl alfaagiale
       61 alalpiapgl rraaavvlil lgavapvqaw igwlrteaal rlgrslpppa lalplglglv
      121 laaglilvgl vr
//
LOCUS       WP_357578556             255 aa            linear   BCT 28-DEC-2024
DEFINITION  YqjF family protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357578556
VERSION     WP_357578556.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..255
                     /product="YqjF family protein"
                     /calculated_mol_wt=28193
     Region          16..240
                     /region_name="YqjF"
                     /note="Uncharacterized conserved protein YqjF, DUF2071
                     family [Function unknown]; COG3361"
                     /db_xref="CDD:442589"
ORIGIN      
        1 mdtepidaap gqafprailr qrwddltflh wavapervap llpagtrpdt ldgvsyvgli
       61 gfrmvglgfg rgpgipyfgs fwetnvrlys vddtgrravv frsldasrlv pvlvarvtlg
      121 lpymwsamrl drdgdrytyr crrrwpgpvg atsrmvvrvg epvaeptple hfvtarwglh
      181 traygrtlhl pnwhprwplh raellhldde lvaaaglppp agapvsvlys pgvpvrfgpp
      241 vargraraaq vrqss
//
LOCUS       WP_357578555             257 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Micromonospora].
ACCESSION   WP_357578555
VERSION     WP_357578555.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  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..257
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..257
                     /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=27022
     Region          98..251
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 maveeaprsr rsdvvgavgi fnvalvglag lyaatsslwl tgaggavaag lagayllsgr
       61 hdpaaavlae agfaelapaa pdttpddgeg saqlmeerdd ertdfaeffr aeyprlvytv
      121 mrlgateaea edvvgdvltr lyarwgsied papyayrsvv ngyrsslrsa grtvsldavg
      181 arlpgvdgsd igqrerrile avdrlpaaqr vvvalhyagl snaeiaeatg svaetvrsnl
      241 rharkrlkal liaddll
//
LOCUS       WP_357578609             215 aa            linear   BCT 28-DEC-2024
DEFINITION  IclR family transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357578609
VERSION     WP_357578609.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..215
                     /product="IclR 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=21322
     Region          7..192
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdttargget aqtldrglrl lhlvadapgg ltvteaanrl gvgraavyrl vgalaahgml
       61 rrdgegrlrl gagvlhlarr aqpllaegal palrrlaeqa gatahltvve ggegvalvvv
      121 epswtsfhva yrtgarhple rgaagraila gragaagpvs tagelqsgay gvaapvlgvp
      181 gleasvgvva lapldaevvg aqvltaatai atals
//
LOCUS       WP_357578589             391 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: trans-sulfuration enzyme family protein [unclassified
            Micromonospora].
ACCESSION   WP_357578589
VERSION     WP_357578589.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 391)
  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 391)
  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 391)
  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..391
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..391
                     /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=40421
     Region          3..377
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mtgtgtiavh gddglspgga vsppivqsat fsaesdeqfa avatetrgna fytrygnpnh
       61 aqvaavvaql egveaglvta sgmgaistia lallsagdhv ivqrstyggt tslvtgllar
      121 fgvaftqvdq tdteafvral rpqtrlvlve tpsnpllelt dlaavvelah andalvavdn
      181 tfatpvnqrp aefgadlvwh sgtkylgghs dvsagvvvgs adlvdrvwqt aivtgstlgp
      241 idawlllrgi rtlslrvdrh nanalalara veghpavrrv rypglpthpq helagrqmtg
      301 fggvlsvelr dgraaaglld glrlakraas lgsvstlvvh prsmwagivd aeqlaatgig
      361 eglvrvstgi edtedlvadf laaldaadra e
//
LOCUS       WP_357578673             190 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357578673
VERSION     WP_357578673.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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 190)
  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 190)
  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..190
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..190
                     /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=20744
     Region          17..186
                     /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 mdsshplvag ivhqapgstv rlrpvaeddl amlrrfavep gligldwagf rdaaaparrf
       61 aedgylgert gglivqvepa adapagylsy lqgqyggrap yweigivllp ewrgqgigwr
      121 aqallcdylf shtpaqriqa sthaentaeq rslekagfql egvvracefr agawrdgwly
      181 srlrddpspl
//
LOCUS       WP_357578696             332 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Micromonospora].
ACCESSION   WP_357578696
VERSION     WP_357578696.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..332
                     /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=35761
     Region          36..320
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msvnatpaga dvaadetaar pgrdakvpaq rtgrgrkapl senkkaerrl gwllcapaal
       61 vmvlvtaypi iysvwlslqr ydlrfpaerq fvglenyatv ltnefwwtaf gvtalitvvt
      121 vavelvlgmg lalimhrtlv grgivrtaal ipygivtvva afswryawtp gtgylanlfs
      181 dgaplteras slaiimlaei wkttpfmall lmaglalvpe dllkaastdg atswqrftkv
      241 mlpvmkpail vallfrtlda frvfdnifvl taggnetssv smlaynnlir glnlgigstm
      301 svlifltvai iafvfvklfg taapgsddge rr
//
LOCUS       WP_357578722             291 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified
            Micromonospora].
ACCESSION   WP_357578722
VERSION     WP_357578722.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 291)
  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 291)
  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 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   5  (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
REFERENCE   6  (residues 1 to 291)
  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 291)
  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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..291
                     /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=30689
     Region          26..228
                     /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"
ORIGIN      
        1 mmagtsptag aaagyrpsat lpfgaefrrq asrrrtqlal gfmvllplii liafqfdtsg
       61 dddngrgefg slvefatsgg lnftlftifv sasflmvvvv alfcgdtvas easwgslryl
      121 lavpvprarl ltvkllvalv ysalalllla gtalligtlr ygweplrstv aaqlepgegl
      181 lrllgvlgyl avvllvvagl afllsvvtda algavggavl lwilssildq italgalraf
      241 lpthystawl gllstpvqtd dvvrgaisai syatlfwgla fwrftrkdvt s
//
LOCUS       WP_357578824             448 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: M16 family metallopeptidase [unclassified
            Micromonospora].
ACCESSION   WP_357578824
VERSION     WP_357578824.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 448)
  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..448
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..448
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47340
     Region          54..429
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtliadrpgp gaarpyrfpq vvrrtvaggq vvaahlpgqn lavallllda gavreptgke
       61 glgavlakal eegtaqrdat ayalaieglg telvigldwd sfqvsvqvpv erlnaavell
      121 aeavrtpkld pddvrrvrdd eatalrmdwa npgpradaal radlfgagnr wgrplygdpe
      181 svaaldvedv tvfhsewfir pgtlvvagdl drldldalga aafagtgggp vdrggpievp
      241 trpgrriilv drpgsvqstl rlghpsphrs hpdhvpmtla gtvlggafts rlnhlirevr
      301 gytygirgdf assrrfgrfg vsssvqtavt apavveavge itrtretgvt eeelavarsw
      361 ragqlsvelq sprsiasalt tlvvhdlpdd yharlresll sadlaevsaa aathlrpedl
      421 tivvegdaav irdelvaagl gelvehas
//
LOCUS       WP_357578949             420 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357578949
VERSION     WP_357578949.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 420)
  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..420
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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=44982
     Region          205..420
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mellrwplrv atatllcgpl lalywtdpwe laclavtgvl hvevglrlwr erpdnrigpl
       61 lvvcglvwll dawgrvtlpa lftaammlsi vhdpmhlhag lvvssgrlrg rwerlvaaag
      121 yaywpvlvag amvagtlstg hllhlrawsy plvgaflagl fivryrradr aerhvyapfw
      181 aalavnglct amlstvaygs ghwpttlyal gaalipvgaa lsmhraerrh lirardrerr
      241 rverdvhdgv qqrllvaamm lrqedpalva rgaaeveqai adlrdlvrgm npaalvchgl
      301 sgavaaiaer aavpvlvddr vshltlpepv avaayfvtme avtnsqkhaq agqvsvtlaa
      361 sggrvevtvh ddgiggalav pggglhglre rvescggtlr vsstrgrgta vravmplaas
//
LOCUS       WP_357578984             283 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357578984
VERSION     WP_357578984.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 283)
  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..283
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..283
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30765
     Region          14..277
                     /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 mpfitvgten sapvdlyyed hgsgqpivli hgfpfngatw ekqvgpllaa gyrtitydrr
       61 gfgssaqpas gydydtfaad ldvlmteldl rnailvghsm gtgevtrylg vygsqrvdra
      121 vllaplapfl lktsddpegv ekslfqgfqq aiiddrfayl ttfceaffny qenkgrlvse
      181 eafrahweig arasakgthd svdawqtdfr gdvsridvpv livqgdadav lpypatgqrl
      241 qpmlpgsqlv tlkgaphgip wtnaaevnrs imdfigapam ara
//
LOCUS       WP_357579055             334 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Micromonospora].
ACCESSION   WP_357579055
VERSION     WP_357579055.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=36165
     Region          17..306
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mndvdrsmpa aevgplarsv leavgqvvvg krdalelvla gilagghvll edlpglgktl
       61 tarsfaqalg ldfrrlqftp dllpadvtgs flydqrsgdf sfragpvftn llladeinrt
      121 ppktqsalle amqekqvsve gvtykldepf hvlatanpie yegtyplpea qldrfllrvs
      181 fgypeaeeew evlrrrmarr reeaeikpvv daatlramqa aledvvveds vgryivalta
      241 atrehpsvlv gasprgslal lllsrvravm agrdyvvped vkevaapala hritlrpemw
      301 lrrvdpsfvv gevleatpap asgalpsyaa gpgh
//
LOCUS       WP_357579070             465 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: amidase [unclassified Micromonospora].
ACCESSION   WP_357579070
VERSION     WP_357579070.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..465
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..465
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48548
     Region          7..456
                     /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 mavqdimptw vgatakqiar gvrrgdvtat qvvadhldhi arvdadlaaf rtvrggeait
       61 eaekvdeqed lanlplagvp vavkentpva glptwngsaa vrtpvaeadh evvrrlrgag
      121 avilgvtrmp elglwgltdd etavtrnpwd trrtpggssg gaaaavaagl vpiahgndgl
      181 gsiripaacc glvglkpgrg vvpcqlgadd wfgltehgml tstvadaavg fsvlagrrpd
      241 klvppqrlrv gvslrspvrg vhadapnrda vaaagrllaa aghdtvpadp vyptalglqg
      301 iatwfaaaaa dvraagldrr glqrrsrrhv algewaqrrg yvreadraaw rersigffad
      361 hsvdllltpa latappeagg wsgrswranm ltnvryapfa apwniaglpa lvvpvgrrpd
      421 glpvavqlig ppgsellllg vagqfemqap wsrhapgypr ipapv
//
LOCUS       WP_357579107             267 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579107
VERSION     WP_357579107.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..267
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28453
     Region          25..259
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mrgrewarpv rpvrrevlga npeveqgrpp llfvpgfghg awafaehwlg haasrgfpay
       61 alslrghgds gpapeatlra yahdvtqvaa glprqavlvg hgagalvvah alaryparaa
      121 vlvapvfggw atfgaalrrn pvgtlpavfg gplrlhrrql fsrelpeaea rgyagrlgra
      181 grraqwqllt graaepavgd ppvlvlgspd drvvpsaalt raarrygsap llfpgmghdm
      241 mldarwrepv daildwlekd paptgrp
//
LOCUS       WP_357579170             337 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Micromonospora].
ACCESSION   WP_357579170
VERSION     WP_357579170.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,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..337
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..337
                     /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=37214
     Region          1..332
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtenilevrd lvkhypvtrg vvfkktighv kavdgvsfel kagetlgvvg esgcgkstla
       61 rvlmnlekpt ggsvhykgqd iskfsgpalr rlrrqiqlvm qdpytslnpr mtvgdligep
      121 feihpevapk gsrrekvrel ldlvglnpeh ihryphqfsg gqrqrigiar alalrpeiiv
      181 cdepvsaldv siqaqvmnll eklqgelgls yvfiahdlsv vrhlsdrvav mylgkiaeig
      241 tedeiyerpt hpytqallsa vpvpdptvrd nkaiirltgd vpspvsppsg crfrtrcwka
      301 qdvcaeqvpl leirsgsdhp sachfaekre ivqthea
//
LOCUS       WP_357579106             551 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [unclassified Micromonospora].
ACCESSION   WP_357579106
VERSION     WP_357579106.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 551)
  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 551)
  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 551)
  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 551)
  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..551
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..551
                     /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=59327
     Region          2..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 mtqaeleall qrlteelaaa llaepidlrv ghrvgtelva ahiasaealg rtvevvqlrl
       61 ardlglveee vedrlarlla avttgyaram rdrtldeqet irraamtara eaeralrsse
      121 arfrhqathd pltdlpnrtl lterlsaaid spaggsarlg vcfldldrfk vvndshghqv
      181 gdgllvavad rlrlaldghl varlggdefv vlvegttgtd davavaetal aavrepvlvd
      241 ghelsvsasi giverevagt spgdlmraad stlhwakaag garwalydad rdrqdlarya
      301 lsaaipaale rgefyldfqp ltslrdgrvl gmealvrwrh pelgvlrpds figlaeetgl
      361 ivplggwvla eacrqaeswa vgtgpapfvs vnlavrqvrr aglvqevral lrhtglsper
      421 lqleitestm mstaeepvra lrvladlgvr iaiddfgtgy cnlaylrdlp vtelkvagef
      481 vaglrapear aderilaslv slahaldltv taegvetagq aerlraidcd agqgwhfgrp
      541 dsaervlarl r
//
LOCUS       WP_357579177             308 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579177
VERSION     WP_357579177.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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 308)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..308
                     /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=32092
     Region          1..134
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
     Region          164..291
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 meqrrrvgay gvcrgsdgrv llvrgsalcp vpgvwqvpgg glehaehpah avvrefaeet
       61 glavevtglr avsadvtafr aadvavhtdr vvfdvvargg elrpepaggt delgwfttde
      121 aaavplmpft aellgvpvsp lpsdlprssa tepaaalpsd rrqrfgaygl vtdpagrvll
      181 tmiadgypga grwhlpgggt dhgeqpvaal lrelveesgq lgrvveligv dnlhnpaalg
      241 pegrpldwhg irvlyrvavd apteprvtel aggstaragw ftpeelaglp lsgiaalala
      301 naptderp
//
LOCUS       WP_357579250             249 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357579250
VERSION     WP_357579250.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 249)
  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 249)
  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..249
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..249
                     /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=24843
     Region          1..248
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msraprrivv vtgagtgigr atargfsaqg arvvavgrrp aplaetaagh pgieplvadv
       61 tapgaaeliv gtatqrhgrl dvlvnnagva gggplgslap dtvarhlatn lvapilltra
      121 avpaltdsrg vvvnvttsvg arawpgssly aagksaldsl trswavelap sgirvvavap
      181 gavdtpigah qgltpqqqad vrrwqvartp lgrvgrpeev awaircladp aagfvtgvvl
      241 pvdggavia
//
LOCUS       WP_357579282             449 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Micromonospora].
ACCESSION   WP_357579282
VERSION     WP_357579282.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..449
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..449
                     /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=48111
     Region          18..403
                     /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 mtsvrgdapg atsatgerar priffpeleg mrgvaavmvm lthialttgl iasdmygaag
       61 npvvgpifnt mdvsvpiffv lsglvlyrpf alatltdrpp malkpyfwrr alrilpaywv
      121 ltvtallvln adavtglwhv lrsllvlhvy qpnamptgme qtwslateva fyvtlpllaw
      181 alrrwavraa dpgararrll vplgalvltg agfaayhhlp smgafpiqhl wpteyvgyla
      241 vgmilailsa vaevapertp aayrflirhp gaawigaala yaaacsplgg pnemnypplg
      301 samvdhvlyl aialllvapl tlpagrpgym raalsnpvlr flgrisygvf lwhvfylwiy
      361 fgttgtplgt gnfwlvtaav agasvvtatl sfyllerpam glrpwlgrap vdpgaqapst
      421 vreqlpagre aaqreprgte paapavaae
//
LOCUS       WP_357579295             208 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CGNR zinc finger domain-containing protein
            [unclassified Micromonospora].
ACCESSION   WP_357579295
VERSION     WP_357579295.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 208)
  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..208
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..208
                     /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=22590
     Region          12..208
                     /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 midaasgltl tspegtrylf dpgalclefl ttggpgalar ydvlhrpgdl adwlalsrlr
       61 ldparvevta delaaarrlr dalwrlvcvr tgarppaadp adfdatpddl atlnrlaaga
      121 plapqltadg trrwalparg gqalatiard avdlftgphr drvrecathd cylvfvdtsr
      181 pgrrrwcame rcgnrhkvrs lrarraad
//
LOCUS       WP_357579267             221 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357579267
VERSION     WP_357579267.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 221)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..221
                     /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=23784
     Region          5..127
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          77..203
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mprprqalls rqrivetaaa lidaeglegf strrlaaelg vrgpslynhf atkdeildav
       61 adsvtgqvdv sffgsvdwre alrrwghsyr aalaahpniv pylargpgrr paalamadav
      121 ygglvaagwp parathvgal mryfvagsal gsfargfved pglyaeqyph ltqahrlaeh
      181 qqrvdegafa lgldalihgl srtyeehigp lpplppadea y
//
LOCUS       WP_357579293             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579293
VERSION     WP_357579293.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30941
     Region          36..295
                     /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 mrgfrwpppp dggprtwgpg pgaprtgrpa lpepdtelva tphgvrleql vtgagdpvtv
       61 fahglgngia ttrpfgsgvt grklffqfrg hgrsdappgp wsyldlardl ravadlggat
      121 rafgaslgag alcrllaesp erferlvvfl paaldrprge vararltalf eavesgdaaa
      181 vadvvqaelp pavrntpagw aylrqrldql lrdglapgla slpeqaplrd agalaavtap
      241 alvigcagdd lhpvevaeql aaalpratlh vydrpgvlwt eradlrsris aflne
//
LOCUS       WP_357579326             321 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357579326
VERSION     WP_357579326.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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=34752
     Region          4..314
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mshpaarvlg mlellqshhr ltgaelarrl gvdgrtvrry aatlaklgip vaaergrhgg
       61 yrlrpgyklp plmltddeav avllglvaae rlglgteepa tatalakirr vlpptlsdrl
      121 aavqehlgft lrqsapqprp atgtlltlga aarhrrrvrl ehrsssgtvt rreldpyglv
      181 fhsgrwyvtg hdhlrgevrt frldrirevl pgeetfavph gfdpvaqvtr slarvpyahd
      241 vevlleadla aarrrlppsv aelrttdggv llraraenla gmaqllaglg wpftvvrpaa
      301 lraevaahar glaawaarvp g
//
LOCUS       WP_357579443             396 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579443
VERSION     WP_357579443.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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=41136
     Region          137..393
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mkaagwvgag tggrdfvlac aslvggvvly glgtqpqlsw hpdlpeplfl lplavvctav
       61 glrrvatras lalgtvavla dlamggslat vlvytqvlyd acvfgsartw rrllqvtigl
      121 svlgtavgvl lrgdwrgvgi gapvvlagvl pvltgisvrq yrdqavaera raeqtarlve
      181 ldrrqavgae rarmarelhd vianhlsava ihataalsvp glersqvesa lrviressvq
      241 glgemrqmig llrepaegga aldatdettr arlsevdalv drvraagltv ratrrgepra
      301 lpvgvdlaay rivqesltna lkhgageadl lvayepagvv vgvenpvgag rgtltgagag
      361 ligmreraal lngrfaagpa ggrwrvrvel ptevap
//
LOCUS       WP_357579454             705 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579454
VERSION     WP_357579454.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 705)
  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 705)
  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 705)
  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..705
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..705
                     /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=77127
     Region          5..701
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mtdqttleqe maveqrhldr vyarlaelrr savsaekegy rlarvgnfga lverdamvfh
       61 aarrrhmlda eheglvfgrl dlldrqvlhv grlgirddda stlvvdwrap aaaafyqatp
      121 aqplgvvrrr tiqssaervt rieddlldpv aapvdmavvg dgallatlsk atgrgmrdiv
      181 atiqqeqdea irspgsgvti vsggpgtgkt avalhraayl lysdrsrfag ggilvvgpss
      241 vfveyiasvl pslgedtatl hslgtlfagl tatrtdppav aavkgslrmr rvleravrda
      301 vpggptelrl lyrgellrle rreldgirdr amprgarrne vrragfdgvf aalwaqarrl
      361 gvgrlpeqra fedeiaerpe freflkawwp rlhprhvlgw larpdrlhry aegilsraei
      421 rlltdayrsl daagltiadi alldeldall gkpmkparak rdpfqlaggv relstfadrq
      481 raareaarer pddyreyahv vvdesqdvsp mqwrmigrrg rlaswtvvgd paqtawtgep
      541 eelnrardqa lgrrkrhhft lttnyrnsae ifavaaaeir rlhpdlplpr avrstgvdpv
      601 alsvppaele aavvaaagal ladvegtvgv impvprrdev agwlgglgap rlqvvtslea
      661 kgmeydgvvl vapgeiradp gsgvrtlyva lsratqrltt vdpig
//
LOCUS       WP_357579457             325 aa            linear   BCT 28-DEC-2024
DEFINITION  1-phosphofructokinase family hexose kinase [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357579457
VERSION     WP_357579457.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 325)
  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 325)
  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..325
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..325
                     /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=34026
     Region          28..301
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 msghvmvfap tprltvtvdq pseapelhlh pggqgvwqar mvmslgvdvv lcaalggeig
       61 qvlepllvse gvhlkvvvrd sgsggyvhdr regsrqeivd vpgqplsrhe ldelynlalg
      121 eglrapvsvl sgpnepslvp adlyrrfaad lgangsrvvv dlcgehldav ldsgvfflkv
      181 sheeliadgr adgedeeqla ralydlhagg aenvvvsrad kpalalvdge vfevemprle
      241 aadprgagds mtagvaavva rggdvrtair tgaaagalnv trhglgtgrl dsiaglvdrv
      301 rlvpagsrpq ertspdelae raaer
//
LOCUS       WP_357579473             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Micromonospora].
ACCESSION   WP_357579473
VERSION     WP_357579473.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 150)
  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 150)
  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 150)
  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 10140345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..150
                     /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=16473
     Region          7..142
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04663"
                     /db_xref="CDD:467548"
ORIGIN      
        1 msevrvriaa yvvrdaptgp ellvfdhrdq peagtqvpag gvdageslee avirevaeet
       61 stvgitlrrs lgvqqrphph tgqprvtify yatttetrdr wshlvtesag tdegmvfdcf
      121 fvpvvqaldl lpdrqdefip vllkllsdea
//
LOCUS       WP_357579482             441 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357579482
VERSION     WP_357579482.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..441
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..441
                     /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=45859
     Region          2..441
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mgtevaviga gfsglaaala laragvrtrv leardrvggr vltrwladgt qldlgaqwvg
       61 ptqdlvngll arygiatfps aahgaspvif pdgrhaeape aaarvldlld ayaervdpva
      121 pwagaeaaew drttlagwlr taapdpatar ylgrllaggl laagpdeisv lqlafylrsg
      181 ggsrallama ggaqqdrivg gppvlaeala aalgpdavrl sapvraiaqd ragvvvhtdt
      241 drveadtvvv avpptlagri rydpplpplr daltqrmpmg saikvhavyp epfwradgrs
      301 gvafclagpv tetvdnstpa sprgaltafs ygpeanalrr mppgdrrasl ldalaavagp
      361 aarrpeefve ydwsadewtr gcfcgaptpg swcgygpelr qpvgrvhwag tetatrwagy
      421 ldgaieager aaaeilartg g
//
LOCUS       WP_357579514             485 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: argininosuccinate lyase [unclassified
            Micromonospora].
ACCESSION   WP_357579514
VERSION     WP_357579514.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Baruteau,J., Diez-Fernandez,C., Lerner,S., Ranucci,G., Gissen,P.,
            Dionisi-Vici,C., Nagamani,S., Erez,A. and Haberle,J.
  TITLE     Argininosuccinic aciduria: Recent pathophysiological insights and
            therapeutic prospects
  JOURNAL   J Inherit Metab Dis 42 (6), 1147-1161 (2019)
   PUBMED   30723942
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Erez,A., Nagamani,S.C. and Lee,B.
  TITLE     Argininosuccinate lyase deficiency-argininosuccinic aciduria and
            beyond
  JOURNAL   Am J Med Genet C Semin Med Genet 157C (1), 45-53 (2011)
   PUBMED   21312326
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415011
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..485
                     /product="argininosuccinate lyase"
                     /EC_number="4.3.2.1"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004056 - argininosuccinate lyase
                     activity [Evidence IEA]"
                     /GO_process="GO:0042450 - arginine biosynthetic process
                     via ornithine [Evidence IEA]"
                     /calculated_mol_wt=51091
     Region          9..451
                     /region_name="ArgH"
                     /note="Argininosuccinate lyase [Amino acid transport and
                     metabolism]; COG0165"
                     /db_xref="CDD:439935"
ORIGIN      
        1 mstpalttyq rhhlrptydh hvgylfpamv rasqahvvml veqglvpaer garllrglae
       61 lradtagape fdgtfedtyy lmekrlaqac giptseldvq marsrndlda gvfrmllreq
      121 llgvldrvla agataldsah ryadvvitgy thrrpaqptt ighalagyae alageavaya
      181 elidqlnvsp lgscafagtd ldiaparvae llgfdglvtn syeavagadh lvrvgtlnaq
      241 alatgarlar tlmdwlswrw vstpgdftqg ssimpqkrnp vvlehlvsma gataadaasv
      301 lnnvgaawwe dsnnattdvq vrlwesndrt drffallggf laeieplepp saeeivasga
      361 tttaaadalt rhgvpfraah svvgrlvrgg apatwtaqtv raaaegiadg ltdaavadli
      421 aaavrpelvl draqvdgpga davraqvavl rgtfdtvagr laavrdrlaa adealdavaa
      481 qgaar
//
LOCUS       WP_357579548             522 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: amidohydrolase [unclassified Micromonospora].
ACCESSION   WP_357579548
VERSION     WP_357579548.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 522)
  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 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..522
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53938
     Region          4..518
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mtnpstlyrg gtlhcpadps atallvtdgr iswlgvdada pvaervvdld galvtpafvd
       61 ahvhatdtgl alsgldlsav rsaaelldav agfaaglpsd avvlghgwde sgwpvprlpd
      121 aamldraagg rrvylsqasi hsalvsaall aacpqvvsaa gydasgwlrr dahhvvraaa
      181 fasvtraqrv aaqraalaha aslgiaavhe cggpeisdee dftgllalsg dgvaevygyw
      241 gelmgaarar elgavgaggd lfadgalgsr tahvsrdyld geggcghgyl saeqvrehll
      301 dcaahgvqgg fhaigdaais tvlegfagaa eklgtdrvra grhriehaei mnkrliagfv
      361 eygivasmqp afdrlwggag rmyesrlgld rslesnpmga mhgvgvalaf gsdspvtpld
      421 pwgsvraavw hhsptqrmsv rsafaahtrg gwravrldne gvlalgapat favwstpagv
      481 drglpvllaa dpeargpqdp tplpvcrrtv lrgdviyeeg ss
//
LOCUS       WP_357579590             943 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579590
VERSION     WP_357579590.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 943)
  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..943
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..943
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=101005
     Region          49..943
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msprihlpsg lvtfvftdie gstrlaqllg pdyrpvlreh rrllrrtiaa tegaellteg
       61 dsfflvfpda taaltaclta qralashewp tadamprvrm glhtgwaepr dgeyvspevh
      121 raariaaaah ggqvlcsast erhaqplppd aslhdlglhr lrgfddrerl fqlvapgler
      181 qfprprtada sahnlptpvt sfvgrhaert elkrlveahr lvtvlgagga gktrlavela
      241 vdlveshpdg vwfvdvaavt dpglvafeva avlglrpepg rpmvdtlvey aaarrmlvll
      301 dtcdaqpaas advisrllag gvgvrvlats resfglpgev vwripslsvd ppvggaesda
      361 vallldrtaa arggrppdpg esadlrrvvr rldglplaie laaarlrvls vgqlaerldd
      421 vlgtldagre dpeppvepdr adgrpdtvdl vaavgmvpps pavravqrsa terhltmqat
      481 vtwsyrtlgp raarllrwla vfagpvdlat vewllgddpl dplsvlvdks mvlaephasg
      541 styrmldpir ayaarrlaea geeksarnrh vawsthamer ahlgpdgrpv tlslyaldpl
      601 agelraalrw catggsarag lrlaggldqw wrerglareg rlwlfrlygr iaetgeripe
      661 aelaaayhmh slhagadgef aeelrysqra eaaarqagda gllarvlagr aaplvdmgqf
      721 aeaericrev idwasgqevl gdalfgvfsl aellwrrgal deaaellgaa rpveaarpve
      781 rgrrsvdmll gmvalargdl vaahehlqva lrsrmshgfh gracdtlnam avrcaaggdg
      841 ltaarlfgaa gatrasmrca pgiyggywaq rqgelrqelg datfdgayge gtelgleeaa
      901 alalavehpd lavgsarfga gharvaprqs vapdrrrhht gha
//
LOCUS       WP_357579591              73 aa            linear   BCT 28-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579591
VERSION     WP_357579591.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 73)
  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..73
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..73
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7028
     Region          1..46
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mpryefrcra cgdtfevnrp msqaaepasc pqghadtvkl lstvavtgrg gggaaggapa
       61 parggccggg cgc
//
LOCUS       WP_357579671             365 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine recombinase XerC [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579671
VERSION     WP_357579671.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 365)
  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   4  (residues 1 to 365)
  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 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..365
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=38354
     Region          1..365
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Region          <149..210
                     /region_name="PRK12438"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:171499"
     Site            order(217,311,314..315,346)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 mreavddfag ylaavrnrsa htvrayvgdv vslldhahrm gcaelpeldl avlrswlakq
       61 rtmgaartsl arraasartf sawahrcgll padvagalss prahrdlptv lradqaaalv
      121 eapgrfapav ppppaeddsr ppspdeddsa psspggegsr pappdgegsr paspdekgar
      181 paspessgpp paadqvaeav llrdrallel lygtgvrise acgldladvd harrvvrvfg
      241 kggreravpy gvpaqralde wlrhgrpala aphsrdalll garggrlnpt tarrivggya
      301 eaaglppisp hglrhsaath lleggadlra vqellghssl astqiythvs verlraayrq
      361 ahpra
//
LOCUS       WP_357579615             123 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357579615
VERSION     WP_357579615.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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=13106
     Region          33..108
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(38..39,43..45,59..61,70..73,75..76,79..80,82..83,
                     89..91,96..98)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mskqslpvvd lqavaccspi avrpleaeqa alvapmfkal gdpirlrlms miasvpeicv
       61 cdltpafdls gptishhlkv lreaglvdsd rrgtwvwyra rpeafrqlga lldlpagsaq
      121 ata
//
LOCUS       WP_357579795             263 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579795
VERSION     WP_357579795.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..263
                     /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=27982
     Region          19..214
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mapdahrlel vvdparptgr tllaagveqs yvdvteprhl hfeyvrrmaa vadlaappgl
       61 pldvlhlggg aqtlprylaa trpgsaqlvv erdpavvdlv arelpalpae vevrvadare
      121 alvdappagy dlvladiyra armpahvrsv efvaevvrtl rpdgiylvnv tdlpplvfar
      181 vqaatlrvvf advclvadrr mlrgrrygnv vfaaalragr lpvarltara ardpvpggvl
      241 hgptldafva garpatdaal apr
//
LOCUS       WP_357579895             455 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC1 kinase family protein [unclassified
            Micromonospora].
ACCESSION   WP_357579895
VERSION     WP_357579895.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 455)
  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 455)
  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..455
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..455
                     /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=48857
     Region          1..453
                     /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 mtdiprravs rtaklaalpl gfagrtvlgm gkrvtglasd visaeiqqrt aeqlfsvlgq
       61 lkggamkfgq alsvfeaalp eeiaapyrqa ltklqeaapp lpaasvhkvl aeqlgpdwrd
      121 rfvefddtpa aaasigqvhr avwrepgygp sgapqtrdva vkiqypgagd alladlkqls
      181 rlggmfraiq pgldvkplla elreriteel dyeleaesqr afaaayaddp eihipavvsa
      241 sprvlvtewv egtplaeiir egteeqrdea grlmailhls apqragllha dphpgnfrll
      301 adgrlgvidf gavarmpegt pepigriaal alqgdadevv aglrsegfig steeidaeav
      361 ldflrpmlep iaadefrftr awlrteatrl asprspayql srqlnlppsy llihrvtlgs
      421 igvlcqleak apyrgilerw lpgfapsagr psagg
//
LOCUS       WP_357579889             443 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357579889
VERSION     WP_357579889.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 443)
  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 443)
  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 443)
  AUTHORS   ter Beek,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..443
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..443
                     /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=47577
     Region          18..347
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mpvarsplpr aeadpgrrrv laamlgapvl atggltgcte gqaapvetgp velsvfwygg
       61 akraelterv lrlytdrnpr vgfrvtwqga ggyydrlatq aaggnvpdli qlddsmltey
      121 arreivldls gyvadhrldl rtlpqglvry gqvdgrtvgv aaaqtaaavv ydrtllrrlr
      181 lpepntgmsw aeyvawarrv trasegrvag tmdpsgdyra lwlwlrgqgg efyrgrqlgf
      241 dadalvewfd lwrrarssra tpsaalveqa dggeptqqlv vtgataasfa wshqlpelqr
      301 ltdaelglaa mpgppeaqwh rasmywaafr gtrhpdlvad vinfltgnge agsalgherg
      361 lspslavrsy vegnitepaq rraaalgtal aarlgpapsp ppqghlrvra llleaaesir
      421 ggrtgpraat trfmaqadaa lag
//
LOCUS       WP_357579931             104 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: antibiotic biosynthesis monooxygenase family protein
            [unclassified Micromonospora].
ACCESSION   WP_357579931
VERSION     WP_357579931.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 104)
  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..104
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..104
                     /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=11076
     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 mavvkinaid vppgageele krfaaragav enspgflgfe llrpvagenr yfvytrwete
       61 eayqawaagp sraahagtge krppvasgas llefevvqqv pprp
//
LOCUS       WP_357579950             529 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D family protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357579950
VERSION     WP_357579950.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..529
                     /product="phospholipase D family protein"
                     /calculated_mol_wt=58915
     Region          13..436
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
     Region          270..410
                     /region_name="PLDc_vPLD1_2_like_2"
                     /note="Catalytic domain, repeat 2, of vertebrate
                     phospholipases, PLD1 and PLD2, and similar proteins;
                     cd09105"
                     /db_xref="CDD:197204"
     Site            order(375,377,390,392,403)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197204"
     Site            375
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:197204"
ORIGIN      
        1 maprnwflsa aeranpvsel pvwssgnlae plihgaeyfd rlvdevqale agdhlfftdw
       61 rgdpdqrlrp dgptvaqlfa raaqrgvvvk gliwrshldl layseaenrn lsetvsaagg
      121 evlldqrvrr ggshhqklvv lrhlraperd vafaggidlc hsrrddaahr gdpqavqmsa
      181 rygdhppwhd vqlavrgpvv galdttfrer wtdpmpldse nplaylrdrl rgadlrpdpl
      241 ppqpadpppc gphdvqvlrt ypavrprysf apdgertvar gytkavrrar rliyledqyl
      301 wssevadlfa ralrenpdlh lvavvprfpd vdgrlalppn tvgreqalsl ceraapdrvh
      361 vldvenhagt pvyvhakvcv vddvwasvgs dnfnrrswth dselscavld gtladraptd
      421 paglgdgarv fardlrlrlw rehldrdpdg gedadlidpa davaaisaaa dalqrwyddg
      481 qvgprppgrl lphraerlpw ytrawalpay rlvydpdgrp lrarragtw
//
LOCUS       WP_357579972             154 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Micromonospora].
ACCESSION   WP_357579972
VERSION     WP_357579972.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=17447
     Region          8..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maqprwlder eqsawrgyrr mrrlldlela relmrdagls epdydvlsdl setpdqrlrl
       61 seladrmlws rsrlshhltr mqqrglvare ecasdgrgav vvltaegrra ieaaapghva
      121 avrrhlidll tpdevaalda lthrvvdhlt rpge
//
LOCUS       WP_357579979             113 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357579979
VERSION     WP_357579979.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   4  (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
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..113
                     /product="PadR 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=12347
     Region          1..101
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mkaqalhghl dalllavleq gslhgyaiie alrnrsdgql dlptgtiypa lrrleraghv
       61 astwstvngr errtyqltde grralagers gwrefrstvg rfldtdtppa apa
//
LOCUS       WP_357580035             253 aa            linear   BCT 28-DEC-2024
DEFINITION  sirohydrochlorin chelatase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580035
VERSION     WP_357580035.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..253
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=24983
     Region          4..241
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mseaadpvvl vahgsrdpra aeatralara vsaarpgtpv laswldhtep gpatvlrnla
       61 aaghpravlv pllltaayhr rvdvpaavaa aresgapiav rvtdvlgpsd gavdagllag
      121 lhrrlgeaga grfdglvlaa agtrdararg svgrvaaalr aglgvptrvs yasaappava
      181 aavarlrsrg agrvavsayf lapglfhdav ataargagav avsapltdap eladlvlrrv
      241 daasrlagit agp
//
LOCUS       WP_357580053             308 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357580053
VERSION     WP_357580053.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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 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
REFERENCE   4  (residues 1 to 308)
  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 308)
  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 308)
  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..308
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..308
                     /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=32383
     Region          6..269
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mrrfvftggt avvtgaasgi gealvhglar rgsdlvlvdr dagrldavva avraaypdrq
       61 ltayvvdlad aavtarvaee irrrhpalrl lvnnagvalg grfdqvslee fswvvdvnfr
      121 avaqlthall ptlrvepgah lvnvsslfgi iapagqtaya askfavrgft ealrqelage
      181 gigvtcvhpg girtriaqna rvgvgvpaee fetgrrqfek lltidparaa evilrgvhrr
      241 rgrvligwsa klpdllarva pvsyqrvlaf aldrvagdat rglttgspap aqrepeappa
      301 adpaggpa
//
LOCUS       WP_357580099             140 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Micromonospora].
ACCESSION   WP_357580099
VERSION     WP_357580099.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 140)
  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 140)
  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..140
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..140
                     /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=14992
     Region          4..137
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 malpngpvtp sseaeaalfd lvdvydraye aaaaelslsp aqacvlgrld errgmgalae
       61 elgcdasnit qivvrlealg lvtrepnprd rrarlvartp rgdetnrrfa taftfartav
      121 grlspdeqdq ltallrkalg
//
LOCUS       WP_357580069             279 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357580069
VERSION     WP_357580069.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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 279)
  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 279)
  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 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   6  (residues 1 to 279)
  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 279)
  AUTHORS   Rosinski,J.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..279
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..279
                     /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=31476
     Region          1..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          108..263
                     /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(109,111,113,122..124,126..127,132,141,148,150,152,
                     154,163,165..166,168,171,177,179..180,209..210,212,214,
                     224,226,228,230,236..240,247..250,252..254,257)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mddvfralad asrrrllddl nrrdgqslre lcagldmtrq svskhlvvla aanlvttvrr
       61 greklhylnp vpinavaerw idrydrervr aladlrtale repmdsptfv yttyvnttpe
      121 rlwaaltepa ftrrywggva lrsdwrvgsp vlwqdepgge frdlgqrvlv aepfrrlsys
      181 whgfqpehaa hfgwsdeela arlgerrsrv tfdiapyggf vkltvthedf spgsemyrav
      241 sgqldgsggw pellaslksl letgeplpep rpesataqg
//
LOCUS       WP_357580127             416 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580127
VERSION     WP_357580127.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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 11461692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43546
     Region          <172..407
                     /region_name="LytS"
                     /note="Sensor histidine kinase, LytS/YehU family [Signal
                     transduction mechanisms]; COG3275"
                     /db_xref="CDD:442506"
ORIGIN      
        1 mggnlsgvfg vvsllaalga alfavvrlra rrgiatatqr atyevlhtag laaeplragl
       61 stanaakair hlralvgaag laltdresll aldgrgghhh aqlvaaarra vatgrstvlg
      121 epelhcdrvd cpvrgavvap ltgadgrrvg vlvavadgqp epglvqatle tahwagnqla
      181 laeldssrer laraevralr aqisphfiyn altaigsfvr tdpdrareli lefaeftrys
      241 frahgefttl aeelrsidry ltierarfgd rlqvrlqiap evlpvtlpfl clqplvenav
      301 rhglsrkpgt gmvsiearda gtechitved dgvgmdpstl tagiaelaga agepgdaala
      361 gvgddpgqhv glsnvderlr svfgdgfglv vetglgsgtk vsmrvpkfhp gvrags
//
LOCUS       WP_357580163             291 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TauD/TfdA dioxygenase family protein [unclassified
            Micromonospora].
ACCESSION   WP_357580163
VERSION     WP_357580163.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..291
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..291
                     /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=32397
     Region          21..289
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 meehvlaave rattrppery dtitvrpisp vigaevsgld latelsdgql aevrraflah
       61 hvlvfrdqvl saedhkrfag lfgelrrqpl adldggdpav leisagrdsr fvagedwhtd
      121 gtaeaepslg smlyvtrtpe igvggdtlwa nmhlayemls ppmrafldgl taihdglipw
      181 qghtpppeyv vpksehpvvv rhpetgrkll fvnagftshi vqlsrhesra lldmlfgwva
      241 qqpilscrvr wtpntlvfwd nrctqhhavw dyyphsrygq rvtingsrpv a
//
LOCUS       WP_357580164             351 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FAD-dependent oxidoreductase [unclassified
            Micromonospora].
ACCESSION   WP_357580164
VERSION     WP_357580164.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..351
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..351
                     /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=38201
     Region          8..321
                     /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 miaghwevvv vggriagact awalapyaer vlvldasrpt aywpqqstwd rsgnlawael
       61 glletvlacg aprtygdtqr igedvvervy predaysyrm svprevldpa llaaargrgn
      121 vtvrrparvr dltidggrvr gvtvrhgavd sevtcdllvl adgrlsrnae rvgaeayrvv
      181 espwfallay yenlplptdr syfslqdrsv listpcgdkq wcvaldlhqs lidetgrhpa
      241 rsyermvrdd pylgpavaag rrstsiggag rmrmlrrpms gpgwclvgda gyhldpvtaq
      301 gtraavvtar ilrdriagag rvagadltgl tgerdaaldd dwayteqivr g
//
LOCUS       WP_357580204             862 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease, partial [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580204
VERSION     WP_357580204.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 862)
  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 862)
  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 862)
  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 862)
  AUTHORS   ter Beek,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 862)
  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 862)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..>862
                     /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          12..822
                     /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 mfratlksll arkvrlilsg lavvlgvmfv sgafvltdtl grsfdaifad ayegvdvnva
       61 akpkidgsea egmpvvaapv paatldkvra vpgvaeatgv vgvdgarlig gngkvvasfg
      121 ppqlgenwtg esdlvrlreg rapqaddeiv inkalatagk vkvgdrvgvl tlqpkqefti
      181 vgvfgysggr dsigganeim fttpvaqklm lgapdtfsnl svtaadgvsd ealrdavaaa
      241 vgadfevktg tqlsedaaag mkealsffnr illgfaaval lvgtflilnt fsiivaqrtr
      301 elalmravga sgrqiigsvv leavavglva svlglgagig igallaylfs tfaggltlag
      361 igvplsavvg afsvglvitv vaallpalra srippiaamq dvatpdrplt kvtvagaivt
      421 avggallalg ltgnaggntl atilggvlfa figvalltpl isrpvvsllg alfawsvpgk
      481 lgrlnsgrnp rrtaitaaal mvgialvtgv tvildsakss igglaqdslk aelviagaqs
      541 gprppsfdpa vlekaaaipg vrladgeygd lamvggqrtw vaassdvaal rlifgaepta
      601 gdidrlapdg mlvssdtata rglsvgskvp vqtsrgeart ytvtgiyass qltnpvvlpa
      661 eaasgfaipq piqgfiqlap gtrvadvqpq iealladspe vsvadreafi eqqtgqldgl
      721 lmmiqillal aiviavlgii ntlalsvler trelgllrai glrraqtmrm itveavvisv
      781 fgallgvvvg aglgaavvea lrdegitdlv lpwtqmgifl glaaivgvva aarvqsrigp
      841 leqetersra dvgemavtay kt
//
LOCUS       WP_357580232             378 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580232
VERSION     WP_357580232.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..378
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..378
                     /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=40122
     Region          11..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 rhgidavvye reagrsarsq ggsldlhpes gqralaragl
       61 agrfrsearp egeehrildp agrtlvhhtp rpgsfsgrpe idraalrdll ldslpgdava
      121 wqhrlvaatp qpdggfgltf dgghradcdv lvgadgarsv vrslltdakl syvatlvels
      181 isdadrrhpd iaelvgpgnl wcvgvnqila aqrlgdggir vgislraddr hldtyrskra
      241 llemfdgwdp gltalieagd saptprriea lpigtrwahq pgvtligdaa hlmppvgega
      301 nqamldgael agelaanpad pdsairayee amftriipia emsarvqamm lsptaaddiv
      361 rfftprpaqq elappyeg
//
LOCUS       WP_357580243             231 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357580243
VERSION     WP_357580243.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     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=25300
     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 mnrtdrlyal veelravspr prsarwlaar fevssrtier digalqesgv piwaepgrtg
       61 gyaldrartl ppvnltpvea vamavalhrm rgtpfaaaag talrklisvm paadaaeahr
      121 laarvhligd gpvtpvpaav adavrarrvl rlryadrsga gslrdveplg ylgnprhwyl
      181 lgwcrlragi rafrvdrits vttlaervpe relsaddidi pqerirrlsl v
//
LOCUS       WP_357580251             419 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580251
VERSION     WP_357580251.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 419)
  AUTHORS   ter Beek,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 419)
  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 419)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..419
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42910
     Region          15..415
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mtttvvqkdg pgavtppptl gshvrnyvsr vrggdigalp avlglvvlct vfsimrpsfl
       61 tagnfanlft qgaavtliam glvfvlllge idlsagfasg vcaailanvv tvlgypwyva
      121 vlaaivtgva igttlgflva kigipsfvvt lagflafqgi vlmlmeegtn isvrddvlva
      181 ianrnlspvl gwvlaavava gyaavqllrh rtraarglvt dpiavvfari gglalilgaa
      241 vfilnlersr nivisslkgv pivvpiiavl lvfwtfvlqr tsygrhvyav ggnkeaarra
      301 ginvdriris vfvicssmaa iggivaasra nsvdpntggs nvllyavgaa viggtslfgg
      361 kgrvldavlg gavvavidng mglmgyssgv kyvvtgvvll laasvdafsr rrstatgnr
//
LOCUS       WP_357580272             860 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580272
VERSION     WP_357580272.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 860)
  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 860)
  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 860)
  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 860)
  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..860
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..860
                     /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=91356
     Region          13..843
                     /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 mesadsrnsv ppgrarpffa fvwsvsalaa vlcvrplldl paelprlpva fwvmaalavg
       61 cdarpfvppg rrqtsavfps tcftfaillg wgfgpavlvq avavvvsgwr mghapwrtaf
      121 naaqyaaalg aayavtwlgp gsifdggrlr gtdvlavgga tvawfavnya lvsaavrlrf
      181 gdrwwpslrq glgfellstg sllllapvlv aaarasaali plvlvplfav yrmarlsveq
      241 qqlasldplt glpnrkalla evgeqvhvhs eraargepaa rlalllidld rfknvndalg
      301 havgdrllve vsarltdvvg egmvarlggd efaivmtglt dvdearelag rvvralaepv
      361 sldglpldvg gsigialfpe hgedfatlmr hadvamydak hrndtvaiya aesdhnsaer
      421 lglladlrrv leagrpetap pagdgagapg dgavavpatp ggrlrgdgra ggarggdgae
      481 lpadvagltp ssgrwrlrrr rerpgpppgd elinrivtaa dpirrrtmaa getgpdrgdg
      541 pgrrngaghp ggqggavvrr qgppvddgag drggdraptg rrgarhdaag rrdadtaaai
      601 dageitmyyq pqvaiatgev vgveallrwr hprrgmvdpe elirvaeqsa vmrlltrrvv
      661 ddvveqlakw saagmglpaa lnvsvrdlht geiadqiadr larygvppqr lqleitegal
      721 madprrvlat itrlhrigvg islddfgtgy sslqhlrrlp lsevkvdrsf vlgmvedadd
      781 aaivkstiel akalglrvva egvedertwr mlhaagcdaa qgwfyarpmp aeelvgwlar
      841 yrpvrptpsp daeiprrhar
//
LOCUS       WP_357580405            1825 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580405
VERSION     WP_357580405.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1825)
  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 1825)
  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 1825)
  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 1825)
  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..1825
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..1825
                     /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=194381
     Region          6..1303
                     /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 msdscqrypa lavqrgmvlq tlrqpaggvd vqqvtirwdg mpdrdafsaa wqaatrrhav
       61 lrtafevdgd hgvaqvvrst vapdlrwret tlddflatdr yepfdvgrap mlrvtalsdq
      121 hvvvtfhhai ldgrstrmll devladyaar ragrvpdppr rppfadfvhw wgtrdpstgd
      181 afwkghlaga pmpralpgrl dtdpdargvp vshevvvtrp dsdrlraaaa vagvgvsavv
      241 haawallrgg yggvddvtfa vtrscrydsv pdaekilgll lntvplrirl dpgwtvrrll
      301 advagrirri rehqltplht vldqaglapd tplldslvvf erqrlstala eggpeearrs
      361 arvhrmpgyp ltvhafdepe lrlgvtwdgt rlldasarri laqlhrtvle laerpdarla
      421 dldlgaagea plraawnatr rpyprdnsvp evfaarvadd paatalvvgd ravayaeldr
      481 aadrlawtlr rhgvagetpv avllprgepl irallgvlka ggaylpvdas apparianll
      541 aasgtrlllt taatapdlpd lgpvrvldvd apagepapag pppgrihpsq laavlhtsgs
      601 tgapkrvgit hrgvvrlvag pdfatlgpge rllqvaptaf dastweiwga lltgatavva
      661 ppdpvdltrl talirdggvt valltaglfr qlaeedvtsl agvrqlltgg dvadpgavra
      721 vlaardglpl vnaygptent tltschrmsg ggpvgdrvpi grpvpqttvh vldgsgrpvp
      781 vgvagelytg gdglargylg dpaatarafv pdpqapgerl yrtgdvvrwr adgvleflgr
      841 rddqvkirgf rvepgeveaa lrahpqvasa avgvrgdgpe rhlvgyvtpa gpaaptkasl
      901 rahvaarlpa hlvpaayavl drlpltaygk vdraalpapg paeedpdvag pasptehrla
      961 elwsrllpgg rpparigres sffalggnsl tatrlmfrir eafgvelgvg pfyraptlaa
     1021 taatidattg sapgdraqag palrrrdrvp hgsgrdlpah larltdgwal wrtvclrgag
     1081 lpvdllaplg daelaaaadr vvaaradgdp agvaaaeaay aaaypeavgr lavalhtvaa
     1141 hprfreavaw qnphalrtgv dallrrgada ptrntkhrqh ealvtsylqr ycakndtigf
     1201 fgpvgwarie pgagvrvdpa dppallaert vylegwavaa vlapyaqrlr pwlvprlmpf
     1261 lelagttlrv plappvaltd aeaavlracd gvrdahevag avlaepgsgl rstrevhevl
     1321 etlagahria wqpevaphdt rpertmrarl arvtdeavra palaaldelv aardaltsaa
     1381 gdperltgam agleatftrl agvpatrrag tmyagrtpvy eeclragsvg vgeasldgir
     1441 dalglvlesa rwftaagatl yrrlcaeiyr rraaelgtda vpladfwlla gealfhpprr
     1501 ltdlltaalh rrwadvlalp pdrrrirlta aelapavaaa fppgrpgwpt arqhspdlmr
     1561 agdewvlgel hpgvntlrya twvayhpead alraalardv gagavypaet gqeggvptrq
     1621 snalagpddv rlvfahdsfg hdprrslrvg ecdlvevagg lrvrsrdgrf dvdlmhvlgd
     1681 vvgaglsqlf rvlppaahqp ritidslvvs reswtfaaad lafadtrdea lrfrqarawa
     1741 gahglprhvf lrcagerkpv hadltslasv dlvsrsvrra rrhggddatv gvvemlpapd
     1801 qlwltgpdgr ytaelrvvav dgqvr
//
LOCUS       WP_357580406            1111 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580406
VERSION     WP_357580406.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1111)
  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 1111)
  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 1111)
  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 1111)
  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..1111
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..1111
                     /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=115601
     Region          1..>1045
                     /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 mavfefpasa aqrrmwlldq ldpgqptyhv gwavwldgpl dtaaldgawa aavarheilr
       61 trfranggrp iqvidddapa taievvaldg lpvadreaaa raalrehart plplergplt
      121 rvrllrlapq rhvlalvahh aiidgwsvrl lldelsadya alragrppvs vepplqyadf
      181 alwerehdda gghaeaerfw paelagappe vplpvdhpyp drlspaaaev avpvdgelag
      241 alrrlagarg stlftvllta yaallsrlgg addvlvgvpv agrtrietep mlglfantva
      301 iratlhgdpt laelldrlha ataraqahqd lpftrvvelc rpqrqptrap lvqvmctvee
      361 alptlergal rwrpelvptg tgkfelelaa vagpdeltvr lryltdlftp dgagrladal
      421 gailaalata pqtrvcdvdl lspatadlvt rvwpaarsgs lpppectaaa lvadvdagdr
      481 vviegddatl tgaavrglag riatglrglg vrvqetvgiv lprgarplpa llgvwwvgaa
      541 ylpldpthpp grlrgmlada gvrvvvtdsg gvpapllael aasvtlldla epagsgaqpa
      601 vpagaeaqpv lpppcavpas aaayvlftsg stgrpkavtv tqgavahllh afremvplgp
      661 adrvlsvspf afdialldll lpllcgapvv vagdddvidg nrlrrllatt gatmlqatpt
      721 twrmlvaagg vpagvrlrls ggealprala dalaepgtrl wnlygptett vystgaevep
      781 gsappdlgpa vtgsrvyvld rwlrpvppgv vgevciggag vgrgyadapg wtaerfvpdp
      841 ftpggrlyrs gdlgrwlpsg rieplgradr qvkvrgfrve taeveavlrg hpqvrdavvt
      901 avsdvahdgv rlvgyvvtdp psadppadlp eyarrflpah mvpavlvalp evprtsrgkl
      961 dlralpppgr gagsgeppva prsplerela glvadllglp gpvgvadnff vlgghsvkat
     1021 qlmarvwtty gidlpvrtlf ddptvaglaa avtaagagnr atpagaapag tgapgagapa
     1081 gpdgagyldt ltdddvddll agmdgpsrwd g
//
LOCUS       WP_357580507             292 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580507
VERSION     WP_357580507.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 292)
  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..292
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..292
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31430
     Region          11..292
                     /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 mtitipgfdy qrvavdgdvt mnvavggtgs pivllhgfpq thvmwrhvav dlatdhtvic
       61 pdlrgygasd kpdardvdty skrtmaadiv tlasrlgher falaghdrga lvairagldh
      121 patithlail dvlptldmwd ilhgssaava fhlylmaqpp glpeqmisas adaffgyfld
      181 vwaknpqaip adlraeylna sreavpsiva dyrasagidi ehdqadraag nrlpmpatvv
      241 qqdwgaalgy daaalwhtwa adldhrttsa ghfmaeeapd eiikvlrsll ar
//
LOCUS       WP_357580548             284 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580548
VERSION     WP_357580548.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   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 284)
  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..284
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..284
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31275
     Region          6..277
                     /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 mielddgaql rtwttgspdh adiplvmlhg gpglpdylgp vagmvedlcp ihrydqrgtg
       61 gsgwegehti arhvrdlasl ldawgrdrav lvghsfgtnl acyftlahpe rvagliqiag
      121 pfldpwrdad rvaqrarrse aqqdrlddle anasrtdaee ieyltlswft dhadrnrawd
      181 walasahalr pvnyvmnsql naakkadple shvdelrerl pvgtviigga ddsrpaealr
      241 rlgahlecev vlipnaghhp wleapdqfta afrtavatqt rkrs
//
LOCUS       WP_357580567             306 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase family protein
            [unclassified Micromonospora].
ACCESSION   WP_357580567
VERSION     WP_357580567.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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..306
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..306
                     /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=32556
     Region          31..284
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtgteptarr elrppagyrl aasvraltfs pydpcarvaa gtfwwaartp dgpatlalrp
       61 aggallaegy gpgadrvvqw adaiaglrdd vsgfgalaaa hpvvarlaaq hrglrmpatg
      121 qvfrqllrav feqkvtgkea yrayaatvrh faeaapgpmq plllppepaa vaatpywvfh
      181 pfgveqrrae tlrrvaavad rlercadsae atrrltavag igpwtaaevv riaygdpdav
      241 svgdfhvpnt vawalagepr gddarmlall epfrghrgrv cvllaaggvq apkygprmpi
      301 rsfarf
//
LOCUS       WP_357580582             158 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Micromonospora].
ACCESSION   WP_357580582
VERSION     WP_357580582.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 158)
  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 158)
  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..158
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..158
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17917
     Region          7..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrpaaldwsv enctiarame ilgerwtlvv lrevfsgvrr fddmrvrtgv prqvlanrla
       61 mlvergvlrr epyrepgsre rheyrltgmg ldlwpvlvav lgwgdrylad pegspltvah
      121 rdcgaevrve lrcerghevd rprdvvprpg pgarrrag
//
LOCUS       WP_357580606             363 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357580606
VERSION     WP_357580606.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 363)
  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 363)
  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..363
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..363
                     /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=36543
     Region          22..361
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msaptapaag rpagrfrvgv tslpgrslvr igpvsvqvrr rsvlvaaalv vlllaagvls
       61 lslgtpyvap advlralsga gtpydlvvld lrlprlvlaa vagatfgvag tliqsvarnp
      121 laspdvvgit qgaglaatva lttgaaavlv apaallggla aaallfllga rhglaaqrfv
      181 lagvavafal ralievvllt adpidglraq iwligtlagk gwneslwial tlaallpvla
      241 wagwalnsta ldddtargig lrpvarrvgl agtgvlaaam vtaqvgavdf valvapqlar
      301 rlvraerppl lcaallgall lvladlggrr lfaptqlpag vltaaiggpy liflllrgrr
      361 rps
//
LOCUS       WP_357580616             345 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [unclassified
            Micromonospora].
ACCESSION   WP_357580616
VERSION     WP_357580616.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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 345)
  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 345)
  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..345
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     Protein         1..345
                     /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=36399
     Region          5..330
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msagrklrag liglgamgrn harvlagldg velvgivdpa gdttgtlrap vvpelsdlla
       61 lgvdyavvac ptalheqvgl elaangvsal iekplaqsvd aavrlveafe aaglvagvgh
      121 ierynpalqn lrtrleagel gevyqvvtrr qgpfphriad vgvvmdlath didltswvtg
      181 qeytsvsart vsrsgrlhed mvavvgqlad gtmvnhlvnw lsplkerstv itgdrgcfva
      241 dtltadltfy angaidtewe alrafrgvae gdmvryaipk repllveher frdavegkes
      301 divtlrqglr tvevagavlr satdgstitv gtgtaspagd tvptr
//
LOCUS       WP_357580684             441 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580684
VERSION     WP_357580684.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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..441
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..441
                     /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=47351
     Region          1..414
                     /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 mdaqpsvavi gagaaglatl kaladvgvpa vcfesadrvg glwvygapgs payrtlhlnt
       61 sktrtefvdh pmpahwpdyp dharvagwlt dyadrfglhd avrlrhtvdr verggdgrwt
      121 vhadgpdggv evtvdavvva nghnrapkpp tpahpgdcta eqlhshayrg pdqlagrrvl
      181 vvgggnsamd iavdasyaar rtllslrrgv wvvpkhllgr psdtlngala rrlpwrlrqr
      241 itqrllaatv gaptryglpa pahgflqdhp tlsdgllsrl thgeieprpg iagfdgdrvt
      301 ftdgrvdevd lviwctgyrv eipfldpall gdgadtlply rhvfhldapg lafvglmqst
      361 gaafplveaq aklvaaqlsg ryalpethrq raacraelra atarwgqrrp amrvdfdayl
      421 aelrrelaag trrargsgat a
//
LOCUS       WP_357580721             541 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580721
VERSION     WP_357580721.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 541)
  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..541
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..541
                     /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=55265
     Region          8..259
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,32..33,62,67,72..75,87)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,70,86..89,93,95,132,134,
                     136..137,139,149..150,153,167..170)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,70,86..89,93,134,136..137,
                     139,149..150)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,93,95,132,134,136,153,167..170)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(149..157,163..170)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mtgwqvsgyr pvrqlgagas grvdlavhea tgtpvaikyl tggigddpaf rtafraearl
       61 lagiddphvs rlyeyvespg gaaivmelvn gvslrqllra hgattpesal cvlkgslagl
      121 gaahargvvh rdykpenvlv taegtsklad fgiampvges sgvsvtgtpr ymapeqwtga
      181 paspacdiya atatfyeclt grppfdgrnl ltlrqqhaha piptepapep vhellrhgma
      241 kqpaerpqpa qvflavlerv aadaygrrwe erglrelarr aallaallpf pdgtggatsv
      301 astafgeatd rwtwlrsgra raalvgggla aalllggagf syagreeplp aagtpapeap
      361 aeptgapses apapsptagt tpsptppvap tattaapepa gtgapttsap apptasasas
      421 aapadtvaps vdrvaaspge ldprgcpygp tsstisavva ddrtatgelr vslrytldgr
      481 ttevpmasga rgvfrgvlge lpqpksstri pvrvvavdea gnaspegppv yvtlrsfctp
      541 g
//
LOCUS       WP_357580755             444 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580755
VERSION     WP_357580755.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..444
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..444
                     /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=46622
     Region          5..444
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mtdrtdfaav eaelaergft rmafeldkie slldllgspq raypsihltg tngktstarm
       61 idsllrafgl htgrytsphl esvrerisld gepvdegrfv atyreiepla rlvdersaep
      121 ltyfdmttal afatfadapv dvavvevglg gaedatnviq agvcvltpvg ldhtewlgdt
      181 iqdialakag iihkgatvis aaqeeeaagp ilercaevga tiaregaefg vlrravavgg
      241 qvltlqglgg vyeevfiplh gahqaqnaav alaaveaflg agakrqldve avregfatas
      301 spgrlervrs aptilldgah nphgmaatvt alqeefafsk lvavvgvlad kdaasllell
      361 epvvdqvvvt rnsspralpa relaalaaev fgpervevae empdaieaav amaeedvpge
      421 lsgvgvlvtg svvtvadarr llkr
//
LOCUS       WP_357580773             299 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357580773
VERSION     WP_357580773.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 299)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..299
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..299
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30949
     Region          81..279
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mssptiaarp rpvarlagla vaavlataga laappaaqaa anpyergpap tvalleasrg
       61 pfatasqsvs slsvigfggg viyyptstae gtfgavaisp gytaawssid wlgpriashg
      121 fvvigietnt rldqpdsrgr qllaaldylt qrssvrgrid asrlavsghs mggggsleaa
      181 varpslqaav plapwnldkt wsdvrvptli iggesdsiap vsshsepfyn sipassekay
      241 lelngashff pqtvntptar qavawlkrfv dddtryeqfl cpgpsgsaiq eyrntcpsa
//
LOCUS       WP_357580774             410 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580774
VERSION     WP_357580774.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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 410)
  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..410
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..410
                     /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=45070
     Region          20..407
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(57,64,90..91,98,102,109,240..241,244,248..249,252,
                     285,290..291,294..295,297,321,348..350,353..354,356..358,
                     362)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(64,84,86,89,91..92,177..178,188,239..240,243..244,
                     248,291,294..296,397)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mvdfsaaptt qidsrggkcl yaqidefraa gpavavelpe gmlawsitrg dvvrrllthp
       61 gvsrnvkknv psytpgeikw lspwvdvesm staegrehqr lrqlvapalt pkridamrph
      121 velvarrlld dlathpadep vdlhtiysqq lptrvicdlf gvpddlrpev lrilrvvlnt
      181 dnvpeeesaa vyvdmnvamr tlidlkrrep sddltsflma arvegeepls eqelvdmlll
      241 ligggsqttv tlidhtvrel lanpdqlatl ladparwpda ieealrahcp vaalpmrwak
      301 edidlgegvv iragdailis ylahgrdpav henpdvfdid renkehlafg agphfcpgar
      361 larleaavav palfarfpql alavapdeiq plrsfmandv aslpvllnhr
//
LOCUS       WP_357580791             829 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580791
VERSION     WP_357580791.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 829)
  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 829)
  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 829)
  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 829)
  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 829)
  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..829
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..829
                     /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=90710
     Region          106..827
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 megtvyptgd adgsatapng daqapeagpg vtvpaepvrp dtptatagga gaaaegvllp
       61 fpadvvgdhm psagfalsta ptgrrvrarl arfnapwqss qvsevlepli sthrdahpka
      121 darllqrafd taarwhsgqy rksgdpyith plavatilan lgmdtttlva allhdtiedt
      181 eytldqmrad fggevallvd gvtkldkvkl gdaakaetir kmvvamakdp rvlvikladr
      241 lhnmrtltfl prpkqeqkak etleilapla hrlgmntikw eledlafgtl fpkryeeinr
      301 ligehqpqre allrqvtqkv qtdlkaakik aettgrpkhl ysiyqkmivr grdfndiydl
      361 vgvrilvdtv rdcyaalgvi hanwqpvpgr fkdyiampkf nmyqslhttv igptgkpvem
      421 qirtyamhrt aefgiaahwk ykehkgtqiv gppahidemt wlrqlldwqr eaadpsefld
      481 alrfdlssqe vyvftpkgdv iplptgstpv dfayavhtev ghkcigarvn gklvplestl
      541 sngdvieift sksdtagptq dwlgfvkspr artkirqyfn kerreeaiea gkdaivkamr
      601 kqgmplqrml tsdalmaiar dlhladvasl yaavgdsqvs aqsvvqklma ayggeegaae
      661 diaetavatr pprsrqssad pgvvvrgvsd vwiklarcct pvppdsvfgf vtrsggvsvh
      721 rddcanaedl raqaervvev swkltsastf lvaiqveald rhklladvtr vlseervnil
      781 satvtttrdr vavsrfsfem adpkhlghll aavrkvdgvf dayrvtsga
//
LOCUS       WP_357580807             444 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357580807
VERSION     WP_357580807.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     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=48163
     Region          36..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(148,150,291,293,322..324,367)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrpttrpkal lallltavla atgcgsgags sadgpvrllv fgapeelaay rtlveayeka
       61 rpgadvqlve asdrkdllar latsvaggap pdaflmnyrf ygqfaakdvi eplddrlaas
      121 eavdpadyyp vawnafrwqg rqlclpqnvs slavyynrtl fakhgvpepr agwtwndlva
      181 tatamtrdsr gvvvkatese gaalrpavhg lgvepsiirl apfvwsggge ivddpakptr
      241 ltldtpaare alknlvdlrl aygvvptdee veaeddesrf angrlamlms srrstttfrs
      301 itgfewdvap lpvykeqvgv lhsdaycmtr gakhkdaawr flefaiaeeg qriiaatgrt
      361 vpshigvsrs paflspaqpp rsakvfldai ptvralptvs twpeiedvty gilenamhrg
      421 drlddvirdl drqtrpifar gehg
//
LOCUS       WP_357580823             175 aa            linear   BCT 28-DEC-2024
DEFINITION  Rho termination factor N-terminal domain-containing protein
            [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580823
VERSION     WP_357580823.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..175
                     /product="Rho termination factor N-terminal
                     domain-containing protein"
                     /calculated_mol_wt=17555
     Region          53..>143
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
     Region          130..>158
                     /region_name="Rho_N"
                     /note="Rho termination factor, N-terminal domain;
                     smart00959"
                     /db_xref="CDD:198027"
ORIGIN      
        1 mtdptrdvad lvtallrglp aadlaalaeg rarlavvpvd pappapttpa gqpaaaradr
       61 pspaghpaae sadgttpagp paaestdrgg aparpsarra asapdpvaar aalasmsrrd
      121 dgtaylsgwt ardlrvlaas lelrgvaglr kadlvarivd rtigfrlasa airrl
//
LOCUS       WP_357580838             149 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357580838
VERSION     WP_357580838.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 149)
  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..149
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..149
                     /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=14884
     Region          29..134
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 myvsarsdya lramlavaaa apvgggglvk agtladsqgi plsflqgilv dlrragllvs
       61 hrgteggyal arpaveisvg dvlraiggsl ttvrglpaer agyagvatgl rdvwlavhga
      121 ialvvdratl adllgaehlp agagenrah
//
LOCUS       WP_357580919             241 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357580919
VERSION     WP_357580919.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 241)
  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..241
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..241
                     /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=25584
     Region          4..226
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtfapvprss vsdhvfgqir daivsgvyrp dealpgerel aatfgvnrha vrealrrlqq
       61 lglvrvsqgg atrvldwrvh agldlalslt rfhdtlpvdt lvrdmlemra cigvdaarlc
      121 aergdpavra ailraveeya glapdltgmg eativlwrhi vagsgntayl lafnslvaga
      181 lavgevppqr raaelldvag hrrladavvt grsadaarea ralltapltt paaaprrear
      241 a
//
LOCUS       WP_357580982             348 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049060].
ACCESSION   WP_357580982
VERSION     WP_357580982.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 348)
  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 348)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 348)
  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..348
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..348
                     /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=36663
     Region          121..346
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrglllalis afgllavpga alrlgfalfl lmvvgavvdy wagfsggsaq lalaftavrv
       61 vaicvtqeqt ggqpnqwavn alttvaitmq wdwspkvslp avagllmvdv avvgvregvp
      121 lglrllvecv marlafvllr qssrrvdtlw arqaalarae avavarhrqk reflallhdt
      181 asatfllvta hgrdtdpgqv aeyarhdltv ltgaadgqas qdspveltaa lrsvvgrspl
      241 sirvrwqaem vvpasaalal vravrealtn vdrhagvpna tlsvdlegnr mvvtvddagv
      301 gfrpeqvphs rrgirgsiie rmtaaggsal vtsrpaagts vrlvwpdg
//
LOCUS       WP_357581010             515 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase, partial [Micromonospora sp.
            NPDC049060].
ACCESSION   WP_357581010
VERSION     WP_357581010.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049060
  ORGANISM  Micromonospora sp. NPDC049060
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 515)
  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 515)
  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 515)
  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 515)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Micromonospora sp. NPDC049060"
                     /db_xref="taxon:3154828"
     Protein         1..>515
                     /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]"
     Region          <2..>515
                     /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 mpfdklveht rptrdrhtpp liqtvfttme gtdpaplhta tmrplpideg vakfdltvqv
       61 qvepdgvrvl fdyacdlyep atmaeladsy ralvaavlae pdrplstvva vtaaqrerla
      121 daliaspvpv ppgdlgcvpr lvtetarrqp dalavvdgtg aityreldew snhlahqllh
      181 hgarpdhpva vslppgtpai tamlavlkag aaylpidpta pparrhhlit nsavtilitq
      241 dphdtdtppg vvalaphpap atatatpppl dvhpeqvayv ihtsgstgtp kgvmvphral
      301 tnlvhwhlna hptgpgqrhg qvaslgfdaa iweiwpalvs gatlhiadpa drldpaalhd
      361 wlvredvtrt flptpiaeav lrlptpstsr lrtiftggda lttrpsahap ytlfniygpt
      421 ettvavtvgp vrpdgvhrpd lgvpiagari hlldadlqlv ppgapgevcv agdvvsrgyl
      481 nkpgqtaerf lpdpygppgs rlyrtgdlcr lrtdg
//
LOCUS       WP_357581075             522 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581075
VERSION     WP_357581075.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 522)
  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 522)
  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..522
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..522
                     /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=53876
     Region          <89..>261
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          179..400
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
     Region          <454..509
                     /region_name="PLN02217"
                     /note="probable pectinesterase/pectinesterase inhibitor"
                     /db_xref="CDD:215130"
ORIGIN      
        1 midsadgrqr rrgpavspvl rpalwsalla avastvlaap ayaepgipvt vpdtgsrpvv
       61 tgplqlpgap agttpglvpp algtpgasal etqinaaear vaelgtrlle leqqrnevqt
      121 qflaaerdle fargavqqaq qradqvaaea ikaaaalppg gfatdlrdle llrranrgek
      181 vdhatgpaag elartradeq vatqaytaaq srlqgveqqy tatqqalrda eakliklrde
      241 nsaqlvelar qqeaaeqqlg adyvdqsagg mvahptalaa vayarkqlgd pyvwgatgpn
      301 sfdcsglvws ayrsagyyql prvsrdqyya trsrtvqrda llpgdlvffa sgsswrtihh
      361 mgmyigggkm ihapttgdvv kistvrwsrl yaatrvvgav papttsptps qpptpkpkpt
      421 pkptpkptps ktpkpttspt psptpsgsqs ptpspsgstt psatpsdptt psatpsstas
      481 ptlgassfap ttsagtadpt saassaaped sasaspsaag gr
//
LOCUS       WP_357581110             260 aa            linear   BCT 28-DEC-2024
DEFINITION  IclR family transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581110
VERSION     WP_357581110.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..260
                     /product="IclR 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=28251
     Region          8..258
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrdplaepsd lirsvsralr vlesvgrapr gltvkqiarr celtvattyh lvrtlayegy
       61 virredgtyi vglevadryr elvaafrgsp aigeslrraa letgwshflg rfvggqvait
      121 avaegnrspy ledlvpgfde gahatalgka llatltteqr hrylreygmr pftsatlttp
      181 eafeadltag errgmqlelg qfrqgvacaa vlvspdkdme rrtvlacalp asemmtsarv
      241 vrtklltaar tiadglaadt
//
LOCUS       WP_357581112             230 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581112
VERSION     WP_357581112.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 230)
  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..230
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..230
                     /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=24529
     Region          1..151
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mnrcefafdd gayvlgalsp adrvtyerhl vdcpacqqsv seiavlpgll grldpasleq
       61 flpppenprv pellnaarer rrrerqagrl ryaviglaaa afalvvgfgv atvlpgqgld
      121 gpgaqvrmvq mqpvagtvpv haeigltgtn wgtevtmhcg yderagygka nafrlvahag
      181 dgsqeqigsw laapgddlri tgatrftnae lvrlelirad gtpvlayevr
//
LOCUS       WP_357581155             227 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581155
VERSION     WP_357581155.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=24451
     Region          13..205
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtaettppga ptlvedllll lfqprsgtia gentlfyvla gavladlaln dqvtmadrrk
       61 vkiveghaps ddllrsawdy vsekprgvqt vlaaigpelr kpvlerlier gditredrrm
      121 lglfrttalr dggngrrtrl leevrqvlvd gaepstrvaa laallsgsgt lpqfyrdipw
      181 tspvitrake leqgnwgaga aaeavtrtmt atvvnsvivt ttviprs
//
LOCUS       WP_357581259             791 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581259
VERSION     WP_357581259.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 791)
  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   3  (residues 1 to 791)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 791)
  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   5  (residues 1 to 791)
  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 791)
  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 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..791
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88489
     Region          9..765
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mireraypve pwhvretrld mdvlaqsesv falsnghvgl rgnldegeph glpgtylnsf
       61 yelrplpyae agfgfpesgq tivnvtngkl irlmvddepl dvrygevlah erildmragt
      121 lhrslhwrsp agrevrvnst rlvsfrqrsv aairyeveva dgkplrliiq selvanetlp
      181 pqsrdprvaa vlesplqaee elttpaggll ihqtkvsglr vaaamdhevt spartsvgse
      241 gyedwvrttv acvlapgqkl qvvkyltygw ssrrslpalr dqvgaalaaa kldgweglvr
      301 eqreyldefw daadvvvdgd pevqqavrfg lfhvlqagar aerrpisakg ltgpgydgha
      361 fwdtemfvlp vltythpaav rdalywrfst leqarerart lnlagaafpw rtiegpessg
      421 ywpagtaafh iaagiadalr ryvlvtadrq lereiglell vetarlwrsl ghhdragnfh
      481 idgvtgpdey tavkndniyt nlmaqrnlht aaevamryrd eafhlrvtde eaaawrdaaa
      541 amhipydeel rvhqqvegft rlqewdfeqt ppdkyplllh ypyfdlyrkq vikqadlela
      601 mhwrgdafta eeklrnflyy errtvrdssl sactqavlaa evgysdlahs ylreaalmdl
      661 hdlnentrdg vhmaslagaw ialvagfggl rdhdgmlsfa prlssrlnal sfslqwcgmr
      721 lrvdvrghdt tyalhhaapd avielrhhge pvrvtcdepv tvpnppprtd lpvpeqapgr
      781 apllrlpenp a
//
LOCUS       WP_357581266              69 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357581266
VERSION     WP_357581266.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 69)
  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 69)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..69
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6885
     Region          1..69
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mvsttyqvqg mtcghcvsav steigaiegv kdvqvdlaag rvtvtsdqpl sddavraavd
       61 eagyelaga
//
LOCUS       WP_357581306             185 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581306
VERSION     WP_357581306.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 185)
  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..185
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..185
                     /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=20316
     Region          4..184
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdaadegelv rrvargdrra fdelyrrtap wlevrlrrrc adpdmvaevl qdtyltvwra
       61 agsfagvpaa rgggaqgsav gwlwtiaahr lvdafrrrar rarvpqvqlm pdtapaaede
      121 vmaarvgqel eqallvlppe vraalratvl dglsmreasv llgvpentvk srvrrarial
      181 reals
//
LOCUS       WP_357581313             231 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581313
VERSION     WP_357581313.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  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..231
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..231
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23804
     Region          1..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msllrrviga vlrrerqhqg rtlrevaraa gvsvpylsev ergrkeasse vlaaicralg
       61 lhlsdlleev rdelrrverr lpaggpagrv patrpgdpta apagrgtdgs aqpvarlntv
      121 gfgfgsdlta glggndpyga wtrsggqfgt agtaggglsg saviggglig girvlafadp
      181 igpvhlvarg pllrrrspgr spvgplhrpg arrravrrta avrvtvgshr g
//
LOCUS       WP_357581349             207 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581349
VERSION     WP_357581349.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  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 207)
  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 207)
  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 207)
  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 207)
  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..207
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..207
                     /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=23103
     Region          59..197
                     /region_name="SpoU-like"
                     /note="SAM-dependent rRNA or tRNA methylase related to
                     SpoU; cd18096"
                     /db_xref="CDD:349969"
     Site            order(132,134,154..157,160,174..175,177,183..184,186,189)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349969"
ORIGIN      
        1 mtgeqlevgv gpwpgdlpdd prydpellta gdrrnvvdry rywrreeiva dldrrrhgfh
       61 vaienwqhdl nigtvvrnan aflaaevhiv grrrwnrrga mvtdryqhvr hhetidqlva
      121 waaendlplv gidnlpgcrp letatlpqrc vllfgqegpg lseaahsacd qifsiaqygs
      181 trsinagvas giamhawirt haapppt
//
LOCUS       WP_357581380             533 aa            linear   BCT 28-DEC-2024
DEFINITION  (2,3-dihydroxybenzoyl)adenylate synthase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581380
VERSION     WP_357581380.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..533
                     /product="(2,3-dihydroxybenzoyl)adenylate synthase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0008668 -
                     2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
                     [Evidence IEA]"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56609
     Region          1..530
                     /region_name="EntE"
                     /note="2,3-dihydroxybenzoate-AMP synthase component of
                     non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1021"
                     /db_xref="CDD:440644"
ORIGIN      
        1 mlegcepwpp eaaeryrrsg ywgaetlasl lrevaatdgd rvalvcgsrt vsyahldawa
       61 drlagglhrl gvrrddrivv qlpnvpefaa vavaafrlga lpvfalpahr rseitylcah
      121 tdavaylttg tvagfdhrrl aaevrrevpg lrhiliaddd ageftplsav hgppvavdvd
      181 paevafflls ggttgtpkli prthrdydfq irataaemgf dadgvylaal pvshnaalgc
      241 pgllgalrag grvvlassps pdevfplvtr ekvtlttlmp aylplwadla gvfradlsav
      301 tievggapla pavaqraeaa lgctitrwfg maegllvftr rddplevrtg teglplsaad
      361 eilvvddedh pvppgasgel ltrgptvlrg yyraadynar aftsdgflrt gdrvrldeng
      421 rlvvlgrikd vvnrggekvp peeveehllt hgqvreaavi giadavlgek tcavvvaage
      481 pptlaglrdw ltgrgvadyk lpdrlvvvtg lprtgvgkvd ktalvatvid rda
//
LOCUS       WP_357581438             283 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581438
VERSION     WP_357581438.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 283)
  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..283
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..283
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31074
     Region          14..277
                     /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 mpfitvgten sapidlyyed hgsgqpivli hgfpfngatw ekvsgpllda gyrvitydrr
       61 gygnsaqptf gydydtfaad ldvlmteldl rntilvghsm gtgevtrylg aygservdra
      121 vllaplapyl rhapdnpegv easifegfkq aivqdrfayl tqfcnnffny denkgklvse
      181 eayrahwnig amasakathd svdawgtdfr advsridvpv livqgdkdnv lpypktgqrl
      241 qpmladsrlv tlkgaphgtp wtnatevnqa imefigspam ara
//
LOCUS       WP_357581481             113 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581481
VERSION     WP_357581481.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   4  (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
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..113
                     /product="PadR 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=12273
     Region          1..101
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mnaqalhghl dalllavler galhgyaiie alrarsdgrl dlptgtvypa lrrleraghv
       61 vstwstvngr errtyeltdg grraladqrs gwhefrstvg rfldpgttpt tag
//
LOCUS       WP_357581493             224 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581493
VERSION     WP_357581493.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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..224
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..224
                     /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          15..189
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtgvplaeel lllayddetg katlprisld lgmaaavlie lalagriaya dgaltavdpt
       61 ptgepvtdav lakivadtph spsswvqrlr hglrdrilgd lcdqgvvrdv detelgfihv
      121 hrypvvdpsv eeetrqrlav vltgaapder taalatlvav lrmesalgvt gedadaarqr
      181 leeiasgagf sgevsledsv irpsvalvva algravehal gprr
//
LOCUS       WP_357581529             380 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581529
VERSION     WP_357581529.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 380)
  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..380
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..380
                     /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=39406
     Region          29..310
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mrdefdvvvv gagpagvaaa laarragaev llldraefpr dkacgdgiaa haldvlaelg
       61 vrdavagfap vpalrlvapd ggavarelpr paytvprqvf darlvaaavr dgvplgrrav
      121 rrvevradrv vldgeisagv vvgadgagsv vrralgepnn pdrhlalair gyapappgpp
      181 aqlivtsaar wpayawsfpi gdgranvgyg evlrgeslsr ahlldrlaal lpgtdpaavs
      241 slrahhlpls tfrpaagrgr vvlagdalsl inpltgegif yalrsgalag haaigapeha
      301 arryadelrr rlgthlrhss aaawlarrrl vvdaavraag rdgrvfgrvv elglgdglld
      361 grtlglialg lsvrhrppah
//
LOCUS       WP_357581638             161 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581638
VERSION     WP_357581638.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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..161
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..161
                     /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=18238
     Region          7..143
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mshelartsa iadlmragre tsrlsmvfry aiaerlgltv sdlecldyla dvgsatagqv
       61 aertnlttga vtsmlrrlqq agyvtaerdp adrrrvivtl rpervaeltr pyerfaerae
      121 rlvegyrvee imllvrhydr mqemylaeld rlrsgdaqrs a
//
LOCUS       WP_357581644             245 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581644
VERSION     WP_357581644.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 245)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..245
                     /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]"
                     /calculated_mol_wt=26523
     Region          25..162
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mserqranpq lsavmsaqdr intywtgrap gydeyqqrtd rltadtraws qiwaealppa
       61 plevldvgtg tgqvamvlag lghrvtgidl aegmlaqarh haatiadgpv irhgdavhpd
      121 fpsasfdavv srylmwtlre petavanwar llrpggtvav vdstwfpegl dnasenfadh
      181 ydgqvravlp laaatsidqt vavleragit gvtatsltsi feldrrfgva pnhehrmqyl
      241 iagrv
//
LOCUS       WP_357581647             362 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581647
VERSION     WP_357581647.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..362
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..362
                     /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=36813
     Region          41..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 mtttalpesr adllgvaaqr rrtgiwllal tvglivtgva avgsgavgip pitvariigh
       61 hlvglpgevt wtaaqdaivw qvrlprvllg mlvgaglaac gvalqamvrn vladpyllgi
      121 nsgassgaaa ailfgagagf gqyalsssaf lgalgasllv fliarsggrv tsirlllsgv
      181 avgyalyatt sflifasgsa egarsvmfwl lgslglarwn vlllvaaivl ggmigyltiv
      241 grrldvlaig detaqtlgvs pdrfrlrllv lvslsvgvlv saagsigfvg lvvphlarri
      301 vgaphvrvvp vaallgaill vwadvlarvl lapqeipigi itallgapfl lvlirrlhat
      361 ga
//
LOCUS       WP_357581745             417 aa            linear   BCT 28-DEC-2024
DEFINITION  GMC family oxidoreductase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581745
VERSION     WP_357581745.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..417
                     /product="GMC family 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=44470
     Region          <5..417
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mvtgpifkrl edhplgasdv rgadgplrls tatgtdevce dtiaaaeelg wrrvddlnat
       61 dderigylta tirdgrrssa adaflhpvrh rpnltvlvnt vvlrvliehg ravgvrtrqg
      121 gntvdrrata evvlaagala tpqllqvsgi gpadvlreag vtalldrprv gtgmrehrtt
      181 pmqfrltgra gynprlngpl gqaremlryl ltrrgplalp vydlgayirs apevahpdaq
      241 lliapfsaap rrpgraiele sesglmaqit vtrpesegsl aitsadpatp priianyfda
      301 ahdrrtatga frrarelfat aplakrisae tlpgtavrdd gdiieaglal gycgyhavgt
      361 camgpdddhv vdpqlrvrgv aglrvvdasv lpilvsgyln apvmalawra adlmraa
//
LOCUS       WP_357581749             235 aa            linear   BCT 28-DEC-2024
DEFINITION  RICIN domain-containing protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581749
VERSION     WP_357581749.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..235
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23844
     Region          <119..>198
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(154..155,165,167,177..178)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mllgrwlaaa glvvltgtav gvysmgpasg dgatdgvrts gdgpvgvaag ettpagdapa
       61 gvaaagaqpp gttpvaaapr pttvkdplls gkrrvtivrv gafesglall ddgrlaevdd
      121 dqgrqvfvpt pvgsgqflik ayygggtgqp vcwqvrnpgd grplyvrgat cragdpaqrf
      181 eitavagggp reylisnrwa ylrdsarsgl imeelgdapp assfrftdtg paprr
//
LOCUS       WP_357581766             148 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581766
VERSION     WP_357581766.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=15295
     Region          2..134
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mhisarsdya vramlavaqh hpevvkaavl aasqdipypf lqgilldlrr agllhslrgt
       61 dggyaltrap aeiavgdvlr atagalttvr gapaevatyh gvatglgevw lsvhraiegv
      121 vdgtsladll grdrlvrrsv adcgpdaa
//
LOCUS       WP_357581769             278 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfate ABC transporter permease [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581769
VERSION     WP_357581769.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790587
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..278
                     /product="sulfate 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:0015419 - ABC-type sulfate transporter
                     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=29607
     Region          1..278
                     /region_name="CysW"
                     /note="ABC-type sulfate transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4208"
                     /db_xref="CDD:443356"
ORIGIN      
        1 madssiaapt pvgrrpgrhv lravvvaylf flvawplylv grnafadglt sfqdiltdpd
       61 vthalqltvv iavvavvint vfgvgisill vrydfpakra lnalldmpls vspivvglal
      121 ilvyggrdgw fgptleaagi qiifavpgmv matvfvalpl virevvpvlq evgdeqeqaa
      181 rslganawqt frritlpsik wgviygvvls larslgefga vkvvsgnvlg dtrtatlvve
      241 ekylnfdkgg ayatafllal vavaciivvs vlrpkeer
//
LOCUS       WP_357581863             272 aa            linear   BCT 28-DEC-2024
DEFINITION  CoA transferase subunit A [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581863
VERSION     WP_357581863.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..272
                     /product="CoA transferase subunit A"
                     /GO_function="GO:0008410 - CoA-transferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29374
     Region          1..229
                     /region_name="AtoD"
                     /note="Acyl CoA:acetate/3-ketoacid CoA transferase, alpha
                     subunit [Lipid transport and metabolism]; COG1788"
                     /db_xref="CDD:441394"
ORIGIN      
        1 maklvpladg iaelvrdgdt valegfthli pfaagheiir qgrreltlvr mtpdviydql
       61 igagcarrlv fswggnpgvg slhrfrdavq nswpvplele ehshagmanr yvagasglpf
      121 avlrgyrgtd lprhttnirs idcpftgetl tavpalnpdv tvvhaqradr agnvqmwgit
      181 gvqkeavlaa rrslvtveei vdeltpvagq vvlpgwavta vahvpggahp syahgysvrd
      241 nafyvawdei srdrdtfqew iarhvqnaga ka
//
LOCUS       WP_357581882             214 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphate signaling complex PhoU family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581882
VERSION     WP_357581882.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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..214
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..214
                     /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=22818
     Region          8..212
                     /region_name="PhoU"
                     /note="Phosphate uptake regulator PhoU [Inorganic ion
                     transport and metabolism]; COG0704"
                     /db_xref="CDD:440468"
ORIGIN      
        1 msrdsfdeql drltgvlalm sreagaairg astallevdr gaaetvlagd avldarraev
       61 eamipevlvr hqpvasdlrl vvcalriaga lermgdlavh vakvalrrhp vgvvpepamp
      121 vmtalaeaaa rvadksalvl atrdrldamq lgldddevda aqerllsllv sgwpygvesa
      181 idlallgryy eryadqavnv grqvvylvtg tirl
//
LOCUS       WP_357581894             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357581894
VERSION     WP_357581894.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32834
     Region          21..81
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(26,30,55)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(29,54)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(36..37,48,51,55..56)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          107..287
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtmvsaeegp aagptvlrml lgaqlrrlre srgvtresag weirsseski srmelgrvgf
       61 kerdvadllt lygvtaeqer aamlklarda nnpgwwhryg dvlpswfqsy lgleaaaali
      121 rsyevqfvpg llqtpeyara vvllghstag peeidrrvdl rmrrqellar prpprlwavv
      181 deaalrrpig gpevmrgqle allkatrtpn vrlqvipfaa gghaaaggaf tilrfgdqdl
      241 pdivyieqlt saiyldkred ldfyavamer lcveaepper tpeilermia dlaph
//
LOCUS       WP_357581904             433 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357581904
VERSION     WP_357581904.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 433)
  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 433)
  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 433)
  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..433
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..433
                     /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=44020
     Region          100..355
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrvralavgc vvlvavtipa tpgaaaitvg sgrvaavalp tpaptpppap gsvapaptav
       61 pcpkavapkv vrspkptppp svpehrvvgg dvlatpgliv ppgvptppkv tatswlvadl
      121 dtgevlggcg pheyatpasv qklllaatml prldparvvt vtredldiap gssavgllpg
      181 gryrvetlwl glllqsgnea analarlggg aegvaggvra mneqarrlga qqthavtpsg
      241 ldapgqftsa ydlaliarac fadpafrryv ltertripaq kalrakgfei qnenqlvyry
      301 pgalggktgf tdyarhtyvg aaerggrrlv vtllgaeprp rrgweqgaal ldwgfalprq
      361 msvgrlvepg eldaepppav pgpadaapsa gpastadgpg agmfvalavg avaialavla
      421 grrsrsavtd lpe
//
LOCUS       WP_357581941             517 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581941
VERSION     WP_357581941.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 517)
  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 517)
  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..517
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..517
                     /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=55805
     Region          35..498
                     /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 mtlpvhtaea tpthpeprpt parahllsde tveryrqava agtdrvarrv aeatgpftgv
       61 rpdelapqve aidldrplgd ttaaldeled vylrdavwfh hprylahlnc pvvipallge
      121 avlsavnssm dtwdqsaggt lierrliewt adriglgpaa dgvftsggtq snlhalllar
      181 eealaaatpa drrillpqlr iiasaaghfs vqkaakllgl apdavvvvet gpdrrmrpga
      241 vrheiarcrr agltvmavva tagttdfgti dpldeiaevc atagvwlhvd aaygcgllvs
      301 ptrrhlldgi eradsvtvdy hksffqpvss salvvrdrrt lrhatwhady lnparmvaqr
      361 ipnqvdkslq ttrrfdalkl wltlrvmgpd avgelfdevc draaqawqlv aadprfevlt
      421 rsqlstvvfr wrptgpgrdl tdaanlrare alaasglavv agtrvdgrqy lkftvlnpat
      481 ttddvayvld liaehagrhv hehagsaasa dltcpvg
//
LOCUS       WP_357581972             522 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357581972
VERSION     WP_357581972.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 522)
  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 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..522
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53754
     Region          5..518
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mtnnpstlyr agvlhcpadp satallvrdg rivwlgsdad apsadrvvel dgalvtpafv
       61 dahvhvsdtg lvlsgldlsg vrsagellda vsayaaglpa daavlghgwd estwpvaqpp
      121 sagqlgraad grrvylsqas ihsalvssal laacpeaaaa pgydesgwlr rdahhvvrav
      181 arasvtraqr vaaqrvalgy aasvgiaavh ecggpeisde edftgllais gagvpevygy
      241 wgelggaara relgavgagg dlfadgalgs rtahlsqpya dgdgcghgyl sadqvrdhll
      301 dcaahgmqgg fhaigdaavs tvlegfaaaa rrvgtdrlra arhrvehaei vdrrliagfv
      361 eygvvasmqp afdrlwggag rmyetrlgla rslasnpmga mhgvgvalaf gsdspvtpld
      421 pwgsvraava hhnpvqrmsv raafaahtrg gwravhldse gvlalgapat favwstpagv
      481 erglpvlqae dpeargaddp tplpvcrrtv lrgeviyeeg sa
//
LOCUS       WP_357582024              80 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357582024
VERSION     WP_357582024.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 80)
  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 80)
  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..80
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..80
                     /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=8865
     Region          3..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 mpelsrraqk dlddlpaalr nraetiiarl drepglgkkl lgplagvrsa rlgrshrilf
       61 rmtdegafvl tvaqrrdayk
//
LOCUS       WP_357582046             511 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582046
VERSION     WP_357582046.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 511)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..511
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56216
     Region          84..483
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvssdp rrqppgatst applppvngw hhqptdvppp vatpqaappp rprvdfqvvr
       61 elrrqlserl trwqrgrefs vaeedterar lavelvaeya dsvrragtpm aageerllld
      121 qvtaelaglg rlqtllvddt ieevhilgcd qvritrhggg vdwadpiads ddelveilqa
      181 aarragater slstskptld lqlpdgsrla avflvshrpy avirkhntld vtlddlaggr
      241 gdldemidpl lrdflrasmr aglnimvagl agagkttvir ammseippde pyvlleesre
      301 llparrserh ravmsfeare ghgergpdgr pagevsiadl ipvslrmgvl riivgevrsr
      361 eivpmlqamt tsrgsmctih artpagvser iielalahgr emtvdqarrm agnaldlivy
      421 vnvddetgig grkhrfishv eevlgvgegs ritttqvfgp gpdgravprh lpervreqll
      481 rvgydarlls rwieagqgaw rrprqtrlgr r
//
LOCUS       WP_357582056             492 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582056
VERSION     WP_357582056.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 492)
  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 492)
  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 492)
  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 492)
  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..492
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..492
                     /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=51134
     Region          22..490
                     /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 maepelvdvv vlglgvggee vagrlaeagl tvvgverdlv ggecpywgcv pskmmiraan
       61 avaearrvdg lagtaqvtpe wapvakrire eatddwddrv avqrftdkgg rfvrgsgrid
      121 gpgrvrvgdq vfqarhgivl gtgtrpsvpp vdglaetpyw tnraaievee lpasllvlgg
      181 gaiglelaqv farfgvrvtv vealdrvlav eepesseaaa aalradgvei htgvkaarve
      241 hgaggftlrg tegeeftaer llvvtgrrah ldelgldtvg vdasgrylpv ndrlhvtdgi
      301 wavgdvtgeg afthvamyqa sivvadvldh vrradggadp sgtasvvgga vgsasslaat
      361 gssgaagsvp radyralprv tftdpeigav glteqqarer ginvqvgftr lsssargwih
      421 rtdevgfikl vadadqgvli gatsagpagg evlsalvvav haavpltqlr hmiyayptfh
      481 raisdalrnl gr
//
LOCUS       WP_357582145             179 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582145
VERSION     WP_357582145.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 179)
  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..179
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..179
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18885
     Region          11..176
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtdsphpert lvllrhakae qpttdrpdve rplatrgrad aaaagawlar hgllpdvvlc
       61 saavrtrqtw hdvqlgitgs ppesgpagpa pavryepday eahpedllsl vrqvpstaat
      121 vlliahnpgi sllselldpv radpeglrtg glvvhrtavs waelsrgtag iearhtarg
//
LOCUS       WP_357582169             624 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582169
VERSION     WP_357582169.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 624)
  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 624)
  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 18791949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..624
                     /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=62349
     Region          30..624
                     /region_name="COG4935"
                     /note="Regulatory P domain of the subtilisin-like
                     proprotein convertases and other proteases
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:443962"
     Region          125..379
                     /region_name="Peptidases_S8_PCSK9_ProteinaseK_like"
                     /note="Peptidase S8 family domain in ProteinaseK-like
                     proteins; cd04077"
                     /db_xref="CDD:173790"
     Site            order(128,131..132)
                     /site_type="other"
                     /note="calcium binding site 2 [ion binding]"
                     /db_xref="CDD:173790"
     Site            order(156,187,246..247,274,341,344)
                     /site_type="active"
                     /db_xref="CDD:173790"
     Site            order(156,187,344)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173790"
     Site            order(293,295,318)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:173790"
ORIGIN      
        1 malpqrsvfv glatlamvaa atpamaaepv gtvrsaggat avegsyivvf kdsevsrttv
       61 gssvdrllrr hggatartyt aavrgaelrv saraaariaa dpavayveqn hvvsiagtqt
      121 nppswgldri dqrnlplnss ytypntatnv tsyvidtgir tthsdfggra twgtntvdsn
      181 ntdcnghgth vagtvggsay gvakatrlva vkvlncsgsg tnagviagid wvtanavkpa
      241 vanmslggga ntsvdnavin sinsgvtyav aagngnalgq rqnacnyspa raapaitvga
      301 tqnndaaasf snfgtcvdil apgvsitsaw htndtatnti sgtsmasphv agvaalvlsa
      361 npswtpqqvr dylvnnstpn visnvgtgtp nqllyvvngs tppptndfsv svsptsgsva
      421 agssatatva tattngsaqs vslsasglps gatasfspat vtsggsstlt istsastpag
      481 typvtvtgta asgtrsatyt ltvtgsgggg csgtngtdvs ipdagsavts sitisgcnrn
      541 assastvavn ivhtyrgdlv idllapdgss yrlknssifd gtdnvnttyt vnlsseaang
      601 twrlqvrdvy ggdtgyintw tltl
//
LOCUS       WP_357582172             291 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582172
VERSION     WP_357582172.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 291)
  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..291
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32510
     Region          14..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..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mserrsptir rrrlgaelrr qreaagitie avaeqlecsa skisrietgh ttatprdvrd
       61 mlriygvvga esdelvqiar earqkgwwhp ystvlvgayv gleaaassir ayeqqvvpgl
      121 letedyasam iraarpdfsp eqvqqrvrvr lgrqslltqd dpvdlwvvld eavlsrpvgg
      181 dtvmrdqllr lvevaqlpnv tlqvlpfevg ahagmdgtft ilsfpeagdp dvvyaenatg
      241 glfleksdel qkysfifdhi raaakrpees veyiarlaee plwkwrrkds p
//
LOCUS       WP_357582200             429 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582200
VERSION     WP_357582200.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 429)
  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 429)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 429)
  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..429
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..429
                     /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=45127
     Region          141..428
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 magqstqrrv rpwvtdvllg vgvavtvsiv itaneggrhg pdrvaylwav glgalmlvrr
       61 rypvlvlavs vlglfayyaa gypavglavp vaaalfsaae hgritasiva avlvivvsvv
      121 frlaegqdfs fvvgyelagh vllmgaaial gdslrsrraa qadarriael tearyrqeaq
      181 arlrdermai ardlhdslgh ttsvialhad varealgrde taarsaleli rstahrsmdd
      241 lrrtvtllrs pgdpprtvvs lanldavtra asaagfdvdv rvavdaplpa pveaaafriv
      301 qeavtnvvrh sagsrveiha eqhgdqltvt vtdtgsdptp dpgptrnaep thsaeptrna
      361 eptrsvelae ppayrdaang vveppavars ghgiagmrer aeslggtlta ghrqtgfvvr
      421 avlplaepg
//
LOCUS       WP_357582253            1031 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582253
VERSION     WP_357582253.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1031)
  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 1031)
  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 1031)
  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 1031)
  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..1031
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..1031
                     /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=112132
     Region          1..246
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          129..1030
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mqiqvlggla vrlgsqalpp gtpkqqtvla mlacnagqlv sveqlvdelw fedpppsaip
       61 nvrtyaanlr rsleamlpnr evlirtrdgy rldvecsdvd lcafrtevte arrllgtdkr
      121 eavrlvsral arwrgpmltg ialgpllsaq vaaatedrll atelygelqi qlgrydealp
      181 vlrellirhp lrepahlllm qalylggdsa gavaaytaar qtlreqlnve paaelqrlyr
      241 riarndgkpr ptgaggslgk aptasadqtq qpffflprtv pdfvgrvdav ehlvgrtlra
      301 gasasvvhlv dgmagsgktt lavhvanrla drfpdaqlfi dlkghdpaek lspsaataal
      361 lrqlgtpssr ippdfgdrld lwrrelagrk viivldnaad aaqvrpllpt apgnlvivts
      421 rrringldvd ppvslpllep aegvallast agaervaaep eaaaavvesc ghlplairla
      481 gsrlahrpnw qvtdlaklla skarpldhlt sgdrsvagaf aasyaslsep aqrmfrllsv
      541 hpgdefgrla asalsglsld dtadvlddll dshlieelta gryrmhdlir hyahdlssgm
      601 dqvevrreal aglldlmlhm sfsvaedleg sriridvalg vprrpdlvem kngpaekwme
      661 teranlvllv gsaqewgfrq eswqlarvlw rflytrgcye divltslqgl aaaeksgdeg
      721 avavmhnyla saylrtgnyp galthvekav eicercgdrs nlaryqanlv avywlfgepe
      781 kavavalerm rkggvaethe tathlpnlgl alallgryde alrvhrlhly vgrqigsqfh
      841 ilnalghiga vkcrmgqyav aaralrtali mrqrtghrya epevrndlgv alrglgrmte
      901 avleheaark mavaagephv eaatindlal tladsaetak lielhrealr vatriahpye
      961 qgralaglae hmwsvdpaea rrhwaralai frrmgvpeqf dvarrlteae aqqppestps
     1021 taaaqirpaa i
//
LOCUS       WP_357582278             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582278
VERSION     WP_357582278.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..265
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27209
     Region          30..240
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpsdpravlt rpapepdvtv aygehpdqia dlrrpagsgp prplvvvvhg gfwraeydrr
       61 htgplasala algypvaqle yrrtgqpggg wpgtltdvla gvsalpglae aalpghvtsg
      121 ppvlvghsag ghlalyaaah apgavagvla lapvadlaea yrldldagav aallgggpad
      181 vperyatadp rslvplrprt vvihgtldqq vpidisrnyv aaaraagtdi rlielpeceh
      241 fgliapgssa wpevtsalrs lhedh
//
LOCUS       WP_357582337             165 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582337
VERSION     WP_357582337.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 165)
  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 165)
  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 165)
  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 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..165
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=17207
     Region          62..135
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mtvlhptrrg pvtlvtgvgv wsairllarc vgrprilssa gmlavltvva vwtvlmwagf
       61 allflpnltg lsyspsvsyg slnfldalym sgmslttvgf gdvvggtdal rlitvleaaa
      121 gfglitaait yvlsiyplts qlssagwvsa srrrstggvd artlr
//
LOCUS       WP_357582349             216 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582349
VERSION     WP_357582349.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 216)
  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 216)
  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..216
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..216
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22619
     Region          3..167
                     /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 mqlvldllhe tmsspwvyla lfgvavvdgf fpvvpsetav itagvfaatg qpvlsvvivv
       61 aaagalvgdh isyaigrrgg grlltrlpeq grrravygwa srgiavrggl iltvaryvpg
      121 grtavtmtmg atrfsrsrfl mfdalaagtw giysalvgyl gglafeqdpl rglllglgla
      181 lsvtvmveta rwayrrrars lpavveagar gsigda
//
LOCUS       WP_357582350             269 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582350
VERSION     WP_357582350.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=29020
     Region          6..258
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtpdrttsdr walitgatag igaafasrla adgwhlvlva rdttrlaaqa aeltgrhgve
       61 tetitadlst ddgcaaterr ladgppvell vnnagislnk pflrssvqde trllrlnvha
      121 vlrltlaala tmterrsgav invssvagfg avmpgstysa skawvtnfse svgqsarpfg
      181 vrvmalcpgy trtefhqrag idmsktpewm wldasnvvde alrdlrkgkl vsvpswkykl
      241 avaglrhapr rlldvvsrdt rgrigrdrr
//
LOCUS       WP_357582369             296 aa            linear   BCT 28-DEC-2024
DEFINITION  transketolase family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582369
VERSION     WP_357582369.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..296
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31072
     Region          1..291
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mrdrfvettt allaedprta lvladisaaa fapaarrhpd rvlnvgireq lmlgvaggla
       61 ltglrpivhs yapflveray eqikldldhq dasavlvsvg asydraaagr thlspadvsl
      121 idtlhgwtvh vpghpdevpa llraavaaee saylrlstls nggphggdga lvvvrdagpg
      181 aallvavgpt ldaalaatsg lpvtvaythr phpfdtaglr alvdrevilv epylagtsar
      241 vvsaaltdrp hrllalgvtr eelrrygsae dhtrwhglda sglrrsitgf lspalv
//
LOCUS       WP_357582414             158 aa            linear   BCT 28-DEC-2024
DEFINITION  glycine-rich domain-containing protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582414
VERSION     WP_357582414.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..158
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..158
                     /product="glycine-rich domain-containing protein"
                     /calculated_mol_wt=18904
     Region          31..151
                     /region_name="COG4278"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443419"
ORIGIN      
        1 mteiavkpae elrwdvprat sinriadlae vrryidaidf gplkyrltqg rdmlgsewsp
       61 aradyferly knwlylrrry egellpphid idefwhghil dthayfvhcd rifgyylhhl
      121 pyfgrrgpag rtnistawqq tqdryhaefg eyiydfme
//
LOCUS       WP_357582390             368 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582390
VERSION     WP_357582390.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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 368)
  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 368)
  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 368)
  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..368
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..368
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39865
     Region          34..330
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 maqpttpdap ppngaqpqal appttpaqda tlleralfei krvivgqdrm vermfvalla
       61 rghcllegvp gvaktlavet lakvvggsfa rvqftpdlvp adimgtriyr qssekfdvel
      121 gpvfvnflla deinrapakv qsallevmse rqvsiggesh rvpnpflvma tqnpieqegv
      181 yplpeaqrdr flmkiivgyp tdaeereivy rmgvappept avfdtedlia lqhkadqvfv
      241 hnalvdyavr lvlatrtpae hgmpdvaqli qygasprasl glvratrala llrgrdyalp
      301 qdvqdiapdi lrhrlvlsyd aladdvpadh vvhrvmstip lpsvaprqqa tppagavapt
      361 sgwpgqrp
//
LOCUS       WP_357582428             492 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582428
VERSION     WP_357582428.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..492
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..492
                     /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=51592
     Region          18..>167
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrrlarlaar tppdreryld llralaiilv vlghwaiaav eydesgrpdg hsaltalpwa
       61 ypltwavqvm pvfflvggya naaslaahqr rggdaigwll grsarllrpt salvlvlagg
      121 alvarlggaq pdevrpvvwf atiplwflaa ylavvpltpv myalhrrlgl lvplvlvllv
      181 aagdlgralg paglalpayl lgwlavhqlg fawydarqgr crpagrdtap dqaptttggr
      241 gngdggsqqp rpddtgpagg ptglrtrclp msrrsaiaml lgglvvavll tgpgpypism
      301 inlpgqrlan aappsvalla vataqlglil llrarverwl hrdrpwqavi avnsvvltvf
      361 lwhlsaavll vgalhglgll ptppagtaaw lawrlpwvlm lavvlavlva ifgpieastg
      421 rprhlrasar wagaraaltv gafaavvyal aangatakta peplgwpvaa lvaylagagt
      481 lrllrsgwgs rg
//
LOCUS       WP_357582419              98 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582419
VERSION     WP_357582419.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 98)
  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 98)
  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 98)
  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 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   5  (residues 1 to 98)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..98
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..98
                     /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=11087
     Region          6..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdadpdlfka igdatrrtil delidrdgqt lfeicgrltv khnltssrqa isqhlavleq
       61 aglvltrrqg rykfhhidts plrsiverwp idreapep
//
LOCUS       WP_357582446             125 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582446
VERSION     WP_357582446.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..125
                     /product="YybH family protein"
                     /calculated_mol_wt=14300
     Region          2..108
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mdrkqvadwi aayervwrtp gtealvtlft edasyqqgpy wtpvvglpai aqmweqqrkg
       61 pdevfqmase ivavdgdvav arqevrygdp vdqeyrdlwi mrfagdgrcr sfeewpfwpg
      121 qqpas
//
LOCUS       WP_357582473             242 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582473
VERSION     WP_357582473.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 242)
  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..242
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..242
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=25534
     Region          13..227
                     /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 msdsaaprps rnvvlvhgay adgsswsdvi pilqraglrv tavqnpltsl addaaatrra
       61 ldrqdgptvl vghswagtvi seagdhpnvs alvyvaarap dagedftala arfptppana
      121 glvhsdgyaq lseqafledf aggvdqvrar alyavqgpis gelfsartst aawrdkpcyy
      181 sistqdrtsa pelerflaer mgattieves shlamvthpe aiadlilmat rdtqgprptg
      241 pr
//
LOCUS       WP_357582482             324 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582482
VERSION     WP_357582482.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=35027
     Region          17..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 malpdtaapp rasaspstpt akgprrpgrs saaywlyllp gavlfllvig vplvytgyls
       61 ltrwsgvgdp tfigldnyrn lltddvfwts fkntvamiva mvvvptlvgl llaavlfdti
      121 grkfrprtaa alraafylpq vlpvvvagiv wgwilrpdga lnglldavgl gslahdwlgd
      181 pntalpavma vmiwvqlgyp vvvfmaaler vnpelyeaae idgagwfrrf raitlpqirp
      241 etfvvgltct iaamkvfgpi faltrggpen atnvpsyfay ftffkrlqvg ygsaismvlt
      301 liivvvavlf iraqnraerr dgvl
//
LOCUS       WP_357582487             636 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582487
VERSION     WP_357582487.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   3  (residues 1 to 636)
  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 12993645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..636
                     /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=66206
     Region          8..267
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,32..33,66,71,76..79,91)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,74,90..93,97,99,136,138,
                     140..141,143,153..154,157,175..178)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,74,90..93,97,138,140..141,
                     143,153..154)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,97,99,136,138,140,157,175..178)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(153..161,171..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <198..389
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mraviagryr lldlvgrggm gtvwraedel lhrqvaikqv vlpawlggde ldqvrartlr
       61 eartaarlsh pnvvrvydvv seadapwivm eyvpsrtlqd lldadgplpp rraariglal
      121 ldalraahda gvlhrdvkpa nvlvaddgrv lltdfglavf dggdqtmtgp gtilgspqyv
      181 aperagegvs sepadlwslg atlhaavegr apyarstama tlsalasaap dpaphagpls
      241 avlagllrrd pahrtdhaet rrrllaaagp dpadtpdrag edtaplpttg sshagtappv
      301 raapvpantp aaprseptrs yggddptqtg ggdpahtggd dpthtgegdp ahtggddpth
      361 tgggdpaqag gppirtppag trrtspgaeq rrgavarpwa laavavlvam aagigtaltv
      421 vgtgadqpgp atqsppsydv gapgpggpfp rdgrrppgpp pgglvppplp cvrpwvdgas
      481 lrtapprpsd qfrppagwvw hadtggfrva lpadwrhsrd ddvacfqdpa tgraftvads
      541 adagtepisr fkavrdrela egtlpgyqef rlgrvgdate wefgwltphg drlratqivp
      601 dgatpgrswt lgwitheqdw aaaaselatv rlsfrp
//
LOCUS       WP_357582575             359 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582575
VERSION     WP_357582575.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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..359
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..359
                     /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=38424
     Region          156..329
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrartirgrr ltypilalal alplltvgqp aqaaphadgd sirqvgtavs aeawaagrqr
       61 ygaqvtadaa ieaywtperm rnarpveesp sykaaarrfa qsrgtssaap tnrsrpvdvp
      121 pvaglmgtpg mstqainpnl gsnhptarsn gkvffnmdgg swvcsgavin svgfntvwta
      181 ghcihggpgs slatnwsfvp aydddlanpr phgtwtarel wtwsswidss nweadmavai
      241 mntrngvriv nqfgghgfrt hqgftvginn fgypsgapfd ggnllrcsgn stqsgariri
      301 ncdltagasg gpwlinwdgn wgylngvnst lnsyaaptlw wspyfddtas elynftatr
//
LOCUS       WP_357582579             259 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582579
VERSION     WP_357582579.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26453
     Region          1..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mprfanqtvl vtggtggqga shvralhaeg anvvigdida ergaglaael gggvrfvhld
       61 vsqeeswaaa ieetekafga ltilvnnagv qnppaliest drvtwariid inltgtflgi
      121 kaaapalrra gggaivnias tmgfggtacy apyvaskwav rgltqtaale lgrdnirvna
      181 ihpgvvatpf itepaagsda piadfyspep favprlgqpa ditalllfli sphaafitga
      241 eyvldgglll gpalqkeaa
//
LOCUS       WP_357582581             108 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582581
VERSION     WP_357582581.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..108
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11620
     Region          3..108
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mvrdellrlr aravaeastl aqdlealfla srdsnaddeh dpegatigfe raqltallag
       61 areriadvdd alrrvdaaty gvcercgqpi gderlaarpf arfcmaca
//
LOCUS       WP_357582585             245 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582585
VERSION     WP_357582585.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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
REFERENCE   4  (residues 1 to 245)
  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..245
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..245
                     /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=25544
     Region          6..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 mrnitfdftg rtvvvtgaar gvglavgryf rqagatvylv dleagpvkea adeigatgla
       61 advadtgqvt evvervvses grldvlvnna gnlrdgvvwk lsdddyesvm avhaggtfrf
      121 travvphfrr qgagriinvt sytglrgnpg qsnysmakag iigftrttak elarfgitvn
      181 aispsaqtrm iasvpqekla qltaaipmgr fadasemaaa vaflasdeas yitgvvlpvd
      241 ggmai
//
LOCUS       WP_357582648             134 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357582648
VERSION     WP_357582648.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..134
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15190
     Region          15..119
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maasqptwea smsadpeqac piapvvdivf srwttpilwa lhqygrqrfv elerrlttit
       61 pkvltqrlrq lerdglvart yhpevpprve yeitelgasl aplfahlaew aatnldaveq
      121 srhtydtaqq srpr
//
LOCUS       WP_357582599             299 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582599
VERSION     WP_357582599.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=33123
     Region          2..295
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtppapgrsr rlsdrglava fispalllll amsvfpllwa lylsftdysa trggsprfig
       61 fenytailts aqvhqraltt liyvvgavtl qtvlgfaiay lisrrthgrg llttlflvpm
      121 mlspvvvglf wrfmldaqfg vinsmlgsig lgqvewltrq rtalislivv dtwqwtpfim
      181 lialagltav pkylyeaasi drasewfrfr titlplvwpl lliavlfrsi eafrlfdlvy
      241 iltnggpgvs tetlsfhvyk vaflgfntgt asaygilmvl vvivltqlyl rylnklkeg
//
LOCUS       WP_357582761             327 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582761
VERSION     WP_357582761.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..327
                     /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=34378
     Region          33..322
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpignaepsv rpvsagrtdg aaaagsagrr rgtgsrpvrg gsraerfapy vlvapailii
       61 vvlrlyplll gvnfsftgdg erngttvgld nylellddpl frtalsnvgl lvlllpvava
      121 ipgllatfiy lrvpghrfyr svyffpavls pvivgaifnl llafdgpvna gleaagispv
      181 dwlgnpgvam fvvvgvhiwa tfgmalvvfl agfatldaal ldaarvdgas lpqvirhvii
      241 pglsrtiafv avttmvgmlt smfgllyvmt sggpegstyl peyyiwiqqg qmnrpalasa
      301 astvlfviml vvgllqvkll rragged
//
LOCUS       WP_357582766             408 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582766
VERSION     WP_357582766.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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..408
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..408
                     /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=43614
     Region          209..392
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkpalrrlrt vtvtfaacal glnllsapae aypvqpvapl sdrapesdqf saegvttvge
       61 lrtvdgslsy ardgrtqiir hpgatyvkvh fsslrlapge yvtvaspdgr esyrydrhln
      121 ratgadyttd grpgfwamsv egdtavvtlh gnrssrgsva tidrfwrgyd rteitqynfs
      181 tqsvcstdar rdvvcyqssh pteyargnav arllisgggm cttwrvgntn rmltnkhcfs
      241 tqaavsgsem qfnyqcatcg ganpgagtkv sgatlyrvss ggssqldyal fsvnnfaaiq
      301 gfgtlylats atttgtqmyi pghgdgspkr lsifedtqng arctvrnany ntwnisyscd
      361 tsggnsgspv lnsshrvial hhlggcpsnq gakahliyne iaslidng
//
LOCUS       WP_357582785             162 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582785
VERSION     WP_357582785.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 162)
  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 162)
  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..162
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..162
                     /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=17787
     Region          1..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpeeprwlne cerdawlala slmfklpgal daqllrdnnl tlfdyfvlsg lsmtpgrtlr
       61 lsalasqvss slsrlsnvvt rlerrgllrr epdpespryn ravltdagwd lvvaaapghv
      121 aavrrfvidg lteeqvtalr evagrvtqqv neaaaedsqr gc
//
LOCUS       WP_357582883             291 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357582883
VERSION     WP_357582883.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..291
                     /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=31954
     Region          2..288
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mraiirltwv vpalvlvgvf vylplvqnfg fstlewdiys gsreyvgldn yrklvgdpvf
       61 wssfgnnlly aaisvavqvf galvlaalie svrserwrrg lrvvyfipsa isltvagllf
      121 yflyepnlgv lnhaleaagl ghlaqawlgq edtamlavia msqwqgfgys tllfavaiqr
      181 ipseiygaaa idgtgpvrrf fsvtlplvre mtglmtmvti sgafqvfnev mvmtgggpdn
      241 stqvlgtwly rsgfvrndfg yaaaiatvlf vitlavalaq lwvtsrrrve w
//
LOCUS       WP_357582940             336 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357582940
VERSION     WP_357582940.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..336
                     /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=36962
     Region          1..332
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 msdvvletrd lvkhfpltrg ivfkkqygav qavdgvnlql rrgetlgivg esgcgkstla
       61 rmlvgletpt sgdlfvqgkn mskvgaeerr rgrrniqlvm qdpytslnpr mtvgdiigep
      121 fevhpdvvpk gkrrakvqel ldlvglnpdh inryphqfsg gqrqrigiar alalnpeiil
      181 cdepvsaldv siqaqvinll eklqaelgls yifiahdlsv vrhiadrvav mylgkiieig
      241 tedeiydkpt hpytqallsa vpvpdptlrg lrdqivltgd vpspanppsg crfrtrcwka
      301 qdicaeqqpa levrdksghp sachfaevrd vvhate
//
LOCUS       WP_357582941             311 aa            linear   BCT 28-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357582941
VERSION     WP_357582941.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 311)
  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..311
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..311
                     /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=33804
     Region          146..251
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mavnsrpave espdqqtglr gfirrrplvs ffvlanlmsw iawtpyvlsa tglgvldftf
       61 psvlgttqft gvlpgaylgp ifaaylvtri adgregvrrw lgrmtkwrvs wvwyagtavg
      121 vpavlvltga alseepvrmp pvallvayvp glllqmvttg laeepgwrdf alarmqrrfg
      181 plagtlvlgp lwglwhlply lsewggwpdv twmrigeffa fccvfsvvvt wvfnrtgqsl
      241 plvmllhvgv nnfmsmayae lfpsiaspeq asrvtllagt taalvvlaat rgrlgyspee
      301 patadpsgra a
//
LOCUS       WP_357582968             789 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582968
VERSION     WP_357582968.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 789)
  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 789)
  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 789)
  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 789)
  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..789
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..789
                     /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=83785
     Region          105..780
                     /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 mtqvalrptt gptvgvaarn srtamryvqa tvavaalgta wcvanftvga gtealayafv
       61 pvggvlaags vvhllrradl dpvprrfwrt llvaavtiti gygwlaldml thaaeartrs
      121 mplpaaacva lgfivaiwav arvpvveagg verwrilldr miaflgcaal lcyvglapmf
      181 ssaepwspqa malvglaflv avgaatkvsf iaggpvdrva lrfvaasggv tagivavlav
      241 rygyvaaipa qsivmpltpv fftlgvtaqw raqlgtrrdq artgmllpyl avvavdvpll
      301 avafgapltw pvrvvliaav vvtalvsarq fiayrenarl lrntriqeer lqyevshdgl
      361 tglanrvlfr drlaaalttt tpasvllvdl ddfktvndll ghgvgdrllv svaqllraev
      421 gddglpvrva gdefavlltg tdadpeelag rllaaldhpi sqhrllvqas igiadaapga
      481 tvdsvlrdad vamytakqrg kagfvryvdg mgepvlahmq lggelrrald dnelrvvyqp
      541 ilrlddnrlv gvealvrwhh ptrgvvspae fipaaertgl ivplgrfvlr etcrqaaaws
      601 lefgpdalre aglnvsarql hdpdfvsdvt aalaesglpc erlvlevtes avlrgqqvsr
      661 tlfeldrmgi rlslddfgtg esslsllraf paaivkldrs fvegieiddg qaaaanarqa
      721 varaviqlah algletvaeg vesaaqvavl rdlgytrgqg fhlarpmtad giscllarqr
      781 tvtairppt
//
LOCUS       WP_357582946             171 aa            linear   BCT 28-DEC-2024
DEFINITION  chloramphenicol phosphotransferase CPT family protein
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357582946
VERSION     WP_357582946.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008105
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..171
                     /product="chloramphenicol phosphotransferase CPT family
                     protein"
                     /calculated_mol_wt=17986
     Region          1..171
                     /region_name="COG3896"
                     /note="Chloramphenicol 3-O-phosphotransferase [Defense
                     mechanisms]"
                     /db_xref="CDD:443103"
ORIGIN      
        1 mttqvivlng gsssgksgiv rclrhllpgp winlgiddli erlppsmvtf gpqgevilge
       61 gfddmqhaww igvaamagag apvivddvfl gggasqqrar ryleglrvlw vgvrcapdia
      121 aareiargdr vtgmaasqae ivhqgvaydv vvdtshtesl dcaraiveqv s
//
LOCUS       WP_357582991             362 aa            linear   BCT 28-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357582991
VERSION     WP_357582991.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 362)
  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..362
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..362
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38701
     Region          144..358
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mrvmlkecaw erlgdelivv hdpreaftla dpegritall delgrgpata eelaaalaar
       61 dvavtaeevr dgltgldslg lvedaagrwl gdpgaderhf snltffgafa rlgtsraefv
      121 rrlreahvlv lgaggggssl vqclaglgvg altlvdrddi aprnfarqfl yrhadigrsk
      181 veraaewvre ydpgievrav drwisgpedl kdltegvhvm aggldgapda nlwvneaalr
      241 agvplvaggm trtqliyfsv dpgrsaclrc desdlpgpee rtsagvahrl trglqlangl
      301 tgpmamqvgs lvayevmryl tgveppraag arvvldlrdg lvpvrvpfpr dpdcpacala
      361 rr
//
LOCUS       WP_357582999             342 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357582999
VERSION     WP_357582999.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 342)
  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 342)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 342)
  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..342
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..342
                     /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=35392
     Region          140..342
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtllwiavsa slllpvalva lsrtplaarl peltcvaavv slavtlaqly gvvpseqpaa
       61 algmaeslaf mvlaglivrd aparraavaa paaglaaatw llrflqpasp leavgacafw
      121 glgallaagl ggylrllgvr qrralddtrt alrlrlagdl hdflahdise mvahaqagrv
      181 tgdparaler veaagqrals mldrtldmlh hdrpatsagg ledirdaaer fsaagparvr
      241 lrmdpalqvp agsaalayri vvegltnvrr haaragrvdl dvsvadgrle itmtndgvtp
      301 srsgrtggag lpglaalvea qggelvsrav pdgwsltawl pl
//
LOCUS       WP_357583034             163 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583034
VERSION     WP_357583034.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 163)
  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..163
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..163
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17755
     Region          16..>62
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mkpdvkfwae hgamllkhar htarlhqqql aegsgtsrtt lsayehgrks ptletagril
       61 daagfrlale pkvefagsvp sclprlpvsa algivahggr vydladreqr reayaallse
      121 grpqdvldhv dgvllvelwe dldlpapvrt awaplierak rgd
//
LOCUS       WP_357583084             536 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583084
VERSION     WP_357583084.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..536
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58728
     Region          16..521
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mghvevghlt yvlpdgrpll ndvsfrigeg vkaalvgpng agkttlmrlv agdlqpvegs
       61 vassgglgvm rqfvgsvrdg stvhdlllsv appavreaaa rlekaelvmm erddekaqlr
      121 yaqaisdytd aggyeievlw dtctvaalga pydnvkyrdv stlsggeqkr lvleallrgp
      181 dqtllldepd nyldvpgkew leaqlretpk tvllvshdrq llanaadriv tvesgniwih
      241 gggfgtyaea rrarnerlde lrrrwdeeha klkalvnmlk nkaryndgma apyhaaqtrl
      301 rrfeeagppe qapsdqnism rlrggrtgkr avicerlelt glmrpfdlei wygervavlg
      361 sngsgkshfl rlvageqvah tgvarlgarv vpghfaqtha rpdllgrtpv eivmtehakl
      421 kneamkalar yelaglvaeq rfdtlsggqq arlqilllel sgatllllde ptdnldlasa
      481 ealqdglnaf dgtvlavthd rwfaadfdry lvfgsdgvvy eapepvwdek rvvrar
//
LOCUS       WP_357583086             478 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Nonomuraea].
ACCESSION   WP_357583086
VERSION     WP_357583086.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 478)
  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..478
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..478
                     /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=50562
     Region          2..167
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msdrdlveal rsgdpgavav lydtyaegiy rycwtllrnt dsaqvalrda liaaeahaaa
       61 lsdpdllrpw lyalargecl rrrmadlpda getlaeapei tdpddadlrv vawnavqslp
      121 tadretleln arhglpmphv aavlgvtarq aeaaheaard rlrdaitvef larkgpydcp
      181 rrariltgfa geltagmreq lvahvarcet caphrnrqvs aakvyellpq itlpdvlrvr
      241 vlscfvdpel hlyrryvarr sealdaagfp vavvrgprkw pralagalaa vatlvaiati
      301 fdyfgkevgg lpgvasvafp pqgeppgltl pwsdrrqvpg svevdstatr plgvtpatag
      361 qqtpspqppv ftpiggdpep vpstppptgp dlgdptldpv hpvdpvtppp gkprpsgkpp
      421 vmpspqpdpt paptpttptp spkpspkpta kptgkptsta tppatatpte svspsvts
//
LOCUS       WP_357582993             964 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357582993
VERSION     WP_357582993.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 964)
  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 964)
  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 964)
  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 964)
  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..964
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..964
                     /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=102037
     Region          1..238
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          113..964
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          752..784
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          792..818
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(794..795,798..799,801,830,833..834,837..838,
                     840..841,868,873..874,877..878,881)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          828..858
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          867..897
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          907..935
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdfailgpvr vaeagrpvrl tgkpravlsv fllhpntvvs sdrliasvwe epprsalanl
       61 qnyvsvlrka aidvetqeqg yrlclrtdrl dllafdedvr rarlesargd laeahrlfar
      121 alplwrgrpa edvplsgevs ariaeleerr esarlgwidv rlrlglhdel vgeltplvet
      181 aplnerlwhr lmlalhrsgr raealeayrr arsvlvaelg vepgqelrda haailndapv
      241 eppgpavvpa epaaperepa wagicllpad lagfvgrete tremitalsd pggaapaivt
      301 vsgppgvgks tlavhvahll rdrypdgqlf vrlggaspnp rdpadllael lralgvdpgi
      361 lpaateeqaa myrariadra vlvllddagd etqvepllpg tpgsgvvvts rgplptvpgt
      421 valvldvppp sdardllarv vgadrlaadp esaeailrac grlplalria garlvtrpaw
      481 ppaelarrla dtsarlnelh agqldvratf atsyaslspp arlafrllga vaadsvaawa
      541 vaalagagvr evddsleela aaglisasdv daakqtryrm hdllwsfaae lfaaeesedg
      601 raaalarlta eacarvtaaa relplapapp ppgapartpp spddgawlaa ergmlvalva
      661 aaaraglasa aaglahalap flvvrgfhed avtmldaave aagaagddaa etrlrlvrad
      721 aemdrgraha vgaefrglla rseragdqhs aayallgvaa slvddleaal dtavraagrf
      781 ralgdangll tawtevavvq lylgrydeaa atsrralgla agesavhrar flrslgvach
      841 etgrteeavg hyrasldlsr elrwnngeri alrrlaeaeg alghfgsaer mlaecaemca
      901 ragdelgeal taytlgdvrr rqgderaala hfttchtvls ahreliwsar areqiarsra
      961 algl
//
LOCUS       WP_357583137             896 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583137
VERSION     WP_357583137.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 896)
  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 896)
  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 896)
  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 896)
  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..896
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..896
                     /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=96898
     Region          2..235
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          112..896
                     /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(712..713,716..717,719,749,752..753,756..757,
                     759..760,783,786..787,789..790,793)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          712..736
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          747..777
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          782..809
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          821..848
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtvtfhvlgp levrsagrpv risgrkprll latllldagr vvggdqlaev lwpqrpprsa
       61 qanlrtyvss lradlsraar agdalrgags gyaidvpadt ldllvfqdhv ehgryadala
      121 lwrgapladl pgsplwerrl dplhearlra aeqliaqrld radhagavre lrallaehpy
      181 redlwsrlil alhaggrkae alrayagira rlvdelgvep gielrrayet vladdslptt
      241 phqlppdipd ftgrepelaa ltrprpaava vitgppgagk salavraahl lrprfphgql
      301 hldlggrhpa dllaealral gaerppptlh ersallrsll aerpmlilld daldaaqvrp
      361 llpgndsavi itsrrritel pgarhvtlae lpeddalrll ariagpdrva reradalaiv
      421 tacgrlplal rsagarlagr pgwslsvlrq rlqddrlgel eevrarldrs yshlpaeaar
      481 tlatlgllga apqpgwvvaa aldrhraddv tdllvdvnll elvgtdpvgq pryrlpdlir
      541 qhstsrtphr dglarvlaaw tatteharar lpttvfglta adaprwrlpe plldrltadp
      601 lswfeaehdt laaavtvaar tglaasawgl aaamvpyldl rchldtwqrt htaalaaara
      661 agdtygeaam lrglaqvaly rdryeeaadg ftrsrrlfhd lgdlraeats vcglgavhqf
      721 rgrharslgh frralamfla agdqhgeafa rqaigraclr agdlaqases ltqamrlaqe
      781 lgdshregcv clqmghlhqa msfhrhalei feslgdrhcg ayalqslagl qvargdlapa
      841 saglersllv frelgdrsge asttqlladl hlsagrtgla ldyqahatal rrtlpa
//
LOCUS       WP_357583169             452 aa            linear   BCT 28-DEC-2024
DEFINITION  TrkH family potassium uptake protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583169
VERSION     WP_357583169.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 452)
  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 452)
  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..452
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..452
                     /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=48057
     Region          17..447
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mrrvraasfs lggyshpaqv iatgfstaal igtlllmlpf atteglspgw ltavftatsa
       61 vcltglvvvd tpthwstfge vviiglvqig glgimtlatv ftvlvsgrlg lrarlfaqae
      121 tktptmadmr kvvrkvvvfs lvceaiaavv ftlrfligyd epigealylg vfhgisafnn
      181 sgftlwsdnv igfvtdpwic ltiaaavtvg glgfpvvfel lkswrhpsrw svltritvva
      241 tivllvlgtl vylatewrnp gtlgalddsg kllaafflss martagfnsv nigelypssw
      301 lftdlmmfig ggsagtaggi kvttlgllaf vmwaelrges kvnighrqis esaqrqavti
      361 tmmsaglvav ctyvllvltp hsldrvlfev vatfstagls tgitadvtvp gqvlmvllmf
      421 vgrigpltig salalkertr hyelpeermi vg
//
LOCUS       WP_357583174             314 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357583174
VERSION     WP_357583174.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..314
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..314
                     /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=34054
     Region          1..314
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mravllvnpk atttserard vlvralrsev dlsvrytrqr ghattlarea aeegvdavvt
       61 lggdgtvnev vnglmtatta ggaeptadrl palatvpggs tnvfarslgl prewpegasm
      121 ileglrlgrh rtiglgladd ryftfcagfg ldasvihrve earrrgrvss pslyfrafta
      181 qfllgnerrh paiqlerpge vtegelatii vqntapwtyv gdrevnpnpe asfdlgldvm
      241 alrqlgvast trtvtqffss tpdprgrkvl rlhdvaeftl vasrpqafql dgdylgerek
      301 vrftsvpaal rvic
//
LOCUS       WP_357583205             311 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357583205
VERSION     WP_357583205.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (residues 1 to 311)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..311
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32452
     Region          14..230
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtdgrpsptn daqivvsglt kryrnvlavn nlsftvepgr vtgflgpnga gktttlrmll
       61 nlvtptsgga tiggqrypdl adplrhvgav leassahkgr tginhlrvic aaaglprera
      121 dqalelvglt paakrkfkgy slgmkqrlgi aaamlgdprv lildepangl dpegirwmrg
      181 flkglaaegr tvlvsshlls emqlladdvv iiaagqlvrq gpvdqvigsm aqgvrvrvrt
      241 pqadvltaal kdgpatvend gqgalliggi dapavgraal aagvelhelt terpdlervf
      301 leltagkagi r
//
LOCUS       WP_357583247             349 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583247
VERSION     WP_357583247.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=37418
     Region          19..308
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpktsarlla llsllqarrd wpgallaerl disprtvrrd vdrlrelgyp ilaikgpdgg
       61 yrldagselp pllfddeqav alaialqgaa rsgagieeaa aralhtvrqv mparlrhrid
      121 tfqvtaadav rpetrvdsgv lmtlsaavha revlrfdyrr rtgerdpgpa rrvephhlvt
      181 wggrwylvaw dldrgdwrtf radritprvp aagprftpra lpggdaaafv agrfrgaggp
      241 gdwpcrgevi lglpaaevsr fagealveel gpdrcrvvlg swswpglaaa lgrfdadiev
      301 vgppelrdaf arlarryaaa aagpgvgpev sgpptpagpr rgtraaagp
//
LOCUS       WP_357583257             433 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [unclassified
            Nonomuraea].
ACCESSION   WP_357583257
VERSION     WP_357583257.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 433)
  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 433)
  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 11457453
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..433
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=47931
     Region          158..401
                     /region_name="ViaA"
                     /note="Uncharacterized conserved protein, contains a von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG2425"
                     /db_xref="CDD:441973"
ORIGIN      
        1 mtdtraeenr rqvllwrlla rvfetdeqpa leaasvaavd alglppalld psvsvdtlvq
       61 rfpelaeefr glmapgedde eprdrartaa lasklllnlf atgsgdvsat klaawqqdag
      121 wfeqalgcep gelraqpgrn glggllagle gdlvkrmrlr evladpalsr qltpsmslie
      181 qllrdkdnls gvalanakal irryvdevaq vlrtqvqqts agtidrsvpp krvfrnldie
      241 rtiwknltnw spdderlyvd rlfykhtakr tvparmivvv dqsgsmvdam vnctilasif
      301 aglpkvdvhl iaydhraldl tpwvhdpfev llrtqlgggt ngmvamslar pkimdprnta
      361 lvwisdfydn rdvqtefesl hrsgvklipv gsvsssghqs vdswfkqklk dlgtpvisgh
      421 irklvfelkn fln
//
LOCUS       WP_357583248             268 aa            linear   BCT 28-DEC-2024
DEFINITION  Fpg/Nei family DNA glycosylase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357583248
VERSION     WP_357583248.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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..268
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..268
                     /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=28924
     Region          2..267
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpeghtihrl aarhaelfag dkvlaaspqg rfadgaaris gtvlegteay gkhllhhhad
       61 evtlhvhlgl ygkvtdgdge ppepvgqirl rltsdrhwld lrgptacell sppevaalra
      121 rlgpdplrad adpdrayari srsatplaal lldqsvvagt glifvtealf raglsprlpg
      181 reltragwqv lwadlvelmt lavatgridt vraahlpeam grparvdrhg gevyvyrrpd
      241 qpchvcgtpv nrgtvtarnl ywcptcqs
//
LOCUS       WP_357583259             371 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583259
VERSION     WP_357583259.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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 371)
  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 371)
  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 371)
  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 371)
  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 371)
  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..371
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..371
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40762
     Region          80..221
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mtdemlrapa evkyaeeldw lesiddgpkp fswrlsprmv slfvlgsers dgldreiaqk
       61 wfgdrsfver aivtlasdrg llligdpgtg kswlaellaa aisrnstlvv qgtagttedh
      121 ikyswnvsmv iakgqsresm ipspimtame qgvigrfeel trstsdvqda lisilsekyv
      181 sipeldddni vfaqpgfsii atansrdrgv ndlssalkrr fnfvripvvt nkkseaeivr
      241 frttellrrh nidlelpptl ldillqsfad lraaaasaqs ddgklesals taeqigvled
      301 ailhsnffgd rtlraetlag slvgslarrt pedlailnky whgvveprsk kdggewqgfl
      361 eggrqaiatl s
//
LOCUS       WP_357583294             511 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583294
VERSION     WP_357583294.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..511
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..511
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=54314
     Region          215..499
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mlkldrlvnv lggygarlrl apasrgvelr svvvhdpadd rpaggdvyla vgvestaeai
       61 rlaraaravv vlvregvpgd dealtgarda gmavlavdpe vswsqllgvv yglvlegret
      121 eagrgptdlf afadtlagel gnpvtiedqm srvlaysgsq qssdpvrlet ilgrrvpdsm
      181 rrllarkgvf rhlatsdepv fvapspehgl rgrmvvavra grellgsiwv ecerplegap
      241 ltvladgara valhllrsrv sadlerqves dlviqllegt adapalisrl glpggqfrvi
      301 alqahvgdea haailmafer attgfgwsrp grsalfgntl ytvlpsggep tpardwvaai
      361 ahvlprrvtl magvggpavp aqlpasrqea deslalraar pdgdlavvyd eswdaillqr
      421 lraaasagrt pargpvaelt rhdaehgtry ietlrawlea qgdlavaatr lgvhpntvry
      481 rfrkmtaitd lgldqpekrl amiialaaas p
//
LOCUS       WP_357583332             590 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: flavin-containing monooxygenase [unclassified
            Nonomuraea].
ACCESSION   WP_357583332
VERSION     WP_357583332.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 590)
  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 590)
  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..590
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..590
                     /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=65564
     Region          49..527
                     /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 mdkeairrry leerdkrlrp dgndqylrlt gqlshylddp ytpmtarepr rdhvtvafig
       61 ggfaglvtga rlkeagvddv rivekggdfg gtwywnrypg aqcdtasyvy mplleetghv
      121 ptekyahape ilehcrrigk qyglydnalf htevtdltwd gtrwivstnr gdaftaqfva
      181 mgvgplhvpk lpgipgiesf rghsfhtsrw dyaytggdal gtpmdrlagk rvaiigtgat
      241 avqcvphlar acgelyvfqr tpssvdvrgn rptdpewfas iatpgwqqrw lenftanqtg
      301 alaeedlvmd gwtdiarrvr ariaelpage rtlermleaf edsdfekmae irarvdaiva
      361 dpetadrlka wyrqlckrpc fhdeylqayn epgthlvdtd gkgveritet gvvangreye
      421 vdcviyasgf evgtefsrra gydltgrdgv rlsehwadgm rtlhgihvhg fpnafivqpt
      481 qganlisnip hnlteagrti ativkhaldh ghtqveatae aedawvelll sgagsllgsp
      541 dctpgyynne gvdpgragrl mvghpqgava yfrfidewrs sgdfdglafr
//
LOCUS       WP_357583397             211 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583397
VERSION     WP_357583397.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 211)
  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..211
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..211
                     /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=23427
     Region          5..>106
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrtgrppkis radivaaahr vieedgvesl tmrrlarevg stamalyhhv rdkeelllll
       61 lddyaasrpr paelpeepre rvvavatamr ealsgcpwiv dvlraddlls vgalwyperi
      121 idaaveaglt tesaveayri iwhytagelg graaarrrra qggstyrerv faeldaeefp
      181 rlaevgrrwe eltakdtydr glralvggll p
//
LOCUS       WP_357583424             509 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583424
VERSION     WP_357583424.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 509)
  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..509
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..509
                     /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=52967
     Region          12..447
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mpeplnllpd dprtvgpyql egrlgaggqg avyaargpeg ervavkllhp yliadeearv
       61 rflrevetak rvapfctaqm ldsgfagsrp yivsefvdgp slqesvrasg prgaaalqrl
      121 aintatalaa ihaagvvhrd fkpgnvllgp dgpvvidfgi akaldlsqsv vtsqpigspa
      181 ymapeqiagr evgppadlft waatmhyaat gsrafggdti patlhavlns epdldglevr
      241 farllrecls kdpakrptaa qvverlralp ppawqhapas aknarkparr ravvaasvag
      301 algvaagvgf yalapataqq qaaaptssvt gtpgtptgsp pppttpptth lpsitamqgd
      361 vsdlakssaa tptkaprras tappadpdpd pdppssrkpt tapktarptp kvthqsttpk
      421 tpadqettrp papapstgqv swndatayck eqgykgisym agwqgmkcqg sdheispttl
      481 cawkypaysn avgeqpsnpy tpmatcrls
//
LOCUS       WP_357583449             204 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583449
VERSION     WP_357583449.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..204
                     /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=21431
     Region          7..196
                     /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 mdvadltggg apqlgelppi elgntthavr gqvldglrtv ehlaawlrdv rdrlavplsd
       61 adllgvtgdd lrharelrea vralaaatva gqepgpgsva tlnahaarap rwhelrtgpe
      121 pqavvrtagr avdaalsala edavtlfagp qrhelracqa pgcvlyflre sarrewcsag
      181 cgnraraarh yakvrgtkkp tgaa
//
LOCUS       WP_357583469             196 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357583469
VERSION     WP_357583469.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..196
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20097
     Region          58..196
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mgpvpptgrv tgaataalla avlatagcgt gpnaeaaspa ggpasatada tspsagpasp
       61 vpvpdtlrft gttldgaafd aatlagrpvv lwfwapwcat casqawtiae iepgfrqsvp
      121 iigvaglger kamtdfvtef elgpmpqied regaiwrrfe vveqstfvii drdgrvihqg
      181 wldgedltrr vtalaa
//
LOCUS       WP_357583473             482 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-amylase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357583473
VERSION     WP_357583473.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 482)
  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 482)
  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 482)
  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 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..482
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52701
     Region          38..388
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(82..83,86..87,122,125,180..183,213,215..216,
                     218..219,241,243,248,304..305,310)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(124,185)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(215,241,305)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          395..480
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 mhrrrlrpai valaviagll apgvvtappa vaapsggkkv ianlfewnwp svasecsstl
       61 gpkgygfvqv sppqehvrgn qwwvayqpvs yriesrkgtr aqfktmvdtc haagvkvivd
      121 avinhmsgqd nggtgwagst yqhhvypgiy qaqdfhycgr ngnndivnyn dryevqncel
      181 vnlsdlktes dyvrsrlaah lndllslgvd gfrldaskhm paadianirs rlnrsayivq
      241 eviygagepi tpneytgngd vhefrygkdl arvfrserla ylrnfgegwg hlpssvssvf
      301 vdnhdtqrdd ggvltyrdrg iyalanafml awpygsptvm ssytfssrda dppsdgsnkt
      361 lnavcysgwe cehrwpvian mvgfrnateg agvsnwydng nnhiafsrtg rgfitindeg
      421 saingrsyyt glpagrycdv ihgtftngtc sgpvitvdan gwfaanipah daialhlnar
      481 lp
//
LOCUS       WP_357583534             115 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357583534
VERSION     WP_357583534.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=12722
     Region          1..94
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mstslaapap eldsafaalg dpvrralvtr largdatvge laepfdltpq aishhvgvlr
       61 rcglieqrre gtrrpcrlsv dklsmlgtwi ddqrriwddr ldalerhlvd keavr
//
LOCUS       WP_357583537             518 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583537
VERSION     WP_357583537.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=56170
     Region          4..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(173,176..181,183..184)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(176,293..294,315..320,398,410,413,424,504)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(176,217..218,265,267..268,271,293..294,315..320,398,
                     410,413,421..424,485)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(217,267..268,271,293,421..423,479,485)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mlnlsiiled saravpdrta lvygdlrlpy amvdsvanqv anllvergig rgdkvallcp
       61 nvpyfpfvyf gilkagatvv plnvllqpre iayhlddsga kalfcfegtp elptgargre
      121 aadategceh ffvlpatpla teseygesfw aaldgksgef etvgtgaedv aailytsgtt
      181 grpkgaelth anlllntmvs demfprdpeg dvslavlplf hsfgqtsvmn vslrrratlv
      241 lvprfepgqa lelmrgervt mfagvptmyw amlakihage aevpaslqva vsgaaacpve
      301 vlkdfeatfg ipilegygls etspaacfnq lsrptrpgti gfpvwgvemr lvdddwntve
      361 gegpgeiavr ghnimkgyhg rpeetaevlr dgwfrtgdia trdeegyysi vdrtkdmiir
      421 ggfniyprel eevlmthpav slvavvgvph gshgeevkay vipspgsavt eaelvdwcre
      481 nmaaykypri vefceslpmt atgkilkrel rrsradvg
//
LOCUS       WP_357583563             125 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583563
VERSION     WP_357583563.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..125
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13929
     Region          13..117
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 metivessgl padafsakcp trqvldhiag kwtilvvdal ldgtmrytdl srriegvsqk
       61 mltqtlrsle gdgfvtrtvh ptipprvdye ltalgrslae pitalrrwte dnineierar
      121 erahd
//
LOCUS       WP_357583583             423 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583583
VERSION     WP_357583583.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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..423
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..423
                     /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=47795
     Region          88..418
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maktmlgtpe eepkrrtgrr irkrsngegs iwprkdgryg yaafvqttag tvkrvqgsar
       61 tqedarkklt ellrqadegi pvssenwtla dflnywlkni vsqerrpkty qgyegvvrlh
      121 lipglgkkrl gklnaqdvrl finrvrsecq ccrngwdasr ekpvccalkg gqccdsrlst
      181 rmvqsihavl rnalecavre eiiarnvakl ikvpvpkykv nrgltvpqar avlkaardhr
      241 lyalyvlalc lglrrgellg lrwtdvdlea gklevvqslq rvagrlqfvr pktsdsertv
      301 plppicveal rehrrmqfae rsdrweewke hglvfpsrcg tpmepdnlrr swgairntag
      361 lgemrfhdlr htcvtlllnl gvppqvvrdv vghsdievtm tiyahvsldd krlalgklgd
      421 ala
//
LOCUS       WP_357583628             155 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583628
VERSION     WP_357583628.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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..155
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..155
                     /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=16114
     Region          2..134
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrltaftdis lrivmrlavv sgdellttra aadvlaipyt haakavsrls emglvetrrg
       61 rggglqltaa grqatvgsiv rrlegehevv gcedallpcp lraacrlrga lrqaqeafya
      121 sldtltvdal vtgptgpvll glsvpprsgt gepal
//
LOCUS       WP_357583648             417 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357583648
VERSION     WP_357583648.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..417
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..417
                     /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=44029
     Region          11..407
                     /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 mtnteispst aapvrprlgw ldalrglaal vvvyehalnp lypelrgvtg pwfdagwygv
       61 ivfflvsgyv ipaslerrgs vagfwigrgf rlyplwavvv caalllvvtg idgihvyltd
      121 npvtatlahl tmlqdllnap nvvnvlwtls yemafyllvt alfvarwhrr saevaagfgv
      181 lavvaggvlp tillthrgpt lvttlaavvl gggglagvls srpalrraga valavlplgl
      241 iavnsripaw qsltilatmf agtalyrwqa gqisrgrgwa vaggvpvaat gaallwhdgd
      301 plpwvaavla awatfgagml ladrrvpaww awlgmvsysv ylihpillei vdgflddpaa
      361 vawpyrvglg alvvavllgc saltyrlvea paqrlgrria arstgssnar rsspggg
//
LOCUS       WP_357583650             302 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357583650
VERSION     WP_357583650.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   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 302)
  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..302
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..302
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31437
     Region          1..302
                     /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 mdtghvtsad gtvigfhrlg agpglvvlhg qmesarshle laealagtyt vylpdrrgrg
       61 lsgpygphhv adreaedlea llahtgasrv favsvgalva lhtaarhrag stgspkehag
      121 glrtagagli relalyepal fvdgpaptaw leryerelaa grdaaalita mkaarlgpai
      181 fdlmprrlld alsarmlaaq drkagdgdvt mrmlaptlrh etrvvaelar sqaaygavga
      241 rtlllggsrs payfkaalda lervvpgaar velagvghsg sgnadtggrp ervaaelrrf
      301 fg
//
LOCUS       WP_357583686             254 aa            linear   BCT 28-DEC-2024
DEFINITION  metal ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357583686
VERSION     WP_357583686.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,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 254)
  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..254
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..254
                     /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=26226
     Region          1..226
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mtpdvitvth gvvgydgrpv lrdvsltvta gevvavlgan gsgkstlira ilglvplsag
       61 tvtlfgrpvr rfrqwhrvgy vpqrlgagsg vpatvaevva agrlarrgil rppgrtdrda
      121 vaealhavgl adrakdpvtt lsggqqqrtl iaralagrpe llildeptag vdaasqeafa
      181 galrdftvgg gtvllvahel gplrplisra ivvhqgfvah dgavpepagh haapdhdhvh
      241 phgpeepagl wsar
//
LOCUS       WP_357583703             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357583703
VERSION     WP_357583703.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,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 265)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..265
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28545
     Region          15..257
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnvpattsql qepairvrgl eksykqlrvl rgvdldvarg sifallgsng agkttvvkil
       61 stllkadagt ahvngfdvaa qaadvresis ltgqfaavde iltgrenlvl varlrhlkap
      121 dviaddllrr fglteaggrr vatysggmrr rldiamslig nppvvfldep ttgldpqarl
      181 evwqavnela qggttvlltt qyldeaenla driailhegr iivhgtldel rrilppaeve
      241 yvekqpsled ifltlvgagt dkeqp
//
LOCUS       WP_357583788             308 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583788
VERSION     WP_357583788.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..308
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..308
                     /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=31529
     Region          5..304
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msvlslavga qdiplgevwq qfwqpdggei aavvhdlrvp rtllgicvga alglagalmq
       61 altrnpladp gllgvnsgas lavvcsilff gasdmstwvw fsmagalias vvvyalgahh
      121 ptrlvlagaa vsasliaain gvlsldagvf dqwrfwdvga lagrsldvvq qvapfvlagt
      181 llalglgrgl nalalgeqtg qalgvrlgri rlltgiaitl lcgaataaag pigfiglmap
      241 havraftgpd hrwvigysav fapalllaad vlgrvvvrpa elesgivtaf lgapifiyll
      301 rrrkaipa
//
LOCUS       WP_357583781             379 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357583781
VERSION     WP_357583781.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..379
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=39809
     Region          1..342
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mnivvigagy agltaalrld rthhitlisa eahftqrirl helaagrptv rvplaeltrg
       61 tgietvvarv aaldpsarvv rtedgrefgy dtlvyalgsr tdvrvpgvae haytaesaaa
      121 lrtrlasggg dvavvggglt gvemaaelae typawrvtlv sgnepvlsar grrhvagals
      181 rlgvitrygv rasgvsagtv httdgdisad vvvwagsftv ptlaaeaglt vdargravvd
      241 atmrsvshpd vyvvgdaaav ripgagesrm scaagmpiaa haadsvnara agrqarpfrf
      301 ryliqcvslg rrdgliqfvr hddspvetvl rgrgaafvke licrstvafl rlerrrpgty
      361 mwvkgpkpap aerlagara
//
LOCUS       WP_357583818             244 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583818
VERSION     WP_357583818.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 244)
  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 244)
  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..244
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..244
                     /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=24683
     Region          6..235
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mnhsyvvtga grgigravve rlgpatvvav erdpdalawa gpgvipvigd aadeavlvra
       61 aglaeeagal tgwvnnaavf rdaalhtspa geiraliaan ldlavtgcav avrrflaaga
      121 ggaivnvtsh qarrpvpgsl pyatakaave gltravavey grhgiranav apgsvatery
      181 erllaerpgt eeemavlhpl grvatpaeva davayllsas fvtgvtlpvd ggrtvlgldp
      241 eare
//
LOCUS       WP_357583824             272 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357583824
VERSION     WP_357583824.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..272
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29312
     Region          24..251
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 maesrehqfn gtrgvnvvre wphpdpryva llvhgygehi gryehvadtl vrhgaavygp
       61 dhmghgrsag ervliedfed vvtdvhtveq qaradhpgvp vvlighsmgg liaaryaqrh
      121 gaglaalvls gpvigvwevv dtllpldelp dtpldpatls rdpavgaaya adplvwhgpf
      181 krptlralat tletitkags lgplptlwih gaddqlvpla gsrtgidavr gddlteriyp
      241 earhevfnet nhdevladvt afidrtltsp dv
//
LOCUS       WP_357583852             388 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357583852
VERSION     WP_357583852.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..388
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42688
     Region          2..388
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
     Region          309..338
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          342..370
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mleeafrdew grvvaslvgf lgdfdraeda aqeafavaar twprtgppds pgawlvttar
       61 nraidrlrre ralagkmhll aepeatvdea ddtlikderl eliftcchpa lplegqvalt
      121 lralgglnta eiaraflvse etmkrrltra ktkiraagip ftvpgahllp erldavlavl
      181 yliynegysg rvdlgaeair lgrvlaallp depetyglla lmlihharrr arfagerged
      241 lvllddqdrs lwdldriaeg ravldraial ggrgayvvqa aiaslqaher vdwpqvaely
      301 rrlaaltgsa vvelnraval aqagdpagal cavdrldldg ylyfhstrge llrrlgrdge
      361 araayrrald lavstperrf ltrrleql
//
LOCUS       WP_357583874             388 aa            linear   BCT 28-DEC-2024
DEFINITION  homogentisate 1,2-dioxygenase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357583874
VERSION     WP_357583874.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..388
                     /product="homogentisate 1,2-dioxygenase"
                     /calculated_mol_wt=43304
     Region          1..385
                     /region_name="HmgA"
                     /note="Homogentisate 1,2-dioxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3508"
                     /db_xref="CDD:442731"
ORIGIN      
        1 mpyyrsvgel prkrhtqfrq pdgslyteel mgqegfssds sllyhryapt aivaaeefvp
       61 paltrmpnlp lkprhlrthk ldgtgadpvl grryllandd vriayvladr psplfrdatg
      121 dhclyveagt lrvestfgvl davpgdyvii ptstvhrlvp tgdtptrlla veasghigpp
      181 krylsvrgqf lehspycerd vrgpdapllv dgtdvevlvr hrrgwtrhvy anhpfdvvgw
      241 dghlypwafs ihdfepitgr ihqpppahqt fagpnfvics fvprkvdyhp daipvpyhhh
      301 nvdsdemlfy tggnyearrg sgieqgsisl hpsgfthgpq pgaaersigv dffdelavmv
      361 dtfrpldlcd aaaeceddgy awtwarrp
//
LOCUS       WP_357583915             126 aa            linear   BCT 28-DEC-2024
DEFINITION  response regulator transcription factor [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583915
VERSION     WP_357583915.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 126)
  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 126)
  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 126)
  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..126
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..126
                     /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=13719
     Region          7..>123
                     /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 mgevlgkvlv vdddevirql iavnlnlegf evttatdgqd cldqvldvmp dvitldvmmp
       61 cldgwttaqr lraeeatshi kvvlitaraq dddkrrgrgl gvdayltkpf dpaeliqvvr
      121 elaaks
//
LOCUS       WP_357583921             508 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583921
VERSION     WP_357583921.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 508)
  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..508
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..508
                     /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=52925
     Region          1..508
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mfdvvisggr vldgtgapay radvaisgdr iaavgrldga gaaavidaag rlvapgfvdc
       61 hahgdavvfd rgvqlaalrq gvttfvlgqd glsfapgsae tvayasryfa avnglltegp
      121 ltvaelldgy drsvalntay llphgtiryd vmgaspeaas pedlagmlar verglsegav
      181 glssgleylp gryasagela elcrplaglp yvthmrayga ragvgmadvv eiaqlsgaav
      241 hvshlhgpad vllplideah gkdvdltfdt ypylrastil amvvlppsvp gaevdralem
      301 iasteldaww aglaptwprl tishapglew aegltmveaa eragvdpaaf crrllvetrl
      361 eagcvaarpd egpageesvr avlrhpsqtg gsdgiyvggh phprgfgafa rflgrhvrel
      421 gdwtweqavv hlashparrf gmhdrgllrp gfaadvvvfd pltvgdqaty daprtlaagv
      481 ddvlvsgqrv laageltgat pgralrpr
//
LOCUS       WP_357583924             363 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357583924
VERSION     WP_357583924.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 363)
  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..363
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..363
                     /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=39471
     Region          1..363
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvtyakas riypgterpa vnqldlqigd geflvlvgps gcgkstslrm lagledvddg
       61 aiyiddrdvt hlppkardia mvfqnyalyp hmtvyenmaf alklrktsks eidrrvkeaa
      121 allqleeyls rkpkalsggq rqrvamgrai vrepqvflmd eplsnldakl rvqtrtqias
      181 lqaklgittv yvthdqveam tmghrvavml dgvlqqvdtp rtlydtpanv fvagfigspa
      241 mniktvsfse qgaafaemlv pltreqaeaa nseggngkvt vgfrpedcdi vspteggmpv
      301 vvelvedlgs danvyghaal dgaserfvvr tdrrtmpnmg dtifvkprtg qshvfhaatg
      361 qri
//
LOCUS       WP_357583970             256 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357583970
VERSION     WP_357583970.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 256)
  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..256
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..256
                     /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=26552
     Region          69..256
                     /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 mdfvqspdwp aappgalaan saaaryggsa ptppsigrat appppthsat apppyrppaa
       61 tpaatgtpra tppipvkilv aggfgvgktt tvgsiseiap ltteaemtta gigvddpgqr
      121 sgkttttvam dfgcvtidrs lklylfgtpg qtrfgfmwdd largalgalv vvdsarlddc
      181 ypaidffera glpfvvgvna fdgrlahdlg airwalaige hvplvqfdar drlsvrdall
      241 vvldraldra trekra
//
LOCUS       WP_357583984            1000 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357583984
VERSION     WP_357583984.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1000)
  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 1000)
  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 1000)
  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 1000)
  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..1000
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..1000
                     /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=106520
     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          104..1000
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrfrvlgplr vedgqgpgpa khrallaall lsagravpve rlvsvlwgdq ppqsadpvlr
       61 vyvsalrkiv dgittvpggy liaadpdevd chrferlvgq armardagav aeaagtfrea
      121 lglwrgqala dvdsaelrra hgvpleelrl taveerveld lrlgrgaevv gelralvnah
      181 plrerawahl laalhqagrr sealaayqea rrilvddlgl epgaelreah ervlrgevaa
      241 vpvaerrvpl netppdisdf tgradvlawi lraatpeggg gapvllvvhg ppgsgksava
      301 vraasrmdlp dgrlyavlgg rapgavledl lrslgcpdgs vpptlgervr lyrrltsgrr
      361 lllvlddaad etqvrpllpt gagsvtlvts rsplagleaa rayelgvlap dealdmlagv
      421 agrdrvaaep eaareivrlc gglplalria gsrlarktgw tvahlagrlg derrrldels
      481 agdlavrgsl avgyrglaep errllrelga wtgpdfadwa lgadleplae agllqslgld
      541 eagqerygwh dltrlyaver laeaggpgpv lracaaevld rarrarsall paepgsgrtl
      601 vstpddpptp rpmpargdqa grgpvaapyg vfplsgegar reeagaggpv aapygvfphs
      661 gegapweeag agwgpgvgrr eetsrgtawl rrearwlaae rrflaaavgd fhraglheaa
      721 wrlafyltpl felgghhddw hattatglda araaghrqge alllrgladl hrvegradaa
      781 aaalraaqpl veglelarvt lrlglveprr peaervlrra ltvfeqagdl rgradalrgl
      841 gallddqaml erslagyeel gdprgaaear ldlarlhlra gryaeareha elriaanrrl
      901 gdrlpeaagl lvlaavaraa gvpesaaepa rqaaetytay gdrrnaaaal lvlartylel
      961 grndgavdal mramgefdvl gdrqsraeae hlarearrrl
//
LOCUS       WP_357584025             242 aa            linear   BCT 28-DEC-2024
DEFINITION  ComF family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357584025
VERSION     WP_357584025.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 242)
  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 242)
  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..242
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..242
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=24382
     Region          13..202
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mlgpvlgpvv gpwldlvlpr pclgcgaage rlcegclgrl adparrtpdp vpaglpacws
       61 agpytgalrt alvackerge aslgaaladl laftaltalt asgdaavtvv pvpsarraik
      121 grghdvvgal aapvvrqlra hgvaatlwpg lgqvrrvadq aglssteraa nlaaslgvrr
      181 aagtppaapv llvddivttg atlaeaaral raaglrvpla vtvgatrrst rpymatrrrv
      241 se
//
LOCUS       WP_357584085             435 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: purine-cytosine permease family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357584085
VERSION     WP_357584085.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..435
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..435
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46132
     Region          2..430
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mttdsdyple rvpqsarypw fnvavqrfgq lsdltqfllg atlgaglsfw gafwaftlgs
       61 vilevvcifv giagmregls tsmlarwtgf grygstligi vitlslfgwf gvqtavfaag
      121 lhsimswlpl wawsliagig vtllvirgfk amgmtafitv paflglagwa mwveisrhdl
      181 gtlvasppfg episiatgat ivagsyivga vttpdmtrfn rntgdvvkqt lvgislgeyv
      241 lglagvllay avktsdviai itassgvvgv ivlisatvki nnwnlysstl gllnavettt
      301 gvrlnrvtvt igvgvlgsvl aalgilerft dfllilgvvt ppiagimvae yfvvrrwrpv
      361 ldasraagrl pdtepawvpa tlviwaaaal fgwlsehyqw igipalnsll laglayvvag
      421 rlglvrasre qpvla
//
LOCUS       WP_357584116             306 aa            linear   BCT 28-DEC-2024
DEFINITION  type II secretion system F family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357584116
VERSION     WP_357584116.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..306
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32734
     Region          130..>295
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mvetvlaggv aglglfvllr alfparpglv arllaldavr edaespriql vlpdeevsaf
       61 rrglglrlvr lygargwevr siradlalvg rsfegflatk allavsglla fpvlfgwlvl
      121 mgwgaspaip fwvaliaavv ffflpdlqir rdaaarrrdf rhvvgafldl vsmnlaggrg
      181 vpealmmavs vsgeqpnwai grirdalsga rivgitpwqa lgqlgeeini delrdlsaal
      241 glvaddgakv rasltaraat lrrrelaeie gragersqsm lvaqlllcag fviflsfpaa
      301 mkmlgs
//
LOCUS       WP_357584119             268 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357584119
VERSION     WP_357584119.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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..268
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..268
                     /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=28842
     Region          9..260
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtsrvpvlls sssvfperta aafqlaathg ydglevmvwt davsqdagal rglsdhygvp
       61 vlsvhapcll vtqrvwspdp werlrraavl aetleaptvv vhppftwqre yargfaegld
      121 rvagefgglr favenmypvr magrqfvpyl pgwdpteagy asytldlshc aashtdalam
      181 adrmgdglah vhlgdgtgeg rdehlvpgrg nqpcaellrs lagrgftgsv avevttrgak
      241 srqvreadlr ealafarqhl ntpspvda
//
LOCUS       WP_357584138             724 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357584138
VERSION     WP_357584138.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 724)
  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..724
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..724
                     /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=75161
     Region          9..463
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     Region          <500..>577
                     /region_name="PspC_subgroup_1"
                     /note="pneumococcal surface protein PspC, choline-binding
                     form; NF033838"
                     /db_xref="CDD:468201"
ORIGIN      
        1 mhplrpgdpe rigdysilgl lgegprgetf lgresddapi rvikllpgvp epapdalapy
       61 laaqrvsssy varvldagyl adrpyvvreh vegkslaetv eadgpltgda lervavgvlt
      121 alsavhlagl thrsltphnv ilaaegprvt dvtvgdpvge pgyqapeqlt glqygpyadv
      181 fawaatmtfa atgkppfadr davltgepev gvgdealrrv llsalakdvs qrpttysalm
      241 qvlgdpgagr qqapdqtaie gvpvpgvalq gvpipavplp gmqpmvppqg gpgqpmqgpp
      301 mqhptmqgpp mqgspvpgvp qqaepmwgpp epggqpqqpp qpqqirleav qprgsqgprr
      361 kfpmglvagv gavalvsaig lwganryvey qqvgttvaaq asadgipvpn sasaapvpqg
      421 tapdggpvpq qpqptvtvpw gatpdvdeag vaplvlptew ptttagvpel tsvpttptam
      481 ptqpvvvptv tqqptaapta eaeptptkrk kkpqptatvt ktekpteqps eqptekpsek
      541 pteqpseqpt ekpsekptek psekpsekpt ekptqapepk ptptkpkptp tqpkptptqp
      601 kptptqpkat akqaapvknp ytptqvcgsg fvvqrsssfs ggatyqlwnn stgqncvvtm
      661 ktvdvgkatp vratlevqng psktdsgnfe yyagpvklpa agkcvrysgs vgsgstsagw
      721 ancg
//
LOCUS       WP_357584190             416 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357584190
VERSION     WP_357584190.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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 416)
  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..416
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..416
                     /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=44397
     Region          35..412
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtrptrgtgm tgpsvvswpy pqgglggnpn lppgerlrvl lveddegdaf lvgellaetn
       61 sgidllvats lsearrriag vdcvlldlgl pdaqgldglr qvlemsgsaa vcvltgrtde
      121 hlgivavaeg aqdylvkgqv dgvlltralr yaverkrade narrlrevel rqaesarler
      181 gllpqplmst dqiavhtfyr pgrhaaligg dfydvvqtrp drvdliigdv cghgvdeaal
      241 gvelrvawra lilagvpdde vlpaleqvlm serrlqeifa tvatarldla agratvrlag
      301 hpppvllagg rvtpvpapgg lllgvrprrp vafdlkfdte dwsllmytdg liegrvgagd
      361 erldvpgltr llaepasrav plpdlpawlv graeqlndgp faddvamllv trgggr
//
LOCUS       WP_357584163             433 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357584163
VERSION     WP_357584163.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=46620
     Region          3..345
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mirktgvaal vavtlalsac gggggepaad pgqprvlklw hyeaaesamg kawaeaikkf
       61 eathpgvkvr feeksfeqiq ktasmvlnsd eapdlmeynk gnatagllsk qgliadmsee
      121 vtkrgwdkll pgglattary ddrgvmgsgn wyglpnygef vmvyynkdlf ekhkvevpat
      181 yeeftaalda fvkagvtpvs lagaeypaqq ivyqlalska drawvdayqs ykgkvdfqgp
      241 eltygattfa dwvkkgyvde kasglkaedm gvafmkgdfp vmisgswwyg rvaeeakgfe
      301 wghflfpgst mapgssgnlw vvpeksankd laydfiditm skeiqnllgn sggvpvaadp
      361 aaitdpkske lietfnklta adglafypdw papgyydvlv agtqqlinga kspaevltei
      421 agpyednlad lgn
//
LOCUS       WP_357584161             285 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357584161
VERSION     WP_357584161.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 285)
  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 285)
  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 285)
  AUTHORS   ter Beek,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..285
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..285
                     /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=31776
     Region          2..285
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrrrgywpyl apslllflgv ivvpflmnlg vsftrwsgvg tprwvgldny arllederfw
       61 lsfqnnvali vamaivptvi glvlaaalfd yvgkrfgtrt aaalramyyl pqvlpvavag
      121 vvwgwmlhps ygavnrafgl eldwlgdpdl alatvmavmv wfqlgypvvi fmaglqrvdp
      181 ayyeaaeldg aswwrrvwhi tvpqirpeif vvlltctiaa lkvfgpifvl trggpgnatm
      241 vpsyfsylnf fqksnvgygs aiatvlalii vvvtflflrv qerer
//
LOCUS       WP_357584202             223 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357584202
VERSION     WP_357584202.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=23965
     Region          <4..189
                     /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 msdrkpdegg iaviglgrfg shlaeslsal grevlaidrd aqqvqkwspm ldqvaqadat
       61 deealrqlgv tdlgravvai gasveasvlt vlalvelgvp qiwaratsgq hakilssvga
      121 hrvifpeaet gerlahlmis rmldfvefge afavarirvp aslvgrptte vrlldrygvr
      181 vigikrpgeg ryryvsdgle laedtvlive gtieqvqrfs tls
//
LOCUS       WP_357584216             248 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357584216
VERSION     WP_357584216.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  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 248)
  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 248)
  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 248)
  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..248
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..248
                     /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=24937
     Region          1..246
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mserlavvsg ggtgigaava ralvvdgcsv lvvgrrpevl taaterigae sgrpdairsv
       61 tadltdpdhv vkvveavggr pvdvlvnnag gyhsadsgtl agiaanwrat ldtnvltavl
      121 ltealrpalr rpggrvilis siaaqrgggd aysaakaalh gwayslaaql gpdqitvnvv
      181 spgyvaetef fagrmtpegh aqrvaatlvg ragvpddvae svrylaspaa gyvtgqvlgv
      241 nggsvlgr
//
LOCUS       WP_357584252             487 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357584252
VERSION     WP_357584252.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=50409
     Region          8..384
                     /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 midenrsdgm paeqvlaeir elramdrpth ggrlfayvyd savpgldala aaayaesahv
       61 ngldptafps llamentlva aaarllgggp gtsapdvvgs vtsggtesli lavktardar
      121 pdiaaprivv pasahaafak aahylrvdld tvpvdpttlr ptvadvaaav rpetvlvacs
      181 apsyahgvvd pveqiaevaa aagvrchvda cfggwtlpyl rrlgtpvppf dlavpgvtsi
      241 svdlhkyaya pkgvsvllhr dpqlrapqyf ayadwpgytm inpvisstrs ggpiaaayat
      301 lrhlgddgyl eltrrtwvav rtladavrgt dglrlvaepe stvvcltatd dgpdlfvlvd
      361 elavrgwhtq pqlsyaglpa svhltvtaav apraaefgpd ladavsaara agpvglppel
      421 ralagtlape altgdlvagl aaglglgpgg glpermapvn tlldaappal rerllvefvs
      481 llqrpaw
//
LOCUS       WP_357584287             277 aa            linear   BCT 28-DEC-2024
DEFINITION  polysaccharide deacetylase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357584287
VERSION     WP_357584287.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 277)
  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..277
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..277
                     /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=30343
     Region          5..272
                     /region_name="CE4_HpPgdA_like"
                     /note="Catalytic domain of Helicobacter pylori
                     peptidoglycan deacetylase (HpPgdA) and similar proteins;
                     cd10938"
                     /db_xref="CDD:200563"
     Site            order(11,13,82,86,234)
                     /site_type="active"
                     /db_xref="CDD:200563"
     Site            order(19..20,26..27,29..31,33..34,41,60,63..65,84..85,
                     87..88,91..92,95..96,99..100,103,123..124,126,144..150,
                     181..183,188..190,192..194,211..212,215..216,219,240..242,
                     244..245,248)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:200563"
ORIGIN      
        1 mpenticltf dfdaislwla rgmtspgpvs rgefgahamp rilkalarrg itatffvpgh
       61 tvdtypaeca aiaeagheia lhgyahepvs kldragelaa avrardsirr vtgyeptgnr
      121 tpswdftast vdvllelgce ydsslmgtdy tpyyarrgdv adadgpyrfg eptplvelpv
      181 swslddypqf eylrtdtaim pglrdpgtvf gnflddvdym vreepggvcv ltfhpqvigr
      241 ghrmiglerf ldaclerpla frtcqevara fragdgs
//
LOCUS       WP_357584278             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357584278
VERSION     WP_357584278.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31335
     Region          36..295
                     /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 mrafrwpppp dggprtwgpg pgaprtgrpp lpdpetelva tphgvrlerl vtgvgdpvtv
       61 fahglangia ttrpfgsgvt grrvffqfrg hgrsdapdgp wsyldlardl raiadlsgat
      121 rafgaslgag alcrllaesp erferlvffl paaldrprgp vararltell savesgdasa
      181 aaevvstelp pairntpagw aylrqrldhl lrdglaaglv dlpeqaplpd asvlarvtap
      241 alviaaegdd lhpvevaeql aallpratlh rydrpgvlwt eradlrgris dflng
//
LOCUS       WP_357584291             244 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357584291
VERSION     WP_357584291.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 244)
  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 244)
  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..244
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..244
                     /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=25426
     Region          21..243
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 meleglvaav tggaaglgaa ivdglrarga qvvygdlrdd rppsagalyh pldvrdrdsw
       61 dafaetvrat hgrldilvnn agvsvrsgll dtadddwdrv lrtnlwapwt girafaaelt
      121 asphasvvni gsvygqvppp gppsppssva yqvskaglhm ltrtaavela grgirvnavl
      181 pgvfvtpllr qlsddqlrpr ierapmarpg dpadvaeava ylasprasfv tgvllpvdgg
      241 ytas
//
LOCUS       WP_357584348             315 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357584348
VERSION     WP_357584348.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 315)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..315
                     /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=34387
     Region          14..300
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpavtapera prgasvmpdt pgwarwandh rkwlfaapam afvaaliifp lawtgylslt
       61 dsagsvraes efigfgnyve vltdtdrfwp avartgaftg valfvevvlg mavalllwrp
      121 frgekwvrva illplvatpv avgmmwrlif dpniglanqa lgwvgigpqp wlagqhtalp
      181 ttifidiwqw tpmvvlilla gltslsdepq eaamidgasa wqrfrhvtlp llmptvivai
      241 llrgidalkt fdilyatkgr gggsfhevet lnvyayglsf dyneyglsst vlilffliii
      301 gsmwaltarr kgagr
//
LOCUS       WP_357584420             325 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357584420
VERSION     WP_357584420.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 325)
  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 325)
  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..325
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..325
                     /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=35442
     Region          71..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mcygydgmaa lrrsvldrrg llrgsvaama gvglatagvg ataaaakpgh gpghghgpgh
       61 agrrrvppgl isiqlwtvrd alngepgyda tlrhlarigy pkvelalgyf grnaaqlrrf
      121 ldsicvkats shdgisetpa alrekisnav tlgqkfmvvp ylysenaddw krwaeqmnve
      181 aaaaaraglr ygyhnhahef tidlgggrtp wnilteeldp rlvhleidiy wavtggiesg
      241 dgvtdpegft ldvirsapqr vlqyhvkdrh aadgdmadlg tgmidfarif rkhsvleyiv
      301 endtpdvtpq rtaeigyryl rnlry
//
LOCUS       WP_357584462             164 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357584462
VERSION     WP_357584462.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (residues 1 to 164)
  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 164)
  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..164
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..164
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18366
     Region          27..127
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mevgtsqslg ycgdtggdyd vlqwdtredc evrqildrva dkwsllvial ldrrslrfse
       61 lrrmidgvsq rmltrtlrhl erdglvsrtv hptvpprvdy eltslgatlh stirelvtwt
      121 eshqneiata raaydarvla eqeaaeadag rraeiarsvl tgsr
//
LOCUS       WP_357584482             451 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357584482
VERSION     WP_357584482.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=48660
     Region          99..447
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrlglrarv taafaigall lsasmalvsy eltrrtllde rertvlraay ydaavvragl
       61 ntenpdvaea lraldtgtgr rplvllngew yarsadnglt tivparlqel vsagepavqr
      121 vrvndhpvml vgvplsesta fyeiaslrel eqtfqilala ltavaimvag sgaalgwyat
      181 rhglrpltav adaaeriaag dfttrlapdt dpdltrlsts fnrmvdelag ridrdrrfaa
      241 dvshelrspl qtlaaaasvl srrrenqder tataarlvad eidrfqqlvn dlldlargdq
      301 pvhrepvdlp elarqacqdr dlpesmvqla agtptswrvd rrrvtqvltn lldnaeryga
      361 gpvavrlsht adtgvievdd egpgvpmedr evifdrfvrg raanyrgggd gtglglalva
      421 qhaaahggda svsdrpegga rfrvtlpgsv s
//
LOCUS       WP_357584474             319 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357584474
VERSION     WP_357584474.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=33847
     Region          36..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 mstsvvvdpd spqapavtvg tvavvahrkk nlgggldelr avlvgagveh llwyevpksr
       61 kapkkvrkal dkgaelvfvw ggdgmvqrca dtlagtripm ailpagtanl fatnlgiped
      121 lreavriglh grrrrldlgk lngehfavma gagfdgdlir eadremkgrl grlayvwtgl
      181 rhvrgeltrt ritvdgatwf dgaascvlfg nvgtitggip afddarpdsg aleigvstas
      241 gavdwartlg kmatgrsdds kfvritrgrk vkvrfaepkt yeldggarst arklkvravp
      301 aaltvccpep daeeasasr
//
LOCUS       WP_357584559             445 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357584559
VERSION     WP_357584559.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=46256
     Region          3..438
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 msdvlvvgag fsglaaalrl aragvrvrvl eardrvggrt ltrwlddgtq ldlgaqwigp
       61 gqdrvhdlvr ryaletfpsa algapvvmwd gvrrdappdv aarvidlldg yadlldpaap
      121 wtapeaarwd attlgdwlsg tapdpvtary ldrllaggll atsanqvsvl qmacylrsgg
      181 gagsllgmag gaqqdrivgg paalaeamaa glgpgvvrls tpvvaieqdd gsvvvraete
      241 rfeaaavvva vpptlagrir yapalpplrd glaqrmpmga alkvhavype pfwradgwsg
      301 vatcsdgpit etvdngtpts prgvltmfsy gvaanalram tpperaaall dalaaiagpa
      361 arraeeiidh dwsadpwtrg cfggaltpgs wreygpslrp pvgrihwagt etairwtgyl
      421 dgaieagera aaevlsripa apgpa
//
LOCUS       WP_357584552             355 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357584552
VERSION     WP_357584552.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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..355
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..355
                     /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=37660
     Region          1..340
                     /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 mdtivigggq sglaaaralr lrgrtpvile agpepagswp hyydsltlfs parysampgh
       61 efpgdpdhyp trdeaaaylr ryadsldvei rtgvrvtavr pdgaggflvh patgdpirtk
      121 gvvaasgsfg npyvpilpgq dgftgralha aayrdpgqha gqrvvvvgag nsavqigyel
      181 artatvtlat rapirffpqi iagrdahhwh tttgfdtlpp pwlariatgt lvmdtgdyaa
      241 sleagrwdrr pmftafdgdr vvwadgsrep vdtviyatgy lphldylrpl galderglpl
      301 hdggistttp glayvglefq rsfasntlrg vhrdadhvaa pvaayaggal taygl
//
LOCUS       WP_357584577             251 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357584577
VERSION     WP_357584577.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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 251)
  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 251)
  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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..251
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26200
     Region          24..>215
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mpdhaeptnp vpdadgrgps rrqvravlfd fhgtlaqvee psrwvlaaaa acgveldrvr
       61 ataladrllt agraggplpa rvpphlaelw adrdlyehah rgaytglagt vdagidgfae
      121 alyervlvpq gwvpypdtgp tlaalraagv rvavvsnigf dirplfdawg ladlvdahvl
      181 syevgrckpd paifwracgm lgvdpeeslm vgdtpadaga vaagcaalil paadpgrpna
      241 lgsvlnflpt p
//
LOCUS       WP_357584582             318 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357584582
VERSION     WP_357584582.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 318)
  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 318)
  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..318
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..318
                     /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=33357
     Region          76..311
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mwaeplaqtt aeaqdvakfw lndgganlrn atpyavqtta ggerlttdiv pggppasipp
       61 legptlpdgs apaasgrvff igsdgkphwc tgtvvnslyr nlvataghcl ldieapmgsl
      121 gkwvfvpgys dgqipfglyv gkrasvhhdf eglrdfdrdy afanvysgvv laspgvlsnv
      181 grlaenvgaq gmtinqplap tvdvfgypag phpdgslpyt getlerstgs tfamntrlfr
      241 adrpigansp ftaegslgss wltgyasgsr tghlngitvs vsdtdgdnry dsgispyfds
      301 elyvvyrnaa smwtgvia
//
LOCUS       WP_357584609             205 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357584609
VERSION     WP_357584609.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 205)
  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..205
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..205
                     /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=22088
     Region          <76..160
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mnirmaivig gvgpdrfgpa aadwltcrag lrkhppgdqa aapavvmgvd vdvdvdvldl
       61 aeawlppvpc erpsvappav rdlapwlasa dafvivtpeh nhsfpaslkn avdwyrdewr
      121 akpvafvsyg ddgggtaave qlrpvfaald avtvsgglaf rhgrpppvaa aehlldrllw
      181 waralraard tlpmnwryhh vprqp
//
LOCUS       WP_357584604             205 aa            linear   BCT 28-DEC-2024
DEFINITION  dTDP-4-dehydrorhamnose 3,5-epimerase family protein [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357584604
VERSION     WP_357584604.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 205)
  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..205
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..205
                     /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=21978
     Region          1..177
                     /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 mklrplsieg aweitpqqhg dprglflewy rfdrlaeavg hplrlaqgnl svsardvvrg
       61 ihfadvppgq akyvtcvrga vldvvvdlrv gsptfgrweg vrlddvdrra vylaeglghg
      121 fcaltddatl tylcsttynp saehavhpld eelgidwpat vpqlsardaa aptlaqaraa
      181 gllpgydtcq ryvatlaata gstdg
//
LOCUS       WP_357584617             434 aa            linear   BCT 28-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357584617
VERSION     WP_357584617.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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..434
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..434
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44470
     Region          12..381
                     /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 mtrrllrlvp pgtlpvgigl avvglasyvh lalaghnlaa adysslsvlw svvftlgigv
       61 ffpveqevar lvaarrtrrl ppgpvlarga aiaavvlgll llltigtadi lterlfdgdp
      121 amvpalggal aalavahttr gvlsglrrfg wygtqlgldg glriglvaal avtgvdspva
      181 yalvlvvapl tavaltaapv vrtisrgptv pwrpllrglt lltvssllaq vvvnvgvinv
      241 rlldptdvat agallsalvl vriplfvfgs mqaallpgls taaatgdepa frallhrsla
      301 vvtalgalgg ilaalfgpwl vralfdtpdv lghgdfawls vatlaylwam vlgqallard
      361 rhhaqalawt vgvaalvvat lpplpvalrv elgytvgsvv aaavmvtllr rhrrpppapt
      421 vaapipatts ggtp
//
LOCUS       WP_357584648             412 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049891].
ACCESSION   WP_357584648
VERSION     WP_357584648.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..412
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44552
     Region          2..411
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mdeptvedll rrlapqvlga lvrryghfdt aedatqeali aaatgwprdg vpenprgwlt
       61 tvasrrltdl lraeqarrhr edvvgrrvla ewrlppaadr tadsddtlil lflcchpslp
      121 patqialtlr avgglstaev araflvpeqt mtrritrgkq rirdsglpfa mpapaevpar
      181 ltavlrvlyl ifnegyastf gpgllradlc aeairltrll srmlpdaaev lgllallllt
      241 darapartgp hgelvpmgeq drsrwradqi aegtslvvea lhrgkpgpyq vqaaiaalhd
      301 eapgpdetdw pqiaalyevl temdanplva lnhavavama dgpeaglalv dkvaadgrla
      361 rdprlpavra hllerrgdpa aaraeyrtaa aqatnlaqqr ylnaradrlt gg
//
LOCUS       WP_357584655             161 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357584655
VERSION     WP_357584655.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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 161)
  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 161)
  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..161
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..161
                     /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=17523
     Region          6..161
                     /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 mgqiglrewr eddapavlra frspdmatqa swpvvtlqda vgwiaswsgv ghafavtlgg
       61 rvvgnvavtg idrhdngwvs ywtvpevrgr gvasaatael arwafgergl frlelghrtd
      121 npascrvatk agfrpegver gklhydgiry dverharlat d
//
LOCUS       WP_357584793             466 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA cytosine methyltransferase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357584793
VERSION     WP_357584793.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 466)
  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 466)
  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..466
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..466
                     /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=51272
     Region          30..364
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtekhphgve sgpgdggqrp gsakaqqkdm levveicaga ggqslglera gfrhrlavel
       61 deqaaetlrh nlvkvfgyae nearetvrtg dvadipgvwk pdefegvdll aggvpcppfs
      121 iagkqlgatd erdlfawave lcgqikpkal llenvkglsg srftayrqrv ldrlkdhgyi
      181 aewkllqadd ygvsqlrprf vlvalrpeya eyfewpqpha erppmvgell kdlmaqgdwp
      241 eekleewvkg askiaptivg gskkhggadl gpsrakaawe amgvdakgva ngppgpgnpr
      301 vagaihpmlt vemvariqgw hgpdfeqwef lgkktsryrq ignafpppva kalgdairka
      361 lrqegeprtl vensdgvldp vykillgsar gltteqiver lakenvrmeq peverrlnhi
      421 ghdfelitte qangdlryrl gefkafvgqa nhqrhdlfsq nrrlis
//
LOCUS       WP_357584824             943 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Nonomuraea].
ACCESSION   WP_357584824
VERSION     WP_357584824.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..943
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..943
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=100582
     Region          <6..922
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mslnnavagf svpserrsaa dafptmplrg repelsllrd rlhdlrrghg gavliegapg
       61 tgksrllaev adlaaagslr vragagtqdg havpfaplld allsgpaplv arerllalse
      121 aeeqrfwllr elqheleraa saaplvilmd dlqwcdaatr salrtlptrl sgrpilwvla
      181 ireqhqagta rawpaerivl rplstkaval laqdilqava epvllelark adgrplllve
      241 llngmreega iliqdgmahl taaegipmrf rssirqrldr lsplardsvr faamlgrdad
      301 vdvlaellrc spvdlmgplq ealradlltd ldgrlalrnd lvreavrnsv paafkdlirr
      361 qavdvrlrrg aaamevaadl aevaqpgdhe avsllrraat dlaptspaaa aalsgralel
      421 apadhpdrpa liaetavllw ltghddeara taagalagll epegeaqvrl slarlssqss
      481 faeavrqcrv alalpglset tlahlltlqa lslvvagdve etgraaeaal laggycgnra
      541 ieatamavea tlsfhrtdwr hafdrqdeav rlatdagilh spwipgpswq sflwssagep
      601 lrgleeidla lgrarthgqv aaarmwslyr vrmlldagrl agaraeaeaa laeegatgnt
      661 advtaryalg rsalyagdrl giaqlasdgl rmtgdeapfv tragswmlal vadcdddpar
      721 alahaaaava lgpdgatgat pldaaddvvf vrmalragdr eaavrmvcet earagrnpgf
      781 pfltavaeha rglldddaal lsraaerfag fprpivrasa ledagralaa tdrraavarl
      841 ktaselyeqa galrdaarvr rrlreagirr rgrksgaahg wdgltaaelq vvrhvaqgat
      901 nrqvaerlfl sphtvnthlr haytkldvns rveltrlvve hdg
//
LOCUS       WP_357584828             272 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357584828
VERSION     WP_357584828.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 272)
  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..272
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..272
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28374
     Region          37..266
                     /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 mrhrpsiwqn saaalglaav tlstapamag taegtrptvv lvhgafadas swdrvtaqlq
       61 rrgypvvaap nplrtlsgda ayiasilkgi pgkvilvghs yggvvitnaa rdadnvkalv
      121 yvaaflpdkg estetvldpe kfpgsllgpa tldqrpytda agegvdlyik pasfpavfaa
      181 dlpadtarrm avaqrpfgvg aytgvsgapa wkkipswviv sgedkaiapa gqrwmaarak
      241 artievkssh amslshpsvi tdvivdadrr tr
//
LOCUS       WP_357584845             210 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357584845
VERSION     WP_357584845.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 210)
  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..210
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..210
                     /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=22434
     Region          10..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtppkpgvra aktaqtrarm laaarelfve rgytatsmqa iatqggvavq tlyftfetkr
       61 ailkelldve vagddapvat ldrpwaaqal aapppellhr lveatadiha rvapllevar
      121 saaatdpeia elwrtnitqr htvlavftga laaknalrad lnalraadma lavlapetyh
      181 lltghrgwns rawadwaaqt listllasse
//
LOCUS       WP_357584922             201 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357584922
VERSION     WP_357584922.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 201)
  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..201
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..201
                     /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=21425
     Region          22..>121
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkpridlltg rpagggarpr eradaarnra kvlaaaaelf asrdprgvtm ediakaagvg
       61 rgtlyrrypd tvsiaqalld ehefalqerl lrgdpplgpg appgdrlaaf yagmvdllea
      121 hislvlgaeq gelrfttgay gfwrahvrtl liqaavpepe alvdallapl gpdvfaeqrr
      181 rgltpeqita alarlahgvt r
//
LOCUS       WP_357584926             404 aa            linear   BCT 28-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357584926
VERSION     WP_357584926.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 404)
  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 404)
  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 404)
  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..404
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..404
                     /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=41073
     Region          15..385
                     /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(25..26,29..30,33,65,114..115,117..119,122,141,
                     144..145,148,217,220..221,224..226,229,256,260,308..309,
                     313,317,334,337..338,341..342,345)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 mskraggrsg qallvwgllv vaanlrpslt gvgplldrvq adlglapava gllttlplla
       61 faavspvvpr maarwgperl lwgallvmtf giavrwipsa galfagtvli gagiavgnvi
      121 lpslikrdfp drvglltsay atvmggvaav asgvavpiae aapggwytal gcwivpalva
      181 valwfpqvra arpadgtvrr rrlpwrspla wavtafmglq slgfyvavtw lpqvfqdsgv
      241 gaatagwllf lyqavalvts lavpialrwa rdqravaavs saalltgyag llvapgwvla
      301 wtvvlglagg aclvlalafl slrahdatga gelsamaqsi gylvaaagpv vfgllhtvss
      361 gweaplalmc vaatgqvivs iaagrgtvpg agadrdplga gepr
//
LOCUS       WP_357584930             308 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357584930
VERSION     WP_357584930.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 308)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..308
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..308
                     /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=33851
     Region          9..307
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrashdvrar ragganserr rrqtliawlf tapfvvvfav fmilpiassi gfsftdmtaq
       61 diqspfnvdf vgfeqyanvl sdpefqnaaw vtalfvivgi pvtvalglgl alalnsgirr
      121 lrpiyrvafy apvvtsvvav sviwryilar dgllnmvlal vgiegpdwln sttwalpsli
      181 lmavwrntgt lmiiflaglq aiptdvreaa emdgagrwrr lrsvtlpllr ptmllgsvli
      241 svgylqffee afvmtqggpl sstlsmtyyt fntfgfgdfa kasaasyimf vviaavsilq
      301 frllrrst
//
LOCUS       WP_357585029             518 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357585029
VERSION     WP_357585029.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 518)
  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   2  (residues 1 to 518)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..518
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55151
     Region          18..515
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mtvkrtlgaa vlslafvmag aapaeaaprd vvrtdtglvr getardhrtf rgipyaappv
       61 gdlrwrspqp apawrgvrda trpgdrcaqs tdlwglpasd sedclyldvt aprpatarsp
      121 rpvmvwlhgg sltkgagsdy datrlatrgd vvvvtvnyrl gvfgffghpg lagggaygle
      181 dqqaalrwvq rnaaafggdp rnvtlfgesa gahsvcahla sptaaglfhr aitqstfcsq
      241 taftgsrlrp vmdlpmwvpk taheahgatt atalgctdpk tavaclrrkp vsqllaqqpl
      301 plpgygnavl padpatvfaq grfhrvpilt gitrdegtlf tslifpglte qeyqqglrdl
      361 fgddaaaiaa eypsrgrpaq avaaimsdld wawagrasdr llsertpvys yafadrtapp
      421 ifplpggvep lashgselsf lfpgapltre qrelgdlmia ywsrfaatgd pnapglprwk
      481 pvraghvhrl apgpggvggy dqdalhnlaf wdrlahrp
//
LOCUS       WP_357585052             184 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357585052
VERSION     WP_357585052.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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 184)
  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 184)
  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..184
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..184
                     /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=21146
     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 mlkprypitt prltlrpftt ddldalhaye srpdvaryly wtprdrntvr ehldkkitrt
       61 qlhdegdald vaitrndtga ligntlliwt srthrqgeig yilhpdhhgh ayaaeaarem
      121 lrlgfdhlgl hrivgrldar ntasarvlqk lgmrqeahli dnehvkgewv semiyamlet
      181 ewtp
//
LOCUS       WP_357585066             292 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: M23 family metallopeptidase [unclassified
            Nonomuraea].
ACCESSION   WP_357585066
VERSION     WP_357585066.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 292)
  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..292
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..292
                     /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=30687
     Region          25..230
                     /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 mrstrwvaat aallavaacs patgvagvsa rtpaspgtsg apsspgtggs aavtatippp
       61 tperqasvra pegddpvrvp ppklskytyt fpvrgcrvsy qrrllvlpkt tiwaaegcaf
      121 vapvggvvde vntrnrwlps tdagahregr fvtiigddgv rylgghldsv adgirpgvrv
      181 sggqvlgtvg nsgnarttgp nlyfaiswkt gpslwwvrrg mvepwdylda wlsgnrtlsp
      241 rqetlamrar lgesprctvl ctskkapktt kspkpdddpf tlnptgnpat mq
//
LOCUS       WP_357585111             143 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357585111
VERSION     WP_357585111.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 143)
  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 143)
  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..143
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..143
                     /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=15160
     Region          8..139
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtatglgssl ayllssaers vnrglaaala gedvtveqwr ilraladgrg hsmgelaaav
       61 lmphptltka vdrlieralv yrgpsagdrr rvavfvagrg adllarvdga vaehhrliad
      121 alghdrmerl msdleslvae ldr
//
LOCUS       WP_357585165             162 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357585165
VERSION     WP_357585165.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 162)
  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 162)
  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..162
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..162
                     /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=17838
     Region          15..156
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 medsvdrhla rwrgkapyde rvegivtrmq vlvkhlahsk etalaqvgmq dfeyetlhrl
       61 vaaggtatps qlaaelllsp agmtgrldtl eksglvrrvr gtsdrrrvdv elttrghdlw
      121 meamllraev etaliaaltp aerqtldgll ktlltsvesr ps
//
LOCUS       WP_357585195             202 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357585195
VERSION     WP_357585195.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 202)
  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 202)
  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..202
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..202
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20913
     Region          <55..>138
                     /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 madqlaqvge lpvivlmavl gvvmlfdavp lfgvlvpgdv avlaavavgs pttglatfva
       61 vvtgcltgws lsflvgrrwg drlrhsrfgg wvgetrwtaa eailrrdggr lvliapflpv
      121 fnallplaag glhmsyrrfl gfaalgaagw aglylavgta srtlaglfpa gaspllvtml
      181 gglllaalvl lgtrrrlrav tr
//
LOCUS       WP_357585219             284 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585219
VERSION     WP_357585219.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..284
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31505
     Region          13..76
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(19,23,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..280
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mplptspvir rarlgaelrq lrrrealtle qvcerlgwas tsklsrielg qsrpdladvl
       61 dlldvyevps vqrdalivia rdaatsrgww kslgemgerq rtyaeleaga agiveyqpai
      121 vpgllqipay arlrivagql idptvdvead lraraarqav lrrveppryt alitelacep
      181 gddpaevwre qlhhlldlaa lphvtirllr tgagrgplpl tpfssysfpd padprtvmle
      241 alttdvrltt atdvdryerm tdclletalp eeetvrvlar rldg
//
LOCUS       WP_357585269             429 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Nonomuraea].
ACCESSION   WP_357585269
VERSION     WP_357585269.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=45532
     Region          12..342
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mnlssrktmw kvaalsvavl tavtacgsgd sgeggggegg kttitfaywg sdarqklteq
       61 viakfeeknp tidvegdfsn wdsyyeklat kvaandapdv lsieirglse yagrgaladl
      121 agkvptadld qqvlasgqid gkqyaiptgv nafsmvanta alekakkelp kdtdwtwdqw
      181 malaqeisga ggvtgaeynf npaflqiyaa qrgekfydgn kigvspdtlk swwaihqkli
      241 etkgspdaak saeigatgpe qsllgtnaga mgmwwsnqln altkssgsem tllrmpkleg
      301 attggmflqp amfyaasaks ehsaegakli dflvndpdaa aillsdrglp tntkvldavk
      361 tklpetdqkt lafidevrse lspiqvppkg alemedilkr nseevmfgra tpdaaaqkfl
      421 teanaaiag
//
LOCUS       WP_357585273             264 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357585273
VERSION     WP_357585273.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  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 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   3  (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   4  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..264
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..264
                     /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=28269
     Region          2..219
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilmtgaag kvgtllrprl aregrtlrls dllplepgpg eeaavadlad esamakamag
       61 vdavlhlggq srehpwadiv ranidgtqvl meaarregvr qlvlmgshha agfqtrppsg
      121 edlpdyafpr pdtfygvskv vmeglgslyh drfgmnvtvi rlgtcnegpa dtrglatwis
      181 pddlarlvea alvapgfhvv wgvsdnarrw wslreaeaig yvsrddsevf agplvaelge
      241 pdlsdpvhdr aggvftlkel ggsw
//
LOCUS       WP_357585306             957 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585306
VERSION     WP_357585306.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 957)
  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 957)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 957)
  AUTHORS   Rosinski,J.A. 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 957)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..957
                     /product="helix-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=102665
     Region          <7..908
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <887..956
                     /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 masdvdttpl vgrdalvatv rsallddvtp ghtaavfltg esgvgktrll revgdrlgda
       61 galvltgscl digdasplhp lrqalrrlda dlappaaasv rallgvfaed ragpdgagal
      121 lervsrglnv iaggrplvlv lddlqwvdrt trqlllylla glgdlqlsvl aavrseslqg
      181 ahplrrvlte lrrlrsvrvl dlapldragt eelaaavmrr pltpeaaerl wqrsggnpfv
      241 veelsrelrd grdglsdtlr evflarvdal prpahravha vaagvepveh wllarvvgip
      301 ehelldavra avshrllvgs ddgyrlrhrl vaevledell paeraalhrr yaealtsapa
      361 elhqarlahh wrlagepera lpaavaaaee aerlygyaea hrhwsvavqs aeglpgvdra
      421 tllgraaeaa hhcgeyaral alleelasad tdlpacelhi rrarylaaag rsalaeveye
      481 qalavadctp gqrataaarl aelllqlgry aeagqrarea lalaeqvdga ttevvlasaa
      541 lgfseayrqd pdaglavlrr alataeragr pedvalaylh laelltgpln ileegvvvar
      601 rgaervaelg lgrsyetrll aiatnglfrv gqwaeaekvv asalrhrpsg adavelllar
      661 crlsvgygdv eaadrdldav atilagggar hviplltlra glamwqgrhd varhavqrgl
      721 tetrsddlvi lavlvwhglr aeaeahasrt vavddnavrr lrgiadrvaa rseraarpvr
      781 yvidgylalc aaevsrldga dpelwaraaa ewdhrnhpyp aaysrlrqae allasrrkaa
      841 tagkllrhay qmaqslgavp ltdeirtlag rarvaleerg avgaatpdes ggeelaalta
      901 rerevlaava egltnkeigq rlfisertig vhvshifdkl qvrtrvqasa iflrsra
//
LOCUS       WP_357585337             263 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357585337
VERSION     WP_357585337.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 263)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..263
                     /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=29659
     Region          38..197
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mkphaelkdf wesrlqsdwt esgvgykalg rafniwmyrv raegfrreaa aipldltkar
       61 vldvgsgtgf yirqwralgv etitgsdltq aavdrlrerf ssasflrldi adpagalepg
      121 sydvvsamdm lfhitdddry kaalrsigea vrpggvfvls enflhrpeqr sdyqvnhtlp
      181 witaaldeag fdvirrvpml vlmnaqvdah plwrklwggl lravtltevt gwlagallhp
      241 lerrlvrvlr espttelmlc rrr
//
LOCUS       WP_357585346             206 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585346
VERSION     WP_357585346.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 206)
  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..206
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..206
                     /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=22971
     Region          5..203
                     /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 metfedvrrl rlvggnlald fvntrtgppv gppdddvltg ypelvawagy agvltdaema
       61 rslrlqrddp datqaafvrs qrtrdrldev fralatgrdp srsalarlrd deaealghar
      121 ldragsfvwt wrddhtadrp lrpvvhaavq llttgtldri kgcggcrfvf idesknrsrr
      181 wcsmddcgta ekarryvaar rtrasr
//
LOCUS       WP_357585415             407 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357585415
VERSION     WP_357585415.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=43120
     Region          140..399
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msamifgrrl pavafdvala glvalasvag gpvqpggwws taigigmala llfrrvrpva
       61 vtvvvavlaf tqvalgwapm lydvavlial ygvvkyaerl rdgaiagava vlgavfaavr
      121 dplpaawyya aiyytlltga vwlvalnvrt rrqyvlslee raatlerere aearaavaee
      181 rtriarelhd vvahsmavmi lqadgarymi dqnpetsrda lkivadtgrq aledmrrlvg
      241 vlrepdvaep epappvrpvp elaepahrrp svaelpalld rfreaglrvr ytvtggpvtl
      301 ppaleltvhr laqealtnvl khagvgasve itldhaadgv alvvvddgrg hgpltptppg
      361 ghglvgmrer vsvydgslta garlaggwqv rawlpvpsap gaeviaa
//
LOCUS       WP_357585425             453 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357585425
VERSION     WP_357585425.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 453)
  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..453
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..453
                     /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=46478
     Region          11..263
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <228..446
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mlssevvlsg ryrldervat ggmgdvwrat dlilgrqvav kvllpslvsd pdfiarfrae
       61 arimaalrhp givqvydcge ddlpgggrad ylvmefvtgq plskrieaeg rldvgvamsv
      121 vaqaaqalha ahlggivhrd vkpsnllmqe dgtvvlvdfg varstnvtsi tstnavpgta
      181 lymapeqaag rpvsgatdly algavayccl tgsppftgdn plqvavrhld dpppelphdi
      241 peavrvlvdr alakdpadrf ssgaamaeaa raavsdgtlp ttvvpmargl rdagpdtrsg
      301 lpvidapppg rrrrgklvga ltavlvglta lgaalgatqd antpavklpt taptvestde
      361 eeappsqqes apaqvplrpa gsttrptesp spepsspqps essepaspep ttpspdpept
      421 gtsssptppv tptssapstp pvveppgtgd geg
//
LOCUS       WP_357585463             388 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585463
VERSION     WP_357585463.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..388
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40982
     Region          6..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 mtadlptgpl tgvrvvelag igpgpfaamm ladlgadvir vdrvtevdat afgtphpdll
       61 nrgrrsigvd lksadgrevv lalvshsdvl iegfrpgvte rlgvgpadch avnpglvygr
      121 mtgwgqdgpn aphaghdiny laltgalhgi grageppvpp mnllgdfggg gmmlalgvvs
      181 alyavrggat gqvvdaaivd gvavlstqih alrqlgmwqe prgvnlldgg apfydtyeca
      241 dgrylavgal eprfydelvr ltgfplapde pvdrtdpanw ptlraawarl frtrtrdewa
      301 tlltasdaca apvldwqeap ehphlaaret fvlrdgvvqp apsprfsatp tairrpppwp
      361 gehtdeilae agfdrdriar lraagaig
//
LOCUS       WP_357585478             267 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357585478
VERSION     WP_357585478.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 267)
  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..267
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..267
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28747
     Region          8..250
                     /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 mdvrsrnnvr iigpqdgrvv mlahgfgcdq nlwrlvapvl aqefrvvlfd yvgsgrsdls
       61 awseeryatl hgyaadvldi crdldlrdlv fvghsvsamv gvmsaarepg rfaglvllvp
      121 spryvddegy rggfsaedid ellasleany lgwsatmapl imgnpdrpel geeltnsfcr
      181 tdpniarafa ratflsdsra dlagvqvptl ildcaedmia prevgayvhq aitgsrlvtl
      241 aatghcpqls apdataaaia aftresm
//
LOCUS       WP_357585488            1348 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357585488
VERSION     WP_357585488.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1348)
  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 1348)
  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 17582184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1348
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..1348
                     /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=141828
     Region          148..620
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
     Region          832..956
                     /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            911..913
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:238300"
ORIGIN      
        1 malprpplar rtavlltavt tlagvltagp atatppdtpa asptgspase aqpakdvals
       61 gvrarklvvt litgdkvqlt rspagryrve papgtrqdgr rinlftqftp dgvfvlpdda
      121 vaavqaglvd rrlfdvkyla engyaddvak rlpvivqypg tqaeaevkrs aaavpaaept
      181 rtlesihasa ldvakaeagt fwqavragqd sgqglakapa tlgggiaklw ldakvkadld
      241 vsvpmigahq awergqdgtg vkiavldtga dtghpdlagk iadsrsfvpg qavqdghghg
      301 thvastiagt gaasggkhkg vapgaqlvvg kvlddsgsgq eswiiegmew aarsgakavs
      361 mslggapsdg tdplsqavnd ltaetgalfv iaagnlyeae tistpgaada altvgavdkq
      421 dqlagfssrg prpggglkpd iaapgvdiva araagtamgt pvdehytgss gtsmatphva
      481 gavaimaqrh pdwtarqlka almstakddg ftvyeqgagr vdldratrqq vfadsggvdf
      541 glletgsapk tgqisyrnlg dapvtltlka amsgdaepvl adttltvpag gtagttvtld
      601 paelpigtys gavtaeadgv rlttplgavr dvpkydlair tldrdgkprt ptamsvvdvd
      661 gakgelgphr iddvglvvtr vpagtvsllq vldwvdgddr anrawlfepe ltitgdtevt
      721 ldarkateis fsapktaqpl nntydlffqr tlpngevfgg sllssrplgg wekvwalptk
      781 kvtkggfrft gqwelgvpev tmtmrasgra akrttlhpvs rvhmidagev hggyvpfdgv
      841 kdlrvvdagk grpedlagkd lrgalvlida epaegifgta cglqiervgp irdagaagvl
      901 afnerasicp iplpitqkpf sgpfkpvnip vayvsnaegq kireaagrge vtvraegtpn
      961 tpysyvfkpy adgripasmr ykvterqlhr vdldvhagpy tkymnwrstw rtdditytgt
     1021 gtnmlhwssp mperrpqwvw pldptivsqa gisallpsep gaeveetryr tdvfdrpgst
     1081 rqqwfatpst pgaatasgkl yalgggpddv pleklviglp caicvhdgnl wvtpsmvngv
     1141 gerrddgvaf gdlaprydlh lyrdgkeipn apvagfdklp ryplpegqgg yrltaknelq
     1201 diewtftapp ardqvlpgsn cyawfvdgpl eqcrttpavy vsydlgdsls adntvaagrr
     1261 htfeveayhg psaakmpaia gvrlwtstdd gatwqpadlk rgrdgvhtar vkypahhatk
     1321 gavslkaeaw daagnrvkqt tlraftlr
//
LOCUS       WP_357585581             570 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357585581
VERSION     WP_357585581.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 570)
  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 570)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 570)
  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..570
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..570
                     /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=59303
     Region          373..570
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrtnlaavla aataavtlva atvatggpla sqaafvavgl ilpalgllla lrrpdvpygr
       61 lllaaavcfg vglsgvalad vapglaraal aamavfygls wvyvpllfpe grlpsrrwrp
      121 vawlagvaia lhaagnltvs flpgrpidvh gpvqwagvfa saagqftvwv lghvvfaglv
      181 lrwwrsrppe raqygwmaag aaanqigivl gylflsggqa pavglvgmla vlgalpgaiv
      241 vavarhhlld iriglrgsrl llvfdvrptv gevlsslapd ledsrepveq lgrlaeavrt
      301 gletrwaavt ladgrrvvsg aedgpaaltl pvrggqgrle cgprvsgrlt redrrfleal
      361 avpaglaiqs aglatrlvna qeaerrrier nihdgvqqql valiagiela ratgggaatl
      421 aglreqarqt ladlrelaag ihpsalsqgg lveaveerca rlpvpvhvha grdlraerfp
      481 devegamyft vseavanalk haaaarievr lsrddgrlgv tvgddgagfe arpgvlgtlt
      541 drltalgggl rvdsergkgt rvhawvpvdg
//
LOCUS       WP_357585602             173 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease [Micromonospora sp. NPDC049891].
ACCESSION   WP_357585602
VERSION     WP_357585602.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 173)
  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..173
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..173
                     /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=19211
     Region          78..136
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mwsplcylds pdrrpvssyq stpaarrdiy rrwisagyva dlgeavrrde aqrqrwisyh
       61 rahprrdvqd aallrasrrq rrinaartal laagaachyc ggghrlgvdh vrprsqggtd
      121 apwnlvlacv rcnsakggkt veqwraqraa aglpwppvwp arpqapdtrq aaa
//
LOCUS       WP_357585616             279 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357585616
VERSION     WP_357585616.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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 279)
  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..279
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..279
                     /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=29794
     Region          4..272
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mfvmriaaci gsallvliag tpayaadtpt vkakvgyvvd sagtihfgkr etarvpvasl
       61 vkvmtayvvl rearlgdtit vtaadvrhav rngatsaalk kderltvrdl lyglmlpsga
      121 daahalarry gpgtnafvrk mnataralgl ddtrytnadg lpkpslggys tavdqaelar
      181 ralenpvfrt ivgrevhrvp ktsahrahtw rntnklltra dgvtgvktgy traagfcllf
      241 agerggrqvi gvllndqder rfstaerlld hagsqievs
//
LOCUS       WP_357585629             364 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357585629
VERSION     WP_357585629.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=38388
     Region          1..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 mrvvvigagv aglalaralm ggghevevfe eapeprtagg svtlwpgsta ilrelgidaa
       61 aagrrletle swsargrmls aadltdaera yghptvhvar gelvallaeg vpvtygaaae
      121 dvdpggarar laggrtvrgd vlvgadgrrs avrhamlggd parlsgwatw qgftteptpl
      181 isagravlis gegglcglip agggrllwwf dvrtapgrpl wgddpdpvgk lrrlfgdlpd
      241 pvprilatmt apeffphhtw kipdvwghgp ttlagdsaht mpptlaqgan qaledawlla
      301 rsvtgdlray erararmvrr savlagieit nrheplarlv pkrvatglct rwlrwasgyl
      361 ltas
//
LOCUS       WP_357585653             211 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585653
VERSION     WP_357585653.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 211)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..211
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..211
                     /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=22143
     Region          2..200
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkladheer ralivaallr iaasrglhaa smrtvaaeag vsvstvqyyf gtkerllfag
       61 lqhqaeavgr rieaglaanp ggsvrdslya wlvqlipvde qqragytvfa ayhalaltdp
      121 alaeqsytrg saelevvlra lladaqqage lspgrdvgae agnllalatg ladsvmadmr
      181 tpeaaialld yqldqlfvaa fstspaaagr r
//
LOCUS       WP_357585697             129 aa            linear   BCT 28-DEC-2024
DEFINITION  YidH family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357585697
VERSION     WP_357585697.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..129
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..129
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13780
     Region          9..126
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 mwqmirnwfd pqelrsvgdt pdyrfslane rtflawlrtg laliagglaa aqflptlslv
       61 hlreviavvl lllggavair avdhwarter airlgeelpa srfpavlali vglgalslvv
      121 avlagaisg
//
LOCUS       WP_357585675             337 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585675
VERSION     WP_357585675.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,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 337)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..337
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35742
     Region          6..228
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtsgvieieg lrktfhslrr grrtavdgfd llveagqvhg flgpngsgkt ttlrallglv
       61 raddgrmrvl ganapdqlpq vagrvgaive spqfygnftg yrtlrllala ggvpvarvde
      121 vleqvgladr gdervkgysl gmkqrlavas allkrpelli ldepangldp agiremrdlv
      181 rslaangvtv lisshilaei qlicdhvtii srgrrvtagp vaevlagfdh nehlvrvddl
      241 araeelllaa gltvtghadh lvvsgvpdpt tvsrtlgeqg vwvreltplr pdlesvflel
      301 tgspahpgvp rqvdgstppd qpatgqeidl gmrgvda
//
LOCUS       WP_357585718             258 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357585718
VERSION     WP_357585718.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 258)
  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..258
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..258
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27812
     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 mselfwtesg tgrplvllhg gflhhrmwdd qipafaerfc viapdarghg rspnatepyr
       61 ltddlaallr hlgtgpailv gvsmgaatav dtalehpdlv savvvtgagt sepyftdpwt
      121 trawagwqaa maagdldasv eghllfaagp hraldtldpd vvtrlrrmar etmskhapge
      181 pnhlvpvhdt werlpsvrvp vlaingslds pdhlgmadrl tttvphgsth tidgtahypn
      241 leqpdaynkt lesflhtl
//
LOCUS       WP_357585747             330 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585747
VERSION     WP_357585747.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 330)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..330
                     /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=36990
     Region          21..324
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msttraapdp ttrrprpapg rsatwrdrlh rfdvryvpyl miapffllff vfglfpmvfn
       61 gvvalrhwrl ddpeltgwag fenfsrlftd gdfgnalynt fgifllstvp qlllaliias
      121 mlnrrlraqt wwrvgallpy itpitastlv fnvffsrdlg manwalglig igtenpidwr
      181 adklhswiai atmvnwkwig ynallylaam qsiprdvyea saldgagpwr qlwritvpmi
      241 rpvviftvvl stigglqlft epmlfdlnaq aatggsggew qtvaqliykv gwkdlnlgya
      301 aamswalfli ilvvaalntl ltnrisggrk
//
LOCUS       WP_357585793             803 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357585793
VERSION     WP_357585793.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 803)
  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 803)
  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 803)
  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 803)
  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..803
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..803
                     /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=84795
     Region          67..737
                     /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 mhtppamigv avlsalialt agvllaaavr craaphrpay avlavggafa vvtmlvgvtv
       61 avttsehwah eqqqrvswat lvalgtatgg llfcfgllrl pgvtgsvpsa arlaldsviv
      121 gtalwfvgwv lfseptrllg datptacpsi llasvsaals aglsaimvlr apaprrclav
      181 lgtgitaasv gglgvaaglc qagpglaltg avvlavglli aavaayridp pgqlaidvir
      241 rdgeyafvpm valaasamyh llqdgrfdgl aiaagsvegf alvarqyltl hdvrayarrl
      301 adreahfrql ahtdaltgla nrrgllqalh rcaeaqvpcv llgldldgfk nvndmrghdv
      361 gdavlaevgr rlrgnlrpgd laarlggdef avlmrggpae agvvaerllr vlggayeqpe
      421 apvflsvsig lagwaeepdv elllrhadla lryakqrgkn rierydgayd rllrrrttle
      481 helrgaierd elrlvfqpva slpsvrpvga eallrwrhpe lgnvrpdefi plaeesgmia
      541 klgawvlhqa cyqlsrwlae ghdvwvsvnv sprelhapey vvqvaealra hhvppqrlvl
      601 evtehavatd ldelirrlta lrltgvrial ddfgagyssl nqlrrlpidi lkidhglvae
      661 hepvqpegrd gpafapmvdi vmrlghqfgl eviaegvttp telaavvaag crfgqgalfg
      721 wgvpaehlea mldaatspga rparpaaggh piprpvgppl qrrgesvpgq vipgptgapg
      781 gdaptsvnqn vgsvdsshem rqs
//
LOCUS       WP_357585798             279 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357585798
VERSION     WP_357585798.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 279)
  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..279
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..279
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29433
     Region          3..275
                     /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 mrtpllfvhg fwhgtwcwse vlarvaetgr palavdlpgh glrarrprsv tgrpfdpahl
       61 atepspvagv tldeagehlv aqlkrlgrgg pvtvvahsmg gtvltraaeq apelvahavy
      121 laafmpasev pafdyalmpe negeligpsv radpaavgal rldvassdda yrqqlretfy
      181 gdidpeaada aialmtpdap agialgtttl trqgwgsvpr tyvgcardmt irpplqhkfv
      241 aeadtafpdn ptatvwldas hspflsqpgr vaeivggig
//
LOCUS       WP_357585860             999 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-mannosidase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357585860
VERSION     WP_357585860.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..999
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=108730
     Region          248..998
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhddralvea rlkrvlderi rpavypesvp ldvavwhapg epvsvaegla avpapiaagd
       61 awgapwgtsw ftvtgtvpaa wrgriveavl dlgfdenmpg fqceglvhlp dgspvkglnp
      121 rnqwvrvaap arggesvrlh veaasnpvil ghplfrptal gdrdtagtap lyrlgrmdla
      181 vfdrtvwdlv ldlevlgelm aelpvdgarr wdvlravdra ldridlqdvn ataaaarael
      241 agvlavpaap sahrisavgh ahidsawlwp lretvrkvar taanmtalla depgfvftms
      301 qaqqwawike hrpqvwaqvv kavaegrfvp aggmwvesdt nmpgseamar qfvhgkrffi
      361 defgidneea wlpdtfgfaa glpqiikaag arrlltqkis wsrvnrfphh tflwegidgt
      421 rifthfppvd tyncsmkgge lahaarnfre kgaarhslap tgwgdggggt tremvgkaar
      481 lrdlegsptv twespaaffa raeadypnpp vwvgelylel hratltsqag tkqgnrlcea
      541 llreaelwaa taavrtgapy pyeqldrvwk tvllhqfhdi lpgssiawvh reardtyarl
      601 areleeivla aqralagdap aggrlvfnaa pharrgvpag gaapaepapa atvrprdggg
      661 yvlddglvra eidgrglivs aydhrarres lppgdaaall qlhqdlpnrw dawdvdefyr
      721 ntvtdltcvd dltadgravr vtrsfgsssv tqtytlaagr ievrtevdwh etekflklaf
      781 pldvradrya aetqyghvqr pthtntswea arfeacnhrf vhveetgwga avvtastygh
      841 dvtravrddg gttttvrvsl lraprfpdpe tdqgahafvh alvpgaaigd avregyfltl
      901 perelpgdvp vaplvtvgdd avvvtavkla ddgsgdvvvr fhesrggraa ttlragfpvg
      961 tvtatdller plrelphedg avaltlrpfe lvtlrltrr
//
LOCUS       WP_357585878             154 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357585878
VERSION     WP_357585878.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=17140
     Region          7..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maqlgltere lrawrtsfrm vellrarieq qlqavgglsn adytvlalls eapgrrmrsy
       61 elarvagwek srmhhqltrm sgrglvvrep cgsrgieavl tedglaalrk aapghaeevr
      121 rlfvdrltpe eldrfaalaa kvldsleadr pprp
//
LOCUS       WP_357585923             200 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sp. NPDC049891].
ACCESSION   WP_357585923
VERSION     WP_357585923.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 200)
  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..200
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..200
                     /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=21939
     Region          10..188
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtgirqqpgt pedelahrfr agdeqalrea ydrygravlh latstlvnrs daedatqatf
       61 vaawlgretf dptkgslvgw llgigrrkvi drlrsaaren rvvetvrqlp dpvptgndpd
      121 tvvdrlvvad elarlpdeqr rmlelaffdd lthqqiatvt gvplgtvksh irrgmaslkr
      181 rwevdgaapg arpagisgar
//
LOCUS       WP_357585884             188 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357585884
VERSION     WP_357585884.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 188)
  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..188
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..188
                     /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=20305
     Region          9..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mseetpplrr daehnrrrtl aaarevfaar glqatlndva hhaglgvgtv yrrfpnkevl
       61 aeavyagkld elratardal tgqdagralt aflehalela atdrglrelm rqgagdseqi
      121 araregiaes cglliarare qgtiradltv ddiapivtmi dsvmdlpstg gtqpwrryla
      181 lvldglrp
//
LOCUS       WP_357585927             802 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585927
VERSION     WP_357585927.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 802)
  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 802)
  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 802)
  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 802)
  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..802
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..802
                     /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=89801
     Region          5..>627
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mravpgqqvp peidgatvpa tlpgcvhtdl laaglipdpy lddnetalaw igrtdwvyet
       61 tfdrpagehs rldlvcagld tvatitlngv evgrtenmhr shrfdvtsll rvednnlavr
      121 fdsayryaea qrdrlgdrpn aypepfqfir kmacnfgwdw gptlvtagiw qeialhgwsv
      181 arlaavrplv tvdgdtgrve vhveveraad rpltvraqva gqraevtvpp gqrstvlalt
      241 vhrpelwwpr gygaphrhel tvtlhdsdgs pldewhrrig frsvrldttp dehgapfaly
      301 vnevpvfvrg vnwipddvfp tritrqrlah rfdqaeaanv nllriwgggr yesedfydla
      361 dergllvqqd flfacaaype eepfatevaa eaaeqvtrla phpslvlwtg nneniwgwhd
      421 wdwqaplagr swgrgyyldl lpriiatldp trpywpgspw sgseeihpnh paygtthiwd
      481 vwntddyvky reylprfvae fgyqgppaya tlrralsddp lahdspgmah hqkaadgdrk
      541 lrrgldahlp eprdfddwhw ltqlnqarai algvehfrsh rgrcmgtivw qlndcwpvts
      601 waavdgdgrr kplwyalrha yadrlltvqp rgsglalvav ndggqpwras atatrltlag
      661 epkakttlel dvpayssvtv alpdelvrpd dapdellvad tgdptgraww ffaedrdvrw
      721 paaafdatve paddcqrvrv tartilrdvt lypdrldpaa evdtalvtll pgesasftvr
      781 satpldptal ttrpvlrcvn dl
//
LOCUS       WP_357585938             358 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357585938
VERSION     WP_357585938.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..358
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37502
     Region          28..344
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mirallitll aatlqvptaa sasvpqpgst avpvlpaptg thpvgtvsrd lldasrpdpw
       61 vaaerrrlmv tvwypatras gararyvtpe esalllaaqg lppgdllsri rghartgapp
      121 vpgrrplvvl spgfglprss ltvlaedlas hgyavaavdh tyesaattfp ggrtttclac
      181 giedapglvp diraadvsfv ldrlirdrrl pvdprrigma ghsiggnsaa hamtadprid
      241 agavldgafv vppppgglar plllfgtpdv ptwaenwpll tgwkrwaeva gsehdsftdf
      301 pvlaeqlglp agslagvraa aitrayvrdf fdvhlrerpa tllngpsaay pevtfrtg
//
LOCUS       WP_357585944             323 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357585944
VERSION     WP_357585944.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 323)
  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..323
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..323
                     /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=34986
     Region          11..321
                     /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 miyaktpltr eireavalaw gvtgegerlh ggeesaayrl dghvirvgpa grsaaesewc
       61 haiarhaaag lpeavaplpt adgtatvvvv agrpiscwpy vegswadsdv paqreagarl
      121 larlhqslag frpgprpvpa fqesglygpp prpeaepkep glerqskdpe pknpglepps
      181 gdpdlqdpel drwlvafhaa hpvrhplhgd yytgntlvrd grivavydwd esfvgapele
      241 laaaalewgd dltgpskvfv aayheaggta ghldeeslaq lvrhklrreh ayfakavrsg
      301 vkhdeediay ararvelfrr lrp
//
LOCUS       WP_357585946             292 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357585946
VERSION     WP_357585946.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 292)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..292
                     /product="phosphotransferase 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=31215
     Region          <77..237
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtertarvlm qlppshrall srllpgvtpe dltvrqgqfh qvvigadrvv clprtdaaat
       61 rlphraailr llaaldlgfa tprpleegsa dglpylvlsr vpgapleaea ledpqvaeav
      121 atqyvtllta larngasdqv raalpaprdr wrrfaadvra elfglmsdgg rqraerelaa
      181 ldslphltda vvhgdlgaen vlwerkdglp vlsgvidwde vaigdpaedl aavaasygas
      241 flnrvltlda rpgstmtari aviratfalq qalsahrdgd eeeladglaa yr
//
LOCUS       WP_357585959             475 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585959
VERSION     WP_357585959.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=50508
     Region          27..475
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mtipypntqp vpaiaavtpp sgasrprvtf lgtgylgaty aicyaelgye vlgfdvdadk
       61 iaklnagevp ihepgldell rrnlaagrlr fstniaetaa fgdvhficvg tpqradgmga
      121 dlsyveasvt slaqhltrka livgkstvpv gtaewveqlv gkhtpadlgv evawspeflq
      181 egfavddvlr pnrivvgvks ewangmlyaa hkgvfdlaat edrevplvvt dfataelvkv
      241 aanaflatki sfinamaevc easggdvtql araigydpri gnrflqaglg fggaclpkdi
      301 rafqaraqel gagealrflh evdlinlrrr trvlqlaadl lgrrsgpagp dlsgtriavl
      361 gatfkpntdd vrdapalava allhkagadv hvydpegmdn arravpelsy eadmaeavtg
      421 adlvcvltew adfrnadpgl lgdlvagrrv vdarncldpa lwtqagweyr gmgrp
//
LOCUS       WP_357585974             330 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585974
VERSION     WP_357585974.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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 330)
  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 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   5  (residues 1 to 330)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..330
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..330
                     /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=35803
     Region          257..322
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlkihfsged ilrtrvapaa dpvwemvlsl hllpgrsrdp llagwrrevs rglrrevdad
       61 alrllstlsp prgyfpdflt pyesvhgfea gmealrrtpv tllqrdltll annnrnlpvg
      121 vaalargepe altrltetmg ryrelalgpy wtrvqgavea drarraraml dggieglltt
      181 lrpglrwesg vleipayprs relhlqgrgl llvpsffcan tpvalldpel ppvlvypvdk
      241 lggltgevpg agdtgresla allgrtraav laasddgctt gelarrlris aaaasqhttv
      301 lrnagllvsh rdrntvlhtl tslgravlnp
//
LOCUS       WP_357585992             458 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357585992
VERSION     WP_357585992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..458
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..458
                     /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=49242
     Region          27..411
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mryhdlsywl sttddpltpr palagdtdad vvivgagytg lwtayylara dptlrivile
       61 rqvagygasg rnggwcsall ptsltglarr hgrdaavamq ramhdtvrev grvvtaegid
      121 chwsyggtvv larsgpqldr araavaearq fgfgpddldl igsdeatarc aaegvraaty
      181 tphcaalhpa rlvrglarav erlgvslyer tpvtairpga avtptgtvta rvvvrategy
      241 tpslpghrra iapvyslmva taplpastwa riglaeretf sdhrhviiyg qrtadgrlaf
      301 ggrgapyhya srvhpdfdre prvfaalrrt lgelfptlgp dvpvthswgg plgvardwsa
      361 svgydraagl awaggyvgdg vgssnlagrt ladlirgert altrlpwvnh rsprwepepl
      421 rwlainaglr vmssadeaes rrnrpsrraa afsrllnp
//
LOCUS       WP_357586070             232 aa            linear   BCT 28-DEC-2024
DEFINITION  ComF family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586070
VERSION     WP_357586070.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 232)
  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 232)
  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..232
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..232
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=23890
     Region          4..228
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mtgglwadla dlvlptecag crerrpglrh gvcpdcvdvl galrpapvrp vpappdlppc
       61 halgayggpl retllaykeh grhglarplg allaevvaaa vgpvgpvllv pvpdtpaaar
      121 arygdhlgrl trhcarrlrs agwpvrvhna vraaprpdsv tldsagraaa atasfrarsg
      181 rgpaaagsrv vllddivttg atlaavsrvl tvrglspfga avlaatrkrh qq
//
LOCUS       WP_357586112             525 aa            linear   BCT 28-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357586112
VERSION     WP_357586112.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 525)
  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 525)
  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 525)
  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..525
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..525
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=57598
     Region          23..>203
                     /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 mtlsapttst ataphaldde qfeeellrvd patlvvganv rldprlrkty vdnvrqrgvl
       61 epviayrddn drlvvlrgqr rtlaavqaqr pwvrvmvvpk pdeadrltdq vnendhrepl
      121 tvaervaayd qlalcgvpag eiakrmstsr pvvdkalsva rsklahgatk rwefltidqa
      181 vvvaefedda eavkqlvvaa qrggfdheaq klrdaraeea akaetaaala aagisvvdrp
      241 vwndekvkrl selkhgeeql teenhascpg haaflddewv hpdegdtdee edpwgddtst
      301 eadedaqepe parpyriwvp eyvctdfaah ghalrwrghd sgsgrktvae mtdaereear
      361 aqrrdviqsn kawdsaetvr rnwlrtflar kiapktaagf iagslaradh avtsaltggn
      421 rlandllglp dqaptlgrra pamvelvgka sderaqmial glllaayeea tsrnlwrsvs
      481 dsttrylryl eangyelatv elracgeapl patdtnpatl aadea
//
LOCUS       WP_357586121            1099 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing serine/threonine protein kinase
            [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357586121
VERSION     WP_357586121.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11600203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..1099
                     /product="WD40 repeat domain-containing serine/threonine
                     protein kinase"
                     /calculated_mol_wt=115841
     Region          12..251
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(12,35..36,59,64,69..72,84)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,39,41,67,83..86,90,92,126,128,
                     130..131,133,142..143,146,162..165)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,39,41,67,83..86,90,128,130..131,
                     133,142..143)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,90,92,126,128,130,146,162..165)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(142..150,158..165)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          475..895
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          680..1060
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          870..902
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          908..945
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          950..984
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          990..1026
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mliegdpqrl grywlagrlg aggqgvvyea yaedgrrvai kvlhgdqvaq lgreaaaaqr
       61 vasfctapii eaklegprpy ivseyvegps lrtagrifvg ddlhrlatai ataltaihda
      121 gvihrdlkpd nvllgpdgpr vidfgiarta emsltatgvv sgtptymape vfigqradas
      181 advfawgavi vfaatgrdpf haenlgsvmh qvlsatpdls alpgtlrrlv slalakepaq
      241 rptarellla lvsgdggldt arllaqgghr aagigaqghd palgtlaeqa yamldpaere
      301 lvpevllrlv tvdeagelst rhaelaelie grashevaav rrilavfgyf larqdggvrl
      361 arpalpqawp ryrrwietnr dglavhrqil taarrwqaag rrdgdlfqgs sldsalewaa
      421 tarrditlsp terdflsaaa tltrhrarra rltslslggl lvialvaggl avqqgavadg
      481 raeqiagqlt rseaarlagv atttrgsdph qamlaslaaw rldrtpatra alvaslaqre
      541 tamfrdpsta gdtvralgad grtlisadst atrvwdvrng rllrtrgarr aepmdsvtls
      601 psgkvlvtvt arrasavdla sgrkisdhvf paakdftnew vdvaferdds vlleeadrrt
      661 rwdlrtgaak algpaaagtf srdgawravr rgrlleltnl rtgakdfigd kdgagtqgtw
      721 nggaavfgag lvatvasrsi qfwrrsdtql lttvqvrggv deavqgafdg stfrylvgdq
      781 vfsvdvadlt tedddrlvsa aalsgdgrlv vrdgelsavg grkvgalpea eyavfspdar
      841 fvamfgpgvr ivdtasaavq gtlrtsaaqv afspdgarlv vvtekggvel wdrqtgrrmw
      901 saeagaakya afsangrtlv vagdrvhlle taagkalgpa fggggrnaeg vrayftrsgk
      961 avvvldarrr mtvwdvatrr rlatargfgd paayspredl laslqvggrv rlvdvmsgtd
     1021 lgalldqggg qdpeigapld vaftgdgsav ltvngngavr rhavggeala aavcakaggl
     1081 saaqwrvivp tlpyrkacp
//
LOCUS       WP_357586123             257 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357586123
VERSION     WP_357586123.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   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 257)
  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..257
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..257
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=26842
     Region          16..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 mevahslggl pclslgtgpp livllftpqa avpagwgrry lmrlvkpfte hftvhaltrr
       61 pglppdttma dlaahyaggi eaaftgpvhv lglstggsla lqlaadhpgl varlvlggta
      121 aapgpicera nrayverarr grrpspplad lvtespigrt lvaalawlad grgdhtdgat
      181 mlnaeigfdl rarlpeitap tlliqgqkdl ayplelarqt aagipgakli vypgrshgat
      241 ftdprfaada ltflrsp
//
LOCUS       WP_357586143             623 aa            linear   BCT 28-DEC-2024
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586143
VERSION     WP_357586143.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..623
                     /product="type IV secretory system conjugative DNA
                     transfer 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]"
                     /calculated_mol_wt=66399
     Region          187..575
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 msgirnqqpi yprgsaggyp lapwlilgac aataaltwla wiagrlaavt agrpwdtgps
       61 fgweftkrll dqdwqhlwpg vppllvally allltttvvp gfwawawwqa rrpqagdplp
      121 slartrdvde ligatalara qrlrpslagr apkqvpttai gialgrlvtg grrrgpvlrs
      181 swedvllavm apragkttsl avppildapg pvlatsnrsd lwaatarare rvgrvwtfdp
      241 qrvtrqpqtl wwnplating veeaarladh fiqeirgvgs sdpfwplaag dllmclflaa
      301 ansggtltdv qawlsdvtsr epvtllraag ypqaaralag rqggapetrd gvyetartaa
      361 rclsdpeima wvtpptsald rldvttfpgs rdtlyllske gagaaaplva altdavfrta
      421 vvhaeaaggr idppvlavld eaanickind lpqlyshlgg rgvipitiiq niaqgqgvwg
      481 ergmtalwsa atvkvigagl ddarhaedis rligdhdvat tsinrdgngh tsyststqrr
      541 rilepgdlra lkrgrailla tgaraamidl mpwyrgdhad iigadttanv eaitrtarad
      601 latnhpgpss sdtttstnrg dls
//
LOCUS       WP_357586203             333 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357586203
VERSION     WP_357586203.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 333)
  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 333)
  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 333)
  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..333
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..333
                     /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=34894
     Region          9..284
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 maeprtgsfg pspaalaait rvpdlsaapd phsarlceal arryalppea fvvgpgtasl
       61 lhhlvartaa sgggetvysd psfhlyaslt rdygltgrav plrayrhdla altgavcdrt
      121 rivlldsphn itgtttslpe vialaetvpd gavvvldnvy gefqndvidr wfgeliecga
      181 pivvcrsfsk ahrlfglrvg ymigapalle tlgpivlryd vgtltqaaaa asladhatve
      241 anrrlvadar rrlaavltna giafvpsesa silinvgpva nqlaywltgv gcslrspsts
      301 gvpaghiqlf idnadtparv aralsdvrep hqs
//
LOCUS       WP_357586253            1058 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357586253
VERSION     WP_357586253.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1058)
  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 1058)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 1058)
  AUTHORS   Rosinski,J.A. 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 1058)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1058
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..1058
                     /product="helix-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=110989
     Region          <102..1006
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          700..730
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(702..703,706..707,709,740,743..744,747..748,
                     750..751,774,777..778,784..785,788)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          735..768
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          773..802
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          992..1055
                     /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 mgenqpaevk hrarpdtatg vgtgpvtggd tstgpgtsss agtdpgissg avtsttgtvt
       61 sttgtvaasg tgtssgpavg dredgrragg ggrgmlgpvt vrptstvlvg rqremtrlre
      121 avarartgep vtvlvggeag vgktrlleef grsvgdnarl lvgqclelge aglpfapfaa
      181 vlrtvlrrdg tgvldgydae farllpelar pagatapaaa ppsdaprgyl felvaqlfgr
      241 laaeqplilv iedlhwadrs trdligflvr aghtgrlllv ctyrtdelhr ghplrpflae
      301 ldrvrgverv elsrlerdgt gavlagllga epaaravddi hdrtqgnplf ieelaaagsp
      361 igcaalpdtl rdlllarvdr lpetaqrvlr iaaaggnrla hqllaevagl peaelddalr
      421 aavaaqllva dpdgdyefrh alvreavhde llpgeharlh arfaaaveaq phlvaagrap
      481 aeiahhwhaa hdhpralvsa rvaacaaadr yayaeqtrll ervlelwelv pdaadrlgmd
      541 hlavleetls aattagdykr altltraala evdteaqplr aarlldrrgr mlamlgksdg
      601 atelreayrl vsgvsdgper lrlladladh laridhadaa riaaevvtaa qtggadcall
      661 pvqlavlsrr egaadlglae lrrcealara agevpalvsa lvhisdvlfe lgrydesaqa
      721 aadgmsearr vgisrstgay llsnraeall algrwaeadq vcaeaarldp pgvsglhwlq
      781 lravlrlaqg hpradetvar algflakpyl hphnrlplhq lrleaalvad drfeavraaq
      841 asltdpaivd yprygwpvla atarvarhtg deevaaevak laggvaarfp aerayaaeva
      901 atvaagaeal aawqaavaaw rtagqpgela rvllgyaeaa agagerdevg aavseaaala
      961 dglgairlaq qaatlarrvg lrgagrgrpg adllterere vlrlvavghs nsriaeqlfi
     1021 spktasvhvs riiakldvtn rveaaavahr lnlltdqp
//
LOCUS       WP_357586292             640 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357586292
VERSION     WP_357586292.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 640)
  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..640
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..640
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=67212
     Region          63..248
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          347..626
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mvrrflella reasavefeg pviearaaga dpaaieeler akvealrvra llrrrarrea
       61 elsalydtag dlaalrdlda vleaivhrar qllatdtayl tlhdpdrgdt ymrvtdgsis
      121 akfrslrlam gaglgglvaq tavpystady fadarfrhkd dideavqeeg lvailgvplr
      181 lgqrvigvlm aanrsarpfh qeevsllasl aahaavaidn arllqetrna leelsqahrt
      241 arahaeaver aatahdrmts lvlrgggied vaavvtdvlg gslavlddlg rpltghvagl
      301 tdpvraagpd adapggvdpg vleaaqasra lgrtvrrgdl ciasvdvgge plctlvlrsd
      361 daderilera alvcallllf rrsvaeaegr vrgellddli srpgspglad rarrlgidlt
      421 aphvvvvarh dgqreraafw assqaaqrhg laaarpgevv lllpgrdpga laqrtagdls
      481 aslgtpatag asapetgpvg varayrearr cadalvalgr agdgasagel gfvglligeg
      541 rdvpgfvaga lgpvieydar rgtalaatla ayfgsgmsps rtaetmhihv ntvtqrldrv
      601 akllgdgwqe peraleiqla lrlhrlghtp ssqsvgpati
//
LOCUS       WP_357586373            1187 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586373
VERSION     WP_357586373.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1187
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..1187
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=127306
     Region          28..1186
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 megviaaqcd rcgrtaaegd rfcggcgael gavcphclrp lapdvafcts cgapragtdl
       61 pgslnqedrr rvsvlfvdli dftpyverad pelvrgmqtg ffsaarrvvg qyggvvekyi
      121 gdavmalfga pvatetdalr cvraglelqr vltrftptgt dglrfrvgva tgealvdvaa
      181 ardggqaiva gdvvntasrl qsaappggvl vdgathaltr dtirydeqpp vtlrgrsapt
      241 evwlarsavr qqptdrepdt tplidrehel gmlvnalhrs lrdrrpqvvt vfgragigks
      301 rlvrelhrht srlvdepltw rigrcppfge nvtfaaladi vkaeagildt dpaasaaqrl
      361 atavgelvgv nerdrvadal rplvglagnp lpaeeaesaw rrfllalaar rptvlvfedl
      421 hwaddamlrf vellgaaard vpllllctar pelvdrdpsw agtitgsvti alpplrdtgi
      481 aalyahmfgq aafsadlltp lievaggnpl yaheyvrmli eqgalrqsgr gwslekhldl
      541 pmpesvhavi anrvdlldak dravllaaav vgvqfwpgav aaavgqpves veralrrleq
      601 rdfvheqaas tmagqpeyrf rhvlvrdvcy qrlprterva rhertadwld tlsqsrdtdl
      661 aevlahhrwa aheiarslgm etrryaapar aalhraarra yalhgldaaa shaaralgla
      721 ddsdpvgrlq lellsteisf hrdgnaflsg ggpeqvqala erllaygdea caarawtllg
      781 qaawlradrp aalacldrav rlfeplpdsa qkadafaelg rlhmlnyerd pavaaadtaa
      841 eigerlglte irtnaritaa taryqagdra gldelytive fsragqllal pratqnlaya
      901 vceegdwvrs dallsavpar tasgqtltts ysseamrawf egdfgrllaa aeafvdtptg
      961 swdmqvrglr scllvlrgqp vppgpsadqs ppgtpprddv aaaldfarrs gfhrlhwtml
     1021 amgalcravq grvdeaaalv delaeswtav palasgewia aaswaaslag rkpaarvram
     1081 ldqvghrtpw seaalrtvtg alagadddhr haaelhlaaa etyagipdvt drmlaltfav
     1141 reltfagdha aagaplaelr afahrngapg llalthppad aaqtlac
//
LOCUS       WP_357586383             350 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357586383
VERSION     WP_357586383.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..350
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..350
                     /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=37606
     Region          12..337
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mtprhdprlk afasdnyagv hpeilqaiae angghqiayg edvytealqd vfrrhfgdga
       61 rawpvfngta anvvslramt ahweavvcae tahintdegg apevtggikl ltvptpdgkl
      121 tpelidrqaw gfgdvhraqp kvvsisntte lgtvytpaei aavcdhahel gmlvhldgsr
      181 ltsaaaaldv plralttdag vdvlsfggtk igllygeavv vlnpeaatgi dylrktfmql
      241 sskmrfvsaq feallsgdlw lrnarqanam grrlaeavre lpgvevprpv eanavfavlp
      301 advtarlqkr frfytwneat gevrwmcafd tteedvdafa aaiaeelaag
//
LOCUS       WP_357586413             412 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357586413
VERSION     WP_357586413.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 412)
  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 412)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 412)
  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..412
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..412
                     /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=42186
     Region          138..411
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtsspassav ssassassar rlasglliav svaysiigll yfltgtlang lvasaamagv
       61 vglnhvnmra alrgarpplf pltvllqavv tyvpdyllpa gysavaapml agaalvflpl
      121 gwgaatvglm maymwaglfq vlppvvmlfy lmtvpitgal syalvrfvrv sadleearae
      181 laeaavlker lrisrdlhdg lghsltaial kgdlaarlip rdpsaahgev talvkvarea
      241 aqdvrqvarg yrrlsltgev dravalless gvscqahlad aplprhadea lawavreaat
      301 nvlrhtratt ctittsahag rlrlevandg vtppatppat msatppatms atlpaamsgg
      361 yahpvpgdaa vteppagggl vglaerveqa ggtlhaarsg pdgfllalev pa
//
LOCUS       WP_357586448             257 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357586448
VERSION     WP_357586448.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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]"
                     /calculated_mol_wt=28131
     Region          46..161
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mispssranr gwwdgnaddy qlehgdflrd dgfvwcpegv deadarllgd vrgrrvleig
       61 cgaaqcarwl lgqgarvaaf dlshrqlrha qridldgapg gravplvqad aealpfaaes
      121 fdlacsafga lpfvadplgv lrevrrvlvp dgrfvfsvsh pirwafpddp gprgltsdrs
      181 yfdrspyteh dengnlsyve hhrtlgdwvg lvvasglalt gllepewpeg hervwggwsp
      241 lrgrhlpgta ifscart
//
LOCUS       WP_357586440             351 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586440
VERSION     WP_357586440.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=38297
     Region          22..312
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtqqtwdevg gllpydefra asdaivtnie qviegktatv rlalavllae ghlliedvpg
       61 vgktklakal arsidcsvrr iqftpdllps dvtgvsvynq ethdfefrpg avfanlvvgd
      121 einraspktq sallecmeer qvtvdgvtyq lqtpfmviat qnpiemegty plpeaqrdrf
      181 tariamgypd ptaelamldg hgavdplsgl rpvsdadtvr rlighvrqvh vadavkqyav
      241 dlvtatresp dlrlgasprc tlqmlrtara vaaldgrdyv lpddlqvlav pvlahriipt
      301 adaqlarrtt daivadlvhr lplphdrkrs pydtrpptgg ngrapfeprr p
//
LOCUS       WP_357586593             290 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586593
VERSION     WP_357586593.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 290)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..290
                     /product="phosphotransferase 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=30499
     Region          <73..234
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mfaskkrprw aelpasvrgs iegllggava yaescaggfs pgfasrltlh gghrafvkav
       61 dahhwpieas hhraeadvag rlpaglpvpr lldvcddgrw vilafeqvdg vapgkpwtap
      121 qirrvvaqav dfaqaatpsp ielprdhprl ggwaglaldq ptsarlrtvs awaphplgrl
      181 talereglra aqgdslvhcd lyphnvlvgd drvvfvdwph arlgapvidl valltgvaad
      241 gvdpepyllp vlpalncspa sfdailaaht gflmagalap mpigleaiae
//
LOCUS       WP_357586584             265 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586584
VERSION     WP_357586584.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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..265
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..265
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=28361
     Region          52..264
                     /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 mkkrliiaac lllvgvlgaa gtvgylafgr paanppteac adgrkpgalp avvaagssst
       61 qgrlgadwvg alrerledrg yefvnagvng ntsadlrqrv dtdiiacrpa avmiliggnd
      121 vrddvpldqf rdnlgaivdq vrsrttaria llslpplged ldaelnqkvs lyntviqqta
      181 trfqadylpv heqladiirq rvgdpapydf sfplafgaat qhylfgrswd qvardggrel
      241 hvdhihlndr ggavitelaa qwlas
//
LOCUS       WP_357586596             471 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357586596
VERSION     WP_357586596.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 471)
  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..471
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..471
                     /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=49124
     Region          12..241
                     /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..37,65,70,75..78,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,73,89..92,96,98,135,137,
                     139..140,142,152..153,156,164..167)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,73,89..92,96,137,139..140,
                     142,152..153)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,96,98,135,137,139,156,164..167)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Region          <318..>371
                     /region_name="MSCRAMM_ClfB"
                     /note="MSCRAMM family adhesin clumping factor ClfB;
                     NF033845"
                     /db_xref="CDD:468203"
ORIGIN      
        1 msdatpslva gryrldelig sgpmgelwrg ydtradwtva vkvlgarakg aatrqvlreh
       61 aqavarvihp nvamvldvgd hegapflvme fltgpsldee laargplkvv evcdligqaa
      121 agldaahrag vvhghvrphs frqagsgvlk vvgfglgeqa pgdgdphyra pegeggppad
      181 lyalgvvcye lltgqkpagq ppgalrqgvp aeldrlvmsl lsadpgrrpa sgeslrrala
      241 avarpratvp ppttevharp plqapaprag dtavfdaael appppggggg gnrrlyvqfg
      301 aalaaivait vvmilwgasg deqpvaentp apsvavtstp dttpepmptv eplptttpep
      361 areptslret dganpkgtvg vgvppggweg ylrqfgsalt aqmrlngidp rvagkaqdkl
      421 akaarkfaeg hedsgrdhvr gvlrdllraq ekgeiakegp lpewlsewrl e
//
LOCUS       WP_357586630             532 aa            linear   BCT 28-DEC-2024
DEFINITION  murein biosynthesis integral membrane protein MurJ [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357586630
VERSION     WP_357586630.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Kuk,A.C.Y., Hao,A. and Lee,S.Y.
  TITLE     Structure and Mechanism of the Lipid Flippase MurJ
  JOURNAL   Annu Rev Biochem 91, 705-729 (2022)
   PUBMED   35320686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     gene            1..532
                     /gene="murJ"
     Protein         1..532
                     /product="murein biosynthesis integral membrane protein
                     MurJ"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=52284
     Region          10..441
                     /region_name="MurJ"
                     /note="Lipid II flippase MurJ/MviN (peptidoglycan
                     biosynthesis) [Cell wall/membrane/envelope biogenesis];
                     COG0728"
                     /db_xref="CDD:440492"
ORIGIN      
        1 mtprlargva ggalliavit vlarvagfak qyalaqtvgt ncltsayfta nqipnivfev
       61 vvggalagav vpvlaepaat gdreragrig salltwslvv lvpvavltal lagpimglfg
      121 ggdcemhava armlvvfapq iplygvvvvl ygvlqahhrf tgpavaplvs slvvivayll
      181 fvplsdgrag saevplaael alsvgtslgv lalvltvagp vaglglrwrp afrfpggvav
      241 rvrrlalagi aallaqqaam agvlalsnnv igggalavyn yawaiylvpy avlavpiats
      301 afprlsaveg draafaelaa rttravvlvs gvaagvlaaa sgpgavvflg dkstvsspve
      361 laravalfap gligygliah lsrvlyaagr gravaagtva gwgvvivaqt vfalafprew
      421 qvaglalgms agmtaggall lasvvrarga aaiaglgrag aaalagggag fvaggwlagl
      481 fsgagtwgsv agtllaavva laagvgvval vdradaaava allrrrggpa gg
//
LOCUS       WP_357586631             275 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357586631
VERSION     WP_357586631.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 275)
  AUTHORS   Rosinski,J.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..275
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..275
                     /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=30066
     Region          30..>79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          103..265
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mpttalgafl tarrarltpd dvglvssgtr rvaglrreev avlagvsvdy ytrleqgrer
       61 npsssvlaav araldlgpda rdhlfrlagl ppggaptpar pqvgqslrel ldawpdtpav
      121 vidrrldlla gnaladafya dfaeadnlvr mtfldpagpt ffvdwrraaa tcvanlrlal
      181 ghdpqdrrar elveevsaas pefrrlwerh dvqgktheak tfrhgavgem tlsyhafdvr
      241 dapgqqlivy raephsrsae alrllgtlaa sewfr
//
LOCUS       WP_357586723            1892 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586723
VERSION     WP_357586723.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1892)
  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 1892)
  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 1892)
  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 1892)
  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..1892
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..1892
                     /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=208532
     Region          15..1317
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
     Region          <1294..>1879
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
ORIGIN      
        1 mtmpdldams tadkrrllae rlrarvrefp lsfpqqrlwf leqlvpgsaa yhvpiavrlh
       61 gpldlgvwrr ccdeivrrhd alrttfaeve gqpvqrvaat gradlavvdc aggdvrqllr
      121 devqrpfdlg tgpllrvrff rvapqehvll itmhhivadl wsvavavqel itlypvlrdg
      181 glsplpdlpi qyadfaawqr rqmagpgfaa dlaywtaale gappvlelpt drprppvqts
      241 rggstefrlp gplaerlral srqegatpfm tmlaafavll rrysgqddlv igapianrtr
      301 peverlvgff vntlalridl tgeptfrell srvrdaclga yahqdlpfer lveelhpqrd
      361 lsrsplfqvs fvfqnievpd ldlgglrvtp ytvesatarf dlelqvfdrp dglggwfeyn
      421 adlfdgatve qmsralrrlv ehlteapdrp vvrldllsgd errrlaqepn dtrrvwadlt
      481 wahlevagra aadpdaeavr cgertltyae ldrranqlar hlrglgtgrg dlvgictert
      541 pemvvamlgt lkaggayvpl dpaypterla fmmadsglkm lltegqladr lpdppavvvc
      601 ldrdadalaa edtaapevvv dgddlayviy tsgstgqpkg vqiphralan flrsmrerpg
      661 ltpadtllav ttlsfdisml elllplttga rvhllsreva adgarlgaal tasgatlmqa
      721 tpatwrllrd tgwtppagfr mlcggealpe dlarwlvgcg aelwnmygpt ettiwsavsr
      781 vtegvrlgdp iantelhvld aygelvppgv pgelhiggag lavgylgrpe ltaerfvphp
      841 fpiglgekly rtgdlvrrra dgsleflgrm dhqvklrgfr ielgeieavl arqavvrqav
      901 vlvredtpgd qrlvayvvad aapaqpdelv qwrsiwdsay dgsapevdpt fdisgwnssy
      961 tgepipaaem rdwvdrtael vrerapqsvl dvgcgtglil havaphclry wgtdfstval
     1021 drlrdsstry agdvqlheca adqldrlpeq lfdvvllnsv vqyfpdeeyl arviegaldr
     1081 lapggavvig dvrslpllea fhtsverhra gpgesddtlr arvrhrvsee eelvidpryf
     1141 qalrhripgi advrvrpkrg rfaneltrfr ydvvltagvv vppadcpwre wtsltalrdq
     1201 vggdvlalrd vpnarvlhsg gidpeelfrf geevgyqvel dwsdhgpdga ynvvlrrsgv
     1261 adhpvapvap ppdgplsawv ngaatrrark lqpqlraala erlpeymlps afvfldafpr
     1321 tpndkvdrra lpapdllrpi lrtpyepprd evqralaeiw gellrvdrvs vhddffelgg
     1381 hsllatqais rmrarlgvdv slrdlfeqpt vamlaawlta rapaptvtal taiepvprgg
     1441 dlplsfaqeq lcvdfpvppq hpfhtvvtaa rlrgaldeea lgraldhlvr rhetlrtrlv
     1501 trpgglvqvi ddqgkwplvr srldpadlad pmsairslld eeagqgfsla egplvrarli
     1561 tlsdrdrilv laihhavtdn wsygvllrel avaydafagg rdpwlpplpv qfadfagwqr
     1621 reyesgaldq harywrdrla dlppapsfdv ahlpaaeaas gaddhfvlga eltaglqala
     1681 tqenatlfmv llaaydalla aytgsrdlav gfptagrdrp eaenligylv nslvlrvdla
     1741 gdptfreaia rvrertleah ahhavplqpl rrempaardr vrlgfnllna plpptvlrdv
     1801 qlepvsvehg gvfvhvppgl rpaevdlgli vmadagllrg lwlhapervd arlvgrlrrq
     1861 werllemvva dpdrsieelg rvlrtdgagq pt
//
LOCUS       WP_357586750             481 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357586750
VERSION     WP_357586750.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 481)
  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 481)
  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..481
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..481
                     /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=49768
     Region          149..481
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrlslrarl llftagllla glslagavva dqleryqlgr ldgqlrslta lvssvpapgp
       61 pdladaaarp gllaqgldvf gspylvylda ggavaasvhs prvaaatlpr ledlravpad
      121 asaadlpaad gsgrwravar patgrggtvi aaaplaeada tiarvrassv isgavllvll
      181 tgagwfalgr glrplrrieh taaaiaggdl srrvpvlapp gteighlaas lntmlgqler
      241 afadraasea rmrafvsdvs helrtplfvi kgsaelhrmg alaspadvde amrridreat
      301 rltaltedll llaqldegad eqlelapmdl rtlandarhd lraldparpv evtgpdggpp
      361 gpapvhadea rlrqvvanlv gnaaahtppg tpvrigvgta dgravldvad egpgmtaeqa
      421 grvfdrfyrt drsrdrsvga gaglglaiar slarahggdv elrtalgega rfrltlplln
      481 p
//
LOCUS       WP_357586795             214 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357586795
VERSION     WP_357586795.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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 214)
  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..214
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..214
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22364
     Region          1..203
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 meavffdmdg llvdtekvwl eietgvmarl ggewspehqt hlvggsmert veymlavsgs
       61 daseatvrew mvsgmvttln ggvevmpgas elldalrdeg vpvalvtssl reiadavlka
      121 vgrdrfdaiv taddvtrtkp dpepyltaar llgvepvrcv vledspngva agtaagcavv
      181 avpsllpidp apgrlvvssl tevtpadlra lipa
//
LOCUS       WP_357586754             304 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Nonomuraea].
ACCESSION   WP_357586754
VERSION     WP_357586754.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,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 304)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..304
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31496
     Region          4..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttidvkglt krygpdtvvd dlsftvspgq vtgflgpnga gksttmkmim glaaptsgsa
       61 tvggrryrdl pvpltevgal ldagavhggr taydhllala vsnglprrra devlartgle
      121 svagkraggf slgmrqrlgi aaallgdpav lifdepvngl dpegirwirg fmrslaregr
      181 avlvsshlms emaltadhlv vigrgrliad tgmgefvrga gegavlvras gadsfarrlt
      241 aagaavrggp esslvvsgmt saeigklaay hgvelseltp qrpsledafm eltrdsveyq
      301 gara
//
LOCUS       WP_357586811             548 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357586811
VERSION     WP_357586811.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 548)
  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..548
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..548
                     /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=56994
     Region          4..546
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mnadlliagg lladgtgapa rradvavtgg ritvlergaa agpgatggpg gvdaagrvda
       61 aevvdaaevv daaglvvapg fidvhthsda vtllgeeawe lavapvrmgv tteicgncgs
      121 glfpglperl pemrassrvt fggrvpifpd fegfaeahra aprsnhlssl vghgtlragv
      181 lgyedrpasp reldvmrgll ddalaagatg lstgliytpg tyggtdevva laavaarhgr
      241 pyvthlrdem arveealeea veiarrsgaa lhvshhktag rhawgrtvrt lariaelreq
      301 gldvtcdvyp yteastslaa mlppwandgg tralltrlad pgqrdlmrra iadgvpgwen
      361 tvgnggwdri svacaprnpa vegrtiadlg gdpvdvaadl llsedgevti ishsmreddv
      421 qrvlaspftm igsdgvpkpg hphprlagtf prvlgryvre qglvtleeav hkmsgmaaar
      481 fglrdrgvvr dgahadlvlf dpatiadgat ytdpllpptg lrlvvtagqv avrdntvtpa
      541 rpgrivtp
//
LOCUS       WP_357586816             462 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357586816
VERSION     WP_357586816.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 462)
  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..462
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..462
                     /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=48075
     Region          <110..324
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtralvlggg lagvlaaavl arhagevllv egdhyppgpl prrglpqsrh shvlvsggar
       61 aldellpgtv aellargaqr rglpgdalvl aaqgwfrrld tgacllscgr glldqvvrer
      121 alpgvtvltg tralglagdr rrvtgavvet agggtrtita alvvdatgrr skapgwlrai
      181 gapaveevtv ssglaystrh yrapdglaeg mpavmlhprp apgrpgqgat lfpvedgrwi
      241 vtltgtrgge ppvdergfta faralrdplv adlmaaatpl ggvrpyrdta nrrrfferaa
      301 lpggflaigd avcalnpvhs hgmsvaalga lrlaaelarh gadpdafpav qsavaaqaet
      361 swrlalaqdr prddgareas afqreilarr srallsspel aagffraqal lpppaqdgaa
      421 varaltgepe plltteeava qhpalhawwa tharaggepi rr
//
LOCUS       WP_357586823             532 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586823
VERSION     WP_357586823.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..532
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..532
                     /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=55125
     Region          11..532
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mtggevpgra dvvvvgsghn glvsaillar agldvlvvea aeviggatrt enpfpkvpel
       61 rhstgsyllg lmppellaal dvripvlrrd phyflptpgg vgspyllfgt dtaatrtqla
      121 effspadaaa dealqaelaa lredlapawl aeplsveeta eryvrpelrq vfvdlvrgsv
      181 adylarfdfr sellismyav tdglsglnag pddpgtghnf lvhnmcrlpg sggtwmiaeg
      241 gmgtvsrifa daarasgari vtgapvtait ldggaasgvv ladgrqigae vvlgacdpyr
      301 lmellpdgal pttlsgrmaa vrrtgstlkl nlalrdlprf sclpegapsp fgstihllpg
      361 saslsggtge spmaalramw advragrlpe eptiewylht tvdpsladpa ghhssalfvq
      421 svpyelagtt wdaalpgyvd klvgicerya pgtgdliada vplpppgiea hfgitgghih
      481 hvdntvsfad rmpyatgvag vyagsagchp agsvigaagh naaqriladl gr
//
LOCUS       WP_357586838             223 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357586838
VERSION     WP_357586838.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=23509
     Region          13..220
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 msdddldala llhdpvrrsl yeavagrgge vgraeaaeaa gvsrtlaghh ldrlveagll
       61 esgfraperk gpgsgrpakv yrraagelsv slppreyatl gavlaevvee lgaeeraeaa
      121 arragerlgr rvappagptp sdgdpaeavl rergyepyae dgrlrmrncp fhalameqpl
      181 lvcsmnlalc qgllaglgdd pdrarldprp geccvtlskt ngd
//
LOCUS       WP_357586839             416 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586839
VERSION     WP_357586839.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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 416)
  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 416)
  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..416
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..416
                     /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=44473
     Region          1..409
                     /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 msfafgvvlf algilisvsl heaghmltak afgmkvtryf vgfgptifsf krgeteyglk
       61 giplggfcki vgmtpqdddv epgdekramw rypvwkrtiv msagsvthfg laifaawlaa
      121 mtfglpnpdf prneeqirae paviaiqdcv lpdttyreca tgdapspaat gglqngdrit
      181 singtpinny gdllttlrat tpgsaatigy erngqagtae ttlattkrpp idnpngpvte
      241 vsalgvglvl stpglvsygp veavgatstf igdmavataq alqrlpekip alwraitgge
      301 rdidtpisvv gasvlggeav annaweifim lfislnffig vfnllpllpl dgghiaiawf
      361 erarswlyar lrrpdpgrvd yfklmpftyv viliggvftl ltitadvvnp itlfpk
//
LOCUS       WP_357586850             369 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357586850
VERSION     WP_357586850.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=39256
     Region          13..369
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtssdlypvs rlaavqeata kagldalllt pgpdlryvsg ydakplerlt clvvpaaaep
       61 ymmvprlelp aaeaspasrl gldfvawdet ddpyriaadr lgpasrvgla drmwamaslr
      121 frdvlpdaeq vlagtvlrel rmrkspaeva alreagaaid avhrrvpefl ragrtereva
      181 rdiaeailaa ghatvdfviv asgpngasph hdvsdrviqa gepvvvdigg qlhngycsds
      241 trnycvgepp adyaasfevl rraqdaacaa vrpgvscesi daaareviae agygelfihr
      301 tghgigieth eepyivagnd eamepgfafs vepgiylpgs hgariedilv ctetggerln
      361 dsprdlviv
//
LOCUS       WP_357586859             720 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357586859
VERSION     WP_357586859.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 720)
  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 720)
  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 720)
  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 720)
  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..720
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..720
                     /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=77288
     Region          38..719
                     /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 magtgafggn tvdpagaqry aadwaravhr lgfvplsaae teqlllghti rlaevllsae
       61 ppaaaaaeig rslvdahlag pgviewsvrt lserfptevl adpagrpglg eriaavqgal
      121 aagfaralre rtfvqqegia ramwqardda eqalrdsear fravfdgaai gigiagvdgt
      181 iidvnhafad mlgypveelr qtnvaslfha ddaagmwely qeliegkhda vrvekryyrk
      241 dgsavwtdla vslirhddgr prftvavved iteryelqqr lrfqalhdpl tglpnrtlff
      301 dtlaglveqp dspgrvgvcf ldldgfkain dslghalgdr llvmiarrla dcvaeqgylv
      361 armggdefvi lvdgvaaved viavaesala avsapvcvgd qqlavsasig ivdsavagps
      421 vaelmkaada tlywakaegr drwavydper sardiarsal aaglpaaldr gefvlhyqpi
      481 vslldgrmla vealvrwqhp qlgligpdrf iglaeetgli irlgewvlrq acrdaqrwht
      541 dfpdarlvvs vnlaarqadr paivdtvada lassglpael lqleltesav mgsageplrt
      601 lhrlaalgvr lavddfgtgy snlaylrrlp itclklagpf vegirgtepv aadhrderiv
      661 dalvrlahal elwvtaeave teaqaerlra lrcdtaqgrl fgppgpaetv varlrgdkss
//
LOCUS       WP_357586883             390 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357586883
VERSION     WP_357586883.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 390)
  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..390
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..390
                     /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=42043
     Region          5..114
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          137..373
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrlaellard dlrltlvtgt gtldrevrra yptdlpdprr ylrpgdlvlt sgvwygepad
       61 cerfadalwa sdvaglvvgl ivlgelpqal vtacerrrvp lilaapdqsf gaiteavvae
      121 afaaerrrae rgraqtlldv lasqqiapge vsahlrllga dpglpttamv vsgpgghdlp
      181 amlhealark grhlivggra deaivlvngr atrkalseel ralaadrpgl rlaagisdat
      241 asvsqlgeal etarrgmesa rdgegpvsim svadidsydl llaalpmgvr rsfrdhllgp
      301 veeydarhgs ellrtldvfl etcgswqraa delyvhvntl ryrmqrveel tgrrmssmrd
      361 rtdlylalra gqlgsgqhrs geaagddvtp
//
LOCUS       WP_357586885             260 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Nonomuraea].
ACCESSION   WP_357586885
VERSION     WP_357586885.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 260)
  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..260
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27424
     Region          4..253
                     /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 migrtvlrvv gpllpsvliv vaawwlflea fgisplvgkr phqvweylft apeaaahrda
       61 vfgalgitir daaigfttgm vaavvvamtf vlfrtveqtf mpvamllrsv plvvmtplit
      121 lvfgrdllgv aviggivvff palvniafgl rsaspqatdl vmayggtrtt vlrkvavpta
      181 mpsvfasari svpssiigal iaewlatgqg igaeilraig gfrydevwad ivvvtsvsiv
      241 ayaavgvves lvlarfsdtr
//
LOCUS       WP_357586931             815 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357586931
VERSION     WP_357586931.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..815
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..815
                     /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=86723
     Region          88..203
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          205..806
                     /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 magrtpqasr rrgasprgst nsrarqpakk trapvrrrts tkgpgpaayv graiqalwmg
       61 lahgvgwavr aagrqaasar dldpehrrdg agllfiglal lgagaiwfsa agpvgarlad
      121 tvrlflgais ivvpvllgig awrlmrqpgd pehrgrglvg wgsmlvstaa llhigqqpag
      181 pgerdfaggl igagvgsvle ravtawvavp llvlllvfgl lvvtatpink iperlgllag
      241 gmvgqddpet teapatparr rptkrtappv dpdefddldg adlqetmvlp rkapsrvpas
      301 rkpaeppehs paptraeqla ltglagdytl ppsnmlgsga apktrskand eviaaltgvf
      361 dqfdvdaavt gftrgptvtr yevelghgvk veritqlsrn iayavkspdv rilspipgks
      421 avgveipntd penvalgdvl rsraatsdhh pmvvalgkdi eggyvvanla kmphiliaga
      481 tgagksscln sllmsiltra tpdevrllli dpkrvemtgy egiphlvtpi vtnakkaads
      541 lewvvremdm ryddlaangv rhiddfnrkv rngeikappg seremrpypy llvivdelad
      601 lmmvaprdve dsivritqla raagihlvla tqrpsvdvvt glikanvpsr lafatsslad
      661 srvildqpga ekllgrgdgl flpmgaskpv riqgawvter eindvvkfck dqrepefrpd
      721 vlapaqdskk kidedigddl dllvqavelv vtsqfgstsm lqrklrvgfa kagrlmdlme
      781 trgvvgpseg skardvlvkp deleevlegl rggdg
//
LOCUS       WP_357586945             344 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357586945
VERSION     WP_357586945.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=34812
     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 msatavaprl hgirhhritv lavlaaavla gvvlsitigs rsvapldawh altapgdtes
       61 diiirslrvp rtalgvlsgl algvagalmq ghtrnpladp gllgvtqgaa famvasimwl
      121 gassllayiw fglagalvas vgvfalgmvg grggptpvtl alagtavsaf lyaltsalvl
      181 ldeqamdvfr fwqagsiaar gpdvvwqvlp fiaaglvlam inapglnals lgedvarslg
      241 qhialtrtvg vaavtllsga avaacgalaf vglivphlar alsgtdhrwl ipysgllgaa
      301 lvlladvvgr vvappgelev gvvlaligap ffvalvrrrk pvrl
//
LOCUS       WP_357587069             343 aa            linear   BCT 28-DEC-2024
DEFINITION  LacI family DNA-binding transcriptional regulator [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357587069
VERSION     WP_357587069.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..343
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36495
     Region          13..341
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 maekrspaal gsatiatiar evgvssatvs kvlngrsdva avtrarveas lqrhryrrra
       61 rrapgegqid lvfhefgsdw aleiirgvea vatltgvnvv lsqlnaarrp pqswvdaava
      121 rrplgvllvm cnltdsqrqq lqrqsipvvv idtdsasvas vptvgsnnwn ggliatrhll
      181 dlghrriavi sgprdvlcar artagfrcah eelgvpidat lirhgnfhld agythgiell
      241 srpdrptaif agsdlqalgv lraarqlgld vpgdvsvvgy dnlplsawig palttvnqpl
      301 rdmagtaaqm lldlargnal ptsridlvae lvirestapp shp
//
LOCUS       WP_357587082             859 aa            linear   BCT 28-DEC-2024
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587082
VERSION     WP_357587082.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..859
                     /product="type IV secretory system conjugative DNA
                     transfer 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]"
                     /calculated_mol_wt=92444
     Region          444..>759
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 msinlpsspt psrdapcllc giderdvqda ldflaelpar lpefaltygp yllaaltaiw
       61 svaaavryvl gwahhadmtp qarlieissp prsdpdgavv lwrqlvgllr pawkrlftgq
      121 phlvweyhgs dagvriclwv pgtippgive kavqaawpga ttttrpaisp lpegarvagg
      181 rlvlagpehf plttdhdhdp arslleamgg lregehavvq ilarpttgrr lrhayraaah
      241 lrgggsrnhv grffdvilpl psdahdhrpg evarvfpera eqvrailgka gqpryevair
      301 yavsirrqpa ttaqqpvgvr adaaasdlvr gwlrgqahtl agvfalytgs hqylrrarlw
      361 rpgraigsrr ldhgyllsva elaalahlpw didapgiara garpiapppa vprntaggta
      421 rilgdadsgp qrpialpvad grhhthvlgg tgvgkstlla nlvladahag rgalvidpkg
      481 dlitdilnrl ppraigktvv fdpqddappp sinilaghdp afavdsvvti fhrcfstawg
      541 prvddllrst cltltsvlgr katladvprl ltdrafraqi iaklddsllg gfwdsyealt
      601 pagqatvigp vmnklravll rpfvrqalas pnttvpigql ldhgglvlaq lpkgilgdda
      661 arlfgsilla htwqattrrs nlaeadrpda slvidechnf lnlpghindv laeargyrls
      721 lvlahqhldq lpadlreals adarskiyfn aspkdandlk hhtaplispy dlthlgayqa
      781 aarliidgqq ttaftlrtrp lpapiegrqe airqasrerf tqphavvrpp arrarlvaae
      841 pdvrpglqgq paaldeqlg
//
LOCUS       WP_357587100             295 aa            linear   BCT 28-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357587100
VERSION     WP_357587100.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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 295)
  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..295
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..295
                     /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=31795
     Region          30..231
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 maevtssvwa tgqqpsrvqr rgryvpesmr hpgkmlpsia arviatysrp gelvvdpmcg
       61 igttlvealh lgrhatgvey eerwarlava nlgharkkga sgsgrvvagd srhigrllpd
      121 ltgraalvlt sppygtythg hvrstrdtge pgvrkwnhhy sanpgnlahq plpallegfs
      181 rilagcaell rpggvaavtv rpyrvrgelv dlpgqvhrva eqaglvfedr iacllcglge
      241 ghllnrasff qlhearkawa rglpvhaiah edllvfrrpq tpataipgag lrdsr
//
LOCUS       WP_357587109             275 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357587109
VERSION     WP_357587109.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 275)
  AUTHORS   Rosinski,J.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 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..275
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30964
     Region          12..>69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          92..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mrkvelepal rnpkrafgah lreyrklagk rqkelatilg wsvskismve rgerpasedf
       61 araadnalga eggllarwre tveqagrwpv wlaqlveieq radmlrawep liipgmlqte
      121 ryaravfrgr pgttpdlveq gvtarlnrqr ilewengptl wavldegvlt rpigseevma
      181 eqlahlavmd dhprvhvril phdawlttgl qgafmlaggp empdtayies itlsqitadp
      241 grvlevksry emlhgdalpr raslhlieek akrwk
//
LOCUS       WP_357587144             325 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357587144
VERSION     WP_357587144.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 325)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..325
                     /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=36113
     Region          41..322
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matttsppaa drvagtarpa rsaarrprrs llpylllapa vvlelaihvi pmlvgawmsl
       61 leltqfhird wsgapfvgld nyrvvfdvns aagaellrsf rvtvvytvls vglswmlgtt
      121 aavllqrpfr gravlralfl tpyalpvyta vitwtflfqr dtglvnhvlv dqlrlvdepp
      181 fwligdnsfv allivsiwrt wpfaflcvma glqnvpdely eaaamdgagf wrrlrsvtlp
      241 mlrpvnlvll lvlflwtfnd fntpyvlfgg sapaeadlis lhiyrssfqt wdfgtgsams
      301 vvlllflllv tagyllltnr rrnda
//
LOCUS       WP_357587152             298 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357587152
VERSION     WP_357587152.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   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 298)
  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..298
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..298
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31529
     Region          16..292
                     /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 mtprisgfdq qrvpvadgva lhaaiggsgs pivllhgfpq thlmwrhvaa dlaadhtviv
       61 pdlrgygdsd kpadpdgtay akrtmaadvv alagalghdr falaghdrga lvairagldh
      121 perisrlavl dvlptldmwd vlhgvdaavg fhlylmaqpp glpeqmiaas adaffghfld
      181 gwtrdpgaip tdvraaylaa sraavdsiva dyratagidv vhdradraag nrlrmpvtvl
      241 qqgwgaalgy daaglwrqwa pdlvhetvtc ghfmaeeapa dvvralrall areparpa
//
LOCUS       WP_357587120             340 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357587120
VERSION     WP_357587120.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 340)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..340
                     /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=37160
     Region          26..330
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msetqhesvr lapdpspglt taggdtpavs ppagrrrrkg igwparleia lmtgptlivf
       61 lsfvilpvam aayygffswq gygpaedfig frnyllifed stfidalrhn giivvlslll
      121 qgpaaillal llnrqmwgqt lirvlvfipy viaevvvgtg wslmlhgegv vnavlekvgl
      181 gflqndwlsd priaiwtlmg iltwkyigfa vilflaglqg ipeelteaaa idgasywqiq
      241 rritlpllgp tiriwaflsm igalqlfdlv yiiwgqyvaa tagtstmaty mvangrnage
      301 ygygnavavv lffvslfaal lyqrfilrrd tegaitggrr
//
LOCUS       WP_357587158             287 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357587158
VERSION     WP_357587158.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 287)
  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..287
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..287
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31505
     Region          7..285
                     /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 mrfasgaggr rltveitgkp dgvpifllhg tpgsrsgpkp rsgvlyrygi rlisydrpgy
       61 ggstprpgrt vadaaediaa iaedldiyrf svvgrsgggp halacaallp havtrtavlv
      121 gfarpdvadl ewfsgmaasn vrdfaaasdd rhrlmerlra qaartrrdpe slltqletdm
      181 twpdrrvvrd lairrliaqa yrealrsgpq gwiddvlalr rdwgfnlsai tapvrlwhge
      241 qdnfapvsht mwlarqihta evqvqpgaah fgaveilpem lewlsnw
//
LOCUS       WP_357587190             367 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357587190
VERSION     WP_357587190.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 367)
  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..367
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..367
                     /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=39089
     Region          133..367
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrrvgtdews glamlvvafa vagpgifgal gttiprgwwi alfagylaal lvsvatrvsr
       61 vvrymafavt vaaawalllt asnlgllpvl lvltaavsvy vvpvpvglav vvantlvitf
      121 aaasltrapa dgamllifyl liqvatllss vtllreqrmr relaeahvel qaasvllses
      181 aataerlris relhdlighq ltvltlelet arhlegpavr thleradrva rdllgdvrat
      241 vgqlrtespd leqalrrvtr dlpgldvtid vspgvrided dsaafvratq eivtntirha
      301 darslrisvt gderetvlda rddgrgapep tlgnglrgls erfaalggdl avdggdgfrv
      361 tarvpar
//
LOCUS       WP_357587186             290 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587186
VERSION     WP_357587186.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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 290)
  AUTHORS   ter Beek,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..290
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..290
                     /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=32384
     Region          2..287
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrawlpglll vtpsivaigv fvygllgwnf rlamtdqhde vseggfvglr nfidiwdqar
       61 whlsvnhaiv ftvvfvtgal vlgwflaflm ekgiwgegtf raiylfpmav sfvatgivwr
      121 wlmnsgmder avglnrlfda vglpqwewfr nqewgmaama lpavwqmsgy vmalflagfr
      181 gvpeelreaa rvdgatewgv yrhvvlpllr pvtlsaliil ghislkvfdl ivavsgkqiv
      241 tdvpavfmwv avfdshdpak gatiasyivl svavfvipyl iwsvrkerrs
//
LOCUS       WP_357587223             343 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA dehydrogenase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587223
VERSION     WP_357587223.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 343)
  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 343)
  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..343
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..343
                     /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=35628
     Region          1..341
                     /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 mklvlsqeqq elraavrafl aaasplpkar egydpavyar lngelglagl ivgeeyggag
       61 agfadlaval eetgaallpg pflattfaai alagtpdkel ltgiaegria aalvlpgtai
      121 plrdgeltgt lpqvlsgmda dvllvpattd ggavltavtl dgpgvtrtpl etldltrgqa
      181 rveltaaaar vlgplpdaag vadrlaiala aeqlgvmraa ldaivayaka rvafgryigs
      241 yqgvkhklad mhgkleqaes ivryaawaad espgelpeaa alaqayvgra cfevardhll
      301 lhggigytwe hdahlyykra ktdevllgpp rehrarlarl lel
//
LOCUS       WP_357587230             342 aa            linear   BCT 28-DEC-2024
DEFINITION  copper resistance D family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587230
VERSION     WP_357587230.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..342
                     /product="copper resistance D family protein"
                     /calculated_mol_wt=34616
     Region          130..>340
                     /region_name="PcoD"
                     /note="Putative copper export protein [Inorganic ion
                     transport and metabolism]; COG1276"
                     /db_xref="CDD:440887"
ORIGIN      
        1 mtatqvaagr avrgqlaggv favsavvaav vastltaqea vpgipmpgpl vtvglpvvrv
       61 lldvaavavv glslvpkllg fdapersepv lrrvrplavt aawawavcal ltivfrtael
      121 npgrvptlgm iasyvdtvgt gqgllfsaac alaaagiglm avrfgekvpa elrivvalfg
      181 llpipvtgha vdsvwhdpim immevhviga aawtgglial avfvaprael lavalprfsr
      241 latvcllmvg lsglvsglgt maltpgvelp gaivtsqygl lvvvkvtlta llvplaahir
      301 frllpairag ratavagwat aevavmglay gvavaitras ig
//
LOCUS       WP_357587259             277 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357587259
VERSION     WP_357587259.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 277)
  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..277
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..277
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29757
     Region          3..274
                     /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 mpfvtvsdgt qifykdwgsg rpvvlshgwp lnsdsweaqa lhlaangyrv iahdrrghgr
       61 stqtwhgndm dtyaddlaav vealdlraat ligfstggge varyigrhgt graaqvalvs
      121 avppfmlmte dnpagvpvev fdglragslt draqlykdla dgpffghnrp gsvvsqgird
      181 vfwlqsmaag hrnayecvaa fsatdfrpdl dafdvptlvi hgdddqvvpf evggkasaar
      241 ikgarltvyp gaphgitdth kqqlgddlla fleeyqp
//
LOCUS       WP_357587284             449 aa            linear   BCT 28-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357587284
VERSION     WP_357587284.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=47476
     Region          31..425
                     /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 mtpdpgeadr pnpghpdpqp rpptagrgdg flrksgtfft gtllrtlaqg alfvllarem
       61 eldtyglfvg vtaliavvsp fasagapsli mqnhadspte wdrhlvrglf vsmvfgcaat
      121 vlvsaaglai wgvdvglvdl lclafadlva wrlieavaas iqvrgrilla alvpallhlc
      181 rlaaalvlal spgpialhdw avasavistv vcmpvllggl rgahhgalrf agslaqartg
      241 mmfavglsaq svyndsdkvm lsrlstpena aiyaaayrvv dlaytplrsm saiayprffq
      301 agrngpreal rlarrllprf lafsapmsll lvafawmmpl vfgadfaaav palqwlsvll
      361 vlkslhylaa dalsgarmqg rrtvcqigig vanallnlwl ipaygwqgai vsslvcdall
      421 aillwgclav svrrdpadts asarpmerv
//
LOCUS       WP_357587351             214 aa            linear   BCT 28-DEC-2024
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357587351
VERSION     WP_357587351.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..214
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /calculated_mol_wt=23960
     Region          2..201
                     /region_name="NahD"
                     /note="2-hydroxychromene-2-carboxylate isomerase
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3917"
                     /db_xref="CDD:443122"
ORIGIN      
        1 mrfyfnfrsp yswltlhdll aerpglarrl dwipywdpee atlreldaag grfgysamsr
       61 ekhlyilqdv rrlarargle pswpldrgpr wevphlaylv aadhgvgqef aagvtelrwq
      121 rgadvcdprv vaelgrslgl deaaltgaad dpelrergie alrtadrdgv fgvpffvhgr
      181 erfwgldrla afaesageqe adayppedhp ggcg
//
LOCUS       WP_357587353             160 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357587353
VERSION     WP_357587353.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 160)
  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 10002379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..160
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17231
     Region          9..143
                     /region_name="FabA"
                     /note="3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier
                     protein) dehydratase [Lipid transport and metabolism];
                     COG0764"
                     /db_xref="CDD:440527"
ORIGIN      
        1 msgpeeigvd rirkviphrf pillldrvva vtpgeslvav kavtctepcy egigdeagpa
       61 aydypwplll eswaqaaall alwespnpdv lagdvvlagg mrnvrfhrpv rpgqviehrv
      121 rmvrkvgena vmegeslvgs evvqemgtmi ettrpigvla
//
LOCUS       WP_357587370             214 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357587370
VERSION     WP_357587370.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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 214)
  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..214
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..214
                     /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=22628
     Region          3..214
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mvnvvvfgag gtagsrivre afdrghrvva avrrpeadap ylpagvrvvt gdatsersvr
       61 elapeadalv laigggsrsl wpdaaravld alrgmpaapr vihvgggatl lspagtrlld
      121 dpdfpaeyrd aalgqaeald lyrssadgvt wtylsppple fhpgertgry rtgtdepvtd
      181 aqgrsvlsye dlavavvdei engrfrnmrf taay
//
LOCUS       WP_357587393             167 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357587393
VERSION     WP_357587393.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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 167)
  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 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   5  (residues 1 to 167)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..167
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..167
                     /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=17770
     Region          84..164
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 manveerlaa leaqvaglve rladadeptp ppegvlwald glkqrlpaeg sgavlytgtv
       61 rlagqhydwq ygrgvedlla ddwaelpavl salahpvrlr llreilggrq gtaelagied
      121 lgttgqlhhh lrqltaagwl rsagrgryai paervvplla iltaagr
//
LOCUS       WP_357587430              62 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357587430
VERSION     WP_357587430.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=7136
     Region          1..62
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mnpatqrtws tedvsiflgv pvatlyqwrh rgigpkaarv grhlryleed vldwfrqqrd
       61 aa
//
LOCUS       WP_357587467             267 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TrmH family RNA methyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357587467
VERSION     WP_357587467.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=28059
     Region          7..265
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 magteltnlr sprvkaarrl tkrafreqdr kflaegpqav realkldgvt lelfttaeae
       61 lrhpelvtqa tlqglpvhra sgevmaelsq tvtpqgllav crhvhvplge alpaepklva
      121 llahvrdpgn agtvmraada vgadavvftd asvdpyngkc vrasagslfh lpvvigepva
      181 aavarlkerg lrvlaadgag khtlddvdls gpaawifgne awglpddvla laddvvrvpi
      241 ygqaeslnla taaavclyss araqrvp
//
LOCUS       WP_357587529             139 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587529
VERSION     WP_357587529.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=14563
     Region          16..126
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mvddrvmnvv aaavvergrl lvvskkaape vfylpggkpe agespketlv reldeelgva
       61 prdldllglv edvaalegvp mrmtvftaal tgrprpaael aalgwtdgrd gyaprlapav
      121 rhhvlpvlvr agalaldgp
//
LOCUS       WP_357587568             449 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587568
VERSION     WP_357587568.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..449
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..449
                     /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=48578
     Region          1..355
                     /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 mevtivgagl vgcllacfla rrshrvtlye rrqdprerga drgrsinlai sergidalrr
       61 vgldrevlkd aipmpgrmmh aldggltfqp ysadhrqain sigraelnmk lldaatalpg
      121 vevrfghrlt gldertgrlt fetetgpgea rarvvigadg afsavrarlq alpgvsfsqs
      181 yldygykelt iparggafal ergalhiwpr gasmmialpn pdgsftctlf wphrafaelg
      241 dparvrehfa ehypdasalm pdlaadfaan pvghlvtmrc dpwhvttdaa vvglvgdaah
      301 aivpfygqga ncgfedcvel drcldetgdd fagalalfer rradtdviar lalanfvemr
      361 dkvgsrmfla gkrlehaler alpgryasry elvsfsttpy aeverrvarq rgwaagglll
      421 gaaglaglag lgmmargrrp ggldktdnp
//
LOCUS       WP_357587530             508 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357587530
VERSION     WP_357587530.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 508)
  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 508)
  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 508)
  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 508)
  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 508)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..508
                     /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=51908
     Region          18..483
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mserverngn laalaaavlq pgfvgtvppa wicrwlgdgl gsvvlfsrnv vdpgqvaalt
       61 aalraerpdv ivaideeagd vtriesgrgs srpgnlalga vddpalteev ardlgeelaa
      121 agitlnyapd vdvnsnpdnp vigvrsfgae pslvarhtta wvrglqaggv aacakhfpgh
      181 gdtrvdshhd lprivadrar lhavelapfr aavaagvqav mtghllvpal dpdlpatlsg
      241 rilggllree mgfegvvvtd avemgavadr ygfagaavra laagadaicv ggehadeeta
      301 rhlrdaivda vvagelpeer laeaakrvgq laawtvaart arpgtraaaa gtgstvglta
      361 arlavrvtta eatattlplt gpshvvefqp phniaigset pwgvaeplta lvpgttsvry
      421 vehsvpadpt vgatgrplvl vvrdlhrhaw mrdavdrala arpdavvvel gvpalvtgav
      481 hvathgatra agraaaellg ggavspgw
//
LOCUS       WP_357587572             219 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent F420 reductase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587572
VERSION     WP_357587572.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..219
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22028
     Region          3..197
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mrigilgagg madalgtqwa raghalmvsg rdpgraaata atltaaaphg lpatagtfee
       61 aaafgdvvvv avleeaadqv vraagpalrg kplidvtnav gpgaydvtrs vaeriaaltg
      121 ghvvkafnlc hvdvwrmtpp vfdgrplavp lcgdddhalg lartlvtdlg ctpvhgggld
      181 raklleataa fmiglwisga daqavlpplp hsgphpdep
//
LOCUS       WP_357587609             438 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357587609
VERSION     WP_357587609.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=47149
     Region          42..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(143,145,289,291,321..323,366)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrtprtrqaa llaaaalltl tacgsgdagg gdggggekvt ltyrlwdeqq kagyekvmaa
       61 fekanptidv qiellpydqy wtkltadava gsapdvfwmt ptqfpeyvtk gvlaevkvda
      121 skyhptvvgs ftyegklygv pkdwgtvgll ynkdlfkkag vempdkltws pdgggtllev
      181 arkltvdeag khpgedgfdp gkvktygfgs wnhyqtqwmn wvnsnggkll dkpfgkytfn
      241 deasvqalqw gvdlvnkhhv sppasqtnpp tgkitdmfta gevamfpann allpfvapga
      301 gfemgvalmp egpqgrsvnl nglseavyak sehpeeamkl aaylgteepq klmadggyvf
      361 painglaqgy vdywkakgld vspfleeaeg ttfplpvttg ftgfetklnq ifnemylgkl
      421 tpkqaadqav aegnatie
//
LOCUS       WP_357587633             182 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357587633
VERSION     WP_357587633.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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 182)
  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 182)
  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..182
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..182
                     /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=19728
     Region          7..178
                     /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 mrrvvckggr lwlgevtead vaalhavygd pgatqhmpfa plslpqvagl vdeavraaaa
       61 eprrlyvlav lepgepeaig varlrvdaeh phsaeiglgl rpdhwgrgmg tdlvrlllkf
      121 gfkqlglhri wgarspanlp aqlamltagm veegvlrhhv stpwgwrdsv ihaaledewt
      181 dr
//
LOCUS       WP_357587593             436 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357587593
VERSION     WP_357587593.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=46631
     Region          45..426
                     /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(152,154,282,284,317..318,360)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mriksalaaa avvalaagcg gsggdsgssg tpnepvkldf lslawqkesv aankalveew
       61 nkanpniqvt yvqgswdnvn dqlvtsfegg dapdvihdds palsgfaskg ylldltgkvp
      121 delksdipqa awdtvtfddg kgnqgvygvp flqesqviia nkklldaakv riptagepwt
      181 wdefaevskk ltkgdtfgva wpmkspvnkt lnlalnfggt ffqtgadgkt tvkvgaeeke
      241 vlqrihdqly kdktadtsal gmgtadplpg ffadkyamlp vgvylrqqva eqapdgfewv
      301 tlpplkgttt eqgavsqtls iaadskhpee amkfmaffln gpnqaklakg dwllptsqka
      361 aadpaittee ngwdvatasa kslvvapflk vngfdewksk vatpvlqeff ankitldeaa
      421 krlveegngv leryqr
//
LOCUS       WP_357587736             365 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587736
VERSION     WP_357587736.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 365)
  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 365)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 365)
  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..365
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..365
                     /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=37790
     Region          4..>66
                     /region_name="PNTB"
                     /note="NAD(P) transhydrogenase beta subunit; cl22917"
                     /db_xref="CDD:473992"
     Region          128..365
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mawigglsgr rgdgviaavt taatlgpllv sgpkawwiva lgvaasapvy wrrrapmtva
       61 llvgaamsvm vfwekpflpf gplvavhtia drspawqrla aipaiaaivg vslalpgeds
      121 etfrlvgiaf vaayalgtsa rasrsrtael aerarrleqe hvaavaeera riardmhdii
      181 thavglmvvq aeagpvvvrs dapraeavfd aiadtgrgal telrgllaal rtsavpaged
      241 lgpaqprldg laslagrsgl dvdiaveger rpvpagleaa vyrivqeslt nvrkhagvda
      301 vrlrlrwtaq elvveladeg ggparggsgy gligmreraa acggtltagp gpaggyvvra
      361 vfple
//
LOCUS       WP_357587724             967 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357587724
VERSION     WP_357587724.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 967)
  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 967)
  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 967)
  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 967)
  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..967
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..967
                     /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=104400
     Region          42..273
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          130..967
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          724..751
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          763..791
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(764,767..768,771..772,774,804,807..808,811..812,
                     814..815,844,847..848,851..852,855)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          802..832
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          843..871
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          882..910
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          922..950
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpatpapeis asplmcppvl yvprpgeils egvdtfahmv smrfsllgtv evsadghvlg
       61 gaprhramla ylllnagstv stdrlieamw gptppetaka qvqasvmair rmlraaqaen
      121 vvqtrpagya vvtepgqvdv hefrrlaagd reeirqalgl wrgqaladvq adfvpatral
      181 leeqrltale rlaeleleag ryavlldela aevaghplre rlrgqyvlal hrsgrqaeal
      241 aaardyrttl aaqqgldpsr efaaveeavl rddrpavvnf lpydvpdfag rdaelerlaq
      301 lpdgvsvvai dgmagigktt lavhaghlla erfpdgalfv dlqahtagrd pvdpgdalei
      361 llrqlgvpae rvppgtsera alwraelsgl ralvvidnaa daqhvrpllp ggsgsmavit
      421 srrrltdldg ahaisvdvls erdavelftg vvgpraraep aavaevlslc gflplavria
      481 aarlrhrprw tvdylavrlr dqgrrlaela taergvaaaf glsyeqlsad hrrmfrllgl
      541 hpgqdidaya aaalagltvt raeslledll dthmllqqep grytfhdllr dharsaavle
      601 eqdasakaal trlfafythl tgmaadlrya drvlpaphep apgletppls dradaaawld
      661 telpallavg ahaaehgwht qafflsttlf pfleergrrg aaltlhlqtl savrqaadlw
      721 segrtladla rthhalgnva qavqyaheai stcraagdpe geavghhflg hslerrgdvh
      781 gahdhyrqal elfqkadnrv gtgvllidmg etyrqlgkpd lardyltqaq rinheigsqa
      841 slwnaqlalg nlhtdqsehd aarraferay aisrdlgphl qaetlnalga aaramgdhhq
      901 alidhdaala lateiddphe aahghlglak arhalghtal trthaqeavr lleeldnpaa
      961 dtarall
//
LOCUS       WP_357587756             185 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357587756
VERSION     WP_357587756.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 185)
  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..185
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..185
                     /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=20059
     Region          12..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msrtrseqaa wrrerlldaa lrvfadkgvd gatvkdvaqa aevtpgllyr yfdskeamve
       61 tllsergflp rlrelraeqe ndprpavvvl aetlaafdrl ladnaelmav ffssaqarvp
      121 laalvgegqq ligdfllerv eagelrphdt ataarslfaa vavnrrlgtp idvaalvgll
      181 fpeeg
//
LOCUS       WP_357587776             177 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587776
VERSION     WP_357587776.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 177)
  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..177
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..177
                     /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=19836
     Region          3..163
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msdeagftrm fhehyeavlr yawrrvgpve aadiaaetfk vawekyhrfp sgqplpwlya
       61 tarnlisnai rrdnrrdgll wdgslmlsdv eddhaagvaa rqealtalrs lseadrelll
      121 lmswegldlr qaaavvgcsr ptaamrlhra rkrlshllsk dappiadrkp sfegnsl
//
LOCUS       WP_357587816             255 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357587816
VERSION     WP_357587816.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..255
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27232
     Region          19..250
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 msrtrrsdrs wvrtltsvdd ptarlvcfph sggtaavyrp wssvvpagva lhavqypgha
       61 drlaeepaas iaematevaa ellrmpparc alighslgal vayetarvlr dngspvhhlf
      121 vsgaagpwla gggvshrlgd eelwsavatl ggiepeiadq pelrdlllpv lrsditlhet
      181 yrpapdaapl dcpvrgyynt edplvdadqv aawaavndge fsmrawpggh frllshpgel
      241 vadimatlte sgvrr
//
LOCUS       WP_357587808             177 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357587808
VERSION     WP_357587808.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..177
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19224
     Region          23..122
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mssvrtdaph gtpslsgpka ripdcplgrt vavvgawwtl eilheifngh trfaairhhl
       61 gtpaelller laelqgrglv epavdatapd greyrltplg rtlrplllvi aawgnhqlap
      121 edrsvilvdt dtgvevdpiv vdrrtgrpie tenvvfargp kaselvaery pkimlts
//
LOCUS       WP_357587817             496 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587817
VERSION     WP_357587817.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 496)
  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   2  (residues 1 to 496)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..496
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=52290
     Region          2..489
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 msgeptvrtt egvvqgrrrq ghavfrgipy arppvgplrf aapapphrwe gtrqavefgp
       61 vvplslpidv ppqgddwltl nigtpvpgaa glpvlvwipv ggylsaassd pmfdpaalae
      121 agvvvvtinc rvgaegfafl ddappnrgfl dqiaalewvq hniaafggdp grvtvggvsa
      181 gagsvaallt mkparglfrr aiahsvpglh stpalarqvt aafadrlgaa aptaealrdi
      241 apwrlaaelt sfnaglhahr eswgrltetg talcpvvdge vlpetpwpal tgaradgtel
      301 vvghtrdefr yfsvmsgryg afteedahaa lellapqpdg arayraafpq agpeelvetv
      361 ysdalfrmps qklaeanaaa ggtsylfelc wtapvrggil gachsldmpl afgtldspvg
      421 aqligeqptp eaaalsrelq eawvrfvttg dagwpahrpg erltrvldte setlpypeea
      481 srqiweghap apfdlp
//
LOCUS       WP_357587818             541 aa            linear   BCT 28-DEC-2024
DEFINITION  (2,3-dihydroxybenzoyl)adenylate synthase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357587818
VERSION     WP_357587818.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..541
                     /product="(2,3-dihydroxybenzoyl)adenylate synthase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0008668 -
                     2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
                     [Evidence IEA]"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58339
     Region          1..533
                     /region_name="EntE"
                     /note="2,3-dihydroxybenzoate-AMP synthase component of
                     non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1021"
                     /db_xref="CDD:440644"
ORIGIN      
        1 mldgfvpwpp dvadryrrag ywrglslrql fddsvrrhpd rvaavdatrr vtyaeladea
       61 driaaglldl gigsrdrlvl hlpnvnefls vllavfsiga ipvlalpghr rdeithlara
      121 sdavaylgpd rfqgfdhral areiradvps vrhvviagds aeftslaela rseprqlppv
      181 dageiallll sggttgvpkl iprthddyay nifacaevtg fgadsvylaa npvphnaalg
      241 cpgvlgallv ggkavlaanp spdhvfplig regvthtalv palallwtea aqtmpvdmsg
      301 mtlqvgsskf gpaaaqrvss glrcrimnvy gigeglitht rlddplevvy ttegtpicpd
      361 devrivdped revpagvtge lltrgpytir gyfaapehnr raftvdgfyr tgdlaklted
      421 griviegrlk diihhfgekv saeeveghvl thplvrdaav vgvpddaide ricvfvvlta
      481 aadaaatpls lrtvrehird rglapyklpd elvvvpdlpr tpvgkidkga lragrrelqh
      541 r
//
LOCUS       WP_357587836             262 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357587836
VERSION     WP_357587836.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..262
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28323
     Region          16..249
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mpadelfpga frrlaprpya rarvvlfphg ggsasyyrpw ttsapwdief lavqypgred
       61 rfaepapvdi relvdtvaad lplagsptpt vlfghsmgal vayevarrlt aagdppaalv
      121 vsghpaphla rpgqvhlgsd delieelrrt eathldildn pvliqaflpv irsdyrlset
      181 yrplpgvrlr apvtvlhgdr dpevtaaeaa gwcdatdglc esrvfagghf yldehrdavv
      241 elltararam satsavpwps tp
//
LOCUS       WP_357587875             149 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357587875
VERSION     WP_357587875.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 149)
  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 149)
  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..149
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..149
                     /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=16732
     Region          8..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdtawlgade eqawrafrrl lialpariar dlardsglsa adyevlstls ekpdrrwalr
       61 elaakmewsr srlshhaarm qarglidkep dpqdargcll hltddgfavl eqaaphhvvs
      121 vrsrflehvs adelsmlrei striadlpd
//
LOCUS       WP_357587894             237 aa            linear   BCT 28-DEC-2024
DEFINITION  MIP/aquaporin family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357587894
VERSION     WP_357587894.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..237
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24045
     Region          5..220
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mvdvrrylae figtfvlvff gvgsaiaari eggvvvvsla fgfvllalvy tigqlsgshv
       61 npavtlgvll sgkitalgav aywiaqfaga avasfllwvl vrwggvndqt gvlgangygt
      121 ninaggamll etvltflfvl vvlvvskrst dlsgfaglai glalgvanlv gvaltgaavn
      181 parafgpaif egglalrqlw vfivfpllgg vlaalvaplv ehgsgvtrig tprpsgr
//
LOCUS       WP_357587900             393 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357587900
VERSION     WP_357587900.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..393
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..393
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41905
     Region          128..382
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 miapvsatpw rhlptdlaaa mrphlpatva gvavavteat pafagiaddk fardvrtavq
       61 valdrfldli gtgepalppr frevfvglga aearedrgpe allaalrtaa rlllrtasqs
      121 larlrpvdpe elidlsdavs ayvaelaaas tdgyalqlre qagegdrrrh laelllrgdg
      181 lpsavesaaa rigwadldav vpvllpldqa rdarfrygpd glviergrda vlllrsgara
      241 sratlaeala grpavvgpel gwpqvpaavr laelaaglvg pspgpvfvdd hlvtltlrge
      301 qralavltar rlaplahlrp aqresllatl yawlrhwgsr aevsaelfvh pqtvsyrlkr
      361 lrdlygddld datarfellv vltgrlntrp gag
//
LOCUS       WP_357587947             306 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357587947
VERSION     WP_357587947.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..306
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33510
     Region          2..193
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mvptynrpgp lrqalasvva qravpgsvev vvvndggcdv stvahaareq glvvrlidld
       61 qngglpsarn vgiqvargdy laflddddif lpshlgttla vlstgdadla ytvcvvqear
      121 vdptnppafs tpttfsfdpd llsvanfmpv htavlrrppe sarfdadlpa ledwdmwlrl
      181 ardhryrfvh vpeptvvyhr itseasmvga tvgdghalah fgtlteqmwc rwpartpkaq
      241 hfrlyiavmy whslarlaag halsdqyfqr cvaeiaavwh gersetglrq riidsiketa
      301 dvahaa
//
LOCUS       WP_357587901             293 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357587901
VERSION     WP_357587901.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 293)
  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..293
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..293
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32651
     Region          9..289
                     /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 mtipvlartv hrhldvdgvr vffreslper adapvllllh gfpsashqyr rlidvlgtry
       61 rliapdypgf ghteapagft ysfdrladit egfvrklglt rfvayvfdfg apvgfrlaer
      121 hpewiaglvv qngnayeegl sdgardfial rpdrpgaeet vralftlpgt rgqyetgvav
      181 pglvapdgwt ldqhfldlpg rkdaqvalaf dyhsnveryg awqewlrtht pptlitwgan
      241 dpffpepgar aylrdlpdae lhvldtghfa ledhlhqiap lvagfldrvw hag
//
LOCUS       WP_357587952             343 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357587952
VERSION     WP_357587952.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=36129
     Region          1..343
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mqssahtvav fgayghtgrf vvarlrergf vplltgrdsa rlkelahetg lefrtasvdd
       61 pgaldhalag aaavvnaagp fattaapvie aalragipyv dvaaeieana dtfahfgdra
      121 raagavivpa mafygglgdl lttaamgdwt sadeahiayg lsgwhptagt raagvvsrqr
      181 rdgqrvrfan grleyrhdep pvlewpfpap lgprpvvgef smadivtvps hlsipevrty
      241 mtveaarevv apdtptpapa delgrseqtf lvevvvrsgg aerravargr diyaftaplv
      301 veavdrlltg rtratgvvsa gevfdapdfl ralsadltve les
//
LOCUS       WP_357588035             114 aa            linear   BCT 28-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357588035
VERSION     WP_357588035.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 114)
  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 114)
  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 114)
  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..114
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..114
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12394
     Region          1..113
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 matkttailv ddldgstddv gtyqfafngv tyeidlssgn fdrmaaafgp fitagrrlpk
       61 qpstpgrpaa sgrgrtreir twwwttnwqe rnlpqprtgg aipaavrday haah
//
LOCUS       WP_357588039             534 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase, partial [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357588039
VERSION     WP_357588039.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 534)
  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 534)
  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 534)
  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 534)
  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..534
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..>534
                     /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          12..38
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          40..>514
                     /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 mtetgrarpm gtedklrayl kratveladt rrqladeegr rhepvaivgm acrypggvts
       61 peelwdlvas ggdaitefpa drgwdldgly dpdpeaagks yvrhggfvhd agefdagffg
      121 msprsalatd pqhrlflesc wealeragid pgtlrgsrtg vyagcmyehy strflelapg
      181 svegtlftss assvlsgrvs ytlglegpsl tvdtacsssl valhlavqsl rrgecalala
      241 ggvtvmaspv pfiefsrqra lsadgrcksf sasadgaaws egvgvlvler lssairngrr
      301 vlavirgsav nqdgasnglt apsgpaqerv igqaladall dtrdvdavea hgtgtrlgdp
      361 ieagallaty grgrgegqpv wvgsvksnig htqaaagvag vikmvqamrh gvlprtlhvt
      421 eptahvdwes ggvrvateev alpadrpart gvssfgvsgt nahvileavp aptgtpattg
      481 eplvwtvsak tetalraqaa rlrryaatat dadlratgra larraafahr aavv
//
LOCUS       WP_357588111             288 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357588111
VERSION     WP_357588111.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31759
     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..281
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maevgstvpr relgrllrqt reqagiglea aasdlewsra kmyriesgqt piraldveqm
       61 crlygaspet sevlislake skgkgwyhay gaviprwfql yvglesaash irtyehglvp
      121 gllqtpeyta avarsrpgit deevaklvel rlerqrvlar rrpaaptlda ildegilhrs
      181 vtgmaeqidr liaasekpnv sirisplgsk ltraavagsf vildfptqga rsaepttvyc
      241 egltgalyld rleevrayae lwnhisaeal sveasqtlmr qikerqhd
//
LOCUS       WP_357588119             224 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357588119
VERSION     WP_357588119.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..224
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24009
     Region          5..99
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
     Region          <104..212
                     /region_name="BDS1"
                     /note="Alkyl sulfatase BDS1 and related hydrolases,
                     metallo-beta-lactamase superfamily [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2015"
                     /db_xref="CDD:441618"
ORIGIN      
        1 mtyahhgdac raanaldlvg drwtlivvre lllgpkrfad lqesvrgitp avlsdrlrsl
       61 rqagivdqvt ltdlartray avtewgrgle svlaslgrwy ssgpdprtsg gmtpdamala
      121 mrtmappvpe glpptalrfy darqpdpavr dyrlttvdgl ldvrpgaavd pvatvtaest
      181 awsgvlfggl pltdaeragt vrvegdrdtv trvvrlylga slsr
//
LOCUS       WP_357588126             806 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing serine/threonine protein kinase
            [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357588126
VERSION     WP_357588126.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11600203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..806
                     /product="WD40 repeat domain-containing serine/threonine
                     protein kinase"
                     /calculated_mol_wt=80427
     Region          17..266
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(17,40..41,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,78,94..97,101,103,140,142,
                     144..145,147,156..157,160,175..178)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,78,94..97,101,142,144..145,
                     147,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(28,101,103,140,142,144,160,175..178)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(156..164,171..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <508..805
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          557..598
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          599..633
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          641..678
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          717..772
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          776..801
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 msdirplrpg dperiggyrl tgvlgsggqg vvyhgtaddg rpvaikllhs hlghdddvtr
       61 gflreveaar rvaafctaav ldvgtlderp yivseyvagd tlqalvrssg prtgggldrl
      121 aiatltalaa ihragivhrd fkpgnvlmgp egptvidfgi akaldattha sgpvgtptym
      181 speqftgerv gpasdvfswa gtmvfaatgr ppfaggtvpv ilnailtdep dltgvpphla
      241 epiraclaks paarpapadl laaltqsgap rrrpaphppp gpprrpahpd pawsvrpgpg
      301 tgqarpsgqg sysapqdagq gpaqgggggg ghagradrkp egaygaapga praqgpygpg
      361 apvppfgapg aggperalpp gpgahtasss gepetvagrg gavsrrvlig gvaataaaav
      421 safailrpgs gvfeangpad ptatgtarta spgttgttgt tgttgtatag atptategtp
      481 gaatapataa pqpvpfgsfv vepvtlprgs gtpvtlaasg arvacgtgng tvltwdlstt
      541 ataarmarlg dggaavtcva cedgdrvvsg hadgrmrvwg pdarhgagdp iigvtlaggk
      601 avaisqkydl vrdlysvarl wdvaggeqlg kpmgehfqgi galafgrldg rdvlvtadgr
      661 nrvrvrglsg ggvahdfrtg diggverlac veregrtllv sthldatlrv hdlasgkrsg
      721 kwsfgargta alvaglldgv pvavvahspg ggtyvrvwnl dtgevigell ttgpevrala
      781 laevagrpvv agagggvlyv wslggt
//
LOCUS       WP_357588131             258 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357588131
VERSION     WP_357588131.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  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..258
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..258
                     /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=27388
     Region          8..>59
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 msrvdhmdva ayalgvldeq dmerfeehla tcwacagele tmvpvvglls dideesital
       61 eqthsdpvll drtlvalrth rrrarfrqvl ataaavvvfg gltgvvfsnl tdsstappla
      121 gpttapvdtp tnrpgnpsgp nvggneqege qvdvtdpatg vdatfwlisk dfgtkmdfsl
      181 sklpgprtcr lvvvrddgst evvstwlvpd ggygtnanpq llalsaatst klddikhfev
      241 qeidsrgatd tlvtvpta
//
LOCUS       WP_357588192             402 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357588192
VERSION     WP_357588192.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..402
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..402
                     /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=42157
     Region          16..>64
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          44..385
                     /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(61,63,225,245,317)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mslllrdall ldpdtgdfte tdlrcadgrv aetgrgltap dgtrvvdlag avvvpglida
       61 hvhvtaatad lggltswsps yvaahsarim ggmlargftt vrdasgadyg ladaqaegli
      121 rgprllfcgr alsqtgghgd srgrgtrvhd dhpccaglgr vadgvdavra aardelrkga
      181 hhikvmasgg vasptdrids tqysmeelra iveeteaanr yvaahaytar avnraleagi
      241 rsiehgnlld drsvelfler daflvptlvt ywalkeegva hglpepswrk vdavlgagla
      301 aleraarggv rlvygsdllg gmhrhqnqef rlrgevqkpl dvlraatvna aellgmagei
      361 gtlavgahad llvldgdpla dlgvladpgr irhvvqagel vs
//
LOCUS       WP_357588229             256 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357588229
VERSION     WP_357588229.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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 256)
  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 256)
  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 256)
  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..256
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..256
                     /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=27230
     Region          19..255
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 msrdardevr rftltdlkle tvggsvvgnr yrdnydvlhl dstlpfavva dgmgdgegsr
       61 ragaaavstf aalvreawpd vgaerlrtvt htvqaavlea grgspqltgc tltglvvepq
      121 ggqgwvvqlg dsrayrlrdd llelvttdht vawlgllhgw ypadspaaar aryqltryag
      181 hpaapeadll avtlrpgdtw llctdgvsdq vgyhvmreal trpdpadavr tlllasldag
      241 gadnasavvl rarpah
//
LOCUS       WP_357588234             331 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357588234
VERSION     WP_357588234.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..331
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..331
                     /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=36281
     Region          11..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 meagrhegpl rsavvvnpvk vtdldalrrt vgdtldaagw peplwfettp ddpgrgqtek
       61 alaagvdvvf acggdgtvma cvdalvgtev alavlpqgtg nllaanlgls ddlaaglava
      121 vergrrlldv gevdgqhfav magmgfdaqm ldatsettkr rigwpayvvg avrhlrdrpm
      181 rvwirlddqp plrrrarsvl ianvgrlqgg vtllteaepd dgyldvavlt prtlrhwlsl
      241 gwavlrqrdr vprmevyrar rveitsnrnq preldgdlie pgrelrvqir rralwlcvpr
      301 peqdpdlaed araaaerger lveegrgere e
//
LOCUS       WP_357588242             296 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357588242
VERSION     WP_357588242.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 296)
  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..296
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..296
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31488
     Region          53..290
                     /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 mirrsrpggr peppaartaa rraaadrsgp aplrlalsap adaagltsew hmvdglrthv
       61 rrtvrkdrpg ppvllvhgla vshryltpla ailadthpvy apdlpgfgls grpsrvydaq
      121 qhsdhlaall aayrlppvcv lghsfgaeia aalavrhpea vravvlagpt sdpgarsrra
      181 qagrwlvdst realwqvpil lrdvvdarpw rvwatlshsv rnrieddltr idvpalviag
      241 ardplvpaaw rtrvaelvpg agtvsvpgaa hnvattaprq vaetvralla mnipts
//
LOCUS       WP_357588265             196 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357588265
VERSION     WP_357588265.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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: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=21598
     Region          8..196
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mahyfserpe taskpgsvdl vlpdlhlrle tdrgvfsper vdagtrille tvppppqegd
       61 lldlgcgygp ialtmasrap gatvwavdvn rrsleltern aqaarlykvr pvhadempdd
      121 vtfqaiwsnp airigkaalh emltrwlsrl apggaaylvv qkhlgsdslq rwlgeqgwqa
      181 sreasraayr ilkvqr
//
LOCUS       WP_357588269             151 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357588269
VERSION     WP_357588269.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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..151
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..151
                     /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=16233
     Region          2..140
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mqisargdya vratlslaaa ypsllstqai saeqdmprkf leavladlrr agivraqrga
       61 eggyalarpp revtvgavlr aaegplagvr gmrpeetqye gvaahlpqfw vavraalrrv
      121 vdevsladlv dgrlpahvrr lttlpdawep r
//
LOCUS       WP_357588294             229 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357588294
VERSION     WP_357588294.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 229)
  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 229)
  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 229)
  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 229)
  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 229)
  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..229
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..229
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24945
     Region          71..227
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msseaerrqa arkrnvtvsv tvigvfvlav aalfafgrpg peaveqagls agesqlvrad
       61 shrlqsaadg kvtlvefldf ecegclayyp aveelredya gkvtfvaryf pmpghfnger
      121 aaraveaaaa qgafeamyrr myetqpqwge krvpadetfr gfakdlgldl aawdrayddp
      181 atlarirkdm adgralgvqg tptfflngtr ieprtlaefr aaidaalae
//
LOCUS       WP_357588271             299 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357588271
VERSION     WP_357588271.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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
REFERENCE   4  (residues 1 to 299)
  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..299
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..299
                     /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=32842
     Region          36..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          191..272
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvpsghlata ppdaaaspve idtitlgdla pdsgwrrpvl ldrelivltt sghglaevdf
       61 ralpcrpgtl lrirpgqvlr calpqldatv vrwhpealhg ldvdadhvpn wvqlageded
      121 aiinevsqlt vdasrhrdth aarsllrhql svlllrlsml psgagrpsrp eeetfrrlcr
      181 evergyqatr rvedyadrlg csvrtltrac laitgrsakq vvdervalqa srllaatdep
      241 iarigrqlgf septnfgrff trevgmspga fraarerpap apmvrprppv darldarrm
//
LOCUS       WP_357588301              88 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YkvA family protein [unclassified Nonomuraea].
ACCESSION   WP_357588301
VERSION     WP_357588301.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..88
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..88
                     /product="YkvA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=9240
     Region          <27..74
                     /region_name="YkvA"
                     /note="Uncharacterized membrane protein YkvA, DUF1232
                     family [Function unknown]; COG3339"
                     /db_xref="CDD:442568"
ORIGIN      
        1 mtgawgwdll lgvvaallia ylalpldlvp dfipvlgyad daiivtavlr svvrraglpa
       61 vrrhwpgtdd gfavltrltg ldrppaap
//
LOCUS       WP_357588297             237 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357588297
VERSION     WP_357588297.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..237
                     /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=24674
     Region          27..227
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtprwqgwaa lrpgvlcygg rigatgphah raaqlltgeg lvlrgadgrd havraalipa
       61 naphtivrgt adgllalvdp arigqpgrgd atpgsaaawr lgpdvpvtgd ldtltalvda
      121 ltghvaprpp hpalagaera vrrmlpgrvr lsdvaravhl seswlshlft aefglpfrpy
      181 vlwarldgvw salaagatlt eaahaagfad aahlsrvvrr mmgnapstmt agvrwls
//
LOCUS       WP_357588306             328 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357588306
VERSION     WP_357588306.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 328)
  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 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   3  (residues 1 to 328)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..328
                     /product="GlxA 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=35893
     Region          4..322
                     /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 mtphrvavla vdqvvgldlg tpaqvfstar daadahfytv dtctpggrpv rstagfrvlp
       61 dhglelleqa dtvivpgvhg datlrpdvip aevtgalraa ydrgarimsi ctgafvlata
      121 glldgrratt hwayadrfrr lhprvdldpe vlfvaddrvl tsagvaagid lclhvvrtdh
      181 gsevanqaar rcvmppwrdg gqaqyierpv pqapdtstat arewarqrlh epvslrdlag
      241 qarmsvrtft rrfraetgls paqwllhert dharlllest dltveqiarr sgfgttaalr
      301 qqlhlrigva psvyrrtfrr tpesadtr
//
LOCUS       WP_357588313             518 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357588313
VERSION     WP_357588313.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 518)
  AUTHORS   ter Beek,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 518)
  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 518)
  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 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..518
                     /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=53956
     Region          2..517
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mntgtlirli lrrdrvwqpl wilsvtlfva atvttirell ptpearrdyf vniidnpaim
       61 llqgpaygds vgaaaaqqrg aattifaala sillvvkhtr sdeeqgrrel vgsaavgrha
      121 pltaalavvl ganlvlalli tvvgasaglg lagplawglm aasagwlgag laavtvqltr
      181 sartagaaaf avffaaylvr gisdlagpgl ewlgwlvpng wilrarafga erwwvfllla
      241 afvaalawla ytlsarrdlg ggllaprlgp arapaalrgp lglawrvhrg aalawiagaa
      301 fvgaglglag psvleqfgqs ggldhwarrt gtddpveiff rlvvyelavf smslyaimtv
      361 lrlrgegate lflsgpvsra rwvlghlafa aavpgamlvv aglglglgsg dvgsglaltt
      421 vvlpgvwvma gvavaayglf rragtvvawt alalaialel gwelrlvndq vfmispfahv
      481 hystladpgp gtllgltlva aaftalglyg lrrrdltl
//
LOCUS       WP_357588332             282 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome c biogenesis CcdA family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357588332
VERSION     WP_357588332.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..282
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=28398
     Region          8..181
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mslssslsea plalaltagm vaafnpcgfa mlpayltlli tgrsaapvrq alvlaaamta
       61 gfvtifglfg lvvtvlavsv ggrlpwatla igavlaglgl wllsgrelvl rlpglptgrp
      121 ttsplslygy glsyavasls ctagpflavt saalsgsgva ggmaaftaya lgmglivavl
      181 slavalaraa vvarlrrvlp yvsrvsggll alaglyvlyy gwyelrvlag qdardpivga
      241 atevqaalar wvaglgpgpl llalvlllvl aaaavrrarq kp
//
LOCUS       WP_357588363             428 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357588363
VERSION     WP_357588363.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=43633
     Region          1..427
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrvavigsgi vgaaaahhls grgvsvtvvd gaypgeatqa gagivcpwvd hwddedwyrl
       61 tregarhypg lveelgedfg yarvgallva eepadlepvr allerrraea pemgevtdvp
      121 apsalfppla edlvalhvag aarvdgravr dallhaavar gaevrpgtav ltpsgqvlvr
      181 etraadarar vharhaappr pagtwrqgdp apgapegapa egapgegapa egapsagpaf
      241 gvgreveggp ggeagealea davivaagaw ageacrplgv elpvfprrgq ivhatldgvd
      301 tawwpivlpr sgpyllgfpg srlvvgatve dvgfaprvtm ggldevlqag lriapglfga
      361 tvtearvglr pvyapgrpli grltdrvvva tglsayglta gpfagriaaa lalgeeppid
      421 ltpyappv
//
LOCUS       WP_357588369             262 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357588369
VERSION     WP_357588369.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26330
     Region          4..259
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdlrltgqta vvtgagrgig laivrtlree gmrvvagart itpeliatga tgvsvdlstp
       61 agpgelvera laelgeidll vnnvgggdgg dgqtggflgf teeqwrlthd lnflsavrat
      121 raalpsllrg sgavvnvssn garmphagpv pyttakaalt awskalaeef gpqgvrvntv
      181 spgpvltamw eapdgygaal agafglpheq llaglpgtmg mttgrfvtpd evaslvayla
      241 splaasvsga dyvvdggatk tv
//
LOCUS       WP_357588437             149 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357588437
VERSION     WP_357588437.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 149)
  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 149)
  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 149)
  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..149
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..149
                     /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=16359
     Region          9..148
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 mtapsthpvd vllllthadh vllalrdgtg yadgqwnlps gklepdedai savirearee
       61 vdvrlspdel qlvttvhhrn psgharvglv ftathnprqq geptnaephk cakiewfpis
      121 llpmntypyt taciqafsdg rplvldgwr
//
LOCUS       WP_357588498             259 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357588498
VERSION     WP_357588498.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..259
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27807
     Region          1..259
                     /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 miefgyagtp fgqihyascg rgepvlllhq sprswdeyre vlpllgrtrr avamdtlgfg
       61 asasppehsv eayaggvlal mdalgleraa iaghhtggvi aieaasrare rvtalvlsst
      121 plvdaegrrv rrerppvdha eesadgshlt alwagragfy pperpdllar fvrdalavwp
      181 dvelghrava ayrmedrlgl ircpvlvvga sadpyafpel kalagrlpga rtavieggmv
      241 plefqaeafa rviqnflde
//
LOCUS       WP_357588462            1087 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357588462
VERSION     WP_357588462.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1087)
  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 1087)
  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 1087)
  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 1087)
  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..1087
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..1087
                     /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=112740
     Region          1..235
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          178..1072
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrigvlgple vvadggpvdv ggfrlralli rlaldpggmv tsralaealw pdggpanpap
       61 alhslvsrlr ralpgrdalr sepagyrldl pgdsvdvtrf erlaaqghra lregrpdaal
      121 palagalalw rgepladaaa lpfaasaavr leelwlgale drieaelatg hrppgdvael
      181 eqltaahplr erlralhlrt laahgrqaea laafetyrrl laaelgtdpg pdlralhlhl
      241 lhgtpptplp sdppppgatp dgahprelqd rtpsvadere dqrpskgerp hgsqtphgge
      301 gphgaegahl pgsrtgpsge gpfggegrvp valtelvgre aelrliaarl aagrlvtlvg
      361 pggvgktrla iaavatggvp aearrsdpsr rvwwvglaav adagdvalav aralglrvra
      421 daveqlaeaf agarallvld ncehvadpva rlveallgrc pglrvlatsr eplridgeal
      481 cpvaplplee aerlfsaral avrpgfvpsg rvgevcarld glplaielaa arlrtmtldr
      541 ladglprgdg pfrlltggsr tasprhrtlr gvvewswdll dggvreaaer aavfpasfta
      601 qaaagagvge dalhalvdks llqldgdryr mlgtireygl lrlaesgrlr aareahaacf
      661 lalaesagpe lrgagqlgrv arlaaerdhl laalrtacdh gdadvavrlg aalamfwtvr
      721 gehaeavarl raalqvpgrs apgprrtava vfllnalmtg dlagaaaalp pgdpggsgee
      781 galgafagal lalargeads glsglepyle agdpwtrgmv wlarsllrgt dagmaagrad
      841 lvaavagfre agerwglalt lmslasveia adaydaavaa leeaeglaad lgthhelgvw
      901 vamvrvhagq pegararllr laeegepgpg gprraavarv aladlarceg dlgeagrqlr
      961 lageegdtpy rtlyaagagr lavaagelea aarwlgeala laaampdppm vaqvgvgltd
     1021 lllrrgepvr aaetlgaaea vrggpdarhp dvvrltrall vtsgrraafe rgrrldraaa
     1081 laalrav
//
LOCUS       WP_357588589             373 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357588589
VERSION     WP_357588589.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 373)
  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..373
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..373
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39407
     Region          5..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 mtegrqgpla gvrvlelagl apgpfagmml adhgaevlrv drvgavsdrp rtdvmdrgkr
       61 tigldlkspd gvaafkdlar aadvvievfr pgvaerlgig pddlhavner liygrmtgwg
      121 qdgplaptag hdidyiaisg vlsmlgregd kptppinilg dfaggglmla ygvllalfer
      181 ertgqgkvid aamvdgaail famfyqgvrg gfwgprgtnl ldtgapmydt yetadgqyma
      241 vgalepqfwd tmvrlmgltg lpdrddraqw palrerlaae frtrtraewe avfdgsdacv
      301 spvlsmaeap dhphnvarga fvesgglsqp apaprlvgap apdlspamrl adlsawgina
      361 eaaaklraqg vla
//
LOCUS       WP_357588618             469 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357588618
VERSION     WP_357588618.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 469)
  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..469
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..469
                     /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=49564
     Region          28..399
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 maalrgllsr plasyhllla saglllligl tmvfsatsvr dyaqggnasa sltkqaifav
       61 igivafwacq rlpartyral grptlavavg llvllnllva ygrltngdak igpleaellw
      121 lyiggislqp selakfalvl wgahvlarkg aalgwwrela tplfpvvgll fvlvgyndlg
      181 smlcllalvv gllwaagvrl rvfaalsaig llgigllvav aslgagsgvr geenyrlarl
      241 tvffspppld ackeqlcyqm vqaryaiang gwfgtglgqg rtkwawlpaa endfifavia
      301 eelgvvgcav vvtlfavlgy tglriarrve dpfrrlaaag atawlvgqaf iniggvigll
      361 pltgvplpfi sdggsalvvt laavgmlasf araepdaara lharpparwv rlvwaplppl
      421 pgrrrrvapp stargsvpqa rkrrrddqaa prgtrdgrgr ggsaderrr
//
LOCUS       WP_357588612             381 aa            linear   BCT 28-DEC-2024
DEFINITION  branched-chain amino acid ABC transporter permease [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357588612
VERSION     WP_357588612.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 381)
  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 381)
  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 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..381
                     /product="branched-chain amino acid 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:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41668
     Region          60..366
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mreldrsrvn alhsvadrwk alpkwqrsla fvafvvflyy lpllgipglt wlrtdsisgg
       61 snwagvlftc avyvlvaigl nvviglagll dlgyigffai gayavalfgs vnspvvqyfq
      121 refdlpptwa vtwaicafia lvmalisgvi lgwptlrlrg dylaivtlgf geiirivarn
      181 megvtrgpqg iaaipgpegp pssdnqifgl idikpwywla itvvllmvfa vrrlehsrvg
      241 rswlairede daaavmgvyp fkfklwafai gaalggfagf lfasryafid ptqfnvnlsi
      301 lfvamvvvgg sgnmvgvsvg avllaylper freiadyrwl afglamvlvm ilrpqglips
      361 rrrarelkdr aaeaeeapah v
//
LOCUS       WP_357588647             407 aa            linear   BCT 28-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357588647
VERSION     WP_357588647.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 407)
  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 407)
  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 407)
  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..407
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..407
                     /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=42208
     Region          21..393
                     /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(31..32,35..36,39,71,121..122,124..126,129,148,
                     151..152,155,225,228..229,232..234,237,264,268,317..318,
                     321,325,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 mtvlaapesr grtnslawll vlgivlaaln lrtavtsvgp lldqlaaglg mtsvgtgllt
       61 tlpvlafatv gaitptlahr vgqhrlllla lvtlgagmlv ralvdsapvf llssavalsg
      121 gavgnvlips likrhfpart gvmttvytta latgtmlaaa atvpierasg dwhvalgvwa
      181 afaaiaavpw lallrseper akaragagmr slarsklawt vavyfgtqsm iayimfgwla
      241 tiltdsgytt aqagmvlgvf talnipvsil ipvvasrfrd qrpivvglvv ayvigffglw
      301 fapastapvw vvfvaigmgs fplaltmlal rtrtpeatga lsafgqsvgy lisgagpllv
      361 gvlreagggw alpytmmlvv ivvqlvsgly agrnrylede rsarmtg
//
LOCUS       WP_357588659             201 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357588659
VERSION     WP_357588659.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=21594
     Region          10..201
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mtgdhyftae pnapaqarev qftvagrdyt lvsasgvfsa srldpgtavl lrkaeppapt
       61 ttgalldlgc gfgpiacvla tvaptattwa vdvnerargl taenatrlgl sgrlrvtape
      121 evpadlrfaq iwsnppirvg kdelhqlllr wlprlapdgv awlvvarhlg gdslqswlve
      181 qgwqvtrhas qkgfrvlrvt r
//
LOCUS       WP_357588651             229 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357588651
VERSION     WP_357588651.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 229)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..229
                     /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=25122
     Region          11..140
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          81..223
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mssvwsrpap qrrpaltrea ivaaavavad aeglaavsir rvaaelgara mslytyierk
       61 edllalmlde isaeldtgep lpadwrealv qlaraerdlv rrhpwrveli sqpvavgpng
      121 lrhverrlsa fdglgldrlq twramaavvd yvtgfvvrea aerarpradg vndaeraala
      181 epyirdlvat gefprlapmi eqgvrgaddt ferglrwvld giegdlpgr
//
LOCUS       WP_357588888             871 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357588888
VERSION     WP_357588888.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 871)
  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 871)
  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 871)
  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 871)
  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..871
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..871
                     /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=89541
     Region          24..849
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 magqvqvadg dvrrestvaa epgtglsste aarrrqadgp naaaapprrh latrivhqlt
       61 dplvalllaa avvttvlrdy pdtavillvv avntaigvvq evradraiaa ldqlaaptar
      121 vvrdgrdavl patelvrgdl vrveagdvvp adlllhdanr lhldesaltg esvpvsraag
      181 eeasagtvvt tgraagtvvr tgaasalgri atlaattrpt atplqrrlas lgrilglaav
      241 alsglvfavg vvsgrplvdm avtavslvva avpeslpavv tlalalgarr maaaraiprr
      301 lhavetlgsv tviasdktgt ltegrmavqq avtgdgtrfg vtgsgyaphg tvhrdgapva
      361 vpdelrrlar agllcndatl appteqrprw gavgdpleaa lvafaarcgl dpqttrnawp
      421 rvaehpfdqq lrrmttvhrs cdrrylvvck gapenvltap lldadadela altaaahrla
      481 gdglrvlala aalvdhppad panpeglrpv glvavgdplr agapdiadgf adagvrlvlv
      541 tgdhpataaa iagqlglwte gdpvvrgddg dpaeappatr vfartqpeqk ldiiaglqsr
      601 ghvvamtgdg vndapalrra digvamgggt evarqaadlv lvdddlstva taigegrriy
      661 dnirrflrya lsggvaeiav mllgplfglp vpllpaqilw inllthgvpg valgaepaep
      721 gtlrrvprsp qesvlgaglg rqilvggali aavtlgagvl aahwdrpwqs vifivlglaq
      781 lgvalavrap rppgqrrgnl alplavavsa llqvagvllp qlrellgtea lgvtellacg
      841 avsvlpglvl rltrrrprtd dgmsaypdav r
//
LOCUS       WP_357588938             503 aa            linear   BCT 28-DEC-2024
DEFINITION  deoxyguanosinetriphosphate triphosphohydrolase family protein
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357588938
VERSION     WP_357588938.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..503
                     /product="deoxyguanosinetriphosphate triphosphohydrolase
                     family protein"
                     /calculated_mol_wt=55177
     Region          26..490
                     /region_name="Dgt"
                     /note="dGTP triphosphohydrolase [Nucleotide transport and
                     metabolism]; COG0232"
                     /db_xref="CDD:440002"
ORIGIN      
        1 meppveprar rlfggsaral gdlatspfra drdrivgspf ftrlggvtqv vspggsgllv
       61 hnrlthslkv aqvaraiaer ltadghqrdl veklggcdpd vveaaalahd lghppfghlg
      121 ervldrlarh rlgltdgfeg naqsyrivts teirgaattg ldltaavraa mlkypwtrld
      181 hpdphprtmd ppprgatppp ddpdsgsakf gayrtelddl rqarapfagr iadwqqtvea
      241 svmdtaddia yaihdvedfy rvgvlqqgav aaelmawqre gghlraitds alatsarrpg
      301 ssierlrrql hhkdawiadd eafaaavehv reelveglla lpfdgsieae qyvarfsarw
      361 ttrfvdaitv veqpavrsgh vllapaqwhe vqvlkfvhhr fvlarpdlal hqrgqarlld
      421 tlvealrewl ldpeeesrlp rrlhdlvela eaelhprtpd rigkargrai vdfvaqltds
      481 qavamldals grsgalwtda fvl
//
LOCUS       WP_357588997             208 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357588997
VERSION     WP_357588997.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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..208
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..208
                     /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=22005
     Region          4..203
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mltadeffli ahndtrgkak lhpaatslgl aggllgelvl yghitvsagq vgvidrrppa
       61 dalahtvldq lvgeaqhqsv rtwlsflaqt svnsvgdrls ragvlrrqes rrllrtavty
      121 qpidlnvvaw patrlralle raeppsvpda tllglvaaag ltrevlwsag prahhrlnli
      181 ipalpaplke lvahteaavg aavlrgap
//
LOCUS       WP_357589040             537 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357589040
VERSION     WP_357589040.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..537
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..537
                     /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=56278
     Region          10..502
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mtspgshgae radavivgag hnglvaanll adagwdvlvl eatgvpggav rsaevtapgy
       61 lsdlfssfyp lgfaspvlrg ldltrygltw rhapdvlahl fpddraavln rdpavtaasl
      121 etfapgdger wltayeqwqq vadpmmqlit tpfppvrggl gllrrlrvgg slrlarrlvl
      181 pasrlgeelf tgaggpalla gcalhtdlst eeagsgvygw llamlgqqvg wpvpeggaqk
      241 itdalvarlt erggrilyga rvdrvlvarg ravgvrtvgg tnwrarravl advpapalyl
      301 dlvgpavvpp rlvadlehfr wdgstlkvdw alsapmpwtn rslatvgtvh lgadlngltg
      361 yaatlalgel ppdpfllvgq msvadpshsp pgteslwsyt hlpfrrhwra ddimahverm
      421 eavleaaapg frglvvgrhv agpaeleean pslvggalgg gtaapyqqlf lrpvpglgra
      481 dtpvdrlfla sasahpgggv hgapganaar aalardralt ggwyqramat ahravya
//
LOCUS       WP_357589261             145 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589261
VERSION     WP_357589261.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 145)
  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 145)
  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..145
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..145
                     /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=15755
     Region          2..117
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mernlslnlh vllarldraa drmlraehdi sysrflaltl iselgvstqr aladglgvte
       61 psvsrmtavl aadglldvqp dpaggnrrql sltgkgerlv aslrqefeek laalvehsgv
      121 pyaefaehta rllatldrve reaar
//
LOCUS       WP_357589307             533 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Micromonospora sp. NPDC049891].
ACCESSION   WP_357589307
VERSION     WP_357589307.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 533)
  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..533
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..533
                     /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=56815
     Region          21..531
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mstldtaidr sspafranrd allerlaeld aalataragg gekyvtrhhq rgkllpreri
       61 ellldqdspf lelspvaafg tdfpvgasvv tgigvvegve clvvandptv rggavnpwsl
      121 aktrrageia lanrlpmvnl vesagadlpt qaeifipggr vfrdltrlsa eriptvsvvf
      181 gnataggayv pgmsdytimi rdrsqvylag pplvkmatge daddeslgga amhastsgla
      241 dflaaderdg irlarqcvrr lnwrkqgpap rnpmpqppky dpeellgias adlkvpfdpr
      301 evlarvldgs efdefkpayg talvtgwgel hgypvgvlan argvlfsaea qkatqfiqla
      361 nasdtplvfl qnttgymvgt eyeqqgiikh galminavsn stvphltvnl gasygagnyg
      421 mcgrayeprf lftwpnaksa vmgpaqlagv lsivarqaaa argrefdeds daamrmmveq
      481 qiesqsgalf lsgrlyddgv idprdtrtvl glclsaihng pvkgadgfgv frm
//
LOCUS       WP_357589310             530 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589310
VERSION     WP_357589310.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..530
                     /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=54830
     Region          8..530
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 msatmtrgga ltgtgillgl alrrdriklp awtliialfv pyfatvaart nptpealrrt
       61 mdmmdvpmlr lftgpsygtg dltvqrylia vyfvefllga almnilliar htraeeqtgr
      121 aeliraavvg rhapltaall lsvittavla glmtvtaiga glpagsallf avataatglv
      181 fagvtavsvq lteharaaag iaggvlgvvw virgagavqd tegggltwls plgwsqltrv
      241 laderwwplg lsaaltavlv taayalaarr dlgagvvatr pgpasapgwl rspaalslrl
      301 qrssilwwsg slvagglvfg alagsmrdgl atdfldagpd vlsgylslmv vgmsfivgif
      361 ailavtrlrt eevrgriapl lttptsrwaw lgssllvtaa aavtllalsg lalgagaals
      421 lgdggyvgel tgavlarape illllaitla lygfaprava vawavlaygg fvrfwatdlp
      481 aalkvlslfd hiprmpiegf tpaplvtltv laagvtllgl ygfrrrdldg
//
LOCUS       WP_357589422             234 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357589422
VERSION     WP_357589422.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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..234
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..234
                     /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=24810
     Region          39..194
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mrepagrqpp gwlgpllgrl dtartedftq lrtpdrggre savlvllged attgpdvlvl
       61 qraatlrnha gqpafpggaa dpedadaaat alreaneevg ldpasvtvla qlprlwipvs
      121 dfvvtpvlaw whaphpvdsr epaevahvar lpiaelvdpd nrvrvrhssg wvgpafsvrg
      181 mlvwgftagv laallemggw srpwprsrvi dlppvgaspa psagtdevde salr
//
LOCUS       WP_357589461             656 aa            linear   BCT 28-DEC-2024
DEFINITION  YncE family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589461
VERSION     WP_357589461.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 656)
  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 656)
  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..656
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..656
                     /product="YncE family protein"
                     /calculated_mol_wt=68873
     Region          7..194
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <105..>289
                     /region_name="COG3292"
                     /note="Periplasmic ligand-binding sensor domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:442521"
     Region          286..518
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mlrsllvvva gllpalvspg aasaapsrcg dpavttygpa svtaaivgaa vhegrayvvs
       61 rgpkppviae idlatrkvvr satlpdgpad gepeggwava vsggkvyvgt ypvpdlysfd
      121 iatgevahlh sfgkvggfvw slaaapdgtl yagtssdgrv weyvpgtgav rrygvlaqge
      181 hyvravaadd ryvyagllek kllvrvdrvs gevtrlaeag aafgvvtlng drvvaaagpe
      241 lidvrkdgtd lrrvtvetgl ldaltpaadg svyaasrpdg avhryrtgds altrvaapps
      301 ygdetrllhv tgenavlsfa gsgglwaldg gtgaaeftdl idagmpagae rtqsmvlvpg
      361 ravyagghfa ldirdlrtge qrrirvpgep kamvragdkv yaamyptgei vsvdvrtdev
      421 rslgylghdq krpwdieydp rtgkllvats slsasvpgal svvdprtgak dvyagvipgq
      481 nlmslaldee rgvvylagdv fgtstptasv aafdlarrtv lwqadpmpgh rtfqdvklhk
      541 gllyasfkre sgawmamdpe trqvvrqgti sgygeltthr grlfasvfrg ggnayeldag
      601 rgatllatgl gdewhtnpql hfepgswnaw aivgrdlarv rldprcpplt lpagts
//
LOCUS       WP_357589490             542 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589490
VERSION     WP_357589490.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 542)
  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..542
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..542
                     /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=57434
     Region          21..140
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          280..540
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 meppvrlast gtiihgvsvg evlgvstlag arliagergl grivqrlnvm evpdilawvk
       61 phelllttgy plrntpqslg rlvadlderg laalgiklgr yvdelpaema eqaerlgfpl
      121 illpndvgfd dilnqvltdi lnrqaavlvr aeeahralvq vvlaggglde vtaevaalld
      181 vavaavdgrg rvlaaagpre hvaalresaa hdglpasagq gqpgqpgagp rgrvmasvpv
      241 tagghhhgri vayspagair dsdvgilera atvaalavtr qeavhavesk yradflrdvl
      301 tgragtaerv aararafgwd lerpvtvlva eldpdsdert aqdrlvtcwt aalrrhdpgg
      361 avagfshevv avvgaevdas rlardaaagf advppatfst gtsrpspgva tlpeaytqal
      421 kaarvgrqlh gpgavahfdq lgvyrllslv sdtdelhafv ketlgplssd tdaenadlrr
      481 tlqvlletnl nvaetarrlh fhyntlryri gklerllgnf tddphlrlnl tlalhvlrmr
      541 gi
//
LOCUS       WP_357589524             276 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357589524
VERSION     WP_357589524.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31074
     Region          6..68
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(11,15,40)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(14,39)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(21..22,33,36,40..41)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          92..271
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mlrillgtql rrlrtergis redagysira shakisrlel gqvsfkerdv adlltlygvt
       61 dpderaplia lakqanapgw whkygdllps wfevyigleg aasairtfen qfvpgllqsp
      121 ayaravielg neraapdeld rrvqlrvarq rrltgddrln lwavideavl rrapggpeam
      181 reqiehllam taernvtvqv mpfdrgghaa aggsfsilrf perelpdvvy meqltsalyl
      241 dkaaesehyv kvmdrlsvqa qepkesrrfl eslldr
//
LOCUS       WP_357589534             295 aa            linear   BCT 28-DEC-2024
DEFINITION  sirohydrochlorin chelatase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589534
VERSION     WP_357589534.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..295
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29431
     Region          21..283
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 madgagqggp lgsppgggvp lvavahgsrd praaatveal leevrrarpg lpvrgayldh
       61 saptlaqalh ghaeavvlpl lltaayhsrv dlpaalnear ardpllrvhy gdtlgphpll
      121 vsvlerrlee agvtpgdpgt avvlvsagss daranavvad lartwrpspg rasgplsdpt
      181 sgplsgplgg plggratgpa sggggwwavt aayasaagpt paeavallrr agaprvavap
      241 yllapgyfad kvrrdtlaag advvadvlgp apelaqvvlr ryeaalrapv daaas
//
LOCUS       WP_357589539             289 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357589539
VERSION     WP_357589539.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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..289
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..289
                     /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=29277
     Region          3..278
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mcdllviggl gvdvrvrvpr lplpvvdsvt vdpielrvgn tgagvvlaah alglrvtvvd
       61 tvgadpagav vraalagtgv rtvladdpag trrsvnlvdp dgrrmslydp rapegpppfa
      121 aaqlaelvrd athvhlsimg wvrellpdlg dvlgegvgts tdlhdwdghn ayhrpfaeva
      181 elvlisgaal gdraaavagt laprpvlvtr gadgadlhlg ggvqripaav ppgpvidtng
      241 agdafaagii aarsrgatwa eaagyasrva aaacthdgme yppallpra
//
LOCUS       WP_357589619             283 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589619
VERSION     WP_357589619.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 283)
  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..283
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..283
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29221
     Region          4..189
                     /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 mtvpatgrlr vagatlhyev rgqgplllli pggagdaasy dgvadvlaag wtvvsydarg
       61 msrsplddpg aeqhvashad dayrliells pgaparvagc ssgaivalhl lathpdrver
      121 vvaheppvve vlpdaaehra mlarvqdtfr reglmpavae faaalrrpgg aepagpaesa
      181 apaelppgaa araertmanl pyflgrivpa fmayapdvdr laalagrlvl aagdesrgel
      241 pyrpaaclav rfgtelvhfp gghtglsthp aafaellrkt lag
//
LOCUS       WP_357589600             341 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357589600
VERSION     WP_357589600.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 341)
  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 341)
  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 341)
  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 341)
  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 341)
  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..341
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..341
                     /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=35604
     Region          31..321
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mfgsekelee rlatpsaalv adaarldgdl vllgaggkmg pslarlarra ldaagrsgtr
       61 vhavsrwsde aaaralredg vdvvrhdlmg gddlaglpda ggvvflagak fgtsaepyra
      121 wavnaalpaa vgrryrdaai aafstgnvyp lvdvtrggsa eddepgpvge yamsclgrer
      181 vfehaaavlg arvailrlsy avdlrygvla dlasavrdgr pvdvttghvn vvwqgyanev
      241 alrsllhara pepfvlnltg petasvrraa trlaallgag prfageesgt allsdasrch
      301 glfgypdvpl dtlvawqaaw ltrglplagk ptkfsvrdgr f
//
LOCUS       WP_357589629             407 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589629
VERSION     WP_357589629.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 407)
  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..407
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..407
                     /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=43820
     Region          24..401
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(54,61,89..90,97,101,108,237..238,241,245..246,249,
                     282,287..288,291..292,294,317,344..346,349..350,352..354,
                     358)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(61,83,85,88,90..91,171,179,236..237,240..241,245,
                     288,291..293,392)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 msttepqild lmtaadrdaf ltglagngpv srgryldgtl iwlvtgydec vtaltdprfs
       61 sdisrqskld vaaaaglpdd vapyllrtlg aydppdhtrl rrlvsrgfta rrverlrpri
      121 qeitdalldg lpaefdlier fayplpiqvi cellgvpsad rdiwrawagd ltapdparia
      181 agarglvaym selvaakraa gtdgvdgaed llsalvrvqe ddgdrladee lvalgismli
      241 aghettvsli sqsvrllltr pellarlrdd rdavpaavee flrvtgpaei avmrytlepv
      301 elggtripag eavqvvyaaa nrdprrfdrp elldvgrgdn ahlgfghgih yclgaalara
      361 etqialrtli drfpglelav paaeigwrpg mqraltalpv rtdggas
//
LOCUS       WP_357589637             397 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589637
VERSION     WP_357589637.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 397)
  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..397
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..397
                     /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=40689
     Region          6..388
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mttlntitvv gaslaglrav qtlrgagfag eivvvgaerh lpynrpplsk smlrgddeit
       61 lpgaeelgdr wlrgrnavrl dtagrlvtld dgtqvrydgl viatgarprp lpdalegvht
      121 lrtvedalal raelaaghrr vvvvgggfig gevastarsl glavtlvdaa pypmsgvlgd
      181 lasrwlaghh rsngvdlvpg rrvtglegag rvsgvrlddg rtlpadlvia atgvvpetgw
      241 lrgsgltldd gvvcdaalfa agadgvvaag dvarwphary ggasvrvehw ananeqgaaa
      301 alnllagred atpyaglpaf athvhgvrvq taglphlade arvaagdpee grfavafara
      361 gtlvgvvgvd aprdfvrikr avaagdples vlaasmg
//
LOCUS       WP_357589673             332 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357589673
VERSION     WP_357589673.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..332
                     /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=36362
     Region          24..322
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtstnptldl aggasappag prparrssar aaetrrkwye iiglttpavi vyvmfvlvpm
       61 gfafyyslfr wrgvgpptdy vgfdnyvlaf qdpifldalr nnaiivfgsl liqgpialgv
      121 alllnrnfrg rtvfrllafv pyvlaevtvg imwklllsda gtvnamlesi glgslvqawl
      181 adldvviwtl lavltwkyvg faiilllagl snvpqelnea aaidgaswwq iqrhvtlpll
      241 gptiriwmfl smigslqvfd viwvtsvpav rslgasatma tymvdngffa rlwgygnava
      301 vilfaisfva avlfqrfllr rdiegaitrr an
//
LOCUS       WP_357589736             229 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357589736
VERSION     WP_357589736.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=24718
     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 mrvaiagagn vgrsiaqeli enghqvmlie rqprmlrpar vpdaewvlad acelasleea
       61 elagcdvvva atgddkvnlv vsllaktefa vprvvarvnr aenewlfteq wgvdvavskp
      121 rvmaalveea vtvgdlvrlm tfrqgeanlv eitlpptapy vgrplrdvpl prdsalvail
      181 rgkrvlvpsp ddpveagdel vfvctaemed avravvlgpd svertresr
//
LOCUS       WP_357589738             220 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357589738
VERSION     WP_357589738.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 220)
  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 220)
  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 220)
  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..220
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..220
                     /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=23524
     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 mhvvimgcgr vgstlahnle srghsvavid qdadafrrlr pdfagvtvtg agfdgdvlrq
       61 agieradafa avssgdnsni isarlaretf gvvrvaariy dqrraqvyer lgiptvatvr
      121 wtadrmlrhl lpegnveifr dptstvsive vpvhkdwigr pvraledatg arvaylirfg
      181 igtlptassv vqegdqvfml vtddmvaavt svaatpeggq
//
LOCUS       WP_357589742             406 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent RNA methyltransferase [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357589742
VERSION     WP_357589742.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..406
                     /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=42642
     Region          8..404
                     /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 msgleeaerv eltvaavapg ghcvarvdgq vvfvrhalpg ervlaevtev hrsfvradav
       61 tvleaapdrv tppcpyarpg rcggcdlqhv apdaqlrwke avvreqlirl ggldeagcda
      121 lglrvtalpg gslgwrsrvr yavdaagrag llkhrshevv pvdrcliahp aiqelpvlta
      181 agaswpdaea vetvastggd vavtavaags srrvsgperv reraagrewv lptssfwqvh
      241 paaadtlvda vleltgprpg erawdlygga glfaaaladr vgetgrvtlv eaagdgvtaa
      301 renlrdlpav evvaarveta larrrvtgpv dvvvldpprt gagtrvvrdv vaagpravay
      361 vacdpaafar dlrgftelgw rlaalrgydl fpmtrhvelv glltpa
//
LOCUS       WP_357589787             326 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589787
VERSION     WP_357589787.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..326
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..326
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=36240
     Region          21..310
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mtadidlgyv tddargdgwh lmlgdacerl aeietgsvgl svcsppfaql ynyspsprdl
       61 snsgsrdeff ehysyvvreq lrvtapgrla cvhvqqitlq kvmhgviglt dfrgqviaaf
      121 qdagwifhge itvdkdpqaq airtksqsll fvtkerdssa lrpaladyvl lfrapgdnqv
      181 pvktdvtnee wiawarpiwp svgdaaaiea mrelglampr pcwydiretn tlntrvaked
      241 aderhicplq ldliercvrl wsnpgelvls pfagigsegy valkqrrrfa gvelkgsywk
      301 tavdnlrtae hemaipalfd adefas
//
LOCUS       WP_357589770             143 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357589770
VERSION     WP_357589770.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (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   3  (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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..143
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15887
     Region          15..133
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtttkaaqrq aqareeynaf lavcpsrqll drisdkwvvl ilcalggdaa qrpdasdapr
       61 amryselarl lagvsqkmlt qtlrslerdg lltrtvtptv pvtvtyeltd lglslhrttr
      121 eirywaqahm gevlahrddy das
//
LOCUS       WP_357589789             511 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sp. NPDC049891].
ACCESSION   WP_357589789
VERSION     WP_357589789.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=52839
     Region          23..503
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mrklaprpal laastaavav aliplvylav rtaeagadri aaelwtervg llalrslgla
       61 svvtvacvll gvgtaflvtr tdlparrlfa vlaalplavp tyiaafawvs taprlegfwp
      121 aalvltlcsy pyvllpvaaa lrgadpaqee vsrslgrsgw rtftavtlrq vrpataagal
      181 lvalyvlsdf gavsilraet ftraifvsfd lgfdrtgalv lssvlvaltv lllggetttr
      241 rrgaryarls garrpasrls lgparwpama alvvvavlal gvpaaslgrr laagtsrpga
      301 lpevltaagn sltvslagaa ltmllalplg llaarapgpl ttaldrlayl ghalpgvvig
      361 lsliffginv ayplyqtrwl lalayatlfl plavgavasa aaqsparlee varslgrgpw
      421 tvlrtvtlpl ilpgigagaa lvfltgmkel patlllrptg tdtlatelwt stavgayaaa
      481 apyavllvvi salptwllva rsglldkekr a
//
LOCUS       WP_357589806             338 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357589806
VERSION     WP_357589806.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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..338
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..338
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35081
     Region          <31..198
                     /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 matgqlided paealahala arrlasrisa vreavglaay hagewqsaia elrtyhrmsg
       61 aqshlaviad seralgrper aidlfrgadq ekldpavaie llivaagarg dlgqrdaava
      121 mlqvpdlttd avqpwtarlr yayadallav grraearewf sraaevdtea etdaaerlle
      181 ldgvviegdd edevteelva gpgapgavpa rpdagpstta evsdqddpag sdlasdepqa
      241 daavvgkpng ddvaveertd dhpiddqsad dqpagaefpa qsqavdasgp dgerdaadgd
      301 vaedvapdie aapgaapeva eldadpadgt depearqr
//
LOCUS       WP_357589848             380 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589848
VERSION     WP_357589848.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..380
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..380
                     /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=39948
     Region          20..319
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mppargfvrr iadatpadrd rgvdalrala ilgvvlghwl vtavvadsgt lrvtsplkql
       61 peltpltwll qtlavfflva grvstqgyvr araaggtypq wlgprlarls rpvvvvaavw
      121 avaavamlaa gadqdtvwal vklvwsplwf llvlalltal tplaarlspw wplvavalgd
      181 lvrkglddpa pgwvegvnvi cgwlvpyclg aawaqgrprg raarwgllag gavvaaglva
      241 wggypaamvg vpgaavsnla ppslaavafg laqcgaamll agplrralrr prlwagvalv
      301 nvgamtiflw hqtamiavta valtsgtavt glhtvpdgfg wvawrvawlp afaaalavcv
      361 lafhayerrr pprrrrtrpg
//
LOCUS       WP_357589880             659 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589880
VERSION     WP_357589880.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..659
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..659
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=68987
     Region          2..137
                     /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          404..651
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mthlpwscwa papapdrsav vygsdrdgtp rawirparge prpvptgphp ivdvhwaptg
       61 arlavllapg ggehtevwtv rpdggdlrpl aappggsavf irwtergedl lvaethaggr
      121 tdavivdaat ggrqivasgp llrpaavsrd hatvllrhgp rgarrmsvrh agggehella
      181 glpgttdygi lapdghtayl ltdagrdrta lvavhgdglw qasdegpwqg tlggpdggpg
      241 ggpgggpggg sggglwagsg gglrhgsgga llrgsdgglw qgsgggirrg lgepevlaer
      301 adaeldqfal sadgrhavlv wnehgrsrle lldprtgltv plpglpadvv tsvrvsldgg
      361 vavlaaegpa qpsqvyacdl qtgayehvag agrlpeavea epvrfpardg lglaawlyrp
      421 arargaapyv vhlhggpedq erptynplyq hllahgigvf apnvrgsggy grafreaddr
      481 errfravddv adcvaelvrl gaadpsriac mgwsyggylt laalvahpal fragvevcgm
      541 adfatfyert dpwvaaaavr eyghpetdrd llralsplra fdrlrapllv vhgrhdtnvp
      601 fhqaeqvlaa aaalglpcds llfddeghhi rqvanrvafi skvtgwlehq llgsfadra
//
LOCUS       WP_357589911             556 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            sp. NPDC049891].
ACCESSION   WP_357589911
VERSION     WP_357589911.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 556)
  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 556)
  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 556)
  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..556
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..556
                     /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=58296
     Region          117..551
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtstregafa datgewadeg rsgrpatgvp lptppvdael arelldglde avlttngagl
       61 vglanamage llpdvvvgtd larsplaaav atgadefege hlgrrlrgvr ralggnrsaw
      121 yvrdvtdeha raeellaerr rtrflarsgr elglalerdq alravatlpv pyladlalvv
      181 hlpptpteyr phwvrhaadd tapasgavew dvvaavpglv ealdgeptdp rrwpgtgreg
      241 fdpllpagfg ppatllvspm pgagrtagal vllrrserag fdrrdvelvr efaaragaal
      301 ttaqlhdeqs hlarvlqnsl lppklptvag mslaggyraa gdslriggdf ydvlptdgga
      361 lfavgdvcgk gvgaavltgr vrqslqtlrl veqqprellr lldqalldip dasrrgqltt
      421 lllgalrpgp egelrvriag gghpaplvir adgtvtavrv ggmpvgalpg arftatdlll
      481 spgellftrt dgvaearggp hgteifgerr lrralaagag lspaalvdrv lrevdtwcag
      541 hrhddiamla igptgd
//
LOCUS       WP_357589920             986 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357589920
VERSION     WP_357589920.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 986)
  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 986)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 986)
  AUTHORS   Rosinski,J.A. 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 986)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..986
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..986
                     /product="helix-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=103643
     Region          <2..913
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          929..985
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msttlygraa eqeavrrlld garggdggal avlgapgigk tavlelaasl vneftvlrar
       61 gvrqeahlpl sgldallrpv adrvrsgvlg ralrtgvagg gvalpvavle flrelaaeqp
      121 vlvrvddvhl ldrasreavc faarrlager ialllsartp gdppvpddvp vlavgplddt
      181 ashalardll sgraseglca clvrvahgnp lglrelaesl taaqlaglap ppdtlppdgr
      241 lhrahaerla glpdearall lllaaapglp tsdllqaaed ppcarptaap lgarqttdws
      301 avrtgdpvai pappsrradd ppaeaapvrs tdplavlava eragvirpdg dryvfadetl
      361 ravayaeapl arrrevhrll grqltglpga whraaaldgp pdelaadlaa aastaarttp
      421 yapapppiya psqshtpgti hepttdnaaq gpggpngpsg sggghchptp slayeraaql
      481 ggdeaskaaw laaaarhawm sgdfprarsl laglhrpvvt deaelmygrl ellsghadsa
      541 sakllaaaar lvdrdrlvav kallhaaeas ymsgdirtfh aiahqaallr rsddcqdtql
      601 mfeylegiaa tfsgrhraaa gplwrvvala pavrnpttlv wacvaslllg edataielsa
      661 raidtarrrg avsvvpqlle sliqaefwlg ryssvathaa dglrlaqasg qlnsaarhlg
      721 wlahaaavqg daqgcrerah aaldlaeshg lgiatslgnw alahldlatg rpaeaaaklr
      781 ghrgndhvvi rvmasphfie aaartgdrrr asaalrvldr wagstrspdr ralvarcral
      841 latggeagel frealelhac pfetartqll ygvalrrerr pgaarehlhg aletfqrlga
      901 glwserarte lrasgetvvp iapadgperl ltaqqlriar lvaegatnre vaaqlflspr
      961 tidhhlrnvf aklgvrsrve lsrlls
//
LOCUS       WP_357589976             298 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357589976
VERSION     WP_357589976.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   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 298)
  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..298
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..298
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31882
     Region          30..289
                     /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 maepvphwpg rmvgdvhvrs tppgapeqav fvhglagaat nwtdlmdelk ddvtghaidl
       61 pgaghspapa dgdysvaaha aavvrlleqv gpahlfgnsm ggavcvrvaa grpelvrslt
      121 lispalpdll prsgpvrvaa aatprlgewv asrlklipae qrinasfavv wadmaavhpv
      181 rlreaieeqr rrdelpysaa amigsargiv aeyfrrgadn lwrqaekiqa ptliihgrhd
      241 rlvrpamaar aarafrdlrl vllpraghva mmevprvvaa earrliretr lgnaplpg
//
LOCUS       WP_357590071             302 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357590071
VERSION     WP_357590071.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..302
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..302
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32342
     Region          15..299
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mlfepvstel sfehdgdelv gdlvrpptpg pypavvfveg sgpggrdlge wptrlaaagf
       61 aslaydkpgs gastgdwtrq rltdraeetl aavralrqhp dvradavali ghsqggwvap
      121 laasrsdtva avvcvsgpgv gvlaqeeyrl rhqlpaegft eadveqaltl lheqirrvrs
      181 gddpvrvhaa qapwhtapwy ttlagttpps iaflagiadh dpttalrslt cpllaiygae
      241 dllvpvresa rvvatilrea ghddheivvf pgadhnlrvg tarapgfdel vvtwlhrrly
      301 hr
//
LOCUS       WP_357590078             194 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Nonomuraea].
ACCESSION   WP_357590078
VERSION     WP_357590078.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=22059
     Region          14..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mardenrrit dlgtlkalah plrlklyral shagtatash ladqvdeavs lvsyhlrkla
       61 ahglileaep qsadgrerww qidrglqiqd rdfrdapera aayasftrla frehnelyer
      121 yldeqsawdp ewraaafssq ylprltadel trlndelaev lrrweahats aaeagdvegr
      181 envvlhlygf ptrp
//
LOCUS       WP_357590147             108 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357590147
VERSION     WP_357590147.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     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=11606
     Region          6..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdelldrata qtyaswfral adptrvqive ylarhnrpms vgeivaavgl aqstvsqhlk
       61 ilaevrfvlv epagtarhyr indacvdcfp saadvvmgrp aptpngac
//
LOCUS       WP_357590154             375 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357590154
VERSION     WP_357590154.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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..375
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..375
                     /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=40057
     Region          32..348
                     /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 mtaqvdpvii igggqaglaa aratlaaglr pvvlhadtep vgswpgyyds ltlfsparys
       61 alpglafdgd pdhyphrdev laylrryaat ldaeirtgvr vtevhphagg gylirtdagd
      121 eiaaagvvaa sgsfgnpylp dlpgrsdftg gllhvadyrr pepyegkrvi vvgagnsavq
      181 vayelaahah vtlatrepvr flpqriggrd lhhwlrvtga drlprriltr lirhaavldt
      241 gvyrkaitsr qlarrdmftt ftpdgvvwsd gttdavdavi fatgyrpdlg yleplgtvaq
      301 gtprqvggls tthrglayvg lefqrsfasn tlrgvsrdat hviralaahl sgrrrlprsa
      361 mvptsarsgt agapr
//
LOCUS       WP_357590155              69 aa            linear   BCT 28-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590155
VERSION     WP_357590155.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 69)
  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..69
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..69
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6758
     Region          1..45
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mprydyrcra cgstfelsrp msaaddpatc peghadtvkl lstvamtgsa atprptgggg
       61 gccgggccg
//
LOCUS       WP_357590159             168 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357590159
VERSION     WP_357590159.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 168)
  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 168)
  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 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
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Rosinski,J.A. 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 168)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..168
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..168
                     /product="helix-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=18597
     Region          <48..>166
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 matvvkpqtr plttaeiaal alslahlgsg pqavtarrgl qhafdhldld daviattlat
       61 ltdplpvdva srarliadai tsrmmvrlhy rdasgtvtsr dvepvtclvh rehwylvgvc
      121 rmrrgirafr fdriiavept ltpsrphlad rflpfqrrkr prptqipa
//
LOCUS       WP_357590171             419 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357590171
VERSION     WP_357590171.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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 419)
  AUTHORS   ter Beek,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..419
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..419
                     /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=44531
     Region          41..414
                     /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(147,149,272,274,303,304,345)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mktrtkvaaa laaallasac sqgsatkaps geggrttlry ftfsaapdhv kdldaivaaf
       61 ekqnpsidvv vetapfdeyf tklqtsiagg tapdtfelny enfvtyagag slldlgavgg
      121 dgdlsayaae slnafkrdgk qyalpasfst vvlfynkdlf ekagvdlpta dwtwadeqaa
      181 aekltdkkkg vygdfqpvqf fefyktlkqa ggeflsadgk ksafdspqgv kaaewlvskv
      241 grtmpteaei ggtadydtnl fksgklamwh ngiwqfaglk dvpfewdvvv epgdagkasa
      301 vfhnavavss ttklgkeaya warflsssdv aastriassw elppvadqqv lagylkdpkp
      361 anrqavfdal esialppvik rqqemqdavt kelseaasgr kpvpdalkaa aaevdallg
//
LOCUS       WP_357590241             502 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590241
VERSION     WP_357590241.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 502)
  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 502)
  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..502
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..502
                     /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=54277
     Region          112..>203
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkrilipagg avlatgllaa glagsatats diakdpmats aanakaiadf wadnnnaalk
       61 aatqsnvwdn advaklktag gysadtkpgs aapigeekks ssksqnvnmp ktigkvffvn
      121 kkgekkwcsa tsiqskyrnl vataghcvyd tannadtmdk wvfvpgyyqg ktpygiyvgk
      181 qafthydfav yedydrdyaf vtvyngvylg ggkakqvsks eydkfqglke akdvaitaae
      241 yqkcvdlhgg etpdcwaktd tkvdvvgpdy pgavkaftev tkeqydaapt gkkngtkapt
      301 qtktdfvtes eykaykgpgy rkidskgnft ithyfikhfv kktdvkgyfk tvftivegwv
      361 kdagrlgdvv ggqgfawnqp tgkyvrvfgy pasahpdghk nytgitpkwc ygkttkklvg
      421 saakkieehv alkcamtega dggpwlynyk nskrlgyvng vtstfndqdg nnrvdyissp
      481 yfdgetasiy kaaanswsgk vv
//
LOCUS       WP_357590251             111 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357590251
VERSION     WP_357590251.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..111
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11916
     Region          37..>90
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtsfpkwsdv radivaasgg eeavaearrr nqayidgyrl aerrkslgls qtdvadlmgv
       61 tksrvsqier gevstvevia ryvqalggsl qisavfgddl yilrgtdtha a
//
LOCUS       WP_357590263             510 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590263
VERSION     WP_357590263.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 510)
  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   2  (residues 1 to 510)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..510
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=53189
     Region          37..509
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mtpsygrlag vlaagllata tpalpaaaat apvvvgtatg evrgsaaagv rsfqgipyaa
       61 ppvgdlrwts prpaapwtgv rdatrpgpac aqptgypigv psenedclyl nvttpakakg
      121 klpvvvwihg gslmygtgdm ygparlasag avvvsmnyrl gvmgflsspa lggsggfgle
      181 dqqaalrwvr anigafggdp gkvtimgqsg ggyavcghla spaskglfhr aivqsapcat
      241 ggsrtraaae aesakviekv gceeagdvaa clravpaadl laaygafaep rpvagtallp
      301 rtparalrdg rfnrvpvlvg vnhdeergmv agaelapggr pmrageyapa iraqfgadaa
      361 avlkryplra hgsagaalaa vrtdhawaap tldtarllsr wtptrmyefa ekdtpwfagy
      421 patsfpvraq hmaelpylfd lklfeklppr qarlaermig awvrfaatgd pgwarfaerd
      481 rhvrsltagt wkraaferdh ayafwtglsr
//
LOCUS       WP_357590325             371 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590325
VERSION     WP_357590325.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 371)
  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 371)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 371)
  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..371
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..371
                     /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=39310
     Region          123..371
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstpvvstrv iagvavalfa apmvfslasa vvafstgtag rwwpltlail lvtlltvsya
       61 rvlwaaflgr ltwrhrldva aiaviaygvp lfagagwigl pmafisvasv vfvrpavtwt
      121 vtlaaiavtp vlilligvpl pvallyglla mptiapmtyg vawlcrlidd lrearaelar
      181 ravdeerlrf srdlhdtlgh tlhaialrae lgerlvttsp eragaelaei qriartsvhd
      241 vrelvrgyra tslateldgv aavlgaagir cdkpelpael pghvhaplgw vareavtnvl
      301 rhstatwcev tvhteegsvh leivndggps tgrfsrgngl tglaermkaa ggaleaecgg
      361 grfritasvp l
//
LOCUS       WP_357590338             438 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590338
VERSION     WP_357590338.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 438)
  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 438)
  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..438
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..438
                     /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=44213
     Region          23..>426
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mllvaaatts allaataagq adtgdpvisp aliaqldthq kvrsivevkp gqsvtavagd
       61 vekgsssarv lestesptff vaeldadala llrkdarvka vyedalskpf laettkviga
      121 drahaagwtg kgatvavldt gidrdhpfla grivdeacfs tsdaasqavs lcpngqanqt
      181 gpgaadaetr qcldgganrc dhgthvagia agklvagapa ngvapeagil piqvfsrins
      241 avacgttrvp cflsytsdqk laleyvarva kernvaavnm slggggphrr hcdadpgage
      301 lkpqfdqlma lgaapvvaag ndgwtdavas pacvstavtv gatddadrma pfsnrgvlld
      361 llapgadvta svpddayglm sgtsmaaphv agsfallkqa ypnltaaqal qrlqttglri
      421 dttarvdaaa attgtpqv
//
LOCUS       WP_357590370             377 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590370
VERSION     WP_357590370.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=40024
     Region          186..377
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mkrlrranrq qvirdvllwf llsvavsimg pdpldglpaf alvtvprial mgvvvlvgrp
       61 wplaavalll pfgpwdfreg fatsdltwls ppssgvkilp llpvsafvmw yayltgrrla
      121 rvwpalalaa vatgigvvlv ltrggtlalw vtmtsglagt yavpyllgll rrrllqqraq
      181 arhstaeqar lrerariard mhdslghdla liavraagle mspnldpaqv kaagelrlaa
      241 adaterlhqi igvlrddtdt aplvpvhedv talveraras gmritldvtg pvpelahavv
      301 qegltnaakh apgaavtvei gphrvtvrng patgprpalp iggglglagl rervrladgt
      361 ltagptpqgw iltatlp
//
LOCUS       WP_357590438             281 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357590438
VERSION     WP_357590438.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 281)
  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..281
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30888
     Region          10..66
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(16,20,45)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,44)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,38,41,45..46)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          103..262
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgasrlnked latalrelrq asglpakava rsavmspskl skienghlap tltdverilt
       61 alavseqvka gfiqaarlaa teatawrlyr rmgphkkqaq iqaveaqtsa lrlfqistip
      121 gllqtpeyvr avvarrdytp eettrtvgar lerqailyet arsfhfvite svlrwlilpp
      181 amlagqldrl isisrlpnvs igvvpmsapq rdlpgtpfci fddrlvtvet phaeivttdp
      241 rdigtyrtkf dgfaqaalyg demsvfvagi rdellleret p
//
LOCUS       WP_357590523             154 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357590523
VERSION     WP_357590523.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 154)
  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 154)
  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 154)
  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 10140345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..154
                     /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=17056
     Region          8..142
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04663"
                     /db_xref="CDD:467548"
ORIGIN      
        1 mrliprlrva ayvvrvtpdg vqllvfdhvd hpdagtqvpa ggvkpdetlp davlrevaee
       61 tglhdislvr eigtehrphp etgqprhtty fhlrtpahtp dawqhtvtgt gqdsdirfac
      121 rfaslplpah ladhqdalld ridptwttrp qpmq
//
LOCUS       WP_357590619             399 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357590619
VERSION     WP_357590619.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..399
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..399
                     /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=43152
     Region          15..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 msiapaassg tasdsagshs rlawldalrg igalavvaeh mlpwylpsar pywfsfgvfg
       61 ifvfflvsgy iipaslerhg dvrafwlsrv frlyplylav svlvlalaww vpvreavprd
      121 ggsvaghatm lldvvgvggl adtmwtlsye mvfyllvtal fllrlhersa llsvlfaatg
      181 vvtglvmsra lfggawvaya scavfvagla cviggrfrra aalsmgvmal vllvlnsrvp
      241 wlgaaivalm fagtavhrwe rgrgslwpva lttalvavsp fwavqngwww vqpdvwvtti
      301 alsaavfgga malrgrrlpk altwlglisy slylvhhpvl kyvsavagdl raaslpvqlt
      361 atvlvtaliv avsaltyrwv erpmqelgrr lsrrwatar
//
LOCUS       WP_357590527             144 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590527
VERSION     WP_357590527.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=16013
     Region          1..136
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msvtrtvqih fddldamgll hnsryallve ravgafwaeq gwnfdpgvsr frdvymavre
       61 fkitynapis gagevavefw ldrmgrtsgv ygfrvlsadr sivhaegyrv nvnldpatfr
      121 papfsqelrd aaaplmledl taaq
//
LOCUS       WP_357590624             289 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590624
VERSION     WP_357590624.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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..289
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..289
                     /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=30296
     Region          3..283
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mkdvlvlgga gvdstvyvpe lplpyrdtyh vppvvdrign tgagvtlgca algldvafad
       61 ligddpqgal vrdalrgvdc awghaeagtr rsvllvgpdg rrtslfdpka tpgerlprhl
      121 ytgirarhah vsitdfcrhv ypdlagtpts tdlhdwdgvn pyhedfahrs dlvflsatal
      181 pdppatmrai largrahtvv ctrgadgclv ltrdgdlraf paaslpgpva dtngagdafv
      241 sgflygtlrg lpvdtcarlg aiagahactt pgthespite atllersrt
//
LOCUS       WP_357590698             122 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357590698
VERSION     WP_357590698.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 122)
  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..122
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..122
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13143
     Region          67..116
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(69,73,98)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(72,97)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(79..80,91,94,98..99)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 miltitweip pgltaeraaa laerwaagel nsederlprp kriratatde peivsaaraq
       61 aiaegrmlnq rrnqlglsqr slarlarvpr aaitdvengr rgpgsataia mrraldavka
      121 ar
//
LOCUS       WP_357590737            1041 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590737
VERSION     WP_357590737.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13449935
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..1041
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=111542
     Region          <10..401
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          336..1015
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mlvvhgvwag dgvafwaedt alapraargp aprahpwaap verlpaggpr tlelllpgsa
       61 aeplpspetg llsavtrpsl rpwrvpavvp plpaavhlla pdptpaaapa adpdpapgpd
      121 lapgpgpdad agpgsdsgpg ltgwgdavpg atvrhwrava afardlvrrg rvvpqlelte
      181 adgearaawr avvtgadaay frdlaltmpp acrtwaverp shevlrqald afadtfarta
      241 lnarpphtgt gtgtgrgrwl aalaspdttc pgaassrads pgaacpddpd lrraleewrr
      301 svesaegatr vcfrltepvd ppapagdgrd daagehrwrv elavqaaddp slyvpagkvw
      361 gggpvaglpa gaerellagl gravrlypel dralrvpqpe elvldtagaf aflreaapll
      421 qaagfgvqlp rwagrarlgl kvttrtktqs aaasqgfglr elvdfrvdla vggetigeee
      481 laelarlkvp lvrvrgqwve lderqlaaal ravggerggv lpaaevlrhv vqgddelpll
      541 evdadgvlge llsgrpeggp egrpavigtp agldatlrpy qerglawlsf lselglggvl
      601 addmglgktv ttlallvher aaeptllvcp mslvgnwqre aarfapglrv hvhhgsgrda
      661 triadadlvi ttygtaqrdl etlrrvpwrr vvcdeaqaik nsgtlqaqav rsipagtrla
      721 ltgtpvenhl aelwsimefa npgllgpkar frtrfqepie arqdeqaaqa lrratgpfil
      781 rrlktdasii sdlpeklevk ewctltpeqa slyqavvddm lgriddsegi errglvlaam
      841 aklkqvcnhp ahllkdgsrl agrsgklarl eqlaeeilae gekallftqy aefgsmlqpy
      901 leqrldrpvl wlhgglpkka rdrlvdrfqq ddepmlflls lkaagvglnl taashvvhvd
      961 rwwnpavedq atdrafrigq rrnvqvrkli cagtleervd emierkkala ervvgagedw
     1021 ltdlstrelr evfrltagav g
//
LOCUS       WP_357590830             181 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357590830
VERSION     WP_357590830.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 181)
  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..181
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..181
                     /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=19575
     Region          5..177
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mwslsdesli aaiaageaea tvafvrryqa rvyglalsvv gdpglaeeva qdafvrawrh
       61 aarydpgrgr vsswlltitr nlavdalrlr rdqpvdpawl psprdgrgdg gddgrealge
      121 vervrdelrv lpaelsrpil lsvcygltaa eiasreglpl gtvktrirrg larlrqaaav
      181 p
//
LOCUS       WP_357590876             345 aa            linear   BCT 28-DEC-2024
DEFINITION  glutathione S-transferase family protein [Micromonospora sp.
            NPDC049891].
ACCESSION   WP_357590876
VERSION     WP_357590876.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..345
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38829
     Region          16..317
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mgedgkgtgg ryvepgefkr dqnyittrit adgrdgypve pgryrlvvsr acpwanrlii
       61 vrrllgleda ismgvagpth darswtfdld pdgrdpvlgi eriqdayfar ypdyprgitv
      121 palvdvptgq vvtndyaqms ldlstewtay hrpgapqlyp ehlraeidev naavfadvnn
      181 gvyrcgfags qdayerayrr lfdrldwlte rlagqrylvg dtiteadvrl fttlvrfdpv
      241 yhghfkcnrq klsempvlwa yardlfttpg fgdtidfdhi krhyyevhrd inptgvvplg
      301 pdlsnwltph drealggrpf gtgtppeppt ptervdptht plpip
//
LOCUS       WP_357590880             228 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent F420 reductase [Micromonospora sp. NPDC049891].
ACCESSION   WP_357590880
VERSION     WP_357590880.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..228
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23144
     Region          19..195
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mrigilgtgt latalaaawt raghdvsigg rslqradaaa ktsgararrl pdiavnadav
       61 llcvhwegit diltaagapa galagkplid ptnavdhgig vlrtepgrai aqhvadlapg
      121 ahvvkalhlf pstqwttpap tpvtvamcgd dpraleitgs lvrdiggipa vlggldrarq
      181 leevagfvit laftahdpqs aipavpqptt plpgpeprqg qkrmglsg
//
LOCUS       WP_357590983             213 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357590983
VERSION     WP_357590983.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 213)
  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 213)
  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 213)
  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 213)
  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..213
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..213
                     /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=22256
     Region          2..209
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mritvfgatg gtgravvqra laaghevvaa vrdparlpls hpaleiatad vfaprtlepl
       61 ltgsdavlsa lgpnsrndts rvcsagiaai ltamdatgvr rvlalsaqpv lrtgagesll
      121 wrrlgmpavr avfgtvyadl ermertlaas tadwtvlrpp rltgkpatgr yrsavdanvp
      181 gsmtrgdlar amldmlpdpf tvrraigvag prr
//
LOCUS       WP_357591001             252 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Nonomuraea].
ACCESSION   WP_357591001
VERSION     WP_357591001.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,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 11417809
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..252
                     /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=26199
     Region          1..236
                     /region_name="LivG"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivG [Amino acid transport and
                     metabolism]; COG0411"
                     /db_xref="CDD:440180"
ORIGIN      
        1 maallrldgv tksfgrvtva ekltlsveag ealgivgpng agksslfami sgdlrpdgga
       61 vwfggrevtg appyartrag igrtyqvprp fehltvfenv lvcahqgagl rggraqaham
      121 dvlertglaa lantpggrlt llqrkrleva ravgtaprll lldevagglt epevaelvav
      181 vrglhadgla vvwiehvvha lvktvgrmvc laggavvadg epmrvladpk vrelylgggp
      241 etetttgeee rp
//
LOCUS       WP_357591012             435 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Micromonospora sp. NPDC049891].
ACCESSION   WP_357591012
VERSION     WP_357591012.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..435
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..435
                     /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=45707
     Region          2..435
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 meaelaargf trmvfeldri sslldllgsp qraypsihlt gtngktstar midsllrafg
       61 lhtgrytsph letvrerisl dgepvdearf tavyqevkpl aeliddrsae pltyfdmtta
      121 lafatfadap vdvavvevgl ggaedatnvi qagvcvltpi gldhtewlgd tlqdiavaka
      181 giihpgatvi aaaqeeeaar pilqrcaevg atvaregsef gvlrravafg gqvltlqglg
      241 gvyeeifvpl hgahqaqnaa valaaveafl gagarrqldv eavregfaat sspgrlervr
      301 taptilldga hnpqgmaatv talqeefafs klvavlgtla dkdaasmlel lepvvdqlvv
      361 trnsspralp vkelaalaae vfgpdrveva eempdaieaa valaeedvpg elagvgvlit
      421 gsvvtvadar rllkr
//
LOCUS       WP_357590939             435 aa            linear   BCT 28-DEC-2024
DEFINITION  cupin domain-containing protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357590939
VERSION     WP_357590939.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..435
                     /product="cupin domain-containing protein"
                     /EC_number="1.14.11.47"
                     /GO_process="GO:0043687 - post-translational protein
                     modification [Evidence IEA]"
                     /calculated_mol_wt=46420
     Region          44..338
                     /region_name="RoxA"
                     /note="Ribosomal protein L16 Arg81 hydroxylase, contains
                     JmjC domain [Translation, ribosomal structure and
                     biogenesis]; COG2850"
                     /db_xref="CDD:442098"
ORIGIN      
        1 mtrldppggh grpaapspsa vapgldepad aaaaalarcv sveaakfaaa hwgrtpllsr
       61 aaelpnpagf tdllspadad ellsrrglrt pflrvakdgq vlpaarytgg ggagaeiddq
      121 vldekvlqly adgatlvlqg lhrtwpalid ftrnlslavg qplqvnaylt ppdsqgfath
      181 ydthdvfvlq vdgrkhwrih ppvlpdpler qpwggradev gataqgpaal dvilepgdal
      241 ylprgwlhsa qaqessslhl tvgiraltry alveellala addqrlratl pfgtdvadpd
      301 aiepeltetv ealrdwllra dpaavaarlr qrawsasrpa pirplaqaaa italtadslv
      361 marrglrwql vgegdrvtlr lfdrtislpa qcepavrall agppirvgdl pgldtdadrr
      421 tltrrllrea altpa
//
LOCUS       WP_357591130             171 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF421 domain-containing protein [Micromonospora sp. NPDC049891].
ACCESSION   WP_357591130
VERSION     WP_357591130.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC049891
  ORGANISM  Micromonospora sp. NPDC049891
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..171
                     /organism="Micromonospora sp. NPDC049891"
                     /db_xref="taxon:3155655"
     Protein         1..171
                     /product="DUF421 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18311
     Region          4..156
                     /region_name="YcaP"
                     /note="Uncharacterized membrane protein YcaP, DUF421
                     family [Function unknown]; COG2323"
                     /db_xref="CDD:441897"
ORIGIN      
        1 mvlnnpadla rllviaaivy palvvilrvs gkrtlsklna fdfvvtvalg stlatimlsr
       61 dvslvegila lillvalqya vallavrwpp sqkllkdrpt mllrdgqlrt ealrstrvae
      121 seirqaarsq gtgdlddlaa vvletdgsls vitrrqlgdg sslvdvrdeg r
//
LOCUS       WP_357591125             112 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591125
VERSION     WP_357591125.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=12348
     Region          1..82
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mddalravad ptrrailvlv rdrevpagei agrfpeisrp avsqhlrtla aaglvdvrra
       61 gnrrfyrlrp eglaeavtfl esmwstslgr lqreaereer adtgehdakg sl
//
LOCUS       WP_357591165             381 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591165
VERSION     WP_357591165.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..381
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..381
                     /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=40961
     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 mkalvigcgi ggpalamalh evgieaeiye aygdtaqgvg sflnlasngl dalrslglhr
       61 evmaagiptp amvmwsgtgk rlgtvangla lddgtvshti lrsdlyrimr dgaarrgvrv
      121 sygkrmvsfd dtgdqvtatf edgtrakgdl liaadgvrsr trhlldpqap apryaglysg
      181 ggiihdqdft gepgvyhmvf gkraffgysv aesgetwwfa nlpralgdvp ddwrpvlvea
      241 fkddanfsae lvrraeigpm lpihdlppvp vwhqgrvvlt gdaahatsps sgqgaslave
      301 davvlarclr deagheaafr rfeaerrgrv ervvayakti snskaagpva rvfrdalmpf
      361 flkksasqes lawmyrhqvs l
//
LOCUS       WP_357591196             319 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [Actinomycetes].
ACCESSION   WP_357591196
VERSION     WP_357591196.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..319
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..319
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35636
     Region          53..319
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mehnimtqtt stpsreeada ivesmvaifs kpirspvigk ptdfglqyed vffpaldgvp
       61 leawfipcvg sdkviicnhp vwcsrtglpa drepwrsiga aggndfafsf lpdykilhda
      121 gynvlaydlr nlglsgeang gigsigvlea rdvvgslnyv rsrpdlkgkk iglfsrcmgg
      181 natffamaky peqfndvrcv vmpqpismra avgvatelag ipdrldeide rlamvtsfhl
      241 ddmdpsvpar tntsvptfiy qvhddvmtrp sdvqnifdsm pvkekqlhwi rntthrwdgy
      301 lyfqrepklm ldwfnnymn
//
LOCUS       WP_357591189             931 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357591189
VERSION     WP_357591189.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 931)
  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 931)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 931)
  AUTHORS   Rosinski,J.A. 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 931)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..931
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..931
                     /product="helix-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=95956
     Region          <1..889
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          874..931
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlygrtaeta aideligstl agdgralvlr gaagvgksal ldlaasragg atvlraggve
       61 geadlafaal hqlvwpvigl ldalpgpqrd avagafgmaa psqdrflvsa gvlsllveaa
      121 adsglicvvd dfqwvdrasa dallfaarrl rtervgmvla vrgdapvkgv pelrvdglda
      181 esadalldar aevvpgvrsr lvaltggnpl vlgeavavlt adqlagrtpl pdplpggeql
      241 fgdqvallse garrvllaas lesdlgpalg aadalagare rgtheaglhe aeraglvvvs
      301 gavvrfrhpl vrsavhaaag arelrrahev maelvdgdrr awhlaaaavg rdesvagala
      361 aaagraqarg gygdaatala raaeltpdpl irarrlkdaa eaawlggrpg qaqtylaear
      421 llveapsera etpalgeagg pgvtggpgea halaeapape earalgegrg pvegcalerg
      481 grgevageva rlrgrfelns gdaaeamrvf sagdslemla daweaasvvg dvaamvdvgr
      541 raegfapgfl rdilvgvaam lrdgsgggll rgalartgel sgaaeflwaa aaasylgead
      601 vsaelirrag rvarvsgmvg qlpvvlefvs taervggrla esaavaeegl alareagytn
      661 seaahlanla vvaalrgeee rcrayageal aiavphrvgl raavaayala mldlgmgrfa
      721 aahdrfeair aagpgaghpt vvwrstpdrv eaamaagdsa aarealegld rwaaqartde
      781 aralrlrcvg lvegaiepfe ealrlhgepf eeartallyg erlrrghqpg qargplraal
      841 etfqrlgaep warrahaelr aageaverpa gdalaaltpq elriarlvae gasskevaar
      901 lflsprtvey hlykiypklg itsrtelarl l
//
LOCUS       WP_357591199             201 aa            linear   BCT 28-DEC-2024
DEFINITION  TenA family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591199
VERSION     WP_357591199.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..201
                     /product="TenA family protein"
                     /calculated_mol_wt=21833
     Region          1..199
                     /region_name="TenA"
                     /note="Aminopyrimidine aminohydrolase TenA (thiamine
                     salvage pathway) [Coenzyme transport and metabolism];
                     COG0819"
                     /db_xref="CDD:440581"
ORIGIN      
        1 mtiseklhai grplldaqla hptvvgigrg dlpepvfrsw leqdylflmd ytrvfarlaw
       61 qapdghlgdl vdlahatfhe eldlhrslsa gfgadlegar kgpacaayta fllesagsya
      121 eglaalypcm wgystlgqil aenppaepry rawadtyadp gfaalaaria qmideadpdp
      181 araeamfteg mahelafwdv p
//
LOCUS       WP_357591202             447 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357591202
VERSION     WP_357591202.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..447
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..447
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46690
     Region          21..398
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mahdvrddev pltlegaapk tlgvldqgal wanlavsllg fsgalflldp lgnaplslta
       61 alaaavvgsl igtamvglsa ipgtqtgqpa mvllrglfga rlsyvptvln iiqmigwgaf
      121 elwviaqgam avfgdtvpya vwvivagvlt taltiwplga irllrryita lvivaliwft
      181 fqflgdappq sggswtafap avdyvialsv swvplaadfa rhsrssraaf tgvvggytla
      241 qvaclglgvy avaiagaaav qndstavfgp fvavplgavf fgilvlread qsfanvystt
      301 vslqnlmprv drrilsvaig vltvaialvv dvtsygaflg vigavfvpmf avlavdyfll
      361 ggatrwntae daparwsmla pwalgfaayw lttstptveq wdgiwaaare aigferqpwm
      421 ngalgaalva alvtlalgai rrrgarr
//
LOCUS       WP_357591290             387 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357591290
VERSION     WP_357591290.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 387)
  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..387
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42056
     Region          142..384
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnpidrarrh tlhmmasivv mlwlfiigrl flhaedvhwq rvvpgliavt aftwyyhrav
       61 savlrdryar revtiagvla lvtasaggad pmswgftlaa wlsvaaigvr vrtatvmavg
      121 tmaagvllgl gnylldpdvl llrdvtagpv vaylvfiygl fcvafpwtnr vwmwiwqlav
      181 qasegkeaht rlalaeerlr fsrdlhdlvg hqlsaiavkt elavrladad tgaakaemte
      241 vhaltrkalk elrqavrgyr eldlgaelns vkgvleaagv rcetrlphre lpegvapvfa
      301 yvvreavtnv lkhstatfcd ilirftdeea evrvrndgat grsgdelgsg lsglaervga
      361 vrgtltagpv ddghfllrav vslpiag
//
LOCUS       WP_357591308             272 aa            linear   BCT 28-DEC-2024
DEFINITION  cell division protein FtsQ/DivIB [Micromonospora parva].
ACCESSION   WP_357591308
VERSION     WP_357591308.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..272
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..272
                     /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=28744
     Region          71..272
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mspgpargrt saadggaprr gparrwqlvr agrdavppst rrfmararqr rmraalpwav
       61 aagvlalagl iawtvlgtgl fgvrevrveg aelatpvqvh davdvpdgvp larvdldaaa
      121 rrvgalpvve ratvsrdwpd alvvrvtert avavvpqgea favidgsgva frtverrpag
      181 lpqvtvarpa addpgtragl evlvaltpql raelvdvnvq glarislrlr gdrtviwgda
      241 trgtdkarva talldedtdr idvsapdvvt fr
//
LOCUS       WP_357591355             688 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591355
VERSION     WP_357591355.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 688)
  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..688
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..688
                     /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=73820
     Region          32..411
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     Region          <560..>637
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
ORIGIN      
        1 mpdiaplrag dpprigglel lgrlgeggqg evflardpsg tqvavkwlrp esagdevsvg
       61 rflrevqvaq qvapfctaav lgtgvehdrp yivsefiegp slqrvvqqeg pragsalhrl
      121 aigtatalaa ihqagivhrd fkpanvilga dgprvidfgi araldatsti snmpvgtpsy
      181 mppeqvlghq vgpaadmfsw agtmayaasg rapfgsdtmp avinrvlnqp pdlieldgtl
      241 revvlaclsk dpaqrptaeq vimrllqrpm apgsgilaqg saasaagpvh apspapapqh
      301 aqpwappgpy qpvthpsgrp qlrrrssrpa limgvtlgca llllagivti irldratvaa
      361 tqspspgrsg sarttdpptp ertavtavpa rgtaralpga satvyehpsd aitltsyevy
      421 nesgkewtdy arkslrgkfa kyprnkesmv spdgrylaar gkefnsddyd yidiidqktg
      481 ekttvttvka plestirsws qdgtkillni eeetgdewyy igfavvdvag rfpklslvrd
      541 rqvretgfgw dgeeqgavnv yggknkglrf ydaagrklrd vprigelasg tsamfspsga
      601 lfvtncpggg dgdhcvwdsk tgkrsrafts dcdkvlgwyd ekhlycweqd neardavqvv
      661 dfrgklvrkl ldiaedvdfs piytvnpr
//
LOCUS       WP_357591361             256 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591361
VERSION     WP_357591361.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 256)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..256
                     /product="phosphotransferase 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=28143
     Region          7..186
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 madlqgthav evrgdvvtkr ykeeklgaae rewraltlla ryapglaprp isneggvtms
       61 ridgvplrgl adapahaadl atalaelhaa vppqvlagvp vrrwgpqala gqvgqwceqw
      121 qprdpaadra vsegrrwler wrpsegdppv lgagdgnlan flwdgervri vdfedsgrsd
      181 rvyelaelsq hvsmwvdgev dvlrhvelta aerarlrecs rlhaltwlfl lsgegprnpp
      241 gtfrrqverv lavlea
//
LOCUS       WP_357591384             472 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591384
VERSION     WP_357591384.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..472
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..472
                     /product="PhoX family protein"
                     /calculated_mol_wt=50259
     Region          5..469
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mdrvrmdrrg fltravlaag pfagvacagq rggaapapgy grlvpvadqr dgevrlhlpe
       61 gfryrsfnaa gekfsdgstv pgrhdgmaaf pgprgsailv rnhevngpvg afgderlayd
      121 pmagggtatl rvsrygevae srpsltgtmm ncsggpmpwg awvsceetvn gpdvgddftg
      181 gdnsrltekh gylfevplkg vsrarpiraa grfahesaaf dpatgtlylt ednfgfpsgf
      241 yryvpprhpm regrllddgk lqmlavadrp radlstgqep gaafattwvd iddpdpaftg
      301 rpsndvavqa vgrqgraaga aifsrlegav fhqgivyfvs tqggdpapge tppdgfgrgr
      361 gqvwayetws grlrlvyqsp raatldlpdn vtvsrrgtlv lcedgdgdny lrgltragki
      421 fdfcrlapip gdagaefags afgpgghtly vnvqskrgrs faiwgpwqrg df
//
LOCUS       WP_357591418             259 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Micromonospora parva].
ACCESSION   WP_357591418
VERSION     WP_357591418.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..259
                     /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=26217
     Region          45..142
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mllrktalvl alataallas tatataapad paptpfaaaa aanpvivvgg lsgvavayep
       61 iaarlradgy rtfiyqlpgl glgdiptsar afatyvdqvr astgaatvdl vahsegglvs
      121 ryylkrlggt aavgryvslg tpqygtyvan ivaflglgtc agvvacqqmt igsafladln
      181 agddtpgavr yttirtlqde lvrptgnaav ndgatnvliq aycplrvvgh lglvldgtay
      241 tivrgalvdg pvrpnclal
//
LOCUS       WP_357591428             460 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Micromonospora parva].
ACCESSION   WP_357591428
VERSION     WP_357591428.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..460
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48326
     Region          37..448
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtsaatgdva saaarlrall gdrlhepgdp gyatttrlwn gavartpalv aqcldadeva
       61 eavrvaarch lpvsvrsggh dwagralrdg alvldltglr avrvdpdaat vtigggatva
      121 eliaaarpyd lvvptgtvga vgmagltlag gygplcgrfg laldsllgae vvladgrrvt
      181 agprhdaely walrggggnl givtelrfra hrlpgvlagm imfalseapa vlrgygalva
      241 eapdeltvmt gflpgpagep vifvcpfysg pdldaglpwm drlralgnpl vdqispmpya
      301 dalrmfdggm vdgnhyllrt rwlpaltdgs vdalvdaarq vsspfsavav hhfhgaatrv
      361 rpvdtafglr adhlmaeiia vwapgdqpdp hqewaertsa alaphalpgg ypnllapqet
      421 drvrlaygan warlrhakrr ydprdllhav ptlppfghpe
//
LOCUS       WP_357591558             465 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora parva].
ACCESSION   WP_357591558
VERSION     WP_357591558.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 465)
  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..465
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..465
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49638
     Region          46..462
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 msrafsapfp pdrrgvapsr dtgagrsggt aravtrtlsd dplggtirrt vlpsglrvlt
       61 eaipamrsvs fgiwvavgsr detgpqagaa hflehllfkg thkrtaleis sqieavgget
      121 nafttkeytc yyarvldedl plaidvmcdl vadsllepad vetergvile eiamhddepg
      181 devhdlfvqa vygdhplgrl isgtaetvtp mtrrqiqnfy rsrytapqiv iaaagnldha
      241 avvklvrqav rgtpldsdpa spaphraatp avrtrpvttv vepketeqah vilgcpgidr
      301 lddrrfalgv lnnvlgggms srlfqeireq rglaysvysy asqyadsglf avyagcapgk
      361 vdevlaltra elarvaaegl teaevargkg mskgsfvlgl edtgsrmsrl akgellygdl
      421 mpvdellrrv davtvedvnv laaellsrpm slavvgpfga gdfav
//
LOCUS       WP_357591579             819 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Micromonospora parva].
ACCESSION   WP_357591579
VERSION     WP_357591579.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..819
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..819
                     /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=87327
     Region          88..>172
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <333..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 magrtsqasr rrgasprggt nsrarqpakk trapvrrrta pprpgpavyv graigalwmg
       61 lahgmgwavr aagrqaasar dldpehrrdg agllmfglal lsavalwlsg agpvgarlad
      121 tvrlflgais vvvpvllmig awrlmrqpad pehrgrglig wgsllvstaa llqigqdpad
      181 tlerdfaggl igagvggmle ravtawvavp llillllfgl lvvtatpink iperlgllag
      241 glvgtpepge eeadepvakp arkrpakrmp ppldpddfed ldgadlqetm vlprkapakv
      301 pasrkpqvep pehspaptra eqlaltglag dytlppanml sagaaaktrs kandeviaal
      361 tgvfdqfdvd aavtgftrgp tvtryevelg hgvkveritq lsrniayavk spdvrilspi
      421 pgksavgvei pntdpenval gdvlrsraat sdhhpmvval gkdieggyvv anlakmphil
      481 iagatgagks sclnsllvsi ltratpdevr lllidpkrve mtgyegiphl vtpivtnakk
      541 aadsldwvvr emdmryddla angvrhiddf nrkvrngeik appgseremr pypyllvivd
      601 eladlmmvap rdvedsvvri tqlaraagih lvlatqrpsv dvvtglikan vpsrlafats
      661 sladsrvild qpgaekllgr gdglflpmga skpvriqgaw vtereiadvv kfckdqrepe
      721 frpdvlapaq eskkkidedi gddldllvqa velvvtsqfg stsmlqrklr vgfakagrlm
      781 dlmetrgvvg psegskardv lvkpdeldev lvglrgdvd
//
LOCUS       WP_357591582             374 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591582
VERSION     WP_357591582.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..374
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..374
                     /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=39876
     Region          1..366
                     /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 mrhriavvgs gpagltfarv lhrhghsvtv lerdpapdar ppggtldlhd tlgqvaldka
       61 gllaefrals rpegqamril dpdgtvlrdw rprpddranp eidrgqlrdl llgpldvrwg
      121 ravtevapga pdgvrvrfad grqetydlvv gadgawsrvr aalspatphy tgvtlvetal
      181 ddvdtrhpdl arligdgava vygvnrslva qrnsgghvkv yaqfrapldw hagldladae
      241 avrssmlalf dgwaapvldl lrrgaafahr plhvlpvpht wthvpgvtll gdaahlmppl
      301 gvganlamle gaelaesvaa apgpgeldda vrafeermwe ragrcaamta aglerlvspd
      361 padalaffde lqps
//
LOCUS       WP_357591638             385 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591638
VERSION     WP_357591638.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=39404
     Region          104..384
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mktfalvcgm gvvvvystll atgnqpdarp ldlagyvlla vaalglawlp rdpvaalvac
       61 agaaalcfvq gyayafwcap aliavfaaid agrraagwag aaflvavplt gaiahpsadr
      121 lvgvviwall vlvvaqpaev srarrdhtae aerraadaer treeealrra qeerlrvare
      181 lhdvtshtis vialhaavaa eavtraggpp eaaaalqvir assrqamtem ktilgilrpt
      241 aagagerqpq pgaaqlpala gsaglpvtle vagarrdlpp vvdlavyriv qealtntlrh
      301 aaatraavtl tyepdavrvr veddgagaga apaspgpepe qahargqaqg hgltgmaerv
      361 aaaggrlstg dgpaggfrvd awlpa
//
LOCUS       WP_357591653             467 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357591653
VERSION     WP_357591653.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 467)
  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 467)
  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 467)
  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 467)
  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..467
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..467
                     /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=48393
     Region          2..465
                     /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 mseeydvivi gagpagenva dravrgglsa aivedrlagg ecsywacips kallrpvela
       61 geagrvpglt lgpidaaavl arrdeavsry ddsgqvgwie glpaayvrgr grldgpkrvr
      121 vatpgggerm ltarhavvla tgttasvppv pglreakpwt shevtaatsv perlvviggg
      181 vvacemaqam hglgarrttv lvrggsller mepfagelva asfaasgidv rtgaeaarve
      241 rpvpggpvtv hlaegpplea dellvatgrr aataglglds vgladgpvev ddslrvpgld
      301 wlyavgdvng rnllthmgky qgrvcgdvia arakgepddl pslrasadgf gapqvvftdp
      361 qvcsvgrtea aarrdgfrvr aveydlasva gayllgdgyr grakavvded rrvllgvtfa
      421 gpgtaellha atvavtaevp lerlwhavps fptvsevwlr lleaygl
//
LOCUS       WP_357591673             359 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357591673
VERSION     WP_357591673.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..359
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=38870
     Region          50..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          159..341
                     /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 mtdamlaigt rkglflarss ggsafeiepi qfstvavhav aidtrgttpr lfagieyghf
       61 gpsvlysddl gktwqeadrp pvafpddtga tltrvwqltp spsepgvvwa gaepaalfrs
      121 edggvtyslv eglwehphrp qwqpgggglc lhtivchpsd prvmaiavsa agfyrtadgg
      181 ltweaanqgi rapflpegqq ypefgqcvhk vamhpsqpgr lflqhhfgvy rsddfggtwh
      241 digsalpsdf gfpivthpae pdsvyvlplh advdrtpvdh ryrlyrsdda ggawrplerg
      301 lpegpvyatv lrdamtfsea glffgtrdge vhgsrdaget wepvarhlpd vltvraavl
//
LOCUS       WP_357591686             189 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora parva].
ACCESSION   WP_357591686
VERSION     WP_357591686.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  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..189
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..189
                     /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=20469
     Region          17..187
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msepdqaddd isgigadpva fevfyrrhle avgrfvarrv ddphlaadlt advflavies
       61 aagyrpdrgs qigwlygvar nvigderrra aqrlrvtgrl agrrdlgpdd iarieerida
      121 esaarrthra lselpedari lvelvavdgl tvaeaatvlg vspvaarvrl hrarrvvrav
      181 larpaatla
//
LOCUS       WP_357591789             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            parva].
ACCESSION   WP_357591789
VERSION     WP_357591789.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..416
                     /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=43895
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..379
                     /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(349,351..353,355,366..367,371..372,375,379)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 midelvraet avgscadaaa walsegdlie aldashrlqq rlaavqlavv reldgrgvav
       61 aqgasstavw lrerlrldvs aarrlvglaa svdvappavr ealaggavsa eqarviadta
      121 atvsasagae vadkavgvlv ewarqfdptl lrrmgtrild hvapdladaa aaaalaaeaa
      181 ratrdrhvti seqtggrlrl sgtldaeaaa llravidpls apsgpddarr agqrrhdala
      241 dvcrlalrtg elpesggdpa qlvvtidydg larqvgggnl diglrlapdt vrqlacdavi
      301 lpavlggagq vldvgrqrrl vtgplrralv lrdggcafpg cdrpprwcaa hhirhwadgg
      361 ptsldnavll cghhhrhvhr sewtvrlgdd ghpefvppaw ldpeqlprrn hyhrrt
//
LOCUS       WP_357591693             284 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357591693
VERSION     WP_357591693.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..284
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..284
                     /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=29397
     Region          16..279
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtappvpppv tppvtwlyvp gdrpdrfaka aasgadvvii dledavtpar kdearahava
       61 ylrgrpgdga vhvrindlat prgrddleav gglagavrlp kvepgtplel verlgaraya
      121 llesaagiag areiaahpsv agvalgeqdl aaelsitdeg amnhlrmrvv laaaaaglpp
      181 vpmsvypdvr deagllasca agrgmglfgr taihprqipv irrafrpgee etaraaeivr
      241 aaeeaeaaga gavalpdgrf vdapivarar rtlelaarlr ddlp
//
LOCUS       WP_357591768             418 aa            linear   BCT 28-DEC-2024
DEFINITION  vanadium-dependent haloperoxidase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591768
VERSION     WP_357591768.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15731518
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..418
                     /product="vanadium-dependent haloperoxidase"
                     /EC_number="1.11.1.-"
                     /calculated_mol_wt=44822
     Region          54..>111
                     /region_name="VCPO_N"
                     /note="Vanadium chloroperoxidase N-terminal domain;
                     pfam17897"
                     /db_xref="CDD:436126"
     Region          188..410
                     /region_name="PAP2_haloperoxidase"
                     /note="PAP2, haloperoxidase_like subfamily.
                     Haloperoxidases catalyze the oxidation of halides such as
                     bromide or chloride by hydrogen peroxide, which results in
                     subsequent halogenation of organic substrates, or
                     halide-assisted disproportionation of hydrogen...;
                     cd03398"
                     /db_xref="CDD:239492"
     Site            order(290,297,333..335,384,390,394)
                     /site_type="active"
                     /db_xref="CDD:239492"
ORIGIN      
        1 msvlrkavga vvafvvvaga pgasaaeara penavivwdr naetaiweva rqqpqvqars
       61 famvhgavyd avnaiagspy epylvapkag gsasteaava saafgvlral fpeqrerlea
      121 qygeslaavp dgaakrrgia vgaraaaamv aarrddgafg dqtwptgtep grwrptppgf
      181 gsdgawvgel kpfmlprpsm frtsgppalt seqyardfne vkavggkdst lrtadqteaa
      241 iwwhdrhlae weikrqlatt qrlstlrtar mfamvgmaea datiacynek arwafwrpvt
      301 aireadgdgn petaadpgwt pllvtpphpd ytsghtcfsg agmsalthff grddiafsgf
      361 shdagttrhf rgfshalaev teariwggih traadvagak igrqvtaymv khhfrprr
//
LOCUS       WP_357591815             990 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357591815
VERSION     WP_357591815.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 990)
  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 990)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 990)
  AUTHORS   Rosinski,J.A. 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 990)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19885263
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..990
                     /product="helix-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=104452
     Region          114..>739
                     /region_name="PRK04841"
                     /note="HTH-type transcriptional regulator MalT"
                     /db_xref="CDD:235315"
     Region          801..985
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <925..986
                     /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 maelpvirdg llgiapgrpe iavgtpqwra wlaeatafav ehpaggftvr retsgngrgt
       61 gywrahrrvl gvrrrvylgg shqvtakald aaghalaaaa sdsepleatk vgvppartga
      121 varpqlyaal draarlpltl vcapagsgkt ttlaawaatt sarvawlsld rddndpvtfc
      181 rglaaaldvt mpdtaihsrp alrrrfagli nelagrpgdl vlvlddyhli gsadlhdava
      241 hlverlppri hliiatrcpp plplaawrar hrmcdldaar lrftttetaa flggtmglrl
      301 garavadlha rtegwpaglq laalalrrga pagheiaaat gdlddylvte vldglpdetr
      361 rlvlatcvls rltpalcdal tgrtdgaral talagsglfl spldasdgsy ryhqlfaaav
      421 rrylarrspe llpelhrraa dwhgsagdlr eavehalagd dppaaarlla rlaehdgglw
      481 leharlsrwl grlpeptpad npvlcllvaf tlihgslreg acshpyatdd paawlarvda
      541 arlppkaral hatilahrlf ldgspaaaid aaqaalnepc ltepgmrlqt vlrltdplgh
      601 gvqegpgrra qqecarlsrs ehdvihrlda llvlaqahlc rgdlrramas cresaalaaa
      661 rrvepdehla aaplvmveal leghriseav ahahdlqaat dhhdpgvrlh gyraaadlcl
      721 argdergtlh afdamadyia gtpgldnpgf gaaarrsava rrayalltfg hlaaaehtlt
      781 qaraitvagg eppaglrlye eliaaqlala grdwatadai asqamtrhad vvcaashlrl
      841 rvvaalarqa agdrpralaa lagalaqaap gaylrpfaeh gddlapllae aagkarqlav
      901 qerftrqayl actgtagakp gapelsgrei evlsllaegl sapqvgerlg laastvrshl
      961 ervyaklgah tgpqavarai rqgllpgpvg
//
LOCUS       WP_357591820             549 aa            linear   BCT 28-DEC-2024
DEFINITION  stealth family protein [Micromonospora parva].
ACCESSION   WP_357591820
VERSION     WP_357591820.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11246919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..549
                     /product="stealth family protein"
                     /calculated_mol_wt=61187
     Region          237..264
                     /region_name="Stealth_CR1"
                     /note="Stealth protein CR1, conserved region 1; pfam17101"
                     /db_xref="CDD:465346"
     Region          274..381
                     /region_name="Stealth_CR2"
                     /note="Stealth protein CR2, conserved region 2; pfam11380"
                     /db_xref="CDD:463267"
     Region          425..472
                     /region_name="Stealth_CR3"
                     /note="Stealth protein CR3, conserved region 3; pfam17102"
                     /db_xref="CDD:465347"
     Region          508..545
                     /region_name="Stealth_CR4"
                     /note="Stealth protein CR4, conserved region 4; pfam17103"
                     /db_xref="CDD:465348"
ORIGIN      
        1 mnntpvvpqr avvpsgavng agsgqaggvg qgpgglrevl vdggrrtahv hadltpmlgr
       61 qlnvdavsga leahgvdyfl vrgmddrtpv igvsevdrla vlgaleklgg tetcyvsqvl
      121 prppivgglt daseaaawte lyaaqaiklt wfradpslkl ilgpaygcdi efwkpdrmag
      181 llrsprpnrm mravaldgap vqvgehrlsr laspvkwhpp rrsrpefdhl lpddidfpid
      241 vvytwvdgad pewqqrragv rgeslhaeaa sesryinrde lkfslrslhl napwvrniyi
      301 vtdhqrpawl dlsagniflv nhdeifaapd alptfnscai esqlhridgl aehflylndd
      361 mffgrplapq tfflangntk fflsqnripl geiteldspv damiknnral iekrfgrtlt
      421 qgsqhvpypl rrsilaeier efpieheatm rsrfrsandl tityslhhyy afltgralpg
      481 rvnygyvqla vpdlearlrr aearrdwdtf cindafstfa qlqhqmtile pfmeayfpvp
      541 spyelrtvg
//
LOCUS       WP_357591828             260 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Micromonospora parva].
ACCESSION   WP_357591828
VERSION     WP_357591828.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 260)
  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..260
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..260
                     /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=27212
     Region          1..134
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 msrpdhmdva ayalgvldeq dterfeehla tcwacaaele tmvpvvglls didgetmmal
       61 eqtatdpall drtlgavrad rrrtrfrqml ataaavvvlg gltgygfvsv tgneqppgvl
      121 adstpsapnd pptsvptaap sgpgvggtev egdqveatdp ttgvqttmfl vtkdygtrin
      181 fslrklpgpr vcrlvvvrkn astevistws vpdggygtst rpqglelsas tsalpteikq
      241 lqvqsvdang vasplvtvpm
//
LOCUS       WP_357591830             285 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Micromonospora parva].
ACCESSION   WP_357591830
VERSION     WP_357591830.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..285
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..285
                     /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=30377
     Region          28..226
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mgrkrtadrv ieqvdtglae lvpdpdrags wtllldgapq shvdladpth lefeyvrrla
       61 aavdlvapag aplrvlhlgg galtlpryvs atrpgstqrv sevdgalvel vrralpwpsd
      121 prlkvrvqda ravlastrea sydvvvadvf agartpahlt sleyaaevar vlrpdgwyla
      181 nladgpplrh argqvatvrs vlpqaclvgd aavlrgrryg nlvlvagrse ppvpeltrra
      241 agdwfpgrvv addeldrfag gaqvvrdada tgsdppppgl fsvrr
//
LOCUS       WP_357591844             414 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Nonomuraea].
ACCESSION   WP_357591844
VERSION     WP_357591844.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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 414)
  AUTHORS   ter Beek,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..414
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..414
                     /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=44408
     Region          20..343
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrlaplaaav llsvaacaps spstpaqsqd kvtlsvwgwg peenfdkmfa ayeklnpgvd
       61 vdarsfttst eydtilatgl agdsgpdlaw lragpkiqpl veagrllple tadipglkdy
      121 dedvlrsakg dkdgkvygvp favqtlqviy nkkifadngl tppqtwadmi aaaeklkakd
      181 ivpfafggkd dwmlpivagi fgtanwggda flddvrakkk kftdpafvag idqlnklrpy
      241 fpdhmtgvsy tdaqilfssg kaamfpgglw elnfftenak didlgvftpp apgggpglmp
      301 gftdgsygin aktkhkaeal kfaawlaske ygqlytdtlr vfsavpgvtp tdpllkevst
      361 tfdkqgatyf mnefaygnps sqtvfskalq emllgritae eaagqldqsv atwl
//
LOCUS       WP_357591897             213 aa            linear   BCT 28-DEC-2024
DEFINITION  gamma carbonic anhydrase family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357591897
VERSION     WP_357591897.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 213)
  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
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..213
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22200
     Region          10..169
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 miaeargiri rhrghepqvh ptayvaptat lvgdvrvgpr arvmygavld aegsrievge
       61 aavicentvl rgsavagdqp vlvgdhvfvg phatllgcev grcayvataa tvlqcarlga
      121 gsvvavgalv hartvlpdey fvpphtvald apvrllapgd pgladavrrv gfaqvafgvd
      181 aewtdrisry ehiaevrvae fgahaddevl npg
//
LOCUS       WP_357591903             186 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357591903
VERSION     WP_357591903.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=20481
     Region          4..179
                     /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 mfpvklsspr lgmrefepgd vdpllaiygd plvaehmsfe prdrdqvtgi vdramkaarr
       61 perneyslag vlpggelvah lrlavdighp lqssgqigfa fradqwgrgl gghgiqlllr
      121 lgfehlglhr iwgarspvne rsarvmaqeg mveegtirgh lklaggwrds vvhsilrpew
      181 dgqdee
//
LOCUS       WP_357591922             172 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora parva].
ACCESSION   WP_357591922
VERSION     WP_357591922.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 172)
  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..172
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..172
                     /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=19374
     Region          2..169
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msdellvvrc qlgereafae lvqgwhpave ryvgrmlggs dddvvqeiwl avlkglprlr
       61 qpdrftpwlf tiarravmnr lrdayarpep epidelpgdd eaegvvnret lagalaelpa
      121 rerevlllfy ledlpldaca qicavpvgtv ksrlnrartl lrrelvrkgy ea
//
LOCUS       WP_357591940             334 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora parva].
ACCESSION   WP_357591940
VERSION     WP_357591940.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=35984
     Region          17..307
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mdagqdrrpa ggdgglrsav vvnpvkvddl delrrtvdda laaagwpapq wyettaddpg
       61 rgqteqavka gvdlvfacgg dgtvmscvsa lvgtdvalav lpqgtgnlla anlglstdla
      121 aglqvaverg rrlldvgave dkyftvmagm gfdaqmldat settkarigw payvmgavrh
      181 lrdrpmrvqi riddrppvrr rarsvlianv grlqggltll teaepddgwl dvavltprnl
      241 rhwlalgwav vrrsgevprm evfrgrrvvi ssnraqprel dgdliapgrq lraeirpeal
      301 wlcvpqpeda pdlavdvqsa gergeqliee arre
//
LOCUS       WP_357592088             937 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357592088
VERSION     WP_357592088.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 937)
  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 937)
  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 937)
  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 937)
  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..937
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..937
                     /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=102066
     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          124..926
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          727..755
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          767..795
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(768,771..772,775..776,778,808,811..812,815..816,
                     818..819,848,851..852,855..856,859)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          806..836
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          847..875
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          881..915
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfealgplr vrlgagqisl gaareqrila allldanqvv pmsrlvdviw dehpptssvk
       61 vvrncvstlr rqlarageiv tdsggyllrv pddeidlrvf verarqgrrl aaagdltgav
      121 vhlrealalw rgsaftgvtg rlveaaaaql ndqrrslqee rlsleltlgg gaelvdeiad
      181 lvaaeplrer ahgqlmlaly ragrrtealr tyhqvrrllv gelgiepgpe ltelhrailn
      241 adprlapvta paaisrpeps qpeastttkp vpaqlpaspy aftgrtaeld elsglldaga
      301 rtrtamvavl sgiagvgkta lavhfarlva drfpdghlhv dlrgfhptgp pldpgeavrg
      361 fldafevpaq hlpeglaaqs allrtllagr rvllvldnar dsehvrpllp ggpgcltlvt
      421 srsrltglvm tegahpitvd plplgdahsm lirrlgatrl taepaavati aarsaglpla
      481 laivasrlvd hprfslraia eeldlahggl egftdaetdv rsvfswsyra lsgpaarlfr
      541 llgihpgpdl gvvaaaslag vpparvrpll aelahahmvt ehtpgrytmh dllrayamer
      601 tdieedgaer laatnrmfdh ylagahladl rlhphrdpir lppavagvtv aaigdrevar
      661 twfsqeypvl ldllrraggd gydvhawqlg walttfldrc grwhdqaivq qlaleaarrv
      721 gdrdgqarah rnisiahlrr glhgeardhl whavrlyrgl gdqvgqartl lnlgtvaehr
      781 gqprlalrya elaqrlfraa ghragqanal nnagwyhsql gdheralhhc qralllqqea
      841 gdrywqahtw dslgcvhhhl gqypeatecy rqalslwrea geryyesttl thlgdthlav
      901 gersaargvw realdivvel gqdadrilek irtvttg
//
LOCUS       WP_357592111             822 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357592111
VERSION     WP_357592111.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 822)
  AUTHORS   ter Beek,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 822)
  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 822)
  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..822
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..822
                     /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=83419
     Region          4..818
                     /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          130..351
                     /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 mtglaarllr hragpaaatv laltvgvlil vamgtlvesg lrfraeprlw atadvvvanr
       61 tvshtfkefg dtttstvalp eggtvdaavv drirqvpgva avagddavvi gspaavghgw
      121 dtysftgrri aagaapradd evlvdtrfgv apgdridlvv ggvgrsylvs gttetgtaav
      181 fftdaqaarl sahpgrvdai gvrmvpgadv gavreiasaa gattyagndr gtveqsdnla
      241 artllveags afggyvvlli ifvvagtigl svrhrrrdla llravaatpg qvrrmliaea
      301 allalvgsav ggpagllaar wvhgelverg fvpasfpmtg glfavpaavg tavlvavlaa
      361 lvaarrvtgi kpiealgeia veprrngrvr liagvltlaa agtsgaftlg aggstgalag
      421 aagmlylfvi avallaprin ayaarlltpl lprvwrvsgy laaanlrana qgmatvltal
      481 vlsvgfggsv wflqtnlerq tatqssagtl aervivapgg lpedaareir emtgvraatg
      541 vrrtqvvvra lggiepvgaq svdpagitst mdlavragnl adlragtvav satqasssgw
      601 dvgdradlwl gdgtpvtldv iaiynrglgf gdvtlaaetv aghtagntnd evlvsagpea
      661 dtalatwsag kpgtevldaa trtrlistdl algawlnrll iavmvgyaal aaattmvmaa
      721 larcrelall qlvgvtrrqi ramvqaeqag llgtavliga tiaaltlsai vngltgspip
      781 yvpplgwvav lggttllala ttvwpvrrll gappidsigv ke
//
LOCUS       WP_357592119             954 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357592119
VERSION     WP_357592119.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=102736
     Region          1..254
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          126..946
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          720..748
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          753..789
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          800..828
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(801,804..805,808..809,811,841,844..845,848..849,
                     851..852,879,882..883,886..887,890)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          839..869
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          878..906
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdvailgpiq lrrdgapvpl gpqlttllai lllelgkpvp srrlatlltg ddasdaarat
       61 lrshvahlrr alepaergrr gnwliatvgr gaaagyrldl epacvdavrf edalresrrl
      121 lafgdaehad qaaamlrsal dqwhgepyad ladkpfalae varlravhrt alllyaeavn
      181 glgrhaeamg dltgavaadp ydeglrcmla ltlyrdgrad eaaevcrdgl allgrrglda
      241 pelhdlqrdi lrrevrqpag gsagrppvpr mlpsdlpffv graqelstae arlvdrdeqr
      301 paillvvgpa gvgktsssvr lahrlaprfp dgqlyanlrg fdataaaltp tevlraflea
      361 lgvapeqipt tlnaqvaryq aqlrdrrili mldnahsadq vrpllpgsat cvtvvtsrnr
      421 mssliavdga hpltlgllde reaaqlvsdr igidraakep eavfeiarlc aglplalsia
      481 aaraaanpqf tlrslagdla sagvldrltd sdssvdvrav fswsyraltp aaarlfrllg
      541 lhpgpdftaa aaaslaglsr raanallvel tgahltgerv pgryvlhdll rayagelced
      601 eperqaarrr lldhylhsav aadkvlmpyr qpvavvapee gvtpedpaev dplawftveh
      661 qtliavvgca ahagldrhaa qlawsmatyl grgsywhdvl ttqslalsaa vrlddrsaqa
      721 qcrrelshal aglgrleqar dqlhralvdl sdvadpigqa ynhlslgwly elqgdqrsat
      781 hhdqvaldlf rrggdrsgqa ralnavgwdy aqvgnyrqai gycrqalslh aelgddagav
      841 ntwdtlgyay hhlgeytiai ecyeqalcln vghrfkeaea lahlgdchha lgdmaaaans
      901 wgrayaimae lragdadavr akleltrerv pavghgeger galrtapsir spek
//
LOCUS       WP_357592190             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357592190
VERSION     WP_357592190.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,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 265)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..265
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28755
     Region          15..261
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msippptaqa eqpaihvhgl eksfkqlkvl rgvdidvarg sifallgsng agkttvvril
       61 atllkadggt arvagfdvat qaadvrqais ltgqfaavde iltgrenlvl varlrhlrep
      121 gviadellrr fslteavsrr vqtysggmrr rldiamslig nppvifldep ttgldpeari
      181 evwqavrela sggttvlltt qyldeaeqla driailhegr ivvngtldel rqllppaeie
      241 yvekqptled vfltlvgtkt ekeqr
//
LOCUS       WP_357592213             323 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357592213
VERSION     WP_357592213.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 323)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..323
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..323
                     /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=35187
     Region          20..320
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrattetsta vrdqggaast appgpppsra rrpnrwlawg flapvtiyla afyayplyrn
       61 velslreytv rsfvqggapf agvdnyrtvl tdpafwptlt htvvftaasl afqftigmal
      121 alffhqhfpl srtlralflv pwllplivsa stwswllnsd sglvnsalgv vgvdpvnwlt
      181 spgwsltsvi ianvwigipf nlvvlysglq aipaemyeas aldgatgwqr fwgitfpllr
      241 pvsaitlllg liytlkvfdi iwimtkggpt gssatlatws yrlgfgnllp efgpgaavgn
      301 llivlalvag lvyirierrq qlr
//
LOCUS       WP_357592209             570 aa            linear   BCT 28-DEC-2024
DEFINITION  amylo-alpha-1,6-glucosidase [Micromonospora parva].
ACCESSION   WP_357592209
VERSION     WP_357592209.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..570
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..570
                     /product="amylo-alpha-1,6-glucosidase"
                     /calculated_mol_wt=62922
     Region          215..558
                     /region_name="GDB1"
                     /note="Glycogen debranching enzyme (alpha-1,6-glucosidase)
                     [Carbohydrate transport and metabolism]; COG3408"
                     /db_xref="CDD:442634"
ORIGIN      
        1 mtvapsgpef giqdipfsyr gswfnispvv aektyaddlh lvshqtglhp vlrltptaag
       61 ttvvatptvl twhngtgrie avydgpdtlr irghrlglrv aaaahtltpf sgtylyadpv
      121 dgshvftsye tgrryrvtvl cgalsrtdga qalgtadrsv dlpgdqpwei aieeyatarr
      181 pyagsvafer lcrdrmaeft afvdaiapwr gaetpaaela ayvlwsatva pagfvtrpav
      241 lmskhwmdkv wswdhcfnam alaagepela whqfqlpfdh qdetgalpds vthsevlhny
      301 vkppihgwal rhlrrrlpep pdraalaqty drlarwtgfw ldarrapghd lphyhhgnds
      361 gwdnattfdd nrvletadla aflvsqlrcl adlatelgep atrwsreadr ihaamlrdlw
      421 dgerfrardp rtgqrrssrs lldlmpvalg adlpapvaaa largvethlt thglateptd
      481 sahyvadgyw rgpiwapstv lvedglrrag qtriadeisr rflalceksg faenfdaetg
      541 tglrdraytw tassylilaa aaerrrvrsg
//
LOCUS       WP_357592232             420 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora parva].
ACCESSION   WP_357592232
VERSION     WP_357592232.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=44643
     Region          1..358
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrqramwsav lvvglalagc gsasdsgkst ssdgklvvwd wksgepfaks yldkakadfk
       61 kkhadvevef vaqpfdqyyt llgaaiqsgk gpdvmmfngg gqirdrvdal vpitdyvaed
      121 kqrlagweaf tkdskvygsp vtlqgypiyy nkdiyqkagl dpaspattwd kfvadcaava
      181 kagskcfalg nkegvgiqfw lssmgsvtlt aaeydawitg krdwtspnvk rvfetwketg
      241 dkkmntdgan stamfndsfa afqsgkaahv mglmsdvghw kafnefltpe klgvmkppvv
      301 tagttpslpy dggigyavak wtkdpkvaad lvrsltsada lkafyadaga iaadttidvs
      361 qagpaastiv selksgkpal hvalssktid lmgrlsqqll sgsitvdevv kqlaasdqag
//
LOCUS       WP_357592269             317 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357592269
VERSION     WP_357592269.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..317
                     /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=33758
     Region          20..291
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtsalgsapt grddrrarpt ptrahrsrwa raagtgwlyv lpalvmyavf vlrplaltlq
       61 yslydwngig varwvgldny ltvftdsdll kiignaivli vffsfipval gllvasmvrr
      121 ittgpfgtvv rtilflpqvi plvaagiaws wllssnglvn qvlravglgg varawlgdfd
      181 talpavgvig awvllglcti llvtgmskid palyeaarld gagpvreffa vtlpslrqei
      241 gvcltvtiia alasfdivyi stsggpglqt tvpgleiyrl afsqrqvgla salavvlmll
      301 vlacvlpiqr lsrgeks
//
LOCUS       WP_357592316             501 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592316
VERSION     WP_357592316.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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..501
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..501
                     /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=52731
     Region          36..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 msndplvetg ldeltpvead ldgagpydlg vdaggrllae taalvaghtg evvhgpvapa
       61 svdterirdw lagfdfaeak padavlgsvm salrkwtvht thpryfglfn psptwwgmag
      121 dlivagvnpq laayshapaa temerhvlrl langlglpsd tdgsftvgga eanltaviva
      181 ltrrfpeygs agllglpgrp vfyasaeshl awlkiahmtg lgrdavrlvp vdaalridld
      241 rlreayaadv aggripfmiv gtagttgagv ldplgpladl atewglhfhv daawggaaal
      301 sdrlrpllag ieradsvtvd ahkwlsapmg agvfltrhpa alaasfqcst gympaevggt
      361 hdpyttsvqw srrfiglkvf lhlavaglpa vaeqlerdvr lgdllarrla ergwqrinqt
      421 plplvcvvdp eadaageers grwhaevagh vvrggqawvs pvrldgrsai rlcvtsyrtt
      481 asdldravaa ldaaraatsl t
//
LOCUS       WP_357592326             470 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora parva].
ACCESSION   WP_357592326
VERSION     WP_357592326.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..470
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49972
     Region          3..414
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mnteprvedl lrelapqvlg vlsrrfgdfa taedavqeal laaatqwpse glpvnprgwl
       61 iqvgyrrmie lvrgeqarrr redlvarqap ddrqyapapd eelaaerddt lvllflcchp
      121 alaptsaval tlravgglst aeiaraflvp eatmaqrisr akqrirasgl sfrmpepaer
      181 adrlvavrqv lylifteght stsgphlrri dlaaeairls ralhtllped sesagllalm
      241 llteargpar tgpsgelisl adqdrsrwda aaidegitlv tralprgpvg pyqvqaaiaa
      301 vhdeapsteq tdwpqilaly qvlerlagsp vvalnravat amvhgpaagl aaldalahdp
      361 qlaghhrlaa arahlhemag draraiadyr taaartssrp eqlyltmraa rlaaepgegp
      421 paavevddgp aaavevgegp paavevgegp paavevgegl paavevevep
//
LOCUS       WP_357592341             317 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592341
VERSION     WP_357592341.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (residues 1 to 317)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..317
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33040
     Region          2..218
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 midvrgltmr ygrtvavdgl tfsvrpglvt gflgpngagk sttmravlgl evpaggealv
       61 dgrsyaslrr pmrtmgalld agavhggrta rdhlrclars ngigagrvde vlgqvgltdv
      121 agrriggfsl gmkqrlgiaa allgdpavlm fdeplngldp egirwirdll ralaaegrtv
      181 llsshlmnel altadhvvvi grgkliadta igelagrfrr dvlvraadpe rlagvlrahg
      241 atvtpeeapp gppardpsvr glsvrgldae vigelalgag valreltprg asleeafmel
      301 tedsveygar tgteqgr
//
LOCUS       WP_357592339             370 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592339
VERSION     WP_357592339.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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 370)
  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 370)
  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 370)
  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..370
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..370
                     /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=39088
     Region          61..367
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtllyggift vitlgalvva qrlqgdavgr nlqdvavrrk aegpcepgap cllppgvetf
       61 vradeleqel vdsqrvitlv tfvaiavlaf avcwwltgrl lrplhritat arrlslstlh
      121 erialtgpqd elkeladtfd amldrlerav agqrrfvana shelrtplai qrtavevgla
      181 dpsperlawi raellrnter serlidgllv laqgerglda papvdlaavv eqvvaeqspa
      241 ardkdvtvav svtggpvvva gdevmltrlv anlvenavrh nhrggrvlve lspaaglvvg
      301 ntgplvppgr agelfepfrr ldpdrtgsag gaglglsiva aitaahggrv eavpnpdggl
      361 rvtvalppst
//
LOCUS       WP_357592374             223 aa            linear   BCT 28-DEC-2024
DEFINITION  urease accessory protein UreF [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592374
VERSION     WP_357592374.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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..223
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..223
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22892
     Region          2..221
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 msllaqlqlt dsafpsglyt lshgleayaq agpvdvaall edvllnaagp gdaaalalvh
       61 ravtagdwdt vvavdrrlha vklnreiraa avrtgnqvlt taalvfatpe ldrlarlage
      121 kvtpgnhavv lgaayaglgv pvdaavtgdl yafaaswvsa avrlrrldfr qaqatlwgaa
      181 gaigraaeha laaagpldly aatpladtms avheraearl ftt
//
LOCUS       WP_357592384             316 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592384
VERSION     WP_357592384.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 316)
  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 316)
  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..316
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..316
                     /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=35476
     Region          8..204
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mplpdfliag vpkagttalh talrrhpdlf lsrvkepkff ltdgppphtg gpgdadtyre
       61 hvwrrtdyea lfadappgal tgestpfyly dtaaqrriha lipdvkiilt lrdpverahs
      121 nwthlwsagl epigdlvrac eaepkriadg wghfwhytgl grygeqlahl fslfpreqvl
      181 ifryrdvvdr paatldqvca flgvrtgllt evprqnvtah pqagarhavl atlrrrlpap
      241 lagpvegllq rrgqarrple weqrqrlipc faddirllqe ltgddygdwl rhrprsgglv
      301 gvrppgqrqa rngrrs
//
LOCUS       WP_357592409             401 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592409
VERSION     WP_357592409.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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 401)
  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..401
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..401
                     /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=43908
     Region          20..397
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(52,59,85..86,93,97,104,233..234,237,241..242,245,
                     278,283..284,287..288,290,314,341..343,346..347,349..351,
                     355)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(59,79,81,84,86..87,172..173,182,232..233,236..237,
                     241,284,287..289,387)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 msseppildp tgrrlyeqvd elraagpavr vrlpgdlvaw svtrgevakk llvhpgvskn
       61 artswpeyrp faigwltawv dvismftvdg ddhkrlkdlv gkaftprrie amrpaietiv
      121 edlladlela ppgrpvdlra sfsypiptrv icdlmgvple qrpqmlrcid avldtsltpe
      181 qanvvqrdmf aamhalmhyr ranpgtdlts lmlaaqeega plsteelvst lilmigagse
      241 tavslidhat vamlshpdql aavradparw ddvieeslrq hapimhlpmr yattdidlge
      301 gvmigkgeli liafgahgrd pavnpdpdrf disraerqhl afghgihycl gaplarleaa
      361 ialpalfsrf pelrlvsrpg rhtsfigndy pslpvvldpa a
//
LOCUS       WP_357592449             340 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592449
VERSION     WP_357592449.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=36338
     Region          2..339
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtgpvrfgvv glgeiyqlah hlafqraagl eavvvcdldq dvaartaqsl gaeagtdyrr
       61 llederiqav dlvlphhlhy kiarefletg khvliekpmt vgaadarelv alaadkglkf
      121 tvnentrfvp ayqatldavt ggevgdvtlv rtlisgnefg rlgnpslwkg rqdgsgggti
      181 idagahsfyl lkwmfgevas lralserlvd vsqvedwsvv agrmrsgalf svestftsgg
      241 pwnerlevhg teglivvdqh qnppamifrg krdhagsplp gttyepgtwk ynsiaagves
      301 farsiaddep tavspedgay avhvielayq svasgsavta
//
LOCUS       WP_357592456             556 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora parva].
ACCESSION   WP_357592456
VERSION     WP_357592456.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 556)
  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..556
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..556
                     /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=58386
     Region          6..264
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(6,30..31,64,69,74..77,89)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(13..14,16..19,21,34,36,72,88..91,95,97,134,136,
                     138..139,141,151..152,155,173..176)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(13..14,16..19,21,34,36,72,88..91,95,136,138..139,
                     141,151..152)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(17,95,97,134,136,138,155,173..176)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(151..159,169..176)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mliagryrll dlvgrggmgr vwrardemlh revavkeivp pgwlddrgra elrsrtmrea
       61 raaarlnhpa vvrlydvvav ddspwivmey vpsrtlqdvv daegplepar aariglavld
      121 alqaahsagv lhrdikpqnv lvahdgrvml tdfglatfdg gdgamtrpgm vlgspqyvap
      181 erasdgvssv aadlwslgat lhaavegqsp yarstamatl salaagppdp aphagalapv
      241 lhgllrrnpd drldhdaarr llrtaaggra dppavtdrps vdgtasgvvd agteaddvdp
      301 tiplpdpade pavteaggas papdpsaagr tarrvavvav allvavvagv gtaltvtgdk
      361 pgdttgwssp tpgagplgpg ppprgrgipp ppfacvrpdi vgtpvragtp sagdgfqppp
      421 gwiwyaditg frvsvpatww tsrdgtvvcf qdpatgrafs vaeggavepl rrlralrdka
      481 aaagalpgyd eirlatadga aewecrwqtp hgrwlrarqq tlgadrwtlg witfdedwgg
      541 aaadwetvrk sfrqpr
//
LOCUS       WP_357592463             249 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592463
VERSION     WP_357592463.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..249
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=26811
     Region          1..249
                     /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 mrdaqvlpdg srirwaevag repvrvyvhg lgaaaapyfl eaasrpelag hrslfvdllg
       61 fgtsdrptsf gysmeehada latalraadv raaqviahsm ggtiavhlae rhpelvaelv
      121 lvdanldpiq ptprptiaty tedgfvrhgw detltrvgph waatmrlagr ealhrsavhl
      181 tqadvrerlr rlpiprayly paidgelaga aeletsgvrl iavpdtghni midnakafas
      241 evgglltrs
//
LOCUS       WP_357592499             402 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357592499
VERSION     WP_357592499.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ter Beek,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 402)
  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..402
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..402
                     /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=43751
     Region          1..389
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 madivldkvs ksfpdgtvav qdvdleiadg efvilvgpsg cgksttlnmi agledissge
       61 lriggqrvnd kaprdrdiam vfqsyalypn mtvrenmafp lrlakldket inqkvdeaak
      121 vleltslldr kpanlsggqr qrvamgraiv rqpkaflmde plsnldaklr vqmrtvvsrl
      181 qkqlgtttvy vthdqteamt lgdrvvimrg gavqqvgppq elydhprnlf vagfigspsm
      241 nflhaavqdg elhtalgqvp lgdrvrrele tadaprelil girpehfeda elvdddtrrr
      301 gmefeapvdi vesmgsdkyv yftvegekas aaeleelaad agaadfagag gnlvtrlsae
      361 spategqsrr vwfnlekihl fdptngrnlt lhegraagal ad
//
LOCUS       WP_357592614             628 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592614
VERSION     WP_357592614.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 628)
  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 628)
  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 628)
  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 628)
  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..628
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         <1..628
                     /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          57..613
                     /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 prgrtrdgsd ghrgrdggeg yrsaredggr rppprgprqg ggrppvpprp plvlrlgnpr
       61 rrinigligm tfvlsifagr liqmqgldsk vyeaaavdqr qqteeiqakr gsitdvnghd
      121 lavtvearei aidptkvpee vrgkvaalla rhlgkderel aaklarvdtr yqllardvep
      181 vvatrllkep ipsltatety rrvypggdla gsligfvgde ksglagmeqa rdsvlagrdg
      241 evrmetgrdg lripmtssqr tppvdgrdvr ltidrdiqwa aqkaiaeqtr ksgassgtvi
      301 vmdvrtaqii amanapeldl anwrkapesh yvnraaaevf epgstnkvit aaaaleagvv
      361 epgtvfhvkd niqcadrvlr dahahppqnm tfqqavaess nvatvmaark vgsqglyeml
      421 kafgfgtrpg ggvpgaeagl lpdyktwsgs qsctvaygqg vsvtalqmas vyqtianggv
      481 kiepqivagt tdaagrfvpa ppgkqtrvts eetakeistm leaavsaegt gelaaipgyr
      541 vagktgtanr ydaelgrydg ytasfvgftp adaprlvvls vlqnpknghf ggqlaapvfk
      601 dvmtfaiksr kipptgsaas pvrtragq
//
LOCUS       WP_357592628             280 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592628
VERSION     WP_357592628.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   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 280)
  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..280
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..280
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30073
     Region          1..280
                     /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 mrvqvngttl yvdvegaale pdgctmrekp tlvllhggpg hdhtifkpay rqladvaqlv
       61 yvdqrgngrs qdsdpatwhl dqwaddvral cdtlgivspi vlgwswggav amnyaarhpg
      121 hpaklilqst varwdvdrvv egfraeagee aalaakaflt egtpetfaaf grlcapaysp
      181 dpafpseadi qamarmtpnp eltmsfmsta rfdlrdrlaa ircptlvvag srdpitpldt
      241 aqeiaagvpg arlevfggsg hfvpdteger ffsllrafva
//
LOCUS       WP_357592615             178 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357592615
VERSION     WP_357592615.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 178)
  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..178
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..178
                     /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=19087
     Region          18..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 miegtplrad arrnrarild aaeavfaefg prgsteevar ragvaigtvf rhfptkddll
       61 aaimkqlltq lvedadqrdl fdflthmvaq aaakktvvdl lagsgvdirl paavnqleda
      121 vdrllhkara agdvaatvrl pevmallaal cqgalhggwd eqlqtrtlav ifaglkrn
//
LOCUS       WP_357592699             254 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357592699
VERSION     WP_357592699.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25519
     Region          3..253
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mstrfadkvi litgatsgmg rataervaae gakvvlaars kdageafaae lrsagrdaff
       61 vptdvtveae marlvqqavd hygrldgafn nvgaataygp vteingdawg aelalnlnsv
      121 fhglkhqipa lqasgggsiv nnasnlgvtg magmaaysaa khgvvgltrs aaldvaatgv
      181 rinalvtggv dtpllrgnmg pnpeealraa gamhpvgrig rpeeiaafaa fllsdeapfv
      241 tgaalaidgg ltal
//
LOCUS       WP_357592754             349 aa            linear   BCT 28-DEC-2024
DEFINITION  thiamine-phosphate kinase [Micromonospora parva].
ACCESSION   WP_357592754
VERSION     WP_357592754.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Begley,T.P., Downs,D.M., Ealick,S.E., McLafferty,F.W., Van
            Loon,A.P., Taylor,S., Campobasso,N., Chiu,H.J., Kinsland,C.,
            Reddick,J.J. and Xi,J.
  TITLE     Thiamin biosynthesis in prokaryotes
  JOURNAL   Arch Microbiol 171 (5), 293-300 (1999)
   PUBMED   10382260
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427471
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..349
                     /product="thiamine-phosphate kinase"
                     /EC_number="2.7.4.16"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009030 - thiamine-phosphate kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36602
     Region          54..323
                     /region_name="ThiL"
                     /note="Thiamine monophosphate kinase [Coenzyme transport
                     and metabolism]; COG0611"
                     /db_xref="CDD:440376"
ORIGIN      
        1 mtsttrnrlp lsaaesslim airermtrsp rqlnnafead aelldlgaag llavtvdtln
       61 dgaelatast pyakgwlttt vsvsdlaava adpvavlvsc slrpdswtpe earefgrgas
      121 eaaerygchi vggdtnwane esftscalgt vpresvvnrm garpgdalyv tgpigagnav
      181 gfralalgga gegepwlpea rvtaceplrr yaracidtsd gllsaavsla evnglgaevm
      241 lhdevyapiv savadaaglp rwcsaaaewg efellyaidp adaracseal trrglrpfhv
      301 ghlvagpell mvdesgqrre lrdlltrmra ldpagslltd lravlaegs
//
LOCUS       WP_357592752             306 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora parva].
ACCESSION   WP_357592752
VERSION     WP_357592752.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..306
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..306
                     /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=32750
     Region          9..306
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 maadendpvv citnptsgvr rrdtimrria aelpeaqcws trypghgial grqavedgya
       61 tvvaiggdgt lsevangvle aggekvrlay vpagtcndfa rglrpvtdlg dlldrtrdre
      121 tdvgtvtftr pdgtrdqryf lvsctvglis vigqrftekt pvnrvlkrln lqlaettssi
      181 rtlagwrpva vrleldgeas hqsisnlavl kvpyfagglt fgrtqpprag yldavrvsgv
      241 grlgvaglmw qvfrgaaagh paihrqevrt vcvdadsplp vevdgeivgy tpaefsihps
      301 clttvv
//
LOCUS       WP_357592780             355 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357592780
VERSION     WP_357592780.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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..355
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..355
                     /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=38616
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 magievtalh krypdgtvav ehvdlsighg elfvmlgpsg cgktttlrai aglerqtagd
       61 irigdtlvnd lrpaerdiam vfqfyalyph lrtrdnlafp lraeglpkqe vnarveeaar
      121 lmrlgpllnr rprqlsggeq qrvalaralv rrpraflmde pltnldaelr admrteikhl
      181 qgelgatmvy vthdqveams lghriailnk grveqigtpl evydrpaslf caafigsppm
      241 nlieveiadg qlhaqgglvl tppsglprdr rlvagvrpea levtapgaeg siparvvsve
      301 wlgdeiiyvv dhggqrdvrv rmpptvrfaa dakvglrhtg gtpavydvst eelva
//
LOCUS       WP_357592838             708 aa            linear   BCT 28-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein [Micromonospora
            parva].
ACCESSION   WP_357592838
VERSION     WP_357592838.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 708)
  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 708)
  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 708)
  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..708
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..708
                     /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=79775
     Region          190..522
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 msgtvkaali yppltdptsg yhslnyldsy araqghqpae iidanieafh hsytpsayew
       61 lrrelsrlsm ddlsgpdalm aranqlglpd pdperlrrsi gvlqdptlfy dyrhyqdave
      121 gviswmdalg svgfpgqfha gfrlhpppmi sigsvaaltd eallarlnrp flpyyedvli
      181 prlaagghqv igisatyqwq lpfalwiarl vrqacpdvfl iaggteisdv wkcaskpeyv
      241 fqvladfdai vvgegesayt eildavaagt lpaghpnvrl hprygrqrhl plryerlaqv
      301 pvpdfsglpw dlylspekfv yysptrgcyw nkctfcdygl ntdgptspwr qdtvgtmiad
      361 vtelskfakf iyfsvdvlap atilrfaeqv vergldfrwg aeirlekyws dercellrrs
      421 gcvaisvgfe sgnqrildli dkgtrpeqvr rtmtamtkan igvqmmgftg fptetreeal
      481 dsvtflrdnp dlwtlgglgd fmltpgaiva keperfgitn vrpvegsdiv rmlkydepvt
      541 eaaqaevaqa kaglnpghyh rpwlgstdtp htffyhdryg tavrgvland rvrhdtddqt
      601 eflangsfve rddeqvweay rrirsdeqdg tlgdlpadrh lfrrvdgqvf alnrssrlfl
      661 dlfsapltla eaqrrlwive ptvadrvwrt figqrlirrh rlpaepar
//
LOCUS       WP_357592884             723 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora parva].
ACCESSION   WP_357592884
VERSION     WP_357592884.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 723)
  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 723)
  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 723)
  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..723
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..723
                     /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=78615
     Region          30..716
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mrrksapsns tagvsdetpd ghltaaaega alrsavaeeq aflhvatarr drladhlqie
       61 lstaavdpme qarqrmlrrq ydelrragdg lvfgrldsld gavrhvgrig lrdegegsep
      121 llvdwrapaa rpfytatagd pqgqarrrhi rttgstvvgv ddepldgsmt aelvgegall
      181 aaldqrrtgr mstaistlqr eqddiiraea tgplivqggp gtgktvvalh rvayllftyr
      241 kmaeravlvl gpsprflryi aqvlpalget avvsatcdtl ladiqvgrde srllaeikgr
      301 alwqgtlery vasllprpre lklrwdgefy vidaatvaqa ltsatqgrpy hraraafaeq
      361 lhhlladvva eqrealmdem eegfedilar vdqsmenehh aprtstgsdi dgllseeeie
      421 hlrsriaent avarfveaww ptldagnlla glltdpalla rfapqlspee iaavsaeptg
      481 wapsdiplld alaellgevd apqpqgefva drarrqrgwv yghvvvdeaq elsemqwqmv
      541 lrrcpsrsit avgdidqaea ahrhtswaqa vravfgdrwt aaelticyrt prevmdltgp
      601 vltkagshst ppravrssgi epweltvapa elagaaveav rrlrqrwqgg tvgviapadr
      661 vgellavlsd vpvltatqsk glewdatllv dpqgiaaepr gwnglyvalt rctqelgqll
      721 ltp
//
LOCUS       WP_357592996             419 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357592996
VERSION     WP_357592996.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 419)
  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 419)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 419)
  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..419
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..419
                     /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=43792
     Region          159..416
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpdlpideda glgrfrrgtw wsvtattgff lvfvagawvl dpavalwarv tgaaalaatg
       61 lsgmalltrr mtpspdtpsp vsapsvvrlp vgwtvaggag aavlgglmla hgddgrwslp
      121 aalvvsiaat flrpaprwgl igasalaasg vgalsgaplp gaavlppavv lvtawttlam
      181 lwgwdvakrl ndvrrlaael avkeerlrfa adlhdiqghh lqvialksel aarlaeadpa
      241 raaaemhevr rlaadalsdt ravvqgyrrt tldaeianat gvlaaagida rmsvepadar
      301 rlpeagrhll glvmreattn vlrhsrarha evdyrvtgdl arlrvtndga gdlarlrvtn
      361 dgagdqpsdq hgdqpgaggt glrtlaerla saggeltweh dddrfavvar lparsaedr
//
LOCUS       WP_357593047             414 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357593047
VERSION     WP_357593047.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 414)
  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..414
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=43880
     Region          162..413
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtlraalapl vagttwrrgv flllggvlal pygllaavfa qmladsaipr plvyvllvia
       61 vliavvplll dgsraleiaa arallgvdlp epapghhgdr etrlrsalwi vthlvvgalv
      121 mlalfsalpm alafiaqqfg igaeltsrqr ygpldgqdsg wltvtgvlll vglgyavagl
      181 galagsmapa llgpaqaeri aaleaqanrl aernrlarel hdsvghaltv atlqagaare
      241 vldtdpefvr raltaiedvg rtamhdldhv lgllreggrd rpavarqrtl adldrlvtda
      301 raaglavhar ragdparvpa vvsregyriv qegltnaarh ghgpvtirld lhpdalelel
      361 vnalrhpvrg qpgrggrgld girervlllg grltvgpdgd rwlirarlpy eetr
//
LOCUS       WP_357593053             650 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Micromonospora parva].
ACCESSION   WP_357593053
VERSION     WP_357593053.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 650)
  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 650)
  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..650
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..650
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=71655
     Region          292..650
                     /region_name="COG4867"
                     /note="Uncharacterized conserved protein, contains von
                     Willebrand factor type A (vWFA) domain [Function unknown]"
                     /db_xref="CDD:443895"
ORIGIN      
        1 magnrfrygq wnggpdplap pydvreavda vgaqvlaggs lrealrdllr rgpqgrggld
       61 dlaararrlr reamrrgdld gavtraqall dqalaaerde lrgrdddaar faeavldnlp
      121 rstaravqel sgyqwasdda rrsyqqildq lrddvlgqrf aglrdavras adpaaqqrla
      181 emmgdlndll arhgraedtt dafaefmrrh gdffpekpet vdelidvlar raaagerlmn
      241 slserqrael aglmqqslgd rlagemsald anlralrpdl rwgrgervrg dqpldyadaa
      301 galgeigdld dlldqldqeh pgatlddvdv davartlgrd aaddvrrlrd lerelrrqgw
      361 vsrdaegltl spkalrrlgg talrrvfael tagprgqhdl rsagaagevs gasrpweygd
      421 eqpldvvrtl travsragpt vpvqlavddf evvetekras aavvlcvdls ysmisqgrwg
      481 pmkqtalala hlmetrfpqd alqivgfgre amtltqqela avepdleqgt nlqhalrlag
      541 rhlrrhpdae pvvlvvtdge ptahldpddg ealfhwpplp etieatvrev drlsrygatl
      601 nlfmlgddpg lrrfvdavar rsrgrmftpd tddlgeyvvs dylrsrqsrr
//
LOCUS       WP_357593076             751 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora parva].
ACCESSION   WP_357593076
VERSION     WP_357593076.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 751)
  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 751)
  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 751)
  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 751)
  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..751
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..751
                     /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=79864
     Region          84..740
                     /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 msrqdgtqaa galnpagafv aaavilleag wlvaalpgaa lvsdvgamlv agwatlacvg
       61 varrhpaplr rfwtllavtm alaaigraiw taqrlvggdl phtpvvgvvf tagiltgtaa
      121 lltspsaprt avgrartlld gvivalalvp vgwvlvfrgv aaaeladpar tlgllfpmfd
      181 lmqltilvav sgparpmwrp msilaasltl rvvadvvyvs lvaradytag hpidlcwpls
      241 ylliglatrn ppppdcdgtd dtaesplppw wrvalpylpv ggaivavvla rrptgqtphl
      301 vfvtmmvlla alavrqglaa nenfrlvvrl rrlaygdqlt glpnrllfnr rlrlalrdgr
      361 pvavllldld gfkqvndrfg hstgdtlltg laarmrtavn gdgtiarlgg defavlvdgd
      421 rpvsperlae rlldalrpsd deedvgvhps asigiaefgp qhashtdllr dadiamyaak
      481 aagksayrtc tpalresavs raeliadlrr avdedqlrle fqpivdlatg avrsaealvr
      541 wrhprlgmla pakflplaee tglilpidrw viheacraaa twrgrvpdat vavniaaahl
      601 rrpdliatvt aatsaaglap raltleltes aliegteavl erlhqlrelg iriaiddfgt
      661 gysslsylhr ipatelkidr sfvarlgtdd rayatvemvt rlagafdlav vaegveterq
      721 heavaaigcp rgqgylygrp dgpamvgqnr s
//
LOCUS       WP_357593137            1108 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357593137
VERSION     WP_357593137.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=118926
     Region          <2..901
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mdarrgdaii grdhsagllr aeldrastsh gglvlvtgep gigkttlvts aarearhrga
       61 lvlgaacwds dsapgywpwv qvlrglrrsa ddwavarpda epalaallge tdaskqqaer
      121 ltswagvdtd sadqeafaly davtaalvav sqqrpvvvvl ddlhwadpas lrllsfaaqh
      181 twferlllvg tyrdaeiesg ehplrpllmp llakattitl tglardevaa lmartagrap
      241 dadlvdevhr rtggnpffie qtarlwhadd aagtiapgvr eavrrrlaql ppsvvealtv
      301 aavlgrefhr qvlaacgaap vaqvdrlldr avtarlvmar gggrfafahd lvretlydgl
      361 tdddrrarha avvravddlr eltdrlipad larhaylagp aldparaatl lvaagrdafa
      421 rlagdeaavh frralevvdd reqrvrilve fgetqyhhag reeatvllte agvlartldd
      481 pvllarvali vnrarqveia fsteaaelvr eayrrligep dagasvgtlv adlitateti
      541 arrgqddeal tfslwarhda twglgtaaar avltaeirdv arrtpdrete lwatalrwva
      601 llelgdpgfm gefstfvnad rhgdltrhri aasvdsaiia afrgdfaead erfaditdia
      661 dpshaefgfm ghhlrwsrll legrfaeadt lldglaptdy pyrellrait agergdgeta
      721 vrltagieaa avryprpvsp lwlrlraqaa aasadpqrcd aaraalaphr gewmvalfgc
      781 disgpvdywl alidaaqgrw ddavagftaa rdsadrlgsr pwsllartgl vnalagrghp
      841 ddtaaltalr aatvqeasal gmaqvldrlg vptaidagrp aqavgsapav gsaqvvaagq
      901 avgsgqsigs sqgvapgqaa pgatavegye frrdgpvwql ayagvvvhlp dakglhdlhl
      961 llsrpgsdvp avelldpsag pelvaarrmg adpvlddeak aryrrhlarl deeidraaar
     1021 ddhrrvsqld tergalldel raaaglagrs rrlgdeaera rktvtarird tlrklderhp
     1081 tlaghlrdcv stgstcrylp psplpwrl
//
LOCUS       WP_357593172             182 aa            linear   BCT 28-DEC-2024
DEFINITION  SOUL family heme-binding protein [Micromonospora parva].
ACCESSION   WP_357593172
VERSION     WP_357593172.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10521978
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..182
                     /product="SOUL family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=20049
     Region          2..179
                     /region_name="SOUL"
                     /note="SOUL heme-binding protein; pfam04832"
                     /db_xref="CDD:461449"
ORIGIN      
        1 mteqqpyrvv srhpgfelrr ypahlvaemr iqasftrapi eafrplaayv gganrarrpv
       61 gaeaaggsek iamtvpviqi egespgayli qfimpatfts atlpepvdar vrirevaaql
      121 aaamrfsgrw teqtfgqrat mlgrsvtaag lqptgavrya rfdlpwkpwf lrrnevvlpv
      181 ve
//
LOCUS       WP_357593248             304 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357593248
VERSION     WP_357593248.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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
REFERENCE   4  (residues 1 to 304)
  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..304
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..304
                     /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=32339
     Region          33..289
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          203..284
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msagekvryw rhpgmggldl mraryvghrf srhshdtyai gavesgaeai hlpgglahag
       61 vhevvlidpg vvhtghahtp ggwtyrvlyp tpaqltaltg rdapsfarpv vtdarlaalv
      121 vaahraaete dpltadtalh lllarlvatq arpraaartl sralsrtaag ptaaarardl
      181 lhaclspetp aaapaawnfh arppglrela eavgttpfal vrtfrraygl pphayltqlr
      241 vrrarellar gtppaeaaqa agfcdqshls rhfrrivgtt pgayqravqe hpiphtpglp
      301 tvsg
//
LOCUS       WP_357593197             238 aa            linear   BCT 28-DEC-2024
DEFINITION  MIP/aquaporin family protein [Micromonospora parva].
ACCESSION   WP_357593197
VERSION     WP_357593197.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..238
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24256
     Region          2..209
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 msdfrryaae flgtlllvff gvgsavaarv qggvvvvala fgfvmvalvy tigplsgshv
       61 npavtlgvll sgkisvlgav aywiaqfvga tvaafvlwal trwgdvadqt galgsngyga
      121 hinrggaavl evvltflfvl vvlvvtsrse npgtaglaig lalaatqlvg vtltgaavnp
      181 arafgpavfe ggvalrqlwv fivfpllgga laalvapllm gaqrhywggh eksvgrpe
//
LOCUS       WP_357593253             321 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora parva].
ACCESSION   WP_357593253
VERSION     WP_357593253.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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..321
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..321
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35013
     Region          62..280
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msegpfavra aqltdrdpra lqplpgapgs nvdaptvglt gpvrpavdap tvgltepvrr
       61 vtpaisvcia vrdrpellvt sirsvlsgtf ddfeivvvdd gstvpaqecl aaaglladqr
      121 irlvrqkpsg isaarntalr vargryitvl dsddeftedg lariqeflnr tgavwvytdy
      181 eelvgssars islpsyptar rmlwsvltrp rlpfkhsgms ierelllrlg gydeklpikv
      241 dvelvlrala dgvhpahldr pvvrfhrheg sisrrriagl svwfqlisry trprvpglal
      301 vikavrasse igkwlvsalg r
//
LOCUS       WP_357593285             254 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Micromonospora parva].
ACCESSION   WP_357593285
VERSION     WP_357593285.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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..254
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..254
                     /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=26950
     Region          11..239
                     /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 migvvqtavs ldvrgvryay pdghvalqgv dlvvprgdrv allgpngagk ttlvlhlngi
       61 lsptegsvsv ggltvtpdra tlaevrrrvg ivfqdpddql flptvaedva fgpanlglrg
      121 aelaarvdea laavgmgehr drapqhlsfg qrrrvavatv lamhpeilvl depssnldpa
      181 arrelaeilr glpvtllmvt hdlpyaaelc ersvilddgr ivadaptntl lndatllaqh
      241 rlelphgftp tprp
//
LOCUS       WP_357593260             218 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357593260
VERSION     WP_357593260.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 18527459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..218
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23213
     Region          6..74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          84..217
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 mtgtgdlgrr iayhrerlgl sreqvagraa mspgylqyle enpgnpsada lsrlatalgt
       61 tsedllggta drppgggpaa esphvevldr eeclrliepg gigrvafdgs hgptvlpvny
      121 rlhdgailfr tayggpmdrd lrtgvqgvei vvgfevdrid eaqregwsvl vqgpfhhvap
      181 deaaglsasd vtpwvggdrt lyirivphqi tgrrihgl
//
LOCUS       WP_357593289             238 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Micromonospora parva].
ACCESSION   WP_357593289
VERSION     WP_357593289.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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 238)
  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 238)
  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..238
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..238
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25167
     Region          76..226
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mssrkgqrda arvvreqlar errrrrtiwv saaavvvlvi agvvgwavws sqrsddfttp
       61 pgantagtgi vtgngpvtvd vyedflcpac kqfeqtsgst leqlvaenka tvvyhpvayl
      121 nrfstteyst rssaasgcaa aggkyheyak alfaqqppeg sagltddqli digtgvgldr
      181 gsfgtcvkdq tyrtwtqhvt ddasrnnvtg tptvrvngqp venptpdalt aavaaagk
//
LOCUS       WP_357593319             200 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Dps family protein [unclassified Nonomuraea].
ACCESSION   WP_357593319
VERSION     WP_357593319.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 200)
  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   3  (residues 1 to 200)
  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 200)
  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 200)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..200
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=22257
     Region          36..190
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 magkrtsrng rkadsqpwph lngvqiqeyg tvrmfplgls yearmyscqr lnqiladtqi
       61 lyalykkhhw lmrgptfyql hllldkhaee qnklvdliae rvqtlggvav gdprhvaeit
      121 vvprppdgae evpamltrli eahetilvaa hdaaartaem gddgtndllv sdvirtgelq
      181 twfliehlvd tplvepppgd
//
LOCUS       WP_357593355             318 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357593355
VERSION     WP_357593355.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=35591
     Region          1..317
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkfdrllsim lvlqhrrlvp akelaellev sqrtiyrdie alsaagvpvy aergkhggvg
       61 llagfrtdvt glttdearal fvlsargaha algldqafgs amrkvmaalp aphrpaaelt
      121 srrilvdpdr wlagprpdfq ldtlldavlt drrlrlryrh sgqravrgyt vdpyglvaka
      181 gvwylvadhr rspylyrter isrvtvtpep vrrrpgvela qawdelrrqv eqrgdgirie
      241 trirrsrldm vtriaggyfs gppeddgpdw vrvpftypel gavchllqfh adlevtappe
      301 ardylsraas aisalyrd
//
LOCUS       WP_357593370             332 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357593370
VERSION     WP_357593370.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 332)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..332
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35385
     Region          5..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msavieiegl rktfhslrsg rrvavdgfdl lveagqvhgf lgpngsgktt tlrallglvr
       61 adsgrmtvlg apspellprv agqvgaives pqffgnftgh rtlrllarag gvpvsrvdev
      121 ldlvglhdrg ddrvksyslg mkqrlavasa llkdprllil depangldpa giremrdlmr
      181 slaangvtvl vsshilgeiq licdhvtiis rgrrvaagrv devlagydrh eylvrvaepe
      241 ravellhtag ltavvdgeal vvsgvddptv vsrvlgeqgl wvgeltplrp dlesvflelt
      301 gayghqsvpr qvddssrphd gavidldrgv da
//
LOCUS       WP_357593397             200 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora parva].
ACCESSION   WP_357593397
VERSION     WP_357593397.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 200)
  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..200
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..200
                     /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=21838
     Region          13..188
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtappenpdp pvddtalrfr agdeaalrea ydrygravlh lattmlanra daedvtqatf
       61 vaawlgrdtf dpakgsligw llgigrrkvi drmrasaret rvvetvrqlp epaqtgpdpd
      121 rvvdrlviad elaqlpddqr rilelafydd lthqqiaamt gvplgtvksh irrgmaslkr
      181 rwevdgaapg prpaglsgar
//
LOCUS       WP_357593410             160 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357593410
VERSION     WP_357593410.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..160
                     /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=16544
     Region          9..124
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mevggisfrl aayavcvedg rvllarhvpp eggsawtlpg grvghgedpf davirevaee
       61 tgcdavaerl lgvdsrvipa aearagvehh nvgvfyrvri tggrlrpepg geiaesvwtp
      121 vadvvglrrs slvdvglala ltvpptghva pvpvgglvqh
//
LOCUS       WP_357593434             412 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357593434
VERSION     WP_357593434.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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..412
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..412
                     /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=46402
     Region          79..404
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maerkrarng qgtitprkla sgstvydawa sikdpqtgkt lrpgkrghkt edeaarwirk
       61 tmeaaeagtr vvamrggptv seaaeawtkv thlkesswkl yyarylstva pligtepisk
      121 vrqthidqll stlrqthapg tlitaikalt hiwdyavang datgnvikss pwpariared
      181 kaariereqd kedqdgglir vftpeqiarl feyerkiglr hlwqfiastg vrrgealall
      241 wsdvdlgkri irirrnvtav nreiihldsp ksnrprrlyv ddsviallqa qqaflaecrq
      301 rhgdawnehd lvfpyadark dassrpgewh nptnisdafs rrlrmldmpr itlhglrhtw
      361 asaayaagvd lktiqdhlgh rvdittlvyv htdqeakrea vtrvvdylgr sa
//
LOCUS       WP_357593498             284 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora parva].
ACCESSION   WP_357593498
VERSION     WP_357593498.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 284)
  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 284)
  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 284)
  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 284)
  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 284)
  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..284
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..284
                     /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=27916
     Region          109..>283
                     /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 mavqtglgep rgpwfispel dpdgrgwwda perdpggrrp rrllaalavv vlstisgava
       61 gglvagrdga ggpaaasaap vpaelvtaae rtvpgvvsvl aggassgsat gsgfavddqq
      121 hlitndhila kggggpvtve lpdgrrfaae vvgreprsdl avlkvpasag ltplplakpg
      181 atrvgepvla vgsplglagt vtagivsald rqvrlgnnrh savqtdasin pgnsggplvn
      241 argevvgvnt aiatidgngs igigfaipid qvqqtadtii gkgg
//
LOCUS       WP_357593639             170 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: flavodoxin family protein [unclassified Nonomuraea].
ACCESSION   WP_357593639
VERSION     WP_357593639.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..170
                     /product="flavodoxin family protein"
                     /calculated_mol_wt=17561
     Region          5..152
                     /region_name="FldA"
                     /note="Flavodoxin [Energy production and conversion];
                     COG0716"
                     /db_xref="CDD:440480"
ORIGIN      
        1 mspvalvlye srygstrlia eavaeglatr mpaeareaaa tparlgedvt llvmgaptha
       61 spmsrapvpr gggvrewlaa ldpppatlgs aafdtrvgrp rlpgsaaral trslrrlgvr
      121 svaparsfav taaqgppaeg eldrarrwge tlaarhlpae qdaatasvrg
//
LOCUS       WP_357593681             323 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357593681
VERSION     WP_357593681.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 323)
  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 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   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..323
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..323
                     /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=34994
     Region          1..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 melrqlryfv tlaeelhfgr aaarehivqs alsqqiqrle revgvrlldr sthhvaltpa
       61 gsaflvearq ilnhvsragq tarnaaastp tlrvgiidag ydtmpqilre lqeshagiti
      121 hqveagtpeq yrqladgrld iaighasqap aevtsklvrl dplgvlvpdd hrfaeldgvp
      181 vialadelll lgeesqtpel nqfvlalcrs agftpalyeg tvessraaad lvlqhrcvhc
      241 vpssfrssnr pgttwrpltd pathypwsll whqdnpsshi atvidsarhl aerldwlepv
      301 apviepapge gapstagtgd apa
//
LOCUS       WP_357593691             345 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora parva].
ACCESSION   WP_357593691
VERSION     WP_357593691.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=36021
     Region          71..343
                     /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(72,136,140,160..165,183..184,188,210,227..228,230,
                     250..251,277..279)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mgnwvvslag prrislepcp pdplgpgqvr vrtcysgisa gteltlyrgs nprlskdwdd
       61 aarmfvprqt pvpypligfg yeevgeviev apevtdrhpg qlvwgiwghr aeavlaadav
      121 ralptgldpl aavfarpgai altavlagdl hlgdwvgvfg qgvigllatr lavlsgarvv
      181 avdpvptrla haarygarst vdatissaaa vlrqatdgrg advclelsga ypalheairs
      241 tthagrvvaa gfyqgqadal glgeefhhnr iqlvaaqvsg ptpapsmagr wtgdrvaqtf
      301 mdlvadrsvd plplvshvvd asavadalal ldrgagdvlq vvlrf
//
LOCUS       WP_357593687             318 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357593687
VERSION     WP_357593687.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..318
                     /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=34938
     Region          31..317
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtttapgpgr sptrerpapp rrrpltlrrr esraglalva ptllvtivvi gipivwtvvl
       61 afqrvrlatl rktglfgeft mdnidrvlht pgfaetlwvt liysiggtvg sivlglvaal
      121 vvrrpfrgrt lvrasmllpy vapvvaatfv wqvmldpqlg vvnawgqrll gwdapvpflt
      181 qestalatvi ifeawryfpf aflfllarlq avpgeleeaa rvdgatptqr fryillpqll
      241 pviallgvlr fimtfnkfdd vylltggaag tevvsvrvye fltartdiga aaaqavvlav
      301 vlivfvliyl rffgrrvs
//
LOCUS       WP_357593679             333 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA desaturase [unclassified Nonomuraea].
ACCESSION   WP_357593679
VERSION     WP_357593679.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 333)
  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 333)
  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..333
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..333
                     /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=36422
     Region          21..318
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mtiseqvaer rqdydgtspf peaedhvpag rlqvaltgai vvlpfvalga avllawgrgv
       61 tltdlllaai lyvvtglgvt igfhrllths sftarpwlrv alavtgsmgf qgnvidwvav
      121 hrrhhaftdr pgdphspyry gtglrgqlrg lvhahlgwlf addptpaery apdlladram
      181 srvarafpal calslalpfl agwaitgtly ggltaflwag lirvallqhv twsvnslchv
      241 igarpfktrr hdrstnlwpl allsfgeswh nghhsepsca rhgldrgqld psaaviglfe
      301 rfgwagdvhw pdrervqrrr vgprrqarap agd
//
LOCUS       WP_357593694             192 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357593694
VERSION     WP_357593694.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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 192)
  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 192)
  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..192
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..192
                     /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=21571
     Region          9..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 mtatlpapvv lenddvrlep ltlahvpdlf aagggddelw rwlpvatprt eeelaavaha
       61 lieddkhvph avivkatgra vgwtaycdvp gfdesieigw twygraywrs avntacklll
      121 idhafdklgh nrvllktdcl nersqnairr iggvhegtlr rhrrrsdgtw rdtvcfgilv
      181 eewpdhrarl nr
//
LOCUS       WP_357593708             340 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Micromonospora parva].
ACCESSION   WP_357593708
VERSION     WP_357593708.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 340)
  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..340
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..340
                     /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=36158
     Region          15..289
                     /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 maqdvvrqvv ervragfglr lstmervnhg adqharlwla qaadggryav klsgggtpag
       61 lvvtahlagq gvpgiaaplr svdgrlsidh dgrrlsvvpw vsdqraldgp mtgahwrayg
      121 evlaavhavp vteelsrllp mggaaypsiv tatravaerl rdpdqgdlad plvaelagvw
      181 savadrlrfl treverraag qrgrpgshvv chgdphlgnl llgadgqvwl idwddavlap
      241 pecdlmfvlg gvlafapitp dqqravlagy gttevdrarl awflavrald disdwtrqal
      301 dcdagaadrg raarivrglv splglvslad aalrdldrqr
//
LOCUS       WP_357593729             384 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357593729
VERSION     WP_357593729.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 384)
  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..384
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=40801
     Region          140..384
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 maaqrrtgrw wlrlpvgvaa gtvtaavefv flvvaavaft gcafapaagr ritgltsryg
       61 gwlvrvehrr lvgllaaadl papnavatrr qvgylaarll pgtlgllaya vlgvgvvlag
      121 ivlraavrge ltlldavsqi avgavlllln gqaiasiaal dvrlarrllg pgsraeltrr
      181 vhelttsrag viaavdaerq rierdlhdgl qqrlvalgml lgrarrtrdt drtralllqa
      241 hedvqraide lrqvawrvyp saldggdlge vltivtrgse vpvriryelp vrpqrqietv
      301 lyfvacealt naakhaaatl vaveigvqdg wirmrvhddg vggadptgrg lsglmrrvaa
      361 mdgqltvtsp aggpttvlte lpcd
//
LOCUS       WP_357593810             391 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357593810
VERSION     WP_357593810.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 391)
  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..391
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=41254
     Region          166..347
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfanvvrsar swldfwgtrs tlakdsalaa sltllgfvpt lstiaarigd laerpsdaaa
       61 vvltlaqsap lavrsrwpal clavtgtafa lhqalayppt fasiglylav yaagahqarf
      121 rrglaaasta gyavlavvlh glgspsrvqd fvafyltlav iwtagaamrr wradeaerrr
      181 lsadvaraae rariarelhd vvthhvtamv vqadaaqfts gttagfaais dsgrraltel
      241 rhllgvleat gdsggadrap tlagiaglve narlsgqpae ltehgeqrpr avdvelaayr
      301 vvqealtnam khapgrrttv tlhhhpdhla vevandgpdg tvqavpavps ggrgldglrr
      361 rlrlldgelv tehrpdggfg vrtriparse t
//
LOCUS       WP_357593830             273 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357593830
VERSION     WP_357593830.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 273)
  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 273)
  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..273
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..273
                     /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=27824
     Region          4..253
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdlgldgkva lvaggssglg lataaelare gahvaigard rprlesaare iervargrvh
       61 atgvditdrq aarrwvgtva aelgalhvvv vsggsppigp asgfevedyq aavdkvlmpa
      121 vnltlaalph lkaagwgrlv yvasetattp ipplalsgvt raallrfaqa lasdvgrdgi
      181 tvnviapgha rtppiermaa slggdveeql armghhsalg rmarpeevaa vaaflasera
      241 sfvtgavhav dggaavtgpd lphltrtrkd tnt
//
LOCUS       WP_357593919             254 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC023979].
ACCESSION   WP_357593919
VERSION     WP_357593919.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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 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 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..254
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26173
     Region          97..251
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mraivgslgl vlvltacgga vstsaapsps pppsttpapt ptptptptka kgpnvsgcyt
       61 rddgkiftyg ddmpgvitgk gevgvvitye rrgnvcswrp lsdrlvaagy rvllyarksv
      121 dlpedtalam arrlakekgv ervflaggsi gatvsataal elgdkaagvi alsgaidaae
      181 aaklkvpllq igtehdsygg addlqtahda atrapdrqih vikgesahas dlfrgpyate
      241 vidrvvafmd rhkg
//
LOCUS       WP_357593936             776 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora parva].
ACCESSION   WP_357593936
VERSION     WP_357593936.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 776)
  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 776)
  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 776)
  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..776
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..776
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=78428
     Region          53..>255
                     /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 mdktetllta paapepptaa rpdeetpqar rppawarpal amlllatgll ylwglgasgw
       61 ansfyaaavq agsvswkafl ygssdaansi tvdktpaslw lmalsvrvfg lnswamlvpq
      121 alcgvasvgv lyatvkrwyg paagliagav lavtpvatlm frfnnpdall vlllvagaya
      181 tvraletast rwivlvgvlv gfgfltkmlq aflvvpvfag vyllaaptal wrrvrqllla
      241 glavvvsagw wvalvelvpa gsrpyvggsq gnsileltlg ynglgritge evgsvgggga
      301 rpggggpfsg qtgvlrmfgg eiggqvswll paalvllvvg lllagraprt drtraglllw
      361 ggwllvtgli fslmsgifha yytvalapai galvgigvtl lwrqhrllsp pagvqsgtla
      421 avpaaaptag tpagdplpas aegaaggrrw qrwrplaasa tlagtlsvtv wwawvllgrs
      481 pdwhpwlrtt vvaaglvgaa llllasrlpr rlvpvvlglg aaaalagpva yavqtaatph
      541 ggsipsagpf vaggfgrggf pggrppggme lpaggqlpgg gqfpggfpgg gqfpggfpgg
      601 gqlpgggrng dgqngdgrng dgrngggqvp gfpgggrngg ptggqgrsag ggmgglldar
      661 epsaalrdll ehdsadyiwv aatigsnnas gyqlatgepv mpiggfngsd psptlaqfqr
      721 yvadgkihyf iggggfrang gssasqeiaa wvgqtftaqt vdgvtvydls agteas
//
LOCUS       WP_357593941             411 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357593941
VERSION     WP_357593941.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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 411)
  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 411)
  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 411)
  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 411)
  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..411
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..411
                     /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=43449
     Region          105..408
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnpaslrwki aalvtlaaav aaamvgllvh qatwqraldt getqaleale kslasgrpgv
       61 valaelpgdl aarlrpgrpa vgygldhrde pwmwaaqpyg dgrhavsvqi smgsqllrlh
      121 aldrdmakaa ltalavvvpv saglaelanr rlrrvartar riaagdldar trpapphrar
      181 wrgrdeitdi aaavdsmaaa lqhrllaeqr ftadvahdlr tplmglvavv elleegeaad
      241 lvrdrvrvlr klvedllevs rldagaevae rarvplaela eesaarlgve arviaggnpv
      301 aetdprrldr ilanlvlnah rhgappveit igvttgghvi evrdrgpgfp aelldggper
      361 frtgaaergh ghglgltial gqarvigael slantpdgav avlrlprgpa g
//
LOCUS       WP_357593965             175 aa            linear   BCT 28-DEC-2024
DEFINITION  3-hydroxyacyl-ACP dehydratase FabZ family protein [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357593965
VERSION     WP_357593965.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 175)
  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 10002379
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..175
                     /product="3-hydroxyacyl-ACP dehydratase FabZ family
                     protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18880
     Region          29..167
                     /region_name="FabA"
                     /note="3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier
                     protein) dehydratase [Lipid transport and metabolism];
                     COG0764"
                     /db_xref="CDD:440527"
ORIGIN      
        1 msaveseavp agatgrdtps epgptmgfte ikswlrhrhp mlyldrvldy epgvrlvssl
       61 svsaqtdaia ghfperaifp ashlsqafaq sgiilfqlst srladdeltl igsmnsrffr
      121 ivapgdtvti tvqadrllga tfffsgravv gsttvaafra slvrrkaadm ghqww
//
LOCUS       WP_357594022             402 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Micromonospora
            parva].
ACCESSION   WP_357594022
VERSION     WP_357594022.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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..402
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..402
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=41557
     Region          201..351
                     /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 msgrkfpgfd vdtvteavsp ppldelhata rsrrrrsvgv vatalvalvg lavvpmvsgs
       61 dratpaeppp psggsvsqlt ltgptsgvdv rhegcvvrfa ytgdggrsws dwdaarfegt
      121 rcaagtaagt pgsgtdfsvl gersylvtds gvthlstdyg rtwrdgnsai vavpafpvta
      181 rpvlcgfgcg plseplavdp ssgtvyrlta aapswrplfs lypaadgsiw atyrmgggqg
      241 stvarsadrg atwtsweagd dagviaavgl ndregyvlte psatgdgvrl lrttdgaktw
      301 tdtgaelsnq ihydltvgsd gsllvitpgg gtepdpparl lvsrddgrhf tvareygrlv
      361 gsvsvapgfa wlfgsddgpt gepdhvlvtt dgstwtrfsl ap
//
LOCUS       WP_357594025             180 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357594025
VERSION     WP_357594025.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 180)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..180
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..180
                     /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=19083
     Region          5..167
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 msaarnpaer rrriveaacd lipevgvggl thrlvaarad vplgattyyf ktlgdlveaa
       61 leaaaeltae wlrrwagela saadvpatla vltaaylrer drmvtwnemy aaaghrpelr
      121 plarawndgl tevlaahvgp eaarraavfv dgavlhalvn ddpldqdala galaalmaqp
//
LOCUS       WP_357594030             191 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora parva].
ACCESSION   WP_357594030
VERSION     WP_357594030.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=20822
     Region          16..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 mdsdgtslpa sadltirlrp vaepdlamfr rlrtepglig ldwagftdag aparrfavdg
       61 ylgeddgrli veveqeraaa givsytagcy agrasywsig ivllppwrgr gigwraqall
      121 cdylfqhtpa qriqagthpe nvaeqraler agfqlegivr asefragewr dgylysrlrd
      181 dpspwdagtg g
//
LOCUS       WP_357594060             916 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357594060
VERSION     WP_357594060.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 916)
  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 916)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 916)
  AUTHORS   Rosinski,J.A. 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 916)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..916
                     /organism="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     Protein         1..916
                     /product="helix-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=97235
     Region          <1..875
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          857..913
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlqgresela avdallagar egrsgalvir gdagigksal layaaerarg gltvlrgsgv
       61 eqemelpfag lhlllrgvld gadalpdgqa ralrgalglg qappgtdrfl vglavltlla
      121 glaeerplav lvddahwldh ssaqallfaa rrleaegval vfaardddrp faapgvpelr
      181 lgglaaepaa rllrehapdl apavceqvmg qaqgnplali elpatlspqq ragalpvqav
      241 gsgslpapgr vlrtfherla alpddtrtll aiaaadsgel glvieaarrl ggsleavtpa
      301 etarlihiad gtlhfrhpla rtaayrqvpi tvrlavhral adaldgrpda atrrawhlaa
      361 aatgpdesta lalersaeea rgrggyaavs aayeraaqls agrdgrgrrl aaaaraaaes
      421 gqhqraetla gqalpqladp lelaqlaetr amiatargrn dqahpalaaa aralstggdp
      481 aaatelyfea mttawlagdf palaaiaaqa atspegarah plwravaglg slatdeperr
      541 lpwlrevieg vrataepdgl qqraqlaiwd mligddhasr eraaalehdc rtagaigvlp
      601 valllkarae mlsgrhrear asageglrlt rdteqsqyad lltgitayls aiegdedqvr
      661 eltglisgsd dpgsvgmrya alnlidlvrg ryepvvrrag dyalhapaar tmmllhrapd
      721 vveaaarlgr ldvartvnrr vqiwapltgq pwaravglrc tallsegada drayadavrl
      781 hrhggrifer artellygew lrrerrsgqs rpllesamei feslgsrpwa erargelraa
      841 grrhladpar rdrsdladll taqelqivrm aadgmsnkqi aarlfisprt vgyhlhkvfp
      901 klnvasrgel arlrld
//
LOCUS       WP_357594101             326 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC023979].
ACCESSION   WP_357594101
VERSION     WP_357594101.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC023979
  ORGANISM  Nonomuraea sp. NPDC023979
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC023979"
                     /db_xref="taxon:3154796"
     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=35843
     Region          21..321
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrqtsarlll llsllqaqre wsgpalaerl dislrtvrrd ierlrdlgyp vhvtkgpgat
       61 yrlsagtdlp pllfdddqai avslalqlap kavvgfgeaa aralatirqv mpprlraqid
      121 amritaiana wefpgpsvet gpltmvgaav rerevlrfdy atteaeagwt pplrvephrl
      181 lvwsgrwylv awdldraewr vfrvdrivpr mrtglrfqpr elpmpnvaay vkthldrgdt
      241 veewacqgva ilevsaasia ewvpggavve eigpercrls mgawswvgla alygtfaadm
      301 qvigppelia acgelatrya avqaph
//
LOCUS       WP_357594094             425 aa            linear   BCT 28-DEC-2024
DEFINITION  cupin domain-containing protein [Micromonospora parva].
ACCESSION   WP_357594094
VERSION     WP_357594094.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..425
                     /product="cupin domain-containing protein"
                     /EC_number="1.14.11.47"
                     /GO_process="GO:0043687 - post-translational protein
                     modification [Evidence IEA]"
                     /calculated_mol_wt=45432
     Region          33..315
                     /region_name="RoxA"
                     /note="Ribosomal protein L16 Arg81 hydroxylase, contains
                     JmjC domain [Translation, ribosomal structure and
                     biogenesis]; COG2850"
                     /db_xref="CDD:442098"
ORIGIN      
        1 mtyldppggh hgrpavssae ataalarcvs vepakfaaah wghtpllsra adlpdpagft
       61 dllspadade llsrrglrtp flrvakdgql vaaarwtggg gagaeigdqv ldervleqya
      121 sgatlvlqgl hriwpplvdf ardlglalnq plqinayltp agsqgfathy dthdvfvlqv
      181 dgrkhwrihp pvlpdplekq qwggradeva ataqgpaald vvlapgdaly lprgwlhsaq
      241 aqdasslhlt vgiraltrya lveellalaa edqrlraslp fgtdvadpda iepeltetve
      301 alrdwllrtd pgavaarlrq rawpaarpap irplaqadal atlnadswva lrpglrwqlv
      361 phdpetvalr lfdrtitlpv gceaavrvll agavtrvgdl pglpddadrv tlarrllrea
      421 vlipa
//
LOCUS       WP_357594193             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357594193
VERSION     WP_357594193.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=36051
     Region          4..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msrtrterlv nlvicllstr rfltaaqiaa tvpgyehdpd dardheafqr kferdkaelr
       61 elgvpletgt asafdaepgy riahreyalp dillepdeaa avgiaarlwq haglaaaass
      121 glaklraagv dvdpqatlgl epmvtvdpaf apltaaardr revgfdyrvp drdapsrrrl
      181 qpwgvvcwrg rwyvvghdqd reatrcfrls rvvgavrvtg apgayeppan vdlishvarw
      241 sgpvertgra tvlaapgraa glrrwalevt agpdgdrlvl pyadpdelag hlvgygpdvr
      301 vldppevrea viqrlkeiav rhdelavggg ar
//
LOCUS       WP_357594226             297 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Micromonospora
            parva].
ACCESSION   WP_357594226
VERSION     WP_357594226.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=32348
     Region          9..295
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtnpalprrv vvtgatgklg ravvahlrav gvdvlavdra ggrdprdvng eflladltdy
       61 gqvveaftgg adehagrvda ivhlaavpap glmsnsttfa nnsaatynvf aaaraagikq
      121 vvwassetvl glpfdtpppy apvdeeyapr pestyslnka leeemarhfc rwdpelvmvg
      181 lrfsnvmdve dyapfptfda dpqlrrwnlw gyidardgaq averalaydq pgaevfiian
      241 adtvmtrssa slmaevypdv eirkelgehe tllsidkarr vlgyepqhsw rdhvdvl
//
LOCUS       WP_357594263             854 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357594263
VERSION     WP_357594263.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 854)
  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 854)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 854)
  AUTHORS   Rosinski,J.A. 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 854)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20189366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..854
                     /product="helix-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=88598
     Region          <102..633
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          653..835
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          777..832
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mimndlavpg ltvdkglqal ldtvaqnptg plavgiagpa ghgktallae lervhqragi
       61 avqtaapepg apvdtdtvll vddahlldda rigallrlva grrhrlvvah rpwprsaafs
      121 elvdalrrdg qavlltpftr eqtaahlaat pelgrpddlv dfvhtqtagv prdverlarg
      181 lagvesrtga mvdpprsvil efapdldvqp tgvrrlllav aaggtlpvsm lgallgrdpa
      241 gvdeliattr aagllgadgr lapivrrava tlspaterta vwrrltelql arggavlplv
      301 rsllavgalg dcpaatlaaa agealadepa faaelfaaat aagqppnarq alaaalagdl
      361 ddalrladrl lattappdrs eaamvaatal ahrghvgrsv elfrwsgtas arafaivggi
      421 atgdpaaste spagdpagep ptlhasaarl madgvresvt gpptaalsal vqaaallepd
      481 gravllpdsp aalaaltamh cgeleiaerv lhralaagvg gplmarrhrl lqawilmvrg
      541 eihaagerlt tvtldgrhle srdqlfaaai rmgigrrnsd lgalkrgwgq aleavvrhpv
      601 dlftllplge laiagarlgd larlepylqq gralldglgn pplwsvplhw sglhaailtg
      661 eptvaddhva allaaaghsr yaavvaaaae swvevlrgvv dparveaaar glhdtglcwd
      721 garlagqaai rtadrramtt llecaralqg rpsggpagqt pptgasttrv agptqhglsd
      781 reyevaelvl agltyreigd rlfisaktve hhvarmrnrl ncanrtella llrtlvadra
      841 sdtagqpwpq ragr
//
LOCUS       WP_357594294             428 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora parva].
ACCESSION   WP_357594294
VERSION     WP_357594294.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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 428)
  AUTHORS   ter Beek,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..428
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..428
                     /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=45476
     Region          33..406
                     /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(145,147,271,273,308..310,353)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrcrlvigts lavvaamslt acggdggged sktvrvtlvn hvwtenirka lpefekqsgl
       61 tvdvtqlged qlsdqynvkl nagsddidvm myrplqegkl faknkyladl servksdsaf
      121 evgdfqagpm qattyedtvv glpiiteqev lyyrkdlltk sgftappktl delkaqaaki
      181 eadnpgvagf vartgkaaav tqfssflfsf ggdfvdssgk atvnteqakq ayayyggllr
      241 dhgpenistd mswseamaif tqgkaafyte anslyknatd ptkskvvdtv gfaafpagpa
      301 gskpynipsw algvndssen kdnawkfiqw aagkeqalaq qtagvpgart svwanpagta
      361 sypkdlaean tvstangvgh drplvvkvae areivgqpiv daitgkdaaa saetanaafq
      421 kflddeak
//
LOCUS       WP_357594300             251 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357594300
VERSION     WP_357594300.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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 251)
  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 251)
  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..251
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..251
                     /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=24879
     Region          4..243
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrcdglvavv tgggsgigla cvrafaaaga rvgvldlels glpedpgvlg vradvadras
       61 lstavasvaa afggvdilvn nagisavgtv eedddarwsr vldvnvsgva rtsavalpyl
      121 rrsssaaivn issiaatvgl prralysask gavhaltlam aadlvtegvr vncvapgtvd
      181 tpwvarllag aadptaekrq lasrqptgrl vtadevaaav vylaspatgs vtgsslpvdg
      241 gmsglrlpaq r
//
LOCUS       WP_357594352             713 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora parva].
ACCESSION   WP_357594352
VERSION     WP_357594352.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..713
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=76986
     Region          70..361
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
     Region          413..713
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mrrrlsaaft agviataavl lapqpaaadt pwldvsedry asftvpaayv qeklgtvsqv
       61 vvegnfgpsa swaefgltrr gdvwsgvlga lepglytyql taddtltikd ptnstgvasd
      121 pllstflvag dsarwlvdap agtggkietl tyrtgnaqrs avvwtppgya akgpkgypal
      181 flqsgagvaa tdwldlgrsk qildnlsaag amspmvvvmn nadvsdakev kdlrkavtdt
      241 yrvlrdpahq aiagvsdggt qalraaltkp gqfahvgwfs gssapeidrk darainrsvk
      301 llrlytgnvt dpaynatyrl tkaldradvr fefdgvnpdg ganwttwqen lvdfvprlfr
      361 dvrdhgpspg hqplkreftp ppagttptpf vtedgfvtfe tttdftaaqh vtvwanvapg
      421 gswlrlplkr dgdrwratvg plkpwfyyyr livdrvavkd tsnptkvtte pmwstffipg
      481 pgarllsdvp agqggtvesm tysstvagqd rtalvwtppg ydpgreqpyp vlylqhgggq
      541 nytdwvemgr akqildhqfl dgdltpmvvv mgngnssnfn relrenivpt arsryhissd
      601 psqqalagls mgggqafgvl kaypgefayv aafsagfgss tgvdaaainn gtkmlrvyvg
      661 dqtdfvypsf maslttmdnl giryefdgvt pgphgwdvwq knlidlaprl fkr
//
LOCUS       WP_357594373             237 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357594373
VERSION     WP_357594373.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   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 237)
  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..237
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..237
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24629
     Region          6..236
                     /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 mpdpqptivl vhgafaesas wngvlermga aydsvavanp lrslagdaay vrdvvrgigg
       61 pvilvghsyg gmvitqaaag dtsvralvyv nalapdtges alslsgkfpg stladtlvqy
      121 pvstggneva iaqdryhaqf cadasgdmaa lmartqrpit eqalgdqltg dpawrslpsw
      181 fvfgdldkni pveahrfmae ranprgqrel vggshamava kpsevaesvi eavrgvs
//
LOCUS       WP_357594417             308 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora parva].
ACCESSION   WP_357594417
VERSION     WP_357594417.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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 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
REFERENCE   4  (residues 1 to 308)
  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 308)
  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..308
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..308
                     /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=31785
     Region          1..251
                     /region_name="fabG"
                     /note="3-oxoacyl-ACP reductase FabG; PRK05653"
                     /db_xref="CDD:235546"
     Site            order(12,14..15,17,36..38,89..91,140..142,155,159,185,
                     186..187)
                     /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 maldgkvaiv tgagrglgla yarelarrga svvvndvdae atadavaaie asggravavv
       61 apvgptetat alvstavehf grldilvtna gvlrdtvlwk msdddfdtvi nvhlrgtftt
      121 vreavrhmrq ageggriicv gsptgqrgtf gqtnyaaaka givgmvrtwa lelqragita
      181 ntvvpvaatt mtatvpyfaa avraeangep mpaffrhelg fgtaddaagl vaflgsdaaa
      241 svtgqvigvg gdrlqiwthp eaaltahrdg gwtydallea wpttfagaaq svgerfpklp
      301 eefeppts
//
LOCUS       WP_357594437             338 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357594437
VERSION     WP_357594437.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=35979
     Region          101..335
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrdvllifai algaalgigl agavllralr rssitvhlnv lltttvvava vgvmavaeam
       61 flsthdtevv litvaaaavv slavgghfgr rlaraavwrd qarererqle kgrrdlvawv
      121 shdlrtplag lramaealed rvvrdpdtvd eyhrrirvet drmtrlvddl felsrinaga
      181 lrlsltavpl gevvsdalas tvplaearri kliasesgwp tvaasepela rvvanlllna
      241 vrytpvdgtv rieagreedq awlsvadtcg gippddlprl fdiafrgepa rtpgpgdgga
      301 sgglglaivr glveahggrv evrntpdgcq fmvrlata
//
LOCUS       WP_357594434             175 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357594434
VERSION     WP_357594434.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=18504
     Region          21..160
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdddriadiv gqwgrerpdl dptplliigr iqqlaaalda alrppfaaad lgngdfdvla
       61 alrregqpyt ltpgqlsqrm lvttgavtkr vdrliarglv srsvstadar grvvgltpag
      121 valtdrliee hlaneaailr gltdsdrkal erllaaidrn lasqdrgpeg gsptg
//
LOCUS       WP_357594449             230 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine hydrolase family protein [Micromonospora parva].
ACCESSION   WP_357594449
VERSION     WP_357594449.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..230
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24291
     Region          20..205
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mltiasarpg pyafdiatta llvidmqrdf lepggfgesl gndvgqlrrt iaplaallad
       61 aravglsvlh treghlpdls dcpaaklsrg apsrrigdpg pngrilirge yghdivdelr
      121 plpgepvvdk pgkgafhatn ldvllaergi rsllvtgvtt evcvhttvre andrgyeclv
      181 ladcvgsyfp efhrvgldmi aaqggifgwv adsarvraal ptnpvlqpss
//
LOCUS       WP_357594543             298 aa            linear   BCT 28-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Micromonospora parva].
ACCESSION   WP_357594543
VERSION     WP_357594543.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  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 298)
  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..298
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..298
                     /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=32705
     Region          9..282
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 meaapakter aavaerllts alrtsydptv eidwdaphtp gaywlppqrs slygtplwer
       61 lseeqrvdlt rhevasaasa glwfetilmq mlireyyrad ptsrqaqfal tevadecrhs
      121 imfgrlieam gcpvyrastv dhhlgrflka tasgprmyaa iliaeeilda fqreitades
      181 lqplirmvsr ihvveearhv rfareelaaa vaatgpvgma yarllvgraa ytianrlvhp
      241 dvyaavgipp avgraaaran phwratlrws aarvhanlag vglvagpgrl lwaragli
//
LOCUS       WP_357594570             329 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357594570
VERSION     WP_357594570.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 329)
  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 329)
  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 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   5  (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
REFERENCE   6  (residues 1 to 329)
  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 329)
  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..329
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..329
                     /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=37159
     Region          32..329
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mtstlrpppp apprspqeah spaprpprrg rswrqalrrd wqlyslailp llfflvfryl
       61 pmlgniiafr rfkpggsifg eywvglryfr mfltdptfwe vftntlvlga ltllfcfplp
      121 ivlalllnev rarrfkrfvq svsylphfls ivivaamvmq ltsiegtanq lvslfggdpv
      181 aflqkpewfr tiyvssevwq tvgwgtilyl aalttidedl yeaaridgag rlrqtwhitl
      241 pgirptmmtl lilnigsfla vgfekillly npltyptadv vstylfrmgf qssnfsyaaa
      301 iglfeavigl ilvlsanvis rrtvgtslw
//
LOCUS       WP_357594483             161 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357594483
VERSION     WP_357594483.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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..161
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..161
                     /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=17784
     Region          1..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpdeprwltd herdawlala klmfnlpsal daqllrdnhl tlfdyfvlsg lsmapgrtmr
       61 lsdlashlsc slsrlsnvvk rleqrgllrr tpdpenpryt vasltdagwd lvvtaapghv
      121 aavreyvidg ltasqidvlr evachvtrri seapeagtrt p
//
LOCUS       WP_357594590             267 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357594590
VERSION     WP_357594590.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (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
REFERENCE   4  (residues 1 to 267)
  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..267
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..267
                     /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=29682
     Region          8..263
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          182..263
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maarlagshv sawrpavagv aevfhahfvd hayprhihev wtllivddga vrfdldrhrh
       61 galrtsvtll pphvphdgss atpdgfrkrv lyldtsalda eltgravdep dladpqlrdr
      121 ihhlhqalaa pgdefeaesr lalildrlrr rlrqrppvdg qpagrglavr lrelldartv
      181 egvtlgeaaq llhahpthlv rtftqvygvp phsyltgrrv elarrlllag qrpvetavaa
      241 gfydqahlar hfrrylgvsp aryparr
//
LOCUS       WP_357594678             198 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora parva].
ACCESSION   WP_357594678
VERSION     WP_357594678.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=21466
     Region          6..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          90..176
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(93,106,108,119,124,128,162,164,176)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 manedsaala avgprlralr hrrgttltql adltgisvst lsrlesgsrr ptlelllpla
       61 rayqvaldel vdapatgdpr vrpkpivrhg vtylpltrrp ggvqafkqif ppdpsaggri
      121 pqvhegyewl yvlsgrirll lgdrdltltp gevaefdthi phlfynpgpg taealslfgp
      181 qgerihvrar paspdkql
//
LOCUS       WP_357594674             464 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora parva].
ACCESSION   WP_357594674
VERSION     WP_357594674.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=49083
     Region          6..461
                     /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 mtdqpeefdl lvvgggkagk tlsmdvarsg qrvamvergm iggscinvac iptkalvtsa
       61 raarqlrdas algltvdggr vdvdllrahk qdvvegmvaa nrqqfldsgl hlvigearfv
      121 gprtvrvala dggerllrgt dvvintgtrp hlpsvpgmae agvltsdqll rldrlparlv
      181 vlgggtvgve faqmfasfgs avtlveggpr lltredpdvs davmrvfldd gidvrvgvav
      241 arvdrdpdga lrvtlddgav vigddvlvaa grepvtdglg ldvagvrlse rgfvevdehl
      301 rtsaehtwaa gdvagspqft hvslddyrii ranlaggrrs ttdrlipytv fttpelarvg
      361 ltetearrag ydvqvahlpv aaiprartlr qtrgmwkvvi dtgtdrilga allgaeagev
      421 itsvqlamla ampwtalrda vithptmteg lnllfasles rpvr
//
LOCUS       WP_357594685             337 aa            linear   BCT 28-DEC-2024
DEFINITION  LacI family DNA-binding transcriptional regulator [Micromonospora
            parva].
ACCESSION   WP_357594685
VERSION     WP_357594685.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..337
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36014
     Region          9..335
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mteatmrdkq psmtdvaraa gvsaqtvsrt lrnspnvnae trrrvlnave qlkyryngap
       61 rllssgrsft lglvllqagg yysrsgvtag veaaagqagy svsiatiael dtalmeksll
      121 klsdqgvdgi iiavplisvt qrmeditrdi ptvtvdgsrt tgarvlgidq heagraatqh
      181 lldlghrqvw hvagpdewie arqrrqgwqe claaagidap palegdwspe sgyrlgqila
      241 mipevtavfv asdemafgli kalrergrsv pqdvsivsvd dielaaychp plttvrqdfy
      301 rsgaaavall ldsgsegesl tpatlivres taaprpr
//
LOCUS       WP_357594717             339 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora parva].
ACCESSION   WP_357594717
VERSION     WP_357594717.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..339
                     /product="phosphotransferase 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=36750
     Region          9..279
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtavsptqqs ltsadvahll gasfgpgtqv rdagpltggg yatvwwalld dgrrvvlkla
       61 psaetpllry erglcaaeer yfrlvaerap qvpvpavlwh gtdpaygewl vtellpgrsl
      121 vdlaeaggav ddgparydlg valaalhqvt gnrfgydggr aagatwraaf tamldellad
      181 aadwdvrlpv tpqhlhellg rhadvldevr rpallhfdcw dgnvlaapdg dgrlrlcglv
      241 dgerflygdp lldlvsprlf qraeddpehp llrgyqaaap rplvldasar rrltfyrlhl
      301 yllmtvemps rgmtaqthpg ryaqltalld eeitalasa
//
LOCUS       WP_357594737             187 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora parva].
ACCESSION   WP_357594737
VERSION     WP_357594737.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 187)
  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 187)
  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 187)
  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 187)
  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..187
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..187
                     /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=20677
     Region          7..177
                     /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 mfavpltedv elrplepwra eeflanldra rehiqpwvsp tfvatdlssa ravlqryadr
       61 wasdsggiwg lwwrgtlvgg vllvsfdvtr gvcevgcwve paaegrgmva pavrrivdwa
      121 vrergiqrve wrtnadntrs kalagrlglr ldgtlrqvap gpngridlev wsvladewla
      181 gspatvh
//
LOCUS       WP_357594750             327 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Micromonospora parva].
ACCESSION   WP_357594750
VERSION     WP_357594750.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..327
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..327
                     /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=35131
     Region          1..326
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mrafryhrpa dvaeavavlt aepqaaylgg gtnlvdlmkl gvqrpdvlvd vtrlpldtve
       61 elpdggvrig atvrnsdlaa hpvvrrdypv larallaaas gqlrnmattg gnllqrtrcv
      121 yfqdtgkacn krepgsgcaa lhgqnrdlav ldwseqcvat hpsdlavala aldtvvevhe
      181 sdgardipia hlyrspgthp erettlarga litavrippl paarrstylk vrdrasfafa
      241 agsvaavldl dgdvvrdvrl aygavahrpw rayraeeelr gqrfspelaa raadaelaqa
      301 rplrhngfkl pltraitvra ltelass
//
LOCUS       WP_357594742             147 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            parva].
ACCESSION   WP_357594742
VERSION     WP_357594742.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..147
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16261
     Region          18..135
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mttttaaqkr aqakveydaf laqcpsrkli driadkwvtl vlaalnsdgs hrfgldcagk
       61 prsmrysels rllagvsqkm ltqtlrsler dglitrtvvp tvpvtvsyel tdlgislhhl
      121 mrglkswaet hmddvlanra tydnrda
//
LOCUS       WP_357594756             432 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora parva].
ACCESSION   WP_357594756
VERSION     WP_357594756.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 432)
  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 432)
  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 432)
  AUTHORS   ter Beek,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..432
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..432
                     /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=45371
     Region          8..348
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msrrhlgift aavlaaaslt acggsgddsa aspktltywa snqgaslead ktilqpeldk
       61 fekqtgikvt vevvpwsdll nrllaaaasg kgpdvvnign twsaslqatg alvefddatl
      121 qavggkdriv paalaaagap gkppaavply smayslyynk kmfadagita ppttweqvae
      181 ygrklstggk wglaieganp senahhaftf sqqyggewfd sagkptfdtp qnvsaikryi
      241 dfmaadkitn psnaeyaqnq svsdfangka amllwqsags nlktqnmpad aygvapvpfl
      301 anppaggkkv nsmvaginma vfkhtknkdg alsfvkfmts deeqtilnkt ygslpavkta
      361 aadpafsate qktiqetlvt taaplpqvpd estfetlvgt amkelfadaa sgkpvteesv
      421 kakltdaqqk mr
//
LOCUS       WP_357594759             440 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Micromonospora parva].
ACCESSION   WP_357594759
VERSION     WP_357594759.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..440
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..440
                     /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=46168
     Region          6..439
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 madalrvvvv gagfsglaaa laltragaqv rlleardrvg grvltrwlpd vtqldlgaqw
       61 igptqdrmya lvaehglttf asaafgaptv lwagqrraep paqaarvlgl ldeyaarldp
      121 aapwqapeag qwdrtvlggw lratagdddt adylgrvlag gllatgtdev sllhllfylr
      181 sgggtgpllg maggaqqdri vggppalaer maaalppgvl tlatpvrave qnvdgvtawt
      241 dtgrvdgdfl vvalpptlag riwyapplpa qrdgltqrmp mgsalkvhav ypepfwradg
      301 fsgvststtg pltetvdnst ptsplgvltg fsyasdaavl remspeqrrr clldafaavv
      361 gpragdpvdl veydwttqew trgcfcgalt pgawsaygpr lrapvgrvhw agtetatrwt
      421 gylegavrag eraaaevlag
//
LOCUS       WP_357594765             541 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357594765
VERSION     WP_357594765.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..541
                     /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          2..540
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 msaltgttrl arlvlrrdri rlaiwilgtp llgyalagsv agiypdqdar lgyattsass
       61 lvarafngpi hgtdlgavvv aetyvtlali vallstfavt rhtrqneetg raellganvv
      121 gryapltaal lvivaanala aallavalvg aglpfagsva aaaaiggvgv aftaiaavta
      181 qlsvtargan alaaatvgls fvlraagdvl geqsadgtrv rsawpswisp lgwgnqvraf
      241 dgerwwvlal pvalllagva layalaerrd qgagliaprr gpatgaplll spvglawrtq
      301 rgtllgwavg vtalglpmgv aadefndmid anpaaaeain amgggddlik ayltamlglf
      361 altigayvvq allrvrgdea dgvleaalat avsrtrwlgt qvlaatlgav allllagvtt
      421 glgygivigd plgqavelgg aallrlpall vvagvvtaff gllprwsvvl swtallvfll
      481 lgqlgavlel pqaalnvspy thvpavpavh paalplvvla avaallltag vaafrhrdvp
      541 s
//
LOCUS       WP_357594821             386 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora parva].
ACCESSION   WP_357594821
VERSION     WP_357594821.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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..386
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..386
                     /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=41895
     Region          149..284
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            order(177..183,205..206,232..234)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mpqpldaalt evrallldpa ltravaagrr rgrrptvera elrpvtlkag priqittsdg
       61 arpytrniaa gpeaaaavde llaepfgnwh vetadatlql rvtksgeaqv hraatsrpaa
      121 tptgndrtke ylldpgdpif aeiggsaakr rqvdaflral aatlpddltg plrvvdlgcg
      181 nayltfaayr yltgrgldvq lvgvdvredq rrrntelaqr lgwadqvsfv agtiadavvd
      241 papdlvlalh acdtatdeal aravrwearw vlaapcchhd lakqlrahpa papyelltrq
      301 gilrerfadv ltdalragll rlhgyraevv efvdsqhtpr nllirarrtg agptgaqrae
      361 yrelvdqwqv kprletllaa deasas
//
LOCUS       WP_357594836             399 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            parva].
ACCESSION   WP_357594836
VERSION     WP_357594836.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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 399)
  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..399
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..399
                     /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=42931
     Region          8..395
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpyphgglar hanlppgerl rvllveddeg daflvgella etnsmidllv atslrearqr
       61 igdvdcvlld lglpdaqgld glrqllemss gaavcvltgr tdehlgvvav aegaqdylvk
      121 gqvdgvlltr alryaverkr adenarrlre velrqaesar lergllpqpl mttdqvtvht
      181 fyrpgrhaal iggdffdvvq thpdrldliv gdvcghgvde aalgvelrva wralvlagvp
      241 ddevlpaleq vlmserrlqe ifatvasvrl dldanratvr laghppplll sggrvapvpa
      301 pggrllgvrp rrpiaydlef dtddwsllmy tdgliegrvd agderldvpg lsgllgepan
      361 rsvslpelpa wlvgraeqln ggpladdvam llvsrgggr
//
LOCUS       WP_357594855             289 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora parva].
ACCESSION   WP_357594855
VERSION     WP_357594855.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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 289)
  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 289)
  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..289
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..289
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30796
     Region          32..256
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 marsrkvtvs tdaeghtagw aetdlapvsa pdptgaaffd vdntmmqgas iywfarglas
       61 rnyvttadla rfawqqlrfr llarehagdm slakeaalaf vegwrvneve hlaeeifdel
      121 mapriwagth qlaqrhldag qrvwlvsaap veigrviaar lgltgaigtv aevvdgaytg
      181 rlvgdlmhgp akaeavtqla avegldltrc aaysdsandl pllsvvgrav avnpdgvllr
      241 qarrhgwevr dfrtgrravk iavpstaaag lvagavtagl alqrrrrag
//
LOCUS       WP_357594877             332 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357594877
VERSION     WP_357594877.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..332
                     /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=36714
     Region          17..317
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtvqldprpp vapvagtprr ssgrlsrldt rfspylyiap fflifaifga yplaytfwvs
       61 lhdwdllgad hpfigaenyt rlladpdfwh alvntlgifv istvpqllaa lwlanllnrg
      121 lrartgwrma vlvpnvtsta avaivfgvlf grefgmvnwl ldlvgldaie wksnrfaswv
      181 aisamvdwrw tgynalilla amqaiprdly eaaaidgasr vrqfwsvtvp llkptiifct
      241 iiatigglql fteprmfhsg tnpirggplr esqtltmymf enafaphynf gygsavawll
      301 faliaivalv nvlilrrlgg rsgpdgrkga ar
//
LOCUS       WP_357595000             313 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora parva].
ACCESSION   WP_357595000
VERSION     WP_357595000.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..313
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34717
     Region          <52..>96
                     /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 mtdasdhtdg gdhtdhtnha dggdhtdegs gtdggngvel grtlralrrr adlsqrqlae
       61 rsgvpqptla riesgrsadp rfrtverlvr aaggqlaigt ptaiagitep tpvphddmrd
      121 eadrrypahl dvwpvheprd wpgawwaewy rlpperyplp lppaayelnr ryrdnrrwga
      181 evqrtaqvrr vfgndlpats wryvaelpdg klvgelrahe rspflefgew hpgmperemv
      241 ldgvlvdary rrlglgrrlv talitgmrea giddaaaiae gfgielllac gfeiegprpa
      301 alrlgqpgkr cfs
//
LOCUS       WP_357595077             248 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357595077
VERSION     WP_357595077.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  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 248)
  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 248)
  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 248)
  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..248
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..248
                     /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=25224
     Region          1..243
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrrldgknal vtgamggigg aiarrlaaeg aavglldvad taplaeelta rgdralsvvg
       61 dvsdeadwta avnavrdhlg pvdilvstay avqvapahet srqswdhqlg vsltgsflgv
      121 raclddlrar sgavvlissv halvglpgrp ayaaakgglv algrqlavey gpqvrvntvl
      181 pgpiltaawa dvseedrqrs vaetvakrfg tpdevattva flaspdaayi tgaslvvdgg
      241 wtavkasa
//
LOCUS       WP_357595082             843 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357595082
VERSION     WP_357595082.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..843
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..843
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=88602
     Region          <10..841
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 midggedktr gggsptpvrp erlrgpvefv grtaelarlr rlvatppcli llegepgigk
       61 srlvaellae lpgrhlvgec ddvpepfplg vlldairgnt erpgplspva galapllpel
      121 advlpdappp ltdpaaerhr lfravaavla alspatllle dlhwadpatc ellaylsthp
      181 vdglavllta rtatpgsstp ihdalartpp wsvtrvalsp ldaddvrrla artlrlddpp
      241 qqltaalldr tagipfvvee vlrtlaergg dpladdsvpf vlrdvllwrl rpldeatrev
      301 lgaaavlgmt pdqrilaavl sldrvaigaa ltaahragll hdagdglrfr hdlarqvvyd
      361 llpresrewl hlrvarvleq elprpvaqla hhyrragsga dfvrnaeaaa dlatergdda
      421 taasfllqtm dvaelprpvr vrlaaklgrs aidglsqaea ipvlerllad rrlppgarge
      481 lglvlgrmlr qqgealrgyt eieravpylr aprrkapala vlaapdtvvg rhvddhlarc
      541 teaeaaaaas gdpgshlavr iaraslllel gdpaawaiit elrasielad rpreharacl
      601 nwaqgalhag hpaqaealla agralvdetg yerlaslvea tqlsldraag rldglaerlg
      661 rlvasaermp vtlldarael atvlaltatt anagstnaaa anataanagt anagtaaglg
      721 drtggldvve aaeralrevv adarrvgaiw plvqalsala rltvtgqpde avrhateals
      781 vvrgkgilaw aadavlvlae aaaargepar aaaavaelea giagrdtpla raalrrcrel
      841 vpa
//
LOCUS       WP_357595141             301 aa            linear   BCT 28-DEC-2024
DEFINITION  transketolase family protein [Micromonospora parva].
ACCESSION   WP_357595141
VERSION     WP_357595141.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..301
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31274
     Region          2..299
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mtatvsarea yrleltelaa ddprivclea dlggpkhcfq dqfpdrflnl giaeasavdi
       61 avglasaglr pfvstfatfa alragesvkl glgylgapvv lvspyggvsg awfgpthhcl
      121 edlavmqslp gvriavpage aetreairaa adgdwpcyvr lgrnevfdas fapagrgavt
      181 wvnpmggdtc vvsigekpta lcqaateqqp dlghahlcwv deesltlalp qladarrlvv
      241 veehraagsv astlalllpd revlsvnaga dwpaeggnhd etlaalgltt savlsavlkg
      301 k
//
LOCUS       WP_357595126             145 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl-CoA carboxylase biotin carboxyl carrier protein
            [Micromonospora parva].
ACCESSION   WP_357595126
VERSION     WP_357595126.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 145)
  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..145
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..145
                     /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=14934
     Region          <64..138
                     /region_name="AccB"
                     /note="Biotin carboxyl carrier protein [Lipid transport
                     and metabolism]; COG0511"
                     /db_xref="CDD:440277"
ORIGIN      
        1 mpegnadpld aavrslarli gstpgpvrra rlqhgdlvve vewpdgagvv aaapaappve
       61 adaglhyvca pmvatlylap spgadpfvre gdqvvpgqqv aileamkmmi pveadragev
      121 vkvlvpnatp veygerlial avsed
//
LOCUS       WP_357595350             652 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Micromonospora parva].
ACCESSION   WP_357595350
VERSION     WP_357595350.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 652)
  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 652)
  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 652)
  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 652)
  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..652
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..652
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=70636
     Region          48..626
                     /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 mitrrgllaa gatggaaali pagwaasgra faaaasldar dipkyvtplr ippamptvat
       61 dperdtyeia vrqfrqqilp pswprttvwg ygstahpgsf gypaptimar vgrpvrvtwv
      121 nqlvdhrgdh lphllpvdpt lhwanpaggi ehrdrhgrwd gspqgyrgpv pqvvhlhgah
      181 ssqesdghae awylpvardl ppdfavsgsa yrefrsrfae rsglrwapgs atfeyandqr
      241 pctlwyhdht lgltrenvya gpagfyllgg gdelpeealp gpaptradpp nasyhdiplm
      301 iqdrsftadg qlrypkrysa sgdgppvavp gfsgstivvn grtwptltvq rrryrfrlln
      361 gcnsrfllls vaahatarpa rpvlpvwqig sdggflpepv phervslgpa qrvdaivdft
      421 dvpagtelyl vnegpdgmyg ggrpgvdfpp adpqttgqvl rfvvtdaaga dpsvppeqlr
      481 lpahprlgaa qrvrrlslne rgsggstvml lgvldergrg lplrwsdpvt eqptlgdtev
      541 wevrnftrhv hpvhlhqvqf ellgrghsgr srpgladrgr mdtvlaypwe vtrikahfdl
      601 pgryawhchl lehednemmr plnvlprdga aagdggaaag aegagtastd ag
//
LOCUS       WP_357595351             511 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Nonomuraea dietziae].
ACCESSION   WP_357595351
VERSION     WP_357595351.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 511)
  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 511)
  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..511
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..511
                     /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=55282
     Region          4..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(173,176..181,183..184)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(176,293..294,315..320,398,410,413,424,504)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(176,217..218,265,267..268,271,293..294,315..320,398,
                     410,413,421..424,485)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(217,267..268,271,293,421..423,479,485)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mlnlsivled sartapddta ivfgdmrlpy smvdtianqv anllvargig kgdkvalacp
       61 nlpyfpfvyf gilkagatvv plnvllqpre iayhlddsda kalfcfegsp elplgergka
      121 gfeaaegceh ffvlpatala tesaygesiw aalngmagef qtvqtapedt avilytsgtt
      181 gqpkgaelsh qnmlmnamvs demfprtpgg dtylavlplf hsfgqtvvmn tgfrrrstiv
      241 lmprfepgea lalmtkenvt ffagvptmfw amltkihaeg vpvpsalrva vaggasspve
      301 vlsdfqqtfg vdilegygls etspvasfnq lgrptkpgti gtpiwgvemk lidsdwktie
      361 gegpgeiair ghnvmkgyyg rpeatdevmn dgwfrtgdia trdadgyyai idrakdmiir
      421 ggfnvyprel eevlmthpav slaavvgvah eshgeevkay viltagasit eaelvdwcre
      481 nmaaykyprv iefrdslpmt atgkilkrel r
//
LOCUS       WP_357595408             529 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D family protein [Micromonospora parva].
ACCESSION   WP_357595408
VERSION     WP_357595408.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..529
                     /product="phospholipase D family protein"
                     /calculated_mol_wt=59043
     Region          13..412
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
     Region          270..410
                     /region_name="PLDc_vPLD1_2_like_2"
                     /note="Catalytic domain, repeat 2, of vertebrate
                     phospholipases, PLD1 and PLD2, and similar proteins;
                     cd09105"
                     /db_xref="CDD:197204"
     Site            order(375,377,390,392,403)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197204"
     Site            375
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:197204"
ORIGIN      
        1 mplqdwflta eeranpvsgi pvwttgnlae plihgaayfd rlvdevealg agdhlfftdw
       61 rgdpdqllrp dgptvaqlfa qaaqrgvvvk gliwrshldv layseaenrd lsetvsaagg
      121 evlldqrvrr ggshhqklvv lrhpgaperd vafaggidlc hsrrddaahh gdpqpvqmsq
      181 rygpnppwhd vqlavrgpvv galdtlfrer wtdpmpldse npmaylrdrl rgsdlrpdpl
      241 peqpadpppc gphqiqvlrt ypavrprysf apdgertvar gytkavrrar rliyledqyl
      301 wsaevadlfa halrdnpelh liavvprhpd vdgklalppn mvgreqalsl ceraapdrvh
      361 vfdvenqagg pvyvhakvcv vddvwasvgs dnfnrrswth dselscavld etpdqreptd
      421 pagrgdgars fardlrlrlw rehldrdpdg rddadlldpa davaavtaaa dalqrwhddg
      481 qvgdrppgrl rphrperlpw ytrawalpvy rlvydpdgrp lrarlagtw
//
LOCUS       WP_357595384             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            parva].
ACCESSION   WP_357595384
VERSION     WP_357595384.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..416
                     /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=44227
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..371
                     /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"
ORIGIN      
        1 mleelaqaea avagclgasa walaehdlva aldaahrleq rlaavklalv reldgrgsat
       61 aqgasstavw lrerlhlgvg varrmvelaa tldaapagvr dalaagsvdv eqvrviaatv
      121 etvhsaagte vadkavgvlv dwaaqfdatq lrrlgtrild hvapdvadaa aeaalrades
      181 ratrdrhvti seqtdgrlrl tgildpeaat llrtaidpls aptgpddtrt sgqrrhdala
      241 evcrlalrgg elpdhggdpt qlavttsydg ltrqlgtgal dtglqltpea vrrlacdaai
      301 lpavlggsgq tldvgrqrrl vtgplrralv lrdqgcafpg cdrpprwcda hhirhwadgg
      361 atsldnavll cghhhrhlhh sdwsvrlggd ghpefvpptw ldpdrlprrn qyhrrt
//
LOCUS       WP_357595428             955 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Nonomuraea dietziae].
ACCESSION   WP_357595428
VERSION     WP_357595428.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13307259
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..955
                     /product="glycoside hydrolase family 3 protein"
                     /calculated_mol_wt=103773
     Region          1..822
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
     Region          840..946
                     /region_name="CBM6_xylanase-like"
                     /note="Carbohydrate Binding Module 6 (CBM6); many are
                     appended to glycoside hydrolase (GH) family 11 and GH43
                     xylanase domains; cd04084"
                     /db_xref="CDD:271150"
     Site            order(856,867..868,921)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:271150"
ORIGIN      
        1 mkraflalal vvslsafttd apvyqdpsrp laervedllg rltpdekisl lhqsqeaipr
       61 lglpyhkngt ealhgvgwsn dhgdgwkqkf asgtifpqav glastwnpel ikrvgaatgd
      121 evrgyaaenp elwgtqvwap vvnllrdprw grneegysed plltgaista ygkglsgddp
      181 vylktapvlk hylannneyq rsltssnlpp rvkheydeaa fkpaisadaa tgvmgsynlv
      241 ngrpntvnpd qdevvrtwtd kvlynvsdaw apqalyqven yypdeptsya atlkagqdsf
      301 tvdgmdtapm tasikaaler glitqadidt avrhvlsiri rlghadpggg pyakitkevv
      361 dspahralnr rtaaeamvll rndgrlpldq drtrsvavvg plqdrlhrdw yggalpyqvt
      421 pkralaeraq vtgldaldrv alrhtatgky vtasadlaqa vtvgadrtaa aqwdltdwtg
      481 gvstlrnaas gklltgnwga flansdepdg wfvqqqfrfe kqgdgsyliq yvgyevnesw
      541 wsipehyltv redgtlamga kadaarfame vvsdgvkqav eaakgadaav vvvgshpfva
      601 greihdradl tlgasqlrli eavqranpnt vvvletgypv tvtakallwt thagpetgha
      661 vadaifgein pagrltqtwy rssdlpdild yditktgmty lyhrgdplya fghglsyttf
      721 gyqglkvtkd gqvsvrvtnt gsragdevvq lythqqrsrv vqpvkqlrgf qrislrpges
      781 revrftlkke dlalwdvtrg rwtvesathd vlvggsssai rqratlqvag eripprelsk
      841 ptraidfddy kgvrlvdlsk ergeavggka gdwlafkdsr lgsaftaqla svtggsvevr
      901 lgsptgrllg tlqapatgdv ytyatamtpi tpvrgvhdvy lvftgdvrvg tftla
//
LOCUS       WP_357595461             218 aa            linear   BCT 28-DEC-2024
DEFINITION  FMN-dependent NADH-azoreductase [Nonomuraea dietziae].
ACCESSION   WP_357595461
VERSION     WP_357595461.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 218)
  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..218
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..218
                     /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=23429
     Region          6..192
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkritmpqll hidasaihdg svsrqvarsf rdawegevvy rdlgarpvph lteagivarh
       61 apaqehdaeq ataaflqeal veellqaeay lfavpmynfg apstfkawld qvlipgrtlg
      121 mspddspiag rpatlisvrg gaygpgtpre gwdfadpylr kiltevfgle lrvitaeltl
      181 adttpamagl reaaaasqaa ahvaarehar risarslv
//
LOCUS       WP_357595203             326 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357595203
VERSION     WP_357595203.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..326
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35350
     Region          1..322
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnpheagfap dladrlkapa aelhglvimk dgrlvlehyg egedhswgvs hgvvdfgpdt
       61 lhdlrsvtks vvsllygial adglvpephe pllahfpeyp dlaadprraa lrvehaltmt
      121 lglewredlp yttpenseia memasdrhrf vldrpivaep geswnynggs sailarlvvk
      181 gageplpefa rrrlfeplgi trfewmagdd gvhsaaaglr mtprdlallg qavleggagv
      241 ipsswleqal rprvelgegs aygyqwwlgt grpptlsang nggqrlvlyp elglvvamta
      301 gryddpdswr apqavldvll eartea
//
LOCUS       WP_357595515             215 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357595515
VERSION     WP_357595515.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 215)
  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..215
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..215
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23019
     Region          11..>76
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpgssttpwt aaytrlvadn vrhhrtrqgl svqkladrct amglpmersn laklesghra
       61 svtvpellvl ahalntppll llaplgrads veilpgveat pqeavfwldg taplvhgdde
      121 gadaraelqs lrdhqrlvde wsahtraaga araraedekd phraawaeaa rtqaeqaght
      181 adkighlrgt irlrgltlpd vppglthldg ppfst
//
LOCUS       WP_357595555             244 aa            linear   BCT 28-DEC-2024
DEFINITION  response regulator transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357595555
VERSION     WP_357595555.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 244)
  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 11450879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..244
                     /product="response regulator transcription factor"
                     /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=27246
     Region          <155..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 mitparytel lglagqlcrs aeagvdlgti aellrtslel picvfsevdf akgltigygw
       61 petvftddlm teattrnarg hplvrhyvls gdltpleitd tvsmrqwrss regsdlyetv
      121 gvlhhlavpl tapagamrsf alsrgrerft aqdrafverl hpllvaldeq hrravpshlt
      181 prerdvlgll rrglsrrama rrlgisqrtv dkhlenvyrk lsvpdrmaav rfgrerrtps
      241 dlal
//
LOCUS       WP_357595599             170 aa            linear   BCT 28-DEC-2024
DEFINITION  HIT family protein [Micromonospora parva].
ACCESSION   WP_357595599
VERSION     WP_357595599.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..170
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18590
     Region          33..159
                     /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(58,60..61,68,70,116,124,126,130,132)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(128,130,132..134)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            130
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 madglerlwt phrmtyisge drpaegyekp tgcpfcrgpq lppeqslvva rgehvfvvln
       61 lypynpghll vcpyrhvady tdldvpetae laaytqtamr virkvsnahg fnlgmnqggv
      121 agagiaahlh qhvvprwggd anfmpvigrt kvlpqllgdt rdllarawps
//
LOCUS       WP_357595621             415 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357595621
VERSION     WP_357595621.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  AUTHORS   ter Beek,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..415
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..415
                     /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=44156
     Region          31..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(138,140,271,273,301..303,344)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrrvvtgial aalltltacg ggetpqegav titmwtraat qaqserlvka ynaghknqvk
       61 ltviptdnyq priaaaagak qlpdvfaadv ifvpnytsqg lflditdrin alpykaglap
      121 shmklgtmdg rqytlphtld lsvwfwnkdl yakagldpek gpktlkefae hatavqdklg
      181 gdgkvhgtff ggncggcyvf tfwpsvwaag gqvmnaegta slndqaamse vfaiwrglyd
      241 ksvtgptake eqgptwtgyf akgeigvmpm psttlglmpa dlkigvapia gpsggestfv
      301 ggdsvgisst tehadaawef lswtvsdeaq vevmaknkdv lartdlaana hsakdprvvl
      361 inslvakgqt pyaprfgqtf ndpqgpwlrl areamfgdtt kvarlnaevt aslqq
//
LOCUS       WP_357595643             445 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357595643
VERSION     WP_357595643.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..445
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..445
                     /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=47923
     Region          3..391
                     /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 mtarrdeiai igaglagcla acflarrgyp valyerrsdp ragvaergrs inlalsergl
       61 dalrriglae qvmtdalpmr grmihpvege qqfqsysaag drainsisrg alnnalldea
      121 aalpgvrvvf dhrlvgldpv dgtlsfetpq gavaakasvv lgadgagsav rgqllaygll
      181 desvdfldyg ykeltipplg gdfaldpdal hiwprgtsmm ialpnpdrsf tctlfwpndg
      241 agsfasltsp aeierhfaeh ypdvvplapn lvddyqhnpv gvlgtvrctp wqvngkvgll
      301 gdaahaivpf ygqgancafe dvveldrcld ecaddwlaal plfqrrrqen aeaiatmalt
      361 nfvemrdkva spvfqtrrrv ehaleralpg ryvsqyelvs fsttpyaevl rqvrrqhrvl
      421 gavvggaall lvgaigaaln rgrra
//
LOCUS       WP_357595650             188 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357595650
VERSION     WP_357595650.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 188)
  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..188
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..188
                     /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=20309
     Region          9..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgervlprae rrrrtegkil daaralfael gferttirav akaaevdpal vmqyfgskqq
       61 lfqqavrvtp agdgeltaee lveellgtln vkmgalpqss lammrsmlth peaaasarqv
      121 lgsqidrlae aipaddarlr aalmttimlg iavghqllel eelrevsqde iarllrpslr
      181 altggpeg
//
LOCUS       WP_357595656             641 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357595656
VERSION     WP_357595656.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 641)
  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 641)
  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 641)
  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..641
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..641
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65763
     Region          3..387
                     /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 mvseaksrwa paalligtav lyvwglgasg wansfyaaav qagsqswkaf ffgssdaana
       61 itvdktpasl wpmvlsvrlf glnswamlip qalmgvgava lvyasvrrlf tvwagvlaga
      121 vmaltpvavl mfrfnnpdal lvllltaagy cvvraqerga trwlvlagsa igfaflakml
      181 qaflvlpgfa lvylitapva lrrrawqlll agaamvvsag wwllavalvp aserpyiggs
      241 qtnsvlelal gyngigrlng adygglgnln qqagwlrlfd teaggqiswl lpaalallaa
      301 atwltrrapr vdpvraafwv wgswlvvtgl vfslmqgifh ayytvalapa iavlvgmgaa
      361 llwerrslrl aamvtagtav wsyvllsrsa dwnpwlgvvv lvaglgaala mpftrrtlav
      421 vavasvacla alagpaayav dtaasphaga iptagpstgg fgggfpqpgg gggqrfrrlp
      481 gggqalrqpp ggaqgqggaq gqdgggfggg gmgrggagmg gllnagtpaa eltallktga
      541 saytwaaatv gsnnaagyql asgqpvmavg gfngtdpapt ldqfkryvae kkihyfigtg
      601 mdggrrstgg sddaariaaw vqetftgttv ggttifdlsq p
//
LOCUS       WP_357595664             335 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357595664
VERSION     WP_357595664.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 335)
  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..335
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=35500
     Region          120..334
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrpgpsafyv wiavawfpay dllrqpswvg alglavfaaa ylaairmafg egpawaplvv
       61 laavtfalgm ayggkwlylc plvsmacgvv vreraapyal ggvtvvsmlv tlrsgggeda
      121 vaavawgtfv agvvvhvtlr lfeareelar aavlrererf srdlhdllgh tlslvvvkae
      181 avrrlaprda daaarqagdi eqigrralae vrsavagyrg rgladelaaa rlaleeagvr
      241 aevmleeirl spdadallgw avregvtnvi rharatgcai tlrdegervl leiandgaaq
      301 aftrgnglkg laergaavea raedgrfvlr vavpk
//
LOCUS       WP_357595700             294 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357595700
VERSION     WP_357595700.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=32015
     Region          2..288
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrrlrvlepl awvgpavvli alvvlwpvie mirssflkis rfgvvqgsng lanydklfge
       61 kdfadimvrs viwvvavval tvlvslalaq lfnqrfplrk varwaliapw aasvlmtaii
      121 fkwmldpevg vinqirlklg lidamggasa dqlgdastam pwlvfvavfv svpfttyall
      181 aglatipadv yeaakmdgag rfrtywsitl pllrpaltva alinvmnvfn sfpiiwamth
      241 gqpgystats tilmfilkgs nigesaamsv vnfgmviilt aiflkvsrwn keva
//
LOCUS       WP_357595754             346 aa            linear   BCT 28-DEC-2024
DEFINITION  copper resistance D family protein [Nonomuraea dietziae].
ACCESSION   WP_357595754
VERSION     WP_357595754.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..346
                     /product="copper resistance D family protein"
                     /calculated_mol_wt=35186
     Region          134..>344
                     /region_name="PcoD"
                     /note="Putative copper export protein [Inorganic ion
                     transport and metabolism]; COG1276"
                     /db_xref="CDD:440887"
ORIGIN      
        1 mtvtevrpva ragarmpggl ilgglvlaav vsvvvastlt aeeavpgipm pgplveyglp
       61 ivrvlldlaa avvvglsllp kllgfddpgs tepvmsrara havtaawiwa italvtivfy
      121 taelnpgvvp slgmiatyvg tvgagqgllf stacalayag igllavrfge kvpaelrivi
      181 alfgllpvpv tghavdsvwh dpimismelh vmgaavwtgg llavaamvap rgdllalalp
      241 kfskvatisl alvslsglvs glstmalttg velpgdlvas eygllvlakv alvallipla
      301 anirwrlmpg iaarrkssia awaamelvvm glaygvaval trapig
//
LOCUS       WP_357595756             429 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora parva].
ACCESSION   WP_357595756
VERSION     WP_357595756.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=46021
     Region          9..428
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpdsgypwpi qtsrldnglr vvvsedrtap avavnlwydv gsrhepagqt gfahlfehlm
       61 fegsvnvakt ehmkliqgsg gslnattnpd rtnyfetvpa ehlelalwle adrmgglvpa
      121 ltqetldnqr dvvknerrqr yenvpygdaw lrllpmlypp ghpyhhatig smadlnaadl
      181 atfqafhqty yapnnavltv vgdatatdvf aladkyfgal parddippap dgrnvpatgq
      241 tavetvsadv paprvyiahr sypfgspgyd vitvlatvlg sgrgsrlyqr ladgeriaqp
      301 dlvgaygvdl ahgpapliat atarpgvsae rlaeglaevv delatvpvts aeldrakall
      361 stgwwrqlst vdgradllgr yatqsgdpar vadhlpalla vtaeqiaeaa advlatdrvt
      421 ltylpeets
//
LOCUS       WP_357595766             207 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357595766
VERSION     WP_357595766.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 207)
  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..207
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..207
                     /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=22159
     Region          12..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mradarrnrd riveaaravv aergidapme liarraevgv gtvyrrfpdr haliaamagq
       61 yvheiddalt raeaqepgpw aavrsfvmws adqgrgalaa aladlpqelf dampeftrvk
      121 sgmvgrldal vaaaqergdm radvgvadvm rllslftcha dlpqeraahy llvmldgmek
      181 rpdgagkrpd gagdglggaq ekggars
//
LOCUS       WP_357595790             266 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357595790
VERSION     WP_357595790.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=27478
     Region          3..246
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mrspktafvt ggasgigral atalaakgva vtvadlvapd lrgmehveld atsaeavasa
       61 vravrqrhgr ldfvfnnagi avgghaeelt ldhwnraidv nlrgvvhgvh aaypimieqg
      121 yghivntasm aglvpaplml pytaskhavv glsmalraea aahgvrvsvv cpgfidtpll
      181 dnanpglpyt etgaqardaa vmaqgrlypv eslaadilrg varnraliva pasarlawra
      241 arlspsgair aaalairrvs pppkrt
//
LOCUS       WP_357595778             315 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357595778
VERSION     WP_357595778.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 315)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..315
                     /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=34324
     Region          26..307
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mvktapgvlp alrvaapppp rarrgltial fllpavvlfa llvlapilla fyagffkwng
       61 mgglpqdfvg ldnylrlfas evfagdlrnm gllvlaslav qlplslgial llnqrlrgra
      121 gyrllffapy vlseavtavl fsmilapder glanailgaf glsstwfadt stvmpalflv
      181 mtwkyfgfht llylagrqsi pkelteaaqi dggtpwqvfr hvtlpllgpt irisvflsvi
      241 gtvqlfdlvw iitgggpsha setmavtmme fgfkrlqigy asaisvvmfv lslvfalwyq
      301 rfvlrrdleg atvnr
//
LOCUS       WP_357595836             334 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptidase [Nonomuraea dietziae].
ACCESSION   WP_357595836
VERSION     WP_357595836.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..334
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35377
     Region          1..334
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mmvadthndl lmavsarapr qwaeffrsrw lpqlrqggvr lqvlpvfids qfrpegslrq
       61 tlrmiecahv iaegnadava lcldaaqida alaedrialv lamesmpgid asveliptmh
      121 rlgvriasia hwgrtpladg sgedatgsgl tshgvealke merlgilfdv shlgasgvah
      181 vlelatrpvi athssaralr dhhrnltdeq irgvagtggv icvnflaafl tenareatld
      241 hlldhiehiv gvagidhvgl gpdfmdevlr dltppccegv sssgidnrav ipglagpggl
      301 plvgegllar glpkadvrki lggnvhrlfg kala
//
LOCUS       WP_357595841             156 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357595841
VERSION     WP_357595841.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=17069
     Region          8..129
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtsstvqsdt gdglmwnhml tlyahvehsl gtalqrrhgl glseyraldl ladaddgelr
       61 mqdlasrlgl nqssvtrlvs rlnaagytyr dlcpddkrgv ytvitdagra rhrearstya
      121 qvlstaldea arqnpllntl lttarplftt spqdgh
//
LOCUS       WP_357595853             160 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357595853
VERSION     WP_357595853.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 160)
  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..160
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..160
                     /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=17517
     Region          3..157
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mndlvraaqg gdtmamnell dlltpyvtri cgpialadgp daaqealiai fkglrglrep
       61 aalygwarai avreavrvar rsrhtvefed dlpssadleq aadirdllar lspehravlm
      121 lrdveglder aaaellevpv gtvksrlfra renfrkawss
//
LOCUS       WP_357595939             738 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357595939
VERSION     WP_357595939.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   3  (residues 1 to 738)
  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 12993552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..738
                     /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=74971
     Region          13..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,37..38,71,76,81..84,96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,79,95..98,102,104,141,143,
                     145..146,148,158..159,162,179..182)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,79,95..98,102,143,145..146,
                     148,158..159)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,102,104,141,143,145,162,179..182)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(158..166,175..182)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <276..430
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          <359..>543
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
ORIGIN      
        1 mgdpsesrli ggryllaeel grggmgavwr ahdqvldrpv alkqvlvpgw mseqdreraf
       61 ervlrearat arlrnpyvit ihdvvvdegh pwivmellpa sslaqvlers gplseyvvad
      121 igvkllgalr aahaagithr dvkpanvlll ddggvvltdf giahvanspt ltatgmlmgs
      181 paymaperle gepageasdl walgatlyta vegappyamd spvavmaail mreprpmrrg
      241 mrlrpvvegl mrrspeerlt leaasaalvv vagrrhgeea rrregsrala llvrqdqidp
      301 dpptdplraq pqdpgpaspa pdpptppaqd tpdspapsaq dapgspappa ptasgwstpp
      361 spgglesptp pasgtpglsa ppaqddpgsp apraqdasga pasapgtpgs hvppaqdapg
      421 spaprtqdas gaptppapgt pglsvpssgv rdafspggpg apapaarggh gvassprape
      481 tpatstpgtp gsaasrspgr seaadplpgp vpplspagta spagtagaei lreaparsag
      541 ergparegge gggaaavvvr glrfgavtsa tlgvlayavp rvarrmgtel tllapgtall
      601 vlfaavalla vvlprdllpd ggvnatltra lpfvafagyl ggyqtgatah vttslayall
      661 aawaattsar twrrsraaaa vaaaatacma altvahlwid lagrsalttr llealpelta
      721 agwalhtawa wwaarrpg
//
LOCUS       WP_357596036             276 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357596036
VERSION     WP_357596036.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=29123
     Region          1..275
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkpalnqwtt krwtvaeavd gcvrhgleai glwrqevaaq glaesvrlvr daglrvsslc
       61 rggfltsgsk ealddnlrai deaaelgaac lvmvvgglpg ipagqapsgg fsrdlagara
      121 qvaealsvla pyagergvrl aleplhpmyc adravlstlg qaldlaspyp ssqvgvvvdt
      181 fhvwwdpsvy eqiarageri asyqvcdflq plpsdvllgr gmmgdgvidf apltkavlea
      241 gytgdievei fnadvwaadp dtvmatmker faalva
//
LOCUS       WP_357596067             288 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Micromonospora parva].
ACCESSION   WP_357596067
VERSION     WP_357596067.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..288
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..288
                     /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=29235
     Region          <113..223
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 msdalsapla evvaasphrs avleaaglls wdggvpvahp slvpadgptg ssvvqarlss
       61 lrqavaaaaq epsgprgagw aelddevllh qgrasaatgr alatrvvpel pglaerlgsa
      121 dgrvldvgtg vaglavalar alprasvvgi dvlqraldla rgelaeagev adrislrrqd
      181 vaevaepggy dlvwlpapfl peqtltvalp rlvqalrpgg wlvagtnppa gdplraavdr
      241 wnavrnggna fdadrmaqvl aatglvdvrr fptvpggpvl vaahrpvg
//
LOCUS       WP_357596086             256 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Micromonospora parva].
ACCESSION   WP_357596086
VERSION     WP_357596086.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=25326
     Region          40..233
                     /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 mdavslstll aaaamagwvd avvgggglll lpallvaapg lpvatalgtn klaaifgtat
       61 aartyarrtt ldwrvvgpaa glavlssgvg aalagavpas ayrpvvlvvl vavaafvllr
      121 prlgvlpvph rrtptrvaaa iavagvgial ydgligpgtg tflvlafttl lgsdfvhgsa
      181 makvvnagtn lgalvvfavt ghvwwllgag mavcniagav lgarmalrrg sgfvrvvlvv
      241 vvaaliaklg hdqwva
//
LOCUS       WP_357596115             275 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357596115
VERSION     WP_357596115.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 275)
  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..275
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..275
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28995
     Region          16..273
                     /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 meqpttaans sedpamhlaf dqsadtgpav vclpmfstsr aatatafhpa ltgtglreiy
       61 ldlpghgdtp ahcpptsqav ldticawldq hidapvllag gsygaylaag iarqrpdlvr
      121 glllvcpgvt iarhsrdlpa dppldaptgw ldaaptalha hldaalghrt pavvatvlaa
      181 lnsggpgdat fqqelqtgpg yalpdedadv vfdgpvsvit grqdriigya dqframrhyp
      241 rgtyaaidaa ghylpyeqpt llrtltqdwl rrard
//
LOCUS       WP_357596141             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357596141
VERSION     WP_357596141.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=16084
     Region          19..135
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mestapqspa glhttpswll nqaaahasrl isegfaahel rgyhyrllaa laeggpasqa
       61 dlgrrcgidr sdvvaavndl agrglvvrap dpadrrrnvi sltdagtdea hrmtdtvgrv
      121 qddllaplst aerdqltrll trllehharr
//
LOCUS       WP_357596129             296 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357596129
VERSION     WP_357596129.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 296)
  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..296
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32979
     Region          25..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(30,34,59)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(33,58)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(40..41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          111..291
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 meaaenvrpl spaqgggptv lrillgaqlr rlrtakgisr edagyairas hakisrlelg
       61 qvsfkerdva dlltmygvid pddrarliel arqanqpgww hkysdllpgw fevyiglega
      121 asiirtyenq fvpgllqspd yaravislah drapagemer rvalrttrqq rltgerplsl
      181 wavldeavlr rtiggaqvmr aqvehlieas elpnvtvqvm pfdrgghaaa ggpfsilrfp
      241 eselpdvvym eqmssalyld klaesehytk vmdrlsvqad tpaesrrfle rlrkiv
//
LOCUS       WP_357596198             182 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357596198
VERSION     WP_357596198.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 182)
  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 182)
  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 182)
  AUTHORS   Rosinski,J.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..182
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..182
                     /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=19561
     Region          7..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          103..176
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(105,107,118,121,126,160,162,174)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mepqpamdad prvvgdrlrr lrqergvsls elakhsgvdk ailadaetgt hnptletlwa
       61 itaqlgvpig alladppepq imrgtameae llevfederv tyelyrvtvp pgltqtspah
      121 hegvsehvtv ftgtlsagpi depltagpgd hiswvsdvph gyrargpdvv ratvlirypa
      181 kp
//
LOCUS       WP_357596179             171 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357596179
VERSION     WP_357596179.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 171)
  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 171)
  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..171
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..171
                     /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=18801
     Region          32..158
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtttpdtvdq hierwqpvvp dldadvegav trmirltrhl ravkervlvd ldlpaheydt
       61 lhalagrggr aapsdlaadl amapasitar vdtllrrgfv rrmpstvdrr rvdvelteag
      121 raawqgamev qgaeehrllg altaterrhl sdllrrvllv aeqppsapet d
//
LOCUS       WP_357596216             219 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora parva].
ACCESSION   WP_357596216
VERSION     WP_357596216.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..219
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22935
     Region          1..191
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mirgavffdv dgtltptssg qhlaelvgna keiaqiqagy aagtlssdes cvleargwas
       61 rtpaeaqayl esmplvdgia etvswcrahs lvpvlatlaw dfvgthlcsr fgfdracgpr
      121 lqivdgrysg evaeqfdeha krdfavrvaa elgvdlrhca aigdgrsdvp lfgvvgcaia
      181 fnatpearaa asatvngpdl havvpglstw letialpvn
//
LOCUS       WP_357596221             233 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Nonomuraea dietziae].
ACCESSION   WP_357596221
VERSION     WP_357596221.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 233)
  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..233
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..233
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=23451
     Region          1..143
                     /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..65,68,74,76,78,89..91,93,95,104,106,108,110,124..128,
                     130..132,134..136,139)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176853"
ORIGIN      
        1 mkvagsavlg idrdrvwdal qdpavlvrti pgcerleetg pgtyrmtvsa gvasikgvyq
       61 gevalseplp perfvlrarg qgapgtveat vevrladvdg gtridydaea vvggmiggvg
      121 qrmlgsvakr tagdffsave shlispptea taagsgsaap pgaglpsgta vpalaapata
      181 agpgggqvfe rpsqdrqhtq trpwvmlaaf gmgagialgs aaigwvlgra grr
//
LOCUS       WP_357596268             169 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357596268
VERSION     WP_357596268.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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..169
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..169
                     /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=18216
     Region          24..151
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mrqaprrdgg dpvdqaaage ligrefamai vvfheavgql lglsaverkc ldllqrlgpv
       61 tagaigehtg lttgavtrmv drlskagyvq rcpdphdrrk vvvqllpner mdalmaaafg
      121 pfvgditaim grydadelsa ildfvrrttd allantrrit rldpnrpdg
//
LOCUS       WP_357596281             334 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357596281
VERSION     WP_357596281.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10169647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..334
                     /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=34955
     Region          1..334
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(40..42,45,142,146,168..173,191..192,196,211,
                     236..237,256..257,281..283)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mrsyhldsga gidglairwh ddpvpgpgqv lvavravsls yrelmvlrgd yvlpvkpdvv
       61 pvsdgageiv aigsgvrtar vgdrvtatlf pswqdgpfga qhlpqrggsl dgmltelavi
      121 dedalvpipd hlsyeeaatl pcaavtawna ltgdgdglrp gqtllvqgsg gvslfalqfa
      181 kalgarviat tsspakadrl aelgadatid yratpdwpam vreltagqga drivdvtgll
      241 dqslkavaia ghiacvgfvs dtappidprv lfasgatvra vavgsraqfl amnraiedhr
      301 lrpvidrvfa fdeasdayry yasgkalgkv virl
//
LOCUS       WP_357596367             335 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357596367
VERSION     WP_357596367.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 335)
  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 335)
  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 335)
  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 335)
  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 335)
  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..335
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..335
                     /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=35928
     Region          29..314
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrtvaeleer larpsdglvd dlarldgdim ilgaggklgp slvrlalnat kgsrrvvavs
       61 rfsepglaed laregatvvs advadeqalr dlpdvenvvf lvgakfgtqg aehatwftns
      121 ylpgrvadrf rdsriaalst gnvyplvpvt sggateetpa dpvgeyamsc lgrervmshf
      181 sekygtrlal irlnyavemr ygvlvdlaqk vhagepidvs tgmanvvwqg yanevtlral
      241 lhaqappftl nltgpelisv rqaatdlgra mgkepsfvge eantallsna archrlfgyp
      301 elapaeliel tarwvadggp llgkptkfer rdgrf
//
LOCUS       WP_357596409              63 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF362 domain-containing protein [Micromonospora parva].
ACCESSION   WP_357596409
VERSION     WP_357596409.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..63
                     /product="DUF362 domain-containing protein"
                     /calculated_mol_wt=6357
     Region          1..60
                     /region_name="COG2768"
                     /note="Uncharacterized Fe-S cluster protein [Function
                     unknown]"
                     /db_xref="CDD:442050"
ORIGIN      
        1 malvtidacq gcgaclrtcp thaitpvagg ltvradrctg clecleicpv dairvvepse
       61 gar
//
LOCUS       WP_357596390             240 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357596390
VERSION     WP_357596390.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 240)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..240
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25303
     Region          33..240
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 mtafdargli geltvtldvd vlvgayadrd gppgdpssvl aalgenrigv gavaslraal
       61 fdlrsgndev lalpgvvpvg aldlrdpigs vremerlaar gvkavrlfpd eqgveagfps
      121 vrhvarraaa lglvvltggd vrrfwqpfsg leakvvfldt hfyhlgdflv vaadepgfht
      181 strllnspda letvpadrll ygsrtphyep lvpllrlats glkpeeitav aggnarrllg
//
LOCUS       WP_357596375             288 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357596375
VERSION     WP_357596375.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 288)
  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 288)
  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 288)
  AUTHORS   ter Beek,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..288
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..288
                     /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=31954
     Region          24..286
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrhrlrdpvt gllfvlpvlv lflifrifpt lgaagmsltn wniggewdvv gadnyvrlwn
       61 dpnfwaslrv tlvyaaifvp ltvlvslgta lllnavifmr glfrsmlflp yvtsfvfagi
      121 iwrwiyefdg llnglltkvd lgpvqvless slvlpalavv scwkgfgysm lillaglkai
      181 pgsymeaarv dgasawqrfr sitlpllkpa lffvlvieti ssfqvfdtiy vmtgggpaka
      241 sytliygiye rgfrffefgy aatwgmvlfa ivlaisliqr rflgkgnt
//
LOCUS       WP_357596413             315 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357596413
VERSION     WP_357596413.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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 315)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..315
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..315
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33654
     Region          54..293
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mpsrtydlll amfrefreng kdvtldeerl gaeavgdlyq dvpgitdevh pfgrllspae
       61 prddlvilfi hgggfrigta kngrqagvhl aastgarvll pdyrlapehp ypaalddcea
      121 ayldaldrwp earivvgges aganlaaall lrrrdaadtr aaagflycgv fdlrlenyar
      181 gswqanadtd liikpssgpi msadylagrp ptdgyaspal adltglpplf iqasgaelll
      241 ddslalavqa aragvevele vwphmqhvwh latgflpeat eavdrtvafi qrvaegrvvd
      301 gvalsggpas feevm
//
LOCUS       WP_357596465             242 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora parva].
ACCESSION   WP_357596465
VERSION     WP_357596465.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..242
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25198
     Region          57..236
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 msdsapshwd pvpsprdgrl tarhhppvap grtglvpmtg rdgerlalgy vpepagdgsa
       61 yrlvlllhga ggsarqgldl llpvadgqhl llvapdssaa swdliaggfg advrridall
      121 atvfdgypva dvtvggfsdg asyalslgla ngdlidavva fspgfaappv thgrprvfis
      181 hgvddrvlpi dvcsrrlvph lrdlgydvty eefpgghdip vpvrdsavtw ltghppragt
      241 rp
//
LOCUS       WP_357596417             252 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357596417
VERSION     WP_357596417.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25972
     Region          1..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 merltdrril itgagsgiar attlrllaeg arvvaadisa aalnetaela gndrltvstv
       61 dissedsvns lvseaaaelg gldalinaaa ilrgahthec slelwnrvig tnltgtflmt
      121 raalpylles grgvvvnfss taaffahpfm aaysaskggi fsfthsiase ygkrglravn
      181 vvpggissgi tdnighlvpe dtdwdlflkl tpalpggipg pekvagvvam lvsddgsfit
      241 gteirvdgga hq
//
LOCUS       WP_357596488             210 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Nonomuraea dietziae].
ACCESSION   WP_357596488
VERSION     WP_357596488.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 210)
  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 210)
  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..210
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..210
                     /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=21921
     Region          <50..206
                     /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 mvwaaaltgf vvgvlvrala dgfepdpvdp raearrafag lpgrvrlakp viepataavf
       61 allawrmepv ylpallyaaa vgsalavidw rtqrlpdvlt lpsypilall llptgrltda
      121 llggaallll ygvlwfvrpt amglgdvkla gligmaagav gwnawvaaal agqllgalya
      181 iallvlrrad rsaefpfgpf mlagalclaw
//
LOCUS       WP_357596527             610 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Nonomuraea dietziae].
ACCESSION   WP_357596527
VERSION     WP_357596527.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=67842
     Region          4..610
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtmtatrtqt iatrvrrrae espgavamry kdfgiwkevg wlaywthvel vahalmalgv
       61 epgdrvavhs enrpewlyad latvairgit vglyptnppa evayllsnsg akiliaedqe
      121 qvdkalavid ecpdldrivy leprgirgry ddprlmswee llamgaerag pleermagae
      181 pgdvmtliyt sgttgppkgv mltvanvefa vrtlvenggf tspppserdl ivsylplchv
      241 aeraftvwfn saagvqvnfa esidtvqanl revqptilfg vpriwekila qvnikidsas
      301 plkrlttrlw lrvadrigdt lvrtggrhtm gtralyglgw lmcyrslrer lgmrrvryaa
      361 sgaapiapdv lkfymgigva mhevygmsen taiatgnrpg rirlgtvgep qegvelride
      421 ltgeiltrhp gtfagywrnp ratadvlded gwlhtgdvge wvegthvrit drmkdilita
      481 ggknvapsem enalkaspyi keavvigdqr pylvaligie ldtvgewarr rglsyttyrd
      541 lseksevrel vqgivdevnq rfarveqvrr faflpkeldh edgeltatqk vkrsaiaklf
      601 eelvegmyrr
//
LOCUS       WP_357596500             312 aa            linear   BCT 28-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357596500
VERSION     WP_357596500.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=33646
     Region          1..310
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mrditvfsgs ahpelaeeic shlgtplhpv rierfandvl evqlqancre rdvfliqplv
       61 ppvqehlvel llmldaarga saarttvvlp hyafarsdkk daprisigar lvadlmvtag
      121 anrvlamtlh spqvhgffsv pvdhlhalre laahfrqydl sntvvvspdl gnakeaahfa
      181 rllgtgvamg akqrfsddrv vissvigeve gkdviildde iakgstviel ldrlrergar
      241 tvrvacthgl fasgaverls alpevveivc tntvpppkps ekltvlsiap alaeamrrih
      301 dgesvsalfn as
//
LOCUS       WP_357596556             445 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357596556
VERSION     WP_357596556.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=47404
     Region          127..436
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtvatvalfg vvllvgvvti cltlpswara qlvdradeas rmvttlidtr piqgpipsqg
       61 evfllqvvda kgevvaasat legeppltra vpvggdsril drvcraggen clivvgtsnr
      121 staygpavay aavresavln vpllavilga aalvllalmg waawigvgrv lapverirsg
      181 leqisatdlg drmpvpdtgd evarlavtvn dtlgrleeav erqrrfvsda shelrtplta
      241 mlvrleacav rpdpdecaqt leealgdarr lsaivqdlll marldegtrp teelldlgkl
      301 vademdrrsf rlpftacvep rlmvrgnrlr ldrlvtnlls nadrhggqav hvtvsrrgde
      361 gvvevhddgp gipedqreai fqrfarldta rsrdhggtgl glaiardiat ahggtlrvgd
      421 sakgarlvlr lplvssaeea qsgne
//
LOCUS       WP_357596573             189 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxymuconolactone decarboxylase family protein [Micromonospora
            parva].
ACCESSION   WP_357596573
VERSION     WP_357596573.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..189
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20221
     Region          37..175
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msflrqaers pdsermfdtd tkamgylpny trlfahnpav ylawqqlnga vkdgmelrry
       61 elvtlaaara lkssycglah gkllrdkffd aptvaaiasd hgsavlsaqe vavvnfagkv
      121 aadatsvtea dvaglrahgl ddtdifrvil tvgarcffst vlsaagaepd pqyqesldad
      181 lrqalsfgg
//
LOCUS       WP_357596645             175 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357596645
VERSION     WP_357596645.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 175)
  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 175)
  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..175
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..175
                     /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=18958
     Region          <79..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mrrwrsaava tvlvltavta svplglyvsr nivriayeie qrgivyswgg ghdaepgpsn
       61 gtcegyhgri rpcpaartrg ldcsgfarwv yamahgsdvl gpgntndhvr rmrrvvtaip
      121 gdlvffgkvt kkgvktrhvg iylgggkmmd apetgavvrv ddiarrkdfa gfyrl
//
LOCUS       WP_357596802             380 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357596802
VERSION     WP_357596802.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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..380
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..380
                     /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=41250
     Region          1..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 mptpvvliag lhatartaav eqllaehpgs lvihhdlsqi thgrvrrsvr drtgvldtae
       61 vrlahgcvtc tvredllpql vllatgaall ivdlwdavep rsvaeaidcd earetlrlta
      121 vltaldaaal pddltrgerl sevgrpaaag drrylaevla rqleyptalv lhggdeddre
      181 lsrtilthla pftpvhtvea lppladarvc aaelaervdp ataqlpgdlq tgeivtavwr
      241 thrplhparl feavdelvte svrsrgrfwl anrpdellaw davagivsve aagpwlaalp
      301 raawdlvppa rrlaadldwd pergdrvqhl vftgpdldaa rfrallgscl lteeeeregs
      361 dawaryddpf apilaikesa
//
LOCUS       WP_357596806             320 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357596806
VERSION     WP_357596806.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  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 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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..320
                     /product="GlxA 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=34841
     Region          3..317
                     /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 mlrsvavlal dqvapfelgv laevfgtdrt adgfpayrfq vcspdgnpvr tssgfqltph
       61 adlgpvdead lvaipahsqg ttvpgpvlda lrradargah lfsvcsgafl lgeagllddr
      121 ectthwryvd elqrrhprar vrcnslyvqd grlltsagta agidaclhli rqehgsatat
      181 rlarrmvvpp hrdggqsqyv eapipkapea ptlepvlewm mghldrtitv eelaaragma
      241 prtfarrfra etgttphdwl tnqrvllarr lleetplsve avadqsgfgd aaalrhhfsr
      301 rvgatphsyr ttfrdrahsg
//
LOCUS       WP_357596821             201 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357596821
VERSION     WP_357596821.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 201)
  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..201
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..201
                     /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=21752
     Region          30..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msnpdaggtg leavpaspvr rlrrperreq ildaatrafa ragyaptgld diaaeagltr
       61 amlyrhfdsk adlyravldr acvrlaeatg tddfderalp alvraaaadp dgfrllfrya
      121 arepdfreli dsmtaasrev ahrnlarrip agpwldwaan liptltieav iawldagqpd
      181 pdqaaqridq avhgvmaaaq p
//
LOCUS       WP_357596857             312 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357596857
VERSION     WP_357596857.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   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 312)
  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..312
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..312
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33583
     Region          29..308
                     /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 mtdpatsagq vcesnpvrdl plhdlagfth rwvdadgvrl haveggqptg pavvllagfp
       61 qtwwawrkvm pslagqfhvi aidlpgqghs erpersydth tvaahvhaav kalgvstywl
      121 vahdigawva fslalkfesq lrgvalldag ipgitlpeai ptdpdrawkt whfafhlvpd
      181 lpetllagre rdyvgwflkm kalspdtfdd aeldhyaaav avdgglrafl ayyrdaaesa
      241 rknhealkrq hltvpilgis sshgsipdma asispwaddv tgvvvpdagh fipdeqpeav
      301 aaaiadfild gd
//
LOCUS       WP_357596858             678 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora parva].
ACCESSION   WP_357596858
VERSION     WP_357596858.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 678)
  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 678)
  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..678
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..678
                     /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=70946
     Region          1..454
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          594..659
                     /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(616,625..627,634)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            626
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 minrllvanr geiarrifat cramgvqtva vhsdadadap faaeadqavr lpgntpgety
       61 lrvdlildaa rrtgadavhp gygflaenae faaavtdagl twvgppakvi aamgdklaak
      121 allteagvpm lpswtdsdei tdfpvlvkas aggggrgmri vrtadelaea vasarreaaa
      181 afgdgtvfie ryvergrhve vqifgdthgr vvalgdrecs iqrrhqkive eapavvperv
      241 rtalheaava agravdylga gtvefllapg geffflemnt rlqvehpvte lctgldlvgl
      301 qllvaegepl padlpgstgh aievrlcaed atagwrpdtg tlhrfsvgav vtefgglagp
      361 glrldsgvva gsvvgvhyds mlakliawgr traeatrlla galaraelhg vstnrdllvr
      421 vlrspafaav eidtgfldrh pevfdpllpt dqvpltalaa alsgaahrra tapvlsglps
      481 gwrnvpavpq vtrlvqsdgh eieiryrldr tgrltdwgst apdsdaagsa dpptvalvea
      541 tpdrvvldvd gvrrgyrvrr vgsavfvdgp dgaasltelp rlplpttevg agsllaplpg
      601 avtrvhvqvg qrvtagdpll tleamklehp vlapidgvva elpvptggqv qagavlavid
      661 sspapadlep snpeedpr
//
LOCUS       WP_357596876             454 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357596876
VERSION     WP_357596876.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=48431
     Region          139..446
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrrslrsrl tllvtvavav aiaasaglcw fivnrelyaq ldhalaepes psnkrwlvdn
       61 ceeagtsdpf sgiatvlfed gttcslgppi kvepqdklvf gnhgrpgfrf gtttdgksvr
      121 vmasferppd rapgepsgiv ilegrytyqm qstlrnlali lavvaaigvl gaasagllvs
      181 rtalrpvgrl tkavehiaqt edlnttipve gtdeiarlsr sfnamtaala gsrdrqqqlv
      241 adaghelrtp ltslrtnidl llrsehtgra iepkakerll vnvkaqfeel stlvgdllql
      301 srgegdheph velafhdvvs aavararlrg advttdlapw yvegnpssle ravvnlldna
      361 akfspggkve valhegeltv rdhgpgipad elphvferfw rspsarslpg sglglaivaq
      421 avkeaggqvr ldnaagggav awirlpgspv lsqs
//
LOCUS       WP_357596918             668 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357596918
VERSION     WP_357596918.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 668)
  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..668
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..668
                     /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=67721
     Region          12..483
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     Region          <436..537
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
ORIGIN      
        1 mnqfqplaad dprrlgafei varlgeggqg vvylakgqsg eqvavkllhn alvadadart
       61 rflrevavaq rvarfctapv lhadlegsrp yivtdyvpgp slrqlvdreg prrgaalerl
      121 aistatalaa ihragilhrd fkpanvlmgp egpvvidfgi araldspgat atgmamgtpa
      181 ylapeqlsga pvseaadvfa wgvtmvfaat gkpafgsdsi pvvmnrilhe epeigglegv
      241 lgglveacls kdpahrptae qliarltgqq tgespvavhq tgsqlpppfp hpgaasgpqg
      301 aagvpsgpgp hgapagpgpq ggpvpgppgg pggpgphvpg qpggpvpgqh gypgaqvpgq
      361 rppsggtapg satrrrtlti avsaaaagal vlagtvvwaq agknttaslv aangpatsaa
      421 tdpatdpatd paagsteapv dppsdleltp eligesptpk askskksede pavsvphtti
      481 appevrptak pstpkakptk ntdlvdpepe ptgltepttg dyyghsskps pkptvkptva
      541 pkptpkptpk ptpkptpppk pnpyqattvc gsgykvinsh algakatiyl lyntaagknc
      601 vitmskyvvp akismnailq vkggasgsnp gkfstysgpv rlpavkkcvi wggswgtltw
      661 ksgwshcg
//
LOCUS       WP_357596991             151 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora parva].
ACCESSION   WP_357596991
VERSION     WP_357596991.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=16576
     Region          12..149
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mthavadhpt vefghvehvt vhfddldamg ilhnaryavl leraltpywt qrglayrgsa
       61 tppdlfhavr efaityrapi vatgpvavhf wlehlgtssa eyafqfrsvd gdsvhaegrr
      121 aivrldpatl rpapwteaar tvaatllrpt a
//
LOCUS       WP_357596925             451 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357596925
VERSION     WP_357596925.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..451
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=47165
     Region          1..449
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 miealvkalp egrvltdpdv vdsyardrtf lepgkalgvv lattrdevvt tlrwatehrv
       61 pvvprgagtg lagaataseg sivlslakmt airelnpade favvepgvit adldraareh
      121 glmyapdpss yeistiggnl atnagglrcv kygvtrdsal glevvladgr ilntgrrtvk
      181 gvtgydltgl fvgsegtlgv itsatvrlrr aplappatia aefgslrdaa aavsaiiaag
      241 cqpslmelld ratlkaiddw rnigleestq amligqsdas dgqamaammq elceangasf
      301 valsstpeet edligirrma yqakerlgac lvedvcvprs alpdmisaie aaaarhdvmi
      361 ctvahagdgn lhpvfifdhg tveppanvwa aadevfkaal emggtltgeh gvgllkrrwl
      421 alesgpvvte vqqgikrvfd plgilnpgka i
//
LOCUS       WP_357597006             384 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357597006
VERSION     WP_357597006.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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 384)
  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 384)
  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 384)
  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 384)
  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..384
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..384
                     /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=41161
     Region          62..382
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkrfslrarl tliygglflv aglvllavty vlveqrtaqp fgvalrdvkp ivpevgtkls
       61 gnqaeqlrli iskaqddard qtlyslltqg gialglvsvv aiafgwliag ralqplhqit
      121 gtarriavgg rglherislp gphdevrela dtfdemlerl drsfdgqrrf vanashelrt
      181 plalnrslie lavtrtgase dvrrlgesll avnerherli dglltladse nevtarsrvd
      241 ladladhvld qaivgeggpa ttrelapamv hgdpvllerl ttnlvenalr hnvpsggwvr
      301 vstgqrdgrs tltvrnsgpv vpgydveaif epfrrlsger vgggrgfglg lsivravara
      361 hggtvtarpc eggglevtvs lppa
//
LOCUS       WP_357597009             253 aa            linear   BCT 28-DEC-2024
DEFINITION  M23 family metallopeptidase [Micromonospora parva].
ACCESSION   WP_357597009
VERSION     WP_357597009.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  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..253
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..253
                     /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=26383
     Region          37..227
                     /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 masptisrra rpaypvllll apvlaagcat trpgvpdgaa ptppavwata dqpasqpptp
       61 aatdpsppap ssatpsatap rvglkhvfpv radnvdyhpt hgaypatdlf adcgepfvav
      121 tdgtvlevsr vdryrkrgpq gpdngglsvs llgddgvryy gshlsavtsg vdagvrvrag
      181 qqlgkvgrtg nannvchvhf gispgcagkd gwwirrgviw paryldswrr ggnrepaaev
      241 tawqrrhgcp kap
//
LOCUS       WP_357597023             418 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora parva].
ACCESSION   WP_357597023
VERSION     WP_357597023.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..418
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..418
                     /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=44524
     Region          12..390
                     /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 mstaaaptip qtsvtdrlpa ldalraigav avvghhigfq taatmntpwg gwlarldvgv
       61 aiffvlsgfl lfrpwalnaa tgqarprtgr ylwrralril paywlavlvc livlpqnrpa
      121 sagdwirhlt ftqiyepgql rsglsqtwsl atevafylil pliavlavgr swrpvrtvvi
      181 acggllvtag wlallgigwl snglhtmwlp syaawfgagm alaaahvalr tgtapaafrv
      241 lddlasapia cwaaavavma iattpiagpr dltgptaaef avklalylai atlilipvaf
      301 ggrtrvketf aaeparwlgt vsyglflwhp lvieliylid drplftggvf ntfaltmvfg
      361 lmyatvsyyg verplqmlgs qrrkrparrg qapgtpavdv aapavaaptv tpaptvgt
//
LOCUS       WP_357597030             306 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357597030
VERSION     WP_357597030.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 306)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..306
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..306
                     /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=34080
     Region          12..280
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mgrvldgsgf vsrpaftark aglialcllp gvafvavfty ypmvrgsvia fqrynlfdlt
       61 stpfvglenf ravlaeerfw talrntglwv gvslffqfll gfglalllrr hfrgrglyqa
      121 wvffpwamsg fligllwrwm fngqfgvind lllrtgiidt rigflsspgw amtsvivanv
      181 wygvtffaim imaalqsvpr elyeaaavdg asrlrqfwhv tlphirptla livllrviwi
      241 lnfpdliysm tgggpagstd ivttfliqqv mggdygraga vgflvlglll afslfylnat
      301 rfersr
//
LOCUS       WP_357597036             165 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357597036
VERSION     WP_357597036.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 165)
  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 165)
  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..165
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..165
                     /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=18288
     Region          1..160
                     /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 mdvrlrewre ddapvvlraf qtpdlreqap fpvitlqdam gwiagwagvg hafavtvdgs
       61 vvgnvavsri ddhdngwvsy wivpeargrg iavaateela rwafgergly rlelvhrtnn
      121 pascrvatka gfraegierg klryegrrcd verharlatd pvths
//
LOCUS       WP_357597043             324 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357597043
VERSION     WP_357597043.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..324
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35320
     Region          55..322
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 maarvlaagg llalvvavav vlllnnggrq ergplnrdvp agrdaepavt errlddrrme
       61 ltiesaalga ttrvrlllpk gwsreadrtw pvlwllhggf dsytswtsrt dvddltedtg
      121 vivvmpdggr cgsysdwwng gsggpprwat yhlkellpll etryraggrr avagysmggq
      181 gamlyaaegh fqaaasfsga vhilapgvpq avmagttfgc pgtdwkrvwg dpdeqravwr
      241 ahnpydqaer lrgvrlvvas gtaelwedpa ehlagkagra faarlgelgi evethfyrgr
      301 hdhahwqrel rrayptlmra igar
//
LOCUS       WP_357597057             483 aa            linear   BCT 28-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357597057
VERSION     WP_357597057.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 483)
  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 483)
  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..483
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..483
                     /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=51602
     Region          4..473
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mtqltaldaq flsaesatta ahvagvavld pscapsgtit rerlaallle rmhlspalsl
       61 rvtevpfgld hpywapdpaf sidnhlfete leapgedtql adtvarlhar hlnrdhplwe
      121 mhlitglsgg rvavytkvhh aaidgvsgae tlaalldlsp eprsveppsc pppeaphvld
      181 mlagaavrtv thparavrsl vraagdldai pvvatlpgsr liaraarfvt gdersrpdlp
      241 slavphtpfn gpisaerrfa ygsvplkevk hvaksysmsv ndivmalcas alrawlderg
      301 alpdqpliaa vpvavrtasa rdcagnqisa miipmathva dtgerlrata eamntakrrf
      361 arspatwlhe lcamlpspvs altpavfrla saafppinli isnvpgpqfp lylcggrvls
      421 yyplsvltdl sggvnitcfs ydgvldfgvv acpdrvddvw rlmhhlrtam deltfltrdl
      481 apv
//
LOCUS       WP_357597065             365 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357597065
VERSION     WP_357597065.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..365
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=39042
     Region          5..354
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mtsnrpqvvi vgagvagfqa artlsrrlgd raeivlvnrs gvtlhpellp qvmtgvlspd
       61 rvsvplagtl pgvrvvlgtv thidaharrv lydggvldyd rliiaaggvs evaqvsavsa
      121 hsfgfhdveq alrlrdhihr qlamaaestd pferaahctf vvlgagyagt aaasagqsls
      181 qsiacrdprl reqpirwila dpaewllpdm rhrlsrttar mlrsrgvevr tqtslgqvts
      241 rglrltdgef iptrtivwsf gvrpdplvtn lglaaeqgri rvdehlavlg hpeihacgdv
      301 aavpdltrpg kvtpmsgqha lrqgglaggn vaaslgygsr rpyryrirgs ivdlvraseq
      361 plsva
//
LOCUS       WP_357597092             422 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357597092
VERSION     WP_357597092.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=44814
     Region          35..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(143,145,271,273,307..309,350)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrrvigaata aatvafvaac gsgasgdtas dgsvtlefaq wwgaelpage fdkiindfta
       61 qnpkikikll sapyastkqq litgaasktl pdvvgldgaw vndfakqgai tdlsklmada
      121 kydagelasq vqvkgktymi pvvnfvyplf vnkdlltkag vakvpttrtq fldaakkisa
      181 sgsdvkgwal pldsavpngi qndvmswlwa sggsmladgk pnltsaqvks vveyvkslnd
      241 agviapgslt mkeqdkvekf ingqvgmmid slahinlikk nkpdlkfeva alpaedgytg
      301 krgipyaswg igisdstehk aeafkfvsyl lsketnakls tiangfpgnk naqpdfsnsd
      361 plfktafdiy qqgypanefv glpksedlmr sfdeqlqlvm tgktsvdaal aksqeswssv
      421 ig
//
LOCUS       WP_357597100             115 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            dietziae].
ACCESSION   WP_357597100
VERSION     WP_357597100.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..115
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12609
     Region          4..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msfpealsrh cprfqvaiel vgrrwngvil lalargatry gelrddvpgl serllaqrlr
       61 eleeagvvar evtpttpvqi rytltesgaa lveamrplma wadrwaappa dqsat
//
LOCUS       WP_357597119             210 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357597119
VERSION     WP_357597119.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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]"
                     /calculated_mol_wt=22446
     Region          40..165
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mklhhhtdha dgagpivrpr lyevvseigf agrrrlvsir lvalsgahrg dhvldvgcgt
       61 gyltrllarr vgpeghvtgl dvaqpmieha rarapgtcay vlgegqalpf pdarfdvvvs
      121 clavhhlpaa argtalremf rvlrpggrll ivelrppanr laarlagmva ghalrpsmpd
      181 llaelvpaag frveatgelr pllhyvlavr
//
LOCUS       WP_357597183             460 aa            linear   BCT 28-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Nonomuraea dietziae].
ACCESSION   WP_357597183
VERSION     WP_357597183.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 460)
  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 460)
  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..460
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..460
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48613
     Region          47..436
                     /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 masevpgddd rvkvpgkaaa sgqsedgsmp naaatptlad rlrkdlrnpl flqayalmin
       61 taitavlglg ywvlatrlys paafgegqtm isamrlfssl tglafvgama rfipvagrrt
      121 sefvlrgygv agatgvvaal aflltlplwg payaqlggfg pglfflvsvl vwtiftlqdv
      181 tlaglrravw vpanslgfgl vkmvllaala falpegglfg giflswiipt amalipinwf
      241 ifrhaiprhv erteddpprl reigrflagd fpgalslllt lylvpvliaa wlndatvfgy
      301 fsvthtlgcm igllaanmav sltvegsfhp aelarsvrna lrrtvlivvp ivaivtlaap
      361 liltvfsael aeatspllrl malavlpgil ieihlstlrt lrqarrlaiv qiglavimlg
      421 liavlfplag vtgvgyavla anavvalavv phlrrvavvs
//
LOCUS       WP_357597164             194 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357597164
VERSION     WP_357597164.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=21701
     Region          15..81
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkddkswvld dpgrlkalah pmrramlrhl glhgpatstt lgslldaktg ttsyhlrqle
       61 kygfieeive rsagrerwwr rvetgdirlp lpadlspedr pvlaefhrig yeedkgilld
      121 llpaayeadp awvkvsrglg rmrleeleaf feeyvalmkk yshgaadapp garplylrll
      181 alpadlpapp arge
//
LOCUS       WP_357597240             264 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357597240
VERSION     WP_357597240.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27377
     Region          5..261
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mnlqlsgrva vvtgaskgig lavartlaee gahvvavsrt rtdewpdkvv hvaadlmdpe
       61 aparvvarav eefggvdilv nnaggpppga tlprvgfmtp sdddwramfe fnlfsavrmi
      121 raavplmver gggsivniss tmgrqpgamn vdyaaakval shvgkavsee ygpqgvrvnt
      181 vtpgavltdw wtkeggaaev faglvgsdke svisevapam mklatgrliy pqeiadaval
      241 lvsprsgstt gaefvidggq lkel
//
LOCUS       WP_357597192             240 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome c biogenesis CcdA family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357597192
VERSION     WP_357597192.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..240
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=24195
     Region          10..201
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 msdviasgsl llavpiavla gvvsflspcv lplvpgylsy vtgmstdagr grlvlgtvlf
       61 vsgfglvfvl sgalfgglgs vmlghaelit rvlgvltill glaflgvipg lmrdvrihrv
      121 psaglagapl lgvvfglgwt pcigptlavv lalglnegsa argallavay alglglpfvg
      181 aalayskalr tfrairkhsr litrigggmm vavgvllvtg lwgqmiaamq gligtfepvi
//
LOCUS       WP_357597252             373 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357597252
VERSION     WP_357597252.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 373)
  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..373
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=39322
     Region          135..373
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrrtflkivr ffsrprvfdt tlvivftlpa vlalpfmiag gevrgvltmg sylagmalll
       61 mrrrrpllta alvaavdavs iatqlvtfvs pssaialysv grytagrttl itsagayavy
      121 attmelfwrg qggwlgavfa vsvpvgtgli vrlkaelter srrevadaav raerrriare
      181 lhdvvahhit vinalvggar atlppgqevt rdalegaeqt arqamsemrh lldvlradgg
      241 egadaatgvg adrlpsliqe arsaglpasl tvagepvelp atvdhavyri vqealtntrk
      301 halsarasvr ltyepsavev evvddgsaag gvapgfglgg maervalcgg rlstgprpeg
      361 gfrvharipl ett
//
LOCUS       WP_357597254             319 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357597254
VERSION     WP_357597254.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (residues 1 to 319)
  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 319)
  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..319
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..319
                     /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=33338
     Region          1..239
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 madlawgiaa tggiartvga viaaepgmrv aavgsrdrgr aaqlaatlga esaygsyael
       61 cadpavdvvy vatphaqhle vaeaaiaagk avlcekplaa sladaermvk larqagvflm
      121 eamwmrfnpl irgllaeerf galrtvqasf gfvlpyqeeh rlwnpvlggg alldlgiypf
      181 glaqlllgep aethltgsla psgvdaevga lltyeggara lldtslispl antatvvgtg
      241 lradiaapfw apqritlsgp gfeteehvld palngyagei revrealaeg rtesaimpld
      301 eslammrmle earvrlgar
//
LOCUS       WP_357597315             427 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357597315
VERSION     WP_357597315.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   ter Beek,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 427)
  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..427
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..427
                     /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=46783
     Region          1..326
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mstvvldkvt kvypggylav drlslraedg eflvllgpsg cgkstllrmi agleevtdgd
       61 lwldgelanh laprdrdvam vfqngalyph rtvrgnmafp leiakadpal vkervtelsk
      121 alhidetldr rpgtlsggqr qrvamgraiv rqpkiflmde plsnldagmr telrmeissl
      181 vrslgvttiy vthdqvealt ladriaimnr gvlqdvgtpg qiyndpataf vaaflssqql
      241 nllpatvrtp qnqyvlldfg phqlvipwsd prayaisqht ggqiivgirp dglapvqesy
      301 egpsfygrvr aleyhghewl ayvecgvpav avpeppdprq nargsegggg glramvrrmf
      361 gsepdehaqq eqvghnlrdg hhrradlivr lgvrpawrtg daakigvdvt rlmlfkldgs
      421 ridpprr
//
LOCUS       WP_357597274            1060 aa            linear   BCT 28-DEC-2024
DEFINITION  type I restriction endonuclease subunit R [Micromonospora parva].
ACCESSION   WP_357597274
VERSION     WP_357597274.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1060)
  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 1060)
  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 1060)
  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 1060)
  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 1060)
  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 1060)
  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 1060)
  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..1060
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..1060
                     /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=117604
     Region          2..999
                     /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 mspihhesaf gdaivaalla ngwaegdkad yrpelgldtg qlftfigatq aedweelvtr
       61 yggdpteaqr gfakrldqai atdglldvlr kgfkdhgvri rlayfkpsfv eseailadyr
      121 knrltvvrel eyatkqadrg nrldltlfln gipvataelk npltgsgved akeqyrtdrd
      181 ptelifsrrv vanfaidpdl vfvttqlrga qtrflpfntg segpgrpggk gnppateygk
      241 yatsylwdei wqrdnwldll erfvhlhqek vaggrtrktl vfpryhqwha vkqltaraar
      301 hgaghnyllm asagsgksna iawlahrlss lhtlsdpaal dpdalaagvk agspvfdkvi
      361 iitdrrnlds qlrdtvgsfe qtaglvvkid ekhgakseql akalsqetgk ivtvtlatfp
      421 alrdylqrnp teirgsrfai ivdeahssqa geaatdvrrv lrdlgldaes ddpgatsaag
      481 prtteeklaa svrkrqrssn lsyfaftatp khktlelfgt lgedgkyhpf hvysmrqaie
      541 egfildplcn yvtydtywkl vnanpderev dsskankela ryalthdstv aqhaqiiveh
      601 frahtagrlg grakamvvtg srlsavqmsr aikrylddrd ypdpgvlvaf sgtltyegae
      661 vteskenggl petalpkafa ytraddktar agtaagqrey rilvvaekyq tgfdqplltt
      721 myvnkklhgv savqtlsrln rtadrksqgd lavldfvnda eeikeafrpy feeaetlpsd
      781 pnllytaqsr vmsaqllvea emqefveayl aaeeqaagna akweklhael yrhlqpavdr
      841 fdvllnrede sdweaaetfr gdltdyvrky gflaqivpya dselerlyly grhllnrlgr
      901 rgdggvdvge vdlshlrvek tgehdvslnp egaaemkgfg dgsggakepe ksllselver
      961 fnerfgtsft dddvvkplne amadpkvrqa avandeenfg hvfgpvfeek mmdhfetaad
     1021 lgrryfgpep dfrsslnrsa rsaawrlirr qegvvddeaa
//
LOCUS       WP_357597333             434 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357597333
VERSION     WP_357597333.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  AUTHORS   ter Beek,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..434
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..434
                     /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=45969
     Region          24..338
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrtkllgvaa lvvtlaaagc asegaapape atqaapqgpv kltywtwapn mdkivavwnq
       61 ehpdiqvtvs kqaggddaaa kfltaakagn ppdlvqaeyq hlpsfiaada vadltaaaap
      121 vkaefsegvw gqvtlgtdtv yaipqdsgpm mlfyrkdlfd kygiavpktw qeyaeaarkv
      181 heqdpkvflg tfsskdpgaf tglaqqagaq wwaidgeswk vnvadepttr vadfwgglvk
      241 egvidgmpyf tpewnkalnd gklltwpsai wapgvlssna pkakgkwava plpqwkagen
      301 fsgfwggssv avaakskhqa aaatfatwln tdakavdllv keaaiypaat kgqsalteap
      361 dyfstqpdfw qqaagvaasa rgftfgpnvg vtynafkdsf dkavqakssf sdavramqea
      421 tvadmrksgf qiap
//
LOCUS       WP_357597323             287 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357597323
VERSION     WP_357597323.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 287)
  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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32893
     Region          <29..69
                     /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(30..31,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..280
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpsqqgsptv rrlrlgqelr llrerraltg araarelgws askvsrieaa ktmpsaddik
       61 amaelyhldg rkldelfgll rdaeqrgwwe dyedalpeey trflgleaea thqrnwepqv
      121 vpgllqtedy arevilatrg isrithsgvr srvearldrq qrvlhrahac vlnvvldesa
      181 lmrrfgepav mreqmehlle vsllphvsvq vltldalhpv ntgafihlkf safddvvyle
      241 qlytanfved lervagyeta fdnirseald edesrvliqr qamlwrr
//
LOCUS       WP_357597409             226 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora parva].
ACCESSION   WP_357597409
VERSION     WP_357597409.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=23952
     Region          12..198
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mttaplshtp tlvedlllll fqprsgtiag entlfyvlgg avladlalge hlstmdrgrv
       61 sgvpghppsd sllrpaydyl aekprgvqta laaigpvlre pvlhrlvarg didqvprkvl
      121 glfrttalrd grterrarll aevrqvlvdg arpqarvaal tallsasgtl pqfhseipwt
      181 spvisrakel eqgdwgadaa atavtrtvta tvvnsaivai svlprs
//
LOCUS       WP_357597383             231 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357597383
VERSION     WP_357597383.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 231)
  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 231)
  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 231)
  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..231
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..231
                     /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=25210
     Region          <3..212
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mrepvngfla vdqgvanlav tsdsvvlpgs alpgtidgng hvrtlrerrh rqrrrlqkkg
       61 tpaarrvlrr pagrehrmmt nvnhqiptyv vreaertgrg ialedlqgir srvrahrlqr
      121 rtlhswafaq qiaftrykaa ragiaftlvd paytsqacpq cgwtsranrp argrfactrc
      181 glaghadhia arniaqrgaa gwaavnqpha tglasarrdr eskppasags s
//
LOCUS       WP_357597426             395 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            parva].
ACCESSION   WP_357597426
VERSION     WP_357597426.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 395)
  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 395)
  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 395)
  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..395
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..395
                     /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=40254
     Region          62..324
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mtiicivava lslttpavvp appaqlaapy vpcpavkppv apppapsppp vgpadlavgg
       61 eslataglsi pagaprapav tatswlvadl dsgavlggcg pherrtpasv qkmllaaalm
      121 phldptqvve vtradlsdld passvmgvvp ggrysiknlw lglllksgnd aanvlarvgg
      181 gttgrqggvq amndeahrlg anqthaatps gldgpgqyts aydlaliara tyaradfrry
      241 iatraaeipa gpgrpglslt hdntlldryp gtlggktgft dlarqtyvgv aerngrrlav
      301 tllgaetapl gslgeaaall nwgfalppda svgrlvgpde kkpdrpvsqv kadqhepart
      361 grsmswmail gpgavgflav lllvgpvrrr aagrr
//
LOCUS       WP_357597433             262 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357597433
VERSION     WP_357597433.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,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 262)
  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 262)
  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 262)
  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 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..262
                     /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=28386
     Region          25..262
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 mvrtyallaw twtraaaayp asfalmvvfg falaavdvgv ilvvfantts lagftrpevl
       61 flygaaniaf ssvdmcvgni drisqhikag tfdaflirpa stwvqttvdr ftptrigrvl
      121 qavivlgvam aeldvpwqrv wmvpvmiata mvifaslwtl agalqfvvtd apevcnafty
      181 gggqlsqypf svygrdlvrg vtyvlplafi nwqpglyvlg rddlfgtpgf lrfagplaal
      241 llallaalaw rqgvrryrst gs
//
LOCUS       WP_357597477             353 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea dietziae].
ACCESSION   WP_357597477
VERSION     WP_357597477.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 353)
  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 353)
  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..353
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..353
                     /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=37604
     Region          3..337
                     /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 mntivigggq sglaaaralr dagltpvile agehptgswa hyydsltlfs parysampgq
       61 pfdgdhyphr devvdylrry adrldveirt ttrvsavead gsggflvhle gcdtlrtagv
      121 vaasgsfgnp yvpevpgreg ftgqllhvad yrnpkhyagq rvivvgagns avqvayelag
      181 satvtlatrq qvqfmpqmvg gkdihywhtt tgfdslppqw lariatgtlv ldtgdyaaal
      241 eegrmerrpm ftgfdgehvi wsdgtaervd tvifatgyrp hldylrplga ldasglplqa
      301 gglstthlgl gyvglefqrs fasntlrgvh ldaahiatpm aayaggalaa ygl
//
LOCUS       WP_357597480             112 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357597480
VERSION     WP_357597480.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=11795
     Region          3..94
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 memasdielt daargflkam asdtrqqilm lfsggieltv sevaermsla qsatsthlat
       61 lrdggvltsr rewktvyyra dparigrals dlqaslqacc pptdcapggg cg
//
LOCUS       WP_357597502             402 aa            linear   BCT 28-DEC-2024
DEFINITION  M28 family metallopeptidase [Nonomuraea dietziae].
ACCESSION   WP_357597502
VERSION     WP_357597502.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 402)
  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 402)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 402)
  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 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 11454910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..402
                     /product="M28 family metallopeptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008235 - metalloexopeptidase 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=41767
     Region          187..398
                     /region_name="Iap"
                     /note="Zn-dependent amino- or carboxypeptidase, M28 family
                     [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]; COG2234"
                     /db_xref="CDD:441835"
ORIGIN      
        1 mtsspllqap aleavleris vqrmsatvqe lahdrytgrr vgtaggrsaa awlaeqlral
       61 ggevesesft vtsvrelygt pvlewtadgr trrlehrref vehlasaelp hahaapvvaq
      121 tdtadvhgrw vlgdaadwar aeeggaagvl targtdadgw mpkmiagpgv rtvpvialrp
      181 dlhrelgeav trtpvqvtas mplrsvsvdg lnvyahlnrs hgaphvllta hhdgvgddpq
      241 rrlpaaadna sgvaaileaa rvlsaqalpi nlsvafldae eagalgsahh vravppdtlv
      301 inldgaaklh eaasveaggp ahgllaaldq agretgvplr agamasdnrr yaaaglaaig
      361 igmgmpgyqt paetpdrvea gtllaaarlv tatvwrlaht gs
//
LOCUS       WP_357597538             247 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357597538
VERSION     WP_357597538.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 247)
  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 247)
  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..247
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..247
                     /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=26465
     Region          4..244
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtkpisvqly tvrdalaadr dtvlsriaev gyrsvepydp ttdpkgfrev vddlglsvss
       61 thayallske paevfdaiat igtdlvivpg giaheefttr dglsrtadll nglaeqaary
      121 gmrigyhnhw weiepridgr halealadll apevfleidt ywaavggadv pallgslaer
      181 tlalhvkdgp vvkgephtav grgvmpvpei laaapdawri veldecatdi faaladshay
      241 ltslegs
//
LOCUS       WP_357597541             366 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357597541
VERSION     WP_357597541.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 366)
  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 366)
  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 366)
  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 366)
  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..366
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..366
                     /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=37906
     Region          3..339
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msngpvgval vgagnisgqy lrnltafpdv rvlgvadidt eraaavaaeh gvpvsgalat
       61 vlavpeveiv vnltvpsaha avaleslrag khvygekpma mdldeatkiv teaanlglrv
      121 ggapdtflga glqsalhalr sgligepvav taatqslgpe swhpnpeffy qpgggplfdl
      181 gpyyltalvs llgpvtrvaa gtrrarlhrv vgsgpkegkv fpvdvpthvn alldfpgaat
      241 aaatfsfdsp inrrtieiig segalslpdp ntfegpllar glhdtdwher pvagttagrg
      301 igvldlarsl rsgtphrasg dlafhvlelm aaisesgers efrpitsttt speplpedwd
      361 pyastl
//
LOCUS       WP_357597552             320 aa            linear   BCT 28-DEC-2024
DEFINITION  ketopantoate reductase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357597552
VERSION     WP_357597552.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 320)
  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 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   3  (residues 1 to 320)
  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 320)
  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 320)
  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..320
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..320
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34071
     Region          1..288
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mryivigaga vggtigarlh qgghdvllia rgahyaaikr dglrlitpes setldipaad
       61 gpvpvreddv livatksqdt iaaldgwpsd lpvvcaqngv dnertvlrrf ervygmcvwl
      121 paqhmepgiv aahahpysgi lhvgrypqgv ddlarriadd lgkrglvgla qpdvmrwkhg
      181 kllgnlgnav ealvghapgr ekvverarae aravldeagi aystpeeeaa vrgrkadvrp
      241 idgiargggs swqslarssg sieadylnge ivllgrlhgm papvnevlrr eanrfakekr
      301 ppgsmpletl lalidgrsaa
//
LOCUS       WP_357597580             390 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Micromonospora parva].
ACCESSION   WP_357597580
VERSION     WP_357597580.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=40504
     Region          1..390
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 msdavivgav rtpvgrrkgs lasvhpvdls ahvlralaer tgldpaqvdd vfwgcvsqvg
       61 eqswniarna vlaagwpesv pgttldrqcg ssqqalhfaa atvlsgqadl vvaggvesmt
      121 rvpmgssvag gmpfsdqlra ryrgvegfad daplpfnqgv gaeliaqrwr lsrtqldefa
      181 lashekaaaa qdagafdpel tavpladggk faadegirre tsleklgela tpfradgvvt
      241 agsasqisdg aaalavttsd warrhglrpl arihtavvaa ddpvamltap ipatakalrr
      301 aglgieeigv yevneafapv plawlaetea dpdrlnprgg aialghplgg sgarimttml
      361 qhmrdngiry glqtmceggg manativelv
//
LOCUS       WP_357597594             510 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Nonomuraea dietziae].
ACCESSION   WP_357597594
VERSION     WP_357597594.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 510)
  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..510
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..510
                     /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=54566
     Region          1..508
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mlakladlda ehakavaggg ekyvrrhrer gkllarerve llvdpgsafl elsplaawgs
       61 dfpvgasvvt gigvvegvec vitasdptvr ggasnpwtlr ktlrsadial rnrlpyinlv
      121 esggadlptq keifipggri frdltrlsaa giptialvfg nstaggayvp gmsdhvvmvk
      181 erakvflggp plvkmatgee sddeslggae mhartsglad hlaadehdal rigraivksl
      241 gwrklgvrpg pvveprypqe ellgivpedl kipfdprevi arivdgsefe efkplygasl
      301 vtgwarlhgy rigilanarg vlfsqeaqka tqfiqladrs rtpllflqnt tgymvgreye
      361 qggiikhgam minavsnstv phltvvmgas ygagnygmcg raydprflfa wpsaksavmg
      421 paqlagvlsi vgrqaaharg qvydeeadaa mramveaqie qeslpfflsg rlyddgvidp
      481 rdtrtvlglc lsainsapvp etagygvfrp
//
LOCUS       WP_357597670             190 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357597670
VERSION     WP_357597670.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 190)
  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..190
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..190
                     /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=20578
     Region          1..189
                     /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 mdsvlsedpv alkiliaggf gvgkttlvgs iseikplrte evlsdrgigv ddldgveakn
       61 tttvamdfgr itirdglvvy lfgtpgqerf wfmwdelshg algavviadt rrltdcfpsl
      121 dyfeqrgtpf vvavncfdga ashsvddvri aldldddvpi mlcdvrrras akevmitlve
      181 hslrtltsan
//
LOCUS       WP_357597700             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357597700
VERSION     WP_357597700.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=16614
     Region          1..136
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtsatdpvva lmglqqhaaa lgtihaeqia sqlgitatdl kglflllqrp haprelaaal
       61 hltpsaitsv idrmeragfa rrepsktdrr rylvtavpdr aqqaielytp lftsmrevla
      121 hydddqlatl ldfaqrtvha feelttrrre
//
LOCUS       WP_357597726             988 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357597726
VERSION     WP_357597726.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 988)
  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 988)
  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 988)
  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 988)
  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..988
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..988
                     /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=108806
     Region          6..208
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          87..980
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          733..761
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          777..800
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          805..841
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          852..880
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(853,856..857,860..861,863,893,896..897,900..901,
                     903..904,933,936..937,940..941,944)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          885..921
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          932..959
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtlndlvdel wpdgpprsav anvrsyaanl rrafetfgng egaivrqqtg yrlvlpaeii
       61 dlfrfemerv agrealiagr ldralellgs avarwhgpml agvplgpvlt asstaaeeer
      121 llavelltda qlrsgrddla ipllrdvivr hplrepvyvl lmralyergd hagaltayge
      181 ararlaaelg ippgaglqal hhtiltaatp lsrssraarp adptapaqet vvasarprrp
      241 dlvdhlprav tdfvgrehvv srllaetrri eervpavhii dgmagsgktt lavhlarrls
      301 erypdaalfi dlcghgeknr vepanalvtl lrqlgvpadr vpvefdgrve mwrqelarrr
      361 svvvldnaas seqimpllpa epttvvlvts rrrlshpdvg psqtlpvmsp qegvdllgls
      421 vgrdrveaep daaaevvrrc ghlplairla garlahrrgw rlvdladqma gdvpalhhla
      481 qedstvtgaf aasyeplpgs tkrvfrflgl ypgnrfspaa vaaltgltva eahralddlv
      541 drnlvedlds tryrlhdlmr qyavelctrt esasdrkagl aqlfdftlea vlrvadllep
      601 gvirsqvtrr fsgrpelvea vgepctdwle aertelvaiv lsalesklhq hcwqlaralw
      661 rffyirgyfe dmiltfrhal taaeatgdvd amavvnnyla sayvrtgdnq waldhltrav
      721 dlshnsrdvr ntaryranla avyawsghla eavtvgmesl rdykgygnvg vpvvlpnlgt
      781 almmlgryee alrlhrrhla wartksedfh vlnafghvga vrvrmghflq airilkasla
      841 lrdrtghrfa eaevrndlgi ayrglgrlve aqqqheaarq lsitsgerhv eaaalnelgr
      901 tllaqgrgge avemhqaalr latrishpye hgralaglae cfaradpaea rrhweralai
      961 frrmgvperf eaerrlaela pttvisvp
//
LOCUS       WP_357597768             104 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nonomuraea dietziae].
ACCESSION   WP_357597768
VERSION     WP_357597768.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=10606
     Region          2..99
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mnwvylalag lvevawsqsi kptqnftrpv ptaislvlma aavwllskam ntlpvgtaya
       61 vftgigavga itlgivlndd pvtvgrmaal slivggvvla rvta
//
LOCUS       WP_357597771             209 aa            linear   BCT 28-DEC-2024
DEFINITION  FMN-dependent NADH-azoreductase [Nonomuraea dietziae].
ACCESSION   WP_357597771
VERSION     WP_357597771.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 209)
  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..209
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..209
                     /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=23321
     Region          1..207
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mnllhldasa rrasfsrels rihadawraa npdggytyrd laaspvphid eawtelcdyv
       61 laheiteiar yreavrtpaq erawavlepl ldevvaadvi ligtpmynys ipsslkawld
      121 qitfpkmslk grsfvvtsar ggaygpgtpk eavdhqeryl rdfflghfav sevsfvhael
      181 vnslidpgla hlrerhlesv drarkeagr
//
LOCUS       WP_357597868             355 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357597868
VERSION     WP_357597868.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..355
                     /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=36397
     Region          8..354
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mnetavkpsv tpgvrlgsas fvwrpwmvfv tllltaatfl vfclsigvgd fpiglsqvia
       61 tllgqgervd efvimdlrmp ralaglivgv algmsgaitq siarnplasp dilgitggas
      121 avavflvtvs ggaaaaivds vglsvaalag glgtgllvyf lawrrgidgl rliligisvs
      181 avteaitiwl lvtadirdva raqawlvgsl dnrswgevwv alwcalalva vvscvafhlr
      241 plhfgdevaa glgvrysmvr avlllcavll agvavsaagp vpfvalvapq vamrlarypt
      301 pplvasaltg allligadlv artalpvtlp vgvvtaaigg pflvyllvra nlkgr
//
LOCUS       WP_357598093             124 aa            linear   BCT 28-DEC-2024
DEFINITION  PTS-dependent dihydroxyacetone kinase phosphotransferase subunit
            DhaM [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598093
VERSION     WP_357598093.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..124
                     /product="PTS-dependent dihydroxyacetone kinase
                     phosphotransferase subunit DhaM"
                     /calculated_mol_wt=11909
     Region          <37..123
                     /region_name="DhaM"
                     /note="Phosphotransferase subunit DhaM of the
                     dihydroxyacetone kinase DhaKLM complex, contains PTS-EIIA,
                     HPr, and PEP-utilizing domains [Signal transduction
                     mechanisms]; COG3412"
                     /db_xref="CDD:442638"
ORIGIN      
        1 mvglvlvahs aglaaeaaal argiagadap vaaaggtedg glgtsvdlie aalrsvdqgd
       61 gvvlipdlgs svltarllee egrvvvadvp fvegaiaaav aagagvplse vleaaeeara
      121 yrkl
//
LOCUS       WP_357598149             960 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357598149
VERSION     WP_357598149.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 960)
  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 960)
  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 960)
  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 960)
  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..960
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..960
                     /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=103776
     Region          1..246
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          121..960
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          713..741
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(714,717..718,721..722,724,748,757..758,761..762,
                     764..765,793,796..797,800..801,804)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          746..782
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          792..820
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          826..860
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          871..901
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfrllgpmr iqvngspvki tapkqrtvla mllaraghvv pirslvaevw derpprsava
       61 nlrtylmqlr kllhevgaqe wlvtsdvgyl lrvgpeefdl fefealsarg rqalarrdlg
      121 aaeeaftral alwdgtaaed vplgptlrev varltehylg vveehadvql algknataat
      181 rlrevigqyp lrerlhaqlm valyrsgdvv galdafgaar riladelgid pgpdlrrlqq
      241 ailrrdtall tpdrdvpavp vddgrprprl lprapmvfvg rsaelarlht vlyggpgpsv
      301 valhgpggag ksalalkaah gvadrypdgq lyvdlqgstp glpplqpaev lgrflralgv
      361 ppgevpaapa eaathyqsll adrrvlvvld navgaaqvgp llpagggcaa lvtsraaltt
      421 vdavpvavgm ldeadsvrll allasqervs aeveaaaeia rwcgyhplal riagarlagr
      481 pdwslarfgl rlgdqqrrld elqaadlrvr tcfevgygtl tstakaafra fgvlevpevg
      541 velaaeladl dpttaeaald eltearllep vgdgrfrmhd llrlfaaela vthhapeera
      601 ravgraldwy ldhcrrlqal lqphlvpvsg garatgvdlr dlptavrwle telpclvaaa
      661 vqaakgrqgg faielmalik aiamkngywr eletiarlai evarrdgdrt veastlatlg
      721 lvewksgqae aahdllrral elwrdvgdrr eeglalhnlg wlcmqsgdld aaldhisagl
      781 llleahgsnr vglvahnlge vllrlgryte avdrfercls irradrdlyg esitlaalgr
      841 shclldqrek alvvleeala rceetgnred qwevllsrse irlrqgdpaa aeadlarvle
      901 ltakigdayg haagirqlar araalgdpra aadagkaeql fadlatrrdp vlerlltarl
//
LOCUS       WP_357598150             194 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357598150
VERSION     WP_357598150.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 194)
  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..194
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..194
                     /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=20904
     Region          5..148
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mggrpdevra pedwltevek eragrfrfea drasyvaahl lvrlcaaaal gtepheltll
       61 qrcelhgpgh gkpyieeapd lgvsfshtrg yvcagagpgk vgvdaehvpp gpldlalaer
      121 vctpreralv tgndelirhw trkealikrg eltldqlhag gddlagrhll ewsagpdirv
      181 avvtdspatr vpip
//
LOCUS       WP_357598296             764 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357598296
VERSION     WP_357598296.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 764)
  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..764
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..764
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83423
     Region          7..756
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          615..643
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          701..731
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 maesfgrllr slrhaaqlti eelshtsgvs vraigdmerg tsrgpqrrtv ealaealrld
       61 darrvalsea aragrprqea papgacelpr gvgdftgrkr elralrelaa ragdeqaavv
      121 aavsgaagig ktalavraag qlddlfpdgr fyldlrgmdp ipldpgtals rllkalgvae
      181 rripadeedr agryrallre rrcliildna ahegqvrsll psagpvmtlv tsrrplagle
      241 gvhqlplahl aaeeaaallg aivgperaaa dpdgvaqvas lcgnlplalr iagnrlqsrp
      301 gwtagqlaar lgdegrrves lsagdlsvaa afalsyrqls lparqsfrrl alaaapefga
      361 pmtavlaelg rdeaedalee lvdlgllqsp yvgryrfhdl vrlfararls eedpvqaqrq
      421 arrrmddwll evatiagrwf epdygappqd wsslvelnss qqaqewlqte geawlaalrq
      481 afrvgeharv vevaeamhwf sdlwmhwghw pevfdlssra aramgdraqe aahlnylswa
      541 qtycqarfde aeatalrale lareigdvrq qgwsliyatw slwarddqps kesglrytrq
      601 aaecfqqagd tegyaqamss mgnclrrlgr veesvrhnla lverlrdpaf ggspaivnqa
      661 vgatldlvgd gysalgrwqe aadhyrqalw emserpisra vattltslgk alvqleqveq
      721 areafreame lyeasgdavr aarvlelldq larsaaftrp qnag
//
LOCUS       WP_357598188             392 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598188
VERSION     WP_357598188.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..392
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=41409
     Region          1..357
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mtdilvlggg ytgvaaairv avrtrrtggr vrlvnasprf terlrlhqta agrrvadhll
       61 sevvagtgie fvqgrvtgld verrearled grvlgydkli yalgtvtdas vpgvaehayv
      121 yddyastvrf aehvgtldag apkagrlkag tvvvaggglt gvesateiae ahphlhvvll
      181 trgrpgsmmg erarayldaa lrrlgvevrt gvditkvlpd gvelaggeli hsdatlwtag
      241 trglpvaaes gltvdargri vvdralrsvs hpdvyavgda aavsqpygvl hgtcqggipt
      301 glhaadalaa tlrgrgprdf rfgylhqpvs lgrndaviqf trpddsprrw ylkgraavty
      361 ketvssspmp tfkllkrglv pvwmlalsag lg
//
LOCUS       WP_357598302             740 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357598302
VERSION     WP_357598302.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 740)
  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..740
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..740
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80955
     Region          3..735
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mergnlpadv tgfvgrrael kevrrllgra rlvtltgvag vgktrlavra ahsarrafdd
       61 gvffvdlstl hdpglietai adamrltdqt artdeevlta hladkrlllv ldgtehlvgr
      121 caqlvqlllr rspglkilva grqaleiege hllpvpsltl sdavalladr aqaatgafav
      181 taenealvrk lclrldripl aielaavrlr alsveevveg ldhrfklldl gsraggprhq
      241 tlraaigwsh elctpderll warlsvfsgg fglvaaesvc sggrlpraai vdlvgalvdk
      301 silireeree gvryslidsv reygaewlgr lgaaeadalr arhtdfylrl araneadwfg
      361 prqqaifsst raelgnlraa fercldaheq aldmaatlwf ywvgcgqlre grhwlgrals
      421 aapeptsarm ralwvagyvc vligesdsgt rfleecrnhg dqravayavh rlgcaaliad
      481 ehdravplft eaveryaklg vlecnvlmac velaivlafr geldscaelc dqvrdrcerv
      541 geqwvlsyvd yveayaawak gargralsla lrslrvshrf hdlvgivlsv elvallraea
      601 gepevaavlq gaagtiwrsv gpllfdsrhf nrphlicaeq aerelggrvy aaayargrrl
      661 gldeavsaaa ggrepraelp ltrrewevar lvaeglsnre maeqlvlskr tvdahvehil
      721 dklgfssraq iaawvtslps
//
LOCUS       WP_357598320             511 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora parva].
ACCESSION   WP_357598320
VERSION     WP_357598320.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 511)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..511
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56329
     Region          84..483
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvstdp rqqppgvtst appmavpngr hhqsvpqpmp avtpppeppn rprmdfqvvr
       61 elrrelterl tlwqrgreft vdeedterar lavtvvaaya dsvrragtpm aaseerllld
      121 qvtaelvglg rlqtllvddt ieevhilgcd qvritrhggg vdwaepiads daelveilqa
      181 aarragater slstvkptld lqlpdgsrla avflvshrpy avirkhntld vslddlagar
      241 ndldemidpl lrdflraamr aglnimvagl agagkttvir almneipqde pyvlleesre
      301 llparrrerh ravmsfeare ghgergfdgr pagevtiadl iplslrmgvl riivgevrsr
      361 eivpmlqamt tsrgsmctih artaagvger ivelalahgr emtvdqarrm agnaldlivy
      421 vtvedetaig grkhrfvshv eevigageag rittttvfgp gpdgravprh lpervrdqll
      481 rvgydarllt rwveagagaw rrprqtrlar r
//
LOCUS       WP_357598327             255 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaD family protein [Nonomuraea dietziae].
ACCESSION   WP_357598327
VERSION     WP_357598327.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..255
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=26683
     Region          9..234
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mtntlgaglk ltlfalltta caamlalmis gatvapaqvy rglftdatgl rpgddvrvag
       61 vrvgcveeis lygtqaevaf svrrstplpr gvvaairwrn lagrrylalt pgsdatgylk
      121 pgervattrp aldvtalshg frpllkairp edghtlsrqi vqvlqgeegt vesllghiss
      181 vtgpladree vigsvvdnlt vmladiagrd daygslidnl halvkglsae seaigdsprt
      241 pehlagaagp revrr
//
LOCUS       WP_357598346             550 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598346
VERSION     WP_357598346.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 550)
  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 550)
  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..550
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..550
                     /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=57151
     Region          52..>511
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrrvasglta laamaaftac statpttapq kpaapagpey lvfyaqgqqr qareaverag
       61 gttvggdarl gylmasgsgg fveqvgadra vvgvspdrsi gfaagravag ptarsaafpd
      121 aglftksrsg eplagrqwdm rmigadrana kvsgnrqvlv gvidtgvdgk hpdiapnfnr
      181 elsrnfvtdk pkdedgdtld gpcevsgckd pvdedddghg thvastiasp vngigiagva
      241 pnvqivnira gqdsgyfflk psldaltyaa digvdvvnms yyvdpwlfnc aankadskkq
      301 qleqqaiitg mqraldyarq hnvtlisalg nesvdlgnpk vdkespgypa gekkvrqidn
      361 scidvpaesn gvisvsalgp sgrkaiysdy gteqtdlaap ggdaldgega katrsilaaa
      421 pervlraagr idakgepkga dvvkdctagp csyyqyldgt smaaphatgv aailisrfgk
      481 pgkgglelsp atvedllykt atpkacptpr qyvyktygqt vtqecqgdta dngfyghgvv
      541 nawkaatvep
//
LOCUS       WP_357598375             252 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598375
VERSION     WP_357598375.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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 252)
  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 252)
  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 252)
  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..252
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..252
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27003
     Region          87..251
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mnkaertsak tarekikqqq aaarardqrk riatyvtaga vavaavglgw wyaasnsrse
       61 eaaaalapit vqadgsvvma kqgvaspvvd iyedfqcpac kelervsgqt fknlaaegka
      121 kvvyhpitif sqeptksnsv ragsaarcia dgkqwmafhd llyqnqpset eagftpdqlk
      181 nwgkeagvsa pgfdqcvtse knaeaqlsfs kkivdaqkit htptvklngs eidnsalfsp
      241 qelrqaitea ak
//
LOCUS       WP_357598467             348 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598467
VERSION     WP_357598467.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 348)
  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 348)
  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 348)
  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 348)
  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 348)
  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 348)
  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 348)
  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..348
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..348
                     /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=36834
     Region          14..102
                     /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          266..343
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mteirhlsea ptgrrplapg agidahrhdt hqivyacrgv lsvttgagtw vapanraiwi
       61 pagtvhehra hgdtdlrlvg ltdnplgldr pavlavgpll reliiaytad ddrtpappph
      121 patappaprg taapavpegt gtspsrfaef pqappapsaf dtdpalrdpa ahahahatda
      181 chggdergsd ergsdedarr garrghgagd gdddgdgdge rarlwavlld qlrrapeqpl
      241 hlptaqdprl aavcatlhrd padsrtlaql aagvgtsdrt larlcrrelg msfpqwrtql
      301 rlhhalllla dgvpvttvah rcgwasasaf idvfrrafgy tpgraftl
//
LOCUS       WP_357598623              69 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357598623
VERSION     WP_357598623.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..69
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7650
     Region          6..69
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mgervirvrl dellqergmt ltelshrvei tvvnlsilkn ghakairfst lsrlcdalgc
       61 qpgdlltye
//
LOCUS       WP_357598489             232 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357598489
VERSION     WP_357598489.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   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 232)
  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..232
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..232
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24669
     Region          1..217
                     /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 mqlhtrewgt gdrvavlihg imassecwwr vgpalaergy rviavdlpgh gaspraesyp
       61 velmassvle svpsapalai ghslggltla aavdrllpek avysdpafrm pvleggvavt
      121 dgfaaakdwt aeqiaamhpg fsaeevavev emlkgwdprt alalgkvvgi dftpapvvps
      181 lvqiadpsfl vapafaeelr ergfevrivk gaehtihrhl fddflsgldg yi
//
LOCUS       WP_357598483             284 aa            linear   BCT 28-DEC-2024
DEFINITION  PLP-dependent cysteine synthase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357598483
VERSION     WP_357598483.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..284
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..284
                     /product="PLP-dependent cysteine synthase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30341
     Region          18..277
                     /region_name="CysK"
                     /note="Cysteine synthase [Amino acid transport and
                     metabolism]; COG0031"
                     /db_xref="CDD:439802"
ORIGIN      
        1 mswkawalal leeqeeptpl vefpaggpvt vlmkdesahp tgtmrhrhar alfrqaiaeg
       61 lvtegttvve atggnaavaq awfarrlglp yvvvmpgqrr eerarrveel ggecrfvtpp
      121 laiyeaarei eghfldqfgr aaehdladel laqvepdwvv vgantgatsa tlgrrtrvav
      181 adpensayfp gwtldaadya tgmpsriegi grprvepgfr gelvdrvipv pdeesraaar
      241 tiaevtghpv gdasgtalva glrlaermkg glivtviggi pasr
//
LOCUS       WP_357598636             225 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Micromonospora parva].
ACCESSION   WP_357598636
VERSION     WP_357598636.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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..225
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..225
                     /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=22890
     Region          17..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 mrlaalryav ppglpsrpgc dacgapvglt rpwpalgpaa rcghcrarvg pppgtveaav
       61 laavlllafg gpsdgalpal iwwlgwtipa ilvdlavhrl pdrltlpaaa gtwlllgvaa
      121 ldadpghwlr avtggaglal ffastavllg rrgfglgdak lalsvgallg wygwpvllfg
      181 mlltfglsav vslgllatrr anwsshlpfg pflllgtvga vllaa
//
LOCUS       WP_357598640             360 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598640
VERSION     WP_357598640.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 360)
  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 360)
  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..360
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..360
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=39438
     Region          5..359
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mdelvatvtg fartlraagv gadhertrnm lsaldhldva dpgevywagr ltlcatpddl
       61 prydrcfaay fggrkaavli qgartgttsv trhlaaepeg eggddgtaap atasraevlr
      121 qrdvarltea eraevhrmla mlrtgrarrl srrfegarrg vldprrtird alrkgdvarl
      181 rhkrhttrpr avvlfvdvsg smapyaetll rfahalvrse pratrvysvg trltpitael
      241 rhrdpgtaln evskaipdws ggtrlgeelr eylsrysarg aiaviasdgw ergdpellga
      301 qmarlarqah rviwvnphkg yadyqpltgg mraalphidd lvaghslaaf eqlserlaha
//
LOCUS       WP_357598686             167 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357598686
VERSION     WP_357598686.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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..167
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..167
                     /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=18006
     Region          24..159
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mnqdevdglv prwreaglap sliaslelsk rmsrvnglfe qavktelael gltyaefdvl
       61 aalartgpph rlkpselara lfltsggtsn vlqrlaaagy vereddkgda rsrwvqltae
      121 glrvahlale gssrahteam agvpestlrh aadalreltl algrrvr
//
LOCUS       WP_357598706             195 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357598706
VERSION     WP_357598706.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 195)
  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..195
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..195
                     /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=20757
     Region          3..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvravpdthg eilaaaarqf tvrgyrgtsl qdiasevgcs katvlyhfan keallaelma
       61 paigvlrdld drltgltgaa aqevaaegfv dlavrfrrei avlrgefpel lcqpafahiq
      121 qisdrlrdal aghsdrpgar iaalvllagi seacgefadi tdddlrsall tlvrravepv
      181 daalpqqptt edkds
//
LOCUS       WP_357598774             286 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598774
VERSION     WP_357598774.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=30428
     Region          1..280
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mdflrpttwa ealaakaerp davpiqggtd vmveinmdvr rpaalldlnr vaelrewamv
       61 dgvwrvgaav pyttvieelg gplpglaqaa rtvgspqirn rgsvggnlga aspagdshpp
      121 llaaeavvev esrgrgvrmi paadfylgvk rnalepdeli ravhvrpatg pqyfskvgtr
      181 namviavcsf avalhpherr vgtgigsaap tprrafeaee llareldwta pldpalarrf
      241 gelcaaaaap iddvrgtaay rvhavgvlar rtltwawndh lgrraa
//
LOCUS       WP_357598750             389 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598750
VERSION     WP_357598750.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 389)
  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..389
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..389
                     /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=41507
     Region          5..386
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mnvnhvvvvg aglagvrtve alrgrgfggr itligeerhr pydrpplska vlfgdadtsy
       61 vgtdlaaidv dfrpgvsaks lragvvette gelsydglvi atgaepirlp gdgpqhvlrt
      121 iddahelram lvpgarvaii gagwigaeva taarragcav tvieagqapl atavgaeiga
      181 rtqrwydeid lrlgtmvdsv deggvrlvgg efvaahvvvt gigvrpavew ltgadidlhn
      241 gvvvdehlra slpdtvavgd caawwsrrwq trlrvehwdt alnapevaaa sllgedvayd
      301 pvpyfwseqf ghmvqyaghh pagerlvyrg dpegkwsalw ltaddalaav lavdrprdlv
      361 qgrriidagh rldaerlvdp dvplrdcvv
//
LOCUS       WP_357598724             206 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357598724
VERSION     WP_357598724.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 206)
  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..206
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..206
                     /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=22906
     Region          11..149
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvesggvglr erkkqrtrra lveaalrlfd ekgyeettla eiaaeadvst rtffsyfask
       61 edvvfydseg rmeravatla drepgespad vlrriveesl ewlttyeeft cedaglrlrl
      121 vlkeptlqar almmlfenqa rmaralhaay pdkldrveaa aavgavfgav klaiitnidn
      181 drsveqmwht arraaeitls glcslg
//
LOCUS       WP_357598778             518 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357598778
VERSION     WP_357598778.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=55440
     Region          175..512
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnavqqakgr vrsvplrvkl vtsvlalvav allvisslta yflrnylqgq vdgqvrstaq
       61 glgqllpklr sgevgamlps dyvvivadeq qvyqpkyddl sydpdqlpaf ptsragfvae
      121 egeprtvmsh ngytrwrvyy apqpdgsvla vgqpltdvdr avkqlvwidl lvggavliml
      181 asvgaaivrt slkplveieq taaaiaggdl trrvpdpeeg qeyptselgr lsralnamlt
      241 qievaftara asetsarwae saardaaaaa qasesrairs eermrqfvad ashelrtplt
      301 tirgfaelyr qgaarapeqt agllrriede aarmgllved llllarldre rplaltpvel
      361 pvlasdavqa aramapdrri eleiepesgp lvvsaddarl rqvignlvtn althtppdae
      421 irvrlraepg gsavvevadt gpgltaeqae rvferfyrad aartrradgn tgtglglaiv
      481 aalvaahhgs vevtetpggg atfrvrlpll pqvdgage
//
LOCUS       WP_357598816             298 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora parva].
ACCESSION   WP_357598816
VERSION     WP_357598816.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..298
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..298
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30786
     Region          28..276
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mgagrllavl vtallagcap atavaggatd pvparrapeg syavgvrtlt ldprsarplp
       61 vtiwyptstg qvaagrfpvv iyshglgsrp elhaglttrw aaagfvvaap ayphtrqgap
      121 hftradvrhq padawrlirh lgrldrtrad plaghldlts iaaaghsagg fttsgmfseg
      181 hqarlragiv iaggglpgsf agppapvlfv hgtadpvvpv tvgraayart tgpaaflsll
      241 dqdhgayltp ghrgfapvla tttdflrwtl ygdqgaaarl ptdahsptlt ryesrpah
//
LOCUS       WP_357598847             303 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357598847
VERSION     WP_357598847.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 18123688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=32482
     Region          13..199
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          230..295
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mievrfspdd lsrvrfvhsp laelvasswa lrkptkywmh rpwreraerl lpdaglepll
       61 avlrssngyv pdfltpigaa pnlaaelrav agtdpslvrr qldragaprl tadelvaqlh
      121 ryftlliapd wprlralala dirrrtllaa eqggrtllre lhplirwdga alrvavgttr
      181 pagldgrtwt llptsfsgpt vhaiwegdag palcyppagl gdlwaappps aalgallggt
      241 raaalsllda plstgelaam lglapatash hlttlrdngl ivgvrqgrvv ryartvlgdq
      301 lvg
//
LOCUS       WP_357598860             139 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea dietziae].
ACCESSION   WP_357598860
VERSION     WP_357598860.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 139)
  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..139
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..139
                     /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=14934
     Region          1..123
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mrlafiiggg adglavaewl sylacprgfe vdlldlqaag mpevcshevp tppavqdlvp
       61 wlaaadafvv vipecfpmsl adwcapqwra rpaafagrqd ateaagplrp ffattvaevi
      121 rygrprsadr vlsllrren
//
LOCUS       WP_357598866             252 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598866
VERSION     WP_357598866.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..252
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..252
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27074
     Region          4..246
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mplmpgaepy hhdggqvgvl lchgftgtpq slrpwgefla ghgvsvslpr qpghgttwqe
       61 mnrtrwddwy aevekafadl qgrcqnvfva glslggclal rlaevhgaai sgvvvvnpsi
      121 andvpllrla plirwfvpsv agvandvkkp gvtelayart pvkaaaslps lwslvqadla
      181 kvtqpllvfh saedhvvkpt svaiirekvt qatieeltds yhvatldnda drifagsldf
      241 irthasvplq rd
//
LOCUS       WP_357598906             324 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598906
VERSION     WP_357598906.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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..324
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..324
                     /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=34574
     Region          <32..>173
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          111..324
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mrfgrvpvaa glafglilsp igpaladpkp tlrqakakle klndkadkvv dryntaterf
       61 keaksaytkl ndsyerklat vadlraqvin mavngyklga yptslpglvs tddpsalltg
      121 ltlagqiske eaaklaafdr enrglkterd kaeqaleaad rerdgveker kevmklisqq
      181 kklldklnay npgnphsvgi kytgpasgna aavlrfayaq vgkpyvfggt gpngwdcsgl
      241 tqaawraggv slprttwqqw awgagrkvsl selrpgdlif snglghvsiy agngqivhap
      301 qtgdvvkvvk lssygsglvg airp
//
LOCUS       WP_357598944              95 aa            linear   BCT 28-DEC-2024
DEFINITION  Lrp/AsnC family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357598944
VERSION     WP_357598944.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..95
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=10324
     Region          <2..75
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mvtaivhina evdripevaq tiaeiegvse vysitgdydl lamvrvarye eiaevvpgri
       61 nkvagvlhte thiafraysr hdldaafsig fpead
//
LOCUS       WP_357598936             448 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Micromonospora parva].
ACCESSION   WP_357598936
VERSION     WP_357598936.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 448)
  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 448)
  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..448
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..448
                     /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=48284
     Region          1..445
                     /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 mtdiprravs rtaklaalpl gfagrtvlgm gkrvtglasd visaeiqqrt aeqlfsvlgq
       61 lkggamkfgq alsvfeaalp eeiaapyrqa ltklqeaapp lpaasvhkvl aeqlgpdwrd
      121 lfvefndvpa aaasigqvhr arwrepgfda agapnsrdva vkiqypgagd alladlkqls
      181 rlggmfraiq pgldvkpllt elreriteel dyeleaesqr afaaayaddp eiyipevvna
      241 sprvlvtewv tgtpladiir egteeernea grlmatlhls apqragllha dphpgnfrll
      301 pdgrlgvidf gavarmpegt pepigriaam alrgnadevv aglrsegfig sadeidaegv
      361 ldfirpmlep iaadgfrftr awlraeagrl asprsptyql srqlnlppsy llihrvtlgs
      421 igvlcqleak apyrsilerw lpgfapva
//
LOCUS       WP_357598995             526 aa            linear   BCT 28-DEC-2024
DEFINITION  GMC family oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357598995
VERSION     WP_357598995.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..526
                     /product="GMC family 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=56422
     Region          22..525
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mpdsyryivi gagaagsvva arlsedpdas vllleagdaq vtdavttpwr wnevlltdld
       61 waymsepqpg ldgnrvysaa grglggtsni yhmmhtrgrp qdyddwayhg cpgwsfddvl
      121 pwlqrledqr dghnplagkd gpmtvadaae tgnpvsetfi eacvelghpr lddfnaglfg
      181 agwhhvnikd grrrgaresy ldpaldrpnl tvltaapaar llfegtrcvg veylregrth
      241 taraeaevvv cagaiqspkl lllsglgpad dlaalgipvv adlpgvganf hdhplvigpi
      301 gylaepgddp rgnvtevalf cgsqdglpvp dlevalvhra pfgekffanv irrvqtgqpv
      361 apvrelvdph vvlsltglvg pvsrgwvrla gtdptaypri nanyygdpvd lertvtavei
      421 ardiyrtkaf tgrwglseva pgpgvttrde lrawvkantg syyhfagscr mgadasavvd
      481 prlrvrgveg lrvadasvmp slvnahphtt vvmigeraad lvrahe
//
LOCUS       WP_357599092             266 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599092
VERSION     WP_357599092.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..266
                     /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=28948
     Region          1..256
                     /region_name="ModF"
                     /note="ABC-type molybdenum transport system, ATPase
                     component ModF/photorepair protein PhrA [Inorganic ion
                     transport and metabolism]; COG1119"
                     /db_xref="CDD:440736"
ORIGIN      
        1 mhvveledvg vrvvgksllv gvdwqvdygd hwvilgpnga gkttllslag avrhpsegtv
       61 kvlghrlgrv dmrelrrhig lvaasqrlid eelmeqegat ahtvvltght gtsvplwdky
      121 gdgererahr lladlgckdl adrpfrvcsq gerarirvar slmgdpavll ldepfagldl
      181 psredlitav edlaatrpvl ttvtvthhle evpatttham lmrdarvlaa gpvddvltpa
      241 nlsdcfgrpl qvdrldgrwy aravrp
//
LOCUS       WP_357599106             427 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357599106
VERSION     WP_357599106.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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 427)
  AUTHORS   ter Beek,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..427
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..427
                     /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=44575
     Region          12..317
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mttmnrrdal rmlglstlga talaacapda sgggapkgdt aaktfgftsw slneeaqkga
       61 vqaivdayat akqvkvdtas fpyneylnqv tlklrggqvs gaiqldiswl galaamgklr
      121 dlspqaakgg ytevarssgq fdgkqlglpw ttgsiglian tdllkkagvd glpstveefe
      181 talekvgklg ggvvpyaaat kaaqlkdilp wmqtfgspll ngeeiavgdd asvaavewyk
      241 klydakliap dvdrfdaral faqgkaafyd daiitrgvvs sqapdktlte kmaplarpvl
      301 kagdtprall wghvivvvdg egadaaadfa sfatsdtatv agffekvklp ptttagladp
      361 kvagdtfttd wtekitktat pnpfwryagy aqiestiaeq vqavlvgqss akealakaae
      421 takslqk
//
LOCUS       WP_357599131             214 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357599131
VERSION     WP_357599131.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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 214)
  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..214
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..214
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23083
     Region          9..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mgvddergrv ravalfdldg tlidterrnr miwqmlldnh qldhdvaifm grrgrdvlpe
       61 ifpdhdveql iaevfsyddh pglpdvapvp gaaelvrkva aygsriglvt sarrewaetr
      121 ldqvgvrslf evlvtaedve vgkpdpagfl laaarlrvdp ddcvvfedsv agisaakaag
      181 mkcvavatth agedladadl vvadltavgw ppfs
//
LOCUS       WP_357599132             271 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599132
VERSION     WP_357599132.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 271)
  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..271
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..271
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27795
     Region          14..268
                     /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 mpgaagrmsg katsadgtvi afdrygsgpa vvlvhgafta rghatpvgva aglapwftvf
       61 dydrrwrgds gdtptyaver eiedlaavle aaggsamvfg gssgaalale aavrnpaisk
      121 lalweppyhv ddsapplpdd fatrldalvr agrlgeaver fmveaaeapp eavaamrahp
      181 swaelealah tlayeaavmg pgnalpagrl aaltqptlvl ngedspgwms naglavaaav
      241 pgavrrvled qahnvapeal vpelleffva a
//
LOCUS       WP_357599141             254 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357599141
VERSION     WP_357599141.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28042
     Region          47..158
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mlsgssranr wwwdgnaddy qvehgeflgd tafvwcpegv deadahllge vrgrhvleig
       61 cgaaqcgrwl vtqgarvaaf dishrqlrha qridldtglh vpvvqadaes lpfaddafdl
      121 acsafgalpf vadplavfre vrrvlrpggr fvfsvshpir wafpddpgpr gltsdrsyfd
      181 rspyeerdes gtvtyvehhr tlgdwvsllv asgltvtgll epewpegher vwggwsplrg
      241 rhipgtaifs cant
//
LOCUS       WP_357599148             203 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357599148
VERSION     WP_357599148.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=21668
     Region          5..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mglrerkkeq trrriaeval rlfdergyda vtvneiaeaa gvakvtlfny fpakdclvte
       61 gvkddlaaiv agrlegvspl galrehyral aaqgagemdv esllarvrvi ssspalmgav
      121 hgmrmserye laqalkeahp gddltaqlma aqitaavttv qeaffqriaa gesldeaggr
      181 lagdvelafd llehgltskg dks
//
LOCUS       WP_357599187             340 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357599187
VERSION     WP_357599187.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 340)
  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 340)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 340)
  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..340
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..340
                     /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=35112
     Region          110..340
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnigivgaaa avtalawvvv grrrgrahlp aavvlasvvs lvvtlsfvss gprggedlyg
       61 lveslslial lglmarwspv rqavpagalg gvaastwllr yvmpasplea igmcafwalg
      121 vmaavavgay lrsldtrrar avrderaaqr lrlardlhdf vahdvsemva qaqagqvvgv
      181 gdpaqalaal qrveqaglra matldrtvld lhagpglegl aelaarfssa grarvglrvd
      241 drldvpeeta amayrvvvea ltnvrrhape atlvevavra eggmlvvsvd ddgggvapee
      301 grggfglpsl taqveamggr lraaaarggw tlvarlplap
//
LOCUS       WP_357599203             933 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357599203
VERSION     WP_357599203.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 933)
  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 933)
  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 933)
  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 933)
  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..933
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..933
                     /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=99595
     Region          4..242
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          119..919
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          684..712
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(685,688..689,692..693,695,721,724..725,728..729,
                     731..732,765,768..769,772..773,776)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          719..758
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          764..789
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msarfgvlgp llvldgagae vtpgpakhra llvallmsag hpvthdrlva avwgaeppas
       61 aeavlrvyvs alrkivegir tvpggyllav dpeevdalrf ermvanarra raagrvveaa
      121 dalaralglw rgraldgieg elrrahavpl eelrlaalee rveldlelgr gaeligelra
      181 lvaayplrer awaqlmhalt qagrrsdalt ayqeargtlv aelglepgae lreahervla
      241 qelgrsvpne tppdiadftg rqavldwiea alpapgaapv hlvlygpaga gksalavhaa
      301 arldlpdgrl haslrdrapg avledllrsl gcpdgavpss ldervrlyrs lvagrrllvv
      361 lddatseaqv rpllptgagc ltlvtsrspl lgleaarayp ldvleageav amlarivgad
      421 rvaaepdqah rivrlcgalp lalriagsrl arrrgwtleh ladrlgderg rldelsagdl
      481 avrsslalgy ralsdderll lrrlgalscp dfapwiaaal vgrdggrvme slaeagllqe
      541 rgldrygwhd ltrlyaaerl aeeegpasav lagaageild rarrarelml paepgsgltl
      601 shtverdlat arlaesarwl aaersfmvaa vadlhrarld eaawrlafyl tplfelgayh
      661 ddwrttaalg lesarrarhr hgealllrsl adlhraegrl eeaagalraa lpltergeva
      721 rttlrlglvy raqdrlsdae rcfteclaaf gsgqggggdp rgsadalral gelradeels
      781 rralelyrql gdprgeaatl ldlaglclav rrtkearela eraaglsrrl gdrlpaasas
      841 lllagtarae grpeaaraaa tealaafeah gdrrgmakar laiaaaaldl deidgavdal
      901 acimgefdal gdrrglgeaq elarearrrr glr
//
LOCUS       WP_357599229             306 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357599229
VERSION     WP_357599229.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..306
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32122
     Region          8..216
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtgdhlaiev srltkrfgdv tavrdlsftv rpgvitgflg pngagktttm rmmtglvspt
       61 ggtatiggrp ygqlarpsrt vgavfdanaf hpghtardhl rvyaamggyp dsrvtdlldl
      121 lglaeaahrr trgfstgmrq rlnlatallg dprvllldep gngldpegms wlrgflrqfa
      181 degrtvliss halgeiqqlv ddvvvirrge lvaagpcsrl agppavlvts pdadalaavl
      241 aaapanggta phveavgpdr lrvrgldapg iadlaaahhv rvhelvvest sleelflhlt
      301 rdkavi
//
LOCUS       WP_357599250             328 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora parva].
ACCESSION   WP_357599250
VERSION     WP_357599250.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 328)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..328
                     /product="phosphotransferase 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=34510
     Region          24..254
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msppqlppvp yhasaqrpsw palpealraa vadrlgapvv tarvagagft rgfaavldta
       61 dgarafvkaa paaeqphlvd wyareaaild rlpvdlpapr prwtlsaagw fvlctdavdg
      121 htpslpwvpa eldatltgya qvaaaladpp aeltalglpr ladlarsdil wweevaagre
      181 ptpplpapll arlpelvele sllpryaaga tglihgdlrl dnvligsdgr awfcdwawvc
      241 sgpawfdlag llltayasgl dadrlfaahp actgapadal daalaalagy yltgaaaapp
      301 tasphrrahq rwsgeqslsw ladrqgwq
//
LOCUS       WP_357599273            1245 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599273
VERSION     WP_357599273.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1245)
  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 1245)
  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 1245)
  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 1245)
  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 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1245
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..1245
                     /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]"
                     /calculated_mol_wt=129783
     Region          3..1206
                     /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 marpaelial igigcrlpgg vgsadeywdl lcegrdasgp apeerwrdya drgpsyatav
       61 rrtlargsfl dgvadfdaef fglspreael mdpqqrlvme tawealehag vaptslagtd
      121 agvyvgvctg dyghrlledl pdieawtgig satcavanrv syaldlrgps mavdtacsas
      181 lvavhlavqa lragetdval aggvnlilsp getltldaag tlapdgrsks fdaaadgygr
      241 gegavvvvlk rlsdavrdgd rvlatirgsa vnqdgrtagi mapcgqaqeh vmrralrqag
      301 vepgtvgyve ahgtgtavgd pleagalsav ygkgrppeqp cligsaksni ghlegaagia
      361 glvkavlale rgqippsrld tpnpavdwea aglrvvdapa pwpgsahprr aavsafgygg
      421 tvahvvleqa ppaeppaegr agrlfpvsaa sraalrqaag nlagvvgdlp aagvghtlal
      481 rrahlphrav vaaedpaala arlralsagt phdavttgqv lvdpgpgpvf vfsghgsqwa
      541 gmgrellete pafaavvdel epvfaaeigf sprkvltede ltdvdriqtm ifvmqlglve
      601 lwrehgvrph avighsvgei aaavtagals rldgarlicr rsrllrrvag rgamvmvqlp
      661 faetarllge rtdvvaaias spgstvvsgd pdavadvlag wleqgiparr vasdvafhgp
      721 qmdpllaelt aaaadltadt pglrvystal edprtshgfd gaywaanlrr pvrladavta
      781 aaadgyrafv eisphpvvth svletlgagg yeeifvgasl rrnrsprvtl pasvaaayca
      841 glevdwhrlq paggpvvlps ypwqhrrhwr apsapdtagr ghdpdthtll gdgvdlagsd
      901 vrlwrtgvdd qtrpypgsha iegveivpaa vlaatffaas ggrtlgevtm saplltadrr
      961 evqvvrqgge lrlaaraage pdaawqmiat atvpatpgea pdppahplta adpglvmerl
     1021 aavgvpgtgf dwtveellrg hgalrarvrc gpaatwapvl daamsvapsa fpgdpllrmv
     1081 thvdrlvavg eppdtveiev wldperadtv qvrvtdgagd vvgwlsglry pvidvpapae
     1141 ngtdgtrpae siadlgpeel raflleevga qiakemrldp gdlqphrplv eqgldsvltv
     1201 vvrrrlekrf rcslpttllw qqptvaavsd yiaglvsang saeag
//
LOCUS       WP_357599319             129 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599319
VERSION     WP_357599319.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 129)
  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 129)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 129)
  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..129
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..129
                     /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=13330
     Region          <5..129
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrggqslgea lesyltewse rtgivvetwa lpatdvssrv lrgvmaamdd alsnvelhsr
       61 arivsiavtv sksglrmtis ddgqgfsltg agggiarmra afaemggils vnsvpgqgtt
      121 vtgvvprhr
//
LOCUS       WP_357599345             497 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599345
VERSION     WP_357599345.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 497)
  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..497
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..497
                     /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=52356
     Region          5..115
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          226..491
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrisdllave dlrltllagd parefhtvhi tdlpepgryl aggelvlsgl mwwhapedsa
       61 rfvsalvesg vaalgagqaw lghipadlva aceaaglplv evptevsfrt laelvvprls
      121 gdvrdalgrh rrlvaaiaeg adlrelfelt aaelgvtgav vsasgevivg aaadpvrlaq
      181 ayltaprlpv hvgehtifav grghraagwv lacdgdligr adlgyelaac vglersrmee
      241 grrverrlae rlivaalaes dvaelnaglr tcgidaaepy aivnaaaprp gatrgpdpat
      301 lggqiveell grevvaaaga dgavalvplr grttaelaer lragaevlaa lpdtrlcvgl
      361 sgaltgaaai kggveeagha rrlaearagg vvtsdeiyth alllatvpgd vrrsfaarll
      421 splldydrrh qselvrtlgv fldcagswna caerlhvhvn tvryrirrie eltgrnlstm
      481 adrvdfflal rdtglpr
//
LOCUS       WP_357599382             560 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599382
VERSION     WP_357599382.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 560)
  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..560
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..560
                     /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=60226
     Region          15..492
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mplnerslig qevagyyied ivgkggmavv ylaldprlsr rvalkilnpv lsvddrfrqr
       61 filesrtvas iehpniipiy eanadadgvl yiamryvdgl dlrrliydrg alpigqayqi
      121 faqvaaalda ahahdlihrd vkpanillag dhvyltdfgi tkhrssisgl tqtdqfigtp
      181 rymapeqink ehidgrcdqy alacvvyeal sgrlpfqren diallwahla eqpaplsqlr
      241 pelpaqidav mlralakspe qryatctefv talrdaisgg ppdalggahf vprqglpsgp
      301 ypvlgsgpst gpstgpsmgp htgphtgpsp laaptsapha asgpasrlap ptqpnvlkrr
      361 pgrvpivatt lvaavaalal vvmiimnhrs dtwsryktst aapltfeypg dwtvrthqdl
      421 favasphaqe feslfvagpg adwtavsqiv eddpdsasgv yvqvsdtlda ngtsdqmkak
      481 meallpgqvd vgrpvqdqag sspatrfdga lhdpgsgtrl gfvsyvidrq pktmlvmyfc
      541 akttcddatq arirqsvrvs
//
LOCUS       WP_357599408             285 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599408
VERSION     WP_357599408.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 285)
  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 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   3  (residues 1 to 285)
  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 285)
  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..285
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..285
                     /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=29637
     Region          1..284
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mepvavglig agpwaeraha pmlsrgphtr lagvwarrpe aaarlgapvf erieelfdac
       61 eavafcvppa vqaelgvraa ragkalllek pladtlddar rlaeavaeag vasqmvltmr
      121 yaaqtrafla rcreiqafgg haanisgvll gdhpyatpwr ldkgalldvg phvidlldaa
      181 lgrvigvrah gdplawtgll leheggavse aslcmaaagd pppstfavyg ragsavlgrf
      241 dddpmvtlva efaetvrngg ghpldaahgl rlqsiiaeae aqlap
//
LOCUS       WP_357599454             194 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357599454
VERSION     WP_357599454.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 194)
  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 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 14302692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20242
     Region          3..69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          90..179
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(93,108,110,121,126,130,164,166,178)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mvdlavlggh iqalrhdrgl tlqqlaeaad vslsmlssve rgqkaptivv lariadglgv
       61 pladvvappg ggrvivrraa gqdtvdepgg wrrtvltpvv pgvnfewirt tlppacdagr
      121 fpayapgshe yivvesgtlr ltvadasvdl nagdsayfaa dvthayanag sgtctyyvaa
      181 limrprtaqp rtrs
//
LOCUS       WP_357599455             283 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357599455
VERSION     WP_357599455.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..283
                     /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=30572
     Region          29..281
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mhtaqpsqta litaasraah lvvdqepfif rdtvaasllg elaeqfigyh rshgdhlvls
       61 gtraqvtars hyterrlael ardgleqyvv lgagldtfac rpgpevklfe vdhpatqrwk
      121 rdlfaaagvt pshalafapv dfetddlmas lraagfdpsk palvswlgvs myltrdavaa
      181 tlatvgrlap gtelvmeyal psafrderga afadfalpaa aergepwltf lapddlsall
      241 vqhglrateh vrqadsiapa lwrrsdglrp adlcrlarat vlr
//
LOCUS       WP_357599498             106 aa            linear   BCT 28-DEC-2024
DEFINITION  GroES family chaperonin [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599498
VERSION     WP_357599498.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 106)
  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 106)
  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 106)
  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 106)
  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..106
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..106
                     /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=11831
     Region          8..93
                     /region_name="Cpn10"
                     /note="Chaperonin 10 Kd subunit; smart00883"
                     /db_xref="CDD:197951"
     Site            order(9,11,14,45..46,58,68,73,75,91..93)
                     /site_type="other"
                     /note="oligomerisation interface [polypeptide binding]"
                     /db_xref="CDD:238197"
     Site            25..38
                     /site_type="active"
                     /note="mobile loop [active]"
                     /db_xref="CDD:238197"
ORIGIN      
        1 mvepkfeiqm lhdrvmikle peaeerrsgs givipatvkm anrlawgevc gvgtnvrsvk
       61 vgdkvlfnpe dqfevevhaq iylvmrerdl havatqetdh gtglyl
//
LOCUS       WP_357599480             359 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599480
VERSION     WP_357599480.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=36146
     Region          51..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 mrpaeqsagv geaeppfave gggraargrt aalagglvva vavlalvama svalgarsma
       61 fstvidafla pdgsgdhtvi relrvprtfl glgvgatlgl agalmqsltr npmadpgllg
      121 inqgaalgvt lalglfglsd pavyvwfafg gaalasvvvy alasagrsgs spvrlalagv
      181 algmvctava sailrmdtrt fdrmrfwltg slagqtadtl vrlapfmvag lalglllarp
      241 lnmlalgdda gkalgvavnr triltgvavt llcgaataaa gplwfvgliv phavravvgp
      301 dqrwvlpyst laapvlllga dvvgrviarp gevqvgivwa vigapifivl arrkrvaal
//
LOCUS       WP_357599500             882 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357599500
VERSION     WP_357599500.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 882)
  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 882)
  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 882)
  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 882)
  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..882
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..882
                     /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=96097
     Region          2..218
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          85..868
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtsakqrtll avllteanrp vpsdrladaa wgesppapat lrwhvhhvrq alggdrltrr
       61 pegylltvhp geldaerfer lcasaadldd pariaevlkr alalwrgpay adladaapvg
      121 veasrleelr laaverrala lldlgrdgea atelqphlla hplrerlrel lmralhqagr
      181 radalrlyrd grellagelg iepggalrel haeilreepp avsvrpaqlp pdvfaftgrq
      241 aelavlddll esegsarvaa isgvggvgkt glavrwahrv ahrfpdgqly adlggrdpge
      301 vlerflaalg vmrvpegldq raalyrglas srrllvlldn aadsaqvrpl lpaspccfav
      361 vtgrsrfegl vagvgarpvp levlssgqaa tllgrvarve pdealalael cdrlplalri
      421 agarlvtrpg wtprrladrl eqerrrldel rageldvras fevshrdlpa peralfellg
      481 lveapdfapw taaalmdlpl aeaaelleql aeaqlvqqlg fdeagqeryr fhdlvrifar
      541 eralesmala ereaaldrvl gcllalgeea ylreyaggfr largdaprwr lqgevlpahp
      601 mgwlaaerat lmawvrqaaa mgrvaacwdl alfsvrlyel tgnmsdwres stialelcre
      661 hgdsygaavm lvslgslelf ekryepardl lvqalpeieg pyraltlgnl glieralgaa
      721 dtalahmtea reialhegdr ateslmlshm aavhheagrr dtaqailgwa atvaegirrp
      781 qavirfiaar mandrgeyer aerlsaevla elavigdrrl epsvmalrar smrgqgriee
      841 aaacardala maralgdana eqeyarllys lsgepvgqad lt
//
LOCUS       WP_357599516             191 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357599516
VERSION     WP_357599516.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 191)
  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 191)
  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 191)
  AUTHORS   Rosinski,J.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..191
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..191
                     /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=19744
     Region          22..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          99..185
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(100,115,117,130,136,170,172,183)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mnapdrerrp assaaaaaga qiqrrrlqrg msqaelarrt glskgtlsql eagagnptid
       61 tldaiavalg ipltdlltrq agpgthyvpa tpagqdgptr ellrrisggh slelwrlrlp
      121 phtsvdgvph apgtvehllv asgrltagpa ddprllqagd llafagdaph ayrtdatpad
      181 vtvviaspsf t
//
LOCUS       WP_357599524             108 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357599524
VERSION     WP_357599524.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..108
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12157
     Region          1..90
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mfsnkwtgla mgalldgprr fnelrrmldg itqkmlsqtl ralerdglat rtvyptippk
       61 veyeltdlgr saidilraig dwarehaddv taaretydrr akepvrav
//
LOCUS       WP_357599565             186 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora parva].
ACCESSION   WP_357599565
VERSION     WP_357599565.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 186)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..186
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19493
     Region          17..76
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          100..183
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(113,115,127,130,134,168,170,183)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mppepaapla tiaaalrrer ervgisltel arragvakst lsqlesgsgn psvetlwslg
       61 valgvpfsrl vepvddvvrv iragdgsdvr seqadfsgtl lsagaahlrr dvylirlepg
      121 airtgqghtp rsiehvvvaa grlrvgpega sveldpgdya rfpgdaphhy ealaagtfav
      181 limehp
//
LOCUS       WP_357599535             180 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora parva].
ACCESSION   WP_357599535
VERSION     WP_357599535.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 180)
  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 180)
  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 180)
  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 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..180
                     /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=19537
     Region          38..144
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
ORIGIN      
        1 miprsratgr alfyqafyrl plpvrrrlvr lavpkyvvga vtlvrdseaa gagrllmlrq
       61 ppgkawslpa glldrgeapv vgaarelfee sgirlppsrl rpavpnaivh akgwvdmvfe
      121 tdvpasstdl tvdgaevfea awhplddlpk ltwptarlla yydigplagk fpppipddtp
//
LOCUS       WP_357599588             299 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357599588
VERSION     WP_357599588.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=33103
     Region          2..290
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrvragetra allfispwii gflvftawpv insaylsltd ydvindpnfi gfdnyvtlfq
       61 dpkvglalrn tfvftvmsvp vqlvvslgla lllnsaarat gffrtvfflp kmtppvaigi
      121 lllllfngqs glinsalglf giegpswttd pdwvkpglvl mslwtvgasv iiilaalrav
      181 pqqlydsalv dgvgwwrrtl ritvpmispt lfflfvvdsi nalqsfteay taffgsgntt
      241 ysndaalfyv iylfqqafef lhmgyasala wvlfvvimvi tavqilltrr yvyyegdrp
//
LOCUS       WP_357599609             337 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357599609
VERSION     WP_357599609.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 337)
  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 337)
  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..337
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..337
                     /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=36072
     Region          10..332
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtfdtvtedr plraviagag figrqwatel llhpdvslvg wadidpskvp agrgvpafgs
       61 vaemveavrp dflvngtvpa ahhevtlaal ergvsvlsek pmavtfeega dmvaaadrar
      121 rlfmvsqnrr ylpglvayrr tvaelgqlai ltsefyipyk svkfledlph pliqdmaihl
      181 fdaaraisga dpmsvycesf rpaaswytga csataifemt gglryvfsgs wsapglqtsw
      241 tgswraigar gtavwdggsa igaegvtpve lepdphqard rfpglawale efvgalrtgr
      301 ppqgeghdnl aslamvtsal esalrgerik cplygat
//
LOCUS       WP_357599659             460 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357599659
VERSION     WP_357599659.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=49232
     Region          6..367
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msssrralgl livtglglsv aacgstaeqp apassaaggs akaaapvtis vgcqppktnp
       61 lqrkdwdddv aafqklhphi tidskdgfpc hdvktydakl aggqmedvfy gyfgdvqtai
      121 kagqaadita yadtittlrd idpsvmaayt vdgkiygvpr gnykvglvyn rklftqagld
      181 pntppktwae ireaakkisa lgpgyigyge ysagntggwh ftqsiygrgg avvdetgkka
      241 afntpegkav lqnlkdmrwt dnsmgtkqly qwddlmrlmg agkmgmilga pdvitelhdn
      301 rkakyedfgl aafpeakatl gggdgymfnp katpeqikag llwldyyvlt pgrgqfdyar
      361 qkatgravgl pdnnvwgdsp tgqkllelrk anstlptenf aayvegsadi plkleppmnq
      421 qifqildtpm savltrqdad idqllaeaea kvndvlskas
//
LOCUS       WP_357599662             296 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357599662
VERSION     WP_357599662.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 296)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..296
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..296
                     /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=32780
     Region          14..294
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mgrrppsrrg rearrnltay gflvaalicf glfswypmvr evllslqenn fvdaptwvgl
       61 dnfetvvedp afaqawinta aftglallig yvipfcaaii lnelrhakay lrfvvylpvm
      121 lppavsvllf kwfydpgpgl fnqilgffhl pglawldstd talislvivs twmnlgsgtl
      181 iylaalqtip selyeaaeld gagmfkrirh vtipqtklil lvmlllqiia tmqvfiepfm
      241 ltgggpenat vtvaylmyqy afnfgnfggg samglmlmiv livfsavylr vsrent
//
LOCUS       WP_357599680             273 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357599680
VERSION     WP_357599680.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 273)
  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..273
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30753
     Region          2..64
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          88..266
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mlgaslrrlr easgldraqa gfhirasesk isrmelgrvg fktrdvedll tlygvvddae
       61 rrallemvre antpgwwhky saelpawftt yvgleeaael irtyevqfvp gllqtasyar
      121 svfqlgnpgl spdkierrvh mrmqrqerft qkdgprlwav ideaalkrti ggrevmseql
      181 qhllevaalp nitlqvmpfr fgkhaaegga fsilrfpesd lsdvvyveql wgalyldkre
      241 didpyltame qlcvesttpg gtveliggll rkm
//
LOCUS       WP_357599689             153 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357599689
VERSION     WP_357599689.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 153)
  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 153)
  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..153
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..153
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16808
     Region          <42..127
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mvtarilaep ggrddpivae lrdspvrgps wlpgpalgsf lagasvlrre aflecggfnr
       61 rlwlggeeel lavdlatagw elcyleeltv hhqasrlrdp harrrvglrn tlwftwlrrp
      121 lgaalrrtah lartvphdrv salaaldalr glp
//
LOCUS       WP_357599691             317 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357599691
VERSION     WP_357599691.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 317)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..317
                     /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=34983
     Region          23..311
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matlqatarr rhrrlvrhtl dlklspyayi apffllfcaf gvfpliftaw vslhqwtlts
       61 dvhtfigaen fttllgdgyf wnatfntfsi giistvpqlv laiwlahlln rplraqtffr
      121 itllvpnvts vvavvvifsq lfgrdyglin wmlswfgidg vawaegtats hvaisamimw
      181 rwtgynalif laamqavpke lyeaatldga snltqlrkit ipmirptivf vvtvstigam
      241 qilaepllfg agsgaggits ggpdhqfqtl alyvydlgfn kfdfgyasaa swvmflfvvl
      301 aagvnylltr rmggafk
//
LOCUS       WP_357599873             169 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357599873
VERSION     WP_357599873.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 169)
  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..169
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..169
                     /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=18631
     Region          10..137
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtsnrhndgv ldaardclla ygvrrttltd varragvsrm tiyrrwpdvr tlvaelmtre
       61 wvrvvegldl sdpvravvag vrglrahplw rkiveadpel lvqylidrrg asqeaalgvl
      121 eravgdarka ravllvaqsf llsaptmldp vtldelddel aamleaylg
//
LOCUS       WP_357599874             684 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora parva].
ACCESSION   WP_357599874
VERSION     WP_357599874.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 684)
  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..684
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..684
                     /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=71600
     Region          12..268
                     /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..37,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msnalpqlva dryrllsplg qggmgrvwka rdevlhrdva ikelvpppgl tdeerremre
       61 rslrearaia rlnhanvvri fdvlrtdgdp wivmeyvask slqdtlaedg pvsvartvei
      121 glgvlgalsa ahkagvmhrd vkpgnvllge dgrvvltdfg latipgdpnv trtgmvlgsp
      181 ayisperard gtagpeadlw slgatlyaav egkspyarps aigtlaalat epipppknag
      241 plkavlngll rkdpnerita evaerllrra ggkrsrgisl ldgvrrpgpn gpreprpplv
      301 paprpaesvd rpvspppaaa atpaaaatts aatpaadatp tavvssgaaa dptalvsaer
      361 aaaapaepta tidrsseaaa seaaaseaaa seaeptatva aapdtsgdgt tnvddeptvv
      421 dgppvapeqr kpttptslmp pvgpagraav pasdgtkpnn trrnvligav vallliglav
      481 vvpmltsgdg dktpqadptg aaatsapapt saaapppptt gaptpsasat psvdpnalpa
      541 gwklhkdpag falpipdgwv rrdagqntvv fdesngpgel lvqwtstpkd daykdwqrie
      601 pdrreivkny qnlgikrcnf wktcadwewl etrdgqrihv rnrgfvtasn rgyalrweia
      661 qkdwqanlpn fdriakgfvp drkd
//
LOCUS       WP_357600009             133 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600009
VERSION     WP_357600009.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 133)
  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 133)
  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 133)
  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..133
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..133
                     /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=14619
     Region          5..126
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mavgidkiaw ihledgkils trsygkdvyy lpggkrdpge sdldtlvrei deelsvaivp
       61 staahlgtyq aqahghavgv mvqmacytad hhgtptpsne ieeivwltya drdrvspvdq
      121 lifdhlhqtg rlr
//
LOCUS       WP_357600037             376 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Nonomuraea dietziae].
ACCESSION   WP_357600037
VERSION     WP_357600037.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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..376
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..376
                     /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=39867
     Region          1..376
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mermydivlf gasgftgalt aeylaeavpp gcrwalagrd raklealghd vpllhadvnd
       61 paslaalaeq arvvattvgp yirygeplvq acaragthyv dltgepefvd rmfvrydgma
      121 rstgakivha cgfdsipydl gvlhtvdqlp sgvplkvsgf vrsngrasgg tvhsavtams
      181 rarqmaeagt qrrsaeirpk drrvsslpgg lryvggwalp mptidhqiva rsaraldryg
      241 pdftyrqhfa vrrlptalal aagagalavl aqippardwl igridagegp taeqrarswf
      301 kvtflgeggg arvvtevsgg dpgygetakm laesalclaf ddvpevagql ttavamgrpl
      361 idrlqragis fttlqa
//
LOCUS       WP_357600072             257 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357600072
VERSION     WP_357600072.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=26869
     Region          1..255
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrlavstlgm pgegldraie iatgggcqgl elrlhpdtgv hggldaagrr svrerverag
       61 leisalagyv gicepgddep vvealiadlr laadlgapgv rvfprgddpa vgarrlkavs
      121 gtaaalgarv lvethdrmat gaavagllae aacpettgai wdllhpwrhg espadtlaal
      181 gpylsyvqvk davsaedttp vpmwtgsvpl eesgellraa gydgwvslew ertwypqvap
      241 veeilpgaad wvrrfal
//
LOCUS       WP_357600159             348 aa            linear   BCT 28-DEC-2024
DEFINITION  YncE family protein [Micromonospora parva].
ACCESSION   WP_357600159
VERSION     WP_357600159.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 348)
  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 348)
  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..348
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..348
                     /product="YncE family protein"
                     /calculated_mol_wt=35571
     Region          3..>138
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <220..331
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          268..306
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mqigrgftla faaltagllv gavpghaqaa aaptvtplpm ktvgdvvsag drvfvsggrs
       61 stdvvvtsat gavvgtlsgl pgptdlllsa drrtlyvalp sanaiaafdt gsliesaryd
      121 tgagecpssl altgrylwfg ygcdqwggni gqidlgrqpa rltthvaeqd fhdfplltaa
      181 gqnrsvllag qpglspasvy aysigtagtl ttlrtnawsa lgsnlrdial dptgttlyta
      241 agapyevqaf pfadistpsa typtgaypna vevsrdgtri aggadasydp dvfvftpdgt
      301 elarfelgde lspgalawsp ngarlyavay dwtgvnqatl hvlpvpaa
//
LOCUS       WP_357600167             373 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600167
VERSION     WP_357600167.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 373)
  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..373
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=39632
     Region          149..372
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 maarpetark lllywmdavi vllvvlmvti tllhatagli splnatitiv cllgffglfp
       61 fllrdaydar pdrptpklli aalfaavava llphqspqdt pswlevgvlw lsaaalyvpl
      121 avtvclgvgv vglvsgytaa isdrawpdvl ipetisaivl tsamllwrwl wwtirdahds
      181 keakarlavs eerlrfardl hdllghslav itlkselaak latkdagraa demgqvrrla
      241 gdslaevqqa vhgyrtldld eelagaraal eaagarclid aradglspsa rtllawavre
      301 gatnvlkhst atrcaitidg gvlemlndgv peqppvpgng lrglserlat aggsfsaept
      361 psgefllraa vpt
//
LOCUS       WP_357600188             221 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600188
VERSION     WP_357600188.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=24154
     Region          <1..197
                     /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 mhivimgcgr vgstlahile dsghsvaiid rdpqafrrlr agfrgrrvtg igfdrdvlte
       61 agiesaaayv avssgdnsni isarvaretf gvdnvvariy dprraevyqr lgiptvatvr
      121 wtadqimrri lpegaeplwr dptgtvilae vtahsdwigt rvvdlesrvr trvafinrmg
      181 ealtitddsv vqegdvlhvi aaendmdrin kvlaaapeee e
//
LOCUS       WP_357600170             362 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600170
VERSION     WP_357600170.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 362)
  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 362)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 362)
  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..362
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..362
                     /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=38716
     Region          149..361
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrratkldkv rwlivystdg vmlvaligyy dlyvrwqagv slpvlvtgav lllafnvlat
       61 rphriamrgg srptailvvt giialllavi glmwaipawl aalapfvrrr tivvmsvltv
      121 aaynlcmgll gadvlglllv qtlltvisvg gvlanlwlwr vakeahegqe arsrlavsee
      181 rlrfahdlns llgqslvdia artekaahvl padaraaade mfavrdlarq slrevrsvvq
      241 syravdldem lasvravlea advrctvhae tgslppeart llatvvrega tnvlkhskae
      301 rctitiedgv lemsndglsg pagehtpngl aglaqrvraa ggtleaaptp egryllraav
      361 pa
//
LOCUS       WP_357600194             419 aa            linear   BCT 28-DEC-2024
DEFINITION  (Fe-S)-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357600194
VERSION     WP_357600194.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..419
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45315
     Region          4..403
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mdpelikdcv hcgfclpscp tyvlwgeemd sprgrihlms qhvegtpitp emaghfdacl
       61 gcmacvtacp sgvqydrlie qtraevereh vrepreravr glvfglfpyp rrlralrptl
      121 glarrlqpll erahpslgam ialapvpgrr qrlpgrvrav gerravvgml tgcvqneffp
      181 qvnaatarvl amegcevvip phqgccgals vhsgrddqar rfakrtirtf eragvdtvvv
      241 naagcgssmk eyaelladsp ewagraralr tvdlaewlae lgpvaerhpl pvtvayhdac
      301 hlahaqgira qprellrgip glslrdipes dlccgsagty nifepsaard lgdrkaervr
      361 stgaqllvsa npgctmqiaa amrraggeir vahtaeilda slrgvspsfl daaggkprs
//
LOCUS       WP_357600254             457 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357600254
VERSION     WP_357600254.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=48084
     Region          1..433
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtirvrlall ygvlflaaga vllagtyvla trltwpvlpe isfgeppldp vrqraaevrg
       61 fvtaaavglg amtvasvglg wvmagralrp lramtaaare isarnlhqrl gaqgpadeik
      121 dladtfdall erveaafeaq rrfvanashe lrtpltfert llevaladpg adaerlrgvc
      181 graleanrqq erliealltl arsqrgldhr epldlasita gilnaaewaa qdtsaegfll
      241 eghgggqpgl glssspgges plgfssspgr rslfglssps ggrpefglss pggrptlars
      301 rllepavpep geeapgdgtd epveirveae lrrapafgdp rlverlvanl vdnagrhnvp
      361 ggwirvwtgl hdgrptvrvt nsgpvvppar vdslfqpflr meatrtsddg glglglsiva
      421 aittahdadl hatalllggl dvrvafwavp dfvgavp
//
LOCUS       WP_357600289             312 aa            linear   BCT 28-DEC-2024
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Micromonospora parva].
ACCESSION   WP_357600289
VERSION     WP_357600289.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 312)
  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..312
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..312
                     /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=32207
     Region          46..293
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mnrplrtalv gamtaallat vavapaqahp agrppavlal pdgfqpegia tagryayfgs
       61 ratgaiqrvd lvtgrgttig aatgtpslgl kvdprgrlfv aggtagdarv ldtrtgevla
      121 ryqfataptf vndviltrda ayftdsnrpv lyrlpfgrgg alppadavtt itltgayeqv
      181 gtgvnlngit ttpdgraliv vqsttgtlyr vdtvtgastv vdvpghtftn gdgllllgrt
      241 lyvvqnrlnl iavvrlnhag tagtltdtit dpnfdvpttv aaalgrlylp narfttpptd
      301 ttpytavavr ah
//
LOCUS       WP_357600278             252 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora parva].
ACCESSION   WP_357600278
VERSION     WP_357600278.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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 252)
  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 252)
  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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..252
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26535
     Region          25..236
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mpdhaeppqt sppgtaerra srrpvkavlf dfhgtlaqve dpqrwvleaa aacgvtldrv
       61 ratsladrll tagraggplp arvpprlael wadrdlyqha hrgaytglae tvdagidgfa
      121 dalyerllta dgwqpyadta ptltalrdag vpvavvsnig fdlrphfdtw gltdlvdafv
      181 lsyevgrckp dpaifwracg mlgvdpeqtl mvgdtpadag avaagcsvlv lpaaepgren
      241 glgavldlal pa
//
LOCUS       WP_357600297             476 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600297
VERSION     WP_357600297.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 476)
  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 476)
  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..476
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..476
                     /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=53235
     Region          3..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 mspsvaiiga gfgglcmair leragirsyt vfekagglgg twrensypga gcdipshlys
       61 ysfekyaswt rrypeqpeil eylehcadky dvrrkirfga evqraafdgt twqvtsggrt
      121 eafdvvvmsv gqlnrprlpd ipgisnfegv sfhsarwnhd hdltgrrvav igngssaaqf
      181 ipriaeqagh lyvfqrtpnw vipkpdtafg plarlalrfv pglqrvyrew ifryaeatly
      241 palaqgwsae llrkralrhl hdqvpdpalr akltpdyppg ckrvvidsaf ypaltradvd
      301 vvtdrivria pkgiettegr yevdtivhat gfrsteflap mevvgregrt leeqwkggae
      361 aylgismpnf pnlfllygpn tnlghnsivf miecqvrhvm sclprlsatg pievrpeama
      421 awrrqldaam trmvwgggcq swyktpegrv tnnwpgtttl yrkltsrppa payrra
//
LOCUS       WP_357600325             319 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea dietziae].
ACCESSION   WP_357600325
VERSION     WP_357600325.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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..319
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..319
                     /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=33891
     Region          115..313
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mlrlvlavcl llhggpaptr dsrdtvgyws rerivnarpa dllpfprldv appdsappev
       61 plgygarrtv pgrkvltpgg drlgyslvar pytgahrlag illshdpvag tdiacgaavi
      121 rsrsrslvlt aahclyaggr plshvaflpa ynsldagrss rgvwpavrvw vprrwrerpy
      181 speqlpydfg vagvmrghkl leevtgpglr plltprrsav rglellgypv grsypgtdmy
      241 rclgdavdgg aagpgvlvth ncqaangtsg gpavrageva gvvssssplr epagftvltr
      301 ltprpfgrll aradhvmrh
//
LOCUS       WP_357600331             425 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Nonomuraea dietziae].
ACCESSION   WP_357600331
VERSION     WP_357600331.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..425
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..425
                     /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=44469
     Region          20..423
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 msvmvpsrtp alitpgqqal dsalhqlgqa aeelglddgl rtmlatprrs ltvsvpvrre
       61 dgsldvvqgf rvqhnvsrgp akggirfhps tdihevtala mwmtwkcalv gipyggakgg
      121 vsvdptvlst relerltrry vneilpligp ekdipapdvg tdeqtmawim dtysvnagys
      181 vpgvvtgkpm tlggslgrtg atsrgvqiat ltalgrspeg vtvavqgfgk vgalaaqyla
      241 dagarvvavs dvsgavhnss gldvadlraw vtetgsvagy rhadalahde lleldvdvlv
      301 paalegaita snaprvrarl ivegangptt peadeilaaq gttivpdila naggvivsyl
      361 ewvqnmqays wsasevevrl rdlmegafse vksvaaargl tlrqaahvig vgrvaeahqm
      421 rglyp
//
LOCUS       WP_357600351             199 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357600351
VERSION     WP_357600351.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 199)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..199
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..199
                     /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=22173
     Region          9..193
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mssgfsrlrr edllktacev iaeqgfghtr tidiaraagv sqallfyhfe tkerlfaqaf
       61 tyaarlhlna ladieqstgt plerlrtllr lcspaipteg wrlwidawse amrnpeleei
      121 srridyqgrv llrgiieagv acgefkceds ddatwrilal vdglaiqthv hakvlsrrrv
      181 nvlirtaaaa elgisaekl
//
LOCUS       WP_357600373             282 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600373
VERSION     WP_357600373.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 282)
  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 282)
  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 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   5  (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   6  (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   7  (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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..282
                     /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=29849
     Region          15..219
                     /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"
ORIGIN      
        1 mtaatgyaah rtlplrveiv rqfkrrrtmv mfglllalpw ilviafqfgp qssgqgqssl
       61 risdlatagg lnfaafalsv sasfllvvav alfcgdtvas eanwsslryl laapvprdrl
      121 lrqklivalg ysaaaviclp lmallagtla fgwndiqvpg tgetipaldv lprfgivigy
      181 alvsqlvvaa laflvstmtd splgavggav glwivsnilq avealgglre flptfwnnaw
      241 ldalapeldw sgmakgasvs vtyaailvav afrrfrrkdv vs
//
LOCUS       WP_357600381             702 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600381
VERSION     WP_357600381.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 702)
  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..702
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..702
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=77002
     Region          8..700
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(493..494,497..498,500,531,534..535,538..539,
                     541..542,565,568,575,578..579,582)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          493..517
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          529..559
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          564..598
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mstptgwrre gnlpaeltsf vgrtrllatl krhlsesrlv tvtgiggvgk srtvlrlahq
       61 vrshypdgvw fadlgrlqda gmvkqtiasa lgiadqssra eseslaewvg erdmlliidt
      121 cehlvagcae lvhelleaap nlkvlatsrq slnlpyehvm pvpplqvpgd dpgeslftne
      181 svqlfaarag asvpdfvlde nnigpvaelc rrldgiplai elaavrlral sveqilglla
      241 drfsllagas rtalarhqtl raaigwshel cepaerllwa rlsvfagdfe ldaarfvcsd
      301 grlsaehite lianlveksv llirhheagm ryklidtlae ygeewldklg qadqmrqrhl
      361 eyylnlakrg edawsgprqi ywfvrmrqeh hnvrialdya lktpakqpla ltllsslwfm
      421 wvccgfareg rlyleralea nptpsrerck alwvlayvrn sqgdsvggqs aaekcsseav
      481 qvgdsravil askmqgtaam lqgdmqkasa llgvaiefnt dnkelnpgll paivelsivl
      541 taqgefyeae sllqdcllvc kergelwlss haqwalagar latnrpeeal qsvreglrik
      601 lhfhdtlgtl lalesaarif valdrlpqaa sllgalqqnw ksaglpqlga pflsadhnac
      661 vrecarrmge layksafeeg arfdleeasa lalgeldald gn
//
LOCUS       WP_357600439             321 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            parva].
ACCESSION   WP_357600439
VERSION     WP_357600439.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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..321
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..321
                     /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=34548
     Region          64..319
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mdqqlnrpvp tsasepvsrr gvlraatvsa aavgaaglla gpataapgas gaqaqgrrrv
       61 pvdrisiqly tlrdqlaidl pgtldalrri gyrrvehagf vgrtaaqfra alddaglrst
      121 sghvgipqpf daatweqala danvvgckki vhpyfgrdaa gqpirdpavy ralardlnka
      181 grlaeragld fgyhnhqlef vpltggstgf dilssqtdpr lvhfeldlyw twrgahdpvd
      241 viranrgrir qvhvkdldve agfadlgdgv idfgrifahe reagieeyiv erddagtapr
      301 spadaldtar vgfdylaslr y
//
LOCUS       WP_357600408             280 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357600408
VERSION     WP_357600408.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   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 280)
  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..280
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..280
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30544
     Region          13..280
                     /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 mgritvgten stdielyyed qgagqpvvli hgyplnghsw erqtrellaa ghrvitydrr
       61 gfgqsskvgs gydydtfaad lhtlletldl rdvilvgfsm gtgelaryvk nhghervakl
      121 aflaslepfl vaaddnpagv pqsvfdgiaa taqadryawf tqfykdfynl denlgtrisq
      181 evvtanwnta ttsapvaaya vvsawiedfr edvaavraag kpslilhgtk dnilpidstg
      241 rpfhkafpea dyvevegaph gllwthaaev neallafvgk
//
LOCUS       WP_357600449             193 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600449
VERSION     WP_357600449.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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 193)
  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 193)
  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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..193
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21275
     Region          4..182
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mipfdavlsd ldgvlrhfdh aaqadieary glplmktald pklilpptlg qvtedqwfes
       61 ivaalggder arqavtefaq irywvdeevr allakvqqhv pvvivtnamd rleeqldllg
      121 ltyfaddvvs sakvgvakpd rriyeiaaer agaaperclf vddrlpnvea aralgmtgvh
      181 yrtyedlaav lay
//
LOCUS       WP_357600458             419 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357600458
VERSION     WP_357600458.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..419
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44811
     Region          1..>88
                     /region_name="PRK13355"
                     /note="bifunctional HTH-domain containing
                     protein/aminotransferase; Provisional"
                     /db_xref="CDD:237361"
     Region          142..203
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(148,152,177)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(151,176)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(158..159,170,173,177..178)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          231..392
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manfaerldl altkrgftga qvasalteag ipitrayvsq lrtgkqtnpt lqvlralasc
       61 lqvsvgwlvg ddylesgave dlqlraaavg lnasglsess ltvlrgvvel arkaeglsee
      121 sepaasdipd aaaplsgpqr ralgkrlhgl rlaadlsveq vetaigrgta aiaaveqgri
      181 apapisverl ltlygvaapp ireyvlslar gerqaawyda qpvpvwlaat yaleqratvi
      241 rtyqpqfvpp llqteeyara aitaagpatl gqqtvdeala lvlarqeava gdggivvwav
      301 idesvlarsi vgphvqlrqi eqlldhakrp nvslhvvpme dpayvprtgp ftlwrfaeaf
      361 epdiacahgi esdeivadta aveayhqaft klsvttttre etfevlnfhr erlsrslgk
//
LOCUS       WP_357600513             242 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357600513
VERSION     WP_357600513.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 242)
  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 242)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=26586
     Region          1..>223
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnrtdrlyal vedlraiapr crsarelaer fevsvrtier ditalqesgv piyaepgrrg
       61 gyaidkkmtl pplnftpaea vaiavalsra gdqpfgrqar salrkvvaam pgsegelare
      121 larrvqliqh apetgaetqp lgaegisrai eeallrrrvl rldyadakgm ltsrdvepgv
      181 flggrggfwy lvawcrlrdd vrvfrldria aatvtaercp drplegfapd vpemivhgtv
      241 ld
//
LOCUS       WP_357600550             280 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357600550
VERSION     WP_357600550.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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]"
                     /calculated_mol_wt=29834
     Region          39..151
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtsianhqqa eawndwegih waehperyna mleafnaplf aaagitahdr vldvgcgtgq
       61 ttrlaaqqar dgsavgidls apmlerarrd aaaeglrnvt feqgdaqvhp fpdrgfdvvl
      121 srggvmffad hiaafahlrq alaptgrlaf lgpqpggpdr pytrataals pflretspta
      181 rgmgslldpa rvrqvltaag fvdidvapve apmtfgadad davdflfamg ptrynlrdvd
      241 patvarlrad vhdaltefet adgvripgsv wivtaspgha
//
LOCUS       WP_357600580            1024 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600580
VERSION     WP_357600580.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11922920
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..1024
                     /product="non-ribosomal peptide synthetase"
                     /calculated_mol_wt=110306
     Region          32..942
                     /region_name="alpha_am_amid"
                     /note="L-aminoadipate-semialdehyde dehydrogenase;
                     TIGR03443"
                     /db_xref="CDD:274582"
     Region          42..531
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(180,183..188,190..191)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(183..184,304..305,326..331,352,419,431,434,525)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
ORIGIN      
        1 mprhkqnrls ehvlalslgp qhafprhrtv ldlfyeqkeq epdrpairhr dttmsyadld
       61 taanitanql igngvlarql ipvlvadgpe fpvalfgvmk tgsafvpldp dwpidrlgai
      121 maelsppaiv aspatvetia elesglptvi vdcaeepcdp adrksppadr rptpedliyg
      181 fytsgstgtp kcalnrhrgl vnrlttmsrr fgdgadhvtl qnsrstfdss mwqvlwplvs
      241 ggqvvlphrd gildlertam tigrygvtmt dfvpsvleaf vsllevredl reatsslrrm
      301 liggeaaapg avhrlrallp glevtntfgp tecsigsvfh ditdadvdri pigrpidnta
      361 aivldddlep vpvntpgely lggecigagy lndpdrtagv lvanpfpdip geklyrtgdl
      421 arvgedglly yngrldeqvk vggvrvelgd vasalaghpl vgsavalvlg eppestlvcc
      481 vtprspdnpp saaglrayaa eklpaeqvph qivvldalpl nrngkadrka laalivaeta
      541 rqtrpeeqve pptdpmeelv csawrevler dqisvvvpfs eyggtsllay rlttaiserl
      601 gqpvrprdll vastvraqaa rltkgvddds aelayikhdl awrppqtlli tgatgfvgvh
      661 ifaellmhss atliclvrcs dppdgarrlt evldqyglts awqalpmalk tgrvevvpgd
      721 lgsellglpr wrfdaiastv sgvvnaagav nflsgyldhr panvlgvqel iklasggarl
      781 htlstlsifp ppgpgaprit edqipeagqv aadgynrsky vaerlladah rqgvrsvvyr
      841 lgevwphrai gvanpdslah nllyacartg cvfpteaetd vtpvdvvgel varaatgdie
      901 vpdgamhllc parlrfaeaf gvladrcgld lvgyarfrer leaiagpeer larlsmllpp
      961 asagcdaapa efdqlftdgt rhfdtqrfrr haaslaqpta dglrtldryl neltdipafv
     1021 pqer
//
LOCUS       WP_357600563             147 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357600563
VERSION     WP_357600563.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..147
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16248
     Region          18..135
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mptrtaaqnr aqakgdydaf larcpsrqll drisdkwval vlaalgsdgp hltgddcage
       61 srsmrysels rrlagvsqkm ltqtlrsler dglvtrtvtp tvpvtvtyel tdlglslqhm
      121 mrgiklwaea hmdevlanre eydtria
//
LOCUS       WP_357600591             113 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357600591
VERSION     WP_357600591.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 113)
  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 113)
  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 113)
  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 113)
  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..113
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..113
                     /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=11365
     Region          <1..111
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 minaswtlyr glpgaslyaa tkaavhnlth tlaaelrgrg vrvnsvspgy ietamfhani
       61 saeaqaavva avaagrigtp edvadavafl asdeasyvng qdliidgglv aaa
//
LOCUS       WP_357600621             356 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357600621
VERSION     WP_357600621.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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 356)
  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 356)
  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..356
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..356
                     /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=37820
     Region          1..355
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrvgvigaha srgwaravhl pallslpdye itavagtsre sahqaadvwg akhafadpqe
       61 lishpdvdlv tisvqlprrd glveaaisag khvysewpla rsaeaaerlh alaeqagvrh
      121 avglqsrhhp aigylrdlva dgkvgevmsa sltyslsspe vwsvryadlf dhtkgvnhla
      181 vvgghsmdmf gsavgrftei satlatripr itlqetgeqi tvtspdqiaa vgllesgaaa
      241 svhimtggpr gegflievhg ragrlvldsa ddslvgpeft lsfsggtgrt vvlpvpdryv
      301 pmpsdappav rnvrqvyrhl aagipsepdf rtavrthrli daikrsattg erqrlg
//
LOCUS       WP_357600719             114 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357600719
VERSION     WP_357600719.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=12506
     Region          1..101
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msgpvaardv lalfsqtrpl ftalgderrq eiivfllest dprsvgeiaa hlnlsqpaas
       61 hhlkilrdar lvtvrrsgtq rlyalnaedy pqlltpmrdl ltmivscama sppr
//
LOCUS       WP_357600686             274 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600686
VERSION     WP_357600686.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..274
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..274
                     /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=31053
     Region          1..264
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 miefhpvtkh igaevtgvdl rkplsqeeva alragwlehl vlffrdqhid deqhlqfaln
       61 fgtlnhpafk kdsaspihvl dqtspkgegg dewhsdntfe ptppmgsllr cvqlpsvggd
      121 tcwantylay etlspwlqrl cdeltavhdi tmsmkkaiak ghpfdlaeiq akwppverpv
      181 vrvhaetgrk alfvnrastt rlvgltdren eallpllvdh irspeyqvrl rwrpgtlafw
      241 dnrptqhyav adyterrrmh rvtinafpeh adpa
//
LOCUS       WP_357600833             158 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            parva].
ACCESSION   WP_357600833
VERSION     WP_357600833.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..158
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17733
     Region          7..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrpaaldwsv enctiarame ilgerwtlvv lrevftgvrr fddmrvrtgi prqvltnrla
       61 slveqgvlsr epyrepgsrl rheyrltekg ldlwpvlvav lgwgdrylad adgpplsvth
      121 rdcgaevrae lrcadghdvg rsrdvvprpg pgarrrtp
//
LOCUS       WP_357600797             272 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357600797
VERSION     WP_357600797.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 272)
  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..272
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..272
                     /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=29752
     Region          29..272
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mirrlavila lattvlttpa haatavtgva hrgasayape ntlaafelag kqradmfeld
       61 vqetkdhqlv lmhdttltrt tdaervfpdl spwkvgdltl aqireldags wlsdeykdek
      121 vptlgetlse mngsgmglll eikepelypg tearvaaelr rhsswlapgr lvvqsfswas
      181 mrtfhrllpd vpigllgtps taqlpglakf adhinppytt ltssyvrrvh algmkvlawt
      241 vddpdvmrrl laykvdgiit nrpdvlhgll na
//
LOCUS       WP_357600856             253 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357600856
VERSION     WP_357600856.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=27829
     Region          28..153
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtalsnlvrp dvyprsslyd pawlvgldmg pnplwlledl sadlelkpgm rvldlgsgmg
       61 atsvflaref gvevvaadlw iaadtaaavf aeagvadrvq avnaeahalp fepesfdaii
      121 sidsyeyfgt adgylayitr flkpgaqlgi atpgmtreir dlgaipphik alvgweaiaw
      181 htpqwwrfqw eitelvtvts arlqrdgwnd wllwaracle hrpdgreaae qtiamleadq
      241 geflsfalvt ark
//
LOCUS       WP_357600888             251 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357600888
VERSION     WP_357600888.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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 251)
  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 251)
  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..251
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..251
                     /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=26115
     Region          11..244
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 maalspdail ltdrvavvtg aargiglaia eafaalgahv avcdrdrpha elamtldvrd
       61 hvaveifaqa vrerwgrvdv lvnnaggtfh asfadtsprg eqilieenft qvtgmtrqll
      121 pmmrpgasii nvtsseahqa apgfavyaam kaalesltkt lalelaprgi rvnaiapdav
      181 qtegeagvre rmlarplpye pvrvpplghl ggpgdaagaa vflagdlarf vtgttlhvdg
      241 gihaaggwrr s
//
LOCUS       WP_357600889             347 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nonomuraea dietziae].
ACCESSION   WP_357600889
VERSION     WP_357600889.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=35828
     Region          2..239
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mdalavavta nlpvilwgap gtgktssvla lgaslglpve vvvgsireps dfaglpvire
       61 ggtwlapprw aerlaragrg ilfldeltta ppavqaamlr vvlertvgdl alpgevriva
      121 aanppeqaad gwelsaplan rlihldwrvs avsvaegftg gfavpevgaw pvpspaavgr
      181 akalvgaflr vrpelvlavp dgparawpsp rtwelaatav acahgevaae lvrgavgdaa
      241 gfellswlrd ldlpdpetll sdpgaplper ldrvhavlgs vvayvaadgg aetwqrawpl
      301 iarvarrtpd vaagaarsla aarpygaqlp samlelapil raagllr
//
LOCUS       WP_357600925             315 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600925
VERSION     WP_357600925.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 315)
  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 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   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..315
                     /product="GlxA 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=34146
     Region          3..315
                     /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 mthrivvval dhfapldlgv pgqvfgvaet aggeklyevv tcsegrmpvr csagysvlpd
       61 hdldvldtad tvvvpgihag ramrygtvsp alaealqgrp rtmsictgaf vlaaaglldg
      121 rpatthwrda elfarlfpqv kldpdvlfvd dgdvltsagv aagmdlclhv vrrdhgseva
      181 nraarrcvmp pwreggqaqy idrhlpyagg gtaatrdwml ahldrpldla alaeharmsv
      241 rtftrrfrde tgmsparwln gqrvqharhl lettdlgvee varkagfgtv vslrqhlhaa
      301 vgvsplayrh tfrrs
//
LOCUS       WP_357600900             420 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357600900
VERSION     WP_357600900.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 420)
  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 420)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..420
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42738
     Region          15..416
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mtttavrkdg paavtppptv gghvrnylsr vrggdvgalp avlglivlct vfaimrpssf
       61 lsagnfanlf tqgaavtlia mglvfvlllg eidlsagfas gvcaavlanv vtvlgypwwv
      121 avlaaiatgv vigttlgmlv akigipsfvv tlagflafqg vvlllvkegt nisvrdevlv
      181 aianrnlapt lgwaltavav vgyaavqllr hrtrvargli tdpiavvalr igglavilgt
      241 avyvlnlers rnvvisslkg vpivvpviav llvigtfvlq rtsygrhiya vggnreaarr
      301 agievdriri svfmicssma aiggivaasr ansvdpntgg snvllyavga aviggtslfg
      361 gkgrvldavl ggavvavien gmglmgysag vkyvvtgvvl llaasvdals rrraaatgtr
//
LOCUS       WP_357600943             219 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357600943
VERSION     WP_357600943.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 219)
  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..219
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..219
                     /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=22798
     Region          29..189
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdgteisgpq sgsssevlei lrtrppqera daarnrekvl aaaaalfadk gveavsmdai
       61 ataagvgkgt lfrrfgdksg lavalldare rdlqerilsg ppplgpspea grpaatpadr
      121 laafvqayld ylfahldlvr msetaspgar yrigaygfwh rhvaillgea lpgedaevls
      181 havlavlage saaalkdryg eerakaalat talalcpat
//
LOCUS       WP_357600982             374 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357600982
VERSION     WP_357600982.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..374
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..374
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40035
     Region          105..363
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mgslgtaama rmdeqlpwfr alsaedrswv glvaqagiaa fvewfstage drptpsieff
       61 gtaprelkrs islqqtvdiv rvvvevveaq ahelaapgge dqlqqamlry trdvafaaah
      121 vyareaearg swdarleali vdalvrgevd dglhswaaal gwtsspvvvi aghapdddpr
      181 avidglrekg rrigmdllag vqgdrliviv ggagsvndaa kqvvhrfgmg pivigpevad
      241 lhaaassara alaglkascg wpdaprpvhs eellaerald gdddarqqli envylplagt
      301 plldtlatyl eqgtsleata rllfvhpntv ryrlkkitel tgyqptegrs aftlqvglil
      361 grlsesaetw ralt
//
LOCUS       WP_357600988             286 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357600988
VERSION     WP_357600988.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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 286)
  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 286)
  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..286
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..286
                     /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=29784
     Region          1..285
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mepvavglig agpwaemaha pmlakgphtr lagvwarrpe aaarlgapvh erieelfdav
       61 eavafcvppa vqaelavqaa kagkalllek plaadldgar rladavaetg vasqmlltlr
      121 yapqtkdfla rcaqieafgg haanisgalt sggpfatpwr lergalldvg phvidlldaa
      181 lgrvvgvrah ghplrwvgll lehesgavse vslsmaaagd lppqrvevyg rlgsarlphi
      241 dddplsavae efamtvrrgg ghpldaargl hlqeviaeae aqlntp
//
LOCUS       WP_357601005             559 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Micromonospora parva].
ACCESSION   WP_357601005
VERSION     WP_357601005.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..559
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60587
     Region          16..550
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mgyvdvaavg hilpdgrelf advsfrvgeg skvalvgpng agkttllrmv agdlpvrtgv
       61 varagglgvm rqfigmigde ssladlalsl appalrdagr rlgeteaamr aaeahgkfsn
      121 aagkaqlaya dalgawgeag gydaevlfdt vativlgqpw davrdrpvrt lsggqqkrfa
      181 lelllrgpde vllldepdnf ldvpgkrwle arlrestksv lyvshdrell aqsadrvvav
      241 eggsawvhpg gfaswhearv arharldelr rrwdeehqkl relmlmykqk aayndglasr
      301 yqaaqtrlrk feeagpppvp pkdqdirmrl aggrtgkrav vceqleldgl typfdleiwy
      361 gdrvavlgan gtgkshflrl larggtdpdp angpvdgaga lapvthdgva rlgarvrpgh
      421 fsqthdrpel isktlveilw rgdehrtgmd rhaamgvlsr yelaaqgdqr fgtlsggqqa
      481 rflvlllels gatlllldep tdnldlasae aleagltafe gtviavthdr wftrsfdrfv
      541 lfrgdsevve tpepvwdvg
//
LOCUS       WP_357601031             727 aa            linear   BCT 28-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Nonomuraea dietziae].
ACCESSION   WP_357601031
VERSION     WP_357601031.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 727)
  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..727
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..727
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=76733
     Region          14..725
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtqtastrta gpetagrvqq gvgesagrpd atlkvtgefa yssdlwlegm vwgvtlrsph
       61 asawirsidi gpalaiqgvl avlthedvpg ekfyglehkd qpvlaidqvr hqgepvalva
      121 aehpetarra aaaivvdyev reavtdprla tefvrrqpvr vgdtfeaevv vtgeyevgmq
      181 dqaflgpesg lavpaedggv dlyvatqwlh vdrdqlapcl glppekvrls lagvggafga
      241 redlsmqvha cmlalrldrp vkivygrees ffghvhrhpa wmryehgatr egelvyvkae
      301 illdggaycs sspavvgnaa slgvgpyevp nvdivatgvy tnnppcgamr gfgavqacya
      361 yesqmdklaa acglspveir irnavsqgsa latgqiidsp apladmlrel aampmppaat
      421 sdlldlpggv sqtthgegvr rgvgygvgik nicfsegfdd ystarvrael iggephvtvh
      481 taaaevgqgl vtiqaqiart elgiervtva tadtqvgsag sssasrqsyv tggavkaace
      541 avrarfdglp aaqalekfgp ieetreyrhr ptypmdpvtg qadshtqlal cvhravvdvd
      601 velglvkvve laavqdvgkm lnplalegqi hggsaqglgl almeevqvre gkvlnpsftd
      661 yliptildmp pmrisilenp dpaapyglrg agepptlsst paivaavrda tgvaltrvpv
      721 rpehlvg
//
LOCUS       WP_357601034             502 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357601034
VERSION     WP_357601034.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 502)
  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..502
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..502
                     /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=52392
     Region          5..113
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          236..500
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrirdllaas elgltllvgd edteftavhv tdlpdpcryl tggelvlsgl mwrhepadsa
       61 rfvaalrssg vaalgagqaw lghvpddlve acaqaglpll eiptavsfrv vaevaaprls
      121 gdvraalgrq rrivdavaeg adladlfalt aaelgvsgav lsttgelvvg svtdpapeqa
      181 palplrlara flsaprlpcv aeghtlvavg rghraagwal acegdllgra dlgfelaacv
      241 alertrmeeg rrverrlveq lvsaafaaea dpaelsarlr mcglgvaepy svvtataarp
      301 gatrgpdpat lggqvleell grsvvaaaga dgavalvalq gpvsvladrl rsglevlsvl
      361 rdtrvsigvs galtgaaair ggveeaghar rlaearsggv vtsdeiytha lllatvpgdv
      421 rrsfahrlla plfdydaghq selvrtlgtf ldtagswnac aermhvhvnt vryrirriee
      481 ltgrdlstma drvdfflalr sg
//
LOCUS       WP_357601043             130 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357601043
VERSION     WP_357601043.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 130)
  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..130
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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]"
                     /calculated_mol_wt=13469
     Region          <5..130
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrggqsfaea ldshlaewsq rtgiaveiwa lprsdvppti agsvmavvee allnverhsr
       61 agtvsiavtv gasglrltvs ddgggfavph errgiarmra rmaevggtls vnsvqgegtt
      121 vsaavprrpr
//
LOCUS       WP_357601133             399 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora parva].
ACCESSION   WP_357601133
VERSION     WP_357601133.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 399)
  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..399
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..399
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42465
     Region          8..64
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
ORIGIN      
        1 mmsdsatfga rlrtcrerag ktrpvlgglv grsaewvkal engrllpprl pmllrlaevl
       61 dipdlaqltg dqslpvasvt raghsevgkv aavmqrasvp vgavtpvavm rdlvdqawal
      121 whrstterta vaavlpgllt daqrsarmld ggdrrlalve larvyhlvql ylahqplpel
      181 vwlaadrams aatdaddpaa mavaawyyah vyrganqvda aeqvlveaag lvdpaaggeq
      241 larwgqvqlg ialghskagr agrawrawda adsaasrlgd gyvhpwlmfg saacaayavs
      301 ietdlcrtge avrradatdy ralpsqtrra aalidaarah mldrgevaav hllgralres
      361 vdtvrhnpya rtvalelsnr pgtvgedare lalaigmig
//
LOCUS       WP_357601173             407 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357601173
VERSION     WP_357601173.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..407
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43274
     Region          45..390
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mptstpglra rrtgvkamgl alaavatlta spaaaepsav rlrlpaptgg spigvtdlhl
       61 vdrsrpdpwv aarpyrelmv svwypaggsp rlplapqmap laaadfddtl apalfgtkpg
      121 tvdwaattth aradapvdrr agrvpvvlfs agagaprtig atlveelasr gyavvtvdht
      181 yeaaqvefpg grlersafpq rptqedmaka qrvreedmrf vldqlarlgr gdnpdaerrr
      241 lpadlrggld ltrvgalghs mggataaqlt hgdrrvdagv nldggfrgsv attgvakpfl
      301 qiaaenhtra sdpswksfwd rstgwkrelr ftgtahysfs daeavvpqla gelgvpagdi
      361 igtmdprrav taqrayvsaf fdlhlkgrrt tlfdglssrf pevkpip
//
LOCUS       WP_357601176             790 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-glucosidase H [Nonomuraea dietziae].
ACCESSION   WP_357601176
VERSION     WP_357601176.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11444890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..790
                     /product="beta-glucosidase H"
                     /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=84266
     Region          27..432
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          313..663
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          <426..>498
                     /region_name="PA14"
                     /note="PA14 domain; cl08459"
                     /db_xref="CDD:471833"
     Region          713..778
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mdfdelinql dlstkirllt gadmwslpav peigldrlvm sdgpigvrge qwtsadpsia
       61 lpsptalaat wdtglvrqvg rllaqearrk gvhvllapti nlhrsplggr hfecfsedpy
      121 ltgelgaayv egvqeggvat tpkhfvandf etdrftvdvk vsdkvlreay lapfervvra
      181 gawglmtayn svngttmteh selvngvlkq ewgfdgyvvs dwtavrstea aalggtdvam
      241 pgpfgpwgdk leeavregrv pesvvddkvr rilrlahrvg alrppsgapa eraehaaidg
      301 valarevaar sftllkndgd llplegvtsl aligsaadea rimgggsaqv fpdrtvsple
      361 glrargevry algtdprvrl splavpttaq fldaegqvla ehplattear wvgqlppdvd
      421 gerlsavrlr aaytpdltga helsvagvgp ftvrvdgetv fdatielegd dpataflspp
      481 errvavelte gtayelevth pagafggmaf vaytlghanp spgddiliaq aveaarscev
      541 avvvaattle vesegfdren lrlpgrqnel iaavaaanpr tivvvnagsp vempwiadva
      601 avlltwfpgq eagaaladvl ygdaepggrl pttwpvrlad spvvdvtpve grvsyeegvf
      661 igyrgwekle rtpafwfghg lgytswsyds iaaegstvtv avtntgpreg revvqvylsa
      721 ptpdgrparw lagfdvveaa pgetvlttvf lperafqvwt degwttvpge ytveagrsva
      781 drrlgattki
//
LOCUS       WP_357601202             268 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357601202
VERSION     WP_357601202.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,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 11438138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..268
                     /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=28902
     Region          1..253
                     /region_name="ModF"
                     /note="ABC-type molybdenum transport system, ATPase
                     component ModF/photorepair protein PhrA [Inorganic ion
                     transport and metabolism]; COG1119"
                     /db_xref="CDD:440736"
ORIGIN      
        1 mhavelegvs vkvvgralla gidwrvaygq hwvilgpnga gkttllslaa avrhptegaa
       61 tvlgrrlgrv dlrelrgdig lvaasqrlvd eslleeegat ahtvvltght gtsaplwdry
      121 gqaehdraha lladmgckdl adrlfrvcsq gerarirvar almaepaill ldepfagldl
      181 paredlitai edlaereglt tvtvthhlee vpattthall mrdtrilaag pveetltapa
      241 lsecfgrelr vdrlegrwsa ravrtprp
//
LOCUS       WP_357601225             264 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Micromonospora parva].
ACCESSION   WP_357601225
VERSION     WP_357601225.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=26799
     Region          33..248
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mvrwrtltgl latalaavta asltltapaa aadspvtptv vggtraaqge fpfmvrlsmg
       61 cggalysarl vltaahcvgs tgtntsitat lgtvdlqsss ritvrsnyvy rapgyngagr
      121 dwalirlasp vtglstlpia tttaydsgtf tvagwgaare ggsqqryllk atvpfvsdsv
      181 cnanyggdli paqeicagya sggtdtcqgd sggpmfrrda nnawiqvgiv swgngcarpn
      241 ypgvytqvsy fassiasaaa slgg
//
LOCUS       WP_357601231            1077 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357601231
VERSION     WP_357601231.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1077)
  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 1077)
  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 1077)
  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 1077)
  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 1077)
  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 1077)
  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 1077)
  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 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..1077
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=114390
     Region          650..1053
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 misddqrtal eavslnpavt pddvwrpsph nvpelhekva aeilrgvara rtddtsmplg
       61 vamqgragag kthllgavre qiqrdggyff lvdmvsgktf wesvalalve gmgrphvgwg
      121 tqlktflrrl ttqlglpvev rdavagarpv traqldtfiw alrerdrevg rdaqdtaral
      181 vlhgavdfea qdvgyahlis eqgdpaaraa wglsasirtp qqvvqdisrl malaldptvi
      241 avdqldtlfa qtstsllnqh qgledaqakv lgpiadgllk lrditrrtlv vvsclpdtwe
      301 lmtraaptpv adrfrtatlp driptpeigq aivakrlsaa fagmffgpph ptwpiapaaf
      361 adaptltpra llrrvdrhia wcrdrdevve ldrlidgtes tptvsavrga pgvpptderl
      421 heldarfael veaadvsaav dpagedehmp qllaaglaaw iaeqaptgat ykydpppgrk
      481 palhgrliev ldeateneah wcfraiahpn aiavtarvka actlagldrd lpqrrlvllr
      541 ngpwptgkrt tevltgfdaa gglrcgvpea dlrvfaalrv maaepstalq ewlvarrpas
      601 gtelfrtvlp gpdgtrgaap sttpddgepp sdgpepdpts vsaadtaggp stgsvpddpa
      661 dlavdagdpa vglgravdgg hpftvplesl rrhavvfags gsgktvlirr lveecaragv
      721 saivldpnnd larlgdawpd ppdgwgpgda eraadylaht evvvwtprvt agrplsfqpl
      781 pdftslrdwp defdqavrsa vealapragv drssrlaqqg kavltealqa yarsgmvglp
      841 gftefltdlp dgvsrlarag klaeelaeal kaamvtdplf ggvgapadpg llltpsagrr
      901 arvsvisfvg ltsdqerqsf vnqlqmalfa wikrhpagdr plgglfvmde aqtlapstat
      961 tactastial asqarkyglg lvfatqapkg lhnqisgnat tqffgllnap aqidaarqla
     1021 eakggrlpdi gllnsgefya agegfsfvkv rtplclthhp kapltpeevv ararpag
//
LOCUS       WP_357601281             149 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357601281
VERSION     WP_357601281.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 149)
  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 149)
  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..149
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..149
                     /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=16056
     Region          14..149
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtlsdptsta atdsealava ernlcglvna larqieghvr eragalnltt aqavalrelt
       61 gpltmrdlad rmgcepsnat fvvdrleeqg iverrphpnd rrakqlvlta egvalrerll
      121 alltedspla kitlqeqaal ndlllralq
//
LOCUS       WP_357601301             234 aa            linear   BCT 28-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Micromonospora parva].
ACCESSION   WP_357601301
VERSION     WP_357601301.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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 234)
  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..234
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..234
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=24591
     Region          1..234
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mrirpvgaha llldcttptd ipeaalveaw rselwrrrer gdliaveivp aartvlldgl
       61 pdptttaeql trwvsvvtaa itgpkqpdak ahaltqdhna tgddidvgaa dvvvpvsfdg
      121 pdlpavadhw gvdvsavrhr itstrfrvaf cgfapgfpyl tglpaelalp rlatprprvp
      181 agsvalagpy agiypgaspg gwqlvgrtdl vlfdvaadpp arlnpgttvr mvaa
//
LOCUS       WP_357601376             399 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea dietziae].
ACCESSION   WP_357601376
VERSION     WP_357601376.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..399
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42654
     Region          3..397
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 msvegllrel tpqvlgalvr rygdfdsced avqeallaaa vqwkqeglpr dpkgwlitva
       61 srrrielwrn eaarrrrees aaameppaga vpaaddtlil lqmcchpalt pdsqvaltlr
      121 avgglttaei araflvpeat vaqrisrakq rirasgssfs lppsgrlpav levlylifne
      181 gytassgpsl nrvelsgeai rltrqlharl psegemagll almlltdarr parvrddgtl
      241 vplaeqergl wdsaaiaegd alltrtlata pigpyqvqaa iaavhdgaat aeetdwrqil
      301 glydllrala pgpmvtlnri valamvsgps agleelarae sepalaghhr vhavrahlle
      361 lagdregaaa gyelaakatl sdperrylss ravavrars
//
LOCUS       WP_357601386             491 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            parva].
ACCESSION   WP_357601386
VERSION     WP_357601386.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 491)
  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 491)
  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 491)
  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 491)
  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 491)
  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..491
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..491
                     /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=50619
     Region          5..240
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
     Region          <211..>326
                     /region_name="PRK06975"
                     /note="bifunctional uroporphyrinogen-III
                     synthetase/uroporphyrin-III C-methyltransferase; Reviewed"
                     /db_xref="CDD:235899"
ORIGIN      
        1 mtltlryaah sdrglirdgn qdsvyagprl lavadgmggm aagdvasniv igamaplded
       61 vpgdalvdal rsavgtanqq lrdtvdanpq legmgttlta tlftgsklgm vhigdsrayl
      121 lrngefaqit kddtyvqmlv degrisaeea sshpqrsllt raldgrdidp eysvrqvmpg
      181 drylicsdgl sgvvsaetig etmreyadpq qcverlvqla lrgggpdnit viiadatdqd
      241 iveatpivgg aaardrgmat sadnstpaar asalsaprpa apeepaagdd epdrpkrrpv
      301 rtaamalavl vivggaafgg wtytqrqyyv gateegqvav frgvqgqiag mdlssvhrrs
      361 gtrlddltva aqdtvkvgir aksepdaerq laeltsdtps npnlkplcpl dptaaavntp
      421 tptptplglt ptpngspsvn asstpngvvs atptagatta lggagatttp dvtpsdsatp
      481 aldpascrsp e
//
LOCUS       WP_357601424             172 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357601424
VERSION     WP_357601424.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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..172
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..172
                     /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=18580
     Region          1..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtnvfddpri tavgllfeah aglsarftaq leehglsave fevitrlars pgnqlrmtdl
       61 aaqtslstsg vtrvvdrmer dglltrracp ndrrssyavv taagmqrlne tlpghlqiie
      121 qwftgqldpe alaalldglr rvrdaahpca tagsddvdpe qsadadspar rq
//
LOCUS       WP_357601447             280 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357601447
VERSION     WP_357601447.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 280)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..280
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29147
     Region          1..269
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mrigfiglgi mglpmaehlv raghevvghd vvdrpfrtaa svaeavreae vvitmlpadp
       61 qveavfpeit anapqdalyi dfstitpqts rrlaeqwkrt ldapvsggek gavdgvlslm
      121 vggseadfea arpifeavgk tfrlvggpgs gqfvkaanql vvggtyalva eaivlmeaag
      181 vdaaagldvl agglaasril dlkresmlar sfqpgfridl hhkdmgiild aartaevalp
      241 msaltaqlva aaraqghgsl dhsalllvve glsadervsr
//
LOCUS       WP_357601461             635 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357601461
VERSION     WP_357601461.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 635)
  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..635
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..635
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=66831
     Region          65..248
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          369..629
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mdgalvsrry lellareasa vefegpiiaa raagadpami eeleqakvea lkvrellkrr
       61 arreaelsal ydtagdlaal rdldavleai vhrarqllat dvaymtlhdp eqgdtymrvt
      121 dgsisakfra lrlamgaglg glvaqtatpy stadyfadsr frhkehidea vteeglvail
      181 gvplrlgqrv igvlmaanrs arpfhqeevs llaslaahaa vaidnarllq etrnaleels
      241 qahrvarehg eavergalah drmtslvlrg ggiedvaavv tdvlggslav lddlgrpltg
      301 dvgeldagvf eaaqasralg rtvrrgdlli asvdvggepl ctlilrsdda derileraal
      361 vcallllfrr svaeaegrvr gellddlisr pdspgladra rrlgvdlhap hvvvvakhgg
      421 qreraafwas sqaalrhgla agrgdevvll lpgenagrva qnvatelsas lhspatagas
      481 katldgdaag daagdaagdv agdvagayqe arrcaealia lgragdgasa aelgfvgllv
      541 gdgrdvlgfv srvigavidy darrgtaltd tmaayfgsgg spsrtaeamh ihvntvtqrl
      601 drigkllgdg wleperalei qlalrlhrlg htstp
//
LOCUS       WP_357601593             285 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357601593
VERSION     WP_357601593.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 285)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..285
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29923
     Region          1..280
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mshvtvvglg pmgskmaetl laaghevavw nrtasktapl vakgarqaas aadgellvvs
       61 qisyqamyds lgdarldgkv vvnlssdtpe alrgaarwve erggtlitag imvpppgigq
      121 pgaytfysgp kevldrhagt lealsevtyv gpdqglammy yqaqllifws sltsymhama
      181 mlrtagtspm eflpfardlf tqlgsegpmg yakilaeefe agvypgelns lhmqavglgh
      241 avealaeagv ettvpgalka lferadaegr gheglgtvie sirkp
//
LOCUS       WP_357601607             359 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357601607
VERSION     WP_357601607.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 359)
  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 359)
  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..359
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..359
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=39801
     Region          5..354
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mrdlaatmtg fartlraagv gadhertqnl lkalghldva rredvywagr ltlcatpddl
       61 prydrcfaay fggrravrgl traatvtrhl aggegegerg qeavlatasp levlrqrdva
      121 alseaeraev hrmlallrar rerrlsrrla psrrgrldqr rtvrealrkg dvarlrhrdr
      181 ttrprkvvll vdvsgsmapy aetvlrfaha martepratr vysigtrltp isvelrhrdp
      241 gtalaevska ipdwsggtrl geelrellnr tsvrgaivvv asdgwergdp allgeqmarl
      301 arqarrviwv nphkghedyq pltggmraal pfiddlvagh slaafeelse rlsdarhpa
//
LOCUS       WP_357601721             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora parva].
ACCESSION   WP_357601721
VERSION     WP_357601721.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32485
     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          99..287
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpedigstvp rrqlgrllrq frneagvtld aaaealeysr qkiwrlecgq gsvrvldvka
       61 mcelygvspe mteamrglaa etkskgwwha ygdavpnwfe lyvglesaaa hlrrydesli
      121 pgilqtkeya ralyrlggil neeereravq vrlqrqallf rrlpaaprle svlseavlrr
      181 gvggspvmte qfahltklse lpnvsvrvlp laagpqpgav agsfvildfp atkggrtape
      241 psvvyseslt galyldkpde laayervwrg ldalalgeae stdmikriag emrhd
//
LOCUS       WP_357601740             580 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Nonomuraea dietziae].
ACCESSION   WP_357601740
VERSION     WP_357601740.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=63757
     Region          10..326
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mrnftmdgda frldgeefrv lsgalhyfrv lpeqwshrlr mlramglntv etyvpwdlhe
       61 prkgefqrle elaafldaaa aegllaivrp gpyicaewdn gglpswltae lglrvrtrda
      121 eylshverff devvpliaer qvtkggnvim vqveneygsy gsdalylrhl tddliahgie
      181 vplatsdgad dffltggavp gvlatvnfgs gpeaafaklr ehrpdgplmc mefwcgwfdh
      241 wghghvtrda adaadtleri laagasvnly mahggtnfgt saganrvgel adgeyrattt
      301 sydydapide rgaptekfwl frevlsryns dipdlpplpe tlpatrvplt gsvglrdald
      361 qlagpsvtaa lppsfedlgl thglvlyqve vpgprrpyrl rvrgvhdrah lyvdgeqaav
      421 lerggeepvl evagparlev lvesmgrtny gptlgerkgl mapimhdrqy lhgvtarpvp
      481 lrelpalpyg eglsaavpal frgeleverp adgflalpgw gkgyvwvngf llgrywdrgp
      541 qrtlyvpwpl lraganeivi leldrvgepa leirpaaelg
//
LOCUS       WP_357601757             231 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357601757
VERSION     WP_357601757.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  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 231)
  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 231)
  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 231)
  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..231
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..231
                     /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=24957
     Region          4..210
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mrtvvfgatg ptgrqiteqa laaghevvav trrppagppr pgltvvnadv adpdavdrav
       61 aggdavlssl gvpltpkpit vystgnanil aamhrhgvkr litvsssvld ptwrptgeff
      121 fntvldplfn rragrtahed mrrmetlvre sdldwtiarp sglfdhptvt ryqvaenvad
      181 glftaradla asmlaqltde ryvrramavv ttevrpsiag liwreavrkk k
//
LOCUS       WP_357601768             696 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea dietziae].
ACCESSION   WP_357601768
VERSION     WP_357601768.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 696)
  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 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 11443930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..696
                     /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=70409
     Region          202..>656
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrrliyglta aalvtplvvg asvvtapsav paaeimvfya dggqraaiaa ieagggravs
       61 aepklgyvla kgtgpafvda lgrseavvgi stdraigfas aalgargrip fagpvggaat
      121 gslglegrta sagsaeleer sasrgrtekg argassspla nadarqapag dpglpvaagq
      181 vpapagdpgl saaggpgsaa gdlglstvgg pgsaagdpgl saakgpgsaa vdrrgdsagq
      241 vgqarqlvqs gggaqlagvv adgqlpdgsa vrgsaaepla arqwdmrmig adranriapg
      301 tkkvlvgiid tgvdgkhpdi apnfnrelsr nfvtdrpndp kgqpfdgpce ykgckdpvdv
      361 dddghgthva stigspvngk giagvapnvq lvnlraghds gffflkpsld altyaadngi
      421 dvvnmsfyid pwafncmsnp adskreqleq rgiitgmqra ldyarskgvt lisalgngsi
      481 dlgnprtdtq spnypkessr trkidnscln vpaeskgvis vsalgpsgrk avysdygleq
      541 tdlaapggda ldgtsasplr silaaapkga mlrdgkidqn gmpktasvvr dchgsecayy
      601 qyldgtsmaa phatgvaail isrfgrpgeg gvamdpaeae rllyasatpk acptprayvy
      661 dyfgqketht cegdedkngf ygrgvvdayr aatlsp
//
LOCUS       WP_357601895             708 aa            linear   BCT 28-DEC-2024
DEFINITION  MMPL family transporter [Micromonospora parva].
ACCESSION   WP_357601895
VERSION     WP_357601895.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 708)
  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 708)
  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..708
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..708
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=72547
     Region          50..691
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 msvftrvarg rlaawltvaa aivvgaavfg lpqpdnpapv sasglsaqwq stqverlqdq
       61 lpssevqpai avvsrddgga lteadraavt arsgdlgrla vggqvsppqv spdgtvalva
      121 vplsiaggqd evveqvdqvr aaladlpdgl tvdvtgspaf tadlssvfdg aditllavta
      181 avvavlllit yrspflwivp lvvvaateql tlravdvivp gvginlqqgq vtgiasvlvf
      241 gaatdyalll iaryreelrr eedrftamra alrrtaepil asggtvvlgv ltlllseqet
      301 nralavacat gvvfamlsal fvlpavlvlf grglfwpfvp rvggparegr lwgrlgaave
      361 rrpvvvatla tvllgalalg glgirtglse teqfraepea vtgaqtlara fpagstqpva
      421 vittpaavra vtdaasavpg vasarpgdag davaqvdvvl daepgttasd raiealreav
      481 aavpgsappa tvggdtpsga ivggsvaaty dsdeandrdl rlilpiilll vggvlvlllr
      541 gllaplllvl tviasffasl gaawllfdhv lgfpaldsgv lllafvflva lgvdyniflv
      601 traredarsa gtragmlsal rvtggvitsa gvllaavfav lgvlplitlt qigiivcigv
      661 lldtllvrtv lvpalafllg drfwwpgrit kdeaqgtvps pepvaahd
//
LOCUS       WP_357601957             217 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357601957
VERSION     WP_357601957.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=24138
     Region          13..191
                     /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 mrgvdrlrgw patlndgpvg lrplrlsdvr vwretrlrna dwlrpwepsn petplfrtgl
       61 gpyvsmvgtl rrearqglam pwvityggrf agqltvgaiv wgsarsaqvg ywidgalagk
      121 gitptalama vdhcffttgl hrleanirpe nqasrrvvek lgfreegirr rqlhidgawr
      181 dhicyaltve dvpggllvqw rraresaahg gspveev
//
LOCUS       WP_357602004             300 aa            linear   BCT 28-DEC-2024
DEFINITION  M23 family metallopeptidase [Nonomuraea dietziae].
ACCESSION   WP_357602004
VERSION     WP_357602004.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 300)
  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..300
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..300
                     /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=31638
     Region          22..229
                     /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 mrsgrlsavv vgavllaggc gqatgvagvs mrapamaadp sgdpsaapsg tptgaastpg
       61 tehqsgvqrp aaadpvkvpp pkvskydyaf pvkgcktnyq rklliipktt iwaargcsfv
      121 apvdgvidev ninnrwkpst dvgsdregrf vsiigedgvr ylgghldsvt eglapgakvk
      181 agqelgkvgn tgnardtapn lyfaiswktg paywwvrrgm vepwdyldaw lkgnptlspk
      241 eetfklrrkl getpacttlc ssrsassppq eeekekerkk kpstptqtpt ppplndtgtl
//
LOCUS       WP_357602018             447 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nonomuraea
            dietziae].
ACCESSION   WP_357602018
VERSION     WP_357602018.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..447
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=47555
     Region          15..430
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 msrteqdpes setedeadtd avfmalleds aeelyesapc gylstlmdgt iakindtllr
       61 wlgmereavv grrrftdllt vggklyheth fapllrmkge lsgialemkt adggrlpvlv
      121 sstvkhsgeg epllirttvf dasdrrtyee ellhrkreae qaraeaeqar aeaeearrqa
      181 eadrarlsda lavlqqsllp aslpaapgle tavyyhtasp drlggdfydl fpidgarwgf
      241 flgdvcgkgp eaaaltslvr htlraaalhd pepatalatl navlheryaa sgdvryctai
      301 fgivdtgsrp ghatvrlasg ghpsalilra gghaeflptp ggllvgilps apattaetvl
      361 epsdtlllyt dglteartgp thnslygeda lhafatahap ctpqeaigal selldsfgdg
      421 ldddtallal gvpaapphps patkhdr
//
LOCUS       WP_357602026             505 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357602026
VERSION     WP_357602026.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 505)
  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..505
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..505
                     /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=54836
     Region          15..494
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mhlnerslig qevagyyied vigkggmavv ylaldprlsr rvalkilnpi lsvddrfrqr
       61 filesrtass iehpniipiy eansddhgvl yiamryvdgl dlrrliydrg pmpvgqvnsi
      121 aaqvaaalda ahahdlihrd vkpanillag ddasqhvylt dfgitkhrts isgltqtdqf
      181 igtprymspe qinkehidgr adqyalacvv yealagrmpf erdndvallw ahlaespapl
      241 shlrpelple vdgvmmkala kspeqrypsc tafvgalrda isgevaptrp qqpmprpsra
      301 pkpattgrrr lpavligvta avaaitlavl lvlanrgegm ltyrptpavp mtftypegwt
      361 atthvdlfal aspsaaqfes lfvaaanadw sevnaldptd atglyvqlad tfdpkadlqs
      421 mqetlntmlp gkvtftnepa adliagrtat rfegylrsat gtgqlrvtgy lvetptrpal
      481 vlyfcaesac dpallakire svalt
//
LOCUS       WP_357602073             361 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora parva].
ACCESSION   WP_357602073
VERSION     WP_357602073.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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..361
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..361
                     /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=38820
     Region          8..265
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 masvaqtrfg ivgsgwrgef flrlarllpe rfrvtgvvtr tesrgavvta dwgvrtfrtt
       61 aellaherpd fvivsvpwsv tpeatrelva agvpvlaetp paadlaglrs lwadvggsgl
      121 vqvaeqyllm pghaarlalv ragmlgepts vqissthlyh avslirgllg vghetaevna
      181 rafvaplanp lsptgwsgdd tpqqlsttla tidfggrmgl ydftdnqwwn plrtrrlvvr
      241 gsrgelvddr vvrlvdpttp vesslvrrqt gldlnlegld lkhisfdgev vyrnpfvgsg
      301 msdddiavad ivaragawar eegpapysla eacqdhlisl aieesartgq pvatdaeawa
      361 r
//
LOCUS       WP_357602198             369 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357602198
VERSION     WP_357602198.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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..369
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..369
                     /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=40813
     Region          107..363
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mfsrarriai plagllaagl isgtaasats psdvvsqnaa tpaeqaiqfw tpdrvklatd
       61 yddglsltsk gvkgtndapd gppgsvppig eektkatksk hvnlpntvgr vfftlpkadp
      121 rdprswrycs assvqgkyrn lvatsahcvy dtskntfydn wifipsywdg nnawegkapy
      181 giyaaktfna hddfvvkedy dfdyafvnvy ngikvnwekv ngrwqwtvkn vgrlgdnvgg
      241 qgftwnrspk lnvfsfgypa gehpdgdkpy tgrtmkfcyg ktkpmpeark ynlqehigfk
      301 csftagasgg pflynyksas rtgylvgvns vawdtdgndr ydyisspyfn tdtykvykaa
      361 anrwtgnfr
//
LOCUS       WP_357602087             110 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357602087
VERSION     WP_357602087.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 110)
  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 110)
  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 110)
  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 110)
  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 110)
  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 110)
  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 110)
  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..110
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..110
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11944
     Region          7..110
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mdvttarerl edmlaeldrs igvlqgdpva vrehsaadag sdltdadraq amlavattqr
       61 ravieaikrl eegvygrcvd caqpvpegrl earpeaarcv qcqgkqerrr
//
LOCUS       WP_357602199             427 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357602199
VERSION     WP_357602199.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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 427)
  AUTHORS   ter Beek,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..427
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..427
                     /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=45795
     Region          3..427
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 margvfmaga lalsllvtgc vagtssegaa vaddqpfege vefwtinlkk nysdfitgli
       61 ddyrkqhpkv tvnwvdvpgq esatkllaav asgdvpdavn issldlgrfa pslspledyf
      121 kpadladfqp nlveplridg klyavpwyng gapvamyrks vlekagadlg kpptsydeal
      181 aladsvhdkt evygmnsipd hnalryygik llsddkksaa fntpeavail ekfkksydak
      241 giapgavskd irnlpqtlen gqiafkatan aaellniqkn apevyedlvv tppvrmstgg
      301 flllaqqafs ipkaskhkka aaefikfftn ganqlafcki vpiypstvss tkdpffsgsd
      361 gddpmsvars vivkglpele ytpigtakds elgellseev rayltgtksa kealdtaekr
      421 wndalas
//
LOCUS       WP_357602374             126 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357602374
VERSION     WP_357602374.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14056
     Region          18..114
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msqyehtcmi rgdggrtirt ildricdkwt llvvatldqq rlrftdlhrq ipgisqrmlt
       61 ltlrnlerdg lvsrtayaev pprveyalta tgrslippal alagwaidhi adieasraay
      121 enrtap
//
LOCUS       WP_357602234             221 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357602234
VERSION     WP_357602234.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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 221)
  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..221
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..221
                     /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=24768
     Region          2..>64
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          38..208
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mvpsvpvsvd lvvltvrcqa lsalvwrrdn ppflrrwsls ggfiqldedl pdaarrilae
       61 raglpgapvh leqlqtygyp drdprqrvls vaylglapdl pasekahmaw vpvaeltvma
      121 fdhrrimmdg verarakley tplgaafcpp eftvadlrrv yeivwgrald prnfhrkvtk
      181 aegflvetgr tttrdggrpa klyrrgpael lhppmlrslk e
//
LOCUS       WP_357602208             132 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            parva].
ACCESSION   WP_357602208
VERSION     WP_357602208.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..132
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14740
     Region          15..121
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mattsaarrr eqakrdydaf legcptrell srltdkwval vipalaagpl rhgelarria
       61 gvsqkmltqt lrtlerdglv trtvtvsvpv rvdyaltplg helfpvmvai kdwaethmdr
      121 vfeartqfda rp
//
LOCUS       WP_357602228             313 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357602228
VERSION     WP_357602228.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=31914
     Region          32..309
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mtharlavpf alvalvaagl clgtplvspl rglseleqvv lwelrvprtl vallggaaig
       61 vaglllqesl rnplavpemi gvstgaslav gvcvvwalpv pftlypvvgl agaalggvvt
      121 lavartgrsa gavlligaav staiqallla vmstadrlqy dmlfrylvgs ltgvmweqag
      181 rilpwfaaav plvllcvpal gllrlgdeaa aalgaranla rlgvlavaal ligsvtgpcg
      241 plawvgfvap llarrlrprs dargwllwaa algavvtlaa dlaarlafap vetplgawta
      301 vagvllvawr wra
//
LOCUS       WP_357602375             379 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357602375
VERSION     WP_357602375.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 379)
  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 379)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 379)
  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..379
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..379
                     /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=40189
     Region          122..378
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrrdilaava afavgavmlv grayfdrdgv ppwflavpla lacagvavrr saplvclalg
       61 vaavtidgay sgpslpttlv ftdnlysaal ygparasrwl lgvtttaavi igavigmler
      121 swlalaiygv qvslvlvvpv ttamvlrqqr dqaaaerara eqvahlaeld rgaaivaert
      181 rmarelhdmi anhfsaiaiq stavlsrkdl dagavqqima sirensvqgm aemrtmigll
      241 rqegedndat trprladaad lvkrarqagm etvmtvegtp ydlpvsvdla gyrivqealt
      301 namkhgddra evvityvpgl vsvvvdnpln etrtqlpgag aglvgmrera alvggafeag
      361 pyeekgwrvr atlptehal
//
LOCUS       WP_357602395             159 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357602395
VERSION     WP_357602395.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=16941
     Region          11..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mstekdgpav deavrtllll mprlvgrakr lpvpqalqgl dlaprhlall ahleydgpas
       61 vnelaarlev apttvslmvs elsrlgvlqr tadpadrrrr iiaiapaylg pigewlsgsa
      121 sawervmrdl npaeratvig alrayeaale svaspeppa
//
LOCUS       WP_357602411             362 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357602411
VERSION     WP_357602411.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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..362
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..362
                     /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=39323
     Region          1..350
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mttvrvrltl iysglfllts villvtvnll lsqaldrria glpvapvapl pgmandrppr
       61 lpelvdevis yqwgvtaltv gilalvsvvv gwlvagrilr pihritataq rlslstlher
      121 ialvgpkdel keladtfdam ldrlersveg qrrfianash elrtplavqr aaieiglped
      181 vgeirdklll hnrrteslid allvlaqaeh glenrvpval dqvvrlvlae agsddvtltt
      241 riepfavegd pvllnrlvtn lvdnavrynh pggtvemtls hgvltvantg pevprerfgd
      301 lfepfrrlht treqgaglgl sivasiakah eaevrakphp ggglevvvdf aahrpsyadi
      361 qv
//
LOCUS       WP_357602449             238 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea dietziae].
ACCESSION   WP_357602449
VERSION     WP_357602449.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..238
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25278
     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 mtdtavivpa kdeaerigat vtaalqlpgv dlvvvvddgs tdqtgrvara agarvvrhsr
       61 nrgkasames gaeavrllda avprhllfld adlgetaraa aglvepvrag eadmtiavfa
      121 trvklgghgv vvrlsrdgir rasgfsatqp lngqrcltre afeaarplah gfgvetglti
      181 dlvrkgfrvv evevemahra tgtdwhaqlh rarqlrdvar alatrepvir dnlaklrp
//
LOCUS       WP_357602483             257 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357602483
VERSION     WP_357602483.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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..257
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..257
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26993
     Region          5..249
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mgefvsveva dqiatirldr pkmnalnsqv qreiaeaare vdadpqaqav ivyggekvfa
       61 agadikemad msyadmaths rtlqacftav aqigkpviaa itgyalgggc elalcadfrv
      121 agesaklgqp eillgiipga ggtqrlprli gparakdlif tgrhvpapea lamglvdrvv
      181 pdeqvytaal ewaatfvggp tvalraakqa vdrglevdld tgleverlqf aglfatddak
      241 igmrafaeka kpkftgr
//
LOCUS       WP_357602481             269 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357602481
VERSION     WP_357602481.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 269)
  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 269)
  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 269)
  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 269)
  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..269
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..269
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28033
     Region          7..267
                     /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 mpslsaaprl vatdldgtal radgsvssrt aaafadvera gamlvfvtgr pprwmsvvad
       61 avrhrglaic angalvydlh teriveshli epdvlgevva qlranvpela fsveyeggfa
      121 hesdfrlggm dskavaglrv gastltsrpc akllalhpem dpdslheavq dlvghlvtat
      181 hssgraliem saqgvtkasa laalsskngi kpdeviafgd mpndlpmlaw agtsyavana
      241 hpnvlaavdh vtaandddgv alvlenlyr
//
LOCUS       WP_357602427             590 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Nonomuraea dietziae].
ACCESSION   WP_357602427
VERSION     WP_357602427.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 590)
  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 590)
  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 590)
  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 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..590
                     /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=62466
     Region          19..415
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(26..27,30..31,34,65,115..116,118..120,123,143,
                     146..147,150,277,280..281,284..286,289,317,321,374..375,
                     379,383,399,402..403,406..407,410)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
     Region          <188..292
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mvqsrqyshr eileimsglm lamltsmist svvgtalpti vgelggqeqy swvasatmlt
       61 mtvstplwgk lsdlygrkll fqvslglfva aslaaglsqd mgqliaarav qglgvgglsa
      121 lsqvilgdiv pprergrysg ymgavfgist vagpllggfi vdadwlgwrw cfyvcipfav
      181 vafaviqrvl klpkvkrnts idiwgattit agasalmlll tlgghefawn sfwsyflgav
      241 avvslllsvf aersarnpil pprlfrnktf vltslaslfv gvamfgamiy lpqylqivkg
      301 msptasglmt lpmvfalfls gvisgkivtn tgkwkifpvl glllvavglf llsrlhvdse
      361 kwligldvav lgvglglsmq mlilaaqngs elrdmastts gvsffrslgg avgvaafgai
      421 lsnrlkdema elmraahisp aggggsvtlg sptaiqqlpe pirgivlesf trgletvfmv
      481 gvpiallgfv avlflkelpl rgnveppkqp skddlvlagl lleliaqrve rangepsalv
      541 savarmappd dlperdrara vaasvlrpts rallaqatpa vnrvtegvtp
//
LOCUS       WP_357602515             448 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nonomuraea dietziae].
ACCESSION   WP_357602515
VERSION     WP_357602515.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..448
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..448
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47333
     Region          23..448
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mthvvdpkha evpltldeap pktlgildqg afwanlgvsl lgfsfalfli npllddnpls
       61 mtaavtatvv gslvgtamvg laaipgaqtg qpamvllrgl fgaklsyvpt vlniiqmlgw
      121 gafelwvism gaqaifgdav pyavwvllag aittgltiyp lgairlirrv vtigviisti
      181 wfavvflrsa papaggswda fapavdfvia lsvswvpvaa dyarhsrssr aaftgvvggy
      241 tvaqvaclai gvyavaiagh davlndpttv fgpfvaaplg alffgilvlr etdqsfanvy
      301 stamslqnlm prvdrrifsi aigvltigva llvdvnsysa flsiigavfv pmlgvlvvdy
      361 fllgrastwd tsehapsrwp mvapwalgfv twwllaapst iswwaaiwdg arttlgftrq
      421 pwmsaavgaf lvaglvtlai gyvrrsrr
//
LOCUS       WP_357602603             199 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357602603
VERSION     WP_357602603.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 199)
  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..199
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..199
                     /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=21343
     Region          10..196
                     /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 mgyaisdqgd aaplavkili aggfgvgktt lvgavsevap lrteeyltha svgvddlegv
       61 sgkstttval dfgritisse lvlylfgtpg qerfwfmwnd lvngamgavv lvdtrrldvs
      121 fasidffesr gipfvvgvnc fhgvrdrtqe eirraldldp qvplvlcdar drtagrdvll
      181 alidhlmavr srtaphpva
//
LOCUS       WP_357602625             394 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357602625
VERSION     WP_357602625.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..394
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..394
                     /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=41823
     Region          42..374
                     /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(51,53,214,234,304)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mrldgiplwd gteyrgpvdl swepdriisv qpdaeprhdd lcvlpglvdt hvhlvgyagp
       61 gdppdfatwp lvttrdeqvl hgvahaqram rhgvttlrdl agdeaqvalr rvfdagvlpg
      121 prvqvhgvvg mtaghndlfv ppavparkpt adgpdecrkl vrtwaragmd giklttsggv
      181 lsigdrnawr nytrdeirav vdeahalgml vashahsedg irvaveegvd siehgtlmsk
      241 dlaetlaarg tpvaptllin eaiaqgrvpv tpearakaae lvatrdvlla qaaalgvrfv
      301 lgtdanghhv qfgdqfaevv hmtrilgmda gsalraatsd aadsigmpvg riaqglgadl
      361 vvlrgrpwer iedlaveniv avvsrghvva grlp
//
LOCUS       WP_357602649             111 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Nonomuraea
            dietziae].
ACCESSION   WP_357602649
VERSION     WP_357602649.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..111
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..111
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12078
     Region          14..92
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 mdplfdeflh vparlsival lapadwvdfg flrdtigtsd salskqital asagyvavrk
       61 gqdkrarrty vqltptgrha fqrhaaaler ivavarmpte qptqdqgmqs s
//
LOCUS       WP_357602681             393 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Nonomuraea dietziae].
ACCESSION   WP_357602681
VERSION     WP_357602681.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=44393
     Region          86..381
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtrtalatpd depprrarkk kstkrrfgrv rqlpsgryqa ryagpdgvdr papetfatkt
       61 daevwltkie aeildgdwid pdagkvklgk yaqdwiderp nlrprtiely gylrrthlvp
      121 tfgekamnei kephvrrwrk klldggvsev tvakayrllk aifttavddq likrnpcrik
      181 gagqeksaer rvlsvpqvyk lvevieqryr alvllgtfas lrwgelaglq rrdidldagt
      241 irverqliqi tgkglvftdp kseagkrtvv ipeliidelr ahlkdftqeg deglvfvgpd
      301 dgpirnsnfn rrvwpkaved aglpkvhfhd lrhtgnnlaa nagasirelm trmghsstra
      361 amiyqhstde rqrevarkld dlargalkdr sgt
//
LOCUS       WP_357602747             481 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-amylase [Micromonospora parva].
ACCESSION   WP_357602747
VERSION     WP_357602747.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 481)
  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 481)
  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 481)
  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 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..481
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52246
     Region          38..388
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(82..83,86..87,122,125,180..183,213,215..216,
                     218..219,241,243,248,304..305,310)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Region          <102..>167
                     /region_name="pulA_typeI"
                     /note="pullulanase, type I; TIGR02104"
                     /db_xref="CDD:273975"
     Site            order(124,185)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(215,241,305)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          394..480
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 mhrrrrgsal lalgliasll vpttvtappa vaapsgakkv ivqlfewnwp svasecqstl
       61 gpkgygyvqv sppqehvrgn qwwlayqpvs yriesrkgtr aqfqsmvntc haagvkvivd
      121 avinhmsgqd nggtgwagss yshydypgiy qtqdfhhcgr nggddianyn dryevqncel
      181 vnlsdlktes dyvrtkiasy lndllslgvd gfrmdaskhm paadiaairg klsrsayivq
      241 eviygagepv qpteytgngd vhefrygkdl arvfrserla ylrnfgegwg hlptgpasvf
      301 vdnhdtqrds ggvltykdrg iyalanafml awpygsptvm ssytfssrda gppsdgankt
      361 lnttcysgwe cehrwpvian mvgfrnateg agvanwydng nnhiafsrsg kgfitvnded
      421 aavngrsyyt glpagrycdv ihgtyaggtc sgpvitvdgn gwfaanvpah davaihigar
      481 i
//
LOCUS       WP_357602831             344 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357602831
VERSION     WP_357602831.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=35055
     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 msatavaprl hvlrqrrltv llallaavfv aivlsitigs ksvplpdawh altaptgten
       61 divirslrvp rtalgilagv algvagalmq ghtrnpladp gllgvtqgaa famvssiill
      121 gassllayiw fglagalvas vavfalgmvg grggptpvtl alagtavsal lyaltsaivl
      181 ldeqamdvfr fwqagsiaar gpdvvwqvlp fivvglvlam vnapglnals lgedvarslg
      241 qniprtravg vaavtllsga svaacgslaf vglivphlvr plsgtdhrwl lpysglvgaa
      301 lllladvigr vvappgelev gvvlallgap ffvalvrrrk pvrl
//
LOCUS       WP_357602859             479 aa            linear   BCT 28-DEC-2024
DEFINITION  APC family permease [Nonomuraea dietziae].
ACCESSION   WP_357602859
VERSION     WP_357602859.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 479)
  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 479)
  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 479)
  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 479)
  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..479
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..479
                     /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=50291
     Region          14..473
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mrrlpladai glrtgarhsl hrlyrpadlv vlglgvmiga gifsmagrqa attagpgvil
       61 sfmiagiacm laalcyaela saipasgsay tfayvifgev wawvvgwali letqlaaavv
      121 arvwalyatr tladlgfgqa ipqgalaafv latltatval sariglralw vivvakllai
      181 gavivvgath fdaanlggfi apaqpssgpa dtvlglllgp tgsfgwfgvf aaapaiafay
      241 vgfdlvatas eetveaprav pqgmirslai atvlyiatav vmvgmvpytr iaqqapltaa
      301 fetlgeqvmv hvinvgavlg lttvilvlia gqtrivyama rdgllprglg rlsrryhtps
      361 rvtlvigtva illaqlapvl mleqlvvigt lfaflmvsvg vvvarrtmps apreftvpls
      421 plipamsvla tlwlminlrv qtwvwftawm avgllvylay grrrsafaae larggrhrr
//
LOCUS       WP_357602868             220 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357602868
VERSION     WP_357602868.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 220)
  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..220
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..220
                     /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=24368
     Region          1..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meradrilda aaallvrlgy rkvtiediaq ragigkgtvy lhwrtkqqlf dalllreaia
       61 yleslmaelr rdpatvlphr llsfsfvdvh grpvlqtlvt gdtralqgll vdrplrsqel
      121 latkrmfell vghgllrddv phltyamsal nsgfylvdal dpqaaeldvr akadalafvv
      181 rhalepatpp gpeevaqaaa eviavfeeli ppyrqwiyqg
//
LOCUS       WP_357602907             410 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357602907
VERSION     WP_357602907.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 410)
  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 410)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..410
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42699
     Region          27..404
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mstlttdrqd erlqdrdglr galadvldra rggdlgvipv vvglvviwtv lqilnpifls
       61 sanlvnltle saavgiislg ivcvllvgqi dlsvgsvsgl sgavlavlfv gqglpvwlai
      121 aaavimgavi gwvygqlfnr fgvpsfvitl agllaflglq lyvlgtkgsi nlpfdsglvn
      181 faqldfvpaw lsytfavvaa vwlfasgylh aqqrrkagls arsvsvlair svallvvlaf
      241 vvwylgqtrg vgwmfvffva lvlimhylls rtkwgravya vggnveaarr aginvkaiyt
      301 svfvlcstfa avggilaaar laaanqssgt gdvnlnaiaa aviggtslfg grgtafgall
      361 giiviqsiss gltllnldss irfvvtgavl llavivdsvs rrsrtshgra
//
LOCUS       WP_357602912             435 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357602912
VERSION     WP_357602912.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 435)
  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 435)
  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 435)
  AUTHORS   ter Beek,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..435
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..435
                     /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=46044
     Region          1..354
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrplttfaal lgtlaltgca ggsgeapaad vtakpefsgt lsiltkfagd plspyfekla
       61 aayekkhpgv kieliqetdq sikdksktlt asdalpdiyf twtgnwaeny vrggraadlt
      121 kvigpdtewg ktfskaslsa faydgryygi plynngkfmg ynkaaftkag vkppttfeel
      181 isscatlrka gyepiafgnk dgwpalhylq qlfaynvpsa tlradfhpst akladpgyvt
      241 alkqfktlvd tctdtgsgtn gvlytsaqea fsngkaamyy qeilefdsat agrgitpedf
      301 gifplpvpag aagnpkvieg apegylvnak spraalavdf mkfvteqgna ktlssppygq
      361 pstvvgavtp etsskavfeg ielvnkapel aswldmvtvp evadawlagg ealisggkkp
      421 eqvlesvrqa sesak
//
LOCUS       WP_357602992             330 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Micromonospora parva].
ACCESSION   WP_357602992
VERSION     WP_357602992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..330
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34532
     Region          48..>172
                     /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 marhlvatgq lidedpaeal ahalaarrla srisavreav glaayhagew qsaiaelrty
       61 hrmsglqshl avladceral grperaidlf rgadrekldq avaielliva agargdlgqk
      121 daavamlqvp dltseatvpw tarlryayad allavgrrde arewfsraad vdtegetdaa
      181 erlleldgvv iegddedeaa eeiaagpgap gavparpdad ltgddeddad qdvddddddq
      241 ddddddqddd adfdddeeda avgrpgddeg fddededrhp sgsgnadagt agdsgvtsgd
      301 aanrdvakgd tanaagtlpa ggdesgstqr
//
LOCUS       WP_357602926             177 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine dioxygenase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357602926
VERSION     WP_357602926.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 177)
  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 177)
  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 177)
  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 177)
  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..177
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..177
                     /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=19800
     Region          56..143
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mstiqiqdgg tcarlpertl drrelrelvn elaahpeewr dqvafpeegg rhyaslyrda
       61 yvdvwllcwr peddtgwhdh dissgavhvv qgallecnpr iggehletvv segqsfsfgp
      121 dhihrlngav dksvsihays pplwrlgqys iddtgvmrrv svsyadelrp lddavva
//
LOCUS       WP_357602914             321 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar-binding transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357602914
VERSION     WP_357602914.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..321
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34252
     Region          22..316
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mnaadvapet qarfplelmy aaaqqyymee atqgdiakrl gvsratvsrl ltearrqgiv
       61 eikvhrpatl gdgplaaeva ealrlqrvyl vpkvsgptlg pwlapavara lsavglesgd
      121 vvlvssgttv yecareglgh ypgvtiapav ggqeepqpwf qtnettrila ervggvpayl
      181 yapalpgpel fyslqhepsv rrvmdlwaha kcaivgvgsa plmrqmmpal mprdadslre
      241 avgdvcmrvy drdgepityp gserlvatrl eelrriptti avavgaekvl sivagakggy
      301 fnqlvtdvpt aeglvaaarn v
//
LOCUS       WP_357603000             399 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357603000
VERSION     WP_357603000.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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 399)
  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..399
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..399
                     /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=45122
     Region          1..380
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mrtaykcray ptpeqadvln rtfgcvrvvw nrtlawrhqr whgerlptnv peanahltam
       61 kklpelawln evssvplqqv lrtqqkafan ffagrakypr yksrngrqsl eytrsgfryr
      121 dgrlflakmd vplefvwswp dvepttitps tvtvsrdpcg rwfisfavdg ddpeqaaatg
      181 amvgvdlgik dfavtsdgek ivnprtlaqr ernlaryqrr martqrgsnn rakakakiar
      241 ahrkvrtsrq dflhrtstrl vrdhdvivle dlavknmvrn rclakaisdc gwgtfrwmve
      301 ykaartgrhv ividrwhpss ktcshcgyll selklstrtw tcpgcgtlhd rdvnaaqnil
      361 aaglavsacg gdvrhaespr mlspvkqesq pvrvgipsp
//
LOCUS       WP_357602930             465 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357602930
VERSION     WP_357602930.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13398658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..465
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=50864
     Region          11..>242
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
     Region          298..362
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mgdanldays rrlrrihett vgeprqlisa swrrskaagv dpesraaplv ydgslirdvr
       61 eshplqpvlp mlaetlrrma desehimivt daegrilwrd gdfgtmrrad vvgladghhw
      121 seisvgtngi gtalatrkpv hvyseehllr vlhcwscssa piidpdtdtv lgcvdvsgit
      181 rslhpatval vattaklaea rlalmmherd erlrrkydal vqrtgvlitk tgrvlagdhs
      241 grlgaritlp epggtdcpag ilepffdgyl lrpasrteal plrlaflgeg ppiarygdrf
      301 ltlslrhaei ltllalypcg ltaeqlsyyl ygdegnpati rpeiyrlraq lgeavaakpy
      361 rlvaplsadf lelrqlltan dpeavaraya gpllprsesp eirsardele vqvrasllth
      421 gsadalwtya qtvngrddfq ilervaaalp ssdhraaaar arlsp
//
LOCUS       WP_357603023             237 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357603023
VERSION     WP_357603023.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 237)
  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..237
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..237
                     /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=26192
     Region          18..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgrvgrppqd pvqrahgild aaaelvvrwg ydkttiddva kragvakgti ylhwktrdel
       61 faallrrerv ylveairasa patmgelfge fvgsalrrpl mraalvrdse vlgklarmkq
      121 rstmrldmgd afdayldrli ehgavreapr dhmtvitaiv hgfvflpelv peeaqlpder
      181 iaelvadtvd ramgtgralp eqdaqavaqa tldlldsmae vahrrfmasl itkeral
//
LOCUS       WP_357603133             210 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603133
VERSION     WP_357603133.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 210)
  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 210)
  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..210
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..210
                     /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=23112
     Region          2..197
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mladdfflvs wdttgsgkpr lhvqgialgl agaligelvl hqrvtvqgtr lavadprqim
       61 envadkalad ignsphhtdv rtwlaylarr svddvsgrlv atglleretp kllkrkqcrf
      121 fstdfskamw patrlrlalv rweplspqdm alaalvdacd mtdtvlddpa drrlarqylt
      181 rlqdaiprpl gdlsrqvsaa vgdavltyrt
//
LOCUS       WP_357603156             331 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357603156
VERSION     WP_357603156.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 331)
  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..331
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..331
                     /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=34123
     Region          23..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 medwlqqgvr evvilhtwlt drfglkvplv gapmagvgag rlaaaiseag algvigasaa
       61 vtpewiskea avagggpygi glmawalpgn paqfdavlel rpalvsvsfg pyaryveelr
      121 qagitvvtqa gttdearaae qagvdavvar gaeagghgrd evgtlpllqs vldavripvl
      181 aaggianarg laavlaagaa gawvgtafmg cvetalsaea gdrllaaeet gtaygrvfdi
      241 aqrlgwppey ggralrnaff drwegredel aaddsararl eearrvgdfd tayiyagqgv
      301 glvrerrtaa dvvadfaaae rlltrftapg a
//
LOCUS       WP_357603164             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357603164
VERSION     WP_357603164.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  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..190
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..190
                     /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=20896
     Region          10..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprvsqdqld arrqeilsaa racfarlgye gatvrrleea tglsrgaifh hfrdkdslfl
       61 avaeddaaam vetvarnglv qvmrdllara vspdttgwlg sqlevsrrlr tdpafakrwa
      121 ersaaiaeat rdrlarqrda gvlredvpid vlaqflelay dglvlhlamg rpagdlgpvl
      181 dlveeavrrh
//
LOCUS       WP_357603232             536 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Nonomuraea dietziae].
ACCESSION   WP_357603232
VERSION     WP_357603232.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..536
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59085
     Region          16..523
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mghvevahlt yvlpdgrpll ndvsfrigeg vkaalvgpng agkttlmrlv agdiqpvegg
       61 vassgglgvm rqfvgsvrds stvhdlllsv appavrqaad kldkaelamm erddektqmr
      121 yaqaitdytd aggydievlw dtctiaalgv pydrvkyret atlsggeqkr lvleallrgp
      181 dqtllldepd nyldvpgkiw leqqlretpk tvllvshdrq llanaadriv tvesggiwih
      241 gggfgtyaea rrarnarlde lrrrwdeeha klralvnmlk nkaryndgma apyhaaqtrl
      301 rkfeeagppe eapsdqrism rlrggrtgkr aviceqlelt glmkpfdlei wygervavlg
      361 sngsgkshfl rllaeepvrh tgvarlgarv vpghfaqtha rpelhgrtpc elvmteharl
      421 kneamkilar yelagliadq rfetlsggqq arlqilllel sgatllllde ptdnldlasa
      481 ealqdglnaf dgtvvavthd rwfaddfdrf lvfgsdgkvy espepvwdea rvvrqr
//
LOCUS       WP_357603233             188 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603233
VERSION     WP_357603233.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 188)
  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..188
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..188
                     /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=20589
     Region          4..162
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mdplrvavii gstrvgrvgd kvgawfaera grrddlavev ldlagytfpr cypeestpdm
       61 csfagsvgga eafvvvtpey nrsfpaslkq aidfaydewq akptgfvayg sgsagmyave
      121 qlrtvfcalh svtmrdwvgl dllgedvder grprdtddrl ravaamldql twwgralraa
      181 rraqpyas
//
LOCUS       WP_357603240             318 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357603240
VERSION     WP_357603240.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..318
                     /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=35241
     Region          21..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 maitavpetp rkpgrppspy sarpqrtslg rkvrdnltgh afligavlcf vvfswypmir
       61 givmsfqrtr rgettwvgwd nytrliadps fwpawkntfy ftglalilgy avpffvaill
      121 nefrhgkgyl rilvylpvml ppasalflfk fyaydpseag lfnailkalh lptsqwmqsp
      181 emtmpamvva stwmnmggav liylaslqni pgelyeaael dgagiwrrir hvtipqtrli
      241 lallamlqiv atmqlfiepl ilangagaed satsvayliy qhgffqndln gaaalgviml
      301 vvlagfsavy vrltakqd
//
LOCUS       WP_357603294             197 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603294
VERSION     WP_357603294.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  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..197
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..197
                     /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=21322
     Region          20..189
                     /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 mpsttsdavr tplrgtalda lkivivggfg vgkttmvgsv seirplstee vmtqasegid
       61 dasrvraktt ttvafdfgri tvtpdkvlyl fgapgqqrfw fvwdqlfags lgavvlvdtr
      121 rlqdswysid rlehhktpfv vavnrfadgp sleavreala lspdvpliec darkrpsskh
      181 vlitlvkhia gtrdges
//
LOCUS       WP_357603302             136 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            dietziae].
ACCESSION   WP_357603302
VERSION     WP_357603302.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..136
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14722
     Region          15..122
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 matvtaaerr aeakrayday vaacpsrkll dtlsdkwvsl vlnaladgsk rysdlartia
       61 gvsqkmltqt lrglerdglv trtvtaavpv rvdyrltslg esllplmaai kqwaeshied
      121 veaarlryda dsgnsp
//
LOCUS       WP_357603351             331 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357603351
VERSION     WP_357603351.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=35499
     Region          249..316
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgwwqvnadt maegrfalsp laettaalfa lqaglaghpg qrawldahlp ayrkrlaadp
       61 italllraal grtwtadflt paptgedeps fvdelarira tpprtavsdl alsasgpvpa
      121 elhrsdlper aadllewvws etvlpswpqr rrvlhadiva rtslltqggw ataldglrpg
      181 mrwlgdgrlr inaldyppre isgarllfvp vtpltprqgw iawslpsrya vvyacsgvla
      241 eantspvpqa lgaligagra rvlvlldtpk sttqlvaltg qglgsvgrhl rilldahlvr
      301 rrragrsvly yrttagdalv eagagqpags r
//
LOCUS       WP_357603371             208 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603371
VERSION     WP_357603371.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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 208)
  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 208)
  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..208
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..208
                     /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=21375
     Region          4..208
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mtslavvaat grtgrliver alaaghavta varhpealgl dhpeltrraa damdparlre
       61 alaghdvvvs algstgrgpt tlysagtaai iaalppaarl vvissaglat padagpavrl
      121 fgrvlhhvmr hpyadmnrme qllagtslsw tavrptgltd rpgtgrprvs lgaserlgar
      181 tsradlaafi vdhlddpltf grpvavss
//
LOCUS       WP_357603381             907 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357603381
VERSION     WP_357603381.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 907)
  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 907)
  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 907)
  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 907)
  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..907
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..907
                     /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=97565
     Region          1..229
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          100..906
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          676..704
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(677,680..681,684..685,687,711,720..721,724..725,
                     727..728,755,758..759,764..765,768)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          709..745
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          754..784
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvsfhvlgpl earaagrpvr isgrkprmll atllldanhl vgadhlvdvl werpprsaha
       61 nlrtyasslr selgarirae gscylievah deldlltfer lvarrdpesl aealtlwrgv
      121 plsdlpdhpl wtrrlaplpe vrlaaareli aarmergeyg eavtllralc aehpfredlw
      181 gqlmlalhgs grqaealacy teirrqlvae lgvepgaelr evqatvlagt ppsqrvwtpr
      241 qlppdlpdfv grrqalallt rqgdgrgpfp vavisgppgs gksalavrga haladafpag
      301 qlylcmaaad padllaqalr algvsaipat ldersalyrs vlaerpmlvv lddaadaaqv
      361 rpllpgagss vivtsrsklt svpgalqihl eplsppeaee lleriigadr arrereaata
      421 ivracgfvpl avriagarla arpgwslalf qnrlkdesrr igelrigdld vrlgldhsyr
      481 glpaeaartl htlgrlggas lpgwvvdavl grhraddvtd alvdadllrl vgtdplgqpr
      541 yrlpdlvrch aleqgpdlaa larvvatwta ttelatarlp ttvftlssaa aarwwlpret
      601 lerltadpla wfeaehegle eavrvaassg lggqawglaa amvpyldlrc hfgiwqrthg
      661 talaaarvag dsygeaamlr glaqvclyqd ryaeseemfa rarrafhelg dtraeatsvc
      721 glgavaqfrg ehraalahfh ralvmfgsvg dlsgeaytrq aigrvclksg dlvqaaqwlg
      781 qalrlaqqlg dvhregcvsi hlgklgeper fhgraldife slgdrhcgay amqslagfqa
      841 asgelgpasa glersllifr qlgdrsgeas saqllgelhr sagraelard yldqavvlrg
      901 slaaeav
//
LOCUS       WP_357603404             464 aa            linear   BCT 28-DEC-2024
DEFINITION  phenylacetate--CoA ligase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357603404
VERSION     WP_357603404.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 464)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..464
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50252
     Region          29..440
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mftvyhpela dlarslrerh deflaggwda arlaeyqaer lratlayags rspfyrarld
       61 glaegddlat vpfttkqdlr dagldllsrp mheawifyet tgttgaatpc prdnvdtlhn
      121 nsvltayygt vfdqygdaqv igvsgpsemh atgdtfgdvc rnlglavakm wphspmvgfe
      181 ralevmrllp itgmfctpgm alslakrave agldpredfs ievfmltgel aspsllanig
      241 slwgarayna lyasqeasvl aaagadggly taplinyyev idpettrpat pgpdgvrqge
      301 lvvtnlyqga kpliryrtgd mvrmspaapg adipaprvev lgrvgdqlev ngrritgydl
      361 edlllrhvrn cldyqivlad dhvglllhgd lgaddpglrl areecrdtlg telvvsfgdp
      421 gaitstgamv swkaarvvdr rsgrlgarde rearaarala arrr
//
LOCUS       WP_357603435             141 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357603435
VERSION     WP_357603435.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 141)
  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 141)
  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 141)
  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..141
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..141
                     /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=14681
     Region          9..129
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mdgqeregid vvaaavverg rllvvskksa pdlfylpggk pepgeseeqt larelkeelg
       61 aaptgvslla rfegvaaleg vpmrlavfha aldqaplaaa elarlgwtdg adeyvpllas
      121 airdqvvpll kktgaltgsr p
//
LOCUS       WP_357603456             210 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357603456
VERSION     WP_357603456.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 210)
  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..210
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..210
                     /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=22636
     Region          12..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mngpdpedlt ararirdaam qhfaeqgfer atirgiaeta gvssglvrhh fgskqglrea
       61 cdahlakmir rlndevrsgh aldkanpvat anaamgpyqr ylaralvegs aetvfdqmve
      121 lseewlaead ekrsdtpdvd rkaratvgta malavavlhk hvsrglgvdl ytpegdllla
      181 rtlidiyshp mlsveeaaev raaldnlspg
//
LOCUS       WP_357603466             268 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357603466
VERSION     WP_357603466.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 268)
  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..268
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..268
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27900
     Region          11..265
                     /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 mtepvsrtat sadgtriafd rsgsgpavvl vhgaftdrrh ptlysvaaal apwftvfnyd
       61 rrgrgasgdt ppyavhreie dlaavieaag gsamvfggss gaalaleata rdpaisklav
      121 weppyhvdes apclpddfaa qlealvgqgr raevverfmv eaaevpveav tamraepswp
      181 eleavahtla yeaavmgpgn alpagllgai nrptlvlnge rspawmtsag ravaksvpga
      241 lhrvlegqth nvsaqalape lleffvaa
//
LOCUS       WP_357603471             302 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603471
VERSION     WP_357603471.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..302
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..302
                     /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=31285
     Region          4..283
                     /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(32,239,242)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(178,210,237,240..241,244)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtflvigesi vdligspgaw rfnavaggsp lnvavalatl gqpvrlagei ggdffgellr
       61 ghlsrygveq gelvpsaats lafarvgddg sasydfrfdw rfsgsvsldg vtclhtgsla
      121 tlvppgaahv rdvmraaada gvvvsydpni rpsligdrat altqveecvr lsrlvkvsae
      181 dlawlypgep dlnaakrwaa wpgerlvvvt rggdgasail gdsvitcpap vvelvdtvga
      241 gdtftaayla vlgdgeltee rvrdalrygc aaaavvctre gavppepqei dqlissvpat
      301 pv
//
LOCUS       WP_357603484             253 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357603484
VERSION     WP_357603484.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 253)
  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..253
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..253
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27101
     Region          30..252
                     /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 mmnglphlsi gqgpplvvll ytpraadpeg aarwsmtrml rpfaehftvh vvirppglpp
       61 attmaelaav yagaiearfe dpvkvlalst ggsvalqlaa dhphlvdrla lggtaatlgp
      121 vgrraqrayi erarqgrrps palaevvtes vigrrllaal lwlsdgggad htdavtmlna
      181 edgfdlrgrl sdiraptllv qggedvvypv elarqtvegi pdarlivyqg rshsrtftdk
      241 rfardtlafl krg
//
LOCUS       WP_357603491             400 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603491
VERSION     WP_357603491.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..400
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..400
                     /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=43268
     Region          3..369
                     /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 mensrtdvav igagpaglvl tevlarrgms vtiverqddp tlsrqgallq pvtldllhrl
       61 vafehsaeqe gaittieeyg pqgkifsgpf adladtpadh alnitqgmlr kllldrvrrh
      121 psvavrtgaa vqqmdsmrpg rcsivirevn gaetphrids rwivaadgkl setrrlagik
      181 arieggdhql slvpvptpeg yprtirvhrr pdgmattvpg aapgttyvfa hladrdataq
      241 tvvdwamrtv saqddiltta lrshadpaki isippqivht ptwrqdgvil lgdsshgmyn
      301 vggqglntsl qdallvgeai rsddeaggte qldafvrvrr pfidefqaaq rklgsgfwpv
      361 gggtswfrdr feelslgqae lrkrwseivd elsvagqgsa
//
LOCUS       WP_357603504             307 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357603504
VERSION     WP_357603504.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=33068
     Region          2..304
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrvllagatg aigrpllsal aasgheviav irdpakrrlv adhgalpvia dvldrdgllr
       61 avdghaadvv mhqatalrea grrlrpddpt illrgrgteh lleaaravga rrfvtqslit
      121 gygyrdhgsr vltendvfgl hagnvgdlvt dssvaterqv faadgiegia lrygmfygrh
      181 afsdmfadlm rkrapvlprg etgttsfihv edaataavaa mergrdgeay nivddqpasw
      241 rtfltevara hgtprpvvtp rwlirlavpy lgclmidttm rvshakatre lgwtpvyrnl
      301 seglglg
//
LOCUS       WP_357603588             447 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603588
VERSION     WP_357603588.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 447)
  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 447)
  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..447
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..447
                     /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=48228
     Region          10..418
                     /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 mpignqqlds pprgpdvaii gagigglava kalddagvaw ecferrsavg glwsqnpele
       61 dgpaywalhv nssaafmams slpippdfpe fpsreqighy lahyadhfsl sprvrldtev
      121 trvtqepsgg wivetsgggr grygsvvvat ghfsqpimpd ipdffggevl hahdyvsper
      181 fagrdvlvvg lgasgadiac evsrtaarta vsvrggvhiv pkhlfgrpfd tfpvrarprw
      241 lrwqvmrlav hlsrgpqery giarptrplg naavtvtsdl ltrlahgdla vrpalkgfke
      301 davvfadgsv epydtiilct gyrpsfsfld paitppsdgl dlfrrvfhpa atdlafvglv
      361 qilgaapatl erqarlvaak lsgryalpga dgiarelvrd raraarmfgd drragmlldp
      421 vtyrsliere lraglrrarr ngsvgra
//
LOCUS       WP_357603521             287 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603521
VERSION     WP_357603521.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=31528
     Region          56..282
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrnrvgllaa mvagritvrm lrrvgsisgd lakinisdey gqivqqrdla qvtqlvenin
       61 vsldmldrer rfastiahei rsplagirva aeealadpdr vdysgvfegv lrgvdrveal
      121 atdllliars raaeieweqi dlcelvrrev aartdpvpve victsgvlvk amptqiceiv
      181 tnlldnaqry arnqvqvhvd rsdrmarltv cddgpgvpek drkrvfdrmy rlkaisqrgs
      241 tstglglait weivrahhgt vwvepatigg acftvqlpla vpsgpes
//
LOCUS       WP_357603629             310 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357603629
VERSION     WP_357603629.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 310)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..310
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=32064
     Region          20..302
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mtsnntlseq kmpnldtdht pvtviglglm gqalagaflr gghsttvwnr taakaedlva
       61 qgakladsvg davaasplvv vcvsdydaah dlldplgell dgrvvvnlts gtsraaresa
      121 ewagrrgaty ldgaimaipp aigtadalil ysgpqsafdl hapalrslge gatylgedhg
      181 lsslydvail slmwnilngf lqgaallgaa gvdattfapl akagittvad wvssyaqqid
      241 dgaypaldat idthlasmeh liheseflgv taelprfvka ltdravaagh ggnsyaamie
      301 qfrkpsaehs
//
LOCUS       WP_357603638             329 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603638
VERSION     WP_357603638.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 329)
  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 329)
  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 329)
  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 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   5  (residues 1 to 329)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..329
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..329
                     /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=35372
     Region          <151..240
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          246..318
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkarltfsvd dlaetrfvvs pmwevvtsfr alaaaavlgp hrawadqvrp rlaaagldrg
       61 wladmippig hfpdflnpgp ataspglade laaieatgpe qvrrdldrla aeregrlspr
      121 lrslhqapqt clprivaeie aywglaiapy warissllea difhrgrqva eqgtaqalde
      181 lhhtvrwadg slhlverhca itridtgagl llvpsafawp rvltrsvaae ppqlayparg
      241 igtlwerrth aqvdalaavi grsralilve ldspasttel aqrsglsaag vsqhltalra
      301 agltsthrag rsvlyartgl adalltaqt
//
LOCUS       WP_357603640             406 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603640
VERSION     WP_357603640.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=44298
     Region          16..404
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(53,60,89..90,97,101,108,237..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(60,83,85,88,90..91,176..177,186,236..237,240..241,
                     245,288,291..293,394)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mgsaapvvld pfgadlpgev rrlrdlgplv lvelaggipa wavtrhdllk qlildpmvsk
       61 dkrhwrllpq altepgwtwi ltwigvsnml saygeehrrl rkliapsfta rrtramqpiv
      121 egivaellda maaqppgqvv dlrgayahpl pmrvicelfg vpdhmrvema qmmeaimdtt
      181 atpeeaaata aqigtvlpal vaykrehpgd dlttelinvr dsgdslsdde lrdtllllia
      241 aghettvnli gnavhallth pdhlrgvlag eisweaviee tlrwapsian lplrfaiepi
      301 eiggvrieag daiitsylaa ghdpdqhgpd adrfdptker dehlafgigv hrcigaplar
      361 qealaalpal farfpdlrla veeselphvp sfiahgwsrl plllhr
//
LOCUS       WP_357603678             359 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603678
VERSION     WP_357603678.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=38284
     Region          13..355
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mtdvfgtshk dvheqvvfca deqsglraii aihntalgpa lggtrfypye sesaaladvl
       61 nlakgmaykn alagldlggg kaviigdpar dkseallray grfvqslggr yitacdvgty
      121 sedmdvvare srfvtgrtra hggagdssil tafgvfqgmr asaervygtp slhgrrvgve
      181 gvgkvghrlv ellyedgaev vicdvdpeav ervrrrrpev dvvadaeelt asdidvfapc
      241 alggvlddat varlrarivc gaannqlahp gvekqlaerg ilyapdyvvn aggviqvade
      301 iegfdmerar skatqiydtt lkifriaade gvppavaadr laerrmsevg rirgiwlgr
//
LOCUS       WP_357603683             651 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Nonomuraea dietziae].
ACCESSION   WP_357603683
VERSION     WP_357603683.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..651
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..651
                     /product="PhoX family protein"
                     /calculated_mol_wt=69967
     Region          12..643
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mantsdntyf gdvvaqamsr rgvlragalg alvvgtgvag avpafadpga eqgaealgkh
       61 gdhgrggltf kpvapntdda ltipegysss vvvgwgdpvl pdapafdfdn qsaeaqskqf
      121 gyncdfvtlf pmghnrallw vnheysderl mfrgytggat ateeqikigl aahggsvvev
      181 ervkgtgqwk lvtsgrrryn rrvtaqtpmr fsgpatgsdl lktaadakge npigmlnnca
      241 ggttpwgtvl taeenfdqyf vngdktdpnv arytiptgvs sssrrfdrve erfdlakhpn
      301 eanrfgwive idpfdpdstp ikrtalgrfk heaanttltr dgrlavymgd dsrfeyiykf
      361 vsdkryipgy drhnrtllde gtlyvaqftg dspaaeidgs gklpsdqafd gsgkwiplvs
      421 gsksfvdgms aaevlvftrv aadkvgatkm drpediernp vtkgvyvalt nnsnrtaaqv
      481 deanprpsnk hghvleiver rddagattfa wsiplvcgdp ndpatyfagf dktrvspisc
      541 pdnvafdrdg nlwistdgna lkandglfvm pvqgsergyv rqfltvpvga etcgplvted
      601 qrsvfvavqh pgevdgaspe spashwpdgg ssqprpsvav awhsrgkkig s
//
LOCUS       WP_357603724             104 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603724
VERSION     WP_357603724.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=10630
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawivivlag vfevamalsl klsngfsngw walsffvtaa lsfgllsyal rtlevgtaya
       61 vwtgvgaagt avlgmiamgd evslprlvsi alilagvvgl rila
//
LOCUS       WP_357603731             247 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603731
VERSION     WP_357603731.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   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 247)
  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..247
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..247
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=25170
     Region          87..245
                     /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 mrgligvmgf vmalaacgsg ggtgavpaps spavpsasvs tppptgpdvs gcyhqndgki
       61 ftydgdmpgi iggagsvgvv ityerrgtvc swrplfdrlt sryrvlvytr saqslpedta
      121 vamarrllke rgvkrvflvg gsigattavp aalrlgpeaa gvvalsgris eenagrltvp
      181 llqigsandg yggagdlaka hdaaarspdn ellvipgesl hasallasph aqqvldrida
      241 fmarhkg
//
LOCUS       WP_357603744             103 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357603744
VERSION     WP_357603744.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 103)
  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 103)
  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 103)
  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 103)
  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..103
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..103
                     /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=11159
     Region          <2..95
                     /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 mwgidnhhrs ahiglgllps argkgygtdv vavlchygfv vrglqrlqie tladnaamlr
       61 saerngfvre gvlrssawvl gefldevllg llvqdwepaf gts
//
LOCUS       WP_357603751             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357603751
VERSION     WP_357603751.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..212
                     /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=23213
     Region          5..>92
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          68..208
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mgkltaqaia eraleigdae gldavtirrl atelgvtpma lywhyknkeq lifgmadhli
       61 gsfapkradd rpwqeqfrdl ieglirtlrt hrcaksvleq idavevpnfl avwdqalgla
      121 rragfgides cliskyilqs aiaiadapvh vktvdpaavr akmaslqslp egtypylvem
      181 asplikgtep rlydtfgvdl vlsgiealaa rr
//
LOCUS       WP_357603853             406 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603853
VERSION     WP_357603853.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..406
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..406
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44545
     Region          128..403
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mqplffpdnp qfwyetlrtf ghiayggadf gevavtceri tpgdydswyd qwlatadrva
       61 aeartslddg hrisardall rasnyyraae fflhgnatdp rirhaydasv tcfrqaatlf
      121 tpvvepvqip yedtvlpgyl yrvddsgaar ptvvmcngfd gtveemhffg aaaavergyn
      181 vlafdgpgqp gtrhhqglmf rpdwenvvgp vldhalsrpe vdparialfg asmggllmpr
      241 aaafdqrvaa vialdgvydl ghiatasipl praeaerrlr aerdpeldam leaamaaspm
      301 trwaiehgmy amgvdtpraf catyldyhlr dgvaekiscp tlvcagaddg fflgqpelly
      361 ehltcpktll eftadqgada hcqsgaqrla farvydwldd vlghaa
//
LOCUS       WP_357603813             290 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nonomuraea dietziae].
ACCESSION   WP_357603813
VERSION     WP_357603813.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..290
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32407
     Region          16..287
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mnealkelld lldleqield ifrgrspeer iqrvfggqva aqalvaagrt vpegrdvhsl
       61 hayfirpgdp aipivynver vrdgrsfttr rvvavqhgka iftmsasfhi feegvhhqaa
      121 vmpqvaapet lptfqsrmle lvgddsdwkd wlsrprpvda ryvspltwea ykdpslrtae
      181 nnvwfrydae lpddrllhvv laayasdytl vdtvllahgl awgasnvtga sldhamwfhr
      241 pfraddwlly aqespwsgga rglargqmft psgelavsvv qecmirvaks
//
LOCUS       WP_357603862             224 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357603862
VERSION     WP_357603862.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   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 224)
  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..224
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..224
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24717
     Region          6..213
                     /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 mttfalihgg ggsafdwhlv eaevraqghd tvavdlpmsd pqaelwdyad avvqavggrr
       61 dlvvvahswg gfvaplvcar akadalvlvt amipspgeap ddwwehsgrp ssdirdeyql
      121 flhdvprelg ervlahdrvl aekismdral hepwplavwp dvptryvlcr ddrfftpdfv
      181 rrhvkerlgi vpdelpgshm amlshprela dylvgvaggp rqgq
//
LOCUS       WP_357603959             367 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357603959
VERSION     WP_357603959.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 367)
  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..367
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..367
                     /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=38625
     Region          120..366
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvlgvlvfgl slatlsgqmg vatdlpfpll vliaavagva awfaprawwp laavgalahv
       61 gfamwppllv asyyagatlr errdiaayag mgavtvalsa gvgaliggqr ehltgtlgna
      121 tlmgaagigl plvfglwvra rrdvlaaaqe raerlereqv mradqaraqe rariaremhd
      181 vvahrvslmv mhagalevgt sdsrtaqaaa ligdigreal tnlrdvlgvl rapslpapra
      241 pqptladldg lldqsralgi altrhdegea rslgptvert ayrvvqealt nvhkhagett
      301 advsirflps slevvvanhp pvrqaaplpe sgwglvglre rvelvggtlh tghredggfe
      361 lraripa
//
LOCUS       WP_357603966             237 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357603966
VERSION     WP_357603966.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=25487
     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 mnrterlyal vdelravapr prtvgwlaar favsrrtvqr dlqalmeagv pvraqpgqgg
       61 gwfvdrdhal ppinltaaea lavaaalaga edgtpfsaag paamrklaaa lgsstaeevr
      121 alterihvlp artapdvlat veqavarqrv vwiryadssg reserevepg gllaasgswy
      181 llgwcrsrra grgfrldrir aaelrdepsp artvpaldrd laervrraet lrslsga
//
LOCUS       WP_357604005             424 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357604005
VERSION     WP_357604005.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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 424)
  AUTHORS   ter Beek,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..424
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..424
                     /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=45481
     Region          1..342
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrrrlagisl lgvlaltaaa cgsggggggg akpsegpati tmwtraatqa qserlvkayn
       61 sshkniqvkl tviptdnyqp riaaaagakq lpdvfaadvi fvpnytsqgl fmditdriak
      121 lpykdslaps hmklgtldgk qytlphtldl svwfwnkdly qkagldpekg pkslkefaqq
      181 attiqeklgk dgkvhgtffg gncggcyvft fwpsvwaagg qvmnpegtqs lndqaamtdv
      241 fkiwrdlyek kvtgptakee qgptwtgffp kgeigvmpmp sttlglmpkd mkigvtpiag
      301 pdggestfvg gdsvgisatt knpdaawdfl swtvsdeaqv eimaknkdvl artdlagnky
      361 saedprvvli nslvakgqtp yalrfgqtfn dpqgpwlrla reavfgdask vpqlnaeitk
      421 slqq
//
LOCUS       WP_357604017             264 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604017
VERSION     WP_357604017.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..264
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28206
     Region          2..264
                     /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 mskvisadgt aiaytragqg ppvilvdgam syrgqsintg latalatsft vytydrrgrg
       61 esgdtrpfap ereiedlaal vaeagdevrl ygissgaava laavesglpv eklalyeppf
      121 ivddsrppip gdyqrrleem vaegrsadvi ryfmrkgvgl pavvvammrf mpawpkikav
      181 ahtlpydaaf vvpyeqstpy pagswasvkv ptlvmdggks qtwirnaars laevlpnaeh
      241 rtlegqthvv kpaalapvla gffr
//
LOCUS       WP_357604045             244 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357604045
VERSION     WP_357604045.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 244)
  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 244)
  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..244
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..244
                     /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=25419
     Region          2..241
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mktalvtgag rgigraialr lardgfrvav nyvadetaak evvglieqdg gsafavqadl
       61 grqedvrrla ermrgatdvl dvlvnnagig rsssiaeetp eaydrlfavn vkglffltqq
      121 llplipdggr ivnitsgvvr iafpesiays mtkgavqvft lalakelgpr gitvnnvapg
      181 iidtdvnagw lrgnpeaeay aasrhalnri gqvdeianav afvaspeasf itgstidatg
      241 ggnl
//
LOCUS       WP_357604059             662 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea dietziae].
ACCESSION   WP_357604059
VERSION     WP_357604059.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 662)
  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 662)
  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..662
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..662
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73010
     Region          1..>162
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkvsvivnvh npgntadaci rsvleqtlpp ddyevifvdd gstdgiaerl dtvaaarsnv
       61 rvlhlphtgs vmrgrnvgva satgeyvyll dqrdrlerga lklmyerave cdsdvligrl
      121 vrdggrpiaa fevnraradv vrdklltllt phklcrkafl eehmigfavp ggkvaeqtfs
      181 vraylaakvv tvladevcch lgepeersdd eplvvaaelr alldvidagt eagrqrdkmy
      241 ahwfrstvlr lfrsarftrs svdrglvftt frtltlerfp erldrylpvh lramavllra
      301 grldqlisfg tdsrrsalrt dlsevswvgg vlelglavev ythageparf redgdrlhwr
      361 ppgsvdhtll pdevtdvtda vararidvyl rhqdtgdvyf vpvtseavri hergrvrvqv
      421 hgrarvdvat gavgeplpsg qweihvrmyg gahrassris rsdgpltclg vlaehprrrl
      481 vvpcwsdsge lglcveprsf sesialvsaa atvtkreghv fvvvpvpyvp psggpalelv
      541 lrdtsrkare vsvpalvepg lpgktagqlv akvpvkrfmp gpehvgpgaw ltslraedse
      601 tglrfalemr rgrvevrpat avdpeynplg rdtalrrlar rvpgaryavr lvrasthryl
      661 rd
//
LOCUS       WP_357604066             389 aa            linear   BCT 28-DEC-2024
DEFINITION  homogentisate 1,2-dioxygenase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604066
VERSION     WP_357604066.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..389
                     /product="homogentisate 1,2-dioxygenase"
                     /calculated_mol_wt=43023
     Region          1..388
                     /region_name="HmgA"
                     /note="Homogentisate 1,2-dioxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3508"
                     /db_xref="CDD:442731"
ORIGIN      
        1 mpyyrvvgev prkrhvqfrr pdgglyaeel mgeegfssds sllyhrylpt aivkaeavtp
       61 taetrlepnl plsprhfrtq elssagdlvt grmllagngd vrlsyatsdq aselyrnsmg
      121 decvyvqrgr vrfestygvi eagegdyivi ptgtihrwvp dgqvnvlaie agghirppkr
      181 ylsqygqlle hapycerdlr apaepllveg eevpvlvrtr gglsrlvyrn hpfdvvgwdg
      241 ylypfafnid dfepivkkth apppvhqtfe gpgfvvcsfc prpldfhpes vpipynhhnv
      301 dsdefmfyvg gdysarkgsg idvgsislhp agfthgpqpg aveavidavs rgvtttseka
      361 vmvdtfrpld lgqgalsced pgyawtwsr
//
LOCUS       WP_357604123             379 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357604123
VERSION     WP_357604123.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 379)
  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 379)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 379)
  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..379
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..379
                     /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=40645
     Region          <176..377
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlpllrslwd eprparpprr grrdwalvgl lvalavlegv lrpdlpwrav svmltvalvp
       61 tllwrrsrpl pmvaiafgal slaplltggh spetytmvfl lllpyslfrw gagreavigl
      121 aiilgrafls avvdhpglgd ligglailfs avalglafry rararrreld hvkllereql
      181 ardlhdtvah hvsamairaq agiatsatrp saatealvli eseasralae mralvrvlrq
      241 dqpadlapgq siadlerlag rarsgpsvdv eihgdvddlr psvgtaiyrl aqesvtnalr
      301 harhatriev rvsaddtsvr lrvsddgdps svpaapsqgy gligmaerad lhggtceagp
      361 npdrgwtvta vlprkgaat
//
LOCUS       WP_357604106              74 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604106
VERSION     WP_357604106.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   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 74)
  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..74
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..74
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=7598
     Region          <2..74
                     /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 makpdfepvg vlhqvkaptl viegshepak pghsaiiaeq ipgarlmiva gmghtlppev
       61 heelaaaila htae
//
LOCUS       WP_357604128             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357604128
VERSION     WP_357604128.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 Nonomuraea"
                     /db_xref="taxon:2593643"
     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=16737
     Region          8..149
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mltntqhktd lrsdaglasa lrvslarltr rlrrqaaahs ltptqfatla averhsgitp
       61 gelaelekvq ppsmtrviaa leerglvsrs phpsdrrqvt vsvteaaqkl lkeerrrkea
      121 wltqrlkelt peertilrqa apileklsri
//
LOCUS       WP_357604147             406 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357604147
VERSION     WP_357604147.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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 406)
  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..406
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..406
                     /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=45307
     Region          1..405
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mrrsfrfllr ptrkqqialt amladhcaly naalqerrda yrhpsktqir ygdqsaqlke
       61 vrdvdpdgqg rwsfssqqat lrrldkafaa ffrrvkaghk pgyprfrgvn wfdtvdfpkd
      121 gdgcrwdsqp ehpaatyvrl rgighvrvhq hrpvrgrvkt isvkregsrw yvilacdevp
      181 aqplpatgav tgidmgiahf lttsegehqp nprhgrrnad alaeaqralk mfpgrkrdnr
      241 sakhrravek vaklhrrvrh qrtdhahksa lamvgtydvi ayerlsianm vrtpkpkpdp
      301 dnagaflpng aaaktglnks ildagwgvfl gilthkaesa grklipvdpr nssrtcprea
      361 cghvsadnrp tqekfccvrc ghtdhadrvg alnvairagl vlpdva
//
LOCUS       WP_357604184             337 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604184
VERSION     WP_357604184.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,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..337
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..337
                     /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=37241
     Region          7..334
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 maigerilev rdlvkhfplt qgivfkrqig aikavdgvsf dlhkgetlgi vgesgcgkst
       61 lakvlmaler ptsgsvqing rdigkakgge lkrmrrniqm vmqdpytsln prmtvgdiig
      121 epyeihteva prgdrrkkvq ellevvglnp dhinryphqf sggqrqrigi arglalqpei
      181 ivcdepvsal dvsiqaqvin llerlqnefn layifiahdl svvrhisdrv gvmylgkfve
      241 lgkdteiydr pahpytqall savpvpdpdg reqreriilq gdppspanpp sgcrfrtrcw
      301 kaqeicaqee pllqvrpgtg hesachfaet hdvvhag
//
LOCUS       WP_357604244             296 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604244
VERSION     WP_357604244.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 296)
  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 296)
  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..296
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..296
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33563
     Region          1..>170
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mrvtvltpsf nradylpely rslmsqdvdl ewliiddgse dgtgevvrel eaqspfpiry
       61 rhqrnlgkhw alnhgvavae geviaqvdsd dlmcpgalrr llehwhdlsd prvigllghc
      121 vdesgrligt rfpadpidan wqemayrygv kgdksgifrt dilrshpfpe ipgyvaesvv
      181 wrrigqrylt rhvnedivvc rasaanritg rpfaeiasga klqhgitltd dmawfrarpa
      241 afyraavhys racfhlkepv wsrarefdia iskamvlggm plgwllyqrd vrrssr
//
LOCUS       WP_357604225             469 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357604225
VERSION     WP_357604225.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   ter Beek,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 469)
  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 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..469
                     /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=49418
     Region          1..464
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 msphavvdel tvatpdgrel lsgacltara gkvlalvgss gsgkttllra migdlppgta
       61 rtggsvrvlg ldvlgctaad lrelrrtrva yvgqdpgsal nprmrvgtlv tetgsrgeaa
      121 llleevrlpv vpgllrrrag elsggqqrrv alaralarrp dlllldepta gldpalrdei
      181 gellrhlave rgvavvlsch drelvdqlad evlelscagt ppragrtpav rqaaqqgagg
      241 lrargldahv garrlpvlrg vdldapsgaa vgvvgpsgsg kttllralvg lhpfsggsvt
      301 ldgvalhpnv rrrgreqrrr vqfvpqnpmg alnpsttvsa alarplrlhr rrpraavper
      361 vaelleqvgl gaehaaryph elsggqrqrv siaralaaep dvlvcdeits aldgdtaqam
      421 melltrlret remavvfash dlrlveryad svaliggqee rapapgerp
//
LOCUS       WP_357604276             202 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357604276
VERSION     WP_357604276.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 202)
  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 202)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15192454
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22300
     Region          9..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          16..>68
                     /region_name="septum_RefZ"
                     /note="forespore capture DNA-binding protein RefZ;
                     NF037937"
                     /db_xref="CDD:468281"
ORIGIN      
        1 mpedqlqats kaartreril daaldefsak gysgartaai akragvnvql isyyfggkeg
       61 lleelltswq krrsklvpas kaepflesfr mvlnatlrdp rrarlvvwqa lgdypgdtea
      121 larewrtvaa aaveqtrarq aageisdghp pefvtllsfl lafapvalpq vieeiydvdp
      181 lseeyrqrvs ealaafldvr ha
//
LOCUS       WP_357604284             165 aa            linear   BCT 28-DEC-2024
DEFINITION  (2Fe-2S)-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604284
VERSION     WP_357604284.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 165)
  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..165
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..165
                     /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=17318
     Region          1..164
                     /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 mrvngvvesl diepwvslld alrdhlgltg pkkgcdqgac gactvladgv rinaclalam
       61 qyadkeitti egiakdradt hpmqqafvrh dglqcgycts gqicsavaml aehaagmpss
      121 vtprqggtql tddeirerms gnlcrcgayn gildaikdva aqeap
//
LOCUS       WP_357604296             377 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604296
VERSION     WP_357604296.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=40441
     Region          5..343
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpassspvrv avvgaggiak achlpalaaa gdavqvvavs dvdpararel adaydiparh
       61 tdltemlaae spdlvvvatp pvahreavta aldagawvwc ekpptlslae ydeiaahekd
      121 ggpyagyvfq hrfgsaaqrl rrhigdgelg aplvavchtl wyrghdyfev pwrgkweteg
      181 ggptmghgih qmdlllsllg dwhevhavaa tlgrrveted vsfaivrfds gaiasivnsv
      241 lspretsylr fdftdatvev ehlygydnsn wrwtpaphvt dqdriagwap adntpsshra
      301 qlaallaalr agerppasga dgrrvmelit tiyqsaitgr pvaraeldet npfyrslngg
      361 dtpaaasrlk ckentha
//
LOCUS       WP_357604300             428 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 30 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604300
VERSION     WP_357604300.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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 428)
  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 428)
  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 428)
  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..428
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..428
                     /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=47224
     Region          7..427
                     /region_name="XynC"
                     /note="O-Glycosyl hydrolase [Cell wall/membrane/envelope
                     biogenesis]; COG5520"
                     /db_xref="CDD:444271"
ORIGIN      
        1 mneswpadpp aimiddevrh qtidgfgvst afrrnelira lpqdkqreil dlwfsrekga
       61 gltilrlgig sapagspydd mvsiqpedpg gpdappkyvw dgddnsqvwm akaaqeygve
      121 rffavpwsap gymkdngeek nggrlkpewq rayadylvqy trfyqqegir itdlgfanep
      181 dwtakhasmr ftpeeaaafv kvlgpmasdv rvvcceslgw teaqaytlai eadpearrwv
      241 rvysghgyat pvdgplptkr ptwmsewhpn gthwneswyd gsgfdgytia savhdaltlg
      301 nvsaylywlg astgstrall rideaegayh vskrlwalaa fsrfirpgav rieaaagvps
      361 lrvcafrnpd gsrvvevlnt glapvtwsgv setaevyltd anasldlrpv ldgvvtfpsr
      421 alttivlr
//
LOCUS       WP_357604344            1164 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing serine/threonine protein kinase
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604344
VERSION     WP_357604344.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11600203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..1164
                     /product="WD40 repeat domain-containing serine/threonine
                     protein kinase"
                     /calculated_mol_wt=123205
     Region          16..264
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,42,44,76,92..95,99,101,138,140,
                     142..143,145,154..155,158,174..177)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,42,44,76,92..95,99,140,142..143,
                     145,154..155)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(26,99,101,138,140,142,158,174..177)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(38..39,68,73,78..81,93)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(154..161,170..177)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          458..837
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          617..662
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          681..734
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          721..1120
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          741..776
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          779..805
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1025..1059
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 msnplidgdp qrlgaywlag rlgaggqgvv yeaydqagtr vavkvlrgdl agqkelrgrm
       61 arevvaaqrv asfctarvlg adldgprpyi vseyvegasl reavtggrrf agddlhrlat
      121 aiataltavh dagvvhrdlk pdnvllgpdg prvidfgvar tqemsltttg vvagtpgyma
      181 peafsgervg paadvfawga vvlfaatgad pfsgeslgav mhrvlshepd laalpgslrg
      241 lvraalakda arrprsrell lgllnadglt vradgsavra dglagpdgaa getarllarg
      301 addggrlgvp gddpalgvia edayaalspa drelvpdvfl rlvtvtedgf lmprearrae
      361 lpgdadrvla afaylvsavd ggerlrllrp alplawprlr awiaanrdgl sihrqiwtaa
      421 erweergrkd adllhgssld dalrwaaaer rnitltpaer dfleagaalt rrrsrrtral
      481 aaglgvllvv slvagglavr qsvtlaeqge tlawqrdtse sarlagvaes vrgrdpvlam
      541 llsaaagrls ptaearsslf asladqatga fhdpatgpdv aralsadgrt lvsvspgear
      601 iwdvatgrrt ggftgalttp grpaarlrqv avsedgrlla vadtkgvalw nlatgarvgp
      661 rvpaaedfdl evsfsggllv idigqgkiir dprtgrstml peldkvavhp ggdyvvaggk
      721 rwalpsgkal pgfpgicsdc atrpsfsrdg rrlaigddrg ltvfdtrtre elvffenwgr
      781 kvapvfdrdg rmlaelgttl rlydvdavep lmyertppel ataigfgpdg vrylsgdtvv
      841 tlppytveae pvdeaeldps grllashmlk asdvrladtr awdaararta gralaagpsa
      901 pydseltfsr dgrrlalrrs advvvwdtat ggelarvplt gntdgalpgp aglwtaeakt
      961 ftlwalpggr rlkqvsrprl sgwtvtargr lvgldadrlr mvdlesgqpy gprlpfpgat
     1021 edvwfdadak lvaadfagkv gvwdtrtgaq vgdwlrewea pwaaafspdd rlfafasqnk
     1081 tltvwdvgrg qpvgpvvrlt dsagsvvftg dsaevvaigr karltrlpva vgplieavca
     1141 rggrsltaae warylpgray rpgc
//
LOCUS       WP_357604424             371 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357604424
VERSION     WP_357604424.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..371
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=40708
     Region          46..247
                     /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..350
                     /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 msgvrvlvgt rkgaftltsd grrgdwtvdg phfggweiyh lngspvdpdr lyasqsggwf
       61 gqliqrsddg grtwnpvgnd fayagevgeh lwydgtprpw efkriwhlep srhdpdtvya
      121 gaedaalyvs tdgglkwqel talrthptgp twqpgaggmc lhtiildpan kdriyvaisa
      181 agafrsddag aswlpinkgl rsgeipdqda evghcvhhit qhptrpdtlf mqkhwdvmrs
      241 ddaganwrev sgnlpsdfgf piavhahepe tiyvvpiksd sehfppegkl rvyrsrtggn
      301 dwepltrglp qsdcyvnvyr damavdtldp cgiyfgttgg qvyhsadggd swapivrdlp
      361 avlsveaqvl p
//
LOCUS       WP_357604370             262 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604370
VERSION     WP_357604370.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,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 262)
  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 262)
  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 262)
  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 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..262
                     /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=28426
     Region          1..262
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 mvrtyflllw twtraaaayp vsfalmivfg vvtasldvav ilivfanttt lagfsrdevl
       61 flygtagvsf aicdtfvsni drvsqhikag tldtilirpv sawvqlttdr fvpgrigril
      121 qsvivlgyai aaldldgrra wmipvmvvtg vvifaalwtl agamqfvltd apevsnalty
      181 gsaqlnqypl siyardlvra vtyvfplafv nwqpglyvlg radpfgtpel mrfagpaaal
      241 vlallaglaw rqgirhyrst gs
//
LOCUS       WP_357604439             414 aa            linear   BCT 28-DEC-2024
DEFINITION  YncE family protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357604439
VERSION     WP_357604439.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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..414
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..414
                     /product="YncE family protein"
                     /calculated_mol_wt=44298
     Region          <284..379
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mtrisrrtll tvlagagtaa lvgcdrarhp gqaravtipd pllvevddgl gllrgadrrt
       61 fprslatadg raiyatapeg adtalwridt atggtstrvk lpgrwvpqav sangtvalts
      121 tevnatkgrp kgrdvtpvli advtgvrhrl elrgnfvpet ftadlaglfv lewlpatapd
      181 ryrvrvvdla tgtpgplhtr akapvppgae eemrgdgrqa vlspdrttly tlythqpdhq
      241 htrnlvsgrp gnvhafvhtl hlyerwayci dlphpfgaaa aighamtisp dggrlfvadv
      301 tsgttaeidt eelrvrrtdt qprrvgtaha aadrdrlfig agtvvrtmdl trpgraadwr
      361 vrepvsglvl srdgrrlyvg qnagvswhdp gtgtelgrva vprlvgvhgl agra
//
LOCUS       WP_357604495             118 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604495
VERSION     WP_357604495.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=12940
     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 myardnvsga nqsqeqptaa qvnaavdafr mlsdgtrlrl mwllssgeqd vnslaqavgv
       61 prpsvsqhla klrlaglvdt rrdgrrvlyq ardshvwali aealfhadhe lsgrprhd
//
LOCUS       WP_357604513             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357604513
VERSION     WP_357604513.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32448
     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          99..287
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtedvgstvp rrqlgrllrq frteagvtld aaaealeysr qkiwriesgl gpvrvldvka
       61 mcelyhvsae mteamrglaa etkskgwwha ygdavpswfe lyvgleaaas rlrgydesli
      121 pgilqtkeya hslyrlgrtl sdeereravq vrlqrqallm rrlpaaprle svlseavlrr
      181 tvggpavmtv qldhllklse lpnvsvkvlp laagpqpgav agtfmildfp ptkggraape
      241 psvvyseslt galyldkpde laayervwkg ldalalgeae skdmikritg etrhd
//
LOCUS       WP_357604526             531 aa            linear   BCT 28-DEC-2024
DEFINITION  GTPase family protein [Nonomuraea dietziae].
ACCESSION   WP_357604526
VERSION     WP_357604526.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 531)
  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 11466459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..531
                     /product="GTPase family protein"
                     /GO_function="GO:0003924 - GTPase activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /calculated_mol_wt=56958
     Region          10..325
                     /region_name="YeeP"
                     /note="Predicted GTPase [General function prediction
                     only]; COG3596"
                     /db_xref="CDD:442815"
ORIGIN      
        1 mkllrrkegp slddrltall eaarlaegrl pqelvaqare vseragerrs lsvdhtvaal
       61 agatgsgkss lfnalagrdl atvgvtrptt staqaalwdg egagalltwl dvphrhevea
      121 egdlpglvll dlpdhdsiel thrlevdrlv elvdllvwvv dpqkyadaal herylrplsr
      181 hsevmvvvln qidrlsatqa ercladlrrl leedglagvp vlgasartgk glpelrglle
      241 ervsrrrswa erlsadvsta aarlstagde avsvgtpdga rltralseaa gvplvvdava
      301 kahthravaa tgwpmtrwmr rfrpdplrrl gigsgprgei vgrtsvppps avqkarmeta
      361 irdvgeaaar dlpepwatav rhaarshddd lagaldrvva trsagaarrp rwwavigglq
      421 wmvfaatvlg avwlsvlfvl tylrlpdppl ptvvevpwpt vlliggavag vliallsria
      481 awagghrrar kvakalregv gevggrlvlg pvseeldryr sftealgvar s
//
LOCUS       WP_357604581             240 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357604581
VERSION     WP_357604581.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24714
     Region          13..235
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtrttvvtgg gtgigkavaa rfaadgdrvv iigrradvle eaakeiggta laadlsepte
       61 vervradlae rfgtidvlvn naggnvemqd gsggvaerwt gnfranvlts vlptealrdl
      121 lnpsgrivfm ssiaafrgsg gtsygpmkaa lhpyaadlaa dlgprgitvn vvapgfiedt
      181 effsgtldde rramlvaqta tgragtpqdi aetvhwlasp gaghvtaqii qvnggaergr
//
LOCUS       WP_357604584             679 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea dietziae].
ACCESSION   WP_357604584
VERSION     WP_357604584.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 679)
  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 679)
  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 679)
  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..679
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..679
                     /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=73938
     Region          13..679
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpghqlapdi ptdvlaaera hlsesrealr amrkhaqsls sdaagdwvsq qilqslldqr
       61 vaaladhpdt plffgrldra teeeladnle rrleagdelp atiyvgrrhv hdggsralvi
      121 dwrapvsraf yqaspsdpmg vvrrrrfgyq ggdltafede plaeggelgp skiltqeier
      181 prtgpmrdiv atiqpdqdei vrsaltqtvc vqgapgtgkt avglhraayl lfthreklar
      241 agvmivgpnk aflsyissvl palgevkvdq ttvaellgsy daperpevaa akgdarmakv
      301 leralwlhiv kpteglvytk gvhrfrvady evremvaslr gttrygpgra alaqrlahqv
      361 lvrmeqrgds pddrvqdava rskpvkqlve svwpkltpaq vlhrllsdpd flaaaarsdl
      421 sqeeqellvw srphrswksa kwsaadaall deladliert pslghlvvde aqdlsemqlr
      481 algrrcrngs atvlgdlaqg ttpwstrswk svlrhlgqea gevteltlgf rvprevldya
      541 aqllpsiapd laaprslrpg lgslsvrqdg qvleavreal tregsigviv pdslvetvsq
      601 elaglphavl gpdsteehrl lvipatlakg leydhvivve psdivaaepr glarlyvvlt
      661 ravssltvlh akplpaqla
//
LOCUS       WP_357604616             106 aa            linear   BCT 28-DEC-2024
DEFINITION  putative quinol monooxygenase [Micromonospora purpureochromogenes].
ACCESSION   WP_357604616
VERSION     WP_357604616.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=12445
     Region          10..83
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mttvrtvlam rtkegceerf eaewrsaaek iraldgclkq dlvrdaddpr syliisdwad
       61 rerldafgrs ehrdrllqmi relresaqrh tyqvlhsvrs epeesr
//
LOCUS       WP_357604625             253 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357604625
VERSION     WP_357604625.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  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..253
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..253
                     /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=27895
     Region          20..249
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mdqsspgvap vqhapaevgl harvldhlgt aicggevaag svlniddlve ryavsrsvir
       61 evlrvlasmg fvetrrrvgv mirpaeawnv fdpqvirwrl asagrmaqmr sitelrtave
      121 phaawlaagr vdhdeasdlv glaakmwaag kagdegrfls ldiefhrrvl vasgnemfvk
      181 lqelvaevlt grhhyhlmph ypdeqalqlh advaqaiqrr dgerarqamv rimeqafdem
      241 ksmweqtgep gqg
//
LOCUS       WP_357604632             314 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357604632
VERSION     WP_357604632.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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 314)
  AUTHORS   ter Beek,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..314
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..314
                     /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=34815
     Region          13..290
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matvttrtrp hdasatpdtp gwarwandhr kwlfaapamv fvaaliifpl awtgylsltd
       61 aegsvraese fvgfqnyvev lsdterfwpa vgrtaaftvv allfevvlgm avalllwrpf
      121 rgqkwvrvai lmplvatpva vgmmwrlifd pnigmanqvl gwfgigpqpw lagqhsalpt
      181 tifidvwqwt pmvvlillag ltslsdepqe aaridgassw qrfrhvtlpl vmptvivail
      241 lrgidalktf dilyatkgrg ggsfhevetl nvyayglsfd yneygisstv liiffliiig
      301 smwaltsrrk eaqr
//
LOCUS       WP_357604680             172 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Nonomuraea dietziae].
ACCESSION   WP_357604680
VERSION     WP_357604680.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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..172
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..172
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18237
     Region          48..161
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mellaaavvv vgllsmanll lmvgvirrlr klatqaefgs pmmdgllvge rmpeftamtt
       61 agepvthelv sgpaliaffs pgcppceell prfiararrs ssqafavvva dpgedvaekv
      121 erlrevarvv veppmgdlqr afkvqgyptv yvidadgtva gtsldaqvlv es
//
LOCUS       WP_357604740             195 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604740
VERSION     WP_357604740.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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 195)
  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 195)
  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..195
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..195
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21105
     Region          1..191
                     /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 mtwivfdygg vlslpqpesd aeamaravda dpddfkrgyw ehrlefdrag lsplaywsav
       61 vgrpvtqtev arlvamdvas waypdegtva llgeligagr nvallsnapv cvgdgldelp
      121 wiaaigrrfy sgrmglvkpd reiydelvra ldadpskivf iddreenieg aeragltgvh
      181 ftdaaalrga lsral
//
LOCUS       WP_357604792             440 aa            linear   BCT 28-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Nonomuraea dietziae].
ACCESSION   WP_357604792
VERSION     WP_357604792.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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..440
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..440
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46844
     Region          15..415
                     /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 msdrsvlqki lrdlrnplfr ngyalmantg itavlgmgyw llatrfytpe efgsgqalit
       61 amrlfaslta lgfvgalary ipiagrrtad vilrgygmaa atggvaaigf lltlpmwgei
      121 ysvlgglghg lfflgavlvw svftlqdval tglrqavwvp vnnlvfglvk mgllvalags
      181 lpeggifvsw viptaialip vnflifglqv pkhvretage arppglremg rflagdfpgt
      241 lsmlaivylv pvliaarvge atfgrfsmah tlgcmiella mnmaisltve gsfdrsrlaa
      301 narqalkral liitpiigva claaplilav fgsefategt tllrlmalav lprvlievyl
      361 sslralgear klamvqigla alvlvsimal fpfvgvnsvg ygllfsellv allifrslrk
      421 vlkggetgrh rvtqrsseaa
//
LOCUS       WP_357604757             177 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604757
VERSION     WP_357604757.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 177)
  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..177
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..177
                     /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=18384
     Region          1..156
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkiigiaagl hagsfinkll eaaggelpeg vgfsvwsglg eippyargpv pasarglirl
       61 vtasdavllt apehsllpve ltyaldwmsa rdglsgkhva visasaracg amwaqaelyk
      121 rlqaagavvm gdelvispac rhfdedghlm dpalraqvra vigrlcpaev mepalll
//
LOCUS       WP_357604826             169 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Nonomuraea dietziae].
ACCESSION   WP_357604826
VERSION     WP_357604826.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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..169
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..169
                     /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=17437
     Region          <26..156
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mtrkrpalaa vllfccmgsg yesvnageqa lnaalemrgv pyswggggan gpsfgigrga
       61 ttvgfdcsgl tqyawaragv rikrtargqw rngwpvpegq vrpgdlvfyd snpvspgpeh
      121 vgiavdgeri vhapstggfv tfaplvrrgy mgaarpaeta pttseaaag
//
LOCUS       WP_357604852             970 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357604852
VERSION     WP_357604852.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 970)
  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 970)
  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..970
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..970
                     /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=104916
     Region          255..>820
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mgdyrltqlg tsefehmsqs llaaligasn vkvygagrdg grelttdavf eieeglqwsg
       61 ytvaqakfra rpgstdanat wlrsqirael qdwispianr rpkpdnllfi snvplsavpg
      121 hgldavedvf gdfadrlplk ayavwhydhv crlldsypgv raayagllts gdvltelrqv
      181 llgevinige vlhrhaakel vaeqwvrlge sgsraheklq igqvgvdlqa lpavgdtdpa
      241 srpiqvlehm ivagdgvlrp siyegpephr vlvggpgqgk ttvgqllcqi yranlisdld
      301 sigpqaagvv ttlrqhlaas glpipinkrw plrldlsgya dvlggnptts vlrhlasqis
      361 drgadtitag qlktwlsswp wllvldgfde vvapqvream idriadffid aasvdadlmv
      421 iattrpqgys aefspdqyqh lhlmpltsgq aeafarklad vrlgddpdah anvlarisea
      481 ardpltarlm vtplqvtims lllegrarvp qdrytlfady yrtiygreva kntatarlle
      541 rhrrtvdqlh eqvglrlqiq aetsgkadaa lpnrevqtla rqildkedhp veeaqrlaeq
      601 iaaaattrlv llvakhaddv gfdvrslqel maaralttgp ddgimarlra ialsahwrnt
      661 fllaagrlat drrhlvdail vlledldtss yltmylhpaa glaldllddk faapsprvem
      721 klvrkavevl qsppivgfld aadilqratl tgsallgpfi advaktslaa dppqritaai
      781 mmrrwargtg alaalgrqrt agdfaefgsd qaavirahyl trsvaprvkg mpgrprrgga
      841 aatrggaaan tganrchqtv agyfrtgged vavsaifdpe dgrawddilq tfdgiavtsv
      901 gskpmpaikq pryhratlar alnrpavanh laqrllaldp ddwavastva diiknvlqsr
      961 paggalgsqy
//
LOCUS       WP_357604871             149 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357604871
VERSION     WP_357604871.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=15960
     Region          4..121
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mishlpvrpr hcdaqammha aryyeyfeda fldwlgargg ydrlreqgad lvvkasgceh
       61 haparlgdvl avesaparlg ttsitmtftm rradelvavg tvtyvcvrdg raaplppmlr
      121 epawppaata pgtpapstaa apppawprt
//
LOCUS       WP_357604909             411 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357604909
VERSION     WP_357604909.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 411)
  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..411
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..411
                     /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=44315
     Region          21..407
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtqqrpfviv gaglagaraa qtlreegfdg rivlfgeete rpyerpalsk glllrtserd
       61 svyvhdagwy adhdvdlrtd trvtaldrrs rqvtvadgqr fpydrlllat gsrartlpip
      121 gghldgvlrl rtladsdris dalvdganvv ivgagwigle vaaaartrga tvtvvetadl
      181 plrrvlgdql atvfadlhra hgvtfhfgtq vhefqgsnrv savlladgtv laadlvvvgv
      241 gvqpntelae qaglavdngv lvddtlrtsd pdiwaagdla nahhpmlgtr vrvehwanal
      301 hsgpaaargm lgqavsydrl pyfytdqyel gmeytghapp gsydrvvvrg eltsgefiaf
      361 wtaqgrvlag mnvnvwevtg pigqlirsrq pvdldrladp tvaldslirr g
//
LOCUS       WP_357604919             508 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357604919
VERSION     WP_357604919.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 508)
  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 508)
  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..508
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..508
                     /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=54203
     Region          6..499
                     /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(161,164..169,171..172)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(164,279..280,301..306,388,400,403,414,492)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(164,205..206,253,255..256,259,279..280,301..306,388,
                     400,403,411..414,473)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(205,255..256,259,279,411..413,467,473)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 maqlslatvl aesarrrpah paivcgderv tyaelwaqtr gyaaalaerg vrpgdhvalm
       61 aanvpdfpra yyailslgav vvpihlllta eevafvlrds haralvhggg dpaaaekaae
      121 lagipavpld padadslaaa aarlaprpgl vptapddpav vlytsgttgr pkgavlthfn
      181 ltmnatvnaf ddlgvrrddv llgclplfhs fgqtaamnta fraaatlvlq prfdpvqale
      241 lmvahgvtaf lgvptmyial ldaarrgapr pslrlcvsgg aslplsvlde vaatftttvy
      301 egyglsetsp vattnqptfg trpgsvgcpi wgvdvevara dredhvellp pgeigeivir
      361 ghnifagylg qprataevlr dgwfrtgdlg trdeagfvti vdrkkdliir ggfnvyprev
      421 eeallrhpai gqvavvgvph pthgeevcav vipaaevtad eiidwareqv grhmyprrve
      481 fvdefplgps mkvlkrelrw rfaqdrtp
//
LOCUS       WP_357605006             330 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357605006
VERSION     WP_357605006.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 330)
  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 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   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..330
                     /product="GlxA 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=35882
     Region          12..328
                     /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 mrnnramtiv phrvavlaid qvvgldlgtp sqvfgtartk dlrplytvda ctpggrpvrs
       61 tagyqvlpdh glelveaadt vvvpgihggp altdgildpe vaaalraahe rgarimsict
      121 gafvlaaagl ldgrratthw ayadlfrrlh pavdldpdvl fidsddvlts agvaagldlc
      181 lhvirtdhgs evanrsarrc vvppwrdggq aqyierpvph ragtgtagtr ewarqrlhep
      241 vtlrdlaeha rmsvrtftrh frsetglspa qwllqertdh arlllettdl tvdqvahrcg
      301 fgtaaalrqq lrqrigvaps ayrrafhrhp
//
LOCUS       WP_357604965             759 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357604965
VERSION     WP_357604965.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 759)
  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 759)
  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 759)
  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 759)
  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..759
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..759
                     /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=80353
     Region          91..752
                     /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 mlpddarrea vapprptrar rvgavaaalv vlveavwlta alpgaalagd vgaitvagws
       61 tvacvgaarr hpatlrrfwt llavtmalaa agrtlwtvqr lggetlphtp ligaiftagi
      121 ltgtaallcs laaprsavgr artlldgviv alalipigwv vvfrdiadad ladplrtfgl
      181 lypmldlmql tilvavagps rpiwrpltli gaslatraga davyvslvah ntyapghvid
      241 vcwplsylli gvattypppp vgeggdegie splppwwrva lpylpvggai iavvlarhpt
      301 gqtphlvfig mmallgalal rqglaanenl rlvarlrrla yadqltglpn rlmfnrrlrr
      361 alrdgppvav llldldgfkq vndrfghatg dtlltsiadr mrdavgddgt iarlggdefa
      421 vlvdgdgpva perlaerlla alqpsageed vgihpsasig iaeygpqhas htdllrdadi
      481 amyaakaagk sayrtctpgl resavtrael iadlrravde qqlhldyqpi vdlatgavrs
      541 aealvrwrhp rlgllgpaaf lplaeetgli vpidrwvihe acraaatwre rapeatvavn
      601 iaaahlrrpd liatvtaata saglapralt leltesalid gseavlerlg qlrelgiria
      661 iddfgtgyss lsylhripat elkidrsfvs rldtdaraya tvemvtrlag afdlavvaeg
      721 veteeqhaav taigcvhgqg yrygrpgrla dlhpvsapv
//
LOCUS       WP_357605024              67 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357605024
VERSION     WP_357605024.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 67)
  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 67)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 67)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 67)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..67
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6911
     Region          1..67
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mststyvvqg mncehcvnsi ttavgeiagv tdvlvdlptg kmdvtghstl dddlirqave
       61 eagfqva
//
LOCUS       WP_357605061              90 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357605061
VERSION     WP_357605061.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 90)
  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..90
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..90
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10330
     Region          <2..82
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 miealgertl rfselrdeve gishkmltqn lrmlerngla erkvhptvpp rveytltepg
       61 qalratvdli cgwthqyfgh ietarrrfda
//
LOCUS       WP_357605178             552 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605178
VERSION     WP_357605178.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 552)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..552
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..552
                     /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=55951
     Region          1..268
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtsptptqap shalgwllav palfgtlitl vlptvqtiwl slqsggvlte shfvgvdnyh
       61 elartgqvwr alwftlslav vpllvavvva pllafaldra gawprragri alslavvtfs
      121 pvgvaaawlr gllpeasgla glaqglrepa tapgalrliv aaatfgvvca lavmaflpal
      181 ragtvagapg aggggvasgm lvvgtllait mlavglqafs mglvltrggp erstetlagl
      241 qydhafraaq fgpgasvatl tgvilgvlgi vavvivavsr ltitltprat paaeegdeea
      301 aerghgpvgv avgvaalvvf vavalvcawp widgvlaspd spagtlraqv ntwvpavaga
      361 ivsvgvayla algigglrpl grgsewlllv fapwlfvgpg plgvanwqnv rnmglidsfv
      421 alfppllvsv pallvltllc kglaertdkd ffsgvflpsl pmagilagav alvnaqdllw
      481 pllvaqkpal ytspvaqlsq lggfsaaspd agaatplivv alaliavaaa qllyldrlvi
      541 ttkgsrprtp aa
//
LOCUS       WP_357605189             142 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357605189
VERSION     WP_357605189.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 142)
  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 142)
  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..142
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..142
                     /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=15395
     Region          <32..136
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mrddptrlae qvstvlrhlv lllrrtvagq pvtsqqyavl gslehgprrm telaeehavq
       61 lptmtvqinr ledaglvarg sdpadarvrt veltgegrdr llavrraria hlsqelaalt
      121 dderatlaaa lpvlaklgsn pr
//
LOCUS       WP_357605260             353 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357605260
VERSION     WP_357605260.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..353
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..353
                     /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=36845
     Region          1..333
                     /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(8,10,169,189,258)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mpglwdchth lfgapdldpa rvltvspelr aarcvpdlra aldagvtsvr elgglgvhla
       61 pavaegsieg ptiyasgavl sttrghgdlh slpihwvsel sdfrladgad ecvratreql
      121 rknarvikic asggvlsevd hpihqqftva emravvevas maervvaahc hgkpgmmaai
      181 eagvrtiehg tyldeevada mretgtvlva tctvidelmt agglppvlmd klkavaevha
      241 gavalahsrg vrlamgtdiy vsgrgkpnsw grngrelahl vgcglsplea iraatahgpl
      301 tlgaqaprsg vlaegydadv itldadpldd itamsdpdhv tgvwkagrrv kga
//
LOCUS       WP_357605271             427 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357605271
VERSION     WP_357605271.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 427)
  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 427)
  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..427
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..427
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=44048
     Region          <16..216
                     /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 mhisahldvd vlaletddql svlveltapt asardaarpa stlqvvldrs gsmargrldg
       61 aktallglid kldpgdnfgl vafddrveva vaagpladkp avkraiatld argstdlsag
      121 ylrglqeaar vagpagatvl lisdghanag vtdpdtlggi aakahadnis tstlgyglgy
      181 derlmsaiar ggagnehfae eadtagalia gevdgllsqa vqaaslliqp sphvravqia
      241 ndlpvtttgd gllaelgtfy adetrkllit fdipaiatlg laqvatcqft wvelptlaqh
      301 sltvplhvnv vpgdqaagrv pdptvrtelv ylqvqrakrr asghlsasap daalaeirqa
      361 qdalshalpv apahlhddla eeatalayla dqtehgmvar aakyssmdaa yksakrgrtr
      421 ppssgpn
//
LOCUS       WP_357605295             295 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605295
VERSION     WP_357605295.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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 295)
  AUTHORS   ter Beek,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..295
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..295
                     /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=32740
     Region          2..290
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 maasplvrre arrfhlfalp wtigfvfftg gpivvslvls ftryellsvp ewvgldnyvq
       61 llrdpdfwva trntiyfgaa satagvvysl aaalllnvkl rgqaifrtii ympsvisgia
      121 tallwihvlh pdyglvnyli gllgvqgpgw ltdaswaipg lvimttwttg namiiflagl
      181 qgvpvslyea ahidgagwws rfrnvtvpmm spviffnlvv gfigslqayq lilfmtdggp
      241 anstlvlgly vyryafkyfe mgyastiawa lfflvivftv iqfglarrwv hyevk
//
LOCUS       WP_357605391             293 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357605391
VERSION     WP_357605391.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 293)
  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..293
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..293
                     /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=33149
     Region          <20..292
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mravaadtap psrrvrgvlg qavryprfks krksrasaef trsafrwrdg rltlakmgtp
       61 lnivwsrplp egaepstvtv srdaagrwfv silvedptve plppvdaeig vdagitsllt
      121 lstgkkitnp ryertdrrrl akaqrdlsrk ekgsnnraka rmkvarihar iadrrrdhlh
      181 klttrlvren qtvvvedlsv rnmlrnhrla rvisdaawsd lrrmleykaa wygrkmipvd
      241 rwypssktcs acrrinttlt lgvrawtcpg reaehdrdvn aarnilaagl aer
//
LOCUS       WP_357605436             657 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea dietziae].
ACCESSION   WP_357605436
VERSION     WP_357605436.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 657)
  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 657)
  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..657
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..657
                     /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=66896
     Region          66..546
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrfrrlivcs illallpaap alageppsts aptasappes tppaeqpsse qpspeqpspg
       61 rpeekleegl avaegtsrvi veltdaaqta pvaaqaaaqd aqvvlqpetq paaqpfivve
      121 gtaeelakla edprvasihr draypptais slpvigadkv haegrtgagq availdtgid
      181 rdhpffggri vaeacfsste ydgveslcpn gqsqmtgtga adseyakclv ggenlcehgt
      241 hvagiaagqg gvapgasiva vqvfsrvnde dacgaaaclm afesslrlav dhvaslapat
      301 piaamnlslg gqlsdtscdt seegqvfkpk iddllakgva tvvaagneyf egttfpacvs
      361 savavgasdn gdhiadfsnt gplldlfapg vdiessvpdd amathsgtsm aaphvagala
      421 vlkaafpdqa igalveklkt sgrpfsyqag gvqvttprld laaavsgaap qptvsqsgpa
      481 psesgpspep tdedpqsedp rsedpgesde pdptpiplpt vtvtvtvtat ppaapssvct
      541 rgtagtrmta kewavevyrg tgqlsdetlt cylklahkts kvfpeltkas slgkayrvlk
      601 apkgarakld rallaawlnw ahgatstlap vqaaekvrlt akassaslkk ataalgr
//
LOCUS       WP_357605500             231 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357605500
VERSION     WP_357605500.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 231)
  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..231
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..231
                     /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=24209
     Region          5..227
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mplgslrpsp lveqatehlr eqitqgewpv gtrlpgenal akalgvgrst vrealralag
       61 aglvqarqgs gvfviatepa edwparlrra aiadvyevrm mvetqaarla arrrtdedva
      121 aleaalaara gaatgddaaf vdadialhra vvaaagnpvl tdlfaefapa lrgglidlve
      181 vlglrshdrn pghdthaalv sairrgdgda agdilqeele qtlahlhgnr s
//
LOCUS       WP_357605524             304 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605524
VERSION     WP_357605524.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  AUTHORS   ter Beek,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..304
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..304
                     /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=33725
     Region          29..302
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtatvtrpap prgtrrarrr vsrqtremwl lmlpalvpva lfsvgpllyg ialaftdarn
       61 srvhetsfvg lenfgrlltd defwssfkig aiwsvsvtvl qflaalglal llnqnlrfrs
      121 varvlavvpw amppvviglm wklvyhpdag ilndllgtdv nwladfslal paiivvgvwt
      181 gmpqttvvll aglqgvpkel yeagevdgat rwrrfwnitl pqlrpvivai tsldfvwnin
      241 qfglvyvltq ggpggqtrlp mlfayeeafr yrmagyasml glamaivvla vlglylwrqm
      301 reak
//
LOCUS       WP_357605528             287 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357605528
VERSION     WP_357605528.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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
REFERENCE   4  (residues 1 to 287)
  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..287
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..287
                     /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=31520
     Region          25..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          190..272
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mthdwsrywr spdrpleamh ahfvrhvyhr hshdtysfgv tedgaqafkc rgsahtsaag
       61 mvmafnpddp hdghaadqlg ftyrilhigt elvadalqdt tgrrtglplf aepvlddpll
      121 arslhalhla llggasalrr dellratlaa marrgsrsfg svearlpaag gtaliaervr
      181 srlndshldd ltatdlaesa gcsrftvyra fhavygmaps dyqrqlrlrt arrliteglp
      241 lgevaaqagf adqshltrwf trtygvtpga yreaahpepf revtggr
//
LOCUS       WP_357605571             380 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357605571
VERSION     WP_357605571.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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 380)
  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 380)
  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..380
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..380
                     /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=40175
     Region          4..380
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtqttigvgl vgyafmgrvh sqawrnvaaf fdlpvtpvma alsgrslsaa tdaaarmgwa
       61 avetdwkelv nrddvqivdi ctpgdshaei aiaalqagkh vicekplant vaeaeamvaa
      121 aaasqgrsmv afnyrrvpav alaqrmvaag elgqirhvra qylqdwivdp dfplvwrlqk
      181 dkagsgalgd igahiidtaq fvtgqtivgv saltetfvke rplasassgl ggsrtsekgt
      241 vtvddaalfi grmsagalas featrfatgr knalrleing slgslafdfe amnelwvssg
      301 dsgfrrvlvt epdhpyvgaw wppghglgye htftheikdf leavgtgsdp spsfadglrv
      361 qrvlaavees aasgsykeia
//
LOCUS       WP_357605596             362 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357605596
VERSION     WP_357605596.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 362)
  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 362)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 362)
  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..362
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..362
                     /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=38110
     Region          141..362
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlrwarlatl atlgmtvlts lvmpgvgllr epdpllvvlg algivlfaaa lagvlyaavt
       61 psvdpgvrrr vfaaatmasi plagplavpd wqtwawiggs vfatapmltt rrwpalavma
      121 aataasagva lwvgdqvrpy vaitvilgls tltisglqvw lwnllieaqe graaqarlaa
      181 veerlrfard vhdvlghdls vialkaelae rlvslapdka aqeaadlrrv aadaltnlra
      241 avhgyrevdl aaqltavaqv lrssgvrctv tgpdrelpre vavqlatvlr eattnilrhs
      301 tagwceiais gtrmtvtndg agqaapdrhs sglhglrerl aevggalrts vegdvfhlev
      361 tl
//
LOCUS       WP_357605623             306 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605623
VERSION     WP_357605623.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 306)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..306
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..306
                     /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=33798
     Region          17..301
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtttvaapta aapvteakvr rgwtqhgmlf vapflliyva flvwpvllgl rmslssvnva
       61 gtnnhfvgfa nyaeafsdpl mwhslwntvv ftvlstvplv flglvfalla hnlrfvqwlw
      121 rlsffgpfll psavvailwl qmiyppgygl ingtlgtdip wltdtstaml svvlttvwwt
      181 vgfnfllyla alqsipqhly eaaaidgasa whrlrsitlp llgrttaliv vlqllaslkv
      241 fdqiylmtag gpqnstrsii eyaydmgftg yrtgyasavs yilfvliviv slvqlrlfrk
      301 raevss
//
LOCUS       WP_357605625             387 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea dietziae].
ACCESSION   WP_357605625
VERSION     WP_357605625.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..387
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41832
     Region          3..382
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mseellrela prvlgvlvrr ygqfdaceda vqeallaaat qwpkegvpdn pkgwlvtvas
       61 rrmideirse earrrreaeq aleeppavpd qddtltllfl cchpsltpas qialtlravg
      121 glttaeiaga flvpestmaq risrakatik kagatfeltp nrldvvlhvl ylifnegyta
      181 tsgpdlqrad ltseairltr tvrrllpddg evagllalml ltdarrtart gpggslvpla
      241 eqdrslwdkd liaegvelvt galsagplga yqlqaaiaav hseegetdwp qilalyella
      301 riapgpmvtl nqavavamvr gpleglallg tleaeladhh rlhavrahll emagrhgeag
      361 aaylraaelt sslperryle ergrprs
//
LOCUS       WP_357605629             281 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605629
VERSION     WP_357605629.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=31720
     Region          50..227
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mnwqrtmnra lvrftgfqie rvgkapsspp apeirppadp ltdrlleapv fllspvrsgs
       61 tllrailnah salhaphelh irrlrvqfdt klaskamaal ghnqadlehl lwdrvlhrel
      121 vrsgkrfvvd ktpanafahq riatcwpdar flfllrhpas iaaswheasp drrtpeaaal
      181 dalrymkavq rarsalpglt vryeelsaep ervtreicaf lgleweprml sygeqpvlek
      241 glgdwrekir sgtvqpprel psedqipdvl kpicrtwgyv a
//
LOCUS       WP_357605659             513 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea dietziae].
ACCESSION   WP_357605659
VERSION     WP_357605659.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 513)
  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 513)
  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..513
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..513
                     /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=56140
     Region          107..>198
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
     Region          313..482
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkrlliplaa agltaaalaa paaaapswvt dplapkpada ystakfwlna ngaalrkaaq
       61 yhwdskdvtk lvkvsadqpd dgkpgivapt gaaktggkvk nvnlprtigk vffvdrkgey
      121 rwcsatsiqs rhrnlvatag hcvyehgrdv fakwvfvpgy yqgkapfgvf sgayaftayd
      181 ldtyddydgd fafvavhngf sltgsrevpk geftdwagdk wveheeiked eyktgfekyg
      241 tagpywskdf dvtpekvghd ykgektltkv evtekeygda apsttanvng eqyekigptp
      301 iskekyqelt klkadgkfpg klhaevsnga eiawyeshyy lkqwvksgkt vryfrdhyii
      361 gmakdagklg davggqgiaw nqptgqpvfv fgypadphpd gdkpytgvtp kycygktgtk
      421 tyqvnsfrve thqalkcslt ggsdggpwll kynnskrlgy vngvtslfhd qdgndrvdmi
      481 ssayfdgeta dvynkaqyae tkavvgpkge ilq
//
LOCUS       WP_357605188             817 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Micromonospora purpureochromogenes].
ACCESSION   WP_357605188
VERSION     WP_357605188.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 817)
  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 817)
  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 817)
  AUTHORS   Schneider,J.S. and Glickman,M.S.
  TITLE     Function of site-2 proteases in bacteria and bacterial pathogens
  JOURNAL   Biochim Biophys Acta 1828 (12), 2808-2814 (2013)
   PUBMED   24099002
REFERENCE   4  (residues 1 to 817)
  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   5  (residues 1 to 817)
  AUTHORS   Kinch,L.N., Ginalski,K. and Grishin,N.V.
  TITLE     Site-2 protease regulated intramembrane proteolysis: sequence
            homologs suggest an ancient signaling cascade
  JOURNAL   Protein Sci 15 (1), 84-93 (2006)
   PUBMED   16322567
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10145855
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..817
                     /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=86750
     Region          210..331
                     /region_name="S2P-M50"
                     /note="Site-2 protease (S2P) class of zinc
                     metalloproteases (MEROPS family M50) cleaves transmembrane
                     domains of substrate proteins, regulating intramembrane
                     proteolysis (RIP) of diverse signal transduction
                     mechanisms. Members of this family use proteolytic...;
                     cd05709"
                     /db_xref="CDD:100078"
     Site            order(227..228,231,323)
                     /site_type="active"
                     /db_xref="CDD:100078"
     Region          <703..817
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 msvispidtd afpgrggstt aprpegqpdg rgpdhewves sgpevvpara pglellgelp
       61 gsgyrqppgl vrradgqtcq ltrllylile ttdgrrtyaq iaaeltrrts rlvsadnvrm
      121 laevklrplg llrsadgssp iaprsnplla lrfrfvvsnp rvtrritapf avlfrplvva
      181 iilaaflasa gwvlfdkgla satyqafdep gllllvfait vvsagfhefg haaacrygga
      241 tpgtmgvgly lvwpafytnv ddsyrlgrag rirvdlggly fnaivavamf alwaatrwda
      301 lllviaaqvl qmlrqlapfv rfdgyhilad ltgvpdlyar ikptllgllp trwgsaeskv
      361 lkpwarvvvt iwvltvvpll lislvlivta lprvaatawr slqhqavllg vnwadgdaar
      421 igvgllsila islpllgtay llirlvrqtv rsawratagr rkhrmaafaa ggaliaalvw
      481 awwpdgtkyq piqphergav adavpiasrq dtaprvdrpl qvgqrrtvtt vwpstapppv
      541 edqkrlalvm vprhtapsds gtsapawvfp fnppaapgag dnqalavnte dgstlydvaf
      601 alvwatddti dnsnaayala scqdcqtvav afqvvlvvgp advvvpenis aavnyscqdc
      661 ltyalasqlv vtlpgelsdd tkarltalwe qieefgqnlq altpqqiqaq lesykaqila
      721 iisadpaasp apsqtpatva pesspamtpt pnptgtasat plptnsptmp ptpaapaspd
      781 gtpmqgttpp dptaevtspa ptteptssaa peqpptp
//
LOCUS       WP_357605666             404 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora purpureochromogenes].
ACCESSION   WP_357605666
VERSION     WP_357605666.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..404
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42871
     Region          3..404
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mgtadveavw riesarivaa ltrftgdfgl aedaaqeaaa qalvswplaa panpagwlma
       61 tarrraidai rrrtalqdry allaaapavd eeidpdkidd dvlalmfvsc hpvlspearv
      121 altlrvvggl sseeiarafl vpvptvqari trakktiaaa rvpfelpaag ehrerlggvl
      181 svlyvifteg statsgdrll rpdladeair lartlaalqp depevhglla lceltaarfp
      241 artgpdgspv lledqdrrrw dlpairrgla alaeastrgl gpyglqaaia athasapsve
      301 atdwdrivvl yealgrvaps pvvelnrava vamasgpaqa laivdelias nrlpgshlvp
      361 tvrgellarl grrpearael elaarlcanq rersvllrka aalg
//
LOCUS       WP_357605671             111 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605671
VERSION     WP_357605671.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=12621
     Region          3..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpddqlsltf aaladptrra ilarlaegea tvnelaepfd islqavskhl kvleraglis
       61 rgrdaqwrpc rletapldga aewigryrer wsdrfdrleq eirkiqrgeh e
//
LOCUS       WP_357605683             503 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357605683
VERSION     WP_357605683.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11467609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=54642
     Region          12..501
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 mptlsdlvvr htaldaadld wlhslvsdwq lladlsfadl ilwapllerr gpkvldepga
       61 ggdqgwiaia qmrpttgptv yhddivgtva akgerhlidt awnerricre gdpdwstgvp
      121 vreetipvrr alpngegrfl gviqrstnls sartpsrlel tylqsasdla qmvaegrfpf
      181 sgeepilvrs prvgdgllrl dragrvtyas pnalsayrrl glhadlvgae lgrltaalcy
      241 sdepinedlm ivasgraake tevesggtiv qlraiplivg ggrigalvli rdvtelrrre
      301 relmtkdati reihhrvknn lqtvaallrl qarrlqvpeg realeeavrr vgsiaivhet
      361 lsmapeefad fdeiadrvia magevsapea avtprrvgtf gvlpsivatp lamaltellq
      421 nalqhgrprr lqvvveargd rlnvvvwddg rglpadfdld sttslglqiv rtlvegelsg
      481 klaieprhgg gtevtlsipl pts
//
LOCUS       WP_357605687             184 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357605687
VERSION     WP_357605687.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
REFERENCE   2  (residues 1 to 184)
  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   3  (residues 1 to 184)
  AUTHORS   Ramos,J.L., Martinez-Bueno,M., Molina-Henares,A.J., Teran,W.,
            Watanabe,K., Zhang,X., Gallegos,M.T., Brennan,R. and Tobes,R.
  TITLE     The TetR family of transcriptional repressors
  JOURNAL   Microbiol Mol Biol Rev 69 (2), 326-356 (2005)
   PUBMED   15944459
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13585604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..184
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20400
     Region          20..56
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          75..179
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mqparrpggr sakvraavhd avlellreed wdtlsiarva ersgvhqati yrrwgtlpal
       61 vddtvteqls kgspvpdtgs lrgdleayat rvaadvagpl grlyvraahi gtsggdyety
      121 mtdralqlea mlerarrrge dppellelme lvlapiyyha iffnrpigpe hartyvdrll
      181 rlrg
//
LOCUS       WP_357605734             401 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357605734
VERSION     WP_357605734.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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 401)
  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..401
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..401
                     /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=40695
     Region          65..352
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mtvvriaavl lsallatpav avasptlaas apyvpcpavk ppvpppavps pppvgpadla
       61 vggetlatag laipagasma pwvtatswvv adldsgavlg gcgpherrtp asvqkmllaa
      121 almphldpaq vvevtradlq dldpasslmg vveggrysie slwlglllks gndaanvlar
      181 vgggtagrqg gvqamndvah rlganqthaa tpsgldgpgq ytsaydlali aratyaradf
      241 rryiatrvae ipakpgtpaf sithdntlld hypgtlggkt gftdlarqty vgvaerngrr
      301 lavtllgaet aplgslgeaa allnwgfalp tdasvgrlvt pdekkhespi aevrgerdgq
      361 agagpsfsla ailglgaavv lallllaapw rqratrraan p
//
LOCUS       WP_357605718             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605718
VERSION     WP_357605718.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..265
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27646
     Region          19..264
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 malsaltppa gtpavtfdsg gerllgvlhl pagpgphpiv vllhgfpgne rnfdvaqalr
       61 ragyaalvfh yrgswgvggs yswrhaledt arvveavrgd srldaarlal vghsmggfva
      121 lmtaaadpav ravasvaafd mgaaaagcad pavraayvrd fdgellplrg tsgaalvaem
      181 eangaewsla slaprlagrp vlligtgrdp vtpaethhhp lvrafgshpa aqlehhlfpt
      241 dhalsdhrve ltdtvtdfld rtlrh
//
LOCUS       WP_357605746             329 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605746
VERSION     WP_357605746.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 329)
  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 329)
  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..329
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..329
                     /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=36731
     Region          8..205
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mplphflvig apkagttalh aalqahpalh lsqvkepkff ltdgppparg gpgdaqtyre
       61 hvwrradyea lfagaprgal lgeatpfyly dlaaqrriha liprvrliai lrdpverahs
      121 nwthlwsagl epigdlvrac aaeprrvaag wahfwhytgl grygeqlarl ltlfprdqvl
      181 vfryrdlldt pvqaldlicg flgvergllt evprenvtah peaggrhrml saalragara
      241 grllpyelag altepierll qrrgnprrpl twdqrrelip yfadgielle svtgedfsdw
      301 lrprersggl vgrrpegryq srngrprqg
//
LOCUS       WP_357605750             275 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Nonomuraea dietziae].
ACCESSION   WP_357605750
VERSION     WP_357605750.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..275
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..275
                     /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=29395
     Region          21..217
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mpgrypvtfg evellrdldr qhgwmlskdg vpqsyvdled ptyldfeyvr lmadvidvlp
       61 dgplncvhvg ggactipryv aatrpgsrhi vvepdaalve lvrsqldlrs vpklkvrlqg
      121 gleaiagiwd dstdllvlda ftgatmpvel ataeymadla rvlrptgtll inladgkgla
      181 farrlvatvr gtfrhvalla dpgvmrgrrf gnlivaaspa elpvdlltrr aaggltqarc
      241 vygealtnfv agappirqgd avlapvpppa vfgle
//
LOCUS       WP_357605832             267 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605832
VERSION     WP_357605832.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=28114
     Region          7..265
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 magseltnvk sprvkaarrl tkrafreqdr rflaegpqav realklegvp lelfstadae
       61 lrhpelitea tlkgvpvhra sgevmselsq tvtpqglvav cklvhvplde alqgtprlva
      121 vlahvrdpgn agtvmraada agadaviftd asvdpyngkc vrasagslfh lpvvigapvs
      181 aavrqlkerg lrvlaadgag khtlddvdlt gptawifgne awglpeeils eaddvvrvpi
      241 ygqaeslnla aaaavclyss araqrvp
//
LOCUS       WP_357605875             229 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357605875
VERSION     WP_357605875.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 229)
  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..229
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..229
                     /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=25037
     Region          25..213
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtaelveriv rgvhppgtpl ppepalceaf svsrtvvrea vkllqekglv rvrqgsgtmv
       61 tppamwdmld elvlaatiae deslailddl vvtrrvlesd manvaarvag pdtveqlral
      121 vdrmdelvdd patyaesdra fhdtimrasg nriargvvrs legqvvntar ylgrteralc
      181 vasnlghrrv yeriaahdpa gaaeamfqhi teawivrrsg tadpvrlrr
//
LOCUS       WP_357605873             352 aa            linear   BCT 28-DEC-2024
DEFINITION  type III polyketide synthase [Nonomuraea dietziae].
ACCESSION   WP_357605873
VERSION     WP_357605873.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..352
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36745
     Region          4..352
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mtwiaavhgv lppnrypqad lttlaarsfl pegadrrlle rlhagakvdq rhlvlpleey
       61 akldgfgaan dvfvtaavdl gveavagale qaglspadvd limftsvtgv aapsiearva
      121 grlgmrpdvk ripifglgcv agaagisrlh dylrgwpdhv avllsvelcs ltlqrgdasp
      181 aslvasalfg dgaaavvvcg serpartgap tviatrshly pdseqvmgwe vrdsgfgvvl
      241 dagvpdvvrt yladdvhgll adhdlttkdi aawvchpggp kvleavadal dlpagaldlt
      301 wrslaaignl ssasvlhvlr dtlrlrppps gtpglliamg pgfcselvll rw
//
LOCUS       WP_357605880             319 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605880
VERSION     WP_357605880.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..319
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..319
                     /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=33765
     Region          34..314
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpigspsslv rpagsgragg atgthrgtrt trgaraerla pyvlvapavl iivvlrlwpl
       61 vlgvnfsftg dgelngvpvg lsnylelagd plfrtalrnv gllvlllpva vaipgllatf
      121 iylrvpghrv yrsvyffpav lspvivgaif nlmlgydgpv nvvlgaigag pvdwlgdpdi
      181 amfsvvgvhi watfgmalvv flagfstlda slldaarvdg aslgrtvwhv iipaltrtiq
      241 fvfvttmigm ltsmfgllfv mtnggpegat ylpeyyiwhq qgqmnrpala saastvlfvv
      301 mlvvgllqit llrragrqd
//
LOCUS       WP_357605897             152 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357605897
VERSION     WP_357605897.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=16884
     Region          26..149
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maqkeghdva gaadavradi rswptgrlls maarlvegrf hdfleahelt haglialhhl
       61 aegplaqrel arlsrvtdqt msrtiehlrr agyvgkgpde rdrrrvlvri tpagaevlah
      121 areeergsdr llgavdeyds freqlirlit iv
//
LOCUS       WP_357605901             319 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605901
VERSION     WP_357605901.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..319
                     /product="phosphotransferase 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=34636
     Region          23..268
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 meislkaetd gvadpwpayf aerghpgahr igagvegvvy rlgdgqvakv wtgrpptelt
       61 rqvyadiarh rlpfatpeif eihehedvvv tyerelpgvp iqgdsaheny grelpvrhrn
      121 allavlrgla svpgtdamrr lavqgddrpl wqghdrfqda laavvvravg rngaalatrv
      181 pdfgagvert ldalrslpda pvtaihgdlv ppnihiddag rpvavldfgf yttagdpafe
      241 aavtaavwdm ygpyaeehta eltrlfarel ghapaaltay qavyalttyd lfgmgesdgh
      301 frwcaerlrr nlvfsapgp
//
LOCUS       WP_357605944             152 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357605944
VERSION     WP_357605944.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=16636
     Region          24..127
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mgrlsarlta rdyanllsfr vglrrflrws eeraaevglt stqhqlllai rghpdvrgpt
       61 igevadylct rhhsavqlvd rverlglirr nrggvrdrre vrltlteagq aklallsaah
      121 leelqrmapm idtlvdsaat saagchaags lh
//
LOCUS       WP_357605918             181 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357605918
VERSION     WP_357605918.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 181)
  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..181
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..181
                     /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=19555
     Region          1..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrtfwangye ststrdlcea lgldrssvyn aftnkrelfk raltrymaat tadqlrildd
       61 helpaierir alfakilqte aenrrdgygl gcltvnttme lagrdpeial mldrdteyrl
      121 vnlsavigsg qrdgsigstr dpaelarfvn aviagirvaa qggaadatle aiaataldal
      181 a
//
LOCUS       WP_357605954             171 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea dietziae].
ACCESSION   WP_357605954
VERSION     WP_357605954.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 171)
  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..171
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..171
                     /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=18812
     Region          1..146
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mrlaiiigsv rqgrfgptaa awlharacrr ddldvdvidl aeawlptvlp agfpargvtg
       61 ppavehlrpw ladadafviv tpeynhsfpa slknaidwyh eewrgkpvaf vaygeasggl
      121 raveqlrpvf daldavcvge pvslpfhrip pdssaerlld alekhhrdrq r
//
LOCUS       WP_357606017             249 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357606017
VERSION     WP_357606017.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 249)
  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 249)
  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..249
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..249
                     /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=24999
     Region          1..248
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mstfdnkval vtgagsgigr amavafakag arvvvcdvnp esaeqtaadl gdravavgad
       61 iadetsvaal vqaaisaygr idvlcnnagi mdtmalpadi plelwervlr vnltgtflvt
      121 havlphmlrq gggaivntas eagirggaag aaytaskhgv vgltrsvawa yandgircna
      181 ilpgptmtni atnasfdpvg atrlgpvlsl geriaqpeqm adaavflasd aasfingalv
      241 pvdggwsaa
//
LOCUS       WP_357606023             264 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357606023
VERSION     WP_357606023.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..264
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28604
     Region          5..262
                     /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 mtsvrrryvd trlgqmhlae cgsgtpvlfl hqtprswsey irvlpiaggr vhamamdtlg
       61 fgqsartgef sierfadgve avldalglsr valvghhtga vialevaard psrlsalvls
      121 amphvtpgrr arlrdlpqvd hvrpaadgah vtelwrqrrg fydagqeddl trfvidalqv
      181 verlqdghaa vgayemasrl plvrtptlll cgaddayslp dqpalaralg celkvidrag
      241 vclpeqrpda faeavlsfla qsrv
//
LOCUS       WP_357606059             279 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357606059
VERSION     WP_357606059.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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..279
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..279
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=30283
     Region          31..265
                     /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 mirhvltavv lvsgsgsvts saaaaslepl pgvmaalgds vsagfnacgw yvsctsrsws
       61 agdnaevrsh yvrlaergps lrghnrnfav pgatsadlmg qvdkaiaeka eyvtillgaq
      121 dacvpteaam tpvalfrrrv eaamgrlrae lpgarvfvas ipdlrrlwqv gkdnaiartf
      181 wglgricqam lanptstkra dvqrrarvrd rvrdfnrewa racaafgprc rtdegavfay
      241 rftlaqvskw dyfhpnsegq qtladitfdk gfdwsndtl
//
LOCUS       WP_357606067             301 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Nonomuraea dietziae].
ACCESSION   WP_357606067
VERSION     WP_357606067.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 301)
  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 301)
  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 301)
  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 301)
  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 301)
  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..301
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..301
                     /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=30016
     Region          31..290
                     /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 msdpldaysr tvssvaaelq pkvagvragr gsgsavvfta dgflltnahv vgssrsgsva
       61 fadgsagdft lvgrdplsdl avikaqgptp epallgdsda lvvgqlvvav gnplglagsv
      121 tagvvsglgr slpvggrlie dviqtdaaln pgnsggalad ssarvvgint avagigvgla
      181 vpvnsttrai iaalirdgrv rraylglvts paplpealae rlgqrralrv vqvvsgspaa
      241 raglragdlv vnagrspvgd aqslqrlmfa daigrplpit vlrngalvdv itepvellew
      301 a
//
LOCUS       WP_357606094             223 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357606094
VERSION     WP_357606094.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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..223
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..223
                     /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=23488
     Region          56..200
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mpplhtprpg palpspaggv mgeagqllpf dllkaqvtan lamlrpvsvp vgdglrraav
       61 avcvlrdger ppytivikra argrnagqwa lpggrledge qategalrel deetavtgme
      121 vagvlddyvt dsgfvitpvv afggpadprp darevasvhr vpldrllapg vprwnqgllq
      181 mplgpgivih aptgailwqf aevalrgrel rvsgvsqphw trt
//
LOCUS       WP_357606098             409 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357606098
VERSION     WP_357606098.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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 409)
  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..409
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..409
                     /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=44616
     Region          16..392
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mairrstakr hglpsvvqlr ltptppqada ltaairvcnq aaafvsrlaw qqrtfavlel
       61 hrlayhpvra evaglgaqaa vraiarvaga yanrratrkr ahvfrpsgai pydarlmswn
      121 rdartvslwt psgrvhvsyt greqdlkald tlpigeadli grrgvwllqv altlpkppar
      181 elvngflavd qgvanltvts dgavlpgpal sgtidgnghv rtlrerrhrq rrrlqkkgta
      241 aarrvlrrls grehrmitdv nhqiskyvvr eaertgrgia ledlqgirsr vrahrlqrrt
      301 lhgwafaqmt eftrykaara aiaftlvdpa stsqacpecg wtsranrpar grfactrcgl
      361 aghadhiaar niaqrgaagw aavnqphatg lpsarrares kppasaggs
//
LOCUS       WP_357606114             441 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Micromonospora purpureochromogenes].
ACCESSION   WP_357606114
VERSION     WP_357606114.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..441
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..441
                     /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=46374
     Region          20..389
                     /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(29..30,33..34,37,69,119..120,122..124,127,147,
                     150..151,154,229,232..233,236..238,241,268,272,321..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 mrtvrswfrd ttgglprtfw ylwtgtlinr lgsfvlvfla iyltqergfs ptqaglvlgl
       61 wgvggavgtt vggtltdrwg rrptlltahl gaatmmlalg farplwavat galllgmfae
      121 aarpafgamm idvvpvkdrl rafslnywai nlgfacaavl agfaaqagyl llfvvdaatt
      181 vvtaliiftr vketrrvsav paraggaapv galrtiatdr vflgfvvlnl faalvflqhi
      241 smlpiamgds glspatfgsv ialngvlivv gqlfvprlir grsrshvlal aslvmgvgfg
      301 ltafadaawf ygltvliwtl gemlnspsna tliaelspdr lrgryqgvfs lswqiagava
      361 pilgglvrer agntelwlgc aaigalmava hlvsgparer raaqlrpatq pvtpvtavrq
      421 papqaaeaat taepvaahsp s
//
LOCUS       WP_357606108             476 aa            linear   BCT 28-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357606108
VERSION     WP_357606108.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 476)
  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 476)
  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..476
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..476
                     /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=51190
     Region          4..471
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 maqltaldaq flhfetatnv aniaglaild gdlnrsdlqa lleqrlphva alrrklapvp
       61 lgldhpywir eddldldyhv reiglpppgd drqlaeqvsr lharrldrgr plweiylihg
      121 lgdgrmglyt kihhaavdgv ggadvlaall dlsptpappp egepepdepa psrtamvgra
      181 ltrlaanpaq avrfaaravp hldeipvvsk vpgvelvsgl arrvagagda pglpalpapr
      241 tpfsgpisah rrfafvslpl eeikevrkaf gvtvndvvma vcagalrqwl aahggvpdrp
      301 lvagvpfsvr evgearrgnq vtimtaplav hvedpvqrle evrvsmqrik drfslaparw
      361 lrefsesmpa almglasrsa fglvgqtspp invaisnvpg pqfplyvcga rllthypvsv
      421 itdvsggvni tcfsydgsld vgvvtdrtmi pdaweitgrl rdaldelrne afrigp
//
LOCUS       WP_357606125             335 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357606125
VERSION     WP_357606125.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..335
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34226
     Region          40..334
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 matrrkllvv gvaaatalal gacgatadkn egssggdgkp atglrimvpn tpgggydtta
       61 rtaakvmeda kiatgvqvfn lpgaggtvgl qrtvnekgng klamqmglgv vgasytskss
      121 atltqttpla klieeagaiv vpkdspykti gdlvaawkan pkgiavgggs spggpdhllp
      181 mqlaktvgid prqvnfvsyd gggellpavl ggkvafgasg fgefldqvea gqirvlavts
      241 eapidalkdv ptlksagidl vftnwrgiva ppgisdadkk vwidaltkmh eseewkaela
      301 krgwtdafvt gdqfatflte qdksvadllk qlgla
//
LOCUS       WP_357606140             143 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357606140
VERSION     WP_357606140.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Rosinski,J.A. 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 143)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..143
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..143
                     /product="helix-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=15645
     Region          8..76
                     /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 msssddrsvw tflthharvl meitrnphar lrdiaasigi teravqgivs dlhqtgyvtr
       61 ervgrrnhyr vnpdqhfrhp aeanlpirll ldmftqhdls sgtapvaapa hepsaggrta
      121 dpdgrtvlea dtppstsste liv
//
LOCUS       WP_357606142             485 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357606142
VERSION     WP_357606142.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 485)
  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..485
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..485
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=50492
     Region          37..117
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          277..345
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mhakkitrsa vllalvaala lpagqaqaat ptpkntdfng dgyndlalgs pnyagedgsw
       61 nrglvtvlyg gpdgfdghws rrppvgctap ngrrcylwgr qvsagdldad grtdllfaad
      121 dgmrvqswtp qgvteieyhg nnptlnpvgv tlgqfddqpg gdivgawgng nyqsvvggwy
      181 nrdastitrg fdfpdsdvsv ksvatgdvdg dgklemsvia srryngkesa ylwliddprq
      241 qplsisnkaw gwdalckpnt rnflgcprld srvamgdvdg nghldvvmtt pstrslqvwy
      301 gsasgpashp gfsahdldwf dpdplvgrgl avgdvngdga aeiaigtpda tvsgqsraga
      361 ivlipgsagp trgpvlanaq litqdgigpv sapnptpaaa alpdpigeqs eagdrfgeei
      421 riiditgdgk geviigvpdk nrkagmlavl rgsatgvstt aaqvvhprql glapgyitfg
      481 mvmtp
//
LOCUS       WP_357606145             240 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357606145
VERSION     WP_357606145.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Rosinski,J.A. 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 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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..240
                     /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=25091
     Region          18..237
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mplptprwrg wvtikpgrly ygghigagsl hshhavqlli gddliltgad gaehamtaal
       61 ipantphaiv rgsadallal idpaahagpa ldrtrtgsaa awhidldvpa qrdlpslhal
      121 vttvtgaapp rpghpaltea aqiiermlpa qvrlgdvatg vhlsesrlsh lftgefglpf
      181 rpyvlwarlr aalaalsega slteaahtag fadaahltrt vrrmmgdaps aladgvrwls
//
LOCUS       WP_357606176             277 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357606176
VERSION     WP_357606176.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 277)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..277
                     /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]"
                     /calculated_mol_wt=30055
     Region          20..153
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mtlvanvrqe eawngeegrr wadhyqrldr maapanehlf aaagigerdr vldigcgtge
       61 ttriaarhaa rghavgidls tplleiarri saeqaignit fergdaqvhp lsdahfevai
      121 sragvmffdd pvaafanvrr slrpkgrlaf lchragknqt dvifdtlaqh lptpdlqgrl
      181 ggvadftdpt hirdvlndag ftaiatspve yltelgddaa hatdflldvq lagfvsgaee
      241 aamarvraal aealrryerd stvrlrasaw ivtaqie
//
LOCUS       WP_357606193             263 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357606193
VERSION     WP_357606193.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 263)
  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..263
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..263
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27815
     Region          1..263
                     /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 midingarla yddlgsgspv lllhagiadr rmwrhlvpal aerhrviald lrgygdselp
       61 pasyahyddv vavldalgid raalvgcsfg gavaidtala hpqrvsalal fgsavagnqw
      121 seeaeqlwdg lvgevdpedf aasaagevrf wvvgpgrrpe dvdpglvafa eemdqralaa
      181 eqalsaveve eldppaierl aelrlpvlvt agaadvpdis rladriaaev pgavrlpdvp
      241 daahllpler peavdaalrd flr
//
LOCUS       WP_357606213             336 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora purpureochromogenes].
ACCESSION   WP_357606213
VERSION     WP_357606213.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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 336)
  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..336
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..336
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36735
     Region          18..307
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mndvdrksip asevghlara vldavgqvvv gkreslelvl agilagghvl ledlpglgkt
       61 ltarsfaqal gldfrrlqft pdllpadvtg sflydqrsgd fsfragplft nllladeinr
      121 tppktqsall eamqekqvsv egvtyrldep fhvlatanpi eyegtyplpe aqldrfllrv
      181 sfgypqreee wdvlrrrmar rreeaeikpv vdaatlramq aaledvvved svgryivdlt
      241 aatrehpsvl vgasprgsla llllsrvrav fagrdyvvpe dvkevaapal ahritlrpem
      301 wlrrvdpsfv vgevleqtpa pasgalpsya agrpgr
//
LOCUS       WP_357606236             289 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357606236
VERSION     WP_357606236.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 289)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..289
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..289
                     /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=31695
     Region          5..284
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mnggalnrtr teqrlgwlma gpalllmmav tvvpilrtag lsleryslsa pderefagld
       61 nfreiltgqe wwqdlaativ ltvtsvgvef vlgfalamam hkvlwgrrll rtvvlvpyam
      121 ltvvsafafr fafqpsvgfv ggdfnwlget wsaytvivlt evwkttpfma lmllaglvtv
      181 pgevyeaakv dgagawqrfw rvtvpcvrpa imvallfrtm dafrifdtvy iqtqgavgte
      241 tlsflsyrfl irdlevglgs avsvllfacv aliasgfvra frselgggr
//
LOCUS       WP_357606244             318 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357606244
VERSION     WP_357606244.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=34423
     Region          21..318
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mletsarllr llsllqsrmd wtgaelaerl hvglrtvrrd idrlrelgyp vdatpgvagg
       61 yrlgvgaalp plllddeeav avaislrtaa tgsvagleeg avralaklqq mlpsrlrhrv
      121 tafqaatvpl agaaappvsa dvlaglaaac rdhrrlrlry rgrdgvsare vephrlvhtp
      181 rlwyllawdl gredwrtfrv driegplgep garfsprtpp redaaayvsr aitsapyryq
      241 arilfhaple avaprtspga grleavdagt clflagsnsl delavhvavk gfdfevldpp
      301 elvpvlreis erlgraas
//
LOCUS       WP_357606315             367 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357606315
VERSION     WP_357606315.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 367)
  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..367
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..367
                     /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=38602
     Region          154..362
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrqlvrfgrq yaavmrlltl vpicaialfr sapgnlapta lvvavaaawt cgyawwlgrg
       61 rgsvpvvldv vvllglaacv wwtdaiedtn tgwlrllvlf mcvtcqwhtp vlvgaaaala
      121 agggtvvava aagadasvir gllwapaaaa lsrvawtllr raahradlaa deaarargrs
      181 lmaaavraee refanalhdt aattllmvgi gqvrsdagwl paqarrdldr lasgnspaha
      241 hadvvellrt gldavpltve fdapgevrlp ydvaraiada agealtnvrr hadttratvr
      301 lrgdsqalrl diadrgrgfs paevpatryg lresvhgrmt riggtatits apgegtlvrl
      361 ewragdg
//
LOCUS       WP_357606386             292 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357606386
VERSION     WP_357606386.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=32247
     Region          2..289
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mhskrewawg ylliapmalg lavfylwpil qtlylsmtes gvfggytwvg tanfadlftd
       61 eemygalgnt llyavlvlag vplsivvaal lnvpglrgls lyrtlyflpv vtmpaavalt
      121 wsylfngdfg ainhvlgtvg idgpywlgdp dfaiyaiaiv giwssigyna vlflaglqgi
      181 prhyyeaaei dgagrlrqff ritlplltpt tffvmvitmi nalqvfdlvy lmidlkspal
      241 egsrtivylf yetgfvqnqr glaaaiavil lglilvltaf qfrlqkkwvh ye
//
LOCUS       WP_357606389             414 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357606389
VERSION     WP_357606389.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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 414)
  AUTHORS   ter Beek,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..414
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..414
                     /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=44957
     Region          33..407
                     /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(137,139,262,264,297,298,340)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrfrlplacl tglavmtagc gsssepetsg katisyaiwd kndqasaeki iaafqqtnpn
       61 vtvkleitpw dqywtklqta asggaapdvf wmnslnvrmy akggiitpie eskvqglspa
      121 vvdgyrydgk lyglphnvsv palwydkklf daagvaypta dwtwddvkaa akkltdpakk
      181 qfgilahmwd qgafyptmlq agghvlsedg kksgfddpas iqgleywtdm ieqkvapvae
      241 vytdtdpiql fqsgkygmfy ggawlastfw anpeirerid vaplpkgpak eavillglan
      301 avsakskhpk esaafaefva seqaqkilsd sgggslslrd gtqegwfkaf ptfhlketyd
      361 asmpngvpyp vslntaqwqd vqnkllaeaw agkrpvadva keiaaqmnei lake
//
LOCUS       WP_357606395             414 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357606395
VERSION     WP_357606395.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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 414)
  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 414)
  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..414
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..414
                     /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=44013
     Region          1..414
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtltiavvga gargqiyara aaadgrariv avadpdpvrr aalatehdvp eqsrftgwad
       61 laavpklada vviatqdrlh vepavafael gyaillekpl apterearri veavdrsgvv
      121 favchvlryt aytkafkell gsgrlgslss vqhlepvgww hmahsfvrgs wrntveagpm
      181 lltkschdid wllhlvgeep vavssfgslt hfrpenrpkg adtrcvtcpv eptcpysatr
      241 lylgclgdpv refwplgavt sdastagvmr aletgpygrc vydcdndvvd qqvvtlefar
      301 gatasftmta ftplehrktr vfgthgfaeg dgrhirivdf vtgaeetldt gtnagaslad
      361 ghgggdaglv rafidavaag dqaplgagpa ealaghlvvw aaeraretrt vqal
//
LOCUS       WP_357606472             462 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome b [Nonomuraea dietziae].
ACCESSION   WP_357606472
VERSION     WP_357606472.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 462)
  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 462)
  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..462
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..462
                     /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=50849
     Region          14..408
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mrslvkhrsf qfshwsfmfa eiavwsfvvl lvtgavlmvf ydpsmsqvty dgsygplrgl
       61 fvsrafdstm hlslevrggl lirqihhwaa lvfvaavalq llrmfltgaf rrprttqwli
      121 wvtllalgma agetgnalpd dmlsggslwl imsvvqsipf vgtwalsllf gpdfpgdrii
      181 pvmygghlli avvmavllia rellvrrhgh srfiasvsar rsarpmmala tfgmliilgf
      241 gfqiapiwly gpakptqisa gsvpdwymgf ldgalrimpg weltlgdytl slavliptlv
      301 ipglfftala ayptaerflv srrsrrdalg rpkttsrmar vpgaqnmldr prdtptktai
      361 avagitfygl lwaaaandqi ahqfhltvea vtiffryavv igpviafiia rwiclalqqt
      421 drhvvehgme tgiitrspdg gfheqlapaq qepqelaats gr
//
LOCUS       WP_357606482             313 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357606482
VERSION     WP_357606482.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 313)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..313
                     /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=34275
     Region          17..311
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtslrteavm argavhaapr rrsgkwtala flaplviyla lfyayplyrn idlsvhdytp
       61 rafvrgdaef tgldnyvail sddtfvralr ntalftlvsi aaqyalglal avffhrnfrl
      121 savlramflv pwllplivsa stwswmlnsd ngivnaalqa fgigqinwlt spgtsllavt
      181 ianiwlgipf nlvilyaglq nippdlyeaa gldgangwqr frritfpllr pvsaitlllg
      241 liytlkvvdi iwimtkggpa dasttlaiws yreafgtgqp dfspaaavgn lliliafaag
      301 llhvrlqrre dha
//
LOCUS       WP_357606533             348 aa            linear   BCT 28-DEC-2024
DEFINITION  LacI family DNA-binding transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357606533
VERSION     WP_357606533.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..348
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36552
     Region          5..340
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mpasprratl atvaasagvs vatvskvlng rsdvapatrs lvesllrehd ymaqsprrgt
       61 aangavamct vevqfdneln aysteivqgv vsagaelgvg vvvsvrktid hpaswardlv
      121 aagrraliav tcaelddrqv ralsrvqlpl vvidplnlqh dqvtsigstn fagglaatqh
      181 llalghrria yiggpataac nqarlhgyra ameaegvpvp pgytqfghfr yqdgmdhgaa
      241 vldlpeppta vfagcdelal gvmeaararg lrvpqdlsiv gfddtqiawm tspplttvrq
      301 plremggval rtalrladge kidshhvela telivrasta dvacaeha
//
LOCUS       WP_357606552             421 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent RNA methyltransferase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606552
VERSION     WP_357606552.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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..421
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..421
                     /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=43898
     Region          21..416
                     /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 mtgptggvpg tgerhgleea erveltvgav apgghcvarv dgqvvfvrha lpgerviaev
       61 telhkgfara daveiltasp drveqpcpwa kpgrcggcdl qhvtpaaqld wktavvreql
      121 trlggltdae vdalgvavea lpggplgwrs rvryavdaag ragllkhrsh evvpidwcri
      181 ahpairelpv ltpsgarwpd aeavetvast ggdvsvaavt egvatpvsgp qtvrevaagr
      241 ewtlpaagfw qvhpaaadtl vgavldlldp rtgesawdly ggaglfaaal agrvgpqari
      301 tlvessaqgv taarenladl prvevvaarv etalarrrvt gpvdlvvldp prsgagapvv
      361 rdvvaarpra vayvacdpaa fardvrtftg lgwrlaalrg ydlfpmtqhv elvglllppa
      421 r
//
LOCUS       WP_357606581             295 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357606581
VERSION     WP_357606581.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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 295)
  AUTHORS   ter Beek,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..295
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..295
                     /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=31419
     Region          14..267
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtaapggqgr glawlavpal vffvgfavip lvgvfvlsft swdglgeirp agfdswravl
       61 sdpglphalw vtflvialsw avqtpasill gtflagfqry ravlsvvyfi plllssaaia
      121 itykalldpn fglgaglgip llvqdwlgep vlafsvvifv vswqfipfhs liyqggvrqi
      181 prsmyeaael dgagrvrvff sitlpqlkyt iitsstlmvv gslvffdlif vltaggpgda
      241 trvlalemyk rgfqanlmgp asviavilvl vglalalllr rlggrdashs qlega
//
LOCUS       WP_357606587             413 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606587
VERSION     WP_357606587.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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 413)
  AUTHORS   ter Beek,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..413
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..413
                     /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=43996
     Region          35..399
                     /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(146,148,270,302..304,341)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrvrkslsav avalvaalva tgcggsgsgd sgkktvtmwi ypvifdeakh raywdetaka
       61 fqaanpgvei kteifpwanr dqalataiag nkgpdvvyli pdqlpkyarn iepvdayldd
      121 aakadylpnv vesvtidgkm mgapvltsav tpicnkkvfa evgqttypss wndllamapt
      181 fkakgydvta yagdvkntln qtfypllwqa ggdvfspdgk svafnsaegr kalafakqlv
      241 dggfvdksll ttlppieqtr iaqnkvgcvw hvlpaeiekf wgkeniqalp hftetkqigy
      301 gtvgslsmlk nsknkeaagk wiafasdaen akkydvaasf fsakksvgal yaddpvlgeq
      361 ekqvatstvg plnekardvq gvlapeiqaa llgkksveqa lddaakaadp llg
//
LOCUS       WP_357606590             299 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606590
VERSION     WP_357606590.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=32770
     Region          6..299
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mvalptirrr rvrrpsarea gtallfvlpf lmlfalfrfg paiagvvlgf tdyaiggdts
       61 fvgvenfrrl vddptfwsal rvtviftals vplsmlaslg malltrrafr gaklfrsvff
      121 lpvvtslvla gvvfswvfad ggpwsramga lglpqqswla dsvlvipalv lvavwsrfgy
      181 gmlillarmq dipaeleeaa ltdgasawqr fryvtlpqlr palffvalie ttvavqvfdm
      241 iyvmtgggpv rssyslvyll ydqgfkyfdl gyasaigval fvmtivvalv qrltlgree
//
LOCUS       WP_357606613             237 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357606613
VERSION     WP_357606613.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 237)
  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..237
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..237
                     /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=24946
     Region          2..231
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mlrpsplvdq aaqhlreeia agrypvgtkl pgettlaqtl gvgrstvrea lralagagll
       61 qarqgagvfv iateaaeews arlrraavad vyevrmlvev qaarlaaerr rpadlealka
      121 alaarraasa gddaafvdad ialhaavvaa arnpvltdlf aefvpalrqg lidlvdllkl
      181 ragdpnhgda shaglvtaie kfdreaasri vqeelattlr alqklsppps rlsahdg
//
LOCUS       WP_357606620             210 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357606620
VERSION     WP_357606620.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 210)
  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..210
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..210
                     /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=23215
     Region          15..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtqdgrrlrg lrsreaileq avglasvegl dglslgrlat atgtsksgff ahwrdkeqlq
       61 ldavewaarq wtehvvapal rapagvrrlf alhearltfy ddgvlpggcf fftvqaefdd
      121 rpgavrdrva rsmrewqefi rrqvaeaval gelaesvdpa qlayeidalg emviihsrlh
      181 ggpdslrhar ravlqrlral cpdpallpen
//
LOCUS       WP_357606636             291 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357606636
VERSION     WP_357606636.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 291)
  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 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   3  (residues 1 to 291)
  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..291
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..291
                     /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=30952
     Region          5..287
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mahdleiadl rsfatvvrag sitraahalq lsqpavsqri hrleraagdr llvrdargtr
       61 itpageklla yaermlalhd earasidaqg dqatgsrtvg lledlavttl pttladfaal
      121 hpgidlevvi gpaqalrera ehgrldlalg dpsvmpdaav rwrrrvplaw aaaasldpal
      181 dplplvmfsm pchwrapvld alnqrgrrwr iafqstslaa vqaaicagig vgtllagnvp
      241 ahavrlgsrh dlppapqvei aitrrpgten daavdslerl lrqsvaadhg a
//
LOCUS       WP_357606640             229 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357606640
VERSION     WP_357606640.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 229)
  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 229)
  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..229
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..229
                     /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=24283
     Region          4..226
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrsyavqlyt lrdhlaadpa atlsrlaslg yeavepfdlt pvdgfevpsa hapllgpnrd
       61 dylkvagtli vpmvrseeft tqegiertad alnaasawga ehgvtvgyhn hhwelasrvg
      121 grhalevlad lldpavvlev dvywaavgga dvpsllgrlg ervqflhvkd gpatlgepmt
      181 avgsgtlpip dilaaapqar rvveldscat difdaladsl aylrsvegr
//
LOCUS       WP_357606657             272 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357606657
VERSION     WP_357606657.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 272)
  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..272
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..272
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28487
     Region          1..272
                     /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 mkktetlqap garlyyevqg sgpillmipg gptdagifaa vtpllaehft vvpydprgns
       61 rsvpddpale qdidvhgdda arlvaelgge payvfgssgg aqialnlatr hpdlvrvvva
      121 heppcvrllp dadqvaagme evastyereg vpagmqkfne ligmseedap qgppspeqqe
      181 mfgrlmgnlg yflgkgvrpi ssyrpdveal rsgsprvvvg igestegqla rrsaialaeq
      241 aglepvvfpg ghggfadape afaarlaevl ra
//
LOCUS       WP_357606653             336 aa            linear   BCT 28-DEC-2024
DEFINITION  mechanosensitive ion channel family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606653
VERSION     WP_357606653.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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..336
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..336
                     /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=37316
     Region          65..323
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mraalimlat lgvavlldig trrlvrradh gryqwvlgpl rnacrrptaa vllltglyla
       61 lpprptgwlg dvrhviglll igvvawlvim alhvaegvtf srlppevvad rrirrartqi
      121 rpvrrftavv itivaiglim ttfppirafg isvlgsagvv galiglsart algnafagiq
      181 vafsdglhvg dvvviegewg rveevkltnv vvrlwddrml vlptmyfter pfqnwsrhea
      241 rvvgkvqihv dhtadledlr tetqrlvess plwdrsrwvl qmvdataasv vievqataad
      301 gpsawdlrcd lregliryir dnhpqwlprt rseykp
//
LOCUS       WP_357606686             200 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357606686
VERSION     WP_357606686.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..200
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=21342
     Region          3..165
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpptnparrr altdaaiell assgahglth ravekeaglp qgtasnyfrs reallvaaae
       61 riaelhhadt drvteqpatl vdlltrsllt aattlrtryl aifelqleaa rrpalasvla
      121 dlqdtslqit aghhdklgla ipreripali alyggalfsl vtappgsvnr dvvqqvaqvi
      181 vhgcarhedd prparqgsep
//
LOCUS       WP_357606750             328 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606750
VERSION     WP_357606750.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..328
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35531
     Region          4..328
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mttqlrarls eilqagqvsg lhavaavrgg qtlleyygtg edfawgdslg vvefgpetlh
       61 dirsvtksvt allygiahge glvpppaepl lrgfpqypdl aadpqrarlt vehaltmslg
      121 vewredlpyn spanaeiame lapdryryil erpiieppga rwtycggata llgrliadgt
      181 gqslpqygqa vlfaplgidn lgwmtgadgv asaasglrla prdlarlgel mlaegawdgq
      241 rivpedwirt mlqprlqtsw gaqygyqwyi esiegrrlva gmgnggqrlf vlpdldltva
      301 itagnyddpd qwrtplgvle riilpama
//
LOCUS       WP_357606748             484 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357606748
VERSION     WP_357606748.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 484)
  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 484)
  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 484)
  AUTHORS   ter Beek,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..484
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..484
                     /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=53457
     Region          8..348
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkprgttami taamasvlla acgtssngns ggggsqttlq iwdfsaeqvn fhkdigaqft
       61 kehpdikiew rsitqndymk tlplafqsnq apdmfywnat glsqlldqkw irplspsgtv
      121 padftkrwpd gsfleginvq dgktygfpfs enlywgsgym flnkqvfqqa gldvgnppkt
      181 wsdlkntcaq ikartkaeci aaptkgvdmq riwyalissv stdeffdykt gkfdltqpdq
      241 vktfsfiqel skagylapgt ndknfsrqqf aagqagimfd gtwlpsvwas qgfssdkyvv
      301 aprvnpdggq tgaagrkydt nkywvssqtk hpdamwtfiq wmtdpngyfv kqyyksafgt
      361 layvdnekmv tdpalrqimq igskpgyrvq lpvpllkcpd iakskayvna lakspdgewe
      421 amgealvsgq slatvgaaiv kqrqaaleeg lkqeaaaglk vsmdcytfsd wdhtkdytsd
      481 kyrg
//
LOCUS       WP_357606758             257 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606758
VERSION     WP_357606758.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..257
                     /product="phosphotransferase 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=27774
     Region          <105..235
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtsvvifatl adveevevvv ahheratvrv ggvflkidad qtrtdvevea mamapiptpe
       61 ilwrkppvla latlpgtalg rlgepstass aawaaagaaa rmlhdaplpp wpgrrldela
      121 srldgecewl vtngvlptdl vtrnrrvaea alrpwtpvfm hgdlqiahvf vdddeitgvl
      181 dwseagqgda lydlasltlg heehlcdvva gygtdvdldv irawwslrsl lairwlvehg
      241 fdpaapgcev dvlksrm
//
LOCUS       WP_357606767             699 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357606767
VERSION     WP_357606767.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 699)
  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 699)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 699)
  AUTHORS   Rosinski,J.A. 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 699)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         <1..699
                     /product="helix-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]"
     Region          <52..667
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          584..689
                     /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 asrpeplptt gtlpasrpep lpttgtlpas rpeplpttgt lpasrsglfs aagatladle
       61 paetaqlvev rptgltprhl lvlvaayqsa pisarvaahl alaetsperr vwhlaaaalq
      121 pdeeiarele tigtssaler aaelttdpep rgrrhaaaah aacdagqlrr aadlatrate
      181 lsaepstlaa aarvlatves etgsparaar mlldsaarig ddatavvmia dairlsgysg
      241 deglavqiaa avwatpeatp tpeatptpea gptpeaapap sqavrsaarp twsaplarsl
      301 pplakvmagg plsgfsaige lvehtpalat qqaitatslg lmaadagsal rltstlvtdc
      361 rhqdlmgllp yalqlqaqal llsgrnaeal sqateglkla gdlgqthrig hlsglvalia
      421 alsgdekrcr ayaesslayc adhdapasaa latwalglle lglgravaav ghlervvagp
      481 ahhpvvavrc aadlvdaavq adlpgaaaep lallerwagd trqrwvgava lrcralvapd
      541 geaeplftra ldlhgpslas fqrartelay gqwlrrvrrr searshlraa raafeqlgvl
      601 pwaeraaael saageaspae rlpealrglt pqerhvvfla aqgssnreia aqlflsprtv
      661 gyhlyrafpk lgitsrtela ellrrsgtit prpgvalra
//
LOCUS       WP_357606786             221 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606786
VERSION     WP_357606786.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=23739
     Region          <11..206
                     /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 msargtsdga iaviglgrfg chlagaltrl ghevlavdrd sdqvqrwapy lervvqadat
       61 eedalrqlgl adfrrvvvai gvsleasvlt vvaltevgvp qiwaratsdk harilasvga
      121 hhvifpeaet gervahlivs rmldfiefgd dfaiakvpvp pslvgrslrd ltperygvlv
      181 vgtklpgerf ryatpetris kdtvlivegt iaqvqqfanl g
//
LOCUS       WP_357606777              76 aa            linear   BCT 28-DEC-2024
DEFINITION  GntR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606777
VERSION     WP_357606777.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 76)
  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 76)
  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 76)
  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 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..76
                     /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=8172
     Region          5..>74
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mptaeapyrq ianditakik sgelkpgdkl pstrelaeay qvhmntasra lsllhdrdli
       61 tgqpgrgtyv aerpgq
//
LOCUS       WP_357606798             588 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora purpureochromogenes].
ACCESSION   WP_357606798
VERSION     WP_357606798.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 588)
  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 588)
  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 588)
  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 588)
  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 588)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 588)
  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..588
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..588
                     /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=64046
     Region          42..515
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mnsyrpgwtl rrrvsllltv vvvlllglaa aeaavatktr qnmdavlvkt gplrvqgqel
       61 lnalldqeta vrgyavsadr adlapydsgl qqerdtvskm naligdypdi qralavveqq
      121 aadwrsavaq pvittterdg taaaqalitd qarqqfeqir asagvlqaei lderqrtadk
      181 vyessnilvv llivaavvva vagsvlllsl drmvikpltg laeqirevae gdyqhriags
      241 gppefqqlag dvdamrqkia relaevrear esiewvnsql qkqaeeltrs nrdleqfayv
      301 ashdlqeplr kvasfcqllq rryagqlder adqyiafavd gaqrmqrlin dllafsrigr
      361 lttgftevdl nkvmgdvagq teaarqyada eltwdempvi rgeeplltnl lanlvsnsik
      421 frrpdvtpkv hvsarlvdde weitcqdngi giepefadki fvifqrlhak daypgtgigl
      481 aivkkiveyh ggrvwvdtdt degtairftl palpedveaa raaaeaeavt geepagddla
      541 smveidadge petsaptvgr qpdgpagada peaapehgtt ggmketvr
//
LOCUS       WP_357606801             405 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606801
VERSION     WP_357606801.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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 405)
  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..405
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..405
                     /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=43159
     Region          24..401
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 magpsvapyp qgglgrnpnl ppgerlrvll veddegdafl vsellaetns midlliatsl
       61 searqrvagv dcvlldlglp daqgldglrk vlemssgaav cvltgrsdeh lgivavaega
      121 qdylvkgqvd gvlltralry averkraden arrlrevelr qaesarlerg llpqplmstd
      181 evsvhtfyrp grhaaliggd ffdvvqtrpd rvdlivgdvc ghgvdeaalg velrvawral
      241 ilagvadddv lpaleqvlms errlqeifat vatvrldlag nratvrlagh ppplllsggk
      301 vapvparggl llgvrprrpv afdlefdtdd wsllmytdgl iegrvgdgde rldvpglagl
      361 leepanqavp laelpawlvg raeqinggpl addvamllvt rgggr
//
LOCUS       WP_357606815             381 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357606815
VERSION     WP_357606815.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 381)
  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 381)
  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..381
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..381
                     /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=38682
     Region          1..381
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mnevfvvdav rtpigrygga lsgvrpddla ahvikellar spaldpaaig dvvfgnanga
       61 gednrnvarm asllaglpvg vpgatvnrlc gsgmeaviqa yraialgdas vvvaggvesm
      121 srapwvlpkp srafpagnqe lvsttlgwrl vnprmapewt vslgegaelv adrhgvsrqa
      181 qdayalashq kaakadfgae vvavgevvrd esiredtsme alarlkpafr eggtvtagns
      241 splndgaaal llcdadglaa igreplarit gsavsaiepq yfglgpveam rkalrgreps
      301 vvelneafaa qvlgclaelp dldpsivnpr ggaialghpl gasgaritga vahqlasags
      361 glglaalcig vgqglavvle r
//
LOCUS       WP_357606843             406 aa            linear   BCT 28-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357606843
VERSION     WP_357606843.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 406)
  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 406)
  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 406)
  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..406
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..406
                     /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=41289
     Region          15..384
                     /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(25..26,29..30,33,65,114..115,117..119,122,141,
                     144..145,148,217,220..221,224..226,229,256,260,308..309,
                     313,317,334,337..338,341..342,345)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 menastrrsg qalliwgllv vaanlraslt gvgplldqvq adlglapava gllntlpllt
       61 fvalsplvpq laarwgaeql lggalvvltl gialrwvpaa aglfagtvli gagiavgnvl
      121 lpslikrdfp tkvgvltsay atvmggvaav asgvavpise vapggwytal gcwvlfalva
      181 vllwlpqlra prraaqairg hrlpwgsgla wavtafmglq slgfyvvvtw lpqvfqdngm
      241 sattagwllf lfqavavlts lavpgalrwa rdqralatic savmllgylg lfvapgaall
      301 wsvvlglggg aclvlalafi slraqdasva galsamaqsi gyllaavgpv vfgllhtvss
      361 gwqapimlmc vaaagqtvva lvagggtvrs tadrvpsagr wsggkk
//
LOCUS       WP_357606867             943 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357606867
VERSION     WP_357606867.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 943)
  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..943
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..943
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=101219
     Region          44..943
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msprihlpsg wvtfvftdie gstrlaqllg sgyrpvlweh rrllrdtlag tdgaellteg
       61 dsfflafpda aaaltaclta qralsthdwp tpeatpkvrm glhtgyaepr dgeyaspevh
      121 raarvaaaah ggqvlcsaat arhaeplpsg aslldlglhr lrgfddrerl fqlvapgler
      181 qfprprtada vphnlptqvt sfigresera eldllvrrhr lvtvlgagga gktrmavela
      241 ggmveaypdg vwfvdiatvt dpglvafava avlglrpepg rpmldtlvey aaarqmlvvl
      301 dtcdaqpaac aevisrllag gskvrvlats resfglpgev vwripplsvd pqpgrtesda
      361 vallldrtaa arggrppdwa eagdlrrvvr rldglplaie laaarlrvls agqlaarldd
      421 vlgtldagrv vpelpadrgw mgnqqdtvdl vaaaagavpp saahravqrs aterhltmqa
      481 tvtwsyrtlg prasrllrwl avfagpvels tvewlldddp ldplsvlvdk smllaephas
      541 gstyrmldpi rayaarrlve ageeraardr hvawsahale rahlgpdgqp vtlslyaldp
      601 laselraalr wcatggsara glrlaggldq wwrerglsre arlwlfrlyg riaetgevip
      661 eaelaaayhl hslhagadge faeelrysqr aeaaarqggd agllarvlag raaplidmgq
      721 faeaervcre vidwaheqqv tgdalfavyn laellwrrga lneaaellga arpveaarpv
      781 ergrrsvdml lgmvalargd lvaahehllv alrsrmshgy hgracdtvna vavrcaagge
      841 lgtaarlfga aqatraqlra tpaiygsywl erqaelrrvl gdaafdaayg eggelgleea
      901 aalalavehp dlgadsirfr tagaaaprqg gpgrqeldrr era
//
LOCUS       WP_357606878             412 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357606878
VERSION     WP_357606878.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   ter Beek,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 412)
  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 412)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..412
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42845
     Region          29..408
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mtdletptdl kderligrqg lrgaaeglld rvrggdlgvl pvvigliviw svfqvlnpif
       61 lssvnlvnlt lecapvgiia lgvvvvllvg qidlsvgsvs gltsavmavf fvdrrlpvwl
      121 ailaaivigc aigwvygqif nrfgvpsfvi tmagllgllg vqlwmlgakg sinlpfdsgl
      181 vafaqlafvp vwlsyvfvvv aaaglfasgy aharrrrkas lsavstqllv arsvlvligl
      241 gvvvwylnqt rgvgwmfvlf lalvlvmhyv lgrtkfgksi yavggnaeaa rraginvrav
      301 ytsafvlctt laavggvlaa arlaavnqss gggdvnlnai aaaviggtsl fggrgtafaa
      361 llgivviqsi ssgltllnld ssfrfmvtga vlllavavds varrsrvshg ra
//
LOCUS       WP_357606972             169 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357606972
VERSION     WP_357606972.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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 169)
  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 169)
  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 169)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (residues 1 to 169)
  AUTHORS   Rosinski,J.A. 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 169)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..169
                     /product="GbsR/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=18693
     Region          12..157
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mtddrraapd veevhlfver mamafaevgf prmaarvlft vmsadeplta geigerlgvs
       61 aaavsgavry ltqfgmllre pvprsrrdry rvpdnpwyea titktgiykn fidvatagvd
      121 alhgpatpgg ervaemrdff vfvqeeidsl gerwrarraa tghprptdp
//
LOCUS       WP_357607028             227 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357607028
VERSION     WP_357607028.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 227)
  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..227
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..227
                     /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=23939
     Region          12..222
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtptvdsvav pprghrvrqt ieqlrerilg gewpvggrip tepqlvaalg vgrntvreav
       61 ralvhagvle crqgsgtyvv stdelapvva rrltddrmae vvevrrafev eaarlaalrr
      121 tpedlaalda alaareaawr sgrvaefvea daalhtavva aahngmlael yasvgtalrs
      181 tvahamgdal eperyvdhgr lvaairdgdp araaieagaf leppsga
//
LOCUS       WP_357607039             342 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357607039
VERSION     WP_357607039.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 342)
  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 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   3  (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   4  (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 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..342
                     /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=35433
     Region          <3..>249
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          274..331
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mmpvsmvgra geraeldraw stvvdagrps pavtvitgaa gvgksllvaa avegfsprpa
       61 vvlsgaarlh dpapydwlaa vlsgrdtsgl dlppdalawl aqqptaprer yapgtllrla
      121 vrtvrrlvga gpavlvvedl haldpaslnl vgelatagdl pallvvasrp padavapdla
      181 vrvlsrlcgv rgavrqhlgp lgvaevaevl tqvydgtrpt driatavwrr tggnpyalie
      241 llaahagqgp ealaerplpe hlrppaprpa appdaeltgr evevlgclva gmsnkqaara
      301 lgisvrtvtv hvsnllrktg sasrteaalw avrhrvpsrp lg
//
LOCUS       WP_357607078             485 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357607078
VERSION     WP_357607078.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 485)
  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 485)
  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
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..485
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52401
     Region          10..472
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtdgfhlrlv hemlqfastr apgapavrdq hgswtyaefl eqslacagwl seqgvghgdr
       61 vmirarpdrr vlavlfacar lgavfvpvse tataiqvnhi lsdadpvvvi ddelpdwggh
      121 kapgaqaard dpllliytsg stavpkavvg hhshvlfatr aiaerlsyra ddvvlcklpl
      181 sfdyglyqaf ltvlcgaelv lagqdadarl lalikhhgvt vvpvvpslaa mllslgrrdr
      241 sptrvrlftn tgeelprati aglrerfsga gvqlmfgite ckrvsimevd gdlhhpgalg
      301 rplrgtsvri lrpdgseapt gesgeimvsg phvmagywrd pelsarffcr dpltgerwlr
      361 tgdhgwldae gylhfdgrrd qifklhgtrv saleieaaar eipgvseaav vppapgreaa
      421 llviasltpv evlralrarl dasrtpsvcr vvarlprnts gkldraalpe llmpesaina
      481 yqgdm
//
LOCUS       WP_357607090             194 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357607090
VERSION     WP_357607090.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 194)
  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..194
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..194
                     /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=20896
     Region          13..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msttgpapqr rmradarrny erllaaaatv faehgvdasl ediarragva ngtlyghfpt
       61 rqalleallr drmdaltara rdlldhpsph ealviwaraa mahtttyrgl vtalmrsied
      121 esselhaacr avlvggeqll sraqaagtvr edataadlya minavawage qttpaqgerl
      181 ltfsidglhp srsr
//
LOCUS       WP_357607152             310 aa            linear   BCT 28-DEC-2024
DEFINITION  YbgA family protein [Nonomuraea dietziae].
ACCESSION   WP_357607152
VERSION     WP_357607152.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..310
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..310
                     /product="YbgA family protein"
                     /calculated_mol_wt=33975
     Region          67..303
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mirprvaass cllgelvrfn gghsrdrfls galdahvdwv ricpemeagl gtpretlrle
       61 ssaagprlmt rktrldltdr mtalateraa gldvdgyvfk akspscgihg ipstggdrrn
      121 rgvfagvlmd ahpllpvede grlhdalire tfverifaha rlralfatdw tprdlvafha
      181 rhkmqllahd pvgyreagrv varagarpre elaadytrvf cttlarkagv grnvnvlhhc
      241 lgmitldaar radlvevias yqagqvalsv patllrhhar gegagyvrdq tyfspypeel
      301 glrnhvlepa
//
LOCUS       WP_357607188             135 aa            linear   BCT 28-DEC-2024
DEFINITION  tautomerase family protein [Nonomuraea dietziae].
ACCESSION   WP_357607188
VERSION     WP_357607188.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..135
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..135
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=14820
     Region          6..57
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpqffieapt gvrseakqkm mkeitaaida ayhipdvriw lreyapdqva qdgrlaaepi
       61 rplcfleape lasldakrrm agkihtaiae aydgiantee tlilmnhypl enagwagrlq
      121 sdnadiveam aelng
//
LOCUS       WP_357607179             489 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357607179
VERSION     WP_357607179.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..489
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..489
                     /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=52594
     Region          23..>335
                     /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 mkpriavlgg giaglaaaig lvrqgypvtl ierdppppad pgldpflawk rrgvpqfrlp
       61 hgfsarartl laahapevld qlradgieev nvfktfvppe lwepsdeeft vvwarrsafe
      121 lalrrcaeae pgitfrcpev vggllfapee pgpprvtgvr ladgqelaad vvldcgggrs
      181 rvsrwlaaag advpadtqdc qtvyfsryyr ftpgctlpkn amlvrgeles lmyigfpgdh
      241 dtfglclevh psenlqplrn twtweaaars ipalapwidp anatpldgvq imgghhnvrr
      301 rfvaggrpvv tgllavgdal cttnpaygwg asmaltyafa aaeavaahag dpvamalayd
      361 aatateadav yresaamdra riyritgqev peddraemer qrliaegvaa giltdvelsr
      421 afcrrinlag padavinnpe ivlrarenlr qlaaapavel gpgreelrei vltadarged
      481 rarlegshv
//
LOCUS       WP_357607196             148 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora purpureochromogenes].
ACCESSION   WP_357607196
VERSION     WP_357607196.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=16431
     Region          1..144
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msdrfvyhct lrwsdldayg hvnnsrfltl yeearvalmf aggrawgvgs fadgvvirrh
       61 evdylrpvdy algrataeaa ptvrielwve eirasrftva yelydgdvla starsvlvpf
      121 dlvakrprri tsderaflla yapaggaa
//
LOCUS       WP_357607197             402 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357607197
VERSION     WP_357607197.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..402
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..402
                     /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=43764
     Region          15..391
                     /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 mplriiiigg gigglclaqg lkqagvddvh vyerdasprg rmqgyrlris pegesalrdc
       61 lprraqdlla atanlrhelg laaydeqlnp qwapefgdar gdapdkidav drmtlrrvll
      121 agldgvhfdr rftrfeqvgd qvvahfadgg svtgdvlvaa dgagsqvrrq lrpdfrhldl
      181 gvrailsrtp raaaikaglp evlrdrfvnv tganglrlal mpmvfrdtpr eaagrlwpev
      241 emdpaedyym svfsvhrdvl gipdteflsm tgeqlrelvl ertaewhpdl rgvfahaeaa
      301 etypltlkat vpvepwgegr viplgdavht mpptggvgan talrdasvls ralaavarge
      361 vsledaaagy qaemvryate aiemslkiak wsmrkidvep ea
//
LOCUS       WP_357607222             284 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357607222
VERSION     WP_357607222.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=32788
     Region          10..253
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mikvrknpgr lwgisdlhvs hprnrqvles lrpqsdddwl vvagdvaelt pdiewalsll
       61 kerfatvvwt pgnhelwtlg gdpvqlrgee ryrylvemcr rigvvtpedp ypvwtgpggp
      121 vtiaplflly dysfrppevl rqdaldwarr agvvctdely lhcdpyptrd awcgarveqt
      181 errlaerdpa iptvlvshyp lireptlvlr hpefamwcgt erthdwhrrf dvrcavyghl
      241 hiprtswsdg vrfeevslgy prewlqwtrs gtvlrsvlpa eepa
//
LOCUS       WP_357607268             250 aa            linear   BCT 28-DEC-2024
DEFINITION  TenA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357607268
VERSION     WP_357607268.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..250
                     /product="TenA family protein"
                     /calculated_mol_wt=26527
     Region          1..247
                     /region_name="TenA"
                     /note="Aminopyrimidine aminohydrolase TenA (thiamine
                     salvage pathway) [Coenzyme transport and metabolism];
                     COG0819"
                     /db_xref="CDD:440581"
ORIGIN      
        1 mstradlsai arplvakvke hpfwtglrag tlppsslwyf aeqdaryvvp tyaralarca
       61 alaerdehgt llcsaasatf gslpklaagl selaaglsel aaglsepaag lsepvaglsq
      121 paaglpvags dstearpvih aytsfmlaap tisfaagiag llpmswfhlf vsedlrerca
      181 pgsryaswva qyppggdyag yvnaylamid evgahcsdld rkrlveqfli garfewafae
      241 aawrhqewav
//
LOCUS       WP_357607260             279 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357607260
VERSION     WP_357607260.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 279)
  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..279
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..279
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29215
     Region          1..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 mttveadgvt lgvehfgdta aplvllaggt tmlswpdalc ealarggrhv vrydlrdsga
       61 sitvdpeapa ytlrdlaada aalarelddr pahlagigvg gmvaqvaald hpdafsaltl
      121 agtrpvapgp vdddlpdhda atmdrlfsrs mpdwsdraav aefaaagaei lgddpvaara
      181 taerrwdrtp gtepavqman hlgmvfakld ckprwrerls elaipslvvh grrdpffpvg
      241 ngealtreip rarllvlera ataipdaaag evaaamlal
//
LOCUS       WP_357607308            1589 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Nonomuraea dietziae].
ACCESSION   WP_357607308
VERSION     WP_357607308.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1589)
  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 1589)
  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 1589)
  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 1589)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..1589
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..1589
                     /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]"
                     /calculated_mol_wt=167097
     Region          12..39
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          40..1454
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <1442..>1571
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
ORIGIN      
        1 mtatgkappm gtedklrayl krvtvelaqt rrllaeveer rdepiavigm acrypggadt
       61 aegfwdllrd grhavrevps trwdideyyd pdprvpggiy trygtflddi agwdaeffgl
      121 sprealrmdp qqrmllelaw eglenaglsp srlrgsrtgv mvgfmdtlqy grlqiewqgs
      181 dalsdpylgq gaipsvaagr iayqldligp tltvdtacss sliavhlaae slrrgecdla
      241 laagaslslh ptlyiqacag lmmcpdgrck tfdenadgyv mgeggglvvl eplskalang
      301 rriravlrgs avnqdgrsng ltapsrraqa dvitralaaa hvtpdeidyv eahgsgthlg
      361 daielsalhd vfggrpasrp llvgavktni ghtqaaagva gliktvlile nelippslnl
      421 stpaaaipgd gtvqpvtgal plprqdtprl agvssfglsg tnahlvlqap pspaspdrpa
      481 gkasaapyvl plsagseaal reqadrlagw leerpgsgla dvahtlqtgr aeldhrralv
      541 cadtgealrq lrsaaagghr vkrrpriafl lpgvgdqyag lgrelyaaep vyaetvdrcv
      601 elvrrrsgvd lhplffpegd tpagrpadla allgrareep gdshdpldqa aiahpflftv
      661 eyalakllgh wgvtpdllvg yslgeyvaac lagvftleda lhvvverahl isavpagrmv
      721 avaapedrir aalagsgaev dvaarngpam tvlsglpaei davtaalaad glacrplrsa
      781 hafhstllqp areklaavle gvtrrppaia ivsnltgrql tadqatstsy wadqlvgtvr
      841 fadgvrhcle qevsafvelg pgqtlgglvr qnltggtgga aavlgtltpr wnatesrqsh
      901 gdlvatcatl welgvdvtwd larpgrgrvl dlptypfqrv rfwpeptqpl petagtgtae
      961 padhtfaptw rrdpaarats lagrplpgpl vvfadpegtg taladlaaas gthvvevvpg
     1021 tgprregrrl tidpadpaqy aeafaglgdg pvhvahlwsl avpgakgaap pgdddlraav
     1081 ehgfhslmla vqalgerpar lltvtrgaad ilggdataph qalahglgra arheypgltw
     1141 sgadldpgap ldgaaphllt elltepgagd apdspdpltg wrrgrrwvrg wtpvpghaep
     1201 dlppwrpdgt ylitggtrgl gmalarhlvr agvrrlalla rtplpegdee varleaagae
     1261 vllltadagv peqlraalrr arehfgalhg vihaaglpag gllvrrtpae aaqvlapkvy
     1321 amgplaelvg pdtpenerle llvlyssavt afggigegdy caantvlday gqalagaaps
     1381 trvvsvawgp wqhdvwqser lgttggladr vaayrarygf addagcalld rilagghgsv
     1441 mavrqplrev ldawtnmldl dgllqaataa pqgerfprpr lridfaaprt eaearmadlw
     1501 gaylgidqvg vhdpffdlgg nsltgmamvl aiekdlgrpi apavlfehpt vaafaaaldg
     1561 ggdpgaqeal stssargqrr rrarsgnrk
//
LOCUS       WP_357607324             229 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357607324
VERSION     WP_357607324.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=24397
     Region          8..171
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mpdqadaagv rvwrvdldra gaprgwrlls raereralaf adpverrryv vahaalrtvl
       61 gglcgvpadr lgfgrdgsgr pcllplgrrp vpdfnlshsg awalvatapp garvgvdveq
      121 vragfdhlal arrfyqpeev arlraagpeg ffrlwtakea yvkasgvgla gmsdvlvreg
      181 sathatvlsr sarfpecrvr wldvapgyaa alvttapvtt astpaprtg
//
LOCUS       WP_357607353             406 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357607353
VERSION     WP_357607353.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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..406
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..406
                     /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=45178
     Region          70..393
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgrkpngass iykggdgywh grvtvgvkdd gkpdrrhvqa kteaevirkv ralererdng
       61 tvrktgqrwt vekwlthwve niagpvvrtn tldgyrvavr rhlipgvgah rldrlepehl
      121 eklyarmman gsaagtahqa hrtirtalge avrrghlarn paavakpprl pdaevqpysv
      181 pevqailraa asrrnsarwa valalglrqg ealglkwpdv dldngkltvr rallrpkwrh
      241 gcdgkceqkm pgqcpervnt rpvaadtksr agrrsvglpd alvdllrqhr keqeaerdta
      301 aqlwrdegwv fatptgesih qatdydewkr llklggvrdg rlhdarhtaa tvllvlgvsg
      361 ravmgimgws nssmavryqh mtdqvrrdia qqlggllwgt epsrhd
//
LOCUS       WP_357607372             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357607372
VERSION     WP_357607372.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..212
                     /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=23320
     Region          7..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqeglrerkk rqtrqrisev aiglfvergf envtiaevas aaevsvntvy nyfeskedlv
       61 lppeeaspqr ladivrqrrp gesaagavla rlreevrgre rrvglsagfg svlemmraap
      121 tlsarledlg rqmtdaltvv laeetdapty dllprvvawh igclhalvmt eigrrtaage
      181 rpdaiaeavl elldivesll gervlgyavr ee
//
LOCUS       WP_357607408             347 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357607408
VERSION     WP_357607408.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 347)
  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..347
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..347
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=38893
     Region          25..337
                     /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 mtgyrnpfeg qreplpselv ragfrqefad ldgalisyvr gpeggvplll vpgqmslwss
       61 yrlvmpklar rftvyaidvr ghgnsswtpg dyswdsagtd lahflrqvvg rpalvsgnss
      121 ggilalwcaa rvpeqvaaiv ledppifsae lprfrdrdrw vhsslahavq vlgdldhqrv
      181 adilrqeipv setrtvrmpd rfidfldrlv trhrrqhpgr paglgvrwlp rslsepiraa
      241 smfdpdfara fvdgrfygdf sheaalratt vpvlllhanw nryeryglvg amddddarrv
      301 relvpqtvyr ridarhvihd deprefiaav tdfadtlpss igsaprg
//
LOCUS       WP_357607418             287 aa            linear   BCT 28-DEC-2024
DEFINITION  urease accessory protein UreF [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357607418
VERSION     WP_357607418.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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..287
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..287
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28608
     Region          4..287
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mnpallllad srlpagghah sggteqavts gavhdvpsla rflrgrlhta gtvaaalaaa
       61 actqaatsps tplpaatsaa gsppatappr iapraaappg vtmpqraggp dagetafesv
      121 vtdagggvgf pwvlldaead artaapaqre asrtqgrlll rvarrvwpsp vldelardvp
      181 nphhpivlgv aahaaggtpe eaamaaayha isgpataavr llgldpvavh gllaeltpdl
      241 tavaaqahla aagahphlwg tlpaysspal dllaeqhara qvrlfvs
//
LOCUS       WP_357607419             104 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Micromonospora purpureochromogenes].
ACCESSION   WP_357607419
VERSION     WP_357607419.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=10626
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawivlvlsg lletawavsl drsagfsrpl psvvflvtlv lsmlglayal reipvgtgya
       61 iwvgigavgt agygmvalge saslarivcl llvvagvvgl klfh
//
LOCUS       WP_357607459             352 aa            linear   BCT 28-DEC-2024
DEFINITION  LacI family DNA-binding transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357607459
VERSION     WP_357607459.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..352
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36298
     Region          4..352
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 msekvtiatv arhaqvsrqt vsnvlnsphv vreetrrrvq eaidslgyra sqaarqmrtg
       61 rsrliavrie ptrdgingsv ldrflhglte taeaagyram lytaadaaae iatfddllsa
      121 ydldgfvltg tdhgdprtaw laergvpfvt fgrpwddpda hpwvdvdgaa gtaqatghll
      181 aaghrrigfi gwpagsgvgd drragwreal raagvdptgl dreavdgiae gerlaadlla
      241 aaspptalvc asdslalgal qaaraaapst gtaadtaaps tgtaahtaap avpvigfddt
      301 pvaaavglts vsqplgdaaa rcvdlltavl dgpprtpapv llqpslvlrh ta
//
LOCUS       WP_357607514             299 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nonomuraea dietziae].
ACCESSION   WP_357607514
VERSION     WP_357607514.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..299
                     /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=30466
     Region          22..297
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mtpvqvreas raaparwspa pavfvvlwss afiagipgvl aapplllmfa rfavagvlla
       61 gyalvrrapw prgrtlahva lsglliqavq fgafysalga glpaavvslv qglnpvvivl
      121 asrllgerig agqwagfalg aagvvlavad rvslsplgva lclaglagls agtlyqqrfv
      181 prmhaltgta vqllvsapav glaclaagpv rvsdwsafgl svawmalvns iaafillnrm
      241 llrspasrvs tvffltpavt avlawllagq plhplaiagl vlggcgvlla nlstrtrvi
//
LOCUS       WP_357607558             111 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            dietziae].
ACCESSION   WP_357607558
VERSION     WP_357607558.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (residues 1 to 111)
  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 111)
  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..111
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..111
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12255
     Region          5..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msdydvflad cparttldli adtwsvvvvf glghgprrys dlrdqiggis nkmltqtlrk
       61 lergnlverr tlatapagve yrltrlgesl lepvsvlarw aeehadelad d
//
LOCUS       WP_357607605             349 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357607605
VERSION     WP_357607605.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=35401
     Region          1..349
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mritvigsgi vgagaayhlt lrgaevtvvd ggrageataa gagivcpwvd hedddawyrl
       61 alegarhyav lpesvgharv gallvaedpa elepvralla aryaeapemg evrqvarpse
      121 lfppldpkls allvpgaarv dgrvvrdgll rsavrrgatv hegsasltgd gvvtvsggar
      181 leadvvivaa gawtgqvcgp lgvdlpvfpr rgqivhatle gadssawpiv lprrgpyllg
      241 fpggrvvvga tveevgfdpr itvaglnevv aaglavapgl agatltetrv glrpvmatgr
      301 pliarvsdrv vavtglsayg ltagpfagll aaglalgekp aldlapfai
//
LOCUS       WP_357607602             464 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea dietziae].
ACCESSION   WP_357607602
VERSION     WP_357607602.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 464)
  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   2  (residues 1 to 464)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..464
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49083
     Region          2..456
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mvrttagtvr gsregglsvf kgipfaqapy gehwlaapap arpwdgvrea tafgprpaqv
       61 siapgvpews aaeglecltv nvwtpdeggs glpvmvwiyg gayqagsadm peydgsllaa
      121 egvvvvtfny rvglqgfghv dgapanrgfl dqvaalrwvq dniagfggdp grvtvfgesa
      181 gagsvaalms mpmarglfgr aiaqsvpgtf fstayarkvs rdllegrsah dcspeellaa
      241 arrfvarskg valpfspvvd gevlpetpwe afadgagsdi elvvgynrde frmfaamapp
      301 atehdlaevl kefalpdadv vyrtahpdag avelynvals dwlfrmpsal ladahagaty
      361 ayeltwapte lgachaldvp ltfgtvngal agwiirgape aeavsrqfrs awtrfaktgd
      421 pgwpayepva asthvfdvep sdvrdpeaas ralwskrgfp vide
//
LOCUS       WP_357607637             278 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357607637
VERSION     WP_357607637.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 278)
  AUTHORS   Rosinski,J.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..278
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..278
                     /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=30270
     Region          29..>73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          102..264
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mnraeladvl rtararvrph evglpagtrr qvpglrreel atlaglsvdy vvrleqgrgp
       61 rpssqviaal aqalrldddd rdlvfrlagh qppqagriam vvrpsvlrll drmadlpvlv
      121 lsakgdvlaw nplgaalqgd msawpqrqrn liwqrflgss rcqvavgpde ddaagrasvg
      181 tlraaqaryp ddpdlvrlia elrrgsprfd elwregrssp wrtatksvsh pslgtvsldc
      241 damllpdghq tvlvysaepg saqatvldml rvlglqqv
//
LOCUS       WP_357607654             258 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357607654
VERSION     WP_357607654.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=26546
     Region          6..258
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 midpqlsvqn vlvtgggtni ggaisrafaa qgarvavhyl aqeppapdgt awahltptaa
       61 saerlateig gvavsadlsh pdcarqlvda verrlgpinv lvnnaahces adtldtfdaa
      121 slerhyrvna vapalliaev arrhtagvpl cvvnistdaa rafpgqigyg tskaalealt
      181 ratalelgpr girvnavapg pvqtgwmtea ivehstsvip mgrvgepsdi sdavvflasr
      241 qarwitgqvl qvagghal
//
LOCUS       WP_357607665             321 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357607665
VERSION     WP_357607665.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..321
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..321
                     /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=35224
     Region          2..319
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mllevsnlvk hypittgalv khvvgqvkav dgvsfalspg etlglvgetg cgkstlarci
       61 aglhpvtsgt vrfdgaditn lprrrmrpyr rdiqvifqdp ygslnprrrv gsiiadplvi
      121 hrvmsgdrlr ravqelmerv glnpehynrf paefsggqrq rigvaralal rprliicdep
      181 vsaldvsiqa qilnllkdlq aefgltylfi ahdlsvvrhi sdriavmylg kvvelgdaes
      241 vyerprhpyt nallsatava dpdeaqrrrr ivltgdvpsp idppsgcrfh prcpraqeic
      301 ssvepllegs aachfpievv v
//
LOCUS       WP_357607683             417 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357607683
VERSION     WP_357607683.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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 417)
  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..417
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..417
                     /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=45762
     Region          1..382
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mklrynyrly pdagqrqmla ktfgcarvvw ndalaarkaa rkagrpfigd aeiqrvvltq
       61 akktperawl aevssvvlqq svrdvntayr nffdsvsgrr kgpkmglpvl ksrhdrrqsa
      121 rfnanaftlt gegrlylaki gqvevrwsrg glpvapssvt vikdaagryf asfvidvlda
      181 dqllpevgte vgidlglthy avlstgekia npkwlrrrek klarlqrels rkqkgsknrd
      241 marlkvarqh aevadarrdf lhqtstsilr enqtvcietl svrglarsrl akavhevswg
      301 afirlledka arrgrtlvkt gryfpssqlc pccgrqtgkl pldvrewdcp gcgehhdrdi
      361 aaainilteg trcigisgst vaaglaghgi ndcggqvrpg aanptlappa thavqaa
//
LOCUS       WP_357607770             149 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357607770
VERSION     WP_357607770.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 149)
  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..149
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..149
                     /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=15873
     Region          24..140
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrlsarvdya lraaaelaaa gagpttvgel akeqdmppky lenillqmrr aglvrgqrgp
       61 eggyvlarpa adisladvir avdgplanvr gerpehvgyr gpaeslqqvw ialratersi
      121 leevtldnva tgalpervrq laadpaawd
//
LOCUS       WP_357607798             264 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357607798
VERSION     WP_357607798.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  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 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   3  (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   4  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..264
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..264
                     /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=28424
     Region          2..216
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilmtgaag kvgtllrprl aregrtlrls dlhpvepgpg eewvtadlad paqvaeamkg
       61 vdavihlgge sreapwadiv qanvngtqvl leaareegvr hlvlmgshha agfqtrpadg
      121 sdlpdyafpr pdtfygvskv vmealgslyh drfgmnvtvv rlgtcneapg dtrglatwis
      181 addltrliea altapgyhvv wgvsdnarrw wsleeaksig yvsrdssepm aaaliaeqge
      241 pdlsqplhdr aggvftlnel gerw
//
LOCUS       WP_357607800             399 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea dietziae].
ACCESSION   WP_357607800
VERSION     WP_357607800.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..399
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44131
     Region          4..399
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 msqlegvfre eygravavlv rafgdidlae davqdafaea trrwpstgtp pspagwiitt
       61 arnraidrlr restrderha qaalmtatgq tdqvegpvhd drlrliftcc hpslstaaqv
      121 altlrllggl ttaeiarafl vpeptmaqrl vrakgkirda ripyriprea dlpdrlravl
      181 svlylifneg yaasagdrlv reelcaeair lgrllaelmp depevwglla lmlllqsrra
      241 arttpdgrlv plaeqdralw dhdliaeghr ivrrclrrdq pgpyqiqaai navhsdgppt
      301 dwrqilalyd qlllftptpi valnravava evkgpavale lvddldlggf hlfhairadl
      361 lrrtgrdaea lraytaaiel ttnaaerafl rtraeaiar
//
LOCUS       WP_357607804             309 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357607804
VERSION     WP_357607804.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..309
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..309
                     /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=34331
     Region          12..288
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtstltpapg rtatphrrtk rvrwrgplma wlflapalll flyfkfipmf vglwksffkv
       61 qtflgdewlg lenyktiisd adfaaaiwhs ivlamgttig slvlglgfal liegparylw
      121 fvrtaaflpv vttmaavaev wrimfhpads gmlntiigwa gidpqpwlas ehsslwsiml
      181 msiwrgtpyd mmiflaglvg vdrtlyeaaa vdgastwhrl rhitlpalrp vfwilftlaa
      241 irglrvfvev yvltnggpng ssevlmtliy klgfqkndlg vasaggivlf latlaltlia
      301 qmlrrrqar
//
LOCUS       WP_357607837             422 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357607837
VERSION     WP_357607837.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 422)
  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 422)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 422)
  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..422
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..422
                     /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=44589
     Region          226..421
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrepsrivpt alrlgtivll agaqmtatpa pgltgtslai tlmtialaga latvlllsir
       61 rterpvarrr avnppaalrr srlhdlplwk alrrpaspvw npsreepqag dhapaeghrp
      121 vlvfgvpval ialglavils ialgslsrgg aaiavllicv slavtrfpmr qalpigvlav
      181 vglvvagaia gnpaqdlpli lsncliflls yaakqrratr aaqareavla erariareih
      241 dilahslsaq lvhlegakll lraersaeal ervthardla ksgleearra vaalredppa
      301 lpealrtlae dfestthhpc tlrvsgperr lppetelalv rtaqealtnv rrhapgspat
      361 velefgppwc elrvtnpasa ekgspgggyg lvgmrerael lggtlsageh dggflvhlkv
      421 ps
//
LOCUS       WP_357607926             260 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357607926
VERSION     WP_357607926.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26931
     Region          1..259
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mgpltgrtal vtggsrgigr aivqrlaadg asvvftyasa eaaarrvaae idlevgalrg
       61 sadggawpvr ldltdlddiq rlfataftta herfpepgld ilvnnaaiaa drpisevtea
      121 dydhamavna kgvffaiqha lphlrdggri inlstvsttw pspgealyta skaaveqfsr
      181 vaakelagrg itvntispgp tdtdllreat teqqrqavat mtplgrlgtp advaavvafl
      241 agpdsgwvtg qnihvdggli
//
LOCUS       WP_357607964             381 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357607964
VERSION     WP_357607964.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..381
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39857
     Region          75..377
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mgpvtgratl dgraepdstp srprrgrgrg klvaglltvv avagggfvav nsagllhgga
       61 gptrsadalp patttvtrqt lndtrdadge lgygpvttam srkpgtitwl pdsgaqitrg
      121 rslyrvdnkp vmlmygstpa yrdlkvgveg kdvenlernl sklgydgftv ddeytydtae
      181 avrewqedrg ldetgvvelg rvvfapgkvr vesleseegq ptapgqkilt ytgtskvvtv
      241 klesedqrma rkgakvdvtl pdgknvkgkv tevatviepg egqnadpetr vealvsigaa
      301 kaakgldkaa vdvtftastr knvlavpvaa lvalqeggyg levieggrsr yikvetglfs
      361 ggrvevsgdg laegmtvgmp k
//
LOCUS       WP_357607974             256 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357607974
VERSION     WP_357607974.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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..256
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..256
                     /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=27607
     Region          11..239
                     /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 migyvqtavs ldvrgvryay pdghlaldgv dltvprgerv allgpngagk ttlvlhlngi
       61 ltptegtvsv ggltvsrdra elaevrrrvg ivfqdpddql flptvaedva fgpanlglrg
      121 aeltervdea laavkmsehr draphhlsfg qrrrvavatv lamrpeilvl depssnldpa
      181 arrelaeilr glpvtllmvt hdlpyaaelc eravildagr ivadartpei lgdadllarh
      241 rlelpygftp hslprp
//
LOCUS       WP_357608063             388 aa            linear   BCT 28-DEC-2024
DEFINITION  homogentisate 1,2-dioxygenase [Micromonospora purpureochromogenes].
ACCESSION   WP_357608063
VERSION     WP_357608063.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..388
                     /product="homogentisate 1,2-dioxygenase"
                     /calculated_mol_wt=43353
     Region          1..385
                     /region_name="HmgA"
                     /note="Homogentisate 1,2-dioxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3508"
                     /db_xref="CDD:442731"
ORIGIN      
        1 mpyyrsvgev prkrhtqfrq pdgslyaeel mgqegfssds sllyhryppt aivaaeeftp
       61 paytrvpnlp lkprhlrthk ldgtgadpvl grryllandd vriayvladr psplyrnatg
      121 declyveagt lrvestfgvl davagdyvii ptstvhrlvp tgdvptrlla veasghigpp
      181 krylsvrgqf lehspycerd vrgpdapllv dgtdvevlvr hrrgwtkhvy anhpfdvvgw
      241 dghmypwafs ihdfepitgr ihqpppvhqt fqgpnfvics fvprkvdyhp daipvpynhh
      301 nvdsdemlfy tggnyearrg sgieqgsisl hpsgfthgpq pgaaersigv dffdelavmv
      361 dtfrpldlcd aagecedegy awtwsrrp
//
LOCUS       WP_357608026             304 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608026
VERSION     WP_357608026.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  AUTHORS   ter Beek,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..304
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..304
                     /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=33016
     Region          3..301
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 merlrkygfv agflvvpitl ysvfvispyv qafqlsltsw ngyssavryv glenfgrlfd
       61 devfwqalrn hgimllvlpi ativialfls fllnlgggpr gagmrgvwgs tfyrvvfffp
      121 qvlavavvgv lfqavyrpda dgvlngvlav fgaapvgwlt epglalwsii avmvwqgvgf
      181 yvvlfsagma aipkdyfeaa aldgagrvrl ffsitlpllr dtvqvgwiyl giaafdgfal
      241 vqvlagdkge pdgattilpv tiyktafayn kvgyasamgv alffltvtfa vltlrttrre
      301 rvel
//
LOCUS       WP_357608085             312 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608085
VERSION     WP_357608085.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 312)
  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..312
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..312
                     /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=33854
     Region          <2..277
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mglpvlksrh drrqsarfna naftltgegr lylakigqve vrwsrglpva pssvtvikda
       61 agryfasfvi dvldadqllp evgtevgidl glihyavlst gekianpkwl rrrekklarl
      121 qrelsrkqkg sknrdkarlk varqhakvad arrdflhqts tsiirenqtv cietlsvrgl
      181 arsrlakavh evswgtfarl lagkagrygr tlvktgryfp ssqfcpccgw ktgklplevr
      241 gwdcpscgeh hdrdiaaain iltegvrsia atgstvaagl aghgindcgg qvrpgeatpt
      301 lappatyavq aa
//
LOCUS       WP_357608077              60 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608077
VERSION     WP_357608077.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 60)
  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 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   3  (residues 1 to 60)
  AUTHORS   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..60
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..60
                     /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=6628
     Region          2..60
                     /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 mskreaevmd liatgqsngq iaqrlflsek tvknhvnriy aklgvdsrvt aiglwlsrqe
//
LOCUS       WP_357608093             559 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608093
VERSION     WP_357608093.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 559)
  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..559
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..559
                     /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=58391
     Region          11..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,89..92,96,98,135,137,
                     139..140,142,152..153,156,168..171)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,89..92,96,137,139..140,
                     142,152..153)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,96,98,135,137,139,156,168..171)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(152..160,165..171)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mygdgrwgvp gytevrqlgs gatgrvvlar rdrdgaevai kylsdelksd vafvarfrhe
       61 arllgtvqsk hharlidyve tgqgaaivme lingvslrei lrsegptgpe aaltvlkgsl
      121 qglasahaig vvhrdfkpen vmvqddgtsk lvdfgiavra gdgvsvagtp pymapeqwsg
      181 grpapatdvy aatvvffecl tgtrpfrast laalarqhqs aappvedvpv plrgliergl
      241 akdpaerprs aeaflaelea vaaegygrdw eergrrrlat lagllvllfp sepaepaqaq
      301 tslaetrfsg psrilgklsa kvaiaasaag vlivaavvlv nvsmdepalr aqtstvtptt
      361 aapatiepte teeeepapta eettpeestp tptttstqsa apppvrptas trptrtptpr
      421 ptptpvrtpp trtkkptstp tpdqpqvtgt aqdpegqrpp sssapapdpt pttatsqpsq
      481 tpgdpsqgpq eggntggeap tkgeptgggg septpeqprl dragraqaaf vaiglmtsga
      541 vpvtlavkrr magrhrrkr
//
LOCUS       WP_357608143             893 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357608143
VERSION     WP_357608143.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11467590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=93812
     Region          <1..850
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          829..886
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlhgraneqa eierllegar nghsgtlvmr gpagigksal lgyaagraag mrvlrgvgie
       61 seaalpfaal hlllrtgldr ihalpdpqaa alrgalglge appesrflvg latlsllsel
      121 agdgallcli ddaqwfdqas tdalvfaarr leadgiamif aarpdfpapg ldelrlggld
      181 staaaallpa dlppqvrerl iqesdgnpla lielpaalsp eqragrlspv gampvadrvq
      241 aafhaqmael pehartalli aaaggsgela tlvaagaslp gleaaersrl veirgsivrf
      301 rhpliraaay qsasvsrrla vhraladalt sstapaaadr rtwhlaaaal gpdedvaeql
      361 eeaagrartr gghaamaaay eraaeltadp vrrsarlaaa alaasdaglm rraaaladsa
      421 tpdvddptmi laltqvrahr efelgtplaa griimdtvpr vaahateqah wllveavrca
      481 wfagdprlae qaaaklhalp gsplvsqaig ltrllrgdip ggiklisevl dlpalaglgv
      541 pgltftagvc lpagraalce eitgrvvaec qqsgmigwla falqdhgfaq gllgaygeal
      601 atldaglrla telghehrvt hltsciawvl ahqadvpgcr ekaeegvrra ddqglvlaas
      661 igrwalgrle lglghpeaal rqlaaipptg vgvlcaadqi eaavrsdqpd rakepleryl
      721 twarqvgqpa sdaialrcra lvdqdeahfv eavrvhesgd qpyeqartrl aygewlrrar
      781 rradaraqlr galkifdrlg aelwagrara elratgdvpa aprragdpls vltpqerevv
      841 rlaaggaanr digaqlflsp rtvgyhlyka fpklgitsrs qlaaivrsss idc
//
LOCUS       WP_357608195             171 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608195
VERSION     WP_357608195.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 171)
  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 171)
  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..171
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..171
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18917
     Region          <14..>117
                     /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 msgiadplkp swfglphwlv gavlilalfg afqvyywvgr rlgeklydsr vgvrvgreri
       61 akieqvvekw galavygcfw vpmlrhtlpw vagalrvsyp wyvvasalgc ltwaplwwfa
      121 atavvwgwle laarspvtaa vvavlavaai swavvrrrrk rraassealv s
//
LOCUS       WP_357608219             364 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608219
VERSION     WP_357608219.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=39416
     Region          1..326
                     /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 mrvivigagv aglalargll hagheaevye eapeprtagg svtlwpgsta ilrelradha
       61 gigrrletle swapdgrrll tvdltaaerr yghpvvhvar selvelladg vpvsygvpae
      121 hvvperaear lsdgrtvrgd vlvgadgrrs vvrralwggd paelsgwvtw qgfttaptal
      181 tvgrravmia dtngvcglip agegrllwwf dvrsapgrpf wdddphvvgr lrerfrgwad
      241 pvpavletie epgffphhrq piptvwgrgp ttlagdsaht mppamaqgan qaledawlla
      301 hslgdlraye rrrskvvrrp arlaaaeptn taqrpaagll pdglvtrlyt vllrrystyl
      361 ltvs
//
LOCUS       WP_357608268             184 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357608268
VERSION     WP_357608268.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 184)
  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..184
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..184
                     /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=20496
     Region          1..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maskrdwlea glevlseega paltierlca hlsltkgsfy hhfggmaryk sdllehfese
       61 htgryidgae sagdsarakl yhllnlvldd kdtdhdleia vrawalqdae aralqrrvdq
      121 lrvdylrslw relsgsedda gpmgrllylv lvgaqqvvpp vsagelkeiy alalrlapqe
      181 rrse
//
LOCUS       WP_357608271             302 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357608271
VERSION     WP_357608271.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 302)
  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 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   3  (residues 1 to 302)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..302
                     /product="GlxA 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=32901
     Region          4..286
                     /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 mssvvfllip qvhlldvagp aevfstaddl gyaytfayva edsqvatvqg ltlsavtrwp
       61 rlapddliiv pgrrgparsp arqtlrrlre hhasggtvag vwagtdalgr aglldgrrca
      121 lhhcaqeefa rlypraevvk dalyveddri vtsagvasgi dlalhllsmr hgpnaagrva
      181 ramlahahrd agvarlspml rrrshvdqtv hriqdliesr fterlplrll akaagcsert
      241 vtrlfrqatg itplayqtal rleraehllr qgattevaar eagfrdartl rrlrargraa
      301 ss
//
LOCUS       WP_357608302             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357608302
VERSION     WP_357608302.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=34176
     Region          34..312
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matpvlerta arpavrvegi gpfeaarrrm vgpfllpall vyalvmivps vftvwisfnd
       61 wagagpmewa glgnytemia dpvfgqsfvn tmkilfgvgg avflvsfvlt mllqdmvgrk
      121 fvravvffps lvpglviail wgfmldpdgl ansvlealgv aepplwlape nmfttvmagm
      181 twlaagtytv ifmaaadrip rafyeaaeld gasavrrfwh itmplmwdvi gvcavlwaig
      241 alktfefvlv fagatgslpp tglwtfsvya yagafpsdgv prygiasaaa vltmvltvvl
      301 tllvrrvmgr rertdy
//
LOCUS       WP_357608369             956 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608369
VERSION     WP_357608369.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 956)
  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 956)
  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 956)
  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 956)
  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..956
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..956
                     /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=103359
     Region          8..247
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          138..952
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          745..773
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(746,749..750,753..754,756,786,789..790,793..794,
                     796..797,820,829..830,833..834,837)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          784..814
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          862..894
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          905..932
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mggngetrlg vlgsievvrd gravtvraak qrvalatlll sasrpvtvde lieriwdgra
       61 psrargavqt hiarlratls ddgrlietrg ggyviepgsa vidllsfrdl tgraaqaddp
      121 alaaellera lalwrgpala dvpsdslhqd hapqlaeerl ralehwfeln lvlgrheqii
      181 pevtavaath plrerlwsrl mlalhrsgrq aealeaylti atrlreelgv ypgeelrrlh
      241 egiladapds adlapsaelm asahltapaq ltapaglpva tvgpaqwvpr qlppdiarft
      301 grhaelerld elltevdgra gasepiviaa vggaggvgkt alalhwahrv rdrfpdgqly
      361 lnlrgfgpgp vmepapaldt llraldvpae ripadldars allrdvlagr rvlmvldnar
      421 dpaqvrpllp gshsvvlvts rnslgglvar egahrisldq lspaesvall geildadrvn
      481 aepgaaeela rlcahlplal miaaerasrp asgalakfvr qlrdeqarln vldtgddvea
      541 nlravfswsy haldpaaarl frllgvhpgn dfglesaaal tgvapaevrr lldrlvdahq
      601 lqqrrpgrye fhdlvrayaa eeaagdphes daavrraldw ylhgaanara wlrpgqpaip
      661 vpehgvepps fgndrealdw ldgerpnlla airqaaelgl hshtwqlaea twvyfelrqa
      721 wddygaaqli alesarragd ayaeaqalda mgnlyhrtdr lddardcveq alrlfqrlgd
      781 rsqeaialah latvrylegr lgegidlakr sltiarqsgd aqgqvlalna laatytlahr
      841 heeaieaagv avdvqrtlnd rrglayvids lgdahagsga ldaaaaryrq alelnreign
      901 rraeavnlkn lgrvqlraar ldeareslge alliledlgn pdaahvrsll reidgl
//
LOCUS       WP_357608443             156 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357608443
VERSION     WP_357608443.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=16878
     Region          25..153
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mstgdmrhlg ddpatparlr ripsrllsia aaqadrsvsa glaaadahkw hyavlaaldd
       61 sgqasqatls rrtgiyrsdl vsvinelagr glvrrehdls drrrniitlt aegreqlsrl
      121 dhlvsalqdd vlaplspaer eqlvglltrl vqhhat
//
LOCUS       WP_357608482             381 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357608482
VERSION     WP_357608482.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..381
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40847
     Region          31..364
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 meikimrgar vagavtagll allavvpaqa atltrtepaq dkslalpapt gaqpvgtvsl
       61 hlvdhgrpdp wvpsekarel mvslwypaak gagrpapymt deeaeallkg qnltgvpsev
      121 isgakthatt garpagrkga lplivlspgf tmsrssltsl aeelasrgyv vagidhvhes
      181 ygtslpgdrl agcaackeqe adpwafgaka vkgrqadvsf vldrllgrhp vwkgarlidr
      241 shigmaghsv ggssatwtml kdsrvragvn mdgtffvpip dkglarpfml mgagevhepg
      301 gkdftwgrdw armtewkrwi tveggdhtsf tdyplltkqs arelevtray vvafmdrhlr
      361 greqqlldgp satfpeakfw k
//
LOCUS       WP_357608493             432 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608493
VERSION     WP_357608493.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 432)
  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 432)
  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 432)
  AUTHORS   ter Beek,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..432
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..432
                     /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=45383
     Region          22..322
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mnklsasgal alaamlalsa cssgtsgtsa apssrgssgg kqkvtflvfp spnlpesywk
       61 aqvalvtkad pdldvelvaa pseserndya kqlaasgqlp dvqigmqdli alepslapwt
      121 eqelkdflcp tcgavngkvl qlpantqtip nvyyskklfk tagiaappkt yaelladaek
      181 lkaagitpfv sggafvtsqp wtailatdly artpgwiakr ragqvtfagd pamkaatqkf
      241 adlaakgyid krqigqdypk tqeaflagkg amypmgswfa aaadqsdmkd digvfawpsd
      301 dgslhlpaft ggglsvsata knlaaakkfa lafqltrenl dasvkadalf pavkgytpps
      361 ttgpvfkavy dlwqqaikqn atvpafgwea gdaamlpgmq gkfwsaaqdl vsgkkttdqt
      421 lafldtewek sg
//
LOCUS       WP_357608530             967 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608530
VERSION     WP_357608530.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 967)
  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 967)
  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 967)
  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 967)
  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..967
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..967
                     /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=104564
     Region          8..242
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          109..964
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          729..757
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(730,733..734,737..738,740,770,773..774,777..778,
                     780..781,810,813..814,817..818,821)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          768..798
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          809..837
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvveqpvfsv lgplqvrspe gllriagrkp rlllasllld anqvvssdml vevlwprtqp
       61 ssavanlrty vsslrsagvq ivaqpsgyai eidaerldal rfeelvtmar aagrtdeafe
      121 hlrralalwr gaplsdlpas plwdgrlral tqarlaaaee laelklarge hagaiddlrr
      181 ligehpyred lwqrlilalh hsgrraealh ayttirrqlv delgiepgqd lrdvhasvla
      241 gdpapapvta gdpppapaaa phqlpadvpd ftphqlpadv pdftgraadv aaltralsag
      301 erppdgppsi avvtgppgvg ksalavhcah alraeypagq lylclggtdt tpadpldlla
      361 ealralgvae qalpptlrer aslyrsllar rpmlvfldda adtaqvrall pghgcavlvt
      421 srrriaelpg alqleldvlp peeaeellak ivgaervaae reaaqailhs cghlplavrv
      481 agarlagrpg wplsvlrqrl ddetsrldel ragdlevrgs felsyrrlpg daalafralg
      541 llgsqsvpgw vadavldrhr sdtvvdtlvd anllrlagtd pvgqpryrlh dlvrcaamek
      601 agaptidgae rhalvrvlgg wltaaehaaa rlpttlfglt sdgaprwsle retlgrltae
      661 plawfdaehe slvdavrlaa gaglaqsawg laatlvpyfd lhcrldewqs thrvaldsar
      721 aagdrhgeaa mlrglaqvcl yqdryaeagd mfrraraifh elgdtrseai sicglaavnq
      781 fsgrhlralg sfrhalamfl aigdrsgeay arqaigrvyl slrdvrqasr wlgdalrlae
      841 elgdahregc vsmqlgrlyd lvaesdramr fqghaldife algdrhcgay amrnlgglqv
      901 argdrsdgsd qlerslvifq qlgdrsgead tyqslgelyh ssgrsvlarh ylhqarelrr
      961 elsesfa
//
LOCUS       WP_357608532             257 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357608532
VERSION     WP_357608532.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 257)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..257
                     /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=27199
     Region          27..>137
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          96..245
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 makraerpgd pakligllwr pteavsrsgl tpkvitraai aladqdglda ltirrvagdl
       61 gvstmalypy iagrsellel mldavaaevy ahttppaqag qwrariehia qanwdhhmah
      121 pwtvdiaagr pvpgpgisgk yeielsaldg lglsdiemdq tltailglvs naaretislr
      181 rirqessltd tqwwesvgps lgkamagasy pvarrvaasl geatglatdp egafrfglgm
      241 lmdglgtlig argrhpl
//
LOCUS       WP_357608564             333 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608564
VERSION     WP_357608564.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 333)
  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..333
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..333
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35424
     Region          10..>67
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msasgedair qlgaalrarr laqglslral arevglgghg tlvdyehgrr lppldlltaf
       61 ervlkvpqge llqlraaala ergrdeaarl lkkpppgptp apadapprlg vsseeqspss
      121 aghgtpqsvv taperrhrrv wfpfvialti slvvaatlvt asrlpnwpas artavnapyt
      181 paptvrmdfe qpgerlsvfw gsqvatagvt stvarhgrqa vlvtvkgasa ekgysavgvt
      241 hgltglrpgm kvtvwlwvpg aqpgglrffa mnsaskpvwa petleteial pmragwssvd
      301 wtipqvdrlh aigmqfyaet datmsvgida itw
//
LOCUS       WP_357608588             351 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357608588
VERSION     WP_357608588.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..351
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..351
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=36968
     Region          50..351
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mhvrrttarl aaavvaalal gvssapvpat aappatrlaa pgdpeggtpa lraqldaagk
       61 gwidakaale rsikrqreln dqlkniesel avrhgkvgei agvayrtgrl gpvsallnss
      121 spegfldraa aletvasned relrsliqtr ddatrtraal dkeiveerkq vavmakrkqq
      181 aeralavaaa dkpaaradsg asrgtstana rpaprnpdgs wpsescsvnd ptpangcitp
      241 rmlnalkqsq aagftryvsc yrpsgsgehp kgracdfaaq ksgfggdatg gdrtygnnla
      301 ayhvrnadrl gvlyviwyrq iwlpssgwks ysgaggdpss dhtnhvhlsv y
//
LOCUS       WP_357608593             453 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608593
VERSION     WP_357608593.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 453)
  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 453)
  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 453)
  AUTHORS   ter Beek,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..453
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..453
                     /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=48422
     Region          27..343
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mnkkwlsaav amlaattala acssdggagt saasgggasn ctntipkknl pvvtmwgwyp
       61 nmqlvvdnfn kqngevqicw tnvgqggdey dkfqtaisag tgapdvimie mdriptfqiq
      121 kalvdikkyg fdavkadyse gawkdvsvgd avygvpvdgg pmamiyrkdi fekydikppk
      181 twaeyeqaaq kvkdaggpaf gdfaanvsal mmalqiqkga apftyspaqq nsigvklndq
      241 askdvldywa rlakkglvgt qdqftpeyis gvingkyaty isaawapgyl tgagvgkgkd
      301 tgkfavaplp qwdpanpvqv nwggsafsvt sqaknpelaa kvaygfyadk eslthgwtnq
      361 iifplnlkal ndpefvnlkv gffggqqank evyvpaanay kgvtyspfgq yyfdamtkqi
      421 saliegsvtg aqaadrlqed vakyakeqgf tvq
//
LOCUS       WP_357608595             705 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357608595
VERSION     WP_357608595.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 705)
  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 705)
  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 705)
  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..705
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..705
                     /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=77395
     Region          5..705
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mtdqttleqe iaaeqrhldr vyarlaelrr saaqaekegy rlarvgnfga lverdamvfh
       61 aaqrryvlda eheglvfgrl dlrtgqvlhv grlgvrsena etlvvdwrap aaaafyqatp
      121 aeplgvvrrr tiqssaekvt rieddlldpe sapaemavvg dgallatlsr atgrgmrdiv
      181 atiqreqdea irspgsgvti vsggpgtgkt avalhraayl lysdrsryag ggilvvgpss
      241 vfveyiasvl pslgeetatl hslgslfpgm satrtdppev aavkgslrmr kvleravrda
      301 vpdgpdelrl lyrgellrle rreldgvrdr alsrgarrne vrrvafdavl aalyaqarrl
      361 avtrlpeqra fedeiidrpe freflkawwp rlhprhvlgw larperlrry aggilsraet
      421 allveayrtl daqgltvadi alldeldall gkpvrparak rdpyqlaggv relstfadrq
      481 raaraaarer pedyrdyahv vvdesqdvsp mqwrmigrrg rlaswtvvgd paqtawtgdp
      541 qeldrardqa lgrrrrhrfa lttnyrnsae ifavaaaeir rlypdlklpt avrstgvepv
      601 alavaadrlp aatvqavdal ltevegtvgv itpvprrdev agwlggrggs rlqvvtslqa
      661 kgmeydgvvl iapseiradp gsgvrtlyva lsratqrltt idptp
//
LOCUS       WP_357608610             320 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608610
VERSION     WP_357608610.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=35408
     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 mreerarasg tpapsesgrp sgwrrfrrdr slllmilpal vltvvfayvp mlgvvtafqs
       61 ydiysgftgs pwigldnflq lfrdelfwrs mentlvisav qlvlyfpvpi alalilnsvl
      121 sdrirsfiqs vvylphffsw vlvvtlfqem lggagaintl lrrfgmptwd imtnpdafkf
      181 lvtaqavwke agwgiivfla alaaispaly eaaavdgagr wrrmwhitlp gmrgvivlml
      241 vlrlgsalsv gfeqmliqrq avgrdasevl dtfayfygvv nnnfgfgaaa glfkgvlsli
      301 liiaankvah afgedglyrr
//
LOCUS       WP_357608665             283 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608665
VERSION     WP_357608665.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..283
                     /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=31221
     Region          <4..255
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mttlevadlv keyrvrgdgm rrtrlravdh vsftltpgrt talvgesgsg kstvariiar
       61 lerptsgtvv lngagsgdyr dhvqmvfqdp faslnpfhtv ehhlarplrl hgrartraet
      121 rqevarller vnlpaeelaq rrphelsggq rqrvaiaral apgakvivad epvsmldvsi
      181 rldvlkllar lqqeedlail yithdlatar hfaddilvly rgrvvergpa devildprhp
      241 ytkllaaasp dpdargrtfd fdpadvvaag sappydhred tpr
//
LOCUS       WP_357608690             248 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357608690
VERSION     WP_357608690.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 248)
  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 248)
  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 248)
  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 248)
  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..248
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..248
                     /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=24999
     Region          4..247
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtttlldgkv alvtgggrgi gaatalrlaa dgadvavtwq rdaeraatvv kqiealgrra
       61 iamradsadp aalreavdrt adelgrldil vnnagaflig aidefttddl ertiavnvra
      121 pfvaaqaavr hmtgggriis igsnvgdrav fpglaayams ktaltgltrg larelgprgi
      181 tvnlvvpgpt dtdanpadgp nadairgfta lgryaapaei aatvahlagd dagyvtgavi
      241 avdggfts
//
LOCUS       WP_357608701             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357608701
VERSION     WP_357608701.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  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 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..190
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..190
                     /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=20509
     Region          1..154
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 marnverrta ladaglrvla atgarglthr avdaeagvpl gtasnyfrsr damlgalger
       61 imerfapder tlaalgarep slelftdyvr yiverttaqp eltralielr leavrrpela
      121 rilgdtlrrg yrddvafhva aglpggafev allhyaldgl lldllttsid agfdpdevvs
      181 alvsrlvara
//
LOCUS       WP_357608775             238 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608775
VERSION     WP_357608775.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   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 238)
  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..238
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..238
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24823
     Region          4..236
                     /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 mnqpvvllvh gafaesagwn rviqrlrgnq lttvavanpl rsvegdaayl rgvidgiggp
       61 vvlvghsygg mvisqaaagn pavralvyva afapepgesa lllsskfegs tlgqalqsyp
      121 vasggnefri dpakfhrqfc adldteeaal maatqrpvte ralsdglavd eapwrtvpsw
      181 fvhgdkdlni paaalrfmae radsrctrev agashalaas qpdavtatil daadharg
//
LOCUS       WP_357608797             204 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357608797
VERSION     WP_357608797.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..204
                     /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=21426
     Region          12..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msevdagers rrmraegrrs iaaildaavr ilgerpqasm devasgagvs rqtvyahfps
       61 rdallgavar rltaqavaal daaqldqgpa aeallrlldv nwrtfahfpl litvpeadaa
      121 elhvpvferl erlirrgqra gefdpgvtpa wliaatvalg htagnevaag rmsaadaeaa
      181 lrasvlrvyg atptrpthgg dpaa
//
LOCUS       WP_357608811             377 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608811
VERSION     WP_357608811.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 377)
  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 377)
  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 377)
  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..377
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..377
                     /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=41395
     Region          5..370
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(21,28,55..56,63,67,74,206..207,210,214..215,218,251,
                     256..257,260..261,263,287,315..317,320..321,323..325,329)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(28,49,51,54,56..57,142..143,152,205..206,209..210,
                     214,257,260..262,364)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mdilglrawa vtdpallktl ltspdvskng rahypafqqt istwplalwi evqsmltayg
       61 adhrrlrrmv apafsarria elkpiiqslv telvddlaav ppgqvvdlre rlayplpiav
      121 ighlmgvped qrddfrqlvd nvfdstltpe qaqantarlf ettdqliatk rsksgddmts
      181 lligardees dgsgftdvel rdtmilmina gyettvnvid qavfamltsp dqlhlvrtgq
      241 atwedvveet lraepaikyl plrfavtdik lpdgqviaag dpilaaygaa nchpdwhgpd
      301 adsfdvtrkv kdhlafgygv hfclgaplar levaevlrql ferfpamslg apadalrpvp
      361 tlisnghqel vylrave
//
LOCUS       WP_357608827             393 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357608827
VERSION     WP_357608827.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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..393
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..393
                     /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=41798
     Region          4..391
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mpddrpydlv lfgatgftgg ltaeylarha paglrwalag rnpaklaavr drladidaal
       61 aelplltadv tdaaslrava esarvvastv gpfvhhgepl vaacaaagtd ylditgepef
      121 vdrmyvrhha eavrtgarlv hacgfdsiph dlgawytvkq lpsdapitvd gfvragarfs
      181 agtyhsalta fsrtgetnra akerkavepr pegrrvravp grvgrskeig mwavplptid
      241 pqvvrrsaaa rpeygpdfry rhfaavkrlp tvlvsgvgfa glvglvklpp trrwllgrla
      301 sgqgptaeqr akswfrvrfl gsgggrrvlt evsggdpgyd etakmlaesa lclacddlpv
      361 tagqvtpvta mgdalldrlv kagitfrvld apr
//
LOCUS       WP_357608829             316 aa            linear   BCT 28-DEC-2024
DEFINITION  methionine ABC transporter ATP-binding protein [Nonomuraea
            dietziae].
ACCESSION   WP_357608829
VERSION     WP_357608829.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 316)
  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 316)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 316)
  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
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..316
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32857
     Region          1..316
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 miqasglrks ygstvaldgv dldvrqgeif gvlgqsgagk stllrcvnll erpdqgtvtv
       61 agqemtalge relraarqri gmihqhfall ssrtvagnva fplevmgvar seraarvael
      121 ldlvgiadka dahpgqlsgg qkqrvgiara lagnpsvlla deatsaldpg ttssilallk
      181 rlntelglti llithemnvv ksvcdsvaim tggrieesgp irqllttpgs rlaaelfplp
      241 apargdvtit ftgaaeepvi sqlvrkfdvd vsilggalee vaggsvgrlr vsldgaesat
      301 altylrergl ivevaa
//
LOCUS       WP_357608854             158 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608854
VERSION     WP_357608854.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..158
                     /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=16911
     Region          3..139
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mvkptgehmg vvsalvrasf lvsavyadsa reygitsqqg qllcvlmaqp ygmselggil
       61 rlakssltel vdrsaqrglv rrepdprdgr avrvtlterg gevaeafyte tcrridrlps
      121 gldaderaal agllgrvvee nqvpvvflep agasspkr
//
LOCUS       WP_357608872             192 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608872
VERSION     WP_357608872.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 192)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..192
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..192
                     /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=21555
     Region          4..79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          88..174
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(91,104,106,119,122,126,160,162,174)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mdlddvlqsv gprlralrqe rgatltqlsg stgisvstls rlesgqrrpt lelllllara
       61 hqvqldelid apvtgdprvh mrpfkrhgtt yiqlsrrpgg mqaykqiypp rwpgfepeqr
      121 vhegyewlyv lagrlrlrlg ehdviltpge vaefdtrtph afsnpgeept evlalfgpqg
      181 ermhvrarpa ar
//
LOCUS       WP_357608899             201 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608899
VERSION     WP_357608899.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=21886
     Region          1..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 maragltadr vteaaaelad evgfdnitvs alarrfgvad aslyshvknl qdlrtrvavl
       61 aareladqls dattgrsgkd sltgfanawr dfaltrpgry ratqlpvgpd vvaasqghqr
      121 imsityahls ayrlpepdlt dairllrsty qgffeleasg gfqharslqa swtkildald
      181 salrhwqvse rppgndhesd h
//
LOCUS       WP_357608905             212 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608905
VERSION     WP_357608905.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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 212)
  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 212)
  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..212
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..212
                     /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=21940
     Region          2..212
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mritvfgaag avgsrvvaea lsrghdvtav vrhparlpql hpaarartgd asnvddvaal
       61 sagqdlvvsa trpapgyedd lvttakalla gvaatgvrll lvggaagltv pgtggltvvq
      121 tpdfppawrp ialacdrqld acraepvadw aylsppalle pgertgryrl ggdellvdaq
      181 gvsaismedf avalldeaer prhhrvrftv gy
//
LOCUS       WP_357608910             167 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357608910
VERSION     WP_357608910.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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..167
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..167
                     /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=18272
     Region          20..159
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 madhvdlvlr qwaaqrpdld vspmavigrl srvtrlidae lrrtfaahdl dpasfdvlat
       61 lrrsdpphrl tpaelmrasm vtsgaitqrl drlesrglva rtpsdvdgrg vyvtltdegr
      121 alidrvlpdh lateervlaa lpeehrdala rtlavllesl gdtttps
//
LOCUS       WP_357608980             241 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357608980
VERSION     WP_357608980.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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 241)
  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 241)
  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..241
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..241
                     /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=23839
     Region          4..225
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrgvlvigss spigraigra faadgdtvvg valeevdepa ftrslmldca saegaeaave
       61 avadaagrld vvvlaaavmp vapitettda qwraaldavl gtafavsraa lprlaagsqa
      121 dggaivalss vnaflaapgl payaaakagl eglvrqlale ygphgvrvna vapgmigged
      181 vpdaaagypl grtgtaeeva qavrflagag fvtgtvlpvd gglsiaspaa flredlrgrw
      241 l
//
LOCUS       WP_357608989             467 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Nonomuraea dietziae].
ACCESSION   WP_357608989
VERSION     WP_357608989.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 467)
  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 467)
  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 467)
  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 467)
  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..467
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..467
                     /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=48446
     Region          5..465
                     /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 mteqstdvdv vvigagpage nvagrvvrgg lscavvedhl aggecsyyac ipskallrpm
       61 elaaevgrvr glrlegpidv pavlaardka vaglddsgqa gwitglpatl vrgrgrvage
      121 rlvevsghdg tvtrlrarha vvlatgsvpv vpdvpglaaa rpwfsrdatt vsevpgrlvv
      181 lgggvvacem aqalhalgat ettllvrgdr llgrmerfag elladsmrea gidvrmgakv
      241 tgveraadgg pvtvhlagge qveadellva tgrrpatdgl gldldgavev ddsmrvpgsd
      301 wlyavgdvng rnllthmgky qarvcgdvia araagrpdda pslrdsadgr gapqivftdp
      361 qvcavgrtee aaraegfevr vveydlgnva gaslmgegyk grakavvder rrvllgvtfa
      421 gpavaellha atiavtaevp letlwhavpa fpavseiwlr lleeygl
//
LOCUS       WP_357608938            1556 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Nonomuraea dietziae].
ACCESSION   WP_357608938
VERSION     WP_357608938.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1556)
  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 1556)
  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 1556)
  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 1556)
  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..1556
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..1556
                     /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=163944
     Region          32..1454
                     /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 mteaspklpg rpgalpegal arlierrkgt giprrepglv vpltgtqerl wfldqagqda
       61 aaylcwaanr lrgpletaal raalgavvar healrtaive gpsgrpvqvv rdlaeldlda
      121 llelasvppp sgeemarrla dafvarpfal drpplmrall velapddhvl llclhhivcd
      181 gpslevilde vhaalagerq dpappaqfpd yaawlasreg kqleadlryw rrqlagapal
      241 ldlpadrprp papsgrgarh slplphelal rlaefagrrr stpfmlvtaa lavtlarhad
      301 qddivigtpa dnrdlqeler svgmyantva lrfgldgnpt laevhdqvrr vttegldhrt
      361 apfeevvglv ggrrdlshnp lfqvmlvver aarrraptaa gltvdgwapp vpaarfdltv
      421 vavtgpetfe lhldyakdlf degtaaamae rlaavlealv tdedqrmwhv plpspeppaq
      481 pprtedapwq svvdriagwa artpeapavv geegtlgyge lvaradllad rlrtvlarge
      541 rdqivgivlp agaeavvavl avlragaayl pldpghppar laallgeasa aavivapgle
      601 pavgdydgpi lrsdsasaet asagsgtsfs ggggpqevgp edlayviyts gstgapkgvm
      661 vthgtldrlt rsfadlhgfg pgqrllmlpp ltfdasvgdl fpalttgaav vphpeparld
      721 gaelvrfcre hgvtavdtaa slwrrwvgdl aatdvpddwp vrimmiggee araedvrawq
      781 ritagrcdly nhygpteatv catvhrlggg ddlgalwrvp igtplphvta rvldrhggla
      841 pvgvvgelhl ggdclargyl grqdltadrf vpdpygpags rlyrtgdlar mrrdgslefc
      901 grrdrqvkir ghrvepaeve aaiaahlgia daaviakddr liayltltps tpptsptsap
      961 tsptsaptsp tsaptpatpa patpttvtap avplrsatpn pldfattpai avgrggpaap
     1021 ggsatpssan aadgvgragg vgereggvle glrrrlrgrl pghllpsqfi vvpaiprtah
     1081 gkvdqaalpp pdrrtgehvp pvgavetaia qvwaralrvp evgrtdnffe lgghsllaas
     1141 vvaqtrrvlg vevplralle sadlsdlaal ieghrvtedd pdlaaeaalp adlvtlaktr
     1201 evlatpatsp savlvtgatg flgahlvaql avrteadilc lvrasderea aarvldnlrs
     1261 hgleadpari vgvpgdlaqe rygmtpdafa alarrtgvic hnggrvnfae syarlrpvnv
     1321 agtleamrla alggarlhlv stlgvflgda hrgrpvteld ppddpeglgs gydrskwvad
     1381 rlaregrtag lrvsvhrpar vsgdsrtgrg nagdyfsrll atcaalgavp dlpfeedlap
     1441 vdyvaagiah laltsdadge hhyfngatis yagiaramga dlvpwgrwrs avleggerlp
     1501 lapfaatlpe qtprferplf dcgrteklls avgitcppad talldrylgh lgagrg
//
LOCUS       WP_357608996             192 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357608996
VERSION     WP_357608996.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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..192
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..192
                     /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=20719
     Region          10..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtgespkeqr adarrnreri lavargvvqe qgteaslrdi arraevglgt lyrhfptrea
       61 lleallrqgf drlagraeal gesgspyeal veflrdligg agayrglags mmatisdeqs
      121 plhascmamr saagrllera qaegriradi dgtdlfalan alswitdqap slgsrrdhlf
      181 glvmdgltrd pe
//
LOCUS       WP_357609003             749 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357609003
VERSION     WP_357609003.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 749)
  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 749)
  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..749
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..749
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=79459
     Region          107..293
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          256..438
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          558..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 marrrtlsli laatllsggt aalsptgaga apprpedeyr pvrgpsapae yrylqktvrg
       61 ealprhaydt aakagarlpa vggrwtsvgp tniggritsl aldphrpdtv yaaaasggvw
      121 vsrdagnrfe pawpdgwtqa mgavatgpdg tlyagtgean pgggsvtyeg tglyaspdgg
      181 ktwrslglrd sgaigaitvd padpkrifva aagslynggg drgvyrstdg gatwqrilag
      241 aneftgatev lidprdadrl yavlwdhrrt pdlrtyggvg sgvyrsldgg atwarlaggl
      301 paagpevgri glgqsasdpd rlyaivnsta gpfagfygss dggdawtrlp dtpelttsqs
      361 tfgwwfgkvw vdpdepqhvh vagvpllttk dggrtwtads ssthvdhham iwdprrpqrv
      421 ylgndggtyr sdadgdggwv kathepytqf ysvaitpqdv srisggtqdn gslrswggpa
      481 fneylggdge enlinptdke nvyacyqygn cfwsadgget mtyfgnrvta arrnwftpvv
      541 fdprdpavmy yganvlnrst dggrtwtvis gdltggpgrd piytnygtit tvapagdgrt
      601 vyvgtddgrv wvtrdlggsw qlllsgqpwv trvvvdprra drvyvtlsay rsgsqrpyvl
      661 gsldggrhfh dlsgtlpkap vndlaigkgl tlyvatdqgv fvsptgggvw lrqgrglplv
      721 pvddieydgt nhrlvagtfg rgiyavrvp
//
LOCUS       WP_357609014             413 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea dietziae].
ACCESSION   WP_357609014
VERSION     WP_357609014.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..413
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..413
                     /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=43758
     Region          18..311
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mtvllerpat pvktrdtfid vlriagmalv vlqhwtipvl aydgvrlttg nalstpgvwv
       61 itwisqvmpl vffaggaana isfrrahgta pawlavrlrr lawpvlplaa vwipfpqvla
      121 tlgvpeqple vgsrltgqll wflavyviav tatplmlrlh drygllapla laggavvtdl
      181 vrftsgldai gylnilfvwl avhqlgflya drritrpgll avagfgaaal lvafgpypgs
      241 miglpgaems nmapptlaml avslgqvgla tllrpwitrl rtdrlvawag prmmtvylwh
      301 mpalfavtgv vvvalgadtp spgsvgwllg wpvwfgalcl vlwpllrgfa rfeeppalpy
      361 gratwgtsla aaalvgggll gltvygfapg gapvlstlai aggllltapr arl
//
LOCUS       WP_357609027             314 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein, partial [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357609027
VERSION     WP_357609027.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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]"
     Region          1..261
                     /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(30,241,244)
                     /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 mitvvgealm dliehaardv varpggspan vavalarlgq pttlltqlgd daygrtlreh
       61 lsgsgvrlep asvsdlprts vartrvgldg qagydfditw rsfpdgvltg agtpsvclht
      121 gslaavlqpg addvlalvrn rrattmisyd pncrpslmgd qvtarrrvee lvaasdivkv
      181 sledlawlcp grrhervghd wleagpslvv vtqgdggawa atrrcavrvd alpvavvdtv
      241 gagdaftagl laalaerdll gaarrtalra rppppgagrg rgaargaprn rrppgagppp
      301 ppggargggg rggg
//
LOCUS       WP_357609108             195 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609108
VERSION     WP_357609108.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 195)
  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..195
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..195
                     /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=21329
     Region          8..195
                     /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 mvfgrserpr lptaikilia ggfgagkttm vgavsetrpl rteevltdrg igvddltsve
       61 akrtttvamd fgritlgndy vlylfgtpgq erfwfvwdel aegslgavil adtrrladcf
      121 psvdyferrg tpfvvavncf egaptfelde vrlalqlsps tpiimcdark rdssrevlit
      181 lvkhsarlra epvgs
//
LOCUS       WP_357609069             112 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            dietziae].
ACCESSION   WP_357609069
VERSION     WP_357609069.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..112
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12286
     Region          4..103
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mfladcqarl afdllantwn avvvwalrhg psrpadlrta iggispkvln etlrrlefng
       61 ivsrtayaea pprveyalte lglsmlepie afgvwafeha eevmaaqdgf rt
//
LOCUS       WP_357609040             496 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357609040
VERSION     WP_357609040.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 496)
  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 496)
  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
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..496
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52135
     Region          8..489
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mdpvemlllr hvaagqggrt aladhlrtlt yaeltqaace hagalaaagv rrgcralvvg
       61 ddsadtvvav lglwwygcvp vvlspmlrdt eiafvardca aeyawialpk grrdslreal
      121 gplpvhepra traadvgppa pfvpeaevlv qytsgstgqp rgvrhsmagl ravldgfggv
      181 laltpddtvl staklsfgyg fgnsvlfpla agarsvllag pvdpytvita vhrhrptvlc
      241 avprlyaall divargtvld psslrlalaa gehlpaelsa raarllgvpv vnglgatevl
      301 hivlatdpqd ilhgstghpv pgvtatvrdd dgrplpagsh grlhirsasa algyidrped
      361 sartfadggv ytgdiayrte dgdfrhvcra ddllnlggfk vapaeieael rtadgiadlv
      421 vvggrddtgl eqvvvhavpa dgvtpdqarr alrrairenl ppykrpsrve vlaalpttst
      481 gklaryqlrg parepr
//
LOCUS       WP_357609110             449 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea dietziae].
ACCESSION   WP_357609110
VERSION     WP_357609110.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 449)
  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   2  (residues 1 to 449)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..449
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47096
     Region          2..442
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mivktssgrv sgirvenvha flgvpfaapp fgehrfrppa ppepwegvrp avehgpaapq
       61 rpaqdiglfa pdvfrygadc lnldvhtpdp gaaglpvlvw fhggafsvga nsaawqrghr
      121 fardgvvcva vnyrlgfegf lalddvpanp gvldwlaalr wvraniaafg gnpadvtiag
      181 qsaggaavat lmtmpdaagl frraivmsgs atlvtslaea raqakelaav lgvrpvredf
      241 aalpperlla aqpppttgql gslgesvaik pvvdgqvvpg vpleaiaagi gghlrllagn
      301 tsqeadvfvr rmvegidqgt areaaealgf ssdpesppae lvaravthrl firetrlllr
      361 arsaaiapty ayefrwespl espagggrvg avhnldlpfv fdvldapgva rtaghhapqa
      421 lahemhgawv rfvrdgdpgw pagvkrilr
//
LOCUS       WP_357609117             281 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357609117
VERSION     WP_357609117.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   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 281)
  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..281
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..281
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31003
     Region          4..276
                     /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 mpdielsagr idytdtggpg etvvlvpgla fdesvwqavv edlradfrvv vpvlpigshr
       61 rpmrpeadls aqgvadvlae fmerldlrdv tlvqndagta qllvgvrdar igrlvltsce
      121 alenyppgvq grtlhaasrv pgglflllqs frvpflvrmr tslggmakrp ipyelvrrwy
      181 gplladaevr rdfakfcrsv dkdtylkaae rlrgfrgpal vawgaedrmm ppqtgrrlaa
      241 llprgeyvei pdsrtlipld npgglcaelr rfiketstdr t
//
LOCUS       WP_357609122             436 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Nonomuraea dietziae].
ACCESSION   WP_357609122
VERSION     WP_357609122.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 436)
  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 436)
  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..436
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..436
                     /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=47022
     Region          1..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 madlprlavt rtaklatlpl gyagrtalgl gkrvlgrpae lvatevqlrt aeqifkvlge
       61 lkggamkigq llsvlesalp pavvepyraa ltrlqdsapp mpaatvhrvl aedfgedwra
      121 hfasfddlpa asasigqvhr avwadgrsva vkvqypgaak alrsdlrqvg rvaklfgvll
      181 pgldvrafvq elqervaeel dygleaeawh afaqeyaddp dfavplvvaa sehvivtewl
      241 dgtplskvie dgpqaerdra alllvrfsfs sptrcgllhg dphpgnfkit edgrlgvldf
      301 gavkrlpdgh ppaigpllrc gaagdiegva qvfrqegvir egvevdldal asfvapyaep
      361 itsaefsftr dwmrerglym fsdgssifrm lnvppdyvvs frvltagygi lsqlaatgrf
      421 raeaerwipg fapdpa
//
LOCUS       WP_357609154             463 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357609154
VERSION     WP_357609154.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 463)
  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 463)
  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 463)
  AUTHORS   ter Beek,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..463
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..463
                     /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=49101
     Region          26..384
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrtplvrwsl lsvslalalt scakgtggga satpsagqfn sgatfqgtis vmgfgatdei
       61 gttrvdlakk alggadvkli egdldiqqfl ssvaagdppd iiyanrdeig tfasrgaiip
      121 ltscvkgeqi dtsmygkeal sqvtfgdevw aipefnqvqi tmangdllkq agltiddvng
      181 snwdkisaaa eklykapggk lqvigydskl peflplwaka ngadllsadg ktaqfnspqv
      241 vkalefavgi ydaqggfakv kalrdsadff gkgnqfakne lgampmeqwy vnvlndvspk
      301 aplvfdtfrt pqgqplayss gsswaipkgs knaaaacrfa ktmtlvdtwk aaaqarldkr
      361 kaegkpftgv ltgnvqadae iekmltsggp vwdagvkafy eankhtfslp anpadkefkt
      421 awqdavnrvl ngqdkpqpal dkaqrdaqaa ldkawagwtk rtn
//
LOCUS       WP_357609170             438 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357609170
VERSION     WP_357609170.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=47347
     Region          39..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(143,145,289,291,321..323,366)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mitprirmag allgaamltl tacgsgdsgg gegdkvalty riwdeqqrvg ydkimaafek
       61 anptidvtie vlpwdqywtk ltadavagta pdlfwmntgq fpeyvtkgvl adlsalkldt
      121 aaydknvves ythegklygv pkdlgivgll ynkdlferag vempetltwk adgsgtfldl
      181 arkltvdegg khpgedgfdp akvktygfas wnhyqtqwmn wvvsnggkll dkpfgayafn
      241 daasvqalqf gvdlvnkhhv sppatgtnpp tgkatemfqa gevamfpann allpfvapes
      301 tfeigvammp egpagravni nglseavyak tehpdeamkl aaylstrepq klmadegfvi
      361 palgglsqgy vdywktkkid vapylkqteg ttfnlpvttg fpgfepklnq ifnemylgki
      421 tpqqaadqav tegnatik
//
LOCUS       WP_357609181             249 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora purpureochromogenes].
ACCESSION   WP_357609181
VERSION     WP_357609181.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 249)
  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 249)
  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 249)
  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 249)
  AUTHORS   ter Beek,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 249)
  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 249)
  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..249
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..249
                     /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=25126
     Region          26..231
                     /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 mtataaragt npveqaviwl ndplnwtnpg gildrlgehl smsaaavllg clvawpiglw
       61 lghsgrgggl vllisnvtla iptlalltil pltflgfgrp avvvalavfa vppllanayt
      121 gvrqadpear daargmglsg gqllrrvelp lavpylaagf rtaavqvvat aalasfvngg
      181 glgqiiragf gldiaagggq iiaggvlvag lallvegvla lveravtprp lrrargranr
      241 raaaavtgn
//
LOCUS       WP_357609188             250 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609188
VERSION     WP_357609188.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=27448
     Region          4..238
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 maqlrvlavd delpaledls yllradprig evatardgaa alrlldraia dgrpidavfl
       61 dirmrgldgv vlgrllsqfa npprvvfvta yeehavdafe ikaedyllkp vrperlaeai
      121 rrvavsadvp aeggetdtip velggvtrfv ssadviyvea hgdyarlhta tgshlvripl
      181 atleerwasa gfvrvhrshl vavkhieelh idsgkctvrv gdtelpvsrr htrelrdllv
      241 rrarkarsap
//
LOCUS       WP_357609211             597 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357609211
VERSION     WP_357609211.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Rosinski,J.A. 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 597)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..597
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=64742
     Region          <255..477
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          535..>582
                     /region_name="HTH_ARSR"
                     /note="helix_turn_helix, Arsenical Resistance Operon
                     Repressor; smart00418"
                     /db_xref="CDD:197713"
ORIGIN      
        1 mrrlgvqpia dvtdvefael itagiarllw ryrseatpit iallsllagt vlhrwyptww
       61 ptvalmtatt agtlatagrw lnltraierg yaaiaatllg gwltaatilg plssplpavl
      121 algclvlaip wwahrrrrar vrvertlaaw peisqaigla gsrvqsaivd lwgyrtrial
      181 argqtvedai aripgiesal gtrrgavriq pvpekanrle lrvietdpha daiswpgpsv
      241 stihdpmelg vfedgspvrv sfkrrhalvg gvagagksga vnvlmgnlsa cpdvivwgid
      301 lkrgmellpw escldrvavt pkeatallkd avrvldgrae mlamhglrvw epahdapali
      361 ilideyaelv ddapdaihya dsiarrgrav aetliaatqr psqkamgnsa vrsqmdiris
      421 frvrerrdad lilgagmhks gwhadkldap gkfllsapef diprrartyl laddtvqrta
      481 iqhadrrpal daislaalhe ppheredave ssqqsrgrha rqaasqatkd alsaalrnap
      541 regvsvgdlm eaadmsrptl yrrlalledq giavqvsrgr wratatdads pafgdeg
//
LOCUS       WP_357609241             464 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609241
VERSION     WP_357609241.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..464
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48555
     Region          4..456
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mrsidalvss lpearvvtdp dvidsyardr tfvepgkplg vvlatsrddv vttmkwateh
       61 rvpvvprggg tglagasvag dgsvilslar mnairelspa deiavvepgv itadldkaar
      121 ahglmyapdp ssyeistigg nlatnagglr cvkygvtrds alglevvlad grvmdtgrrt
      181 mkgvtgydlt glfvgsegtl gvitaatvrl rrapaappat faaefgslrd agaavsaima
      241 agcqpslmel ldratleafd dwrniglepa tqamligqsd atdsqaaver merlcmenga
      301 sfvavssspq eaeelialrr layqakerlg aclvedvcvp rsvlpdmita ieataarhdv
      361 kictvahagd gnlhpvfifd rgtaeppaev waaadeifth alelggtltg ehgvgllkrr
      421 wlalesgpvv teiqqgikav fdplgilnpg kaiwpdtsgt ltnp
//
LOCUS       WP_357609213             312 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357609213
VERSION     WP_357609213.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=34269
     Region          18..308
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mselrtkdeh teairrdrkv avvvntrsrr grrhyfevie qihnlgfepl velsvynpkr
       61 lrelldtala tkpdllivgg gdgtlssavr hvahrdvalg vlplgttnnf arslglpldl
      121 agairvfatg kvadidlgma ddrpfanlas fgvsvevagr vkpwlkrivg rpaypltalt
      181 ilpghtpfra yitvegqrhe llthqlnian grfhggwqva rdisidngql vayqlgsgkk
      241 lrllgetlir attgrwrsla ggpfvvgrem lletdppmaa dvdgevrlrt pirlrvvpng
      301 vrvmvpdsfe dr
//
LOCUS       WP_357609244             791 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609244
VERSION     WP_357609244.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 791)
  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..791
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..791
                     /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=79019
     Region          12..478
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     Region          <405..704
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mnqsqplaad dprrlgtydi varlgeggqg vvylgkgesg dqvavkllhq slvadadart
       61 rflrevavaq rvarfctapv lhadlegskp yivseyvpgp slrelvineg prrgaalerl
      121 aistatalaa ihragilhrd fkpanvlmgp egpvvidfgi araldspgat atgmamgtps
      181 ylapeqlsgg avseaadvfa wgvtmvfaat gkpafgadsi pvvmnrilne epelgamegv
      241 laelvalcls kdptlrpsad dlivrltgqp apksaiepvt gqqltsaapg gqaggqagpe
      301 sgkpgqggdl ypgpwtqpvp sasgplqags eavpqtgafa hhvaaaqagp aqggpaqggp
      361 aqgapvqgga aqggpaqaas amgggpaggp qaggpqagmp gnaspqpamp gtppgngpqa
      421 qtgpaaphga gapqtphgga pqaphgapqt pqgghlgaaa asgmpphgpg gmpqgqapfk
      481 gqggtpngps rpggptgptr paegapakqr rtlmlslsga aaaallvvvg avvvqansre
      541 vpvvavgnsa nqsngdgsga gqpvdppstd qtlppsvptd taapvptldv dqpskdpktt
      601 kpkqhtqepv sqvpnpvtqp ptshpttsrp epkkspskks tktptmvdpe nvdeagqpng
      661 qpssgptstv rpsatskpyv prkantsspt glcgsgykvv dshalgtnat iyllynagag
      721 kncvvtlsrm ifpekvqmna ilqvkggssa sapgrftana gpirlpakqk cviwggawae
      781 mswksgwshc s
//
LOCUS       WP_357609283             224 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357609283
VERSION     WP_357609283.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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 224)
  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 224)
  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 224)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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   8  (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 19604043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..224
                     /product="GbsR/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=24680
     Region          1..>94
                     /region_name="Tra8"
                     /note="Transposase and inactivated derivatives, IS30
                     family [Mobilome: prophages, transposons]; COG2826"
                     /db_xref="CDD:442074"
     Region          76..223
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mprrrlthqe rqriaaglaa glsyreiarr lerptstiar eiarnggaag ylpqqahqat
       61 iqrarrgtpa spnaatppla ameqeiiema vragmprtaa rvhhdlalae dgrrtaaela
      121 rrlnvspasi svavnflvqq gyarrerdpr srrtiyaidd gawyhavvis rqqtletvra
      181 tkavaetygl dgpvgqrlak taaflervsl diiesadrwr hllt
//
LOCUS       WP_357609255             368 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357609255
VERSION     WP_357609255.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=41715
     Region          5..368
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 maqtvkrtyk yrfyptseqa selartfgcv rlvynralee rtrayaqqgr risyvessar
       61 ltewkrsgey dflsevssvp lqqalrhlqa afanffakra ryptfksrkk srasaeytrs
      121 afrwrdgrlt lakmdapldi vwsrplpega vpstvtvsrd aagrwfvsll veekisplpp
      181 vgqsvgvdag italatlstg ekivnprher adrkrlakaq ralarkekgs nnrdkarrrv
      241 arvyariadr rrdhlhkvtt rlvrenqvia vedltvrnmv qnrslarais daswrelrgm
      301 leykaawygr elvavdrwfp ssrlcsacga lrdkmplnvr ewtcacgavh drdvnaaknv
      361 laaglaes
//
LOCUS       WP_357609302             309 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609302
VERSION     WP_357609302.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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..309
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..309
                     /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=31250
     Region          23..294
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mtggallvvg dvvtdvvalh gspvtsgtdt aadivlrpgg sgantaawaa rlgadvrlla
       61 rlgydssewh taelartgvr thvtvdpdrp tavviamvdr tgertmltnr gagglisead
      121 wdpalldgvt rlhlsgyvmf adaglrlarr amaeaaaagi aisidpastg plrdfgverf
      181 lresapagli lpnldealll tgaataeraa vllsetygta vvklgaqgal aavdgeivat
      241 aagvsaevvd stgagdafaa gfltgtlqgv seeaaleagc ragaecvaqv ggrprygldl
      301 nrlypihtd
//
LOCUS       WP_357609390             406 aa            linear   BCT 28-DEC-2024
DEFINITION  LeuA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609390
VERSION     WP_357609390.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..406
                     /product="LeuA family protein"
                     /calculated_mol_wt=43926
     Region          1..391
                     /region_name="LeuA"
                     /note="Isopropylmalate/homocitrate/citramalate synthases
                     [Amino acid transport and metabolism]; COG0119"
                     /db_xref="CDD:439889"
ORIGIN      
        1 mprvhfldvt nrdgvqtart glskfgktmv nfylaklgva qseigfpflf hevpyvkaqv
       61 alaeagafgg lrlsgwcrgv pqdvekaapl glrhynlsis tsdymiqnkf rgrldrdaii
      121 remtaavrta kaagaqtvgv naedgsrtdd gfllefalaa keagadrvry cdtiggdtpd
      181 rirerfakla satalpveth chndlgmava nsvsgalgdl dagqdawint cvngigersg
      241 nadllstila fqhgfgldae igdaldlswa rrfalwasya fgqplpynqv gvgrnafahe
      301 sgihadgalk dhgnyelyde atlgpfpedw hardgrvvlt geyggkagfr hvmdglgvev
      361 reedlafrlv qlcnamtgrp ltddelrlia ayprelsllf pgherp
//
LOCUS       WP_357609410             660 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609410
VERSION     WP_357609410.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12993149
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..660
                     /product="serine/threonine protein kinase"
                     /calculated_mol_wt=66068
     Region          16..261
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,42,44,73,89..92,96,98,135,137,
                     139..140,142,151..152,155,170..173)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,42,44,73,89..92,96,137,139..140,
                     142,151..152)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(26,96,98,135,137,139,155,170..173)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(39..40,65,70,75..78,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(151..158,166..173)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          171..>456
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
ORIGIN      
        1 mvaplaaedp prlgefellg rlgeggqgiv ylardpvgqr vavkvlirad aeararlare
       61 laavesvapf ctarvltavp daprpyvvse fvdgptlaer vhehgplhgg elerlavgtt
      121 talaaihaag vvhrdfkpsn vllgpdgprv vdfgiarpdg vttmtsglig tpaylapeql
      181 sgapaspasd vfawagtmvf aatgtspfaa agiadvlnri vthepdlsav ppplrdsiaa
      241 alekdpshrp aagellsrli dpvsggrgrs iveltslgsr laaepaddrg tsdaaggrdp
      301 agaagrgdta gpagrgdtag pagrgdtagp ageptappss rapvligwta grgrraalav
      361 aaalvavvvg avawlrpfgg tgsqassgtg epgssaasrp gtspgtsaep psaapsaaps
      421 aapsgsrevs ssgpaspgas avpsgglrvs dtfgrtvstg fgmtddgerh wsvgvpasgy
      481 svdgdkgrit tpsgvassay ldgvkatstd lsftfaadkp pigggiyvsa vgrriptvgg
      541 yrahvslrpn gkvlfqlirf eagrseidla qplrvpglta gagipmrvrv qvagtsptti
      601 rgkvwatgaa epdwllsvtd atsvlqvpgg tgvmtylsrw atdapvtvtv ddlaltatpg
//
LOCUS       WP_357609426             158 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357609426
VERSION     WP_357609426.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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 158)
  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 158)
  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..158
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..158
                     /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=17418
     Region          1..158
                     /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 mrlrewtagd adrvleafrs edmraqsgep irtlddavrw iegwqdrgha faveldglvv
       61 gnvavtgidr hgngwvsywt taqargrgva araagllaew afaerglfrl elghrtnnpa
      121 scrvavragf vaegiergkl vydgvrydve rharlatd
//
LOCUS       WP_357609419             876 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357609419
VERSION     WP_357609419.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 876)
  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 876)
  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 876)
  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 876)
  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..876
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..876
                     /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=96683
     Region          1..239
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          115..852
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          667..695
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(668,671..672,675..676,678,710,713..714,717..718,
                     720..721,747,750..751,754..755,758)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          708..738
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mefrimgals vrdgaedrtp iapkhrdlla mfvlnarrpl tverlrqllw pleegdrsds
       61 lirgyigrlr qligkdvitt vsgtytlavh ddqldvgrfr rliqeglsgh dsgklrealg
      121 lwrgpvladv dpdarrwaet grlreeleel rllalerrie ldldagrhre llselrglva
      181 qhplwqrfrg qfmlalyrsg rrvealaayt alrdeldggh aiepdpelql lyhrmlhddv
      241 mlhvsagppv llprdvthft gradlldqvl sglvvvhgpa gvgksalair aawrhrerfp
      301 dgilyadlre strpgailed flrwlgcpaq avpasegqrq rllrtytanr rmlvvlddaa
      361 desqvrpllt scptvitsrs alggltgavr lplgvlddde ardllvklig eeraddggvr
      421 elvrfcgglp ialriagsrl atrpgwtpgy fagllederg rldrlhsgdq tirsvyaagy
      481 eglptparrm vrllgalsap dvadwaaqvf gdqadvlvda glleahtvda agqvrhrmhd
      541 ltrlyarerl veeegvhavr dalarlqavv iarvqasrfp lvsgeptmrt fvtrdikesv
      601 ewlvaergfl aalvgdlyga gldegawrla hllgpflerr rflddwrsva etglaaarrt
      661 gdaraealll rdqgdlcrae grwaealdll tralgtftsl gtfsgkeaaq vrrrigqayl
      721 eqgrldeaer qltsslhvfs ggraraeaqq algavlrrad rpdeaadrla aaagffdavg
      781 drhrhadtll elaaarlaqr rvpdardcaq rarsiavrlg drlldahall alarvnraeg
      841 drdaarklae dafkifdgia depgratald llaalm
//
LOCUS       WP_357609472             460 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609472
VERSION     WP_357609472.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=48966
     Region          73..436
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mishprsirm rstvvtslla lialavlgvt sslavryrvq ddafnrveqv asqwsaaara
       61 gtipeeipts gdialvqlvd prgrvlaasr sargrpalst lrppvddrvq rrtdgrrllv
      121 airittaada pvvvaerrep allrghnley altaaalall avvswsswrt vgrtlrplea
      181 irarlaeitv sdlslrmpvp paddevamlv rtanqtldrl ddavaqqrrf asttshelrn
      241 piaglrlqle eallhpgevd phetirsals vtdrldaivg dllmlarlga gdpappelid
      301 lgrlvsqeap ragrvpvrvh aapqvwvrgs riqlvrvlan lvgnavrhag savdvfvaas
      361 ggeavltvad dgagiapadr eriferftrl edgrrrdagg sglglaisrd ialshggtlk
      421 aedaprgarf vlrlprldgp pasapnastl atssngrstg
//
LOCUS       WP_357609477             209 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357609477
VERSION     WP_357609477.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 209)
  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..209
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..209
                     /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=22546
     Region          9..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtrrqrltpa drraqllavg arlfaahpya dvlmeevaea agvsrallyr hfpskhalfa
       61 avyqqaaeql laetrldpad slveqliqgm dvhldyfvan rnavlaanrd lagdpviqti
      121 mtneldavra rlltvlplad esardavsgv lkswlvfvrv lcvdwlthat ctrtqlrdvc
      181 igavlgalrp llaedpapgw pppgpgaga
//
LOCUS       WP_357609481             448 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Nonomuraea dietziae].
ACCESSION   WP_357609481
VERSION     WP_357609481.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..448
                     /product="MFS transporter"
                     /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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46330
     Region          1..443
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mddkpgmaek faffsgvwgg vlmgassgfl llyltdivgl gaaavgtlml varvadgasd
       61 pimgylvdhl pptrwgrfrp yvlvgavlcv ccvialfvvp allpdalval wityllwgll
      121 ldlfqipmts lvpamsadqg argqlaaivg vtglfaaala tgltlpvvnl lgggtrgwlt
      181 yvigsailgf clvvvmvlrv rervvplspe ryrlsdvrrv ffsgravpil llskvsvqaa
      241 sgaltaampy fflyyigdtv ylsaaafvma ipmvagavav pvlarragak plyvaslgvs
      301 itglaalmav ppdpvpvlac favtgvglgg avslslvlla eltdytewkh gfrteaslaa
      361 mtsfatkagg gvgggllayt laltgyrsgg vaqseetldg ilmaqslvpa giglvgalaf
      421 llypisgeva reasrrlaer rtavvesa
//
LOCUS       WP_357609508             530 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357609508
VERSION     WP_357609508.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..530
                     /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=54294
     Region          2..530
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mstltgtggl irlilrrdrv rlpawfglva mlvigvassv aaaypteear qaflhttngd
       61 ptqlmmigpi ydssagglaa wrvrgqaall ialaslllvi rstrgeeeag rsellgstvv
      121 grhaaltaal tvacaanlvt alvvtlglmg qglpprgslv mglsvaaagw vfaavaglaa
      181 qltegsrtag glaatamgil yavragadve ksswvswlsp fgwtqhmrpf agdhywpllp
      241 viglilllva gayrmsarrd lgagilpprl gpadaapslr tslalawrlq rgtllawava
      301 ftafgaglgg aarsaaeqlh asealrdlie rmggggrpad gffafviylm sqvitlyaiq
      361 atlrlraeei sgradliltg pvgrlrwagg hlaivaagsg ivlaglgvgm glvhglstgd
      421 pggeiarlvg asltrlpsvl vlaavstlay gllprlaaii pyaalglclv lefavellga
      481 dpailqvspf aqtpglpvaa ftvtplilla vvatgltavg laglrrrdlg
//
LOCUS       WP_357609595             510 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609595
VERSION     WP_357609595.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 510)
  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..510
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..510
                     /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=54701
     Region          1..508
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mlaklselda ehakavaggg eryverhrrr gkllarerie llvdpdspfl elsplaawgs
       61 efpvgagmvs gigvvegvec vitandptvr ggasnpwtlq kslraadial rnrlpyvnlv
      121 esggadlptq keifipggri frdltrlsaa gvptvalvfg nstaggayvp gmsdyvvmvr
      181 erakvflggp plvkmatgee sddeslggae mharisglad hlaedehdal rigrqivrsl
      241 nwrkqgvrpr aareprypvd ellgivpedl kvpfdprevi arvvdgsefe efkplygasl
      301 vtgwarvhgy pvgvlanarg vlfseesqka tqfiqlanqs rtpllflqnt tgymvgkeye
      361 qggiikhgam minavsnstv phltivmgas ygagnygmcg rayeprflfs wpsaksavmg
      421 paqlagvlsi vgrasaqakg qaydeeadaa mramveaqie aeslpfflsg rlyddgvidp
      481 rdtrtvlgmc lsainsapvp epagfgvfrp
//
LOCUS       WP_357609607             382 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609607
VERSION     WP_357609607.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..382
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..382
                     /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=41840
     Region          1..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 mksrdaaldg irafaalgvw llhvgsntgv myregmyawm larlgiavpi ffllsgllly
       61 rpwaravien tprpkpllyl wrrvlrvmpv ywlvvvpalw awsspdwlgw vkwllllqny
      121 fpgeqaaegl yqmwtlpiem afylvlpvla wllhkwarrg gnppvrllag igvlpvisva
      181 tvvvtrefgq pqlalllpyh lvffacgmam avlsvwighs rvidaltpql lvlalllyav
      241 lstglagprt ltlptlwesl lrisleaava mllvapfala prgdslrhrl vgnpvtaylg
      301 risysfflwh aplitlqlkl tgappfggdf psvavvsflg tlllsvgsyh lievpalklg
      361 rlpsaparpp aapspapvap ap
//
LOCUS       WP_357609557             215 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357609557
VERSION     WP_357609557.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 215)
  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..215
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..215
                     /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=23234
     Region          8..144
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpteplsrgr ivaaaidlie regadavsmr riaaelgvgv mslynhvpnk dallngvaea
       61 vlsaieftdd pdahwtdrar tqarafrqia hdyprstmlv vsrqlhstag llpveralat
      121 lrsagfdgad avrmlrmfva yivgsllrev gvtptfapvh nrlvtaegvd aalfpevssl
      181 aplldqcdhe aefefglell iqaisvhaar regtr
//
LOCUS       WP_357609632             359 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609632
VERSION     WP_357609632.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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..359
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..359
                     /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=35110
     Region          76..356
                     /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 mkrivaglat aavllagcgs ppapratsag sptsspaass pspsasplsl asleaayedv
       61 ianvlpsivq intkvglgsg ivydtaghii tnahvvgqst smevtiatgg aprqarlvks
      121 fdagdlavik vdhpdglrpa rfgdsakvrv gqivlamgnp lglsgsvtng ivsaigrtvs
      181 epqeegspga tiagaiqtsa ainpgnsgga lvdlsgrvig iptlaatdpd lgggtapgig
      241 faipsntatd iaaqiikqgr vtnshraalg irgstvigsd grptgvgvvr aepggaaaka
      301 giragdlivs ingkktptma vlaetiatlk pgdqakigvl hpdgstktvt vtlgqlrgd
//
LOCUS       WP_357609608             263 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357609608
VERSION     WP_357609608.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 263)
  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..263
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..263
                     /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=28475
     Region          3..263
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mgdplvfahr gasadlpeht laaylralne gadglecdvr ltrdghlvcv hdrrldrtsn
       61 grglvsartl aelelldfgs whpgcvpadg devldeshtr lltlerllea vlaagrpvrl
      121 lvetkhpsry ggdverrlva llrryglaep gpddpvrvtv msfsplavrr vrelapalpt
      181 vlllevlprw lrlgrlpfga giagpgiglv rarpqlvpal raagnqvyvw tvnepddlel
      241 vlaagvdgvi tdrpartlar lgr
//
LOCUS       WP_357609680              65 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609680
VERSION     WP_357609680.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 65)
  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..65
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..65
                     /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=7223
     Region          1..>48
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mhdevaayvl gvldpeehea ferhldtcer cqaelidlae lpeqldelkn tpsasdddpp
       61 msmsr
//
LOCUS       WP_357609749             378 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357609749
VERSION     WP_357609749.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=42312
     Region          71..357
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 magntkgrkr rfgsvrklps gawqarytgp dglprkaltt fdtkraaeqw lveteagmlr
       61 gewldpdagk islaeyadrw mrerdlkart reeyerhvrl hvrpqlgnha lneitaphir
      121 kwradrladg vgkptvakty rilhaifata vdddlirrnp crikgggqdk aeerptatlq
      181 qvfaiaeaiq pryrlfvlla afaqlrfgel valrrrdidl rtmelrvrra taemedgtqi
      241 dddpkseagk rpislpaglr tdaewhlaqf aeggpngrlf lgtqggiprr rnfnrvwrka
      301 ltaagipdsl glhlhdlrht gstwsaqsga tlkelmarig hsstraamiy qhatrdrdha
      361 iaaaldalie eargkisa
//
LOCUS       WP_357609774             294 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357609774
VERSION     WP_357609774.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   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 294)
  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..294
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..294
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32049
     Region          1..279
                     /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 mavrrgghgg vplllvhgfp ctsliwshni eelaaagfdv aapdlrgygd sdfapdgfyd
       61 faafnadltg lmdafgwera vvvghdlgam iaidlatrhp grvdrlvvld dsmpdlpeaf
      121 aaagippgtp kpavydyqrr qglhadelva eldtperrrr yigeffghrm wcppgafsea
      181 dlevltepya dadrlrasfa dyevvmgarp msapemtdrp vqqptlvlvg pdqvtlgehv
      241 eercaiaypq vvgpfwvrga ghfmpwekpt vvnrairsfc gdllarhads rgal
//
LOCUS       WP_357609779             407 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357609779
VERSION     WP_357609779.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 407)
  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..407
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..407
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44364
     Region          6..73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mrgigqdltv gervawyrrr rgmsqevlag ivgrtvdwls kvennrield rlsvirsvat
       61 aldvsigdlv geptlldwna etgtktvsal reallnyrql tpflpgpvad apevaqlrae
      121 vtqvwdayqa srygyvvarl pqtlaagqaa tqthdgekqe hsfallalty qaaavlltkl
      181 geadlawiaa ergfaaaqrc gdvvvigslf rsvthtllst gryreakqlt sdaaafmqpg
      241 maeatpeyls vygtlflags vaaardedra avrsflsead eaarrlghda nhlwtafgpt
      301 nvaihrvtta mdlddvqvai dlgpridttg lpverqarha letartlsaw nradeamavv
      361 laaeqkapeq irhhaisrql vqnwmrrgrg rpsyqlasla qrvhvta
//
LOCUS       WP_357609827             419 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nonomuraea
            dietziae].
ACCESSION   WP_357609827
VERSION     WP_357609827.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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 419)
  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..419
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..419
                     /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=45137
     Region          22..414
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mggppaplps sddrrpggpm taaellqqlt dqlrrresae tlsvqlghaq rlgnmgwaqw
       61 nlrtgeavws dhvyvifgrd psagpvglse ladhvepadl stldqllwav gegvepvhae
      121 frirrggevr nlrvvleplv gagettgvhg vvqditgrrr aerimsesrr qlieareraa
      181 eernvmialr eailpepvgc ldlprtrvav ryvpaekaan lggdwfeaag lpdgrvllai
      241 gdvsghglpa iahmaqlrha ligltmtgqa adqllswlne lvmhrlhdtt atalighldt
      301 stnvftwgqa ghlapilvrd gtakqldspr gvllgavceq pyelasielr pddllllftd
      361 glverrtrdl deglalalsa arelpvydld sgldrlvasi ggpnpeddac llavgildl
//
LOCUS       WP_357609893             392 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora purpureochromogenes].
ACCESSION   WP_357609893
VERSION     WP_357609893.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..392
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=40790
     Region          62..249
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
     Region          <236..392
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mtwrqraarw ldpalaqada aaasppppen haedlwpaic dqfalrilas ayqmgshlea
       61 vetdeqdper lerlyridha ntrirrhaen lqvllgrrve daspqtvtlv dvvraassai
      121 ehyprvrvgh vvdlgvvefa addvirvlte lldnatrfsp ptssvvvsay vtedgsvllr
      181 aedagvgidp gqlpqlnaml agtapapatg npaahlgllv vahlsrahql rvnltarpsg
      241 gttatvlipg sllcevapaa rpgpagtapt taggrppvwa gipqgsaqms rsddsrhapt
      301 vrlatlldaa pagdgpapdt rppepagglp rrvresvrgq tpspgahrpp ppgtapqppa
      361 papggsawpd etadfaagvg darpatldeg hp
//
LOCUS       WP_357609923             238 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357609923
VERSION     WP_357609923.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..238
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25104
     Region          60..235
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mpitpetarp heqpeensrh grlsvrpgpp vaatdrtglv sfdapdgelv aqayvpapad
       61 ggpyrlalll hgaggsprqa lelmlpvadn qrlllvapqs gaatwdmigv gfgpdvrrid
      121 rvlqeivtgy piagmliggf sdgasyalsi glingdvfda vlafspgfaa pllthgtprv
      181 yishgtadrv lpidrcsrtl vprlqtlgyd vtydefdggh dvpeatvrra vawlepaa
//
LOCUS       WP_357609924             318 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357609924
VERSION     WP_357609924.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=35429
     Region          14..317
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrllsll lllqtrgrmt atelaeelev svrtvyrdve alsssgvpvy adrgpaggyq
       61 lldgyrtrln gltaaeassl flagmpgpaa elglgdvaan aelkllaalp peprsqatmm
      121 rerfhldvpg wyrgaddvph laevaeavwd qrplrmryrr wgrqevdrvi hpyglvlkgg
      181 swymvaappg gdprtyrvsr ilametlqgr ferppgfela efwqayakdf kqkmytaeav
      241 irfepgaegl leytlsmpvp msepdpdgwr tvtvpiesvr harwlllrmg asvevlapae
      301 lrdlmrqsva elckiyqs
//
LOCUS       WP_357609940             294 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357609940
VERSION     WP_357609940.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 294)
  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 294)
  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..294
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..294
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32746
     Region          1..236
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mkiscviltm gnrvaelnra vesalnqidg dvevvivgng advpelsatp pegsaavvks
       61 irldqntgip agrnrgveec sgdvvlfldd dgwyanqkvv ahvrdrfate pdlavisfrv
      121 mdpdggigqr rhvprlragd pqrssavttf lggasairrs aflqvgglpe rffyaheetd
      181 lawrllgegy rieydaetvm yhpqvpptrh aefyrlnarn rvwlarrnlp wplaflyltn
      241 wvvltvvrer asgeplkawf agffeglrtp agerrpmawr tawrmvklgr ppiv
//
LOCUS       WP_357610114             195 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357610114
VERSION     WP_357610114.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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: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=21244
     Region          1..195
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 mpndttlflg qfmrspatig alapssrrla etvctpvper geptvvelgp gtgpftaeiq
       61 rrldgrghhl aielnptlas lladrfprvd vaqddaarlp dllrdrgltr advvvsglpw
      121 aafpetlqer llgavtstlc psgafttfsy ihamplgsar rfrallaerf eevvlgrtvw
      181 rntppayvlh arrpr
//
LOCUS       WP_357610181             400 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357610181
VERSION     WP_357610181.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..400
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43733
     Region          133..399
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mayrfaqdek fnfeiqlalg qvqagagdvg eilsttarvi dgdaeswfte wtrtgervra
       61 laeasaargh qvsarqaylr aaayygtals tidgtedvsr lvptfrvhra cfdefafrld
      121 ppalpveipy eetvlpgylf vppnepaprp tlvvnngsdg pitsawalga agglargynv
      181 llfdgpgqqs mlflhgvpfr pdwervltpv vdflcarpev daggivligv sqagywvpra
      241 lafehrfaaa vadpgvfdvs tswlrnlpde lvalldgger elfdrvvaee msqatpqerq
      301 elawrakpyg igslfdlfte vrgytlagva erittpllit dpegeqfwpg qsrrlfdalt
      361 gpselvafta aegadqhcqp marsladqri fdwfaerlpg
//
LOCUS       WP_357610187             318 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357610187
VERSION     WP_357610187.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Smith,T.F., Gaitatzes,C., Saxena,K. and Neer,E.J.
  TITLE     The WD repeat: a common architecture for diverse functions
  JOURNAL   Trends Biochem Sci 24 (5), 181-185 (1999)
   PUBMED   10322433
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Neer,E.J., Schmidt,C.J., Nambudripad,R. and Smith,T.F.
  TITLE     The ancient regulatory-protein family of WD-repeat proteins
  JOURNAL   Nature 371 (6495), 297-300 (1994)
   PUBMED   8090199
  REMARK    Erratum:[Nature 1994 Oct 27;371(6500):812]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..318
                     /product="WD40 repeat domain-containing protein"
                     /calculated_mol_wt=34838
     Region          <82..>252
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
ORIGIN      
        1 mintpllrga lavgsvlavl taapayaqql devdielpdi gvtlheqadd pkkvsafstr
       61 trayvrssee dsfvkkkgyk eltvspkggk vagvpdtfag ntdsvviids atgktrrirt
      121 vrepletnya lwsrderkla ltiekkvgkk whtlgftlid tvagtakavm ipgvdketsf
      181 ewtpdgryla athhdgvrfy dpdgrvrray pkigtlagge dafspsgkqm vtwcparyte
      241 mfciwdtrsg klanrvgksa edslgwwddr hlislvkeeg gfqavvvdlk gqvvrvladv
      301 sspawekdev ylsytpas
//
LOCUS       WP_357610210             182 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357610210
VERSION     WP_357610210.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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 182)
  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 182)
  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..182
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..182
                     /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=20430
     Region          7..179
                     /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 mselalpirt erlilrryri ddvdallayy sdplvaryip wepwtrefat tvvtkrltst
       61 gitgpesrla vvaehegevv gdvilwpade tlsrgemgwa fhpavsgrgf ateavravid
      121 vafahcgmhr viahvdarne asarlcervg mvqeahlrrd hwtkgewtdt liygllaeqw
      181 hg
//
LOCUS       WP_357610232             790 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357610232
VERSION     WP_357610232.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 790)
  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..790
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..790
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=86617
     Region          2..782
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtaprtsass rqqkarlpae atsfvgrrhe aaevkrclsv sravtltgvg gvgktrlalr
       61 vapdvardfr dgvwfvelaa vedpdmlaqi vvealeirdn rlsspvevlt dhlrdkqalm
      121 ildncehlvh ecavladvll rsapelrila tsrealgfag eqtlsvptlp lpdldgarlp
      181 vkslakcdav clfterarav lpsfaltedn kdvvvgicrq ldglplgiel aavrlralsv
      241 qqlherlddr frlltagsra vlprhqtlra lidwshalcs ekeqalwarv svfagsldle
      301 aaeavcsgsg iareeildlv sglvdksili reehgsqary rlleiirqyg meklvaagee
      361 atlrrrhrdy yralsarare qlfgpsqiaw farlrlehan lhtalehcfg dpsevaggld
      421 maadllyhwi scyylgegrh wldrglaayt epdeiraral wadswlaiiq adltsataml
      481 kesrsigerl elepvlayva lysgmiamce gdaepaialy qealarhrag ddpvgtalal
      541 irlslaysfc gdsaraislg ddclalsdah gedwhraymm malgvevwrq gdaaratele
      601 tksltfnral ddplgtgvnl evlawiaate kqyrraaqll givetawqri gaplsgfghl
      661 shyhhecvqh trqalgdsaf dlafkrgarl tydqalayal gedkrvdeqp aetkgaqltp
      721 reteiaalva qglsnreiaa slvisqrtae ghiehilskl gyhsraqiav wvgeqartad
      781 dgsppdtgvq
//
LOCUS       WP_357610311             186 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357610311
VERSION     WP_357610311.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 186)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..186
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..186
                     /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=20105
     Region          3..183
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 msrrqeiadv aigllaaqgm rglthravdr aaglpegsts yyfrtrqall latverladh
       61 taaeltames sltdrddlve aaaelvgqwl tagrerqlar yelsleatrr pelrdallag
      121 rarlrdmvir vlddsgvada erlagdliay adglvldhll rqgdrpaegp dllprirtll
      181 aaagla
//
LOCUS       WP_357610319             179 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357610319
VERSION     WP_357610319.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 179)
  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 179)
  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..179
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..179
                     /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=19487
     Region          37..162
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msekrkgdvg hnpgvtdrdd vdliveqwrr eragmrpepm avfgriyrla rivgdaqerv
       61 yadwgigrge fdvlaalrrs gepytlapke laaalmltsg gmtgrldrle ragllrrapd
      121 padrrglrvt ltdpgrrave eaaeaglavq rrildalppa dqtrlgdllr allaaaeag
//
LOCUS       WP_357610348             163 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357610348
VERSION     WP_357610348.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 163)
  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..163
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..163
                     /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=17183
     Region          2..148
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mklpvstewv lhcattlaql epgatastaq laqyydlpap ylakqlqalv kagalaattg
       61 prggfrlarp aseitllqiv eavdgtsspy ecreirrrgr galppedcrn tcvlaekmae
      121 ahdawrssla gvsladilds lppstpartr srlagtpghq pps
//
LOCUS       WP_357610355             216 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357610355
VERSION     WP_357610355.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 216)
  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..216
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..216
                     /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=23597
     Region          8..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtgkteradr vsvtrerilt aaerlfaehg vfavsnrqvs eaagqgnnaa vgyhfgtkth
       61 lvraiirkha epveairerm ladmgdsadv rgwaaclvrp vtehlaalds ptwharfiaq
      121 vvtdpslrav vaeetrssps lrrtlegfhr clpelpaevr aergdmarql ithmcaerer
      181 alaegtptpr aswhdaatgl idalvglwla pvtrds
//
LOCUS       WP_357610359             271 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357610359
VERSION     WP_357610359.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 271)
  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 271)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..271
                     /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=28702
     Region          1..197
                     /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 mfvvtgatgn vgrelvrvla dagervtavs rqpapvppgv rhsqadladp aglrtamega
       61 dalfllvage dpeaildqvk sagvrrvvll ssqgagtrph iyrhpvafee avresglewt
      121 ilrpcgfdsn ayawaesirt hrtaaapfae vglptidpad iaevaavvlr qaghagrtye
      181 ltgptpitpr eraeaiggal gapvrfdeqt reearaqmla fmpepvvdgt lailgeptpe
      241 eqkvspdvel llgraprafa dwaarnvaaf r
//
LOCUS       WP_357610361             208 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357610361
VERSION     WP_357610361.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 208)
  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..208
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..208
                     /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=22524
     Region          10..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtigstrglr adaarnseri lraarqvwae hgpdahleei arragvgiat lyrrfpdkae
       61 lvraaldqsi sediapaidq alddddprrg lvtvleaals maarehntla aarnsgamta
      121 qagtpffdsl tllarraqea gliradlvpd dmprimvmlv gvlwtmdpss dgwrryltfv
      181 ldalspeaat plppvvplrq pgdcpvrr
//
LOCUS       WP_357610362             208 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357610362
VERSION     WP_357610362.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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 208)
  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 208)
  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..208
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..208
                     /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=22335
     Region          2..208
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mrftvlgatg gtgvhfvrqa ldadhdvdav vrrpeavadr hpglvvyqgd vmradtlkep
       61 ingtdavvfl vgphstgpct vyssgghnvi eamratgarr ivavtaalvd qpndtliqra
      121 trrivrrvfr eaqadrlvfe relresgldw tivrpprlve gtgkgayrma fdtgvrgglt
      181 lsksdlakal lsmaadpath ghtvdiay
//
LOCUS       WP_357610388             177 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357610388
VERSION     WP_357610388.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 177)
  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 177)
  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..177
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..177
                     /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=19577
     Region          20..161
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtdnldhvar iqqawarerp dvdvspqgvi grlhrlaghl terlcvvyqq yglgegefdv
       61 laalrragap yerapgelaa htmvttgamt kridrlerag lvtrrrsand grgrlvaltr
      121 agrevidqaf tdhmanerrl ldglspeqaa qlesllttwl acfeapqpaq rddqndn
//
LOCUS       WP_357610395            1766 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Nonomuraea dietziae].
ACCESSION   WP_357610395
VERSION     WP_357610395.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1766)
  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 1766)
  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 1766)
  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 1766)
  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 11463197
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1766
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..1766
                     /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]"
                     /calculated_mol_wt=185305
     Region          10..1393
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1312..1578
                     /region_name="hot_dog"
                     /note="The hotdog fold was initially identified in the E.
                     coli FabA (beta-hydroxydecanoyl-acyl carrier protein
                     (ACP)-dehydratase) structure and subsequently in 4HBT
                     (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A
                     number of other seemingly unrelated...; cl00509"
                     /db_xref="CDD:469797"
     Region          <1630..>1750
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
ORIGIN      
        1 mtelsnhsga epiaiigmsa rvpgandlgq fwrnlvdgve svtfftdeeq largvtpetl
       61 asssfikaap vmidmegfdn rlfgmsarea eladpqqrvf leqshaalqd agydpatyeg
      121 sigvyggsgp sqyqwlnlqt npdldsnavk lgmsignnid yvattvsyrl nlrgpamtvt
      181 tacssslval hlaceslrng ecdmalaggv cvelphgagy pamdgfttsd ghvkpfdsra
      241 dgtiwgsgvg vvvikrleda ladgdhirav vlgnainndg snkigfsaps hagqteviae
      301 algvagvdpr tigyieahgt gtalgdpiev aalsevyqrs tgdrgwcgig svksnighls
      361 qasgvvgvik tvlamehgli ppsinferpn paidfdsspf yvvstptkwe dgprraavss
      421 fgiggtnahv ilqeapppaa aasvrgpqll rlsartssal dtmrtqlaeh ltehpelsva
      481 dvahtlrvgr pvlrhrvavv addlagavsa ltdlkrhpag daggtppkva flfsgqgaqy
      541 agmgaalyaa qpafaaavde caellraelg edirqlmfae ggddklretr ftqpalftve
      601 yalarlwqel gaqptgmigh sigeyvaatl agvftlpdal rlvaargrlm qsmpagsmla
      661 vmkdeqevae llidgvsvat vngpgtcvva gtdeaitafa elldgkgvka trlrtshafh
      721 spmmepilae feslvaavpr qtpalpflsn vtgdwitpeq avdpaywagh irrpvrfgdc
      781 varllaekdw vmlecgpgkq laqlarmqlr gakdvlppla slpgpgegag dldvlygsaa
      841 rlwsagvpit vdgdqghrvp lpgypyerey rfispgeaga kpkasqpsgp raledwfeip
      901 awrqltpspl gepvtrclvf vsgergeelv aslgaegaev tvvrpgadys geftvrpger
      961 adydtlisal gdslpsrivh awaldsdqaq aqehgffsml flvqalaaaq radgvrldvl
     1021 tcgtedplgg adltrpeyal magiarvvpl evdglqvrhl dlesggtpaa svlaelrrep
     1081 agdvlalrgg rrwvrefqpv rpsegdsglr eegvylitgg lggigltlae hlgtrlrarv
     1141 aligrggtvt pravraiari eqaggkvtvm aadvtdparl revreevlaa hgglhgivha
     1201 aglpgggmae ikeravaqav ldpkvagtaa lfdvfgdlel dfvalcssvt avsggfgqvd
     1261 ycaanafqda fararhgtrv lsinwgawle vgmaanadaa glaaagptav aegtpvdhpv
     1321 vrsrthdras gplaadthwv ldehriggvp vlpatgqlec araafaavvp apgeghavel
     1381 rdvvflepla vpddtttelv vsfadgsafe vragerlhtq gaaawvrpaq vaavdvaalk
     1441 agmtpeaeqd geyagvltfg prwrspeliw raegeelafv egteqvaaev ghwglhpall
     1501 dvatsfgrgn gggaylplsy grllvrsalp drfyshlrrr gdggaevvta dltlmdeagt
     1561 vlveieefvl rridasavtg slsagdqqsg tgirpadgae affrvlaaad lgpqvvvsat
     1621 alaeitrrer ltrqsleaqa tvarsedfva pegeveaala rvwseilgvp dvgadddffe
     1681 lggnsliavq liaqaraavg vklpmrtlfe apsvrqmaar veqiraeqpa tpastpastp
     1741 astpastpas tpaapattip rvargr
//
LOCUS       WP_357610424             212 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase, partial [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357610424
VERSION     WP_357610424.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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 212)
  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 212)
  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 212)
  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 212)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         <1..212
                     /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]"
     Region          <5..174
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 iggwpapgda atepgvaalv eaarghlgsi dvwignagid rgnglratee dwaashevnv
       61 mahvraarll vpgwvergsg rfvvtasaag lltmigspty svskhacvaf aewlsltyrh
      121 rgvvvqaicp qgvrtrmldn agplqellsh daaitpedva eatwqalhdd rflvlphpqv
      181 atyyahratd tdrwlggmnk lqrrledqga ar
//
LOCUS       WP_357610430             237 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357610430
VERSION     WP_357610430.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..237
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25093
     Region          7..210
                     /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..17,124..125,153,177..178,181..182)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            148
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 msaanqvdav vfdyggvltg pvrdsiaawl hadgidpasf srtlkawlsr gapdgtpvhr
       61 letgaltvde fdallaaela tldgravdpv gvlarlfagm rpdpamfdla rqlrdaglrv
      121 gllsnswgnt yprelidglf dpvvisgevg lrkplapiya ltlerlglpa drvlfvddae
      181 pnvlgaravg mrallhtdad ttrtaiaell pasrtglprp rpgadlphpa rteeltp
//
LOCUS       WP_357610489             501 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Nonomuraea dietziae].
ACCESSION   WP_357610489
VERSION     WP_357610489.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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 501)
  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 501)
  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 501)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..501
                     /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=51701
     Region          36..>321
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mpkpgrdllr ladsvilpgf vgtappdwlr rrlseglagv vlfsrnitgp aqvaeltaal
       61 raenpsalvg vdeesgevtr levakgssrp gnyalgvvdd valteelard lgrdlaaagi
      121 sidfapsadv nsnsgnpvig lrafgadpel varhtrafir gmqatgvaac akhfpghgdt
      181 svdshhgvpv vageieehlr pfraaieegv rsimtghllv prydpsipat lsphvltall
      241 rdelgfegvv itdgiemaav sgaygvggas amavtagada icvggersde ataaevrdai
      301 alavmegrlp eerlaeaagr vtglgawsaa araahaqaar egggrvegei gliaarravk
      361 vtrrssapil pitvaaqvve fapemnlaid kgtpwgvgep lgkllpgttv arltaeesra
      421 avledllrss adrplvivar dahrypwqae aighllsarg davvvemglp ersdlgavhi
      481 atygsarvcg qaaaevitgt l
//
LOCUS       WP_357610536             305 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357610536
VERSION     WP_357610536.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 305)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..305
                     /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=32620
     Region          10..303
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtlsleiapr varvsgkgqr waeartggll alpaalyfll fwlvpfvsav ylsftsydla
       61 gtpewtglan yrrmladpgf wnsakvtavy tvasvvpsiv fglalavpls kpgrynaflr
      121 alimipaamp lvassmtwsv ifadqglant liglagaepk pwltdeglal walvimttwk
      181 hlglfviilt aglqglppav feaaaldgag plrifyritl pllrrtllfv lviavvgamq
      241 sfvpaflltk ggpagatevl plylwatgft fermgyasai amvllvamla lslaqfrvlr
      301 ggdde
//
LOCUS       WP_357610596             381 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357610596
VERSION     WP_357610596.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 381)
  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..381
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=39524
     Region          127..369
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvpyrsalrr lvtsgphais vasvafclfl tvlavktpwa plprgviaaa glvassavwf
       61 rkrwpaavaa vgavayalsg npgplliglf sgagtrlgar faalaaisva gflaqqwidn
      121 ggfgvdalls amaatgavll aglyaatrre ltrslrerae raeterhlrd eqakaaergr
      181 iaremhdvla hkvtlislha ggfevnagae pariqreaal irltaqeale elrkivgvlr
      241 agqdagfpdl rrlveswasa gntvtlhgdl gplpvatara ayrlvqeglt nahkhalgap
      301 vtvsvtgspe dgvtiavvne lrpgahpsgg gaglvglaer frliggtvrs apddaggwrl
      361 egrlpwdasa rgthdqnaag g
//
LOCUS       WP_357610640             473 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357610640
VERSION     WP_357610640.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=51705
     Region          36..418
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 milphtgral aeaapvpywl drperpdplp plhgthtadl lvvgggysgl waallakrdd
       61 pardvllvea gtcgwaasgr nggfcaaslt hgltngvdrf pgeidelerl grenlaaiaa
      121 tveaygidcd fertgelava vepyqlagla edaelarryg hdvrlldrde vraevdspty
      181 lgglwdadrv amldpaklaw glrracldeg vrihehtrvt glrrdgaalr aataggpdaa
      241 pgtvrarqvv latnafppll rrlrawlvpv ydyalmtepl tpaqrdaigw rnrqgladtg
      301 nqfhyyritg dqrilfggyd avyhygnrva peleqrpatf taladhfftt fpqleglrfs
      361 hrwggvidtc trfcpffgta ydgrlayaag ytglgvgatr fgarvmldll sgeetpltrl
      421 dlvrstplpf ppepvraagi nltrwslara daregrrnvw lrtldrlglg fds
//
LOCUS       WP_357610651             362 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357610651
VERSION     WP_357610651.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 362)
  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 362)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 362)
  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..362
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..362
                     /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=38107
     Region          115..362
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdftrrltrg qligldclag waiamvglts aataqapvwa klalafglgp plavrrlwpv
       61 svfglvlavs mvasvsgvvg maylsptyal yvvalerpgr vptnmvaivt vvmavslava
      121 gapagwargv gdvlfglaam ggawtvgrav rerrlyaara verlvteerl riarelhdvv
      181 ahsmgliavk agvanhvmrs rpeeahdalk viesasrdal temrhllgvl rteppdlrpv
      241 pelaelaert rlagvavklr atgvddlpeg vrlavhrivq ealtnvvkha apapcrvtvt
      301 adggqafvev vdegpgrrtl pamveghgli gmrervmmyg gtfsagpgps ggfrvaatlp
      361 yp
//
LOCUS       WP_357610707             468 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357610707
VERSION     WP_357610707.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=50032
     Region          144..459
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrpatwtlrt rlvmavlgla alglvlanva givllhdnlm drvdkqlqqi tkvatakgvq
       61 miprkpivnd vwdvltkria avqqvmiydp dgtlrfrssa ergdpapvld eirtdgpytv
      121 pgtsgpswrv ravplsngst wifaqslael eqtqtsaiai aavvsgfvll llglaadalv
      181 rlglrpltrm eataghiarg dfarrvpahd phtepgrlag amnvmldrlq aeiaartdse
      241 armrrflada shelrtplts vrgfaelhrr ggdageamrr iedeaarmgv lvndlltlaq
      301 ldeerpldrr pvdllevaad tirdtrvrvp drqvklagld grlapvsivg ddarlrqvaa
      361 nlvgnalcht ppdaavtvrv grsggtavle vsdtgpgvps ehvprlfdrl yrvgqgrsra
      421 dggaglglai vsaivrahgg rvevdtapge gatfrvllpd seaapssh
//
LOCUS       WP_357610711             267 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357610711
VERSION     WP_357610711.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 267)
  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 267)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=29729
     Region          8..265
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtqedldlag frtdvtgltt dearalfvla sqgahsalgl dhahgtalrk vmaalpaphr
       61 paaeltsrri lvdpdrwlag prpeadletl raavftdrrl riryrhsdqt tlrtytvdpy
      121 glvakagtwy lvadhrgrpr lfrtdrlsgv svmpaearrr qgveleqvwk elrrqvedrs
      181 egvriavrvr rerldmvtri agayfagppe pledepewms vhlsypvlea vrhllqfgas
      241 vevtgppear aellrasaei agmygaa
//
LOCUS       WP_357610739             193 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357610739
VERSION     WP_357610739.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 193)
  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..193
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..193
                     /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=20808
     Region          21..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtsppapqrr radarrsraa ildaavqlln erpdvsvevi asaagvtrqt vyahfpsree
       61 lleaavdrvt eetvgamdaa gldeesaaea lcrlievsrr mserypvllq mpvspqadqe
      121 rhapvadrlr riilrgqesg efdrrlstdw lvaatialgh aagdeagagr msgeqadaal
      181 rlsllrlyga ave
//
LOCUS       WP_357610757             398 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357610757
VERSION     WP_357610757.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 398)
  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..398
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=42260
     Region          146..379
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrrfrresrr qvlydlllca vlgifvaamg pdpvrdpaaf gmvtvprigl aavavlvgrr
       61 wplaalvlll plgpwrfseg fatvdlswll prrgvkilpl latspfimwy ayltgrrlaa
      121 lwpalvafcl isvvgvgvvl aqgadlalwv smvtgllgty vlpyllgllr rrllqqrtqa
      181 rlsaeaqarl rerariardm hdslghdlal iavraaglel aagldqahvr aagelrlaaa
      241 daterlrqii gllredsdaa plspvdedva elvrrardsg mpitldvapg pvpclahavv
      301 qegltnaakh apgaavtvrv apgqvtvrns rprgrstalp gglglaglre rvrlaggtlt
      361 agpvgdgfel dvtiprtgee dphgsggnrp pgarrsga
//
LOCUS       WP_357610843             167 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357610843
VERSION     WP_357610843.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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..167
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..167
                     /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=18605
     Region          26..147
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mvdavaavle qwrrerpdid irpigvvgri mrisrmwdke ikdflaghgl epgefdvlst
       61 lrrsgepyel tagtflktsl vttgaitlrv drmedkglvt rvrdtadrrs vkirltdlgl
      121 evidrvlplh vanegrllea lgqeerehla atlaallesy gdtpppr
//
LOCUS       WP_357610866             294 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357610866
VERSION     WP_357610866.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=31268
     Region          2..292
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 magrsrrkvg vrapwwfvvp aiavylfivv vpsvngalfs ftdwnglrpd wsvvgldnya
       61 rvfadrtard alvntlvlaa aatvaqnvvg lllalgvnsm vksryvlrvi ffapvvltpl
      121 vagyvwsfll spngavndal ravglgslah dwlgdpdtal yaivaeivwq fsgysmviyl
      181 aglqaipsev leaatidgag awskfrrvvl pllngavvin vmlcligglk qfdqvmamtg
      241 ggpgtateti sttiyksafs lgdfpfsial avvmtvviav lagiqfrltq rkss
//
LOCUS       WP_357610896             202 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357610896
VERSION     WP_357610896.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 202)
  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 202)
  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 202)
  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 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   5  (residues 1 to 202)
  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 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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..202
                     /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=22181
     Region          9..82
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mseglsdpka mralahparl milsrlgveg satatevaei agitpsaasy hlrmlakygf
       61 vedapprgdg rerlwktvdt pisvgvlpgd qpevrdakvs lmlafrrean eeadralarv
      121 etesaewrda trfnrtrirv daeelsrlne siekliepyl ttvrdekaap sgarvaevqf
      181 nlfpvakrpv hglptedhda ar
//
LOCUS       WP_357610913             494 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357610913
VERSION     WP_357610913.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 494)
  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 494)
  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 494)
  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 494)
  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 494)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..494
                     /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=50991
     Region          35..>328
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mplsgdllrl adavlfpgfa ghtppdwlrr rlgdglagva lfsrniagpa qvarltaalr
       61 aenpsvlvgt deesgevtrl evttgssrpg gyalgvvddv dltealardl ggelaaagit
      121 ldfapsadvn snpdnpvigl rafgadpvlv srhtrafvrg lqsagvaaca khfpghgdts
      181 vdshhgvpvv sddgieeall pfreaikegv kavmtghllv psydaelpat lspkvltgll
      241 reelgfqgmi itdgiemaav agaygiggas araiaagada icvggerade ataagirdai
      301 atavtqgllp eerladaarr vrelaswaas sgsrpsrdgs vglvaarrai ritrrsaapv
      361 lpltspayvv elapemnlai drktpwgvge plarllpesv vrrlavgdst gpalerllge
      421 sagrplvvvv rdvhrhawqe qalrhllsar pdavvvemgl parsdlgavh iatygaaqvc
      481 gqaaaevltg rgrv
//
LOCUS       WP_357610900             375 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357610900
VERSION     WP_357610900.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 375)
  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..375
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=39594
     Region          170..374
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrigrpgvra wvtdwtiaic vaaallvtgl sgqhsttnld lfgyalltag glalvarrra
       61 pvpvlvvtgl cavghhaagf dvpavaylfg vyaavraghr aitvaasvtv lallplaala
      121 sglhdtgeaf aqargalela wlvaagaage avrqaerrae eaertreeia qhradeerlh
      181 iarelhdslt hqisiikvqa evavhvarrr geqvpeslla iqeagreaar elratlqalr
      241 dddttpprgl ddvpelvera rsigldatlt iegqrhevpa avsrtvyriv qesltniarh
      301 aaaasasvri dcrpdglair idddgratpd aapvpgvgll gmrervtalg grlraeprse
      361 ggftvqaelp vgqtp
//
LOCUS       WP_357610942             288 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357610942
VERSION     WP_357610942.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 288)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..288
                     /product="phosphotransferase 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=32046
     Region          5..251
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mngdirtlls rhlpdyrvrs vrplgqgldn mvyevndell vrrnkattpd enrqevarla
       61 alrelsplpv pevvfaddes gviayhklpg eplnrhpaqd rqhpapdlrr laeplgeflt
      121 alhaappagl rdvapldvyp aptllqdael dyrdveshvp ekqrplverf feesppdepl
      181 slrfchndlg aehvlvdaea atitgiidwt daaitdpahd falihrdlgp efleatlshy
      241 gfhlddadra rvlfyarcal iedlayglst gphhyadaal ahlawtfa
//
LOCUS       WP_357610937             225 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357610937
VERSION     WP_357610937.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=23417
     Region          15..190
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtgvalaeel lllayddetg ratmprisld lgmaaavlve lalagriaya dgsltvtdpt
       61 pvgepiidgv lgrmaadtph spsswvqrlr hglrdrilgd lvargvvrdv eetelgfivv
      121 hrypvadasv eddsrrrlae alaggqlpde rtaalatlva vlrmepalgl sgdaavdarr
      181 rleeiaggag fsgnvsldds vvrpsvglvv aalaravdqa lgkra
//
LOCUS       WP_357610983             583 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357610983
VERSION     WP_357610983.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 583)
  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 583)
  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..583
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..583
                     /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=60940
     Region          1..451
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          516..582
                     /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(539,548..550,557)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            549
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvirac rdaglgsvav yadsdrdalh atladeayal ggdtaaetyl
       61 ridklidvag rsgadavhpg ygflsenadf aqavidaglt wigptpqair dlgdkvtarh
      121 iaqragaplv pgtpdpvgna devmafavdh glpvaikaaf ggggrglkva rtmeeiphlf
      181 esatreavaa fgrgecfver yldkprhvea qvladqhgnv ivvgtrdcsl qrrhqklvee
      241 apapfltaaq rtqihesaka icreagyhga gtveylvgad gtisflevnt rlqvehpvte
      301 etagvdlvre qfriadgekl rfaedptprg hsiefringe dpgrnflpap gtitalrlpt
      361 gpgvrvdtgi sagdviggnf dsllakviit getraeaier arraldemvv egmatalpfh
      421 rlvvrdeaft tepftvhtrw ietefdntvp pftaaagave apagretvvv evagkrlevs
      481 lpaglgagtt saapaarkpa rrgggakaga avsgdalasp mqgtivkiav adgdtvaegd
      541 lvvvleamkm eqplhahkag tvsglsaevg avitagaaic tia
//
LOCUS       WP_357611037             378 aa            linear   BCT 28-DEC-2024
DEFINITION  epoxide hydrolase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357611037
VERSION     WP_357611037.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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 378)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 378)
  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   5  (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 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..378
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41738
     Region          6..111
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          86..>199
                     /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 msaiairpfr vdipqtaldd ladrlrravw pgelpgagda ygtttdrvre lvtywlekfd
       61 wravearlna hpqfvteidg edihflhvrs srtdatplvl thgwpgsvve yldviaplte
      121 ptdptapafh lvipslpgfg fsgptrspgw nryrtarawa elmarlgydr ygavgndags
      181 mispeigrid pehvlgvhvt qlfsfpsgdp sefqglsead qaalahvqwf fenkfsfnqv
      241 qsqqpqtlaf aladspvgll awngqlfdrs ldpdfvlanv aiywltgtaa ssmrfyweda
      301 httehptgpt tsptglamfp gdfqsirrfa erdhgnivrw tayqadvagr gdvgghyaah
      361 eatdvlvadl reffaalr
//
LOCUS       WP_357611040             213 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357611040
VERSION     WP_357611040.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=22877
     Region          14..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpnptdtppl agrraqaarn davilaaara vfladpkapi aavaeragvg isalyrryag
       61 kedllrklch dglrrfieaa eeaagdpddw hafagflerv vdadvhsltv hlagtftptp
      121 emgrdaaran eltaslvera rgagrlrpdv vvqdvgllle gcaairvpdp ertrqlrrrq
      181 lavllaglav tdpplpgppp aagefdwrwr rpe
//
LOCUS       WP_357611078             573 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357611078
VERSION     WP_357611078.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 573)
  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..573
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..573
                     /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=60497
     Region          4..265
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(4,28..29,58,63,68..71,83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(11..12,14..17,19,32,34,66,82..85,89,91,128,130,
                     132..133,135,145..146,149,161..164)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(11..12,14..17,19,32,34,66,82..85,89,130,132..133,
                     135,145..146)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(15,89,91,128,130,132,149,161..164)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(145..153,157..164)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mvpgyrevrq lgagrtgrvf latyqqtgay vaikylnatl rrdaefmerf rsdthelvei
       61 ddpnvvriye yvetptraav vmelvdgvsl rtlltehrgi speaalavlk stllalaaah
      121 ergvphrdvk penilvqadg sskladfgvv vhaeepdvpa gspeymspel wtqgragppa
      181 dlyaaacllf eavrgrppyr avkegpsggd egaldvpavr dkhvaepipl eltpdtlrdl
      241 lkrgmakdpa aryasarqfa aeveedavag ygpdwekrgr rhlgelatlm alrfplartd
      301 gaagiplrdr vlrmprlpph lwvagatvva vavslmvsgg rlppgpgtil mppprttpge
      361 peptpvdaat ptrtrtsaap rrtapsptrl ptgsappppp tthqdgssvp rpaavryagi
      421 vgwsgtagai kisadgtgpv rlrisytrrd geggvartvr qesrtlrgst sytsgvahdp
      481 gsvscgeray vgivvmtepa aangpqvsev avdgpacpap trsatpaptq ehstpaptps
      541 gteqsfarps deptasgdgl prlvstplde psp
//
LOCUS       WP_357611167             151 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357611167
VERSION     WP_357611167.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 151)
  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 151)
  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..151
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..151
                     /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=16296
     Region          18..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mnenrapqst felvlgggsl lvqvgrelnt eterrlaplg ltaqqaalll hasrgdstps
       61 llksrlgtdt agmtrlldrl eakgllrrvr hpedrrsivi eltdegralv pglppifgri
      121 shqvfagfsp eevaqvtdml rrilgnlaeg a
//
LOCUS       WP_357611259             307 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357611259
VERSION     WP_357611259.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 307)
  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..307
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..307
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33148
     Region          13..76
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(19,23,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..282
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mplssspvir rarlgaelrq lrrrealtle qvcgllgwas tsklsrielg qsrpdladvl
       61 dlldvyqvpa pqrealivia rdaatsrgww kalgemherq rtyaeleaga aaiveyqpav
      121 vpgllqapgy arlrvlagrl lhpdvdvead vrarlarqev lrrpdpphyt glldervcdp
      181 agvpveiwqe qlahllalad lpnvtirvvp rtaappgavh altayscysf pdpadprtvm
      241 letlsndvrl vtdadvarye rmtgwlsava lsaeetaall rdragevang arpggaegep
      301 agqpaag
//
LOCUS       WP_357611263             121 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357611263
VERSION     WP_357611263.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 121)
  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 121)
  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 121)
  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 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..121
                     /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=13520
     Region          2..87
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mrtapgaaav vtdeqnrvll iwrhrfitdt wdweipigki degdsehhif radsaqyigp
       61 pteaweterv ewvpitdirr liderdivsg tsmnarlhtp hrgvvarhpd laspqgpagg
      121 l
//
LOCUS       WP_357611279             546 aa            linear   BCT 28-DEC-2024
DEFINITION  murein biosynthesis integral membrane protein MurJ [Nonomuraea
            dietziae].
ACCESSION   WP_357611279
VERSION     WP_357611279.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Kuk,A.C.Y., Hao,A. and Lee,S.Y.
  TITLE     Structure and Mechanism of the Lipid Flippase MurJ
  JOURNAL   Annu Rev Biochem 91, 705-729 (2022)
   PUBMED   35320686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     gene            1..546
                     /gene="murJ"
     Protein         1..546
                     /product="murein biosynthesis integral membrane protein
                     MurJ"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=54078
     Region          20..493
                     /region_name="MurJ"
                     /note="Lipid II flippase MurJ/MviN (peptidoglycan
                     biosynthesis) [Cell wall/membrane/envelope biogenesis];
                     COG0728"
                     /db_xref="CDD:440492"
ORIGIN      
        1 matdvggpsg rrwvvtrgva gaavligait vlaritgfak qavfagtvgt nclgtayata
       61 nqipnivfev vvggalagmv vpvlagaagr aqvgritsal ltwvlvvlvp lavltavlag
      121 pvmglfsfvg cdaaavsala trmlvvfapq iplyglavvl ygvlqshqrf agpavaplvs
      181 sivvivayll fvplsgdtrd pgtlptpael alsvgtslgv lalvltvtgp alglrlrlrp
      241 tlrfpegvaa qvralamagi agllaqqatm vvvlllsnna igggalvvyn yawaiylvpy
      301 avlavpiats afpglsahaa gqawepfaal aarttravvl vsglaagala aaagpgavvf
      361 lrsltdvppp elaraialfa pgligyglia hlsrvlyaag rgraaatgtv vgwvvamlaq
      421 vgfvlafpeg wqvgglalgm tagmtvggaw llaavararg aepvqgvara tlaafaggga
      481 gfaagsalva lipatgllal tglallagcv alavgaavva lvdradaaal agivlrrrrd
      541 esrmgg
//
LOCUS       WP_357611330             134 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease [Micromonospora purpureochromogenes].
ACCESSION   WP_357611330
VERSION     WP_357611330.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 134)
  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..134
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..134
                     /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=14250
     Region          71..127
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtgrpflcrg edqrshglpt nsrptgaafs lggllssttc trckrliplg tgsrcpgckp
       61 rrvhtlsasq rgytaeyqrn ralvladgpa calcrrrpat tadhirplsr ggtndlanlr
      121 pacgpcnygr gnrt
//
LOCUS       WP_357611347             903 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357611347
VERSION     WP_357611347.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..903
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..903
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=95025
     Region          <2..880
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mplfgreael kvlaglidgp adrsgvlihg eagigksalv aeavsaasaa glhvlmttgv
       61 eaeqnlayag lhqllypvra gvdalpapqr dalrgalgla dttgpsaylv glatlsllae
      121 aaaarpllvv aedvhwldra sadvlafvar riesepigmi atlregersp lqaaglspmp
      181 vdrlsdevaa elldssapgl tpevrarlle eaagnplalt elsaamgdpg gpgpvlplte
      241 rleraftara valpaparta llvaalnqsd svsetlaatg lilgsaaele tlapavearl
      301 ielaigtvrf rhplmrsaip aastiaerrq ahlalaktly ehpdrrawhq aaatsgadea
      361 vaaeldraad rarhrggvaa aiaaleqaar lsegqdrkal rllraaelav esgsrdtaer
      421 lvrdaqalel sprrrataaw llsgfedgvr edvsrvpela elaasvaadg qvepavrill
      481 gaamrcfwse pgpaarrsll dvadrlpvpa gdprmvaiaa yvapferght videlrrlag
      541 aaganpevdr ylgsaalqvg afdlaarfsa aaapglraqg rlgllprala vqawsrarlg
      601 dlatavpvaa eaaafaresg qpfmyglata aqaeiaalrg dhgparalad eaervalpag
      661 arpvlatvql arglaalseg rfddafaals rmldpadpay qlalraycla elteaavrag
      721 rtdamrdivr dlepaasstp spalhiglry aravlapnee aeerftaalr adltgwpaer
      781 grlhlafgew lrrqrraves rthlrtaret fdalgmaawg erarqelrga gesspnrgad
      841 arekltphel niaqlaaegl tnreigqrly lshrtvgthl hrifpklgvs sraelarmlk
      901 tlt
//
LOCUS       WP_357611367             919 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357611367
VERSION     WP_357611367.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..919
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..919
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=97744
     Region          <2..919
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 maearvwpel vgragemsri eaaiadgnrl vlidgepgvg ktrlleylvd haqaagrtvl
       61 aggateferl vpfgmyvdaf trlsdaapgt laeaalrtll sageadqldr yhtyrgiral
      121 lahvadghga vlalddlhwa dapsleltef llrrppaagl llaiacrssm ippavydava
      181 rqdprvirls lgpldedaaa alvppgvdag rrrlmyrvsg gnplflrall dagdttlael
      241 adgrpgatla leqtllavlr reldrlspva rraahaaava gelaslvvis hvaeldapaa
      301 asavdelcrq glgtlagarf afrhplvraa aydtsgagwr vaaharvady lrrtdgslal
      361 lahhtercae pgderaartl gdagiaylns apatavrllr ealrvlperd dlvpyrgqll
      421 tglargtgvm gslaesrrll hevihlphev asvavafssv vsrmlgrlde aralvsaqir
      481 ragqdrrvra qlllelaava mlradpegar lharealglv swaadpelga aayaiqalac
      541 lqdgdlaaar ahskragwlm dsasdttlvp hvelvaplsw seiclqrpta aerhlargid
      601 latmsgrsya mpyllisqaq lkaragrlte aieiaehaaa aseyirsset lamarcvmll
      661 pvlwrdgvqp amaladrlaa drpgsawwqa mayvavaqvr lagraepgyp lpsvltrdtd
      721 verlavqsir agadgdvgaa larsaaavea agdlpyqlgi aydararals grddlagava
      781 aaqiaterfa esgavvergl ahqflatvhs rmgdvaschd eigrakaayk esgadwlagq
      841 larverrlaa rgprqaaret tltarerqva elvsqgltnr evaerlqvsq ktvethvari
      901 fskydvrsrv alarrlasp
//
LOCUS       WP_357611447             198 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357611447
VERSION     WP_357611447.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 198)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..198
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..198
                     /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=21396
     Region          10..193
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 marteaggyr erllagavac lqekgyartt ardlvaasgt nlasigyhfg skdallheai
       61 agffdqwiar versmfatea tspremlera mtelvdafee lrpqltvfve sypaalreaa
      121 lrekladsya rcrevgadmv rravaqlgve lpmapevivs vlvaitdgll lqwlldpaat
      181 pdahqvvdal aalsmlfa
//
LOCUS       WP_357611449             503 aa            linear   BCT 28-DEC-2024
DEFINITION  deoxyguanosinetriphosphate triphosphohydrolase family protein
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357611449
VERSION     WP_357611449.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..503
                     /product="deoxyguanosinetriphosphate triphosphohydrolase
                     family protein"
                     /calculated_mol_wt=54988
     Region          26..490
                     /region_name="Dgt"
                     /note="dGTP triphosphohydrolase [Nucleotide transport and
                     metabolism]; COG0232"
                     /db_xref="CDD:440002"
ORIGIN      
        1 meppadprar rlfggsaral gdlaaspfra drdrivgspf farlngvtqv ispggsgllv
       61 hnrlthslkv aqvaraiaer ltadpahrrl ldelggldpd vveaaalahd lghppfghlg
      121 ervldrlarq rlglpdgfeg naqsyrivts teirgaattg ldltaavraa llkypwtrld
      181 hpdphprhlt paprgaaapp ddpasgsakf gayrteladl rqarepfagr iadwqqtvea
      241 svmdtaddia yaihdvedfy rvgvlqqgav aaelmawqre gghlravtda altgaarrpg
      301 saierlrrql hrkdgwiadd dafaaavehv rqelveglla mpfdgsieae qyvarfsarw
      361 ttrfvdaitv vrrpsvrsgh vllapaqwhe vqvlkfvhhr fvlarpdlal hqrgqarllg
      421 tlvealwewl ldpeeesrlp rrlhdlvela eaelhprtad rigrargrai vdfvaqltdg
      481 qavamldals grsgalwtda fvl
//
LOCUS       WP_357611510             370 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea dietziae].
ACCESSION   WP_357611510
VERSION     WP_357611510.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 370)
  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..370
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..370
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38372
     Region          4..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 meslggllva dfsrvlagpy atmlladlga dvvkierpdg gddtrawgpp yadgqatyfl
       61 gvnrnkrsia ldlrdpgdle varalvarad vlvenfrpgt merlglgyeq vsaanpglvy
      121 csvtgfgagk gaelpgydlv vqavgglmsv tgepsgpgtk tgvalvdvit glhaalgvla
      181 alrhrdatgr gqrvevsllt sllsalanha safaaagvvp ramgnrhpsi vpyevfetad
      241 rpiviaagnd rqfralcevl drqdlaadpr yetnagrvad rltlvpeltr tlatasadtw
      301 faaltsagvp cgpindvaga falasslgfe pvvdgqvanp ialgrtpasy rlpppglgqd
      361 aawvreilgr
//
LOCUS       WP_357611540             159 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357611540
VERSION     WP_357611540.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 159)
  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..159
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..159
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17838
     Region          6..113
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnvpfrvdfr vnncsiertl divgekwtfl vlreafsgvr rfadmqaitg aprqvlsarl
       61 arlvdegllr kepyrepgqr qrdeyrltek grdlypllva lmhwgdkyla deegppvvlt
      121 hrdcgapieq yfrcgeghev ggprevtpvp gsgaelssa
//
LOCUS       WP_357611536             312 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357611536
VERSION     WP_357611536.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Rosinski,J.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..312
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..312
                     /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=34578
     Region          7..>122
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          232..307
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpsdllarsr favspmvdtv aalralynpr tpwqrawrer hieafrrmla arpvarallp
       61 asfnprwtad fltvapaspe ptfaaelaav grlsderira dlratrpepl aaelladglt
      121 rqvvelldwv wthtvepewp ererrlradi vartatlstg gwagvfadln rdmrwlgdgr
      181 lqindylepp lslneaeqlv flpahcrrgw vvwdkptrfg mvypargilv dptspapdgl
      241 arliganran ilarletpls tsqlvvvtgl slgtvsdhlr vlldagavsk rrsgrevlyw
      301 rtplgvalaa ge
//
LOCUS       WP_357611567             314 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea dietziae].
ACCESSION   WP_357611567
VERSION     WP_357611567.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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..314
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..314
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33803
     Region          1..195
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mitvviptig rsslreaipe gvpvivvedt grkgpaaarn agwraadtpw vvfldddvvp
       61 gegwlealtk dleslpedva gsqgrievpl prdrrptdae rntagladae witadmayrr
      121 aalekvggfd erfprayred adlalrmrea gfrlvrgerv trhpvrddgf wasvrfqrgn
      181 addalmrrvh gpewrsliga ggllprhaat talgltalal aaaralsrad dregrglrgg
      241 lrggrglret gaggvwamgi aaagwaglta tfaweriapg prtpgevarm vvtsvaippa
      301 aclhrlrgel rvrr
//
LOCUS       WP_357611645             475 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357611645
VERSION     WP_357611645.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 475)
  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..475
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=52241
     Region          133..372
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlvrrfgqvv vllallviev paialslgml alsfalgmvf lfppqvmmvr rltrlhrrll
       61 rewtgvgiel pylpeppppa pqadgmyrsd rtlyktprip awnnrwkwlv sdpatwrdva
      121 wlaldpavkv almplfalvp grglrvyalw selllgataa srlasqvshl krtrnlaads
      181 qaaemrrier dlhdgtqarl vaigmtlgav eqlvdddpsa akallakare assdtltelr
      241 rlirgihppv laergladav ralamdspmq vtvdvdlphr peapveaavy favsellsna
      301 arhgdaraat vdiscdgpnl rvtvtddgmg ganpangsgl agierrlaaf dgvlalnspp
      361 ggpttvtlgl prvlpehwag kvakmprwka ttiillwgta wcptfpqglv agffkifdld
      421 dkawflalym pevwqwpviv gmitlgtlmy vmafwlsnhh rerwyervlp trlsc
//
LOCUS       WP_357611662             165 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357611662
VERSION     WP_357611662.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=18412
     Region          19..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtardrtdrh ierwlpvlpe ldpdvegavs rmsvvtrhlr tvkdrslael glpaheydtl
       61 halagrrgra tpgeladdmt mapasvtarv dalerrgfvr rmpstvdrrr vdvelteagh
      121 aawhaaievi gqeehrllgv ltpderrlla dllrrvslha erttg
//
LOCUS       WP_357611644             340 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357611644
VERSION     WP_357611644.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=37133
     Region          1..309
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrlvsll lllqargrmt ahelaealev svrtvyrdve algaagvpvy adrgpaggyr
       61 llggyrtrlt gmsadeaaal flagvpgpaa elglgavlta aelklraalp pdlaeqgdri
      121 rqrfhldapg wfrdpeptph ltalaeaiwe erlvdlryqr wkrprevsrv laplgvvlka
      181 grwylvarag eqvrtyrvaa vlaltvrder fdrpadfdlv afwrewtdry ergvyrdear
      241 vrvtaaalef mayvfppams raaraaagap daqgwlyttv piesvrhght ellklgaqve
      301 vlapaelrel maasahamaa iypapadaph astgdstvtr
//
LOCUS       WP_357611724             204 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357611724
VERSION     WP_357611724.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..204
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21551
     Region          12..172
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mppdpirsal apfdavlfdm dgtlvdtegl wweatadvaa glgrelgpsd lphvlgrtvh
       61 dtachlapdd varvsdrltd sfadrirkgv rvvpgarell raltasavpt alvsasprsi
      121 velvlpslgh rfevvvaaed targkpypdp yleaarllet dprrcvaled sptgvaaata
      181 agctvlivst evpslqllya ysfd
//
LOCUS       WP_357611730             287 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357611730
VERSION     WP_357611730.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   ter Beek,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 287)
  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 287)
  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..287
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..287
                     /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=30701
     Region          20..248
                     /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 mttlapvapv petvpsgqar aggsrlwrrf vlalagiyfl vplgasfwft iyneatgvsf
       61 apyaelwtae gflsslllsl glavativlv llltlpamit vrlaaprlrp vmevvctlpl
      121 vvppitfvag isrslqvgge vlaptpfwat liaiqdqdfp lvlvfvyvil vlpfvyrsld
      181 aglrtmdvrt lveaarnlga swpyvmfrvi vpnlrsalas asfltlalvl geytvasilg
      241 yqpfavwivt isgskgqlsv avsvlslllt wlllltisgg trgrrsa
//
LOCUS       WP_357611735             764 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357611735
VERSION     WP_357611735.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=83385
     Region          14..762
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mstqsdgsva qrhddeigre qeyvsllygr lddmreqaaq rlteelrntg gtlqarsqrd
       61 gavqmyadqv eqfsavengl cfgrlddtdg arhyigrigi fdttgdydpl lmdwrapaar
      121 pfylataanp qgvkrrrhlr trqrkvtgln devldlatas ptaheeltge asllaalnag
      181 rtgrmrdive tiqaeqdrvi radlpgvlvv qggpgtgkta valhraayll ythrrelssr
      241 gvllvgpnat flryisqvlp tlaetgvllr tpgdlfpgvs arraesaeta alkgrtvmte
      301 vlaaavhdrq wvpdepleie ierdtvrldp emvrqardra rrsgrphnla ramfdvevvh
      361 alaaqiaeri gadplggenl leeadraeir relreepgir aaldelwpvl tpqrlladly
      421 astdriaaaa pmftdaeral lhrepggwtp advplldeaa ellgederaa aarrerirsf
      481 qreyaegvle iwkgsrsidv edeadggeil gvtdlidadr llerqeeadr lttaqraaad
      541 rswafghvii deaqelspma wrllmrrcps rsmtivgdva qtgalagtps wadalepyva
      601 rrwrleeltv syrtpaeima vaaevlaeid palrpprsvr aggvppwdra vdaaglagel
      661 vaattreaag lddgrlgviv pagradelaa avvealpeaa vgeqpelesr vvvltvgqak
      721 glefdsvlvv dpdaivaesp rgrsdlyval tratqrlgvl rpts
//
LOCUS       WP_357611756             253 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357611756
VERSION     WP_357611756.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Rosinski,J.A. 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 253)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..253
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..253
                     /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=27061
     Region          1..240
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msvwveeise savddrsivh vrepdpatvl afrvseegdg dlmvlgprtr asyltpkvls
       61 rcvtvrlrpg waraalgvpv selvdrvvpl relwgaradl laermkdrpg eesalieeal
      121 lgrlascssa dlsqagllda avgrlsvsrr ppyatregta prvpdvardl giserhlrtl
      181 ftgavgvapk rfaridrvrd vlaragtgsw aslaaesgyy dqshltadfr svmgvspgaf
      241 mvgelpaatt csa
//
LOCUS       WP_357611788             299 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357611788
VERSION     WP_357611788.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   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 299)
  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..299
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..299
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31559
     Region          36..273
                     /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 mrlrptapgr fgtselrlal aaprpaaglt sewrlvdglr thtrrsrnpg sdappvvlvh
       61 glavshrylt plavalsath pvyvpdlpgf glterpgray dvgrhaafla awlaayrlpp
      121 aclvghsfga evaaalaarr pravralvla gptsdpaars rrglvgrwll dtvaeaplqa
      181 pvllrdvwda rpwrvaatvs hsvhnrveed lvrvaaptlv lagardtvvp pawraqvtrl
      241 ipharaatvp gaahnvvtta prqvadaira llapdpdkvd pcasetrrsd psaaasaac
//
LOCUS       WP_357611807             399 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357611807
VERSION     WP_357611807.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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 399)
  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 399)
  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..399
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..399
                     /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=43159
     Region          5..269
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtfslgivga gqfagqfakl wrlhpgvgdi watdlipdra arlvadydla gtmpsfeaml
       61 ssdvdavaif tqrwthgplt vqalragkhv yaavpmavae eeieaiimav qetgliymmg
      121 etshynpatv yarnqiaass fgrlfyaegd yvhdmdlgfy dayrysggdn wkatasyppl
      181 lypthaiggv lgawqthais vsaigvvddr gdgvfdksvs qfgndfsnat alfevegggc
      241 frtnefrrvg ypshiresrf rffgtegsle qlatvslwqd ksgvtdvtdy lqpkptlppd
      301 dpslqhvspa lrdaftsgsa pvhdrsrlpe efthvsnghe gshhfladdf vqgvatgtlp
      361 pvnawvaary tlpgiiahqs alkggerlai pdfgdapra
//
LOCUS       WP_357611815             187 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357611815
VERSION     WP_357611815.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 187)
  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..187
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..187
                     /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=20173
     Region          1..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msndrlaail aaayecftrh gvrrttmddi aatagmsrpa vyqyvrnkdd ayrrlaerlf
       61 adslaqarra atapdadlrq rlhdvlaakl eltlrlhres rhaaelldts trltgdlaea
      121 ytreltdvla galadaagpr aravadvlva ltrgleadlt dpdlprrrlr egvallvagl
      181 ahpgapa
//
LOCUS       WP_357611857             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357611857
VERSION     WP_357611857.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=15901
     Region          1..141
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maedllaqar altsplydla ralrfsgvae aglyalppse levlryvvqe pgvgltalar
       61 algmqasnvs atvrslvgrd lvtrepdpad rrsvrlkptv halhgmalie eawaeifaaa
      121 ladlspsqre sftaaipamv alaealksrr
//
LOCUS       WP_357611843             263 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357611843
VERSION     WP_357611843.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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]"
                     /calculated_mol_wt=28060
     Region          24..250
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgltmaegvp raalrpyvtr lcayrerydr pltrteaavp gavlilafga pmevggarlt
       61 sftgglgdry tvtrisgpte gvevvltpfg arrlfgvpmr eltnlvlpvd dllpawsrta
      121 gerlaalasp terlalaesl laariltapp pdppvlwawe rlvasggsvs vaslagslgw
      181 shrhlvarfh dqvgltpkas arvirfdram gllreglsls dvaascgfyd qphmnrefra
      241 magatpgqir prpqlsrgsd las
//
LOCUS       WP_357611870             494 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357611870
VERSION     WP_357611870.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 494)
  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..494
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..494
                     /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=51248
     Region          11..261
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,103,139,141,
                     143..144,146,156..157,160,177..180)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,141,143..144,
                     146,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,101,103,139,141,143,160,177..180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(156..164,173..180)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <281..464
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mlgsgttlnn ryrlttrlgg ggmgevwrad davlgravav kvllpalmed prfaqrfqne
       61 aramatlahp gvvdvydcgt celgdgrrvs flvmefidge sldrllrrsa ltpeetmrlv
      121 aevadalaaa heqgivhrdv kpanlmirpd gsvtltdfgi ahsasggqlt atgtvlcsag
      181 ycapeqasag titpavdvya lgvvayqclt gelpfdgetp vqiifkhlra pvpplpddvp
      241 agprvlvgra lekdperrwp saadmaaaar haaahpgasi wssaapsaad pghspltqrp
      301 aadapggelp lepgagqeqg sapvtagpat rpaaperggr rralvmaaat aaalvatvaa
      361 vgwtwfrepe plqsvrrdqs vplpvggrti evrlpvkqgq trpptstikd gkvvpsapvp
      421 svgrptttpk psapvtppas ppqeptkept pepsvepstq pspqeptaep ttdpptpdpq
      481 tgpgdvqcvk apcp
//
LOCUS       WP_357611892              69 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357611892
VERSION     WP_357611892.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 69)
  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 69)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..69
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7005
     Region          1..69
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mvtatyqvqg mtcghcvnsv stevsaiqgv sdvqvdlasg rvtvtsespl dtesvraavd
       61 eagydlvea
//
LOCUS       WP_357611907             606 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357611907
VERSION     WP_357611907.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=67429
     Region          88..552
                     /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 mhhsptppah ltvaelgfdp dalrakyrhe rdrrlrpdgn aqyqgargef gyyaadpyte
       61 raerepvrdr vealvvgggf gglltgaklr qagvddirml deagdfggtw ywnrypgihc
      121 diessvylpl leevgylptm ryapgeeirq havaiaklyd lyrdtlfhtr vtelrwddaa
      181 aewqvrtdrg ddfraryvvm sagtltqpkl pgipgietfr ghtfhtsrwd ygytggdqng
      241 glhkladkrv avvgtgatgi qviphlgrds qhlyvfqrtp ssvdvrdnrp tdpawaaslk
      301 pgwqrermen fltvvtggsa eqdliddgwt starlqrhll agtvdtalsp eqreyldeia
      361 dfqkmnqira rvdeivhdpa taellkpwyr ymckrptfsd hylqtynrpn vtlvdtadhg
      421 gitamtesav vvgeqeyevd cvifatgfev gvsgivsgal pvygrdgapl lgtwrqgprt
      481 lhgfyshgfp nlfhlgplqn asavnfvhil qeqathigav vaearrrgia sveptgaaed
      541 awvatirela pdntrfqaec tpgyynnegk prpvsmtygp gpvafhdllr rwraeggmde
      601 vlagnr
//
LOCUS       WP_357611923             410 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea dietziae].
ACCESSION   WP_357611923
VERSION     WP_357611923.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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 410)
  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..410
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..410
                     /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=45679
     Region          15..409
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(53,60,95..96,103,107,114,239..240,243,247..248,251,
                     284,289..290,293..294,296,319,350..352,355..356,358..360,
                     364)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(60,89,91,94,96..97,179..180,187,238..239,242..243,
                     247,290,293..295,399)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mdtvnlmdpa lmadpftgfs rireeapiar acfpgqdtpv wlvtryddvk tvlgehrfvn
       61 npasipggdi pdlreklmka rgipddyvvy ltdgildldg ddhlrlrrlv sraftarrvm
      121 emrprveeis grlldalpgd rvvdlveeya yplpitvice lvgipesdrp lwrewgakmv
      181 slspgamaep vismvdyihd liprrraapa ddlltglika hdddgdrftd telitmvltl
      241 vlaghettah ligngtaall thpdqlamlr arpelmprav helmrwcgpv qgtrvryaae
      301 dvelggmtvk rgeavmavlv sanydprrfe rpdrldltre edgrrevhvg fghglhyclg
      361 aalarqegev afagllsrfp klrlavapde lerqlmpasw rlaslpvllr
//
LOCUS       WP_357611959             794 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357611959
VERSION     WP_357611959.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 794)
  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 794)
  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 794)
  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 794)
  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..794
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..794
                     /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=84737
     Region          16..777
                     /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 metadprnsv ppgrearfag fvaavvglal lvsalpligl pdrlprlpaa fwamaalava
       61 cdarpfvppg rrhtsavfps tcftfaillg wglgpavavq avavavsgwr mrhalwrttf
      121 naaqyacalg aaylvlrlgp gglfdggrlg wpdvaavgga tltwfavnyg lvssalrlrf
      181 ggrwwpsvrq alpyellstg sllllapvlv taarasaali plvlvplfav yrmsrlsteq
      241 ehlaaldplt glpnrkalla evaeqvhlha ervakgdrda hlalllidld rfknvndalg
      301 havgdrllve vsarlvdvvg grdmlarlgg defaivagrl dgvdearela grvvaaltep
      361 vsldglpldv gasigialfp ehgedfatlm rhadvamyda khrndtvavy aaesdhnsae
      421 rlglladlrr vleagpaagr tvrggdgaal psrlaagtda agpdgagang aggrwwprrr
      481 rariavdgsd ellnqiltga dptrrragqp aaeperpelp avpapverae daaadvgait
      541 myyqpqiaia tgevvgveal lrwrhprrgm vdpeelirva eqsavmrllt qrvvddvveq
      601 vakwsaagih lraalnvsvr dlhtgeiadr itdrlaafgv aperlqleit egalmadprr
      661 vlttisrlhr igvaislddf gtgysslqhl rrlplaevkv drsfvlgmad daddaaivrs
      721 mielagalgl rvvaegvede rtwrmlhaag cdvaqgwfha rpmpadelvt wlaryrpvhp
      781 sggpdaeapr rptr
//
LOCUS       WP_357612084             159 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612084
VERSION     WP_357612084.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=18174
     Region          1..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtrwltddeq hawrtfglat rlltdrlerd llaaadmppt yyellvllse aprrtmrmse
       61 lahwtnskps rishavnkle qkgwvrrehy addrrgwlav ltddglaalr aaaprhvagv
      121 rehlidlltp eqlrqladis qvlldhlteq draagrvep
//
LOCUS       WP_357612121             404 aa            linear   BCT 28-DEC-2024
DEFINITION  epoxide hydrolase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357612121
VERSION     WP_357612121.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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 404)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 404)
  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   5  (residues 1 to 404)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15920060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..404
                     /product="epoxide hydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44780
     Region          10..114
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          81..>205
                     /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"
     Region          101..389
                     /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 msatpdnsmi rpftvevpea elkalreril atrwpeketv ddqsqgpqla tmkelarywa
       61 neydwrkvea rlnslpqfit eidgldihfv hvrskhenal plivshgwpg siieqlkiie
      121 pltdptahgg saedafhvvi psmpgygysg kptetgwgpd rigrawvklm krlgydrfva
      181 qggdwgaivv dlmaaeapeg llgihtnmag tvpaeidnlf qkniigsana lenlpaglsn
      241 eerqtceqld fawkhvtyal qmaarpqtlt gladspvfla awmidhdaas lalisrsfag
      301 vpegltrddv ldnithfwlt nsgvsaarly aennfsfwgv kgtkipvavs vfpeemyqap
      361 rswaekaypk lvhynrldkg ghfaaweqpk alvdevragf rslr
//
LOCUS       WP_357612103            1194 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357612103
VERSION     WP_357612103.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1194
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..1194
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=127532
     Region          29..1182
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 megdisaqcd rcgrtaadgd rfcggcgtel galcphclrp latdavfcts cgapragsgq
       61 pvatpqedrr rvsvlfvdli dftpyverad peqvrgmqtg ffsaakrvvg qyggvvekyi
      121 gdavmalfga pvatetdalr cvraglelqr vltrfapsgt delrfrvgva tgealvdvaa
      181 ardggqaiva gdvvntasrm qsvsppggvl vcgtthaltk dairyaeqpp vtlrgrsspt
      241 evwlalspvr rqptdrepdt tplidrehel gllvnalhrs lrdrrpqvvt lfgragigks
      301 rlirelyrhs grlvdepvsw rtgrcppfge nvtfaaladi vkteagildt dpaptasrrl
      361 saavaelvgp gerdrlvdal rplvglagvt lpaeetesaw rrfllalaar rptvlvfedl
      421 hwaddamlrf vellgagard vpllllctar pelvdrdpsw agtitgsvti tlpplrdtgi
      481 aslyahmfgq aafsadmlsp lievaggnpl yaheyvrmli eqgalrqsgr gwslekhldl
      541 pmpesvhavi anrvdlldak dravllaasv vgvqfwpgav aaalgqpves verslrrleq
      601 rdfvheqaas tmagqpefrf rhvlvrdvcy qrlprterva rhertagwld alsqsrdtdl
      661 aevlahhrwa aheiartlgm piqryagpar aalhraarra yalhgldaaa shagralgla
      721 ddsdpvdrlq lellsteisf yrdgnaflsg ggpeqlhala drllahgdda caarawtllg
      781 qaawlradrs aavacldrav alfaplpdsa qkadahaelg rlhmlnyerd aavaaaetaa
      841 gigerlglae irtnaritaa taryqagdra gldelhalve lsrtqqllal pralqnlafa
      901 lreegdwlrs dallstapaa rgsgqtlats ysgeamrayf dgdfgrllaa adafvdtptg
      961 gwdmqvrglr scllvlrglp vppaprplpa agdgpaavga erhrddvaaa letarrsgfh
     1021 rpywtmlgma alcralqgrl deaaalvdel adawtavpal asgewiaaaa yaatlagrda
     1081 avrvramldq lahrtpwsea alrtvtgala aadgdhrrag elhlagaeiy aripdvtdrv
     1141 lalalaaael tlagdpaara plaevrtfal rndapglldl argpvpqagp alas
//
LOCUS       WP_357612124             928 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357612124
VERSION     WP_357612124.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..928
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..928
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=99587
     Region          <11..900
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mgvpavdglp grgqetaale qvlaqarags savlvlrgea gigktalldy aagraagfrt
       61 vaiagiesem elpfavlhql capmlgrlhe lpgpqrdala vafglqegdv pnrflvglav
      121 lsllagaaed qplvclvdda qwlddgsmqv lafvarrlma esvalifavr epdddrklaa
      181 lpelivegls epdarallas avrvpldplv rdrivteahg npmallhvpr alapaelagg
      241 fclpggppla sciedafhqq frslpedsqr llltaaaept gdvgllwrat rlqevpvdaa
      301 apaeaaglve lgtrvrfhhp lvrsaiyert papdrraahr alaeatdphr dpdrrawhra
      361 haacrpdegv avdlersagr aqgrggaaaa asflrraael tpdparrvtr alaaaeldid
      421 aggaeqadnl lavveagpld dlqrarlerl rarlvfsqlr cgyaprllld aahrlapldp
      481 alardtllea vgaaifagrl negpgqreva eaaragpspp tpprtvdvll dsmagliidr
      541 caasvdavrh alhivrqeqk agptdadkrw lwlafrvipe plapelwddd awqematgav
      601 riaretgals vlpmaltyqa cyhvfagefr taaalideat aiseatggap mmytslvlsa
      661 wraqesqamd liettieevs awgegrtvsl adyataalyn glgrydtala aatracqyed
      721 lgffgwalve lieaaartgq qeaavaaldk ltertrasgt ewalgveacs rallsddqda
      781 dslyreaieh lgrcrivvhl ararllygew lrrhnrrqes rtqlrsayea fsrigadgfa
      841 erarrellat getvrkrtag tvteltsqeg qiarlardgh tnaeiaaqlf isprtvewhl
      901 gnvfsklgvs srrqlralps ppkppptv
//
LOCUS       WP_357612125             522 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357612125
VERSION     WP_357612125.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..522
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..522
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=54805
     Region          220..500
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtargrvtlg vlidslgpgl arplalphgr eplvgtpviy dpeepqagld gavllvtgrp
       61 saeilarage ggvavvvvkp gtcdeqalat aakaagtall aappelswgq lytlidalla
      121 vvapagdprg traadlfvla nevavrvgga vaiedlamrv laystvegqr idelrregil
      181 grrvpehptn aeeyaavlra dgvvwshepr efyprlaiav rahgevlgti wavqaeepla
      241 hdaaavleea ataaaphlar inlaadearr rrdeclgwll rgigavdela tsfgllprep
      301 vtvvtlgpya gsadafaath aadllrtafv ayriraatgv vdgrahaiva aeasatllrr
      361 iivdtlarvs erlgggwrag igrtaasvaa vpagarqaee alravcgpfa qelagsheel
      421 saalflmdve aalrpkpsla geplalvaah darhgthyvh slnvwigahy dvpraaemls
      481 lhpntlryrl rrigeliald dpdtrlalal qlrlnaatkq sr
//
LOCUS       WP_357612136             188 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora purpureochromogenes].
ACCESSION   WP_357612136
VERSION     WP_357612136.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=21377
     Region          3..167
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 msradagare erfrslhvet yadllrfver rvpvaeaedi vstvfltawr rfdelpddar
       61 pwlfavarkt manqsrgwlr rraldvrlvs learelsddt vsaatridle rawrvlrpad
      121 revlalvafd gltaeqaatv lgcrrstfam rlgrarqrlr aalepaesva pssfrphdfk
      181 eqqawtqa
//
LOCUS       WP_357612144             255 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612144
VERSION     WP_357612144.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 255)
  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 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   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   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..255
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..255
                     /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=27626
     Region          2..209
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mklvifgang ptgrlataqa laeghtvtav trhpesfpls dpaldvakad aldpeavdrv
       61 vsgheavist lrvpygsevp amfsrsagni vaamaahgvr rlvcvtstgv pmkpppgetl
      121 vyrkvivpml lrmgrplyed aarmedliar tdlawtvirp sglfdgdvvt dytvgppqmv
      181 grftsrrdla dalireaved rnlrsivevl ttdgtpsvyr vflkealghr qgqrltawar
      241 lspcavprlc rrprr
//
LOCUS       WP_357612170             484 aa            linear   BCT 28-DEC-2024
DEFINITION  APC family permease [Nonomuraea dietziae].
ACCESSION   WP_357612170
VERSION     WP_357612170.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 484)
  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 484)
  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 484)
  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 484)
  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..484
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..484
                     /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=50929
     Region          13..467
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtstddgrla dlgytsefrr emslwanfsl gftylspvvg iytlfavsla tggppmiwsl
       61 livgagqflv alvfgeivsq ypltggiypw arrlwgrrwa wmtgwvylva llvtiasvay
      121 gagpylsafl gievsttnti mcalvilava vavnlagtrv lamaaiigft aelvgalavg
      181 gwllltqrrh glgvlfdsfg agsesgyfaa flaagligif qyygfeacgd vaeevpdptr
      241 ripkamrmti yvggaaatfv clalllavpd fgavisgasa dpvsevltta fgptglrvvl
      301 gvvllsflsc alslqaaasr llysyardgm ivgseplsrf savrhvppya lvvaavvpal
      361 vvmgsivsed alvkiisfat lgiylgfqmv vlaalrarlr gwrpsgpftl gaaglavnvg
      421 alvygvlaiv nmiwprtpda pwydnwlval sglvvvglga lylfaarphe hgvapagdai
      481 qeer
//
LOCUS       WP_357612230             406 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357612230
VERSION     WP_357612230.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..406
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44056
     Region          170..400
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtdpsgatsr raahlelder vadrlrgqlp avaertvtai taevpdysgt ltgqmrekie
       61 navrialgtf lqlieradaa dpstplsral eaayalgsge arsgrsmdal laayrvgarv
      121 awrevsattv rdglsaerva dfaelmfayi delsaasvag htdelasagr vhrrylerlv
      181 qqllagepee vlrrsaerae wpppqtltva vlprsnlrgv lamlsphtle sgedlpgvel
      241 aeesavllvp dvhggrrrrl tgavqghrav vgparpwtrv aesyqrvlra lalgldrpad
      301 gapldteqhl arlvlstdpe aladlraqvl qplsalppat arrlaetlrs wllhqgrrdd
      361 vagdlfvhpq tvryrmgqlr elygerlndp atvleltlal aflpae
//
LOCUS       WP_357612237             277 aa            linear   BCT 28-DEC-2024
DEFINITION  PhzF family phenazine biosynthesis protein [Nonomuraea dietziae].
ACCESSION   WP_357612237
VERSION     WP_357612237.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..277
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28810
     Region          9..277
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mhdvlkyvaf tstasggnaa gvvldahgls dgqmlaiaad lgysesaflf pegghayrir
       61 yfsplaevaf cghatiaaav algerigpav vdlftqagpv qveitkgdgi tatltsppss
      121 trpatgeelr ralealrwsa ddldpaypph vanagndhlv laaatrerla dldydfdala
      181 elmaeggwtt vhlfwaesrt vfhardpfpp ggvvedpatg aaaaaftgyl rhlgrlddge
      241 vvtihqgadm grpslltttp vpgdtrvrvs gaavpig
//
LOCUS       WP_357612253             152 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            dietziae].
ACCESSION   WP_357612253
VERSION     WP_357612253.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..152
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16681
     Region          5..103
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkrprpcsia dalavigekh sllvlrevfy gvrrfdglva nigaprdila arlrrlveag
       61 vlekvpyqeh pprfeyhltd agrelrpvll tlmqwgdrhl advppvvfeh acgaeleprv
      121 vcracgeept egsltarfrd pgwtaagaap sp
//
LOCUS       WP_357612276              88 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357612276
VERSION     WP_357612276.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 88)
  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..88
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9029
     Region          <29..>74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvrqpltaeq iaagqrlgaa lraaragrsl vevalaagis petlrkieag rlpapafgsv
       61 vclsqalevp lsdladvwla dmpirqas
//
LOCUS       WP_357612329             119 aa            linear   BCT 28-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612329
VERSION     WP_357612329.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 119)
  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..119
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..119
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=13362
     Region          4..>112
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 mmiledaaaw rswldghhds mteawlvlak kgtshptslt yeqalqealc ygwidglara
       61 rdestycqrf sprrprsaws kpnvarverl rredrmhpag laaveraeag grfpipans
//
LOCUS       WP_357612341             354 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612341
VERSION     WP_357612341.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 354)
  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 354)
  AUTHORS   Rosinski,J.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..354
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..354
                     /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=38193
     Region          14..219
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          247..>314
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mvavrrggvi ayelagmdva dvrfaaspln eltlslrtfr dpgrypvhlp wlrrtehvrs
       61 gldlpllral tndalwspdy ltprphaplt riddelaava rvplermldd lralhpgrlp
      121 aplrgdpatv raritealra ywrtcfapww prmrtvlqad iiyrgqvisa hglaamfadl
      181 servhldegv vrvrlvsntg yrrstggegl tlmptlfsrg vtapispeep plimygtrga
      241 gtlwqaesrr spaaltellg atraglltal etpasstela grlgvttsav nqhlralrdv
      301 glltsarhgr svlylrselg dalimggaag gsdheggpgv lqakaaqapt rssg
//
LOCUS       WP_357612349             101 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612349
VERSION     WP_357612349.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=11192
     Region          9..97
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgrtpphpev sqfdlqqvle alvdpvrrsi vtqldaaaed ikcgdfdipv skstathhfn
       61 vlreaglirq yyvgtsrmnt lrradmeeaf pglldaltra r
//
LOCUS       WP_357612372             232 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612372
VERSION     WP_357612372.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   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 232)
  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..232
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..232
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24644
     Region          5..223
                     /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 mtvfvlvhga whgawawdrv tpllrqagah tvtpaltpdg daglhrhade vvaalealtd
       61 vvlvghsyag lvvreaadlr phlvsqivlm dgwvggdgts lfdlapdsfv tairtaaeah
      121 gggatvpapp pgafgitdpa daawladrlt pqslrsftep trltgavdki pgtgiycrpl
      181 typfdrfade lgyrsipldg phnvmltdpe avarlllqla dqrdygnkkp eh
//
LOCUS       WP_357612412             413 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Micromonospora purpureochromogenes].
ACCESSION   WP_357612412
VERSION     WP_357612412.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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 413)
  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 413)
  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..413
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..413
                     /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=44291
     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 mlyllgvvvi algilisvsl heaghmltak afgmkvtryf vgfgptlwsf rrgeteygik
       61 aiplggfcki vgmtpqdddv epgdehramw rypvwkrtiv msagsvthfa laviaiwlaa
      121 mfmglpnrdl pnplpahvkv vdcviptdav recapgdpvs pakqaglrdd drilavngts
      181 vadytalvkt vrdlppgqpa tityerdgvq gkvqanlasv qrkpldnpdg alvtvsalgv
      241 agpalppgvp anvtygpiea ipatagytkd lavgtyeamk ripekvpalw taitggerdk
      301 dtpisvvgas rlggealeng vwqmlvllfi slnffvgvfn llpllpldgg hiaiawfera
      361 rswlyarigr rdpgrvdymk lmpltyavil vggaftllta tadivnpitl fsr
//
LOCUS       WP_357612394             197 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357612394
VERSION     WP_357612394.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 197)
  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..197
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..197
                     /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=21751
     Region          6..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdgrsrrre dtrqrlfvaa veliaeqgfs attvddiaar agvakgtvyy nfesktvlfe
       61 ellrhgigll tadfraavag lpprealaal vraeleyirr yrafaqllls emwrtnrewq
      121 qtlrllrgea ieviadtvra gvasgdlpad ldvriassal fgvglvvavd wlvfqpdrpi
      181 edvqeallgi vrrvaqt
//
LOCUS       WP_357612460             397 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora purpureochromogenes].
ACCESSION   WP_357612460
VERSION     WP_357612460.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..397
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42947
     Region          5..396
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 msldveaafr aeygravavl vrvlgdidla eeavqdafte avkrwpetga ppspagwiit
       61 tarrraidrl rreasradrh aqaallyaqg ppaeggpvrd drlrliftcc hpalgpaarv
      121 altlrllggl staeiarafl vpeatmaqrl vrakakirda gipyrvprda dlpdrlravl
      181 aviylifneg ytasagerlv rtelcaealr lgrllvdlmp depealglla lmlltearrp
      241 arvtaqgalv plaeqdrtrw dqaliaegqa lvrrclrrnr pgpyqlqaai navhsdaptd
      301 wgqvlqlydq lqalapgpva alnravavae vhgpavalal vddlhldtyh vfhavranll
      361 hrlgrpaeaa aayesaiaht anaperaylr aqlaglp
//
LOCUS       WP_357612467             196 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612467
VERSION     WP_357612467.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 196)
  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..196
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..196
                     /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=20841
     Region          3..152
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 malrigiilg strpgrrgeq iaswvldtar ahggadyeli dladhgldnl deggnpthqq
       61 yehphtrdws alidgfdgfv fltpeynhsf pgalknaldy vyrewndkaa givsyggwaa
      121 gvraaealrl vlaelqvatv raqpavplip afstgafapa egldaavrgm ldqviawsga
      181 lrgvreaksk apaitg
//
LOCUS       WP_357612514             234 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357612514
VERSION     WP_357612514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..234
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24747
     Region          5..217
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 msrpvifdlf htlvhgadde rdrvvgemal mvgvapaalv aayhatwrer lvrwdveetv
       61 rilagrlggt ptdeqvtrag ghrrnlarrl ldsvptatld vldalrddgh plalisnata
      121 etaeawpqsp larrfdvavf scdvrlakpd paiyhtatar lgvapaecvf vgdgadgela
      181 gaaavgmtvl rttehsdtdp swggrafatl gdlpallrap aslssastad rrvg
//
LOCUS       WP_357612527             349 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612527
VERSION     WP_357612527.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 349)
  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 349)
  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..349
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..349
                     /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=36870
     Region          18..337
                     /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 milvigagqa glaagralrl aghdvlllea hprlgeswrr rwdslrlftp aslsalpglp
       61 lpggdrylgk devadylqay aarfelpiql gttvtelrpa pgggfeaatd tgaytgdgvv
      121 vatgpfqqpr lpdlplppei valhsadyrn paqlpdgpvl vvgggnsgvq iaaelaatrp
      181 vtlalgarqp vlpqriagtd vftwlqafgl vrapvtsrlg rlvrdrdpli glgprglrrl
      241 gvrivdrvtt tgttasglll rtasgqtlap rsviwatgyr pdyrwlripg aladglprht
      301 ggispvpglt yvglpfqrcr gsallgwvge daalvaetyt aqrtksrpr
//
LOCUS       WP_357612537             530 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea dietziae].
ACCESSION   WP_357612537
VERSION     WP_357612537.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 530)
  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   2  (residues 1 to 530)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..530
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56444
     Region          22..528
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mrlvtavtgl sviaacaiat dpasssrqpv vhtssgavag vyadrdvqrf naipyaappt
       61 galrwqppqp aqawkgvkdg thtaprcpqn anpadsnpas ttedclylnv taprtvpagq
      121 rlpvmvwlhg ggftqgaggd ydtqrlaeag vvvvtinyrl gifgflghpt lngsgafgll
      181 dqqaalrwir hnaaafggdp rnitlfgesa gafstcaqlt sptaaglfhk aiiqsgtcsm
      241 rqmgidpagg dtvwpsrqsg eqiaaaaaeq igctdaaqtm aclrrapvsa llaaqqkipg
      301 twapsygsdt lpldprravt egrlhpvplm vgttahevry fvamyfdgpg qplsrqtyqq
      361 flrtafdkda rrvaarypvs ahgspslawa aiatdrgwtc ptragnrlla rktpvyqyef
      421 adhtaprpag fpipaafplg ayhggelpyl fdgpgaatdq plstsqrrla dqmiaywtrf
      481 aatgnpndps lprwkplssk sanhvhsltt arrngdgstd hhcrfwdtrk
//
LOCUS       WP_357612547             141 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357612547
VERSION     WP_357612547.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 141)
  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 141)
  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..141
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..141
                     /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=15151
     Region          2..128
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 melrqlqqsf dvfdeaaaar lglnrtdlrc ldvvlgdgpv pagqislalk lspaatttvi
       61 drleragmvf rspdpgnrrr vlvaatdaar saeaeifvpv gqagaqvlqe ygpdelaiil
      121 dflrtarrvq eeqaariral s
//
LOCUS       WP_357612589             158 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357612589
VERSION     WP_357612589.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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 158)
  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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..158
                     /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=17450
     Region          8..145
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mtvytprraa rvllvdaggr vllfsgwdps rpehrywftp gggldpgetp aqaaarelae
       61 etglrldpge lgapvwsetv efpfdgvwyr qeqefflvrv agwevdttgf tdierasvsg
      121 hrwwsvdelt atghryyped lptvltralt dpsggapc
//
LOCUS       WP_357612644             293 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357612644
VERSION     WP_357612644.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=31744
     Region          9..287
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mttdtktnqi gvhalvwagd tsptslayai ektkatgfdl leislhdsan ldvvaardal
       61 rkadlgvacs rglafdadvs sddpsvverg ekllhdslav tgalggthft galysalgky
      121 dhplttagrr nvvsvlrgla qeaqrkvmtl gleicnryet nvintardal vladdigedn
      181 vlihldtyhm nieeddlvrp vhevgdrlgy vhvgenhrgy lgsghldfts ffhaladigy
      241 agpitfesfs savvmrglsn dlaiwrnlws dgedlarhah afitehlhts rsr
//
LOCUS       WP_357612646             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357612646
VERSION     WP_357612646.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32858
     Region          7..288
                     /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 mgavpvahrv vdvdgirtfy reagpvdapv vllphgypss sfqfrnlmpa lgdrwrllap
       61 dlpgfgytra daagfaytfd gyadflrrft dvlglrryai ylqdygsqfg lrlamsaper
      121 vaalviqngd iyedqhgpry aplkemwadp spqalaevae hvsesgfrae flgevpgeia
      181 erispdlwtl swaqvgrppg pdhlvhllad qrstvdwfpr qqaylrehrp ptlivwgphd
      241 gympegaara ylrdlpdael hlldgghwll ethldevvsl mrdflgrvhp pgagt
//
LOCUS       WP_357612710             343 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612710
VERSION     WP_357612710.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..343
                     /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=36766
     Region          33..343
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrsrllpdly afeplclaas rrgicrnvsp itrvgiigag nvaarhadvl sgfpdvtiag
       61 iadtdphrae alasrhdata ygghadllsa ggldavyvcv ppfahgnpeh dvlscnlpif
      121 vekplsldlq taeiiaseie rrslpsavgh hwryldiveq ardllaerpv rlalghwldk
      181 vppvawwlnp smsggqiveq avhvldlarv lvgevtmvha vpadnkidge vdrataavlr
      241 fadgaaglla tsclltqkhr vglevcaegl alelsetrll vdgqrviedd glaktrvdre
      301 finavqgkda dvrvpygeal rthrlalala rsaaegrpvt lde
//
LOCUS       WP_357612753             167 aa            linear   BCT 28-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357612753
VERSION     WP_357612753.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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..167
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..167
                     /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=18001
     Region          1..145
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mytaqlghhf haahrlphid gkcrnlhght whaaitlaap tlnsdgmlve fsafknvmra
       61 widahldhga mlgtddplar vlqakgsrvf vfgedhspdr wptvesvagl laqraaewla
      121 aadprsdayi arvdvaetps nsaswvnpal iytgssawsh aipaaar
//
LOCUS       WP_357612785             445 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora purpureochromogenes].
ACCESSION   WP_357612785
VERSION     WP_357612785.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=43809
     Region          170..442
                     /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 mggtdvtdgw dwrqpggtpa pagppagatp vgpptaphga pggttspwws daladpwrdp
       61 yapaavvipg apdagaapep vsdpdapgrp klrqlllvpl itallagslg galgyafavr
      121 ggagggvalg arpaeapgla qrrpeslagv aekvlpsvvt vrvsslggvs egsgfivsad
      181 ghvitndhvv sgatgrasvv fndgsaapat vvgqdpesdi avikvsrsgl rpvefgdsda
      241 lavgdpvlai gsplslantv tagivsaldr tmqagepggq vryyaaiqtd aavnhgnsgg
      301 plvdsagrvi gvnstikslv aegqeagnig lafaipinqa kritqdiigt gkarrtviga
      361 qvggagtvtg gagvrlaave psgpaagagl kagdvilkln grpmteptdl ialvrkfapg
      421 svvtveyrrg sarqntsvtl aadak
//
LOCUS       WP_357612829             362 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Nonomuraea dietziae].
ACCESSION   WP_357612829
VERSION     WP_357612829.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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..362
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..362
                     /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=39866
     Region          28..329
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtadrlpaat avldgelvsa aavrvdpvrn pyrvyldnlr agdsrrtmrg cldrlsrimr
       61 gapldddqvt gedfpwqmlr yehtsrlrak lleqgwgaay inkhlvalrr vlkeawrlel
      121 mtaedyqrag dlapekvsvq psgrhiqedv lglllaacep anpgderapv dvrdaailav
      181 lytsglrree laalpldayd pdsnalkvlg kgnkqriayi pdetadlvaa wlavrgrtpg
      241 alfpatwkgg rlrtdsdgrp armtgqavrk mlmkrielaa vhapelkkka ltphdfrrtf
      301 igmlldegvd lataqalvgh sspattaryd rrperarraa vnrlrlpgrp apasanerta
      361 es
//
LOCUS       WP_357612816             357 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612816
VERSION     WP_357612816.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 357)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..357
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..357
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38880
     Region          123..324
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msitpcgfar taekglarlh wseggwaveg qppdvpalrp lrgleiewpa aevpldglls
       61 laaagiplta draapwvpag lsalltdrdw lahaadgspr sladlrreeh svrlrrlahp
      121 vdrpkisivm sskrsrmvga alaqmeaqrd veaevllglh gvgfeevrep vescslpvkw
      181 veapesvpfg evlnrtaala ggdylakwdd ddwygprhlg dlfmalsysg advvgttaef
      241 fyleplratv rrttfasgaa ypsevwadhv aggtimvsre kfqeiggfpg lpravdlefl
      301 kaaqkagarv yrthglgyvl rrglsdehtw qlplahflkv avnqwrgfrp sllmeaa
//
LOCUS       WP_357612907             486 aa            linear   BCT 28-DEC-2024
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357612907
VERSION     WP_357612907.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..486
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=51533
     Region          2..280
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
     Region          <341..478
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mafervgvvg lgtmgagiae vfaraglrvi gveadaeala rgrghlerst gkavdkgkla
       61 pgqrdeilgr itlttsredl rdvdlvveai peildykisl fkdldricep gtvlatntss
      121 lsvtaiaaat grpgrvvgmh ffnpapvmkl vevvgtvvte pgvvadvtal agrlgktava
      181 vgdragfvvn rlllpylnha aalmelgvag rddidaamrl gvglpmgpfa lldligldta
      241 yevmgvlfde trdrrhapsp llrelvtagl lgrksgrgfy gasggaphtk qaksrlgtfk
      301 vvgyedegdg laerlraagf ksseepdvvl rladrpvieh avrlpdparm vgvhlvgdqv
      361 aelastalts ehaataardl mkivgltpvp ckdragfvvd allfpylnda vrmydsgyas
      421 iedidaamrl gcgypagpfe mlesfglarv rdglralyte yrepafapap lldqlvtadv
      481 sefprr
//
LOCUS       WP_357612909             235 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612909
VERSION     WP_357612909.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 235)
  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 235)
  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 235)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..235
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25828
     Region          16..224
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 meeiraatvl parrepielh tgdgltlvge lalpldrppv atlvtlhplp thggfmdshv
       61 ykkaanrlpa ladlavlrfn trgtsserga segtfdggeg erfdvsaale yaeyhdlprv
      121 wvvgwsfgte ltlkwahdpl vegaillspp lhratdddld awarfgrplv alvpefddyl
      181 rpdearerfa rvpqaevigv dgakhlwvge pyvrialnei vkrvnpaawp lptev
//
LOCUS       WP_357612936             361 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357612936
VERSION     WP_357612936.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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..361
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..361
                     /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=40307
     Region          40..347
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdphagrtrf elyarkwaag rndeamtkar dasvmrhrvl ptwgevpirr idhsavqqwv
       61 selgahlapa tvrechrllr avlalavrdr vigenpadgv rlpkrrrtda deqvitreaf
      121 agnllpeipe ryralvglag gsglrwgecv glawdaidle ratvrvgrvg ievaghvtfk
      181 pypktragrr avplppfvvk llrahrqlvp pgpagevftn eaggplrrtv frawiwrpal
      241 vragllgkvv qvgprvwrat wrdrdgnevi eefpnrrvar arvsrmaqgg lrfhdlrhsy
      301 atwlvsdgvp indvarvmgh eqisttldry thafeagaek vrasfadfpl tfeadedesa
      361 d
//
LOCUS       WP_357612939              96 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357612939
VERSION     WP_357612939.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 96)
  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 96)
  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 96)
  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 96)
  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 96)
  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..96
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..96
                     /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=10164
     Region          <14..91
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mpnlpeklar lldgrtdgrs pdltvlqlrp ddrlllcsdg lssyvppdli rsalnsadsp
       61 phvadaliaa aldqgghdnv tvmvidivdq aldgrr
//
LOCUS       WP_357612942             260 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357612942
VERSION     WP_357612942.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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]"
                     /calculated_mol_wt=28405
     Region          43..157
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mttdlfdaaa mydedylhff asgadapthg pvvgtaypgr saaadlvwql ldlepgmtvl
       61 dlacghgvla nalaargcrv tgldssavfl eraragaaam avdveyvcgd mrdlpwssrf
      121 drvvnwttaf gyfedptnra vlaeiarvlr sggrlamdld nltkflmsyt psritatrdn
      181 gdmlvdrhhl dpltgrfevv rtvvrdgrar rlafvkrlfa fpelrdwcta agfidvtgyg
      241 edgrplsidh nrmvviadlp
//
LOCUS       WP_357612974             320 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357612974
VERSION     WP_357612974.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=33801
     Region          1..316
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 militgglgf igthttrall dlgescllvq rrpavvperf agepvvveqa dltdesalle
       61 lgkrheitgi vhlagsmpwp pgayeplega dralrsllnv fraagewqva rvgvastigv
      121 yggvtgrlag egalkedvpl pmtaahpipa fkkigellgd hlagtmgldv vnyrigavwg
      181 plghpvspff papqlvhaaa rgaepdlstl ragahlgdgi dlcyaedcgr aiallqlagr
      241 lghrtynvgs grlttngevv aairklvpda radlpegrdp apafwldttr lredtgfepa
      301 ydteraaaay lawlragner
//
LOCUS       WP_357612989             214 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357612989
VERSION     WP_357612989.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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 214)
  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..214
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..214
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22456
     Region          1..168
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 meavffdmdg llvdservwl eietdvmarl gapwtpahqa hllggsmert vdymlavsgs
       61 dvpaetvrew mtggmvrrls agvhvmpgas elldalraed vpvglvtssl keiadavlka
      121 vgrdrfdvvv taddvvrtkp dpepyltaar llgvqpvrcv vledspngva aataagcavv
      181 avpsllaidp apgrlvvpsl ellgvadlra litv
//
LOCUS       WP_357613010             197 aa            linear   BCT 28-DEC-2024
DEFINITION  thermonuclease family protein [Nonomuraea dietziae].
ACCESSION   WP_357613010
VERSION     WP_357613010.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..197
                     /product="thermonuclease family protein"
                     /calculated_mol_wt=21017
     Region          91..>194
                     /region_name="YncB"
                     /note="Endonuclease YncB, thermonuclease family
                     [Replication, recombination and repair]; COG1525"
                     /db_xref="CDD:441134"
ORIGIN      
        1 mstpelgvyh atigvlngtm tpamvdvgfg vrvhaklnla vpgekglrpv rkwvtdrqgl
       61 vvvrvtgrap irtpaelveg sapylyrvad ahvvdgdtld trldlgfgvh idarmrllgl
      121 nvaekttadg vevaawvrew vagqlghltv qtvkdkreky grwlatvygr sglpslnell
      181 laagmaqpyd ggaraga
//
LOCUS       WP_357613006             339 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613006
VERSION     WP_357613006.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..339
                     /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=37199
     Region          4..332
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mteptkepll svqgmekhfp vtkgllkrqv gavkavdgis fdvfkgetlg lvgesgcgks
       61 ttgrlvtrli eptagkvife gqdithmgqg klrplrrdmq mifqdpyssl nprhtvgtiv
      121 gapfriqgvq tehgikravq dilalvglnp ehynryphef sggqrqrigi artlalkpkl
      181 iiadepvsal dvsiqaqvvn lledlqneld ltyvviahdl svvrhisdrv avmylgkive
      241 iadrkqlyas pmhpytnall savpvpdpka rkererirlt gdvpsplnpp pacrfhtrcw
      301 kaqeickkie ppleelaggh rvachfpena patapakas
//
LOCUS       WP_357613065             218 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357613065
VERSION     WP_357613065.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..218
                     /product="helix-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=22674
     Region          4..209
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mssddldals llhdpvrrsl yavvaarggd vgrgeaaeaa gvsrtlaghh ldklveagll
       61 esgfraqekk gpgsgrpakv yrrargersv slpprdyaal asvlagvvda lgaeeqaeha
      121 areagariag rhagepvgqv leargyepya eggalrlrnc pfhvlaeeqp llvcsmnlal
      181 cqglleglgd dparaaldpr pgeccvtlkq tdidiegg
//
LOCUS       WP_357613094             267 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea dietziae].
ACCESSION   WP_357613094
VERSION     WP_357613094.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 267)
  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 267)
  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..267
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..267
                     /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=29359
     Region          37..212
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 meiehtsigs givrsapatv rsrptapapr rlvqapvivl sspragstll rlilgshsrl
       61 haphelhlge itvtapfgvp smamqmlghd qadlehllwd rilhvelers gkqtmvvknp
      121 gdvfvwqria scwpdaryvf llrhpasvla swvaatghpa eastdlllrw mtaldqarth
      181 lpgltiryed lttdpaavvr rvcqhvgvef epsmldygdh tsgryvrgvg dwldrirtgr
      241 iqparelpdq saipeplgpl caawgyt
//
LOCUS       WP_357613170             395 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357613170
VERSION     WP_357613170.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..395
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42895
     Region          4..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 mtsladlrvi daatlfagps aammlgdfga dvikiehprr gdpsrghgas lngvglwwkt
       61 lsrnkrtaav dlshaegqei lrrlaersdv lienfrpgtl erwnlapedl lklnprliva
      121 rmtgfgqfgp marqpgfgtl aeamsgfaam tgepdgpptl pplaladgia glamsyaimv
      181 alrarertgr gqvidlaiie pimgllgpqm taykalgavp rrtgnrsssn aprntyrtrd
      241 grwltistsa qpiaervitl vgrpdlveqp wfasghgrvq hvdeldeava swiaerdaee
      301 viarfeevqa avapiydvtd iaedpqyaal gtfqevpdee lgsltmqnvf frlsdtpgei
      361 rwpgrrlgrd tdevlgeldy pderiaalre agvia
//
LOCUS       WP_357613212             236 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357613212
VERSION     WP_357613212.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 236)
  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 11280949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..236
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=25658
     Region          1..>65
                     /region_name="YndB"
                     /note="Chalcone/flavanone-binding protein YndB,
                     AHSA1/START/SRPBCC domain [Lipid transport and
                     metabolism]; COG3832"
                     /db_xref="CDD:443044"
     Region          6..147
                     /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 mrgiyvetli dapverlwqa tqdpaahrrw darfgridpv pgssparfry atavlpgvri
       61 aghgthager hrpdgtrtsa lrfgsddprs liatgsgywr ylpgpdgvrf ltgytyaprw
      121 glagrladla frplfgwata wsfdrlrlwl ergvpperar rqawrevalr alavacvgvl
      181 aarlgaggag vagavlataa valavpphph tpaarrcrrr padrlaartp sllerl
//
LOCUS       WP_357613227             492 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 4 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613227
VERSION     WP_357613227.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 492)
  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 492)
  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 10133618
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..492
                     /product="glycosyltransferase family 4 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53647
     Region          37..404
                     /region_name="GT4_AmsD-like"
                     /note="amylovoran biosynthesis glycosyltransferase AmsD
                     and similar proteins; cd03820"
                     /db_xref="CDD:340847"
     Site            order(47,240..242,302,324)
                     /site_type="other"
                     /note="putative ADP-binding pocket [chemical binding]"
                     /db_xref="CDD:340847"
     Region          <431..>492
                     /region_name="PRK14959"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184923"
ORIGIN      
        1 mralarkgks amrrlyrgyn rrkaqnappp strqvrilll haygmggtir tvfnlasyla
       61 kehdveivsi lkeaeepffp idprvkfrfi ddrlnpspdp lramlskmps rlipkdetay
      121 hrfnlwtdlk laryirsldt gvlmatrpgl nlvmaqlaqp gvitigqehv alrtqaesmq
      181 elikwryrrl dalvtltkad lrdyrqtlpk kprklaripn avppmsgdvs kldakvavav
      241 grmtrikgfh rlitawetva aahpdwklri ygagpqeenl aqqireagle dkvelpgpts
      301 dvgaelekas ifvlssrheg fpmtileama kglaivsfns phgpkemith evdgllvkpr
      361 tnanlaesii rviedeqlrr slaagaleta rtydvdaige qwdallaell arrdgtyvrp
      421 eppapepspd gaaspgpggv atsapgsdga tsapgsdgat saprsgeaaa tvpgrseqps
      481 pahpsdampp cp
//
LOCUS       WP_357613247             218 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613247
VERSION     WP_357613247.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=22821
     Region          5..194
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtvtiaeell llayndekgt qlvsgtqldp alagallael avngrlelsd kkvtvkdpsp
       61 lgdpeldatl griakegker kpawwvqrlq sanlrkrlls rlaesgvlae qrgkvlgifp
      121 ttrwpeanpd veaavrgrvt salagadpda rtavliaiah aakldgkafp easkqrvkei
      181 aegawtadav aqtiaainav mittitaatv aatttttg
//
LOCUS       WP_357613307             360 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357613307
VERSION     WP_357613307.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..360
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..360
                     /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=38017
     Region          15..355
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mgvfastddp gstgheqvvf cqdkqtglka iigiystalg palggtrfyp yaseeaalad
       61 vldlsrgmay knalagldlg ggkaviwgdp eqikseallr aygrfvesla gryytacdvg
      121 tyvadmdvia retryvtgrs vehggagdss iltawgvfqg mraaaehvwg aptlagkrvg
      181 vaglgkvgky ltkhllddga evvatdvnpk alewvrtthp qvelvddasa lvaadidvya
      241 pcalggalsd dtvpalrakv vtgaannqla hpgiekllad rgilytpdyv vnaggviqva
      301 deiegfnfer aklratkiyd ttreilqlad degvppavaa drlaerrmad vgrlrtillr
//
LOCUS       WP_357613308             246 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613308
VERSION     WP_357613308.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..246
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=26107
     Region          2..245
                     /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 mtlvlvhgvp etaavwdplr aalsrqdvra lalpgfgcpr pdgftstkee yvawlagele
       61 smagdeidlv ghdwggglvv rlvstrpglv rswasdaagl ghpdfewhdl arawqtpeag
      121 eaffeqllav pveeqakaye gfgvphghsl rmasavdqvm adsilalyrs avhvaeewsp
      181 afadipapgl vlapsddpfl trdlarasaa ragaavadlp glghwwmlqd paagaarlea
      241 fwasvs
//
LOCUS       WP_357613350             400 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357613350
VERSION     WP_357613350.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..400
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=41680
     Region          5..331
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 maentdvivv gggyagvmaa nrltrrdgvt vtlinprpaf verirlhqlv ggsddavvdy
       61 qrilaggvgl vvdtvtridt sgrrvtlasg gtlgydyliy avgsgsadps vpgaaehayp
      121 istleearrl rpvvdaapas apatvvgags tgletasela elgrkvtlvc gpvlgpylhp
      181 rarrsvaerl tklgvtvieg pgatvtgvtr davqladgre lgsgvtiwta gfgvpdlaar
      241 sglstdalgr lltdetltsv ddarvvaagd saapsnlpvr mscqsavqlg pqaaetvlsr
      301 iagkqpadfn vgffgqcisl grrtgivqya kkddtatgvf ylggrsmaml ketvckstvw
      361 qmaqearrpg slnlwfkdrq rqelrrakag eapavtgrra
//
LOCUS       WP_357613340             119 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357613340
VERSION     WP_357613340.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=12525
     Region          12..94
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maidcapgla pavalfrslg dptrlailrr iatgearvvd ltgelrlaqs tvskhlaclr
       61 dcglidyrae grqsfyaltr pelldllrsa eqvlaatgea valcptygts teppaevst
//
LOCUS       WP_357613363             237 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613363
VERSION     WP_357613363.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   ter Beek,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 237)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..237
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24813
     Region          2..234
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 miefqhvska yrgvkalddv sftvrpgtvt gflgpngagk stalrvlagl crptsgtatv
       61 lgrpyteler pgfevgtvld agaqhpgrsg revlilgaml lglpksrvde vlelvgltgk
      121 eggravggys lgmrqrlgia hallgrpral ildepangld pqgiqwmrgl lrdlagagca
      181 vllsshllhe veqvaehivm igrgrvlaqg tvaelsrgrg leqtfldlta nadrsas
//
LOCUS       WP_357613364              72 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357613364
VERSION     WP_357613364.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..72
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7577
     Region          2..68
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mpiavdidvm lakrkmsvge ladrvgitpa nlavlkngra kavrfttlaa lcevlecqpg
       61 dllrweadav dg
//
LOCUS       WP_357613374             469 aa            linear   BCT 28-DEC-2024
DEFINITION  amidase [Micromonospora purpureochromogenes].
ACCESSION   WP_357613374
VERSION     WP_357613374.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..469
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..469
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48859
     Region          7..456
                     /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 mavqdimptw igatakqiar gvrrgdvsat qvvadhldhi arvdadlaaf rtvrggeait
       61 eaekvdeqed lanlplagvp vavkentava gvptwngsaa crtpvaeadh evvrrlrgag
      121 avilgltrmp elglwaltdd esgitrnpwd trrtpggssg gaaaavaagl vpiahandgl
      181 gsiripaacc glvglkpgrg vipaqlgaed wfgltehgml tttvadaavg fqvlagrrad
      241 klvppprlrv gvslrspvrg vspdapnrda vaaagrllaa aghdtvpadp vyptalglqg
      301 iatwfaaaat evraagiarr dlqrrsrrhv algewaqrrg yvreadraaw rersinfftd
      361 hsvdllltpa lagpppeaaa wsgrswvanm kaniryapya apwniaglpa ivvpvgrrpd
      421 glpvgaqlig ppgselllls vagqfemqap wtrhapgypr vgtgspaaa
//
LOCUS       WP_357613372             227 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357613372
VERSION     WP_357613372.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..227
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23957
     Region          9..219
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mpaidlsgir avvfdtdgvv tdtarvhaaa wksaldpflr grsapfdvre dylchvdgrt
       61 rldgartfla srgldpseee vaalgeakdr vflaqieryg vaafpaavrl lhelrhrgsr
      121 taavsasthc hrvvtaaglm hlfdvvvagr hdqpgpasfe egarlldvpp aeiavvgdtl
      181 pgieaagqgg fglivavdra glafkelgah vvisdlseld vtgrvrl
//
LOCUS       WP_357613382             141 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613382
VERSION     WP_357613382.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..141
                     /product="YybH family protein"
                     /calculated_mol_wt=15826
     Region          1..130
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mpvetrdqal irtlierwae avhrgdlegv aadhaddivm ydvpppyegl rgleaylkvw
       61 ppffrwqaqg asfaieslev tagediafay allrcgteed lrrdpanrlr ltlglrrqdg
      121 rwvvahehhs fpyvarggqs g
//
LOCUS       WP_357613409             494 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357613409
VERSION     WP_357613409.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 494)
  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..494
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..494
                     /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=51672
     Region          18..257
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,74,89..92,96,98,131,133,
                     135..136,138,147..148,151,167..170)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,74,89..92,96,133,135..136,
                     138,147..148)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(28,96,98,131,133,135,151,167..170)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(40..41,66,71,76..79,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(147..155,163..170)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <307..>366
                     /region_name="rad23"
                     /note="UV excision repair protein Rad23; TIGR00601"
                     /db_xref="CDD:273167"
ORIGIN      
        1 mpqaaplreg dpaaigayli vgrlgeggqg vvylgrapdg rpvavkvlrd gvaaddrfak
       61 eiaaarrvep fcvaqvldas lsgrpyivte yiegptlqqa grhggaelqr lavatatala
      121 aihqagvvhr dfkpanvllg pggprvidfg iaratdagat vtssivgtpa ymapeqlaga
      181 qvgpatdvfa wasvmvwagt gappfgedtl paiinrilhn epqmgdlphq lrsivydcla
      241 kdparrptmq dvllrllggd gqsttpvrgg grtvrvrrrr avvpvaagva vvmsaalvaa
      301 vvwrstspdg agspalaava tpsespaast avtskrgtpr pkrtpkasps srttrsprpt
      361 psdtpatrtp tpspsptttr ptrkpaarvd ldiqpiqlsg gpgqveaegc ymppvhfqtt
      421 vassrkgiwi syrwlvdgmt klsgrswvpe ddytafvtad qymlkagpht vtlrvtspvt
      481 vtrsisidvc svdy
//
LOCUS       WP_357613411             273 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613411
VERSION     WP_357613411.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 273)
  AUTHORS   ter Beek,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..273
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..273
                     /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=30048
     Region          1..269
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mlgfavfylw ptirgvylsf tdyslltppe wsglsnytkl igdgsfwssl avtleyvvin
       61 igvqtivavv lavlmhrltk ssflrgvlll pylvanvvva lvwywmadyt lgvanqflgw
      121 iglgpfgffg eehlviptia lvnvwrhmgy tallifaglq aiprslyeaa avdgstewrs
      181 fwritlpllr pvlamvlvit vigsfqifdt vavttqggpa daskviyyyi fekafsqfdf
      241 gyasamgval ivilagvsml qmrllrages dls
//
LOCUS       WP_357613417             451 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357613417
VERSION     WP_357613417.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=48637
     Region          37..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(148,150,299,301,334..336,380)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mikklpavag vallslalaa cgggnsggaa sadgkatisy wlwdanqqpa yqqcatdfqk
       61 ahpkisvkit qlgwddywtk lttsfvsgsa pdvftnhlak ypefvtkrti lpiddlvkrd
      121 kvdtgiyaeg ladlwvgadg kryglpkdwd tiavfynkkl tekagitdeq lksmawnptd
      181 ggtyekiiak ltvdkngkhg depgfdkskv dtyglwless gngvgqtqws myaasngwkf
      241 tdknpwgshy nyddpkfqea itwwkslidk gympplkate gvawndmlsa gkaamgtngs
      301 wmigsvfgak sakfepalap lpagpsgtrm smfngladsi yagtknkdaa wewvkylasp
      361 acqnvvgeha vvfpaipaav dvaqkkfaek gvdveaftvn vkekttflfp itdhaaqiea
      421 imkpamdavv agtapasslt kaneqvnalf k
//
LOCUS       WP_357613427             313 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357613427
VERSION     WP_357613427.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 313)
  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 313)
  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 313)
  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..313
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..313
                     /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=34424
     Region          <9..304
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mrdfgksrak avkdiierlp vrqragmprf kkkdlagpsl nytkrgfrfk dgrlqlaggi
       61 vvtvvwsrdl pgepssvrvy rdslghwyas fvvlarsepl pdtcrvigid wgvketattt
      121 sstcdlphae hgrkaaakla ryqrmmarrk pqrgqavsng yrqakrqaak lhkkvarqrq
      181 dtgrkwakav vrdhdalave dfkprflaks tmarkaadaa igatkkalve mgrkhgrdvr
      241 lvhpahttmd caqcgarakh alplgertyt ctacgaespr dknsarvmls raglapagad
      301 rvrpdcppdg raa
//
LOCUS       WP_357613437             355 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357613437
VERSION     WP_357613437.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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 355)
  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 355)
  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 355)
  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 355)
  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 355)
  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 10025428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..355
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38897
     Region          23..151
                     /region_name="AAA"
                     /note="The AAA+ (ATPases Associated with a wide variety of
                     cellular Activities) superfamily represents an ancient
                     group of ATPases belonging to the ASCE (for additional
                     strand, catalytic E) division of the P-loop NTPase fold.
                     The ASCE division also includes ABC; cd00009"
                     /db_xref="CDD:99707"
     Site            29..36
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(30..37,93,131)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            89..94
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            145
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mqasvtvtps rlpevllhva vvrpvflwga pgigksslvr qfadslglec vtllgtqlap
       61 edligvpelv ggrsrfappe siardepycl fldelnasap evqkafysli ldrrigsyel
      121 pegsvvigag nrasdnalar pmasalvnrl vhvhlrvsad dwlkwaaang vhpwivdyli
      181 qrpdhlwsap pkteepfssp rawhmlsdvm hsfgpsesld ddtlavlafg tlttshasaf
      241 rayvktvrha ydldavikge vswprrpedr dllyflsetf rarlvkelpa dkrgasargr
      301 dlgfraktll velaeislec aqlvianden gapalptwfl vevgrdlprl iaars
//
LOCUS       WP_357613485             468 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357613485
VERSION     WP_357613485.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 468)
  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..468
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..468
                     /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=49246
     Region          28..398
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 maalrgllar plasyyllls saglllligl tmvfsatsvk dyaeagdasa svtkqavfav
       61 igivafwacq rlpastfrsl grpvlaaavv lllvlnllla ldslfrikal gplranllwl
      121 ylgpiqvqps elaklalvlw gahviarkga algwwkelat plfpvvgllf vlvgyndlgt
      181 mlcllaivvg llwaagvrmr vfaalsavgl lgigvlvava slgagsgavg eenyrlarlt
      241 sfisppdpat cletgcwqlv qarnaiehgg wfgvglgkss lkfgwlpaah ndfifaviae
      301 elgvvgctvi lvlfavlayt glrvarrved pfrrlaaaai tawlvgqavi niggvigllp
      361 ltgvplpfis dggsalvvtl aavgilasfa raepdaaral harpparwvr llwaplpplp
      421 grrrrpatpp aargsvprsr arreddqaap rggrqgrtrg gtanerrr
//
LOCUS       WP_357613518              89 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357613518
VERSION     WP_357613518.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 89)
  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..89
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..89
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9699
     Region          20..86
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtmtitavrp atvnrragln qpvtfgqtva rlrrrrglsq vvcanlvgrs etwlakvehn
       61 ripvdrlsvl rdlarvlgvd lavlievas
//
LOCUS       WP_357613540             482 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613540
VERSION     WP_357613540.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 482)
  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 482)
  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..482
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..482
                     /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=54062
     Region          5..438
                     /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 mpglaiigsg fagigmaikl keagfhdfvi lekaaelggt wrdntypgca cdvpshmysy
       61 syelnpdwsr mfapqeeiwe ymrscadkyg vtphirygkr vvaleyddar rdwtvttddg
      121 emfrtnavvs aigalhipkf peisgresfa gpavhsaewd hsidlagkrv avigtgasav
      181 qfvpqiapva grltvfqrtp pwlhpkpdfa fspgvrrllr apglaramrg aiywalesra
      241 lgfavdprlm kaheklarrh leaqvpdpal rrrltpdyli gckrilissd yypaltrenv
      301 elvtdeitei rphsivdaag aehevdvivy gtgfkvveai qdqhivgrgg lklqdawqdg
      361 ietyygitta gfpnlffllg pntglghnsv vfmiesqvry vidclrllsr traravevrp
      421 evqrafgrrl rerldplvwn aggctswyld ehgvnrtiwp gftfeywart rrvkpeayel
      481 iy
//
LOCUS       WP_357613551             284 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357613551
VERSION     WP_357613551.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 284)
  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 284)
  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 284)
  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 284)
  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..284
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..284
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30596
     Region          1..258
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mntagylsrl glphlinapt sadnlralhi ahiekvsyea leiwlgrttt vdpvesaeri
       61 irgrggycyh lngafsellr algydvtrhv ggiqgrggep gitanhlvlt vrglpsednp
      121 ggewladvgl gdglhaplpl iagtyrqgpf efvlrpseva aggwrfehdp agsfqgmdfd
      181 paptdmsafv emhrqlttsp tsgfvrtaai lrrdaygadi lrglvlsrlg gsvhpvtlds
      241 apdyyaalad ifllplddvs pedkeklwrk vndaheawla gdps
//
LOCUS       WP_357613564             126 aa            linear   BCT 28-DEC-2024
DEFINITION  RidA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613564
VERSION     WP_357613564.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..126
                     /product="RidA family protein"
                     /calculated_mol_wt=13566
     Region          1..124
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mkeelrtseg aapigaysqg lvvgdfvfts gmgpldprtg eivgddvvtq thqvmrnlga
       61 ilaahglgfd dvvkstvhlq hlerdfaayn evyrsyftep yptrttvgsq llgilveidf
      121 vahksa
//
LOCUS       WP_357613597             260 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613597
VERSION     WP_357613597.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,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 260)
  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 260)
  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 10790587
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..260
                     /product="sulfate 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:0015419 - ABC-type sulfate transporter
                     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=27903
     Region          25..259
                     /region_name="CysW"
                     /note="ABC-type sulfate transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4208"
                     /db_xref="CDD:443356"
ORIGIN      
        1 makyglrala llyllfllvl pvvligwrtf englgpvlea lttpqaqsaf rvtlivafwa
       61 vlantvfgvg taillvrhdf pgkrllsali dlpmavspvv vglalilvyg rfapvggwle
      121 nlgvqvifsi pgmvmaavfi slplvirevi pvleelgdeq eqaartlgag pwqtfrriti
      181 pgirwalayg vvlclaralg eygavavvsg rlvektqtlt lfveerfqnf deasafasat
      241 alalvavvtl lltkilrpkg
//
LOCUS       WP_357613600             345 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357613600
VERSION     WP_357613600.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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 345)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 345)
  AUTHORS   Rosinski,J.A. 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 345)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..345
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..345
                     /product="helix-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=37335
     Region          14..321
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrllsvl lllqthgrmt aaalaerlev strtiyrdve slhaagiply geaghaggyq
       61 lldgyrtrlt gltteeaerl flaglpgpaa elgygavvaa lqlkldaalp aalrdraeal
      121 rerfhldtps wysdgdaspy lastadavwr qhrlrvryrs wrgerttvla pyglvlkggr
      181 wyvvadggng pasyrvnqil dltalpetfe rpagfdlptw wrthvmdfra rlhrdealir
      241 lspagrerlr digsavvvar aeagagapda dgwvttvvpi eslthahgdl lrlgaqvevl
      301 aptelrdlla etaaglaaly rtatapsspc spevaastpg qrprr
//
LOCUS       WP_357613613             227 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357613613
VERSION     WP_357613613.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=23780
     Region          31..138
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrtyisrwlf avavavaava vaptpaqaaa ytassdpilf vhgwnssast wntmisrfqa
       61 dgwpssrlra fsyntsqsna ttaqqvgqev dkllastgat kvdivthsmg glssryylkn
      121 lggggkvdgw vslggpnhgt ssanacysta clemrigstf lanlnsvdet pgvptygtwr
      181 sncdgvinpv dstvlsgarn tlascvahns lqsnatiygq vrdfvnp
//
LOCUS       WP_357613705             696 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing serine/threonine protein kinase
            [Nonomuraea dietziae].
ACCESSION   WP_357613705
VERSION     WP_357613705.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11600203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..696
                     /product="WD40 repeat domain-containing serine/threonine
                     protein kinase"
                     /calculated_mol_wt=72987
     Region          2..215
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(4..5,7..10,12,25,27,58,74..77,81,83,120,122,
                     124..125,127,136..137,140,157..160)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(4..5,7..10,12,25,27,58,74..77,81,122,124..125,127,
                     136..137)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(8,81,83,120,122,124,140,157..160)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(21..22,50,55,60..63,75)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(136..144,153..160)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          321..695
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          380..415
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          463..498
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          504..540
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          545..581
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          585..621
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          626..662
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          668..694
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 meeigaggmg rvwrgqdelm grtvavkeir lptadehvhe rvvrevksaa qlnhpciatv
       61 hdivstdngp mivmeyfagr slaqviaaeg plpmahvrgi avdvlnvlve ahqagivhqg
      121 lrpsnillsd arlvvtdfgl srsaeehssr apdapvsaaa flspeqvrge gtsaagdlws
      181 lgatlyaale grspfegptl vatlaavlaa drprpertgp laplldallq rdparrptaa
      241 qalailaatp ptwplaappa alpagppmap paapptspya aslaaphpms paappagpal
      301 lrrrgflygg aaallvgaga taaillrddt ptrpaqaqps tlqetggvld qqsgtpspat
      361 talewkalht ftghhkrqpg qalftsdges vitsryrgdm latwdvrtgq rlrvfgdtel
      421 gsdslsldpd garvvtsgvt waslwnpttg amlkklgghe vpwdtkfspd gsvlvttgkg
      481 epvllwtpdg kllaklkght givwnpafss dstllitpse drtarlwdvr drkllhtfkg
      541 hldivtdasi shdgklaats srdgttrlwd tdtgeqlael egeaynvafr padpavlatt
      601 diggpfrywn paspgqptel pnhgrlnalt fsadgsllat caesgeiflw dgatgaaaat
      661 ltghtgavrf aafnhdgtal ascaedgtar vwqlsr
//
LOCUS       WP_357613730             439 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357613730
VERSION     WP_357613730.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 439)
  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 439)
  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 439)
  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 439)
  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 439)
  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..439
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..439
                     /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=49267
     Region          23..417
                     /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 mtielqrpvg dpividdler lsfrvdrray tdddlaaqem trifdrcwly vghesevpep
       61 gsyvsrdvgg rpvvmargsd gvirvfansc thrgalicsq pagqarsfrc pyhdwtfsnq
      121 gdlvgvpipd gygpgfrkad fglarhrsds yrgfvfvtfd peqprtltey lagateyldl
      181 iddqsevgme viqgaqlhga ranwklmmen svdiyhfral hkryvgymes lgsvpprrrg
      241 gfgralglgh ganelppaaa rplaywtpmf gaevrpriea taarfvdrfg aeraeritht
      301 nravlifpnl miidaiaiti rkidpigagq maitsvalap kdedpdirel rkshyltflg
      361 pagfatpddi eivescqrgy lnrtvrysdl srgmnkevpe ttdelparef wrqwdrlmhg
      421 ddghlevahr temqeaear
//
LOCUS       WP_357613719             218 aa            linear   BCT 28-DEC-2024
DEFINITION  flavodoxin family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613719
VERSION     WP_357613719.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..218
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=23590
     Region          2..>144
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkivalsctq krlpsltdal leaaitgvvr evadaeiqri rlidhriamc egedtcldpe
       61 vgrctldddf qhvvdlaega qamllampvy agnvpavlki fqerlksymn arqrpfgnll
      121 vgtivhsrtm ltepalgslf pwylrlrnkn vasacftqnd hqdltrtaal dlcvavgrql
      181 gmtldgsrsp addrtalplv qpparprcgd paasspga
//
LOCUS       WP_357613741             398 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea dietziae].
ACCESSION   WP_357613741
VERSION     WP_357613741.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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 398)
  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..398
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..398
                     /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=43348
     Region          19..398
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(55,62,84..85,92,96,103,231..232,235,238..239,242,
                     275,280..281,284..285,287,310,339..341,344..345,347..349,
                     353)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(62,79,83,85..86,171,179,230..231,234..235,238,281,
                     284..286,388)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtsgvpevdl tspdvvadpf taygrareqg plarvsapgf slwvltrydd aramlndprf
       61 eitsgsftpp pgipedclpy mrtmtemeap ehlrlrrlva paftarraad frprleplve
      121 allddlprhl ddgavdlmah faaplpidvi celvgvpdad rprwreygaa vaagsgqrfg
      181 eaipailega raaiarrrae pgddlltdli raqdddggrl sdtemvtmvw nlvlagqtpi
      241 nlianavhvl lshpdhlarl raepelmpra veelmrwcgp mllsipryar edvelfgtlv
      301 hkgeavsasi vganrdprvf tdpetldlgr pagtaphlgf ahgphfclga slarvqteva
      361 ltallrrypg lalaaaphea rrvpdpgtwr lftlqvtl
//
LOCUS       WP_357613748             261 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613748
VERSION     WP_357613748.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 261)
  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 261)
  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 261)
  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 261)
  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 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   6  (residues 1 to 261)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..261
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..261
                     /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=29609
     Region          1..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          108..255
                     /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(109,111,113,122..124,126..127,132,140,147,149,151,
                     153,161,163..164,166,169,175,177..178,207..208,210,212,
                     222,224,226,228,234..242,244..246,249)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mdevfkalad asrrrlldsl narngqtlre lcaeldmarq svskhlavle aanlvttvwr
       61 greklhylnt apiseiaerw isrydqarvd aladlkrvle etpmdkpefv yttyigttpe
      121 rlwqaltdpa ftqrywettf ktdwtpgsam twdnhgvvis dpeqvvlese pyrrlsytwh
      181 tftpelaqrf gwdqelqdkv agerrskvtf diepagdrvk ltvihddfdp gstvaqmvsg
      241 gwpeviaslk tlletgaplp a
//
LOCUS       WP_357613784             145 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357613784
VERSION     WP_357613784.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=15670
     Region          11..111
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 maedkqplhs vsvgaavvge gsrllairrr dtgawqlpgg ilerdegplq avrrevleet
       61 gvlvepellt gvyknmilgv vslvfrchvv ggeprpteea tevawltlde ivqqmveafa
      121 vrlqdavaae qkpcvrlhdg isliv
//
LOCUS       WP_357613822             247 aa            linear   BCT 28-DEC-2024
DEFINITION  PIG-L deacetylase family protein [Nonomuraea dietziae].
ACCESSION   WP_357613822
VERSION     WP_357613822.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..247
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26222
     Region          14..238
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mieracdvad lgvilgiwah pddeaylsgg lmamardsgs rvvcvtatcg elgtgdpvew
       61 pphrlaaara relarcleil gvgehhwlgy rdgqcaqvsr sdavarlcdv iarvrpdtvl
      121 tfgpdgitgh pdhqavsawt taafgraasp garllyatfa erraprwsal neslgifppg
      181 ypittpahll avdlvldaet aarkvralaa qetqtgelia gmgvdcftaw vgdesfaepr
      241 ptavrie
//
LOCUS       WP_357613881             170 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357613881
VERSION     WP_357613881.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=18832
     Region          15..156
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtkatpdrrk grqlpsaael rawrdyieta ealrsqlasr lqtesslspg dyavllalte
       61 aqerqmrsse laahigwers rlshhlgrme rrglirrqec atdrggaevl ltpagadafr
      121 rstvphlrai relfvdaltp dqlvaageia aalrahldth qtpqaprndr
//
LOCUS       WP_357613914             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357613914
VERSION     WP_357613914.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..212
                     /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=23377
     Region          7..>94
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstrtgrppk isrpeivaaa lrvieedgtg altmrrlare vgstamalyh hvrdkeelll
       61 lllddyaagi prpalpdepr ermvaaamam hdavsgcpwa vdilkaddlm svgalwypeq
      121 ivdaavragl tieeavdayr iiwrytagei ggraaarrrr eeggptyrer vfaeldakef
      181 prlstvarrw edltardtya kgvralvngl lp
//
LOCUS       WP_357613920             383 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357613920
VERSION     WP_357613920.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=41335
     Region          12..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 mhriaeiqci dmrhriavvg sgpagltfar vlhrhgypva vlerdpapda rppggtldlh
       61 eglgqlaldk aglqaefral srpegqamri ldadgtvlrd wrprpddqan peidrgqlrd
      121 lllgpldvqw grgvtqvvpg ardgvlvhfa dgrqetfdlv vgadgawsri rpavspvtph
      181 ytgvtlvets lddvdtrhpd larligdgsv avygvnralv aqrnsgghvk vyaqfrvpld
      241 whthldladv eavrssllal fdgwaapvld llrhgtafvh rplyvlpvsh twthvfgvtl
      301 lgdaahlmpp lgaganlaml egaelaesia tgpgdldeav rafeeqmwar agrwakitma
      361 glerlvspdp aqalalfdqv qps
//
LOCUS       WP_357613935              91 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF2160 domain-containing protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613935
VERSION     WP_357613935.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..91
                     /product="DUF2160 domain-containing protein"
                     /calculated_mol_wt=9736
     Region          2..91
                     /region_name="COG5477"
                     /note="Predicted small integral membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444228"
ORIGIN      
        1 mlewmvwtvp talvfagval llvvmavwar vsppvarrgf lrietdrgdr lyiglisaav
       61 vlagwmavtd lsmwlalgca llvavvigiw g
//
LOCUS       WP_357613927             426 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357613927
VERSION     WP_357613927.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 426)
  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 426)
  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 426)
  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 426)
  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..426
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..426
                     /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=47163
     Region          1..325
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkyafvglgh raqmyvdall gewrdagtiv alcdtnrtrm dyyverighe vprftpaefd
       61 kvleladavi vttvdathar yvcaaldagr dvivekpltv daegcaaiae aaerstgkli
      121 vtfnyryspr nsavrrllqe gaigrvtsvh fewtldtihg adyfrrwhre rvnsggllvh
      181 ksthhfdlvn wwlaaapqtv faqadlrfyg senarergvt drptrgqgap glgtdpfild
      241 iskdprlkrl yldaehedgy irdqdvfgdg itiddtmsvm vrydngavlt yalnayapfe
      301 gyrvafngta grlelevver awtpphaavd psaaskqhka dawekltlhr hwsrpeeipi
      361 esgagghggg drlllndvfr gpgddplkrq agyrdgirsv ltghsanvsa atgepvhlmd
      421 egtrvr
//
LOCUS       WP_357614123             281 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357614123
VERSION     WP_357614123.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  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 281)
  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 281)
  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 19109191
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..281
                     /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=30422
     Region          7..146
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18877"
                     /db_xref="CDD:467589"
     Region          <230..270
                     /region_name="Fcf1"
                     /note="rRNA-processing protein FCF1 [Translation,
                     ribosomal structure and biogenesis]; COG1412"
                     /db_xref="CDD:441022"
ORIGIN      
        1 maakdgdgwt ecsqghrhwg lhgasgllvv hhdergvpyv lmqkrswwsh hggtwglpgg
       61 ardshedavt talreareea alagdelrvq gvylddhggw afetviaesa ellaavpans
      121 esselrwlpl pevpdrrlhp gfaatwgeiq geirpetvvl dvanivgara ergwwrdrlg
      181 aatrlledvs rlrlahpvla qwyprvvavv egaarsapav pgiqvvgatg sgddaivdvv
      241 rqakpwervl vvtadrglre rvhelgaetv gpkwllsqlg g
//
LOCUS       WP_357614153             244 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357614153
VERSION     WP_357614153.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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..244
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..244
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25750
     Region          42..216
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mssggdtavv ipavneadri aatvaaaadl pgvdlvvvvd dgstdqtgrv araagarvvr
       61 hsrnkgkaaa metgaeavrl ldeersprhl lfldadlgat agaaapliep vraakadmti
      121 avfttrvklg ghglvvrlsk egirratgle laqplngqrc ltraafeaar plahgfgvet
      181 altidllrkg frvvevevem ahratgtdwr aqlhrarqlr dvalalaard plvvqnldkl
      241 rphr
//
LOCUS       WP_357614142             226 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357614142
VERSION     WP_357614142.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 226)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..226
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..226
                     /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=25015
     Region          2..209
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mprlvdhdrr raelgeaair vilreglagv tvrgvaaeag wstgslrhyf rnqhelqayv
       61 vqattdtlrr rvlprvqrpr tassvvegia tiveemlpld aerreeyalw savvawerqh
      121 ppeggsvtwn dqravyrqcv avlrayepvr epsqatlphp daqvelwaal lhtfvdglaa
      181 qimntpgevs adtaaqllrs llqavpparp eqgahrprae satrah
//
LOCUS       WP_357614158             391 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357614158
VERSION     WP_357614158.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 391)
  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 391)
  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 391)
  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..391
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..391
                     /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=39792
     Region          11..391
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mfdasgmttv dtravhagrd dlaglgvhvp pidlsttnpl psvegggday ellatggtlp
       61 agasavyqrl wnptvarfet alaelegtaa avafasgmaa ltaallaatr dgkrhivavr
      121 plyggtdhvl atgllntevt warpdevaaa vrrdtalviv etpanptldl vdiaalataa
      181 gdvpllvdnt vatpvlqqpa rhgaalvlhs atksigghgd vlagvvacda dwaarlrqvr
      241 avtgavlhpl gayllhrglq tlplrvraqq agaeklagwl tghpavvrvh hpsvhdpagl
      301 igrqmsgtgs llafevrgga paaaavagac elithavslg gvdtliqhpa slthrpvage
      361 akpgagllri svgledpedl radleralav l
//
LOCUS       WP_357614159             370 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357614159
VERSION     WP_357614159.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..370
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=38127
     Region          128..364
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mvrsgellmv vavtaglglv iallgigvmw rlrtrsigvm lavvvvvava atlagvvaii
       61 mkmiiggpvk dfvlsvvavg glvglgvafv larrvvresr rlvsavravp feaprglpae
      121 lqtiantlee ayareraleg arrelvawvs hdlrtplagm ramvealqdg vvsdpptvar
      181 yhaqikleve rlsamvddlf elsrihagal rlsrsrigla dlvadtlaga eplarakgvl
      241 ltaeasesvp veadagalgr algnlvvnai rhtpsdrtvv lragvdddgm aclsvadccg
      301 gipaedlprv fevafrgeaa rtpaagggag lglaiaqgiv eahdgvigvv ndgpgcrfei
      361 rlpavgsggl
//
LOCUS       WP_357614204             347 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357614204
VERSION     WP_357614204.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..347
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..347
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37674
     Region          87..346
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mhktddlqdi vdetarllgv satledrsfr llaygaqhgd idtvrqesil rrrassevra
       61 yferfgiara egpvhipase tlmarvcvpl rhtgvtygyl wllgeladaa lerirpliar
      121 aasllaqear srhdlgrela vllsadpeer agaaldltgp vtaiavresa ervaalwtlp
      181 rgvlaragqp vavlapahla geiagqlqtt ygtaaglgap rqepadawqs wrearhalri
      241 aehfprfhpv arwaelgvhr llarlgtadl relaeetapl dgelahtvet yldlgghaqk
      301 aaaelgihrq tlyyrlgkae rltgldlsdg ddrlaahlgl kavrllp
//
LOCUS       WP_357614208             486 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Nonomuraea
            sp. NPDC050786].
ACCESSION   WP_357614208
VERSION     WP_357614208.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 486)
  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 486)
  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 486)
  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 486)
  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..486
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..486
                     /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=51685
     Region          8..486
                     /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 mngtlkriav aclamfallm invnylqavk aedfrtdarn trnfyeryai ergritaggk
       61 vlaqsvetks defrfireyp earlyahvtg ffspesesai eksenqlldg ssadlllrrs
      121 idlftgepak ganvdltinp kaqkaaydal rqsgkrgali aldpktggil amvslptydp
      181 telsgtdktk vfprydelak ekgqpllnrt idqtyppgst fkvvtaaayl eddssrgpqt
      241 tvdapqrlpl pntsislpny ggtacgsgsv tltyaleksc ntpfgkigme lgfdkmkeqt
      301 ekfgmgqpla vpmavaqsdf gkdydkaala masigqnsnr mtplqmamia agiandgkvm
      361 kpylvnkitd akgdtvdqad pqelseavss etagklremm vsvvqngtan laqipgvqva
      421 gktgtaetad gqpphawfis fapaqdpkva lavivesgaa nvgaeatggh taapiakavl
      481 eavlnk
//
LOCUS       WP_357614302             216 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357614302
VERSION     WP_357614302.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=23402
     Region          11..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 mgllsrldrf narhpwshnd fygrwvagqv aaggarhvld vgcgtgnlid rlrlravsvt
       61 glepdpptar iaaarfagtd avvieeagfg qrdrdrqwda itlvavlhhl plsetlrelr
      121 eclspggrlv vigcyreatp sdflisaaal aanpvmglik hpalarslpv qmtaptaaar
      181 etldeirvqa aatlpgarir rrlfwryslv ydkpaa
//
LOCUS       WP_357614356             408 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea dietziae].
ACCESSION   WP_357614356
VERSION     WP_357614356.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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 408)
  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..408
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..408
                     /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=44498
     Region          18..403
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(53,60,88..89,96,100,107,236..237,240,244..245,248,
                     281,286..287,290..291,293,316,344..346,349..350,352..354,
                     358)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(60,82,84,87,89..90,174..175,184,235..236,239..240,
                     244,287,290..292,393)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 metertafvl dpashdvhad sarlreagal vpvevegvra waatrhatla avlahpdlsr
       61 dvrhwdpear aaappntais kiasdrsmln aegeehlrlr splsrsftar rvqglraria
      121 elaaglvdhl atlppgpvdl rleyayplpr dviselmgvp ealrdrlhel tdvaarvgdg
      181 pddvsssrae lydlleevie vrrrtpgedl itdlivtreq dgerlteyel ldtvellfia
      241 ghvttvnlit ngarvllthp dqlamvrsga rpwsaaveet lrwdspiahf pmryavrdle
      301 iegvtlrkge avlgcfasag rdpdeygera erfdvtappp shlsfghgph fclgaplarl
      361 eaevalatlf eafpdltlad rgegrrplgt vlgnsarnlp vllgrrag
//
LOCUS       WP_357614360             109 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357614360
VERSION     WP_357614360.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=11436
     Region          24..105
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdepespava psaglpglal dtqeflkalg sptrqrimll faggaelsvg evaeragisq
       61 atasqqltll rrgrvvtsrr dgktvyyrad rdgavaalae lqsylktcc
//
LOCUS       WP_357614363             369 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357614363
VERSION     WP_357614363.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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..369
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..369
                     /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=39672
     Region          1..349
                     /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 mtttsepvii vgggqsglaa aravlsvglr pvvlqagvea vgswpdyyds ltlfsparys
       61 alpgmafgga dpdryptrde vvaylrryag sldadirtgv rvtavhprrg agymvrtdtg
      121 deipaagvia asgsfgnpyl pvlpgqedfa gevrhvahyr rpepyagkrv ivvgagnsav
      181 qvahelasha svtlatrapi qfvpqrirgr dlhhwlhvtg adrlpravlt rlvrhaavld
      241 tgvyreaias glltrremft afapdgvvwa dgsfevvdav ifatgyrpnl nylaplgtle
      301 rgmprqvagv stthpglvyl glefqrsfss ntlrgvgrda ayvvaalter vsgatrrrrw
      361 lterlpvrr
//
LOCUS       WP_357614404             249 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357614404
VERSION     WP_357614404.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 249)
  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 249)
  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 249)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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   8  (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 19604043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..249
                     /product="GbsR/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=27261
     Region          1..>100
                     /region_name="Tra8"
                     /note="Transposase and inactivated derivatives, IS30
                     family [Mobilome: prophages, transposons]; COG2826"
                     /db_xref="CDD:442074"
     Region          81..228
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mprghltyed rrriaeglag klayaeiarr lgrprstvgr eiarnggphg yhaaraqqaa
       61 ewrarrrpsp psitpasada dgrdpqavre leerltarfg giptmaarvm aclfvsdtgt
      121 mtvaelterl gvspasiskg vgwleqvglv krerdrrrer ytidtdvwyr awlvgmrsmt
      181 lwadtvrdgv dvlgahtpag irlrtasrff dlissdmaqa aehyrrtfsg agapdaarqg
      241 sglslpqap
//
LOCUS       WP_357614457             213 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357614457
VERSION     WP_357614457.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..213
                     /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=23183
     Region          13..102
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mngdfvrdhl ppaparvvei gcgplggfvp dllasgygat gvdpvapegp pyhrmefeey
       61 eldgpvdalv actslhhvhd ldevfgkvag altrngvfvv vewarelfde dtarwcfsrl
      121 sdeddswlhr hrdgwaasgq pweaylggwa aeeglhsgae leaalgrwfe plavergpyf
      181 fterdggage raaidaglir atgiryagrp lrr
//
LOCUS       WP_357614506             231 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357614506
VERSION     WP_357614506.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  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 231)
  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 231)
  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 231)
  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..231
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..231
                     /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=24834
     Region          2..210
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mrivvigasg ptgrqltgqa laaghhvtav srrprglprh dhltvvaada tdpaaiepav
       61 agadavlsal gvtpsrkpvt tysaaatavv aamrrhsvrr lmvvsssvld pgwrpsnaff
      121 fnhvldpyvn rvlvrqvhqd mrrmeevvra sdldwtvvrp sglfehptvt dhlvadgsad
      181 gvftaradla aamlrelder rfprramgva ttavkpglvr lvrdevlrsp r
//
LOCUS       WP_357614518             259 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357614518
VERSION     WP_357614518.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..259
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28711
     Region          1..259
                     /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 mrlhvkefdg prdrtllvvh ggpdwdhsyl vepldrlage rrllfpdlrg cgrspvadpl
       61 tpdamvadlv eligsspvdv lgfsygglia qrlairhpel vrrlivasss vlpvpqgafd
      121 gwdeyecrrq ahpsvwdtsa legaeltrae afataplnvw rreslpayle rlervtftat
      181 ylepyrsgrf psarcpdpve rlrgvplfll hgrqdmifpv slvgrtpcae avileeaghm
      241 ahvdqpeawl aavrgllar
//
LOCUS       WP_357614579             356 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357614579
VERSION     WP_357614579.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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..356
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..356
                     /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=38941
     Region          163..288
                     /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 msrttedalr aavqdlvgea rpapdlaava iargrrlrar rratagtavl vavlvvtvpf
       61 vllrpapptr pavpepqptp svhampgtgw kdsplalpgg wrvtggvrgg sgylldrgry
      121 vrtrgydevw paptgtvtav adedrpgqig lvdsrkatvr wyrapgadpq wspdgrrlvl
      181 trfrqgahhi gilaldgtfr eyavdrtryf ctdrclftwa rngrevalpl tdafkprses
      241 erhprwgvqf fsaddgrptr fvtipgdpag pwafspdgqw avvqgqrdpl lvdavtgtvv
      301 rtlpsaevaw vsndrllyrr psgsgdfvla dtegrelerq plprelvdrd vsvapq
//
LOCUS       WP_357614627             200 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357614627
VERSION     WP_357614627.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 200)
  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..200
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..200
                     /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=21647
     Region          16..198
                     /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 mdyvrsdrds sgprlplalk iliaggfgag kttlvsalse vrplqteevl tgagigtddl
       61 sgveaksttt vamdfgriti nedlqvylfg tpgqdrfwfl wdelafgalg avvladtrrl
      121 adcfpsidyf eqrgipfvvg vncfdgfrrf gieavrqald idpdvpvvlc dardrqsakl
      181 vlislvehva rqrgepvpvs
//
LOCUS       WP_357614642             168 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357614642
VERSION     WP_357614642.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 168)
  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 168)
  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..168
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..168
                     /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=18203
     Region          <27..130
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maaeldgaag allslweaar esttsrlsaa qlravmvver hdginlrrla tlldmllssa
       61 srlcdrlvaa gmlerepgrv drreislhlt peargllael rrdrrrrlad vlagmsdedr
      121 qallrgvref driardlees appvvpwqgs gvpphdgaig dpsaarsa
//
LOCUS       WP_357614674             303 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357614674
VERSION     WP_357614674.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 303)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..303
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..303
                     /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=33012
     Region          2..298
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 maapiplrsr lrrygtsyam llpflalfag fllwplansl ylsftkfdgi npavftgldn
       61 faqlagdarf rhalgntaly vvgsvvlgtl lslclalafn gtgwlhrimr tvfflpsvts
      121 sialmlmwkw vlfpsdvgla ntivswfggs avawlatpal aipilvlmsv wggmgygmvl
      181 yvaglgsipe eyyeaaridg astwrqfrhi tlpllrpvtt yvvvtgliga fqvfeavyiv
      241 fstgantvgg vldsglmivp ylydqgfthf rlgyasaiaw vlfliifvls lvnlrvgram
      301 kel
//
LOCUS       WP_357614765             173 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357614765
VERSION     WP_357614765.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 173)
  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 173)
  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 173)
  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 173)
  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..173
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..173
                     /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=18886
     Region          12..172
                     /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 mrylrsagpv girrprpade aefvaaarrs rdlhhpwlta pdtaekfaay lakarrrdqq
       61 sflicdrpsg giagyvnisg iimgplrggf mgyaaflpys gtghastgig lvlahafdtl
      121 glhrveaniq pgnepsrrva rklgfrlegf spdylfidga wrdherwavt apa
//
LOCUS       WP_357614815             168 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357614815
VERSION     WP_357614815.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=18322
     Region          1..165
                     /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 mlrgrsvilr pvtdadvpal aairataevr rwwrggddla aavraeladd dliayavehd
       61 erviglvqyy adpdpdyrha aldiyldpav hgsglggdti rtlarhliaa hghhrltidp
      121 aaantaaira yakvgfrpvg imrryerged gtwhdallme lladelad
//
LOCUS       WP_357614868             201 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357614868
VERSION     WP_357614868.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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]"
                     /calculated_mol_wt=21882
     Region          32..175
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mrqahhsrgi lgwaigwmfa hrpsnrqrni wavslldvqp tdrvleigfg pgvaiaefag
       61 ratrghvfgi dhsramlrqa arrnaaavra hrvhlthasv eglpsfgdpl dailavnsvg
      121 fwpdpverlr elrrllrpag rialvsqprs pgadrdttar aaqelqdmlt qagfthlrve
      181 tldldppvac vladnpsgmp a
//
LOCUS       WP_357614869             122 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357614869
VERSION     WP_357614869.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..122
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13819
     Region          11..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maepldpdmf agcppvvapi rvgdkwtaki irclesaprr ftelqavlrg itpkvltesl
       61 ramerdgllt rtayeeippr veyeltelgr sliepmnagc ewsrrhlael mharetwyea
      121 ar
//
LOCUS       WP_357614932             264 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Nonomuraea dietziae].
ACCESSION   WP_357614932
VERSION     WP_357614932.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  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..264
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..264
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28350
     Region          3..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 mqidtvteil reaahavilp ryralatgev mekspgevvt iadreaeeli trglrgvlda
       61 pvvgeeaaaa dprlidalte aptawlvdpl dgtanfvagn pdyavmvalv hhgrtvaswi
      121 lrpaddrayv aehgagawrd sirlsrepas qdpaelrgav ltrflppsak arvevtasrf
      181 aavepgtkca gvdyprlvdg eldfvvfhrl lpwdhapgvl llteaggvar hhdrtpyrpa
      241 dmrpglltaa daacwqtvrs vlsl
//
LOCUS       WP_357614978             273 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Nonomuraea dietziae].
ACCESSION   WP_357614978
VERSION     WP_357614978.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 273)
  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..273
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..273
                     /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=30148
     Region          28..273
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mfrrlglvis tflatltapa avaassvtvv nvahrgasgy apentiaafe ladeqdadmv
       61 eldvqqtrdh hlvlmhdttl arttdveklf phrapwrvgd ftlaeirrld agswsspeyr
      121 geavptlgea lqamsesglg llleikaprl ypgiesrvae elrrnvswps rlmvqsfdwg
      181 smrrfhrlmp qvqtgllgtp stgqlaglag faaqinpphh eltadyvrrv hdhgmkvftw
      241 tvddadimrr lisyqvdgii tnrpdvldev tda
//
LOCUS       WP_357615065             370 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357615065
VERSION     WP_357615065.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..370
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39390
     Region          123..365
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mrravawiaa vlavlaavgv ggagwyysgl vidpshggsy plevlafdgs tvtlkggsdt
       61 aapgtygltw rdgnatlgpv vsasgatvvr qvtrvrrgtl argvrayfdr wiwghedprs
      121 alglpyetvs irselgdfpa wrlpgtsktw viavhgrnan pseslrflpv fqalgvpvla
      181 isyrndegap asgdgkfhlg atewrevaaa iayargqgat gvvlygfsmg ggivpmaare
      241 lpgepikgli ldspvmdwna pidlgarqqg vplwlasvgk ftverrtgis lddldhvrha
      301 kefrqpvllf vddddasvpi epalrfarlr pdlvtlvrtr ggghvgswnv dqaryeqalr
      361 tfvtaaaass
//
LOCUS       WP_357615094             242 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357615094
VERSION     WP_357615094.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 242)
  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 242)
  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 242)
  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 242)
  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 242)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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   8  (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 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..242
                     /product="GbsR/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=26501
     Region          1..>58
                     /region_name="Tra8"
                     /note="Transposase and inactivated derivatives, IS30
                     family [Mobilome: prophages, transposons]; COG2826"
                     /db_xref="CDD:442074"
     Region          83..232
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mpgdrltded rrhiaaglae glgyteigrr lgrpsstimr evtrnggpdd yraqraqeat
       61 qqrarrrrqa kppappigds shgrdpravq ditqsfatll aqqgmprmaa rvlaclyvtd
      121 sgnltaadlv qrlrvspasi sqtvalleqq gllkrertpg grreryvvdd elwvrstlaa
      181 lqmnetlada sqraaevlga atpagarfgv aaeflllvna slgqvmeqwq qnqdernarh
      241 rs
//
LOCUS       WP_357615112             833 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Nonomuraea dietziae].
ACCESSION   WP_357615112
VERSION     WP_357615112.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..833
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..833
                     /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=88710
     Region          97..253
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          324..826
                     /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 matrtpksas kgpakrstss rstpakrtta qssarskakt tasarrppat hqdpiswvft
       61 migklivglw mlvangigga aralgnqare ldpvhrrdgv glavlagaiv laamtwrqsr
      121 gavsevvnav ahgvfgslaw aiplllglla wrflrhpdqn adtgrmvigw galltgvlgv
      181 ihvvndvpyp agdstdgmdk vsaaggmvgf ivsappasil pawvtiplll llsgfgvlvi
      241 tatpvhripe rlgelrhmlf eksgtpkqge qvrkrvrskk pdlpdgvkpy dtpviaekdk
      301 hspeivpglv ddepqeapep pkpvvaaape ptpaprkveq lvlspqagpy ilpdlqslsa
      361 gsapkqetka nktvvnalts vleqftidaq vigftrgptv tryeielgpa vkvekvtalt
      421 kniayavksa dvrilspipg ksaigveipn adkdlvalgd vlrsqvaqad hhpmivglgk
      481 dvegrtivan lakmphllia gatgagksvc vnglitsill ratpdevrmv lvdpkrvels
      541 vyegiphlit piitnpkkaa ealewvvgem drryddlaas gfrhvdefnk avragklvpp
      601 pgservyqpy pyllvivdel sdlmmvaprd vedsivritq laraagihlv iatqrpsvdv
      661 vtglikanvp srlafavssl tdsrvildqp gadkligqgd alflpmgask pirlqnafvs
      721 ekeiagivah ckqqmqaeyr ddvaavavkk eideeigddl dvliqaaeli vttqfgstsm
      781 lqrklrvgfa kagrlmdlle srgvvgpseg skarevllkp ddlpglladl rge
//
LOCUS       WP_357615138             355 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357615138
VERSION     WP_357615138.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..355
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..355
                     /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=40524
     Region          6..348
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mkverdkyvd wlralslcvv vvwhwaftil qwkptgpept splgftsglw iltwllqvlp
       61 lffyvgghvh llswerarar gvgigsfvwr riralalpal flsgawisig avvtftfrvd
      121 wmwrvvllvl splwflgvyl vliallpval wlhrrydvla liwlggaslv vdvvrfrygv
      181 ewvgwlnmii vwglahqagf fydrivilpr rydvallwtg lfalfglvys giypgsmvgv
      241 pgdkwsnmap ptfvivalll fqiglvevlr psmervlerp gwrrvngfin ryalplflfh
      301 ttgmaialgl swwlfgnlgt eippdlkwwl erpiaiigpl icttpviylf grkra
//
LOCUS       WP_357615188             224 aa            linear   BCT 28-DEC-2024
DEFINITION  urease accessory protein UreF [Nonomuraea dietziae].
ACCESSION   WP_357615188
VERSION     WP_357615188.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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..224
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..224
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22629
     Region          4..224
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mtraalllla dgrfpaggha hsggaeaavt agrvrdaagl eefcrgrlht salvaaglaa
       61 aaatgydpll ldqaadartp apalrrtarr lgrqlmraar atwpsaelda laaarpqgah
      121 qpivlgltar sagltpleaa yaaayesvsg pagatvrllr ldpfdavail arladdidhv
      181 aaqaaeaaqh vpadgldalp aasaplldit aeqhattpar lfas
//
LOCUS       WP_357615227             269 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357615227
VERSION     WP_357615227.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=29510
     Region          11..265
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 madvirvpna kialstasvy pertpdafel aarlgydgve imvgadpvsq didvierlse
       61 hyhvpvlaih apcllvtqrv wgrdpwaklv karkaaerlg aatvvvhppf rwqreyaref
      121 eaglarmrde tdvtfavenm fplkargndv vpyspdwnpi dydfpqvtld lshtavsgsd
      181 amematklgd rlshvhladg lgvtnkdehl vpgrgnqpca pllerlantg ysglvvlein
      241 trkaasrter iddlteglaf arlhlaats
//
LOCUS       WP_357615298             419 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357615298
VERSION     WP_357615298.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 419)
  AUTHORS   ter Beek,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 419)
  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 419)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..419
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42778
     Region          15..415
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mtttllrrdg lgagtpaptv gdhvrdylar vrggdlgslp avigltvlcl afatvrpvff
       61 saanfanlft qgaavtviam glifvlllge idlsagfasg vcatvlanvl svlgypwyva
      121 vlaaigtgvl igltigvlva kvgipsflvs lagflafqgi vlllmkegtn isiddrviia
      181 iennyvppai gwvlaavgva gygavqflrh rnratrglvt epvavvaarv aglalllgca
      241 vhvlnqersi ntaisstrgm pvvvpligal lvfwsfvlnr taygrhlyav ggnpeaarra
      301 ginvdrlkis afvicssmaa vggiiaaskd rsvdpntggs nvllyavgaa viggtslfgg
      361 kgrmihavlg gavvaviing mglldlssgl kytstglvll laagvdalsr rrsvatgtr
//
LOCUS       WP_357615354             399 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nonomuraea dietziae].
ACCESSION   WP_357615354
VERSION     WP_357615354.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..399
                     /product="phosphotransferase 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=42163
     Region          155..315
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mdrtvtawvt sgddylgvvg pfavdvawws evepvvthvr gvlgvevavl rllhvdgggg
       61 grdghvtyhv ealqrpapgl lqpvpvdgsa ltgqeelrsp waraeglrev lgwasdtlaa
      121 agrpvtgpir qrktwnlagl frlptdqgqv wlkttphfaa deaavigafs rldpglapgv
      181 vasgpnrlll ehlpgqdcwd apapiitsav trlvaaqaal arqvdglapr lrdlrgpvia
      241 drvldlldga agreltgeev aaarrlagrw pllegcglpd tvvhgdfhpg nwrsdggppv
      301 vldfadahlg npvldglrvr dflpaadgah aakawaeawr shvpgcepes alsiaeplah
      361 layavryqef ldgiepseri yhlgdpaaai raalrcaag
//
LOCUS       WP_357615358             468 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357615358
VERSION     WP_357615358.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=49425
     Region          2..466
                     /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 madefdvivi gagpagenvv dravrgglta aiveerlagg ecsywacvps kallrpvdlv
       61 gevgrapgls lgpvdvaavl arrdeaighf ddsgqvrwie svpaeyvrgr grldgpkrvr
      121 vttedggerv ltarqavvla tgstpaippt pglaeaepwt shdvtvtdsi perliviggg
      181 vvacemaqam hglgarqttv lvrgrgllpr mepfagella esfaeagiev rdqveavrve
      241 rperggkvtv hlpdgpplea dellvatgrr patrdvglst vglpdgqyve vddsmratai
      301 sdgwlyavgd vngrallthm gkyqaricgd viaarargde lpamrdladg ygapqvvftd
      361 pqicavgrte aaaradgfrv rvvdydmgkv tggylmgdgy rgqaravvde erkvllgvtf
      421 aapgasdllh satiavtaev pldrlwhavp sfptvsevwl rlleaygl
//
LOCUS       WP_357615363             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357615363
VERSION     WP_357615363.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 191)
  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..191
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..191
                     /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=19496
     Region          25..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mppdataaha grpmradarr nrdrilaaae taiaehgaea sleeiarhag vgsatlhrhf
       61 psrqslleav fsgrvealca kagelgaqld papalvawlr avgthaaanr glaasllgsd
      121 pamganchtm ivnaggelle rarrahavre gvaivdllkl vsaislateq epggaaeadr
      181 llalaingvl a
//
LOCUS       WP_357615376             228 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357615376
VERSION     WP_357615376.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..228
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23895
     Region          1..206
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 meavlfdfhg tlaqveepre wvlqaaaacg vtlermrata ladrlltagr aggplptrvp
       61 prlaelwadr dlypyahrga ytglaetvda giegfaealy erllvpegwv pypgveatlg
      121 alhkagvkva vvsnigfdir plfaawgldg lvdayalsye vgrckpdpgi flsacgmlgv
      181 dpertlmvgd tpadagavna gcavlvlpca dpgrenglga vldlalrd
//
LOCUS       WP_357615380             610 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357615380
VERSION     WP_357615380.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 610)
  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 610)
  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 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   5  (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
REFERENCE   6  (residues 1 to 610)
  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 610)
  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..610
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..610
                     /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=66409
     Region          86..603
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mavntrrpae rppapprrrr lvyrlrvlrh dptaalglil lvllaylvva plvavlsdaf
       61 rlqygdgvha gqqpgewtgy ylwrvfrsqi sgllfwepll ntlviavgtt lfalvlgggt
      121 awlvtrtnmp grrwlagalv vpymlpswtf slawlslfkn eraggqvgfl qaqgirtpdw
      181 laygalpiii tlglhyypfv lllvgnalrr idaqledsar ilgapqrtvi rriviplmlp
      241 alssavllvv grvlgtfgtp yvlglpadyr vlstglfqai rdrstgvasv lttvivvigv
      301 livladtrmm rehrrfvtvg grgamdrlgd lrrwrwpafa fgllafavsv vvpvltllls
      361 tvtrtpldls tftldywiae rlpgavgfph gvlrgpelwe aawnsvrivg laslicailg
      421 lligyvvvrg taprvaaflr qvsflpylip giafaaasls lfavargpmp alygttflli
      481 lvmavthlpy ssrsgiaamm qlgrepeeaa qiagaswwqr mrriifpiqk galvtgivlp
      541 fvsglkelsi vimltttgtq llttlsiglv dygytqlana vvlmialisf tmtyltqrlt
      601 ksslasglgg
//
LOCUS       WP_357615382             192 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357615382
VERSION     WP_357615382.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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..192
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..192
                     /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=20644
     Region          2..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marskefdpe valqkalelf wergyeatsm adlvehlgia rasiyatfgg khelylkale
       61 rylgqrdivg plaqpgpavp airafldsyv aecladearr gcmvvnsave fasrdaavaa
      121 kvaaswagle talaaalvra raqgeippgk dpyalarfll vllqglrvlg radpdprrlr
      181 daveqamvav qi
//
LOCUS       WP_357615510             340 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357615510
VERSION     WP_357615510.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 340)
  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 340)
  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..340
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..340
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36400
     Region          1..237
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 misivvptlg rpslgtllda lapqlaelpd geillvddrr daagelavpg alsayakvvt
       61 grgagpaaar nvgwraarrp wvvfldddvv papdwarrll adlavgdrvg gvqgvvavpl
      121 prdrrptdwe rstaglaege witadmayrr aaleavdgfd erfprayred aelahrvrra
      181 gwelvrgrrv vthpvrpedr wvslrvqrgn addallrrly gpdwraelgl ppgrrprhva
      241 vaaagalavt agalrtllpr dgaprrvlgv vaaagalgwa vgtaefaavr iapgprtrde
      301 vstmlltsal ippvavahwv rgwwrhrpsg adgdpagaqs
//
LOCUS       WP_357615403             235 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357615403
VERSION     WP_357615403.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 235)
  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..235
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..235
                     /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=24583
     Region          11..156
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msapghrgrr qaeaerndra llqaarevla adgahasvas iaaragvgig slyrryrtke
       61 elfqrlsals lehwneaaer gladddpwrg lkgfitacve fgqgslspva gtievteqma
      121 assargdell aalvarahea gvlradvtav disllieqlg tsplldqlrk qgrddlvgaa
      181 meararlvti avdglravht eplpggapsg glfterwara peppatgarg sgrag
//
LOCUS       WP_357615545             193 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357615545
VERSION     WP_357615545.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 193)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..193
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..193
                     /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=20780
     Region          3..191
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpppnpqrrd hladaaitvl aeqgsrglth ravdtaaavp agttsryfrt rdalldgvie
       61 ritrrlgerv daytvrpisp adleealvav lttmltggrh dplalfelhl estrnprlrh
      121 tltdalhgrs dlivrqcraa gidisqddam llemsvlgil ftalttgipg apgepirtav
      181 rallahhrtp tat
//
LOCUS       WP_357615552             481 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA synthetase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357615552
VERSION     WP_357615552.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 481)
  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 481)
  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 481)
  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..481
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..481
                     /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=51778
     Region          1..465
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(132,135..140,142..143)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(135,250..251,271..276,356,368,371,382,462)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(135,175..176,223,225..226,229,250..251,271..276,356,
                     368,371,379..382,443)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(175,225..226,229,250,379..381,437,443)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mtpervalty rgrdfsyrdl rertyrlasa ldvgrgerva flgvnqpalv etffaagllg
       61 avfvplntrl arpelrfilq daqpsllvlg eeqdgaglpg rhltaadyeg llasgspepi
      121 depvrqddvc limytsgttg rpkgamltha nltwntfnll vdvplahdev tlvsaplfhi
      181 aalaqtllpt vlkggrvile pafdvdrtfd lieaervtvm fgvpsmfgfl arsprwagad
      241 lsslrhllcg gapvpeplir lyqergltfl qgygmtetap galflgaehs vakagsagvp
      301 cffsdvrlva pggsaagpge pgevyvqgpn vtpgywrrpe etakalsadg wfrsgdvgva
      361 dedgyvrisd rlkdviisgg eniypaeves vlyehaavae cavigvpdek wgevgkalvv
      421 vrdgstveag elltyldgrl arfkipkylq fvaelpknaa gkllktplre lygsalhdhr
      481 s
//
LOCUS       WP_357615583            1218 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing serine/threonine protein kinase
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357615583
VERSION     WP_357615583.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11600203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1218
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..1218
                     /product="WD40 repeat domain-containing serine/threonine
                     protein kinase"
                     /calculated_mol_wt=128092
     Region          15..264
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,41,43,75,91..94,98,100,137,139,
                     141..142,144,153..154,157,174..177)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,41,43,75,91..94,98,139,141..142,
                     144,153..154)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,98,100,137,139,141,157,174..177)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(37..38,67,72,77..80,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(153..161,170..177)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          526..1054
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          653..686
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          690..723
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          728..761
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          764..799
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          775..1164
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          803..879
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          884..936
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          940..977
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          984..1032
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1037..1067
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1075..1110
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mtpllpgdpa qlgeywlagr lgaggqgvvy dayddagrrv aikvvhpdll ehrgaradfv
       61 kevtaarkva afctasiida eldgprpyiv sehiegpslr aaveqqgpfd agrlhrlavg
      121 vatalaaihd advvhrdlkp gnvllgpdgl rvidfglart gemsqttegg faagtppyma
      181 perlagrrgg aavdvwawga vmlyaatgrp pfsgdlallr yqvastrpdf tvlaeplrrl
      241 vteamsldaa drptarslli dliatradrp dpegresgla glaggegrfa glagaagglv
      301 ggegglagll stgsraarev rppaglvtps paelaedvyg slspedqalv ppallrmvls
      361 deraetalre attrqlidea gdpagvervl raftdagllv gegesitlaa aallrawprl
      421 qgwvesdreg ltvhhalnra attwhangrr pddlfrgtil drtvewatng rvllqpnrle
      481 qafldasqer trdlarrrrr vrgtiaalva vllaavgvvv vqnvlgtrqr dtsvarqvaa
      541 ladrtrardp ltalllsvaa wriapvtear aamhaslaqr arsafrpapv sgsarfdlsa
      601 dgtrlavvdg grftlwdvaa grpvrafdgv sgavnermnr pvrasdgvsg svnaialsad
      661 grrlavager svsvwdterg vriaelgeva revafsprrl llaaitpegr arvwdltsqr
      721 pldvgdarev afsaddalma allpggryel rdwqgvlarl pgeavafnpv rrelavrtgg
      781 gvrfwdldar rwrgptlkgv earelrfsqd grflaaydga tiglwtagan agpgpvggrp
      841 sslgaagepg pagvrllsyp vgelvrglrl gdgtlafgll dgtvatldia dltrprtlaa
      901 gvqsglidpa rrtvivtrpk aeawhlatle rlatlpvtpt amalspdgvl lavgtadpar
      961 vslwdlatgr rertipvkga tevgglafgp dgtalavapf qetvtppasn wrdvqlwdvr
     1021 rgvrtrtltv pggsgmvfrp dgrelavnga dgalasldsp aavarpfges adgvravays
     1081 pdgtviatga latgvtlwta adrrllarlp vkgfeavdll afapdgrtla lggshrvqlw
     1141 dvaeraplgp pvvypagevv alafdagdlr tlrtdgtlgd hpaafanvaa alcaragrpl
     1201 srsdwdrlip gapyrpic
//
LOCUS       WP_357615628             390 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357615628
VERSION     WP_357615628.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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 390)
  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..390
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..390
                     /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=42580
     Region          2..382
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkfllrptsk qaaalaacle dhrqlynaal ehrrtaygka gvsirygdqs gelkhiradd
       61 pegqgrwsfs sqqatlrrld kaftafftrv rqgrtpgfpr fkgrgwfdtv ewpkdgdgcr
      121 wdsqpehpsa tfvrlqgvgh vrvhqhrpvr grvktisvtr erncwyvvls cddvpaeplp
      181 atgaavgvdl gvahlvttsd gghldnprhl aatadrlaia qrelarkkrg skrrrkavmr
      241 vgalhakvrr qrldgahkaa lalvrgydvi vhedlkvanm trsasgtieq pgrnvaaksg
      301 lnrnildagw gvflrilahk aesagrelvs vnpagtsrtc arcghsaren rpsqavfrct
      361 acghsahadv naainilrag lalrdaaqaa
//
LOCUS       WP_357615666             493 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357615666
VERSION     WP_357615666.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..493
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=51467
     Region          11..493
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mptpaepypr avldllaaar drpvfehgar tvtgaqmlgl vrriaaglrg aaigpgdgla
       61 mvlgvnpeaf aaiiagyvvg arvvgvrpgm pggqlrhvlh qdiaavvtds agtperaprt
      121 ltvsellaap ddggpphlsg rphdvarlvy tsgstgtpka caqtyaamda awtarpaawp
      181 pairelasrl qrylvfgsls sqvmmeygvl tlaaggtmvv adppafpdai trhrasasvi
      241 tvprlyrlva aqrsapadls slralmvsgs pleaarlrea ldvlgpvvfq gygqsetgti
      301 smatpsdvpp svgfppdvvd vvildpdgrq vpagvdgely vrtpaqaigy waepaetaev
      361 fvdgwvrtrd lghfdeegrl ylvgrardvi ivnanlyyaa piervlatsp diaeayvvga
      421 pdedtgeavh afvvpvagra pdlgalralv gerlgdacvp atitvideap ltpngkpdkr
      481 lltaaiprah gre
//
LOCUS       WP_357615688             364 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase, partial [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357615688
VERSION     WP_357615688.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 364)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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]"
     Region          129..364
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgwvgrlfda rdtfarmlll dlsgvgylvf gahagrsptt tqwvlalvaf avglvchrrp
       61 lvnlvaqaal lavaiplvdd ttinqvgasw allelamrad rpriiwlaag llaavdltds
      121 igdpfrrfls gvfgltvevg vplllglvir ttrelgrqae eraaaeqrrr esesraarad
      181 ersaiarelh dvvahhvasm vlrvgvarhv lteldprvge vfddvhgtgt aaladlrrlv
      241 avlrnpdgvr gdaaltaiep aalpaalgaa vdrarqagvt veadidpavg sldavrglav
      301 lrltqealtn vakhvgtsar arlavsvvdg avhwevrddg rgrvpaavpp ggghgitgmr
      361 erve
//
LOCUS       WP_357615735             306 aa            linear   BCT 28-DEC-2024
DEFINITION  proteasome assembly chaperone family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357615735
VERSION     WP_357615735.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..306
                     /product="proteasome assembly chaperone family protein"
                     /calculated_mol_wt=33424
     Region          15..262
                     /region_name="COG1938"
                     /note="Predicted ATP-dependent carboligase, ATP-grasp
                     superfamily [General function prediction only]"
                     /db_xref="CDD:441541"
ORIGIN      
        1 mldphelyql tddlpdlgqp vmiqaltgfv dagsasrlar eqlltslesr qiatfdvdql
       61 fdyrsrrpvm tfvedhwehy dapelalhll hdddetpfll ltgpepdlqw erfvaavaal
      121 atrlgvrlta glnsipmavp htrptgvtah atrreliagy epwlqrvqvp gsvghlleyr
      181 lgeagrdaig faahvphyva qteypaaaev llssvsrstg lllpsdslrt aaevvrveid
      241 rqvaqtdeaa alvqaleeqy dafargrgek nllaaeagpl ptadelgael erflaeqtrp
      301 gdtpng
//
LOCUS       WP_357615762             696 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357615762
VERSION     WP_357615762.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 696)
  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..696
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..696
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=75787
     Region          2..695
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mpvqdtirnv paagrqqtda pafigrrhei sqvrrilakt rlltltgagg vgktrlarrv
       61 seilphryrd gvrlveltai ededllvpav aaalgirdtt pdlvgllaeh ladkhlllvl
      121 dncehllgac arlaqrllrd tsrlqilats rqslgvyger vlpvpslsip qpgdstrdia
      181 rrdavrlfae raatirpgfl vdaanarava rltrrldgip laielaavrl rttsveglvn
      241 eldqhlevpa evapgtvarh qtlratmdwt fglcspgerl lwerlamfpg gvdletaeav
      301 cpgqglardd vldlmgglvd ksilssaeqy gtavryrmle tiraygrerl paadekalre
      361 ryiahyrrla erlrvdrvap gqidnvralk lelpnvrval dlcfhlpgda pagleiasal
      421 wanwlvagap segrywlgrg lglvpgssva rtmglwakgl lghyqgdpaa aadarecsel
      481 awrlkdetal afavqlsgva alcggdaegg lallndartr hwargdvhav gvtlylaalf
      541 aasmspdraa aygeelvalc edrhaplfra yalyavgmar weqgdwrqte akmrevtafw
      601 saaddrwglp qclevlawta gargrheraa rlqgaahllw eavassplrl qyqarshqec
      661 aerarhalga raytaafrdg trlglarava yaleep
//
LOCUS       WP_357615808             189 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357615808
VERSION     WP_357615808.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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 189)
  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 189)
  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 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..189
                     /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=20019
     Region          28..170
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mseidaihlt dftitkesit vsqiwttrae terdipaire vnlgafptpl eadlvealra
       61 daawlpglsi vaedadgtva gyalltrchv drspalalgp cavlpghqkr gagsaailag
      121 lraardlgen lvlvlghpey yprfgfvpas rygirpsfev pdeammalvf ddslpvpagt
      181 ivypapfgv
//
LOCUS       WP_357615861             306 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357615861
VERSION     WP_357615861.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 306)
  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..306
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..306
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33598
     Region          20..306
                     /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 maevpsdael assldggfvs rhaevngtrl hyvaggrgep llllggwpqt wwefrkimpa
       61 laerhrviav dlrgmggsgk prdgydkktm asdvlelvrh lghdrvdiag hdiggmvaya
      121 faanhpahtr rialldiahp derfyahsll prpgrqqvdg dihaapgrfl wwfafnqvpg
      181 lperllagrs relidwmcdy liedpsaisd rdrdiyahay gtpdairasn awyrafgqdi
      241 adektygkvt apllglggga dghlllktil pdkgtdvevv evpgsghyip eeqpelviay
      301 larffg
//
LOCUS       WP_357615875             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357615875
VERSION     WP_357615875.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32076
     Region          47..292
                     /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 mwpcsvlvav laapgglvqe pvrrygrahh tpgrrstcld lerapvlyvr etgdaagpvl
       61 llihgggvag wmwerqidhf apgcrvlvpd lpghghshdv afttsaavva elaaylgrfp
      121 agaditvagf slgaqlalel aashpemvtr vvitsaltqg iplpglshwl vrltaplarq
      181 twfaklqaks lyipddlldd yirtsttlpr eslialtran aefrtppawr rfpgavllla
      241 gakepralre gmrqlghdhs kseliiheha ghglplqype wfnariegwm radra
//
LOCUS       WP_357615877             318 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357615877
VERSION     WP_357615877.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..318
                     /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=34947
     Region          25..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mvittvpgtt tgagrpaspy pagpqrtslg rkvrdnltgh tfligavlcf avfswypmir
       61 givmsfqrtr rgettwvgwd nylriiddps fwtawrntly ftvlalvlgy avpffvaill
      121 nefrhakgyl rilvylpvml ppasalflfk fyaydpseag lfnailtalh lptsqwmqsp
      181 emtmpamvla stwmnmggav liylaalqni pgelyeaael dgagiwrriv hvtipqtrli
      241 lallamlqiv atmqlfiepl ilangagaed satsvayliy qhgffqndln gaaalgviml
      301 vvlagfsaay lrlsakqd
//
LOCUS       WP_357615881             410 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357615881
VERSION     WP_357615881.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=42077
     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 mrvvvigsgi vgasaayyls rrgaavtvvd ggytgeatha gagivcpwvd hpedddwyrl
       61 tregarhypg lveelgedig yatvgallva edpvdlepvr allrrrypga pemgevtdva
      121 tpselfppls dtlsallvpg aarvdgcsvr dallraavah gaevrtgaaa ltpagevvlh
      181 aiarepvaas apaapvppep apgevagqgg swrqgaplap aepqgpvstr aprfadegvr
      241 leadsvivaa gawtgqvcrp lgvelpvfpr rgqilhvtme gvdtawwpmv lprvgpyllg
      301 fpdsrvvvga tvedvgfapr vtmggldevi saglrvapgl faatvaearv glrpvyapgr
      361 aligrltgrv vvatglsayg ltagpftgei aaslalgeep piditpyapa
//
LOCUS       WP_357615901              62 aa            linear   BCT 28-DEC-2024
DEFINITION  HIT family protein [Nonomuraea dietziae].
ACCESSION   WP_357615901
VERSION     WP_357615901.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 62)
  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 62)
  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 62)
  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 62)
  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..62
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..62
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=7082
     Region          4..>51
                     /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 mplmscvfcr ivagtepsqt ihedehaiaf lnlaqatkgh tlivprahhr dqrrsqwrrr
       61 ht
//
LOCUS       WP_357615972             105 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357615972
VERSION     WP_357615972.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Smith,T.F., Gaitatzes,C., Saxena,K. and Neer,E.J.
  TITLE     The WD repeat: a common architecture for diverse functions
  JOURNAL   Trends Biochem Sci 24 (5), 181-185 (1999)
   PUBMED   10322433
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Neer,E.J., Schmidt,C.J., Nambudripad,R. and Smith,T.F.
  TITLE     The ancient regulatory-protein family of WD-repeat proteins
  JOURNAL   Nature 371 (6495), 297-300 (1994)
   PUBMED   8090199
  REMARK    Erratum:[Nature 1994 Oct 27;371(6500):812]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..105
                     /product="WD40 repeat domain-containing protein"
                     /calculated_mol_wt=11297
     Region          <14..>96
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          14..45
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mrcrsitlat drlldvspdg sllasggcdv rvwsaatges lyvlhghtef vkacrwspdg
       61 srlasigddq tvriwaaasg eveqrsgstr hprtaagcrt rerwp
//
LOCUS       WP_357616101             199 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357616101
VERSION     WP_357616101.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 199)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..199
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..199
                     /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=22601
     Region          2..199
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpkvvdpear reqvaeavfr vvrrdgleqa slrnvaeeag laigsvrhyf aghselmvfa
       61 mqamnervvr rllehvekle ttddrlplve smlaellpld errreeatiw lafataartr
      121 pelrphaees ydglrrlvfk vldgarrsar lregtdlave verlcalidg ltvhavlhpd
      181 rmdaetmtrv lrhhlqslt
//
LOCUS       WP_357616135             416 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea dietziae].
ACCESSION   WP_357616135
VERSION     WP_357616135.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..416
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45760
     Region          1..416
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 migrtgdveh llrteapqvl galvrrfghf dvaedavqea llaasrtwaa dgvpdnprsw
       61 lirigyrrmv dllrseqarr rreqeagmte lamheparqa dppqetddsl allllcchpa
      121 lsatsqvalt lravggltta eiahaygmte ptmgtrisra kqqlaragar ftpptgadrg
      181 drvtavmqvl ylifnegyta sagdqlarvd ltseairltr mlrdslpddp evagllalml
      241 ltdsrraart ggddelvpld eqdraqwdpd viregtelid svwsrrevgp yqlqaaiaav
      301 hataatpeqt dwpqiaalyl wlerlsptap vrlsrvvava qaygpargla llddlnrryr
      361 ldqepltrqr eravrahllh mtgdaagaar lyreaaaltg nqveqrylld radhlg
//
LOCUS       WP_357616045             447 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357616045
VERSION     WP_357616045.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=47338
     Region          35..329
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mtpptvpplr rrsmvsaala laltaslaac ssgdtsspgt asaggpvtlq vwtwnlksgd
       61 peaeaiikky hqenpnvtik lsevggtadt askllaadqa gdapdvvqle yrgvpavvva
      121 gavkditadv agvksgiesn iwalttfnnq vygvpqdigp mtftyrkdlf dkygvkvptt
      181 waeyakaaeq ihkkdpdayi asfsasqlef faaqaaqaga qwwsndgkaw kvgidseasl
      241 ktadfwedlv krdlvkvepl ltpewnaqvn dgkilswaaa awapsvlysv apdtagkwes
      301 aplpqwtpgd pavpflggsa ylvpakskha keaaafaawl gasdegsklq ltldiypggn
      361 agrqatltaa ppklmpqqkd fyqvtdqvik nttipvtwgp nvnvaqtafg dalnkaaldk
      421 asfravyqat qqavvadlqk sgytvtk
//
LOCUS       WP_357616279             215 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357616279
VERSION     WP_357616279.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 215)
  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..215
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..215
                     /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=24003
     Region          23..177
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 malsdshsll erayfdaver vddsdelrtr ildaayeqfc rmgirrstme dvarlakvsr
       61 itvyrrfdtk dtliehvvrr efrryfdqfl idieqadtaa drvvlgfvss lrairgnpli
      121 ggliatepdl lvpsmtadgg qtlatvrhfv agqlrseqra gnvsssldvd lvaemmvris
      181 tsfltipsal inldddeqla avarrfllpm leppa
//
LOCUS       WP_357616313             250 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357616313
VERSION     WP_357616313.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 250)
  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..250
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..250
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27134
     Region          2..250
                     /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 mtivfvhgvp vtsavwtpli selpksqqqd vvrlsppgfg aalpadfgat fldyrdwlid
       61 elsqlrtpvd lvghdfgggy vlevamarpd lvrswisdti ggyepdftwh eiaktwqtpg
      121 dgerhieetf sgdaaertar miswgipepa agqvalgqgp emgrailsly rsvpenmlae
      181 rgrnlpaaaa rpglvpvatd dltagsvalr hraaqragar avdldalghw wmlqdparta
      241 rmlsdfwnsl
//
LOCUS       WP_357616343             433 aa            linear   BCT 28-DEC-2024
DEFINITION  M28 family metallopeptidase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357616343
VERSION     WP_357616343.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 433)
  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 433)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 433)
  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 433)
  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 11454910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..433
                     /product="M28 family metallopeptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008235 - metalloexopeptidase 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=46949
     Region          191..425
                     /region_name="Iap"
                     /note="Zn-dependent amino- or carboxypeptidase, M28 family
                     [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]; COG2234"
                     /db_xref="CDD:441835"
ORIGIN      
        1 mipsaaemva wieaitergi rrpgypaddw aaawaaarle efglegvrla pvelpywkpv
       61 ratlaveggp efeafalpyt kakaqvrapl srevapgail vaetaftelp qsyvrdlata
      121 whdpegvfds ltqvlpfqld yldvlhgamr dgaagfaggl tgvpwetrdy yapydaeprd
      181 ipavwlsgrd arqvlalmde gprtgvltve aetgpavshn vigtlpgasd qwvivgshhd
      241 apwasaveda tgvalvlaaa rhwasvpare rphnlifllt aghmalaagt rafieehral
      301 lpdvvlqlhl ehaalrcvgv dgelvptgdp eprwwftsrr prlerlvhea lvaedlrrsf
      361 vlppdvfspm pptdgayfhp egvplvhfls apmylfdsad tldkvdvagl eplaraavri
      421 vegtagwtar eps
//
LOCUS       WP_357616384             122 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF488 domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357616384
VERSION     WP_357616384.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007029
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..122
                     /product="DUF488 domain-containing protein"
                     /calculated_mol_wt=13681
     Region          8..122
                     /region_name="YeaO"
                     /note="Uncharacterized conserved protein YeaO, DUF488
                     family [Function unknown]; COG3189"
                     /db_xref="CDD:442422"
ORIGIN      
        1 magkskgkvq vrrvyeepag ddgarvlvdr iwprgltkak anldewckqv apsrelrtwy
       61 rhdpelfaef grryrielad peraaamthl relaqggvlt lltatkqpei seaavlaell
      121 qq
//
LOCUS       WP_357616433             588 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Nonomuraea dietziae].
ACCESSION   WP_357616433
VERSION     WP_357616433.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=63841
     Region          3..585
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mssipsllrd rikatpdaea yrhpagsgwa sltwaevger vrplalglag lgasaesrvs
       61 ilcstrlewv ltdlavlatg aatttiypsn taaecafvin dsgstlvvae nddqvaklvs
      121 vrdempdlrh vlvvdgtasd dgwvipldqv sgegdfdamv daikeedlat liytsgttgr
      181 pkgvelthdn wlyaaeavrr idligpddlh ylwlplshsf gkllqvvmid igvptaidgr
      241 ldkiaenlge lrptfmaaap rifekihntv aatvrregga klrifewakq tgirvskarq
      301 rgaaiplttr leyaladrlv fgklrarfgg riryfisgsa plsqdiaeff dgagltileg
      361 ygltessags flnrpdsvrf gtvgpplpgt evriaedgev liggrgvmrg yhglpeetaa
      421 tlddgwlrtg digeldeagr llitdrkkel iktsggkyva ptyiegrika acpylshvfv
      481 hgdrrnfcta lvtldmevvk pwaaaeglpd eaeklrdhpr mreevakavk qvnqtlasye
      541 tvkefailgt dfsvetgelt pslkvkrkvv eqhfgdtlda fykdanli
//
LOCUS       WP_357616436             467 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional phosphatase PAP2/diacylglycerol kinase family protein
            [Nonomuraea dietziae].
ACCESSION   WP_357616436
VERSION     WP_357616436.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 467)
  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   2  (residues 1 to 467)
  AUTHORS   Kanoh,H., Yamada,K. and Sakane,F.
  TITLE     Diacylglycerol kinase: a key modulator of signal transduction?
  JOURNAL   Trends Biochem Sci 15 (2), 47-50 (1990)
   PUBMED   2159661
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..467
                     /product="bifunctional phosphatase PAP2/diacylglycerol
                     kinase family protein"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /calculated_mol_wt=49329
     Region          <40..175
                     /region_name="PgpB"
                     /note="Membrane-associated phospholipid phosphatase [Lipid
                     transport and metabolism]; COG0671"
                     /db_xref="CDD:440435"
     Region          181..466
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrlrsrlnrl dkhlyasvaq arlpgfervl pplsraadna llwagiaggf alsgrrrlrr
       61 aatrgllavs lasplvnlag kqafarkrpv adslpmtrll rmplsasfps ghsasaaafa
      121 tavaleapav vaapvallag avcfsrvytg vhypgdvlag vaigvatgll trriwpeage
      181 agrarasata psfdldplgd glavvvsqee seaartlrea fpraqfvple smdkaegkal
      241 avaggdgtvn sgalaalehg rpllvvpagt lnhfatelgi edadeavaay rggdlvavdv
      301 gevaggvfvn nasvgiypel vdrrearqkr vgkwpallwa laevlgrdaa pfdvvvdgvp
      361 yrawllfvgn crygsrgaap grrarledgv ldirlmtaar tlprvrafgs vvagrlglsr
      421 hyrqwqadtv rvetpsgeir lardgetlta hgplvftkrp rslhvfr
//
LOCUS       WP_357616450             246 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357616450
VERSION     WP_357616450.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 246)
  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 246)
  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 246)
  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 246)
  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 246)
  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..246
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..246
                     /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=25203
     Region          3..>71
                     /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 mtkvvvvgat gnqggagadr llerghevva yvrsqespav kalrargarl atgdlsdpda
       61 lrhactgada vsacrcrsar aartrmsrrd aclstppras tstwgtsglg avtgwwppps
      121 ttptdrpwct qrslartgas sygpsssgvl rtesvdasrd rvgggrdalg dgttapdghf
      181 ggpicldliv elgachalrv grrqvadgea vqsvtdrgal ralrksaagg vqgagdsgrl
      241 icsrpf
//
LOCUS       WP_357616477             415 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora purpureochromogenes].
ACCESSION   WP_357616477
VERSION     WP_357616477.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..415
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..415
                     /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=44404
     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 mtkaliiggg iagpvaalal rragidsaih eayerdavgv gsfltlsvng mdalraigld
       61 elvaglghpt prmamfnhqg rrlgefgtsg trtrgrgstt vrrsdlyral rdeaarqgvp
      121 ivhgarlvsa estgagvrar fadgrsaegd lligadglrs rtreiidpaa papryvplln
      181 asgftrglgl pgepgvmnmv fgrrcffcwi pvgddeiwwf anppqpaelt pdqlaaigpe
      241 esrarlralf addagpalri veatdriryg wptydlpslp vwhrdrmivi gdaahtaaps
      301 sgqgaamafe davtlarclr dlpdvpaaft ayerlrrerv ervvaqgrrn sgtkaagpva
      361 rlvrdialpl yarrmaktgg aslawlydhh vewdapvaag vtaprapgrt rpapr
//
LOCUS       WP_357616496              86 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357616496
VERSION     WP_357616496.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 86)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..86
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9700
     Region          8..62
                     /region_name="HTH_33"
                     /note="Winged helix-turn helix; pfam13592"
                     /db_xref="CDD:433335"
ORIGIN      
        1 mdrgpaltla wvtalieqlf rvsytlrgts yllhrlgwsp qvpqrrtaer dedvvatwik
       61 etwpsverlp gtrthgsasr tkpatr
//
LOCUS       WP_357616485             390 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357616485
VERSION     WP_357616485.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 390)
  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..390
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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]"
                     /calculated_mol_wt=41151
     Region          <192..386
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msdlrflapv rrwssalppl wveaalaglv lvvqlwpllt rdnptggpwh wwgyvvvvaa
       61 tvplvwrrra paavllatlv atgsydlvde vaaqpiwyga giaiytvaay strwtrrimi
      121 vvtvgggllv vgssetamrg vvlcvaayai graaavsrah aaaleeraaq larerqaeae
      181 raaererari ardmhdilah avslmvvqae agpvvvrndp araeaafdai aaagrdamdq
      241 lrrllnvlkk eegsrapqpt iaavadlaeq vraagldvay stsgepgplp pdaevaayri
      301 tqealtnivk hagatradir lawqddtlmi ditdngdgsa sslpsggngl igireraaac
      361 ggtadigrrt dgpgfrvlvr lpvtgravaa
//
LOCUS       WP_357616508             293 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357616508
VERSION     WP_357616508.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..293
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31867
     Region          5..292
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mtrpekvtfd gdeatltgnl flppeqapgv vvagtwttvk eqmadryaqr laergytals
       61 fdftgfgesg geprdvespa rkvrdihhal tflaahpavd gerlgalgic aaamymadna
      121 ahdprvkala lvapwlhdaa iceaayggae avatkikigr earsrydetg evdyvpvvst
      181 ideraampye idfylnpqrg aiptrpnrfa vmawpewlty dsialaprit qpplivhsde
      241 aaipdgahrf haglpgskdi lwiqgiqfdf ydqepqvaia idaavghfgr tlr
//
LOCUS       WP_357616578             423 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357616578
VERSION     WP_357616578.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=44941
     Region          35..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(141,143,269,271,304..306,349)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrslkttall aaaamalaac ggggsggdas gdkvklrfsy wgsdsrqklt eqviaafekk
       61 nptidvvgef sdwpsyyesl atkvaandap dvmtieirgl aeyagrgala dltgkvntad
      121 ldpqvlasgs vdgkqyaipt gvnvfsmlan katiekagqk lpddktwtwd efvslsqkit
      181 eggdgsvyga eynfnpaylt ifaaqrgekf ydngkigitp dtlkawwatf tklietkgsp
      241 daakmgeiaa agqeqsliat nkgafgmwws nqlgamskss gqeltllrlp klpdatnagm
      301 flqpamhwta ssksehqaea hkfidflind peagglllsd rglpinskvl eaiksklppa
      361 dqqtltflds vkselspviv ppkggskmed ilkryseavt sgqqspdeaa tklleeanaa
      421 lag
//
LOCUS       WP_357616603             297 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357616603
VERSION     WP_357616603.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 297)
  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 297)
  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..297
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..297
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32511
     Region          1..231
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 misivivskd epaldstldg vtraaesagl pyeiivvdas egrldaiaaa hphvrwtafs
       61 pppgvlvtip hqrnagvraa egeivvftda gclpqgdwlr rlvtpildeg esvasglvtg
      121 pdghdslyda darrraaary lpecgtgnla vrravfdeva gfdetfgygs dvdfswrvqd
      181 aghrirsage avvthewgdr rrqlrrsyvy gkararlylk hrsrraqllr repmvlaypl
      241 fllglpltlw fplypalllv pawrnrhngp vrvladhlvy gagvlaelat srgragr
//
LOCUS       WP_357616678             304 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357616678
VERSION     WP_357616678.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  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 304)
  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 304)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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   8  (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 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..304
                     /product="GbsR/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=32663
     Region          1..>54
                     /region_name="Tra8"
                     /note="Transposase and inactivated derivatives, IS30
                     family [Mobilome: prophages, transposons]; COG2826"
                     /db_xref="CDD:442074"
     Region          78..214
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mpggrlthed rlriatwlae slgyaeiarr lgrptstisr evarnggpga yladraqqaa
       61 grrarrrgpv qvaeppadev vrgfvdrfat llsatglprm parvfvcllt sdagsltaae
      121 lgrrlqvspa svskavgyle gmelvgrgpd pggrreryfi dddvwlrawq adtgahadla
      181 eaarhgieif gaatpagtrl gqmaqffari sdlmggsrlt davvgdaltm iaallhaarp
      241 ltpdqlatal dwpreravda ldvieqrpvi adpfalhrtg hgtyavttrp drlspaqrea
      301 lrar
//
LOCUS       WP_357616689             377 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357616689
VERSION     WP_357616689.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=38846
     Region          112..356
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mwvaasvpal vpvaavatvl srrrlrsrlp alvwpaaavs lavtlacvfg aiepapeagv
       61 lwmveslalm altglavrya pprqaaaaap aaglaasvwl lrsftpaspl egvgvcafwg
      121 lgallaaavg gylrhaevre travadarta lrlrlardlh dfvahdisem vahaqagtvt
      181 gdplsalerv eaagqralsm ldrtldmlhh drplspagdl sgireaaerf saagaarvsl
      241 rldpvvavpp elgalayriv vegltnvrrh apqatrvdla vtagpgtlei tmandgvtga
      301 rggrpsrrps rrpgrrhsgt glaglaalvq eqggdlvaeg vrdgwslaar lplaqspgwp
      361 sassspttrk asappsg
//
LOCUS       WP_357616750             393 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357616750
VERSION     WP_357616750.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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..393
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..393
                     /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=42658
     Region          1..391
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mrrsftfllr ptsrqaatla acledhrqly naalehrraa yakagvtvry gdqsaelkei
       61 rkadpdgqgr wsagsqqqtl rrldkafaaf frrikagekp gyprfkgrgw fdtvewpatk
      121 ngarwdsqph eparrvyllg ighvrvhqhr aikgrvkais vkregsrwyv vlscqdvpaq
      181 plpatgalag idvgvaslat tseghhignq rhlagcagrl aaaqrelark krgstrrrka
      241 varvaalhak vrrqrldgah kaalalvrgy dvivhedlri anmtrsasgt inapgrnvaq
      301 kaglnrsild agwgvfltil ahkaesagre liavhpants rtcarcghca kenrltqaef
      361 actacghtah advnaainil raglalreaa gaa
//
LOCUS       WP_357616757             345 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357616757
VERSION     WP_357616757.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=39639
     Region          6..215
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 msdrpvfvig cprsgttmlq lmlhshprma vppetrflip ayyrrrtwgd lrvvsrrral
       61 aqwiatdrst kfrelkidkd efirqvvegp gslgsvfgta frmyadrfdk vrwgdkrpsy
      121 vkqvdlllrl fpdaqfvhli rdgrdcvasl kempwytlds fhaistwaea idaggrlrrt
      181 lsddtyyelr yedltddpat elkklchfld edyspamvsp reaaivavpq hkvwhsnthg
      241 evtrsrvgsw anrlddweia laehmlgdrl esmgyeltga prpakehvta cqktmqkrka
      301 srlrkhmrdr lnrlrepspv aamltsgqrs vagvpqqrte ltetv
//
LOCUS       WP_357616756             293 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357616756
VERSION     WP_357616756.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 293)
  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..293
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..293
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31512
     Region          10..285
                     /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 mfpgfaleqi dvgpvrlrvr hggsgppvvl lhghprthat whrvapllad rftvicpdlr
       61 gyggsskppa gpdhagyakr amaadvvgll dalghdraav vghdrgcyva mrtaldhpgr
      121 vsrlgvldgv pigealarcd arfaarwwhw fflaqsdrpa ervinvdpda wyggspaemg
      181 aeayadyhra ihdpatvham cedyraglgp draadeadra agrrigcpvl fcfsnrddma
      241 elygdpaaiw rewapdlrva svdsghhmae eapeqlaavl gaflateavs rpg
//
LOCUS       WP_357616773             374 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357616773
VERSION     WP_357616773.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 374)
  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..374
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..374
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40317
     Region          1..373
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mlpygrqsia esdveavaev lrgdwlttgp avgrfeaela rwaggvpcvs vtsgtaalhv
       61 ayvaagvrag devvtspltf vataataall garvlfadvq pdtgnldpda vaalagertr
      121 avtavdyagh padydelrti adsagavlva daahsigaay kdravgalad lttfsffptk
      181 tvttaeggav aaadptller aarfrnhglv repadqrepd eggwhqevhe fglnyrlpdv
      241 lcalglsqlr rlaafrerrw elvarynall rdvpgltlpa erayvrpswh lypvrvrdgr
      301 rrevyermra agigvqvnyl paywhpvfad lgyrrglcpr aeayyaeqls lplfpdltda
      361 qqdrvvetla gila
//
LOCUS       WP_357616783             255 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357616783
VERSION     WP_357616783.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25371
     Region          14..255
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 masappseap sesrvvlvtg stagigrava atlaaaghdv vlhgrdqera akaaaevaae
       61 sggvtdsvac dvadfgavsa vmrqiyqrhg rldalvvnag vhaggplgmt rhdtvdrlfq
      121 vnavgatytl qsslrllrrg tapavvlvss mmgrmggagq avysatkaal igltlaaake
      181 lgptgirvna vapgyiktdm latldedara atvaatplgr lgtpadvagv vafllspvaa
      241 fitgqvigvd gglvl
//
LOCUS       WP_357616802             275 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357616802
VERSION     WP_357616802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=28364
     Region          4..275
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mlltwlyvpg drpdrfakav tsgadavild ledavvagrk ayarqavaef lgdphpvpvf
       61 vrvneltgpd vdtdlaavag rpglaglrlp kvesaqsvia lagrvdtplh pliesalgle
      121 aayaiaaahp avasiglgea dlrsdlgvdd eaglawargr vvvaaraaal pppamsvypn
      181 vadadadgla ascalgrrlg flgraaihpr qlpviaeafr pserevaraa ellaavaeaq
      241 trdsgtvvlp dgrfadramv aaarrtvdla dryaa
//
LOCUS       WP_357616809             325 aa            linear   BCT 28-DEC-2024
DEFINITION  PLP-dependent cysteine synthase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357616809
VERSION     WP_357616809.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..325
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..325
                     /product="PLP-dependent cysteine synthase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34562
     Region          9..298
                     /region_name="CysK"
                     /note="Cysteine synthase [Amino acid transport and
                     metabolism]; COG0031"
                     /db_xref="CDD:439802"
ORIGIN      
        1 mswnvraldv laageptpli dfpvrapgir lllkdesaqp tgslrhrhar alfrraildg
       61 lvtegttvve atggsaavaq awfarrlglp yivvmpgars eararaveal ggecrfvtpp
      121 laiydaargi pghfldqfgr aaehdlgeel fgqvrpdwvv tgagtgatsa tlgrwirdhd
      181 lpcrvavadp dnsayflgwt ldvpdyatgm psriegigrp riepgfrpdl vdlvvpvpda
      241 asvaaarhir evtglpvggs sgtalwaale lvermrarge sgtvvsvlgd aadrhlatyh
      301 ddawaagkgl dsgrhrdelr srtgv
//
LOCUS       WP_357616822             257 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357616822
VERSION     WP_357616822.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  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..257
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..257
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25344
     Region          40..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 mdplslttll aaaamagwvd avvgggglll lpallvaapg vpvatalgtn klaaifgtst
       61 aavtyarrtk mdwmvagpsa glavccagvg aalagavpag ayrpvvlavl vsvalfvvfr
      121 prlgvvavpa rrtrvrvvaa vavagvgial ydgligpgtg tflvvaftal vgadfvhgsa
      181 makvvnagtn lgalvvfaat ghvwwllgaa mavcniagaa vgarmalrrg agfvrvvllv
      241 vvlalvaklg ydqwrag
//
LOCUS       WP_357616867             567 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora purpureochromogenes].
ACCESSION   WP_357616867
VERSION     WP_357616867.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 567)
  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 567)
  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 567)
  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 567)
  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..567
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..567
                     /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=60516
     Region          2..545
                     /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 mtqaqlelll qrlterlaga lraepfdprv ghqvgaelva ahiasaeglg rtveviqlrl
       61 irdlglvadd vedrmarlla tvatgyaral rdrtldeqes irraamvara qaeralrdse
      121 srfrhqathd pltglpnrvl fterltaaig apgrgadrvg vcfldldrfk vvndslghqv
      181 gdallvsvar rlraalgehl larlggdefv ilvertarvd davaaaeaal aalaepalvd
      241 gheltitasi giverpvagt tpgelmraad stlhwakaag garwsvfdpd rhradlarya
      301 laaaipaaid rgeffldyqp ltslrdgtml gvealvrwrh pelgvlrpgs figlaeetgl
      361 ivrlggwvla eacreaeswg vrapfvsvnl avrqvhrpgl vqevrsllaa tglpperlql
      421 eitestmmst aeepvralrv ladlgvriai ddfgtgycnl aylrdlpvte lkvagefvtg
      481 lrapavdpas rtderilasl vslahaldlt vtaegvetag qaerlraigc dagqgwyfgr
      541 pgpaegclgr spalstvagv epvasag
//
LOCUS       WP_357616918             260 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora purpureochromogenes].
ACCESSION   WP_357616918
VERSION     WP_357616918.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..260
                     /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=27492
     Region          2..201
                     /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 mkvlvtgagg tlgravlprl radgfdvram srrprhdpaa ewvvadvetg vglaeavdgv
       61 davlhlaslp nsrrthrvdv lgtrdlavaa gaagvahlvy vsivgvdrvp yayyrhklaa
      121 ervvaagpvp wtvlratqfp pfldallrta srlgpvigdp avlaqpvdqh evagrlserl
      181 tagplggiee yggpqvlrfd eaarawraar gsrrpllpvr ipgrlgsalr aggltttatp
      241 tgrrtwadhl adtyggtdrr
//
LOCUS       WP_357617004             281 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357617004
VERSION     WP_357617004.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   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 281)
  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..281
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..281
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30160
     Region          2..279
                     /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 mqrfrssdgt elayrrvgsg pplvcvpggp gqaveylael gglsatrtli lldnrgtgas
       61 evpadpasyr vdrlvddvea lrrhlaldrm dllghsasgg icllyadrhp qrldhlvlva
      121 pslrvvdiqs dlavadvlak rahepwyaea vaalhadast eeehqryrwl aapllygrwd
      181 aaaraqasae paqfsapatd gfyagftpdp alparlsalp aptllvaaey diwptatavr
      241 elarlfarae vlvqpraghf pwvddpaafa savegflsae r
//
LOCUS       WP_357616979             311 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357616979
VERSION     WP_357616979.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 311)
  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 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   3  (residues 1 to 311)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..311
                     /product="GlxA 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=33106
     Region          2..311
                     /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 mhrvvalvrp vqstfevgca vevfgtrrpg mpqryefevc tetpgpvpts agyamsvsqd
       61 ltalesadtv iipswlpvea plsdgvrhal lrahargarl iticsgvfal artglldgrs
      121 atahparaeq lrrefprvrv epdrlyvdhg dvatsagaga gidlclhlvr kdhgaahaal
      181 larhmampph reggqarhap sspagdaldg llewagerlg tplavgdlaa hlgvsprtla
      241 rrfadqlgts pgawllsrrv iaartlleet dlpveaiaar vgltsavnlr rrfraqvgtt
      301 pgayrqafrv p
//
LOCUS       WP_357617071             293 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617071
VERSION     WP_357617071.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 293)
  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 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   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..293
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..293
                     /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=30604
     Region          1..291
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 melrqleyfv avaeeqnftr aaervhisqs gvsaqirqle relgaelfdr sgrtatltva
       61 gkaalehara alaaagavge avgevsdlir grlaigmvig ctitplfeal aafhrahpgv
      121 eisllegnsd rlvegvragt ldlalvgtat avheglealt iiserlvvav ppdhplaalp
      181 qvtltdlsty pivcmppgtg lravfdqaca aqgvrpvial qasaadaiad laargvavgi
      241 lsasmtdrha drltartiad vespalvalv wraghrpavr ellaharraf alr
//
LOCUS       WP_357617074             257 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617074
VERSION     WP_357617074.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..257
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27951
     Region          16..245
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mavptdngaw irrfhpapda ptrlvcfaha ggsasyfypv sqalspsldv lavqypgrqd
       61 rraepafedv prlvdalvdq vavwadrpla lfghslgatv afevarrlqa rgtevsalfa
      121 sgrrapsrhr pawvhegdde alisemlkle gtdaqmltdp elvrmilpal radykaaety
      181 ryqpgppltc pvyaltgdad pqvdvpdaes wrehttgpfa lhvfsgghfy lnrhapqvma
      241 lirrhaadgv vagnara
//
LOCUS       WP_357617093             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357617093
VERSION     WP_357617093.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..212
                     /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=22786
     Region          7..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mteglrerkk rqtrqrisdv avglfvergf dnvtiaevae aaevsvntvy nyfaakedlv
       61 lppdeaspdr lagivrrrpp gqsaaaavla rlreevrgre rsvgltpgfg pvlemmraap
      121 tlaarlqdlg hqmtealave laaetgaagd dplprlmawh igclhaliya eigrrtatge
      181 rpdaiaaavl elldvvegvl geqvlayavr ee
//
LOCUS       WP_357617110              97 aa            linear   BCT 28-DEC-2024
DEFINITION  response regulator transcription factor, partial [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617110
VERSION     WP_357617110.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 97)
  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 11450879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         <1..97
                     /product="response regulator transcription factor"
                     /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]"
     Region          <24..81
                     /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 sagaahqrla gllggcdqir tpalealrps lsdrerqiat laaagvtsra iaerlflstr
       61 tvenhlqrvy sklgitgrae lpaalrsftg hdgtesa
//
LOCUS       WP_357617129             211 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617129
VERSION     WP_357617129.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 211)
  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 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   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   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..211
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..211
                     /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=22308
     Region          2..211
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mrlavlgatg gtgqqllrqa ldlghevtav vrdasrlpad lrgrldvaqa dvtdadaits
       61 avkgrdavls amgargrgpt tvqsgsiaav ikamtrtqsr rllmvsasgl vagaddgpft
      121 qyvlkpllqr vlrhpyadla eaerllrasd ldwtivrpsr ltdggrsary rtaldrnirg
      181 glsttradva rcmltlitdq gsirhvvsva s
//
LOCUS       WP_357617136             361 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617136
VERSION     WP_357617136.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 361)
  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 361)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 361)
  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..361
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..361
                     /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=37922
     Region          117..361
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrlaaeglrl lgavalgavt alielvflll tlpfldnpnv gaaarrltrl etrrlrldpg
       61 alqegrplpy laarvpagvl gglvitllvy gadtavrfla awgrgeafdg mrpsiplvay
      121 lavagvvllf lvlsgvvgvh alerrlalrm lgpdptqale rriaelaesr agivaavdse
      181 rrrierdlhd glqqrlvals mligrarrgr selleqahqe aqqalaelre vawrvypsgl
      241 dslgleeala gvaersgvpv rvacdlrrrp pmavetaayf vvceavtnaa khagatlitv
      301 evheedaavv vrvrddgagg aqatggglsg larrvaaldg gfevsspagg pttitavlpc
      361 g
//
LOCUS       WP_357617145             182 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617145
VERSION     WP_357617145.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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 182)
  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 182)
  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..182
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..182
                     /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=19937
     Region          12..177
                     /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 mfalpltgsa elrplppwca eeflahldra rehiapwvga sfvatdldsa rtvlrryadl
       61 wardaggiwg iwddgvlvgg vmfvsfdaal gvceagcwle paaegrglit ravgrivdwa
      121 vgergiqrve wrtnatntrs iavarrlgmr rdgtlrqlyp gpagridiev wsvladewrs
      181 pa
//
LOCUS       WP_357617175             166 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617175
VERSION     WP_357617175.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 166)
  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 166)
  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..166
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..166
                     /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=18292
     Region          17..159
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mgdavdlimt qwlrerpdvd twpmgivgrv srlarlldre lkeffaahgl erwefdvlat
       61 lrrsgppyel tagalnraam vtsgaitnri drlaakglve rmpdegdrrs irvrltehgl
      121 atidglvaph vanearllat lspeerdqla glmrgllesl gdttpe
//
LOCUS       WP_357617200             316 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617200
VERSION     WP_357617200.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 316)
  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 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   3  (residues 1 to 316)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..316
                     /product="GlxA 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=33552
     Region          2..316
                     /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 mhtvavlald hvvaadlatp ievfgrarla dgrrpyrtlv cavtpqvagd aftivaphgl
       61 ealreadtiv vpgcseqagp papevidalr aaaaagtria sicagaftla aaglldglsa
      121 tthwvaagrl aqmyprvqvk pdvlyvdngq iltsagaaag ldlclhiirr dlgsaaaads
      181 arlsvmpler eggqaqfirh aqppvpqgsl lepvlswiee nlahevtlaq marrggmser
      241 tfsrrfreqt gttplqwllr arvrraqfll ettdhgverv aaqagfgsat afrerfkrvv
      301 gvtpqsyrsa franas
//
LOCUS       WP_357617223             157 aa            linear   BCT 28-DEC-2024
DEFINITION  cytidine deaminase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617223
VERSION     WP_357617223.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Navaratnam,N. and Sarwar,R.
  TITLE     An overview of cytidine deaminases
  JOURNAL   Int J Hematol 83 (3), 195-200 (2006)
   PUBMED   16720547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..157
                     /product="cytidine deaminase family protein"
                     /EC_number="3.5.4.5"
                     /GO_function="GO:0004126 - cytidine deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009972 - cytidine deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=16392
     Region          5..129
                     /region_name="Cdd"
                     /note="Cytidine deaminase [Nucleotide transport and
                     metabolism]; COG0295"
                     /db_xref="CDD:440064"
ORIGIN      
        1 mtmldtdral vqaatavakl rcrsdnhtva aaartadgrv ftgvnvyhft ggpcaevvai
       61 gaaatqgage leaivavgdr grgvippcgr crqvlldyfp sikvivgpmd glrpvpvadl
      121 lpetyvwgdh qldapmavrt gqwpmptvps srpased
//
LOCUS       WP_357617259            1039 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617259
VERSION     WP_357617259.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1039)
  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 1039)
  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 1039)
  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 1039)
  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..1039
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..1039
                     /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=110072
     Region          8..1032
                     /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 mtrewtfpas faqervwman qldtaspvyn vstpwrfpag idadtagevv grvvarheal
       61 rthlrmddga llqvvrehep vrlpaddlrd lpeaeraary aalrtelart pipldapplw
      121 rarlvrrdda wtllfvvhha vfdshsavll vaelaafsea altgapaavp elpiqyadfa
      181 vwqrhqltga eldrqlafwt gqlagapavt glpldrprpa qlgfagdevr falpdglldr
      241 vgrlaagsaa tpymvllagf aallsrisgd tdvvvgvsta grdtaeltpl igmfvnpval
      301 rcdvggdpsf tellgrvrag lvdamehgqt pfqriveava pqrdpsvqpi fqtalnfipd
      361 sgldpvelgt tkddlafdvt tgesrlvyrt dlfdrgtaea vvaryvrllt aavddpgqav
      421 salpllddae rdlvlrawng edaapafrsv iervqrqaaa tpdavalvce gvsltyaeln
      481 aaanrlarvl vargaapetr valalprspe llvavlavlk sgaayvpvdt gypagriayl
      541 ladaepalvl alpetaalvp adavvldgev gadqadgdlt dadraaplrp ehpayvlyts
      601 gstgrpkgvv vehravaayl awardaypgl agtallpspv sfdltvtgll gpltaggtvr
      661 lagidsphar vggrpsflkv tpshlpllda alspttdlvi ggealtgeql agwraahpdv
      721 avvneygpte atvgcvaarv apgrpldagp vpigrptaga rvylldaalq pvppgvvgel
      781 yvagdqvarg ylrrpgltae rflpcpygpp grrmyrtgdl arwrtdgtld ylgrrddqik
      841 vrgmrielge iesamlahpq vreaavavrt dsgepalvgy lvgtadeaal aaelarelpa
      901 hlvpaafvrl dalpltangk ldraalpapp atvahdgyvp prtdaenlva evyaeilrve
      961 kvgalddffv lggnslrgmr amariraevd vdlpmralfs spvvadlaaq ieqriaaeld
     1021 elsetevaal laaekdnra
//
LOCUS       WP_357617300             413 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora purpureochromogenes].
ACCESSION   WP_357617300
VERSION     WP_357617300.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..413
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44699
     Region          2..402
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mtadavedll rrltpqvlga vvrryghfdt aedatqeall aaatrwpvdg vpddprawli
       61 tvaarrltdl lrseqarrrr eddvarrlpp eqwlappadr rspeddslvl lflcchpelp
      121 paaqialtlr avgglstaev araflvpegt mtrritrakq rirdsgvpfg lpagpdrear
      181 laavrhvlyl iftegyasta gpllrrvdls teairltrml hrllpddaev tgllalmllt
      241 dargparvgp ngelvpmaeq drsrwradqi aegvalvsav lprgevgpyq vqaaiaalhd
      301 eapsaeetdw pqiealyavl tglsdnpvva lnhavavama rgasagldll aglaadprla
      361 tdprlpaara hllertgdlg aaraayeeaa rrsmnlpqqr ylyaraarla dad
//
LOCUS       WP_357617324             215 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357617324
VERSION     WP_357617324.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22496
     Region          2..165
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlfdmdgtlv dseklwdval relaaeyggt lsdsarhavi gtsmaesmri vhddlgqper
       61 dpqvstrwin arilelfrtg lrwrpgaltl lravraagip talvtssgrp lvevaldtlg
      121 rdsfdavvcg devdlakphp epyltaarll avpigrcvai edsptgvasa laagaavlav
      181 paevpiapid gvhqveslta adlellaall geppa
//
LOCUS       WP_357617332             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617332
VERSION     WP_357617332.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 190)
  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..190
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..190
                     /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=21016
     Region          10..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprvsqdqld arrheilaaa racfarhgye gatvrrleea tglsrgaifh hfrdkdslfl
       61 avaeddaaam vetvarnglv qvmrdllara ispdttgwlg sqlevsrrlr tdpafarrwa
      121 ersaaiaeat rdrlvrqrea gvlredvpid vlaqflelay dglvlhlamg rpagdlgpvl
      181 dlveeavrrr
//
LOCUS       WP_357617333             372 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617333
VERSION     WP_357617333.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=38905
     Region          17..370
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msstqprtvv vgggiigvst arhlaragad vtlitegelt snasgrslsw lnsagvrgee
       61 yhrlrlagid ryrtlaaqhp glswmrfdgg ltweapenad dlhriheyel ahgydshlih
      121 pdrvaeytpg idpaaispag aiwnpgegwv dlpnlaqhli kefaehggrl vtnagparve
      181 taggsvsgvr taegesyaad tvvlatgpav pamaaelgva ipdqtpisll vttkpvdtpl
      241 ravlntpraa vrpaphgala vdsdwttasi rpaadggfav seevvaella easrllagnp
      301 rleperlamg pkpipgdgdp vlgrvdevgg lwaafthsga tlaliagell ayeigtgrah
      361 pmlapfnarr fr
//
LOCUS       WP_357617336             357 aa            linear   BCT 28-DEC-2024
DEFINITION  adenosine deaminase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617336
VERSION     WP_357617336.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 357)
  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..357
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..357
                     /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=39499
     Region          7..355
                     /region_name="Add"
                     /note="Adenosine deaminase [Nucleotide transport and
                     metabolism]; COG1816"
                     /db_xref="CDD:441421"
ORIGIN      
        1 mnldlmpkvd lhchligtvr astfaelarr egldlpdtpe riyadvnslp pdpalyldtr
       61 iavpqgrsad epevsyslfq vsswvlqvlr eaddltrity eafeaahrts atrhlelsfd
      121 altehqeklg yaavieayae girmaerdfg msgrliaaid rsksgeeals wvrtvvdhph
      181 dyvagigldn letagpperf eaafrlagaa glrrtahsse hapvaantit cldvlgcdri
      241 dhgyfvledd evvarvrdeq ipftvistts rrswrpwrra siaamldagl nvipasddpg
      301 mfptslaney rilsgqlavt derlramala gveacwlpep ekdalrerfe relasme
//
LOCUS       WP_357617380             371 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617380
VERSION     WP_357617380.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..371
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=41299
     Region          11..360
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mteqslvvri adhvhgflrd lharglpvpv pkqrvflqai eaagprdtan lywigavtlt
       61 tshedlevys ptfehwfgkv aarripdeef pddeapaprg krdeapltaa sggdaglkag
      121 sseresrpvf gpaseddrav lsllwrelpr avptirsrrr rparrgpwid varicresrr
      181 shgeimtlrr rnrpqrqrrv lllidvsgsm kqhsahylrf ahavvgrldr vevftfgtrl
      241 trvteplrar hvdaavgsls dvvldaeggt rigaslqefl anarqvtvar galvivlsdg
      301 lergdcrpmq aavrrlslls hrllwwspla cdpayrpvtr gmsavlgsvd alagvrdlrt
      361 ayeqvqtwtr e
//
LOCUS       WP_357617382             285 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617382
VERSION     WP_357617382.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 285)
  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 285)
  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 285)
  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 285)
  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 285)
  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..285
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..285
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31502
     Region          6..268
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mlvdretldr rlgaegylad eglltalhla gtlrlpllle gepgvgktev anvlarvlgr
       61 elirlqcyeg ldasqalyew dypkqllslr aaevegrgvg dlyreefllq rpllrslraa
      121 sgavllidei dradsefeaf lleflgdfqi tipeigtita asvpfvvlts nrtrelhdal
      181 krrclyhwip fpdaererai iraqapglde rsaarlvaav hrirglallk ppgiaesvsw
      241 argvqtlare gsswleamrr sagllvkhee dlallgrhta evfgd
//
LOCUS       WP_357617384             338 aa            linear   BCT 28-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617384
VERSION     WP_357617384.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 338)
  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..338
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..338
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=35641
     Region          <4..331
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 malrhgrgya avnyptgmnl ggdpsqalvh attmggfvvt lssvdlgqgl rtviaqcaae
       61 tlgipienii vdtadtdtgp hcmgtfasrg thrvgnavim aareardvml qvaadelevd
      121 aedletdgtg fvrlkgssek kihisdvala ahfrqgrtis grgiylkeps tpvpetgemd
      181 pdscqahact vadvtvddet gvievlrlyn tyeigralnp alatqqvegg awmglshalf
      241 estepyyphs rehgpvdfte ylmpgpadip aqtslflerp agngpfgakg igemtanapi
      301 paianavyda vgvrltsmpf tpekvlrgld elragrag
//
LOCUS       WP_357617435             335 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617435
VERSION     WP_357617435.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 335)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..335
                     /product="phosphotransferase 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=35645
     Region          9..279
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mssptqrlld pdqvrryvaa slgpdvavtg cvplagggfa avwsatlddg rrvvlkvgpp
       61 pevpllryer gliaaearyl rlvaaqapev pvppllhhgs dpvlgdwllt gllagrtlhq
      121 ltvdgapvda vraglgaala alhrvdgdry gydggraaga twreaftamv ddlladatdw
      181 mvplpvpagr irelvhrhaa vldavrrpal lhfdgwagnv lavagpdgvp rlnglvdger
      241 hlygdplldl vsplifrrae depddaflrg yqaaggpvpl ddagvrrrlg lyrlhlyllm
      301 tvempsrgit gdtdpgrvar laelldreva alaep
//
LOCUS       WP_357617460             171 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357617460
VERSION     WP_357617460.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 171)
  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 171)
  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 171)
  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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..171
                     /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=19612
     Region          14..154
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mielpgdlpv vertavrlvv rdaqdrvllf htrdpdhprl gtwwelpggg mdpgetyaet
       61 avrelreetg fvvtatrlgp ptwrrrasfi hrqrrhlqde vvmtvrldaa gpdvdgaerl
      121 dyevedyfgf rwwtvdevvg saerfypgrl pallprflag eeidepfelw s
//
LOCUS       WP_357617478              63 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357617478
VERSION     WP_357617478.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..63
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..63
                     /product="helix-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=7228
     Region          5..63
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mrkrdellti aqvldelggv srrtfyrwre igkapegirl pngelriyrs dleawleslr
       61 saa
//
LOCUS       WP_357617513             152 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617513
VERSION     WP_357617513.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   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 152)
  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..152
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..152
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=15002
     Region          1..>123
                     /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 malrtvivdg spvhvlesgt gpavlmlhgs gpgttgsgaw attaqalgts whlvapdqag
       61 fgrtpipags rgglrlwteq aaglmdalgv ehyavvghsm ggavalalaa arpqqvtrvv
      121 avstmgapga plsaeldaiw aapparsghe tc
//
LOCUS       WP_357617568             299 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357617568
VERSION     WP_357617568.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 299)
  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 299)
  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..299
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..299
                     /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=31409
     Region          1..299
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mlrfglfgtg hwaaethaaa idahpraelv gvwgrnpera aeladrhgvp afgdvgalld
       61 ecdavavalp pdiqadlavr aaiagrhlll dkplaltlad adrvvaaaqq sgvasvvfft
      121 qryhpnvtgf lastaaaggw qharatmfas iyqpgspygd sqwriehgal wdigphalsi
      181 ilpvlgrvtr vaamngpsgl vhlllthvgg atsalsltld apreattrdf vffgengtet
      241 vppgdgdait afgtaidqll eeidagtrdh rcdvrfgrev veilsaaeva raegrtvei
//
LOCUS       WP_357617627             123 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617627
VERSION     WP_357617627.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 123)
  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..123
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..123
                     /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=14174
     Region          2..122
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrfadvdsqg hvnnvrfldy ledarfgmfh idpytageep fkglvvtrhe idyrrplgfr
       61 adpvlvetwv teiravrfal qyeirddsev yvtaksvlaa ydvdragprr ltegelaylk
      121 rfs
//
LOCUS       WP_357617659             210 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF47 domain-containing protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617659
VERSION     WP_357617659.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..210
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=23421
     Region          21..210
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mkrlrrirdl ltgrmdsalt eallgqlkat kegawlamam iggevgrtga heqmraiehl
       61 gdeerarlie elktavvtpi dredlfrlsr aiddvldslr dfvreshlyr vpdqirftpl
      121 ldqvivgiea lessvrdlas rpsvvvrdal eakkaggair rmyqyeisri fseeltadam
      181 kerelvrrle ivgvaignaa daiadgamkr
//
LOCUS       WP_357617655             119 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617655
VERSION     WP_357617655.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=13261
     Region          20..111
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mehytgvrpp snrtrsltht splevslqea ldalgdpirr rivrelagvp dwaracgtfa
       61 hlpvakstls hhfsvlrnvg lleqrdegar rlnrlrrgef ddrfpgllal vldeeqsdg
//
LOCUS       WP_357617674              67 aa            linear   BCT 28-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617674
VERSION     WP_357617674.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 67)
  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..67
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..67
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6604
     Region          1..45
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mprydfrcra cgstfevsrp msasndpatc peghddtvkl lstvsmtgga aapkasggcc
       61 gggccas
//
LOCUS       WP_357617715             326 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617715
VERSION     WP_357617715.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=35712
     Region          7..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mshpagrvla mlellqshhr ltgveladrl rvdertvrry aatlvdlgip vtaergrygg
       61 yrlrpgyklp plmltddeav avllglvaae rlglgteepa tatalakirr vlpaplaerl
      121 aavqdhlgft lrrpdpalrp atgtllalga aarqrrrvtl dyrswrgdps rrqldpyglv
      181 fhsgrwyltg ydhlreevrt frldrigavs tgpetfavpd dfdpvaqvtr slagvpyahs
      241 vevlletdlv tarrrvppsv geltevadgv llrtraehld gmaqllaglg wpftvlrpda
      301 lrdavrahat rlagwadrpg eappsd
//
LOCUS       WP_357617743             326 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617743
VERSION     WP_357617743.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=33792
     Region          65..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(66,68..69,129,133,153..158,177..178,182,197,
                     209..210,212,232..233,259..261)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mirdahafwl rspgvgeirp vtlpapgpde vlvrarysgv srgtetlvft ggvpadqyaa
       61 mrapfqegdf papvkygyls vgvveagpar lrgrtvfclh phqsayvvpa savtpvpdrv
      121 paaravlagt vetavnalwd aaplvgdrvs vvgagmvgca vaallarfpg vrvelvdtdp
      181 araavaaalg vgfaspddaa dgrdlvvhas atgpglqrai dllapegtvv elswygdrpv
      241 hlslggsfhs grltirssqv gtvsparaar rgyadrmala lelladpvfd alltgrsrfa
      301 dlpdvldrla agslpalchl itydge
//
LOCUS       WP_357617748             841 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357617748
VERSION     WP_357617748.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 841)
  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 841)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 841)
  AUTHORS   Rosinski,J.A. 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 841)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20189354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..841
                     /product="helix-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=88382
     Region          <109..661
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          673..841
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <775..841
                     /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 maaswpfigr atqlakirsa aegvvvagpa gtgksrlvaq avhgldgvaw arataaaaev
       61 plgafapllp atppagnplg waaaalrapv lvvddahlld pasaalvhhl vtrggtrvia
      121 tlrsrtpvpd avlalwkddl vprlelepfs peeteallga algsrveaat varlwrasqg
      181 nalylhelvl sgiltedgdv wrwrgpltit ptlretiagr igeltarere alellaygep
      241 lgadllavlg sldavqhled rqlvtvqpdg rrlqvrlahp lygevirdgc gvlrartmmr
      301 rlaqavteag lrrredvlrv avwrldsglp gdpglllagc erarivrdle lavrlgraav
      361 aagggtpala alatvlsysd ryaeaddvfa taweadmtet artdlgvqwa lnlavglgdv
      421 araravleet trlargvgar qgilimravl avltgdiaaa eellartrel gplnphgerm
      481 iggadaavll argraaesla rvaeararlv kqpdamrsla atltgtaana alllgdldga
      541 erladegfdl ggqfgswtra ilefgtvkar vlrlrgrlad alawardttg rlpacsalag
      601 sylgelahay allgdvaaae ealarveatg rpigpsavip lrfaqvwtma grgdaagava
      661 lcleiagsal pcdepfalhd vvrlgrpdlv sarlaaldvd splvalfarh aaardgaeld
      721 avsegfarlg lllyaaeaaa qaaarhreag lwrgaraaet rawqlsqrcq gartlalmdl
      781 dvpgltprqr eiavlaaqgl tnreiaerlv vsirtvantl yavydktgvn draalaailn
      841 r
//
LOCUS       WP_357617786             292 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617786
VERSION     WP_357617786.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 292)
  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..292
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..292
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31001
     Region          8..288
                     /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 mptslltltd aavistdktr igyrsvgtgp alvlvqgamg tcenfvelag mlsdsftvil
       61 pdrrgrglsp rpfepghqva rdvedlaavl datgatdvfg lstgalvale aarvlpgirr
      121 vaafdppvyl dglpdrliar fhreaargdv pgmlitsmkv trlaprlvel vprrlleagm
      181 rlflrrearg epgryastde laralpyeva iveelqdlvr faaidaetll lgaehspaym
      241 raglaalagi ipaaervela gvghgaawna dqggepqava palrrffgpr pd
//
LOCUS       WP_357617793             325 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617793
VERSION     WP_357617793.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..325
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..325
                     /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=34603
     Region          1..324
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mrefayvraa dvsgavrlag prarylagat nlfdlmreev etpelvvdis rlplsavedl
       61 pggglrlgal arnsqvaadd rvrrrypvla rallkgaspq lrnratvggn llqrtrcryf
      121 ydlgapcnkr vpgagcaald gfnrahavlg asrscvavhp sdmcvalaal datvnltgrd
      181 gersvpitdf hrlpgetphq etvlregelv tsvdlppeqp ghgdyvkvrd rasyafalvs
      241 vaaslrveng ritrarvalg gvapkpwray aaeqllagaa ageaafgraa eeavagatpl
      301 eqnafkvela rrlvrrtlie lagrs
//
LOCUS       WP_357617849             511 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora purpureochromogenes].
ACCESSION   WP_357617849
VERSION     WP_357617849.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11467609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=54618
     Region          1..510
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 mstlrdlaee htqlrpadid hlhriagdwq llsdlsfadl llwvpvdgdg tflcvaqvrp
       61 ttaptayldd qvgrivggpe vahlevayrq griwregdpv wygdvparhe aipvrlraad
      121 gesgevvavv grdtnlstar tpsqlelnyl ttaddlaqmt adgtfppprh pgettsaprv
      181 gdglvrldan gkvtyaspna qsayrrlgya shlvgedlak lhrrlasdpl egtdaangvl
      241 aalrgeappr reidargatm ltrslplmpa gvpigalvlv rditevrrrd ralitkdati
      301 reihhrvknn lqtvaallrl qarrvsmpea rvaleesvrr vasialvhet lsmssdeave
      361 fdgivdrvas aatevaatev svgmrrkgsf gvlpaeiats lvmvlnelll navehgfppa
      421 gedgvagpeg gappqvvvta hrfrkqlhvs vadngrglpa efdaerggrl glqivralvt
      481 gelrgsielr pgaaggteav lvvplarger g
//
LOCUS       WP_357617797             228 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357617797
VERSION     WP_357617797.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=25056
     Region          11..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstvkrvdkr tersrqtrak ivaaarelfl ehgygatnlq dvaeragvav qtiyfvfrnk
       61 rallkelvdt tiagddepva tmdrpwfrea caaptaadql rqhvhgtrli ldrvapitkl
      121 leaaaandpe iatmwpaeed prftvqsaaa qalvakpgar pelsaamaad llycllspdl
      181 ylvfvrdrgw spaqwetway etlhtqlceg parstssrrg segtvhas
//
LOCUS       WP_357617873             307 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617873
VERSION     WP_357617873.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 307)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..307
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..307
                     /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=32869
     Region          1..296
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtaavpalgr apadrrrhgr pgalwavpag lfftafglap ilvvaylslt rwnglgdpvw
       61 tgldnwralr ddadlthgiw ttllltalcw vvqtplalll gvwaaaprrn railsaaffl
      121 plllstaaia lawlslldpn fgaaatlgpw lgapdgnlig dpdralyvva lviawqfvpf
      181 htliyqaavr qipaslyeaa aidgadrvrq frsitlpllr htivassvlm ivgsltyfet
      241 illltgggpg tetrvlplhm yikgfvgfdm gyastlsvll vavgtvlsvl ivratgyhrm
      301 asdregl
//
LOCUS       WP_357617901             395 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617901
VERSION     WP_357617901.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 395)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         <1..395
                     /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]"
     Region          <35..260
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 srappgpglp sgalargpeg wmerldtday lllcsrelld hvvreqvlre erigvregtr
       61 vtglvgdadr vtgvrveqgg aeatlhadlv vdatgratsa pkwlvdlglp qvredvvdag
      121 ivyvsrwfte ppgtrddfpg vmiqmqagtg rpgqgagllp mengrwilsl fgsrggeppt
      181 deegfaqfar erhhpiiadl iaqarpagpi rayrsipdqr rrfeklpvpe gflvigdaaq
      241 alnpvhgtgm svaaqcalal rteldvrglr tgfsrnvqaa iakinqgawq iavntdqglp
      301 hvranvplrg gafankmaar vartgcgnrm vintvfnvas lcapmtrmmt paflwavlrg
      361 prtpaltaeq aiaqfpefgd lvkvdaaprs taspa
//
LOCUS       WP_357617884             338 aa            linear   BCT 28-DEC-2024
DEFINITION  mechanosensitive ion channel family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357617884
VERSION     WP_357617884.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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 338)
  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 338)
  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..338
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..338
                     /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=37453
     Region          <147..319
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 migsillvel mrrvlnkagr kwalarhlve hctwpafava avvafnlvfe pgmfgsavge
       61 rgleatvqra lglvtigavt wlivqvsyal tdvvlerlvl vegernrrar rirtqialvr
      121 riaaaviivv aigamlfsfp qvralgagil asagiagaiv giaaqptign alaglqlafs
      181 dalrlddvvv vedewgriee ltltyvvlrl wderrlvlpv syftqnpfen wtrhgsrvla
      241 vvllrvdwsv pvpklrdaly eflqgnplwd qkdwtlqvtd vltnglvelr almsaadsps
      301 awdlkcdvre flvnyvrdny pdslprfrvd tpesrlsh
//
LOCUS       WP_357617919             187 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357617919
VERSION     WP_357617919.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 187)
  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 187)
  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..187
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..187
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18718
     Region          5..>158
                     /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 mldtlaqvge lpttllmgal glvmladavp llgvlvpgdv avlaavgvgr patgaatvaa
       61 vvvgcvagws lsflagrvyg erlrhsrvgg wigesrwaaa egilrsgggr mvlvapflpv
      121 fnallplaag glrmsyrrfv acatagaalw aglylalgta srslagllpg egspmlvtma
      181 vglrgsr
//
LOCUS       WP_357617951             472 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357617951
VERSION     WP_357617951.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..472
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..472
                     /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=51863
     Region          35..420
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrdipltgdf anggvsfwyr qiglperrpa lpgprsydva ivgggytglw tayylkkaep
       61 glriaileke fagfgasgrn ggwlsaefag srkrhakarg rqamidlqha mfgsvdevie
      121 varqegidad ihkgglvhva tnpaqrrrlr aeiedlrawg ygeqdmrlld rdeqrervqv
      181 agtleaaysp hcariqpakl avglaeavar lgvdifedtt vtairprrdg aqaaaittrg
      241 avsadyvira tegftaslag qhrqwlpmns smivteplpp evwkhigwqg nellgdqaha
      301 yiyaqrtadd riaiggrgvp yrygsrtdvr gatqpqtval lwrmlvklfp aaadariqhs
      361 wcgvlgvprd wcstvhldha tglgwaggyv gsgvtttnla grtlrdlvlr hdteltalpw
      421 vgrqvrqwep eplrwagvql iyalfraadr rendhgttts pyarlanlis gr
//
LOCUS       WP_357617960              65 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ferredoxin [unclassified Nonomuraea].
ACCESSION   WP_357617960
VERSION     WP_357617960.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Kim,S. and Koo,J.
  TITLE     Recent advances in utilization of ferredoxins for biosynthesis of
            valuable compounds
  JOURNAL   World J Microbiol Biotechnol 38 (10), 178 (2022)
   PUBMED   35941298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Nzuza,N., Padayachee,T., Chen,W., Gront,D., Nelson,D.R. and Syed,K.
  TITLE     Diversification of Ferredoxins across Living Organisms
  JOURNAL   Curr Issues Mol Biol 43 (3), 1374-1390 (2021)
   PUBMED   34698119
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003036
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..65
                     /product="ferredoxin"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=6735
     Region          2..62
                     /region_name="Fer"
                     /note="Ferredoxin [Energy production and conversion];
                     COG1141"
                     /db_xref="CDD:440756"
ORIGIN      
        1 mmrikaatgl cigsgqcvlt epavfdqddd givalltdhp ddqsaaqarh avtlcpsral
       61 silqe
//
LOCUS       WP_357617986             304 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050733].
ACCESSION   WP_357617986
VERSION     WP_357617986.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,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 304)
  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 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     Protein         1..304
                     /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=32799
     Region          <3..263
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mtdrtptnaa pvleveglrk tfgdvvavdg vgftlsagga lavvgesgsg kttvarmivg
       61 lerpaagria acgrdrsrpa rsarerrrrg gevqivfqdp yssldprqsp aaaveevlrl
      121 htsldadgrr arvaelaglv glderqmaaa psrlsggqrq rvavaralaa eprvvildes
      181 vaaldvsiqa qvlnvladvr ertgvaylfi shdlavvrqv tddvvvmrhg aivergptar
      241 vldepahpyt rllresvprp gwrparrrse ahdhgtqhhp gtqhqetqqs letqqrprrs
      301 tvpk
//
LOCUS       WP_357617991             464 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357617991
VERSION     WP_357617991.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 464)
  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 464)
  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 464)
  AUTHORS   ter Beek,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..464
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..464
                     /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=48788
     Region          6..346
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mssppmrmla atlilavtga sllacsddes ksdsseitvw sledvadrvt atkaiiadyt
       61 aktgvkvnlv tvnedqfpsl iassaaagel pdvvgsvsla girtlagnel lhpdankeiv
      121 dklgrdtfsp raleltsedg kqlsvpsdgw gqllvyrkdl fdaaglpapd tyekitaaaa
      181 klntggvagi taatapgdvf tqqtfehlal anncqltdds gavkldspec veafrfygdl
      241 mrnhsvkgaq dvdttratyf agkaamliws pfildelagl rndakptcpq cakdptwlak
      301 nsgfvtaikg pngaepaqyg eisswavlne aaadpaksfv eyllsdgypr wfgmspegrf
      361 pvrkgtaddk ekfltawnts qagvdakkpl sevygdevlt glrtspdtfq rwgltqgqgk
      421 lvgailgelp vpkaladvvg gksdagaaaa rakkdveaik agvn
//
LOCUS       WP_357618017             467 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618017
VERSION     WP_357618017.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 467)
  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..467
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..467
                     /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=49953
     Region          19..397
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtlsatlael vrdfkangri vivgaslagl raaealreeg fsgsltiigd epyepydrpp
       61 lskqvlkgwv padhtvlpra revdaqwrlg vaatgldrat kqvrladgeq vpydrlliat
      121 gtrarqwpnp aeaalegvfs lrsrddaarl qqalaarpsr vlvigggfig sevasvcrel
      181 dipvtlterg saplvgalgg vigeiaaqmq rdhgvdlrcg vsvsslegda aghvrrarls
      241 dgstveadvv laalgsirnv ewlqgsglaa gfwgvgcdag grafdingvv tdsvyvagdv
      301 araphvlyey qflamehwdn avlgaevaah nmvnlephyr phlllpgfws gqfgvniksv
      361 gvppfgdeiv ftqgsvkdrc faaaygrrgr vvaavtfdhg kwleyyahli eesapfpppp
      421 pgwdrpdvmk pvpaefpapg vptaipdvvl tghdpnerra efrprgr
//
LOCUS       WP_357618109             320 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618109
VERSION     WP_357618109.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=34406
     Region          <60..194
                     /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"
ORIGIN      
        1 miwvtwrqhr aqilvtagll allgalllgs aveaswyvae happgcpgpa vacgelaval
       61 gqrydavysv fgwmplvapa ligafwgapl lgreyergth rlawtqavpv wrwlavklsv
      121 lgaavvaggl llslmvslwr pvfragvdst fgnigvfnmv gvepaawwly afalgtaagt
      181 lfrrtlpama lvvagvtvtm ftlfqlsdyy aepartelsg tvqlddpdar lvgaawveps
      241 grevaepsvs gcprrvdvgq sskntdawqa clfgkgyrya vyyhapsrfw rfqwteagil
      301 alasaalggl avrrtlrrpg
//
LOCUS       WP_357618130             402 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Nonomuraea].
ACCESSION   WP_357618130
VERSION     WP_357618130.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..402
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43929
     Region          3..401
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mdvegvfrre yaravavlvr hfrdidlaee avqdaftval drwpaegtpp spagwiitta
       61 rnravdrlrr essragrhaa aallhaqddp gspaeegpvh ddrlrliftc chpalavnaq
      121 valtlrllgg lgtaeiarsf lvseqamaqr lvrakakird aripyrvpre adlpdrlrsv
      181 lavvylvfte ghtaaagdrl vredlcaeav rlgrllaelm pdepevlgll almllvdarr
      241 aarttpggrl vplpeqdrsl wdreliaegh alvrrclrrg qpgpyqiqaa inavhgdart
      301 aadtdwgqiv rlydqllava pspvaalnra vavaeaedpr aalalveeld ldgyhlfhav
      361 radllrrlgr taeaadayea aidrtanaae qdflrrarat lt
//
LOCUS       WP_357618136             224 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: energy-coupling factor ABC transporter ATP-binding
            protein [unclassified Nonomuraea].
ACCESSION   WP_357618136
VERSION     WP_357618136.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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..224
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..224
                     /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=24449
     Region          2..224
                     /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 mieftdvhvr lgrrdvlrdl tlslaerrvg vigangsgks tlarlingla lpssgsvtvl
       61 grdtrrhgar irrdvgfvft dpdaqivmpt vaedvafslr rkglrpeeve rrvqavlaei
      121 glsehadhpa hqlsggqkql lalcsvlvle prvlvmdept tlldlrhsrq fagvlrglph
      181 pvvvvthdla lleefdrvvv ldagrvvadd epgaairhyr qlma
//
LOCUS       WP_357618141             478 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357618141
VERSION     WP_357618141.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 478)
  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 478)
  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
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..478
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=49683
     Region          3..470
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpvfahvlrh aadrphhpav rsrsgelsya elagrvagaa rrladlrtra apprpdlrag
       61 rgalvavsld dpvemlvavl aadlagatpl vcdpswgpdr raqvmravpv dalvdaalsa
      121 pavcpprpra aapddpawac fssgstgrpr avvrtraswt asfpyldrlt gigpgdvvlv
      181 pgplvsslya faavhtlaig atamlpgrws padlsadlar atvvhlvphr lpavldalsr
      241 ttsplrtavi ggaalpagar eraaeagvhv vsyygatels fvaldadgsg lrpfpgvdie
      301 vrlpqgeglv qqgqglgelw arspwlsqgy lagatgplrt ddagwmtvgd laepyrpgev
      361 lrlrgrgdga iqtggatvvp edveevlrsv pgvgdivvvg sphpylgsvv tavletrdat
      421 ppprarleaa arsgldtaqr prrwyavpel prtatgkpar glvatrladg dpglrrlg
//
LOCUS       WP_357618258             407 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NRAMP family divalent metal transporter [unclassified
            Nonomuraea].
ACCESSION   WP_357618258
VERSION     WP_357618258.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 407)
  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 407)
  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..407
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..407
                     /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=42853
     Region          10..402
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mkkifavtlg iltafggfvd igdlvanalv garfgmslaw vvvvgvvgic lfaemsgria
       61 avsqrpvfdl vrerlgprag vvnlgasffv slltlaaeig gaslalelat gvnyllwvpa
      121 valvawlvmw rvkfetmerv fgllglvlvv favalwklgp dwgelagqlt sppqaegapt
      181 ywfyavallg gamtpyevff fssggveekw tredlsvsra nvfvgfplgg vlslaiaaca
      241 atvflpvqaq vdslaqivlp vglglgqlgl alvilgvfaa tfgatletal scgytlgqyf
      301 gwqwgklvrp veaarfhtvl lvtvvlaaal ilttidpimv teyslvfsaa alpltylpvl
      361 miandpdymg ervngrftna lgtvymlllg vvavaaiplm iatkagq
//
LOCUS       WP_357618207             310 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618207
VERSION     WP_357618207.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 310)
  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 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   3  (residues 1 to 310)
  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..310
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..310
                     /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=33618
     Region          1..287
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 melnslrqfl avarlehlsr aaeelrvaqp slsrtiarle selgtplfdr sgrlrlndag
       61 klfrdyvera lgeldagrra vaeavsegvg tvrlasetfl tltgplaafk qahpavevel
      121 rwmaaedmgr hlraqevdlc vasqpiateg leavelldep vglgtplghp lsnrtsvsid
      181 elldqpfvsa gkghwqrrll drlfaardrt pkivcevdep saiaalisag lgiglvpsfa
      241 rttntripga wvpvdspdcr ravtlywvag shlstaarlm rttianwdwv tgqpqesgsr
      301 rghdgvgyhg
//
LOCUS       WP_357618286             415 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357618286
VERSION     WP_357618286.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 415)
  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 415)
  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..415
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..415
                     /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=42568
     Region          89..349
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrarvlaaat vavllstgta vpadaappta lapgvtapcp klptpavtrp prptppepvp
       61 ahravggeal atpglvappg tpapppvtat swlvadldsg avlggcgphe yatpasvqkl
      121 llaatmlpkl dpkqvatvtr edldiepgss avgllvggry pvetvwlgll lqsgneaanl
      181 larlgagsae agvremnaea rrlgalqtha vtpsgldgpg qftsaydlal iarvcfanpt
      241 frryaltera qipaqpalrk rgfqiqnenp liydypgalg gktgftdlar htyvgaaern
      301 grrlvvtlln aerrpvrawe qgarlldwgf slppdssvgr lvqpgevtad gadatpsaap
      361 dagaavaagr spggapewlg gavvggsagl vgllaallav grrrrrprrr avqwd
//
LOCUS       WP_357618356             374 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618356
VERSION     WP_357618356.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..374
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=39825
     Region          29..328
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mtdhivvlga gyaglgaakr aarrlrgadv rvtlvnater fverirlhql aagqrlpdlp
       61 lagllagtgi elvvarvigi dpearrvrld aapydlsydl lvyalgsaae ldavpgvreh
      121 aytlatadea vrlrarlaet revtvigggl tgieaatefa etipglrvsl lsagligkgl
      181 sararrhlhr sfsrmgiavr ehasvakvgp rgpllesgde lrsetvvwaa gfrvpdlaaa
      241 aglatdrhgr mlvdrslrsv shpevfgigd aaaadrsgrp trmacqtglp mgiyggeava
      301 dlltgreprr arfryvwqni slgrhdgvtq ftrgddspvd avltgpasaa fkeaisrgtv
      361 wamrhpgpyr pfpr
//
LOCUS       WP_357618358            1243 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora purpureochromogenes].
ACCESSION   WP_357618358
VERSION     WP_357618358.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1243)
  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 1243)
  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 10165758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1243
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..1243
                     /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=130126
     Region          229..478
                     /region_name="Peptidases_S8_1"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 1; cd07487"
                     /db_xref="CDD:173812"
     Site            order(238,270,315,334,366,445)
                     /site_type="active"
                     /db_xref="CDD:173812"
     Site            order(238,270,445)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173812"
     Region          <1184..1231
                     /region_name="SO_family_Moco"
                     /note="Sulfite oxidase (SO) family, molybdopterin binding
                     domain. This molybdopterin cofactor (Moco) binding domain
                     is found in a variety of oxidoreductases, main members of
                     this family are nitrate reductase (NR) and sulfite oxidase
                     (SO). SO catalyzes the...; cl00199"
                     /db_xref="CDD:469652"
ORIGIN      
        1 mhrsprwlsa gavgalvvgl tapasadppa rpsgpssatt atsgaparit litgdqvels
       61 paapgrvaat vrpgpgrdri tfhtieadgg lrvlpsdvvp yvssgvldad lfdvqelvad
      121 gygdaaqgal plivryqqpa ggrvrplaga taarplesin gaalrvgkgd ldelwttlrg
      181 apaartaaap arlgagidrv wldgrvhadl ehsvpqigap tawaagrdga gvevavldtg
      241 vdanhpdlag riveakdfsg tgsaqdghgh gthvastiag sggasnglrk gvapgarllv
      301 gkvlddhgsg ygsdiiagme waahsgakvv nmslgggatd gtdpmsqavn dltaetgtlf
      361 viaagnsgaa qtvgspgaat aaltvgavdr ddnlaefssr gprlgdnglk peitapgvgi
      421 vaaraagttm gtpvddaytr asgtsmatph vagavailsq ehpdwtagkl kdalvsttka
      481 npaltvfeqg ggrvdvaral sqrvygsata dfgrvntgga avertvtytn gtsspqtlrl
      541 alelrnldrg aaepdgvsld gtevtvpagg svnvplhadp akldrgvhgg wlvatgadgv
      601 avrtavgltl sgpihtvtlr aldmagqsgv atvftlfgeh resdqlgwip gevqvqveeg
      661 pylleglihh gapldeqltl vtdpelmvdr dltvvldprk atpvrietpk pteqravlsf
      721 fehrifgngr qvdhgvmefs tiqqvnvtpt rpvrqgefef ssrwqlvapl vdakvsnvsg
      781 pldinllhqs pasdgrrklp lvwagdgtpa elsragvega aalvagdpeh vaedqlvada
      841 aaagaamvli vrpanwsawt vwvpdgdrlp ipsmvvaydd gqrmiaaaka grvtldltlt
      901 pnspylydvw qvskgripdr ivhqvtadnt aevtaryadt ggfdwageqr fgwrpwqeys
      961 wmdekrlvrt gtmrqefvsa gdnwwqqrvl hrlpwswgrl tggstqqprq yaaddrvtet
     1021 whapvfrpav pagpgvavpt rtgdnldlrv aefvdadghy spagfseeqd tverrltrdg
     1081 qqiadlsggw apvpttpgsa ryrldvttrr ssdewrwatr tetaweftsa rpagdsaqpl
     1141 pllqvdyrvp adlrgtvagg rphqleltlr qpagvpapkg tslrvevsfd sgatwrsvpv
     1201 hstdtrytas vpagkgavsl rvhaadsagn vvdqtviday glr
//
LOCUS       WP_357618368             201 aa            linear   BCT 28-DEC-2024
DEFINITION  phasin family protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357618368
VERSION     WP_357618368.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..201
                     /product="phasin family protein"
                     /calculated_mol_wt=19916
     Region          1..100
                     /region_name="PhaF"
                     /note="Polyhydroxyalkanoate synthesis regulator phasin
                     [Secondary metabolites biosynthesis, transport and
                     catabolism, Signal transduction mechanisms]; COG3937"
                     /db_xref="CDD:443138"
     Region          70..>151
                     /region_name="COG5373"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:444140"
ORIGIN      
        1 mqdawrayle lamglteapr kkaqdaarrl vgtggataaq lqalaeelvs tgaanrealt
       61 klvrfevdra lgavglatad evaeltrrvh elerqlreak ggpggplpgt spvgvtpsgv
      121 aptgaagpat agdaagptag apsgppvpap tkavakkava kkaiakkppa svstttgdgv
      181 tsparpvkka aprkrttggt e
//
LOCUS       WP_357618426             327 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357618426
VERSION     WP_357618426.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..327
                     /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=36146
     Region          43..324
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matrttprav appdrpadaa gtapgrrrpr rtllpyllla pavvlelavh vvpmavgawm
       61 slleltqfhi rdwstapfvg ldnyrvvldv dsaagaellh sfwvtvvyti isvglswllg
      121 ttaavllqrp frgrgllral fltpyalpvy tavitwsflf qrdtglvnhv lvdqlhllgd
      181 kpfwliggns fvallvvsiw rtwpfaflcv maglqnipnd lyeaaavdga gfwrrlrsvt
      241 lpmlrpvnlv lllvlflwtf ndfntpyvlf ggsapdqadl isihiyrssf ktwdfgsgsa
      301 msvalllfll avtagyllit nrrrnda
//
LOCUS       WP_357618430             243 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Nonomuraea].
ACCESSION   WP_357618430
VERSION     WP_357618430.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,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 243)
  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 243)
  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 243)
  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..243
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..243
                     /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=25101
     Region          3..243
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mgaalagaft nsvfgvlray ilialwqarp glagydvsta vtfcfvtqaf igpmqllggg
       61 ltlperirsg dialdlvrpa plqlwtlaed lgraaqqllv rgvapmlaga vlfgitvpag
      121 paqwagflac ltagvvvsfa wrylvalsvc wladdrgvmv csmllstlls gmmvpltlfp
      181 gtlgevvral pwaamaqapa dvylgtapag ptlafqavwa aallglgala travrhrvvi
      241 qgg
//
LOCUS       WP_357618433             262 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Nonomuraea].
ACCESSION   WP_357618433
VERSION     WP_357618433.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,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 262)
  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 262)
  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 262)
  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 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..262
                     /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=28416
     Region          1..262
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 mvrtyallaw twtraamayr asfvlmvvlg vavtatdvav iivifshtta lagftrdeal
       61 flygsaglsf alcdmfvsnv drvsqhirag tldtmlvrpv gawiqlvtdr faptragrvm
      121 qaaavlgyal svldvdarrl wmvpvmvvtg vvifaaiwtl ggaaqffltd apevtnafty
      181 gggqltqypl svygrdlarg vtyvlplafv nwqpalyvld rddpfgtpgf vrflgpvaaa
      241 vlvlpawlaw rqglrhyrst gs
//
LOCUS       WP_357618437             959 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618437
VERSION     WP_357618437.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13307259
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..959
                     /product="glycoside hydrolase family 3 protein"
                     /calculated_mol_wt=102501
     Region          26..826
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
     Region          845..949
                     /region_name="CBM6_xylanase-like"
                     /note="Carbohydrate Binding Module 6 (CBM6); many are
                     appended to glycoside hydrolase (GH) family 11 and GH43
                     xylanase domains; cd04084"
                     /db_xref="CDD:271150"
     Site            order(861,871..872,926)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:271150"
ORIGIN      
        1 mrkipilaal tlaaallaap paqaadypfq npalpveqrv edllgrltlq eklgllhqsq
       61 aaiprlgiay hkngtealhg vawsndindk wsqklasgtm fpqavglast wdpalikkvg
      121 savgdeargy navdpavwgl qvwapvvdll rdpragrnee gysedplltg aistaygkgl
      181 qgddpfylkt apvlkhylay nnesnrslss snltpklkhe yyepafkaai sanaatgvma
      241 synlvngrpn hvnpdlgttv rswtdktlyn vsdawgphal tdvekyydtk peafaavlka
      301 gldsftiddn nsgplvenlt aaldkglitq advdravrnv ltirtrlghf dpdggpykki
      361 tkdvinspan qklnreaagk aavllrnsga lpfkgpksaa vvgplagtly hdwyggtmpy
      421 qvtpldgike rvadvstgtg lerialkhla sgkyitatgt gpddnaalvd taptaasewd
      481 ltdwtsgvst lrnagngkll ggdwrsldtd ddephgwyvq qqfelqaqad gsyliryagy
      541 etgdgwyglp epyvtvsadg tlglgtkdqa akfgkevvsd giaeaaaqaa kaevavvvvg
      601 snpfvagrev hdranlqlge gqrrlieavr kanprtvvvl etsypvivda pnllwtthag
      661 petghavadv lfgavnpagr ltqtwpatdn lpsiydydla ktgmtylygk dkplyafghg
      721 lsyttfgyqg lsvkgnvvsv kvtntgkvkg devvqlythq qqsrfkqpvk qlrgfqrvtl
      781 npgqsrtvtf plkksdlavw dytrgkwtve nathdvlvgs ssdrirlstt lrvsgetipv
      841 rdlsrttram dfddyagvaf vdetkaggda vegsagdwis ftgasfgsrf tagvssvsgg
      901 aielrsgspt gallgtvqvp atggiyqwgt atasvkagtg slylvfkgdl rikdfalar
//
LOCUS       WP_357618446             435 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357618446
VERSION     WP_357618446.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 435)
  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 435)
  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 435)
  AUTHORS   ter Beek,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..435
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..435
                     /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=47247
     Region          18..347
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mvksraaavl aaavlvlsac gsggsetpaa qnssqprtlk lwhyesadsa mgkawaeaik
       61 kfqashpnvt vkfeekgfeq iqktasmvln sdeapdimey nkgnatagll skqglltdls
      121 deatkrgwdk llpgglqtta kyddrgvmgs gkwygvpnyg efvmvyynke lfekhkvqvp
      181 ttfeqftaam dtfvkagvtp iatagaeypa qqifyqlals kaqkpwldaf qsykgkvdfh
      241 gpeftyaadt fadwvkkgyi aknssgvkae dmgvafmngk fpmmisgsww ygrfaseikk
      301 fewghflfpg atmypgssgn iwvvpeksen kdlaydfidi tmskdiqnll gnsggvpvaa
      361 dpaaitdaks kelietfnkv ttgdglafyp dwpapgyydv lvagvqnlin gskapaavld
      421 eiakpyednl adign
//
LOCUS       WP_357618496             574 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel protein [Micromonospora purpureochromogenes].
ACCESSION   WP_357618496
VERSION     WP_357618496.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13466092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..574
                     /product="potassium channel protein"
                     /calculated_mol_wt=61064
     Region          <26..145
                     /region_name="PRK10537"
                     /note="voltage-gated potassium channel protein"
                     /db_xref="CDD:236711"
     Region          264..541
                     /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 maeplrdrar ratgwrlran getrphyvvc gndplaywvv kallatelaq grvritlvvp
       61 errrsegpdg rdidgiqvvr adrldeaafr raglagadgl allhqddvgn mhaalcaqev
      121 eprlrlvvrm fntslanglr elfpdsavls dasiaapafv aaalgevapt hfrhagrtly
      181 varredvrag dvvcglavta dpalvrvlpa depaadvvla eatgqpagte laarrlvrar
      241 rrrqpvavll ravrsfatrk igiavmvllg viavlgwlns ravdvswtea lyltlvttls
      301 gqdpdvtkpa aaqimqvvln laglalipli tavvvdgivn arlalhagri qpqrtghvvv
      361 vglgnigtrv maqlrdfgve vvaidrtaea rgaalarrlg vplivgdaar eetlrsasve
      421 tcqalvvvst ddgvnlraal naralnaelr vvlrlfdgdf aeriqqafgi gisrsvsyla
      481 apafaaalld raviatipvd rhallvvevp vvagapldgr plaavarpge vrllahtrag
      541 qrtgassrsr crrrwsswpp assprrsgtg raar
//
LOCUS       WP_357618503             128 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618503
VERSION     WP_357618503.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 128)
  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 128)
  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..128
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..128
                     /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=14223
     Region          10..122
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdeefvvdtw hyvlakhaka mcalerelgd rhglgpsefe vldrivhhdr klriqelcde
       61 vhlsqsalsr vvarlekaal vsrgvcdadr rgvfvcitde grarhaealp tqravladvf
      121 adapaltr
//
LOCUS       WP_357618532             145 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357618532
VERSION     WP_357618532.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..145
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16040
     Region          18..121
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mttrtvaerr eearaayday lavcparqll drisdkwvsl llnaladgpr rysdlsrtva
       61 gvsqkmltqt lralerdglv srsvtpsvpv rvdyeltplg rsllpvmqai kqwaeanieq
      121 vtaareayda grpprphrpa trsea
//
LOCUS       WP_357618536             370 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357618536
VERSION     WP_357618536.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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..370
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..370
                     /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=38881
     Region          40..304
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mwtklvpvta liasvsltgg tayaapstpv ggdalgshgl vapegvkkpp kneatsfvia
       61 dvdtgdvlaa kdahgrylpa stlktltavt lipkldknrr vrpsenacnq egtavglspk
      121 ttykvddlfr allmssgnda amalaetngg lartmsdmna eakrlqaydt vaktpsgldk
      181 pgqsssaydl aliaraglan pafrgyistk tanfpapkgh yeisnhnkll wrykgmigik
      241 ngwtskalgs fvgaatrdgh tivvsimrhe gyfwdevakl ldwgfsvrgk vtpvgklvdp
      301 lpdpqaapra sapashvtpv aqpplldtag rkqsdstkli gsvvigggll fgliwlgygi
      361 rrrrrggsrg
//
LOCUS       WP_357618546             426 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Nonomuraea].
ACCESSION   WP_357618546
VERSION     WP_357618546.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 426)
  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..426
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..426
                     /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=46749
     Region          1..421
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mssvvldkvt kvypgdhlav drlslkaeng eflvllgpsg cgkstllrmi agleeitqgd
       61 lwldgqlanh laprerdvam vfqngalyph rtvrgnisfp leiaksdpal vrqrvtelsk
      121 alhidetldr rpgtlsggqr qrvamgraiv rqpklflmde plsnldagmr telrmeisal
      181 vrslgvttiy vthdqiealt ladriaimnr gvlqdvgtps qiyndpataf vaaflnsqql
      241 nllaatvrtp qnehvmldfg phrliipwsd prayaisqht ggqvlvgmrp dglapvpesy
      301 dgpsffgrvr aleyhghewl ayiecgmpav pvpeppdpra rangrpnasg rlgafvkrmf
      361 gqeeerqehe qtgqhpgsgv hrradlivrv ggrpawragd aakvavdptr lmiftldgar
      421 idpprr
//
LOCUS       WP_357618559             409 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357618559
VERSION     WP_357618559.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..409
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..409
                     /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=43836
     Region          27..405
                     /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 mssaasdqpv pslaaredar dpgdenaahr ehrlawldal rgvgamavva ehmlpwflps
       61 lrpywfslgv ygilvfflvs gyiipasler hgdlrrfwvs rafrlyplyl avaalvvgla
      121 wwvpvraevp rdgsavaaha tmlldvvgvg gvadtmwtls yemvfyllvt alfvmraher
      181 sgllsvvfag fsvvvglala gavvtggwlp yasgavfaag lacvvsgrfr tagacvlglm
      241 avallvlsgr vpwlgvavlg vmfagtavyr wergtgalwp vavtgalval apvgaigsgw
      301 wwvqpdvwit tivlaaatfa gamalrgrrl prvltwtgli syslylvhhp llkyfiavtg
      361 dlrrsplpvq lamaatalal vmlvsalayr fverpmqrlg rraarlatt
//
LOCUS       WP_357618560             127 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase, partial [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357618560
VERSION     WP_357618560.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 127)
  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 127)
  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..127
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..>127
                     /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          31..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 mtrldrveqt trgrftgppl tprtaviwsv ladeldrrag aeltvldvgg gtggfavpla
       61 qaghrvtvvd aspdalaalt rraaeagvaa rvravqgdgd alaglvepas adlvlchsvl
      121 evvddpt
//
LOCUS       WP_357618666             314 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357618666
VERSION     WP_357618666.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   ter Beek,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..314
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..314
                     /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=31068
     Region          6..310
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mavlaslalg srplgvgqvw talvapdggt astivrelrm prtalglvvg lalavagvlf
       61 qaltrnplae prilgisaga sfgvvlaiav lgvgslagyv wfgiagalga gllvfavanr
      121 tregaspvtl aligaaldas lasvvyalls idartfeeyr fwvvggltgr dlgvaaqvlp
      181 fvlaglalaa vvargldala lgddvarglg hriglvrlgg gtaavlltga avasagpiaf
      241 vglavphlar alvgadhrwt lgvsallgpt lllgadivgr liappgevpa giitaligap
      301 llaylvrrak vvta
//
LOCUS       WP_357618700             431 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618700
VERSION     WP_357618700.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 431)
  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 431)
  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..431
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..431
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=46148
     Region          1..223
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          375..420
                     /region_name="VWA_3_C"
                     /note="von Willebrand factor type A C-terminal domain;
                     pfam18571"
                     /db_xref="CDD:408355"
ORIGIN      
        1 mgdlptftlt idqnkylptd grevhailtv astggaggav tqsvtaeaae viiidtsgsm
       61 sgskirearq aaatavhtlr dgvnfaviag terarviypg nhaglvkagp atraeaerai
      121 srllahggta mgewlklagh llsahpsair hallmtdgqn nerpevfasv lagwsgkfvc
      181 dslgigedwv paelrkvsea mlgtfdfvrn qgdlseffrr ltqasmsktv aelslrvwvp
      241 qtatlkfvkq vsptlldltg krtdvnpltg dyptgswgte ereyhicvev ppgqigqeir
      301 agwvklvrpd tqevlasgnv laqwtddlaa strinnkvah ytgqaelhel iqdglsaram
      361 gdvdtatarl akakelaaes gredtarlle kvvevdpatg tarlrrnvdk adeleldtgs
      421 vrtsrlrkeg s
//
LOCUS       WP_357618739             973 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357618739
VERSION     WP_357618739.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 973)
  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 973)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 973)
  AUTHORS   Rosinski,J.A. 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 973)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..973
                     /product="helix-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=104519
     Region          <7..925
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <912..971
                     /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 masdvdsapl vgradqltal rsalhdevgp gqtaavfvsg esgvgktrll hevgarlrda
       61 gavvltgtcl digdasplhp viqalrrfda eltatqarts savrgllrtf aeetatadgg
      121 allervsrgl sliaegrplv lvlddlqwvd rstrqlllyl laglgdlqls vlaavraesl
      181 qgahplrrvl telrrlrsvr vvdlapldra dtdrlvaaiv gtpptpeaae qvwqrsggnp
      241 fvveelardl rdgrdglsdt lreiflsrvd alpqhahavv havaagvepv ehwllaevlg
      301 lpeqelieav raavahrllv gaddgyrlrh rlvaevlahe llpaersalh rryaealtra
      361 paelhqarla hhwrlagepg ralpaamaaa reaerlhgfa eahrhwsval qladtppagp
      421 tetapvqvdr atllehaaet ahqcgehara lsllaelagg ddaepscalr irrarylaaa
      481 grsapaeaey qrvleaadct srerataaah laelllhlgr yadagarare alalaaevdg
      541 sttevvlass algfseafle dpdaglavvr raleiaerag rpedvacayl hlaelltgpl
      601 nileegvvva rrgaervael glgrtyetrl laiatnglfr vgqwaeaekv vaaalrhrps
      661 gadavellla rcrlsvgygd vtasdrdlea vatvlaggga rhvlpmlilr aglamwqgrh
      721 dvarqavqrg ltesrsddvv llatlawhgl raeaeahasr tvpvdetvvr rlrevvdrva
      781 rksahaarpv rlgaegflvl ctaelsrldg rgdpdlwars aaewdrrnhp ypaaysrlrq
      841 aeallarrsr sataakllrr ayemaqglga vpltseiktl agrarvelee raqpaggpga
      901 trgepvsdel tvltarerev laavaegltn keigqrlfis ertigvhvsh ifdklqvrtr
      961 vqasaiylrn rad
//
LOCUS       WP_357618786             667 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC1 kinase family protein [unclassified Nonomuraea].
ACCESSION   WP_357618786
VERSION     WP_357618786.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 667)
  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 667)
  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..667
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..667
                     /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=71489
     Region          115..573
                     /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 mdfpvalivs lsalvliill agvarrllgv rlgalrtfla allaftiaap mlspifgsfp
       61 agrdadpgig avwvvllvtm cvvlipmvil vlaealvppg sipgplelar slrgrisrar
      121 rysqitriai rhglgpylrg rgdrvedrpg rqrlaaslrr alddggvtfv klgqvlstrr
      181 dllppefvee lgllqdrvap apweqvepvl taelggpaet vfaefdrtpl aaasiaqvha
      241 arlrsgesvv vkvrrpdidq ivardldivr rlaatlesrt rwgrslgvrd laegfatalr
      301 eeldfrveaa nmaavtasrp aapagtsggg adsgriavty papvtalcge rvlvmerltg
      361 rplaaaagae sgpevarall dcllrqvlve gvfhadphpg nlmllddgtl glldfgsvgr
      421 ldtsmrsalq rfllamnrqd plavtdalle vmprpedide paleralgqf marhlvpgaa
      481 svqmftdlfr ivsghglsvp pevaavfral atlegtlqrl apgfdlmgea rsfagrhlae
      541 rldggalket vvqevtallp mlrrlprrme riasaaehgr lgvnvrllad drdrrfltgl
      601 lhqvlltvlg ataglmavll lgvqggprvt paislfqlig ynllvisgil vlrvlavvfr
      661 rpreqrp
//
LOCUS       WP_357618807             169 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora purpureochromogenes].
ACCESSION   WP_357618807
VERSION     WP_357618807.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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 169)
  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..169
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..169
                     /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=18492
     Region          4..141
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 mpvpayvtrl rahighdlll lpgvsgvvrd dagrvllarr gdngrwsvpa givdpgeqpa
       61 davvrevfee tgvrvrverv ggvathpvvy pngdvceyln vwfrcapvgg epradgdest
      121 evgwfapddl peldewarlr idttlrddap twharpgerh palrrpdal
//
LOCUS       WP_357618861             130 aa            linear   BCT 28-DEC-2024
DEFINITION  Fur family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618861
VERSION     WP_357618861.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 130)
  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 130)
  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..130
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..130
                     /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=13901
     Region          1..123
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mttrrdavhd tlrrsegfrs aqdvyaemrl hgakiglttv yralqaladg gqvdvlrtde
       61 gesvyracas dahhhhlvcr rcghtvevag paverwaeav gsehgftgit htvevfgtca
      121 scstvpakvg
//
LOCUS       WP_357618921             422 aa            linear   BCT 28-DEC-2024
DEFINITION  cupin domain-containing protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357618921
VERSION     WP_357618921.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..422
                     /product="cupin domain-containing protein"
                     /EC_number="1.14.11.47"
                     /GO_process="GO:0043687 - post-translational protein
                     modification [Evidence IEA]"
                     /calculated_mol_wt=44960
     Region          30..312
                     /region_name="RoxA"
                     /note="Ribosomal protein L16 Arg81 hydroxylase, contains
                     JmjC domain [Translation, ribosomal structure and
                     biogenesis]; COG2850"
                     /db_xref="CDD:442098"
ORIGIN      
        1 mtivdppggh grpavpsaae alarcvsvep akfaaahwgr apllsradel pnpdgftdll
       61 sladadells rrglrtpflr vakdgqlvpa arytggggag aeitdqvlde kvlelyasga
      121 tlvlqglhrt wpalvdfard lgaalsqplq vnayltpags qgfathydth dvfvlqvdgr
      181 khwrihppvl pdpleqqpwg gradevaata dgpaaldvvl apgdalylpr gwlhsaqaqe
      241 ssslhltvgi raltryamve elltlaaedp rlraglpfgt dvadpdavep eltetvealr
      301 dwllrvdpaa vaarlrqraw paarpapirp laqaaalaal dadsriapra glrwqltvtd
      361 dhrvalrlpd rtitlpgtce pavrtlltgt vtrvgdlpgl dddadrlvla rrllreavav
      421 pa
//
LOCUS       WP_357618953             362 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein, partial [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357618953
VERSION     WP_357618953.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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 carboxy end.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..>362
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
     Region          9..224
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mvneptratp llsivvpvhg veaylyqcle siradvpage rgtvelvavd daspdrcgdm
       61 lrsyavgrse vrtvhlssnv glgparnagl tvatgdyvwf vdsddwlppg tipavldrlr
      121 ahrpdvllvd hvrvheggrr eldasspllr gvpdvvrlad rpqllrvqht awnkvvrraf
      181 mdelelrfhp gwyedipfsh plligaekis vldrvcylyr qgrqgaitst rsgrhfdafd
      241 qydrlldwvg rrypderlra elfglmvnhm lvvvgnddrl hphlrrdffh rvaaqyrrhl
      301 paggyprpgg vaglkhrlvg rdnylayaal rqahrlagrl rrpaappaga avasagadrv
      361 aa
//
LOCUS       WP_357618960             931 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618960
VERSION     WP_357618960.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..931
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..931
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=98400
     Region          1..501
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          453..930
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mdraaaland lrrrgvadvl tdsttrsvhs sdaslyrvpp llvarprsae dvataielca
       61 rheipltarg agtsvagnai gpglvldfsr hmnrvlhvda gtrtavvqpg vvqaalqraa
      121 apyglrfgpd psthtrctig gmignnacgs rtlgygrtsd nlaglkavag dgtaldlpah
      181 ggpaalrdlv lanlatirte fgrfgrqmsg yalehllper gfdvtgllag segtlavlte
      241 atvklvtdpa hralvvlgya diaaagdaap allehrptac egidarivdv vrrrrgpqav
      301 pplprgaawl fvevagddva evgeratrva sggedalvvt dparaaalwr iredgaglsg
      361 rspaglpaha gwedsavppa mlgrylrdfe elmaghgltg lpyghfgdgc lhirldvpld
      421 rphgalerpg gakalreflv aaatlvagyg gslsgehgdg rarsellplm yseaaidlfa
      481 qvkaifdpgd vlnpgvlvrp rpvdadlrvp aarpvrerla layrhdggdf sqavhrctgv
      541 gkcradntat ggvmcpsyla treekdstrg raralqemvn gsavaggwrs pevhealdlc
      601 lsckgcasdc ptgidmaayk sevlhqsyrg rlrplthysl grlplwarla srlpraanal
      661 lrvpglpaia gvdsrrtlpa fapetfrawf rrrrpapgep vllfvdtftd hfapeagrat
      721 vkvleaagyr priserrqcc altwistgql daarkilgrt vaelgeaaaq gvpivgmeps
      781 ctavlrsdal ellgeeaaap varmtrtlae llletpdwrp pplhglevva qphchhhavm
      841 gweqdarllr eagadvrrlg gccglagnfg vekghydvsv avagqqllpa lrqagaesav
      901 ladgfscrtq iadltsrqgv hlaqlladrl p
//
LOCUS       WP_357618963             384 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357618963
VERSION     WP_357618963.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=40338
     Region          8..371
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mgrelpshas aviigggamg vssayalaaa gvsdvvlidk gplgsgstsk aaggvraqfs
       61 drvnielavr sletfdtfae rfgqeidlhk pgylflldsp esvaefeknv avqndlgvps
      121 rmisvreame lsplidadgl laaaycptdg hctpesvvlg yagaarrlga rllpgcaatg
      181 ietadgriva vrteggriet dtvicaagaw sqpigawagv dlpviplrrq ilvtepvpdl
      241 pptaftidfg ttfyfhregp glllgmsdpd etpgfkldrs dawlprlgea marrapalme
      301 tgiatgwagl yevtpdhnal igtapevdrf iyatgfsghg flmspavgev vrdlylgrtp
      361 fvdvsgfdar rfalagarpe lniv
//
LOCUS       WP_357618971             449 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357618971
VERSION     WP_357618971.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     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=49540
     Region          2..372
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mtagqrrrcf gllrsagdvw acvlevnawr rrrqdaplag yqqlcrelsg pgpgtfgeld
       61 stgarsvlrr fsdawfaaak arqdgdlsvr fprrrralmp vrwyhgtftl dgrrvrlpta
      121 rgtsplwvrl arevpypveq vrsvtllceg grlfldvtae vpvatypagq gpdpdrvagv
      181 dvgiihpyav agpagegllv sgrairaehr mhladtktrr ravarrapkp dqrgsrrwrk
      241 yrrrarlgeg rhrrrvrqaq heaartvvsw aveqrvgvlr vgdprgvldi dagrrhnlrl
      301 rqwqigrlmq vltdkavqag itvdtvnerg tsstcpaclr rvpkprgrtl tcphckfsgh
      361 rdliaaaiia trtpgggptt ptaavalpev vkhrragrhl pgasqsrrdp rrppqaargs
      421 vgprrpaspp ggeslaqtar ihncasetr
//
LOCUS       WP_357618985             199 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RICIN domain-containing protein [unclassified
            Nonomuraea].
ACCESSION   WP_357618985
VERSION     WP_357618985.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..199
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21325
     Region          44..>147
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(54..56,67,74,81..82)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(109..110,122,124,131..132)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mrktavlvla saitasaait astahadgvg gapasaapvr dkdvinkagg grlalssnst
       61 aegataitlr dpgwtyntev weedstwqad eadtyttvlr nqaankclqp aaaapqrgtt
      121 ivvktcdgsd lqkwilraek vvggtytgww mwrpkvnknl amtlnryndg swdslhldta
      181 ypssdrlwri apndapwhl
//
LOCUS       WP_357619017             519 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein, partial [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357619017
VERSION     WP_357619017.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..>519
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
     Region          9..236
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mnwfvspgsr pqapvqlfcl pyagagasaf rrwpegigpd vevlavqlpg renrisedpr
       61 ftvpdvaaai agradrpyai yghsmggrvg fevvrelrrt grplplrlyv ggaraphvta
      121 pslfdglsrv dddellrrlg aggglpaell ehpelvqlll pllradfgrv dsyryvpgep
      181 lpvplvafsg rhdravsreq seawaahtsa gftlheidgg hffltdrlpe llaairadla
      241 davaapaaaa ptaarssaaa sgaaasgavg aegagstgah rvplgdtgws vwrnavlrst
      301 gfpadgltll aaphaaaaad dllatgagad rfdkefdeav raaahrisel agmpllreav
      361 twqnrgalva ldglvrgggd aarnvrrrdr erallkywqr yagknetvgf fgpscwvtld
      421 peqpevaris qgpgltrsrw vwfeswalsa yadrigtdla vrrwwppmlc phlsvrersv
      481 lrpgrppvpl spveaavlaa parpaaaprp arrrlsrcg
//
LOCUS       WP_357619018             940 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357619018
VERSION     WP_357619018.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 940)
  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 940)
  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..940
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..940
                     /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=103219
     Region          174..916
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mietpsyada lrilgckdar lvkvigfasa aartgwalag agqlatglad lrnsialyge
       61 dvvrrmpelk sgvdrftrtq rlaaahaviv vsayfealge tklpftldkl drgdrisrgv
      121 ptperfarlv aslllerlpt pephvpysgt rlaveraylr mseamagyvs glvvwdelsv
      181 ddqlllprml aegppahalr iydedyrsla ldshefgvrs lvtekpppat alsrvawlla
      241 elapprvgdr pmihlarmaa nlldrpllla gklpeavslp llgegylspr frvaeltres
      301 apaqlswwee qrllpdteaf lvghltslra tqapllvlge pgsgktklte vlaarlarse
      361 flpirvelgs vaaradvteq ieqalaavlg eevgyaelva aadgampvil ldgfdelvqg
      421 gvnrydyler vqefqareae lgrpaavivt srtvvaermr lpegllglql qpfdddqvrq
      481 wlniwdqanr allarrdlkp lpaeaalvhg emarqpllll llalydaggn alqhdhgplg
      541 rarlyevllr dyteretggv rrvaidqelv llgavalsml argrqlitde alerdlpalc
      601 hggedepdde dridwarkat erfffvrgng prtgyaflha tfgeflvawl avyalrdldr
      661 rrrlagdepl avvqavdddl lyavtshscl aergptvgfv lelldevpsa vrarcvella
      721 gllrrslher prrhftgfqp vrhtltrrla aysanltvli vcaseepvrv ssilpgpdhl
      781 eqwsslshlw kgqlgqegwt glvtalsahr vvedgkedvv lggdgtggmg dvvvavatgh
      841 tprhrrlldl llralgegrf lpyrdrlail eelvrtvavr spamhralga mwaedgadha
      901 elrpllqaml adpadrmgtw eqlvkagipe talweiqgld
//
LOCUS       WP_357619021             391 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357619021
VERSION     WP_357619021.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=43191
     Region          1..387
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msmrlrfala cagvffviag talvsvyfvv raslqyrasv ftpnsivlpd drwgwlssqr
       61 fddgyelark falkvhgtyq dsvldnlrna gvltvlagtg lafgvgwrta gmvlrplrnv
      121 tdtarrivqn hdlserigyk gsrdeikelt dsydvmldrl arsfdgqrrf vanashelrt
      181 pltinrtlvd vavrrpdate dvkrlgesll lvnarherli dgllaltege qavldrrpfd
      241 ladvaehvld qaageaaere vtmhrlldpa ptageavlve rlvqnlvena irhnhpkgev
      301 wvttrrradr velvvantgl qvppyeieti fepfrrlhgd rlrsdrgsgl glsivrvite
      361 ahggtvaatp rdeggltitv elpvhseggs v
//
LOCUS       WP_357619034             158 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            purpureochromogenes].
ACCESSION   WP_357619034
VERSION     WP_357619034.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora purpureochromogenes
  ORGANISM  Micromonospora purpureochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Micromonospora purpureochromogenes"
                     /db_xref="taxon:47872"
     Protein         1..158
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17790
     Region          7..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrpaaldwsv enctiarama vlgerwtlvv lrevfngvrr fddmrvrtgi prqvlttrla
       61 tlveqgvlrr epyrepgsrl rheyrltekg ldlwpvlvav lgwgdrylad pegpplsvgh
      121 rdcgaevrve lhcaegheva dprdvlprpg pgarrrvd
//
LOCUS       WP_357619042             203 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357619042
VERSION     WP_357619042.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=21922
     Region          21..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mselekgpqg rrrgrgarer ilgasqqlfr eqginrtgmd qlcaaaqvsk rtayqhftgk
       61 delvaeylrr fdpsvlsgvf drtdltprer llaafdippt tplcpyiaaa velhdpqhpa
      121 sqyardykka vaarladtar eagaadpeql geqlallidg aaartrvlna dafptaaaia
      181 avlidnaipa tagddrrree vss
//
LOCUS       WP_357619118             199 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CGNR zinc finger domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357619118
VERSION     WP_357619118.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 199)
  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..199
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..199
                     /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=21218
     Region          12..188
                     /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 msepltvesv lppapgaddy laldfvnsai alpgghfvdl lgtpgatnrw lterglaped
       61 agvqemcaaq lrslrehlrv lfaaragglp vlpaalsavn dalsrapsaa llywddkrgp
      121 yrtapcptne ildralatla anaadlltgp dadrltpcgs tpcnryllrh grrhwcsvrc
      181 gdraraaray arrtrpead
//
LOCUS       WP_357619069             181 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357619069
VERSION     WP_357619069.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 181)
  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..181
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..181
                     /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=20694
     Region          1..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mredtrsriq evalrlfteq gyeatslrei aeelgvtkaa lyyhfktkdd ivaslvdgrl
       61 aqldellewf kgqpkttetr relveryael lsgtrhieva rflernqtam rdhptlikir
      121 drmmdlaaem sgpdatpver isrslamfav hagkwlvkeg elsedevhka alevarrlle
      181 v
//
LOCUS       WP_357619152             245 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FadR/GntR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357619152
VERSION     WP_357619152.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 245)
  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..245
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..245
                     /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=27250
     Region          11..240
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtdtpresgy rpgyevaaeq llelivrmrl rpgdrlpten elarqlgtsr tvvreavkil
       61 salgrvraqk grglyvadde gmlgtgrwas fflptdldhv ymlfefrraq emetsrlaar
      121 ratptelrai eeaaamcrhg fetgredlfn egddtfhtai ataahnmflq iavrearrlq
      181 aqssliglrg svgghaaeav eeheaiyqai ragdpeaaaq aaathidntl ddyrreiqqr
      241 lfssh
//
LOCUS       WP_357619210             390 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357619210
VERSION     WP_357619210.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 390)
  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..390
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..390
                     /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=41742
     Region          1..386
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mdtivvagag hagtrlaaal resgysarlv lageepglpy rhppltknyl ggeleedelh
       61 fhpatfyrdn gielinqrva gidragravr ladgqalgyd hlvlatgarn rrlgvagddl
      121 rgvlslrtrq eaaalrgala takdivvvga gfigmefast anrlghrvti vetldrpmar
      181 lvspqsgrrf ttlhelngnr lifgngvvrl hgdpegrvra velddgtrlp adlvlvavgv
      241 tpetglaraa gldvadgvvv deylltsdph isaigdcaaf phegrrirre svqnaldhag
      301 lvaarltgsr qpygkipwfw teqfdwtlqi aghpdghtas elhesaggvf shqlyqgrrl
      361 iaveslnlpd dhfaalqkls dagepileag
//
LOCUS       WP_357619175             256 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FadR/GntR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357619175
VERSION     WP_357619175.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 256)
  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..256
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..256
                     /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=27955
     Region          20..240
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtasqetaag vpappawarr patlaravta elverivrgv hppgtplppe palceafsvs
       61 rtvvreavkv lqekglvqvr qgagtmvnpp arwdmldelv laatiaedes lailddlvvt
      121 rrvlesdman vaarlagpdt verlrelvdr mdelvddpvt yadsdrafhd timqtsgnri
      181 argvvrales qvintarymg rteralcvas nlghrriyer iaahdpdgaa eamfhhitea
      241 wlvrrtgpad pvrlrr
//
LOCUS       WP_357619213             294 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357619213
VERSION     WP_357619213.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 294)
  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 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   3  (residues 1 to 294)
  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..294
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..294
                     /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=32372
     Region          1..292
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdllplryfq vvarhehisr aadelriaqp slsrtiarle sdlgvplfdr qgrrvrlnrf
       61 gaaflarvnr algelddarr eladaaglqh gsvsiasetl ltltepvkaf iiehpgvgvr
      121 lyqdisdgma erlrkgevdl clasqpldgp glrhvelare evllavplth rlarqeratv
      181 adlageavvt trpgtwqrsl tqrlftdagl eliiacetde atvaielvsa glgvgfvpaw
      241 yvssplaetr apiswlhlda pdcervlrlv wreraylsaa arlfrdhlma sfia
//
LOCUS       WP_357619273             286 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357619273
VERSION     WP_357619273.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   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 286)
  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..286
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..286
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29745
     Region          18..283
                     /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 msvriddpar lgesrlpdgr llgwaewgpp dgipvllcpg aatsrwlgfg adavdalgvr
       61 lvsvdrpglg tstpapgrtf adfvddirhl aalrglgspa lignsqgapf alacaaegva
      121 arlaivsaad evaapefaga lptelrelvd kvacdptgae kfftgfgaaa mwdmvmggsp
      181 esdlevylsp afeaayrral negfaqgagg yardtvlamg rwpfdlekia vpvdvwygeq
      241 dishspdnga tlaaripgav rhlvpgigga vlwthaesil ryltgr
//
LOCUS       WP_357619309             906 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357619309
VERSION     WP_357619309.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11971133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..906
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=97158
     Region          <1..851
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          843..900
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlgrddetdl lesllrhate grgggvillg epgigkttll shaeeraagf lvlravgaap
       61 esdlayatlh qllfpvlgsv delpgpqaqa lnilfgrahg appdpflval stlsllslla
      121 gtlpvlcvvd dahwadqptl ktlafvarrl gnepvalala aradeghgad lpdvrrvplm
      181 glgreaakal laerlggrrl tdseqnhllt atggnplali elagrqqppe gtheplamtd
      241 alqrsflarv rarhaeslpl lqliaahgtg gvdtfekaaa tlqadtgplh raeldellty
      301 dgtrlvfrhp lirsaiyhsa tpdrraaihr alaaafdsla dqhrrawhlg qaamgpdeqa
      361 aeelersaeq aalrggpaaa maalaraael tadgprrgrr lwsaahaaal ggftgkaael
      421 ldraerephl deenriplav mraimaefag spedamdlir pwiprvlrld rrrftptvam
      481 ygdlgtranr pqawselagw lenialapdd pgdavllllr racqarsgrd vapataeega
      541 aiesltdpil mtlagalarg lgehelsrrl yrdagrrart ggslgalawn leyqaadeia
      601 rgrfgfaaay aeegyqfame vgqpstacrh rgllalcaav qgrpdaaela advlaeassr
      661 rladarsyal ralglielga gryreaarrf eavggwdtdt ppdlvvgvvp dlvealvrag
      721 eheraaaata ryvgwarraa slepaalaar cralistdgt addhyteslr lhagfdaple
      781 hartelllge rlrrdrrrse aqhhlrgavd tfrrigalaw aaralselra tgesvrtpea
      841 galstltaqe lrialavgeg ltnreiaaql flsprtvdyh lrkvfqktdi tsraelmrlv
      901 ladrpa
//
LOCUS       WP_357619335              69 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357619335
VERSION     WP_357619335.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 69)
  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 69)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..69
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6810
     Region          1..67
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mstatytvkg mtcghcvssv keevgevpgv tdvevdlatg lltvdsdapi daaqivaave
       61 gagyevanp
//
LOCUS       WP_357619360             204 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357619360
VERSION     WP_357619360.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..204
                     /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=22567
     Region          17..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maqkptplre qtrsvvrsll artaielfaa kgydnttlee vaaaagvsrr tlfnyfrnke
       61 dlalsglseq geviaarlae rpvkedawts lraafqaled idttperrle mitllfgnes
      121 lraghaekqa rwqdlfapli eprlpdsdhr nlqaraiaaa aitclqaane ewvrlggqvd
      181 lfdlydaavq airrpasppe kktt
//
LOCUS       WP_357619362             262 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Nonomuraea].
ACCESSION   WP_357619362
VERSION     WP_357619362.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=28102
     Region          7..260
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mskvdyrrqt vivtgassgl gaefarqlar rgadlvlvar radrlkdlad eltrahsvtv
       61 tvvardlglp dagrtlrael esrgiyatgl vnnagfgthg aftdedpdrl qsmialnvsa
      121 lvdlsrayid pltsadtgvl invasllgfq ptpymsvyga tkafvlsfte alweetrgtg
      181 lrvlavcpga trteffdvag sqsadygakr atpehvvraa ldtldrrsap psvitngrpl
      241 alagkimprr livrfmgrma rr
//
LOCUS       WP_357619384             172 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357619384
VERSION     WP_357619384.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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..172
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..172
                     /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=18839
     Region          25..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mttldprdgv daiiaqwqmv rpdldvspmg vigrlsrssr lieralkenf aahgiepwef
       61 dvlatllrag pphvlnagel saaamvssaa ltnridrlmd kglvdravdp dhrrrvlvsl
      121 tdeglrlvnt lveqhlayer rlldgldpad sdhlaallrr llvslgdttp sr
//
LOCUS       WP_357619468             342 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [unclassified
            Nonomuraea].
ACCESSION   WP_357619468
VERSION     WP_357619468.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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..342
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..342
                     /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=37467
     Region          16..325
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 medaarggvd phtatttlad ygervmhlav rgleaktldp ymagwrkrvv pslghiavrm
       61 itngavdrtv hawiadecsr stvknslail vrvmeqavrd niidrnpari tgwqseykra
      121 edelddpral alpnwaaler laealversi dcyegwgevv ifaactaari gevsgvrvgd
      181 idittwtwtv rrqttpspgg ladkgtkgkr arkvpiiaei relvlrrlea agndpsarlf
      241 tgprggritt avlrdathwd evvaklgyeh lrrhdlrhtg ltwmadagvp vhvlrkiagh
      301 gsltttqryl hpdsdslvaa snalsahltq gwsqtgpklr av
//
LOCUS       WP_357619514             321 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357619514
VERSION     WP_357619514.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 321)
  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 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   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..321
                     /product="GlxA 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=33939
     Region          4..321
                     /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 mdvrrvvvvg yeaaelldia cvttpliman maapppyqve lvtpggrpvt cgtgltihaq
       61 gtlervtgpl dtllvaggig hegaaadrgl vahvrrlare srrvasvctg agvlaatgvl
      121 dgrratthwq wartfavryp avsfdpdpif vrdgrvataa gvtsaldltl afieedhgge
      181 varavarelv tylqrpgnqa qmsmftaapp pgdgvvrrvv ehitsdpggd lataalarra
      241 gvserhlsrl flrqlgvtpg rfvrrartea aaqlltttrl pmaavaarcg fgnaetlrqa
      301 fldhygvpps hyrstqsars s
//
LOCUS       WP_357619632             265 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357619632
VERSION     WP_357619632.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   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 265)
  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..265
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..265
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27902
     Region          1..257
                     /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 mhsaqvlpdg srirwvevag vepalvfihg lgassapyfa paaahpalag rrsllidmlg
       61 fgisdrptdl aytleehada lacaleqagt gaadivahsm ggavaitlaa rhphlarrlv
      121 lvdapldptp lpqtkrpgss giavyrteqe fldhgwdetm dfigplwaat mrlagpqaly
      181 rsamnllrgt vptmrenlek laiprtflyp aadgpradap sltaagvsvm aipdcghnim
      241 ldnldgfara vadtlsapap teheq
//
LOCUS       WP_357619671             396 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase, partial [Nonomuraea sp.
            NPDC050733].
ACCESSION   WP_357619671
VERSION     WP_357619671.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     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]"
     Region          25..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 mrtaicerlg vefplfafsh crdvvaavtn aggfgvlgai aytpeqldte ltwldervgg
       61 rpygvdvllp gkvdasalda earladavpe rhrdfvahlm skygvggsgg piggpgigsa
      121 delgrrvtaa gaaglidval ehpvglvasa lgppppelve karaagvpva alvgtvehar
      181 rqvaagadii vaqgteaggh tgeistmvlv pqvvdavgpv pvlaaggias grqmaaamal
      241 gaegvwcgsv wltteeaeta pavkrkmlaa ssldtvrsrs rtgkparqlr sawtdewdsg
      301 qespgplgmp lqllvaesam arigaaaerg epgalelany fvgqvvgqld qvrparevvy
      361 amvsefadav erlgrlsgca arrrrrsptr gragrw
//
LOCUS       WP_357619692             339 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: fatty acid desaturase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357619692
VERSION     WP_357619692.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 339)
  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..339
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..339
                     /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=37363
     Region          3..337
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 meaprpqrgs dfarlsrria eaglmerrpg syavriglva tlfvgswavf avvgdswwqm
       61 pvavllavaf aqvtllahdl ahgqisrsrr tariagllvg nlavglsygw wmdkhtrhha
      121 npnhedhdpd vspdiliwsr kqaeaarglp rllgrrqawl ffplltlegv nlkvssfral
      181 rrpalknrpa eglllvahvl tyaaalfvvl ppakalafla vhqafygvyl gctfapnhkg
      241 mpvltaqdel dflrrqvlts rnvsggrlld valgglnhqi ehhlfpamps anlrkaqpiv
      301 rdycrslgve yaecgllasw gqalrhlhev grplrragt
//
LOCUS       WP_357619693             326 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357619693
VERSION     WP_357619693.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 326)
  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..326
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..326
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33975
     Region          131..315
                     /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 msaadfaaan lsratgagld pheylrvtgd ltdldqwgea fmraarehla ragqaatais
       61 tgehfqvaar wfhfatlgpn rasalaaaea dtamgralel lepqarrieg pgftgwlrgp
      121 adaaatvvvv pgldsgkeef hdvvaallrr glavyamdgp gqgalaatst vradyhhvig
      181 qvidalglrn vglvglslgg yyvaesaare srvaaavtvs gpfrlhwdvl pppvrdllie
      241 raggeeaarr fagqvdlsal apqiscpllv idggqdvipg vtngeplarl apqgryvslp
      301 hgdhllgnar pdwlamaadw isgala
//
LOCUS       WP_357619714              81 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357619714
VERSION     WP_357619714.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..81
                     /product="helix-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=9301
     Region          22..74
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mhlaraseep satdtsentw rtteevaaml kvdpstirrw rtarppqgpp fvrlsarltl
       61 ynihdvqrwl nqhridprev a
//
LOCUS       WP_357619735             486 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357619735
VERSION     WP_357619735.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 486)
  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 486)
  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 486)
  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 486)
  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..486
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..486
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=53212
     Region          1..>31
                     /region_name="NosL"
                     /note="cl01769"
                     /db_xref="CDD:470335"
     Region          40..469
                     /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 msrrrfltav alsglaagcg ssseageprp vgklafrtql rippllrpet gkdgvrrfrl
       61 tmqsgrtgil pgtstatwgf ngsflgptir asrgdriqma vtnrlpetst vhwhgmrlpa
      121 kmdggphqpi epgatwrpyw tldqpaatsw yhphphgrta thvyrglagm fiidddveve
      181 lpdrygvddi plilqdktfa adgslagdpl kdtfgilgdh ilvngtydpf vnvtterarf
      241 rilngsnarm ynvvfsdrra fhvvgndagl lpapvrvdrv sltpgervei vaafapgeqv
      301 vlrslsgsag idegdldllk iitasrltas vplparlart vpiavppgar vrrfelnghd
      361 ainhkemdps ridevvpaga teiweiennv yahnfhihev afrildvggs pppgyatghk
      421 dtvyvpsktt vrlavqfgry tdprdpymyh chilrhedsg mmgqfvivep gtenqvsrti
      481 pvahhm
//
LOCUS       WP_357619787             192 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357619787
VERSION     WP_357619787.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=20763
     Region          1..186
                     /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 mdfagsspgl tstkivvagg fgvgkttfvg avseilpltt eavmtdasah vddvsltpnk
       61 ttttvamdfg rvsldrdlil ylfgtpgqhr fwfmwddlvr gaigavvlvd trrladsfpa
      121 idyfeeaklp fvigingwdg qfahaeeeir ealsigghip ivrldarqre svkatlitlv
      181 ehaltrhmht pv
//
LOCUS       WP_357619807             503 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: trypsin-like serine peptidase [unclassified
            Nonomuraea].
ACCESSION   WP_357619807
VERSION     WP_357619807.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 503)
  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 503)
  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..503
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..503
                     /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=54291
     Region          111..>209
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkrillpagg ailatgllaa glagtaqaqg dvasdalakt eaqaaevvdf wtksnnaalt
       61 qavafnpdsl evkkiksggg ysadtkpgsa lpigeekkta vktqnvnlpk tigkvffegr
      121 dgklywcsgt siqsqyrnlv ataghcvydm aannevvsrw vfvpgyyqgk tpfgvyvgkq
      181 afthydldvy edfdrdyafv tvyngiggpn aatpkkvtge efdkfggqkf tkaveiseae
      241 yrkckdlngk etadcwakst dssdivgpdy tgktipgike vtaeeyaktp aknsiftqge
      301 kqeenvpesv ykaysgpgyk kiddkgnfti thyfvnyrvk desktvkffr tefyivdgvl
      361 kdvgrlgdnv ggqgvawnqp agavvrtfgy pagphpdgnk pytgvtpkwc ygktaskvlq
      421 vpakkveehq slrcpvtagy dggpwlakys nakrlgyvtg vtslivdvds nnryetitsp
      481 ifdgetaaiy kaaaavwsgk lvk
//
LOCUS       WP_357619811             388 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: trypsin-like serine peptidase [unclassified
            Nonomuraea].
ACCESSION   WP_357619811
VERSION     WP_357619811.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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..388
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..388
                     /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=41722
     Region          111..349
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkrillpagg avlatgllaa gltgtaqara diatdpmars tsqassvasf wlasngaalr
       61 aataytwddk evrkvvskgg ytadgnpgsa spigeekrpv grvqnvnlpk tvgkvffvdg
      121 sgkfrwcsat svqsnyrnlv ataghcvydt dsnkdvlsnw vfvpgyyqgk apfgiyvgkq
      181 afthtdfdvy edydrdyafv tvfngiafeg vkqvdrkdye rfsgpkrswg ghyyillskd
      241 agrlgdnvgg qgvawnqatg kyvrafgypa gphpdgnrpy sgvtpkwcyg kttgkavgas
      301 wlkieehvgl kcpvtpgfdg gpwlsnysns krlgyvngvt stfadqdgnd ridyitspyf
      361 dgetasvyna aknvwsgkiv gpngelyk
//
LOCUS       WP_357619830             204 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357619830
VERSION     WP_357619830.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Rosinski,J.A. 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 204)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..204
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..204
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23331
     Region          10..63
                     /region_name="HTH_20"
                     /note="Helix-turn-helix domain; pfam12840"
                     /db_xref="CDD:432824"
ORIGIN      
        1 meekyeigdp rvlkvvahpl rvrllgllri dgpataselg rvvgessgst syhlrvlary
       61 gfieedddrr dgrerrwrar hfytswdnar maatpegwea vrimqarqve alvramrafe
      121 espdpewvpt agmsdhlavl ppeavrefyr raaelvrele arhaghpear kvhlwaaafp
      181 setrdpdqpt erfpepersp eedt
//
LOCUS       WP_357619853             384 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357619853
VERSION     WP_357619853.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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 384)
  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 384)
  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..384
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..384
                     /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=41090
     Region          7..380
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msekisigvg mvghafmgrv hsqawrsvga ffdlplaprm avlagrsker tsaaaaqlgw
       61 advetdwrel vrrddvqivd ictpgdshae iaiaaleagk hvicekplan tvaeaeamvr
      121 aaasapgknm vafnyrrvpa ialarryvee grigeirhvr aqylqdwivd pefplvwrlq
      181 kdkagsgalg digahiidta efvtgqrvvg vsaltetfvk erplaedsag laatggtatg
      241 qvtvddaalf igrlsggava sfeatrfatg rknalrieln gslgslafdf eamnelwvse
      301 gdagftrilv tepghpyaga wwppghglgy ehtftheikd fleaiadgrd papsfadglr
      361 vqrvlaaver saadssrytv veda
//
LOCUS       WP_357619877             254 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SAM-dependent methyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357619877
VERSION     WP_357619877.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..254
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..254
                     /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=27680
     Region          <27..139
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mhrqlishla hadhpiaapv sesslirllt raklrsgarv ldlgcgegaw liralnlype
       61 atadgvdise ealtsaaeag trlglgdrlr lhqmpadafa aaepyelvlc vgathafgtl
      121 aetldavrrh lrpgglalig esfwerdpsk elhdllgtgp ddyadlagtv arahdagyat
      181 vyahtstrde wddyewswtg tlarwaldhp gpdgdeamaa adthrdmwln gyrdalgfvt
      241 lllrrtdllr rtdr
//
LOCUS       WP_357619995             389 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357619995
VERSION     WP_357619995.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 389)
  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 389)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 389)
  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..389
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..389
                     /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=41744
     Region          <194..388
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfgrvrawsr rhekpaaalr vmplatlcai laipyasmea ptssthldva gylalsaall
       61 lplmwrdrai asfavvslvs fgqwvahvdp lpanlavlva lwavayrcsf rwalaaclva
      121 elgvflalvn wdtptfgmfs sgsifvvtiw ltglyantrr rylegleera eraererdqq
      181 armaaaaera riarelhdvv ahnvsvmvvq adgagyalds dpeqarlavk aisktgraal
      241 aemrrlvgvl redeaaiidy tpqpglgqld elvrgsavpa rlevsgvpre lpegqqlavy
      301 rivqealtna lkhggpgvra vveidyggpe lvvrvtddgr gaaaprspdg hgligmrerv
      361 gmyggaistg prpsggfevl arlpmvnaa
//
LOCUS       WP_357620185             445 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620185
VERSION     WP_357620185.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 445)
  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 445)
  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..445
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..445
                     /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=46263
     Region          53..>418
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 matsdtrfwe qleilnaalp hgmravagpe gaapgsgvqp rfahldghvl vrdadtdrav
       61 aavqgllpgp dpvrvagarh agrgsvrrla vgsrdlhrtv ehlagenias slvhfvsvag
      121 vnlcpgdepv psagplnppl sgrdrgenvt vavldtglvh dyldhqwlaq ssgvpdipmv
      181 tgdvtapgde ldadglikpy vghgtfiagv lrcvapaadv rvydvfpyag aaledelgqt
      241 lhrimdthgw pdiislsagt rtgdagellg laafmdelaa hpgtvlvaaa gndgetlpfw
      301 paayaaepvn vsgdvvisvg alredglgra cfsnhgdwvt vyapgerlvn aftsgpyqyg
      361 yphrttcrfs dqglypgctc latlqdgdka tftglaewsg tsfatpivag lvaarmsqek
      421 vssrvaaadl magrlavpdl sgllr
//
LOCUS       WP_357620086             890 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [unclassified Nonomuraea].
ACCESSION   WP_357620086
VERSION     WP_357620086.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 890)
  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 890)
  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 890)
  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 890)
  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..890
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..890
                     /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=94128
     Region          217..885
                     /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 magglrrsls efetgwattv irwrdprapl taaaatgaag faaallaggp asvtgavagv
       61 laallaavsl lttsarlndh rpaatgtrwm gggavvwagg valrpvaent glmvsfadll
      121 vllgtvllag galiasgrsl pgtvvlrlvt dsylcavslf ligwvvalrr vyeqadpatf
      181 tftmlppmla llvtcaavps afrgrsapla aagvgvlatt tvagiaeava rltdavpplw
      241 svmlapvafl llaavpwaar eqdpppagas lgnvialvpl vlvgvatctl lahlagvrql
      301 apvtgvvvla gsavllllfr vfvlsgangr lrrlavlgdr qlrelaestg dvvlicdyeg
      361 ivrevgagve vtygyrpdel vggtifeyih pedvpgiqaa lramgldddg aspgacliac
      421 rvraadgtwr ptesvatrhl ggedlllvtt rdvsdeealr nqvahltfhd gvtglpnray
      481 feertrevls gragqvavif ldldgftsvn dsvghasgdy llgqaarrlr gavrpddtla
      541 rwggdefavl vetggeaqla vdlaerllre vsqepfrvad rdvaltasvg vafaedemps
      601 gdlirnadva marakemggr rvevfaaqmh advvrrlela adlqralieq qfaieyqpvv
      661 dlatsrvtav ealvrwwrgs vfvppeqflg paedtglivp lsewilreac revaawrass
      721 wdiglsvnls arqitaprfv etveealtes glpasaltle vieemlveda eetirrlsel
      781 ralgvrlaid dfgtgyasla flrqlpvdmi kidpsfvsgl grddtltllt rtivrlghdl
      841 glivvaegie rpeqlellre mgctrgqgfl varpmaargv dslmrtsltv
//
LOCUS       WP_357620211             186 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357620211
VERSION     WP_357620211.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 186)
  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..186
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..186
                     /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=20512
     Region          5..141
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpakrppvpl sreriieaal hiadsqglrr ltmrrlgdal qveamaiyhh lprgkealmd
       61 alaehvttvh veqlptwqet akawcraere llrdhpgvla laltkppkga talaireqte
      121 qlaegglpda aeavralraf vfgsvavevq qsgwadpevd ewvrrderad vdfergldal
      181 lkglqt
//
LOCUS       WP_357620240             300 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: coiled-coil domain-containing protein [unclassified
            Nonomuraea].
ACCESSION   WP_357620240
VERSION     WP_357620240.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..300
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..300
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=32365
     Region          34..>176
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mgvrvgrial fvatlsglll lpvpqaataa pnpaelrklt kqaqqlnery rgqiqsleei
       61 kvqvkkaitt sgalkarldr akadvsaiar hayingpvdg tqllgldgdp saalsqaatm
      121 syiaaeragr vqaiqrlidd akkaevaadd kveklrreik tmqgrrreie rllakygfqq
      181 pggsdgltar mvavraavms nfpmpygvgc lrpgdpgehg kgracdfmms sggraasgad
      241 eergdalaew liqngprigv myiiwkqryy dirsgggwdp msdrggvtan hydhvhvsvf
//
LOCUS       WP_357620258             313 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357620258
VERSION     WP_357620258.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 313)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..313
                     /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=35175
     Region          22..310
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrekglrera vrekvlegvl vrrartwlpg lllvapsiva igvfvygmlg wnfrlamtdk
       61 hdevsegkfv gldnfvsiwd qprwhlsvnh aimftvvfvl galvlgwfla flmekgirge
      121 gtfravylfp maisfvatgi vwrwlmnsgm eeravglnrl fdaiglpqwq wfrdpdwgma
      181 amalpaiwqm sgyvmalfla gfrgvpeelr eaarvdgcne wgvyrhvvlp llrpvtlsal
      241 iilghislkv fdlivavsgk qiitdvpavf mwvavfdshd pakgatiasy ivlsvavfvi
      301 pylvwsvrke rrs
//
LOCUS       WP_357620265             482 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FGGY-family carbohydrate kinase [unclassified
            Nonomuraea].
ACCESSION   WP_357620265
VERSION     WP_357620265.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10167365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=51152
     Region          3..420
                     /region_name="ASKHA_NBD_FGGY_SePSK_AtXK1-like"
                     /note="nucleotide-binding domain (NBD) of Synechococcus
                     elongatus putative sugar kinase (SePSK), Arabidopsis
                     thaliana xylulose kinase-1 (AtXK-1) and similar proteins;
                     cd07783"
                     /db_xref="CDD:466801"
ORIGIN      
        1 msvwigvdlg tqsvramava adgrvlgaag rpltshrdgp rheqdpeqww relaaatrea
       61 lrdvppervr gvavdatsgt illadrdgrp ltpglmyddr raadevervn avgahvwekl
      121 gyrrmqanwa lpkllwllrd apegarlahq ndfvnrrlag revatdlsna lktgvdliee
      181 rwphdvldal gvpaamlpgv vrpggvigev caeaaeatgi pvgtpivagt tdgcaaqlga
      241 galrpgswns vmgttlvlkg vtpelvhdpl gvvyshrapd gswlpggass tgagvlardl
      301 pgrdldalge eaarrfgpgg rkpaattypl vsrgerfpfa apeaegftlg evsddvdrya
      361 ailrgaayve rlcfdyldll gapvdgeiil tggatrsayw nrlrasvlgr pvtlrenaep
      421 algmaalaag pgatdgmvrt reivhpdgad lsehylrfve eletrgwlpa taaaharert
      481 tp
//
LOCUS       WP_357620273             319 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar-binding transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357620273
VERSION     WP_357620273.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..319
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34045
     Region          22..316
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mnaadvapea qtrfpqelmy aaasqyyled atqadiakrl gvsratvsrl ltearrhgiv
       61 eirvhrpatl eegplaaeva ealrlqrvyl vpkvsgpalg pwlapglara lagvglrsgd
      121 tvlvssgstv yecareslgh fpgvtiapav ggqedpqpwf qtnettrlla ervggvpsyl
      181 yapalpgpel fsslqhepsv rrvmdlwaha kcaivgvgsp plmrqvtpaf vpryadslrh
      241 avgdvcsrfy drdgepvsyp gserlvatgl eelrripfsi avaagpekvv sivagarggy
      301 fnrlvtdalt aesllaatr
//
LOCUS       WP_357620276            1242 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620276
VERSION     WP_357620276.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1242)
  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 1242)
  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 17582184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1242
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..1242
                     /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=130118
     Region          105..569
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
     Region          785..>849
                     /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"
ORIGIN      
        1 mltavvvpph qaasaatgpa etqparvtlt litgdvveya psqgsipsia ikpaprpdga
       61 gvtfatlpgk dggylvlpsd aasmvaagtl deelfdvetl areqrveaip llvtyqgdpa
      121 psalasaara lpagenvrvl dsvngaaitv raeraddfwa glrtgnklsg ggiakiwldr
      181 ktkasldksv pligapaawq rgfdgkgvkv avldtgidaa hpdfagriia senfsdsast
      241 adrighgthv astiagagpt ykgvapaasl mvgkvladng lgdwswaiag mewaasqgad
      301 vvnmslgscc gngtdpmsqa lneltkkygt lfvtaagnes dpltvsvpaa adealavgav
      361 dketgttlag fsskgprldd aavkpnivap gvdivaarsa dsslpgipgn drytafsgts
      421 matphvagaa ailaqqhpgw qagelrdalt starrndghn wfeqgsglvd varataqsvf
      481 atsvvdfrll gkpatrqvty rnigaepvtl dvslvtrgws gkpapdkaik lgarsvtvpa
      541 ngtatvaltv dpsagpigay ggwvtaasgs sdvrlvtpfs yytgpathrl gvslvnsygt
      601 keffpgyqae plvyavplkr ansaedpfnp ygyyylhtdy sgngefylpa geyevigvan
      661 esrisnrtsw vienvrldgd ktvtldarkt apirpdtpka ldgggsayyv rtftdraqpv
      721 slygavlggq qlyvtpvpsa kagkvrlshq wnleppvlts vtagsltlhp aydmdamrrl
      781 tsaatypvis vgrgrpedfs gvdvsgkvvl vgipvengyv nagvamddag reaslrgaag
      841 vigfldvdgg rarvplgwam rlglsaaegr avrsalaagp vslrlepyag pasvyhlrfd
      901 srgrvpsrpa rvdmkdlvri naayhadnpd tsgweygest ageepgrlty ggslpmpvtr
      961 teyfgpvsdd vvwsrtitns glilhsddrf agddrrvseq wfkaplvpaa advpsgypvp
     1021 vpcalcrdsd rfvpleqwad sdprhytdls hvtskprlsv ggqevaaqgw rpryfpvpap
     1081 ggayrleavd tpdralsrtv sttsqftssa ppssgaprgy scsfgagcaf qpaiqlrydl
     1141 pldvlnrapa gqsfafdlra gahsavrrap vvnrvrveys vddgvtwhda trvkkrgdgr
     1201 frvevahpal aqtsgfvslr vtasdtaggs ttqtidraya lr
//
LOCUS       WP_357620334             964 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357620334
VERSION     WP_357620334.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 964)
  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 964)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 964)
  AUTHORS   Rosinski,J.A. 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 964)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..964
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..964
                     /product="helix-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=103941
     Region          <8..924
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          903..957
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mavdderqam allhgllaea vagrgrialv tgaiatgksr llygfaddaf ehgalplsam
       61 gsraerdlpl gvlsqllhna pmteehratt lrllqegara hissdprads iehvdvqivd
      121 alctvllels ercplviavd dmhhadrasq lclsylarrv kyarimlvfg tpghqarlpn
      181 llhtevlrqp hcrqvrlghl teqgvaerva rlageeaaar faarchevsg gnrllvdaal
      241 edlqdtgapg drygeavvac lhragpeall maralavagt taaaarllgr adtgdttgra
      301 ettaagetag rgdttaraet agrgdttarv etdrlyggep drlegeldaa raeqaltgag
      361 lldggrfrhe aaraavlagl dgaerallhr raaelayhdg apvaavadhl irgghaghpw
      421 alpvleeaae qalrdgdvep aieylklawq acaderrrar itttlvrakw rinpstpagh
      481 laelttalrn ghlgggdavv lakallwhgh dtdakdvlar lgelaepdre tvaelaaara
      541 wfrssypsfl phlpklsdeq asgaahslsv grrlesagal araladecpd epaataervl
      601 rgcrldemsm dtvesalltl tytgradraa pwcdafiaea asrhapsrqa rlsairaeih
      661 lrrgdlagav ddarraleii ppgswgvavg gpigslllag aamgrfeefl pqadrpvpea
      721 mletrfglhy lygrgrfhlm agqprqalrd lrlcgelmra wgldapgfia wrldvaeali
      781 rleepeearv lvedqlarcd rrsarvhgag lrllaavgep rhrvmmlrqs aellqssgdr
      841 yelartlgel teayramgef rrawmvgrra raladecrit vldpdlapge dedgeaeqgg
      901 vrpvlsdaer rvaalaadgy snreisgklf itvstveqhl triyrklnvt rrtelpadlm
      961 srqa
//
LOCUS       WP_357620364             339 aa            linear   BCT 28-DEC-2024
DEFINITION  type III polyketide synthase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620364
VERSION     WP_357620364.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..339
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36405
     Region          1..339
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mhisgvqsvl pdhrytqaei teafsrltdc dedllrrfht atgvegrnla lpladyakld
       61 sferandmyl evaldlgeqa lrgalrkagi rpekvdhlll csttgiatps ldarlaqrvg
      121 lrpdvkrvpv fglgcaagas glsrlhdylr gwpdhvavlv cvelcsltiq rddtsianlv
      181 asglfgdgaa avvatgrgqg pevvatrsrl ypgtehlmgw evgqhgfriv ldpdltgfve
      241 qalggdiktf ladygltpdq vatwichpgg pkviekivet lglppkavev twrslrehgn
      301 lssvsvlhvl qetrgrpgap avllalgpgf saellllhw
//
LOCUS       WP_357620388             251 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357620388
VERSION     WP_357620388.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=27621
     Region          38..132
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mavdrersvv fgeaveqyds arpdypaqli tdvleyapag palevgagtg katagfaarg
       61 aeltcvepdp rmaaalaakc pgarveigff eeyvpdrafa llysaqawhw iderrrwdla
      121 haalapsgav avfwnhyvvt dprlrgalaa vdshygvtts smhrdgstrg kwsehelahd
      181 prytdldqrh ytrtdrygtg ryldlarsvs ayrildpdtr eevmeefaal lggdgvdltf
      241 ttdltlarra r
//
LOCUS       WP_357620418            2960 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Nonomuraea sp. NPDC050733].
ACCESSION   WP_357620418
VERSION     WP_357620418.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12828924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2960
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     Protein         1..2960
                     /product="type I polyketide synthase"
                     /calculated_mol_wt=303599
     Region          14..1458
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1120..2519
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          2299..2753
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(2507..2508,2510,2531..2534,2559..2562,2583..2585,
                     2606..2607,2629..2630,2644,2671..2672)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(2607,2631,2644,2648)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          <2767..2942
                     /region_name="PRK06060"
                     /note="p-hydroxybenzoic acid--AMP ligase FadD22"
                     /db_xref="CDD:180374"
     Region          2774..2859
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 magestqrag tggpdaiavv gmacrlpraa gpaefwrlls egvdavtaap eerwpgaghr
       61 rggflesvdg fdaaffgisp neaaamdphq rlvlelawea lenaravptg lrgsaagvfl
      121 gaisndyaal qarlgaeerg rhayvganra mianrvsyfl glrgpsltld tgqssslvav
      181 emaceslrrg etalalaggv nlnllaettd aiaglgalsp dgrchvfdsr angyvrgegg
      241 glvvlkrlsd altagdavha vilggavnnd gggegltvps rdaqaevirl acaragvdpa
      301 dvryvelhgt gtkvgdavea aalgaaygaa rpaddpllvg saktnighle gaagiagllk
      361 vvlalkhrtv paslhfeaap peiplgelrl evararrdwp gdgraavagv ssfgmggtnc
      421 hlllteppas sgassttpps plssssplps asvpaiadpc apaapvgpdp favprppspa
      481 tpspttpttp attasatasg tatpgtstpg tearriadae dagapwvvsa rdgaalreqa
      541 rrllplaeda avapgdvals lvrsraifer ravvltpdrp trlaalrala agqphddvvv
      601 gtaangvkgs aargdatgtg ssgevafvfp gqgsqwpgma rellasspvf aarlaecaaa
      661 lapftgfslm dvlqeapgap glervdvvqp alwavmvsla evwrshgvep gvvighsqge
      721 iaaatvagal tladaarvva lrsraiagit grggmlsvaa pldlvrrvia eveapvsvaa
      781 vngprsvvvs gpsdalavla drlsehrakl vpvdyashsa eveevrdevl aalapvrpvs
      841 vattfvstlt gepmdtagld agywyrslrh qvrfaqavet alaggcslfv ecsphpvlvt
      901 gteetaeaag rdvavtgtlr rgeggpervl rslaqaftqg apvdwsgpca tpgarpvdlp
      961 typfqrepcg paivplrpat rvdhaaspgg ravpvaeagg avagsggagg sraearelvl
     1021 gaaarvlghr dpggieagrt fkdlgfdsva avelrdrlra atglrlpagv lfdhptperl
     1081 tdhlhtllas tgtpgtgqaa gtgpvpdapt advptaddpa ddelvavvgm gcrypggvas
     1141 pddlwrlvss gidaigdfpa nrgwdlgalf atgsdrsgts dtrlggflhd adrfdaaffg
     1201 isprealamd pqqrlllevc wetleragld paalrgsatg vfvgamapdy gprldqpdsa
     1261 aeghlltgta lsvvsgrisy llglrgpamt tdtacssslv sivlavqalr rgdcalalag
     1321 gatvmsrpgm fvefsrqggl spdgrckafs aaadgtgwae gagmlllerl sdarrlghpv
     1381 lavirggavn qdgasnglta pngqaqqdvi rlaladarls aadvdvveah gtgtrlgdsi
     1441 eaesliaayg sareghqasg pvwlgslksn ightqaaagv ggvikmvkal ehrtlprtlh
     1501 vdeptphvdw dasgvrllae pvelpdgprp vragvssfgi sgtnahlile sapgagdpgt
     1561 pagddplvwa fsakseaalr aqavrlrgha arlaeeelga agralarrag fahravvvar
     1621 drdellaald alaadaphaa lttgtalddp rpvfvfpgqg sqwagmavdl ldadprfrer
     1681 lehcdralaa ysgwsvvdvl rgadgapple gtdviqpalf avmvslaglw rslgvnpaav
     1741 lghsqgeita acvagvlple eaarvvvlrs rallrlgdrg gmvavslpae raaellgpws
     1801 grlwpavhsg passvvagda daveelvaac pdgvrmrrva vgyaahtphv eelreelltt
     1861 ladvrpgpad tafcssyagd fldtegltae ywftslrnpv lfrqavetva gtgttlfvea
     1921 sphptlvghi qdtlaaaglp ggatgtlrrg dggrqsllra lgqawvlgas ldwtaalgpa
     1981 prhdaglpty pferqrfwld pgpagdssts rhpllgtavp laaddgflla grlsraaapw
     2041 lsdhavdgav llpgtafvel aleaaatagc etvedltlea plylpetgtv haqvavggpd
     2101 aegrrtlavh arpaddpdap wtrhatgllt ptlttptvlp ganaawpppg aepvdlddly
     2161 grlaergydy gpafqglraa wrgdgvayve velpepvrdd aerytlhpal ldaalhlvvl
     2221 eragdpatvl lpfswngvrv taggastlrv rvtdgdgdti slaahdaagr pvgeaaglal
     2281 rrvprtgdaa ragngaasya ldwtpvpvtp adpagqrwav vgvddladei daelaaagig
     2341 apryydlasv admstgeipg lvlapcrgda adlpysahdt lhqaldlvqs wlgderfags
     2401 rlvfvtrpgd aagaavwglv rsaqsehper ftlaelpegf sawdalaggi aagetqlatg
     2461 edgllaprlv rrvpapaspe gpasrdvsae saspeerdgc vlvtggtggl galvarrlve
     2521 rhgvrelvla srrgpdapga ealaaelael gasaqvvacd vsdrralaal lerfpsltgv
     2581 vhtagvldda vveglsaqrl daalapkada awhlheltrd lpltsfvlfs svagllgnpg
     2641 qgnyaaanaf ldalarhrre hglpavsiaw glwdtgahgm agalggadva rlarggiapl
     2701 tveegldlfd lalpgqadpl lvaarwdrag lrdraeagdl ppvlrglvrg srrtvrsaas
     2761 aqpaaagqgl gerlaaltep eahahltalv rshvatvlah sspeqvdvdr afnelgfdsl
     2821 tavelrnrln aetalrlpat lvfdhptvta lagylyrtla pdtpspedal rtavdqaesv
     2881 llaanggada lrgqlvailq salgrigtap aaapaatrsr pggaaeeivt asdeeifali
     2941 dnramtaplk paverpghge
//
LOCUS       WP_357620428             281 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 3-hydroxyacyl-CoA dehydrogenase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357620428
VERSION     WP_357620428.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..281
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=30039
     Region          4..279
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mtvigvigag vmgvgvaqnl aqtghdvvlv dkdeqilada latitrntrm srlmggpald
       61 pdevlsrist svgvagaaka dvvienvten wdvkrevyea ldrecgpdtv fvvntsaipi
      121 tkvgavtgrp dkvigvhfmn pvpakpavel ipgfhtspet iqrtrdllsa mgkkavdvkd
      181 scgfisnrvl mltvneaayl vhegvadaes vdevfrscfg hpmgpletad ligvdtilys
      241 vevlyehyad skyrpcpllk qmtdaglhgr ksgrgfytya q
//
LOCUS       WP_357620442            1566 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: type I polyketide synthase [unclassified Nonomuraea].
ACCESSION   WP_357620442
VERSION     WP_357620442.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1566)
  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 1566)
  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 1566)
  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 1566)
  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 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1566
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..1566
                     /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]"
                     /calculated_mol_wt=167525
     Region          7..1361
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <1450..>1557
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
ORIGIN      
        1 mdqqnpagda diaiigmsgr fpgaadvetf wrnistgves ftrftddeli sagvspatfq
       61 qpnyvrsrpi lddirgfdag ffgynpreat ladpqqrifl ecvwevlesa gyaapegrgs
      121 vgvfagmnis gylltrlraf emgidtsalm igndkdslat nvsfrfdlng pslsvqtfcs
      181 tslvavhlas eslrrgecdm aiaggvsvri pdrigylwee ggqespdghv rtfdaegrgs
      241 mfgdgaavva lkrlpdalad rdtvlavirg sainndgamk fsylapsvdg qrrcvsaaik
      301 ragvdptqis yveahgtate vgdpmevaal trafgatpdk qycllgsikp nvghldrasg
      361 vtglikvvqs lrkelipgtl hyrspnpeid fdnspfrvta eptpwprtge rpriagvssl
      421 gmggtnahvi vteapapepr rprsrrwqil pvsarsaeaa drslarlaer ltdaaddlgd
      481 vaytlqvgrk vfnhrrfvva gtteeaaarl adpaaalgrn datvgrrtgf liagvgeqyp
      541 gmvadlyade pgfradvnec lavlglteaa qlsdvftpae rgaaggdlar mlgraepaap
      601 vstteahlvq pavfvaeyal arqlirwgvt peimvgyslg eyvaaclagv lslpdalrlv
      661 ayraklitsq pegamlavsa derrlrtvlg glyeeeldia vrtgsqtvla gpaeaveaam
      721 avlrelkigh rrletthafh srmlkpiaae ltawisdnvt lnppalpyls nvtgelatae
      781 vvtdpgywar hmcetvefga alekvlgiad lalaeigpgq slgaltrghp acdraqwpli
      841 vttlpgandq qdtgaalata vgrlwltgva vdwaalhedt gwapgrvplp sypfehqeyw
      901 leidesalgg gastpvfdes dptsiakayp rlpdtrwiht pvwrqttlrp pradeaarwl
      961 vytaegvada vaapllahlr atgrevvtvr pgdafssged gitvrpgspe dalavlrela
     1021 asdrvpdrvv hlwcadpdqp aaeclqrglh tlvgfakaag dlglpgwsld ivasggqkvh
     1081 pgdrvvssrg tllgptrlip veyprvttrl vdvdpgdlna gallaelrae padqvvalrg
     1141 ggrwipdyev ldasvieqsp pvaqvrpgga ylvtgglggi glamaerlae qfqarlvllg
     1201 rtpvpprdqw dailasegtv sevrrrlegl rrleaagaev vtvagdvsrv edvrravgaa
     1261 ldrfgelngv vhcagvpavg lmqfktaadi ervlapkvgg tlalaevlrd vpvdflalys
     1321 sttsatggga gqvdycaana fldafalsde lpgvtvtsvd wcewtwngwt dglenydegs
     1381 kqyftwyren fgltfdqgwq tllrvlasge khvvastqdf aplvamsrks sieshqatvk
     1441 kirdafgrhp rpdlstayve pqspteetia gvwaealgle qvgvhdnffe lggnsllgme
     1501 iiaevrrale laylpphily qaptiaslae aaragqepee qpadardqqr sriaqrrtml
     1561 ksgrts
//
LOCUS       WP_357620447             415 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620447
VERSION     WP_357620447.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  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..415
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..415
                     /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=45592
     Region          30..413
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(67,74,104..105,112,116,123,248..249,252,256..257,
                     260,293,298..299,302..303,305,328,355..357,360..361,
                     363..365,369)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(74,98,100,103,105..106,186..187,197,247..248,
                     251..252,256,299,302..304,404)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 myssdqeirn arerammiet lfdedylrdp hpvyarlrae rpvfqtatpq gvrvwvvsry
       61 edvkaactdp rlskdftnnp hlikaneleg gdssgyeavv phnmlfvdpp dharlrrlvg
      121 kvftagrvqa lrprveeisa glldkvgpef dllrdyavpl pamvigellg ipesdwprli
      181 ewsnttiega vldpedvvra avdfttylge lcearraept gdllsalvqa qdeagalsqr
      241 elvdtafllt vaghettvhl icngmlallr hpeqfaalra dpgllpgaie eflrfdgpvs
      301 tstlrftkep vtiggteipq gqlvlvsfls anrdaaqfdd pdrfdvtrap gqhvafghgi
      361 hyclgaplar tegavafghl lerfpglrla vpedrlawrp gllmhgltsl pvsts
//
LOCUS       WP_357620452             196 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357620452
VERSION     WP_357620452.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 196)
  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..196
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..196
                     /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=21460
     Region          9..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mattmgrrer kkaqtrqala daarrlfleh gydkvtvaqi adaadvsiat lfahvpdgke
       61 alifddgaer raglvaavrd rpagqpilaa lrrfmagrgp ftpdmpserr rlrdlivstp
      121 alraysrklw iageeplakv iadetgrdps dmtiralvry vleipdlagt epdpltamna
      181 vfdllesgwp glperf
//
LOCUS       WP_357620458             125 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ester cyclase [unclassified Nonomuraea].
ACCESSION   WP_357620458
VERSION     WP_357620458.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..125
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=13529
     Region          15..117
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mttgvvemtd qvravarrmy eafntrdlda adavfaadfv shplgtigve hvkrawsgmh
       61 smfpgirvdv edmivdgdra avrttlhgvp ggdgqpppam leifhvrdgr iaelwgmstl
      121 srpgr
//
LOCUS       WP_357620465             434 aa            linear   BCT 28-DEC-2024
DEFINITION  phenylacetate--CoA ligase family protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357620465
VERSION     WP_357620465.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 434)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..434
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48167
     Region          21..403
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mrgstfslap vayhlagirr rerlgheaql rlqaqrlral vrhayanvpy yrrtydparv
       61 ealrtahdla gfpvldrmdl hhhgaallad gfteadtrsa ttsgssgipi tirnserdlg
      121 ylratylqdm lssglrptdr iayfrvrpfl rhplerlgvl rnfhvptdrs ldeqvaafla
      181 arptflvgfp nvigsvvdel krrgiaydgv rtvlfggerl tpvarahild yfgaahqevy
      241 acvetftiar acprgslhlr tsdlvveveh ddgtvsvedg rgeilltrlr gqampliryr
      301 lgdrvhitpn dcacgaartp ivrevlgrse driadadgrr yygdfltyvv qdfpevtrmq
      361 liqhrpgaie vvvvptadar hdlttdieqa lrrrapglea tvrtathiap eangkikivk
      421 vhgdpvlsgd sstt
//
LOCUS       WP_357620460             315 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA-guided endonuclease InsQ/TnpB family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357620460
VERSION     WP_357620460.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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 315)
  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..315
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..315
                     /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=34765
     Region          1..>306
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mqlrysyrid ptpaqrialg rafgcartvf ndalrmrnda hegglpfvsd aelsrrvite
       61 akkrpdrawl gevsavvlqq aladcttafr nffasvsgkr rgpklapprf rskkdnrqai
      121 rftrnarfkv taggklllpk igevavrwsr dlpadpssvt vvkdaagryf asfvvevtar
      181 plpvleaeag idlglghfav lsdgtkidsp rllrraekrl kkaqralsrk dkgsknrdka
      241 rhkvarahar vadarrefhh qestrivren qaifvedlav galartrlak svhdagwsal
      301 vnmleytgsh gsaaa
//
LOCUS       WP_357620469             120 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620469
VERSION     WP_357620469.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..120
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..120
                     /product="YybH family protein"
                     /calculated_mol_wt=13551
     Region          5..118
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mefsqaldah lkaieardle aylatvhqda svilpngtll rgkeaiaefh tawfgdpdws
       61 lraetvrvet lgeaafalls veyddldpeg kpyqkvyylt lyftrtdgrw llvhdqntfc
//
LOCUS       WP_357620477             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620477
VERSION     WP_357620477.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32693
     Region          8..286
                     /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 msiarivhrh ldvgdvrvfy reslpdrdda pvllllhgfp sashqfrrli dalgsryrli
       61 apdypgfght qapegftysf drladvmegf vqrlglsrfa myvfdfgapv gfrlaerhpe
      121 wiaglvvqng nayaeglsqg ardfialrpd mpgaektird lltpsgtrfq yesgvadpel
      181 lapdgwsldq hfldlpgrke aqvalafdyh tnvesydrwq awlrrhtppt liawgtgdpf
      241 fpepgarayl rdvpgaelhl fetghfalet hlaeiaplia gfldrvwsek h
//
LOCUS       WP_357620488             315 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357620488
VERSION     WP_357620488.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 315)
  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..315
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..315
                     /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=32897
     Region          53..296
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
     Region          56..88
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          96..131
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mmrsikslga ilaalvlviv mgapagaasd gqpgpggpgr fpgsislpdg fqpegiaigp
       61 gpfafvssma dgsiyradlr tgrgavfshg pgtpslgmki dsrgrlfvag gtggdlrvld
      121 vrtgrvlasy rlttgpafvn dviltqdaaw vtdstnpvly klplrggrlp aaavripltg
      181 dlvyrdgfna ngitptpdgr gllvvqsntg glfrvdrsga trrvnlhges lkegdglllr
      241 grtlyavqnr lnavtvlrln aagtdgrvvr rvtdprfdvp atmaafedrl ylpnarfdtt
      301 ptpttpydav aiprp
//
LOCUS       WP_357620550             122 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620550
VERSION     WP_357620550.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=13276
     Region          6..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrplpepaqe tltlapvlha lgdpvrlelv rrawadpgst csaladgldv pmstlsnhwr
       61 imreagvism avdgrhrrir lrgddlsrrf pglldpilrl aeaesqdgap ssdhpsised
      121 vr
//
LOCUS       WP_357620602             458 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [unclassified
            Nonomuraea].
ACCESSION   WP_357620602
VERSION     WP_357620602.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 458)
  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 458)
  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..458
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..458
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=50811
     Region          6..457
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mgeslvgrhv gfvralreag lpvsvaegld avqalrvidl aereslraay aatmvkrpah
       61 rpgfdvlfdl wfppvmsgpv maggsgdlrp releeasvae lrerlaglvt gggdaelref
      121 arsmverfgr qqagpgrqnw fsysvmrals petlmagilr evlagrergg laertvrqqv
      181 tagvrrfeea vaadvrrria edsgveriar savrppldqv dflratredl allrrevypl
      241 arrlatrlvi rrrrgrrgrl dfrrtvrasl qsggvpltps frpprphrpe lvvlcdasds
      301 vssfahftll ltyalreqfa kvrafgfvdt vdeitrffqp gtdvvdamtr laneadmvrf
      361 grtdygyale rfaerhgdav gprtsllilg darsnyqppa ldtlralagr arhaywlnpe
      421 pkaqwdtgds vasayagvvp myecrnvsql tafiesld
//
LOCUS       WP_357620587             192 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357620587
VERSION     WP_357620587.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..192
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..192
                     /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=20680
     Region          2..192
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mkrseavaea aitllaergm rglthravde taglppgsas nlartraall elalahlvel
       61 eeralapale aglpardrrp sredllellv ealdvqlsda rrtlaryela leatrrpelr
      121 rvydragrrf rdpavallaa lgspdpvrha hqlvaftegv mfdaiagage rpsrddvraa
      181 mrelltgmlg ag
//
LOCUS       WP_357620704             329 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357620704
VERSION     WP_357620704.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=35796
     Region          8..322
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msnavtctyl itggsgfigs hltdallarg davlvlddls tgrlknlrph pnlrfvqgsi
       61 ldevvvdelv hqcdvvvhla aavgvklive qplrslmtni rgseivieaa hryrkkilva
      121 stseiygkns sgplheeadr ilgntgvvrw aystakavde ilanayhher glpavvvrlf
      181 ntvgprqspa ygmviprlvq qaltgvpltv hgdgtqtrcf ahvadvvdal lrllgheaai
      241 gqtfnigsae evsilelakl viehtgstsg vdlipyheay rkgfedmtrr vpdttkirnl
      301 tgwtpqrtld kilmevvrea reelavamr
//
LOCUS       WP_357620724             842 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [unclassified
            Nonomuraea].
ACCESSION   WP_357620724
VERSION     WP_357620724.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 842)
  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..842
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..842
                     /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=86837
     Region          7..256
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(7,31..32,61,66,71..74,86)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(14..15,17..20,22,35,37,69,85..88,92,94,131,133,
                     135..136,138,148..149,152,164..167)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(14..15,17..20,22,35,37,69,85..88,92,133,135..136,
                     138,148..149)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(18,92,94,131,133,135,152,164..167)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Region          <348..628
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <351..>448
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mewsapgyte vkqlgsggsg rvvlavhdet gvrvavkyls ealrrdpeal arfqsearll
       61 vtlrdphiat mweyvqdhdg aaivmelvng vslrallren gttgpeaalt vlkgsllgla
      121 rahrlrlvhk dykpenvivr ddgvsklvdf giavregata rpegtppyma pelwagapas
      181 patdvyavta vffecltghr pyrstepsvl gyqhvyapip vqdapepvre llmrglakdp
      241 adrprgaeaf vaeleetara aygddweerg rrrlaglval lalllpvpet ppaqvstsla
      301 rtvfrgghel grtvaraarh navrlamgag lavvvavaav fvlasrdrll prpidvaaaa
      361 psdsagpael vsppatpvga tesptpepav fppestgpav vvpatsggpt ppatrgrtpt
      421 pppvritrrp tprvtvtppa tqppatrrpt tsppttlppt tppppppttp ppstpppgtp
      481 ppgtpaptpv patsvaalal ggltvnedav aaatvtirat gaapiaatat wavageavht
      541 erlrlsggts ytralshtla erpcgrtvtl tvattpaapg gartatlsvp pcpttvtglr
      601 vsldmspspg tgasarvrvt tsgtgevpvq arfavngdtv gtgtatlagr tsysrsfgqg
      661 frtrpcgatl svtvtaggeq asartrvtcp pgvrrvsivr atvdgrggav svvtvstvnd
      721 rpvrlavtfs aggrqhteql tlsgdtsytr tlshafgelp cgarwavraa trpraagggd
      781 aasgstpecp peeepshgpe pstdppssgp svtpsprpde pttdrpttdr pstdrpapge
      841 pg
//
LOCUS       WP_357620767             276 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TrmH family RNA methyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357620767
VERSION     WP_357620767.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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]"
                     /calculated_mol_wt=29539
     Region          5..271
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mleyvtdaad prladytrlr dvelrkslea erglflaege kvirraigag ypvrsvltar
       61 rwleplsdvl gdalvyvvsd evmegiagfp vhrgalasma rlplpsletv ltgtsgapar
      121 rvlvledlvd hsnvgaifrc aaalgvdgiv lsprcadply rravkvsmga vfsipyarmd
      181 nwytgleqir aagyrtlalt pdqsvtslde vkmtdrvall lgsegdglss rwlaeadeav
      241 cipmssrame agvdslnvva aaaiachglm rsgprl
//
LOCUS       WP_357620798             408 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357620798
VERSION     WP_357620798.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..408
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42368
     Region          27..381
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mvttdrqder lqsrtglrga itdvverarg gdlgvipvvv glvviwtvlq ilnpvflssa
       61 nlvnltlesa avgvialgiv cvllvgeidl svgsvsglsa avlavlfvgq glpvwlaiaa
      121 svimgavigw vyaqlfnrfg vpsfvitlag llaflglqly vlgtrgsinl pfdsglvgfa
      181 qldfvpawls ytfavlaaag lfatgylhar erhraglsak svpmlamrsa allvvllfvv
      241 wylgqtrgvg wmfvffvalv limhyllsrt kwgrsvyavg gnveaarrag invravytsv
      301 fvlcssfaav ggilaaarla aanqssgagd vnlnaiaaav iggtslfggr gtafgallgi
      361 iviqsissgl tllnldssir fvvtgvvlll avvvdsvark srtshgra
//
LOCUS       WP_357620865             448 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620865
VERSION     WP_357620865.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 448)
  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..448
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=45503
     Region          172..376
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msgsrlarvl agvalgmalg lvelaflcva wigrllpaar pvveaargkl maaerarlsr
       61 wlghettrqd ggygflvara algvlsgygc aaglfvggll lfgglwdlaw grmepvpvnl
      121 pgvkivtssg vlgltggavl lalvalmala vgslerrlad rflgpgshel mrrriaelta
      181 trsgivravd derrrierdl hdgvqqrgva lamllgrarh ssdtettagl isqaytesrr
      241 lldelrsvaw riyptaldel glraalagva ersgvpvtvh yglaerpvse vetalyfvar
      301 eaitnaikha gardilvvlt ederavgvai sddgeggadp sggglsglar rvlaldgefa
      361 vhsprggptk itatlpkipp ggfpgatsgt asgaasgtas gassgttsga asgtvpgaaf
      421 gtasgaasgt aaeaarldas gteagpcg
//
LOCUS       WP_357620851             236 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357620851
VERSION     WP_357620851.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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 18603527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..236
                     /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=26347
     Region          35..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"
     Region          <96..187
                     /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 mqpaagdeal enhlggdeak nyrqyeldmv aphvgrsmle igsglghfae qflprldrlv
       61 vsdfdpycve qlrkrfagrd didvlqfglp teiplkekvd tvvmmnvleh ieedaealrs
      121 larvtlpggr iiiwvpgymq lygdfdrkvg hvqrytpktl rstvakagld vdvlkpinfl
      181 ggiawwaavr rggvgypdpr lvkiydrtvv patrfierfv tppfgqtvfc varvpg
//
LOCUS       WP_357620912             230 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: esterase/lipase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357620912
VERSION     WP_357620912.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..230
                     /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=23335
     Region          40..136
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 maglllrtgv valaaalstg lgtglgtgmg satamtrsvp epvilvhgwn gtpdafapmk
       61 taleqaghpt yaidlpgeen vanasaiaal veqvrqthga dkvslvghsm gglsarhylk
      121 slggaaktlg yvsmgtgqrg ywpacllpta qggqmcptst fmrqlnsgdp tpgavrytvl
      181 assldetrad tidgvactae lpgvqhadep gnqlfidavl tvldgrcpap
//
LOCUS       WP_357620921             342 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620921
VERSION     WP_357620921.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 342)
  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 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   3  (residues 1 to 342)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..342
                     /product="GlxA 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=36830
     Region          10..329
                     /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 maafagdgrh rvavlardkv lsfelsivhr ifgqarsaag aalyevvtca pepgeihtda
       61 dftvtvthgp ealaeadtvi vpasqddfep rseplepslt aalariqpgt riasictgsf
      121 vlaaagllag rratthwrss arfrerfpdv vfdhdllytd ddgvltsagg asgidlclhm
      181 irtdygaava ndvargsvvp phreggqaqy vqrpmpdpri sstskarrwa lanlhrpitl
      241 relaaqests trtftrrfre eigtspgrwl trqrieracs llertdlpid evavtagfgt
      301 agsmrlhlqa elgvspsayr atfrgpgpam frghdghsvr ss
//
LOCUS       WP_357620922             127 aa            linear   BCT 28-DEC-2024
DEFINITION  RidA family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620922
VERSION     WP_357620922.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..127
                     /product="RidA family protein"
                     /calculated_mol_wt=13116
     Region          1..126
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mtrtvitten apvlpaplsq gvrkgpvlqi sgqlpfdpat gevagatvaa qtaqalrnvl
       61 avlqaagagw edvvmlrvyl tdpahlaemn qayaaavgep fparttvymp lppgllvevd
      121 alamled
//
LOCUS       WP_357620925             491 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620925
VERSION     WP_357620925.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 491)
  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   2  (residues 1 to 491)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..491
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51057
     Region          3..487
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mnlvttaqga vrglrrgatr tflnipyaap prgagrfapp mphepwdgvr datvpgpnap
       61 qserrlgsvd mspyfgagws rgedyltvnv ftpadgggal pvmvfvhggg fvagstrssm
      121 ydgsafardg vvlvtlnyrl giagfldlag apanrglldv vaalrwvren iaafggdpan
      181 vtlfgqsaga tvvggvlatp eaaglfrrai vqsgsglgaf taeqaarvtv aaaealgvep
      241 haaafadvsd erlvevasgl agldlrteth hdpliglspf slvlgtqpae avaaglsagv
      301 dllvgtntee gnlylvpvgk yatstaadve eaaarshpnp arlvetyres rpgassaelr
      361 saimgdalfg agsralagah aahagsatya yefawrsral dgelgathav elpfvfdlad
      421 rpelngpnal lgpgeapasl atrvheswir fartgdpgwd pydtgrratm ridtewtqvd
      481 dprpqerevw s
//
LOCUS       WP_357620931             932 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357620931
VERSION     WP_357620931.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 932)
  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 932)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 932)
  AUTHORS   Rosinski,J.A. 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 932)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..932
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..932
                     /product="helix-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=98959
     Region          <18..882
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          860..913
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 meiggttqgs tydlelsmvg reteaaeivr rvaagrtrge vliltgdpga gktvlldfaa
       61 drarddgarv lravgsesea rlgfaglhql lrpvlgelag lpprqrsalr tvlgldecde
      121 apdgvlvgsa vltlvsdlae papllvvvdd aqwidrasld vlsfvarrld sepvtllvgv
      181 raatalpgld kgydrleigp lsgeaagrll drqpapptgr trvrilqeaa gnplalvela
      241 ragatrrpgg sgvegplpvt drlerifaeq aqflpeatrr pllllaaada tdaptasrgl
      301 peagdpawvp aeraglvrqd gpwisfrnpl irsavyhaas feerrqahla laklseepdr
      361 rawhlaaatt rpdeevsaal rrtadrarrr gghaaaaaal eraaelsprr adqarlltea
      421 agmavftgql gwverladqv rkhsddpali sraslaagql mtlrrhhaaa fallariage
      481 eaathppral ealaaaavvr yysgeesqrq qiadllpdst aapptmsdaa vlrawvlavs
      541 dpngagarla palpgliaea kgdaagltal avvawildet alaartfdea sdrwqargpl
      601 pdglacavgw tyldqgrwae arsvaaevsa vasaagleha eacahaldat vfallgdtdg
      661 arrgagrala lvdplesrsi avsarralgl aavaegnydt ayaqfraaft ddgdpvhyhv
      721 sstvlaelaa aavrrgrree aaellersar rlstggsari aalldrgral laepddaepy
      781 fraaladdmg eqwpferaqt rldygewlrr qrriaearpl ltaahdtfqr lgarpwiera
      841 kaelraagie aagsvvpsal telspqqqqi vqlaargltn reigdklyls prtvgshlyr
      901 vfpklgitar sqlrdvvega lptsgqhdrv pa
//
LOCUS       WP_357620974             144 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357620974
VERSION     WP_357620974.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 144)
  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 144)
  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..144
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..144
                     /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=15759
     Region          9..132
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mmdesqrhya ayvlfnqama drlqihstdl qcmgllglqs rpvstgeiar ltgltpgsat
       61 rmvdrlekag lvvrqpdpad rrralvtltp larerigaaw dipgkafaev lekyddaela
      121 viadylhraa eagraqadrl tkes
//
LOCUS       WP_357620991             164 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357620991
VERSION     WP_357620991.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 164)
  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..164
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..164
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17935
     Region          8..>67
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 malpkvgsig eyireqrtqa kislrqlaaa agvsnpylsq ierglrkpsa eilnqiakgl
       61 hisaqalyvq agliedretp sdvvtairad thlterqrqv lidiyesfrk ekragdeqts
      121 qkahprsdsv tddeqplpee llaalepyaa stdngtvtqe tkeg
//
LOCUS       WP_357621056             183 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Nonomuraea].
ACCESSION   WP_357621056
VERSION     WP_357621056.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 183)
  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..183
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..183
                     /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=20193
     Region          7..179
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdcldpvqka llddldagfa elygayrdvv fstalrlsgr wadaedltae tflrayrala
       61 gydrervaal rtrpwlltil mniwrncara ksrkpppdlr eepvdavdpr egvedaavrr
      121 etgeelagll allpdeqraa vvlrhvadlp vseiatvlri pqgtvkshvs rglkrlralg
      181 gar
//
LOCUS       WP_357621076             333 aa            linear   BCT 28-DEC-2024
DEFINITION  LacI family DNA-binding transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357621076
VERSION     WP_357621076.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..333
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34902
     Region          4..332
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 malvsikdva ahagvspgtv snvlnrpgkv apatrervea aiselgfvrh gsastlragh
       61 srtiglsvid ignpffteva agvedvasel gyavilgnsa gsqdkedrnl rvlaehrvrg
      121 vlitpsgedp grldrlrerg isvvlvdhpa hrpdqcavav ddvaggraav thllakgars
      181 vayvtgplti rqcverrega kgamraagld pddlkvaeaa tmtarageka aadliagglp
      241 eavfcandll algvlrallr agvrvpedva lmgyddidfa aastvslssm rqptyqlgri
      301 atellldecd npdthahqhi mfqpeliare stq
//
LOCUS       WP_357621093             256 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357621093
VERSION     WP_357621093.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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]"
                     /calculated_mol_wt=27981
     Region          37..137
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mpgysdlvdq avrasirgwd fswlrgrttg gkpswayter asvllstarr vldmdtggge
       61 vlaslaplph htvamegwqp nlpiaakrlg pmnvtllggt adripareat fdlvlnrhgg
      121 ldavevarvl aaggrlltqq vgsrngleln lalgappsad peswtlaiav eqlhncgmlv
      181 ldareemvdh tfhdigaivf qlravpwqvp gfdhdryekp lralherirs egaftvhdhr
      241 ffieaelprt rsrgpl
//
LOCUS       WP_357621109            1246 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357621109
VERSION     WP_357621109.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1246)
  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 1246)
  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 17582184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1246
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..1246
                     /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=131265
     Region          131..573
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
     Region          <801..>887
                     /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            858..860
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:238300"
ORIGIN      
        1 mgrwgaaavs mvmvasvlaa pgahaatvqp gsftnapasd eitlitgdqv qvravdgehr
       61 avtvtpaqra dgsvptfqvl esesgvtvip ddvaalvper ldtalfnvta laeqgfglqa
      121 sgsiplilty agnatkaaip aakqvrtles iggaavqvpa rdaarfgael aelgsapdlr
      181 aagplagvak iwldrkvkpa leqsvpqiga peawaagydg tgttvavldt gvdathpdla
      241 gkvadqrdft gqsvtgdphg hgthvastia gtgadgigkg vapgarllsg rvldadgygq
      301 lswiidgmew aagekhaeiv nmslgsrepg gplteaatrl srqygtlfvv aagndgcdqc
      361 vgapgdapea ltvgavdkqd qlapfssrgp iiadlavkpd vtapgvdita artgggsltl
      421 sgtsmatphv agaaallrqa rpgiagnelk sllmasakpg qdidvdaqga grvdvaaalk
      481 etvvastgsa gfgklttgeq ksrtvgyhnl gqapaelsls tgdaftveps kltvpaggta
      541 evkvtaradk agllreelta avtggatvrt lltgsvddkr velrirgiar dgrtarggft
      601 vlnldegtlv grllpgdpaq pcsdqkygsg tcllvkpgty svlghiftmp atqdsttsgk
      661 plneslvgdp emeitgntev vldarkavev kvetpdhttk rntgaaaalm wyrssktdta
      721 lrggttispg gqieerlfvq ptrkvtkgtf tvatrwrlta peitlstpgl eldpqyvdpi
      781 qfsdfateyp rldgtrllma vdagrgsaee ikardlrgkl avirrtegvp vstqsnaaaa
      841 agarmvavys dqpgadvttg gnrvklavpt vrltheeglk lvqrlrhlpv pvlaegivas
      901 pyvydlylre kgrvrdslty tvrskslari etgyhsqlsd gvtvnesrfv fepwdtssis
      961 tnhpmaktpr trtdyvtpdp elrwsssagt persynnmwp hpdtarisms spefrpyevg
     1021 ervsrtlfkq pllpginprn plrrdgdrlr vsmqgfvdad rnygdaytsq fehglktdfr
     1081 lyqgdtllwq tnylpsgsgt lspekatyri eyavaneadw vklstrtkav wtfgserata
     1141 ttvvplllas fdapvdlrnq agsrrlglsl yqqegaaqsa vkdvslevsy ddgatwtkar
     1201 lrakgersye ttlgrspsgf vslrlnasdv ngstlsqevi rayalr
//
LOCUS       WP_357621173              72 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357621173
VERSION     WP_357621173.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 72)
  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 72)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 72)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..72
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7215
     Region          3..72
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 matttatytv kgmtcghcvs svkeevgevp gvtgvevdla sglltvgseq pieperivsa
       61 veeagytves as
//
LOCUS       WP_357621187             165 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357621187
VERSION     WP_357621187.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=17734
     Region          17..156
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mgdavdvilg qwartrpdvd vspmgvigrv srasrllerg vkeclaehgl eawefdmlat
       61 llrsdaasma mkdlsaaamv spgaltnrmd hlvarglvdr wpapdnrrmt lvaltdegrr
      121 vagdvlerha anqdrllsgl sradrdalag llrnllislg dtgpe
//
LOCUS       WP_357621293             410 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            sediminicola].
ACCESSION   WP_357621293
VERSION     WP_357621293.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 410)
  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 410)
  AUTHORS   Rosinski,J.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..410
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..410
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44770
     Region          18..91
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          139..>365
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
ORIGIN      
        1 maqtprrltp hrsalhgfga alrqwrecrg lsqralgrlv hvsgdligkv ekaerwpsar
       61 fvescegalq tdgelarfls dleserrlts vgyrladgae gqlrasidhp dkpdllrswh
      121 ellaglaiag nrtgyagmas tahaqisvaa airrrsrsad rrdvliaqal waeflswide
      181 qsdaaeadaw lrraqqhaie adaptltsyv lmrqsqrale rfdprnaial aqraleevrl
      241 pgrirallli rqaqayamgg dqnacaasid kahrvagsad wgselpidvg vhcdlvyvaa
      301 heaqcrlllg qpaaaadlye qllrhwpaqw rvdealwrsa lstayvsigd veraateatn
      361 alalatgtss gralrwlnpt avalrqqpav peaaafvlay rqatleacnh
//
LOCUS       WP_357621299             609 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Micromonospora sediminicola].
ACCESSION   WP_357621299
VERSION     WP_357621299.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..609
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..609
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=64441
     Region          194..334
                     /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          357..577
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrlgdrvaev svddavrasv sydqlrigdd glfwletrpd agggttvtqw rsgegkrdvs
       61 pkgfdvasgv haygggsfav aegtlwcvgg dglyrsrrrg delelvahgs fgdltvgage
      121 llavresdqg delvavtltg vppmrtlavs rgflgaprpg pgrlawtaws erdmpwdace
      181 vwvasysprg vienpvklag gpdesaaepq wgpdgalyfv sdrtgwwnly rwdgfkveav
      241 apiagecaae pwelgyasyg flddgrivva vqegprhrlv viepdgvvrp velpytsikp
      301 ylavrgttva migssptaap qvalvdlagt dpevevlarp edaglegvgv stptelrvrv
      361 angrevlalv ypptgaaadw qapvvvrahp gptascllrl dwqaqfftsr gfavvdvdyl
      421 gstgygrvfr eslygrwgld dvgdcaavag hllstgravp gqvfirgasa ggytalhava
      481 qdgpfaaata vsaivdpdrw aqtvprfqqa hakrlrggag rvraaavqrp vllihgtade
      541 vavvedvrdl aeeltslgma pevllladvg hyvasshrag aaleaelahy rsamadaand
      601 qralhsgqr
//
LOCUS       WP_357621304             958 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Nonomuraea].
ACCESSION   WP_357621304
VERSION     WP_357621304.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..958
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..958
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=104697
     Region          <3..956
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mledmlgrsv spvfvgraee latlsqafae arqgnatavl lggeagvgkt rlaqrfaeqv
       61 trdgalilyg gcvelsaegl ayapftaalr qlvreqgrar vaallpegae rdlarllpef
      121 gepsgdgdtd tgrarlfeqi ltllerlaes rptvlliedi hwadrssrdl iaflcrnlsa
      181 pqvlivmtyr sddlhrqhpl rpvlaelgrv ngvlrldlpr lskdevaqqm agilgqspay
      241 hkvekvydrs egiplfveal ldcgvdcafp tsmqdlilga verlpeetqr vlriaaaggi
      301 rvghallaav sglsdveles alrpaiagnv lqiadnrayl frhslireav hdellpgehq
      361 rlharyaeei srdrtlvppg raevelahhw ygarddewal vsaweaaras fhafayteai
      421 pllervlmlw drvpdaqeri gadhtavleq ageaarasgd ldrglkfvka alaeldetre
      481 parvarltvr waqlksykqv tdvveqlrha lrlvpeptsa rvdvivmmsq hlmlrgnaee
      541 gtalteegla larklgdrcq eaelllnlal ghslagdtea tlatnlrale igreegsgrv
      601 itralgnnid tlndlgrwqe alalgeegwr qakkygrvrl sglfsllnma etleaigrwd
      661 ealdtverai nlgpvlrnry hllrvradva igrgevdlve silretgvlt erpedfvqdi
      721 tnsmrlrigw hllrgepdaa lavaertlar paqspkamlg wrllallsvv cdamqeaepv
      781 raravreqaa eiaarlkvsg pvagayrlsy srdfdaaaaa werlnrphnq akahlraagv
      841 aarsgdrdga asrlalarpl aaelraapll eeidalarrv gvpqpqqpaq mtpelltpre
      901 levlrlvalg rtnrdiagel fisaktvsvh vsnilaklgv ttrgeaaaaa hrlsllsl
//
LOCUS       WP_357621360             215 aa            linear   BCT 28-DEC-2024
DEFINITION  FMN-dependent NADH-azoreductase [Micromonospora sediminicola].
ACCESSION   WP_357621360
VERSION     WP_357621360.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 215)
  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..215
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..215
                     /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=22560
     Region          1..207
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mahllhidss itgersvsrr ltaraaaawr aahpggtvty rdlgqspvph ldaagglarm
       61 vppeqhtpeq raswqlteel vgevtradti llglplynyg apsvvkswvd hliapgiayd
      121 patgagllgg refvvlvsrg ggygagtpke gwdhaapwlp hgismtglep rfisaeltla
      181 pvnpamaeli plheqslasa eravdelwvp aaaaa
//
LOCUS       WP_357621403             167 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357621403
VERSION     WP_357621403.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..167
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18438
     Region          3..103
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 meprsgcpin aavevlgdrw sllvlrdvif gdrryfrall tgsiegiasn iladrlvrlv
       61 eagilargta argqrarysl teagiqtlpi iyalgnwgld wrpgsdelrs rqqlmrdegp
      121 afieelmdel rvrhlgappr phegpgpfer ldaayaaaae qehaeqr
//
LOCUS       WP_357621574             465 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357621574
VERSION     WP_357621574.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 465)
  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 465)
  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 465)
  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 465)
  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 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   6  (residues 1 to 465)
  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..465
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..465
                     /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=49896
     Region          128..448
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 myrrlvfmva flacgfavpv gmetavqesr elfvlatrnt geiaalaesa laardlttlr
       61 rwldgrarac gcavfildhr gmlvvaagld lvpgaggdqa vtpasdamag rapvpphviw
      121 lwdrrpfvlg avirhdgrpl gaavtmwptd darsavavrl lllaavvglt vlaaatlvig
      181 plarwvmtpv rllgdateqv gsgyvrvpet agppevrrla cgfndmadrv lalatrqrdf
      241 vaqashqlrn pitalrlrve nafelgsapy esedlklaln evdrlcaivd sllllaksen
      301 neelpvvvdv satvvqrvda wrsaydrnsv plitnipdgv ralclpelie hgldalldna
      361 lkfgeqcpvr vvvqrrgdmi dvvvrdqgpg lpaeelefvg trfwrstrhq nlpgtglgla
      421 iirrlakasg gqvimaasrp hglevrlrvs aapagmgtpd ghalr
//
LOCUS       WP_357621601             428 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357621601
VERSION     WP_357621601.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 428)
  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..428
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..428
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45728
     Region          2..416
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpatphlrrt vlpsglrvit ertpgrhaaa fgvwaatgsr depeechgas hflehvvfkg
       61 tgrrtgeria aemdatgges navtakehta yfakvlhedl plaadlicdm vvdpalngid
      121 veteravlln elamqrddpl qaaqqelayl lfaderlarp aggaeatvga mkrdfvaafh
      181 aehyvpeklv vvatgdvdhd rivelaaagl lrrfgdrrrd pvppregpgs vtdrpgrcrv
      241 lprsvelasl magvpaishl hparyamavl staigggiss rlfvelrerr glayalgsha
      301 qaysdagafa vhgvcrpadv pafleclrte ldriardgls eeeverakrr trgrlalgla
      361 dplaratala qgelsgqapm tvgdlvhkvg ettgeevrdl asqlfsapls lavagpfpnd
      421 rdflsagn
//
LOCUS       WP_357621581             493 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NuoI/complex I 23 kDa subunit family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357621581
VERSION     WP_357621581.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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 493)
  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..493
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..493
                     /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=50881
     Region          1..138
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
     Region          <122..493
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mlrksvtqqy pevkpalppr srgvialvee nctscmlcar ecpdwciyid shketlpape
       61 ggrprqrnvl drfaidfslc mycgicievc pfdalfwspe feyaegdirn llhekdrlaa
      121 wvptvppppa hdpgaeppke laaaprrpag prpggaggrp gaaapeqpst srttprtapr
      181 ttpedpaass gtppegpsas rtteaappst gdgtpsgeda sartasaeda sartasaeda
      241 sartasapda sttgspdvrp pedprsapda rppaprgrrs agepdareat tgprpsdpta
      301 qdapgtqdap gtraadrsaa gpdrpgqaer rarmanirgi rppgalpasp atgdkpgttp
      361 pagdkpgttp pasearnpkt peagarspea pqdgvspapg tddpapatdd adsvpgeaap
      421 assetgaepa gelstgstsg eelstasgep rpnpeaeeqt saprprrrrm adprsirppg
      481 rldpadprep eee
//
LOCUS       WP_357621619             583 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora sediminicola].
ACCESSION   WP_357621619
VERSION     WP_357621619.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 583)
  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 583)
  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..583
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..583
                     /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=60973
     Region          1..450
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          516..582
                     /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(539,548..550,557)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            549
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvirac rdaglasvav yadsdrdalh atladeayal ggdtaadsyl
       61 ridklidvaa ragadavhpg ygflsenadf aqavldaglt wigptpqair dlgdkvtarh
      121 iaqragaplv pgtpdpvgna devmafavdh glpvaikaaf ggggrglkva rtmeeiphlf
      181 esatreavaa fgrgecfver yldqprhvea qvladqhgnv ivvgtrdcsl qrrhqklvee
      241 apapfltdaq raqihdsaka icreagyhga gtveylvgvd gtisflevnt rlqvehpvte
      301 etagidlvre qfriadgekl ritedptprg haiefringe dpgrnflpap gtvtalrlps
      361 gpgvrvdtgi sagdviggnf dsllakviiv getrtealer arraldemvv egmatalpfh
      421 rlvvrdeaft aepftvhtrw ietefdntvp aftaaagaae apaeretvvv evggkrlevv
      481 lpaglgagta aaapaakkpa rrggggkaga avsgdtltsp mqgtivkiav adgdtvaegd
      541 lvvvleamkm eqplhahkag tvrglaaevg avitsgaaic tia
//
LOCUS       WP_357621630             388 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357621630
VERSION     WP_357621630.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..388
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..388
                     /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=40877
     Region          8..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 mtsgesvpse qpgrlggldg irglaalfvv lhhcrllsfp gfpadtgpaw aswllyghfa
       61 vvvfitlsgf slavsparsg wrlgglgrfa rrrawrilpp ywaalvfsla vawalvpqpg
      121 qgaptaksvv fhgllvqdlf gspspngafw siaieaqlyf alpllllvvr rlgavvmvaa
      181 vtvvvvavgl lsdavpavgt lmrltpqfav lfaagvlaag vlrapvrapv laalpwaalg
      241 avvpvavlva vqgpvwtvah ffwvdlalap aaglllaava ggrprplvrl ldsrpirslg
      301 sfsyslylvh apvvvvlhhf vvaprfepgv trflvllala vpvsvvfarg faalfelpfq
      361 rhrgtaallt avrerltrar pvpeapge
//
LOCUS       WP_357621656             192 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: dTDP-4-dehydrorhamnose 3,5-epimerase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357621656
VERSION     WP_357621656.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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..192
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..192
                     /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=20363
     Region          3..172
                     /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 mdplsvegaw lhtprvhadl rgsffeafrt aglphpmepa qvncsvshrg vvrgvhfaav
       61 ppgqakyvmc vagavldvvv dlrvgspgfg rwdavrmdde srravliaeg lghafmalse
      121 ratvvylcsq pynpggehgv hpfdpalgia wpegvepvls dkdaaaptlg earaagllpg
      181 yeecakfyat lh
//
LOCUS       WP_357621681             163 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357621681
VERSION     WP_357621681.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 163)
  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 163)
  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 163)
  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 163)
  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..163
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..163
                     /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=18072
     Region          6..163
                     /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 mlitnirlre wreddapavl aafqdpdlsr qapwpvvtvr dalgwiaawd gvghafavtl
       61 dgrvvgnvav ariddhangw vsywtvrear grgvasaave elarwafrer glfrlelghr
      121 vdnpascrva tkagflaegi ergklrydgv rydverharl atd
//
LOCUS       WP_357621713             164 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357621713
VERSION     WP_357621713.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 164)
  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 164)
  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..164
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..164
                     /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=17837
     Region          7..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maesrapeet aagrpdlaam maplsralva aelpvlrahg lsmwayvvll alsrqpvrsq
       61 salaqaigad ktriigvldg lqerglierr adpadrrthl lsltaegrrv rdaaqagiqr
      121 qedrllarlp aedrdaflra lqtlsalpre eivgngarrp rrsr
//
LOCUS       WP_357621734             281 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: phosphotransferase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357621734
VERSION     WP_357621734.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..281
                     /product="phosphotransferase 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=30450
     Region          6..251
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mrghvpddll emadallpga pldaarlarg gihdvvllpg vaavrvsrrp agaealprrt
       61 evlrliaaag ppfavpeplt pvrmfgdraa vavswidgag lgegegdpgr igellravre
      121 lpvtpelrav lpaprehhgs dnwasilaee viplfpakwr gegrrrleea lalepvpdsl
      181 vhgdlvgsni hwsengklig vldwdrahlf dpaidaafma whgwdnlrqa vdaetyhrac
      241 vwertfgvdh lvavlelsgr plahvesyvr htvawleqha g
//
LOCUS       WP_357621831             458 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora sediminicola].
ACCESSION   WP_357621831
VERSION     WP_357621831.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..458
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..458
                     /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=49066
     Region          27..411
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mgyqdlsywl ssldepltpr aglpgdtdad vaivgagytg lwtafylaea dptlrivvle
       61 reiagygasg rnggwcsalf ptslpalarr hgrdralamq ramhdtvrev grvvaaegvd
      121 cdwraggtvv lartgpqldr araavaeaha ygltdddlvl ldaaeaaarc aadgvrggty
      181 tphcaavhpa klvrglarav errgvrlher tpvtalrpgt avtpagvvra pvvvrategf
      241 tpalpghrrs vapvyslmva tpplpeetwa riglaeretf sdhrhvivyg qrtadgrlaf
      301 ggrgapyhyg srvrpdfdre prvfaalrra lgelfpvlgp dvpvthawgg plgvardwaa
      361 svgldrrtgl awaggyvgdg vgtsnlagrt ladlitgres dltalpwvgh rsprwepepl
      421 rwlamnaglr vmssadetel rthrparraa lfsrflgh
//
LOCUS       WP_357621770             291 aa            linear   BCT 28-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357621770
VERSION     WP_357621770.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 291)
  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 291)
  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 291)
  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..291
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..291
                     /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=31260
     Region          29..205
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 mtsnasvwtt gqqqsrtqrl grylpesmkh pgkmlpsiaa qvidaytepg elvidpmcgi
       61 gttlveaihl grhaagmeye edwaklavan laharrqgat gfgtviagda rgiarllpdl
      121 vgraalvlts ppygaathgh iratrdsgep girkwnqrys rdranlahqg lpvlldgfaq
      181 ilsgcgellr pggvvavtvr pyrhrgelvd lpghvqkvaq raglnfadri vcllcglgrg
      241 kllnrasffq lyearkgrar glpihatahe dlliftkprs lktasaipka a
//
LOCUS       WP_357621815             354 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family transcriptional regulator [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357621815
VERSION     WP_357621815.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  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 354)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 354)
  AUTHORS   Rosinski,J.A. 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 354)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..354
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..354
                     /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=36572
     Region          95..150
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 mtaigaaagm srvaagkiln elerngrarr tagghdgrgr tpdrwypaet ddpadtpepv
       61 ehadltdpae aspmavttdd sdavtssdat edtagldahq eavlavlesn pswsaaaigv
      121 aagltragai kvldqlvaag lasrgdeedr tkdewyqasd eptahdeala vdgelpstts
      181 tgdpaadvda speesaeepe sdpenparae acaellelad lilgtvhamd segnavlalg
      241 rlemamakip qahrnaravl tgttaparsv pgrsgsrsgg sagqvrpgal rdrvlshlte
      301 hpgkdftpye igrvlnassg avanaldrlv slgqaqltce rprrfslaet sape
//
LOCUS       WP_357621920             385 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357621920
VERSION     WP_357621920.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=39918
     Region          <185..379
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 malprpavrr vaavwrflrr ppvldaalvl alvaaaclgl vavvlqgdrd aaagaahfmv
       61 ttvpllvrrr hpvaatalva vldltglatg viegasastv ialysvgryt ggrpavlvtt
      121 aativynvav aiavdgpsav lptaflffap mgvgqfvrvr aqlrerdqte aaeaavraer
      181 rriarelhdv vahhlsvina lvggaratlp pghdvtrdal ssaegtarqa laemrqllyv
      241 lragdgdgsd aatgvgadrl palvdearta glpaeltvtg tavplpaavd havyrivqea
      301 ltntrkhapg ararvllaye pdaveveald dgaagaqtdr ppgfglggma ervalcggel
      361 raghrpeggf rvhariplei pleqe
//
LOCUS       WP_357621943              72 aa            linear   BCT 28-DEC-2024
DEFINITION  RICIN domain-containing protein [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357621943
VERSION     WP_357621943.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..72
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7779
     Region          <38..>72
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(46..47,59,61,68..69)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mklaarvfst tlalllagtg tasaepakaa lsvrhfynvr fqrcldadtn tggnggivql
       61 wdcgpwnqqw wr
//
LOCUS       WP_357621972             314 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357621972
VERSION     WP_357621972.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=35280
     Region          19..311
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mldtsarllr llsllqarpd wsgadlaerl gvaprtvrrd vdrlrslgyp vrstpgvagg
       61 yrlgagaelp plllddeeav avavglrtaa ngtvtgieet slralakleq vlparlrhrv
      121 ntlqrhtvri nregptvdad vltrvaaacr dheqlrfdyt ghqgesalrr aephslvtkg
      181 nrwylvgwdv drrdwrtyra drmrlrtpng prftpreppe pdvaawvqhr lahqmwpfea
      241 rfllhapaer ladrtpgtve pvdertcllt lrgddlrlma vavafldvef evlepvelke
      301 hlralgerll ssri
//
LOCUS       WP_357621979             287 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357621979
VERSION     WP_357621979.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 287)
  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..287
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..287
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32533
     Region          14..76
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(20,24,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(23,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(30..31,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..280
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mssqqgsptv rrlrlgqelr llrerhkltg aaaarelgws pskvsrieaa ktmpsaedie
       61 smaklyrvae akldelfgll rdadqrgwwe dyedslpgey trflgleaea vcqrnwepqi
      121 vpgllqtedy arevisaprs ivrithsgvr srvearmdrq qrvlhrpepp darfvldesv
      181 lmrkfgdpsv mqaqmehlle asllphvsir vltmeslhpv ntggfvhlkf agfddvvyle
      241 qlyagsfved lgrvagyeaa feylgaeald edesrvliqr kamlwrn
//
LOCUS       WP_357621990             650 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Micromonospora sediminicola].
ACCESSION   WP_357621990
VERSION     WP_357621990.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 650)
  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 650)
  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..650
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..650
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=72005
     Region          292..650
                     /region_name="COG4867"
                     /note="Uncharacterized conserved protein, contains von
                     Willebrand factor type A (vWFA) domain [Function unknown]"
                     /db_xref="CDD:443895"
ORIGIN      
        1 magnrfrygq wrggpdplap pydvraavda vgaevlaggs lreslrdllr rgpqgrggld
       61 dlaararrlr realrrgdld gavtrarall dqaiaaerde lrgrdgddar faeavldnlp
      121 gstaravael egyewasaea rqtyqrildg lrgevleqrf aglrdaaraa adpaaqrqla
      181 emmrdlndll arharsedtt dafaefmrrh geffperprd vdelvdvlar raaagerlmr
      241 slsdrqreel aglmrqslgd rlagelsqld ehlrslrpdl nwrrgervrg dqplgygeaa
      301 galdeiaeld elldsldqdq agatlddvdv eavartlgre aaddvrrlre lerelrrqgw
      361 vtrdaegltl spkalrrlag talrrvfadl tagprgqhdl rsagaagevs ggsrpweygd
      421 eqpldvvrtl travrrsgtg vpvrlavedf evmeterras aavvlcvdls ysmisqgrwg
      481 pmkqtalals hlmatrfpqd alqivgfgre ampltqqela avepdmqqgt nlqhalrlag
      541 rhlrrhpgae pvvlvvtdge ptahldpedg eayfhwpplp etitatirev dkltrygval
      601 nlfmlgddpg lrrfvdavar rsrgrmftpd lddlgeyvvs dylrarhgrr
//
LOCUS       WP_357622031             390 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora sediminicola].
ACCESSION   WP_357622031
VERSION     WP_357622031.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 390)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..390
                     /product="phosphotransferase 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=41706
     Region          <174..331
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msrtvtvilv daagrsigal ppfdvpdpww qqvdsvvdga rrrhgvevav lrlldadrpa
       61 ppgghvryla qvadagavpl epvavdlaph plrmpwaeag gpadsvawat delrrlgrpv
      121 tavaqqrtwn lsaiwrldtp lgpawlkqlp pfarhepavl hwllstseag grvevlavgg
      181 egrvlmghvp gedrygageg ermaiaaghh avqvravgev drlvavgvpd lrgaglgrwi
      241 rerlaghdvt aagrlldgld drlarvrdcg lpdtlvhgdl hpgnvrgdes rrvvidwada
      301 fvghpafdil rltedlapaa tdrlvatwad rwradapgsd prravdllrp vaplrlaavy
      361 amflagieps ehpyhvhdvp aalaraaaaa
//
LOCUS       WP_357622051             198 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357622051
VERSION     WP_357622051.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=21488
     Region          6..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          102..179
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(107,109,122,125,129,163,165,177)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mdeavdrtld avgprlkrlr lhrdvtladl aaetgistst lsrleaglrr ptleqllpla
       61 raygvtldel vdapptgdpr inlrpipcgd gsiilpltrr pggiqaykfv lpagkddtep
      121 dlrthegydw vyvlngtlrl vlgehdlilk pgeaaefdtr tphwfgatsa gpveylslig
      181 kqgerahvra aprhgpae
//
LOCUS       WP_357622073             440 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            sediminicola].
ACCESSION   WP_357622073
VERSION     WP_357622073.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 440)
  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..440
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..440
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47370
     Region          18..100
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpesfwehep vrqalasrhl grvirayryh pyhgrnampq svvagwlgit qaqlsrieng
       61 palvhldrla hwatligvpp arlwfatdsh tpagaqadkn svgpdagrra llagiaavat
      121 gaglvgaagd vqprrigsad varlsavldl yrsvdresgg gllyreiarf aesvyrmlew
      181 shadeltprl vaavaaarql agwtaldagr hsdaqrhfia aeraaitvdd mplaalirys
      241 qakqlqhlrh nrdalatlql aqaqlgprat palsalllga eaastaalgd hqgalnslgr
      301 asdrferina erepswmafy draellaqyg rvyrdiarqa gthaeqavqs vesavaafgp
      361 anvrssvlne vglcsalfla deperavvvg aravaqsgsl tsrrvidriv nlrrdltrhr
      421 qlpavaefeh vlkaraavav
//
LOCUS       WP_357622092             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357622092
VERSION     WP_357622092.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..212
                     /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=23242
     Region          11..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdtvkrpdkr aersrrtrek vveaarelfv aqgygatslq evadragvav qtvyfvfrnk
       61 rtlfkdvvda siagdlepva tmdrewfraa cakptaagql rahvqgtrei lgrvapimpl
      121 iaaaaatdpe iaaqwpdgpd prytvqyaaa ealvskpdar pglsvemaad llfgllspql
      181 ylifvrdrdw spdtweewvr taltsqlcad pg
//
LOCUS       WP_357622123             303 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357622123
VERSION     WP_357622123.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 303)
  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..303
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..303
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33638
     Region          11..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 mqrqaaeatp svgrhyqvrd rklflhrsgs gdpavvflpg agssgmdgfi vqqraaeltt
       61 svlydragtg wsdraelprt stqvtdelre llriagvpap yllvghslgg lyarhyaqrf
      121 pdevaglvlv epehedydsy mpkelnelyq twdpdeavpd elpdeiiefy rglfarelad
      181 wpqeirepli erhvspewlk iggqeaanry qlhdevrnag ampdvplivl tataidpfke
      241 avtqgiptsl lheeaeaktr lytalaksvt hgenrvidna ghltvifrrp davlqaiqdl
      301 lgs
//
LOCUS       WP_357622139             283 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: anti-sigma factor family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357622139
VERSION     WP_357622139.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 283)
  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..283
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..283
                     /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=29660
     Region          1..>72
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtceevrial gahalgalep dealevdthl agceacgael velqgvsafl ekvserdvql
       61 vtspprqvld rllnarvkrr rrgrmlmvva asaaaivagg gvwtaavnqp dmttssapaa
      121 srpeegaska rdaapsasta prakategpr akarddqprv laetrqdasg spkpdrrsaa
      181 eqefsgqngy tdayasvaaf pgthgtgisv rvsgvptgtt crlvvvgrdg rrdvtdswtv
      241 nrasyqgkpa fagqtrismg diarfdvvdv ssnrvlvtve vpr
//
LOCUS       WP_357622155              94 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Nonomuraea].
ACCESSION   WP_357622155
VERSION     WP_357622155.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..94
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=10118
     Region          <1..94
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msglmtnllh pkmvtftiaf lpqlinpslg qvwlqfailg vtlivleflv dgavgvlagr
       61 iggwlrhrrt arrridvatg gifvglgvkl aler
//
LOCUS       WP_357622154             412 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sediminicola].
ACCESSION   WP_357622154
VERSION     WP_357622154.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 412)
  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 412)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 412)
  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..412
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..412
                     /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=44150
     Region          149..408
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mssavvpdhp wllpgslvpa raprrtprdw fvdsllflva llwvlvahed avsrdpefal
       61 nvgpdwligi dllagvlatv alwlrrrwpv glavataplt ffsvtagaal livlftvlvh
      121 rplplgltlv gwnvvtslpy ialrpdpamp lwaamawtvl flgivlawal fvrarrqlvl
      181 slrdraerae aeqqlrleqa rhlergriar emhdvlahri sllslhagal efrpdappee
      241 varaagvira sahaalqdlr evigvlraev saeatperpq ptlgdvpalv aesrdagvrv
      301 svvdevtepa evpaaigrsa yrivqegltn arkhapgavv tvrlaggpgd glaveirnpw
      361 pvggpataip gtgtglvgva ervtlaggrl dhgrdadgdf rltawlpwvv as
//
LOCUS       WP_357622204             378 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357622204
VERSION     WP_357622204.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 378)
  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..378
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=39771
     Region          138..376
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mavpfpqrap apvrrsarll dlalalitvv gvvtgvmaae vhespwrgli plalflggll
       61 lfrrhlpmtv lllsiaaifl yrlnshfqgg wiwpasaayf saactprvrw valvgvaqlg
      121 yaaadfwwvl qrnvgrfvlh iageglllam ligaglvcaa vmrwrgqlre sdsraraaee
      181 rlqvarevhd ivahtlavvg vqlnvaadal eedpaeaaaa lcvakdvrnr amadlaslig
      241 vlrdrtdgaa pqpdlaavgt lvtdaraagl rvtldergdp savpaapava vyrivqealt
      301 ntlkhsgaak arvtidcgpr svvvevtddg rgcgeiverh glagmrervg alggaltvep
      361 vpgafsvrae ipvagspv
//
LOCUS       WP_357622215             840 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357622215
VERSION     WP_357622215.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 840)
  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 840)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 840)
  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..840
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     Protein         1..840
                     /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=89150
     Region          111..298
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
     Region          560..830
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mntlngigre saeipgvlaf gacmaaaigl qiahsfgrpg hwplgrrias vtalaalvla
       61 palwigpqaa avvpllpasi llvvpapygw vlygltcvvn pvlyfaqglg avnivfvfvf
      121 tlvqglvfyg lsflaelaqe lergrgslrr iaaagervri ardlhdvvgh dllaftlkne
      181 lahrllpgap graeevmsea lwiarrataa lrmiptgcqk lslagevrsi estlsvaqie
      241 vrmnvsshgl teavdsvlai vlreaitnvl rhskarqcev eggvrdglaw lsvandgadd
      301 gtsddgtsdd gtsddgtsdd gtsddgtsdd gtsddgtsdd sagyeraghe ragheraghd
      361 raaskvissd gsgldnlssr latvggrltv tredgwfrlv aeirlsdvpa gpsappadpw
      421 kpadllrrta vrwapgtanl ltlavllgyi pilitnilwr npagftvdvg icltvllltq
      481 fahsflgprv wpapvraatl tvqavasflp vlwvgalwgs mggflagsip lvlrarwrwv
      541 lytavggvvl vlavaggddt allgylvist lqtglviygl tslsalvael httrkeivrl
      601 aveqerldva rkvnelldrd lstimwncgv argltltape rakehimevl vavrrlvaev
      661 rstasgyrhv slaaevestr aalsaagiea qvdiasgrla eesdvvlamv lrnaitdtvr
      721 rsgvrrcvit vtqengptng ptngptngpt ngptngphng yvrlrvshdr apatapedgr
      781 lkarisrhrt tlsesdeerl ehvrarldav ngslrmette gwfhltaelp sgatpepape
//
LOCUS       WP_357622238             371 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Nonomuraea].
ACCESSION   WP_357622238
VERSION     WP_357622238.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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 371)
  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 371)
  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 371)
  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 371)
  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 371)
  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..371
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..371
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41077
     Region          80..221
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mtdemlrapa evkyadeldw lesvddgpkp fswrlsprmv rlfvlgsdrs dgldreikqk
       61 wfgdrsfver aivtlasdrg llligdpgtg kswlaellsa aisrnstlvv qgtagttedh
      121 ikyswnvsmv iakgqsrdsm ipspimtame qgvigrfeel trstsdvqda lisilsekyv
      181 sipeldddni vfakpgfsii atansrdrgv ndlssalkrr fnfvripvvt nkrseaeivr
      241 frttellrrh rielevpptl ldillqsfad lraasesass dderlesals taeqigvled
      301 ailhsqffgd qtlraqtlag slvgslarrn pedlailnky whgvveprsk kdggewpdfl
      361 eggrqaiatl s
//
LOCUS       WP_357622295             908 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357622295
VERSION     WP_357622295.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 908)
  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 908)
  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 908)
  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 908)
  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..908
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..908
                     /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=96829
     Region          3..233
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          102..908
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          698..726
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(699,702..703,706..707,709,737,740..741,744,746,
                     748..749,778,781..782,785..786,789)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          735..766
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          777..803
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          810..846
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          856..885
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlirllgpve veragqarpv rppqvalsla alaweagrvv pvdsllarvw geaappgarr
       61 tlqtviarir rdvladggav vqrvggylld vdesavdvgr frvlaeraas vadpvaplge
      121 alalwrgdpl tglsgewaer vrqrlrderk eallrwaram tgrdaaavvr alaplaekyp
      181 ldelvaavli ealhacgrta ealahfalvr rtldeelgve pgaslqqvhr tlllsgapse
      241 pvglvpaqlp vglrcfvgra seldrlavia sgerpvtaav caisgppgvg ksslalrwah
      301 lhrdrfpdgq lyadlsgvda gdasmvlprf lgalgvpesq vpsgsesqig lyrslmagrr
      361 ilvvlddarg aaqvrpllat apgcltlvts raelsglavt agahllrldv lpgddayrll
      421 vmwlgearpa aepeaaalii rrcgqlplal aivaarlaqr pelplaeaaa dlersvsgle
      481 pftdvdpavd lrgvfgrsyr dlpapaaglf rrlglhpgph lslaaaasla alpvvrarel
      541 athldranla elrppgrlhl hgllrayaae qgravggraa rgaaivrlld yylhsacaan
      601 avcyphrddl rpgppargva verftgdaea lrwyadevva lpallaeata agldrqawql
      661 awaftefmqr rglweeilrv qavaldaarr lgdrlaearc hnsaarahyr lgrhreaieh
      721 feraaerhrd ldepvlhahv llgltvalsr tdlhealdra lralalfria gdavgearal
      781 nnagwlraet gaydealadc rraqrlladl gyaqgeghaw dsvahvlrlk gdhagavaaf
      841 eraaellrgc ddphaagetl vrlgethlga gdvaaalgaw kqaadcydav gdaraadvrd
      901 riaahrhg
//
LOCUS       WP_357622367             228 aa            linear   BCT 28-DEC-2024
DEFINITION  M48 family metallopeptidase [Micromonospora sediminicola].
ACCESSION   WP_357622367
VERSION     WP_357622367.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 228)
  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 228)
  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..228
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..228
                     /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=26751
     Region          2..220
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mdvvykdikn lhisvyppvg rvrvaapyrl dedtirlaiv qrlpwikkqr eqlqnadrqt
       61 erqmvsgeth yiwgerlrld ssrrgrskvs vagktlwltt pgdyseeqrr avldnwyrke
      121 lkaavpplla rwqpivgeev akvvvrrmkt kwgtchtesr tiwlnpelak knprgleyiv
      181 vhelthfver thnerfvqlm dlhmpdwrar rdelndapla aeewnseg
//
LOCUS       WP_357622297             270 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357622297
VERSION     WP_357622297.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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 270)
  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 270)
  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 270)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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   8  (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 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..270
                     /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=29795
     Region          7..62
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 maggreltpr rwrilsflal hgmattsdva vvagvprlta hrdltwlhav glvgrersae
       61 drahawwyri sgegidllgr dlassgrpvp lrlgrrywga ahyllflpll easrqdpgrc
      121 glfqwlttld tsvwlrergl ahlradgygv wledgrcvrf lvhvdpgpvg eviaererst
      181 sgldgvlvgy rrmdpvvpvg avlviahdaa reanlladla sralrapvav ttldllhrhw
      241 phesvwkvpa agtarqrlid lspsvraarr
//
LOCUS       WP_357622376             438 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050786].
ACCESSION   WP_357622376
VERSION     WP_357622376.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=46942
     Region          38..333
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrlsqktrll caalvpmfal aacsggagga gpaggggdep vkltvwswdg tveravpgfq
       61 aanpnikvev vnggssqdey kaldnaiqag sgvpdlvmfe yfaipyfaip gkltdlgafg
      121 venlkkdyvq aawndvtvng kvyalpsdyg psamfynmat lkkagiseap atwdeyyeaa
      181 kkvralggdh yiaqdtgdlf fllsliwqag grpfkvdgnk vhidftdegt travafwqkm
      241 lneglvntkv tgwsddwnra lndgalatqt mggwltstlp erapkaagdf rvalmpqwkq
      301 gdkvgaengg ssfgipaasg hkeaafkfle yfthggglst rvdagafvpn tsvleseafq
      361 gkankyfgdq kvggvlaeas eivgsgwqyp pffewarsiy gdlaspfytt gkgslteilq
      421 qwkqrcvqyg neqgfqvd
//
LOCUS       WP_357622392             724 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora sediminicola].
ACCESSION   WP_357622392
VERSION     WP_357622392.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 724)
  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 724)
  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 724)
  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..724
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..724
                     /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=76405
     Region          53..656
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mastaadtas kaadiaaeqa yfdvaaahrd rrrddlarlp saaahgaaaa hlrryadtaa
       61 ralgaaddav afgriddeag evryvgrhli rdadgevlvv nwhapaaagw featadnpag
      121 irrkraftct gntiddltdt ilaeiaeavd ahllaelgrg rtgtmrdiva tiqaaqfalv
      181 raprdrvlvi eggpgtgkta valhrvswll fqhradmsap dvlvvgphpt fvryigqilp
      241 algddgvelr dvgrlapdvp rgrvepdava rikgearmag llaraldari gvpdpaerll
      301 vggrfvtlpg aevaealasa raadlpyagr rrllrdrlaa lvtaragvdp grsdavgnla
      361 erlwpqqtpt gllrdllgst arlraaagea ftpaeiaalh rrgadrlsre twsaadlpll
      421 delahlidgp grryahvvvd eaqdlspmql ravarrsatg sltvvgdlaq stgtwardsw
      481 tevlahlpat ypaeiaplry gyrvprqaya taaallpvaa pgvtpvevvr dgpadtgvhr
      541 vglaelaara vavarehaea grfvgivcpa rqrrpveaal aandvawssa drgelggsvn
      601 lispqeakgl efdavvvvep aeivasderg hrllyvaltr ttghldivct gdpvpldapv
      661 rarpplggea easftrreah rlaehlagql rnaappafwa dvlaevratl lpdgavspea
      721 padd
//
LOCUS       WP_357622402             111 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050786].
ACCESSION   WP_357622402
VERSION     WP_357622402.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050786
  ORGANISM  Nonomuraea sp. NPDC050786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050786"
                     /db_xref="taxon:3154840"
     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=11698
     Region          10..85
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgddngilar saaeeyanwf raladatriq ivsllarkne pmsvgaivaa cgvgqstvsh
       61 hlkiladvrf vlverhgtss fyrinqkcvc afptaadvvm gkpapgtpta e
//
LOCUS       WP_357622403             162 aa            linear   BCT 28-DEC-2024
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Micromonospora
            sediminicola].
ACCESSION   WP_357622403
VERSION     WP_357622403.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 162)
  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..162
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..162
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17368
     Region          24..>99
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mtsapgghps dptghgaggi rgftvlydag cplcraarrw lasraqlvpl efvpagsaea
       61 rrrlpgldhd atlrdltvva dtgavytgdg awfaclwala ehrrtaerla rphllplarr
      121 vvaaaaavre rirepgygdd ddraecaddr cgwpehrvdr pg
//
LOCUS       WP_357622416             491 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: APC family permease [unclassified Nonomuraea].
ACCESSION   WP_357622416
VERSION     WP_357622416.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 491)
  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 491)
  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 491)
  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 491)
  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..491
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..491
                     /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=52101
     Region          32..480
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstilrrlpp teasglrtga rhglaelyrp adlvvlglgv migagifsia gqqaatmagp
       61 gvilsfmiag iasllaclcy aelastipas gsaytfayvi fgevwawvig calilelqla
      121 aavvakawae ltvraitdfg lhlphqdlvs gllvlfilav ltgvvalnar iglralwimv
      181 aakllaigav ivvgatyvka anfgdlyapp epldvapstv fdvvvgqsha fgwsgifaaa
      241 paiafayvgf divataaeet vnapravpkg mirslvvatv iyiavavvmv gmtpytrism
      301 daplssafrg vgadwmvhvi digavlgltt vilvlivglt rvlfsmardg liprglsais
      361 rryhtpsrvt lvigvvavll aefapvftlq qlvvmgalfa flfvsagviv mrrrmprldq
      421 gfrvplspll palslaatlw lmvnlqlltw awfglwmvfg mlvyllygrr hsllappree
      481 paeaargrhr r
//
LOCUS       WP_357622425             170 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Nonomuraea].
ACCESSION   WP_357622425
VERSION     WP_357622425.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 170)
  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..170
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..170
                     /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=19346
     Region          3..158
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdeeadftrl fqehyesvlr yawrrvgptd apdianetfr iawekhreip pdrplpwlyv
       61 tarnlirnlv kkekrregll avhdvgdidd havavvarqa altalnslse sdrelvllva
      121 wegldlreaa qvagcsrpta tmrlhrarkr leqsladhpq hqpqfgesav
//
LOCUS       WP_357622456             860 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sediminicola].
ACCESSION   WP_357622456
VERSION     WP_357622456.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 860)
  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 860)
  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 860)
  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 860)
  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..860
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..860
                     /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=90951
     Region          17..838
                     /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 mengdprnsv ppgrtgpffg fvagvgvlal lvsvgplval pdrltelpaa fwtmaalava
       61 cdarpfvppg rrqtsavfps tcftfaillg wglgpavavq avavavsgwr lgyapwrtaf
      121 naaqyacala aayavtrlgp gelfgggrlh wtdvaavgga tvawfvvnyg lvttairlrf
      181 gdrwwpsvrh glayellstg sllllapvlv aaarasaali plvlvplfav yrmarlsaer
      241 eqladvdplt glpnrkallt evaeqvhlha eraargepaa hlalllldld rfkhvndalg
      301 havgdrllve vsarlidvvg erdlvarlgg defaivvprl agldearera drvvaalaep
      361 vpldglpldv ggsigvalfp dhgedfatlm rhadvamyda khrndtvavy apesdhnsae
      421 rlslladlrr vlesppagep vgvrggdgav lapdlpaarp ahdgrpapda rpgrddgrgg
      481 vrpgggsarw rlrrrrerve trpgdelieq iltgadptrr rgaragtpag saaraggdat
      541 sagttaevpp pahaatatet apaaraahat eavvtsggtp tgpattdrpa vreaddpgei
      601 tmyyqpqiai atgevvgvea llrwrhprrg mvdpgeliqv aeqsavmrll trrvvddvve
      661 qlakwsaagl tlraalnvsv rdlhtgeiad qiadrlaryg vpperlqvei tegalmadpr
      721 rvlasitqlh rigvgialdd fgtgysslqh lrrlplsevk vdrsfvlgma ddpddaaivr
      781 smielagalg lrvvaegved ertwrllhaa gcdvaqgwfh arpmpaeela awlsryrpvr
      841 pavaeaggrg gpegeskass
//
LOCUS       WP_357622475             792 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sediminicola].
ACCESSION   WP_357622475
VERSION     WP_357622475.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 792)
  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 792)
  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 792)
  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 792)
  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..792
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..792
                     /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=81732
     Region          131..789
                     /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 mpvtppagpr rlpplpdlaa slggalflla gtaglvpgpa avalavaggs alacvrlawl
       61 aglpptpspg aapaprppap aardhavprp apgtrcpapg pdragtvdqg rseptgrqar
      121 rvalsrrvaa ildaavlvag ltvavlplsd pahrlpvalv glgltaplha aallrlpgrs
      181 rlpgrerlrr gvdmlalavs lvfagwmvlp vgpvpvaarv asvggavala vlavaamaer
      241 rrrpgaarch agagltlagl sllvvllayd apdramsavg ppllagvllt aagarrtsag
      301 erphpgvapa awprltapag vaalaagvhl gtageftpaa malglavipp imvgellaaa
      361 dhrrrverla aseaslrrlv hgeadpadsa pltradlvrv lprrsggall vvdlhgehat
      421 apdaavlaev rrrlragcgp hdlvarvgdt eyavltdlgp vlayalgtrl laalvepypr
      481 aggavrlavs vglaettgge pedvfrqagl arrravqmgr drvewydayl eeqlvrrldl
      541 erelpgavar geldlvyqpv valadrlpvg teallrwrsp algtvlpael lpvaadldll
      601 gevgrwvvdr acrqlaawse ggrelwmavn vtprelaapd fvarvatala aydvpperlv
      661 vevaepavga elstvvarla glrslgvrta lddfraehas laqlrrlpid llkvgphlva
      721 pgadgqrpli dvvanlgdrl gvevvvegle sdgqvagarr agcrygqgfa larpataerv
      781 eawfeefpsa sr
//
LOCUS       WP_357622480             813 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Micromonospora sediminicola].
ACCESSION   WP_357622480
VERSION     WP_357622480.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=90386
     Region          10..>639
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 msrptllheg wtlralpgpq vpseiagvav patvpgcvht dllaaglipd pylddnenrl
       61 twigrtdwvy qttfhhepgg ddrvdlacag ldtvatvtln gvevgrtenq hrsyrfdvrs
      121 llrpgdntla vrfdspyrya eahrdrlgdr pnaypepfhf irktacnfgw dwgptvvtag
      181 iwqqiglhaw saarlatvrp lvtvdggvgr velhvevert rdepvtvhat vagvaaevtv
      241 pageraallt ltvddpalww pvgygeqplh dldvtlraad grdldtasrr igfrsvrldt
      301 tpdahgtpft lhvndvpifv kgvnwipdda fpdrvtrdrl aerfgqalga nvnllriwgg
      361 gryesedfye ladeagllvq qdflfacaay peeepfrtev eaeareqvtr laghpslvlw
      421 tgnneniwgw hdwdwqepla grtwgrgyyl ellptivgel dptvpywpgs pwsgsddihp
      481 ndpahgtmhi wdvwndddyt kyreyvprfv aefgyqappa fatlrrsisd eplahdspgm
      541 ahhqkaadgd rklqrgldah lpppadfddw hyltqlnqar aiqlgvehfr shrpvctgti
      601 vwqlndcwpv tswaavdgdg rrkplwyalr rayadrlltv qprdgglalv avnetgrawt
      661 apatvtrltl agepraktsv dldvpayssv vlplpaelar pdearrellv aeagdtaera
      721 lwffaedrdv ewpaadwdat vepadggrrv rvtartvlrd ltlfpdrldp saqvdqalvt
      781 llpgesavft vradapldad altarpvlrc vnd
//
LOCUS       WP_357622498             575 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357622498
VERSION     WP_357622498.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13398658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..575
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=61251
     Region          118..>337
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
     Region          407..>461
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mlairvdyle wpmsyahrda ysrrlhaahd aalsdaalge srpgdsglgd sglgraapgg
       61 aargdarpgd rgkrselsaa vpdrpatpts ttgaasasgg vpgdhgsags devragsggs
      121 asdgtrrlis aswrrsiqag vdpedgpapl aldlsrlgdl reshplrpvl plltetlarm
      181 adesehvvvi tdregrvlwr dgnpgvmrra dtigltdghg wseermgtng igtalavrrp
      241 vnvysaehll rllhiwscsa apivdpdsge llgcvdvsgt alslhpataa lvgaaarlae
      301 selalrmyer derllrryea lrgrpavlls atgrviagdp ggalgsrvql pnggerlllr
      361 dgrvamtepf wggylvratt taattaappp lrlgflgegv ptatvsdrrl plslrhaeil
      421 allalhprgl saeqlsfhly gdagnpvtir aeihrlraql rgtigakpyr ltspveadfl
      481 elrrllaand paalarmykg pllprsespe irrerdelev qvraclllhg spddlwtyaq
      541 tangrddlqi lerlaeslpf tdhraaaara rlytc
//
LOCUS       WP_357622516            1014 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050733].
ACCESSION   WP_357622516
VERSION     WP_357622516.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1014)
  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 1014)
  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 1014)
  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 1014)
  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..1014
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     Protein         1..1014
                     /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=108463
     Region          9..255
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          151..998
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          786..813
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          818..854
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          865..899
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(866,869..870,873..874,876,906,909..910,913..914,
                     916..917,944,947..948,953..954,957)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          904..938
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          943..973
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 magqsveggm rfavlgpvra wregeeldlg tplqrsilgm lllregravt paemidavwg
       61 ddsppralga lrtyvsrlrt vlepdrpars rpelltsvgr gyalrlsdga ldlvrfergl
      121 qeaeaarktg rpsaaagalr aalalfegep lagavgpyae hqrdrlvecr lsaietlmdv
      181 dlelgrhadv vselialtad hplrerlraq lmlalyrcgr qgdalavfte trhalidelg
      241 iepgpdlsal hqrilaadps laaaaqpvaa vgpgpaeepe preeepvhel prpaqlpatv
      301 sdftgrkeis grlrrmlssh aaaegvpvav icgiggvgkt tlavhvahaa ddlfpdgqly
      361 adlrgytgea tapesalgaf lralgippdv ipevpaersa lfrslladrr ilvlldnard
      421 agqvipllpg spgcaaivts rvkladlpga rlfdldvmep dealslfasv agpervaaeh
      481 gaamdvvaac gflplavriv aarmaarpsw tvaslvprla deqrrldelr vgnlaveatf
      541 algygqldpa qqrafrllsl pngpdisaga aaavlslspf eaedlleslv daslleapap
      601 gryrfhdllk lfarrildrt erqqaktlal rrllgfylas aqsahrlaye gsmiadnlvv
      661 vgtgrafgaa deavawliae gdslfaainq aasdsrtaee llpaadllva meplmesgth
      721 trefdhgtra vlaaalrigd agselrsryv lgrvlfagnr lteaeeqfrt vhelsverge
      781 kivtgevkna lavvvgrqrr htealswfds amrwyrengv pagealvlsy sardhlglnr
      841 pedaiaaaek glaifteigs gagtararyh lgivlsrvgr lteavhhhae claffraskq
      901 rvweqrvcsr laetfiaarr ypeavrhaeq alvvsreigh pygealsltv lgkalkglgs
      961 ttrstdclrq afdifsrlga peagdlkvll dsaaapalvv esvvesvdgp vves
//
LOCUS       WP_357622541             288 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 4-hydroxy-tetrahydrodipicolinate synthase family
            protein [unclassified Nonomuraea].
ACCESSION   WP_357622541
VERSION     WP_357622541.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..288
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..288
                     /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=29271
     Region          2..287
                     /region_name="DHDPS"
                     /note="Dihydrodipicolinate synthase (DHDPS); cd00950"
                     /db_xref="CDD:188637"
     Site            order(43..47,81,83,105..107,136,138,249..250,269,271)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188637"
     Site            order(44..45,133,138,161,187,189)
                     /site_type="active"
                     /db_xref="CDD:188637"
     Site            161
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188637"
ORIGIN      
        1 mlkgihvplv tpftptgeva agaldklarr vldegasglv algttgevaa ltpaeraqvv
       61 evcaevcrer eapltvgvng ndtrsvlaal eelppdvtaa lvtvpyflrp sergvvahfe
      121 aladgtpvpl viyhipyrtg qavgaatlrh lgghpmiagv kyatggvdqd vldllgdlpe
      181 gfdvlggdda vispllaaga sggimasanl apadfadlaa awsagdvtra rdlghrlarl
      241 saalfaepnp vvtkgvlhaq gliptpdvrl pllpasepsv ttalallg
//
LOCUS       WP_357622629             343 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase [Micromonospora sediminicola].
ACCESSION   WP_357622629
VERSION     WP_357622629.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 343)
  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..343
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..343
                     /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=35550
     Region          28..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 mtgagpgptd aewaaaveav rglpadarvl lichvnpdgd algsmlgfgl glrrlgvrhl
       61 qatfpgppgv pepfrwlpgv ellvpqddad pdpdlvicfd aagdsrlgdl vdrlgragts
      121 lvldhhasnt gfgrinlvdp haaatsvval glldrlgvpl daematglyv alttdtgsfr
      181 feattpavhe maarllatgi rpgdisrrif dtrpfgavrl fgevlgratl epaaaaghgl
      241 vwtyathddl arhdqpayvl ealidsvrct aeadvscvvk qsgdaewavs lrskgavdvs
      301 rvavalgggg hrfaagftgr gpldevvgni raalgaevlv phs
//
LOCUS       WP_357622635             924 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AfsR/SARP family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357622635
VERSION     WP_357622635.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 924)
  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 924)
  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 924)
  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 924)
  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..924
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..924
                     /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=101483
     Region          1..232
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          109..924
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          678..709
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(679,682..683,686..687,689,716,719..720,723..724,
                     726..727,754,757..758,763..764,767)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          714..744
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          753..783
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          795..821
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          834..861
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          872..899
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlrftllgpv qmivegaplt giaprhravl aylllnagrv isierlidam wgydrpdtar
       61 sqihasitai rkvlraagav rlletraggy vaqpesgqvd aqeftelvaa gelraaldlw
      121 sgealedvha hyvagvrelw ndrrlsayer lvedelaagr hddlldelaa qvtadplrek
      181 lnghlvlalh ragrqadala aarayraala deqgldpgra fieleravla ddpslrpada
      241 ppvvsgpprr stflpydipd fsgrsaeler lvddyrgpav vtidgmagig kttlavhvah
      301 rlaarypdgr lfidlrahta grepvdaaaa leallrqlgv padripvtpa ersalwrael
      361 adrrvlvvld nafdaehvrp llpghsdtlv lvtsrrrlvd ldgahalsvd vldeadaael
      421 ferivgerar qepeavrevl rlcghlplai risaarlqhr prwtvsylag rlrdhrrlld
      481 gvsaaftlsy eqlheaeqhm frllglvpgr didaygaaal agipeeeaee llealldahm
      541 llqlepgryt fhdllrehar siaeddgavl rlltyylhrs raavdrlfpd slsqregipq
      601 pdapiapird aaeaiawlda ersniiatav hgpeiclgml alamrpyldr qahhddaitl
      661 htlslqrsrk lgrrefeara ltdlawtywr lgeyeraeeh arqaldacee ayerarallt
      721 lgnvalrrrq dtqakqflkq aldltrigad twgeahvlgi lalvleragr peearrhldl
      781 alalhrkvgn pagaaatldh lgvvlrhqge lvqartrheq aaalyrklgd tadeaaaing
      841 laeaagdpar aveehtaala ladrtrnrpe qarahdglar ahlalghaeq acehgrlalv
      901 lygelgvpea eevrafldqa flta
//
LOCUS       WP_357622685             393 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357622685
VERSION     WP_357622685.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..393
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=41006
     Region          2..357
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkhrivvlga gyagantagr lakrlhrddv eiilvngdpe fvervrmhql asgqdlrprp
       61 lrdlyagtgv qvrtaqvtav dvegrtvdlg getlaydtlv yalgstsadh gvpgvaehay
      121 nvagkqaalr lrarlseakp getvlivggg ltgieaatei aeahpdlava iaaqgrvggw
      181 lsdkaqrhlr galdrlgitv hdpaditrve adgvvtgagg kipaqvtvwt agftvhpiaa
      241 attlevsdtg rivvdagmrs vshpdvyavg daalaegagg qplrmscasa npmawlaadv
      301 iaarltgrkv pettigyslq cislgrrdgi iqrvtsddqv tstvftgrta arikemicag
      361 aawsvshptm mmpsrrrhva atgaaktrpl ars
//
LOCUS       WP_357622700             236 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FadR/GntR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357622700
VERSION     WP_357622700.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 236)
  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..236
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..236
                     /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=25958
     Region          4..202
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 msevvrstls daltermlel ihtgglrpgd rlpstrelsq rfavttptlr ealrrleatg
       61 avemrhgsgi yvgadiervv lpnpnmreld gdqlvellga rvviepplaa maarraasgr
      121 ggqlavlerv ldeaarhlrg edaelhetnm tfhratarla gngvlheivd slltvhgaeq
      181 railqifddr rrdyeehrai leaivagdaa aaeermrahl vdvktvveqr lhhppk
//
LOCUS       WP_357622871             198 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein, partial [Micromonospora
            sediminicola].
ACCESSION   WP_357622871
VERSION     WP_357622871.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 198)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         <1..198
                     /product="FG-GAP repeat domain-containing protein"
     Region          43..107
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          96..160
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 arnsstgdiq lyrgngaggf qagtggvign nwsgfdiifs pgdfsgdgka dviarnsstg
       61 diqlyrgnga ggfqagtggv ignnwagfdi ifspgdfsgd gkpdvlarns attdlqlykg
      121 ngaggfqagt ggvignnwsg fsaifspgdf sgdgrpdvla rnsattdlql ykgngaggfq
      181 tgtgsvisnn wsgfniif
//
LOCUS       WP_357622931             318 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            sediminicola].
ACCESSION   WP_357622931
VERSION     WP_357622931.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..318
                     /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=34800
     Region          21..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtvrtvdrva gagrparpgp paarerwsfl dretplgyll vlpmavvvlg lvgyplvltv
       61 wfsltdkslg sdtvsfvglt nylellddpv fartmwntfn ytvtavfakl vlglvmalal
      121 nevrrfrrff raafllpwvv psslsvlawm wmfqadfsvl tylgrqvglv dgnipwlgea
      181 gwamaavqtv niwrgapffg iiilaglatv pkelveaavv dgasawqrlr yvilphltpi
      241 lvvvtlfsfv qtlgdfqivw iltnggpvns thlistlafr tgirgadias gsaisffvfp
      301 alasiialql tvmrrkak
//
LOCUS       WP_357622940             781 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Nonomuraea].
ACCESSION   WP_357622940
VERSION     WP_357622940.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 781)
  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..781
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..781
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=85569
     Region          10..767
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          496..522
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(498..499,502..503,505,535,538..539,542..543,
                     545..546,569,572..573,582..583,586)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          533..563
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          568..602
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtsrgtdgwt agglpaelts fvgrrqdiae vkrllagsrl vtlagvggvg ksrlalrvaa
       61 evrrafrdgv clvelaales sgvlaqavie slrivdhssr epmdvladhl rdrqilmvld
      121 ncehllheca vlaatlvraa pglrilatsr qalgapgeqt mvvpaltvpg mngqrpggep
      181 pecsdamllf aeraravvpg feitdanrea vtricrgldg iplaielaav rlrvisaeql
      241 ltrledrfgl lttgsrarlp rqqtlralid wshalcteqe rllwarlsvf sgsldleaae
      301 yvcagdgiva eeivdvvigl veksillree hgsmvrfrlm etirqygrdr lresgeeael
      361 rrrhrvwyhd latrmhqawf gpdqvtwyql mrlehdnvrs aldycvstpg eaeagmtlaa
      421 alryywiaad spregrgwld rllavdaapv rararalcvd arlavlqsdf gvaagllaec
      481 relgrklgdd giagaaayve glaavlrsdl pealgllgea lecgrvtgdq mlvvnsliyl
      541 gtarsllgra deavdsfeec lrlcdtrrer wfrsytlwty gievwkqgdt rravemerea
      601 irlkepfkdp lgialcaeal awmaagegdg rraatllgal eemrrafggp lfghlshyhd
      661 aceqaaraai gdrrfetacr kgatmtpaqv iayalrddrr tgerprdssp ltrremeiar
      721 lvalgmsnka iaaslviaqr taeghvekil sklgfssrvq iaawigrqel svdepwsggt
      781 p
//
LOCUS       WP_357622953             487 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora sediminicola].
ACCESSION   WP_357622953
VERSION     WP_357622953.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 487)
  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..487
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..487
                     /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=50343
     Region          22..263
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22,46..47,76,81,82..83,106)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,105..108,112,114,150,152,
                     154..155,157,166..167,170,185..188)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,105..108,112,152,154..155,
                     157,166..167)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(33,112,114,150,152,154,170,185..188)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(166..174,181..188)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <324..>401
                     /region_name="PRK14959"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184923"
ORIGIN      
        1 mgrperptpg rwptpgvtla gryrlverig aggmsviwra ldveldrpva vklpgpdrdv
       61 pvdrdalart eartmaavsh pdvvvvhdvg qvaapdgttv tflvlqmlag eslldvlasg
      121 algwrqavri aarlaavlaa vhahgvvhrd vtpdnvmvad gevklldfgi aarigdrpqr
      181 swtfgtppyl aperladapa dpaadvyslg allvemltgr ppddafrmpa aapaevvrlc
      241 nrclerepgr rpsaaevaae ldaltdpmsa grqpprtlap atgravtavl eptadrrgrg
      301 pviagvatvv agalaaavti valtrsptpp teaqppapel swpplirstr ptmtpgpsrs
      361 nkptrvpsai rssapstgrp asattgasas ptvslavaaa qlrellrgdv segtvtsgaa
      421 qkidaqvvnv vnnqnaradn laqlmsdlrr svadeirdgg vsaaaapals davdrvgdav
      481 trstsag
//
LOCUS       WP_357622972            1084 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora sediminicola].
ACCESSION   WP_357622972
VERSION     WP_357622972.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1084)
  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 1084)
  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 1084)
  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 1084)
  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..1084
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..1084
                     /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=117149
     Region          2..1084
                     /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 mtatderpal vranrparip lsfaqrrmwf lhrygesgsa ynltflwrle gavdeqalgq
       61 alrdvmtrhe tlrtifpeea gepaqqvldp avlvtpltvr svaaaeveav vqeladiefa
      121 lqddppfraa lltsgprvnh lalfvhhiac dgwsfgllar dlstayrari agtapdwapl
      181 pvqyvdytiw qqallgtdqq pselttkqlr ywtetldgap elislpldrp rpsvasyrgr
      241 tteltipprl hdelaelaae rgctlfmvlh aalaavlsay gagqdivlgt afagrtdral
      301 eplvgffvdt lvlrtdlsgd psfadllerv rdadlaafth qdvpfervvq avkperssay
      361 hplfqvffaf hdgeaanelr lpgvvsaslp epvntakfdl svdffqqssg ddagvrivle
      421 yatdlfdtat vtqlgarllr llsavsvdpd vpisrlsllt saerrmqlqq wngpvtdeps
      481 ldlpmlvrqi aeqrpaavav sgredqltyr elagtaaria delvaagarp dtlvavlshr
      541 tpwyvaavlg vlgagcgfmp vdastgisra aqmledgrvg lllaatdlvd raesvaasag
      601 lpvrvlspgs gladpatlah rpsrdelaya vftsgstgrp kgvlvphrgl anhlraivel
      661 yklgehdvlv fnapltfdvs vwqaltllav ggrvhtvddd lardpvalad ccadqdvtil
      721 qvvpsllram leaceeaprl agsmtglrlm lahgeelppd lisrwhrqvp gvplanvygp
      781 aecsddvsia mldtdvtgps srasigkpli ntfvyvlder lalvpagvtg elyvagagla
      841 rgyagrpalt aerfipnpfg spgqrmyrtg dlvrwnsdge leflgradgq vkirgfriel
      901 gevehhlrsa pgvdqatviv redrpgdrrl vayftandqv pvsslrtaae esmpnymvpa
      961 afvqleempl tgngkldvra lpapnysggg qepsspeehq lcalfgevlg vervaadasf
     1021 felgghslma trllnrirav mgaeasvrdl fdaptvagla stlagrrhss rpilrrrtrq
     1081 gell
//
LOCUS       WP_357623042             179 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357623042
VERSION     WP_357623042.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 179)
  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..179
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..179
                     /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=18969
     Region          4..137
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgderrydat tvaeiadrag ltrstffrhf adkrevlfgg rdgmaerfae airaappgtt
       61 tagclaaale sfafaftadr hdlarqrqav iaahselqer ellkqarlas amaeaprarg
      121 addttarlaa emgalalata farwaepgnr qpyteiahaa prdlracata lgadagvpa
//
LOCUS       WP_357623089             420 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357623089
VERSION     WP_357623089.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 420)
  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 420)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..420
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42467
     Region          31..407
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mskvkelpge avvaavrsps ighsarayte rvragdmgal pavlglvvlc tafalarpaf
       61 lsainfanlf tqgaaitvia mglvfvllig eidlsagfss gvcaavlavt ltnmglpwyv
      121 gvlaaivtgt ligtvlgtlv akvgipsfvv tlaaflafqg lvlvlvnegt nisindpvik
      181 avaqrnlppa lgwalyaacv layaglqvlr arkraarglv adppsliaar vgalavlagl
      241 avyalnvers fnpafaslkg vpivvpvila llvlwtfvlr rtafgrhvya vggnaeaarr
      301 agiavdrirv safvicssma avggivaasr assvdpntgg ssvllyavga aviggtslfg
      361 gkgrvldavl ggaviavidn gmalmqygss vkylvtgfvl llaagvdava rkraaaaglr
//
LOCUS       WP_357623130             918 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sediminicola].
ACCESSION   WP_357623130
VERSION     WP_357623130.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..918
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..918
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=98052
     Region          <7..912
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mggatvptla dvtardgreg llgrtdecrr laalladasd grggalvvrg vagvgktall
       61 dhcaeravgm rvlratgvpf eadlpfsalh elarplldrl dglpaqqada lrtvfavdgg
      121 sravnrlaay vatltlltaa aettpvlclv ddahwidpas aeallftarr lladrvaivf
      181 atrdvpgfdg rgvpelpltg lapeaavrla mragldrrva telavatagn plalvelpvt
      241 laeerrhgwl pleqplvlad rirtsvlaha rdlpeatwra lvvcavaetp glalldqvlt
      301 vdglgldald ravdaglirv tarevtfrhp lmraavhsaa gpgrrrsahl aiasvltgpe
      361 tadrrawhla aattgpderv aallagsaer aqrrggvvae arayersarl tpdpdvragr
      421 ligaarawtn agasrhaval geealgltrr vdlrcrmtpl lahlaqqhgd ltvvddayla
      481 eaeecartdp lgaakmmsag vnqfwarldv tgmlpfcerv velagtapgt pwpkgairla
      541 aaqvlagrpe gagsardcva acaghadgsa aelaqvfcwl gdldaarall epeidraraa
      601 ddvfllayal prlaelrwra galhdayraa teavgiaeqv alpllraeal atlalveall
      661 gdesearthi ddarrllpae fgevearlry aaammsvvaa rweeavtdle wirsaqargg
      721 itapgwlpva gelaeayawl srperlrdlp dggpaatarv agllaaepdl dvvfpaalar
      781 cdptvvpler artllcygqr lrrakrrrda rvqlhaalrl featgaqgwa rrcrveidat
      841 grgaparddr tvdrltsqer qialhvaegl tnreiatrif lspktveyhl gnvyrklrlr
      901 srpelirhls rrstsepd
//
LOCUS       WP_357623135             854 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Micromonospora sediminicola].
ACCESSION   WP_357623135
VERSION     WP_357623135.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 854)
  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 854)
  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 854)
  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 854)
  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..854
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..854
                     /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=87780
     Region          23..846
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 msnggpgtvt itatspippp aagltstraa aklraegpnt vapprrrgpa grvlrqltdp
       61 lvalllaaav vttllrdypd tavivlvvli ntaigvvqei radravaald rlaaptarvv
      121 rdgrdlvlpa aelvrddlvr leagdvvpad lrltdaarls ldesaltges vpvgrsagee
      181 asagtvvttg ratgtvlrtg assalgrisa lvaatrpapt plqrrlaslg rvlgltvvvl
      241 salvfalgvl dgrpvaqmav tavslvvaav peslpavvtl alalgarrma gsraiprrlh
      301 avetlgsvtv iasdktgtlt egrmavqqav tagraryavt gtgyapdgev rhrdepvgap
      361 delrrlarag llcndatltp ptddrpewsa igdpleaalv afaarcgvdp ettrdawprv
      421 aehpfdqelr rmttvhrrgd grylvvckga penvlttplt dadaeelael tesarrlage
      481 glrvlavasa vvdtppdpar ptdlrplglv gvgdplrvqa pgiaagfeea girlvlitgd
      541 hpataaaigg rlglwtdgdp langddgdpg rahpdtrvya rtqpeqkldi iaglqsrghv
      601 vamtgdgvnd apalrradig vamgggteva rqaadlvlvd ddlttvatai gegrriydni
      661 rrflryalag gvaeiavmll gpllglpvpl lpaqilwinl lthgvpgval gaepaepgtl
      721 rrhprspqes vlggglgrdv lvtgaliaaa algagvaaay adrpwqsvvf vvlglsqlgv
      781 alavratrsp gssdrnralp lavavsaalq vagvllpplr dllgtaplal pdllgcavvg
      841 vlpglllrlt rrsg
//
LOCUS       WP_357623151             147 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357623151
VERSION     WP_357623151.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 147)
  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 147)
  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..147
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..147
                     /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=15661
     Region          5..136
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtsmpvterl gfhlkraeqa lnaakhaalr pagltvpqya allhlaenpg isaaalarac
       61 gvtpptmntv lrnlqeqgli ertphewhkn iletrltakg aqvmasadan avrverglag
      121 afsdeeretl iallarcveq legarpa
//
LOCUS       WP_357623153             335 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357623153
VERSION     WP_357623153.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 335)
  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..335
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..335
                     /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=35134
     Region          54..307
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mrslrtvaaa tgmtlaiala gatpaalaag taatvsapaa tvstafelpg arvypegita
       61 dprtgdlyag sftdgtvfrm tpgrrvaetf lpagadgrht angleadgag rlwvtdstsg
      121 vtvydtrtra llarfevegd eprfvndvai apdgtayltd svravvyrvt lrqlarargg
      181 rapltpyadl sdaagpnapg tftlngivad ragrylltad mtggglyrvd lttravrkva
      241 leggdmlhad glelrgatlw avhntvdtis rwrvtrdgta arverrltde alqlpttltw
      301 hrhglyvvrs qfdkggplgd gtpslpfsva lvrgl
//
LOCUS       WP_357623221             155 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: peroxiredoxin family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357623221
VERSION     WP_357623221.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 155)
  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 155)
  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 155)
  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 155)
  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..155
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..155
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16794
     Region          8..152
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mletgspapd lvledtdgrt vrlsdhrggh avliyfmrst scaicnrhvq dlvrcrdela
       61 addvqvfvav pegrqeaaaw karrripfpv lvgrrdtphe miglsrkvfg slqqsgsilv
      121 dsrgivrhah gatmptsgyd kkgitaavrg lrapa
//
LOCUS       WP_357623290             431 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357623290
VERSION     WP_357623290.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..431
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..431
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44362
     Region          <273..418
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 maalqqsvdd laarlghpll vedrlhrvla hseqtgamdd vrrdsilrrr aapearrwla
       61 aagihdapgp lrvpgapglg llprvcvpvr hdggllgflw fidaepalte aqvaeaaaaa
      121 palgltllhe slaaglpahr eleavaglml gehdaarrlv eagafpraqp vtalvarplp
      181 rpaaggaptd ggapsggeag aaleqgaltl rrrltghhpl hlvrhdhvvl liaaggpagg
      241 gvsssgvsss gvsgggvsgg pgesgapaal ataeelhaam pvpvtvgvgr prpaldgaaa
      301 syaearhaae vaarvpatgr taewtrlgvy rmlthlpghd lhpglepllg ddqhlpllet
      361 leayldlags avatsralrl hrtslyyrlq rveelagtdl kdggerlalh lslklarlsg
      421 ryrprgshpg g
//
LOCUS       WP_357623311             487 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Micromonospora
            sediminicola].
ACCESSION   WP_357623311
VERSION     WP_357623311.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 487)
  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..487
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..487
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51323
     Region          34..429
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msvtelpgdr apdspatppd aarparrpap ltalltrlhf yagvlvapfl lvaaltglay
       61 titpqldaal ygdqltvtav ggqprpladq iaaaraahpd gtltavrpgt gdrttqvvfa
      121 redlgdrqht vyvdpytaev agqlttwfgs tpattwlddl hrnlhlgdvg rhyseiaasw
      181 lwvlalggvv lwwrrraagr aharhllvpd lsagrgvrrt rgwhattgvw ltvgllflaa
      241 tgltwsryag anvgagldal ragtpeistt lddappatgg gehrhgetat apaadpatyd
      301 rvlgaaraag lsgpveiapa ardgaawtva qtddtwpvay drvavdpagg tvtarsdftd
      361 wpllaklskl giqahmgrll gpvnqvllaa lalgllcvvv wgyrmwwqrr ptradrrapl
      421 gappargawr gtpwwallig vpvvaalgwa lpwfggtllg flvvdalagl lahrrrsapv
      481 spapags
//
LOCUS       WP_357623314             429 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357623314
VERSION     WP_357623314.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 429)
  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..429
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..429
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45225
     Region          1..>82
                     /region_name="PRK13355"
                     /note="bifunctional HTH-domain containing
                     protein/aminotransferase; Provisional"
                     /db_xref="CDD:237361"
     Region          147..202
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(153,157,182)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(156,181)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(163..164,175,178,182..183)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          232..419
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maniaerldl alrerglsga qvaaelteag ipitrayvsq lrtgkqanpt lqvlralasc
       61 lqvsvgwlvg eesldsgave dlqlraaaig asasglsdgs lavlrgvidl arraeglpdh
      121 sgpapeapav pavpaartap pepvrvalge rlrglreaag laaeqvesal grgairveaa
      181 etgraapapa mverlldlyg vtalparehv lslargerep awwdtsavpv wlatafaleq
      241 rasvirvydp rtvppllqte ayaraaigaa gpatlgqtsv eaavrlvlar qemvftghga
      301 gqgaghgpvv waimdegvll rsiaeppvhl aqldslidla krpgvslhlv plhdpaylpr
      361 tgpftlwrya eafepdiaca htverdelit epgaveayhq afaklsvttt treetfdlln
      421 thrdriarg
//
LOCUS       WP_357623344             179 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357623344
VERSION     WP_357623344.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 179)
  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 179)
  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..179
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..179
                     /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=19957
     Region          29..167
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msdsvsgpdh adhvarilqa warerpdldv rplgvigrlh rlaghltdrl lvvyrryglg
       61 egdfdvlaal rragepfera pgelaaytmv ttgamtkrid rleraglvtr rpsaddgrar
      121 vvaltdagre lfdeaftehm rnerglldll tpeeadqler llirwlagfe gprpprees
//
LOCUS       WP_357623434             933 aa            linear   BCT 28-DEC-2024
DEFINITION  CHAT domain-containing protein [Nonomuraea sp. NPDC050733].
ACCESSION   WP_357623434
VERSION     WP_357623434.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 933)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18775376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     Protein         1..933
                     /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=95846
     Region          65..286
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          65..91
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(67..68,71..72,74,102,105..106,109..110,112..113,138,
                     141..142,145..146,149)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          99..131
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          137..165
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          176..210
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          218..247
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          238..898
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
ORIGIN      
        1 mtsahpglpr vsrltaaglv tgglvgaaea avlrsvvdpr qamlaaqavl saaeargvae
       61 aavvalramg laarelgdle aaerhlrrav atpgapperp aqarlslvtv rterghplqa
      121 lriaalawpa lspldrakld tqravalahl gryqeavaac dravqvlaaa pgtvddhrfl
      181 aggllnrglv hafrgdwdaa mgdvtaclel arhagldhla rlaaanlpfv avrrgdvaga
      241 fghyraaeda lfgfperlat mradfagall aaqqpgeare lltravpdle asgahvalad
      301 arlklarael ltgdarrala vaeraardle aqgrrswlpl arevvlrarl aldgpapall
      361 ealvacagel erdpahqgga aalrleaaev alalddrpta ltqlthlttv pgdasqdvrd
      421 stavgsaara gseaespdhg rgrgrgvtpa kvaslppalq elvrapeapv vrrvpgpvlr
      481 hamaleaelr gdtaaalraa rdglaevgsq agafddpalr ahmaragerl aglglrlavr
      541 drdaaevfaw aerwravaap pphvadldev raalseaspv gdrpcgtapd gggaggaapy
      601 evgqhgmalv efvavggslv avvvteerav vrrlggleev aeavvhlrya lrrhtlgdgp
      661 panrpvlgpp ahgpgdpvwe aarevgrllf rpveadagdr plvvvpagpl htvpwaalpe
      721 lrgrpvsvaa sasawlaagr rapvpagppe vaaaagpgla haraevdrvv aghprgrevp
      781 arggpmmeal asagvlhlaa hgvfharspl lssitlddgp lmaydllrlp sapglvvlsa
      841 cdsgmarapa egaplglaga flargtacvv agmvpvrddd alsvmtlfhe llargeppat
      901 alaaasakte vtgfacfgag hrpvtppprh pta
//
LOCUS       WP_357623514             983 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357623514
VERSION     WP_357623514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 983)
  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 983)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 983)
  AUTHORS   Rosinski,J.A. 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 983)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..983
                     /product="helix-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=105549
     Region          <7..923
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <921..981
                     /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 masdvdtapl vgrvgtlatl rsallddvap gqtaavfltg esgvgktrll aevgerlrqs
       61 galvltgtcl digdasplhp vrqalrrldt dvaearttsa vrgllqvfde etpgpdgaga
      121 llervsqglh lvaggrplvl vlddlqwvdr strqlllyll aglgdlqlsv laairaeslr
      181 gahplrrvlt elrrlrsvrv idllpldrag tdelaaaivg aplppeaadq vwqrsggnpf
      241 vveelardrr dgrdglsdtl revfldrvda lpqpahavvh avaagvepve hwllaqvvrl
      301 pedelldavr eavahrllvg addgyrlrhr lvaeilahel lpaeraalhr ryaealtaap
      361 aelhqarlah hwrqagepar alpaamaaar eaerlhgyae ahrhwsvala laatpvpvpv
      421 ppdggrpapv evdraellsh aaeaahhsge haraltllee laadasgppa calhirrary
      481 laaagrsapa eeeyrrvles adctprerct aaarlaelll hlgryaeagd qarealdlaa
      541 dvpgstsevv lasaalgfse afledqtagl avmrraleta ersgrpedva caylhlaell
      601 tgplnileeg vvvarrgaer vaelglgrtw etrllavatn glfrvgqwae aekvvatalr
      661 hrpsgadave lllarcrlsv gygdveasdr dleavatvla gggarhvlpm lilraglamw
      721 qgrhdlarqa vqrgltesrs ddvivlatla whglraeaea aasrtvevdp tavrrlrevv
      781 ervtrkseka gapvryvadg flalcdaels rlddgrgdpe lwgrsatewd rrnhpypaay
      841 srlrqaeall arrsrvatag kllrqahama qslgavplsa eirtlagrar vtlddapspa
      901 pvprprtapa vpaaptvdel avltarerev laavaegltn keigqrlfis ertigvhvsh
      961 ifdklqvrtr vqasaiflrn rpe
//
LOCUS       WP_357623437             388 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alkaline phosphatase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357623437
VERSION     WP_357623437.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..388
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40129
     Region          42..383
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 madtaplipa yggssladlp rallaalgvg eaagepgslr ieparavcvl lvdglgaeal
       61 rahagaapfl trgmrppagt apgasvltag fpattvtslc slgtglppge hgmmglvlav
      121 pgtgllfncl rwtlpdglvm dprrwqpapt vferaraagv taayvapgeh agsglseavy
      181 rgvrhlaagt vderverare alreapayvt vyygdldaag hdtgwggeew lrqlaivdrl
      241 aerlaealpd gcalyvtadh gmvnatgkld veaepalrhg vallggeara rhvyaeegav
      301 advlaawrgt lagrawvvtr eeaveagwfg pavraewlpr lgdvlavpyd glalvapgah
      361 preaaftgyh gsmtaaeqyv plleastr
//
LOCUS       WP_357623516             173 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357623516
VERSION     WP_357623516.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..173
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19198
     Region          5..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 malgknyngq dcslarvlel vgerwtmlvv rdalygvrry gdflahldip ravlsqrlaa
       61 lvdagvlerr ryqdtpprde yvptpmgrel wqpvlalgqw gerhltrnga rrlyfhvdcg
      121 aridafssct gcgaphlppe qievrpgpgl edgrgdpvsv alraphrlle plp
//
LOCUS       WP_357623563             374 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357623563
VERSION     WP_357623563.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..374
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..374
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40042
     Region          105..363
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mgalgtaama rmdeqlpwfr alsaedrswv glvaqagiaa fvewfqhage nrptpsieff
       61 gtaprelkrs islqqtvdiv rvvvevveae sdelaapgge dqlqqamlry trdvafaaaq
      121 vyareaearg awdarleali vdalvrgevd dglhswaaal gwtsspvvvi aghapeddpr
      181 avidglrekg rrigmdllag vqadrliviv ggagsvdeaa rqvvarfgpg pivigpevpd
      241 lhaaarsara alaglkassg wpdaprpvha ddllaerald gdedareqlv envyvplagt
      301 plldtlatyl eqgtsleata rllfvhpntv ryrlrkitel tgyqptegrs aftlqvglil
      361 grltesaatw ralt
//
LOCUS       WP_357623606             385 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357623606
VERSION     WP_357623606.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..385
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41026
     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 mlgplddivv ldlsralagp haaqmlgdlg akvikvehpe ggdesrgwgp pfvgpdhdis
       61 tyflaanrnk esitvdlksa ggkklierlv rqcdvlvenf rtgvldrlgf pverlhelnp
      121 rlvvlsitgf ghdgpeggrp gydqiaqgea glmsltgpap depyrvgasi adllagihga
      181 ygvaaalyer ertgrgrvvr tsllaavagv hsyhgtawtv ggkvpvaagn hhvsitpygs
      241 frcadgmlqi aaandgqwrk vaallgidpg dpryasnrer sahraeliad meralaahdr
      301 ghwlvrlaea gvpagairsl devytwdqtr sqgllveveh pvlgrielpg pplrfeglea
      361 vrhrpppalg gdgaavlawl eeres
//
LOCUS       WP_357623663            1212 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357623663
VERSION     WP_357623663.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1212)
  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 1212)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 1212)
  AUTHORS   Rosinski,J.A. 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 1212)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1212
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..1212
                     /product="helix-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=124746
     Region          <1..935
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          1113..1167
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlygrareqa ridaltaaar agqggavvvr getgigksal ldhtathaag flllratgve
       61 pecelpfaal ypllhpvlhp vlhpvrspag rlpadraeal reavkavppe apdrsrvrlv
      121 glavldllad vaaetpvlcl vddahwldra saeallfaar rlggerivmi faahddvpsr
      181 ahpapapgit dgtaaepspt prsgtgtmtg tgveelwpag ldltaaaell agrapglppq
      241 vrhrvaeeaa gnplalvela aaltpqqqag rlgplplace cgplsgrara tfetpvhrlp
      301 eatraallva aaddtgdldv ilraaarlga tpadlepaer dglvrlsatg ltfrhplfrs
      361 aayrtapyfr rvaahralad tlegqahstr rawhhatatp gpedslaaal hdaalhtfph
      421 atsppatapy dlhtdgtltd ethtasapgd gtltdracea glpvvvasva yeragelsge
      481 pgrsaerfva aaelafqagl tgrsatlagr aaalpsapat rarlaavraa ietvhgrpet
      541 aarilltgaq halaaepapa papqqkaiae paprtpprpa spdrpatgqg pttecgaagr
      601 adavgapaar saamrspavr lladavrkas sachgvlagt aatglaaltt hptgataaap
      661 drdivevfaa gmevmgrmva graatdlspv raairsvrvs sadhpdllap aawmavasgd
      721 elvgrelall ltercrrhgl igvlpealtl laqaelsagr hsaaeaaare glraasavrq
      781 pyraahlhal lawlaavngd edrcrhlttt tgaattllav nghtsipsge aasatrvphp
      841 aqaaegagaa qavgtwasgl lelgmgrprp aaerlaalws gachhplval havpdlveaa
      901 vraglrelae qpaaryaewa aasgrpwaga vaarleglla hddeagrhya ravavpagqp
      961 fqqartelly gewlrrahrr searrylraa fetfgalgat pwarraggel qatgeaaapr
     1021 ssaaprspaa prssapprsp atsrslaapr ssasprssat pwvspspasa papgpqartt
     1081 dqdrtrdrat dpgrgrgras eparprgnpp gllgrltpqe rqvvrlaaag lsnrqigarl
     1141 llsprtvghh lykafpklgv asrgqlaelg llaepdplae pgilaepdpp aeagpsaald
     1201 gpdrlsrvtg pt
//
LOCUS       WP_357623669             342 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sediminicola].
ACCESSION   WP_357623669
VERSION     WP_357623669.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..342
                     /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=37693
     Region          12..342
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtapadstkv rgetvlavdd lvkhfpitqg vlfkrqigai ravdgvsfel rrgetlgvvg
       61 esgcgkstla rllmrletpt sgratlegkd lfrasgselr rlrrnmqmvm qdpytslnpr
      121 mtvgdiigep faihpeaapk gsrrqrvrel ldvvglnpeh lnryphqfsg gqrqrigiar
      181 alalrpeiiv cdepvsaldv siqaqvinll eqlqdefgls yifiahdlsv vrhisdrvav
      241 mylgriveig teeqiyqrat hpytqallsa vpvpdpeart ersiirlsgd vpspadppsg
      301 crfrtrcwka eevcatqdpq tvsraadphp sachfaevrp dv
//
LOCUS       WP_357623730             444 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Nonomuraea].
ACCESSION   WP_357623730
VERSION     WP_357623730.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=47455
     Region          40..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(143,145,291,293,323..325,366)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mkkahlaaga lllltaacgg gsggsgsadg pvtlsyalfd daqqagyqrc adafqqanpg
       61 itikitqaaw dqywqnlttq mvsgsapdvi tmqasyypqf vkngqlldie pmvradkvdl
      121 gqyrpglael wlkdgkrygl pkdwdtiaii ynatlakkak ldlsdltwnp qdggtfekai
      181 akltvdtsgr hgdepgfdks kvavygitpe lkddglgqng wgdlavsngf syidknpfgt
      241 ryfyddpkla etitwfkglm dkgyaapydk vsslgpdavl gsgkaalgit gswtiksyle
      301 steqkfafap lptgpqgrks afngladsiy agtkhpeaaw kwvkflgstg cqdiiadsav
      361 vfpaissstq raiaahkaah rdisafttva dapgetfllp vsdhadeinq ivltaleevw
      421 lgqkdartal ttanqqvnal fasd
//
LOCUS       WP_357623742             315 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357623742
VERSION     WP_357623742.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 315)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..315
                     /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=34901
     Region          16..305
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msfsarkhad rpsqwrsmrw ietraallfi spwllgflif tawpiiysay lsltdydvin
       61 dpsfigfdny valfedpkvg lairntflfa vmsvptqlvv alglalllns aakptgffrt
      121 afflpkmtpp vavgvlllml fngqnglins vlgifgidgp awttdpdwvk pglvlmglwt
      181 vgasviiila alrgvpqely dsamvdgagw wrrtlritvp misptlfflf ivdsihalqs
      241 fteaytaffg sgnttysnda alfyaiylfq qafqflhmgy asalawllfv vimaitavqi
      301 lltrryvhye geggs
//
LOCUS       WP_357623756             858 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha-mannosidase [unclassified Nonomuraea].
ACCESSION   WP_357623756
VERSION     WP_357623756.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..858
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..858
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=94184
     Region          31..830
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mtgpagrraa pmanapsgaq pyglpraprp aatpgrtlhm ignahldpvw lwpwqegyqe
       61 aratfwsaih rmdeypdfvf tcdqvvllsw veesdpelfa rirervaegr whlaggwwve
      121 pdcnmpsges fvrqglygqr ylrekfgvma tvgmnvdpfg hhamlpailr gqgmdsycfl
      181 rpgphesdlp gtmfwweapd gsrvlayrip feycsppgev agqtekalgq ldrslgdlmi
      241 fygvgnhggg ptkaniesih rydrmgtfge lvmssprryf devakrlgeq glaglrvwrd
      301 dlqhhaagcy sahsgikawq rraqaavlsa erwaavaghd araelerawk qvlfnqfhdv
      361 lpgsaiepay ddardqlgea vavskriitr aqnviardir vpeetgtspv vvfnphpwpv
      421 tcdvemqygl apggvhvvda gggavasqgt qsvattddqg rgatvfrael pplgyrlyrm
      481 rpgapaprps rlsagatfle ndtlrveidp vsgwltslld krtgvdlvrg apgehtqica
      541 dptdtwghrv lsydwpgepm tttsvvlres gplrarlrve rewgrsamve efllgedsda
      601 vevrvsidwr erahllklrf pvavespvat yeipfghlrr pvdgaeepaq swvdlsgvvd
      661 gvpaglavvn nakhaydvap fgpgrghsig itavrspvya whdprlldpd gfysyqdqgv
      721 qhfryllvph ggdwrgaglt rraallgspv ramlesfhdg clppergfvd dgggqvmvta
      781 vkchedepdd lvvravethg rpvtaslevp lagvrivadf gpcqirtfri pradplatve
      841 tdllelgvrk galtvepl
//
LOCUS       WP_357623802             489 aa            linear   BCT 28-DEC-2024
DEFINITION  NADH-quinone oxidoreductase subunit N [Micromonospora
            sediminicola].
ACCESSION   WP_357623802
VERSION     WP_357623802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 489)
  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 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..489
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [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:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=48759
     Region          93..489
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mslvqsvdnv allpaylaag tavlvllvdl lvarpavtva vaslgaagta lgaglvgaag
       61 drrtfcvaad cswvwngraa lvavvvallt lgvlaisgpl lragrtqtge ycfllacamt
      121 ggvvlgaagd litlvvalet ltlplyvlvg lrrgslagae aavtffvvsv vattvtllga
      181 allyavtgtl hldrlgatla arddltdlpl ttvavalvva glafkvaavp fhawapatyd
      241 gaplpvaayl stasklggvv allavvqral pgevtgpvla vlavltmtvg nlvalrqrrt
      301 vrllawssva qagyilaplg alalaagrtp daragayaaa vaytvffvll elaafaavva
      361 lrpadgdggt ladlrgaarr hpwvggafal aliglaglpp glaglfakvt vvrsllagha
      421 gwlalvvavn avlglayylr vaaslyaapd pavaplrpar lvlvalgvat vaavvigvap
      481 qlvldvaar
//
LOCUS       WP_357623805             189 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357623805
VERSION     WP_357623805.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=20422
     Region          28..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrqikqtayh hgnlrraiid aalaaitefg pagwslrela rragvshaap ahhfgdktgl
       61 ltavaaegfe vfadtleraa edvldvgvay vrfatghrpy fevmfrpely rvddpslkaa
      121 reraahvlvv sagrlspspa qdrlttiaaw slahgfaslw lsgalpetar ddpealarsv
      181 iqlfigmar
//
LOCUS       WP_357623837             358 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sediminicola].
ACCESSION   WP_357623837
VERSION     WP_357623837.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 358)
  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..358
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..358
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=38176
     Region          24..302
                     /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 mkraelwpdh vlpahhvppp wpgrhvrldg tlvhvrdtpa tapgaepaly vhglggsaqn
       61 wtdlagllag rldgqaidlp gfgrsepgrr ytipafadrv vswiehsdrg pvhlfgnslg
      121 gavavrvaal rpdlvrtltl ispalpfldf rrslqgrmlp llaiprgerl aawrlaqlap
      181 evmaqqvmes cvadltrise qrrqeaidei riryeaahya aayvrtfrgl vgsflrsylp
      241 gagalwrqaa avrvptlvvg grqdrlvdvr vapqaarvip dsrlllldgv ghvaqlevpr
      301 tvaravlall aeaapaatpa paatpapaat papngteaqa ramvtgtees gtgrdvav
//
LOCUS       WP_357623849              76 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Micromonospora
            sediminicola].
ACCESSION   WP_357623849
VERSION     WP_357623849.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 76)
  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 76)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..76
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7792
     Region          10..70
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mteqrpvvqt ytvtgmtceh cvravteels alpgveevri dlaggtvtvt sasplpvesv
       61 raavdeagye mvggva
//
LOCUS       WP_357623858             216 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357623858
VERSION     WP_357623858.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 216)
  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..216
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..216
                     /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=23213
     Region          8..144
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtteplsrar ivtaaiglie regadavsmr riaaelgvgv mslynhvptk dalldgvaet
       61 vlseieftdd pdadwtdrvr tqarafrqia hhyprctmlv vsrqlhsaag llpveralat
      121 lrsagfdgpd avrvlrlfia fvvgsllrev gvtptfapth hrhlagaeaa dpalfpevsa
      181 lapllgacdh eaefafgvel liqaitvhpa rregtr
//
LOCUS       WP_357623875             272 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357623875
VERSION     WP_357623875.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 272)
  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..272
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..272
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30110
     Region          1..272
                     /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 mffaatdgtr layedygqgr pivfvasaml csdmweyqip yfvergyrci aldrrghgrs
       61 drpstgydmd taaddlavli erldlreail vghsmggaei arylhrhgde riarialvsa
      121 mlpfmrqtdd npegipgail dasiasldad rpkwlarqsq affathlgnd vspaqveftl
      181 rqclevspwa vrqsqrnvvd fdhratlpei nvptlvvhga adfsapidvt grrtaklipg
      241 avyheyptag hglfvshrdq lnddllafit gr
//
LOCUS       WP_357623878             333 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357623878
VERSION     WP_357623878.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=35357
     Region          6..305
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mptdlsptar alrameilqt rpgvtagela aclgvteraa rryvgilrea gipvesargp
       61 yggyrlgrgt rlppvsftep ealglvmavl dgqpaaadvg dlvgaalgkv iralpesvgr
      121 qaatlrehas aapdrlsarp dpattsalva aiadrrrvvv ayrsgsgnew eaevdpwavv
      181 vrhgrwyllc ychradairt yrvdrvrrvq rsthafeppd gldpvaalee nlgtgwefaa
      241 rvvfdaplae vapwirppmg rlepsgdgcv lvgstsnptm yaqewlptvp fpfrveggpe
      301 lraavtvlaa rlaaavagpp mddatpdpgs drp
//
LOCUS       WP_357623913             391 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357623913
VERSION     WP_357623913.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 391)
  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..391
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=41837
     Region          136..384
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtrrhrlavd vaiavalaal dtvltlvhgs wwperpgtpa wvllgaqala clslvarrra
       61 plavlaviga ftlvvtlliw plgaitpanp dnvwapvsaa slaaygplyh sgqnrrkail
      121 alavftlivv rlwqpsvlll tlgvlrvalg pllalyfdar rrlvqalter aeraererhl
      181 laeqarteer arlagemhdv vthrvslmvl qagalrmtat deetrrqaee lrvagvqald
      241 elrdlvgilr tapegeetps vagfaalvae stvvgnpael veegdpalas pvvgrtayri
      301 vregltnvrk hapgarvtvr veygdaqvrl sirntpptra pgelagtgsg lgiaglrqri
      361 evvhgtlrag repdggfrle atlpayvptg v
//
LOCUS       WP_357623950             328 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            sediminicola].
ACCESSION   WP_357623950
VERSION     WP_357623950.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=36406
     Region          18..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavqldarpp vapaprhsrp argarlsrfd tkyspylyia pffllfgvfg ayplaytfwv
       61 slhdwdllga ehpfigfdny sqlladpdfw hsvvntlgtf vistvpqlla alwlanllnr
      121 qlrarttwrm avlvpnvtst aavaivfavl fgrdfgminw lldhvgvsai dwkanrfaaw
      181 vaistmvdwr wtgynalifl aamqaiprdl yesasidgag rarqfwsitv pllkptivfa
      241 viistigglq lfteprmfns gtnairggpl resqtvtmym fenafaphyn fgygsaiawl
      301 lfaliaivaa invlllrrlg ggsrkevs
//
LOCUS       WP_357623955             447 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Nonomuraea].
ACCESSION   WP_357623955
VERSION     WP_357623955.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=46948
     Region          55..434
                     /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(160,162,282,284,319..321,362)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mtitrrhall lgaalsvslf atacgssgdg gsgtaatrsa stddlqaald aggsitvwaw
       61 eptlkkvvad fqakypkvkv nlvnagtgnd qytalqnavk agsgvpdvaq ieyyalpqfa
      121 lgksvadltt fgadkldgtf tpgpwgsvhs gsgiyglpmd sgpmalfynk dvfdkhkiev
      181 patwdeyiaa akklhdadpk ayitndtgda gfttsmiwqa ggkpyqvdgt kvsvnfsdag
      241 tqkftsawqq lvsgklvapv sswsdawykg lgdgsiatlv igawmpanle tgvkagagkw
      301 rvapmpqwes ggkatsengg sslavpeaaa nkklayafak yasvdegvqa rvdggafpat
      361 kaqlespafr dkkfayfgdq qinqvlaesa sqvvpgwsyl pyqvyansvf ndtvgkayis
      421 gttlqdglka wqdasvkygq eqgftvq
//
LOCUS       WP_357623961             295 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357623961
VERSION     WP_357623961.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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 295)
  AUTHORS   ter Beek,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..295
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..295
                     /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=32833
     Region          7..292
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mgalltrwra wiwvlpaval llvfvyypiv dnlrlsffsw nafspeprfv gldnyretft
       61 dpvfwralln nvayavvslv fqaglslvla alleelvgkr lrgllrtlyf ipaamsitva
      121 gvlfsflynp ryglvnealw avglghlara wlgeessaiw svigmsqwqg vgytavlfvv
      181 amqripreyy eaakvdgsga vrtffsitlp mvremttliv iltisgaflv fnevmvmtag
      241 gpdnssqvlg twlyrkaffe ddmgyaasva tvifvitfai aaaqlavsrr rrydt
//
LOCUS       WP_357623997             136 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357623997
VERSION     WP_357623997.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 136)
  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 136)
  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..136
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..136
                     /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=14862
     Region          2..134
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msrrrlgylf khaqsrlagl tgpaleplgv dtrelavltv ldartpmsqq qaaqalridr
       61 ttmvamvdal egkglvsrrp hpddrrknav eltahgrdvl rdgsaaidea ervflaplse
      121 derrlvrdal drlasg
//
LOCUS       WP_357624021             405 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA-guided endonuclease InsQ/TnpB family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357624021
VERSION     WP_357624021.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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 405)
  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..405
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..405
                     /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=44632
     Region          11..400
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mggarltsvc ryrlqptqaq eaallehygh arfvwnlave qhghwrpgrr sapgfteqcr
       61 qltaarrtsa wlragsvivq qqtlkdfaqa mrnfftgthg rptwrrrgsg egfrivatts
      121 revrrlsrrv gavrvskvgw vrfrwsrpvs agvksyritr daagrwhvaf avvpeaipap
      181 gngavvgvdr gvavaaalst geqflvpglr etekarlirl lrrlarakrg skrrdrlklg
      241 iarlktrerd rrkdwverts tyvarefdvi gvealkisam irsargsvan pgrsvrqkag
      301 lnrgilasgw gmlvarlgqk apgrvvkvka aytsqrcsvc givdreares qavfrcrscg
      361 yaanadvnaa rniayaagha vsarggsssg epvnrepqrd lllie
//
LOCUS       WP_357624146             240 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora sediminicola].
ACCESSION   WP_357624146
VERSION     WP_357624146.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 240)
  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 240)
  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 240)
  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 240)
  AUTHORS   ter Beek,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 240)
  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 240)
  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..240
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..240
                     /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=24368
     Region          17..218
                     /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 mnpvqqavvw lndplnwtnp ggvldrlgeh lsmsalavll gclvawpigl wlghsgrggg
       61 lvllvsnvtl aiptlallti lpltflgfgr aavvvalavf avppllanay tgvrqadpea
      121 rdaargmgls ggqvlrrvel plavpylaag frtaavqvva taalasfvng gglgqiirag
      181 fgldiaaggg qiiaggvlva glallvegil avlervvtpr plrrvrrran rraaaatagg
//
LOCUS       WP_357624164             434 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: M50 family metallopeptidase [unclassified
            Nonomuraea].
ACCESSION   WP_357624164
VERSION     WP_357624164.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  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 434)
  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..434
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..434
                     /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=46691
     Region          4..428
                     /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 mnwlflagiv ifliglmasi alheighlvp akifgvrvtq ymvgfgttaw sirrgeteyg
       61 fkwiplggyi rmigmlpprp gdapgklrgt stgpfqglie tareaameev rpgdedrvfy
      121 rkkwwqkvii msggpamnfv lsfilfsill vgigvptaap vvspqtntcv ipvseqrtec
      181 rptdqptpaa kaglkpgdki vslggqkist wddatrlirg hgagtvalgi vrdgrpmtls
      241 vtliamdrps ptdpkkidkq vgflgvlpsq vmekqsfgmv vgymseltvr vagsllnlpe
      301 kmvgvwhaaf sgqerdpegp vgvvgagrmg geilssdmtt eqkvyqlvsl lagfnlaigm
      361 fnlipllpld gghiagglwe glkrafarvt rrpepayvdi akvlpltyal alvmivmagl
      421 lvyadlfnpl kltg
//
LOCUS       WP_357624198             201 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora
            sediminicola].
ACCESSION   WP_357624198
VERSION     WP_357624198.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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..201
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..201
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20834
     Region          65..198
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mtrrlayllv plllaaagct ataeepagpa patraerpsp fadcapltva pasaapapag
       61 aagvelpdlt lncftggapv rvrdvkgpav invwaswcgp crkelpafqr lseraggrfq
      121 vigvnsrdsr ggaqsigedf gvgfpmlvdq gdafqraler nafpltvlvd adgrirhvda
      181 tgaldddrla klvrthlgvt v
//
LOCUS       WP_357624219             500 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea wenchangensis].
ACCESSION   WP_357624219
VERSION     WP_357624219.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 500)
  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 500)
  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..500
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..500
                     /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=54336
     Region          112..>203
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkrilipagg ailatgllaa glagtaqans dvakdnmatt aanakaiaef waenngaalk
       61 aakesnvwdk sdvaklqtkg gysadtkpgs tapigeekkt takvqnvnlp ktigkvffvn
      121 gkgekkwcsa tslqskyrnl vataghcvyd tgtnsdvmsk wvfvpgyyqg kapwgiyvgk
      181 taythydfdv yedydrdyaf vtvyngvslg ggtakkvtks afdahtgikd ardveitree
      241 frkakldpts tdsywvkrge kakkvgpdyp gavvekvett rdkyraarvg kgegfkfgep
      301 iteqvskady dkykglgekk pdnrgnytit hyyvqswvlp gsdtkfykte ffiiegfakd
      361 agrlgdnvgg qgfawnqptg kyvrvfgypa aphpdgnkny tgvtpkwcyg kttkklvgsa
      421 akkieehval kcamtegadg gpwlykysna krlgyvngvt stfndqdgng rvdyisspyf
      481 dgetntvyka assnwsgkiv
//
LOCUS       WP_357624260             235 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora sediminicola].
ACCESSION   WP_357624260
VERSION     WP_357624260.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..235
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24699
     Region          5..217
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 marpvifdlf htlvhgadae rdrvvgemal vvgvppdalv aayhatwrdr lvrwdveeti
       61 rilagrlggt ptdeqvsraa ehrralarrv lgrvspavld vldalrasgr plalisnata
      121 etaeawpgta lahrfdvavf ssdvglakpd paiyrhaaer lgvapgdcvy vgdgadgela
      181 gaaavgmtvl rttehqdtdp gwdgpsfasl tdlpallsgs lpgrarpapp psyaq
//
LOCUS       WP_357623641              85 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ubiquitin carboxyl-terminal hydrolase 14
            [unclassified Nonomuraea].
ACCESSION   WP_357623641
VERSION     WP_357623641.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Wang,D., Ma,H., Zhao,Y. and Zhao,J.
  TITLE     Ubiquitin-specific protease 14 is a new therapeutic target for the
            treatment of diseases
  JOURNAL   J Cell Physiol 236 (5), 3396-3405 (2021)
   PUBMED   33135160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..85
                     /product="ubiquitin carboxyl-terminal hydrolase 14"
                     /EC_number="3.4.19.12"
                     /GO_function="GO:0004843 - cysteine-type deubiquitinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0016579 - protein deubiquitination
                     [Evidence IEA]"
                     /GO_process="GO:0043161 - proteasome-mediated
                     ubiquitin-dependent protein catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=9328
     Region          3..85
                     /region_name="UBP14"
                     /note="Uncharacterized Zn-finger protein, UBP-type
                     [General function prediction only]; COG5207"
                     /db_xref="CDD:444070"
ORIGIN      
        1 matcehlsha gdpaantpdg ceeclaeggr wvhlrrclec ghigccdssp gkhatkhfhe
       61 lthpvvqsfe pgeqwrwcyv dnqmg
//
LOCUS       WP_357624262             174 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [unclassified Nonomuraea].
ACCESSION   WP_357624262
VERSION     WP_357624262.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 174)
  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..174
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..174
                     /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=19339
     Region          42..170
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 maaglpavpp vvppvgpgek grvgagtvag vvhesletlt rrhvfprmvr fadidslghv
       61 nnvrffdyle darlamfhid pyragdapfk glviarheid yrrplsfrae pvrvetwvte
      121 ikpvrftlay eirdddelfv tassvvvgyd veagaprrlt pqevaylerf kips
//
LOCUS       WP_357624320             250 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357624320
VERSION     WP_357624320.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=25430
     Region          7..241
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msrtnaaglk avvtgggsgi glatatllae rgmtvacldl ippgepfvgi kadvtddasv
       61 raavaeaaer lggidvlvnn agigaqgtve dnpdaewqrv fdvnvfgmvr varaalpylr
      121 rseyasivnt csiaataglp qralysatkg avlsltlama adhiregirv ncvnpgtadt
      181 pwvgrlldaa pdpeaeraal narqpmgrlv taeevaaaia ylagpeagat tgtsiavdgg
      241 mqglrlrptn
//
LOCUS       WP_357624326             513 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [unclassified Nonomuraea].
ACCESSION   WP_357624326
VERSION     WP_357624326.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..513
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54929
     Region          2..511
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msvsvqpger lgivgengsg kstllrllag verpdsgevv vtgeighlgq tlglpphltv
       61 rqaidaalag lramerrlrd ieaalaaapa egcdalleey gelltafear ggyeadaqvd
      121 kalhalglph latgptpsll eqehrtlgsl sggeqarlgl acvlaaapat llldeptnhl
      181 desalgwlee rlrgypgtvv vvshdrifld rvvtavieve gggvtrfggg ytgflaakaa
      241 ararweqayt awreevrqvr ehaattahrv avgrgmrdnn kmaydrnagr vqssiagrvr
      301 naqqrlrrle enpvprppap lrfhgafadv aggipgpaae lrdvrvgdrl hveslvggag
      361 drllvhghng agkstllrav aerargrvgh laqetvfdps lpvleayghg hpderraall
      421 atglfraetl dlrvgalsvg qrrrlalarl laeehdvlll deptnhlspe laeeleqald
      481 hytgtlvvvt hdralrkrfr gtrlevsggr vch
//
LOCUS       WP_357624331             385 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: cytochrome P450 family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357624331
VERSION     WP_357624331.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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 385)
  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..385
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..385
                     /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=41706
     Region          2..383
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(25,32,61..62,69,73,80,216..217,220,224..225,228,261,
                     266..267,270..271,273,296,324..326,329..330,332..334,338)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(32,55,57,60,62..63,148..149,158,215..216,219..220,
                     224,267,270..272,373)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mvlvelaggi pawavtrhdl lkelvlnplv skdkrhwrll pralsepgwt wimtwigvsn
       61 mlsaygeehr rlrklvapsf tarrsramqp ivegivaell damaavppgq vvdlraayah
      121 plpmrvicel fgvpahmree maqmmeaimd tsatpeqaaa taaqigtvlp alvaykrehp
      181 gddlttelin vrdnsaagvg ggaslsddel rdtlllliaa ghettvnlig navhallthp
      241 dqlrrtlage isweavveet lrwapsiahl plrfaveaid vggvrieagd aiitsylaag
      301 hdpdqhgpda aafdasqerd ehlafgigvh rcigaplarq ealtalpalf arfpdlrlav
      361 eadrlthvps fiahgwselp lllhr
//
LOCUS       WP_357624358             201 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora
            sediminicola].
ACCESSION   WP_357624358
VERSION     WP_357624358.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=21619
     Region          17..201
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mtgdhyftae pttparprev efsvagrdyt ltsaggvfsa drldpgtavl lrkaalpsag
       61 etgplldigc gfgpitcvla tvapaatvwa vdvneraral tttnaarvda adrvravapd
      121 empadvtftq iwsnppihig kaelhdlllr wlprlapdgv awlvvarhlg gdslhrwlve
      181 qgwqvdrhas qkgyrvlrvt r
//
LOCUS       WP_357624405             515 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357624405
VERSION     WP_357624405.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..515
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..515
                     /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=55330
     Region          53..511
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 meraaltrrg lligigaagg agamyaamga lglapseqdk aftpprqgdf tlrgkgsakv
       61 vilgagvagl taayelgkag ydctvleare kaggrnltlr ggdrlpelng pvqqaafgeg
      121 qyfnagpgri apwmltldyc relgvpvevf vnhnamayvh tggrtmrvra aradlygyva
      181 ellakatdrg aldravsaqd rerlldflrr fgdlgpkmdy agsarrgfat ypglaegmld
      241 aplsltdvla agtgrlvlnd fghdmatpmf qpvggmdaiv vklteavgad rirtgakvtg
      301 ittladgvev vwdggsvkad ycvaalpphv makiphnlga qvtaalktpv pvaagkigle
      361 ydrrwweted riyggvsetd ldithiwyps hgyhsgrgvl vgyynterda elygvlsped
      421 rrrraltqgk kihgekyrqg vladvsiawh rqphiegawv rwpafdssft llqrpagrvy
      481 fagdwltqli awqagamesa raavtqlhqr avrsa
//
LOCUS       WP_357624464             525 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 27 protein [unclassified
            Nonomuraea].
ACCESSION   WP_357624464
VERSION     WP_357624464.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 525)
  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 525)
  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 525)
  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 525)
  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..525
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..525
                     /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=55295
     Region          39..302
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(46,81..82,123,157,159,192,211,215)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          314..389
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          401..524
                     /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(412..415,425,427,430,434..435)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(421,454..457,467,469,472,474,476..477)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(440,444,446,450,454..456,467,469,472,476)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(497..501,510,512,519..520)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mrrilgltma allaagslva iggatspava ldnglartpq mgwndwnsfg cnvndglirq
       61 tadtmvssgm aaagytyvni ddcwstksrn sngdlvpdpq kfpngikala dyvhskglkl
      121 giyssagttt cagypaslgn errdaalwas wgidylkydn cgdhrgmngq qrytamrdal
      181 aatgrpivys lcnwgqesvw twgmpvgnsw rntgdiaanw ssimgildqq vglesysgpg
      241 gwndpdmlev gvggvtgteg rahfslwsll napliagndl rtmsadtrti ltnteviavn
      301 qdwggrqghk isdngnlevw rkpmkngsva vvllnrgtst stvstsaaal glgsassysv
      361 rdlwahttss ssgtisasvl ghgaamyvvt gggivqpttv aikgvgsgrc ldvtgasqan
      421 gaqaqiwdcn tqanqqwtpt asgelrvygg kcldvydrgt adgtnviiwd cngqsnqqwr
      481 ldsdgtitav gankcldvpe natangtklt iwschgganq rwtrt
//
LOCUS       WP_357624470             858 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Nonomuraea wenchangensis].
ACCESSION   WP_357624470
VERSION     WP_357624470.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 858)
  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 858)
  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 858)
  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 858)
  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..858
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..858
                     /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=90306
     Region          183..853
                     /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 miaagvvala aaflhddqvl vagaviggia alaaaaslvv aslrsgghrp tamgarwmgg
       61 gaviwgagla lrpvdggfva gfadlflllg tvvtaggali aadrklpars vlrhitdsyl
      121 cvasiflvaw vaqlrqvyda aadpptftlv mlppmmgllv tcavlpsvam srarswtlgl
      181 agagalvams vagtavavar ledgappawa vlpapvvfll laavpwvqwp gqgggplaks
      241 ivamvplglv avaagtllvh vvggaagspv tgvvaiavsv vllllvrlvv vsavnvrlrg
      301 lvrlgerqlr elaestgdvv flcdyegvvr eigagvevty gyapdevvgg sifdyihped
      361 vpgiqaalra mgldeedava gacliacrvr aadgtwrpte svatrhvggd elmlvttrdv
      421 sdeealrnqv ahltfhdgvt glpnrayfee rtrevlsgrt vgnvavifld ldgftsvnds
      481 vghasgdyll gqaarrlrga vraddtlarw ggdefavlve tggdaqvavd laerlvravs
      541 qepfrvadrd valtasvgva faeddipagd lirnadvama rskelggrrv evfaaqmhad
      601 vvrrlelaad lqraliehqf aieyqpvvdl atsrvtavea lvrwwrgsvf vppekflgpa
      661 edtglivplg ewilreacre vaawrasswd iglslnlsar qitaprfvet veealaesgl
      721 pasaltlevi eemlvedaee tikrlselra lgvrlaiddf gtgyaslafl rqlpvdmiki
      781 dpsfvaglgr ddtltlltrt ivrlghdlgl ivvaegierp eqlellremg ctrgqgflva
      841 rpmaargvds lmrtsltv
//
LOCUS       WP_357624499             224 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Nonomuraea wenchangensis].
ACCESSION   WP_357624499
VERSION     WP_357624499.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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..224
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..224
                     /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=24158
     Region          2..199
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 maagatglav laspaqattp dkestpaqas npdqaskpdq asnpvqaskp drapktdtld
       61 eraltttltg pelkkirdkq srpawkialn falkkqgipy lwggtgnggy dcsglmlray
      121 qkagiqlprv ttdqyaafdk kvswnhlkpg dlaffsnlgh vgmisrpgym vhaprtgdvi
      181 keeklsswrr safvgavrpd rkgvrqwaer rkepappmpv asvl
//
LOCUS       WP_357624615             397 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sediminicola].
ACCESSION   WP_357624615
VERSION     WP_357624615.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 397)
  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 397)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 397)
  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..397
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..397
                     /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=41100
     Region          158..397
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 meavvprprv varrvrtvli wsavallpva lllaatsgag gpvlvvptpd hsvpvlplry
       61 lapvlvvllp agllrrrpll alglmlagas lvtattnawe qgylnglwyl qflvvdvmlg
      121 vvaaraprrv svpaavlvll vqvaaafvnp aadavdratl svpavlaawv agnsvlarra
      181 yaeqmrahaa teavtaerlr iarelhdvva hsigviaiqa gvgarvidtq paqaraaltt
      241 iettsretla glrrtlgalr rpddaaasld ptpglsdldr lvaaaadagv rvtlavdgep
      301 gplpaevela ayrivqealt nvvrharvdr crvtvrhapd gvrvevvddg rggpvggdgh
      361 givgmreraa llggrcaagp rpeggfrvaa vlpvgpa
//
LOCUS       WP_357624649             182 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine dioxygenase [Nonomuraea wenchangensis].
ACCESSION   WP_357624649
VERSION     WP_357624649.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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 182)
  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 182)
  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..182
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..182
                     /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=20333
     Region          57..144
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mstdqiqqdg gtchalpert ldrrelrdlv drlaagpqew eelvdfpedg grhyaslhrd
       61 ayvdvwvlcw rpeddtgwhd hdissgavhv vrgalrecnp riggehletv vtegqsfsfg
      121 pdhihrltga versvsihay spplwrlgqy sidgtgvmrr vsvsyadelr plddievave
      181 va
//
LOCUS       WP_357624682             342 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357624682
VERSION     WP_357624682.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 342)
  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 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   3  (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   4  (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 11972964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=37237
     Region          12..267
                     /region_name="YrhO"
                     /note="Sugar-specific transcriptional regulator TrmB
                     [Transcription]; COG1378"
                     /db_xref="CDD:440988"
     Region          281..329
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrnespavpd plaalgldpa qsalytavlr lhratltela eamdgpcdkv grqlddlvrl
       61 gvvdehsgey larhpagalg rliaqrldrl aeesrridsa lgsirglird ydagrdyqsg
      121 pfpvelvsga dvlyesvvgm avqsppmtvl taipdertms dfarkfadpw idaqqrgllt
      181 vravvpvetl ampgvrdrlg rllqtggevr tldrvpswfm tagdqaaglp alwggnlpdh
      241 aynfyllrtp ivvgvltslf eewwgrsvpm pwghrsdgtv qvirlaaqgm cdesiarhlg
      301 vsvrtvrarf adamtrlgaq srfhagveaa rrgwlgqatd dr
//
LOCUS       WP_357624652             353 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357624652
VERSION     WP_357624652.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 353)
  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..353
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..353
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=37945
     Region          55..351
                     /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 mttttrrrvg iagaivgaas agvaaatlak ryvvgrirvr pdaelaepfg elrgrertlt
       61 tsdgvnlhve idgpeesgse apltvvfchg yclsleswhy qrrdlresyr vvlwdqrshg
      121 rsqraetgda tidrlgddla elldtfvpgp cvlvghsmgg mtimaladrr pelfgdrikg
      181 valigtsagk laeitlglpa lvskvvhkva pgavsmlgrr galvdrtrha gsdiaflitr
      241 yagfgdsknv sptlvdfaes miratptevi adfypalmnh dklsaldvld pvptaiivgd
      301 kdwltppdhs raiaaalpra qltevpdtsh lvqlerpgav ndvlrdlikr vel
//
LOCUS       WP_357624740             132 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357624740
VERSION     WP_357624740.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..132
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14425
     Region          8..115
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mpedlpptpd daqgscpipp rdlldvvsgk wpiqiivaas tgpvrftele rtvegisrrv
       61 ltltlrdler dgllertvhp tvppvveyqa tpmalelhea mltltawsrr hsahvaasre
      121 rydarqaaat as
//
LOCUS       WP_357624819             416 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357624819
VERSION     WP_357624819.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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   4  (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   5  (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   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 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..416
                     /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=44674
     Region          80..400
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtgrwrprgp rtlrlrltlg ygaiflvagl allgvtyvlf nqqltrsfee rfaappgrak
       61 qffiaegdir ltgdaavewl rrqelelrga agtsllaqgv laltvvggaa vafgwvvagr
      121 mlaplhrvtd tarriaaapm aerglheria lqgpadevkr ladtfdtmve rldhsfdgqr
      181 rfvanashel rtpltlnral velamhrrta spdvkelges lleinarher lisgllllar
      241 seqeiadrsp vdladvvthv vrqtagdaaa akvtvyevag qapvtgdall lerlvhnlve
      301 ngirynlddg sgwvrvvsrt vadggaqvev sntgpevppy dvpplfkpfh rhgaervvta
      361 rsaglglsiv rsiavahggd vsarpredgg lvvtatlpra spwpadeagv pgrgrg
//
LOCUS       WP_357624835            1118 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Micromonospora sediminicola].
ACCESSION   WP_357624835
VERSION     WP_357624835.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1118)
  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 1118)
  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..1118
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..1118
                     /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=121474
     Region          172..1111
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mpdtlsyada vrllggeksk ivdwfdkltg gvllaasvpv pallglfdak aefvrlghev
       61 vrvasekrsg lsrygrtqrl eaahaviavt affealaead lpfdfadlel rrseqltlag
      121 agpesrrsva rvlfevpapl papevpyarl rellrnhyvl lvgrvadfvd glavgerltd
      181 gekqslrqal eripefaver hrdlltalaa dfpevafwag lheheatrge vrqlavglve
      241 lretlaamat ggtpsdwrea larsyraqld rpiinsgevp dglrvpalgv ayvppsyrva
      301 algeqsrpsd eswwavqpar edlvqfligh ltspqavhap llvlgqpgsg ksvltrvlaa
      361 qlpardflvv rvvlrevrle adlqdqieqa vrdatgerla wpklarsagd alpvvlldgf
      421 dellqatgvt qtdyllkvaq fqqrevdqgr pvavlvtsrt svadrakppp gtvalrlepf
      481 dparvarwvt twnaansdgf avlgvppldp aavlthrela gqpllllmla lyaadgndlr
      541 sagtlgrgel yekllrsfar revvkhregl serelsrate aelrrlavva famfnrgvqw
      601 vteeeleadl gelaflagga pqaradgslr vplraaeivl grfffvhrsq alrgdqrtet
      661 yeflhatfge flvarttalv leelaareaa ttmlrsasvd ddplhallsf atltgrapvv
      721 aflvealrss pgdhaagild vllrlfqsvh hgrpgrtfas yrpralsvpe rhavysanll
      781 vlalcaveel sggqlypaep dvrvpwtrqa llwrsqlaeg eyrslvnava ldrrgdgrrr
      841 eiglslapeg wrppdvdlgw tfpptsswes nwlqvesgpd aaflrsvanf ecgvagdavq
      901 haleplvemf ppgfawvvrg gdtgqlsvgr mlvttvlgmp glgpadraah yrvvaslvia
      961 fhgsderdev dmavvlldrl aadrlvtraa aiavlsslef vptagdraag aflrcclali
     1021 gaddletrqv arivgrtlha dqgswsayte elaveavvrl telgidefhl spaeadrlar
     1081 lfagrrpdlv drirplvlap vpprpstgra lpggdvav
//
LOCUS       WP_357624841             281 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357624841
VERSION     WP_357624841.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   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 281)
  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..281
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..281
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29111
     Region          2..275
                     /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 mttrvaangi diayesfgap ggrplllimg lgaqlihwde glcellaeqg hhvvrfdnrd
       61 aglsthfgea gvpgpgtapp yllddmaddt aglmdalgwp qahvvgasmg gmiaqtlair
      121 hpervltlts imstpgpeva pptaeaaail marppadrdg vleqavrtws vigspgydld
      181 herittlagl aydrcfdpag tgrqlaaima sgsrvealgr lnastlvvhg eadqlvplag
      241 gqataaaipg arlvtypgmg hdlpralwpd lvaeitkltt a
//
LOCUS       WP_357624898             281 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357624898
VERSION     WP_357624898.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  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 281)
  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 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   4  (residues 1 to 281)
  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 10099992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..281
                     /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=30975
     Region          5..108
                     /region_name="HTH_BmrR"
                     /note="Helix-Turn-Helix DNA binding domain of the BmrR
                     transcription regulator; cd01107"
                     /db_xref="CDD:133382"
     Site            order(5..7,21,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Site            42
                     /site_type="other"
                     /note="drug binding residues [chemical binding]"
                     /db_xref="CDD:133382"
     Site            order(53,56,60..61,70,86,92,96,99..100)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133382"
     Region          121..275
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mglvsigefa rmsrlspkal rlydelrllv parvdpdtgy rwyaatqldq arlvaglrri
       61 rvplarirdi laldtasaae eiraywteae aehavqrela grlvdrlhgr npamysamhe
      121 vtvrdmpars llsvihrahq devvsigrel fihrlrrggv priagiagap fmiyhgevsd
      181 dsdgpvewcw pvpddqadai aarfpdltlr tepahqeacv rpetparqvs gaqaelaiet
      241 lvawasqrqr rtsggirlll vpnpasggtg pdsefalplr p
//
LOCUS       WP_357624953             315 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sediminicola].
ACCESSION   WP_357624953
VERSION     WP_357624953.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   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 315)
  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..315
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..315
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33233
     Region          1..296
                     /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 mpehrelrls ddvrlhvtvs gpvdaevtvv llhgwtldgr swhhqvaelr erfadrvrlv
       61 tydarghgrs sclalrdatl aqlgddlaav ideivpsgpv vlvghsmggm tvmeyahrhp
      121 drfaartagl vfvsttaegh thtvyglspr iarlirlaet tgagvlarcg gwrpphallr
      181 alrpsirwml fgdrcdpadi rlvtsavaha tlrsiggfra sigaqhrlet ltalgglpaa
      241 alvgdrdrlt pppcaesiaa alptaeltvc pgaghmlmme rpdevnaava gvldrvlaap
      301 gagggdpaav atvtp
//
LOCUS       WP_357624992             370 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Nonomuraea
            wenchangensis].
ACCESSION   WP_357624992
VERSION     WP_357624992.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=41606
     Region          10..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 mtttsslipt lpgrsysdpd vfadeqakif etlwfcavrg edvprpgafr tvqvgresvi
       61 vvrgrdhrlr aflnvcrhrg arlceepage vrrtircayh awsydldgrl aaapnlakmp
      121 didrvahgli pvhlrewlgy awvclaaepp sfeetvtgaa terlgdlaai eryhveelal
      181 grrisydvka nwklivenfm ecyhcatihp elvavlpefa ggyaaqyyvg hgaefaerve
      241 gftvdggpgf gklpdvareq drryyaitvk pqvfvnlvpd hvivhrmfpl avdrtlvecd
      301 wlyhpdvvas gadlsrsvel fhrvneqdfd acertqpgms srayreggvl vpsehhialf
      361 hqwvnqrlrg
//
LOCUS       WP_357625016             407 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357625016
VERSION     WP_357625016.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (residues 1 to 407)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..407
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44512
     Region          27..406
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrillvgagg vgtaitriaa rrtffdhmlv adydlpraka avaalgpdad rftpvkvdaa
       61 drdavtallr ehrcdvllna tdprfvlplf daalaagady ldmamsmsrp hperpyeevg
      121 vklgdeqfar apewaasgrl alvgmgvepg ladvfaryaa ddlfdeieei girdganltv
      181 dgydfapsfs iwttieecln ppviyekdrg wyttepfsep evfdfpegig pvecvnvehe
      241 evllvprwvd arrvtfkygl geefidtlkt lhalgvdrte pvpvrgdgga tvlvsprdvv
      301 aavlpdpagl germhgktca gtwvkgvkdg rprevylyhv vdnqwsmrey gsqavawqta
      361 vnpvialell aegawkgsgv lgpeafeprp fldllveygs pwgmreq
//
LOCUS       WP_357625208             266 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Micromonospora sediminicola].
ACCESSION   WP_357625208
VERSION     WP_357625208.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..266
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27717
     Region          1..242
                     /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..34,73,77..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..215,221,223)
                     /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..222,226,228)
                     /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 midlepvaap daplarrnpv aklaaalvft lvlvatldpv apaiaiaiel avlplfgvry
       61 rvlarrawpl lagavgilvt lvlfaadrsg pvlldagpvl vtqgvlvtal glvlrmlava
      121 lpgivvfatt dpteladali qnakaparfa igalaafrmv plleqewrmi smarrargvd
      181 agrnplaklr lfastafall vgairrgtrl avamdargfd agtprtvarr qhftradall
      241 vvtaallaga alttsillgt frplig
//
LOCUS       WP_357625201             278 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sediminicola].
ACCESSION   WP_357625201
VERSION     WP_357625201.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   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 278)
  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..278
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..278
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29122
     Region          1..270
                     /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 mrvkargltf evrtggpedg dpvlllhgfp qhsgewdavt palhaaglrt yaldqrgysp
       61 garpaaveay ripelvadaa gvldalgvtr ahlvghdwga ivawglaaah pervrtltav
      121 svphpaamgh alatdprqka ksayialfrm pgkaekvlla lrgaalrrll ggvgdadava
      181 ryaepmrdpe altaalnwyr amsgtdmkav gpvgvpttyv wsdrdvaigr taaeacaahv
      241 tgdyrflvld gvshwipdea pgplaaaila rctgaeea
//
LOCUS       WP_357625233             926 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357625233
VERSION     WP_357625233.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..926
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..926
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=99008
     Region          <17..924
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mteanawram agraderslv etaiaerhrl vlidgepgvg ktrllehltd raraagravl
       61 agsateferl vpfgmyvdaf arlsdavpda eaeaalrall sadqageanq ldryhtyrgi
      121 rslmarlade rgvvlalddl hwadgpslel tefllrrppa agftlamacr tgavppavge
      181 avarrdplvt wlslaplded avellvpsav hprrrrlmyr vsggnplflr tlldaddell
      241 aeladarpga tlaleqtlla vlrreldrlt ptgrraayaa avagelaspv vishvaemda
      301 asaaaaldel crhslgtlvg arftfrhplv raaaydtcga gwrvaahari adylrrndgs
      361 lallahhter caehgderag rtlgdagiay lntapetavr llrealrvlp erddlipyrg
      421 rlltglargt gvmgsleesr rilhevihlp hevasaavaf ssvisrmlgr ldearallsa
      481 qvrkagqeer vrgqllaela avamlrsdpa garrhahetl glvsktadpa leaaayalls
      541 vaclqdgdla aarthsrraa wlmdatsdta llphvelvap lawseiflqr padaerhlar
      601 gldlatasgr syvmpyllig qaqlktragr laeaieiaeh aaaaseyirs setlamarcv
      661 lllpvlwrqg vdpamalads laeagpgsaw wqaityasva rvrlagragp dhprpsvltr
      721 dteverlavr siaagadgdv agalarseaa vqaagdlpyl lgiaydarar alighgdlaa
      781 agavaalave rfaesgavve hglahqllat vhgrlgdvaa araelgqakd ayrqsgadwl
      841 agqlarverr laaqgqrhag rettlttrel qvaeligqgl tnrevaerlh vsqktvethv
      901 srifskfdvr srvalarrla sradps
//
LOCUS       WP_357625256             258 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            sediminicola].
ACCESSION   WP_357625256
VERSION     WP_357625256.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=26007
     Region          21..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mnarsyvvtg ggrgvgravv erlagdggtv vvverdadal dwlaghpdad rlhavtgdaa
       61 deavteraad raeaaaplag wvnnaavfrd aalhtapage vfdliavnlr pavvgagtav
      121 rrflaagsgg aivnvsshqa rravpgalpy atakaavegl tralavdygp hgvranaval
      181 gsihterhaa flagldpaga drveaelarl hpvgrigraa evadvvafll strasfvngv
      241 tlpvdggraa lgldpear
//
LOCUS       WP_357625257             126 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357625257
VERSION     WP_357625257.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14509
     Region          11..118
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtkqfqgsl keadlrrads lareifsdva nkwalliidi lgertlrfge vrngiegish
       61 kmltqnlrml ernglvernv hptvpprvey tltepgralr qtvhtmcdwt hqylghieds
      121 rrrfda
//
LOCUS       WP_357625278             244 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357625278
VERSION     WP_357625278.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..244
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=26652
     Region          11..241
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mderwikrfh papdaparvi vlphaggaas ayfklsaalh paldahtvqy pgrqerrhep
       61 pltdvrllaa gvadalpdde rptllfghsm galvafelal ilerrgtaph llvasgrrgp
      121 styrdewvhr rdpagvaael rklngtdpvf lqdpelfemv lpalradyra vetyksdpda
      181 avgcplvvfv gdddpkttve earawqrntt grfdlrifpg ghfylddqva evtdalvalv
      241 alsg
//
LOCUS       WP_357625269             162 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357625269
VERSION     WP_357625269.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 162)
  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 162)
  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..162
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..162
                     /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=17524
     Region          1..138
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msnrheller iiaesqrhya ayalfnqama drlgmhptdl qcvalldlea gpvstghiar
       61 ltgltagsas rlvdrlekag lavreadped rrrslvrlap gvrerigqaw dtpggaygev
      121 lrsytdaele liadylrrat qvgldqagrl ttdrpptapp ga
//
LOCUS       WP_357625319             198 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357625319
VERSION     WP_357625319.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 198)
  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 198)
  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..198
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..198
                     /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=21324
     Region          31..175
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mlppmdelre lvtarlaafp rrevppapgv rraavtvcvl eddagdpyti lirrsphgrn
       61 agqwalpggr lddgeqpvea alrelaeeta vsgvrvagll ddyvtdsgfv itpvvafggr
      121 qrpvadprev asvhavpler flapgvprws agllqmplgp sivvhaptga ilwqfaeval
      181 rgrelrvfdv aqphwtrt
//
LOCUS       WP_357625347             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357625347
VERSION     WP_357625347.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 Nonomuraea"
                     /db_xref="taxon:2593643"
     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=15806
     Region          1..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 meqigldldr svgyqlkrah aalraamdav lrrhglttpq yaclelldqr pglsnaelar
       61 gafvtrqsmn vvlrnlqdag lverpqaaph gralpatlte aggarllaar advldverlm
      121 vrgldpartg lvvdaligma aalgepapds
//
LOCUS       WP_357625249             213 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Nonomuraea].
ACCESSION   WP_357625249
VERSION     WP_357625249.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=22484
     Region          18..>87
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mhdvaviedp aaaeasldpm rsrllaelve pnsattlaar vglarqkvny hlrtlekhgl
       61 velveerrkg nvtervmrat aasfvispva laavqpdpnr spdrlsagwl lavaarlvrd
      121 lgelvtgavr arkrvatfgi dgevrfasaa draafaeelt sfvtalvgry hdesaeggrp
      181 hrlvvavhps vgsarsaqsa qsaqgeapvg teg
//
LOCUS       WP_357625363             265 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357625363
VERSION     WP_357625363.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=26731
     Region          3..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 mattlagrra lvtgaasgig aaiarrllqe garvmiadvd agrgartard lsaafqeadv
       61 sdegsvtalf drvtdefggl dvlvnnagva esgggvigvp vaewrrvldv nvtgtflcar
      121 aafpllaaag ggavvnlssi fgvtglpafp aysaakgaia nltrqlaveg gplgirvnav
      181 lpgyvdndmg rsrdlldadd aaealrqrea aaarqpigrq cspdeiatav afladprssf
      241 vtgtllpvdg gflaqgdwrg sggla
//
LOCUS       WP_357625369             395 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357625369
VERSION     WP_357625369.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..395
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42164
     Region          4..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 mtsladlrvi daatlfagps aammlgdfga dvikiehprr gdpsrghgas vdgvglwwks
       61 lsrnkraaav dlsqsegqei lrrlvarsdv lvenfrpgtl erwgldpkdl lelnprliva
      121 rmtgfgqsgp marqpgfgtl aeamsgfaam tgepdgpptl pplaladgia glamsyaimv
      181 alharertgr gqvvdmaiie pimgllgpqm tayralgavp rrtgnrsssn aprntyrtrd
      241 grwlavstsa qavaervvtl vgradlvaqp wfssgsgrva hvdeldeava twiaardade
      301 viarfeeaqa avapiydvrd iaedpqyaal gtfvelpdee lgtvtmqnvl frlsdtpgev
      361 rwpgrslgrd tdevlgeldy gaeeiaglrg kgvia
//
LOCUS       WP_357625400             119 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Nonomuraea wenchangensis].
ACCESSION   WP_357625400
VERSION     WP_357625400.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 119)
  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 119)
  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 119)
  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 119)
  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 119)
  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 119)
  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..119
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..119
                     /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=11852
     Region          1..73
                     /region_name="Cytochrome_CBB3"
                     /note="Cytochrome C oxidase, cbb3-type, subunit III;
                     pfam13442"
                     /db_xref="CDD:463879"
ORIGIN      
        1 mrlgrelyma tcaschsgaq sggtlahgla appllcstpt qiaeavrigp gampafppsv
       61 lsdaevnsia syltttrpql dhggnplggi gpvaegaval laglgllllf irligkrap
//
LOCUS       WP_357625412             253 aa            linear   BCT 28-DEC-2024
DEFINITION  group II truncated hemoglobin [Nonomuraea wenchangensis].
ACCESSION   WP_357625412
VERSION     WP_357625412.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18524105
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..253
                     /product="group II truncated hemoglobin"
                     /calculated_mol_wt=28473
     Region          <25..93
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
     Region          109..226
                     /region_name="TrHb2_O-like"
                     /note="Truncated hemoglobins, group 2 (O); uncharacterized
                     subgroup; cd14775"
                     /db_xref="CDD:381284"
     Site            order(124..125,137..139,145,148..149,152,164,173,176..177,
                     180,182,187,190,217,220..221,224)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381284"
ORIGIN      
        1 miveyiryri paeaqaefea aygraarsla eapqcvdyel srcvdepacy ilritwtsae
       61 dhlkgfrage hfpaffkeir pyveqieemr hyeqtqvrgp gasvpslhew aggtealerl
      121 terfyelvka ddvvgplfah mdpghprfva mwlaevfggp arytgerggy phmlgmhrnk
      181 giseqqrrrw vnllvdaade vglpddpefr aafmgyiewg trlalansqp gatpveqapv
      241 phwgwgvapp yqg
//
LOCUS       WP_357625449             653 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA cytosine methyltransferase [Micromonospora sediminicola].
ACCESSION   WP_357625449
VERSION     WP_357625449.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12774760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..653
                     /product="DNA cytosine methyltransferase"
                     /calculated_mol_wt=72701
     Region          55..429
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
     Region          440..>653
                     /region_name="mutY"
                     /note="A/G-specific adenine glycosylase; TIGR01084"
                     /db_xref="CDD:130156"
ORIGIN      
        1 mtvtaaepar trkprkregy gvklvrgpfv rlaphpdsce gaadlpayaa rvrrsgkpla
       61 adlfsgaggl slglqkagye vvlsvdhdae avethrhhhg glsvnwdlgd pavirtvadl
      121 vrdcqiella ggppcqpfsk agrsmirhrv ryaerdpyde rrdlwrsfie virlarppav
      181 lmenvpdmal dkemfifrtm vhelesmgys vqaqvvdtwr ygvpqfrqrl ivvaladgal
      241 fewpphaler vtvwnaigdl ppveggwrpe ggaegwtdya epvteyqrsm raevtdadkr
      301 kvfdhitrpv reddarafel mdattrysdl peemrryrdd ifddkykrld edglsrtita
      361 hiakdgywyi hprqgrtltv reaarlqtfp dwfrfagpps aafrqignav pplfaehlag
      421 avrrsiaaar paetstreva allaewfdsa evrglpwlra ttrwqviqae mlldrasvdv
      481 vrplwpliar wtspqatvla eaelgeigrw tgkearagri velagrladn pavldddagl
      541 rsipgvheal adlailvvps ageddseepv lstkgvlrva arylgepvdr rnrltdgrla
      601 varmigddsd arrahlglie lantlcrpve pmcdacplqk vcrssqagsl rlf
//
LOCUS       WP_357625535             228 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357625535
VERSION     WP_357625535.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 228)
  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..228
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..228
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=23404
     Region          3..223
                     /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 mdilligglw ldastwddvv pelaalghrp vpvalpgqgd gsrsatladq vaavlaalda
       61 asgqvmvvgh saactlawla adarpervak valvggfpaa dgaayadffe vadgvmpfpg
      121 wgpfegadsa dldeearraf aaaaipvpeg vakgvvrltd errhdvpvvv vcpefgpaea
      181 kawidagdvp elararnvtf adldsghwpm ltrprelagl laaeageg
//
LOCUS       WP_357625530             334 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050733].
ACCESSION   WP_357625530
VERSION     WP_357625530.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Rosinski,J.A. 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 334)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..334
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     Protein         1..334
                     /product="helix-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=35863
     Region          1..296
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mraarlmslv lllqargrmt aaelarelev sertvhrdvl alsgsgvpvy adrgrgggyr
       61 lldgyqtrlt gldraeaeal flsgvpaalr emglqgvaat arlkaaaals pglrdapata
      121 aqrfhldapg wfapgdpppa alaplaravw sdrpvtaayr drrrtlepyg lvlkagvwyl
      181 agrvrsrflv frvdrfgeve phegvferdp gfdlaafwae haaafarsll retvtlrlte
      241 agvrmlrhva dpaalddala slqpdgtmrl gvesvavays qvlrlgpeae vlgppelral
      301 lagaaarmar lyepreeapg drpfgaalrp lgdp
//
LOCUS       WP_357625575             181 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357625575
VERSION     WP_357625575.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 181)
  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..181
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..181
                     /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=20803
     Region          1..142
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mredtrtriq eialrlfteq gyeatslrei aeelgvtkaa lyyhfktkdd ivasladlrv
       61 aeveevlawa rsqprtlear reivtryaea lrkpryleva rfmernqtal rdhpkllrlr
      121 dtmlelvnel sdpddplavr iarsmalfal hagkwmpqee svseeeinaa slevalrlle
      181 p
//
LOCUS       WP_357625594             382 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357625594
VERSION     WP_357625594.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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..382
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..382
                     /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=42216
     Region          1..381
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msmrlrfala savvtavlgt lvvtgvyltv rhslqyrsgl itptrikvrn gweiprgdty
       61 yevardrvmq vrvayerdtl anvrtvggla vlaaagiafg agrraagwvl rplsdvteta
      121 rrvaqnhdlt eriayegphd elkeltgtyd tmlgrlarsf dgqrrfvana shelrtplti
      181 nrtlvdvavr rpdatddvkr lgeslllvna rherlidgll alaegeqavl drrpfdltdv
      241 aehvldlaad eaaerevtih rlldsapttg eavlverlvq nlvenairhn hpkgevwvtt
      301 rqraervelv vantglpvps yeietifepf rrlhgdrlrs drgsglglsi vrviseahrg
      361 tvvarprdeg gltitvelpa el
//
LOCUS       WP_357625601             600 aa            linear   BCT 28-DEC-2024
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Micromonospora sediminicola].
ACCESSION   WP_357625601
VERSION     WP_357625601.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..600
                     /product="type IV secretory system conjugative DNA
                     transfer 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]"
                     /calculated_mol_wt=63846
     Region          167..556
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 msravgpggs sdssglvagg laglalaaag avwlplrltd ppgydgeglf raaaglisgt
       61 itwtvactlv avaevlvvaa lgagvlllvr grrlrgsrvd raarhmarrg dlahlspdgv
      121 tasarrlras ladagtvapd dagvlighav vggmelrqsw edmavdiwgp rtgkttarai
      181 patvsnpgpt lvtsvkgdii datrelraar geiwvfdpqq vwgqpqqlww nplggiatit
      241 darrlaehfa saerepgmqr daffdpssee lvanlllaaa vggrsvldvy rwavnprdes
      301 padiltgagf qlpadsivgv inmpeqtrgg vyagaqkmlm cltepsvtaw vsppsspmir
      361 qfrpedfvat cdtvyllsqg gpgspaplia altdavlrag emrartspgr rldpplvsvl
      421 deaanicrir qlpalysyyg shglpiitvl qsyaqgvdvw gregmrklws aanvrtyggg
      481 vadpefleel srligehdvm trstsssgsg fgqrsvsrqt rrqrvldvae lhalprgrmv
      541 vyssgappvl artapwqtgp yaeavrasia rwdpdrrndw nlqadtsqlq sfdnavqepr
//
LOCUS       WP_357625602             298 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357625602
VERSION     WP_357625602.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=31001
     Region          1..298
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 marrllamgn paaggddeat rravldvlgg gadavfrale rpddldrala ehpdrepvvl
       61 ggdgtlhrvv aallargele srpvglipmg tgndlartlg ipldpadaar vvldgaprpl
      121 dllvedapgk givlnavhvg vgaeasrrat plkpvlrraa yaagallagv rskgwrlrvr
      181 vdgepvadgr rrvlmvgvgn gasigggtpl tpdarpddgl advvvsyavs pwgrlaygvl
      241 lrlgrhperd dvatfrgrav vvegepvpan adgelcppap hrswtlrpaa wrvvaprs
//
LOCUS       WP_357625642             306 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357625642
VERSION     WP_357625642.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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..306
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..306
                     /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=32646
     Region          54..285
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtphgftita dgpfdfagcl rfaedwpvts alpsdgralr faycaehdwk pigvrvtaap
       61 ggvevattrp agpsirgeva rilsldvdgt gfaktgeadp vlgdvqrrrp glrplcfwsp
      121 weaacwaviv qrssmlvasr vkqriaarfg aevvvdgqaf qafpppvsll eagglglpaq
      181 keewvrglar aaldgvltae hlrslapeea laelralpgv gpfsaglili rgagapdafp
      241 gdeprlfail reayglpedt ppaayrelaa awrpyrswas flfrattygt lddqaltrpg
      301 ppaarr
//
LOCUS       WP_357625670             406 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357625670
VERSION     WP_357625670.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..406
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42531
     Region          129..401
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtppplpavp pdtpsdspst atsddcgpaa sdsgdsgada hgmgsppppt sgrgtsgmga
       61 sgawaaegrg glldpcrril aeaagtgrap drraldscra agvraaelgv plrslvddal
      121 aaavavadgl ppvlpalrra vsalmegyeq aqlaairdee earrefvddl lqgraerlae
      181 raehfglrla esyvvavagn lpptdltphr naveralvtr fgshnvlvav rddllvcvap
      241 atlpaavgef thhvrarfat gwrvglgrah rgpggvvtsy reaaqalela dalslkidvv
      301 raadllvfpv llrdrsaied lvtsvlspll eargghepll etleaifash gnqtaaarrl
      361 rlspravtyr lerirrltgf spddptqrft letavlgarl lgwpng
//
LOCUS       WP_357625677             121 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357625677
VERSION     WP_357625677.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   4  (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
REFERENCE   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..121
                     /product="PadR 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=12708
     Region          1..101
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mtersmqept fliltalaag pqhgygvitd ilrisddrvr lragtlyaal drlqgeglve
       61 aggeevvdgr arryyrltsa gatrlageae rlrrhadtav srlgarlgvp arpaaapgga
      121 a
//
LOCUS       WP_357625752             272 aa            linear   BCT 28-DEC-2024
DEFINITION  MaoC family dehydratase [Nonomuraea wenchangensis].
ACCESSION   WP_357625752
VERSION     WP_357625752.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11973509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..272
                     /product="MaoC family dehydratase"
                     /calculated_mol_wt=29009
     Region          2..269
                     /region_name="PLN02864"
                     /note="enoyl-CoA hydratase"
                     /db_xref="CDD:178455"
     Region          152..272
                     /region_name="HDE_HSD"
                     /note="HDE_HSD The R-hydratase-like hot dog fold of the
                     17-beta-hydroxysteriod dehydrogenase (HSD), and
                     Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other
                     enzymes with this fold include MaoC dehydratase, and the
                     fatty acid synthase beta subunit; cd03448"
                     /db_xref="CDD:239532"
     Site            order(167,170,173..174,178,180,184)
                     /site_type="other"
                     /note="dimer interaction site [polypeptide binding]"
                     /db_xref="CDD:239532"
     Site            order(171,177,179,182,199,201,204,207,211,223,226,228,230,
                     244,253,255,263,269)
                     /site_type="active"
                     /note="substrate-binding tunnel [active]"
                     /db_xref="CDD:239532"
     Site            order(172,176..177,179,182,197,200..201)
                     /site_type="active"
                     /db_xref="CDD:239532"
     Site            order(177,179,182,200)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:239532"
     Site            order(208,211,221,223)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239532"
ORIGIN      
        1 mpldhavvgq egpahertwt ardtmlyalg vgaglselef atekgqrvlp tfavlaaqsp
       61 grrlgdfdra mlvhaeqafe lfrelppagg vrtsstvtgi ydkgsgalvt tearavdlet
      121 gepvivsrss vfirgeggfg gergprddwr apdrapdhki tyatrpeqal ayrlsgdynp
      181 lhsdpefaar agfdrpilhg lctygvtgra llhavagsdp arfkamsgrf sspvfpgesl
      241 tvsiwadggd vlfrtakddg tvvidrgrat vt
//
LOCUS       WP_357625755             189 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357625755
VERSION     WP_357625755.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 189)
  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 189)
  AUTHORS   Rosinski,J.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..189
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..189
                     /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=19548
     Region          15..88
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          98..186
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(101,116,118,130,133,137,171,173,186)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mgsgttgepg liaviaaslr rereraglsl selakragva kstlsqiesg agnpgvetlw
       61 alatalgvpf srlvdpprpa trvvragegp athsevagyt atllascppn arrdlyrvva
      121 rpgeprlstp hppgtvehvv laagralagp aeepvelrpg dyltypgdvp hifdalapdt
      181 savflmehi
//
LOCUS       WP_357625779             512 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine/threonine protein kinase [unclassified
            Nonomuraea].
ACCESSION   WP_357625779
VERSION     WP_357625779.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 512)
  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..512
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..512
                     /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=55734
     Region          15..483
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mqvndrslig qevagyyied ivgkggmavv ylaldprlsr rvalkilnpv lsvddrfrqr
       61 filesrtvas iehpniipiy eanadadgvl yismryvdgl dlrrliydrg plplaqasqi
      121 faqvaaalda ahahdlihrd vkpanillag dhvyltdfgi tkhrtsisgl tqtdqfigtp
      181 rymspeqink ehidgrcdqy alacvvyeal sgrlpfqrdn diallwahla eqptplaqvr
      241 pelppevdav maralakspe qrypscgefv aalrdamsgh ldaqpldrsp agpvpvrrre
      301 paarggtgri grpgrlpiia atltaavaal vlvvlvvvsq rgeswaryrp tpaapvsfey
      361 padwtvrthe dlfavvspha tefesmfvsg agadwapvtp liteepdsva gvyvqvsdtl
      421 sttatdaqmk amlegllpgk ievsgpvteq agtspatryt gsltdrdsga rlgfvgyvvd
      481 rrpkpmllly fcarntcdda vqarvrqsvr ls
//
LOCUS       WP_357625802             263 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357625802
VERSION     WP_357625802.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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]"
                     /calculated_mol_wt=28025
     Region          16..251
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msalglamve avpsaalrpy vtrltayrer pgapvtraep ampgavlila fgtpmevdgq
       61 rltafagglg drftvtrtag ptegvqvflt pfgarrlhgl pmrhltnrvl pagellgpwa
      121 eaaverlaat pswrerlala drlllarlrq gpevgpevpw awarllesgg rvrapelaaa
      181 lgwshrhlva rfqdqvglpp ktaarvirfg raarllrsga apalvaaecg fydqahlnre
      241 fralggvtpg qisprprggr aas
//
LOCUS       WP_357625820             499 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357625820
VERSION     WP_357625820.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 499)
  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..499
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..499
                     /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=50172
     Region          25..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(35..36,65,70,75..78,94)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(100,102,138,140,142,159,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(155..163,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <227..488
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mlgagttlnd ryvlagrlgg ggmgevwrae dnvlgrsvav kvmtpalten atfaqrfqne
       61 aramatlthp gvvdvydygt ceisgrqvtf lvmehvrges ldrvlrrgpl dpaaamrlva
      121 evgdalaaah aqgivhrdvk panlmvregg gvaltdfgia hsvsaghlta tgqmlcsagy
      181 capematsse vtpavdvyal gvvayecltg kppfqgetpv qiifkhlnsp vpelpgevpa
      241 gpravvtral qktpeqrwes aaamaaaarq alaapgvaph gagdtgptaa pgtgvagtva
      301 tgpstgpvtg paggpggfpg vggtasgalp gpadataagt aagtlparpe rrgrrtarva
      361 ltvaaavlvs agvagavwlr pdqssgeatv aptsvadtta tagpktpsts rqqnvppvrq
      421 sptavptkgv tprptpsvtv tptapvtqtp taapttpeps keptkeptpe ptqpgpeppa
      481 teppsdppgd iqcvrepcp
//
LOCUS       WP_357625844             317 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Nonomuraea wenchangensis].
ACCESSION   WP_357625844
VERSION     WP_357625844.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..317
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=33981
     Region          16..>183
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 maasspvpfa islvtaaavl lsmpspaqat apkptesqlr aqlkrlntkv dklieqynlk
       61 rvelakaqet aktakerlat aertlaaseq rvaelarlry qngdlpvpgf mpnaagaavl
      121 dqltaeqqal vqgvatarde kkkaaaeaea lavkiradaa svakqrdeae dviddikdkl
      181 adlvpystgr nsdgswapql psgadnitar trlmreqvtk nfalpfsvgc frsgasgehp
      241 lgracdfmms sggtmpsaan nalgdriaaw alqnqsklgv kyviwkqrin mgsgwramsd
      301 rgsitenhyd hvhismn
//
LOCUS       WP_357625851             329 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357625851
VERSION     WP_357625851.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 329)
  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..329
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=33655
     Region          112..324
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mvsedthsgd rsrgrfarls rlarlgdvpv vamlvwagwl avpwsfsgla qaraaaaeaa
       61 lppppaaaet sppptphvgr gagmpaapak awglpaaarp aatvlpahet getrrdafaa
      121 qrawiagevh daaghglaai amqagvalvt ldddpeqtra slrairetsl talaqlrtal
      181 drldprpsdg tsgtrptdgg lralvdgvra tglrvkvepd dpavpaplqd avyrvvresl
      241 tnvlrhagps agtrvrlaae pdayiveivn hpsgapgrag essaggrgld glrarvaalg
      301 ghltagprpd ggfrvlarfp atgplgeda
//
LOCUS       WP_357625940             392 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357625940
VERSION     WP_357625940.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 392)
  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..392
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..392
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41409
     Region          7..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 mvddgvgple gvlvadfsrv lagpyatmll adlgadvvkv egpqgddtrs wtppvrgevs
       61 tyylgvnrgk rsialdlrdp ddaaaarela rradvlienf rpgglakygl dhasvraanp
      121 rvvyasisgf gsgpgahvpg ydlmvqamsg lmsltgepdg ppyragisvf dvmagnhavi
      181 gilaalrhre atgegqhvev nllssaltgl vnhssayvag gvvpyrmgna hpsvfpyepl
      241 ptadddliva aandgqfrkl cevlgipeta ddprfarnad rtarreelrp ilvaalaakg
      301 avewfellve agvpsgpiqt idggfamaer fgldpvvevg egeravpttr hpirfsatpa
      361 ryplpppeld ehgaelrawl agpdrplgee kp
//
LOCUS       WP_357625957             123 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Nonomuraea].
ACCESSION   WP_357625957
VERSION     WP_357625957.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=13920
     Region          17..98
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mprsgktttp dgvptllddv fpalanpvrr rilqlllqgp qsvnslaahf dmarpsvseh
       61 lkvlrdsglv terrvgrerh yslcqapmqe isdwlhpyea ywrdrlrllr dtvveeegdy
      121 qgg
//
LOCUS       WP_357625963             338 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: aromatic ring-hydroxylating oxygenase subunit alpha
            [unclassified Nonomuraea].
ACCESSION   WP_357625963
VERSION     WP_357625963.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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 338)
  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 338)
  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 338)
  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..338
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..338
                     /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=37404
     Region          29..309
                     /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 mttppapatg qddpvprpmg ehlphegddg lytqswypic maadltagkv vgaeflggrv
       61 vafrdragrp svvsayclhl gadlsvgtvs dgmlrcrfhg wvydeqgvcr rtgsgdpvpd
      121 garlfrfpta erfgvvwafn gtepifqipd lpcpedevra rrgrfghlam epwmvsahtl
      181 dlqhlslphg fdlktppadt arhsahshgy dlvgslpdgt tydvqidihg pnlflqtgll
      241 ngrwyfwmts pslpapgrtd sffvygvrkg eseteesaeq alqqvfeaqm qfysddsdif
      301 dtihfqpgll tsrdrtlatf ldylrtypra nparefls
//
LOCUS       WP_357626015             933 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Nonomuraea wenchangensis].
ACCESSION   WP_357626015
VERSION     WP_357626015.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..933
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=97904
     Region          1..494
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          446..928
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mdraaalasd lrrrgvadvl tdgttravhs sdaslyrvpp llvarprtae dvhaavelca
       61 rheipltarg agtsiagnav gpglvldfsr hmdrvlaldp eartavvqpg vvqaalqraa
      121 apyglrfgpd psshtrctig gmignnacgs ralgygrtsd nvtglkavag dgthldlper
      181 agpaalrdlv aanlatirte fgrfgrqvsg yalehllpen gfdvtrllvg segtlavlte
      241 atvrlvadpa hralvvlgya diaeagdaap gllafrptac egldarivdv vrarrgpgav
      301 pplpggaawl faeiagddea evrkraglla aghpdalvvt dpakaaalwr iredgaglsg
      361 rspagrpaha gwedaavppa mlgrylrdfe ellaghrltg lpyghfgdgc lhiridlpld
      421 rpggrqvlre flvaaatlva gyggslsgeh gdgrarsell plmyspaaig lfeqvkgvfd
      481 pagtlnpgvl vrprpfdadl rvpaarpapg plalayrhdg gdfgqavhrc tgvgkcradn
      541 tgtggvmcps ylatreekds trgraralqe mlnggdvsgg wrspevheal dlclackgca
      601 sdcptgvdma aykaevlhqs yrgrlrpash yalgrlplwa rlasrmprva naalrapalr
      661 rpalalagvd arrtlpafap rtfrswfarr prpaagepvl lfvdtftdhf apevgraava
      721 vleaagyapr vtarrgccal twistgqldq arrilgrtvr dlaaaagdgv pivglepsct
      781 avlrsdalel ldeataapva ratrtlaell aatpgwrppp ldgvrvvaqp hchhhavmgw
      841 epdlrllrea gaevrrlggc cglagnfgve kghyevsaav agqqllpale eaapdaavla
      901 dgfscrtqia dlsprrgvhl aqlladrltp egn
//
LOCUS       WP_357626047             198 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357626047
VERSION     WP_357626047.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 198)
  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..198
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..198
                     /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=21063
     Region          3..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mapedrraal iaatlpllre ygttvstrqi aeaagvaegt ifgvfpdkas llraalasaf
       61 dpqpavdala aidtrselre rlreavtllr agmsananlm tapralmadd aelhqrmldg
      121 rhrigtaiaa lvepdrhrlr rspegtahll lmliavsvhr gfglggefgd medeeivsvl
      181 ldgllvrpsp dpstesps
//
LOCUS       WP_357626082             608 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Nonomuraea].
ACCESSION   WP_357626082
VERSION     WP_357626082.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 608)
  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 608)
  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 608)
  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 608)
  AUTHORS   ter Beek,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 608)
  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 608)
  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..608
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..608
                     /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=65787
     Region          49..599
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mavttrtqpp rrppwrrrll yrlrvlrhdp tallglvlvv llaylvvapl vavlsdafrl
       61 qygdevhagq qpgewtgyyl wrvfrspisg llfweplvnt ivvaigttlf alllgggtaw
      121 lltrtnvpgr gwlagalvvp ymlpswtfsl awltlfkner sggqpgflqa qgvrtpdwla
      181 ygalpiiitl glhyypfvll lvgnalrrid aqledsarvl gaprrtvvrr ivaplmlpal
      241 ssavllvvgr vlgtfgtpyv lglpadyrvl stglfqsird rgtgvasvla tvivvigvli
      301 vftdmrlvre hrrfvtvggk gamdrlgdlr rrrwpafalg llvfavsvlv pvltlllstl
      361 trtpldlstl tldywladrl pgavgfphgv lrgpelweaa wnslrvvgva alicavagll
      421 igyvvvrgta priggflrqv sflpylvpgi afaaaslslf avargpvpal ygttfllilv
      481 mavthlpyss rsgiaamtql grepeeaaqv agaswwqrmr rivfpiqkga lvtgitlpfv
      541 sglkelsivi mltttgtell ttlsiglvdy gytqlanavv lviallsftm tsltqrltks
      601 glasglgg
//
LOCUS       WP_357626090             287 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome c biogenesis CcdA family protein [Micromonospora
            sediminicola].
ACCESSION   WP_357626090
VERSION     WP_357626090.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..287
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=29451
     Region          14..248
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mgetfaelas sgplllavga avlaglvsfl spcvlplmpg ylsyvtglag sdlegarkgp
       61 rltppveega plntvggagt gvgvverape rttaavkgrv lagtllfiag ftavfvstai
      121 lfssvgrlff ryertleivi galvvvlglg ylglvpgmqr efrirwlpaa gllgapvlga
      181 vfalswlpct gptlgavlgm avteggtdra vvlavayclg lgvpfvafgl gfqrllgvfr
      241 avrrnsrwvt riggallivi glalvtggwq nvviwlqthv gvgevsi
//
LOCUS       WP_357626107             266 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Nonomuraea wenchangensis].
ACCESSION   WP_357626107
VERSION     WP_357626107.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=28886
     Region          73..>210
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mmtramslat avavtvpaag lpahavagat raavacpqvf ghggyptgan pwdrdkirqp
       61 nnpralndqk swgadgvegd vqltrqgtka vmwhntstng ltgtkqnitd lwwaagtgnl
      121 qsrtitrgpy tgervytlre wldqvrsrgl valleikpet kpilsnatya taawkeisdp
      181 ikerqgaqri lvystdtwiq aelakrhptl lkggaarwtd svgweeppps wtgntahwqs
      241 vlaaapasvm tnytkeyraw lkgkca
//
LOCUS       WP_357626155             209 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: adenylate kinase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357626155
VERSION     WP_357626155.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 209)
  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 209)
  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 209)
  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..209
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..209
                     /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=23746
     Region          1..202
                     /region_name="Adk"
                     /note="Adenylate kinase or related kinase [Nucleotide
                     transport and metabolism]; COG0563"
                     /db_xref="CDD:440329"
ORIGIN      
        1 mgvqgsgkgt qsklladgld lthinvgeif rwhvkqhtki gaqvrrvvaa gelvgddlve
       61 dvvrerlqqh dwnygfvvdg fprnrrqaef flesydidgv ihldlpdeev rrrvlarrlc
      121 srcgmdynli ahrpetegrc dvcggelvar eddtpealar rlrdyhdktd pvlelfrgke
      181 yvtsvdargd katiqrtire rlglppyqp
//
LOCUS       WP_357626172             514 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Micromonospora sediminicola].
ACCESSION   WP_357626172
VERSION     WP_357626172.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 514)
  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 514)
  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 514)
  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 514)
  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..514
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..514
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=55883
     Region          47..492
                     /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 mglsrrallr gaavvgatvg lpaaglagyv wtttrrsnvg rvsfdrplai pllaagvrga
       61 dgrllvdlrl qsgrtellpg rqadtwging sylgptvrvt rgdvlaprvr ndlpeattlh
      121 whgmelpaec dggphqmirp galwqpawrv dqpaatlwyh phphgrtkeh vyrgvaglly
      181 vddgeadgll pddygvddip vivqdrnftr qgrldedgia fgglsvtgll gseilvngvw
      241 gpvldvrter vrlrvlnasn ariydlvldh grgfhvvagd ngllpapvpv dhlrlspger
      301 aellvelrpd ervrlqsrpp dldanlavdr laggadefdi lelratpslr papplpvalp
      361 apprlappla grrervlrfg dflidgramd lsridavvpl gsteiwrlrn dvgtphnfhi
      421 hnaafevldv agrppgaaww grkdtvyvpp dtevrllvqf gaypsptrpf mfhchllahe
      481 dagmmgqfvl vppgtdprvv apppvvdhts phhd
//
LOCUS       WP_357626209             332 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357626209
VERSION     WP_357626209.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=33382
     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 mwlagaaavl aasmiagllg gaadispgqv alqaldwlpl vhvdsglapv eqgllyeirl
       61 prvllagvvg allavagagy qgvfrnplad pyllgaaaga gltatvvivl fptgagavpv
      121 aafagavggv vlayalgnta grsggtatlv lagvavtsfl taiqtfvqqf kveelqriys
      181 wimgdvgggw eqvrlvlpya avssvllllh grmldvlsvg deeatslgvr agrvrlavll
      241 aaslataaav avsgligfvg iviphvarrl aggsyrivlp lsllggaafl vladvvartv
      301 iapaelpigv vtmfvgapff vgvlrltrrt tt
//
LOCUS       WP_357626248             151 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357626248
VERSION     WP_357626248.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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..151
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..151
                     /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=15077
     Region          3..150
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 myisaradya lramlavada gstgdggsgg ggsgggelvk aasladsqdi plsflqgill
       61 dlrragllhs hrgteggyal trppaeisvg dvlravggal tsvrgmpadr tgyhgvatgl
      121 rdvwlavdga ialvvdrttl adlladrapa p
//
LOCUS       WP_357626277             265 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357626277
VERSION     WP_357626277.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=25943
     Region          2..223
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtgagrglgh ayalacaahg aavvvndvdg aaahavaaei aaagghavae pgsagsweva
       61 arlagtaele fgrldglvan agithhgppw eedearlrri tevnvlgvqf aavhamramv
      121 rrggggsivt vvsgarfgip gmsaygatkg avaamtagwa rdcasagirv navsplaetd
      181 maaldtrpdr palgapgdva pvvvallsda trgvtgrivr fdgaelgvya pevlapvtgw
      241 aagdpaasia ealarlggaa aagpd
//
LOCUS       WP_357626294             274 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357626294
VERSION     WP_357626294.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=28364
     Region          6..274
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtethpllgr tavvsgagrg lgraistala gagavvcgvs rnaeelesla aeikaaggqa
       61 yafpadirsp adldrlrdav saevggvdil vnnagnlvkr pvvplpvdea agekvgqpgs
      121 gpagvamtde ewdsvldthv rgslhlvrsf vpgmlerrhg rviniasssv arsanltvsy
      181 qvakgaiaql tralakewaa fgvtvntiap ghfrtsmtqa lhdspegqaw lkeripmrrt
      241 gdprelgala vhlsgdlasf itgqtifidg getl
//
LOCUS       WP_357626332             249 aa            linear   BCT 28-DEC-2024
DEFINITION  sirohydrochlorin chelatase [Micromonospora sediminicola].
ACCESSION   WP_357626332
VERSION     WP_357626332.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..249
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=24891
     Region          7..245
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mrpahltaap pvvlvahgsr dpraaeatra laravavacp grpvlpswld htdpgptevl
       61 rglaadghsr vvlvplllta ayhrkvdipa avaaagadld vrvtdvlgpt ggtvdgrlla
      121 glrrrlaeaa gddpgdldav vlaaagtrdp aargsvgrva aalgaglgvp crvsyasaap
      181 pevgdavarl raagagrvav aayflapgrf hdgvraaars agavavadpl tdlpeladlv
      241 rrrvdaaar
//
LOCUS       WP_357626344             321 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora sediminicola].
ACCESSION   WP_357626344
VERSION     WP_357626344.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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 321)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..321
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..321
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32870
     Region          56..301
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrrrpvalat aaalfgaglt gcseptaptg rpapdtpptt taptprvpag kaptesfavg
       61 vrqvklnrdg drplpvtlwy paegaaggaa ersapaadgr fpvvlfshgl garpedyqvl
      121 ltrwaaagfv vaaprfphtg rggdgnpldv lnqpadvsyv ltrvlalgek agdplrgrld
      181 pervaatghs aggvttiglf tagrderlda givfagtalg vgtafagaaa pqlfvhgead
      241 evvsyaagra vydavpwpka mlslpkgdhg rallgdgral gvvadttvef lrwtlygdpa
      301 akkrlpadaa rgglatlddr l
//
LOCUS       WP_357626404             447 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Nonomuraea].
ACCESSION   WP_357626404
VERSION     WP_357626404.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..447
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49037
     Region          19..431
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mtdgtarrpe aesslevepd mtaevehllr veapqvlgal arrfgqfdia edavqealla
       61 asrawpvdgv penprswlir igyrrmvdll rsdqarrrre qeagmaelam reparqarps
      121 qetddtltll llcchpalsa tsqvaltlra vgglttgeia haygtaentm gtrisrakqq
      181 laragarftp ptdadrdsri aavmqvlyli fnegytasag dhlsridltr esirltrmlr
      241 dslpgdaevt gllalmllte srrgartgad delvpldeqd rtqwdpelir egtelidsvw
      301 sgrevgpyql qaaiaavhaa apspertdwp qiavlylwle rlnptapvrl srvvavakay
      361 gparglalld dlnrrhrldq dpltrqrera vrahllqmtg daagaatlyr eaaaltdnqv
      421 errylagrad rstsavtgas aagrrpd
//
LOCUS       WP_357626421             413 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357626421
VERSION     WP_357626421.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 413)
  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..413
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..413
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43307
     Region          5..405
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mpgpgyaffg eeeeknilea vrhwrdasga fgaptapsqi grfeaeaaar fgarhcvavn
       61 sgtsalltal aalgigpgde vivpgymfva slativysga tpvlaeidds ftldvadvrg
      121 rigprtraim avhmlgapsa mqelrelade hgvaliedva qacgatyrgr plgtwgdaga
      181 fslnpfkvit ageggfvltd ddrthqrafs fhdhgflpgg vevgdgdllf glnlhitefg
      241 aavaraqldk idevlrrtre vkrafveqiq drpgvrrrtl ndaegecgtl avyvfddasd
      301 aravaadlgv tvlaespkhn yaripalpal aagprspapf raslpasaaa syrpgalprt
      361 ddllgrsiav aiglsdtylg agfgatvrss aeqidqaaat frsaldrvlp srs
//
LOCUS       WP_357626440             170 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357626440
VERSION     WP_357626440.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=18725
     Region          27..162
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msqpkplnlp fdpieraaqt wrvhfgpssa maavtsimra hqillsqlds llkpydltfa
       61 ryealvlltf srtgalplwk igerlmvhpt svtntvdrle rsglvsrmrn pkdgrgvlae
      121 itdagrdvvr ratadlmaad fglsmygege lhamfdqlrt lrvaagdfge
//
LOCUS       WP_357626486             315 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PLP-dependent cysteine synthase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357626486
VERSION     WP_357626486.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..315
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..315
                     /product="PLP-dependent cysteine synthase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34015
     Region          1..295
                     /region_name="CysK"
                     /note="Cysteine synthase [Amino acid transport and
                     metabolism]; COG0031"
                     /db_xref="CDD:439802"
ORIGIN      
        1 mrfdsliesv grtplvglpr lspapdvrvw akledrnptg sikdrpalwm iqqaekdgll
       61 tpgctilept sgntgislam sarlkgyrli cvmpentsee rrqllrmwga eiisspaagg
      121 sneavrrake laaanpswvm lyqygnpanw rshyettgpe iledlptvth fvaglgttgt
      181 lmgvgrflre rvpgvrivaa eprygelvyg lrnvdegfip elydesvltt rysvgsadal
      241 rrtrellaae gifagvstga alhaalgvaa kavkagerad vvfvvadggw kylstgayeg
      301 tldeaeerle gqlwa
//
LOCUS       WP_357626490             197 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora
            sediminicola].
ACCESSION   WP_357626490
VERSION     WP_357626490.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=20985
     Region          1..194
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 misdapaflg qfarhplatg avlpsgsala rditaaiprt gqplvvelgp gtgaftrtiq
       61 qrlagrgqhl avelnpsfaa alsrrhpavr viradaatld rvlsdrhlpa advvvsglpw
      121 aafgagrqla vldavlrtlr psgafttfay rhalatrpar rfrrlltgaf eevtvgrtvw
      181 snvppalvyh crrpvpr
//
LOCUS       WP_357626495             242 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Micromonospora sediminicola].
ACCESSION   WP_357626495
VERSION     WP_357626495.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 242)
  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 242)
  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..242
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..242
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24897
     Region          36..>167
                     /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 mafldslvdr ldalppglll lvaaavlage vgllagvvlp aattmltvgl laraghvdlg
       61 valavttaaa fagdqlgyle grllgprlrr gplgrrvgee rwrraealva akggsavllg
      121 rwtafvrtlv prvagaaglp yrrfvladgl avvvwvpgtv lvgwaagglp agvpaaagva
      181 vvaavalalg frhlrvrrrr tvhracsgsv rgrrgptrrr pgsrrpgagr tapvrrgaid
      241 rc
//
LOCUS       WP_357626515             836 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Nonomuraea].
ACCESSION   WP_357626515
VERSION     WP_357626515.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 836)
  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 836)
  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 836)
  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 836)
  AUTHORS   ter Beek,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 836)
  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 836)
  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..836
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..836
                     /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=85346
     Region          21..814
                     /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 mlrttlaglr ahrlrlllts laitlgvgfi agtfvltdti eaglaqkvta dagkvdvavi
       61 aegpdgrlpa allgkvrglp gvtdaqgvvr gpapligkdg kaagdapttg lsissgplsr
      121 avivsgtgpg sddlaavlde ntakaqgvkv gdtitvldpq rrkrmfklvg lldpgvdqel
      181 aytgvvgftp amaqrmtdek gfreidvaga dpdalrrtva aaaggegrev ltgtqladrl
      241 arqagvqtka ltvgllmfgl vsmlvaalvi yntftilvaq rtremallrc igatrgqvfg
      301 svllesvvig llsavlglla gyglgagtla vlgaldaplp tgaavrltpg tigvglavgl
      361 lvtigsavlp artatrvapv aalrtqleeq afrtgllrmv aagvfllagl gttgvgalvl
      421 epgqqvslfv vmgggaltfl gvlilgpvlv rplsalvgav parlfgvpgr lavdnsgrnp
      481 rraatttval tvgvtlmtli svlttstrvt ltdklddqfp idyllatqer dsaiprsvge
      541 elrrrpelas vvqirdieak vsgpkggasr fdvgaydgpm dppvtagsmr glgdgqvave
      601 ddvaarlgvr vgdslslttk eagavtlavv amlngsestl pdltvaataf dryfgalpds
      661 rvmvdaksdv aadrsravvd aataayptvk vssstevrge fdealdmllm ivtgllglai
      721 lisllgiant lslsvhertr esallralgl trpqlrrmls vealvlglig alvgvvlgav
      781 fgwaavrami dgavyvvpyg qvalfvvlsg lagvlaallp arraarasiv galasg
//
LOCUS       WP_357626546             285 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357626546
VERSION     WP_357626546.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 285)
  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 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   3  (residues 1 to 285)
  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 285)
  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..285
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..285
                     /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=29557
     Region          1..284
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mepvavglvg agpwarmaha pmlakgphtr lagvwarrpe aaaelgapvy erieelfdhc
       61 eavafcvppg vqaelgvraa ragkalllek pladsldgar rladavaesg vasqmvltlr
      121 yavqtrtfla rcgkiqpfgg haanisgvll gdhpfatpwr lehgalldvg phvvdlldaa
      181 lgpvvgvrah gdpfgwigll leheggavse aslsmaavgd lppatfavyg rtgnavllpf
      241 dddpldavae efartvragg ghpldaahgl rlqhivadav sqlrg
//
LOCUS       WP_357626576             466 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357626576
VERSION     WP_357626576.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..466
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..466
                     /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=48499
     Region          1..447
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mdadavvvgs gpnglvaavm laragrrvll leaadrfggg lrsgeltlpg rvhdfgatvm
       61 amalaspafr glelkgvefv hppvpaahpl dgrpavlvhr dpvrtaaglg rdarawlatv
      121 gataraglpl velllkplgp wggvppaafa aaagfgaaal lpattfarra frttearavi
      181 agmaahsvld lrspvsagyg lllaslahlv gwplvrggsq vladalvael ralggeavtg
      241 hrvrrlaevr apvvvldvtp rqllamadlp payrrrlery rygpgvfkld waldgpvpwr
      301 dpavagagtv hlggtleeia lseaeasrgr vsprpyvlvv qpyaadptrg ghtlwaychv
      361 pngsradltg aieaqierya pgfrervlar hamgpaelea fdpnlvggdi sgglsslaqf
      421 lrrpvwspap wrtplpgvfl csaatppggg ahgmggwqaa rlalrp
//
LOCUS       WP_357626589             497 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357626589
VERSION     WP_357626589.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 497)
  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..497
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..497
                     /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=52024
     Region          5..113
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          <348..491
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrirdlldip glrlrlltgd pdrefgtvhi tdlpepgryl sggelvltgl mwrqepedsa
       61 rfvttlaeag vaavgagaal lghvpddlva acaaaglpll evptevsfrt ltelaapras
      121 gdvraalgrh rrlvaavaeg adlrelfela aaelgvtgav vtasghvvvg tvaepeevar
      181 ayltaprlpa raagrtifav grghraagwa laldgdlldr adlgyelaac vglermrree
      241 grrverrlae qlvvaalada daaelnarlr tcglgaaepy avvdvsaprp gatrgpdpat
      301 lggqvveell grevvaaaga dgavavvplr gstagelaar lraaaevlsa lpgtrvcagl
      361 sgsltgaaal kggveeagha rrlaearggg vvtsdeiyth alllatvpad vrrsfaarll
      421 tplldydrrh qselvrtlgi fldcagswna caerlhvhvn tvryrvrrie eltgrnlatm
      481 adrvdfylal rdsappr
//
LOCUS       WP_357626598             147 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357626598
VERSION     WP_357626598.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 147)
  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 147)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 147)
  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..147
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..147
                     /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=14729
     Region          <5..147
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrggqslaea lesylaewge rsgiaveiwa lpatdvpagv cegvmtamre aldnverhsg
       61 artvsiavta gsgglrvtvs ddgrgfdasg aatgrpaght rrpakgqaag qgiarmraaf
      121 aevggslsvn svlgegttvt gvvpkrp
//
LOCUS       WP_357626638             201 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357626638
VERSION     WP_357626638.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 201)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..201
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..201
                     /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=21994
     Region          2..198
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 maqrksrtdr ridlieaarr aiirhgidgv qlshvaeeag ltsgavlyhy pdlsellvea
       61 qhagmerfye qrlrqlstvt dpvkklvmti rsglptgpld pdvrllnelg gaagrnrvyg
      121 vlltslydrq vsmyqsildt gsalgvfrls gdsqslarnl valedaygyr itarhpvigp
      181 eeaaelilsy artatgndlv h
//
LOCUS       WP_357626649             380 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357626649
VERSION     WP_357626649.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=39887
     Region          1..380
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mripqapvdg srpmtvpiyq tsgfsfsdpe vmadamgnps gpfvysrytn ptvrslelav
       61 sgleggagai atgsgmgain tvllgllrpg dhliaqqaly ggtsamlgdl adrfgigvty
      121 vpendpaalr aarrpetklv yletisnpaa lvadlpgmca aarelgllsm vdntfatpml
      181 crpiehgadv vvhsttkyms ghsdviggla vfadaglyer iwrfsielga aadpfaawlv
      241 vrglqtlalr merhcanadh latrlaehpa vsavhwpgla thpsyelark llpgfggvfs
      301 felaggraag erfmkavrla mlapslggve tlvmhpatts hrslnaeela angigegtvr
      361 iavgiehped lwadisqala
//
LOCUS       WP_357626650             485 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: dihydroorotase [unclassified Nonomuraea].
ACCESSION   WP_357626650
VERSION     WP_357626650.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 485)
  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 485)
  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..485
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..485
                     /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=53058
     Region          5..482
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
ORIGIN      
        1 mtdlllknvr vvthdrsepv madiavtggr vdqvtpglpt egvpeviega grlafpgvvd
       61 ahqhwgiynp ldedagsesr asaqggvtta ltymrtgqyy lnrggayadf fpevlaraed
      121 rayidygfhl apmsrghiee lpdlverfgv psfkifmfyg ghglhgrsad qsaflmlpeg
      181 erydyahfef vmrgvqaare rfpelaseis lslhcetaei mtaytrlvee agdlsglaay
      241 sasrpphseg lavfiasyla hetglgnvnl lhlssrkald aavrmartfp hidfrrevti
      301 ghlladieta sgigakvnpp irpredveal wkyvldgtvd wvvsdhaccr eelkfgapae
      361 dvflakagfg gaeyllpgli tegrrrglpw griaaltswn parryglrtk gtiapgfdad
      421 iclvdpdatw tvraaesdsa qeytpfegfe ltakvtdtfv rghhvldtgk ivgrpqgrfv
      481 rrpva
//
LOCUS       WP_357626689             400 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Nonomuraea wenchangensis].
ACCESSION   WP_357626689
VERSION     WP_357626689.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=40978
     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(34..35,38,41,74,124..125,127..129,132,152,155..156,
                     159,227,230..231,234..236,239,267,271,320..321,325,329,
                     345,348..349,352..353,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 msstsvekpp sfmraqvggl prpfwalwgg tlvnrlgtmv mpftgvyltq srglsvtaag
       61 lvmgvfgvgs llsqplagml tdrigrratl sggmlatgaa mlalgysvsl pavlasmlvl
      121 gvvvdlyrpa snalvadlva paerpraygl lfwginlgys vgmtaggwla glgflwlfwi
      181 davscvvfav lvwravpetr pegarqatgg fgavlrdrvm vaftlvvlgn alvyaqtmtm
      241 lpvamtkaag lstaqygtam alngvlivvv qplvsgwlgr rdpartfalg lavmgagfal
      301 tafvsstlgl tatiavwtag eivtagiagt ivaalappel rgryaglfgl awsaaavlap
      361 llggpllelg pgalwftiga vglvsaagml algpairrrt
//
LOCUS       WP_357626700             642 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea wenchangensis].
ACCESSION   WP_357626700
VERSION     WP_357626700.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 642)
  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 642)
  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..642
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..642
                     /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=65479
     Region          31..>435
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrlrsllasa svlaftttga liaapahaaa gdpeiaknvt aevrgghkvr avielkkgqs
       61 vdavaadaek askgtqvvdk klsddflvat ldkatleevr tddrvaavye drlsvatldv
      121 stkligadka naagwtgkgs tiavldtgid rdhpffagri vgeacfsats tdpyygakpl
      181 cpngqsvqtg agaadaetaa cvanganqcy hgthvagiaa gkkaagapsn gvapeagilp
      241 iqvftrldgp vcqeelgraa pcfatfvsaq kaalqyvdsv hagknviavn mslgggakqt
      301 khcdadpsag alkdeivwlk qfgvsvviaa gnegftdgvs spacvsaava vgatddqdav
      361 aafsnrgall dlfapgvqin savpgggyrv lngtsmaaph vagalalvrq aypqlsgegr
      421 iaklqdtgka ityggvttkr idltaalppk tspsptptpt gsptpaptgt htpgpsptat
      481 ptptpttspe dghrnvdpgi ygdpqpvpdt csrgrggkpl sakawateml rgkgslsddt
      541 lrcyltlaqn gskvfpeltg agtlgkaykv latkskaaka lldrellaaw lnyahgvyns
      601 sakvhgrttl kqavaaaerh ragksaaamk kaalylyrhv nk
//
LOCUS       WP_357626754             271 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357626754
VERSION     WP_357626754.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 271)
  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..271
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..271
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27593
     Region          13..270
                     /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 mlgaagvlsg tavsadgtpi aydrygsgpa vvlvagamme rahptmagla ealapwftvf
       61 sydrrgrggs gdtapyaver evedlaavia aaggsakvfg gssgaalale aatrlpgvte
      121 lalweppyhv ddsapplpdd faeqlaalva agrrdtvver fmveaaevpa eavagmraep
      181 fwaaaeatah tlayeaavmg pgnalpaarl agidrpalvl ngedspawmr ragaavaaal
      241 pgavhrvlee qthavtveal apelleffvr g
//
LOCUS       WP_357626706             237 aa            linear   BCT 28-DEC-2024
DEFINITION  PaaI family thioesterase [Nonomuraea wenchangensis].
ACCESSION   WP_357626706
VERSION     WP_357626706.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 237)
  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 237)
  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..237
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..237
                     /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=24584
     Region          <159..237
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mttaalqtvl tvpqrfrgpe gvsnggwiag tmaealnggr savevtlhap tpletelrle
       61 hvantvslsr gddllveaip vaedlkgpgf vpfndaarae agfagfkahp faecfacglr
      121 epgdglrifp gpvagsdlva agwrvpftva gedgvpasii gavldcitgw ahfgpgesal
      181 lgrlavqihr rvhpggrysv varptgrdgr kmfgesaiye adgtlvaaar atwiapr
//
LOCUS       WP_357626842             334 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 5 protein [unclassified
            Nonomuraea].
ACCESSION   WP_357626842
VERSION     WP_357626842.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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 334)
  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..334
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..334
                     /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=37658
     Region          5..324
                     /region_name="BglC"
                     /note="Aryl-phospho-beta-D-glucosidase BglC, GH1 family
                     [Carbohydrate transport and metabolism]; COG2730"
                     /db_xref="CDD:442036"
ORIGIN      
        1 mrrygfnlqw mfwkepgaep apvdervlda iaswgfdfvr mpcdyrfwtr gldythpder
       61 vlqvldgyla acrerglhls lnlhrapgyv itgwesehhn lwadqeaqdg fagiwtgfaq
      121 rhlgvpaeal sfdlvnepps vgergftrda heavirrvva eirkidperp lvidglgggh
      181 lampeladlg vihstrgyqp msvshyraew wpgspdlpep aypgdydgrh wdraalrdfy
      241 apwlavaarg vpvhvgefgc yeyspndval rwladvlgvf asfgwgyalw qfegpfgvvg
      301 hrrpgarfer ldgfevdrdl lellqahrag avsp
//
LOCUS       WP_357626850             269 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357626850
VERSION     WP_357626850.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   ter Beek,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 269)
  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 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..269
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /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=28867
     Region          2..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mslvrcdgvv qiyraqdvev valrdvdlti gvgetvallg psgagkstll wllagllrps
       61 agrlwldgad lgrldqrrld rlrathigmv lqnparnlig hlsaaqniaf aqravrrdrr
      121 rarellarvg ladaadrpag rmsggeqqrl alavalanap kllladepts qldeesgrrv
      181 ielvrdaadd gttavvvthd pavgealdrt vtirdgrvga egrrgedfvv vgregavqvp
      241 peyhhllppg smvrieeled gialrraep
//
LOCUS       WP_357626904             252 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357626904
VERSION     WP_357626904.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..252
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..252
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27214
     Region          4..246
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mplmpgaepy hhdggqigvl lchgftgtpq slrpwaefla ahglsvslpr lpghgtrwqe
       61 mnrthwedwy aevekafedl qgrcaevfva glslggclal rlaevhgpav kgvvvvnpsi
      121 asdvpllrla pllkwfvpsv pgvandvkka garelayart pvkaaaslpg lwalvqadla
      181 kvtqpllvyr svddhvvkpt svaiirrrvp hatieeltds yhvatldnda dtifagsldf
      241 irthasvplq rd
//
LOCUS       WP_357626963             179 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: cysteine hydrolase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357626963
VERSION     WP_357626963.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..179
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19839
     Region          5..172
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mpgiamivld mlnpyeheda drlvhgvepi vpklaelagr ahrrddveli yvndnygdfa
       61 atredlvtra lkgrrpdlvr pivppsdcaf lakvrhsafy gtalehmlrq rgigtvlltg
      121 qvteqcvlys aldayvrefd vvvppdcvap vhgdlgraal rmmernmsae iipsrrllv
//
LOCUS       WP_357626990             197 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: D-glycero-alpha-D-manno-heptose-1,7-bisphosphate
            7-phosphatase [unclassified Nonomuraea].
ACCESSION   WP_357626990
VERSION     WP_357626990.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  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 197)
  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 197)
  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 197)
  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..197
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..197
                     /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=20916
     Region          9..173
                     /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 mfvqrgpgav lfdrdgtlir dvpyngdprk vqpmpgavea lsrlrraeip vavvtnqsgv
       61 akglitpdem gqvnarveel mgpfdawaic vhddgdcctc rkpapglvir aaavldvspr
      121 dcvvvgdigr dmeaaraaga rgilvptpqt lhqevleaae vaadltevtd rllgdleaap
      181 vpaghsrrar vigwsrw
//
LOCUS       WP_357627109             237 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357627109
VERSION     WP_357627109.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 237)
  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..237
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..237
                     /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=26216
     Region          17..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtgkqissvw trdarpartp grtreeiara tlelldaegl dglsirklga klgagatsiy
       61 wyvenkdell elaydeiwge itlpipqslg wrdtvsafay smrhvmlrhp wvgsligrlp
      121 algpnalsms drlrktfrla gfdgmdidya natltayvlg tvipeiawsa tmggeeldkd
      181 amretfehva rdfpdllerl vevneevtvs etdtlravsf dfglvavldg learlrs
//
LOCUS       WP_357627047             369 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea wenchangensis].
ACCESSION   WP_357627047
VERSION     WP_357627047.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..369
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=40516
     Region          14..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 mtdrdaagda gglvavmtgf artlraagva adhdrtqnll aalahldvtd raavywagrl
       61 tlcaspddlp rydrcfaayf agrratlart avtsvtrhla aredpggeee gdgeataapa
      121 tasraeilrh rdvarlteae raevhrllal lrdrrarrrs rrferahrga ldrrrtirea
      181 lrkgevaglr hrahatrpra vvlfvdvsgs mapyaetllr fahalvrsep ratrvysvgt
      241 rltpltaelr hrdpgtalne askaipdwsg gtrlgeelre ylsrfsarga ivviasdgwe
      301 rgdpgllatq marlsrqayr iiwvnphkgy edyqpltggm raalpyiddl vaghslaaye
      361 qlserlaha
//
LOCUS       WP_357627096             330 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Nonomuraea].
ACCESSION   WP_357627096
VERSION     WP_357627096.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..330
                     /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=36223
     Region          3..319
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mekhfpitkg llkrqvgavk avdgisfdvy kgetlglvge sgcgksttgr lvtrllepta
       61 gqvlfegrdi thmsqgrlrp lrrdmqmifq dpysslnprh tvgaivgapf riqgvqtdng
      121 ikkavqeile lvglnpehyn ryphefsggq rqrigiartl alkpkliiad epvsaldvsi
      181 qaqvvnlled lqneldltyv viahdlsvvr hisdrvavmy lgklveiadr kslyaapmhp
      241 ytnalmsavp vpdprgrarr erirltgdvp splnpppacr fhtrcwkaqd ickkveppla
      301 elatghrvac hfpenapdvp aagkddpvta
//
LOCUS       WP_357627116             514 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357627116
VERSION     WP_357627116.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 514)
  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..514
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..514
                     /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=52114
     Region          12..269
                     /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..37,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msdsaavtvg gryrllkaig kggmgkvwqa hdevlgrdva vkevlpppdl tgperevfsr
       61 rtfrearaag rvahpgvatv ydvleedghp wivmqlvrsr tlgeairedg plsphdvaki
      121 gvqllqalra ahaagvlhrd vkpdnvllae ddravltdfg iatteddstv trtgvligtp
      181 afiaperaag graspasdlw slgvtlyqav eghspfqrtn plttlgavmh aepepatrag
      241 vlapvlggll rknpaermtl ddaerrlaai vmggspgpas ttrimptpvv gagaagldag
      301 tvpggpadag aagetraaga gmagmdawgt agtatagada raayggaeaa dghygtasag
      361 agvaggsgrr rrgvtlaala ggvvlvaavt ggaawwssra tdsehtpsst qpavvtesss
      421 rpsskeeesr paqteppssr sgeapapers pdaspsptgd rptqkktpar tsapaddedq
      481 nggddnggge krdtgegddk psdsdtsgvi egsq
//
LOCUS       WP_357627126             600 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357627126
VERSION     WP_357627126.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 600)
  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..600
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..600
                     /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=64551
     Region          14..269
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(14,38..39,71,76,81..84,96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,79,95..98,102,104,141,143,
                     145..146,148,158..159,162,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,42,44,79,95..98,102,143,145..146,
                     148,158..159)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,102,104,141,143,145,162,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(158..166,175,176..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msdrkqagrr iagryqlqei igrggmgivw rahdelldrt vavkevryaa algeevqlln
       61 rrtmrearaa arfehpnviv vhdvieeddr pwivmqlvqs rslgtvikqe gplppkrvae
      121 iglavldaly raheagvlhr dvkpenvlla ddgrvvltdf giatletetq ltvtglagtp
      181 afiaperlkg lparresdlw slgatlytav egrsphergm alatmhavlt depdpaphag
      241 pladviagll akepvqrlty eeaermlrra iaqaspeatt qfpasapret rssakparpr
      301 rqpyqpkppa eddtptdpdl lpaaagtppe tgarltpvtg gpkppaestm dagapsqqrr
      361 pgpviaaala vllvagvagy lglrqgpgdd pgdagastag vptsasppss psspsasegt
      421 psddpspsas aspsasasps aspsetksad aalpkgwkwy kdkkmgftig lppgwdvwdr
      481 gglqvkfkgp gaasnayvmv eeapkpgkdp ykdwkkqepv lkhnfggykk ldikrvdyqk
      541 saadwdftwn tntgktrvrn rgfvtdngra yaiywhtlns hwksdyrffe gfcasfkpak
//
LOCUS       WP_357627115             237 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357627115
VERSION     WP_357627115.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 237)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..237
                     /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=25483
     Region          9..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          75..226
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 maeqaevlrr tplsrdrilr aavaladgag ieslsmrnla qdlgvvpmal ykhvankdel
       61 ldgmidvvvg eiappepdtd wkpalrrrvl aarqvmrrhp waplaiearn matvavlayl
      121 dsvvgtlrag glsvdlthhv mhamgsrvlg fsqelfddar ragrsgaves gppaalppea
      181 aarfphlaav aaaashddds vvgsgcddqf efefaldlll dgverlhrrg wtshgrr
//
LOCUS       WP_357627139             314 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357627139
VERSION     WP_357627139.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 314)
  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..314
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..314
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=34857
     Region          42..310
                     /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 mrlssalala ataialpall srsrgetvpm dararqdapg sfvrlrhgtt hvvtdgpesg
       61 epilfipgat lslwvwdgly erlaragyrt irydrygigf sdrpevehdq qlfeeqivdl
      121 ldtlgidrpv tlvalafggp iaaefavhhs ervsrlclvs pdgfatplnp glrlamlpgi
      181 glpffrvfgd ralksrlpgy srdrrvvarv qarmlpelry qgfkrsllsa lrnvpvhgae
      241 ylyrfvdtgd vpvqvvwgrq dpvtpmppee vlrtvfsrad lrlldgvghl phyerpdeta
      301 aivldflrah qera
//
LOCUS       WP_357627156             493 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea wenchangensis].
ACCESSION   WP_357627156
VERSION     WP_357627156.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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..493
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..493
                     /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=50945
     Region          120..354
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 martlvttlv taltalggla iqpspattgs agsgtavaqv raraeasplm rpgqavrywt
       61 parqaeagat plpatrpplv pasasrllsv pdgkritpgg dangyarvrr pytgaarsrv
      121 tgrlffvnsg gqgdscsasv vrsasgllva taahcvysvp egaergrwhs hfafvpaydg
      181 ratderqrep ygrwggrraw kpgaytglag gdwnsvydfa lievgrrert lqdavggalt
      241 plrsqggwht viatgypgvl grkpydgrdq lwclartqpa raltavnaat vpatvsaavp
      301 aagpagklet ynchlskghs ggpfvvkgtr dlvgvlsagt edgeadgysv analnvesyg
      361 vivgeadprg vydalsitat gptgpvrrgr tatvtatvtm rgllaaaqvp vtfrvpdgaa
      421 ftalsgaaca rtarqaacai dtvrpghpvr ltarvrltad aprqvpvtah vaatrldpsr
      481 rdntavarlp vqg
//
LOCUS       WP_357627171             736 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [unclassified
            Nonomuraea].
ACCESSION   WP_357627171
VERSION     WP_357627171.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15774079
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..736
                     /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=73664
     Region          12..703
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          18..287
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,68,70,99,115..118,122,124,161,163,
                     165..166,168,177..178,181,197..200)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,68,70,99,115..118,122,163,165..166,
                     168,177..178)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(28,122,124,161,163,165,181,197..200)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(64..65,91,96,101..104,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(177..185,193..200)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          515..573
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          578..637
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          643..703
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
ORIGIN      
        1 mptaqplrtg dprrlgsyel tgrlgeggqg vvflgsrgee shgeqssgdg shgekrcgee
       61 rrgeeryavk llhgpvgder aaflrevela khvarfctaq vieagfdegr pyivseyvdg
      121 pslqrhvvlt gprggaaler lavstatala aihragivhr dfkpqnvllg ddgprvidfg
      181 laraldaaat vsgrgvgtpa ymapeqitas avtgaadvfs wgatmcfaan avapfgqdsv
      241 apvlhrilta ppelgrldgr lreivaacld kdarnrpgsr elllellgda dgvpaevlrs
      301 ppphilrasa swpsdpagph sasgtdsgaa sgpasgpvag aapayalags apvarpeatg
      361 tphgyhlpeg asfhtgrppg gsaqssggay papgtyhsal gtgraardse qtrrvgqafn
      421 raglavsaal lvsaavlvtv vvpafrhagf gpaaagptvi ttapagtmpg tghatprker
      481 hstgahtqpa adpatdpvsv paaeppvpva ggvhvpalgg ldrgsavkal eraglvagtv
      541 tqvdsprkvg qvlgsqpqag vavpkgteva lrvsaglvvp avtgmrrgpa etaltsagla
      601 lgavstscsa rpdgqvlsss psagtriags gkvalvvskh gtkvpgllgr tgeaasgtlr
      661 gaglavtqdt rlvsdesrag tvlaqsvaag tcakpgsgvv ltvgvlaqsd pdptepsepp
      721 atepptptat asdrpa
//
LOCUS       WP_357627252             108 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357627252
VERSION     WP_357627252.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..108
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11632
     Region          <29..108
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mvrdellrlr araeaeaatl aqdlqalfla srdsnaddeh dpegatigfe raqltallag
       61 arkriadvdd alrrvdaaty gvcercgqpi gderlaarpf arfcmaca
//
LOCUS       WP_357627268             434 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357627268
VERSION     WP_357627268.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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..434
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..434
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45447
     Region          4..434
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
     Region          193..>278
                     /region_name="PHA03269"
                     /note="envelope glycoprotein C; Provisional"
                     /db_xref="CDD:165527"
ORIGIN      
        1 mrcdprfsrv revferhfad geeegaafav yldgepvvdl wsgvadrhtg rawqedtpvy
       61 aysctkavta tvllqlaerg lvdvgapvae vwpefaaegk ervtvehllt haaglpvved
      121 pvpveefgdh paiaarlagq rplwepgsah gyhalsygfl vgevvrrvtg ksvgelvaae
      181 iagplgldlw mgapdpvlar aarltaggdr phatltptpd tstpdspapd spatvspapd
      241 spapvspatd spaagdapsa salsdlagas ddggafgrma rdvrdpqslm nralgnpsmq
      301 rlkgganhpv imragwpaag lvttaralag fyrsllagdl lrpetlrdal rprvggpdrv
      361 lhldssfglg ymrpastffv psatafghtg lggfvgfgdp ehgvaaayvm nrmadavsgs
      421 lrayrlteav yrsl
//
LOCUS       WP_357627322             281 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: phosphotransferase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357627322
VERSION     WP_357627322.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..281
                     /product="phosphotransferase 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=30302
     Region          2..249
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 miadiralla rrlpghevrs ivrlgqgldn vvyevdgeli vrgakvadgd atrreaalla
       61 avrdisplpv pevvfsdpda aviayrklpg rplnlspvpd pgllaeplga flsalhaapa
      121 dglrelappd hypaptllqd agqdyrdves hvpeehrplv eaflrapvpa etdtvrfchn
      181 dlgaehllad petglltgvi dwtdaaltdp ahdfariyrd lgpevfeata ahydgglged
      241 drdrvrfyar caliedlayg lstgprryad aalahlartf s
//
LOCUS       WP_357627339             175 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Nonomuraea].
ACCESSION   WP_357627339
VERSION     WP_357627339.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 175)
  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..175
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..175
                     /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=19039
     Region          1..173
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mnsetaarap appgagpvla glyrehwlal vrlalllvgd resaedvvqd vfsrlhgkrp
       61 etlslayvrv cvlnasrsvl rrrgvaarav pgrrdepvgs aetaallgea raemlaalgr
      121 lprrqrevlv lryyldlsda diaratrvre stvrstasra ldrlkrelge pevqa
//
LOCUS       WP_357627352             420 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sediminicola].
ACCESSION   WP_357627352
VERSION     WP_357627352.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..420
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45309
     Region          1..414
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mtptdhaved llrelapqvl gvlarrfgdf ataedavqea llaatrqwpa egvpehprgw
       61 ltqvayrrmi elvraeaarr dreeraarrs gddrrtapaa depltgerdd tlvllflcch
      121 ptlstpsaia ltlravggls taeiaraflv peatmaqris rakqrirdsg lpfrmpepad
      181 rqarlaavlh vlyliftegh taslgddlrr vdlseeavrl tremrrllpd dsevagllal
      241 mlltdaraaa rtgpsgelip laeqdrsrwd aaaiaegtsl vtaamirgpv gpyqiqaava
      301 alhdeapsaa dtdwpqilal ygvlerltgs pvvalnrava tamvhgptag ldalaglagd
      361 srlagshrld aarahlyema gdrdaavthy raaaarttsr peqeylqlra ahlatppprr
//
LOCUS       WP_357627364             198 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357627364
VERSION     WP_357627364.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 198)
  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..198
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..198
                     /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=21339
     Region          10..195
                     /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 mgyansdhgd taplavkilv aggfgvgktt lvgavsevap lrteeyltha svgvddldgl
       61 ngktsttval dfgritisre lvlylfgtpg qerfwfmwnd lvngamgavv lvdtrrldvs
      121 fasidffesr ripfvvgvnc fhgvrdrape eirkaldldp qvplvlcdar drkasrdvll
      181 alvdhlmaah srqtapgs
//
LOCUS       WP_357627393             296 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357627393
VERSION     WP_357627393.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 296)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..296
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30413
     Region          10..292
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mtsnteqsav tvlglgpmgr alagaflavg vrttvwnrtp gkerelverg aavarspeea
       61 agaspltvic vvnydavdav vrrpevagal kgrtlvnlta dtpdrardta awagdhgigy
      121 ldgaimtptp tigtpagvfl hsgpeelyrt hrptldalgg ththlgadvg raaaydiall
      181 difwtamagy ahalavarae gisarelapf aqgigailpp lfeegaadad sgtysgegnp
      241 itsavssmah ivhtseahgi dasvmraaeg larrvigrgh gddgflrvte llnpsa
//
LOCUS       WP_357627433             377 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DHH family phosphoesterase [unclassified Nonomuraea].
ACCESSION   WP_357627433
VERSION     WP_357627433.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 377)
  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..377
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..377
                     /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=39542
     Region          63..343
                     /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 mtpdvharta ppdrtappdr tappdhtapp gravtppeag atgdrgvtgq dpsgagvpea
       61 aweravelis radeialach vspdgdalgs mlatgfvlrs lgkrvvasfg drrfavprll
      121 gflpgqdmls ppedypaape lmitfdsass drlgllgana aaarelivvd hhpsgsgfgt
      181 lglispkaaa tamlaeqliy rlggtldrdi atclyaglvt dtgsfrhsst spaahemaar
      241 lvatglrtde iarelwdrsp fgylkvlaaa ldrvtledgl vwtyvtrvdr aayglpysel
      301 egvidivrra deaevavvck edddgawqvs trskgavdva avctamgggg hhsaagftsh
      361 dgveetmarf rellrkv
//
LOCUS       WP_357627446             324 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357627446
VERSION     WP_357627446.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=34824
     Region          3..314
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 marptarvla lleilqaggg ftvadlagrl gvdertvrry aahladlgip vearrgrygg
       61 yrlapgyklp plmltdeeav avmlglvaat raglvttega aaesatakir rvlpavlarr
      121 idsllgtvdf tapirrsapp gievllvlae aarhqqpvsi tytswrgrsg erqldpyglv
      181 fhasrwyvtg hdhhrgavrt frldrigtar ptqgrfdvpa gfdpttqvla glaavpyahd
      241 isvvlhtsle earrrippsv galtevpggv rlttrverld gaaqmlaglg wpftidrpqe
      301 lrdevralat rlladaddvr aggr
//
LOCUS       WP_357627455             437 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: M16 family metallopeptidase [unclassified
            Nonomuraea].
ACCESSION   WP_357627455
VERSION     WP_357627455.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=46946
     Region          17..431
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtltttlhpg hegagvvrrt vlpgglrvvt etmptvrsva vgmwvgigsr deapehmgat
       61 hflehllfkg tptrdameis asiegiggei naftakeytc yyarvldedl avavdvladv
      121 vtsslitddd vesergvile eiamhdddps dvvyeqfaaa lygdspigrp ilgtvesina
      181 lpreriaeyy hryyeprrtv vsvagnvrhe dvvelvaray eragalggpl dcdpprttgp
      241 giethsgvtv ldrpteqanl vlgttgmart ddrrfalgvl naalgggmss rlfqeirekr
      301 glaysaysyt sayadtgqfg iyvgclpski ddvlkicrde varvvsegld pdeivrgkgq
      361 mrgglvlgle dtgsrmsrig knelvydell svdevlarid gvtpdevaev aadvltrplt
      421 lavigpygdk dfsgais
//
LOCUS       WP_357627481             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sediminicola].
ACCESSION   WP_357627481
VERSION     WP_357627481.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=16408
     Region          20..147
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdtpdqdvvp arlaglpswl isqtavragr mvsdglaamd argyhfrlla tldefgaasq
       61 aalgrrsgih vsdvvaalne ladrdyvtre pdpadrrrnv vtitpagrrq lrrletrlav
      121 vqdellapls peeraqlsrl ltrvlrhhsa
//
LOCUS       WP_357627482             110 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Nonomuraea].
ACCESSION   WP_357627482
VERSION     WP_357627482.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=12067
     Region          9..110
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mteaavppdp dvvralrals npmrlqllsw lreperhfpp eqaiadpaev gvcvshiqak
       61 aglaqstvsa ymaeleragl vrstrvgkwt hykrdeqria qlvtvlgetl
//
LOCUS       WP_357627519             598 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea wenchangensis].
ACCESSION   WP_357627519
VERSION     WP_357627519.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=66192
     Region          55..503
                     /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 mtaaigridg takealrrky reerdkrlrp dgndqylrlp adylddpytp rterapktdh
       61 vtvavigggf aglltgarlk eagvqdvril dkagdfggtw ywnrypgaqc dtasyvympl
      121 leetghmpse kyahapeile hcrrigkhfg lyddalfhte vtglewlggr wlvrtgrgda
      181 ftaqfvvmgi gplhvpklpg ipgmadfrgh afhtsrwdya ytggdpagap mdrladkrva
      241 iigtgatavq cvphlarsaa elyvfqrtps svdvrdnrpt dpewfagiat pgwqrrwlen
      301 ftamqtgaqa eedlvmdgwt dlarrvrari aelpevtprt llaafedsdf ekmeeirarv
      361 davvrdpeta rglkawyrql ckrpcfhdey lqafnlpgvh lvdtdgqgve rvtergvvva
      421 greyevdcvi yasgfevgtd wtrragydlt grdgrrlseh wadgmrslhg ihvhgfpnaf
      481 lightqganl lsniphnlte agrtvaavva halahghtev evteeaengw vdlllsgngp
      541 llgspdctpg yynnegqdlg vrgrlnggyp ggaaafftyi dqwrssgtfe glrftqmp
//
LOCUS       WP_357627544             190 aa            linear   BCT 28-DEC-2024
DEFINITION  anthranilate synthase component II [Nonomuraea wenchangensis].
ACCESSION   WP_357627544
VERSION     WP_357627544.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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]"
                     /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."
                     /calculated_mol_wt=20480
     Region          4..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 msrvlvvdnh dsfvhtivqy lrvlgaecdv rprddvread adgfdgvlvs pgpgtpeaag
       61 vsvplvrrav arrqpllgvc lghqaiavaf gatvtrapel fhgrtsdilh dgegvfetlp
      121 spvrmtryhs lavlpgtvpe alevtartad gvvmglrhrr apvegiqfhp esvlsehgyt
      181 llgnwlrrtm
//
LOCUS       WP_357627566             349 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: M24 family metallopeptidase [unclassified
            Nonomuraea].
ACCESSION   WP_357627566
VERSION     WP_357627566.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 349)
  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 349)
  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 349)
  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..349
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..349
                     /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=36960
     Region          18..349
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtilserrar laaalpahgv etllvtsrvn vryltgldss naavlvgadg sarlatdnry
       61 veraqaldvp vveavdtaga lavpgtgiea asmsvatyrr lldrlggdal vplehvvegl
      121 ravkdedele llrtacaitd qafadvcrai apgltereva hllearmael gaarpafdsi
      181 vaagengsvp hhipttrplr agdlvtldfg aqyegyhadm trtvslgepa awqrelydlv
      241 adaqragrea lepgadvrqv daaarsviea aghgghfrhg lghgvgleih eepflgpsrt
      301 grledrvpit vepgvylpgq ggvriedtlv tregepellt kttkellvl
//
LOCUS       WP_357627592             380 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora sediminicola].
ACCESSION   WP_357627592
VERSION     WP_357627592.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 380)
  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 380)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 380)
  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..380
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..380
                     /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=39703
     Region          125..379
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mttwpgvvrr vepylpvlla gavaaatwas atgglgvrsp lptvvillla latgasvlss
       61 rrwalpaaaa vcwlvlaawa avvvaswrag tglrgrqlaa yllgtfpvml vgvavgsavg
      121 gerrlvmatp gnavvfyawl viapaivglw irarrdalaa lrdraerler eqearadrvr
      181 aeerariare mhdvvahrvs lmvvhagale vttadpatve taalirstgr aaltdlrevl
      241 gvlrqepplp lpgrdavgel vresraaglr vsltdevapg pvpgavartv hrvvqegltn
      301 vrkhapdgav avrlrhlpeg ievtvrndps artgpvlpga glglvglrer veltggrlta
      361 gptpdggfll halmpageat
//
LOCUS       WP_357627595             230 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Micromonospora sediminicola].
ACCESSION   WP_357627595
VERSION     WP_357627595.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 230)
  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 230)
  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..230
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..230
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24129
     Region          10..166
                     /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 mdaalellhd tisspwvyla lfaiavvdgf fpvvpsetav itagvfaatg qpdlplvigv
       61 aalgalvgdh vsyaigrhgg arlldrvprd grrraavdra rrgiavrggl iltvaryvpg
      121 grtavtltmg atrfprrrfl afdalaaatw gtysasvgyl gglaferdpi rgllfglgla
      181 ltvtlvvevv rwvrgrraar iraarvlkgd psstagvnrg pfltpppgar
//
LOCUS       WP_357627608             260 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357627608
VERSION     WP_357627608.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..260
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27583
     Region          6..259
                     /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 mrsdptprlv atdldgtalr rdgtvsprta aafarvedsg amlvfvtgrp prwmggvasa
       61 vrhhglaica ngaliydlht eriveshlie aevleevvaq lranvsdlvf sveyeagfah
      121 esdfldrrav eaqaasmtar pcakllalhp hmdadelhvv vhdlvghlvt athssrrali
      181 emsaqgvtka talaafaeeq gieagevvaf gdmpndlpml gwagtsyava nahpdvlaav
      241 dhvtaanded gvaqvleklf
//
LOCUS       WP_357627631             192 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357627631
VERSION     WP_357627631.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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..192
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..192
                     /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=20887
     Region          18..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meaqvtesqv tesrprgrea trerilqaar tlfgeqgyeq vtvrtiaaaa danialvgry
       61 fgskaglfaa vlegeptidr llegeraelp rrlaeyaaer mrrppdspil ralersarhp
      121 eivdvgrerl iaavlqplqa rlgggpdala rarmatavvl gigatrrrlg pavptardvd
      181 rltevfracl ee
//
LOCUS       WP_357627703             196 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea wenchangensis].
ACCESSION   WP_357627703
VERSION     WP_357627703.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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..196
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..196
                     /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=21002
     Region          13..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mnyhdsrlta lglltevhag imarlhpala raglseidfe tvirlarspe qrlrmsdlaa
       61 qtglstsgvt rvvdrlereg lvarqacpsd rrasyavltp vgrerlesvl pehlhdidrs
      121 ftrllpdgel eaflaslrki rdvvrpcata gadltsdaag cekaagrddh dpgrddagrn
      181 ddavpaapls pakpgl
//
LOCUS       WP_357627649             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357627649
VERSION     WP_357627649.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..212
                     /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=22729
     Region          14..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msnptddlpl agrraqaarn daailaaart vflddpkapi aavaeragvg isalyrryag
       61 kedllrtlch dgllrfvaaa eeaaaepddw aafagflerv vdadvhsltv hlagtftpte
      121 emgraavran elvddlvrra rdagrlrpdv vtqdvgllle gcaairvpdp drtrqlrrrh
      181 lavllaglav pgpplpgppp apgefdwrwr se
//
LOCUS       WP_357627745             719 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Stk1 family PASTA domain-containing Ser/Thr kinase
            [unclassified Nonomuraea].
ACCESSION   WP_357627745
VERSION     WP_357627745.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15774284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..719
                     /product="Stk1 family PASTA domain-containing Ser/Thr
                     kinase"
                     /calculated_mol_wt=75886
     Region          10..638
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          446..506
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          515..574
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          579..637
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          645..717
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          664..718
                     /region_name="PASTA"
                     /note="PASTA domain; pfam03793"
                     /db_xref="CDD:461053"
ORIGIN      
        1 mdtttadplv grlldgryri esriarggma tvylaldvrl drtvalkvmh rslaedpafv
       61 rrfigeaksv aslshpnvvh vfdqgtdgdv vylsmeyvpg rtlrevlher grlpareale
      121 ilipvlaalg aahqagmvhr dvkpenvlmt adgrvkvvdf glaraieatn qtrtgvmigt
      181 igymspeqvt tgradvrtdv yaagimlfel vtgrqpydge tpmsvayrhv hdtvpapssl
      241 tpdvppvvda lvahatarep darpadatam lvaavevhrq lprltapgvs hssaqhslpg
      301 tgsyapsgpl aaptaqpssg ahpvpsgpht gahtgahtga rtgpqsgarp tgpaaggyga
      361 qpasqpglpa gspamtlamp qvppggapgp nptvvqprie gpaehaggrr rggfrpswii
      421 iglavvmvaa igltgwyvsr pqyvavpadl vgkdvsiveq kltaggfkvr lapgeyndkv
      481 neglvlrvdp vtgqqvlagt tvtlvpslgp klvlvpkvag msaddarati akagltvgsv
      541 rrlaspdvar ntvirtsplv geklkegskv siyvsagltm pdvshmpkdq aaaflqeqgf
      601 qvqvnevddd aepctviaqa pkanaevdrg avamvtvarc qtgfeewfrr gdnearedqq
      661 fqmipqvmgk nvndarqelq qlgwrvkvrk lgrgsgvvrf qqplpnserp pgsevtlwh
//
LOCUS       WP_357627773             425 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sediminicola].
ACCESSION   WP_357627773
VERSION     WP_357627773.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..425
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45897
     Region          8..416
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mnapsevtae galtrahree warvvadltr rfgdlhvaed ataeafaaaa arwpcegvpp
       61 spggwlatta trkaidwlrr esqrdakhra alimyddtpp rptgpiaddr lrlvficchp
      121 algmearval tlrlvggltv aeiaraflvr etamarritr akekiraagi pyrvpsaddi
      181 rerldgvlav vhlvfnegyl agegddplrv dlsdraihlg rllrtllpdd gevagllalm
      241 llvdarrpar vsrtgelvtl aeqdrgawdr araaegralv rerigalaag gdppgryqlq
      301 aainavhmea pcaadtnwst ivalydrlvl ldpspvvrln ravavaevdg pgaglaeidr
      361 ltpaldgyha lhaaradllr rlgrddaraa ydraiglagn aaerayltrr rdqlggdpvl
      421 vpdgr
//
LOCUS       WP_357627764             848 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora sediminicola].
ACCESSION   WP_357627764
VERSION     WP_357627764.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 848)
  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..848
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..848
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=89409
     Region          5..847
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtpdhdrsrs pggrtllsdl vrghrlaagl tqaelagrag vgvrtvrdle rgratrpqrt
       61 tvdlladalg ltgddrrefv ttarpaptdp apripaaddp gtptalpqpv allgrdrdva
      121 evsdligahp vvslvglagv gksalaltva havaarhpag vvgvlvgegs dtadvlaaaa
      181 avfgvsrlad lscrlagrpa lllvdavera pgpvaealrs ltaaaptlrv lvtgrrpvgl
      241 pgelvrpvap ldvpppgarp teradldrwp aaalfaarlt qarhapptpa elsalaalvr
      301 rlgglplave lmaargrild vtelldrygd rvldladvrp ggqpaagtvt lreavatsyh
      361 llapaeraal rrlsafrnrw svelaeella tgadrwdavp lldrlrelgl lsvrgtgpfr
      421 frlldavrdf aaeqadaege tdairlrhat vvaglvrrta pglvgaelpg tvhlldeats
      481 ditaalayag erapatalll aaalprwwrl rgrdvsgrrw lrrllddprt agvppvlraw
      541 allgaarlav ehgagaeelp aaraalvtft evgdvtgels arsvlcallr glgahdeare
      601 qaeaalslat rhgraremav aqhhltwhdv rvgqlagarr rlatvdrlaa qcgdqrlrll
      661 aradlaeltr wegryaeave qgrraaaalv elgdpgrrrr vvgtvglala lqgriddasa
      721 vvaelwpsgp vpgprrpsaa ersdppgagr dvrtedalrg liegqvalhr gdrelaaewf
      781 aaaaeaasgg adrrdlveal vglaastgev avldrldrar qatgvsllpr eeellyslva
      841 qrdrvrrg
//
LOCUS       WP_357627776             246 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LytR/AlgR family response regulator transcription
            factor [unclassified Nonomuraea].
ACCESSION   WP_357627776
VERSION     WP_357627776.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=27076
     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 mlrllavdde lpaleelayl lrqdarveqv ltasdgvaal qdmvqmigag drldgvfldi
       61 empglsgldl arlvggfpsp pklvfvtahe rcavqafele avdyllkpvr aerlseavrr
      121 lqaaagpaae pghedvipve lggrtrfvpq qaiwfaeakg dyvrlhtvdg sylvrmslaa
      181 lerrwaeagf irvhrstlvs arhvsemrfe ggrvtltvgt eilkvsrrhs rqvrealvhq
      241 hrgaft
//
LOCUS       WP_357627833             252 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357627833
VERSION     WP_357627833.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..252
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..252
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27439
     Region          4..246
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mplmpgaepy hheagqigvl lchgftgtpq slrpwaefla ehglsvslpr qpghgttwqe
       61 mnhtrwedwy aevekafkdl qgrcaevfva glslggclal rlaevhgeai kgvvvvnpsi
      121 andvplmrla pllkwfvpsv pgvandvkkp gvtelaytrt pvkaaaslpe lwslvqadla
      181 rvtqpllvfh stddhvvkpt svtvirqrvp qatieeltds yhvatldnda drifagslgf
      241 irthasvplq rd
//
LOCUS       WP_357627872             189 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357627872
VERSION     WP_357627872.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 189)
  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..189
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..189
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21034
     Region          17..95
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maertqknpl gptgeclsen isrlrrargm syrelsekls elgrpiptlg lsrienrerr
       61 vdaddlmala valavnpnal llppvsdkte veitaggsvp twkawrwgdg replkdpfde
      121 ddfadfqlna rpkgrrryhv pgertsdqka aqraasaeia arlypddvpk qqaflereak
      181 mdpeawagd
//
LOCUS       WP_357627874              64 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357627874
VERSION     WP_357627874.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=7416
     Region          1..63
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 metkmrplge paevaaflgv peatlrqwry mrkgprysvv gkyvryrwsd verwldenar
       61 ggdd
//
LOCUS       WP_357627889             309 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357627889
VERSION     WP_357627889.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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 309)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..309
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..309
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34128
     Region          1..287
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mehvtfnslg trcagdlylp etsdpvpglv lghsgvmvke alaffaphfv kagfavlaid
       61 yrtvgssege prgldypqrq vedfrsavsy lqtrpevqpe rigvwgvsig gsvaaqaavl
      121 drrikcvvvq spsvwngwry lerllgragv halrdqlqqd wqrryeggqs arvphltleg
      181 dsvkdtpdms trlfpayrne ktldsaehll tfapenlihr laptpllmia nggwdpyhvl
      241 eeaqsafaka gepkrlavlp ydvlglytgp gleeamalai dwfdlylrrt rladitptpt
      301 yesvaamkq
//
LOCUS       WP_357627891             151 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GbsR/MarR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357627891
VERSION     WP_357627891.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 151)
  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 151)
  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 151)
  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 151)
  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 151)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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   8  (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 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..151
                     /product="GbsR/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=16937
     Region          3..143
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 msteeqqdrl lrwvervaaf cveewglppi tgrilgwlmi cdpaeqsagq iadviqasra
       61 sltsnmrflt aiglvkkvrr pgdrvsyyri eddawqkviq rkleslsafg eiadegvdia
      121 ggeghrteri kaahdsltwl qnlaarhplr r
//
LOCUS       WP_357627924             936 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357627924
VERSION     WP_357627924.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 936)
  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 936)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 936)
  AUTHORS   Rosinski,J.A. 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 936)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..936
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..936
                     /product="helix-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=100374
     Region          <1..886
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          864..920
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlvqreeqld llrdtfrncd rqrrghvslv tgavgsgkts vlesfgdwaa taggrvlsaa
       61 asraeqelhl gvlgqllqga rlapetgvrv erllrdappa pghdgpdgpv gadrisapvl
      121 hglfstlldl aeagplvltv ddvhhadpas lhcllyvarr lrhtpimvvl aeartlrpph
      181 phfraelfsq phftrislpp ltveaitrlv ddgvepaare taerclrmtg gnplltrali
      241 eerpraeage eppsdptlgd vfdqavlgcl yrhepgvrrv aqamavldrp gpadllghll
      301 dvvpesvspm vrvlrttgll dedrlrhpri rrsiladmsv derrelhqra aevlhehgve
      361 pyavaehlva agwaeagwtv pvlhdaaaqa lavgrpdvaa gclrlvgrad vddeqrvatt
      421 amvvrarwqi npltvngqld qlvgaaragg wpagaalstv pyllwqgrve eadeaitgcg
      481 gddeqahaat asrrramhll lglshpdhlt avreaagapr asllaggssp vqalsllgaa
      541 ltptgdhdpv agaeqllhrh hgedgmlpll tapllallwa gradrvaaws aalldrpavr
      601 haplwravlr alraeaalrl gdltvaeqqa raalddlppa awgvaltgpl atlvacates
      661 grhaeaerwl aqslpagafr tplglhylaa rarhhlalgr ahaatadlrr cgelmrawgv
      721 dvaglvpwrl elarvqlavg nkahatqllq eqlrvphgvd drtrgrtlrl lagttapdhr
      781 rkllseavnl lqgcgdrlel vralgdtgqt lqragdsaqa rllvrrayql aqdcgasvla
      841 qrlvrrepgg vpagppaetp epedglseae rrvaalaaqg htnrqisskl fitvstveqh
      901 ltrvyrkldv krrsdlparl vafaeplgee iqpaas
//
LOCUS       WP_357627927             916 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357627927
VERSION     WP_357627927.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 916)
  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 916)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 916)
  AUTHORS   Rosinski,J.A. 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 916)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20665278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..916
                     /product="helix-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=100173
     Region          4..167
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
     Region          <240..773
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <781..913
                     /region_name="MalT"
                     /note="ATP-, maltotriose- and DNA-dependent
                     transcriptional regulator MalT [Transcription]; COG2909"
                     /db_xref="CDD:442153"
     Region          855..912
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 maerdrqfdv ltdrladlhr adgpadtsdv itvvtgpvgv gktallqsla rrcaetgvay
       61 lgasasrser tvplevirql vrratwdetd rervgrlldr avlrwsettd eealapltaa
      121 iggelldlat rtptliavdd vqhadvpslr cldhlarrvt glpvlivlte aprtrawhpt
      181 ayaellqpar lhrirlplls adgtfrilad rlgvpvarrv adeayrisgg npllvhalad
      241 dhpagadapv pgeafreavl sclyrcellv lktarvlavt eeplhgpllp hlldlpteph
      301 lsavdpstsa glvtadglrh pavrravldg mtveerarlh raaaqllhdd gapptrvaph
      361 llttdeltep wmaqtlldag eqaltdgdvd tarrylrran rdcpdeclra rirsalarae
      421 wrldpqaavp hlhgvatavr aghlgsrqaa gpiqyllwhg qpdravelih hlgeradsld
      481 thtavdlmii rgwmatlypg apvdapawpv ptrdplalar vrhrlrgvll lrtvlergdl
      541 daledaertl atlslddeps mwsavcavia miyadrldla dewcdrldri asarrhrtpr
      601 alltavaatv agrrgdlhra leladsalnr lspkgwgvai gaplavrlwt ltrleeweea
      661 aaclrtpvpp alfetpfglh ylharglhai aagspeaala dfqlcgqlmt swrldlaplv
      721 pwrtesaral lqlgrrqqae klvreeldrl rptdlrwrgi alrvlgtase gpdrirylrg
      781 avrllrqcga rvelahalgd lgqaqqqagd lrqarstsra ardlaedcgi palrpavaag
      841 rtaaadpdad tgllltglsd aesrvaalaa qghtnreiae rmfltvsaie qrltriyrkl
      901 dvhsrselaa rlrfdr
//
LOCUS       WP_357627932              95 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357627932
VERSION     WP_357627932.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..95
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=10257
     Region          <2..75
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mvtaivhina evdripevaq tiaeidgvse vysitgeydl lamvrvaaye eiaevvpgrl
       61 nkvpgvlhte thiafraysk hdldaafsig ftesd
//
LOCUS       WP_357627959             312 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: diacylglycerol/lipid kinase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357627959
VERSION     WP_357627959.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=34237
     Region          18..308
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mselrtkaeh teairkdrrv avvintrsrr grrhyvevie qlhdlgfepl aeigvynpkr
       61 lrelldtala trpdllivgg gdgtlssavr hvahrdvalg vlplgttnnf arslglpldl
      121 qgairvfdtg kvadidlgma ddrpfanlas fgvsvevagk vkpwlkrllg rpaypltalt
      181 vlpghrpfra yitvddqrhe llthqlnian grfhggwqva kdisidngml vayqlgsgkk
      241 lrllgetlar attgrwrsla ggpfvlgrem lletdppmaa dvdgevrlrt pirlrvvpng
      301 vrvmvpasfe dr
//
LOCUS       WP_357627972             552 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea wenchangensis].
ACCESSION   WP_357627972
VERSION     WP_357627972.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 552)
  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..552
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..552
                     /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=58484
     Region          2..211
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
     Region          <440..>500
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
ORIGIN      
        1 mndrnlveal rardpgapav lydayaegvy rycrsllrda daaqvalrda liaaeahada
       61 laeparlrsw lyalaraecl rrrtaalrpv tpassdppaa dppaadspaa dspaagwpda
      121 gwpdaqwase aewpdaewas deppdvpgdt rqrvmawdav hslpsadrel leltilhelp
      181 dselalvlgi sarqlasare aalgrlraav tvellarqep gecprraail rgfsgrltte
      241 rrerlvqhls ecaicaprrg rqvaaakvfe llpkpelpda lrlrvlscfa dpelapyrry
      301 varrtsrlgv agfplpqkka arrwpralac llaavgavva iaivlqglgr dgivsdvata
      361 afppsgrppa vhlpwqerpq depvtvepva natdirrdlp apvdfvngvt rstptgrppv
      421 ggdpaepqag ppdprpggps aepsapidpa athdpgeprg pgrshgprap rpgssalpsy
      481 hgrperpcqg rfrphclppk ptptvtaapt ptppptqept tppatqppas ppapptppap
      541 tataeetpas ts
//
LOCUS       WP_357628025             299 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357628025
VERSION     WP_357628025.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=33379
     Region          2..294
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msqaarpaft grrarfvalc llpgvvfvll ftyypmirga viafqrynlf dltstpfvgl
       61 enfravlaed rfwtalrntg twvavslffq fflgfglall lrrhfrgrgl yqawvffpwa
      121 msgfligllw rwmfngqfgv vndlllkagi idgrigflas pgwamtsviv anvwygvtff
      181 aimimaalqs vpaelyeaas vdgasrlrqf whvtlphirp tlalitllri iwilnfpdli
      241 yamtgggpag stdiittfli qqviggdygr agavgmlilg lllafsvfyl natrfersr
//
LOCUS       WP_357628123             192 aa            linear   BCT 28-DEC-2024
DEFINITION  O-methyltransferase [Nonomuraea wenchangensis].
ACCESSION   WP_357628123
VERSION     WP_357628123.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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..192
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..192
                     /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=19443
     Region          27..189
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mntetpglvg aaveraraag fafscdpavg rllavlaagv pecgrvlelg tgtgvgtawl
       61 vsgvlprrdv tvtsveldpe raalaasgdw pgfvdlrtgd vlellpglga felifadaaa
      121 gkqvglelti aalgprgvlv vddmtpapgv twdagfaarq eevrrtllgh erlaavelgg
      181 hgsgvilata rn
//
LOCUS       WP_357628096             546 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357628096
VERSION     WP_357628096.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 546)
  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..546
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..546
                     /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=56797
     Region          9..119
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          245..516
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 maltvartma lpgmrmrlla grsgtwravr wahvseladp vpwlsggelv mtiglglpae
       61 pdgrrayver laaagcaala falheameev pddlldaada cglpvlevlt sfisvteava
      121 rwhadervrg errvvaaqea maraalahgt agilrtlaeh aagealllgp hgehkhavpa
      181 rerpwharaa eaaaasgggr sagvlddgie avqvhslgfs gaatgwlavr taspldwhvr
      241 mltshaacll aiellglrvg rsrmhaqrga llaavldgrl paarlgelcs vaaapyevvv
      301 arpgvsleaa vealeevtea gdeetalvcv rpegtvfvlp entglpgeqa gglpgeqagg
      361 rpggqaggrl gvrlcarlgv agggcraagl eevpaavrha aalvargggd gyahvddmep
      421 qallrdafvp eaarrfstav lrplrehear hggdlvgtlr ayleagdnae taarrlgvhr
      481 ntlrrrlaaa ervsggpltd pghrlrlwla lslpdlvppg ssraangdav rldrrarnad
      541 aegphp
//
LOCUS       WP_357628133             250 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357628133
VERSION     WP_357628133.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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: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=27459
     Region          38..132
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtvdrtrsvv fgetveqyea aradyparli tdvldyappg palevgagtg katagfaarg
       61 vdltcvepdp rmaaaltvkc pearveigvf edyvpdrafa llysaqawhw vdrerrwdla
      121 haalapsgav avfwnryavt dsdlraglae vddrygvtnt tlhqnttipa gasehqladd
      181 prftdlderh ytrtrwyead ryldlirsis syailapdtr dalvrevagl lgdgvdmtlt
      241 tdlalarrar
//
LOCUS       WP_357628140             923 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Micromonospora sediminicola].
ACCESSION   WP_357628140
VERSION     WP_357628140.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 923)
  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 923)
  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..923
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..923
                     /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=98661
     Region          215..898
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mtvtpradlg rcgivllpad ppragtlacy dptgdalpqa ydalgerrel tlalpldgpv
       61 eawhvpvvav pvgaalsrlv aprpdgdatp aaafwcavar tglhlvargr llpgvspdgh
      121 dawrvgpfda adverirala aampaaaraa pvdpdaekll lpdaealvra fldavadtla
      181 rtpdgagrfa gpepvgsael rdwarelsag vdtglraalr lagpadpdga ltavvrmrsl
      241 adptlvvdaa alwagddhpl getatveamr avrraatvwt plqrlldrad pvtlpllded
      301 vadlldgaga rldaagvtva wpdalhrdlr aralvttppq ppvdvaghlr saapmplswq
      361 ltlagepltd aetaqvatgr pvrrlrgrwv avppelarra rdrslpplrg ydalaaalig
      421 stevagerve vvadgwldal qnriaepdgg deplaappgl agtlrayqlr glrwldrmta
      481 lglggcladd mglgktvtvv alhlrrrsgp tlvvcpasvl gnwereirrf apgvpvrrfh
      541 gaartldgva dgfvvtsygt lrrdaatlaa rrwdlvvade aqyvknrlsd tagalreipa
      601 darvaltgtp vendlpdlwa lldwttpgll gaagafrarw arpigtdrdp aaldrlsrlv
      661 rpfllrrrks dpgiapelpp rtvtdhpvpl tdeqaalyrr vveevmaeir datgvtrrgr
      721 vlkllvalkq vcnhpahylg evdgpltgrs eklqllddll gtvlagdgav lvftqyvrma
      781 rllerhlaar gvpaqllhgg tpvagreemv rrfqagdvpv fllslraagt glnltradhv
      841 vhydrwwnpa veeqatdrah rigqtrpvqv hrliaqgtle eriaallesk reladavltg
      901 getaltelsd adlfrlvrle eta
//
LOCUS       WP_357628159             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357628159
VERSION     WP_357628159.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=36150
     Region          19..315
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpttsarlla llsllqarrd wpgrvladrl gvstrtvrrd vdrlrelgyp igsakgpdgg
       61 yrlgagsalp pllfddeqav altvalqtaa ttvtgieeaa aralttvrqv mpprlrhrvd
      121 alrvvavera daaakprvep gllmtlsaav harevlrfdy rsaaaepadd ppprrvqphh
      181 lvtwsgrwyl vawdldrddw rtfrvdrisp rtptgprftp relpggdvaa fvagrfrgat
      241 gpgdwpcrge vildlparvv sawtrdglve elgpdrcrlv lggwswpgla alfgrydadi
      301 evvgppelrd afahlarrya daaasaapdv rp
//
LOCUS       WP_357628205             286 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357628205
VERSION     WP_357628205.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   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 286)
  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..286
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..286
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30416
     Region          8..274
                     /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 mteavlhdgg aievevhgsg pvvllpvdpr piegeqaeem rkwgadpalg rslidglsda
       61 frvvafdytg hlmavpkpdt ltpdnvaadl lavadavgag rfayygyswl alsglqlalr
      121 tdrlaalamg gyppyegpya emlkvttaty ekalappppa tgpvepgdws svqnlpsepq
      181 arqfvtlyea lqdfddkavr ltcprlcfag sadaivyaee wggttvdlag plsrhrgele
      241 argwevavld gldhmgamra enalpvlrpw lervlleggp sgvlge
//
LOCUS       WP_357628225             253 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357628225
VERSION     WP_357628225.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25530
     Region          4..253
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mserfagkva lvtgatgvvg gavarayare gaavlvagrd agrlsglvke ieaaggrasa
       61 faadvsrsae aaamvaaavs rhggldvacn aagifgalap vadydedvfd evlavnlkgv
      121 flsmkhevah mrthgggtiv nvasnmgahw rlagagayva skaavshltr taardhiadg
      181 vrinavspgp idspmstrpg etaeqrnerm rdalpigrva apeeiaaavl wltspessyv
      241 vgqdhvvdgg ata
//
LOCUS       WP_357628211             269 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea wenchangensis].
ACCESSION   WP_357628211
VERSION     WP_357628211.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 269)
  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 269)
  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..269
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..269
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29734
     Region          6..>122
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mhgseldvlv ptkdrpgala vtlaglaaqt aggfrvvvsd qsarpvaedp lvaaavrile
       61 hrgspveplr nvppkglaeq rqflldrarr rfalyldddv wlepdalatl tgalaelrcg
      121 fvgyalhgls hredvrphel asyeewagpv rpervrrdqp awrrhtlhna anplhlaakv
      181 gadrawrayk vawiggcvly drerlvecgg fgfwrsvpra hagedvvaql rvmeryggag
      241 llpsrayhle lpttvmdrra ecydhvlea
//
LOCUS       WP_357628243             372 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357628243
VERSION     WP_357628243.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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..372
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..372
                     /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=40832
     Region          74..347
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mqspaewpil vvsvvgaill vevtrrllkr agrkwalagh lvehctwagf tvaavvacnl
       61 vfgpgmfgds preqqlaatv erglglvtig svtwlivqas yaltdvvler lvrvegernr
      121 rarrimtqia lvrriaavti ivvavgamlf sfpqvralga gllasagiag avvgiaaqpt
      181 ignalaglql afsdalrldd vvvvgdewgr ieeltltyvv vrlwderrlv lpvsyftqnm
      241 fenwtrhgsr vvavvflrvd wsvpvqklrd elyafiqgnp lwdqkdwtlq vtdvlpnglv
      301 elralmsaad spsawdlkcd vrehmvtyir enfpealprf rvetpetrag vpwtaelsds
      361 gapapkpgtq qr
//
LOCUS       WP_357628256             182 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357628256
VERSION     WP_357628256.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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 182)
  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 182)
  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..182
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..182
                     /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=20157
     Region          7..178
                     /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 mrhvqcngar lclrdvtead vaalhaiygd psatrfmpfg altfeqvral vdealeaaea
       61 eprrlyvfav edadhhevig varlhvetdl phsaeiglgl rpdqwgrgmg tdlirlllsf
      121 gfkqlglhrv wgarspdnlp aqlamltagm veegrirhhl ptpdgwrdsi vhsaledewt
      181 dr
//
LOCUS       WP_357628259             235 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sirohydrochlorin chelatase [unclassified Nonomuraea].
ACCESSION   WP_357628259
VERSION     WP_357628259.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..235
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=23313
     Region          23..229
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mptslpsdap vlvlaapgda sgvaseiaav vrvdnpqiev rlatvadlad slpsgrdavv
       61 vplltwddpa vladigkava agdsgavvte algphpllae alhirlaerg laradrvrll
      121 nvsspvdavi lgtaggarav qavqatavll asrltlpvva asldsepgvt maaqrlraag
      181 agrlalapcl ighevapgtv eraaaeieag haeplgahsa iaelvarayg sqlat
//
LOCUS       WP_357628322             835 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [unclassified Nonomuraea].
ACCESSION   WP_357628322
VERSION     WP_357628322.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 835)
  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 835)
  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..835
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..835
                     /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=92758
     Region          14..821
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mgtvsllidr lpeeidadpd aifdafvswn sergltlypa qeealievvs gsnlilatpt
       61 gsgkslvaag ahfaaltrdi rtfytapika lvsekffdlc avfgtenvgm mtgdasvnpg
      121 apiicctaei lanvalrdga aadigqvvmd efhfyaepdr gwawqvplle lphvqfvlms
      181 atlgdvsmfe rdltrrtgrp tsvvkhaerp vplvysyrmt plhetleeml stgqapvyvv
      241 hftqaaamer aqalmsinma tkaekeaiaa miggfrfttr fgralsrlvr hgigvhhagm
      301 lpkyrrlver laqagllkvi cgtdtlgvgv nvpirtvlft alskydgnkv rrlrarefhq
      361 iagragragf dtigyvacqa pehdienaka lakigddpkr rrgyarkkpp egfvgwseet
      421 feklqtaepe plasrfkvsn amllavinrp gdcfqamkhl ltdnhedrkw qrrhisqtia
      481 iyrsllaggi veqlgepddq grrarltidl qedfalnqal stfalaafdl ldqespgyal
      541 dmvsivesil ddprqilsaq lkkargeava qmkadgmeye ermealaevm ypmpledlll
      601 gayetyrrgh pwvgdytvsp ksvvrdmyer amtfgeyiqf yelarsegtv lryladayrt
      661 lsrtvpehlk tedlvdliew lgelvrqvds slidewekla npaealeahq qletrvrpvt
      721 antrafrvlv rnamfrlvel calekdaele elapdvdwga aldayydehe eiltdadarg
      781 pallrieees glwkvrqtvk dpagdgdwgi daqvdlaasd eegravlhvi glnrl
//
LOCUS       WP_357628340             845 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora sediminicola].
ACCESSION   WP_357628340
VERSION     WP_357628340.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 845)
  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 845)
  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 845)
  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 845)
  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..845
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..845
                     /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=89878
     Region          134..788
                     /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 mtrvhardng tdrrllllvg lvvfsasiat lvsirlidtg dlatqknltr aitiaflvav
       61 aatvnvriri ratthgvswt daasviglav apvpwvvvat gvgvaiarli grltpiklaf
      121 gvakemtlaa agglvlvlag wswpwsgsig rslpalvlay ltvvvldell tfpvlafatg
      181 tpirkrfreq vdlrlasvla rfsvvlctll ilrinptflv vvpplvlslh layssrlrsr
      241 aerkawqrla rttdalnvvd ldqvlttavt qatelfsade veielreegr vvrgvggait
      301 yrgpagepsa vegsvlasrl eghdqtvdig vlrlrfagpv elsereqytl rtfasalcta
      361 vrnaqayael ariadahaya athdaltgls nrrhlldegt thltsrhadg vtalvlidln
      421 hfkevndtlg hgagdrvliq vaerlrgaar pddlvarlgg defavllral papavaahra
      481 eallsalhdp ldldgmrisv easggiavap atggmaellr radvamyqak ragqriatya
      541 pardtadlgr ltlggelpra vadheftvnf qpivdlasge vtgaealarw hhpthglidp
      601 lrfleaveps gllpafaeai ldqaliaagt wrdagfdlpv svnvsprsll darfpgavla
      661 rlrahdlppd rlvleltetl tlsqldvvdr vlsrlrdsgv rlalddfgtg ysslsllsri
      721 pvhelkidrs fvtametape aaavirstld lgrsldltvv aegvesepqr ralwelgcaa
      781 gqghlfarpl pagallaalq rgaggrpgal applhdtgav irlpgrrtgg prtrpaapaa
      841 dsrqp
//
LOCUS       WP_357628411             175 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora sediminicola].
ACCESSION   WP_357628411
VERSION     WP_357628411.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 175)
  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..175
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..175
                     /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=18899
     Region          5..159
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtvsdgdlia elyagsfrrl vvqlyavtgd lseaqeavqe aftkalvapg rfarldnpea
       61 wlrrvavnva rsrhrrrrvl drlllrigpp pavadrspeh lalltamrdl pegqrtalal
      121 hylvdlpvde iaatlgisag tvksrlsrgr qalaalltep hltggagqgr idvrs
//
LOCUS       WP_357628421             323 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Nonomuraea].
ACCESSION   WP_357628421
VERSION     WP_357628421.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 323)
  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 323)
  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 323)
  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 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   5  (residues 1 to 323)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..323
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..323
                     /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=35305
     Region          1..231
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          240..318
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpltlaftaq dmanirfavs plgevvasvr vvkdpaahsa lrpwaeqvrr rladvdfrll
       61 sdlvpvptvs iagftctpps tstpdlevel atmraaagrv radldsvggp rtervqalyd
      121 dpdkglerla eevggyweaa iapywprirs lldgeilrra rvlaeggadr mladlddsvt
      181 wedgrlhlrh ryvsgvrslr glglllvpcv fawprvfsvt tppyqptvry pprgvatlwe
      241 rgeadtpaal atvlgrtrar llaeldqpts tqelarrlel aepgvsrhlt alrdaglcts
      301 hrtgryvlya rtavaeallg hnp
//
LOCUS       WP_357628445             269 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357628445
VERSION     WP_357628445.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27920
     Region          7..255
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdiaqafdft gykvvligtg igvngpedva sssaaaftrc gaevlvaqat keaaeataea
       61 ireaggeprv vvhdprdpyg pqrlaadlpe gwdtvdtlvt hhfandfgrf pdlsieqfee
      121 tvrinltgvy aasqaflphl krssrasmvh agsidgtygn pnvvsysask gavhslvhvl
      181 aaelassgir vngisragss amplktdiva elgratplrp vaepdeyaaa vlylasraag
      241 yvtgvllpvd ggrtaatpgc spgytgyrh
//
LOCUS       WP_357628468             281 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357628468
VERSION     WP_357628468.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..281
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..281
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29398
     Region          55..125
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mklsscaavl aaavlfasls gvtgaaaaqk adaealpgvn meaavkaaqi dprrpdstlt
       61 pgakagvllv eealrdlhfl dakwvdgyfg tttvaayany qkslgltgld anglpgktsl
      121 sklgagrftv tnvitpgprv saggsvlntr trdmlaeakr vlgrdfeldq gsynpggdpt
      181 svgthdgggv vdisvegmna atrtavvral rlvgfaawlr spqqgdwpwh ihavaisdtd
      241 lssqaqhqvg dyylglngla nrgpddgprt tirtweeyrr r
//
LOCUS       WP_357628582             229 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357628582
VERSION     WP_357628582.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,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 229)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..229
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24042
     Region          4..228
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtaitvtdls ksfgavravd qvsftvepgt vtaflgpnga gktttlrmil glvtptsgta
       61 liggtpynrl anpiakvgav leatafhpgl sarahlevlr taagldparv slvleqvdlt
      121 qaadrriggf slgmrqrlai asallgepev lildepsngl dprgiswlrg flrahahegr
      181 avlvsthvla eierianral iisagrlvrq aeltpdstdl ehlymeats
//
LOCUS       WP_357628585             365 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357628585
VERSION     WP_357628585.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 365)
  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 365)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 365)
  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..365
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..365
                     /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=38446
     Region          119..364
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msflrrplvr vvfralvvsy llfgsvyavv dawprlgwav gigvlllsam tfaasvrgav
       61 fpgsghllla alagglamha vspysglavl yvvvyaapyr lplrwaaafv aadiggtvlv
      121 slllglpvpe tfgntmglcy svilafllrq ltlsrelaes raresaqaer ahlareihdi
      181 lahaqsaqiv hlegarllle rgdvptaldr vtralrlars gleetkravd alrgqdirll
      241 ellerltveh rsaggapcev evsgdvsalp agarlavart aqealtnvrr hapgaavtvt
      301 lrnvrgwcel evrddggaap paqdgggygl vgmreraell ggslttgpeg agfrvllrlp
      361 agaas
//
LOCUS       WP_357628598             119 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357628598
VERSION     WP_357628598.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 119)
  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 119)
  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 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   4  (residues 1 to 119)
  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 10140843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..119
                     /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=13148
     Region          1..43
                     /region_name="HTH_MerR-SF"
                     /note="Helix-Turn-Helix DNA binding domain of
                     transcription regulators from the MerR superfamily;
                     cd04761"
                     /db_xref="CDD:133389"
     Site            order(2..4,18,34..36)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133389"
ORIGIN      
        1 mriteaarrl gmsprmlryr ealgllppvr eqgahrrfgp eelaavaqgv elekqfdvsp
       61 aelafalrvl septvaaavr dlgvrigrip vprraldfek ekalrllrts tpvhtskks
//
LOCUS       WP_357628611             223 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sediminicola].
ACCESSION   WP_357628611
VERSION     WP_357628611.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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 223)
  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 223)
  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..223
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..223
                     /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=24603
     Region          59..195
                     /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 mtlaevwpvr rlrvttsvle lavpgedela elaihaaagi ydpqsrflar spvagwesgp
       61 spqaewsflr yywasladwq prrwnlvmav kvdgacvgvq eigaqdfgit rtvstgswia
      121 rrfqrrgygk emraailhla faglgadrae saawstnaps lgvswslgyq sngttirafd
      181 garqeqinlv ldrerwesrr ddiaihglse evlelmdvsa asr
//
LOCUS       WP_357628620             337 aa            linear   BCT 28-DEC-2024
DEFINITION  mechanosensitive ion channel family protein [Micromonospora
            sediminicola].
ACCESSION   WP_357628620
VERSION     WP_357628620.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 337)
  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 337)
  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..337
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..337
                     /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=37297
     Region          82..337
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mttrtvlvva vavvvaagll agvlvqrrag grsyrwllap lyracrrpav avlllaalyv
       61 giraypgpgp hmvrrvvvvl liagvtwlvl ralhiaeraa fsrlpgetra drrirrartq
      121 irpvrrltsv vvtvvaiglv lttfppvrti glsvltsagv vgallglsar talgnafagi
      181 qvafadglhv gdvivvdgqw grveevkltn vvirlwddrm lilpttwfte hpfqnwtrhe
      241 trvvgetrih vdhtavlddl raetrrives splwdrhqwv lqmvdatpqt vvvqvqasaa
      301 dgpsawdlrc dvregliryl rdhhpewlpr trgefhp
//
LOCUS       WP_357628670             253 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent DNA methyltransferase
            [unclassified Nonomuraea].
ACCESSION   WP_357628670
VERSION     WP_357628670.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 253)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..253
                     /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=29401
     Region          <81..230
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mkhnrssiah qaryalthpe riaphlrrla rdtwlrlrtr dhvayyravm rsdtarspeg
       61 avgshshkrw lalgrmqfdy lkqhglkpdl rmleigcgnl ragrlfidyl dagnyygvdi
      121 spdiliaaqd tlvahglrdk lphltpvrdl rfaflpdehf dvvhahsvfs hspphvieec
      181 fahvgrvmrp dgwfdftfdr tegeehhvlr edfyyrtetl valadrygld avlmedwerl
      241 phkqskirvt rra
//
LOCUS       WP_357628712             985 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Micromonospora sediminicola].
ACCESSION   WP_357628712
VERSION     WP_357628712.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 985)
  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 985)
  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 985)
  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 985)
  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 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..985
                     /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]"
                     /calculated_mol_wt=101422
     Region          5..>957
                     /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 mardrsldia vsgmagrfpg speltrwwsa ltdgqvltrr yqrhelaaeg vpqhllddpd
       61 yvpvhghlad adrfdnglfr mspreaemld pqhrlmleca wsaledagvn pldtglttgv
      121 yasasssdyl rrmvaggrlt pltledalhg tqpdflasll syrlnlngpa lavqtacsss
      181 lvavhlavqa llngdcdqal vvaagmafpq aghlhvpggi hsptghcrpf daradgivag
      241 sgvacvvlrr ladalddgpa phgvilgtav nndgsakvgy yapsvegqqa viraalrtad
      301 vdgetigyle shgtgtrigd piewaaasaa lrasgarpaq vavgalkant ghldnaagva
      361 glikailvvr dgvippvagh galnplldhe esplyvpdqa rpwpgdgprr agvssfgvgg
      421 tnahvvveqp pvaspaaqag pghrlvvlsa adgaaldraa trlaahlgah rtepgdvart
      481 latgrahlte rlavvaadtd qlarrltsgg alragvpasg paplvlafpg qgaqhpgmar
      541 platglpgfa palatvlgay dpatadlvgr alhdprfpad elaetalaqp alfaveyaaa
      601 aalralglrp aavighslge itaacvagvl dladaarlvt vrgqamqqcp pgamlaltcg
      661 raeaddlira sglalevaav nspdhtvvag ppdvvdafea glppgrvrar rlrsrrafht
      721 alvdaadapl realgatrlr pptlpwaans gdvlvpgtpv eatrfttqar htvhfgpale
      781 klagrfpgav vvevgpghal stlaesgglt avplcggrtd ddeavltalg rlwtmgqpva
      841 ieatcptgrr vhlpgyafhg prhlaaeaap vadgatppag vpplvaattt pgpdhpagpt
      901 ghdvpalvgr lwrdllgrdq lsddadffdl ggdslsvthl arrlrtdlgv rvpirdlmtr
      961 ptlgdhtslc ralldddtra rvtvg
//
LOCUS       WP_357628722             167 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357628722
VERSION     WP_357628722.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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..167
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..167
                     /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=18827
     Region          33..156
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mssraeaadm pydgetqtpe rlrrrasrll sgmsarsdrl mneglaqvda rkwhyavlas
       61 lqeygpgsqa tlsrrtgiyr sdmvgvlnel aehglvermp dpddrrrnvi titaqgrrhl
      121 rrldkvlddl hdellapltp aerdqlvhll trlldhhtqq aphppts
//
LOCUS       WP_357628747             104 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357628747
VERSION     WP_357628747.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..104
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11427
     Region          10..104
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mthtlddraa tlrellerqf ddhtgqltel taaarqpdhg ghdpdtlrrl veaarqgvad
       61 tagalqrmsd gtygvcercg ddiptarlei rpsarfcvpc qqrr
//
LOCUS       WP_357628802             349 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sediminicola].
ACCESSION   WP_357628802
VERSION     WP_357628802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..349
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=37133
     Region          68..326
                     /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 mqfqklrtav akmipigpgk rrrtalaaaf siallagsga savaiptaap aghgeqrisg
       61 lslrqgnvtv dgatlrytia gsgsplvllh gwpqtwwswn kvlpalasqh tviafdlpgl
      121 gastppasgy dkattakrir qgvnqlgyrq vallghdvga lvayayardf ptevtrmgav
      181 etplsgfgle nlygvswhfl fnaspapipe rimdnddvpt ylgmlfdgar hpeaidrnvy
      241 yrayadpvkr kagyeyyraf aadaadnqan aqskrlaipv mamgaefvfg pavaasfqqv
      301 asdvrtvvap dsghwipeen aqffsdcall ffgpaggaap rpeltnctp
//
LOCUS       WP_357628801             230 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357628801
VERSION     WP_357628801.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Rosinski,J.A. 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 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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..230
                     /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=25024
     Region          <22..210
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mprfdvghgy alyqgpswdt afhrhaafqi avaiegdvgm vdssetchra valvvppmvr
       61 hrmlattdlr vffvepqcay adrlrerygp gigaapelrr lsdddvrrag arpsgeldpr
      121 llaamdalvd gsgsmqdlav rvglssqrlr alahsqlgmp larwrvwarl rravealrag
      181 rtlaeaaams gfadqahltr wtremmgltp avllpvlrgp vaagqprkat
//
LOCUS       WP_357628855             304 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Nonomuraea].
ACCESSION   WP_357628855
VERSION     WP_357628855.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,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 304)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..304
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31941
     Region          2..217
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mislknltkr ygdrtavddl slevrpgavt gflgpngagk sttmrlvlgl drptagtali
       61 ggvpyheirn plrtvgamld aralhpgrsg hahlaalars ngiargrvae vldkvgmtda
      121 arkragalsl gmsqrlgiaa allgdpevlm fdepvngldp dgvrwvrhlm rslagegrtv
      181 fvsshlmsem qltadhlvvi grgrlimdap laeviagsal tavavrtpha ddlavrlsaa
      241 gitverlgen elvatgatve rvgdlayeag irlhelrtre asleqayqel tassveygte
      301 kaga
//
LOCUS       WP_357628972             300 aa            linear   BCT 28-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Micromonospora sediminicola].
ACCESSION   WP_357628972
VERSION     WP_357628972.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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 300)
  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 300)
  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..300
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..300
                     /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=33279
     Region          10..282
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 mertsagfpr eavadrllta svrtsydplv dldwsappvp gaywlpprrs slygtplwdd
       61 mteeqrvelt khevasaasa glwfetilmq mlirhyydad ptsrhaqyal tevadecrhs
      121 imfgrlieai gtpvyraapv dhllgrwlka tatgpqmyaa iliaeeilds fqreimades
      181 lqplirmvsr ihvveearhv rfardelgrq veaagpvalg yarlvigraa ysitrrlvnp
      241 rayaavgiap avglaaaran phwqatlrws aqriaehlte lgliagpgrl lwrrsglieg
//
LOCUS       WP_357628986             311 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357628986
VERSION     WP_357628986.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 311)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..311
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..311
                     /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=33772
     Region          11..308
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mttqhlavpa rrpsrtprgr rtlrrnligw vflapaiali gvftitpfaq aillsfqswd
       61 gvspdtpwvg ldnyhfvasd pifwasmrnv lffgvvgfvv gngvalgmal avntvtrgrt
      121 ffrtvfylpg vlsvvvvgll fsfilapgsg vlnrllglvg lgalqqnwlg dpavalpvva
      181 avfvwfhwgf gfllflaglq dvprelyeaa eldganrwsk fryitwpqla pvtsivsllt
      241 llaalqifgt vqvltnggpg hhtmvptlai yneafvnwry gsaaamsvif ggalvllsli
      301 qlaitrrrsh v
//
LOCUS       WP_357629006             463 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357629006
VERSION     WP_357629006.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..463
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=50075
     Region          4..399
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mthrprvvii gggfagynaa rvlnrkhrre idvtllnptd fmlyqpllpd vvagivhprh
       61 vavslaaalp ytrllpgtvt gldadqrevr yvdsegrsrq vgydrlivsv gavskvlpie
      121 gsqtyshglk glpealylrd hiirqvelaa vaedpeerra rltfvvvgag ytgtetaavg
      181 qlftrslqrr yrslagvpvr wivvqyderv lpelrpslgr taervlrkrg aelwlgttvr
      241 kaapdgvlls dgefvpartv vwttgvrpdp vidafglptv ggriqtdefm avsghpeiya
      301 agdaaavpdl agpgeitpmt gqhaerhgaa varnvaaslg lgrgakpyrh rllgflvdlg
      361 gwqaaadplg vplsgvaakl vtrgyhlyvm pgnrirvaad wlldavlprq vvqlglvrgd
      421 avpldspdpe lprrvyptrs pqgehtetvt plssagylya hhh
//
LOCUS       WP_357629023             115 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF488 domain-containing protein, partial [Nonomuraea sp.
            NPDC050733].
ACCESSION   WP_357629023
VERSION     WP_357629023.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007029
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     Protein         1..>115
                     /product="DUF488 domain-containing protein"
     Region          4..>77
                     /region_name="YeaO"
                     /note="Uncharacterized conserved protein YeaO, DUF488
                     family [Function unknown]; COG3189"
                     /db_xref="CDD:442422"
ORIGIN      
        1 magvrmrrvy eepagddgtr vlvdrvwprg lskaaarlde wckqvapste lrrwyghdpd
       61 rfaeftrryl aeleepergg ggvgpraprp ggprtpldpp pgrpnnpnpp rrrrp
//
LOCUS       WP_357629042             382 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            sediminicola].
ACCESSION   WP_357629042
VERSION     WP_357629042.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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 382)
  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..382
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..382
                     /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=42227
     Region          1..377
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkivvqvrly pdsvqeaals atlklcndga nlasaeafgh riygkrelqr ltygrlkalg
       61 lsaqpaihvv rkvagayatl aantragnlg kpgskrrvka dskpiqfrrd agqpyddrcl
      121 swqlaertvs iwttsgrltr vrfgcslqqh atlvayrrge sdlihrdrkw flyatcdidd
      181 vevkepdgfl gvdlgiania tisdgkrhcg krlnrvrhrn qrlrtklqrt gtksakrllk
      241 arrrkearfa adtnhciakq ivteakrtgc gialedlkgi rdrvrlrrpq rvtlhswafd
      301 qldrliayka aragvgvvhv dpaytsqacs scghvakanr pnqftfrcms cglaehadvn
      361 aarniaargv adwaaaslpn aa
//
LOCUS       WP_357629060             331 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357629060
VERSION     WP_357629060.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 331)
  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 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   3  (residues 1 to 331)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..331
                     /product="GlxA 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=36162
     Region          15..331
                     /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 maqessqpvh qgrphrvvvi vdensnpfel gcatevfglr rpeigrdlyd frlcspeprt
       61 lmrdgfftlt gvagldaaes adtlivpnrp dvevprrpav leairraher garlvglcsg
      121 aftlaeagvl dgrratahwq wadsfrgrfp svrletdvlf vddgdiltaa gsaaaldlgl
      181 yivgrdhgae iansvsrrlv faahrdggqr qfverpvpev pdeslapvla waqerldapl
      241 tvsdlaaras vspatlhrrf qsqlgttpla wltgerlaqa crliergesr felvarhsgl
      301 gtaanlrglm rrktgltple yrrrfgpgqg r
//
LOCUS       WP_357629095             266 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357629095
VERSION     WP_357629095.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   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 266)
  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..266
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..266
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27803
     Region          1..266
                     /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 mttthtlrvp garlryevrg agpvllvfga pmsaaaftpl aealagdhtv vthdprgiag
       61 svlddpaqds tpdlraddva alldhlgadt adlfgssgga vtglavaarh pgrvrtlvah
      121 eppllellpd aaerravvdd ivetfrregh gaawmkfmtt sgfdvdgaap pqgefseqdl
      181 adsarfflhe lrgttryvpd vaalkagpgr vvvgigaesr rlltyptsta laellgtppv
      241 efpgehggfv thpepfaevl rktlag
//
LOCUS       WP_357629143             449 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [unclassified
            Nonomuraea].
ACCESSION   WP_357629143
VERSION     WP_357629143.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 449)
  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..449
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..449
                     /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=46218
     Region          15..267
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(15,38..39,68,73,78..81,93)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,42,44,76,92..95,99,101,138,140,
                     142..143,145,154..155,158,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,42,44,76,92..95,99,140,142..143,
                     145,154..155)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(26,99,101,138,140,142,158,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(154..162,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <246..>393
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          363..>425
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
ORIGIN      
        1 miqplveddp rrlgpydiag rlgqggqgvv ylgrtasgeq vavkllhhgl laepdarsrf
       61 lreveiarrv arfstapvlh adlagqrpyi vseyvpgpsl rdlvtvegpr rgaaldrlai
      121 statalaaih ragilhrdfk panilmgpeg pvvidfgiar aldapgtsts agslmgtpsy
      181 lapeqlgget vteaadvfaw gvtmvfaasg rpafgadstp avinrilnqe pvlsgldgpl
      241 ldlvtaslsk dparrpsadd lvatltsqps rpshppqhpp argrrrpvvl tiagcaaaal
      301 lvtggvlinv gghpavtpae geatslstvr ptaaptgapt tvpalatald tsrttsrtts
      361 gtaapspsra agrrtsppaa eptprrrtsa ptakqvrtgn pagtpvgqep rkepapdpgd
      421 estpqsaett slpyptpppn pftcipstc
//
LOCUS       WP_357629074             192 aa            linear   BCT 28-DEC-2024
DEFINITION  dTDP-4-dehydrorhamnose 3,5-epimerase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357629074
VERSION     WP_357629074.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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..192
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..192
                     /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=20234
     Region          3..168
                     /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 mdqlsiegsw lftprvhadp rgafleafka aelphplgva qvncsvsrag vlrgvhyadv
       61 ppgqakyvtc vsgavldvvv dlragsptfg rwesavldde trramlvaeg lghafmalse
      121 qatvvylcsa tynpagehgv npldpdlgid wpaglepvls dqdaaapsla ealaagllpd
      181 yhacrefyat lh
//
LOCUS       WP_357629066             304 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nonomuraea wenchangensis].
ACCESSION   WP_357629066
VERSION     WP_357629066.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  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 11430850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..304
                     /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=29975
     Region          1..287
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
ORIGIN      
        1 mrngpiavva aavlwgtagt agllvsadsv alaaarlvvg gaalalmags girrvlspgl
       61 llgavavaay qlcffaavar tgvaigtvva igsgpvftgl lswllhrrrp srrwamataa
      121 aicgcaaliv gggvsaagst sgqvvsgvlf allggllyaf yavmaarais dggesnavmg
      181 vmfggaalim lpvlvvnggv gweprglvav lylglgttal syflygrglr ttpvataatl
      241 alaepavaal lgvvvlgerl apvsvaglvl lafslaavai peraarpevr vpaeagapgv
      301 rerr
//
LOCUS       WP_357629126             306 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357629126
VERSION     WP_357629126.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 306)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..306
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..306
                     /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=34018
     Region          24..303
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mitkpaptap rarprgrraw rdilvgwsfi lpnfagfllf tiipmlaafa lafldwdsys
       61 dpewvgldnf arlltdqnfh valrntlfya aghipltlaa alglaialnr klrgvpffrt
      121 aaffpyitsl vavavvwnml fnptagpinq vleaigvshp prwvastdwa mpaviitsvw
      181 rdmgyymvly laglqtipke yyeaarvdga nawqrfwgit lpslrpttff vvvmltiqsf
      241 kvldlilvmt dggpgrstlv laqliyregi tegkfgyssa ialvlfvivl tvtvvqfrin
      301 errsas
//
LOCUS       WP_357629171             337 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sediminicola].
ACCESSION   WP_357629171
VERSION     WP_357629171.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 337)
  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 337)
  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..337
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..337
                     /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=34960
     Region          1..318
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrvglvgagg vaqrharvlt gfedvellgv tdvapdaara ladahggraf rdveellaag
       61 pdavyvcvpp fahgpaeeav vaagvpmfve kpvavdleta eriadlvqrr glltgvghhw
      121 rylhvveear rllagrpvrm vngawldkvp pvawwarrdr sggpvveqaa hvldlvrllv
      181 geatevtayg dgtpppvdga didsvtaatl rfasgavgtl aaacvltwkh ragleiladg
      241 lalslaedgl tirdadgerh lpadpdgarv avdrafvdav rgvgddvrvp yaealrtqrl
      301 alavaesart grpvalptgp aarltaavad agvgvda
//
LOCUS       WP_357629231             189 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea wenchangensis].
ACCESSION   WP_357629231
VERSION     WP_357629231.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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 189)
  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 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   5  (residues 1 to 189)
  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 189)
  AUTHORS   Rosinski,J.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..189
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..189
                     /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=21784
     Region          1..78
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mrqiddldvl kvltsrfrmk lfsllfrigp vtvselarrm gadpgqvsyh lrqmqkhgli
       61 edvpelards rerwvraaml gweldtdfea peaaavvqaw tsqwvidqfe rlrdyqrthm
      121 tlpedwrgag fgssrhlrlt kdelarlgdq ldavlqpwre ltksrvesse appdtapilv
      181 fyhafpeep
//
LOCUS       WP_357629277             247 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357629277
VERSION     WP_357629277.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=27181
     Region          5..147
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mrqediwdae taqsydtpgv gmfapevlep tvdrlaelag egralefaig tgrvavplae
       61 rgvpvtgiel sspmidqlrt kvdkatipvi agdmatatap gkytlvylvf ntisnlltqa
      121 eqvacfrnaa rhllpggrfv ielwvpelrk lpsgqqavvf hsepgyigld tydivrqhlv
      181 shhftfdasr qarlfrsphr yiwpseldlm aqlagfeles rhadwagadf taesrshvsv
      241 yrippgn
//
LOCUS       WP_357629317             395 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357629317
VERSION     WP_357629317.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..395
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40262
     Region          1..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 msgalsgllv adfsrvlagp yatmlladlg advvkverpg vgddtrswgp pyageeptgg
       61 eatggeatgg eatggeatyf lavnrnkrsi aldlrdpada evaralaara dvlvenfrpg
      121 tmdrlglghd alrelnpglv ycsitgfgeg egaklpgydl iaqavgglms vtgepggpgt
      181 kagvalvdvi tglhatvgvl aalrhrdatg egqrvtvsll ssllsamtnl asgyaaagvv
      241 ptamgnrhps ivpyevfqaa drpiviaagn drqfralcev lgradlaada rfaansgrva
      301 hreelcaelt ralaartaga wfadltaagv pcgpintvag afelatglgl rpivgegpaa
      361 qvanpiglgr tppeyrlapp slgqddqwvr eilgd
//
LOCUS       WP_357629352             303 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357629352
VERSION     WP_357629352.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 303)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..303
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..303
                     /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=32819
     Region          34..277
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msptlrqqeg raglalispt lvvtvvvvvl pllwaimlaf qdvrlinirs kglfggytle
       61 nfryvisepg fwsalvntlv ytvagtalsi avglvaalal rdrfkgrtlv rasilvpyva
      121 pvvavaflwe tmlnpqygiv ntwlsqpiaf lsqakgtllg vevpvalltv iafeawryfp
      181 faflfilarl qalpadleea avvdgatpaq sfrhvvlpql arviallavl rfvftftkfd
      241 dvylltggga gtevvsvrvy nfltarddig asaaqaivla vvlvvflvly lkffaggere
      301 rdg
//
LOCUS       WP_357629356             295 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357629356
VERSION     WP_357629356.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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..295
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..295
                     /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=32512
     Region          1..293
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklgfltacl peldlvdvar waaahgfeal evagwpstdt rnhirvdrfd eaerervgri
       61 faetgltlss iayyennlhp ragaevnahv rrcvdaaaal gcptvgtfvg rdpglsvrdn
      121 leraegvfrp lvayardhgv dlvienclmk swhpdgypgn layspelwew mftlglrlny
      181 dpshlvalgi dpvaaampyv sqishvqakd tellpgtinr fgfygpisge kgwyrfrvpg
      241 lgqvdwsqvi galrrggydg vvsvehedpe wtgstdrvqt glgiayrtlr hlvrg
//
LOCUS       WP_357629383             195 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357629383
VERSION     WP_357629383.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 195)
  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..195
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..195
                     /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=21193
     Region          10..141
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkdsrtpsmd rrvlrtrsal aralltlvee relsrigvsd vaeragvsrt afydhyrdvh
       61 elaeaactam idgltrslpt prpdsadlqg eatrsleaff aslaehagly rsllgpqgsa
      121 rvadhirrrl tdgvrehvre ahdvpaafta gaiygvaadw lqrgcpeppa rmaaltwplf
      181 halydvvsap pppat
//
LOCUS       WP_357629366             350 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050733].
ACCESSION   WP_357629366
VERSION     WP_357629366.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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 350)
  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 350)
  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..350
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     Protein         1..350
                     /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=36565
     Region          24..350
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mfpmaarlnv lfdfaqkwdm rdvssttrvg iigagnvaar hadvlsgfpd vviagiadvd
       61 plkaealaar hgvpaydgha glleagrlda vyvcvppfah gkpeqdvlsc nlpifvekpl
      121 aldlttaeni aseiqrrglp savghhwryl dvldrardll adrpvrlalg hwldkvppvg
      181 wwldparsgg qvveqavhvl dlarvlvgev tmvhavpaap aapaapggdg aagaagevdr
      241 avaavlsfag gatgtlatts llrhkhragl evyadgvale ltetsltvng gevvedagra
      301 ktlvdrafvd avrgadgdvr vpyaealrth rvalalarsa aegrpvtldd
//
LOCUS       WP_357629402             183 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Nonomuraea wenchangensis].
ACCESSION   WP_357629402
VERSION     WP_357629402.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 183)
  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 183)
  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..183
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..183
                     /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=19621
     Region          <35..183
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 msgrrrtala pltvlvtvll laltlaasvp vstwtqprvv rlayelgrlg veyswgggha
       61 eapgpstgtc qgyqgrirpc paartrgldc sgftrwvyal ahgrdvlgpg ntddhvrrmh
      121 rvrsaplpgd lvffgviagd tvrthhvgvy lggglmmnap etgarvrvdr lagredlagf
      181 yry
//
LOCUS       WP_357629419             570 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing serine/threonine protein kinase
            [Nonomuraea wenchangensis].
ACCESSION   WP_357629419
VERSION     WP_357629419.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11600203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..570
                     /product="WD40 repeat domain-containing serine/threonine
                     protein kinase"
                     /calculated_mol_wt=60574
     Region          11..279
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,68,73,78..81,97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,76,96..99,103,105,141,143,
                     145..146,148,158..159,162,183..186)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,76,96..99,103,143,145..146,
                     148,158..159)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,103,105,141,143,145,162,183..186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(158..166,179..186)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          253..564
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          342..379
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          384..421
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          428..464
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          470..510
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mtvrdqllgg ryrlvrqlge ggmgqvweaq detlgrpvav kvisllaggg slgdeararf
       61 lrearitarl qhpnivtvhd lgetggaddr vpflvmelvr gegldatlrr gavalpdaar
      121 wgaqicdalg dahdagilhr dikpsnilit psgtvkvldf gvaraadpna tadrltrtgf
      181 lvgtppymap eqargfpepr sdlyalgcll felitgrlpf hapdtvgylt ahlteepppp
      241 ssvaqgippa wddlvlallr kdpgrrhrna adlaqalrrl dhapapntst lpltkldipv
      301 apepgeyfla tsiggegtlr lwdpatgrpv tqpltghtgt vfrmafspdg rllasasvdt
      361 tarlwdaatg rpvgepltgh tntvvgvafs pdgrllatts mdttvrlwdp atgrpvgkpl
      421 tghtghvlrv afspdgrlla tssrdwtarl wdpatgrpvg kpltghtgnv wdvafspdss
      481 llgthsednt allwdlatgr lvgrpltapa nghvgavcsl dgllvvatmd ehgtvqlwdl
      541 ttrqpvgrpl ttraglpvyv alsprighrh
//
LOCUS       WP_357629443             951 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357629443
VERSION     WP_357629443.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..951
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..951
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=103947
     Region          <2..951
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mrgrsvspvf vgreeelaal sesfedalkg kvtavllgge agvgktrlvq rfaercaadg
       61 aqvllggcve lsteglayap ftaalrqlvr eqgpaavaal lpegaerdla rllpefgepv
      121 gdgetdtgra rlfeqiltll erlsdarptv lviedihwad rssrdliafl srnlhipqvl
      181 ilmtyrsddl hrqhplrpvl aelgrvqgvd rldlprlsrd evaqqmtail grvpeyarve
      241 kvyersegip lfveamldgg edcgfpesmq dlilnsverl peetqrvlri aaaggirvgh
      301 allaavsgls dieletalrp aiagnvlqva dnrayvfrhs liqeavheel lpgehqrlhs
      361 ryaeeiskdr tlvppgraav elahhwygar ndlwalisaw eaarksfkaf ayteavplle
      421 rvlmlwdrvp daaerigadh tavlerasea anaggdvdkg mkfvkaalkq ldetteparv
      481 aqlivrraaf ksskghmgvi edlrdalrlv pqdsleraev vtplsrhlml rgriaeasel
      541 iteglrlarr hgdrclesdl lmnlalghsl ngetesvial neqaleigre eqshriilra
      601 ignnidslie mgrheealal seqgwetark wgrlrgsglf imnnwaevle aigrwdeaie
      661 iveaalaygp alrtryallr vradialarg evelvenils evgvvkdrpe dfvqditnna
      721 rlrigwhllr geptqalata eqvlahptrs skaklgwrll sllrnvcdaa gpaepertaa
      781 vraraaevaa qlsvigpvve ayrlsysgdf daaaagwerl nrphnqakal lraaadaart
      841 gdregaaarl kvalplaral ratpliediv tlsrrvggga pqsqepsell tprelevlrl
      901 vtqgrtnrdi aaelfisakt vsvhvsnila klgvttrgea aaaahrlsll a
//
LOCUS       WP_357629454             549 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine/threonine-protein kinase [unclassified
            Nonomuraea].
ACCESSION   WP_357629454
VERSION     WP_357629454.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   3  (residues 1 to 549)
  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 12993645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..549
                     /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=57040
     Region          12..268
                     /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..37,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <274..457
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mpehqtrlla eryelisplg rgtmgtvwra rdralgreva vkeirqdsgl teeqraelre
       61 rmvregriaa rishpavaai hdvliedgsp wiimelvear sleqvideeg plpprlvael
      121 gvdllgalra ahaqgithrd vkpgnvlite tgrvvltdfg iakaegdprl tktgmvigsp
      181 gytaperarg eytgpesdiw slgatlyfav egrpayeras iaetlaalls enadpptqag
      241 qlgpvltgll nkdhkkrlsa akaetmlrmv adtpthempv itaealtgqe asvpdatnst
      301 ggpgrpgspa sgpqrgagar pqgggtagsq gsgrdgsgtv prpkagaapg aqtgpqqagp
      361 qqagsrqpaa qqsgpqqpgs qrtggqgpgg avpdsertvs lmrpktplpg rpqqgppvde
      421 gslhtqriqt prphsappgq qvyppapgqq parpvppsrp gqypqqpvpg qgpyqgpppg
      481 prqpgpapyg pqgmaterpd skglgtdlfa iagpeerpsg nrtgmlvlma vaaaaavmia
      541 ilivailss
//
LOCUS       WP_357629544             210 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora
            sediminicola].
ACCESSION   WP_357629544
VERSION     WP_357629544.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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]"
                     /calculated_mol_wt=21613
     Region          22..148
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mgvshpifar lfarasvald eagvaahrrr lvaglrgrvv evgagngrnl phyppavtgv
       61 lavepeprlr alaraaapaa rvpvtvaagl aealpvadga adavvfslvl csvpdqaval
      121 aearrvlrpg gelrfyehvv aqtpglrrvq rvadatlwpl fcagchtard tvaaigaagf
      181 tvtgldrfrf peaglpapas phvlgtaira
//
LOCUS       WP_357629551             338 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora sediminicola].
ACCESSION   WP_357629551
VERSION     WP_357629551.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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..338
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..338
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36309
     Region          31..240
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mislvvptlg rpslavllda laaqlggdda paevelllvd drrddtgela vsgaltayak
       61 vltgrgagpa aarnlgwraa rgewvvfldd dvvpapdwir rlradlavpg rvggvqgvvq
      121 vplpahrrpt dwergtagla egrwitadma yrrvalaavg gfderfpray redaelahrv
      181 rrvgwelvrg rrrvthpvrp esrwvslrtq rgnaddallr rlhgrrwrae ldlppgrrpr
      241 hvavtaagav alaavaarav trpssrsrra sgvlgglaal gwaagtaefa rariapgprt
      301 pdevatmvat salipplavv hwvrgwwrar alpvgagr
//
LOCUS       WP_357629598             754 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: WD40 repeat domain-containing serine/threonine
            protein kinase [unclassified Nonomuraea].
ACCESSION   WP_357629598
VERSION     WP_357629598.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11600203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..754
                     /product="WD40 repeat domain-containing serine/threonine
                     protein kinase"
                     /calculated_mol_wt=75545
     Region          31..267
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(40..41,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(101,103,140,142,144,160,175..178)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(156..164,171..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          362..754
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
ORIGIN      
        1 mpeprvlhad eppeiggyrl lgglgdggqg svylgkdagg rrvavkvlha rlmgndratr
       61 rflqecvlag rvaafctarv idsgladgrp yivseyvpgp slrelvaeeg prtggaldrl
      121 avgtvaalga ihragivhrd fkpanvlcgp dgprvidfgi akgveaatsa stvvgtpgym
      181 apeqiagdpa tpasdlfawa atmayaatgr slfagesipa vmhrilteep dlsgvdeplr
      241 sllaacldkr paarpsaada lsalmegglm eggpaeggpv lertllegtp fedagrrgvg
      301 grgedgrged ghgafpaevr tarpgrrhgp rgtsrddgnp pagrlragnr qveglesgdp
      361 erdeglvvsr rgravavggl avlvlggval glnwngsslg srsgsassaa grggpdgadv
      421 aeaygpssgv alrgreaaal avgemggrav vavaregepv qvwdaatggr laaapeparg
      481 vtslafaevg gaptvvwaae dgrvsrwtpt ltpagptasp aagevsaasa gargavraft
      541 actsrspqaa ataavmavvg reegpavavg caggmvrawd llsgrksglf fageaaitgv
      601 awpgsgsrvv fgtaathfqi gdlwghekav kvhvdgrvsh vvsrgglvaa svegrggatv
      661 ydvtgrevcr vpaqeapgta alalteaggr allagavtag gglrvwdart cgrvatllps
      721 gsvtalaagp ldgspglvaa vggtmrawtl ragr
//
LOCUS       WP_357629559             969 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357629559
VERSION     WP_357629559.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 969)
  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 969)
  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 969)
  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 969)
  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..969
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..969
                     /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=104783
     Region          19..260
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          140..952
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          787..815
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(828,831..832,835..836,838,868,871..872,875..876,
                     878..879,907,910..911,914..915,918)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          828..855
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          866..901
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          906..934
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 maarsrgreq eaetgtregv efrllgpvgv wdagrllgps taqqrtvlat lllepgrpvp
       61 varletalwg aeppdssrna iqghisrlrr llapfpeaal ttsahgyclt varervdlhr
      121 frdlvreagg epeperaagl lraaltlwqg tpladaagrw aadvvapgle eerltalerl
      181 aaldlrqgrh qevaaelval lgehplrerl vsllmtallr ddrrtealav frrvrrrfae
      241 dlgiepgeel qrlhqailag heppaaaapg gshdgpsggp aalavprhlp pdtelftare
      301 eelaaldrlt lppdgspvla pcvitgtggv gkttlavhwg hrvrdrfpdg qlyvnlhgfg
      361 pthglrppae avrlfldalq vppqhipatl eaqvglyrsl laerrmlill dnaldsdqvr
      421 pllpntpgcl alitsraelt glvaaegaht lslglfspaq srelltrrlg vdkvgaepra
      481 vddivsrcag lplalaivaa ranerpafpl gtlvsdlage gdssedldvf dggdaatnmr
      541 tvlswsyral spdaarlfrl rgllpapeis taaaaslagi pvprarrllt eltranlate
      601 rtpgrygwhd llrayaeelt rlhdsaaerr ealhrlldhy lhsarvgdrl ldllhrvplt
      661 pppprpgvvl aritdpaqsr awfaqehrtl laairhaara gfdvhawqla gacwgflsqd
      721 vrsddqaaif tiameaasrl gdpaaeahar vglahaftrl grdedgeshl rrarelfagl
      781 gdpagealcl iylsvlmdrh dqyadglals eealrlcraa gdragegrvl nnigwfhaql
      841 gayeealrrc eealaihrel tdlpgesatl dsmghihhll gqyeeaiayy rrslawrggg
      901 kralgartlr rlgeaqlaag rlreggetlr qalalisela pgdaealrar vaslpdapgt
      961 hpprprart
//
LOCUS       WP_357629689             165 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora sediminicola].
ACCESSION   WP_357629689
VERSION     WP_357629689.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 165)
  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 165)
  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..165
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..165
                     /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=17916
     Region          1..149
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mdvreaapad lddivdlhtr arvayygagg lptgeivnpe lareqrdgwt aaiaaphkhv
       61 rcavvdgrvv gllamgpphs sevdaaqlyq ihvdpdcwgr gvgstlhglf lrhleaegla
      121 vgvlevwern trarvfytrh gwrpdgttrp gpadapylgm rlhhp
//
LOCUS       WP_357629787             390 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357629787
VERSION     WP_357629787.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 390)
  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..390
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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]"
                     /calculated_mol_wt=41226
     Region          121..390
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpaplsyppl vdaarrrlre lpplladaal taaillaqlw pllfgdsshd gpwdwwgyav
       61 aagaslplvw rrrapatvli tslsvgalyd ladnvarqpi wygatvafyt vaaysprwkr
      121 lvmlvltlsg gllvvgsses alrgivvfva ayaigrtaat srahaaalee raaqlekerq
      181 meaeraaere rariardmhd ilahavsimv vqaeagpvvv rtnparaeaa fdaiaaagrd
      241 amaqlrrmlg vlkegeapra pqptvgdlpa lagqvsgtgl dvtfsetgep rpltpdcava
      301 ayritqealt ntvkhagarh adirltwedh nlmiditddg qgsgrglpsg gngligmrer
      361 aaacggaata gprqdgpgyr vsvrlpvvtp
//
LOCUS       WP_357629839             389 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: homogentisate 1,2-dioxygenase [unclassified
            Nonomuraea].
ACCESSION   WP_357629839
VERSION     WP_357629839.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..389
                     /product="homogentisate 1,2-dioxygenase"
                     /calculated_mol_wt=43004
     Region          1..388
                     /region_name="HmgA"
                     /note="Homogentisate 1,2-dioxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3508"
                     /db_xref="CDD:442731"
ORIGIN      
        1 mpyyrvvgev prkrhvqfrk pdgglyaeel mgeegfssds sllyhrhlpt aivkaeavtq
       61 daatrlepnl plsprhfrtq dlagagdlvs grvllagngd vrlsyattdr pselyrdsmg
      121 decvyiqrgr vrfestygvi eagegdyvvv ptgtihrwvp dgqvnalvie aaghirpprr
      181 ylsqygqfle hapyserdlr apaepllvdg eevpvlvrtr ggltrlfyrh hpfdvvgwdg
      241 clypyafnir dfepvvkrth apppvhqtfe gpgfvvcsfc prpldfhpes vpipynhhnv
      301 dsdefmfyvg gdysarkgsg idvgsvslhp agfthgpqpg aveavidava rgvtttsema
      361 vmvdtfrpld lgqgalsced pgyawtwar
//
LOCUS       WP_357629862             312 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357629862
VERSION     WP_357629862.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 312)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..312
                     /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=34494
     Region          18..309
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msslgraaat raavrpatrr rlrdrdwvwg yamiaplvlg lgvfylwpvv qsvyysftew
       61 tlfgdatwvg lrnyeqlltd panakalrnt flygglsllg iplsiavaal lgtrglrlvs
      121 lyrtlyflpv vtmpaavami wtwlyngdyg linyllslag ihgtswiaep stalyalvav
      181 giwtqigyna vifmaglqsi pahlyeaasi dgagrarqff ritlpllsps vffvsvlsvi
      241 nglqmfdlvy lmlrrgnpar edtqtvvslf fsrafeegak gyaaamavvl maitlvltvi
      301 qfrvqkrwvh ya
//
LOCUS       WP_357629865             419 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Nonomuraea].
ACCESSION   WP_357629865
VERSION     WP_357629865.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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 419)
  AUTHORS   ter Beek,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..419
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..419
                     /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=45677
     Region          34..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(145,147,270,272,302..304,344)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mtgkmralmc agalvaglag csssdgggsg gkvtltyayw dsenqgqamt kivqeftkth
       61 pnievklqft pnkeywtklq taaaggtapd vfwmngprig lyasqgalmp lsdriaadkl
      121 dlgkypkslv dlytldgkqy gipkdfdtig lwynkdlfda akvtypdasw twddvraaak
      181 kltdpakgvh gigampwsqe lyyntifqag gyvisddrkk sgyddpatie glkfwkdlld
      241 rklsptvqqm tdndpiemfk sgklamwydg sydasqyfkt eglkagvapl pagpkgratv
      301 ihglanvvya ktkhpdeawe fvkflgsera nriqaeagav ipayeglqes wvksmpglnl
      361 qafidqvpda rpypvsknta awtrletdai tkaftegqdv eavarqlaaa mnaalsqek
//
LOCUS       WP_357629887             378 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357629887
VERSION     WP_357629887.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=40392
     Region          1..377
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrwtvrlrlt llytglflla gtalvvlvyv lveyspfprp paapappggt gpvppgtvad
       61 apreaelrrl lvnslvalpv mafasmalgw hvagrvlrpl armtatvrhi tadrldrrla
      121 akgpddelke ladtfdalld rlesaftaqr afvanashel rtpltlqram aevaladpea
      181 daaalrvvle rllaagrhqe rliealltla rsrqsperrr pfdlseitrq aiegrdgdtg
      241 pragtgppsa patgprvead lrtapaagdr alverlvanl ldnaarhnvp ggwirvvtgv
      301 eagrptlrvs nsgrvippdr vatllqpfqr letgrrttdd glglglsiva aiveahrgtl
      361 earaqpdggl evavtlpp
//
LOCUS       WP_357629913             303 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357629913
VERSION     WP_357629913.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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 14302731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..303
                     /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=33267
     Region          32..>82
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          105..271
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdraqqlsef lktrrarlgp detgagnfgg qrrvpglrre elallagvsv dyytrleqgr
       61 arnvsadvld avagalrlda deraylhnla kpsatrkrps rpqqvrpemr qaldalsavp
      121 ayiigrrldv lawnelarll iadfpalpaa ernmarlvfl deaahdlypd weakardtva
      181 nlrfdagrhp ddpqlatlvg elslhsadfr rlwadhgvrg kthgrkrfah prlgelaldy
      241 vamrapddpd ltmmiysapd gsdataslhl lasftapssa tagpqhdtaa krqgldnqpa
      301 rha
//
LOCUS       WP_357629956             447 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora sediminicola].
ACCESSION   WP_357629956
VERSION     WP_357629956.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=47012
     Region          8..429
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtliatrpgp gaarayrfpq vvrrtvaggq vvaahlpgqt lavalllldg gagrepvgke
       61 glgavlakal eegtaqrdat ayalaiealg telvagldwd sfqvsvqvpv drlsaavell
      121 aeavrtprld ptdvlrvrdd eatalrmdwa npgpradavl radlfgadnr wgrplygdpe
      181 svaalevddv tvfhsewfir pgtlivagdl eridldalga tafagtgggp vdrggpiett
      241 lagrrrvilv drpgsvqstl rlghpsphra hpdhvpmtla gtvlggafts rlnhlirevr
      301 gytygirgdf assrrfgrfa vtsgvqtavt apalvesvge vsrtqltgvs eeelevarsw
      361 ragqlsvelq spraiasalt tlvvhdlpdd yharlreall aatveevsaa aaahlhpesl
      421 tlvvegdaav irdelvaagl gdivdhg
//
LOCUS       WP_357629959             492 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357629959
VERSION     WP_357629959.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 492)
  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 492)
  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
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..492
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52942
     Region          6..491
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mgeltlgrla eeawnrfddh davhydgvwh rghalaerar rvcggfveag irpgdrvavm
       61 manspdvavi yqalwaagav vtpvvslvga gelrhiltds gasaivtspe llaiveeagv
      121 gvrtfldtse lreadehgpv prepgdlaal mytggttgka kgvmlshrgl wqvardayem
      181 shqdgldrai vpvplshayg livtvagmha ttpqqavlmr sfdpkaflsl aaeqrvqygt
      241 vvptmlhmll aepleshplp dlkfltcgaa plgrdvlaef errmpgtqil egygltetsa
      301 vttfnppgrr ragsvglpla gyelairdss geevecgdvg eicvrgeslm lgywgehahd
      361 pdgtalagge lrtgdigcvd ddgylyvvdr kkdliirggf nvfprdveda lnehpevvms
      421 gvvgrpdprm geevvafvql mpdatvtaae liawarqrvg rvkyprevvf vdsvpvtsvl
      481 kldrkalrar lp
//
LOCUS       WP_357629986             247 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea wenchangensis].
ACCESSION   WP_357629986
VERSION     WP_357629986.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 18603527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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: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=27593
     Region          43..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"
     Region          <108..195
                     /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 mssgydrvvq paagdealen hlggdeakny rqyefdmvap hvgrsmleig sglghfaeqf
       61 lprldrlvvs dfdpycveql ekrfagrdei dvlqfglptd ipledkvdtv vlmnvlehie
      121 ddaealrsla rvtlpggrii iwvpgypqly gdfdrkvghv qrytpktlga tiaragldve
      181 vlkpinflgg iawwaavrrg gvgypdprlv kiydrtvvpl trlierffrp pfgqtvfcva
      241 rvpqsrs
//
LOCUS       WP_357630032              86 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [unclassified Nonomuraea].
ACCESSION   WP_357630032
VERSION     WP_357630032.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 86)
  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..86
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..86
                     /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=8919
     Region          2..>66
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawfmivaag lfevamaysl klsdgfsslp psicfgvfav asfgllafal kslevgtaya
       61 vwtgigrpvr ppaappepev iqvltt
//
LOCUS       WP_357630066             216 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357630066
VERSION     WP_357630066.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 216)
  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..216
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..216
                     /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=23641
     Region          10..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtarsaravr vgetreqilt aaerlfaehg vyavsnrqvs eaagqgnnaa vgyhfgtkad
       61 lvraiarkha qpierarrrm laemgdstev rdwvaclvrp vtdhlaalgn ptwfarfgaq
      121 vmtdpalrei midesltsps lrqiidglrr hlpelpedvr aeraemggql mvhmcavreh
      181 alaegvptpr stwhdaatgl idaitgvwla pvtrep
//
LOCUS       WP_357630101             187 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: cysteine hydrolase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357630101
VERSION     WP_357630101.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..187
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19853
     Region          8..168
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mtsrtgrlav idmqrifgep dspwfaprfa eivepirklv gafgpwvtft rfvapeapag
       61 awvdyyerwp falqppgsha yglvddlagl aadagptlda ptfgkwtpel agrvgqdgrl
      121 vlagvstdcc vlstalaaad agvevlvaad acagaddtsh qralevmrly eplirvvtvs
      181 dilarpd
//
LOCUS       WP_357630106             170 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sediminicola].
ACCESSION   WP_357630106
VERSION     WP_357630106.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=18717
     Region          22..159
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtdrdsvdqh varwqpvlpd ldpdvegavv rmmlltrhlr avkdrvladl dlqekeygtl
       61 hvlagrgrra apseiadalr mapasitarv dalvrrgfvr ripsevdrrr vdvalteage
      121 aiwrraldvv gdeehrvlga ldaaerrtla dllrrvnsaa erptgnvggp
//
LOCUS       WP_357630161             242 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            sediminicola].
ACCESSION   WP_357630161
VERSION     WP_357630161.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24269
     Region          4..242
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtsvtivtgg grgigaatar rlaadghdlv igyrtdhaaa esvaadvraa grravtvaad
       61 tcdpeqvsrl faaadqlgpl tglvnnagvt spigpftdlr aedlrevvdv nlvgyvlcaq
      121 qaarrmtagg aivnvssaaa tlgspgeyih yaavkaatdt ltvglakela prgirvnava
      181 pgiirtdiha rsgvpdrpdt aagriplgra gepdevagai ahllgpdasy ttgavlrvag
      241 gl
//
LOCUS       WP_357630108             473 aa            linear   BCT 28-DEC-2024
DEFINITION  uracil-xanthine permease family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357630108
VERSION     WP_357630108.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 473)
  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 473)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..473
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48590
     Region          11..466
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mvwgwtrhgd gkhlapgevv rpderlswpr tvgigaqhvi amfgatfvfp lvmgldpnia
       61 vmmsgvatil fllivkgrvp sylgtsasfv ggvlairava ggdtagadav vtgailvvgl
      121 vlaligvaih flgvqiihrv fppvvtgavv mligfglayv vadvywpqdh wvalltmlit
      181 fvmivafkgf igrigvlvgl vagfvlswvl drlagpitsv lpganlrdaa gnacapegpy
      241 clatafphdr vsfdnvakad wfglpnfhgp dfrfsavllv lpavialvae nvghvkavge
      301 mtgtdvdpyv gravaadgva tvvasavggs ptttyaenig vmaatkvyst aayyvaavia
      361 ilfglcpkfg qlvaatpggv lggvtvilyg migllgakiw ienrvdfadp vnmvptgagi
      421 ilaigpvthf vggdltlegi algtivvlgg yhllraiagr plepappvgs eag
//
LOCUS       WP_357630162             187 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea wenchangensis].
ACCESSION   WP_357630162
VERSION     WP_357630162.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 187)
  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 187)
  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 187)
  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 187)
  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..187
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..187
                     /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=20703
     Region          19..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 mkqlftvglg ddgallgale pwraeeflah iergrehigr ytgladvvtd lesarsylls
       61 yadkaaadtg rlygiwldgl lvggvlfrtm dvarglaeag cwlepaavgk glvtravrvi
      121 idwaveergi hrvewwaaae ntasvavarr lgmtrdgvlr ehyphrgrrl dmeiwsvlap
      181 ewraarr
//
LOCUS       WP_357630175             113 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357630175
VERSION     WP_357630175.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   4  (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
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..113
                     /product="PadR 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=12557
     Region          1..96
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mksnaprmtl ptqavlrall adparerygl elcdlaglpg gtvypilarl erlgwvesrw
       61 edpgaheeag rprrryyrit pdgaergrda varayrsrrq pvpawllhpg gts
//
LOCUS       WP_357630214             381 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050733].
ACCESSION   WP_357630214
VERSION     WP_357630214.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 381)
  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..381
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     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=39903
     Region          135..378
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtsarladpa tdlagvrrwv veaglgglfa gtivfvayri avswggasww fgaaagavvc
       61 glallrrrhr vraavaglav aaaailtarl ahlpaepspa malalavltg savralpwrq
      121 aggiaaggla vapaalasfs grpavavlng aawlaavglg lgarllrarr qaavervrrd
      181 erlrlarelh dvvahhvtsv vlqtqaarvv arrhpervdd cladieaags dalagarrav
      241 gllrddappp dpparlrelv erfagppvrl tlpeeepvwp pemartvyri vqesltnvsr
      301 haphartvtv cvtedldtlt vevtddappa parflhrggy glagmrerld alggtfaagp
      361 rpdaagwavr atlplpprer g
//
LOCUS       WP_357630245             144 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357630245
VERSION     WP_357630245.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 144)
  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 144)
  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..144
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..144
                     /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=15806
     Region          10..140
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msltpddspg fllwrttlrw qravtaalep fdlthvqfvl lacawwlnrq gelpnqlava
       61 rqagadvkma sqvlrkledk gflvretdpa dsrakllrvt drgsgliera vaevertdta
      121 ffaaapdhas listlrslad gdhp
//
LOCUS       WP_357630265             596 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Micromonospora
            sediminicola].
ACCESSION   WP_357630265
VERSION     WP_357630265.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 596)
  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 596)
  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..596
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..596
                     /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=63955
     Region          38..572
                     /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 mtsssgasrr qvlavaaaaa tapllagapa eakpkqpktw dltvlgtsdt hgnvynwdyy
       61 kdaefddskh ndvgiaklat lvnqiraerk gratlvldag dtiqgtplat yyakqepits
      121 tgethpmana mnvlkydavt lgnhefnygl pllatwieql gfpalaanai naktgkpafl
      181 pyvikevrlg ghgapklrvg ilgltnpgva iwdkanvegr lvfadmvata akwvpemrrr
      241 gadvviisah ggdsgtssyg pelpnenpta liaeqvpgid ailfghahne vpekfvtnlk
      301 tgkavltsep skwgqrltrm dftltrekgc wkvvdssatt lntntvvedp avlaavrgqh
      361 aktveyvnrv varssvelsa aesrykdtpi ldfinhvqte vvtaalagga yaglpvlsia
      421 apfsrtavfp qgdvrirdva glyvydntle avvltgaevk ayleysakyf vtvpvgapvn
      481 petisdpavp dynydvfsgv dydidiskpv gqritrlvla gtdtpvaada qfvvavnnyr
      541 rsgggnfpgi vktqvyneqq eirqllvdwa qakgvidpad ffvpnwklvr egvpvf
//
LOCUS       WP_357630285             375 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357630285
VERSION     WP_357630285.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 375)
  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..375
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=39408
     Region          178..373
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlrqrpfglt awpawspirp grgrreargl lvlvafliwp lwdllgreha gplavalmlv
       61 ygaswvtama ygvgrpprer vallawllvl tvaltlvrqd qaghvplggl ayaltaavwl
      121 lpalwgllva vaaaaarlli lygttggavw gavpsvladt lapvavvllv rllvqlgqan
      181 qeiealataa erarlardlh dvlghsltai takaglarrl lergagpeqa laelrdverl
      241 srqahaeira tvsgvrrpsl taelsgvrva lraadiaavl pssveevaed lrepfayvlr
      301 egvtnvirhs gatrcevrld assleirddg hgggtgagta gsglaglger lrvvggslea
      361 gplpqggfrl rasrp
//
LOCUS       WP_357630359             669 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Nonomuraea wenchangensis].
ACCESSION   WP_357630359
VERSION     WP_357630359.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 669)
  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 669)
  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..669
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..669
                     /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=69710
     Region          3..475
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          598..664
                     /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(621,630..632,639)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            631
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mlfdrvlian rgeiavriar tlrrlgvtav avhtpsdada rhvreadlal evpsyldada
       61 iagaalasga qavhpgygfl aenaafarac aaagtafvgp paeaidamgd kirakatvsa
      121 agvpvvpgga epgdvleewr dfpalikpsa ggggkgmvlv rsaaelpdal asarrtalaa
      181 fgdatllier yvesprhiei qvladalgga vhlgerecsl qrrhqkviee apspfvtsel
      241 rarmgaaave aaravgyvga gtvefivdga tgayhfmemn trlqvehpvt elvtgldlve
      301 lqlrvaagep lpfgqddvrl sghavearvy aedpargflp tggrvlllre pgvpgpaaqs
      361 aaqsaaqpds rpagsgplvr tdsglteggv vgsefdpmls kvvawapdrk aalraldral
      421 agtavlgvvt nvpflralai hpavrageld tglieralpe lvtdadvpad vlaaaglvfh
      481 alpqgddpwe vtdgwrvger awttwrlasr dgvhdvrvrg lpaesaevlm eerpvparlr
      541 aegpevdvtl ggrtvrylca rdgdtlwlgr dghgwaftrh ligdpgdrpg aaasgdgvvr
      601 spmpgtvlvv kaqpgdrvta gqplviveam kmehavtapc agvvtdlpvq pgrpvdmdav
      661 lavvtpeee
//
LOCUS       WP_357630364            1027 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357630364
VERSION     WP_357630364.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1027)
  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 1027)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 1027)
  AUTHORS   Rosinski,J.A. 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 1027)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..1027
                     /product="helix-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=109902
     Region          <4..938
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <963..1024
                     /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 mtvhavsplf vgrarelaal rdalaearag vpatvlvgge agvgktrllg efadraddal
       61 vlvggclelg teglpfapft avlrglvrrl grdgvaalvp ggatsglarl lpefgepgre
      121 gaeararlfe lvlgllerla eerpvalvie dahwadrstr dllsflvryq rtagrlllvv
      181 tyrsdelhrt hplrpmlael grvewvsrve lrrltrreav aqaasilerr papadmdliy
      241 arsegnplfv eallsegggr gdlpeslrdl llarverlpe etqellrvas aggqriehdl
      301 lsavaglddn alsralrpav agnvlvvdge gysfrhalir ealhddllpg ehtrlhtrya
      361 ealerdpsil paprgaiela hhwhaahdst walvsawraa aaartstayd eqlrmlsrvl
      421 elwdqvpeaa grigadrlev lrqtavvahl ageyersial agallaelda etdpvrtavv
      481 lrqrgltryd lgrpgnlddl rraaslvpae pptrlraqvl eslsrmlfap edkdekiata
      541 eiareiarav gdanveansl itatwaryrf heveaqmeaf aearriaaaa daynalmrcs
      601 isesdalega gwheraaeva ragiadsahy glartsgtfl tinlaeplvs lgrwdealev
      661 ieqaldltpp apyraslqgl atdialargq fdraeqlfda srgvlsrgty rdqtllphlr
      721 rkvrllearg evgeavreva ealaerdlvs spryvwqllv tfahlltsaa agagggraap
      781 grasvaeaaa aslprlreva rrigtegelq eaqrltfeal lgpeppvagv earpgpespv
      841 agadalagpv tgagarlgpg vaaddveara gwrvkaweaa agawvdlgqp ypearallgs
      901 aqallaagdr qeaaarlera relatglgaa plleqldvvr rrarlggggt adepagdgqp
      961 lgltarelev lrevtngrsn reiaetlvis vktvsvhvsn ilaklgvagr geaaatahrl
     1021 hlfddla
//
LOCUS       WP_357630371             309 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357630371
VERSION     WP_357630371.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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..309
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..309
                     /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=31372
     Region          6..294
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mtdrgllvvg davtdvvalh gspvlagtdt aadimlrpgg sgantaawaa hlgadtrlla
       61 rlgydssdwh iaeltksgvr pqvtvdpdhp tavviamvdp sgersmltnr gaggliserd
      121 wdpallegva rlhlsgyvlf aapglglara amadaaaarv avsvdpastk plldfgverf
      181 maetaaadll ipnldealll sgaptperaa ellserygta vvklgadgal aavdgtitar
      241 vpglpgqvvd ttgagdafaa gflaatlrgc geraaleegc ragaacvaqv ggrprygldl
      301 nrlypihtd
//
LOCUS       WP_357630385             306 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357630385
VERSION     WP_357630385.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 306)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..306
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..306
                     /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=33827
     Region          25..286
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtatatrsap ptppgrrarr rgisrqtrem wvlmlpalvp vllfsvgpll ygiglaftda
       61 rntrnhetsf vglenltell taedfwssfr igmiwsvsvt glqflaalgl alllnqdlrf
      121 rgvarvlavv pwamppvvig lmwklvyhpd agilnsllgt hvnwladfsy alpaiivvgv
      181 wtgmpqttvv llaglqsvpr elyeavevdg agrwrkfwni tlpqlkpviv aitsldfvwn
      241 inqfglvyvl tqggpggqtr lpmlfayeea fryrfagyas mlglamavvv lavlgvylwr
      301 qmreak
//
LOCUS       WP_357630411             467 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357630411
VERSION     WP_357630411.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..467
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48222
     Region          4..451
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mrpidalvrs lsearvvtdp dvidsyardr tflepgrpla vvlaasrddv vatlrwaseh
       61 rvpvvprgag tglaggavag dgavvlslar mtairelspa deiavaepgv itadldraar
      121 ehglmyapdp ssyeistigg nlatnagglr cvkygvtrds vlglevvlad grvldtgrrt
      181 vkgvtgydlt glfvgsegtl gvitaatlrl rpapagppat faaefgslrd agaavsaiia
      241 agcapslmel ldratleaid gwrgiglepg tqamligqsd agdgqaaarr mericadnga
      301 sfvavstgpg eteelvglrr laypaterlg aclvedvcvp rsalpdmita ieaaaarhgv
      361 rictvahagd gnlhpvfvfe hgaaepppev waaadevftr alelggtltg ehgvgllkqr
      421 wlalesgpva aevqrgikav fdplgllnpg kaiqqlsdvq slpsrdl
//
LOCUS       WP_357630430             214 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NADPH-dependent F420 reductase [unclassified
            Nonomuraea].
ACCESSION   WP_357630430
VERSION     WP_357630430.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..214
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22013
     Region          3..200
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mrigilgagg madalgtqwh raghevmisg rdpertvaqa armtraaqar erevltgtfa
       61 eaaafgdvvm aavleagltd vlaaagtalr gkplidvtnv hpdaydptrp iagaaadltg
      121 ahvvkafnlc hvdvwrmtpp vfdgrplavp lcgddpaale pvrrlvtdlg ctpldgggla
      181 ratlleataa fviglwfaga daqailtpke hagv
//
LOCUS       WP_357630427             122 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357630427
VERSION     WP_357630427.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..122
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13430
     Region          4..103
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mfladcqarl afdliantws avvvwalrhg prrpgelraa iggvspkvlt etlrrlesng
       61 lvvrhayaea pprveyeltg lgrsllepie rlgewafdha devmaaqdrw egtgeleerp
      121 ag
//
LOCUS       WP_357630457             406 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357630457
VERSION     WP_357630457.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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 406)
  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 406)
  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..406
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..406
                     /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=43933
     Region          9..383
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mndewicgrl gedepwtlga vnppvfensl ftfatagelg eairnedery vywrgtnptv
       61 dlaqrklaal ergerakcfg sgmgaiaati sslvsagdhv lvlgavygpt tqflrylekf
      121 gvththvsdl aecdsairer trllyfesps ymayaivdia evaawargrg lvtvmdntws
      181 tplfqkpltl gvdlvvhsls kyvgghsdlv ggvvigpsrl irplalteyq lygaamsphd
      241 aakvikglrt lpvrmpahqe rglavarfla ghpgvrevnh pglpshpgha ialrqmsgfs
      301 slfsielatd etdqvaifld klrhfrigvs wggfeslvna paltteesvr atmgipaglv
      361 rlsvglepad tliedldeal kaikgvngmt drssrekdls pqvhpn
//
LOCUS       WP_357630446             249 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Nonomuraea wenchangensis].
ACCESSION   WP_357630446
VERSION     WP_357630446.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=27458
     Region          4..238
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 maqlrvlavd delpaledls yllradprig evatardgaq alrlldraia dgrpidavfl
       61 dirmrgldgv vlgrllsqfa npprvvfvta yeehavdafe ikaedyllkp vrperlseai
      121 rrvavsadvp aesgesdtip velggvtrfv ssadviyvea hgdyarlhta agshlvripl
      181 atleerwapa gflrvhrshl vavkhidelh idsgrctvrv agteipvsrr htrelrdllv
      241 rrarkgrpe
//
LOCUS       WP_357630497             450 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Nonomuraea].
ACCESSION   WP_357630497
VERSION     WP_357630497.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=47292
     Region          31..343
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mgskisraar iaaaaaaigl aaacggggep vgtpagggas gdpakpvtlt fwswvpdiqk
       61 avdqfnashp gvkvnletit pgpdggyakm laavkagnap dvaqvgydsl psflvngalq
      121 dvteyagdda akfvdwqwqt gvfggkvyai pqasgpmgfy yrkdlfdkwg ieapktwddf
      181 aaaaatirkk dkdayistfa anqapwlisl aqqagqqwfg tegdswkvti dnpdtrkmaa
      241 fwqkllddkv lkteadlsna wykdlqtggi vgwiggswgd aiirgnapgt sgkwavapmp
      301 qwpgatafts aswgggsssa ilkgtknpaa atefavwlns dpqsvntlls agygwpsvkd
      361 tskvtnlqkd dtvfpfyggq niwdvfkesd aavttdwrwp pvsdalyatl tdnakaavqg
      421 qgtltdafak tqqamveqlk akglsvvtgg
//
LOCUS       WP_357630500             314 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357630500
VERSION     WP_357630500.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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 314)
  AUTHORS   ter Beek,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..314
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..314
                     /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=34016
     Region          40..310
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mlqrtpagtt gttstsrrrp rrprahvavf vvpffvafal fylapigyav hqsffrltss
       61 glgltepvle faglgnyaaa ltseafvasi grvlvfslve vpvmvvaala lallldsara
      121 rfraffrvsf flpygvpgvi asllwgflyv pqtsplidvl aaaglphdfl spqtillsia
      181 niatwqfagy nmlvliaglq aipqelyeaa rvdgaselri awhvkvplvr aplilitvft
      241 ligtlqlfve plilkpltta insdytpnla aynqafgqan ihlasaeatl iaimafvisf
      301 gflrlvnrkg rraw
//
LOCUS       WP_357630535             226 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357630535
VERSION     WP_357630535.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 226)
  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..226
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..226
                     /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=24525
     Region          6..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msavraervn atraqilaaa erlfaergvy avsnrqvsqv agqgnnaavg yhfgtkadlv
       61 raivrahter vellrrrlla gaegsddvrd wvgclvrsft ghlddlgppt wyarfaaqvm
      121 tdpalrlima eealnsptlr rvvdglrrcl pelppevhae raemagrlvv hmcaerehal
      181 aegrptlrps whdaatglid avvgiwtapv ttgrdntavp aieeda
//
LOCUS       WP_357630545             249 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Nonomuraea].
ACCESSION   WP_357630545
VERSION     WP_357630545.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 249)
  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 249)
  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..249
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..249
                     /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=25452
     Region          7..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 mtaanggrva lvtgasrglg gviarrlaae gwavavnhrs sageagavve riradggaae
       61 afaadvtddt eapalverva grlgpvtalv lnatgpqpav pvedltweah ldqlrffvks
      121 ptllvraalp gmraagggrv iqigsdivdr alpgmsayta akaaqfgltr twarelgphg
      181 itvnlvapgw ipverhahhg pediaayrdd vplgrmgtpe dvaatvafla sdaasfvtge
      241 rvtvngght
//
LOCUS       WP_357630560             279 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate deacetylase [Nonomuraea wenchangensis].
ACCESSION   WP_357630560
VERSION     WP_357630560.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..279
                     /product="carbohydrate deacetylase"
                     /calculated_mol_wt=29918
     Region          3..272
                     /region_name="ChbG"
                     /note="Chitooligosaccharide deacetylase ChbG, YdjC/CelG
                     family [Carbohydrate transport and metabolism]; COG3394"
                     /db_xref="CDD:442621"
ORIGIN      
        1 msrrlvitad dlgreagste vilgllaegh vsattlicls psaahaaerv relgvvprvh
       61 vtltsergvp rwrpltggas ltgpdgtlfd dpfalgarga aedvereaea qlgwmrehgl
      121 apeaadshag tlyglhgrsw laetlrwcar hglafrlprd pepymggplp pelaavhera
      181 valadalgva lpetiatnrs taaelggyer lredylrrla alpegtself lhpsseeava
      241 gpdgvvrswe arllrdpvwh dalksedvev vggwwparp
//
LOCUS       WP_357630580             287 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora sediminicola].
ACCESSION   WP_357630580
VERSION     WP_357630580.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 287)
  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..287
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..287
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32463
     Region          6..286
                     /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 mfddftderi dvgevelrvr hagqgppvll vhghprtgat whrvaprlve rgfavvcpdm
       61 rgygrsgkad lrpdhsqqsk ravaadlrrl mdllghprfa tvghdrgayv alrlaldhpd
      121 avdrlvvidg vpisealarc datfarewfh wfffaqpdip ervitadpda wyaakarpes
      181 mgaenhrefl ravrdpatvr amledyragl gvdreheead rragravrcp tlflwstrdd
      241 merlygdpla iwrpwaddlr ghpiesghhv aeenpddlte alhrflt
//
LOCUS       WP_357630588             360 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea wenchangensis].
ACCESSION   WP_357630588
VERSION     WP_357630588.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,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..360
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..360
                     /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=36175
     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 mktdssepra varadssgrr avprtgssew ravpaarrrv vvlaafvlll laalvasvcv
       61 garaiapadv wralvgadgg eaylivhdvr gprtllgvcv gaalgvagll vqtltrnpla
      121 epgllgvtsg agfainvggl lglaggqagq lalaslgaal tavlvyalgs aeplrlvltg
      181 valsavlsgi slglrltlpd vfdryrfwsi gslagheqap lalpaativl alagavlvtr
      241 plnalvlgde aarslggnvv rtrvavlvlv tllagaatav agpiaflglm vphlarrpag
      301 gsvpwlmayt mvlgpvllla sdvtarvllp tgevpvavvt afagapaliw avrrrgrvaa
//
LOCUS       WP_357630590             436 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Nonomuraea].
ACCESSION   WP_357630590
VERSION     WP_357630590.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 Nonomuraea"
                     /db_xref="taxon:2593643"
     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=46186
     Region          1..354
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrisrlggsi aalgtaavla acssgtpgga gtpaantgpv tlefwcwgsp qkanveafnk
       61 ahpniqvkht dvgggtdtat klltanragn gpdaacmeyd tlpslivaga ladisaytgd
      121 ikdafspevw nltsfdgavy gvpqdvgpmv lvynnkrfqe lkieppatwq dfakvaadvr
      181 kkdpeaylat fapaefgnfa glaqqagasw wkvqdqtwtv giadqaslev adfwqglidk
      241 dlvkaepllt pewnnklnkg kiltwpsalw apgvlygiae kqagdwaiap lpqwkagddr
      301 vafqggsalt vtkaskhpea aatfakwmnt nktaydvqis lgeypaslag qkaasssppp
      361 kltanqkdyw diatkaaqrt iphiswgpnv ntaksayqda lsaaiknhtp lrdaltkthn
      421 lvvqdmkatg fkvagp
//
LOCUS       WP_357630611             333 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA desaturase [unclassified Nonomuraea].
ACCESSION   WP_357630611
VERSION     WP_357630611.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 333)
  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 333)
  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..333
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..333
                     /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=36385
     Region          23..318
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mtiaeqparh rqdydgaspf pgaedhapag rgqvalmtai vvlpfialgi aiflawgrgi
       61 aladlllaag fyavsglgvt vgfhrlithg sftarpwlrv vlgvagsmsf qgnvidwvav
      121 hrrhhaftdr pgdphspyry gtslrgqlrg lahahlgwmf tddttsaery apdlladpam
      181 arvarafpal calslalpfl agwtitgtly ggltaflwag lvriallqhv twsvnslchv
      241 igsrpfrtrr hdrstnlwpl allsfgeswh nghhseptca rhglgrgqid psaglirlfe
      301 rlgwatdvhw pdpgriqrrr aeplrqarap sre
//
LOCUS       WP_357630616             319 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357630616
VERSION     WP_357630616.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (residues 1 to 319)
  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..319
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..319
                     /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=35192
     Region          1..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 melrqlryfv tlteelhfgr aaarehivqs alsqqvqrle relgvrlldr sthhvdltpa
       61 gaaflvearq ildhvsratq aarnavassp tlrvgiidag ydtmpqilre lqrghpeiti
      121 hqveastpeq yrqlsdgrld igigpasatl tvvtsrlirl dplgvlvpeg hrfagmdgvp
      181 vaaladelll lgeeeqtpel nrfvvelcrs tgfaptlyeg tvestraaad lvlqhrcvhc
      241 vpssfrssnr pgtiwrplte pvthyrwsll whdanpsshl aavinsarql aqrlgwlrpa
      301 epgpfadvpq llrqgdeia
//
LOCUS       WP_357630657             463 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            sediminicola].
ACCESSION   WP_357630657
VERSION     WP_357630657.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 463)
  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 463)
  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 463)
  AUTHORS   ter Beek,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..463
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..463
                     /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=48544
     Region          19..345
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msspstrlla sslilalagt gatacsddgq ksdssqitvw sledvadrvn atkaiiadyt
       61 aktgvkvnlv tvnedqfpsl iassaaagdl pdvvgsvsla gvrtlagnel lepdangavv
      121 dalgrdtfsp raleltsddg rqlavpsdgw gqllvyrkdl fdaaglpapd tyekiaaaaa
      181 klntggvagi taatapgdvf tqqtfehlal anncqltdda gkvtldspec veafrfygdl
      241 mrnnsvkgaq dvdttratyf agkaamliws pfildelagl rndarptcpq cqsdpawlak
      301 nsgfvtaikg pngtepaqyg evsswavldg aadpaksfve ymlsdgyprw fgmspegrfp
      361 vrtgtkedkq kfrtawntsp agvdtkkpls evygddvltt lrespetfqr wgltqgqgkl
      421 vgailgelpv pkaladvvgg ksdargaadr adkdveaiak gvn
//
LOCUS       WP_357630679             203 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            sediminicola].
ACCESSION   WP_357630679
VERSION     WP_357630679.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     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=21793
     Region          10..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtgprttlre qrraetqrli qahavrlfaa rgyddttvnd vaeaagvsam tvyrhfptke
       61 dlvladrngp lvaeriaatp agqplvrrig salvesarsl tegddrflla rlrlmiatpa
      121 lrarhldnhy vlqqaivdgl geeaadpdsa fraaaaasac lavmhtalvr waeedgradl
      181 pdliatalaa aftlpdparp dpr
//
LOCUS       WP_357630688             398 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357630688
VERSION     WP_357630688.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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 398)
  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..398
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..398
                     /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=43810
     Region          3..364
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 msrfrlqptp aqeaalaehc aharyvwnla veqhahwkpg rkmapgfaeq crqltearaa
       61 spwlaagsvv vqqqalkdfa qamanffggt hrrptwrkrg qaegfrivav kagdvrrlsr
      121 ntgevkipkv gwvrfrwsra ipdgaksyrv trdragrwhv afatvpqpip apgtgqvvgv
      181 drgvavsaal stgellnvrg lrdtekarlr rllrklarak rgsnrrtkvk taiarlkare
      241 adrrkdwvek tstdlarrfd viavedlkir amtrtargti edpgrnvrqk aglnrgilaa
      301 gwgqlvqrle hkapgrvqki nprhtsqtcn ackyvaresr esqalflrva cghqdnadvn
      361 aakntrdtaa ghavaarggl algglvnrep qpglpsva
//
LOCUS       WP_357630725             172 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DedA family protein [unclassified Nonomuraea].
ACCESSION   WP_357630725
VERSION     WP_357630725.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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..172
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..172
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=19108
     Region          <18..>121
                     /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 msrpalavps ptepfwlglp ywlvgailia alfgafqvyy wvgrrlgerl ydsrigvrvg
       61 reriakveri verwgalavf gcfwvpmlrh tlpwvagalr vsypwyvvas algcltwapm
      121 wwfgltalvw gwlrlaaasp vtavvvavla vagvvaftlr rrrkraakal vs
//
LOCUS       WP_357630794             464 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357630794
VERSION     WP_357630794.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 464)
  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..464
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..464
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=49761
     Region          59..>122
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <272..402
                     /region_name="FxSxx_TPR"
                     /note="FxSxx-COOH system tetratricopeptide repeat protein;
                     NF040586"
                     /db_xref="CDD:468560"
ORIGIN      
        1 mtdvhvqycg cgtrlardna tgrcaacttg trsaaagppe vppqfwnhpg vraaldawhm
       61 grviaayrsh phhgrplrqe tvaawvgitq pqlsriengp pmtdlgrltq warllrippg
      121 llwfqvpqqr pahapavpaa aqaavpgsrg gggdaaavav wrtvdaqigg ahlyatvtsy
      181 lrdhiaprlf ggrddegagv ftaataltem agwmahdagh ddqaerhfar ardlsgvgdd
      241 tqlrvhvlas lahlaahrah addaigyaaq gqrelaagps hpelaarlwa lqarghaatg
      301 rsrethallr raetalqgah gtapspwvsp fdagslagda arclrllgdl paaqhhaqrv
      361 lelrpagrtr srafgcltla gvliergele racavatdvl httgslgsyl vnrqlrelrd
      421 qlhphrassc arsfldhlde alrqrewlyr lttditrprt gltp
//
LOCUS       WP_357630814             440 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase 2 [unclassified
            Nonomuraea].
ACCESSION   WP_357630814
VERSION     WP_357630814.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13389872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..440
                     /product="DNA-3-methyladenine glycosylase 2"
                     /calculated_mol_wt=47628
     Region          3..321
                     /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          235..433
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 msdpdhlhal ltsrdrrfdg rfvvavtttr vycrpscpap mpkpahlrgf pspaaaqqdg
       61 yracrrcrpd aapgspdanv radvagramr lisdglvdre gvaglaarlg ygerqlhrhl
      121 vaelgagpqa lararraqta rdllestdma aadvafaagf asvrqfnetv rrlygttpta
      181 lrgarrsrsa tgaavelrla yrppfdaaal fgylaaralp gveeggpgfh rrslrlpygm
      241 gvatlrdggg hvrcellldd mrdlaaavnr crvlldldad preigetlga dpvlaplvaa
      301 rpglrvpghp dpgelalrlv arsperlver fgrplrepvg tvthafpspe alaeadtevt
      361 llaralasvw vvldpgvdrd eaerrlaavp gvdawtaryv rmraladpdv wpsgemcdrw
      421 rpwrsyalhh lwagrrqava
//
LOCUS       WP_357630841             110 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357630841
VERSION     WP_357630841.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   4  (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
REFERENCE   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..110
                     /product="PadR 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=11984
     Region          3..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrtmqeptfl iltalaagpq hgygvvtdve risegqvrlr agtlyaafdr lqeegliaed
       61 reeivdgrvr ryyrltgdgt arlaaeaerm rrharaatar lralgaggta
//
LOCUS       WP_357630875             431 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            sediminicola].
ACCESSION   WP_357630875
VERSION     WP_357630875.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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 431)
  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..431
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..431
                     /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=46791
     Region          41..389
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mpwsgfdlin afngwkrsga agrvmvaagd gtvtvkvtgl awrgevcqqv feeatvdlgr
       61 glsayaasrg grgrrvgfpr fktkkrapls frlrsktsaa gragvrvgeq aprtvtlpgm
      121 gvlkvrqdtr rlrrmlakgr akivsatvty rggrwavslt ceaadlhear rhqppttapg
      181 wvgvdrglst fvaaaradgt pvlrvdawpr partamahqr rlsrevtrkq rgshnrakaa
      241 arlgrrhart aairrrflhq vcnalvnthd rlaietltig giianrrlaa avadaawgel
      301 arllaykqqw rggqlalvdr wypstktcsa crtvgpampl qqrtftcqvc ryqadrdhna
      361 avnlavwaeq hhaqvrdlpa ggpvtnarrg egsgprprag etgpddagta ptppgarrgr
      421 prralshnst e
//
LOCUS       WP_357630914             248 aa            linear   BCT 28-DEC-2024
DEFINITION  IclR family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357630914
VERSION     WP_357630914.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..248
                     /product="IclR 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=26577
     Region          7..246
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtgdaqpsdl irsvsralrv leevaradrp lpvkviarrc glnlstsyhl vrtlcyegyl
       61 hrrpegdyll gskvaerfhd mldgferpph agsvlrhlae atghtaylaq fadgrllvvd
      121 vaegprspwl edlqagleta phatalgkal lralpardrr eiltgygrlp rftsatpatm
      181 edveeelasl ppgqvvveeh gqfreqvaca gvvvagtawa igistrglel papavallta
      241 aardlagg
//
LOCUS       WP_357630920             235 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea wenchangensis].
ACCESSION   WP_357630920
VERSION     WP_357630920.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 235)
  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 235)
  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 235)
  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 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   5  (residues 1 to 235)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..235
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..235
                     /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=25030
     Region          1..92
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mehiardadi apvaaliadp traailtall dgralaagel arvagvsaat asahlarlld
       61 grlvdvvrqg rhryyrlsgh evaevlevla risarppvrs lrqsrqarll eeartcydhl
      121 agragvglld glrtggfyag adltgegerl ltglgvdvag argsrrrfap ecldwterra
      181 hlggalgaav tyalfergwy rrgtvpravi ltdegregls alfpskelts htpvt
//
LOCUS       WP_357631099             236 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora sediminicola].
ACCESSION   WP_357631099
VERSION     WP_357631099.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..236
                     /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=24909
     Region          3..219
                     /region_name="LivF"
                     /note="ABC-type branched-chain amino acid transport
                     system, ATPase component LivF [Amino acid transport and
                     metabolism]; COG0410"
                     /db_xref="CDD:440179"
ORIGIN      
        1 mslnlerlca gydggtvlhs idlaldqgqv taivghngag kstllhtiag lhpstagrii
       61 ldgrdvtvlr ahrrnrlgia yvpqgarvfa tltvdehltv sfrktrygsa wtpaavrelf
      121 palrdrhrhr aallsggerq mlaiarsllt qprlllldep teglapavvd qladviavlt
      181 srgmtlllat pqlefatava grlavltsgr ltqqfdaaeg vsgasalrsa laplap
//
LOCUS       WP_357631157             389 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357631157
VERSION     WP_357631157.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 389)
  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..389
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..389
                     /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=41138
     Region          18..389
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 matylivgag lagakaaqtl reegfdgdiv lvgaenerpy erpplskdyl qgkserekiy
       61 vhpedwyagn gvelllgtpv triepadhav tlaggarrpy dklllatgat pkrlpgpavy
      121 lrtagdsdal krslaeiggs sgrvvvvgag wigletaaaa rlagcevtvv epeptplhrv
      181 lgpelgevfa glhrrngvdl rlgtgaaeit eegvrlttge llaadlvvag igvapevgla
      241 reaglevgrg vltdaslrts hpdvyaagdv aepfnplygr rlhvehwana lnggpaaara
      301 mlgqevvydr vpyfftdqfd lgmefsgdtt gydeivhsgs vddlefvayw lregrvvagm
      361 nvnvwdvvgg iqdrirsgdv vdpkeltsg
//
LOCUS       WP_357631217             434 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Glu/Leu/Phe/Val family dehydrogenase [unclassified
            Nonomuraea].
ACCESSION   WP_357631217
VERSION     WP_357631217.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..434
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..434
                     /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=45203
     Region          29..432
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mtvmvpsmtp altnpafsad lttpgrqald salqqlhhaa ehlgldhglr tmlatprrsl
       61 tvsvplrred grmdvvqgfr vqhnisrgpa kggirfhpat dihevtalam wmtwkcalvg
      121 ipyggakggv svdpkaltpr elerltrryv neilpmigpe kdipapdvgt deqtmawimd
      181 tysvntgysv pgvvtgkptt lggslgraga tsrgvqiaal aalgrspegv ivavqgfgkv
      241 galaaqylad agcvvvavsd asgavhapgg ldvaalraha aeaggvlgyp hadalghddl
      301 leldvdvlvp aalenvitaa naprirarlv vegangpttp eadeilaagg ttvvpdilan
      361 aggvivsyle wvqnmqaysw sagevdvklr dlmesafgev rslagerglt lrqaahvigv
      421 grvaeahrmr glyp
//
LOCUS       WP_357631248             221 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357631248
VERSION     WP_357631248.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   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 221)
  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..221
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..221
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=23982
     Region          6..217
                     /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 mttyalihgg ggsafdwhlv eaelrdrghd pvavdlptsd pgaglwdyad tvvravagrg
       61 plvvvahswg gfvaplvcar vpaaalvlvt amipapdepp gdwwersgrp psdiddehel
      121 yfhdvprdla rrvldhdgal aahmnmdrac aepwplpawp dvttryllcr ddrlftpdfv
      181 rrhvkerlgl tpdempgghm amlsrpaela aylagilpaa p
//
LOCUS       WP_357631249             445 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357631249
VERSION     WP_357631249.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 445)
  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 445)
  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 445)
  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 445)
  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 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   6  (residues 1 to 445)
  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..445
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..445
                     /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=47337
     Region          127..439
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnsrlvitft tliaflital avplalsyas hrtnrllldr radatrfael adqaardgdh
       61 tgltsevvry aelygaavrv rdrggrvlvt agrfeaddae athlalsgrt tedlptvgpf
      121 gpatvllaep agrdaqlsga vllqartdqa rqdvglvwga lalgslialg ygvlaarrla
      181 rwvlrpvtel drttraiaeg hldarahpgg gptelrrlee rfnamadals gamerqrafv
      241 adashelrtp ltvlglrlen lephltddgs aefeeamael drlavlvedl lalarveaga
      301 vpddkeaelr vrlgvwrevy aaqdltlamd vpemsvvpea aariadiald naqkfvpagg
      361 tvtvtlrdgv lrvaddgpgl seeeradalg rfwrsvghan vpgsglglai aaelaklcga
      421 tlsllpadph glvveirlpe pyang
//
LOCUS       WP_357631318             212 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357631318
VERSION     WP_357631318.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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 212)
  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 212)
  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..212
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..212
                     /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=22348
     Region          2..212
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mrlavfgatg giglelvrqg ldrgheitav vraaarlpag lrervevvea dvmdpaavap
       61 gvegrdavls amgsrergpt tvhsgsvaai teamrragvr rvltvgaagm vadagdglft
      121 ryvlkplvvq plfrhsyadl aaseellrra gldwtvvrpg rlrdapptgr yrtswdrcvr
      181 gghstvradt adcmlslldd pasaghvvyv ts
//
LOCUS       WP_357631321             314 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357631321
VERSION     WP_357631321.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=33096
     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 mradrlvaal lllqgrgrlt aselagelei svatarrdle alsaagipvy pqpgrgggws
       61 lvggartdlt gltaaearal flllgpatpa apaltsalrk lvralpatfr adaeaaarav
      121 vsdpagwgea greppalvrt lqdavvagrk vrltyarkgg epaerlvdpl glvdkdglwy
      181 lvagtgagrr tyrvdrvtaa eptdlpaerp dgfdlaaewe rvvgeverrr slvtavvlva
      241 erhagilrdh fgrhcevlgh epdgrarlrv aapmalsiae qlagwgaqve vvepeavrae
      301 larigaelva ryap
//
LOCUS       WP_357631324             238 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357631324
VERSION     WP_357631324.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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 238)
  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..238
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..238
                     /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=24785
     Region          17..238
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mviivtggsr giggsiverl sadgasvlft hsgsdaeare lerrlgprvr glrhdvrddp
       61 eplfaaaeem gevtglvnna gvtgrlgpfa dltdddlrrv vevnlvaplr lcreaarrwr
      121 grppgekaiv tvssvaartg spgeyvayaa tkaavdtmtv glakelapgv rvnavspgti
      181 dttiharage pgrawrvaer vplgrpgrpe eiaaavawll sdeasyvtga vldvaggl
//
LOCUS       WP_357631329             290 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357631329
VERSION     WP_357631329.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 290)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..290
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29866
     Region          29..284
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mtnhdiqvsv lglgemggal aaalvaaghp vtvwnrspgk adplvargar aaatagdavr
       61 agrlvivcll ddasvrevle pladdlagrt lvnvttttpa qsremaewad rvgvayldgg
      121 imavppmigr pgasvlysgs adafhehrhl ldlwgsstyf gddaglasly dlallagmyv
      181 mfagfahgaa mvapagvtag efaamaapwl tamtgafegf aavidggdyt vpgqqslefs
      241 dltylvaasa dqgvstevva mvqrlvqrqv eaghgkegfa riiesirrpg
//
LOCUS       WP_357631374             293 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Micromonospora sediminicola].
ACCESSION   WP_357631374
VERSION     WP_357631374.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 293)
  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 293)
  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 293)
  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..293
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..293
                     /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=29903
     Region          19..280
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mqspsqgrrl davpgpftpr tprvvaarrl qrrrdreqtg rflaegpqav realalggav
       61 velfgtpaal dryadlaaga aradvpvsev tddalaalae tvapqglvav crhldvpmde
      121 alargprlva vlagirdpgn agtvlrtada agagavvfag eavdpyngkc vrasagslfh
      181 vdvvraadpl aavealraag lsilattgyg dsdlddlada grlaaptawl fgseahglpe
      241 elttaadarv rvplhgraes lnlaaaaavc lyssaralrr ptvtqdgage sat
//
LOCUS       WP_357631384             100 aa            linear   BCT 28-DEC-2024
DEFINITION  Lrp/AsnC family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357631384
VERSION     WP_357631384.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..100
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=10568
     Region          <4..90
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mlyfaveydr eplgqgveam cwltcapyal aeagqavagh gevrfaaavt granlavlvl
       61 crttgdlyty lserlggltg vqsvettlal rrvkaltyap
//
LOCUS       WP_357631388             412 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357631388
VERSION     WP_357631388.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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 412)
  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 412)
  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 412)
  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 412)
  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..412
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..412
                     /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=41894
     Region          106..409
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrwlallva attsvvlial lvpmallira vaengamsra tgaaasvgva agtddlplav
       61 ervelpvtvf lpdgrtlgap aprseavrla atgrsvtaea pggrevlaaa qspqgtvvtr
      121 vfvsedeltr gvreawgala glglalvvlg illadrlala vtrpvdglar vshrlaggdl
      181 earaepggpp evrsvalaln hlagrigdll taeresvadl shrlrtplta lrldaeslrd
      241 peeaarlgar vdalervvsa vitgarrrsa grqtcdaaav vrervrfwsv laedqgreve
      301 vsvpgtalpv avgaqdlaac vdallgnvfa htpegaalsv rlgprpegvv lvvadqgpgf
      361 epallrrgds gggstglgld iarrtaessg gslgvsrgpd ggavvevvlg gg
//
LOCUS       WP_357631433             373 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora sediminicola].
ACCESSION   WP_357631433
VERSION     WP_357631433.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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 373)
  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 373)
  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..373
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..373
                     /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=38670
     Region          12..284
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtgsqpvaaa grtvrvavag lgwagrqiwl prlaahprft vtavvdpdaa ardraradhg
       61 vpdayadvad lpagaadlvv vavpnhlhaa vaarllrrgv pvflekpvcl tsaeaddlad
      121 aersggavll agsaaryrad vralvdaaag lgpvrhvdva wvrargvpda ggwftrrdls
      181 gggalvdlgw hlldtvlpll gpapvahvvg svsddfvndd aaraawrgta gtggrgdved
      241 taraflltad gasaalhacw asheardrtt vsvhgtagsv tlrctfgfsp nrdatpeltr
      301 trdgetvrlp lpaepigaey drqldalpdl ladpasrgva aadarrtida iervyrcarp
      361 tppvhalaga rdr
//
LOCUS       WP_357631440             381 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357631440
VERSION     WP_357631440.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..381
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40380
     Region          32..365
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrqilaaaag lvvlaasacs aptpprsavp satptspatl paptgahrvg ttvlylkdas
       61 rpdpwnldad arelkvtlwy pteqrdgrra aymtpkesql tlrglgvagv pddtlsrtrt
      121 navedaaptg rklplvvlsp gftkpmstlt slaedlasrg yvvagidhty esyattlpgg
      181 rvaeclacds dtdpgfgtgl vagraadvsf vldqlparwd gsdridrsri amvgqsigga
      241 gtlatmvkds rvragidmdg ttyaripkrg lsrpfmflgs pqhvpggrdt swerdwkllt
      301 gwkrwlvlsg aehqsftdgp llsgalgvtp psgvlpaara aeltrsyvaa fldqhlkger
      361 qplldkpsar hpevtfcpet c
//
LOCUS       WP_357631456             311 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357631456
VERSION     WP_357631456.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 311)
  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 311)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..311
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..311
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33218
     Region          7..296
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mpakrakvrf asgdtecaaw hypgtngacv imaggfavpk epatdlfaqr fqeagfsvla
       61 fdyrglgesg grsrlvlpvr sqladwdaai afaatlpevd parlalwafs asgghvirva
      121 arnprlaavi aqtpnvggpa atrsvssfqk pfgmlrftgr giadalgalv grppllvpla
      181 gepgavamlt tpdvgdgpka ldpenrhahw qqrvaarsal rlafyqpgrd tprvrcpllv
      241 ltcdqdqtap pgpaveaarr apraelvrmp grhyapfmem heravdvels flrrhlldht
      301 ptepgtvpar h
//
LOCUS       WP_357631451             295 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Micromonospora sediminicola].
ACCESSION   WP_357631451
VERSION     WP_357631451.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..295
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..295
                     /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=32799
     Region          48..179
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mlenlrtlgr vvrtlatkdp vtrvrrfyei qspdvefaar tsrymnvgyw eegvtsidva
       61 gealanklae aagfkpddtv ldvgfgygdq dfawlrdrrv arvhginvtp rhvehaqera
      121 rregladrad frlgtatalp fpdasvdrvv alesafhfhp rsaffaealr vlrpggtlat
      181 adiiplsndt prmsinsgpl sfvkfslpde nwhdrrtyge qlteagfgnv evhsiadrtw
      241 egwrrfqaar padpafraav dgsavkgman hwrdadlikk elglldyvia vaqkp
//
LOCUS       WP_357631458             139 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea wenchangensis].
ACCESSION   WP_357631458
VERSION     WP_357631458.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 139)
  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 139)
  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..139
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..139
                     /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=15666
     Region          2..132
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 merpigywlk hldrlieaea ervlteerlt rrhwqvlnvl rqspqtasgl aetlrpfwqp
       61 gaitledvtg elarrgwlte daegrhtltp egltghaavr ekmhgirsaf ltglteeeya
      121 atvrtlqrma anlearqas
//
LOCUS       WP_357631473             148 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Nonomuraea].
ACCESSION   WP_357631473
VERSION     WP_357631473.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 148)
  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..148
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..148
                     /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=16343
     Region          <27..145
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mamndllsel tpylgricgp ialdsgqdav qealiavfrn lralrepdal ygwaraiavr
       61 eavriarrdn rigsaepgdl psrqdvehav dirdvlerlt pehravlvlr dvegldeata
      121 arllevpvgt vksrlararl sfrrawqs
//
LOCUS       WP_357631476             311 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357631476
VERSION     WP_357631476.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..311
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=34451
     Region          44..310
                     /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 mrtrtlvvla ttltllvcaa lygaygyrpa rqsgyrpaha ergqfletpl arfhyvkqgt
       61 gspvvllspg aswvygwrrq lpelarehtv yvvdlpgqgf ttlkdrgftw dldgmteaig
      121 afldaagier palgglswsg gwalayaqrh pgqvagllll apsgaatrdt wvyeimkypv
      181 igelwnnwfy adrsssleal krihvhqdqv teedvdafwa pgtlddnles qyllergldw
      241 setiaamprt ttpalvvwgr qdtvnpvgqa refrrlmpga rvheldgcgh alttdctqqv
      301 nrlmadflts m
//
LOCUS       WP_357631495             372 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            sediminicola].
ACCESSION   WP_357631495
VERSION     WP_357631495.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 372)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..372
                     /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=40653
     Region          28..334
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matdtlaapg tasagpprrr rggirgnenl agwlfvapvi vilglflllp ilmalwvslt
       61 dwngqgspft gdvpfvggdn ysrlftedgl arrdfmtair nniyyvglvv pvqtvlalgl
      121 alvvnnrllk gkgffrsafy fpsvtssvai svvflflfan sgavnrllgl lgidgpewfa
      181 dgrgvlhllf gafgmdsppa altsggpfgl twwdwlsgps vamtsiiclv iwttsgtfml
      241 mylaalqnvp valdeastld gasrwqrfry vtlplikptt flvvtlglig swqvfdqvyv
      301 msqgdpaktt ltpaylsyrt afrdfdygsg aaisfvlfli iilltlfqrr lmadrdgprr
      361 grwwrrrvpe gs
//
LOCUS       WP_357631522             317 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357631522
VERSION     WP_357631522.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 317)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..317
                     /product="GlxA 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=33157
     Region          2..316
                     /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 mhtvavlald qvvaadlatp vevfgrvrvd grrayrvlvc avtpqvasda ftivapygle
       61 alreadtivv pgcseragap dpaalealra aaaggvrias icvgaftlaa aglldglsat
      121 thwaaaarla eayplvdvrp dvlyvdngqi ltsagaaagl dlclhlirrd lgsavaaaaa
      181 rlavtplere ggqaqfvaha rppaprgsll epvlswiedn lagevtpaam aaragmsert
      241 fgrrfreqtg ttplqwllra rvrraqllle ttdhgverva aqagfgsata frdrfkrvvg
      301 vtpqsyrasf rtrgpav
//
LOCUS       WP_357631529             281 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357631529
VERSION     WP_357631529.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  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 281)
  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 281)
  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 19109171
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..281
                     /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=30501
     Region          7..147
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18877"
                     /db_xref="CDD:467589"
ORIGIN      
        1 maagdgdgwa ecgrghrhwg lhgasgllav hhdeagepyv lmqkrswwsh hggtwglpgg
       61 aldshedava galreareea alsadalrvk gvylddhggw afetviaesa ellpavpanr
      121 esvelrwvrl peithlrlhp gfaetwqevr qelrpetlvl dvanivgara ehgwwndrlg
      181 aatrlleevs rlapahpvle rwyprivavv egaargvpdv agvqvvaatg sgddtvvevv
      241 rrarpwervl vvtadrglke rvtelgaatq gprwllsqlt g
//
LOCUS       WP_357631566             132 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea wenchangensis].
ACCESSION   WP_357631566
VERSION     WP_357631566.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=14379
     Region          23..107
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mfvvretsnk vawaivkqas hpspeemtlv tvmgalsdpi rvglvrilad grergwgelr
       61 apiakstlsh hlrvlrdagl trtrqegtrc fvelrhhdln trfpgllhav leaahnddvg
      121 ahvtaagdpq pt
//
LOCUS       WP_357631593             447 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: purine-cytosine permease family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357631593
VERSION     WP_357631593.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..447
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..447
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46494
     Region          19..396
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mthavnevpl tldetppktl gvldqgalwa nlgvsllgfs galflldplg gapltvaaal
       61 taavvgsllg tamvglaaip gtrtgrpamv llrglfgarl syvptvlnii qmvgwgafel
      121 wvismgasai fgpavpyavw vvvagvltts lsiwplgsvr llrryvtvav vialawfavd
      181 flgqaqpqag gswqafapav dyvialsvsw vpmaadfarh srssaaaftg vvggytlaqv
      241 aclglgvyav aiagaaavqa dgtavfgtfv aaplgalffa vlvlretdqs fanvysttls
      301 lqnlmprvdr rvfsvsigvv ttavalvvdv nsygaflgii gavfvpmfav lavdyfvlgg
      361 sarwntdeda psrwsmlvpw vlgfaaywlt tstptvgawd gfwaevreei gftrqpwmng
      421 algaalvaal vtlalglarr raladra
//
LOCUS       WP_357631600             292 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Fpg/Nei family DNA glycosylase [unclassified
            Nonomuraea].
ACCESSION   WP_357631600
VERSION     WP_357631600.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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..292
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..292
                     /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=31177
     Region          2..276
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpelpevesl agflreravg rtvlavdvva iqalktfdpp vsalgglsvt gvsrhgkfld
       61 ldcdglhlvi hlaragwlrw rddlsgakpv rpgkgplaar vrfapddegl apgfelteag
      121 tqkrlaiyvt rdpaevpgva slgpdplaes ftvetlkqiv ggnrtqikgl lrdqkviagi
      181 gnaysdevlh aarmspfkia ssltdaqiad lheaivttlr eamerahgla akdlkaekks
      241 glrvhnragq pcdvcgdtir evsfadsslq ycptcqtggk pladrrlsrl lk
//
LOCUS       WP_357631603             201 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TenA family protein [unclassified Nonomuraea].
ACCESSION   WP_357631603
VERSION     WP_357631603.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..201
                     /product="TenA family protein"
                     /calculated_mol_wt=21727
     Region          1..199
                     /region_name="TenA"
                     /note="Aminopyrimidine aminohydrolase TenA (thiamine
                     salvage pathway) [Coenzyme transport and metabolism];
                     COG0819"
                     /db_xref="CDD:440581"
ORIGIN      
        1 msiseklhaa grplldaqla hptvagiarg dlpeavfrsw leqdylflld yvrvfarlaw
       61 qapdghlgdl vdlahatfhd elslhrtmsa gfgadlegav kgpacaayta fllesaatya
      121 dglaalypcm wgystlgril aqdppaepry rawvdtyadp gfaalaaria gmideaapdp
      181 araerlfreg mahelafwdv p
//
LOCUS       WP_357631606             219 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GOLPH3/VPS74 family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357631606
VERSION     WP_357631606.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 219)
  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 219)
  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..219
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..219
                     /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=22686
     Region          5..194
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtvtiaeell llahsedegk qlvsstqldp alggallael avngrielsd ktvtvkdptp
       61 lgdaeldgal ariaaegrer kpvwwvqklm sgkprprllt rlaetgvlte qrgkvlgifp
      121 ttrwpeadgs veadvrerva salggadpda rtavliallh aakidrkafp gaskervkei
      181 aegawaadav aktiaainaa mtvavtsaav aastsaatg
//
LOCUS       WP_357631710             206 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine hydrolase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357631710
VERSION     WP_357631710.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..206
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21445
     Region          12..183
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mtvpplnprt tallvldyqq atlaalpdpa gplsrvaaai adlrahgati ayvrlgftea
       61 dwaaippdna tfsvlgrqrl lhhadpatav hhllapepgd ltvrktrvga lsttdldrrl
      121 rergittlvi agvttsgvvl stvtdaadrd yrlyvlsdgv adpdphvhrt lmtgvlprla
      181 rvidtaglra llpgsgagag slepag
//
LOCUS       WP_357631820             106 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nonomuraea wenchangensis].
ACCESSION   WP_357631820
VERSION     WP_357631820.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=10921
     Region          2..105
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawlylsvai vfeigfalgt natrgftrlw psvftllsaa ggiytlslal rtldvgvgyt
       61 iwtgvgsigt vilgallyke kitlaklssf aaiiggvvll kvaagi
//
LOCUS       WP_357631722              51 aa            linear   BCT 28-DEC-2024
DEFINITION  response regulator transcription factor [Nonomuraea wenchangensis].
ACCESSION   WP_357631722
VERSION     WP_357631722.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..51
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..51
                     /product="response regulator transcription factor"
                     /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=5439
     Region          <1..43
                     /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 marglstaei atdlfispht vrghlkavfg kagissrgel varmfsswrp r
//
LOCUS       WP_357631866             185 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357631866
VERSION     WP_357631866.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 185)
  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 185)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..185
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..185
                     /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=20662
     Region          19..185
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mknpnpatqa rsrrrrttll naavdllaeg gfaavthrav aqrahlplaa ttyyftsrdq
       61 llaeafaqlv eteltttatw itrhgltglp eilttdadrt rqlglwelyv hagrdpvlqq
      121 iarrwtdgct rliaqaldlp dtdprarlly ttlstlwlel vveqrpaeha rtllthalen
      181 llppr
//
LOCUS       WP_357631823             151 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea wenchangensis].
ACCESSION   WP_357631823
VERSION     WP_357631823.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 151)
  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 151)
  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..151
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..151
                     /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=15879
     Region          4..143
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mattsapvsd aaaawqrvll lharvesrla aalqrrhgig lsefralghl aaspagelrm
       61 qeladkvgln qssvtrlvar lnaadfayrd lcpddrrgvy tvitetgrar haeagrtyee
      121 tlaaaleeag qadprlaaal talgvthgtp a
//
LOCUS       WP_357631895             253 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357631895
VERSION     WP_357631895.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26147
     Region          9..252
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mshylqqlfs lhgrralitg gssgighaia ealgragadv vlvarrptel dqaadhlrhh
       61 gvtttcisad lahrddvqrv cdtagdidil vnnagnnirk pmaelttddy eltvavnlta
      121 pyllgqhfgp rmaargwgri inigsqqsis afgdsgayga akaglagltr sqaeawsaag
      181 vcvntiipgf vltpltapaq avpgrveala arhmtgrngi padfagaavf lagnasafvt
      241 gqmlyvdggf svh
//
LOCUS       WP_357631907             250 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357631907
VERSION     WP_357631907.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..250
                     /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=25929
     Region          5..204
                     /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 msvttfavag atgrlgrhvv evlterghrv vpmsratgvd vitgqglaea lagaevivdv
       61 aswhasdqda ateffrtsag nlqeagreag varivmasii gvekatagfl aakkvheerl
      121 lsgpvpvril raaqfhefvg qlldwqqgdv ayipalpsql vacrtvaeel adlataptsp
      181 gtpipeiagp rreilaeaaq llgarrgvkv vgvdgsampd aelaaagafl pgphaklagp
      241 tfrewldtqp
//
LOCUS       WP_357631943             384 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357631943
VERSION     WP_357631943.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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 384)
  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 384)
  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 384)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 384)
  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..384
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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: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=42409
     Region          <105..379
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 msdvsgirpl ppprvatglg glpmgrwfav vgsvvtlafa taivftilli dqiraarprp
       61 eveahlgrly valivlllil lvtgvvlgcv lryvvlkpia qlteqvrqva agdfdhrptv
      121 ehpaelaels ghvdamreri vtawrraeeq aaelrrsnge leqfayvash dlqeplrkia
      181 sftqmldqry gdrlderarq yihyavdgak rmqllindll dfsrvgrvsg ertpvdtgpa
      241 lsaaldnlsa aleetdatvt adplprvlgn rlqltqlfqn lvenavkfrs aepprvriea
      301 vrkddmwefs csdngigieg kyadriflif qrlhprdvyp gtgiglalcr kiveyhggrl
      361 wldgdaegpg atfrwtlpav gdda
//
LOCUS       WP_357631958             325 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357631958
VERSION     WP_357631958.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=35053
     Region          16..315
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mletsarllr llsllqgrpy wpgaelagrl gvsprtlrrd vgklrhlgyp vdavggvggg
       61 yqmgsggalp pllldeeeav avavalgtaa ggavtgiaet svralakldq vlpsrlrhqv
      121 gtlgaamvam paggptvdpa tltaiaaavr drerlrfgyv aregeesvrd aepyrlvsgg
      181 rrwyllgwdt trddwrtyrv drmslrvpng prfvprplpd edvarylaaa tatrphrhqa
      241 vltmyapate vagevpvtlg vvepidertc vlrigsdsld hlavwvaafg fefevreppe
      301 llerlrtltg rlqraawppe rplgg
//
LOCUS       WP_357632030             299 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea wenchangensis].
ACCESSION   WP_357632030
VERSION     WP_357632030.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=33393
     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 maglsgqrrl errwgrlmal pavlgflift agpmvaslaf sltdwqvggt psfvgldnyt
       61 amasdelfwt slgattyytl gavplvlvvs favamllnqr vrglslwrti fylptlvpsi
      121 anvvlwiwif npdfgllnsl lrqaglpsgq wiydeataip slivmstwgf gntmviflag
      181 lqgvprhlye avsidgggaw rrfwhvtlpm mtptifynlv vgvvgtfqvf nqayvmtegg
      241 pnnatlfyvy ylfrkafres emgyasalaw vlfmiimvit fllfrnarrw vhyemagar
//
LOCUS       WP_357632068             414 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357632068
VERSION     WP_357632068.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..414
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..414
                     /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=43865
     Region          9..414
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mvgnwprsvi vvgagivgls tawflqergv qvdvvdrggl aagaswgnag wiapglaipl
       61 nepavvrygl rslldpaapl hvpatldpgl wafltrfaan srwrswtraa ranlplndec
      121 veayevlaan gvsapvvaap itaafrtpge aegllrelrr leaigqrveh tvldgqrlve
      181 qvplageelt tgvridgqry vdpgafvhal gravmqrgat vyavevddvr tdgrkailss
      241 akgtvlsada vvlatgawlp rlarqwgvrv plragrgysf tvpverpvhg pvylpgvrva
      301 ctpyqgglrv agtmefrdpd apqvparlea lvasvrpllr gvrldersdt wvgprpvtad
      361 gralvgatst ptvyvagghg mwgmahgpit grllaeqitt gkqpaalael dplr
//
LOCUS       WP_357632080             303 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357632080
VERSION     WP_357632080.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 303)
  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..303
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..303
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32206
     Region          18..294
                     /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 maaepiphwp grmvgsvhvr stpdgapeqa vfvhglagaa tnwtdlmdel kdvvtghaid
       61 lpgaghspap gdgdysvaah araviglleh tgpahlfgns lggavavrva aerpdlvrtl
      121 tlispalpdl lprygpvrva aaamprlgew vadklrlvpa eqrinasfam vwanvaavhp
      181 vrlrdaveel rrrddlpyag aamigsargi vaeyfaeyfr rgedslwrca arvqaptlii
      241 hgrhdrlvrp amaakaartf qqvrlvllpg aghvammemp svvaaearrl igetrlgnap
      301 ltg
//
LOCUS       WP_357632091             222 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357632091
VERSION     WP_357632091.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 222)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..222
                     /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=23995
     Region          10..126
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mfapeavepa vdllaelage gralelgvgt grlalplarr gvpvhgidls ramverlrak
       61 pggadvavti gdfattkvag tftvaylvfn timnlttqda qvdcfrnvaa hlapggcfvv
      121 evgvpdlrrl ppgqtavpfh vgdgswaydl ydvatqamss nyvdvaggkg rfrsipfryv
      181 wpaeldlmar lagmrlrerw egwtrepfta estrhvsiwe kp
//
LOCUS       WP_357632193             220 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: cell division protein FtsQ/DivIB [unclassified
            Nonomuraea].
ACCESSION   WP_357632193
VERSION     WP_357632193.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..220
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..220
                     /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=23357
     Region          19..220
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mrartallvl ltvgvvgvaa wlvffspvlg vrsveivgnl tvpedrvkek aavpglhpla
       61 tvdldevear vltlpqlata kadrvwpgtl riqvterrpv aslpvggraa lidahgvvie
      121 vrdlapawlp vlkvdrpaag dpatmaalkv vqnlprslsg kvrqvratta egvsleltdg
      181 rtvfwggaer geekarilar vlgrkadlyd vsspdvvtlk
//
LOCUS       WP_357632218             924 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357632218
VERSION     WP_357632218.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 18732943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=99095
     Region          <5..888
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          864..924
                     /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 mngllvgrsv eldrlvrvle sategtagva lvggdagigk trlvgelvar arergfhvlv
       61 gqcaelgdal pylpladalr gaepavresa aahpllgqll pgtesapssg ltqqrlfgsl
      121 lglladvqpv lfviedlhwa drstrdllvf lsrmlqseqv cvmgtyrtdd lhrrhplrsv
      181 laelkrlptv tgvelgplst gdlsdyvatm grvgaqelge ivaradgnpf yaeelfaala
      241 egdtlpdgla sllmsrvevl seasqqvlra aavagrrved ellrevsglp laefeeavre
      301 ivsrgllrvd gfgytfrhal lqeavytdll pgertrlhaa farlltapae lahhylaghd
      361 lagalkasae agrlaerlga paeahshydq alglwdrvdn aaeltgesra elafrsaima
      421 adsgdnhrav vqlralppts evserlayyl wetddpagav aaaeravesa dndadlaral
      481 athartlfws prlkevetla graldtaraa gaadaevgal ltlaiyreyh gdigrahelv
      541 etasalttcd lamdlrarfh harihyeqgr lghaaevadd gikmaldtgl kwstygtdlr
      601 flrflihyva gewdqaeava atfpvrvgtq peatlssfsl fvevgrglpg vesrlswlrp
      661 fwsddlvaym srglaaehal wqgdpagale hvraamaplt pgeagalrls alglaamtel
      721 gdfdraeade llerarftve hgpagqpghl gpeglawglr aeaewqrahg rhdvelwrrv
      781 vaafdfgfvy evarsrwrla eallahgere aaqaewelar etagklratp lenaltefgr
      841 rarfgggsgg gggasggpgg pgsltarele vlrlvaeglt nrevaerlfi aqktvsvhvs
      901 nilaklevat rtqaaasarr agll
//
LOCUS       WP_357632226             257 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [unclassified
            Nonomuraea].
ACCESSION   WP_357632226
VERSION     WP_357632226.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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..257
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..257
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28693
     Region          1..210
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mplvsvvmpv ynsaatlgaa vrsvltqths dvellvtddq ssdgsmdllr efaaqdervl
       61 pqlapergga ararnlamer argdyvafld sddmwlptkl ekqlafaaeg dapltftsyf
      121 kmdadftges tdwvpngrvv rareyvdyra mlrrdyigal tamydrnvlg trlmpemrkr
      181 qdyalwlsim rdgavargla eplavyrahr agslssnkls lvqynwavyr ehehlsvlra
      241 tqalagavwq slrnsri
//
LOCUS       WP_357632296             290 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357632296
VERSION     WP_357632296.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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 290)
  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..290
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..290
                     /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=33266
     Region          8..>262
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 meegvsrmla grkyrlefds gqrafaerlg gicravwntg leqrreyrrr gkwinyaeqc
       61 rqladakkdp ycgwladapa qvipqtlkdl dqacrkhgaw tvrwkskakw rpsfrfptar
      121 hlpverinrk wgrvflpkfg wtrfrmsrrl ggsvksatvs rdgrhwfisf liddgiaere
      181 ehtcpqwagv drgvvtaavt sdgeffdrrh agsdgvssrq lpretkqdrk ddlgyltpge
      241 aerylrlqrr lartktgskr rktvtaamse imrraprsta raaqaaraaa
//
LOCUS       WP_357632238             485 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea wenchangensis].
ACCESSION   WP_357632238
VERSION     WP_357632238.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 485)
  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 485)
  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..485
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..485
                     /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=54128
     Region          1..441
                     /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 mgeqpgiviv gagfagicma vklkeagyhd fvilekagep ggtwrdntyp gcacdvpshm
       61 ysfsfelnpg wsrmfapqee iqrylracad kygvtphirh grtvtaleyd derrswsvtt
      121 gdgqtlrana vvsaigalhi pkypdipgre aftgpafhsa twdhsidltg krvavigtga
      181 savqfvpqia qraahltvfq rtppwlqpkp dfafsprarr llrlpgaara lrygiywale
      241 tralgfavhp rlmkgherma lrhlerqvpd pelrraltpd ytigckrvlv ssdyypaltr
      301 dnvslvtdav teirerslvd atgrehpadv ivhgtgfkvv dsfteqnilg rgglgiqdaw
      361 kdgveayhgi aasgfpnlff llgpntglgh nsvvfmiesq akyvveclrl lsrtrarald
      421 vrqeaqaafn rrlrarldpl vwnaggcrsw yldehgvnrt iwpgftfeyw artrrvkped
      481 yeliy
//
LOCUS       WP_357632338             212 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea wenchangensis].
ACCESSION   WP_357632338
VERSION     WP_357632338.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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 212)
  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 212)
  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..212
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..212
                     /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=23440
     Region          11..188
                     /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 mrnwplfnls ittprlvlri psledldelg draaegihed gfmpflfpwt egepaerarr
       61 taqyhfrawg altaddwale favlyegqvv gtqgvqaknf avtreagtgs wlgrrfqgqg
      121 igtemraavl hlafaglgar yavteafedn hasmavtrkl gyredgfwth arkgepvvsq
      181 rfrlaaqdws etpgieihnl gpclpllgld gs
//
LOCUS       WP_357632341             217 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357632341
VERSION     WP_357632341.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11552340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23698
     Region          7..207
                     /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..14,124..125,153,177..178,181..182)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            148
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mavvtgvlid wggvlttslt dsiakwiead ridgehyrsv mremidhayg egagesavha
       61 lergeldgpa ferdlaarll tldgvppvad gllermfagf erveamhdml rdvraqgvrt
      121 clvsnswsht yqrdgwddif davvisgevg mrkpeprifh halalvglpg aecvfiddie
      181 anitaaralg magihhrdad ttiaelesll rltlrra
//
LOCUS       WP_357632381             268 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357632381
VERSION     WP_357632381.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27490
     Region          15..253
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 maspgevddy vgrlrldgrg vvvlgtgqgi ggavceavaq aggrvlcvdr dgaqaeataa
       61 rcggeamaad vtdraqlgsv fdraeelfgd dlygivdvvg vsmpelladg teesmqrqfd
      121 lvlrhpvllt qvaiprlarr grgsvvfvgs lagvantrrl glygtakaav hhlatacaqe
      181 fgpqgvrtna ivvgrvlqsg gdpnpddeav raveravpqg rcgvpgdias vvlfllsdla
      241 gyvngaripv dggigvvspl pstqranr
//
LOCUS       WP_357632464             337 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357632464
VERSION     WP_357632464.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 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   4  (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
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..337
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..337
                     /product="helix-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=37161
     Region          1..324
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrlvsil lllqtrglmt arelaerlev svrtiyrdve slhaagiply gdagpsggyr
       61 lldgyrtrlt gltadeaesl flaglpgpaa elglgavvta vqlklmaalp velrdragri
      121 qerflldaps wyrdaepvth lpavaaavwd ehalqvryrr wktpqeverr lepyglvvka
      181 grwyvvarse rqvrtyrvsq ilelhplhee rftrppgfdl aahweayrse fearlrrgea
      241 vvklsprgle rladlmtpgv vaaaratagp pdeegwtrvt vpiesvehat gellrlgldv
      301 evlsppelrh avaavaralt rryassadrs aaldgpg
//
LOCUS       WP_357632429             731 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA-transferase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357632429
VERSION     WP_357632429.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 731)
  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..731
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..731
                     /product="CaiB/BaiF CoA-transferase family protein"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77502
     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"
     Region          350..731
                     /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 mttprpahdl rvvdlgagma aallstllad ggavvhrvap pgdevfdeiy pahrgwrsvt
       61 vpaeagdlde lleradvclv ggedhpavat rrdaqalaar hpglvvvhlt gyvdryapea
      121 pavdllvqar tglaaeqysd rpmyfavpfp tygqavlaal gawaalldrv dtgrgqvvta
      181 slqqgaamfm mpfwmraerp ddefhkvtpk dvqhltfrca dgtyvqfvmg vpaavaklyg
      241 ilgidepvdp edrgipriga spdtyfgnrp liapavarmn rddilaaaae vglpaapvle
      301 lgefwddeql aanrllvdra gaigvgnvig lsgtapvpea gphertggap lagitvldfg
      361 syvagpfasr lladlgasvv kvesltgdpn rglqrhflaa hvgkralavd akspagaevl
      421 rrllsgadvv mhnfrpkaae rlgvdptsvr avkpdavtlq slafgpsgpr adapgfdmvi
      481 qaligllrra ggpaapplwi rtpyldyagg algavavlms lyerrtagrv gdrwlsllna
      541 gmfllsdlrr aadgtmrgap pldaarqgvh pgerlyrtgd gwiavaarte eaanamwrvl
      601 lpgeepqpra dwddavaarf deqasrwrse ellaalagag vwaelcrtdg laelldnpas
      661 taahvlvdra ddrygrltgc fgplvnfsrt eipvhdrpga pgfgahtgqi laelgyteae
      721 ieellrdgvv r
//
LOCUS       WP_357632537             339 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: type III polyketide synthase [unclassified
            Nonomuraea].
ACCESSION   WP_357632537
VERSION     WP_357632537.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Shimizu,Y., Ogata,H. and Goto,S.
  TITLE     Type III Polyketide Synthases: Functional Classification and
            Phylogenomics
  JOURNAL   Chembiochem 18 (1), 50-65 (2017)
   PUBMED   27862822
  REMARK    Erratum:[Chembiochem. 2017 Jun 1;18(11):1048-1049. doi:
            10.1002/cbic.201700230. PMID: 28586514]
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Shen,B.
  TITLE     Polyketide biosynthesis beyond the type I, II and III polyketide
            synthase paradigms
  JOURNAL   Curr Opin Chem Biol 7 (2), 285-295 (2003)
   PUBMED   12714063
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Austin,M.B. and Noel,J.P.
  TITLE     The chalcone synthase superfamily of type III polyketide synthases
  JOURNAL   Nat Prod Rep 20 (1), 79-110 (2003)
   PUBMED   12636085
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Moore,B.S. and Hopke,J.N.
  TITLE     Discovery of a new bacterial polyketide biosynthetic pathway
  JOURNAL   Chembiochem 2 (1), 35-38 (2001)
   PUBMED   11828424
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Funa,N., Ohnishi,Y., Fujii,I., Shibuya,M., Ebizuka,Y. and
            Horinouchi,S.
  TITLE     A new pathway for polyketide synthesis in microorganisms
  JOURNAL   Nature 400 (6747), 897-899 (1999)
   PUBMED   10476972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465765
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..339
                     /product="type III polyketide synthase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35700
     Region          1..339
                     /region_name="BH0617"
                     /note="Predicted naringenin-chalcone synthase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3424"
                     /db_xref="CDD:442650"
ORIGIN      
        1 mhisgvhtvl pdhrydqaei teafsrltea drdllehfqs atgvqsrnla laledygkld
       61 sftranetht eialdlaera vlgaltkagl spdkvdhlvf csstglatps ldallvqrag
      121 lrddvkrvpv fglgcaagaa glarlndylr gwpghvallv caelcsltlq rddtsvanll
      181 agalfgdgaa avvatghgag pevvttrskl ypgtghlmgw eigrhgfrvv lddglagfvq
      241 qvlggdvkaf ladngltpdq vgtwichpgg pkvietmvev lgvppsafav treslrehgn
      301 lssvsvldvl qrtrgrpgqs gllmavgpgf saellllhw
//
LOCUS       WP_357632613             237 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PaaI family thioesterase [unclassified Nonomuraea].
ACCESSION   WP_357632613
VERSION     WP_357632613.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 237)
  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 237)
  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..237
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..237
                     /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=24944
     Region          <157..237
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mttaalqtvl tvperfrgpv gvanggwiag tmadafndnr savevtlhap tpletelrle
       61 hvantvtlsd gdrllveaip vaqdldapef vpfkdaarae vgfagwkgha fpecfacglr
      121 epgdglrvfp gpvegkdvva agwrvphtvv dedgvpgsiv gavldcvsgw ahfqpgesal
      181 lgrltlqihr rvypggaysa varatgregr klfgesaiye vdgtlvaaar atwiapr
//
LOCUS       WP_357632620             412 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357632620
VERSION     WP_357632620.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 412)
  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..412
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..412
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45728
     Region          13..81
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mddgtsgssa pvrtigqriq hlrerrgmtr evlaglvgks eswlkavehg rrqqnprlpi
       61 llqlaealrv rdlseltgdq sipvrmftgs ghpalsavre alnavpiqpg gtvqpltslr
      121 arldagwrar haspdhrtal gkvlpdlird vqlaawmyre ehrrtaqall aetygltqmf
      181 layqpapdll wrvadralta aqesedplal scavwflvqa hrdaadfdaa yeinrqgmaa
      241 iephlddpgt dllamwgals felaftaart gdigeawrhw deaarvadrl pddyyqpwts
      301 fsrvimrpha vtiavelhqg gesarqsdha eavpipsrpr rgrhlievar ahllqrdhaa
      361 vlgtlqlahq aapetiryng yarrmtldly etgpanlrlq areladhigl mi
//
LOCUS       WP_357632652             568 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357632652
VERSION     WP_357632652.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 568)
  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 568)
  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
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..568
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=58972
     Region          20..558
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mstywpegmp tsldypeltv gelltaaadl ygdrtavvdg derltftelg eraaafahgv
       61 rdagvrdgdv vllhlpnsvw flvgyygall agatvspanp lqpapalraq lldtgavlav
      121 ghpahvatlr eagagsalrt ivvvppsaca psaeppaggd glaaladfva drptvapesg
      181 vtadgvahia ytggttgvpk gvrvlhrnvv anvtqmtawr aahlvtvtgs gdlrlrpipg
      241 phdagvrpga gvtvlvpplf hahalihlsf lllcgttivl tgrfspelll eaverhraty
      301 vtgspamwha lldspvlhar dvtsvrviss gaapidpatl ralaaafpga mvsegyglte
      361 gtclvaagpl lrgarsrpgs vglpmfdttv evrpvtggat alganeagel wvrgpqvtag
      421 ylnqpeatae qfaggwlrtg dighldeegf vfiadrakdm liykgynvyp reledvlhgh
      481 pgvaraavva rsvprvgqep vafvvprpgv avdpgevmaf vaervlpykr iravhvvdal
      541 ptsaagkilk aelralvawd dppapssr
//
LOCUS       WP_357632634             329 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357632634
VERSION     WP_357632634.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=34013
     Region          10..292
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtsknvsglr iflaggagvl grriipllva aghtvvattr heartgplrd lgatparadv
       61 ldaaalaaav rdsgadvvmh qltdlaggdl aanaalrrdg trnlvdaala agvrrivaqs
      121 icwtyvpgeg paresepldl gapeprrttv agvaamesav aelpewvvlr ygllygpgtw
      181 feprglraae aregrlvaga dvtsfvhvdd aaaaalaald wpvghvnvcd depaagldwa
      241 pafcravgap appvsgapah pvargadnrh arrdlgwtpa ypswragfaa lagdrdipdt
      301 grsrqfpsgr vghsggghde svplrrkar
//
LOCUS       WP_357632656             285 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HpcH/HpaI aldolase/citrate lyase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357632656
VERSION     WP_357632656.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..285
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..285
                     /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=29962
     Region          8..268
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtplveqvrd artllfvpgn rperfakaha sspglvvldl edavpaadka darrqvtgwl
       61 aaghtgavri nppgtpwhde dvravaaygc avmvpkaeda galrdlagrl aclialveta
      121 rgvieapria sapgverlaf gsfdlaaqlg vapddrgala ssrgalvlas aaagiappvd
      181 gvtgdvrdpe plrddvrhar rlgftgklcv hpgqvpvaee alrpadeevr warsvveagg
      241 aggvvvldgr mvdkpvvdra rrilrtsrpr tsqdrvessh ertdr
//
LOCUS       WP_357632715             740 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357632715
VERSION     WP_357632715.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 740)
  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..740
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..740
                     /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=75850
     Region          14..435
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     Region          <290..591
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mkmhplrpgd paklgaydia grltdgprga aflgkesdda plrvikvlps aqeagsddva
       61 rltgvqrvss syvartldag lhdghayvvr ehvegrslae avaadgplda dalervavgv
      121 ltaltavhla githrgltph nvilgpdgpr vtdvdlgepa geigyrapeq irglaygpya
      181 dvfawaatva faatgqppfg qdeeavlnge pelgslaepl rrvvqaalsk dtgqrpttym
      241 allqllgdkr ggvaqklesg pdvvldgipl qgvvipglaa pgapvpgppi agvppqgmpv
      301 egvpmqgvpg pgapvpglpm dgvppqqtwg pppvppqggl apagpepvqg vplppppmwe
      361 ppreqqrqap vqgqtvpsrp prkfplglaa avgalallsg vglwganqya atqkfepvaa
      421 agdqktqgpa aagdasvnan qnglpqpnnq dqtgqnqpev tvpwantpgt dqndvgpmtl
      481 psdwtsqapt ppeystvpsp lpintqriaq ppvttqpaat qtaapqptvt vtmretptpt
      541 ptptnvatmg psetptagpt vtvtatptpt vtetptpsat ptvvpsatpt vtptrsqptv
      601 rpthtttptr trtpssrptv aptsvpttpa pviknpyspg qvcgegfyvq rkqsfstget
      661 fqlynastge ncvvtmktse vgkstpvsvt levqgggsrn qsgnfeyyag pvklngkgkc
      721 vrfsgsvgsa gtsagwancg
//
LOCUS       WP_357632810             946 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NACHT domain-containing protein [unclassified
            Nonomuraea].
ACCESSION   WP_357632810
VERSION     WP_357632810.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 946)
  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 946)
  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..946
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..946
                     /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=103647
     Region          131..946
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mvynleqlgp igfqdlaaal amqtfgagvq vmgagrdggr dlyfkgpliw qsaedqssev
       61 wdgytvfqvk hkdqlaarpq ddtswlwghv rkeldawadp akgrnpvpdh lviitnvplt
      121 pvpgsgghdt lndniqryld aladdsrdig dgaerkakla rlsrlrkwrl wdgnqiqall
      181 hrhpgvrqaf pgfltatdvf anlaeiagsl pldqlepglr aharttlige gtiyfdeags
      241 sdgkglpvhe vaidlpvtag ggaergsvir hvldrgehml rptlttrrgp rhlivagapg
      301 ngkttiskfl vqayraamla gasnlsgehq dvisgmeqal arlgaalphh rrwamrvdla
      361 eyahehgtee dttliryiae rvskrsdlgn vmpsalsawm rrwpwflvld gldevteptv
      421 rkrliervte lvttaegddc dlfvvlttrp mgyteniapt qferidldyl qpdeavrygt
      481 lvttvrlgkd qdrvekiatq lrqaaddegl rnllrtplqv limtiilgga gslapdrfsl
      541 fwtyyeivfr rerdkqtsfn rilqehglqi qqlherigfe lqarsesgdr snavlthqel
      601 enltwqvlde agfkpsgada dlrvkivtaa trrlvliapr sdegygfdvr slqelmaamh
      661 lttgplervt qrlrtaaasp hwrntwifaa grlystpqdh qhqavvelve tidegaearl
      721 gtvvpigprl aldliddgma rswpkwrdrl iacglsvlqg pgpadldfla iarilvraag
      781 sgdtqhhlva egvrdalggt ptaqatavdf ltllsalake pdalpkalal skivprasmn
      841 tpepppdgwa dfeeeiqtsp lsgdsllkvt aaatairqfs qgggsapdae ailtvelrta
      901 leddqaaqvl aaalnhvvah eprlvatlrd evlpavhrap vgellr
//
LOCUS       WP_357632842             400 aa            linear   BCT 28-DEC-2024
DEFINITION  (Fe-S)-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357632842
VERSION     WP_357632842.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..400
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43459
     Region          4..396
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mdpklindcv hcgfclptcp tyvlwgeemd sprgrihlmk qhvegtpvtp emaghfdacl
       61 gcmacvtacp sgvrydrlie ltrveverrh erdpqeravr givfslfpyp rrlrltrpvt
      121 plarrmagyv granpslgam aalaprverr erlprvvrar gerravvgml lgcvqreffp
      181 qvnaatarvl smegcdvvip prqgccgals vhagreeqar rlarrtvrvf eragvstvvv
      241 nsagcgssmk eygellgeep gfevrdlsef laelgpvaer hplpltvayh dachlahaqg
      301 vrsqprella gipglevrei pesaiccgsa gtynifrpea ardlgdrkak avgstgaell
      361 vsanpgctmq iaaamrragg dirvahmaev ldaslrgvsl
//
LOCUS       WP_357632931             856 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357632931
VERSION     WP_357632931.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 856)
  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 856)
  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 856)
  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 856)
  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..856
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..856
                     /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=93473
     Region          1..233
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          101..856
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mefrimgple vrdadgadrt pavpkhrdll amfllnagrp ltaerlrrll wpreggersd
       61 slirgyvgql rkligqdtia tvsgayvlhl gdgrldvdrf rllvgegaye ealglwrgea
      121 ledldpdger wvetrrlree leelrllale rrvqadldag rhrellaelr qltkrhplwq
      181 rfrgqymlal yrsgrrvdal aayavlrdrl dgghaiepdp elqllyhrml hddvslhvsa
      241 gppvllppdv adftgredll gevvgglvvv hgqagagksa lavhaawrar erfgdgilya
      301 dlretttpaa vledflrwlg cpaqaipagl eqrerlfray tasrellvll dnaaseaqvr
      361 pllsacptvv tsrsplgglp garrlsvgvl ddeaalella rssgragddg lrglarfcgg
      421 lpialriags rlaarpewtv gylvrllede herldrlhag dlavrsvfai gfdglpeaar
      481 rtlrglgals apdfadwvte llggqaealv dagllethgv dvagqvryrl hdltrlfare
      541 qpvpevlpkl aevvlervra srfslvsgdp attvatrdir esvewlaaer gflvslvtdl
      601 haagldgpcw rlahllapyl erqrflddwr avtslalvsa rrsgdgeglv lldlgdlhla
      661 erdwaraeer llaalaklag qpresahatr rlgrvhlelg rleeaertll aclaraenqr
      721 daadaeqvlg mvlrragrld eaadrltaav grlaalgdrh rqadtllela aarlaqgrkp
      781 daraaaeqar slavrlgdrl ldahallala qvgraegaag ragelaraal eifdrtgerr
      841 gaanarslla llgtta
//
LOCUS       WP_357632971             270 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea wenchangensis].
ACCESSION   WP_357632971
VERSION     WP_357632971.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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..270
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..270
                     /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=28654
     Region          53..248
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mlslllldps avievsqrni paprvltpdg drlgyapvpr pftgarqltg vlvgrdsvtg
       61 qdimcggtvi gsrsrslvlt aahclyhqgr llgrltflpg ydrgrarhgv wpvvrswvpa
      121 rwrnqpyste llpydvglag vvrrgrplea vtgrgltamp ttrgtalhgl ellgypagkg
      181 yprlrlhrcl gdttegvseg pglmvtrnch aaaggsggpa lyggavagvv ssssplsdtk
      241 gytvltrlgg rpfermlaka dramraerkd
//
LOCUS       WP_357632951             241 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357632951
VERSION     WP_357632951.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=26460
     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 mnrterlyal veelraaapr prtvgwlaer ygvarrtvqr dlqalmetgv pvrmeagrqg
       61 gwfidrdtsl ppinltttea lavaaalaga eqttpfsaag paamrklaaa lsesaaeevr
      121 altdrihvlp artapdvlpv ieqavarqrv vwiryadsae rrserevepg glltasgswy
      181 ligwcrsrra grgfrldril aaelrdepcp aremptldrg laqrvrradt lrslsrerga
      241 g
//
LOCUS       WP_357633014             295 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357633014
VERSION     WP_357633014.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=31233
     Region          3..293
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtrtlvtgsa grlgrsvvat laqaghevig vdvvpgtpre aastlpadlt dlgqaydvla
       61 rfrpdvvvhl aaiatpfsrp egviyrtntq lafnvceaas ntgvgrvvia ssptvigyga
      121 prgwaprylp ideehpaepw nayslsklva eqtmaafard setrfaavrp cfvvapeewa
      181 gaptqsghti aerldrpeia gvslfnyida rdasemlsvl idrmwdipsg evffagaada
      241 lareplaell pavnpataat aaaltgtapa ftsakaerll gwtpkrdwrt eleig
//
LOCUS       WP_357633020             162 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357633020
VERSION     WP_357633020.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 162)
  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 162)
  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..162
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..162
                     /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=17611
     Region          14..155
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtdatptrrg rqlptadelr iwrdfietta algsrlesrl qsdsslstgd yavllalsea
       61 qgqamrssel aahigwersr lshhlgrmer rglirrqeca tvprgaevll ttagaeafkg
      121 atvphlrair elfvdaltpd qivaageiat alrarldalr ae
//
LOCUS       WP_357633025             373 aa            linear   BCT 28-DEC-2024
DEFINITION  dienelactone hydrolase family protein [Nonomuraea sp. NPDC050733].
ACCESSION   WP_357633025
VERSION     WP_357633025.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 373)
  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   2  (residues 1 to 373)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     Protein         1..373
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39596
     Region          70..358
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mperepgqap alrhlgefsg laevaargrg lfpeaapgpa lrraardavg vldlaaddvr
       61 verswtsgdl dgeelswslg ygprtrayll rprgatgplp gvvalhchag mkfagkekva
      121 dgpeppspev arlrgqiydg rayagdlarr gfavlvhdvl gwgsrrfple ampepvaala
      181 agdgpeglse adrydraaaq hehllekyct llgtslagav agedlaaaay lrsrpdvgpv
      241 gcvglsgggl raallgafdp gvravvvaam masyrdlldr hvashtwmly ppglsrvcdw
      301 pslaaarape pllvlygerd elfppagmrr aheiisrayp eggyegvffd aphaftlpmq
      361 ehafgwlsrh laa
//
LOCUS       WP_357633069             325 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357633069
VERSION     WP_357633069.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 325)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..325
                     /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=34477
     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 mgntqpsvrp asagraggaa vtpaaahrsg vrqrrarggp gaeryapyil vapavliivl
       61 lrlyplilgv nfsftgdgaq ngtavgfgny relfadplfr talsnvgllv lllpvavaip
      121 gllatfiylr vpghrfyrsv yffpavlspv ivgaifnlll afdgplnavl gsvgvgpvdw
      181 lgdpdiamfm vvgvhiwatf gmalvvflag fatldaalld aarvdgaslr qvvwhvvips
      241 lartiqfvfv ttmigmltsm fgllfvmtsg gpegstylpe yyiwiqqgqm nrpalasaas
      301 tilfvimlvv glmqikller agked
//
LOCUS       WP_357633093             429 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea wenchangensis].
ACCESSION   WP_357633093
VERSION     WP_357633093.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 429)
  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 429)
  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..429
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..429
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=45972
     Region          <22..222
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          373..418
                     /region_name="VWA_3_C"
                     /note="von Willebrand factor type A C-terminal domain;
                     pfam18571"
                     /db_xref="CDD:408355"
ORIGIN      
        1 msdqptftlt idqnkylpld grevhailtv gatggittqa agpaeaaevi ivdtsgsmsg
       61 skirearqaa vtavqtlrdg ayfaviagtd ratmvyprgn pqlvkatpat kaeahraidk
      121 llahggtaig ewlklaghll tahpsairha llmtdgqnne radvfgavla awsgkfvvdc
      181 lgvgadwapa elrrvaeaml gtfdfvrdqg dlpeyfrrlt qtsmsktvae lslrvwvpqt
      241 arlkfvkqvs pvlldltgkr tdvnpltgdy ptgswgaeer eyhvcvevpp gqigqeirag
      301 wvklvrpdtg dvlasgnvla qwtddlaqst ringkvahyt gqaelhdliq dglsaraagd
      361 vdtatarlak areiavesgr edtarllekv vevdpasgta rlrrdvdkad eieldtgsvr
      421 tsrlrkegs
//
LOCUS       WP_357633179             311 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357633179
VERSION     WP_357633179.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 311)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..311
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..311
                     /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=33330
     Region          17..311
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 maqvtsppdl agaatdstar rysvdaaglg rwragafvap allliavflv fpalwvlylg
       61 ltdyrltgva aadpkfvgld nflsaigdps fwnstwltvq fvlgsavigq vglgfaiawl
      121 lrdrrgplkr iveglvilaw ilpsavvsfl wvalldadgg tlnallatgd yawllehpml
      181 sivifntwrg tafsmmlyga algnvppshl esarlagasg wqqlrdvvfp hikghiltnl
      241 llislwtfnd ftpfmitagg pegksevlav hvykvalqgg qlgygaavst aillinlvva
      301 vfylrllrsk r
//
LOCUS       WP_357633128             366 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357633128
VERSION     WP_357633128.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 366)
  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 366)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 366)
  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..366
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..366
                     /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=38312
     Region          113..366
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mttaavgvlv atmlwsatrs ssagmigvdv alavtalilv pvvirrprtg gvlagvlval
       61 spvatpvasf avlflarnrp frqaaavaav svageavqaf wrpvpslpyg wrlvlmtiay
      121 aalfgwgtwa qarnallael rdrarraere qerrvdeara aergriarem hdvlahrlsl
      181 laaaagamey rpdapperls aaagvirasa hhaldelrev itllrsddae sptdappgqt
      241 ladlpsllhe araagqriev ddplgppvei paavgrtayr iaqealtnar khaagqpvrl
      301 vlggapgtgl riavsnpttp hggatgsagt gliglaeraa ltggrvthhv datgrfhlta
      361 wlpwpt
//
LOCUS       WP_357633180             954 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357633180
VERSION     WP_357633180.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=102743
     Region          1..254
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          126..946
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          720..748
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          753..789
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          800..828
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(801,804..805,808..809,811,841,844..845,848..849,
                     851..852,879,882..883,886..887,890)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          839..869
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          878..906
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdvsilgpiq lcrdgvpvpl gpqlttlfai lllelgkpvp srrlatlltg ddasdaarat
       61 lrshvahlrr alepgergrr gnwliatvgr gaaagyrldl dpacvdavrf eealresrrl
      121 fafgdaehad raaamlrsal dqwhgepyad ladkpfalae varlravhra alllyaeavn
      181 glgrhaeamg dltgavaadp ydeglrcmla ltlyrdgrid eaaevcrdgl allgrrgida
      241 pelhdlqrdi lrrevrqpag gsagrptvpr mlppdlpffv graqelstae arlierdeqr
      301 paillvlgpa gvgktsssvh lahrlaprfs dgqlyanlrg fdataaalap tevlraflea
      361 lgvapeqipt nlnaqvaryq aqlrdrrili mldnahsadq vrpllpgsat cvtvvtsrnr
      421 mssliavdga hpvtlgllde geaaqlvrdr igidragqep eavfeiarlc aglplalsia
      481 aaraaanpqf dlrslagdla sagvldrltd sdssvdvrav fswsyraltp aaarlfrllg
      541 lhpgpdftaa aaaslaglsr raanallvel tgahltgerv pgryvlhdll rayagelced
      601 eperqaarrr lldhylhsav aadkvlmpyr qpvavvapee gvtpedpaev dplawftveh
      661 qtliavvgca ahagldrhaa qlawamatyl grgsywhdvl atqslalsaa vrlddrsaqa
      721 qcrrelshal aglgrleqar dqlhralidl sdvadpigqa ynhlslgwly elqgdqrsat
      781 hhdqvaldlf rrggdrsgqa ralnavgwdy aqvgnyrqai gycrqalslh aelgddagav
      841 ntwdtlgyay hhlgeysiai ecyeqalcln vghrfkeaea lahlgdchha lgdmaaaans
      901 wgrayaimte lrtgdadavr akleltrarv pavghgeger galrtapsir spek
//
LOCUS       WP_357633295             464 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357633295
VERSION     WP_357633295.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..464
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..464
                     /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=51654
     Region          33..407
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mdplkalada erkpywldtp arpeplprlf ghtsadlvvv gggfsglwta lmakerdpgq
       61 dvvllegrri gwaasgrngg fcmatlthgl anglerwpde idrlerlgvd nldeieatlg
      121 rygidcafer tgelnvatep wqleslnehl dviadlgldy vpmdrdqvra eldsptylag
      181 lwdrrgcaml dparlawglr eaclrlgvrv yerspvrsld ddgvtiglrt phgvatgrrv
      241 algtgvfppl lrrlkhfvvp vydyalmtep ltpsqlgalg wgnrqgvgds anrfhyyrlt
      301 ednrilwggy davyyngglv kpeydqrdet fatlarhffa tfpqlagvrf thrwggvidt
      361 csrfsafygq ahggrlayaa gytgmgvgat rfganvmldl lsgerterte lrmvkekpvp
      421 fppepmrsgv iqftrwsiaq adrhegrrnl wlraldrmgl gfds
//
LOCUS       WP_357633228             293 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea wenchangensis].
ACCESSION   WP_357633228
VERSION     WP_357633228.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 293)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..293
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..293
                     /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=31649
     Region          2..290
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msvrtprtla gryartaylf llpailffaa ffylpignvv atslrtgpqa dqwaglgnya
       61 dalgdpavrh sflvtvafav mvvvgsivlg lalalaldqp lrgrvvfrvl llvpyltsva
      121 iigllwrnil dpelgvlnrv laglglpgqq wlntapllti acvtlwqsvg ytmvlflagl
      181 qgipetyhea aridgadawr rfwritlpll apttlfvsvm avisglqafg qayiitnggp
      241 gdatdlsvfh ifnvafrtrd fgyssaqsvl llvvivaftl vqlragrrge vty
//
LOCUS       WP_357633367             193 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357633367
VERSION     WP_357633367.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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 193)
  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 193)
  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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..193
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20952
     Region          4..182
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtpfdavlcd ldgvlrqfdh avqadieary glplmrtafd pafigpavlg vtterewaea
       61 iavalgdder arqavaefie vpfwvddevr allakaqehv pvvlvtnamd tveehldrmg
      121 ltyfadalvs sarvglakpd rriyelaael agaaperclf vddrlenveg arslgmtgvh
      181 frtaadlasa lgw
//
LOCUS       WP_357633383             184 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TlpA family protein disulfide reductase [unclassified
            Nonomuraea].
ACCESSION   WP_357633383
VERSION     WP_357633383.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..184
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19157
     Region          56..170
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mpylvaimvl vgvlclvdll ltlgvvrrlr ehtklidaly evvgaggppg agaslpigea
       61 vgdfdattvd dvrvtrdglp egtvvaflsp dcrgcheqlp eltswaarhd rsrvlavvdg
      121 rsgdpaelvt tlspvaqviv ertspqvaea fkvqafptff qvaaggklla taprvtrlpa
      181 gapa
//
LOCUS       WP_357633429             208 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357633429
VERSION     WP_357633429.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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 208)
  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 208)
  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..208
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..208
                     /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=21581
     Region          4..208
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 matiavigat grtgrvlver alasghdvta iarrpetlgl rharltphaa dvlrpgdlag
       61 alsghdavvs algstgrgpt tvysagtaai vaamgtsrrl vvlssaglet ppgagpvtrl
      121 agrllyrvmr hpyadmrmme rllagtdldw tamrptgltd rpatgrprvs vgatervgtr
      181 tsraelaafi ldrlddpvtf rtavaiss
//
LOCUS       WP_357633601             772 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora parva].
ACCESSION   WP_357633601
VERSION     WP_357633601.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 772)
  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 772)
  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 772)
  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..772
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..772
                     /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=84639
     Region          13..760
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msrhsggsge lplddeigre qeyvsmlyhr ldelreqaah rltaelhhtg gtlqdrsqrd
       61 ssvamyadqv eqfsavengl cfgrldgddd srryigrigi fdttgdydpl lmdwrapaar
      121 pfylataanp qgvrrrrhlr trqrkvtgln devldidsas pgaheeltge asllaalnag
      181 rtgrmrdive tiqaeqdeii raelpgvmvv qggpgtgkta valhraayll ythrrelssr
      241 gvllvgpnat flryisqvlp tlaetgvllr tqgdlfpgvs aqrsepaeta alkgravlae
      301 vlalavrdrq wvpdepleie veretltldp eivraardrv rrtdrphnla ralfdveivh
      361 alaeqvaeri gadplggdnl ldeadraeir relreepeir aaldqlwpvl tpqrlladly
      421 adpdriaaaa pmltaderal lrrerggwtp advplldeaa ellgederaa aarrdrirmm
      481 ereyaegvle iargsrsidv edeaeggeil gvtdlidadr llerqeesdr lttaqraaad
      541 rtwafghviv deaqelspma wrllmrrcps rsmtivgdva qtgalsgtps wadalapyve
      601 qrwrlteltv syrtpaeima vaadvlaeid palrpprsvr esgvppwdra vpdgrlaael
      661 vaevtreaag ltegrlgvlv pagrvgelga avtaalpeaa vgehpelesr vvvltvaqak
      721 glefdsvlvv dpdrmvaesp rgrsdlyval tratqrlgvl rptptptptp tl
//
LOCUS       WP_357633670             196 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea wenchangensis].
ACCESSION   WP_357633670
VERSION     WP_357633670.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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: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=20955
     Region          1..195
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 msndtalflg qflrspavig avapssrrla aavcapvper geptvvelgp gtgpfteeiq
       61 qrlggrghhl avelnapmar llaarfplvd vahadaarlg ellrerglrq advvvsglpw
      121 aafperaqrd llgavtaamg qgaafttfsy ihaiplssar rfrallaerf eevvpgrtvw
      181 rnappafvfh arrpra
//
LOCUS       WP_357633656             318 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357633656
VERSION     WP_357633656.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (residues 1 to 318)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..318
                     /product="GlxA 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=33946
     Region          2..317
                     /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 mhtvavlald hvvaadmatp ievfgrarla dgrrpyrvmv caatpqvagd aftliapygl
       61 qalreadtiv vpgcseqagp pvaevldalr aatvagtrva sicagaftla aaglldglga
      121 tthwaaarrl aemfplvevr pdvlyvdngq iltsagaaag ldlclhmirr dfgsavaads
      181 arlsvtpler eggqaqfiph arppvpqgsl lepllawied nlahevtlte mamrsgmspr
      241 tfsrrfreqt gttplqwllr arvrraqsll ettghsveri aaqagfgsat afrerfkrvv
      301 gvtpqsyrss frtnvrtn
//
LOCUS       WP_357633675             230 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Nonomuraea].
ACCESSION   WP_357633675
VERSION     WP_357633675.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 230)
  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 230)
  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 230)
  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 230)
  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..230
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..230
                     /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=23065
     Region          4..229
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msavlvagse ggigracvea veasgvpafg vdlsggidit rpggaekala qataahgavs
       61 gvvhavgmsg ralgdggvad ctdaawsevh rvnhesvfrl lraaipampr ggsivvigsa
      121 lgtsidddfr tvayasakga liplirtaar eaapqgvrvn lvsaglvatp msrraqssea
      181 iqarlpalmp lgarlcrpee vaqavlwlls pssgrttgav ipvdggwhlr
//
LOCUS       WP_357633708             604 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-dependent nuclease [unclassified Nonomuraea].
ACCESSION   WP_357633708
VERSION     WP_357633708.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 604)
  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 604)
  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 604)
  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 604)
  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..604
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..604
                     /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=67757
     Region          34..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 mndlntpltn dqvimkkvhq dlsgilragk fepfiqyirf phfrnlregt ridfvhpitv
       61 lvgangtnkt ailralqgcp dlynvgqywf stdldpikaa drhrfihgyv arsvgevvev
      121 vksrierand pdyfeparpl iqdgmahmpr fsegdklppe rsktrwkaiq knvvyldfrs
      181 elsaydkyff haafdgrvnt laekkafirr rssqlafsfk tgreshvmhr reriveaake
      241 mtelqrqais ailgrnyesv lilkhtyfgv egatimmkas glqyseafag sgefavamlv
      301 nhvteapers lvlldepevs lhpgaqrklm dflcqqakar fhqvvisths peivrdlpar
      361 aikvfhssdt dgkvelisqe seateaffrl gvpkertkti yvedrlaaai vrrairplge
      421 sfssqleiqa ipggtnsiqq hfipafalsg nmnclilldg dqasknhrts veevsdadle
      481 ifvkemlnga pklslngsgg qsapgekalq lrtilgwcht nldylpgrdp eslllemtge
      541 tgaidkaksf wveltrkalg rsawepvnss evlgeqeral arvdddasel rqirervqkf
      601 aqqa
//
LOCUS       WP_357633732             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            parva].
ACCESSION   WP_357633732
VERSION     WP_357633732.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..416
                     /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=43788
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..379
                     /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(349,351..353,355,366..367,371..372,375,379)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 midelvraea avvscadaaa walserdlia aldathrlqq rlaavqlavv reldgrgval
       61 aqgasstavw lrerlrldvs aarrlvglaa sidvappavr dalasgavsv eqarvvaeta
      121 atvtasagse vadkavgvlv ewarqfdptl lrklgtrild hvapdladaa aaaalaaeaa
      181 ratrdrhvti seqaggrlrl sgtldaeaaa llravidpls apagpddtrc agqrrhdala
      241 dvcrlalrtg elpenggdpa qlvvtidydg larqvgggtl dvglrltpda vrqlacdaai
      301 lpavlggagq vldvgrqrrl vtgplrralv lrdggcafpg cdrpprwcaa hhirhwadgg
      361 ptsldnavll cghhhrhihq adwlvrlggn ghpefvppaw ldpdqiprrn hyhqrt
//
LOCUS       WP_357633759             297 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357633759
VERSION     WP_357633759.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (residues 1 to 297)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..297
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30968
     Region          4..216
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msgvevrnlt krygtltavd dlsftvrpga vtaflgpnga gktttmrmmv ghvaptsggv
       61 tiggrryrdl prpttvvgaa fdgaafhprh sarnhlriya amgghpgrrv eellgllgla
      121 aagdratgty stgmrqrlsl atallgdpgv llldepgngl dpegtawlra flrelagegr
      181 avlvsshalg evqqvaddvv virrgrlvaa galgelagaa hvvrvsspda drlarvlapa
      241 araidldgph dlrvhglepa riadlaaahe lrvhglaadr psleelfldl tgertda
//
LOCUS       WP_357633784             210 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357633784
VERSION     WP_357633784.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 210)
  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 210)
  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 210)
  AUTHORS   Rosinski,J.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..210
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..210
                     /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=22697
     Region          13..91
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          99..189
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(102,117,119,130,133,139,173,175,187)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mtgesvlssg lsmaelgqrv raerrargls ierladlagv srsmvsdier gaktptvlvl
       61 drlatalgts iarlldepah gamrvlrhae qrvlrdpsgw errvlspvlg dvefefmrtt
      121 igpgvdagef aphapgsrey lavergslrl tidgrahtle agdsayypgd rrhafandga
      181 dtcvyylame lgtpghtnhh epsrkgqldd
//
LOCUS       WP_357633832             302 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357633832
VERSION     WP_357633832.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   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 302)
  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..302
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..302
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32689
     Region          6..282
                     /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 mtrqeatqrt vttpdgrhla vetsgapdgp avfllhgtpg srsgprprgi vvyrlgvhlv
       61 cydrpgygds drhegrrvad aaadvaaiad dlgidrfavv grsgggphal acaallpdrv
      121 traavlvgla pagapdldwy agmaesnied ygqadedlae ltlnlkvrae earrdpmtll
      181 dflrpqlpde dirvvddvai rrlltdmyse alrhgpegwi ddvlairrgw gfdlgairae
      241 vrlwhgeqdr fspvehshwl asripraevq vqpgaahfga veilpqtlaw latpdlatsp
      301 hl
//
LOCUS       WP_357633836             465 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357633836
VERSION     WP_357633836.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..465
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..465
                     /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=47149
     Region          17..462
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrvvvigggi vgaaaayylt grgasvtvvd ggyqgeatqa gagivcpwvd hpedddwyrl
       61 nregaraypg lvealgedfg yakvgallva edpaelepvr sllhrryada pemgevvdvp
      121 apaelfppls dtlsallvpg aarvdgrsvr dallnaavar garihagaat ltpdgevrvh
      181 aaagapsgeg rtwtpgggtg qarneetgsw rqaaprgpaa aqgseaardp gtaqsaraah
      241 gaeagrpgsq taqgsqtgpg wqagprpqaa rgpevvrpva agagrvfade gvpveadavi
      301 vaggawtgev crplgaelpv fprrgqilha tlegvdtaww pivlpsdgpy llgfpgsrvv
      361 igatvedvgf aprvtmggle evlraglria pglagatvte trvglrpvya pgraligpln
      421 srvvvatgls aygltagpya grlaaalalg etppidltpy aptcl
//
LOCUS       WP_357633848             264 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357633848
VERSION     WP_357633848.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  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..264
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..264
                     /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=28941
     Region          3..229
                     /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 meellggsvn rvvrvgdtvr rltgpwtpav hallahlaer gftgaprahg vdergreild
       61 hvpgdvpdyp lpawaltddv pagvarllrd fhdatagfpv dpgltwyfpa vspaevvchg
      121 dvapyncvfr dgrpvafidf dtahpgprvw dvayaayrfv pltdprrpdg qpvdaqacrl
      181 rlfadaygld pagrdalvdt ararlahlvr hmreqaaagh pgfashlerg ddriyladde
      241 hlarhrdtfr ralrvhpqga pppr
//
LOCUS       WP_357633868             175 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357633868
VERSION     WP_357633868.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 175)
  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 175)
  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 175)
  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 175)
  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..175
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..175
                     /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=18679
     Region          14..171
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 maheeirppa gpgmeirpmr eadadevlai yqagldtgqa sfeitapswe gftsgklphl
       61 rcvaadtgtg eilgwaaasa vsarpvyagv vehsiyvhpg cqaqgvgrsl ltafvraced
      121 agiwtlqsgv fpenqaslal hqalgfrvvg trerigrhhg awrdvvlier rsrsi
//
LOCUS       WP_357633884             183 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Nonomuraea].
ACCESSION   WP_357633884
VERSION     WP_357633884.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 183)
  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 183)
  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 183)
  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 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   5  (residues 1 to 183)
  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 183)
  AUTHORS   Rosinski,J.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..183
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..183
                     /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=20777
     Region          1..97
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mstepvmhtp aamkalaspl rreilrhlaq hgpatsttla kamgqntgtt syhlrmlsdt
       61 gfvtelrdra kgrerwwdvv kadrrmppre eltdteqdla erlgdsrlae dlrllsafvh
      121 nrdeagdwqq gsrasafmtk aqlkefheey lklvhrfsvd rdnapadarm illrwigfpd
      181 prg
//
LOCUS       WP_357633949             377 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357633949
VERSION     WP_357633949.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=39939
     Region          1..362
                     /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 mktpvtiiga glgglvlarv lhvhgipsti feaeasptar aqggmldihd yngqlaleaa
       61 glmdefravi legrqamrll dkdgdvmfek gddgtggrpe vqrgdlrril leslpagtvr
      121 wgrkvsgvra lgggrhevtf adgstaetsl lvgadgtwsr vrpllsdaip eytgesyvet
      181 ylydaqtrhq saaravgdgs mfasapgnai vahrergdtl hayvsltrsl ewfdaidfsd
      241 qaaaaarvvq efegwapelt alitdadsgp llrplfalpv ghrwdrvpgv tlvgdaahlm
      301 ppngeganla mldgaelgka iaahledvea aldeyeqamf prtgeipqgd elvaslfgdn
      361 ppesllalla eegltts
//
LOCUS       WP_357633977             531 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Micromonospora parva].
ACCESSION   WP_357633977
VERSION     WP_357633977.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..531
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..531
                     /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=55181
     Region          10..530
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msseiparad vvivgaghng lvsavllara gldvlvleaa dviggatrte npfpkvpglr
       61 hstgsyllgl mppellatld vripvlrrdp hyflptpggl gspyllfgtd taatraqlae
      121 ffspadvaad damqaelaal redlapawla epltveetae ryvrpalrav fvdlvrgsva
      181 dylarfefrs ellvsmyavt dglsglnagp ddpgtghnfl vhnmcrlpgs ggtwmiaegg
      241 mgtvsrtfae aaraagatil tgtpvravtl dggaasgvvl adgrevaarv vlgacdpyrl
      301 mellpdgalp arlgermaav rrpgttlkln laltglprfs clpdgtpspf gstihllpgs
      361 aslvggaeas pmtalramwa dvqagrlpae ptiewylhtt vdpslsdaag hhssalfvqs
      421 vpyelagttw daalpgyvdr ligiveryap gtadliadav plpppgieeh fgitgghihh
      481 vdntvsftdr mpyatgidgv yagsagchpa gsvigaaghn aarrilkdls t
//
LOCUS       WP_357634031             316 aa            linear   BCT 28-DEC-2024
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Micromonospora parva].
ACCESSION   WP_357634031
VERSION     WP_357634031.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 316)
  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..316
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..316
                     /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=33006
     Region          34..>247
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mkkllasata glavltvavp apalaerprp dtyvvsrasg vlpegiavtr dgtlyvtslg
       61 tgavyrghvr drelrqflpp gadgrtraag lhvdrrgrif vagwdtgalf vyapdgella
      121 rrtgpgaaln dlaltadavy vtdsatgtlw raaldgptvg nlvrwlapad fpvapgflng
      181 ivvtdggria lvgdqgngqp gterlwrvdl vgrtaravev idgqlgadgl lvegdrlygv
      241 vnfpdgaggw dfavnlaivd adrrtarvvr qsrpaglaqs pttivrdagr llwvnsqlna
      301 stpappftvt qvpglr
//
LOCUS       WP_357634060             283 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: phosphotransferase enzyme family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357634060
VERSION     WP_357634060.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 283)
  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..283
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..283
                     /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=31163
     Region          58..>216
                     /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 mqasevarav aaamstaasl gltvddaivl hdsnkltlrl lpcdvlarva peahqvarfe
       61 vqlaqrlaes gcpvavlepr veprvherdg fvvtlwtyye pvtprevspa gyadalerlh
      121 agmrrldvpa phftdrveqa qrlvasrdrt paladadrel lgdtlrslrr vigerggaeq
      181 llhgephpgn vlattngllf vdletccrgp vefdlahape evsehypgvd qellsvcril
      241 vlamittwrw drgdqfpngr rlgtewlsri raaldregld irg
//
LOCUS       WP_357634071             244 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357634071
VERSION     WP_357634071.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..244
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..244
                     /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=26196
     Region          17..220
                     /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 mtthystcrt gqnrnervsi vgagpggltc arilqrhgip vtvydrdphp earnqggtld
       61 lhaddgqlal reaglidaff rlarpegqem rrldpagrll ghhvpaegel fkpeidrgrl
      121 reafsgwspp mlqmitdndg pyvdrplfal pvahawehtp svtllgdaah lmpplgvgan
      181 lamldacela lalagsatvg eavgvyektm lpraadtarl lengagalle rhdkgeiaea
      241 rwdg
//
LOCUS       WP_357634072             450 aa            linear   BCT 28-DEC-2024
DEFINITION  TrkH family potassium uptake protein [Nonomuraea wenchangensis].
ACCESSION   WP_357634072
VERSION     WP_357634072.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=47503
     Region          15..445
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mmratstlla rfqhpaqvva agfavaiglg alllsmpaat agdvsagwln alftaasavc
       61 vtglvlvdte ahwsvfgevv iaglaqvggl gimtmatvft llvsgrlglr ariaaqtetk
      121 slsmsdvrrl vlkvvafslv ceavaaavlt grfvlgyges fgralylgvf havtafnsag
      181 falwpdslmr fvtdpwiclt iaiaaivggl gfpvvfelar lwrqprkwtv ltritvgtsl
      241 illvsgtlvf latewrnpat lgglddghkl maafvtavmp rsagfnvldv aqmypsswla
      301 tdllmfiggg sagtaggikv ttfgmlafiv wtemrgesrv nigrrrlpet tqrqvvtitv
      361 lgvtlvavst yvllaltpyk ldqvlfevis afgttglstg itadlgtpgh vllavlmfig
      421 rigpltlgsa lalnrrarry elpeervivg
//
LOCUS       WP_357634108             310 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357634108
VERSION     WP_357634108.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 310)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..310
                     /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=33903
     Region          32..303
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mthaadhspv lersrpdtaa preprigfeg rmmspgllll aalsivpfia liamsfahvr
       61 llggvrldli glrnwarfft dadmwmswlr tivyfvltvg lemvlgvava lclfrvlrgr
      121 nvllgllllp mfvapsivgl lgryltdstf glyawvlrsl gytgdilgsp vsafaavvlm
      181 dvwewtplia litlaglssv pqsvreaaav dgapgwmtlr yivfpaianv llvallirsm
      241 dairyfdiiw vttnggpada tkivpvrlye tafrffdlgy aaaiglamla fsifiartfv
      301 rlldvrgltr
//
LOCUS       WP_357634127             312 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357634127
VERSION     WP_357634127.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 312)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..312
                     /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=33760
     Region          14..307
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mdqatasama lpdarrhpap arkrrksqig lafiapfgal falvfvvpil yaaylsffqd
       61 klvggntfvg fanygklfqd pqfwdgvvrv fgftlvqvpv mlvfamalal aldslrlhgt
      121 rflrvtvflp yavpaivatl mwgfllgiky glfgslnkal gtdfdpfapd ttlisigvmv
      181 twaftgfnml ifyaalkavp relyeaaaid ganelqivrg iklpalrgsl vvtvifsiig
      241 tfqmfnepqi lpsmvansgv ttfytpnlya ynlaftgsqq gyaaalalvm aaitiavaya
      301 vqirglrnas dh
//
LOCUS       WP_357634131             347 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LacI family DNA-binding transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357634131
VERSION     WP_357634131.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..347
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36523
     Region          9..345
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mrrrgrsera tladvarlag vspataskvl ngrsdvgakt rdlvlramae tgykptavrh
       61 eppqgrtlvt vldivesrya gtvlqgilma atsaqaelll rlppdepist srtaartwme
      121 qqrasgvvgi ialavavpdp vllaaedlem pvvtidpidt tesrlvsigs tnwaggrsat
      181 ehviklghrr iawiggplgs apslerfhgy qaaldsagit pdrtlihhea fsveagqrhg
      241 hdilalderp taivagndei avgvlaaake lgisvpgels vtgfddtpqt qwttprltsv
      301 rqplvgmgrm avetilgmad gvqpasrhlq lattlsvrds tgpapss
//
LOCUS       WP_357634171             994 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora parva].
ACCESSION   WP_357634171
VERSION     WP_357634171.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13307259
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..994
                     /product="glycoside hydrolase family 3 protein"
                     /calculated_mol_wt=107002
     Region          27..854
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
     Region          873..985
                     /region_name="CBM6_xylanase-like"
                     /note="Carbohydrate Binding Module 6 (CBM6); many are
                     appended to glycoside hydrolase (GH) family 11 and GH43
                     xylanase domains; cd04084"
                     /db_xref="CDD:271150"
     Site            order(890,900..901,960)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:271150"
ORIGIN      
        1 mrnwrlrrgi talalallal pavpgtalae ptypfqdpdl pvsarvddll grltqdekis
       61 wlhqyqpavp rlgiglfktg tealhgvaws tdidnggavv kargtafpqp vgmastwntd
      121 lirqvgsavg deargyhaqn prvwglnlwa pvvnllrdpr wgrneegyse dplltgaist
      181 ayglgmtggd pnhlksaptl khylaynnev rrdvtssnvp prvlneydra afkpaiaada
      241 atgmmaaynl vngrpatvdp dldtvvrgwt dqtlmnvtda wapnnlvnsq kyystqaean
      301 aaiikaglss fitddtnaqp tvtaikqala agllteadid arirdiltir frlgefdpgg
      361 gryggitadv insphhqrla rqaageamvl lknerqalpl dpartrkvav lgplgdtlys
      421 dwyggdlpyq vtaldgirer lggsasvsgl dgadrialkd vrtgkyvsat gttdanpvlg
      481 tgatpalvaq fdvvdwgqdv vtlrnaangr ylgynwgpfv trdeqpngwy vqqqfklepq
      541 pdgtvvlryv gyetkeswfg adtyvtigdd galklgastp aaathfsrel issgihrava
      601 aakaadtavl vvgsnpfing reahdrtsta lsagqealvk avvranprtv lvlqtsypvt
      661 irweqehvpa ivwtthagae tghavadvlf gdrnpsgrlt qtwyrsdsql ppdlleydii
      721 ssrqtylyst akplypfghg lsytrfrygq lragaqsvaa dgtitasvdv tnvgsragte
      781 vvqlythqrt srditpirql kafeqvrlap gqtrtvtlrl patdlahwdv trsrwvvess
      841 vhdlmvgasa ediraraavr vrgetipard lsrptraenf dryagvrlvd etkpsgtavg
      901 atgagqwisf dgsalragaq tfsakvakag agagtiqirl gsptgrllgt atvpstgddy
      961 ryvststela ravgtrdvyl vfdsplrlae fsis
//
LOCUS       WP_357634181             412 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357634181
VERSION     WP_357634181.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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 412)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..412
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..412
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43284
     Region          66..398
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrqhhaeefa rragrprlta avplavaacv mtacvvtaas paapalaapv pvaapaagpv
       61 savrlelprp tgpyavgrdt lhlvdearkd pwvpqdgprq lmvsmyypar sdagpsapym
      121 tvaeaesllr rkapgatipp etvsatrtya htgaaprhgr fplvvlspgl glprasltfl
      181 aeelagrgyv valvdhayes sgttfpdgrt ltcaplcdqp kppeggqati tksrtldvsf
      241 videltgrrp awkkaamiap krigmaghsl ggdasaatma adkrvlagvn ldgtfhpaip
      301 agalggrpfl llgsqndhvp gkddtwdasw phmdgwkrwl tvartdhtaf tdlallqqaa
      361 gmstpgalpp qrslqltray vgaffdlhlk grkqplldgp agadpevafh tp
//
LOCUS       WP_357634206             360 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Nonomuraea
            wenchangensis].
ACCESSION   WP_357634206
VERSION     WP_357634206.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..360
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35717
     Region          36..329
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mtngalavll lggaafaysq lgteeaases avrtvtasrg tvvaavsatg avessrfral
       61 sfgtsgtvek iyvkagdkvs kgqilarldd aaaqenlsaa kasydsalad gtdtaqlyaa
      121 yvkarnsyre aqrtvaatvl kapfggtvta vngsvgqsng gqssggqgts gststsgsts
      181 gsgfveladt aklqlvgtft esdvgklkkg qsatvtfdal pgvsatgkvs qiepvattsn
      241 nvvqypvtvt ftevpdavrl gqtatvevvt graenvvavp staistsggq ttvtvlqqgr
      301 qtrtpvevgv rgttlteirs gvsegdqivp pavstgttqg gngrfgggfp ggggmpgggr
//
LOCUS       WP_357634214             197 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357634214
VERSION     WP_357634214.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  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 197)
  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 197)
  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 197)
  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..197
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..197
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21510
     Region          1..191
                     /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 mtwivfdygg vlslpqpead tlemaramna epeaflrgyw qyrldfdrad ltphaywaav
       61 lgrsvthsev arlvamdvag wahpdrgtva llgelladdr dvallsnapv clgdgldelp
      121 wiaaierrfy sgrmglvkpd reiydevara lgtepaecvf iddraenveg aeragmtgll
      181 ytgsadlrad lravlaa
//
LOCUS       WP_357634223             667 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357634223
VERSION     WP_357634223.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 667)
  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 667)
  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..667
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..667
                     /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=71515
     Region          116..573
                     /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 mdvlaqlfig lfalltiill alaaqrllgv rfgavrtlva alaafllaqp llgplftaln
       61 lpadgqlpda galgvlllat mamvlipmvl lvlaealvpp gsvpgplell rsvrgrvsra
      121 rrysqitria ikhglgpylr grgerledrp gkvrlarslr qaldeggvtf vklgqvlstr
      181 rdllpaefve elgrlqdqvv papwaqiepv lvaelgapvd evfaafdrtp laaasigqvh
      241 aarlpggedv vvkvrrpgig kvvakdldiv rrlaatlesr trwgrslglr dlaegfaaai
      301 reeldfrvea vnmaavtapq ppggaesgae ggaeggprvr ypapmtglct eqvlvmrrls
      361 grpvtdaape dgprlardll dcllrqilvd gvfhadphpg nlmllddgal glldfgsvgr
      421 ldaavrsalq rfllamdrqd plgvtdalle vvprpedide aaleralgqf marhlgpgmd
      481 svqmftdlfr ivtayglsvp pevaavfral atlegtlvrl spgfdligea rafagrhiae
      541 rsepaavret ltqelaallp mlrrlprrve riasaaehgr lafnvrllad erdrryvtgl
      601 lhqvlltvlg atsgvmavml lgndggpqlm pgatlyhlig ynllgisail tlrvlapifr
      661 rrpesee
//
LOCUS       WP_357634257             128 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: response regulator transcription factor [unclassified
            Nonomuraea].
ACCESSION   WP_357634257
VERSION     WP_357634257.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 128)
  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 128)
  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 128)
  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..128
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..128
                     /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=13924
     Region          7..>128
                     /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 mgevlgkvlv vdddevirql iavnlslegf dvstatdgqd clervldvmp dvitldvmmp
       61 yldgwvtaer lradeatshi kvvlitaraq dddkrrgmgi gvdayltkpf dpaeliqvvr
      121 dlaalars
//
LOCUS       WP_357634314             364 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Nonomuraea wenchangensis].
ACCESSION   WP_357634314
VERSION     WP_357634314.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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..364
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..364
                     /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=38784
     Region          8..364
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mypvsrlaav qeatakggld allltpgpdl ryvsgydakp lerltclvvp asgepfmmvp
       61 rlelpaaeas pasrlglefv awdetddpya laaarlgeva kvgladrmwa msslrfrevl
      121 pgaeqvlags vlrelrmrks paevaalrea geaidavhrr vpellragrt erevardiae
      181 ailasghatv dfvivasgpn gasphhdvsd rvirpgepvv vdiggqlhng ycsdstrtys
      241 vgeppaefaa yyevlreaqe aacaavrpgv scesvdaaar eliaaagygd yfvhrtghgi
      301 gietheepyi vagngeplep ghafsvepgi ylperhgari edivvctetg gerlnntpre
      361 lviv
//
LOCUS       WP_357634346             219 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357634346
VERSION     WP_357634346.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   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 219)
  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..219
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..219
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=23959
     Region          6..213
                     /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 matfalihgg ggsardwrlv vpelrrrghe avavdlpved esaglrdyad tvvkavggrs
       61 dlvvvghswg gfvaplvcdr vraellvlvt amipapgerp adwwhntgwr qggwegvdlf
      121 lqdvrpdlaa emmagsrrhs gtadaepwpl drwpdvptrf llcrddrfft pafmrevvra
      181 rlgvtpdelp gghcpmlarp aeladrlvgy lasprrkag
//
LOCUS       WP_357634363             133 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357634363
VERSION     WP_357634363.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Rosinski,J.A. 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 133)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..133
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..133
                     /product="helix-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=14131
     Region          41..>78
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mnsptnpadq ttrtttdntt apsvgrvwti eriralgvtt tlattasvlg isrsqayrla
       61 atnqfpvpli ragsriivpv aallyllqpe pngasggrld adakvsvdam tpppadstrh
      121 rwrhhtkhpg dde
//
LOCUS       WP_357634372             410 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea wenchangensis].
ACCESSION   WP_357634372
VERSION     WP_357634372.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..410
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44107
     Region          2..410
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mteveallre lapqvlgilv rrheqfaace davqeallda avqwpregvp dnprawlvtv
       61 asrrlidlvr seharrrree sagvgepada htvagpgeep agdrddtltl lflcchpals
      121 ppsqlaltlr avgglttaqv agaflvpeat maqrisrakq rikaagarfe pppegeraer
      181 lrvvlhvlyl ifnegytata gpelhrdelt geairlarav hrllpddgev agllalmllt
      241 earrpartgp dgrlvplaeq drglwdrrlv aegvelvska lstaplgpyq vqaaiaavhd
      301 eapsaaetdw pqilalyrvl sglddnpvve lnhavaeamv hgpeagldrl drlaaggrlk
      361 ghhrpaavra hllelagdpa gaagayreaa rltasaperd yleeraarlr
//
LOCUS       WP_357634378             472 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357634378
VERSION     WP_357634378.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 472)
  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   2  (residues 1 to 472)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..472
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=48573
     Region          1..468
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mqviaktaqg pvrgavregv vsflgvpyaa apegplrfrp papppawdgv rdavaygaap
       61 pqlppapgvp piwrpgdgla clnlnvwspd pggaglpvmv wlyggawqig atampqydga
      121 vlarsgvvvv tvdyrvgfeg fghlpgvpdn rglrdqlaal ewvrgniaaf ggdpgnvtvf
      181 gqsagaasva lltaapaaag lfrraiaqsi paglrtrdea grvtealaaa agvpatyegl
      241 aglppeavla ardvtgaggs pfgpvvdgel vtgppwagma gpaargveli cgftheeyrg
      301 lapggppaga dpaaaaasfg ldadavptyg lahpgagdae lftvlmsdal vrmpttwtae
      361 aharaggrtw lydftwkgpa lgaahgvdvp ftfgdgrsrf aarllgsppp agfaelserv
      421 rrawtsfaat gdpgwprfdl dqrrtrlwdl ppadvaypla dfrriwgrpp qr
//
LOCUS       WP_357634409             683 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Nonomuraea].
ACCESSION   WP_357634409
VERSION     WP_357634409.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 683)
  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..683
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..683
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74738
     Region          30..678
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtsaqtssfi grrgevsgar rllargrllt ltgaggvgkt rlalrvaetl rpafddgvei
       61 veltsledpd llvpavatal gvrdagaspm tvladylsgq hlllvldnce hlldacaklv
      121 dgllrgagrl rvlatsrqtl gvageqvlvv pslsvpdpaa apraiarsea vrmfadrvar
      181 vrpgftvdrt daalvarlcr rldgiplaie laagrlhsmp veelerrlde rfevldaegs
      241 gtvpprhrtm haavdwsfgl ctqaeqrlws rlsmfaggld vdtaeevchg rgidredvfd
      301 llaglvdksi lvadhqegrv ryhmldsirs ygreklaesg eedalrrryc dhyrrlvaee
      361 rvdrlvpeql dryrllatel pnirvaldls ysrpeeaagg ldmvsamwgy wilagsvteg
      421 rhwldrgldl vtsgsrarrt alwasamlal lqgdraeaev mleeshrlar eagdeetraf
      481 atqvsamlaf sagdarsgma lmekaraghq drgdlsalai nlfydvsfsa gedperagel
      541 aqefltlcvk rraepsrgya lfavgitawh qghprraeet lreavairrt isdrwglaec
      601 vevlawiaga qgrheraarm lgvanalwqa mgasparlwp hmrdhehcva rarealgtra
      661 ytaafhsger lgldravayv ieg
//
LOCUS       WP_357634422             252 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Micromonospora parva].
ACCESSION   WP_357634422
VERSION     WP_357634422.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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..252
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..252
                     /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=26776
     Region          11..239
                     /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 migvvqtavs ldvrgvryay pdghvalqgv dlvvprgdrv allgpngagk ttlvlhlngi
       61 lsptegsvsv ggltvtpdra tlaevrrrvg ivfqdpddql flptvaedva fgpanlglrg
      121 aeltarvdea laavgmgehr drapqhlsfg qrrrvavatv lamhpeilvl depssnldpa
      181 arrelaeilr glpvtllmvt hdlpyaaelc ersvildggr ivadaptntl lndptllarh
      241 rlelpygftp qp
//
LOCUS       WP_357634440             173 aa            linear   BCT 28-DEC-2024
DEFINITION  flavodoxin family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357634440
VERSION     WP_357634440.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..173
                     /product="flavodoxin family protein"
                     /calculated_mol_wt=17835
     Region          3..164
                     /region_name="FldA"
                     /note="Flavodoxin [Energy production and conversion];
                     COG0716"
                     /db_xref="CDD:440480"
ORIGIN      
        1 myalvvyesm ygntkavaes iaeglasamr aevaevagap gvvgadvsll vvggpthafg
       61 lsrvstrqsa aqqaegvplv srgrgvrewl aalrtssaal daaafdtrva kprmpgsaaq
      121 gvarrlrrag vrlacparsf yvegtlgplv pgeldrarew geslarahtv pvp
//
LOCUS       WP_357634444             329 aa            linear   BCT 28-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Micromonospora
            parva].
ACCESSION   WP_357634444
VERSION     WP_357634444.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 329)
  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 329)
  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 329)
  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..329
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..329
                     /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=34890
     Region          89..245
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 mnavaehtta gssgasepdt nsstvgedyp vrhreyegrh radpgglsvw ataqstgpvq
       61 rrgryvpesv rhparmlpai aahaiaaytq pgdlvldpmc gigttlveav hagrdafgie
      121 yepqwsniad anirhahdqg asgrasvirg datrlmslvp kaltgqvalv vtsppygptv
      181 hglvrpgehg vvkyddrynd gedkgnlayr dltgltdgfa eilrgcatll rpggavvvta
      241 rpwrkrgeli dlpsaviaag lraglapter cvallaavrd gqlvarpsff qlqqvrkart
      301 sgvpmhliah edvliftktr ledgsgvva
//
LOCUS       WP_357634527             451 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357634527
VERSION     WP_357634527.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=48372
     Region          133..450
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msavfrsiwg rslrgrvtli ativaalvll pmgvagvvva rtlvessvfa dtrdtaqrva
       61 yemrsgglpq gsaiplpnps vdliqvisad grtlatsdaa rtlppltdlr ptqqdpeidv
      121 fnclptecvh lsairvnvsp espvvlagrs tpdvlatrtl efivfaevav lvalagwatw
      181 litgralrpv atmraqldav htgdlssrvt eppgedevaq larsingtlt rlersaeqqr
      241 qfasdashel rtpiaglraq lesaqlypdd tdlrslvsss lrdtdrleai itdllllari
      301 gsqvdaaker vdlatlvrqe lgrrsdklpv hadlaagvev dgvrlqlarv ltnlldnaqr
      361 yaethvqvrv trkngtavls vendgqeipe adreriferf trldasrsrd aggtglglai
      421 ardvalahgg qisaedfpgg arfvlklpaa t
//
LOCUS       WP_357634606             377 aa            linear   BCT 28-DEC-2024
DEFINITION  epoxide hydrolase family protein [Micromonospora parva].
ACCESSION   WP_357634606
VERSION     WP_357634606.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 377)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (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   5  (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 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..377
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42086
     Region          1..106
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          72..>196
                     /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 mtpfridisq sdlddlrdrl srtrwprslp gtgwsrgvpv dylreltgyw andydwrahe
       61 arlndfpqll teidgldvhl lhvrspepda lplllthgwp nsvvefteli gpltdprahg
      121 gdptdafhvv vpsvpgygfs qappagftid rlarmwaelm arlgyhrygt qggdlgayva
      181 prvaavapqr vvgvhidggf gfptaadvpd msvaeraewe qmqrwmsggv dhhallraap
      241 qtfsyawnds pvgllawmmq kfkeftmtvp tpeqvidrdh lltnvslywf tgtsgtsswp
      301 myerltvted ggfawptgqr rvpsgvyggg salmrrlaer dntivhwpqg npgshfvamd
      361 eplahaadir tffrelr
//
LOCUS       WP_357634618             452 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357634618
VERSION     WP_357634618.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=48583
     Region          138..452
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 maerspgspl awwrrqglrf rlsaaavavl alalalsasv llsvldralm atvddgtrrq
       61 advvrvaads gtlttpitth dgtivqvlda rnrithvtyg adrlvpllda agraralesg
      121 kavevdgrpy avpgflhviv lradrgqtvl aarsiseirt slgtagrvlm vgtpalvvll
      181 avaswlmigr tlrpiaalrr gaaeithtar srrlpvpasr devhhlattl ndmlarleea
      241 eqrqralvsd aahelrspla sirlqleval ghpegqdwqe taegvledtl rlsrlaedll
      301 alarldergg vparrepvel devvrrvvdr yaearltacd pvvvrgdald lsrvltnlmd
      361 navrhtsskv evaltaggvl tvtddgpgip eqdrervfnr ftrldsgrsr deggtglgla
      421 ivretvrahg gtvvledaap glravvrlpv sr
//
LOCUS       WP_357634616             188 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357634616
VERSION     WP_357634616.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 188)
  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..188
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..188
                     /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=20942
     Region          15..156
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtpptpsdpd aprrrldarr nqerviaaar elfteqglqv tvpqvaerag vgratvyrsy
       61 pskedlivav vqrqfeeleq riraaldgad ayqewcsfvp dlfgrlardr vladaffegr
      121 lvpaarilsl igqlvaaarl sgkirqdage ldirvllcga vrqlivlder dpavwrryad
      181 lvlnalrp
//
LOCUS       WP_357634619             114 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357634619
VERSION     WP_357634619.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=12827
     Region          1..92
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 makhvggdal dgvlhalsdp trrqvverla agpattsela rpfdmalpsf tqhlhvlers
       61 glvtsekrgr vrtyrlapqs lerldtwlaa qrarwtrrld qldsvlydlk eqqr
//
LOCUS       WP_357634651             406 aa            linear   BCT 28-DEC-2024
DEFINITION  YeiH family protein [Micromonospora parva].
ACCESSION   WP_357634651
VERSION     WP_357634651.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..406
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..406
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42036
     Region          59..389
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 mtadatrtgs epgapdatra sdapaedvae pstspttvdp agptsvvrdg afwawtavgl
       61 livvglaalt rfleqnvpaw aegtavedig aaieypvyai llgllgnvav tvlgwrdria
      121 aafrteffik tglvllgasi nlavivsaag paiaqailli sgvflftwwl agrfglddkl
      181 rallasavsi cgvsaaiaaa gavrarreql aytaslvivf alpsifilpw ladvfglsda
      241 vagawiggni dttaavtaag alageealqi asivkvtqna lmgvvavalt ayftlrverr
      301 pgaarpglge lwtrfpkfvl gfiaasviat wyldatgadg katiaivndl rvwflilafv
      361 siglevrvas lreagwrpva vfasatvfnl alalglasll frnfsa
//
LOCUS       WP_357634656            1049 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Nonomuraea].
ACCESSION   WP_357634656
VERSION     WP_357634656.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1049)
  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..1049
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..1049
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=112990
     Region          109..1039
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrivllgpvq vhgddakpve iagarlrmll arlaleagrp vsadsliddl wgaeapagas
       61 aalqglvsrl rralvgtgtv elvaggyrlp vraedvdahr feelagqgrr elaagrlqea
      121 aalsgaaldl wrgtaladvl eapfarnaat rldelrvaal edrcdaevrl grhaevpadl
      181 ravaaahplr ertaelrmra lsaagrqsda lavyeeirgr lgeelgvdps pelqevhlal
      241 lrgeldrpvv ppeaaasrlp aqltsfvgre deldrlaelm aasrlvtivg pggagktrls
      301 leaasrdrac grgrvwfvpl agvgqpdqla davlgalggl ygsgqpqqad padrmverld
      361 vgdavllldn cehlvedvaa ladqllerlp qlrilatsre plaitgeslc hlgpldvpsg
      421 epeleeaaga agvrlfvdra asvrpgfald astvdavvei crrldgmpla lelaaaklrs
      481 mgvqqiarrl ddrfrlltsg srtalprqrt llalvewswd lldepervla rrlsafpgga
      541 sltaleavcp deslpaedvl yvvgslveks ivqqagdryh mletirayaa srlaasgddv
      601 ttrfadhfla laeehepllr trdqlraiav fdaeydnmaf glrtaleagd apraaefvrs
      661 lfwywglrgm ttqystsvae vlrlgdalpa qvraafsvvq saagpvvaae nvadtdatat
      721 mafhpalpml rmaqlasvag sselvelqlk ealsspdpwv rasvlwtqdh irveegdltt
      781 gtrirqealr gfeeagdrwg lvmtllrisr dhslraehde svaaaqrava isseldtelh
      841 lywtrtrlar ermnsgdldg alrdihaalr qakerghrri eanmlsslat ayrlskdver
      901 adgaldrmee lakrlpsfeg lpsdavagfr mcnrlaegaa gparellpgl irvmfahgha
      961 nglswaaell gwllaleddp agaatalgms avirgwfdeg dpelrvvvag lverlgeday
     1021 rsayrrgaem prrealdrlv alggrpvsp
//
LOCUS       WP_357634771             428 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357634771
VERSION     WP_357634771.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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 428)
  AUTHORS   ter Beek,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..428
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..428
                     /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=45454
     Region          34..342
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mdgpltrrgl lrgsvlfvag aavaacggdp laktkstpaa ggapkitlnh wyheygeegt
       61 qqaamryaad ftkanpdiav kvswipgdya tkwtaavlta dgpdvyevnd vspnmvkagq
      121 vtpldevlga eksdfdpkvl apytwggkvy avpmiidpml lfyrkslfqk agvavpgsfp
      181 elvaaakklt agkqkglfag ndgvgalntm vpwsngnlli ddrkityddp kvvealiglk
      241 elydakttlq gystdwwdpg alingaaamq wvglwavpgm tealgddfda falpafgpgg
      301 rpvvnmggwv qvvngksrnl daakryvrwl wventaaqtd wslaygfhvp prvsaaakad
      361 kltsgpaktv mdavaahgvk qpalwtaevr qpytdavtai vkkgadpakt laeaakrsqd
      421 ildkvpvl
//
LOCUS       WP_357634802             257 aa            linear   BCT 28-DEC-2024
DEFINITION  cupin domain-containing protein [Micromonospora parva].
ACCESSION   WP_357634802
VERSION     WP_357634802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..257
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26250
     Region          9..124
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 msdrfavrrp ddppargatr adraaplpgg igvsrlrvyd tvapdglvgg tphvhlccte
       61 gyvvtdgega vqtlttagfr etplrpgvvv wfepgtvhrl vngdglsivv lmqnsglpea
      121 gdavltfppe vladpaayaa aaalpdggap gadvhaayrr rdlavagfqa lrsggpaala
      181 afhaaavalr qpllgrwrqr wedgagraaa gtaaqldale rgdaghlgda gvyavaepve
      241 rgrlgmcgll dtypaag
//
LOCUS       WP_357634776             192 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357634776
VERSION     WP_357634776.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 192)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (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   5  (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 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..192
                     /product="PadR 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=21513
     Region          3..90
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          94..177
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mtstlgfail avlargertg ydiaaamrrp vsyfwtaghs qihaelqklt agglvafetr
       61 hgpgpqdkkv yrltpeggda lrawiteppr grperdelvl ktyaswladp elvrrlfaeq
      121 lraheerlae yereeelfgg ppdpgdprfg nyaalrcglg yerhraewcr wmvgqlsasl
      181 kpsweavkps ep
//
LOCUS       WP_357634844             359 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Leu/Phe/Val dehydrogenase [unclassified Nonomuraea].
ACCESSION   WP_357634844
VERSION     WP_357634844.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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..359
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..359
                     /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=38060
     Region          13..130
                     /region_name="ELFV_dehydrog_N"
                     /note="Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
                     pfam02812"
                     /db_xref="CDD:460706"
     Region          147..348
                     /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(181,183..185,204..205,209,240..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 mtdvfdpshk daheqvvfca dprsglraii avhstalgpg lggtrfypye seqaaladvl
       61 nlsrgmsykn alagldhggg kaviigdpsr dkseallray grfveslggr yvtacdvgty
      121 sedmdvvsre srfvtgrtla qggagdssil tafgvfqgmr asaervygap tlrgrrvgve
      181 gvgkvghrlv ellredgadv vvcdvderav ervrlrhpev dvvadaealt gsdidvfapc
      241 alggalddat vtrlragivc gaannqlahp gvekqlaerg ilyapdyvvn sggviqvade
      301 lrgfdmerar akaariydtt lkifaiagde gvppavaadr laerrmsevg riraiwlgh
//
LOCUS       WP_357634875             203 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Nonomuraea].
ACCESSION   WP_357634875
VERSION     WP_357634875.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=21749
     Region          40..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 mmgeiyadal dgapveiehv dgaravleaa rwlepmdgde amlrrcagpt ldigsgpgrl
       61 tvalkrrgva algiditpha vrltrraggf allrsvfdel pgsgrwetal ladgnigigg
      121 hpnvllrrvr elvrpggevi veverpgvas rvervrlrrg stvgewfgwa vvsaddiarv
      181 ahssgfalad cweevgrwfa glr
//
LOCUS       WP_357634867             327 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Micromonospora parva].
ACCESSION   WP_357634867
VERSION     WP_357634867.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..327
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..327
                     /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=35049
     Region          1..326
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mrafryhrpa dvaeavavla aepqaaylgg gtnlvdlmkl gvqrpdvlvd vtrlpldtve
       61 elpdgglrig atvrnsdlaa hpvvrrdypv larallaaas gqlrnmattg gnllqrtrcv
      121 yfqdtgkacn krepgsgcaa lhgqnrdlav ldwseqcvat hpsdlavala aldtvvevhe
      181 sdgardipia dlyrspgthp erettlarga litavrvppl paarrstylk vrdrasfafa
      241 agsvaavldl dgdvvrdvrl aygavahrpw rayraeeelr grpfspelaa raadaelaea
      301 rplrhngfkl pltraitvra ltelass
//
LOCUS       WP_357634890             541 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357634890
VERSION     WP_357634890.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..541
                     /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=54698
     Region          2..540
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 msaltgttrl arlvlrrdri rlaiwilgtp llgyalagsv agiypdqdar lgyattsass
       61 lvarafngpi hgtdlgavvv aetyvtlali vallstfavt rhtrqneetg raellganvv
      121 gryapltaal lvivaanala aallavalvg aglplagsva aaaaiggvgv aftaiaavta
      181 qlsvtargan alaaatvgls fvlraagdvl geqsadgtrv rsawpswisp lgwgnqvraf
      241 dgerwwvlal pvalllagva layalaerrd qgagliaprr gpatgaplll sptglawrtq
      301 rgtllgwavg vaalglpmgv aadefndmid anpaaaeain amgggddlik ayltamlglf
      361 altigayvvq allrvrgdea dgvleaalat avsrtrwlgt qvlaatlgav allllagvtt
      421 glgygivigd plgqavelgg aallrlpall vvagvvtalf gllprwsvvl swmallvfll
      481 lgqlgavlel pqaalnvspy thvpavpavh paalplvvla avavallavg vaafrhrdvp
      541 s
//
LOCUS       WP_357635042             318 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Nonomuraea].
ACCESSION   WP_357635042
VERSION     WP_357635042.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=33936
     Region          19..304
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 maargeaare alaalraevs kavvgqdavv tglviallcr ghvllegvpg vaktlmvrtl
       61 aaaldlefkr vqftpdlmpg dvtgslvyda rtaefefreg pvftnlllad einrtppktq
      121 aalleameer qvsvegdarr lpdpfvvcat qnpveyegty qlpeaqldrf lvkltvplpp
      181 reqeiavler hahgfdprdl shvrpvataa dlaagraava gvhvapevlg yivdvsratr
      241 nspslqlgvs prgatallaa srawawlsgr ayvtpddvka larpalrhrv qlrpeaeleg
      301 atadglldgi lasvpvpr
//
LOCUS       WP_357635208             206 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357635208
VERSION     WP_357635208.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..206
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..206
                     /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=21285
     Region          84..196
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 malialivyl vwallafglr swvqwrrtgd agfrgaglar gslqwwaril faaalaagva
       61 gpiaglagap plpgtdrplv qaagtvlala gvaatlaaqt smgaswrigv aesettalvt
      121 tgafalarnp iftamvataa gltamvpnai slaalllavv sievqvrave epyllrvhgp
      181 ayrqyaarvg rflpgigrlp ydartw
//
LOCUS       WP_357635211             396 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357635211
VERSION     WP_357635211.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..396
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=41398
     Region          2..335
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkhrivvlga gyagayvagn larrlspkdt eitvvnavpd fvqrmrlhql aagrdieapk
       61 ladvfagtai rlrlarvtav dperqvvalt sgggelgydt lvyalgshga dhgvpgaaeh
      121 afdiaarpsa lrlrerldsl dglggrvlvv gdgltgieaa teiaesrpgl svaliargel
      181 garlsagars hlrracdrlg vtvlehtsvd aveatrvlcs dgtalasdat vwtagfavsp
      241 iaaagglevt eysrivvdrt mrsvshpdvy aigdsahaig dngrplpmsc asagytgrqa
      301 ieaivgrltg rtiantklvy tynhislgrr dailqgvdde grakptymsg rktarikasi
      361 lsmslwatsh ptygmptrkh rvaaahassp vgsrpa
//
LOCUS       WP_357635219             273 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family oxidoreductase [unclassified Nonomuraea].
ACCESSION   WP_357635219
VERSION     WP_357635219.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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..273
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..273
                     /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=28346
     Region          2..272
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mrilivggsg flgselarrs vaeghevaat clshpgkveg vewsaldvrd reavaglvga
       61 fgpdvvvnaa frqadwtata dgaahvalgv saaggrlvhv ssdavfsgra vtyaeecvpd
      121 pvspygaaka aaevavrais paavivrtsl ilgdgrsghe sfvrdlatgr rqgtlftddv
      181 rcpvhvgdla aallelaasd rqgvhhvags davsryelgc lvarrdgldp srlargrrad
      241 tdlagpldvr ldctmtrrvl gtrlrgaref lqp
//
LOCUS       WP_357635223             354 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357635223
VERSION     WP_357635223.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..354
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..354
                     /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=37410
     Region          1..354
                     /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 mkvivagagl gglclagalr ragievavhe rdpalstrrq gyrlhlgetg iqaltavlpp
       61 grweeflata hvpeprfvrl dpalnvldvv ehhgrhlavd retlrrtlla evedavtfgr
      121 rltafdarpd gvtalfadgs tatgdvlvga dgvnsavrrq clpharvvtt glvqlygkip
      181 hgladdmgnv ftaisgpghr vvgvaptrdy ttcsfsarae dlppgldelg qerlramvmd
      241 mtpgwhprvh dmiahwtevf plelrtsvpv pawptsrvtl lgdavhamsp aagagagial
      301 rdatvlasal arggdpleal rayegemvey gfaavrasaa ngarflgqdp lpaa
//
LOCUS       WP_357635275             514 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PP2C family protein-serine/threonine phosphatase
            [unclassified Nonomuraea].
ACCESSION   WP_357635275
VERSION     WP_357635275.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 514)
  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 514)
  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 514)
  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..514
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..514
                     /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=54717
     Region          116..514
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtaspqavla atfapgetav paamrftrev mtawavggal lntaeqvtgd laeqvvdepf
       61 evvwkhfgda vqvelkqrna pqgdpkapaa vvaewgitfs rdghvhwarl tlpgstetvv
      121 sdrpsessrg phwlgflada sdllagtlnp dmvpaivaqv vvprlsswca vytadnatgp
      181 mrlvyvwhad earidglrqe ldgvdvdsag tqpsilhvgd sqvltvplta rgrslgvmcl
      241 grsdrfpdev iqlaedigrr aalamdnarl yaqqaaanra lqrsllppne pevpgldygv
      301 iyeaagevne vggdfydlfk agddswrfai gdvcgtgpea aavtglarht lrllaregyg
      361 vaavlgrlnq aileegerar fltllhgdit pvetgleirm vsaghpealr lkangevesv
      421 ttpqsllgvf pevvfeadtm hldhgdvlla vtdgvterrc gdrlldddgg lakllaecag
      481 lsaravaeri rrgvadfave psaddlaivv lrar
//
LOCUS       WP_357635333             347 aa            linear   BCT 28-DEC-2024
DEFINITION  LacI family DNA-binding transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357635333
VERSION     WP_357635333.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..347
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36217
     Region          9..345
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mrsrgrserv tladvarmag vslataskvl ngrsdvgprt relvleamae igymptaarh
       61 eqtrgrtlvt vldivesrya gtvlqgilva atsaqaelll rlpsdgaaat sptaarawme
      121 rekasgvvgi ialavavpds lllaaeelmv pvvtidpidt sesrlvsigs tnwaggrsat
      181 ehvitlghrr igwiggplgs apslerfhgy qaalssagia pdgalirhea fsveaghrhg
      241 rdllalderp taivagndei avgvlaaakd fgisvpgels vtgfddtpqt ewttprltsv
      301 rqplvgmgrm avetvlgmad gvqpasrhlq lattlsvrds tgpvprs
//
LOCUS       WP_357635578             387 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357635578
VERSION     WP_357635578.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..387
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41048
     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 mhrqqlpldg vkvvdltnvl agpycsyqlm lfgaevvkve lpgtgdlarr lgpdpdlnre
       61 rmgasflaqn agkksveldl kspagraafe tmlaeadvll enfragvlar lgygwerlre
      121 lnpglvycai sgfgqsgpms gapaydqiiq glsgmmsvtg tpdtaplrvg fpicdtvggl
      181 maglaicaal agrqrsgrgc fldlsmleas isamgwtvsn ylvsgvepep mgdqnataap
      241 sgtfetadgp lniaanqqaq fetlcrlvgr pdlaadprfa erearkkhrq alnrelnkal
      301 rartalewee llsragvpaa riltvpqala ldqvrhrgfl tetplpgsgg rpvtvtgngv
      361 vidgvalrpr gpapllgqhn sefeavr
//
LOCUS       WP_357635485             120 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357635485
VERSION     WP_357635485.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=13763
     Region          1..83
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdevavaiad pvrrrilsml rdeplsagvi aarftisrpa isrhirllre sglvrdelvg
       61 rqriyrldpg plaplldwlt glatvdrwer hldaletevy rtrrerrsrg paehrrehta
//
LOCUS       WP_357635507             267 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357635507
VERSION     WP_357635507.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=28711
     Region          7..252
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 maevdyrgqw tlltgassgi gaafahrlaa rgsnlilvar rrdrlealas airqehdvri
       61 epvvadlsvp dggravaaev mdrglpvtsl innagaityg plheadldrl treialgvsa
      121 vvelthaflp tlrdarrgvl vnvasmaayg adpylavyaa akafvlslte svwyesrgtg
      181 lrvlavspgp trtefidavs naehlykglp latpdqvare tltaldrrna ppslpigran
      241 rafvrlntvi srraftnfvg rktrprr
//
LOCUS       WP_357635591             159 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RrF2 family transcriptional regulator [unclassified
            Nonomuraea].
ACCESSION   WP_357635591
VERSION     WP_357635591.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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..159
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..159
                     /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=16547
     Region          2..133
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrltaftdis lrivmrlava rhdelmttra vadqlavpyt haakavarls elglvearrg
       61 rggglqlteq grrasvggia rslegagdiv gceddppcpl raacrlrtal rgaqeafyas
      121 ldavtvaelv apptgpalls lsaprdgvpp arrtstpal
//
LOCUS       WP_357635599             578 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: S8 family peptidase [unclassified Nonomuraea].
ACCESSION   WP_357635599
VERSION     WP_357635599.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 578)
  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 578)
  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..578
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..578
                     /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=58850
     Region          75..>537
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrrlvsslaa vtaaaaltac gpastpaaap masylvfyag grqddaraav sraggdavgg
       61 darlgyllae gggdafvdal gddpavvgvs tdraigyass tgaswrgfps grttaatpas
      121 aaaanaassa ntasspagds rgafpdgpsi atgeaagepl asrqwdmrmi gadkahaatn
      181 gsrkvlvgii dtgvdgthpd iapnfdrals rnfvtdrpkd gngdtldgpc evsgckdpvd
      241 rdddghgthv astigspvng igiagvapgv rlvsiragqd sgyfflkasl daltyagdig
      301 vdvvnmsyyv dpwlfncahn kadskkeqle qravitgmqr aldyarkkgv tlvsalgnga
      361 tdlgrpkvdr nspgyprgde kvrkvdnscl nvpaeskgvi sisavgpsgr ksiysdygie
      421 qadlsapggd tldgkgtsat rgilaaapes alraagkldg sgkpksaeii rscakgtcsy
      481 yqylegtsma aphatgvaal lvsrfgkpgk ggveldpatt elllhrtarq kacpsprayv
      541 ykvygetetq tceggaakng fyghgivdal kaatvkkq
//
LOCUS       WP_357635614             270 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357635614
VERSION     WP_357635614.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 270)
  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..270
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..270
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28559
     Region          1..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 mvnmssmvld gcalryadsg gdgvpvvfsh gagadhvmfe aqyeyvraqg hravmwdmrg
       61 hgssrpagal ftaeraiadl raliehlald rpvlvgqslg gnlgqaivrr hpglaraliv
      121 igaawntapl swkerllvkt aapglamipa ghlprvmaea savsqaarad arrafsqlsk
      181 keflqvwrat vgfltpdpgy rtpvplclir gerdrtgnia tampawaqae gvkevvipga
      241 ghianqddpq avnevigafl rtipapkgas
//
LOCUS       WP_357635698             280 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea wenchangensis].
ACCESSION   WP_357635698
VERSION     WP_357635698.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 280)
  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..280
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..280
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29422
     Region          22..274
                     /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 msvattraka gveglvapep prpagrhpav tfalraigpv lllttwyaat asgvltedvl
       61 agpqdvvttf aelwadgqlp ealrvsitra glglvlgast glvlgvvsgf trlgeelvds
      121 smqalraipf laltslfivw fgieeaskil ligvactfpm yvnvasgvrn vdrkvveaar
      181 sfglgrmava revvlpgalp sifaglrlst tlsvialiaa eeinvtaglg ylmaratdyl
      241 rtdilalcvl lyaviglvad ltlrlaervt mpwrravsir
//
LOCUS       WP_357635731             386 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora parva].
ACCESSION   WP_357635731
VERSION     WP_357635731.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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..386
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..386
                     /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=41830
     Region          149..284
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            order(177..183,205..206,232..234)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mpqpldaalt evrallldpa ltravaagrr rgrrptvera elrpvtlkag priqittsdg
       61 arpytrnias gpeaaaavde llaepfgnwh vetadatlql rvtksgeaqv hraatsrpaa
      121 tptgndrtke ylldpgdpif aeiggsaakr rqvdaflral aatlpddltg plrvvdlgcg
      181 nayltfaayr yltsrglgvq lvgvdvredq rrrntelaqr lgwadqvsfv agtiadavvd
      241 papdlvlalh acdtatdeal aravrwearw vlaapcchhd lakqlrahpa papyelltrq
      301 gilrerfadv ltdalragll rlhgyrtevv efvdsqhtpr nllirarrtg agatgaqrae
      361 yrelvdqwqv aprletllaa deasas
//
LOCUS       WP_357635735             710 aa            linear   BCT 28-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Micromonospora parva].
ACCESSION   WP_357635735
VERSION     WP_357635735.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17571359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..710
                     /product="RecQ family ATP-dependent DNA helicase"
                     /calculated_mol_wt=76492
     Region          10..561
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
     Region          <586..709
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
     Region          <645..>701
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 metaeragvr eraeavlrrl agdharlred qwraiealvv drrrvlcvqr tgwgksavyf
       61 vatallrdhe hgdqagptvi vspllalmrn qveaaaragi rartinsanl dewdeitaei
      121 qigsvdvlli sperlnnpdf rdgvlpklaa ttgllvvdea hcvsdwghdf rpdyrrlrtf
      181 laelpdrtpv lattatanar vtqdvaeqlg dalilrgtld reslrlgvld lpspahrlaw
      241 ladhldqlpg sgiiytltva aagetaeflr srgypvasys gqsddadrra aeqdlldnki
      301 kalvatsalg mgfdkpdlgf vvhlgappsp iayyqqvgra gravehaevl llpgvedaai
      361 wryfaslafp peqqvravla alhtdrplst qaleplvdlr rarlelmlkv ldvdgavrrv
      421 rggwlatgep wvydearlrr vaeartveqq amreyattsd crmrylrerl ddtgaadcgr
      481 cdrcadplft advstaalaa aqtflgrpgv eiapkklwpt gldavgvplk griapaeqal
      541 pgravgrlsd lgwggrlrdl vgpdapdtpv pddvagavve vlkawahgdd pwprrpvavv
      601 avgsrrrprl lgsladriat vgrlpllgev ttagpggpag prgnsaqrvr alhdtftvpt
      661 dladalagld gpvllvddli dsgwtmtlva ralrragatd vlplalavag
//
LOCUS       WP_357635767             946 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357635767
VERSION     WP_357635767.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 946)
  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..946
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..946
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=101166
     Region          38..946
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mspriqlpsg wvtfvftdie gstrlaqllg pdyrpvlaah rrllrrtlas tggaellteg
       61 dsfflafeda taamtaclta qralashdwp taeaaprvrm glhtgyaepr dgeyaspevh
      121 raarvaaaah ggqvlctast arraepmppg atlldlglhr lrgfddrerl fqlvapgler
      181 qfprprtada vahnlptqvt sfvgrqaeri elgllvrqhr lvtvlgagga gktrlavela
      241 sgvveaypdg vwfvdiasvt dpglvafaia avlglrpepg rpmldtlvey aanrrmlvvl
      301 dtcdtqpaac aeviarllsg gsgvrvlats resfslpgev vwripplsvd pradgaesda
      361 vallldrtaa arggrqpdpa esadlrrvvq rldglplaie laaarlrvls vgqlaerldd
      421 vlgtldagrv dpdpppverg wsgnqqdtvd lvaaaagasp pspasravqr saterhltmq
      481 atvtwsyrtl gpraarllrw lavfagpvdl etvewllgdd pldplsvlvd ksmvlaepra
      541 agstyrmldp irayaarrlv eageeqaard rhvawsahal drahlgqdgr pvtlslysld
      601 plagelraal rwcatggsar aglglaggld qwwlerglar egrlwlfrly griaetgeri
      661 peaelaaayh mhslhasadg efaeelrysq raeaaarqag dagllarvla graaplvdmg
      721 qfveaervcr evidwahgqd vvgealfavf slaellwrrg aleeaaellg avrpveaarp
      781 vergrrsvdm llgmvalarg dviaahehll valrsrmghg yhgracdtln avavrcaigg
      841 erltaarlfg aaqatrasmr atpgifggyw aqqqgelrav lgdaafdday gegaelglde
      901 aaalaldveh pdlaadstrf stglsqptpr rpadpdrhpa trtega
//
LOCUS       WP_357635751             254 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Nonomuraea].
ACCESSION   WP_357635751
VERSION     WP_357635751.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25998
     Region          24..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 mrglqgkrii vaggatgiga asaerlaaeg arvtvgdvnl dgaratagri aqaggtaiav
       61 efdladeasv ealagaaiae fggvdglynv gadlsattlg rdsdlltidl dvwrrtfevn
      121 llgyartcra vmphllaqgg gvivntasga asgtlpnrpa ysnskagava ltrhiasrwg
      181 kegirancvs pglvmgetqk rqndqqlqaq alqivrstrl gepadlaaav aflfsddaew
      241 ingqiwsidg gmtl
//
LOCUS       WP_357635779             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea wenchangensis].
ACCESSION   WP_357635779
VERSION     WP_357635779.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=15917
     Region          10..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mprandgvta aqvadefsrt akvlvrhfne rlgehgvstp rsrlvvevar sqpvrltela
       61 lavgiaqgta stlvdalvrd gllerqtsad drrsvllrvt aqgaalaqdw tagyelaaee
      121 lfrpltpeql stlvdilrtl sagetsaagd
//
LOCUS       WP_357635799             218 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea wenchangensis].
ACCESSION   WP_357635799
VERSION     WP_357635799.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 218)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..218
                     /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]"
                     /calculated_mol_wt=23759
     Region          48..191
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mqtagtslrq ralrylvsqa hhprgvvgwa ngwmfahrps nrkrniwavs lldvrptdrv
       61 leigfgpgva iaefaaratr gqvfgvdhsr amvrraarrn aaavrarrvh lahasverlp
      121 sfggpldail avnsvgfwpd pverlgelrr llrpagrial vsqprcpgat rdttaqaare
      181 lqdlltragf thlrvetlel dppvacvlad npghppgr
//
LOCUS       WP_357635795             479 aa            linear   BCT 28-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Nonomuraea wenchangensis].
ACCESSION   WP_357635795
VERSION     WP_357635795.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 479)
  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..479
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..479
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52783
     Region          1..479
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 msfasplflw ffmpatlltf walpsrhrna vvaaasllfy awgagphtpl llsaiavnyg
       61 aglaldsarl rdrprarrgv llaavgwnva mlavwkyagf ateqldaltd alglghspvv
      121 alalpigisf ftfhhlsyvv dvyrvstpaq rspvrfityi amfpqliagp ivryheiaeq
      181 lgdirrdrlg dlaagfprfa lglakkviva dslasvadaa faqaggpvnt ptawlgasaf
      241 alqiyfdfsg ysdmavglgl mfgfrlpenf drpyaaysvt dfwrrwhlsl srwfrdyvyi
      301 plggnrggap rtyrnlliif vlcgfwhgad wtflvwglyh gallvaerll gwdrpprtvw
      361 tlalrravtl llvvvgwvff ratsmteaws mlramftwrp geldefvawa anhqrmavfv
      421 laalavvalp asralgpliq sgrgpavrla raavtwvaap yaallvaagt fspflyyqf
//
LOCUS       WP_357635784             289 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora parva].
ACCESSION   WP_357635784
VERSION     WP_357635784.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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 289)
  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 289)
  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..289
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..289
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30728
     Region          32..256
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 marsrkvtvs tdaeghtagw adtdlaavsa pdptgaaffd vdntmmqgas iywfarglas
       61 rnyvttadla rfawqqlrfr llarehagdm slakeaalaf vegwrvneve hlaeeifdel
      121 mapriwagth qlaqrhldag qrvwlvsaap veigrviaar lgltgaigtv aevvdgaytg
      181 rlvgdlmhgp akaeavtqla avegldltrc aaysdsandl pllsvvgrav avnpdgvllr
      241 qarqhgwevr dfrtgrravk iavpstaaag lvagavtagl alqrrrrag
//
LOCUS       WP_357635888              80 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357635888
VERSION     WP_357635888.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 80)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (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   5  (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 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..80
                     /product="PadR 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=8802
     Region          3..64
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mallvlasla egqkhgcrmi qdieefawer gwidpvvssg rrkpyrites grgvlreqla
       61 tlrraeetga grlniawgpa
//
LOCUS       WP_357635866             322 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora parva].
ACCESSION   WP_357635866
VERSION     WP_357635866.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  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 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   3  (residues 1 to 322)
  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 322)
  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..322
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..322
                     /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=34198
     Region          1..244
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtrwgilatg hiasrfaedl rlvpdaelva vgsraaqsaq rfadtygakr aygswvelaa
       61 dpeldaiyva tphsahyeaa mtcltagrav llekpftldl atstelvdta raagvflmea
      121 mwmrlnpmil rmveliadga igtvsgvrad fgvagpfppe hrmrnpalgg galldlgiyp
      181 islahlllgv pqhirswaql gpegtdentg mlfgydtgal atlscgmvgl sgqtasitgt
      241 lgridvpepf frpgsftlhr vgaepetfta deagngyqye aievqrclaa gltespvvph
      301 attlevmall dtvreqigvr yv
//
LOCUS       WP_357635899             162 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357635899
VERSION     WP_357635899.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 162)
  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 162)
  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..162
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..162
                     /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=17175
     Region          1..143
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mhhiddprlt amgllaevna glnsrmqpvl saaglsdidf etvlrlgrsp gqqlrmtdla
       61 aqtglstsgv trvvdrlerd givervacas drrasyaalt dagrarleav lplhlsdies
      121 cftgllddde ltaflatlrk irdvvrpcat agtgegplgp rp
//
LOCUS       WP_357635917             367 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357635917
VERSION     WP_357635917.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 367)
  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..367
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..367
                     /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=38493
     Region          122..361
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstgrtgsrk arlvdlalal ltavgvglgp ammgapllwh gapalgvllg gllparrsrp
       61 llvlvlsavv ligyqssglf eggwiwplsa alftaslsrp gwaggvgvlt laygvswdrl
      121 daaeafargg vellwlavml aaasavrqyg rwraehqvrl lqleqtrlae qrlhisrevh
      181 dvvahtlavv gvhlnvavaa lddspeeara alrtalavrn qatrdlkafv gelrdtpqqg
      241 lesvtdlvaq arsaglkvry epegdlgsvp aaqaltayrv vqeavintlr hsdadcltiq
      301 lqaasqdlrv rvadngsaaa dfaaghgltg mrervvalgg tlrvdagrgf evqavlplta
      361 hlsglas
//
LOCUS       WP_357635981             395 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357635981
VERSION     WP_357635981.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=40936
     Region          25..382
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msagsagsad lvvvgagvvg aagayfasla glrvvvverg piaggtssag egnllvsdke
       61 agpeldlaly sqrvwredla ghaglwefea kgglvvagse asvaslrelg ahqrrhgvev
      121 rdvgrdelrd yephlspela gaafypqdaq vqpmlvvahl lrlarglgae vrtrtevtaf
      181 lrdgdrvtgv rttggdisag avlnaagtwa gglaglagvs lpvlprrgfv lvtqpmpprt
      241 irhkvyaaey vgdvassdaa lqtspvvegt dsgtiligas rervgfdrtp sveaiaalaa
      301 kaialfpmlr evramrtylg frpycpdhlp vigpdprapg lwhacghega giglsagtgk
      361 lvaqaltgrg pdldlkpfap drfpdsfpdm eevlp
//
LOCUS       WP_357636015             191 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [unclassified
            Nonomuraea].
ACCESSION   WP_357636015
VERSION     WP_357636015.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 191)
  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..191
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..191
                     /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=20769
     Region          8..164
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mskpvlqiiv astrpgrvgr siaewfrdra vaaggfdiel vdlaevglpf ldepnhprlk
       61 kyehahtkaw satvdrgdaf vfvtpeynhs fnavlknald ylhqewqhka agfvsyggvs
      121 ggtravnglr qvtsslkmvp vvesvnipff pqfvgedgvv rpdemmnaaa daliaeltkl
      181 tgalrpmrla a
//
LOCUS       WP_357636023             149 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357636023
VERSION     WP_357636023.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 149)
  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 149)
  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..149
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..149
                     /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=16825
     Region          1..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtrwldddeq rawrnfvaat qllyaaldrq lqrdagmpha yyvvlvglse aperrmrmse
       61 latwaqssqs rlshavarle ergwvrrerc pddgrgsfav ltdegfaala gaahghveev
      121 rrslfdvlsp eqvralddic atvrdtler
//
LOCUS       WP_357636116             276 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357636116
VERSION     WP_357636116.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 276)
  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..276
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..276
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30068
     Region          3..>158
                     /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 mngflsvpga rlyyevrgtg pvllisqsge gdagrtvdlv drlvtdytvi tydrrglsrs
       61 tlddpaggat vaehaddvhr llaeltdepa rmlgcsfgav lglhlavrhp aqlhtlvahe
      121 pvapallpaa errhheeelq elqrlyrdqg lagtfgkiae vlgiqlgrqe tepgltqhpm
      181 ddrrranfdf firndfgaiv hdtldtldtl dtaaiaggpv rvipaagrtt prhvfdhrca
      241 helatlvgre veefpgghng nlthprayas rlrdll
//
LOCUS       WP_357636208             159 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357636208
VERSION     WP_357636208.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=18048
     Region          2..140
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtdqrrtrly eelsmesrry laayvlfnqa vadhlglhpt dvqclsllta epgpltvkqv
       61 admtglttgs atrlvdrler ggyvvrapdq edrrrvlvtp vpdrlarvta lwddlgqtwq
      121 tllddhtede levitrhmrr anvlsqaqmr rlrsmpkpa
//
LOCUS       WP_357636220             310 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357636220
VERSION     WP_357636220.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..310
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..310
                     /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=34259
     Region          1..302
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mrsrrsvlav pgssprflek aqtlpvdevf ldledsvapa akedarrnvv aalregdwsg
       61 ktrvvrvndl atqwtyrdvi evvegagefl dcvmlpkvqd ptevvwldtl ltqiekamgy
      121 epgrigieaq ienarglvnv dviagssrrl etlvfgpadf masinmrtlv vgeqppgyte
      181 gdayhyilmr llmaarshdl qvidgpylqi kdvdgfrrva rrsaalgfdg kwvlhpsqvd
      241 aanevfspeq edydhaelil eayeyyttve krgavmlgde mideasrkma lvvaakgraa
      301 glsrtvtftp
//
LOCUS       WP_357636226             146 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357636226
VERSION     WP_357636226.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..146
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16154
     Region          18..114
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mseyehtcmi rgdggrtira ildricnkwt llivatldqg rlrftdlhqq vpgisqrmlt
       61 ltlrnlerdg lvsrtvhaev pprveyeltp tgkslippal alagwaiehv phieasreay
      121 qtrdqrpdqa agaafsssrg kkgssr
//
LOCUS       WP_357636049             326 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha-ketoacid dehydrogenase subunit beta
            [unclassified Nonomuraea].
ACCESSION   WP_357636049
VERSION     WP_357636049.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..326
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35053
     Region          1..324
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mrvgenlnqa lhgllgddpg vyvlgedlld pyggafkitr glstrfpdrv lttplsegai
       61 vgaasglala gekaiveimf gdfaalafdq ivnfagksvs mygrrvpmpl iircpsggnr
      121 gygpthsqnl qkhfigvpgl slfemspfhd nravldrmla leepcllfed kvlytrrmye
      181 vdelftwdlv qdvavvrfdg dldyaviapg gvahraiaam rtlllshdla gavlvpsrly
      241 pfdpaallpl lgraglicva edgsaggtwg ahlaadlhtr lwdslrrpir lvssadsvip
      301 tavhlerdvv lqdsticrav lealdg
//
LOCUS       WP_357636246             338 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050733].
ACCESSION   WP_357636246
VERSION     WP_357636246.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Rosinski,J.A. 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 338)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..338
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     Protein         1..338
                     /product="helix-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=36483
     Region          19..326
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpktsarlla llsllqarrd wpgallaerl disprtvrrd vdrlrelgyp ivafkgpdgg
       61 yrldagtelp pllfddeqav alaialqiat ttgagieeaa aralntvrqv mparlrrrid
      121 tlqvtaverp avrpdaqads gvltalgaav harevlrfdy apasppgpdg ngvpaparrv
      181 qphhlvtwgg rwylvawdld redwrtfrad riaprtptgp rftprelpgg evaafvaarf
      241 rgsdgsgdwp crgevilhlp aaevsrhtrd gvveelgpnr crlvlgswsw pglaaaigry
      301 dadievvgpp elkdafahla rryadaatgr acipgsag
//
LOCUS       WP_357636378             220 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357636378
VERSION     WP_357636378.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=23329
     Region          4..213
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mredhleals llhdpvrrsl yeavagagge vgraeaaeaa gvsrtlaghh ldklveagll
       61 esgfrqqerr gpgsgrpakv yrraagersv slpprdygvl asvlagvvda lgaeeraega
      121 araagarlar ahrgepveav lrdrgyepyt eagrlrlrnc pfhalsqeqp llvcsmnlal
      181 cqglleglgd rperaeldpr pgeccvslag psrssktned
//
LOCUS       WP_357636350             309 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357636350
VERSION     WP_357636350.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (residues 1 to 309)
  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..309
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..309
                     /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=33147
     Region          1..289
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mqlqqlayfv avaetrhftq aaermrvaqp slskqikale sdlgaplfsr argnvtltpa
       61 geallplarr mladadtarq evaqlaglrr grvrlgatps lcaglladal arfhraypgi
      121 ellveeggsr dlvralargq ldlsliimpl qsddpalvte eilrenlvvv spsheparrp
      181 ymeigelrgr pmvmfrrgyd lreatltacr hagfeprfav qggemdavlr fveaglgvav
      241 vpsmvldgrp glagtplapp glsrtialah rkdvepttaa qafrgvllsf vveagvegtl
      301 pqgveliae
//
LOCUS       WP_357636388             321 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357636388
VERSION     WP_357636388.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=34877
     Region          6..318
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msgsadrlpr llalvpylms hpgaqvgeva evfglsekql iddlqlvwmc glpghtpgdl
       61 idvswdggei lidnadtiar plrlgideas allvalrmla ampelaevpg dalprvvakl
      121 eraagegass vssqvavdvd aapdalprvr ealtgrrrls lryyvpgrde vtprevdpmr
      181 lvvadgrtyl egwcyraeam rlfrldrmlg vdvldvpadp pagaepidva qgvfrpsptd
      241 emvelevtaa grwvaeyypc eraeelgegr lrvtlrarde dwvvklalrl gdtgrivspp
      301 smaarvrqea esalaryahr s
//
LOCUS       WP_357636389             200 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357636389
VERSION     WP_357636389.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=21121
     Region          17..>124
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrgrpslpvl gqpqperada arnrqkiida tariiaerga aaglsldeva rmagvgvgtv
       61 yrrfgdrngl vlalmdeqer rfqteffsgp pplgpgappg eriaaflgal vdrvlaqqel
      121 flllekggkp wyggpyrvhh ihlatlvgqa rpdvdaayla dallapvnag liahqrearg
      181 msvaqikagl aalataavra
//
LOCUS       WP_357636501             337 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YeiH family protein [unclassified Nonomuraea].
ACCESSION   WP_357636501
VERSION     WP_357636501.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..337
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..337
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32821
     Region          11..316
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 mvvsvrrarg agagsvvpgl vvvaagvvva fvvnalvpav splvaavvlg aamtnlgvrg
       61 aalepglafa arrllrvgvv llgaqlavsd vvalglpvll vvvatvavtf svtwwlgwrl
      121 glgrglsvlv atgfsicgaa avaamegvvg gareevvtav alvtlygsla mvvlplaggv
      181 lglpaegfgv wagasvheva qvvvtaqtag saalgvavvv kltrvvllap liagvglwrr
      241 rveglsgggg rapvlplfvv gflvmvglrg vgvvpvgwla slggaqvvlf aaalfamgaa
      301 vrlrvlartg gravllggva tavvvgvala gvgllvs
//
LOCUS       WP_357636620             290 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Micromonospora parva].
ACCESSION   WP_357636620
VERSION     WP_357636620.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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..290
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..290
                     /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=29364
     Region          3..260
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mvdllvlggl gvdvrvrvpa lplpaadsht vepielrign tgagvalaar alglrvlvvd
       61 tlgadpagel vraaltragv pavlaenpdg trrsvnlvdp ggrrtslydp rpwrggppfs
      121 aaevaalard arhvhlsimd wavpllpavr aaiaagvals tdlhdwdgen tyhrpfadva
      181 dlvlvsgvrl gdrgaslagt laprtvlvtr gadgaelfpg dgtvtpvppa tapapvvdtn
      241 gagdafaagl iaarlrgepl adaaryaarv aaaacahdgm eyppgllpsg
//
LOCUS       WP_357636642             397 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified Nonomuraea].
ACCESSION   WP_357636642
VERSION     WP_357636642.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 397)
  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 397)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 397)
  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..397
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..397
                     /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=40704
     Region          122..396
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtsssaqrla rvlitsvsav ytligllyyt vspaygllat gaiivlaamy ylnmraalrd
       61 erppvfpltl vlqavatygp dallpggwsg vaapmlgaav lvmlplrlgg plvalmtvyd
      121 tamlfpvavv alfygltvpl tsgmvyalvr lvrvtsdleq araelaeaav mrerlrisrd
      181 lhdglgrslt aialkgdlag rlmerdpaaa rgevgelvrv areaaqdvrr vargyrelsl
      241 tgeanrgaal lesagvgcqv hladvtlpra seealawavr eavtnvlrhs aattctists
      301 vregavrlev tndgvpvape apaapgdgvp gegelagdal agdglvgggs agdglagrgl
      361 agggltglee raahaggtll aartpaggfr ltmevpa
//
LOCUS       WP_357636653             577 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora parva].
ACCESSION   WP_357636653
VERSION     WP_357636653.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 577)
  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 577)
  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 577)
  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 577)
  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 577)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..577
                     /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=57230
     Region          68..572
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mggvsnrpwr apvavaalta llvagcsggs prpaptpspt apsggpsapa appaadpagr
       61 aaalvatlsd edlvgqvlmp yaygdsatkv sagsaagnqa lagvdtpadm iakyrlggli
      121 lvgfsaddpt kgnqettnvd npqqvheltt glraaagrla tgpaplligt dqeygvvtrv
      181 tdgvtvlpsa laagaagdpk lteaawraag telaamgini dfapvadvla trstvigsrs
      241 ygadpkqaaa qvggavrglq asgvaatlkh fpghghsadd shqdlpvltq saaalqsgaw
      301 ppftagmdag amavmsghld araidpgtpa tfshklltdv lrgqlgfkgv vitdgmnmpp
      361 akrwapgeaa vralnagndl ilmtpnvaqa ydgllaalrg gslprtrlve avtrvltmkf
      421 qlaelpaaqm stlntpahra aaealaaaav tvlrgtcgae vrgpvtvtss ggrdgtratl
      481 taaltaagvs vkpsggtvvh lvgygdgaed lradaavtva mdtpyvlaga tsptllatys
      541 ssrasmtala avlggkarpg grspvavpgl pastcrt
//
LOCUS       WP_357636655             383 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA-guided endonuclease InsQ/TnpB family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357636655
VERSION     WP_357636655.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=42367
     Region          4..375
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 midvklvvqv rllptpeqaa aleatlravn aaachvsaqa ydqqtfrnyd lrkhtytqik
       61 dryglaaqaa qhvikkvada yatlhahlra gnlgqegspr rtratskpit frpdaaqpyd
      121 drclswqinv rtvsiwtvag rvrnmaftas pdqitmlsah rkgesdlllr dgmwfliatc
      181 dlpdrpvtdp dgflgvdlgi vniattstgs rhcgkglnav rhrrrelrrr lqakqtksak
      241 rllkkrrrae arfaantnhv iakqivteae rtgngialed lqgirdrvrl rkpqrvtlht
      301 wsfhqlgrfi aykaaragva viyvdpafts qqcslcghad rrnrldqasf actscgfaeh
      361 advnaarnia argvagwavs haa
//
LOCUS       WP_357636676             952 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357636676
VERSION     WP_357636676.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 952)
  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 952)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 952)
  AUTHORS   Rosinski,J.A. 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 952)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19885644
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..952
                     /product="helix-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=100129
     Region          16..>399
                     /region_name="PRK04841"
                     /note="HTH-type transcriptional regulator MalT"
                     /db_xref="CDD:235315"
     Region          <565..901
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          771..937
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          889..937
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mleqnqvrve papgppllas rltpavppep vvarprllrr ldegsagpvt vvaapagwgk
       61 ttllaswvrl ggaapdvqpg evvpdsgdls vspadtpvsa wmsveagdds drlwaylaaa
      121 lrsaigstdd gpvpdrpprp dqlealaarl aaadrpvlli lddlhrvtdp aaltglefll
      181 rhagrrlrlv igaraglhlp lhrlrlagel teigpdelaf tddevadllt ahaaalpasa
      241 vhrlrertgg wpaalriaal avrgqpdper wvgqfggdqp eiagylheev latldpgevd
      301 llrrtalvdt vcadlaealt gradagqala dlagtggllh redtrppwyr ceplladllr
      361 adlarlpade lrelhvraad wyagdgrpad glrhalaagr wdlagdlfva hwpeltryds
      421 gpvhapapap ppaeviradp evalacaaer ayagdlpaad ghlraaagha aglpvprrdr
      481 flrlvtalel tvarladdrg evraaaarll rtrpsdatpt rvpdspptgv vssaptaggg
      541 gaaddldlra ftgtalglve madgelptar fvraraaare aerprtelvg asraalllav
      601 rgelrsaeqa ardalgmppc rgwscrldcg yaylalavva llrdqpdeat anlalalaal
      661 dvaggwsgda evgdewlaaa sgepvaaava alcgaqlrrd sgdpaagqrl lvrarealad
      721 rpsaarltgl llaaeaelra argdldsard lltdaaeegt dpvlavtlak mqllagdtaa
      781 aartlpawqa paatawplpv rldaglldav laeragdgrr agrileqtld lagpqgcrrv
      841 ftraeppvrd llaahldagt ahfalvsdlv rgagqstagp atgmrgalde pltereltil
      901 rylqsilsnv eiaselslsv ntvkthvrni yrkldatrrr eavrrarelr li
//
LOCUS       WP_357636699             376 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357636699
VERSION     WP_357636699.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=40438
     Region          125..369
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdlstgqpwp vsrhwrytgw llaavwlffl nvplatalhq pepwrrilgv stlvvfsvgy
       61 vllfqwarkl rqslrpipag raraglalll avglaslpgt ggdwlatlvy vaaaavfllp
      121 qwealavval cavtpvlasw lvpgweaehg ivfavllasf amfgvsqlaq rnselraaqq
      181 eigrlavaee rartardlhd ilghsltvva ikaelagrll dvdreraaae iaevealara
      241 aladvrqtvg ayrevslaae vagarsalaa agiaadvpte vpdlprewdr lfgwavregv
      301 tnvvrhsgar ccvirvhpdr veisddgrgp stpdasghgl vglrerarrl davvtvgrrp
      361 tgdgfllrvh sqeaar
//
LOCUS       WP_357636741             430 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357636741
VERSION     WP_357636741.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 430)
  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..430
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..430
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46386
     Region          1..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvqaatcfgq elrrrrlaag ltltalsnrv hyskaqlskv erdlkspsrd larlcdsalg
       61 adgelmalip trpkdakarr tsdeedvwlm alsrdgqswf qplsrrqlms mgvaasvgmn
      121 ighpetttpa gdatlltasr tlfdnyrqlg qaaspgallp aliaqthslr dlsartgart
      181 rdgllrlasr yaeyagwmmq eigsdqgalw wtrhavelav aggdhdlaay ghvrhalvtl
      241 yrddaaqtld larqaqsskl pprirglaaq reaqghalag dydacmrsld rarallttpa
      301 sqpdgppvig ttnlpdpvgm itgwclydlg rpreaaevis gqlalvppha lrtrvrygmr
      361 ralahamage lehaceltdr llpaaaavss atiatdmral artlsrhpkn aavrrvapel
      421 stalqvvntk
//
LOCUS       WP_357636836             440 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: KamA family radical SAM protein [unclassified
            Nonomuraea].
ACCESSION   WP_357636836
VERSION     WP_357636836.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..440
                     /product="KamA family radical SAM protein"
                     /calculated_mol_wt=49394
     Region          17..385
                     /region_name="EpmB"
                     /note="L-lysine 2,3-aminomutase (EF-P beta-lysylation
                     pathway) [Amino acid transport and metabolism]; COG1509"
                     /db_xref="CDD:441118"
ORIGIN      
        1 milnqagtrr fraytskhln dlllragldd edrlkvrava tvlpfrtnay vvdelidwsa
       61 apddpmyklv fpqadmlpap dvarladllk aeapaaeina eanrirarln phpagqmeln
      121 vprlddepvp glqhkypetv lifpkqgqtc hayctycfrw aqfvgdadlk fasddieqmv
      181 ryirrhpevt svlitggdam imgepvlkry leplldleql esvrigtksl aywpqrfttd
      241 pdagstlelf ekvvaagknl afmahfthpr elepplveaa vrnilgtgat irtqaplirs
      301 inddpalwst mwrrqlrmgm ipyymfverd tgpqdyfavp laraheifrd ayasvsglcr
      361 tvrgpsmsat pgkvcvdgvt eiagervfvl hfiqardpsl vgrpffaryd ptarwltdlr
      421 pafadrfpfe paveeallav
//
LOCUS       WP_357636961             709 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Micromonospora parva].
ACCESSION   WP_357636961
VERSION     WP_357636961.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..709
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..709
                     /product="PhoX family protein"
                     /calculated_mol_wt=75395
     Region          47..703
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msdrprllpl ltgarhgtrd amtclyrcgn acdhpvpnts dnayfgdvvn aemsrrgvvr
       61 agavgalvlg fggaaagala gaapavaapa ttpdvpeafg fgrpstgvgs galtfkpipp
      121 nkldtlvvpn gydhavvikw gdpvlpgape fnlhhqsaaa qskqfgynnd fvgvlpldkq
      181 grrallvvnh eytnedlmfp gfpgldglsv eqlrtamaah gmsvvelerv agtgqwqpvs
      241 kgprpynrrv talstkfdlt gpaagsawlk taadpkgrtv vgtlnncagg vtpwgtvlsg
      301 eenfnqyfvg adaapaelkp kldrygigta srypsgsrrw eraderfdla khpneahrfg
      361 wvveidpfdp esrprkhtal grfkheganv ivakdghvva ymgdderfdy lykfvsdkkf
      421 mkgnswaark hnltllesgt lyvakldqss aaeidgsgrl ptdgafngrg rwiklvsgnr
      481 sfvdgmtaad vltftrlagd kvgatkmdrp edvepslltg kvyvaltnnt nrgvgsnpka
      541 deanprtank hgqilelved rndnaaetfa wslpivcgdp tdpstffagy dkaqvsaisc
      601 pdnvafdatg nlwistdgna lgsndglfat avegpqrghl kqfltvplga etcgpfitgd
      661 nrslfvavqh pgeisgasve npasnwpdgd yakpgvvvtw rldggpvgs
//
LOCUS       WP_357636966             844 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea wenchangensis].
ACCESSION   WP_357636966
VERSION     WP_357636966.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 844)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 844)
  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 844)
  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 844)
  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 844)
  AUTHORS   ter Beek,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 844)
  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 844)
  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..844
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..844
                     /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=85320
     Region          21..828
                     /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 mlrtalaglr ayrlrlllts laialgvgfi agtfvlndtv qagfsqkvta dagkvdvavl
       61 akdgvlaedv lrrvravagv tdaqglvrgp vrllgkdgkv agdlpatais vvrgplqrtt
      121 ivagtgpgtd draavldent arvngfrlge dvvvldpage rhtfklvgll dpgvdqelaf
      181 tgavglttsa alrmieekgy heidvaggap glkqavaaaa gpgaavktgd elaadlaaaa
      241 glemrtltvg lllfgvvamm vaalviyntf tilvaqrare lallrcigat rgqvfgsvll
      301 esgvvgllas vlglatgygl aalalallaa fdaplptdas valtpvtiav glavglvvtv
      361 gaallparsa trvppvaalr tqadeqafrm gaarwsvaal fllagagatg fgvlgmppgg
      421 vatlvvvmag gmltflavlv lgpalvrpls avvgrlparl agvpgrlald naarnprraa
      481 tttvaltigv tlmtvisvls astratvmek ldeqfpvdyl lsaqggeaav prsvaeelrr
      541 apelasvlqi retpaevtgp aggarmydlg tfngpvtpev vtgsmaagls egqvalldrv
      601 atelgvrvgd tvqvsvrdkg ragsgragga gsvplrvvav ldgggsalps ltvaesafdr
      661 yagalpdarv lvtirdgvsa drarvvvrea vadyptvlls sstevrgefd etldmllmiv
      721 ggllglaili sllgiantls lsvhersres allralgltr pqlrrmllve alvlglvgal
      781 vgvvlgglyg wvavlamldg avlsvpvgqv vlfvalsgva gvvasllpar raarasiaga
      841 laag
//
LOCUS       WP_357637002             713 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Nonomuraea].
ACCESSION   WP_357637002
VERSION     WP_357637002.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 713)
  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..713
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..713
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=77864
     Region          4..712
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(491..492,495..496,498,530,533..534,537..538,
                     540..541,564,567..568,577..578,581)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          491..515
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          528..558
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          563..597
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msfrwltahe gnlaapttaf vgraevcarm araigqtrlv tacggggmgk trialhvarq
       61 lradfpdgvw mvelsgledp dvlpsavina fgladvsard eaevlgehla nrhlllildt
      121 cerlpqpigt lisallraap mlhvlttsrv plgledeyvi hvgpmqvtda dapdmagetv
      181 eglelffrra rqaaqfeahp hhlalaqevc qklegiplal elaaaglrhl slaqileqin
      241 etralhanat leglpqrhrt lyaaigwshq lcepterllw arlsvfagdf dedavqqvcs
      301 daqitdtpal ldslvrksil trddahnrry rmldtlreyg amwlaelget erlrrrhrdh
      361 yltlarcgea awsgsgqvhw ylrmrdelpn iraalewsls hpeeihhgle lagalwflwv
      421 acgfsaegrh hlrraltint tpsttrckal wmeaylanaq gdltratsta ttcrdeaiai
      481 gypegvvvat kmlgtaaflg gdlqgagryl gqaleylrgd ptylnpgllp aivelalvii
      541 mqgqpqqalg llseclehch angelwlrsy alyvqalafr aldriqdait slhaslkikr
      601 hfhdvlgivl clealsqlvv ragypasaaa vlqgaaevsw reyglpmmgs prfadehaqc
      661 aqqvqemige qrykqafahg lslslpdaig falgeggapg lamdvldlia ags
//
LOCUS       WP_357637110             511 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora parva].
ACCESSION   WP_357637110
VERSION     WP_357637110.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 511)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..511
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56237
     Region          84..483
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvstdp rqqppgvtst applavpngr hhqsvpqpmp avtappeppp rprmdfqvvr
       61 elrrelterl tlwqrgreft vdeedterar lavtvvaaya dsvrragtpm aaseerllld
      121 qvtaelvglg rlqtllvddt ieevhilgcd qvritrhggg vdwaepiads daelveilqa
      181 aarragater slstvkptld lqlpdgsrla avflvshrpy avirkhntld vslddiagar
      241 ndldemidpl lrdflraamr aglnimvagl agagkttvir almneippde pyvlleesre
      301 llparrrerh ravmsfeare ghgergfdgr pagevtiadl iplslrmgvl riivgevrsr
      361 eivpmlqamt tsrgsmctih artaagvger ivelalahgr emtvdqarrm agnaldlivy
      421 vtvedetaig grkhrfvshv eevigageag rittttvfgp gpdgravprh lpervrdqll
      481 rvgydarllt rwveagagaw rrprqtrlar r
//
LOCUS       WP_357637043             205 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357637043
VERSION     WP_357637043.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 205)
  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..205
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..205
                     /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=23074
     Region          8..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtavglrerk kektrlaild aalelfleqg yesttveqia gavdvsprtf fryftskdhl
       61 vlwfhdqsee illetmaarp pdeppftalm halramladi edatpqeher flklrrilde
      121 nprlvgqsva rgteterrla evvaarrgvr adedqlshli vafamstmrv gfecprsdgs
      181 lpeitgrmae sielaerslr pgwda
//
LOCUS       WP_357637209             296 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357637209
VERSION     WP_357637209.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 296)
  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..296
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32829
     Region          25..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(30,34,59)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(33,58)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(40..41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          111..291
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msapsaegsv lgftpgsptv lrillgsqlr rlrtekgisr eaagyairas hakisrlelg
       61 qvsfkardva dlltlygvte eaerapllsl arqanaqgww hkygdllpaw fevyiglega
      121 asvirtyenq fvpgllqapg yarevirlah dvapqdeier rvslrttrqr rltgegavtl
      181 wavideavvr ralggpevmr eqidhllemt glrnvtvqvm pfergghaaa ggpfsilrfp
      241 erdlpdvvym eqltsalyld kpaeaehymr vmdrlsiqae sparsrkfle elrssl
//
LOCUS       WP_357637298             209 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [unclassified
            Nonomuraea].
ACCESSION   WP_357637298
VERSION     WP_357637298.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 209)
  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 209)
  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 209)
  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 209)
  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..209
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..209
                     /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=22129
     Region          2..209
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mritvfgatg rtgrrvveqa leaghdvtav vrdparlapy gprltvlrad vmdpddirpa
       61 vagrdavvsa lgphgrgpst icagastsiv rameaegarr lvvvsasgmi tegdgpvtrl
      121 vfkpvlgrvl rnpfadmlrm eevvrasgld wtivrpprlt egprtgsyrs aidrnvrggl
      181 rvsradladc vlrcldehgp lhaalaigd
//
LOCUS       WP_357637318             347 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357637318
VERSION     WP_357637318.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..347
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38501
     Region          <1..>197
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mlpwsaelag rldhrvidsa llrgnplgdp herpllvyvp pgyddeprrr ypslyvllgy
       61 tghvamwlnr apfrrpfpel adamfasgea ppaivvyvda wtalggsqyl dspatgryhs
      121 ylceevvpwv danyrtlpgr dhravtgkss ggygamvtam laphvfgala thagdalfev
      181 smrhafpgla rrlrdmyggs ydafladfrs rlagtregdl ellemyayaa aysadedgtv
      241 rlpfddtgat vpevwrrwla rdpvvmagep ryaealrsmr giwvdaghrd eyfldfaava
      301 frravaaagv pdervrfelf daghggieyr yplalawlar rlserng
//
LOCUS       WP_357637384             426 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357637384
VERSION     WP_357637384.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 426)
  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 426)
  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 426)
  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 426)
  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..426
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..426
                     /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=46924
     Region          1..325
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mryafvglgh raqmyvdall gewrdagtiv alcdlnrtrm dyyverigqe vpcfapdefd
       61 kvleladavi vttvdathar yvcaaldagr dvivekpltv daegcaaiaa aaerssgkli
      121 vtfnyryspr nsavrrllme gaigevtsvh fewtldtihg adyfrrwhrq rassggllvh
      181 ksthhfdlvn wwldaapelv faqtdlrfyg agnarkrgld erpergqgap glgsdpfild
      241 isadprlkrl yldaehedgy vrdqdvfgeg ididdnmsvl vrytnravlt yslhahapwe
      301 gyrvafngta grleldvver ewtpphaavd psaaakehat gsserlllrr hwsepeeipi
      361 engagghggg drlllndvfr gpdndplarq agyrdgirsv ltgvaatvsa rtgapvrlad
      421 hgtrvs
//
LOCUS       WP_357637453             179 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF421 domain-containing protein [Nonomuraea wenchangensis].
ACCESSION   WP_357637453
VERSION     WP_357637453.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..179
                     /product="DUF421 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=19232
     Region          6..169
                     /region_name="YcaP"
                     /note="Uncharacterized membrane protein YcaP, DUF421
                     family [Function unknown]; COG2323"
                     /db_xref="CDD:441897"
ORIGIN      
        1 mrigltwtda gtvvlstvvi ylaflvliri vgqralatms sfdlaaaval gavmgravlg
       61 ytptllagli gmctlfalqt gfrlmrrnsr leclmsnapl llmadgavlh dnlrkaqine
      121 delrqklrla svhrygdvaa vilertgdis vlrrgeaidp efladvkgcd rlrpghsga
//
LOCUS       WP_357637334             269 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357637334
VERSION     WP_357637334.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..269
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28326
     Region          3..268
                     /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 mptltipggs lhyelrgtgp lllisqsgeg dagrtadlvg hlaesrtvit ydrrglgrst
       61 vpdatvsvre hagdvhhlla hltdepvvml gqslgasigl hlaadhpeql slliahepvs
      121 pwllpepdra rhraelaair dlylatdlpt alkevtrvlg itpggdaepg ltafpmtaer
      181 eagfgffirh dfqaviddpg pddpaacrvp vvpaagertp aavfdrqcad rlaaltgvpl
      241 avfpgghngn lshprayaar lrevigstp
//
LOCUS       WP_357637458             286 aa            linear   BCT 28-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase, partial [Nonomuraea
            sp. NPDC050733].
ACCESSION   WP_357637458
VERSION     WP_357637458.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050733
  ORGANISM  Nonomuraea sp. NPDC050733
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Nonomuraea sp. NPDC050733"
                     /db_xref="taxon:3154633"
     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]"
     Region          109..253
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 aaappgapdg ldppdgmgap dglgapvgle vsatfvgrrs ysrfdvedav gaglsralgm
       61 pyhsraggva lppgavpwrv tiegdqavia vrlgerplhr rpykassipg tlhpplaaam
      121 avlaglgrpp aggaspgsga gpvvldpccg agttlaeagl laprarlaga drspvsvraa
      181 aantaragvr aalavadagr lplpsrsvdr vlvnppwgrq vaasgllard ggllwrevrr
      241 vlasgglava lmdgvpegfr vervvevsls grhpaiavls vprrrr
//
LOCUS       WP_357637461             278 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357637461
VERSION     WP_357637461.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   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 278)
  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..278
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..278
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29510
     Region          4..275
                     /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 meirtihang vefaylavge gplalclhgf pdtahtwrhl mpalagrgyr avapfmrgya
       61 pteipadgay egaalaadva alheelgggd davvighdwg afpvyglggr frrsvtlavp
      121 ppgamltsff syeqlkrsfy vflfqtglae taaaepgfle glwadwspgy darrdlefvh
      181 rslgrpgnla aaigyyraml gttppsgrhp dpepttgpil ylhgsgdgcl gagvvkdapd
      241 hlpagsraee vagaghflhl erpeevnrli ldwlgpas
//
LOCUS       WP_357637496             608 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-galactosidase [Micromonospora parva].
ACCESSION   WP_357637496
VERSION     WP_357637496.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14423454
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..608
                     /product="alpha-galactosidase"
                     /calculated_mol_wt=66077
     Region          46..374
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(53,87..88,151,219,221,252,272,276)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          384..458
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          470..603
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(482..484,495,497,504..505)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(529..530,544,546,553..554)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(578..580,591,593,600..601)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mrvvlvplaf rrvaallvvl lvaagvvaad pperavawdn gvadtppmgw nsydsfnwsv
       61 teadvranad ymatnlrqfg weyvvidwaw yypgrhnnsp nqdanlqprl rmdangrllp
      121 dttrfpsaag dngfkplady vhqkglkfgv hlmrgiprqa vadnvpvlgt tcranqvnns
      181 ttaawlnlmw glnmanqcaq tyldsmfqll aswgvdyvkv ddiaaptyrq sevegyrlai
      241 qrsgrpmvls lspgptslas gahvqanahm wrivndlwdn wssvdalfdq lrnwtpyrat
      301 gawpdadmip igrlskygpv gsprysnlts deqrtlmslw ainraplmwg gnlvenraae
      361 lalmtnaavi gvnqnstnnr qlyggsqqvw aadvpgsnhr yvalfnrnss aaqvsvnlad
      421 lgigsaavtd lwsgaalgtv tgtltrslpa hgsglyrlap dttvpvptay tvtarhsgkl
      481 ldvynnattd gadvvqwaan gqpnqrwrfq dagggyqtvi svhsgkcldv yggatatadg
      541 vrviqwscng gtnqqwrvqd vgsgyvqlva rhsgkclevl naattdgarl aqwtcgtgth
      601 qqwrrtsv
//
LOCUS       WP_357637538             594 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: type IV secretory system conjugative DNA transfer
            family protein [unclassified Nonomuraea].
ACCESSION   WP_357637538
VERSION     WP_357637538.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..594
                     /product="type IV secretory system conjugative DNA
                     transfer 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]"
                     /calculated_mol_wt=66836
     Region          136..531
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mphtgirpmp aaaamdgwql ltrhgmlvai aagllgfvla flvlrdrlrd prrrqglalw
       61 wrlrwrlypg kgfarrlelw rhyglpaark vaqqarpslr gwwtrylvrh sevavflgwa
      121 qgwifrfrty aafednllvl apqkegktah lagriidapg aviatsirdd ivtltaglra
      181 qrgrvhlfnp ervgeyastl rwspvdgced qatairraah mvaatqtggl sdegfwtsqa
      241 amvlaallha aalerltler vyawaldedq aplkildrqg rgtdraaalv rryhalhvrt
      301 rdsifltlrq alrcmedpat awavcpkpgq gldleevlrr retlymiage dahpaipvlf
      361 ttlvaeihhq arqlasqrps rrmdpptmiv ldeapeicpi tqlpgwlata agsglffiva
      421 gqshsqfrqr wgaegaktiw nntkakllag atsdpddlev msklcgeial pyweesvdgs
      481 gkrqrtrrwe tvpvlppeqa rrlptgralv lrrnatptiv rmeqvwrrad yrrwrakdgt
      541 vplprhptat ptpltlpepe ptrrswprlp rgrsdqeraa rpwhiasaet egdq
//
LOCUS       WP_357637562             541 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora parva].
ACCESSION   WP_357637562
VERSION     WP_357637562.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 541)
  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..541
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..541
                     /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=58045
     Region          9..267
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(9,33..34,67,72,77..80,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,75,91..94,98,100,137,139,
                     141..142,144,154..155,158,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,75,91..94,98,139,141..142,
                     144,154..155)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(20,98,100,137,139,141,158,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(154..162,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <182..399
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mhqlliagry rlldlvgtgg mgrvwlarde mlhrdvalke vvppswlaet eraelrlrtl
       61 reartaarln hpnvvrlydv vhdrdspwiv meyvpsrsvq qiisaegpls pprtarigla
      121 vlaalraaha agvlhrdvkp hnvlvaddgr vmltdfglat fdggdgtmtg pgtvlgspqf
      181 vaperaregv sdartdmwsl gatlyatveg qspyarssam atlsalatep pdpmrragpl
      241 rpvltgllqr dpwrrltale vepllrsaaa spdepaapar saavaavrsa grastphpve
      301 pappsdepat qtprpprrtv wrrrlialgg aaaallvagg vtlalvdrhd ertppsgagg
      361 gapthrpaaf acasspppsa tpvvsvsppa daryrlpegw twhddptgfr iaapvgwarw
      421 tegpvtcfrr ssgsrvlsve agparadpva ywkaeesrlt tsaalpgyrk vdisamdife
      481 ggavwecgwl nalgvavhsf rllintsagr sytvswltee fdwqvnaayl pmirqsftpt
      541 p
//
LOCUS       WP_357637617             690 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [unclassified Nonomuraea].
ACCESSION   WP_357637617
VERSION     WP_357637617.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 690)
  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..690
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..690
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=74910
     Region          30..689
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mavvsestfv grrhevaaar kalararllt ltgtggvgks rlalrvaatl rgafrdgiev
       61 vqlssleage llaptvaaal glrdcesdpm alledhlagr rmllvldnce hlleacarfa
      121 arvlreaprl rilttsrqrl gvygehvlpv pslpvpdqgl pphviarhda vrlfadraad
      181 aspgfrltre naadvamlar rldglplaie laaarlrtvp lerlarelde hlqavtspat
      241 lpprqrtlra tmewsyrlcs ageqrlwarl smfpagagle taeavcagge vdrsevldlv
      301 aglvdksvlv geqaeggvry rmldtirayg yerlageeer elrerylghh rdlvarnrih
      361 etvpdqpery rllrrelpnl raaiepcfgg pgppavglem aaalwsfwll sgsategryw
      421 lergldrvta pgrdratalw vysmlalrqg dpaaaaprle ecralvrreg fadvlpyavr
      481 tsgvaafstg epgrglalle eslalhraag dldgvvfnly yvaaygasqs pgraaecgee
      541 mlalceehga pvtrsyaqlv lgivlwnlgd lrraeelvge aagftrdidd kwcltqcvev
      601 lawaagahgd hgraarllga ahalwqsvda spirlsyhap whercaarar calgvrayea
      661 afregvrlgl dprlltgsgr qgahhasgrv
//
LOCUS       WP_357637626             340 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora parva].
ACCESSION   WP_357637626
VERSION     WP_357637626.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 340)
  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 340)
  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..340
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..340
                     /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=37169
     Region          46..325
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mttgpdrvat arallehlgl taadltgsnr pamptvaeyl pavvaaaspg trrtygsswr
       61 rmaaalgewr idavrasdie almrqaaada rprrnsrngr hagehliaaa rafynraiad
      121 gyltvvdspa hrvrkprrlp ntrraltpde ladinaaars ggndivldal llrlhtetac
      181 rrgdalalrl idldtdhali rlsekggtqr wqpitpmlaa rlsehaqarg avtptdallr
      241 yrngqpatyr rydllwarig rrlpwvaaqg itmhwlrhtt ltwverhfgy gvarayaght
      301 drrgpattty ikadlhavat alaaftgqph plavgesvlr
//
LOCUS       WP_357637734             411 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Nonomuraea].
ACCESSION   WP_357637734
VERSION     WP_357637734.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..411
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44965
     Region          1..411
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 msdveeavtr ahhdewarvv aaltrrfgdl diaeeaaaea fataverwra nglppnpgaw
       61 ltttanrkai drirrenkrd dkhkeaqmlh dnappgplga idddrlrlif icchpalave
      121 arvaltlrmv ggltvpeiar aflvrgttme qritrakaki kaaripyrmp saddlparvs
      181 gvlavlflvf negylatgpd tdpvrhdltt eairltrlir allpqdgeva gllalmllie
      241 arrparvsan gelvaldeqd rgawdgelva eghrlvrerl aaaaagvapg ryqilaaina
      301 vhtsardird tdwsqvlaly dqlvrldpsp iialnraiav aeldgpeval aivdrlaeal
      361 agyhayhatr adllrrlgqs qesraaydra ielagntget ayltrrrdql q
//
LOCUS       WP_357637761             420 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora parva].
ACCESSION   WP_357637761
VERSION     WP_357637761.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..420
                     /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=44945
     Region          23..414
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msitlaivga gargaayarl avatanatia avadpdparr itladefdvp derrfaswed
       61 laaqprlada vivatpdrah vepvvafaer gyaillekpm aplpeqaeri vaaavdndvl
      121 lavchvlryt pysqtlkrli dagrigaivs idhlepvgww hhahsyvrgn waveaesssm
      181 llakschdid wlghligrpv rrvssfggla hfrpenrpag atercvdcpv erscaysair
      241 iyerflgdpv heawplgvlt ddvsadgvrk aledgpygvc vyagrndvvd hqvvnleyeg
      301 gstvaftmta ftaldfrktr ifgtlgsieg dgrtlrvhdf ltddvetidl dpdgdasaad
      361 ghggadaali eafiaavttg drslvtsgpe esisshrvvw aaeqsratgs vvelipatpv
//
LOCUS       WP_357637803             838 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357637803
VERSION     WP_357637803.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 838)
  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..838
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..838
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=89395
     Region          2..838
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mllrshrlrr qltqealaer agissrsvae lergrgrspr prsleqlata ldldgeeree
       61 fiatghtlfw asrtgrtdrn pagesvpdag stcrqlpadv pdfvgrddel allasvldpg
      121 nhnarlavls gppgvgktal avhaghrfas wfpdgqlyat lrggtadpvd padvlaqwlr
      181 algvdgsalp vgvdaraalf rdrlavqrvl lvvddaggyr qveqllpakg vamvvtsrlp
      241 ltglpgvtsi dlrplsgpta vqllsqvage drvraepaaa delvsacggl plavriagar
      301 laarphwsve alnerlader rrlnelrhgd lavrpglhla hegltptaar afallgelgv
      361 psfpewavaa llgvdpaagt avleelldar llealgsdra gqpryrfhdi trlyarerre
      421 atisrsewta alarattgwl amarhaqdhl dclrfylddr dhpaavadqr aaaavadrpv
      481 ewfeaereal avlvsacaea glaatarcla gcsadfyelr gyyddwrram svaqaacqra
      541 ddrageatml rglgscliel ddpkaamsal nsaralaeei gdpagsalag keigfmlsli
      601 grtqeaeael rtaaerlgqa dlplaralal tslgfvlrer gdtdeavdvi tsalsiarsc
      661 garfteayal rglagalrac drprqaqaaa raaaaifeqv gdligtaqsl rvlgealahe
      721 phrleevqqa ltaaaaifre qghrwglalt elslgeiear qgnpqatarl rrslkywvde
      781 qvpalqartl valadaaeqq gdpatrellv qayeiyqale apaaadlacr lglpappa
//
LOCUS       WP_357637806             111 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Nonomuraea].
ACCESSION   WP_357637806
VERSION     WP_357637806.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=12284
     Region          6..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrrlpepare sltlapvlha lsdpvrlelv rrawdtpdst cavladgmdv pmstltnhwr
       61 imreaglism svdgrhrrir praddmsdrf pgllepilrl gaaespysgs l
//
LOCUS       WP_357637865             193 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta fold hydrolase [unclassified Nonomuraea].
ACCESSION   WP_357637865
VERSION     WP_357637865.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   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 193)
  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..193
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..193
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=20354
     Region          <115..187
                     /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 mrittavlla lasipvtsar hpaevdgvil tgessapdta afermgagir raaddprfag
       61 rglddgyltt rpglratwfy hrpgadpevi aadeaarttd vfppgdsytp psinrgiqvp
      121 vlivngehdr llagarasaa lhaqeapfyg praeletvvi pgaghvlngh rtaprwfaqa
      181 rawadrhvgg aar
//
LOCUS       WP_357637961             155 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357637961
VERSION     WP_357637961.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 155)
  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..155
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..155
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17479
     Region          8..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnvpfrvdnc siertldivg ekwtflvlre afsgvrrfad mqavtgaprq vlsarlarlv
       61 eegllrkepy repgqrqrde yrltekgrdl ypllvalmhw gdryladdeg ppvllthrdc
      121 gapielhfrc edghevtgpr dvtplpgaga rtrsa
//
LOCUS       WP_357637995             362 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357637995
VERSION     WP_357637995.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..362
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..362
                     /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=39306
     Region          25..355
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mpeagppvrr slflhapnrr rprvmlerml alvdddtpad gpegpvavle rrlagllgke
       61 salffpsgtm aqqtalrvha drrgrrtfaa hpqthldvwe eqgynavhgl tlrragdpye
      121 lmtakdlaaa vgeppaavvw elpqrdlggl lpewddlceq talvraagaa thldgarlwe
      181 aqsyyrrpfd eiaalfdtvy vslykslqgv rgavlasdaa tvkaaavwrq rlgggigdaw
      241 plalaalvhl dtladrmpay rehaiavaaa inadgaarah pdppqtplfh vhlpadrrav
      301 eqagqeilae hgvqlwgrvr sasepgrcaf evtvgename fspdevvali hdvlarvarr
      361 rp
//
LOCUS       WP_357638017             308 aa            linear   BCT 28-DEC-2024
DEFINITION  YihY/virulence factor BrkB family protein [Micromonospora parva].
ACCESSION   WP_357638017
VERSION     WP_357638017.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..308
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32561
     Region          16..255
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mnvigrieag idrwvsgarh rsslfdhvwr agvlygevla grlaaaiayy gffavfalal
       61 vafsvfgail edndevsaaa adflkenlpf ldaeqianss gtvgvvglvi lvftgigwve
      121 airssqrlmy rlnqqpgnlv vrrlvdlgvm igvfvllgvs vaavdalesl lrfllrstgs
      181 vglttisavl svlvntvlat alllavprlr msrsrlrpvv llvaigitll ntvgryyvvr
      241 ternpaytvv agavglllyl yllnqlvlfg aallatsttg rvvdlaetpt ppkdvdegid
      301 pgtpggag
//
LOCUS       WP_357638023             476 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357638023
VERSION     WP_357638023.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 476)
  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..476
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=52634
     Region          134..370
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlrrygrvat llallvvqvp liavslvmlv lsvalgmvfl fppqvrmvrr vaelnrrlir
       61 swtglaieap ylpkppppvp qadgfyrsdr tlyktpripa wndrwkwlit dpatwrddcw
      121 llldplmklt lapvflllpa qglrlyalws dlllgatans rlanqvthlr rtrnlatdsq
      181 aaemrrierd lhdgtqarlv aigmtlgave qlvdqdpsaa kallakarea ssetltelrr
      241 virgihppvl aerglgdavr alamdsplkv svdvdlphrp dapveaaayf avsellsnaa
      301 rhgeartaav dissreadlr itvtddgmgg adptkgsgla gierrlaafd gvlalnsppg
      361 gpttvtmhlp kvlpqhwasd lpklprhkmi ivgllwataw cptfpqgfva aifklidfde
      421 ktwflalhlp epwqwptiia mialgltmhi mairipavhn rerwmieatp tkpwcp
//
LOCUS       WP_357638044             197 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora parva].
ACCESSION   WP_357638044
VERSION     WP_357638044.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 197)
  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..197
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..197
                     /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=21441
     Region          5..195
                     /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 mshrppnpsg rvtsakivia ggfgvgrttl vgsvseitpl tteaimtsag vgvddtrqvp
       61 gkttttvamd fgrisidrdl ilylfgtpgq trfwfmwdel vrgaigavvl vdtrrladcf
      121 aaidffehrr lpylvaincf dgmqyhdpqd vrdalaissd vpvvacdarn restkhvlis
      181 lveyvltmrr travapa
//
LOCUS       WP_357638047             314 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357638047
VERSION     WP_357638047.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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..314
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..314
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33636
     Region          1..313
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mderveavlr dgrapgfhgl vvmrggevvl erygagpdhr lgeplghvtf grdtlhdlrs
       61 vsksvvally gialgdglvp epgagltaqf peyrdlaedp gkahltieha ltmtlgldwn
      121 edapytspln deiamelapd ryryvlerpv aeeagkrwry cggatallgg iiargtgrpv
      181 eeyaaealfg plgitdfawt kggdgvasaa aglrlrpvdl aavgqlvldg grgivpegwl
      241 revlrsrvpi dgsftygyhw yvieeerrrl qgignggqll vvvpgeelvv avtagdydqd
      301 stgsreivaa vldm
//
LOCUS       WP_357637624              84 aa            linear   BCT 28-DEC-2024
DEFINITION  GntR family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357637624
VERSION     WP_357637624.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 84)
  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 84)
  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 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   4  (residues 1 to 84)
  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 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..84
                     /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=9304
     Region          6..>75
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtidhegptp lyrqlaellr tqiadgtlpp nrpipteqrl mhehelgrdt vrkaiailre
       61 eglviairgr gtfvatledp gtnr
//
LOCUS       WP_357638084             127 aa            linear   BCT 28-DEC-2024
DEFINITION  group I truncated hemoglobin [Nonomuraea wenchangensis].
ACCESSION   WP_357638084
VERSION     WP_357638084.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 127)
  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 127)
  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 127)
  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 127)
  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 127)
  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..127
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..127
                     /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=13606
     Region          9..119
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(11,16..17,20..21,24,54..55,58,87,90,94,97,108,111)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(25,34,37..38,41,45..46,49..50,52..54,56,64,66..69,
                     72..73,76,78,82..83,86,111,114,118)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(27,30..31,89,92,96..98)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mtispsyydq vggapavrdv vdlfyvrvld daalkpyfag idmprlkrhm vvllcsvlgg
       61 pdpyegrdla eahrgmgita dhyakvgeil lsvlqgagvg deilrhvelt lnkvessiva
      121 epvetad
//
LOCUS       WP_357638088             583 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora parva].
ACCESSION   WP_357638088
VERSION     WP_357638088.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 583)
  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 583)
  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..583
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..583
                     /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=61170
     Region          1..451
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          516..582
                     /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(539,548..550,557)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            549
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvirac rdaglgsvav yadsdrdalh atladeayal ggdsatetyl
       61 ridklldvaa ragadavhpg ygflsenadf aqavidaglt wvgptpqair dlgdkvtarh
      121 iaqragaplv pgtpdpvgsp devmafavdh glpvaikaaf ggggrglkva rtmeeipqlf
      181 esatreavaa fgrgecfver yldqprhvea qvladqhgnv ivvgtrdcsl qrrhqklvee
      241 apapfltdaq raqihdsaka icreagyhga gtveylvgvd gtisflevnt rlqvehpvte
      301 etagidlvre qfriadgekl ritedptprg haiefringe dpgrnflpap gtvtalrlps
      361 gpgvrvdtgi sagdviggnf dsllakviit getrtealer arraldemvl dgmatalpfh
      421 rlvvrdeaft aepftvhtrw ietefhntvp pftaaagtad apaerdtvvv evggkrlevs
      481 lpagfggstt taapasrkpt rrgggakaga pvggdtltsp mqgtivkiav adgdtvaegd
      541 lvvvleamkm eqplhahkag tvsglsaevg avitagapic tia
//
LOCUS       WP_357638115             372 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea wenchangensis].
ACCESSION   WP_357638115
VERSION     WP_357638115.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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 372)
  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 372)
  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..372
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..372
                     /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=41668
     Region          195..357
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 msvepvrrrs dltafirfph lihrpadpwi ppldrerraf ldprrnpffd yaeaglflar
       61 rggrvagria avrnprhnel hgadegffgm fecvddpeva ralfeaaagw lagrglrtml
      121 gpvslstnhe cgllvdsfdq apavlmpynp ayyprlleac gcvkakdlwa weltwdqvpg
      181 eflpladala egspytirpl rladldtaas hiwaifnqvw agnwgfvpat ekefrhlvrt
      241 lkpilrpelt lvaerdgetv galiglpdag pafkaargrl tplgllrfvr alrhvdaarl
      301 illgvraenr ddkvvlelga ramrsarelg irrvefswil ednvaangva ryigarrsks
      361 yriyrrdcep pr
//
LOCUS       WP_357638164             383 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357638164
VERSION     WP_357638164.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=41368
     Region          19..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 mngsitiaga glaglalarv lhvhgiastv yeaeaspsgr tqggqldihd fngqvalqqc
       61 qlmdefhsiv nmgaeamrfl npdgelvgei pddgelsnpe vlrgelrril ieslphgtiq
      121 wghkiasvtp gdghrphvir fangssvste vligadgaws rvraslngam peylgtlwve
      181 tflhdveknh pqsaalvgsg amlamkpgrg ifghreandv ihtyvvlkkp lewmqsvdfs
      241 dreralrlva eqlgqgwape llelvtrget tpvarpiwgl plehtwdrvp gimligdaah
      301 ltppdgdgan walydgaqla qaiaatpadi dtafntfaeq mlprsaasst egyqsfeqtf
      361 gynapanlrd mmnrtktygh qhq
//
LOCUS       WP_357638175             332 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357638175
VERSION     WP_357638175.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 332)
  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 332)
  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 332)
  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 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   5  (residues 1 to 332)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..332
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..332
                     /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=35858
     Region          259..324
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlkihfsged ilrtrvapaa dpvwelvlsl hvlrgrtrdp ltanwrrsvs walrqdaase
       61 qlsllfalnp prgyfpdflt pyasvegfea gldalrrtpi emlhrdlsvl atenqlpssa
      121 talargevsa lhhladsmqq yrslaispyw griqaavaad rarraralld ggveglltsf
      181 rpamrwdsgv leirsyphsr elhldgrgll lvpsffcaai pvalldpalp pvlvyqvdrl
      241 gglvttdang afapgagres laallgrtra avlqasdegc ttgevarqln ispaaasqha
      301 tvlrnagllv shrernsvlh tltplgraml da
//
LOCUS       WP_357638240             411 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357638240
VERSION     WP_357638240.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 411)
  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..411
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..411
                     /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=43457
     Region          21..406
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mpttfviagg glaaakaaea lrkegfdgei vlagrephlp yerpplskgy lqgaderqki
       61 fvhdadwyrd havdlrtgvt vtdidpaahq vtlsdgerlr ydklllatga tprrltvpgh
      121 dhgnvlylrt vddcdrlrat lsatqsaagr iavigagwig letaaaaraa gvevtvieqe
      181 rqpllgalgp eigavfaalh rdhgvdlrlg arlaeitetg vrladgthid aaavvagiga
      241 vpdtelaaaa gltidngvkt tadlrtsdpd ifaagdvana yhprlgrhvr vehwanalnq
      301 pavaaramlg reavydeppy fytdqydlgm eylghvppgv srdvvirgev agreflafwl
      361 gdddtvlaam nvniwdqgdq lkalvlsgsp vdrgaladpa vpldglvrsg g
//
LOCUS       WP_357638300             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357638300
VERSION     WP_357638300.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..212
                     /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=23153
     Region          11..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msdvkrtnkr aekaketrrr ilaaalelfi qdgygatnlq diadkagvav qtiyfvfgnk
       61 rallkelvdv tiagddepla tmerpwytga lasptaqdll layvggttsv mervapitkv
      121 leaaiasdpe vaalwphdvd pryvvhhgaa kalagkpgar aevsveeaad llygllspel
      181 ylllvkergw prerwerwvg etlrsqlcvt ea
//
LOCUS       WP_357638374             348 aa            linear   BCT 28-DEC-2024
DEFINITION  bile acid:sodium symporter family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357638374
VERSION     WP_357638374.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001259
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..348
                     /product="bile acid:sodium symporter family protein"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35387
     Region          11..338
                     /region_name="YfeH"
                     /note="Predicted Na+-dependent transporter YfeH [General
                     function prediction only]; COG0385"
                     /db_xref="CDD:440154"
ORIGIN      
        1 minlvvgavq rrllalmivc yllaavaprp gealramalg sggpvtvpmv llavmlstag
       61 lgvrvrdlra vvgrplrlas gvamnallpv vllpvaamcl rawpdsaeve clavglllvl
      121 ampiaggaas wgqnaggnvp lvvamvvgst llspvtvpwg ltvsaalvgp ggarslddta
      181 rldrlagtag agafalaliv lpslvgilar amlgerraar iapvvklvni vnilllcyln
      241 asgalgqals ppdpdflala vgvagavccl sflvgrwmsr wtrcdtpdgi sltfatgmnn
      301 tsaaavlats wfahrpqvlv pilaysllqk laaslfgtqp parpaals
//
LOCUS       WP_357638449             158 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            parva].
ACCESSION   WP_357638449
VERSION     WP_357638449.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..158
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17743
     Region          7..112
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrpaaldwsv enctiarame ilgerwtlvv lrevftgvrr fddmrvrtgi prqvltnrla
       61 slveqgvlsr epyrepgsrl rheyrltekg ldlwpvlvav lgwgdrylad adgpplsvth
      121 rdcgaevrae lrcadghdvg rprdvvprpg pgarrrtp
//
LOCUS       WP_357638450             393 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357638450
VERSION     WP_357638450.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..393
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=41106
     Region          2..357
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mkhrivvlga gyagantagr lakrlhrddv eitlvngdpe fvervrmhql asgqdlrprp
       61 lrdvfagtgv qvrtarvtav dvegktvelg getlaydtlv yalgstiada gvpgvaehah
      121 nvagkqaalr lrarlsevrs gatvlvvggg ltgieaatei aeahpeleva iaargrvggw
      181 lsdkaqrhlr galdrlgitv heqvditrve angvvtgags eiraevtvwt agftvhpiaa
      241 attlkvsdsg rivvdagmrs vshpdvyavg daayaegagg splrmscasa npmawlaadv
      301 iaarltgrkg pettigysvq cislgrrdgi iqrvtpddqv tstvftgrta arikelicas
      361 aawsishptl mmpsrrrhla vtgaagtrpl trs
//
LOCUS       WP_357638481             219 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357638481
VERSION     WP_357638481.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=23504
     Region          4..219
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mrnvartslv daaidelrre iaggtwpvgt kipsesqlaq slgmsrlsvr eavrvlahag
       61 llhtrqgdgt yvtatdesrv alrrrldtaa atdiidvrrg ldlvaarlaa grrtdedlla
      121 lreilarrad aardgdldgf adadvefhvr vadaahnall adlyrgmsda lrdsvrdqee
      181 aaltpdnshe ellgaiedgd pgravavsia ildqqardl
//
LOCUS       WP_357638492             420 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357638492
VERSION     WP_357638492.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 420)
  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..420
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..420
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45172
     Region          1..>88
                     /region_name="PRK13355"
                     /note="bifunctional HTH-domain containing
                     protein/aminotransferase; Provisional"
                     /db_xref="CDD:237361"
     Region          143..204
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          228..393
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manfaerldl altkrgftga qvastlteag ipitrayvsq lrtgkqtnpt lqvlralasc
       61 lqvsvgwlvg ddglesgave dlqvraatlg lsasglseas lsvlrgvvdl arraeglpde
      121 pgpepadgip eaaaplsgpq rralgrrlhg lrlaadltve qvetalgkga apitaieegr
      181 lapppitver lltlfgvgsp pireyvlsla rgereaawyd ahsipvwlat tyaleqratl
      241 irtfhtqfvp pllqtedyar aaitvmgpat lgqptveeal alvtarqeal nresgvvlwa
      301 iidesvllrs ivgrhiqlrq letlmdqakr pnvslhvvpm ddpayvprtg pftlwrfaea
      361 yeadvacahg ierdelltdn gaveayhqaf tklsvttttr eetvellsah cerlsrslgk
//
LOCUS       WP_357638516             708 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357638516
VERSION     WP_357638516.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 708)
  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..708
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..708
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=78171
     Region          12..707
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(497..498,501..502,504,535,538..539,542..543,
                     545..546,569,572,579,582..583,586)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          497..521
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          533..563
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          568..602
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrlrmatptg wrregnlpae ltsfvgrtrl lanlkrhlge srlvtvtgig gvgksrtvlr
       61 lahqvraqyp dgvwfadlar lqdagmvkht issalriadq ssraesesls ewvgerdmll
      121 iidtcehvvq gcaelvhell eaapnlkvla tsrqslhlpy ehvvpvpplq vpgddpaanl
      181 ftnesvqlfa aragasvpdf qldesnigtv aelcrrldgi plaielaavr lralsvdqil
      241 glladrfsll agasrtalpr hqtlraaigw shelcepaer llwarlsvfa gdfeldaarf
      301 vcsdgrlpse ditdlvtglv eksvllirsn hagvryklid tlaeygdewl dklgqreqmr
      361 qrhleyylsl aqrsedawsg prqiywfvrm rqehdnvrva lehalktpgk eilaltllss
      421 lwfmwvccgf aregrlyler alqanpefsk erckalwvls yvksaqgdsa gaqssaeecs
      481 teavrvgdsr avilaskmqg taallqgdlq kasallgvai efntdnkeln pgllpaivel
      541 slvlcsqgel yeaesllqdc lqvcrergel wvsshaqwal agtrlatgra dealhnvrea
      601 lrikrhfhdt lgmllaleta arifaalnhp amatqllgal qqnwktaglp qlgapwmtdd
      661 hdecirackr elgeltykdt feegarrdld easalalgel datdesrs
//
LOCUS       WP_357638555             390 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357638555
VERSION     WP_357638555.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 390)
  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..390
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..390
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43118
     Region          1..68
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mlgerlqsyr klrglsqrel aarsgvalsl irkveqgerk svrietvraw ataldvttta
       61 llgpvpeteq qngngdrlap lrqalqgvpa dvedvptadg lrsaiasavr lyhddeyael
      121 ttilpvlvke aqtlveqggp ealavrarvl qlvgslatqt rafdvaeial egavtdaiet
      181 gdrieaasav itscwlllrq rrldearsra vdwadeiepr msratstels awgwlllrgs
      241 aaairdnrpd eademmrlal sgavrmgreh gsyheyfttf gpatvqmkrv enaiiehqpe
      301 ralrlareip pglrptsdnr nrhlldvana hvmlreydka ldilsqlare apawlpnqry
      361 akdmlqtivg rrrtltpemr klanavglep
//
LOCUS       WP_357638571             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357638571
VERSION     WP_357638571.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32551
     Region          10..291
                     /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 mfdgfdvfdi etpgatihgr rggsgppvll lhgipethlm whkvaprlae kytvvatdlr
       61 gwgdsgtpps tsdhepysmr aiardqiemm rilgyqqfrl vghdrgarca yrlaldepda
      121 vtrlavmdvv pigdvynrad rafslsywvw sflaapapvp eqfikaapsv lvdfmldtwp
      181 evkdafppev raayvkqfsd pakahaicee fraaatvdyq qdeadrgnrk iacpvlflws
      241 qrgqvaklyd dpmaiwrewa ddvrgepvpv ghfipeeapd etsrqlldfl g
//
LOCUS       WP_357638584             393 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357638584
VERSION     WP_357638584.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   ter Beek,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 393)
  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 393)
  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..393
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..393
                     /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=39175
     Region          56..392
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtttqrtsgp sdasdaaass aasaagspaa asaspgaagl sstavpsges irlagrsllr
       61 igpvsllirr ravlvaavlt vllllavvls lslgtpyvap advlralsga gtpydlvvfd
      121 lrlprvvlaa vagaafgvag tliqsvarnp laspdvigit qgaglaatva ltsgmaavlv
      181 aptalvggll aaallfalga rhglaaqrfv lagvavafgf raltevvmlt adpidglraq
      241 iwligtlagk gwteaawiag tllvllpvla wagwalnsta ldddtargvg lrpvarrigl
      301 agtgvlvaam vtaqvgavdf valvapqvar rlvraerppl vcaallgall lvladlagrr
      361 lfaptqlpag vltaaiggpy liflllrgrr rss
//
LOCUS       WP_357638602             345 aa            linear   BCT 28-DEC-2024
DEFINITION  MraY family glycosyltransferase [Micromonospora parva].
ACCESSION   WP_357638602
VERSION     WP_357638602.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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..345
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..345
                     /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=35503
     Region          33..274
                     /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            86..87
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133464"
     Site            197..200
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133464"
     Site            order(245,256..259)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133464"
ORIGIN      
        1 mlsvplaggi vlalvvgtll qplvlrllra aavldipser sshstpiprg ggvgvaaaag
       61 lalllnehar siavpllffa aiglledlrg vpirsrlllq vlaglgtavi lvpggqawyv
      121 hvllvlalaa wvtsyvnafn fmdgingisa vhailgglay avlgvltdlp lliaagslia
      181 aasltflpwn awvakvflgd vgsyalggal stiaayaivr gtppeaavap lalyladtgw
      241 tllrriskge awyrphrnha yqrltdggws hqrvtattav vgatvagclv aasfsgpvtr
      301 valdatalai laaylaapaw ltaqraqpsp egrtihartv sstsr
//
LOCUS       WP_357638611             221 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357638611
VERSION     WP_357638611.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=23877
     Region          <1..197
                     /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 mhivimgcgr vgstlahile dnghsvaiid rdpqafrrlr agfrgrrvtg vgfdrdvltd
       61 agvesaaafv avssgdnsni isarvaretf gvdnvvariy dprraevyqr lgiptvatvr
      121 wtadqimrri lpegaeplwr dptgtvvlae vavnpswigt rvidvekrvg vraafinrmg
      181 ealtitrdsv vqegdvlhvi aaendmdrin kalagapegd d
//
LOCUS       WP_357638613             404 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357638613
VERSION     WP_357638613.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=42746
     Region          171..403
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtppsktdpt apeagptvtp adpagvavev ggragplrrl rtaskldkvr wvivystdlv
       61 tllsliglyt lylqwqagml pvlaagaavl lvvffviclr pfrvavrggp rptkllavsg
      121 gialllavva vvwalpswla altpfvrkrt ialastgliv alaligslsg arladvlalv
      181 lvmtfltvls vvatwanlrl wrlaqeaheg eealarlavs eerlrfardl ndllgqsltd
      241 vaaraghaee rlpldpeaaa aemfevrdla rrslrevrav vqnyraldld evlasvravl
      301 eaagvrcavr adtaalspes rtllatvvre gttnvlkhsr aerceirien gvlemsndgv
      361 sgpvgrhapn glaglaervr aaggsleaap tpegryllra avpa
//
LOCUS       WP_357638635             481 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357638635
VERSION     WP_357638635.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=51122
     Region          142..455
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrrlvisyl llmvlvlial etplaatmas retervradr ladatrfasl agpalrdggp
       61 gpieseltsy ddlysisaai vdrdrntpvs sprwqptpgt atvldvalsg qqtsapesvw
      121 pwttdsvvva vpindggevl gavvivtpad pirravvaww lllalaglla vlacvltafg
      181 lagwvlrpvt eldavtheia egdrgarvqh rlgppelrrl aasfnhmadv vsdvmdrqra
      241 fvahashqlr npltalrlrv eelgpsltde dgrsehrlal eetdrlalvl dalltlarae
      301 reenervtvd aaavaasrva awaplarhrs valrlattda payaqtvpta vdqaldalid
      361 navkfsgagg avtvtvarrd ggvalevrds gpgmtesqlg qaterfwrap daqnvdgagl
      421 gltiaavlvd asdgrltmrp gesrglvaal wfpapvlsve paeeepaqee patdlrpspa
      481 r
//
LOCUS       WP_357638664             937 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357638664
VERSION     WP_357638664.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 937)
  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 937)
  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 937)
  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 937)
  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..937
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..937
                     /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=101856
     Region          1..246
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          132..936
                     /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"
     Site            order(727,730..731,734..735,737,767,770..771,774..775,
                     777..778,807,810..811,814..815,818)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /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"
     Region          845..875
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfellgpfr vyhdgrsvpl gsvkqrllla tlllrpnevv gtdeltamlw gddeppsaaa
       61 nlrtyvrglr rslgggatwd gitaaaggyl lrvgpderdl dlfdaaaarg realaaadld
      121 raeaelsdal rlwrgaplsd lplrprlarr vaqleerrll veedhaeaml algasadvvh
      181 rlrglldrhp lrqrawgqlm vglyrigdva galdayrqar qklaeetgld papelvalyd
      241 dilhhrpglt aqpptgpdrp asgtavgplh qrpeqlprav pefvgrsvel asldrllsgg
      301 aelptsvtis vvsgmagvgk ttlalhwahr vadrfpdgql yvnlrgydev glvspadals
      361 gflealgvph aripsdtear tglyrsllas rrmllvldna rdsaqvrall pgagrcmvvv
      421 tsrdrlgglv asecatpltl dvltaeesms llarrlgdnr lasasgavad iieaagrlpl
      481 alsivaaraa thptfplsai aaelhwaear ldaladgdvr rvfswsflal gadaarlftl
      541 lglhpgpdlt aaaasalagv patavtpilr eltrlhllte htpgrfafhd llrayaaela
      601 qssergdehv aarqrlydhy lhaaypaall lqpqwpaiep vaplpvparr pvtdhdgala
      661 wftvehrvlv rvvrqaaqng feayawqiaw alttfsaprg lwqdqlaiqs valtaaekid
      721 dlagqavanr llsralirlg drttaehrlk ralelherlg dpigqaqtlh nycelcyldg
      781 rldealthgr ealrlyrlvg nhageartln aigwllattg dyvqaiascr ealdqqrrtd
      841 drngqaatld slgfaydrlg erdravdcye qaihlfrasa dryheaetli rlgdtregmg
      901 drnaaaaawr laariyedvr dpaaeevrrr lerlalc
//
LOCUS       WP_357638721             292 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357638721
VERSION     WP_357638721.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 292)
  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..292
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32569
     Region          25..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(30,34,59)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(33,58)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(40..41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          111..289
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msaesaegkl lsyapgsptv lrillgtqlr rlrtqkgisr edagysiras hakisrlelg
       61 qvsfkqrdva dlltlygvtd pgerqqlldl akqanapgww hkygdvlpaw fevyiglega
      121 assirtyenq fvpgllqtag yaravielah ekatraeldr rvalrttrqr rlesgltlwa
      181 videavvrrt lggpdtmraq iahlldvtae rnitvqvmpf drgghaaagg pfsilrfper
      241 elpdvvymeq ltsalyldkp adsdhymevm drlsiqaetp ketrrflerl is
//
LOCUS       WP_357638731             189 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora parva].
ACCESSION   WP_357638731
VERSION     WP_357638731.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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 189)
  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 189)
  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..189
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..189
                     /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=20427
     Region          14..187
                     /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 migqvavrrf paltvstprt evrqltaada aaageifadk ltrrwlplpg dsgpidglaw
       61 ctdlarqrrd sgegdhyavv rreddqvvgs lwtrrtdwga rlteisyama asargfgfaa
      121 eavdavaial ilehgfqrve lrvapgnlas rrvaekagfs yegllrnagf vsggrvdlel
      181 wsfvaadlr
//
LOCUS       WP_357638847             273 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357638847
VERSION     WP_357638847.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=28221
     Region          1..271
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mippvtwlyv pgdrperfak aaasgadvvi idledavvpa rkdearanav aylrerpaag
       61 aavhvrvndl ttargradle avgdladgvr lpkvedpavl dgiadgrayp llesaagilr
      121 aaavaahpav agialgeqdl aaelsitgea amdhlrlqav laaaaaglpp vpmsvypdir
      181 dedglaascl agramglfgr taihprqipv irrafrpgee evaraeevve aaeragragl
      241 gavalpdgrf vdapvlarar rtvalarhla aev
//
LOCUS       WP_357638879             298 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora parva].
ACCESSION   WP_357638879
VERSION     WP_357638879.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..298
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..298
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30844
     Region          40..276
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mgagrllavl vtallagcap atavaggatd pvparraleg syavgvrtlt ldprsarplp
       61 vtiwyptstg qvaagrfpvv iyshglgsrp elhaglttrw aaagfvvaap ayphtrqgaa
      121 hftradvrhq padawrlirh lgrldrnrad plaghldlts iaaaghsagg fttsgmfseg
      181 hqtrlragiv iaggglpgsf agpaapvlfv hgtadpvvpv tvgraayart pgpaaflsll
      241 dqdhgayltp ghpgfapvla tttdflrwtl ygdqvaaarl rtdahspnlt ryesrpah
//
LOCUS       WP_357638883             659 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357638883
VERSION     WP_357638883.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 659)
  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 659)
  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 659)
  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..659
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..659
                     /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=71308
     Region          3..658
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mgtldeeray vercraglrr mlegardnvi vgesvagdry saerlgrhlk slakelseep
       61 egppffgrld fgddsaehrg rayhigrrhi tgehggppvv idwrapvara fyragardpq
      121 gvavrrrfgw sgmtltsyed erldrgeegg grllaaeier prvgpmrdiv atiqpeqddl
      181 vragldvsvc vqgapgtgkt avglhraayl lyahrrrler ggvlvlgpnr aflgyisavl
      241 palgevdveq ttlerllatv pvraadseea aavkhdarma evlrralygr irkpvepvtv
      301 adgsyrwrvr edelrrivdd arraalpygv grervhartl davrrqaear gvsataawsr
      361 rtsralapal dalwppvkpe evlyevlsgp addgadparg vltgaeraai twarlprgpr
      421 sarwtaadvv lldeiaglve rprgyghviv deaqdlspme cravarrseh gsltvlgdla
      481 qgttpwaaas wpermallgk pegevvaltt gfrvpgavve langllesle advpptrsyr
      541 sdgrvrvtav eelgkgvvaa vreaygfegs igviaadpga aelaaalrde gfelggrlsv
      601 veaslvkgle ydhvvvaepa aiaegerrgl nrlyvaltra vsrldvvhar plppqlarp
//
LOCUS       WP_357638885             204 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357638885
VERSION     WP_357638885.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..204
                     /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=22402
     Region          8..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtglrelqrq rvreaisaaa iglflrrgfd evpvteiaaa agvskptlfk yfpakedlvl
       61 hriadheges arvvraraeg etplealrrh fldglarrdp vtglndhpev vafhrmvfst
      121 pslqarmfqq isrderalad alaeqggtdd ltaallaaqv latqrvlasr iwqrlaegrp
      181 laevepeavd aanrafsllt indy
//
LOCUS       WP_357638923             392 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357638923
VERSION     WP_357638923.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=40299
     Region          175..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpavatpavp pptldnpagg alglifttlp allrltcglf gaavavsvqt ppveqavllp
       61 avgvltgwsl wyahralrhg igpalvagdv avtasacllm pvlvapevlp gegswiavla
      121 sttvintqat alarwsipag llvivtyvtg aqaagnptea rahaatllaq tactammagv
      181 mrrrigradr afaahqrltr ealvaraare aerqqnrdlh dtvlgtltmv glgavagpst
      241 vfrdrcaadl rtlvslsdvg pvagdgpvpl dgrlrsvver lpelavrldl tscavpvgva
      301 daisesayaa lsnvvrhapg aeatlrlvrd aigvvvevad dgpgfdlatv pphryglres
      361 irgrmatvgg raevhsavgm gtrirlewpg vg
//
LOCUS       WP_357638929             270 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Nonomuraea wenchangensis].
ACCESSION   WP_357638929
VERSION     WP_357638929.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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 270)
  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..270
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         <1..270
                     /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          <58..260
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 laaqpyddrc lswqhdartv siwttagrlk gvtftgsarq lallaahrrg esdlicrdgm
       61 wflhatveva drppsepdgf vgvdlgiani attsdgvrhr gkglnavrhr hrrlrrrlqa
      121 krtksakrll krrrraearf aanvnhiiak sivteaertg rgialedlqg irervrlrkp
      181 qrvtlhswsf hqlgafiayk avragvavmv vdaaytsqqc shcghvdkrn rpdqatfmct
      241 scgfaehadv naarniasrg etgwavshaa
//
LOCUS       WP_357638940             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            parva].
ACCESSION   WP_357638940
VERSION     WP_357638940.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..416
                     /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=44718
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..371
                     /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"
ORIGIN      
        1 mveelaqada avaacvdaaa walseqdlia aldaahrleq rlaavklavi reldgrgtat
       61 ahrasstvvw lrerlrltia aarrlvdlaa vldtgnpgvr haladghitv dqarviadti
      121 dtahtvagpe aadkslgvlv ewagqfdptl lrklstrild hvapdiadaa aeaaldaear
      181 ratrdrhltl stladgrlrl tatldtetag llratidpls apsgpdders pgqrrhdalr
      241 dvcrlalrtg elpenggdpa qivvttsydg ltgqlgggtl dtglrltpea vrrlacdaai
      301 lpavlngagq vldlgrqrrl itgplrralv lrdrgcafpg cdrpprwcda hhihhwangg
      361 ttsldnavll cghhhrhihh sdwtvrlaad ghpeftppaw ldpeqlprrn hyhrrt
//
LOCUS       WP_357638991             262 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357638991
VERSION     WP_357638991.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25840
     Region          4..243
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrcdglvavv tgggsgigla cvrafaaaga rvgvldlels glpedpgvlg vradvadras
       61 lstavaavae afggidilvn nagisavgtv eenddeqwsr vldvnvsgva rtsavalpyl
      121 rrsssaaivn issiaattgl pkralysask gavhaltlam aadlvtdgvr vncvapgtvd
      181 tpwvarllag aadptaekrh lasrqptgrl vtadevaaav vylaspatgs vtgsslpvdg
      241 gmsglrlpap arpaadpaes ga
//
LOCUS       WP_357639038             588 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357639038
VERSION     WP_357639038.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 588)
  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 588)
  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..588
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..588
                     /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=62498
     Region          35..564
                     /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 mqtkklalag taaltalala alpaqagaaq agptktvtvt vmgtsdlhsn vlnwdyfkda
       61 ayadsagnsv glakvstlvn tiraergpgh tllfdsgdti qgtplayyya kiepitetga
      121 thpmakamna igydavtlgn hefnyglpll atwikqmkap vlganavhak sglpayepfv
      181 iktmkvqgek pikvgvlglt npgvaiwdka nvegklrftd lvdsakkwvp virglgadvv
      241 vvtahagdng mssyggdlpv enasalvaeq vpgidavlfg hahndvpqkf vtnkvtgqqv
      301 lltepgrwgq rlsrldfqla kqrgkwvvtg kssatintnt vaedpkivsl lkpqhdttvg
      361 yvnkvvaksa qelsaaespy kdtpildyiq qvqtetvrqa lpdntlpvls iaapfsrsav
      421 fpagdvrvrd vaglyvydnt llaikltgaq ikdyleysak yfnqlapgap vdvatltnas
      481 gtpdynydql sgvsydidvs kpvgqrianl tydgqplpad kefvvainny rqsggggfph
      541 vttapvlyna qveirqalie yatakgtidp adfaapnwkl tregvpvf
//
LOCUS       WP_357639053             349 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357639053
VERSION     WP_357639053.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..349
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37340
     Region          67..345
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mralaalaaa talllscaap asadpdwsfa qeseppraep ttggyapgqr alpgparvva
       61 errldtrtld llvsspavgk ltpvrlllpr gwsrtagrtw pvlyllhgga ddytswtrmt
      121 dvatytanld aivvmpeagr agnysdwhna grggppkwat fhtsevrrll esgyragtrr
      181 avaglsmgay gaikyaaanp gmfrfagays gimatrlpgi pavimnaqas ekqdplalwg
      241 dpkrdakvwa andplalaag lrgtslyvss gstslngpld lpgaawnpah lgepisayta
      301 ralserlkrl girhtlhlyg dgthtwpywt refkrsypmi vralglrrg
//
LOCUS       WP_357639076             130 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Micromonospora parva].
ACCESSION   WP_357639076
VERSION     WP_357639076.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..130
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..130
                     /product="YybH family protein"
                     /calculated_mol_wt=14811
     Region          2..108
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mdrthvedwl aayerlwrtp gtdglvglft edasyqqgpy wtpvvglpai armwekqrkg
       61 pdevfqmtte ivavegdtav srqevrygdp veqeyrdlwv irfagdgrcr sfeewpfwpg
      121 qqpasspdgs
//
LOCUS       WP_357639074             200 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Micromonospora parva].
ACCESSION   WP_357639074
VERSION     WP_357639074.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 200)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..200
                     /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=21650
     Region          1..175
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 metdpvrqay tsvaelyiem fgtkeqvhpd dlalierhlg drqgpvldlg cgpghltgyl
       61 ralgvdaagi dlvpefiaha raahpdvefr lgslahldva dgsvdgilaw yslihlppqe
      121 ldgvltefhr alvpagrlvl gtfsadevga fdhkvvtayr wpldalserl tqagfrever
      181 lpragddqhr phaamaavvv
//
LOCUS       WP_357639092             287 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Micromonospora
            parva].
ACCESSION   WP_357639092
VERSION     WP_357639092.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..287
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..287
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30228
     Region          60..130
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mrrqwlsvgl aalcvavgvp ahawaatsgt taqrtvttav rpvvdmeatv laaqidprrp
       61 dntltpgaks svlaveqalq aqgllnaqwv dgyfgtvtis ayaayqrtlg ytglaanglp
      121 gttsltklgq nrytvvntig pgakvprdgy vvnartqaml aqaqrllgyp lvldqgsynp
      181 ggdptsagth dgggvvdiav tgmtaarrta varalrqvgf aawvrnpdqg dwpwhihata
      241 indtdlssqa qhqvgdyylg lnglanqgpd dgpqvpirtw eqyqrgq
//
LOCUS       WP_357639121             669 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357639121
VERSION     WP_357639121.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 669)
  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 669)
  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 669)
  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..669
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..669
                     /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=72236
     Region          13..668
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpthqlapdi padvlaaeqr hlaesraalt amrahaqsls adaagdwvsq qilqslldqr
       61 vaaladhpdt plffgrldre sgddlpgtiy vgrrhvhdgh skplvidwra pvsrafyqas
      121 paepmgvvrr rrfgyhggtl tayedeplge ggvelgpski lteeierprt gpmrdivati
      181 qpdqdeivrs glaqtvcvqg apgtgktavg lhraayllft hrerlarsgv mivgpnrafl
      241 syissvlpal gevkvdqttv agllgehaap edplvaavkg darmaavler alwlhitkpe
      301 eglvftkgay ryrvadhevr eivaslrgtt rylpgraala qrlahmvlvr meqrgespdd
      361 rvqdavarsk pvkqlvdavw pkltpeqvlh rllaepefla raarselspe eqslllwpkp
      421 yrshksakws aadaalldel rdlmertpsl ghlvvdeaqd lsemqlralg rrcrngsatv
      481 lgdlaqgttp wstsswqtvl qhlgqaegev teltlgfrvp revldfaarl lpsiapglaa
      541 prslrpgags lsirpggsva qaadaalaqe gsigvivpda lvgevsrals grphtvldpd
      601 apeegehrll vvpatlakgl eydhvivvep adivaaeprg larlyvvltr avtsltvlhd
      661 kplpaqlam
//
LOCUS       WP_357639142             823 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing serine/threonine protein kinase
            [Nonomuraea wenchangensis].
ACCESSION   WP_357639142
VERSION     WP_357639142.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11600203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..823
                     /product="WD40 repeat domain-containing serine/threonine
                     protein kinase"
                     /calculated_mol_wt=82044
     Region          17..267
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(17,40..41,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,78,94..97,101,103,140,142,
                     144..145,147,157,160,175..178)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,78,94..97,101,142,144..145,
                     147,157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(28,101,103,140,142,144,160,175..178)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..164,171..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          442..823
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          557..593
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          599..644
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          648..686
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          696..731
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          791..820
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mpqirplrpg dpervagwrl vgvlgsggqg tvykavgddg revavkllhs hlsgddaitr
       61 gflreveaar rvaafctaav ldvgtaderp yivseyvagd tlqqvvrseg prtggtldrl
      121 aistltalaa ihqagivhrd fkpgnvligp egpividfgi akaldattma sgvvgtpaym
      181 speqfegqwv gpasdmfswa gtmvfaatgr payagatvpa ilnavlsgsp dldgvperla
      241 evlracfard palrpsptel mkrlmthrgp avpfplpdhp egttppatpt ptgpsapppa
      301 paagpgappp gpgampgaag rggvaaghaa avpgggdgvp asspsgpwsg pggggvpgtg
      361 pgggggrpap eghggsgglr gqgtvegrgs gargrgfqgs yhggmtdaet spgggrkgvs
      421 rravlsagaa alataavsaf valrpdggaa ghdgtlgqpp vpdtgigtgt gatgtppatg
      481 spiplttqta atpvaaepfg tligepaalp agtgapsaam gargpfvalg ggngsvvawd
      541 ltagparrlg dggaattava ygnsrgepvi asghadgrmr lwspsgksla thkatdpiia
      601 vtvtaegrvv avsqkydslr dlrgtvrlwd vttgrqigpt stehfqgvng lafgrlgdad
      661 vlvtgdganr vrvrplstgv vsgtfkteei ggiellacae lkgepvlvst hldatlrvyd
      721 lksgkrrkkw dfsdrspddr gtaalvtgtl ggvpvavvah tpsggdafvr vwsladgelv
      781 gefgsgeggg iralalaeqp vtrpvvvavg adrrlrlwsl gag
//
LOCUS       WP_357639127             308 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora parva].
ACCESSION   WP_357639127
VERSION     WP_357639127.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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 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
REFERENCE   4  (residues 1 to 308)
  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 308)
  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..308
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..308
                     /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=31797
     Region          1..251
                     /region_name="fabG"
                     /note="3-oxoacyl-ACP reductase FabG; PRK05653"
                     /db_xref="CDD:235546"
     Site            order(12,14..15,17,36..38,89..91,140..142,155,159,185,
                     186..187)
                     /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 maldgkvaiv tgagrglgla yaqelarhga sivvndvdae ataeavaaie asggravavv
       61 apvgptetak elvstaverf grldilvtna gvlrdtvlwk msdddfdtvi nvhlrgtftt
      121 vreavrhmrq ageggriicv gsptgqrgtf gqtnyaaaka givgmvrtwa lelqragita
      181 navvpvaatt mtatvpyfaa avraeangep mpaffrhelg fgtaddaagl vaflgsdaaa
      241 svtgqvigvg gdrlqiwthp eaaltahreg gwtydalvqa wpttfagsaq svgerfpklp
      301 eefappts
//
LOCUS       WP_357639333             967 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357639333
VERSION     WP_357639333.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 967)
  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 967)
  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 967)
  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 967)
  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..967
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..967
                     /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=103253
     Region          13..253
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          154..955
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          791..819
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          831..859
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(832,835..836,839..840,842,866,875..876,879..880,
                     882..883,906,915..916,919..920,923)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          864..900
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          905..939
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mearghdapa plfrllgpvv leagagqvtf tgkqgalltv lllhagqvvs tprlaetvwd
       61 ppmpsapaar vrmlvsevrr acaavgadvi etrrpgylls pgaggidltl frsqvalare
      121 aaaagrhaea lahyeralsw wrgapldgvt gsfaearaer lhglkldave erqevllmld
      181 rygdvvsevs aladeaplre rlhgqlmral yesgrrteal evyrrlrrrm vdelglepty
      241 elrrlqsril rsdpppvsag dgagppgpdg ggpqagapaa arpavvlpvp cqlpapppsf
      301 tnrdheleel ddlrrpgtdg vgvaaisgpg gigktwlalh waharrdryp dgqlyvnlrg
      361 fdeteepvpp gtvlrqflga lgmpdavipt gqeaqaalyr slladrrllv vldnardsaq
      421 vtslipgspg ctvlvtsrnp ltalhtthsa rllkvgafse eesrrmlrrh lgadrmaadp
      481 gavaalvehs gglplalgvl asraatdpgf plaaltqelr dpatrldale tgdlgaglra
      541 vfrssyaald aasarlflll gsapgpdvgl aaaavlaglp msatrtllsa letaglvrrl
      601 tparywmhdl vrlyaaeraa vdlparelgq alarlvetqa atacaadrll sphrlavpss
      661 papssgaspp cavpfadaaa alawfeaelp gltatqllav elgldqacwr lawglttfll
      721 rryltrerlg vwtvalaaaq rigdprvlal chwqagyaya higadrlseg ledlnlalel
      781 feqvgdrsgq aqvhhtvawv wsvrgqperg leharaalri qrdagdlvwe analsalgwi
      841 hlqlgeheta relceqaltl frhhhdesge aatldtlggl alrqgahera ldlyeqclav
      901 ragngnafqa adtlvglgdt hhalgqtera haawsealal yesqhrrdla ervrakllrp
      961 gsssaah
//
LOCUS       WP_357639358             289 aa            linear   BCT 28-DEC-2024
DEFINITION  serine protein kinase RIO [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639358
VERSION     WP_357639358.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448151
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..289
                     /product="serine protein kinase RIO"
                     /calculated_mol_wt=31520
     Region          39..278
                     /region_name="RIO1"
                     /note="Serine/threonine-protein kinase RIO1 [Signal
                     transduction mechanisms]; COG1718"
                     /db_xref="CDD:441324"
ORIGIN      
        1 mpkhssprrr gkyaldaddl ewldsapvdd gppvgdrwst wdqstpterg pkphpdwlvt
       61 elaavdtelg ilktgkeadv hllsrgvpdt drvcllaakr yrsaehrlfh rdagylegrs
      121 tresrmnram anrtafgkql iagqwaaaef galcrlttlg lpvpypvqiv gteilqefig
      181 tsdgyaaprl anvsddlddl wtqlvealvi lareglahgd lsaynllvre grlviidlpq
      241 ivdvvshptg pqfldrdarn vatwfaakgv asadpdalsa llqseagml
//
LOCUS       WP_357639371             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357639371
VERSION     WP_357639371.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..212
                     /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=23002
     Region          11..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mekvkrpdkr aersqrtrek vieaarelfv aqgygatslq evadragvav qtvyfvfrnk
       61 rtlfkdvvdt siagdtapva tmdrewfraa cadptaagql rghvhgasei lgrvapimpl
      121 iaaaaatdpe iaaqwpddad prytvqyaaa ealvgkpdar pgltvemaad llygvlspel
      181 ylifvrdrgw speaweewar atltsqlcad ag
//
LOCUS       WP_357639397             389 aa            linear   BCT 28-DEC-2024
DEFINITION  epoxide hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639397
VERSION     WP_357639397.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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 389)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 389)
  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   5  (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 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..389
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42184
     Region          2..107
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          69..>198
                     /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 miapfritip qtdlddlkdr ltrtrwprql pgggwrrgvp vgylrelaay wadefdwraq
       61 eaklnafpqf ttdidgqrvh flhvrspepg alplivthsw pntvaeflnv igpltdprah
      121 gldpatafhv vapslpgfgf spfpepader pwsilrvart waelmarlgy erygahgnda
      181 galvtpqlaa idgdhvigsh itaglgiptg dpaeldgate aelaeltdlt qrfaggsgyg
      241 pylakrpqtl sfgfadspva qlaylverfk efdgwpdeea aepidrdlvl tnaslywlta
      301 tggssswpyy egaagmpinq tavpsgvshg gspllrriae rgnrvvhwag ehgdshmvam
      361 nspgplvrsi rtffatlegt pegalegar
//
LOCUS       WP_357639429             336 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora parva].
ACCESSION   WP_357639429
VERSION     WP_357639429.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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..336
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..336
                     /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=34790
     Region          1..321
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrkcrvglvg aggvaqrhar vlagfddvel vgvtdvapea asalaaqhgg racadvgell
       61 atgldavyvc vppfahgpae eaiieagvpm fvekpvavdl dtaeriadlv arrglrtavg
      121 hhwrylsvld qardlladrp vrmvsgtwld kvppvawwsr rdrsggpvve qaahvldlir
      181 vlagevtevt aygngtpppv dgadidsvtt aalrftdgav gtlsaacvlg wkhragleil
      241 adglalaite dglsirdadg erhlpadpea arvavdrafv davrgigddv rvpyaealat
      301 qrlalavads artgttvrla tatapavlas gvtvda
//
LOCUS       WP_357639505             301 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357639505
VERSION     WP_357639505.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 301)
  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 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   3  (residues 1 to 301)
  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..301
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..301
                     /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=33283
     Region          4..283
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mdvdlrklry fvavaeelhf graaarlhia qpvlsrqira fehelraelf vrdrrstvlt
       61 eagrqlltda rallasaeal rrrvqraahg rptftiafmp gllvtadara igqrhpdlav
      121 nvvrtsyddq adivrdgrad vsyvrlpvdq rglrlrplfs eprvvvlptd hrlagkesvd
      181 laelagerll qdpdavpewr dlpnrpidsd prprpalnsv eeklehvaay vgtvilplst
      241 atfytrpdvv hvpvadlghn qvclawaedn rsplvhefvd laapppgdrr qggsgapegl
      301 a
//
LOCUS       WP_357639526             273 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357639526
VERSION     WP_357639526.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 273)
  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..273
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..273
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29160
     Region          3..273
                     /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 mktgtlrvpg aelfhevrgt gpmlllvpgg ggdagtfdgi advlardftv vaadprgysr
       61 srldspepvd qrvetqsedc arlidhlggg sayvfggsdg aivvldllar hpgrvrravv
      121 heppcvavlp daaeqlrffg rvyeiyraeg laaagaymse giggtlrplp dpatlspraa
      181 ervvrtvanm plfmehelrq ftayepdlea laavadrlvl aagretrghl pyrpaaelar
      241 rlgreltefp gghggyteap eefaellart lrg
//
LOCUS       WP_357639528             264 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357639528
VERSION     WP_357639528.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..264
                     /product="phosphotransferase 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=29204
     Region          7..212
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 madlqhthev afdgdvvtkr yraskpgaae rewqaltlla ehapglapep iafeagvvrm
       61 srldgeplrg lpvtdghlta lagalaelha avprpvlrev pvrpwqreav rdwlrgqgar
      121 wrsrdpladr avreglcwle gwrpdgsgvr pvfgggdgnl anflwdggrv rvvdfedsgr
      181 sdlayelael aehvsmwvdr aevgaelvar felgaaeerr lrgcrrlqal vwlfllaqdd
      241 pdnprnppgt frrqaerala rlda
//
LOCUS       WP_357639636             554 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639636
VERSION     WP_357639636.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 554)
  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..554
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..554
                     /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=56926
     Region          8..454
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 msdatpslva gryrldelig sgptgevwra ydqradwtva vkvldtgaat pevlrqhaqa
       61 varvihpnva mvldvgdheg apflvmeflt geslgeevag ggplpiveac dligqaaagl
      121 eaahragvvh gqigpdsfrr agsgvlkvvg fgladqafsd dgvlyrapev idgrggqaaa
      181 dlyalgcvcy evlcgrppfe gspdevgdrh lhaepeppsr hraevpgeld rlvlamlakd
      241 paarpagget vrralaaiar pprtppgpat gpqpsqatsp mapqggqagp yqggasqggq
      301 agpyqggapq pgqatshpgg vpqtgqifaq pgaggpaagr gvdaaragag dthampagaf
      361 hdsggprkgd taiydapppp ppsnrrlfvq lgaalaviav vtvglilwag srgkpeagpt
      421 psvtpittts apeptptetp epstsiaplp tdpgstpnpk gtlsnsvpig gwekwlsefd
      481 ksvtaqetig diepraakka hekirkagrk fldkhddsvl hqvtgimrdl rkaqekgdvp
      541 tsgplndfld nwkp
//
LOCUS       WP_357639650             827 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357639650
VERSION     WP_357639650.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..827
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..827
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=87561
     Region          <10..827
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 midggenktr gggsptpvrp erlrgpvefv grtaelaqlr rlvatppcli llegepgigk
       61 srlvaellae lpgrhlvgec ddvpepfplg vlldairgct erpgplspva galapllpel
      121 advlpdappp ltdpaaerhr lfravaavla alspatllle dlhwadpatc ellaylsthp
      181 vdglavllta rtatpgsstp ihdalartpp wsvtrvalsp ldaddvrrla artlrlddpp
      241 qqltaalldr tagipfvvee vlrtlaergg dpladdsvpf vlrdvllwrl rpldeatrev
      301 lgaaavlgmt pdqrilaavl sldrvaigaa ltaahragll hdagdglrfr hdlarqvvyd
      361 lvpresrewl hlrvarvleq elprpvaqla hhyrragsga dfvrnaeaaa dlatergdda
      421 taasfllqtm diaelprpvr vrlaaklgrs aidglsqaea ipvlerllad rrlppgarge
      481 lglvlgrmlr qqgealrgyt eieravpylr aprrkapala vlaapdtvvg rhvddhlarc
      541 teaetaaaas gdpgshlavr iaraslllel gdpaawaiit elrasaelad rpreharacl
      601 nwaqgalhag hpeqaealla agralvdetg yerltslvea tqlsldratg rldglverlr
      661 rlvasaermp vtlldarael atvlaltata nggtanagsa aglgdrtggl devevaeral
      721 revvvdarrv gaiwplvqtl salarltvtr qpdeavrhat ealsvvrgkg ilawaadavl
      781 vlaeaaaaqg eparaaaava eleagiagrd tpparaalhr crelvpa
//
LOCUS       WP_357639651             287 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639651
VERSION     WP_357639651.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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 287)
  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 287)
  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 287)
  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..287
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..287
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31459
     Region          6..273
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mdiqspdkli elldrhayla deglataafl alrmgrplfl egeagvgkte laktlaalle
       61 aplirlqcye gldaaqalyd wdfarqllhl kaaeaagitd vgrlegeiyd rrfliarpll
      121 kavetqpsvl lvdeidradd efeafllevl sdftisipel gtvsaktppv vvvtsnrtre
      181 vhdalkrrcl yhwlehpdfd revaillrrl pdctetlavq varaaarlrq aglvkppgva
      241 etldwteall tlgakeldpg raaatlgaal kyredienvl gngllha
//
LOCUS       WP_357639680             343 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639680
VERSION     WP_357639680.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..343
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..343
                     /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=37525
     Region          1..331
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtekllelsg vvkhfpvrgg flvkhqvgvv havdgidltv hagetlglvg esgcgksttg
       61 rlaarllept ggsitydgrd ithagrrelk pirpeiqmvf qdpysslnpr htvgsiirgp
      121 mdindinppg greararell eivglnpehy nrfphefsgg qrqrigvara laleprliva
      181 depvsaldvs iqaqvinllq qlqrdmgiaf lfiahdlavv rhfsqrvavm ylgkiveiad
      241 rdslyerprh pythallsav pdadvegpar qrirlagdvp splnppsgcr frtrcwkaqe
      301 kceveepplt rlsgnrdghl tachfpeapt tqgedvvldp ala
//
LOCUS       WP_357639688             325 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357639688
VERSION     WP_357639688.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=35280
     Region          9..319
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 marptaqvla llellqsggv rtmaelaerl gveprtvrry vshlvdldlp vesvrgrygg
       61 yrlaagyrlp plmfnddeal avllgliagr raglatatdt agetaaakir rvlpprtadr
      121 ldaalqslaf taepgdfpap qtevllavae avrhhrpisv qytsgdgrrs vrvlhpfglv
      181 nhagrwyvtg vdpdigeert lrldriadar plpgsfeppa gndpaghlln smarapypha
      241 vslriqgtve qirrrlpasi aevregadeg wqdveiraes ldwlpgvlaa ldlpfvierp
      301 delrdrvval aerlaasarr esars
//
LOCUS       WP_357639694             575 aa            linear   BCT 28-DEC-2024
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639694
VERSION     WP_357639694.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 575)
  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 575)
  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..575
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..575
                     /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=59746
     Region          96..574
                     /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 mgqgprrqnd grptgtghgs ggragqggqa ggrggqsggq agrgggrsgq aghgdgrage
       61 gggqagqgsg rggqgggrgg grgrprgpar dharnaafdv mravderday anllmprllr
      121 ergvkgrdaa latelaygtl rglgtydaii emcvdrapds dvrdalrlga hqllkmrvpp
      181 haavgttvdl vrlrigagaa kfvnavlrki gsrtieewip ivapdeahdp aghlsvaysh
      241 prwivsafrd algsradeva dllaadnarp lvtlvarpgr ssveeladsg adpgryspya
      301 aylpegdpgr ipavaetraa vqdeasqlva laltrvpldg rdelwldmca gpggkaglld
      361 aiatygdlaa sddrylgggg gggggggvaa addrypadpv glgvravayp ggarllaadv
      421 qyhrarlvwq ttrdaavvaa dgtepawrpg afdrimldap ctglgalrrr pearwrrdpa
      481 diaelgrlqr rlldaaldav rpggvvayvt csphlaetrv vvgdvagrrg dveqldardy
      541 lpeidglgdg phaqfwphrh gtdamflall rkrpi
//
LOCUS       WP_357639706             279 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357639706
VERSION     WP_357639706.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 279)
  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..279
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..279
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29815
     Region          4..277
                     /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 meirtvhang lefayltlgd gplalclhgf pdtahtwrhl mpalaergyr avapflrgya
       61 pteipadgay egaalaadvr alheelggga davvighdwg afpvhqcagr frravalavp
      121 ppgalaggff dyeqlrrsfy iflfqtplae taaaapgfld glwrdwspgy datedlafvr
      181 rsllddpanl aaaigyyram lgttppsgry pepepeargp vlylhgaqdg clgaglvkdv
      241 tahlpagsra evvadaghfl hlerpdevnr lildwlgpa
//
LOCUS       WP_357639712             513 aa            linear   BCT 28-DEC-2024
DEFINITION  GMC family oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357639712
VERSION     WP_357639712.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..513
                     /product="GMC family 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=55278
     Region          1..513
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 meydyvivga gsagcvlanr lsadpgvsva lveaggqddk leirmpagfa klfktdydwn
       61 yttakqdels grelywprgr viggssslna qmwvrgcard ydqwevpgws yadvlpyftr
      121 aehrigtndg dvygtggplh iselrspnvt taaflracee lgyqrlreln gpsnegycpt
      181 pvtqyrgrrw ssadaylrpa lkrsnltvvt gvtvervlfd grravgiehg gaqlrarrev
      241 ilaagaigsp hllmrsgvga aaelreagve vvhdlpevgr nlqdhlasgv yvaclqpvtl
      301 tkaesvgnll rylvlrsgml ttnvgeavaf lrtspeepap dielvfapvp fvehglvpat
      361 ghgltvgvvl lqpesrgrit lngrdpvidp aylsaeadvr rlvaglkaak qvfttsamrp
      421 yaggpmdpyw gpesdeelaq wvreraetly hpvgtcrmgv degsvvdpsl rvrgveglrv
      481 adasvmptln rghthapaim igekgaelil gga
//
LOCUS       WP_357639761             317 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357639761
VERSION     WP_357639761.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 317)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..317
                     /product="GlxA 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=34652
     Region          4..316
                     /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 mrrhriavva lnhfapldfg ipgqvfwaae tpggeklyev vtcsegrrpv rcsagysvqp
       61 dhdldvldta dtvlvpgiha gralkdgtls aglraalrdr prvmsictga fvlaaaglld
      121 grpatthwre aprfaelfpq vkldpdvlfv ddgdvltsag vaagmdlclh virrdhgsev
      181 anrtarrcvm ppwreggqaq yverplphep agglgptrew mlahldrpld lnalagharm
      241 svrtftrrfr eetgvsparw laaqrvqhar hllettdlgv eevarragfg tavslrqhlh
      301 aavgvaplay rhtfrrv
//
LOCUS       WP_357639770             581 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 97 protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639770
VERSION     WP_357639770.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Naumoff,D.G.
  TITLE     GH97 is a new family of glycoside hydrolases, which is related to
            the alpha-galactosidase superfamily
  JOURNAL   BMC Genomics 6, 112 (2005)
   PUBMED   16131397
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10628658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..581
                     /product="glycoside hydrolase family 97 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=64280
     Region          8..242
                     /region_name="GH97_N"
                     /note="Glycosyl-hydrolase 97 N-terminal; pfam14508"
                     /db_xref="CDD:464192"
     Region          247..484
                     /region_name="Glyco_hydro_97"
                     /note="Glycoside hydrolase 97; pfam10566"
                     /db_xref="CDD:463149"
     Region          487..577
                     /region_name="GH97_C"
                     /note="Glycosyl-hydrolase 97 C-terminal, oligomerization;
                     pfam14509"
                     /db_xref="CDD:464193"
ORIGIN      
        1 msqwtlsded leveialsad geptlevrra grvlvrpsrl glraahedls aglafdgmss
       61 rqvaesyetv tgkrrehryt akewtlsftk gahrldlevr igghgvayry vvpwtgpvtv
      121 ideiseyvvp gearavllpy engrcdyeei hrhgpvadae pilygypslf qigdtwllvt
      181 esnldsgyag trlrfdghaf rldlpdpyvt aasplvtpwr tmiigelati vasdlvtsla
      241 apsavadtsw irpgaaawsw wsdgpstrdl deqkrwvdfa aahgwpyvla dagwnkqwmp
      301 eliayaaarn vgvwlwshwq hvdtelehre klalwkewga vgvkidftes dgqdrmrwfd
      361 ailaatarlr lmvvfhggti prgtertwpq fmtaeavkga ewikpkpgkl plyppehyls
      421 laftrnvqgp mdftpctfta vrtisagfel alsvifesgv qhfadgieay earpealrll
      481 sgvptawddt rllsgdpadh illarrsgge wyvgagvsge artltvpldf leegewaaei
      541 yrdapddgil aetatvsagg kldlavspng gftlhlrret s
//
LOCUS       WP_357639773             477 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357639773
VERSION     WP_357639773.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 477)
  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 477)
  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 477)
  AUTHORS   ter Beek,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..477
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..477
                     /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=52490
     Region          104..467
                     /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(194,196,324,326,356..358,400)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 memnrrqmla lavaaatapa lsacagdtrq qrqaaaptks gvptldpnrp gndtwpfaea
       61 eqlnnsltwp ktevadpask vtltvaitad viaevrnaqf dfffhkrhpn ieikretsqf
      121 dsyltkymaq aaggsmpdvi ythyswaqnf iandifqpld eyiaktpefd kqdlpvnalg
      181 yyerdgklfg lptdmapkll fynkdifdka gekypdeswt vekmmevakk ltsgsgaeki
      241 ygftpmllpe pditpralaq ygarylnade svsmisqpea qkvfgmwldl lnkdkavpsl
      301 aelnqvlakv epfkvghaam tingawilte lakqkaftwg aaptpkgpkg rftpvigsal
      361 amyakspqkd aawiylneyl sstgqqfrri saparqsawe pnaealgipk dvvetvksam
      421 keygtgdgvl klpankkvve takpiwervm igktdlasgl keitdkitpl laenkia
//
LOCUS       WP_357639813             387 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639813
VERSION     WP_357639813.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 387)
  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..387
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..387
                     /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=40978
     Region          1..384
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mnhvvvagag lagvrsveal rakgfdgrit ligqerhrpy drpplskavl sgssdssfvd
       61 adlavlevdf wpgvsvkalr pgvvettege lgydglviat gaepitlpgd grqhvlrtld
      121 dalelrarlv kgaqvviiga gwigaevata arragcevtv ieagptplaq avgpeigart
      181 qgwyegidlr lntlvgsvdd ggvtladgsl ieahvvvtgv gvrpavgwla gsgidldngv
      241 vtdehlrtsl pnvvavgdca awwsrrfetr lrvehwdaal nspevaaatl lgveaaydpv
      301 pyfwseqfgh mvqyaghhpa gdrllyrgel ggkwsacwlt sddtlaavla vdrprdlvqg
      361 rriieaghrv daerlvdpdv slrdcvv
//
LOCUS       WP_357639848             390 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639848
VERSION     WP_357639848.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11461692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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]"
                     /calculated_mol_wt=42136
     Region          <145..386
                     /region_name="LytS"
                     /note="Sensor histidine kinase, LytS/YehU family [Signal
                     transduction mechanisms]; COG3275"
                     /db_xref="CDD:442506"
ORIGIN      
        1 msttacvvls cltfvlgyav alvprgrrep repsdpagpp pgdwkdeaty talhiaalaa
       61 pslraglnrd sarkavrhlh allgtyavai tsteaalawd gpctdevlty artalasgrp
      121 qvfagepyga vvvpllvdgk lvgtlaafdq evsaalvrtv tevgrwvsgq lelaeldtsr
      181 rraleaemra lraqisphfi ynalttiasf vrtdparare llldfadfar yalrrahdft
      241 tladeltcvd rylllerarf gdrlrfsvqv apevlpvpvp flclqplven aikhgmgsrg
      301 gigqvrvvar dagpeahitv eddgtgmdpe hvrrvldddp rregngigla nvdvrmrqiy
      361 gdgyglvvet algsgttvrl rvpktrlssl
//
LOCUS       WP_357639859             208 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357639859
VERSION     WP_357639859.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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 208)
  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 208)
  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..208
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..208
                     /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=21678
     Region          25..208
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 msryvifgag gragrravae arrrghqvta vvrdparydg paddgvrvaa gdvtdaadva
       61 alavghdaai ntaavigsdt ffsdaaralv kglrqagvdr lvavgiatll pgpdgirlld
      121 apgfpaefrp fclahaagle vlraegggld wvyvspagdf dhegersgry evrehgdmal
      181 rvsyadfaiv lldeaesprh rgghlavt
//
LOCUS       WP_357639899             155 aa            linear   BCT 28-DEC-2024
DEFINITION  Dps family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357639899
VERSION     WP_357639899.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..155
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=16779
     Region          8..153
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 matitgplsg dakktvatal qgalvdlldl sllakqmhwn ltgphfrqih lqldevtala
       61 rehadtiaer avalglnpdg raatiakstk lsqpengwie dgkvvatmtd ileavgkrmr
      121 ervavtdepd pvsqdlliav aqdidkqhwm fqaqr
//
LOCUS       WP_357639872             380 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357639872
VERSION     WP_357639872.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 380)
  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 380)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 380)
  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..380
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..380
                     /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=41762
     Region          143..372
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtassprfte stqgrlrrln latslppvvf aavvlvytdm rtwwhliila pgaaaalvaf
       61 erwtandlar vvlpclvvaa avwplgvlvs gspnaywgfc avgslgmrev rrhrklvlag
      121 lfgyvaavga arllvqrndi ghvlvtyvli ptvltmlvtv ftivgerfyd lireleqtre
      181 reaelavvre rvrfasdlhd iqghtlhvvk lkialaqrll lrdtarveqe lretyalvsd
      241 tiaqtkelay aqrrlnltae ienaknlfea agirvrvtre aevdtrasel lgqvlrettt
      301 nilrhaqarq vqitlsesgi tivndgvsat appelrglaa lrqrvagdgg eltvhqqqgt
      361 frtaatfpaa raetergdgr
//
LOCUS       WP_357639904            1075 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora parva].
ACCESSION   WP_357639904
VERSION     WP_357639904.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1075)
  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 1075)
  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 1075)
  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 1075)
  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..1075
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..1075
                     /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=116375
     Region          6..1074
                     /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 mvrtgrasfa qerlyfldql qpgnpayvva favhlrgalr pealraaltr vvarhdalrt
       61 tfavvdgvlt qrvsstpavd vditadgwvd ratqeahlrt lvaeqarqpf dlangpvvra
      121 ylrswgpdeh glavlvhhia cdgwsvglll rdlaaeydaa vdgsvaayee paesylayae
      181 rqhetwrrds sgldfwraal vdvpqlalpt dfprpsvlgt tgavlrrpve pelvrrlgew
      241 grargvtlfa vtlaayasvl sryarqdevv vgvpvanrmd daeerlvgcl vntlpirldv
      301 sgrpsftelv drarrtsmaa fanqdvpfeq ivratvgerq lshaplfqts ltvqnfpfaf
      361 pefagvrlte vdveidvtkf dlgltldvst dvpflraeys telfraetvg tllthyltfl
      421 rsivdeeqre psmvdeaera qltegvnppl asapvthpsv lrrfadhvaa tpdavavrhr
      481 dveityaeld rwagriaagl adrgvrpgvr vglllgrspa vvaailgvwk lggvyvpldp
      541 dyprqrleli aanagmavlv vdpetaeaaa altrdsgtpl adahtldgis vieetfpgpd
      601 dpayviytsg stgvpkgvlv ghggldalns ptpagldvta advwlaassf sfdasvwemw
      661 galttgarlv iaervdlvdr erlarlvrre avtvlfqtpg alyrllppyl raleedetsr
      721 iryvvlggea lswsrlasli adapglqtvf vnmygitegt ihvtifqasa advprvpega
      781 igvplpsarc yvldedlrpt glnvpgelyc ggalvahgyl dnreltearf ppdpygggvm
      841 yrtgdvvkwg ldgsmvylgr ndtqvqvrgy rvelaevega llthaavqsc avaaeddelv
      901 afvvhgigpd aehdlrahlr etlpaymvps riltvatipl tahgkvdlpr lladsraart
      961 vtapsrppas vvgtgleeri racwvevlrr pdvglhdnff dlgghsfali alqqrmseeg
     1021 ldvsvtdlfr cgtiagcaaa lqhtapvvad pntaqrrqgr alladrrrsv ragrg
//
LOCUS       WP_357639909             257 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea wenchangensis].
ACCESSION   WP_357639909
VERSION     WP_357639909.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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 257)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..257
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..257
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25829
     Region          100..254
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mrktlsavgl vtmlaalaac gsggatgaap vpptpatptt aatsaapssp pptgpnvsgc
       61 fteadgkife ydgglpgvit gtgstgvvit yerrgnvcaw rplsdrlvaa gyrvllyars
      121 vaavpedttv amakrlakek gvgrvflvgg sigattavpa alrlgpekia gvvalsgeia
      181 aedaakltvp llqigsehdd yggrealdaa raaatkapdt qalvipgerl hasqllaspy
      241 adqvlstvet fmnrhkg
//
LOCUS       WP_357639983             321 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora parva].
ACCESSION   WP_357639983
VERSION     WP_357639983.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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 321)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..321
                     /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=33650
     Region          1..153
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
     Region          181..316
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mqlmrrvgvy glirdsgrvl vvrdgvegef pglwrlpgga vghaedpera vvrevaeqvg
       61 ltvtvsrlla vvadvatsse grislhtdrl lfelstphga lsdaprpqaa qpqdaqpqga
      121 qpeagaglvd qsrwlspaev aqvpltpfta ealgvpvtpl ppgthrprhp aapphpdrrl
      181 rfgayglvtd pagrilltqi aqgypgaglw hlpgggtdhg eqpatgllre lveeggqvgr
      241 vvellgvnnl hnpaaygpeg rpldwhgvrv iyrvlvdvpt datvteaagg staragwftr
      301 aeavdlplsd iaavaigqsg r
//
LOCUS       WP_357640009             344 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357640009
VERSION     WP_357640009.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..344
                     /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=37586
     Region          13..343
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtaspakptk vrgetilsvd nlvkhfpitq gvlfqrqiga vkavdgvsfe lrrgetlgvv
       61 gesgcgkstl arllmrletp tsgratlegr dlfkasggel rrlrrnmqmv mqdpytslnp
      121 rmtvgdiige pfeihpdaap kgskakrvqe lldlvglnpe hinryphqfs ggqrqrigia
      181 ralalkpevi vcdepvsald vsiqaqvinl lkqlqgelgl syifiahdls vvrhiadrva
      241 vmylgrivei gtedeiyera thpytqalls avpvpdpear dqrtmirlvg dvpspadpps
      301 gchfrtrcwk aqeicavedp atvpraadph psachfaelr ptpa
//
LOCUS       WP_357640058             294 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357640058
VERSION     WP_357640058.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 294)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..294
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30503
     Region          8..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mntdrrsvtv vglglmgsal agalldhghp ttvwnrsahk arplvdrgar paatpreaie
       61 agglvvacvl dyealravle pvagslsgkv lvnltsgspe qahefatwag shgadyldga
      121 imttppgvgs pemmflysgp dlvfeahrst laalgdplyl gadpglasly daallglmws
      181 tmtgwlhgaa vvgaektpaa vftpvairwl tavagflsay apqvdagryp gddatvdvqi
      241 aaidhllhaa earrvdnalp ellkslmera kaaghgsdsy aslievlrep adgr
//
LOCUS       WP_357640060             334 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea wenchangensis].
ACCESSION   WP_357640060
VERSION     WP_357640060.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..334
                     /product="GlxA 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=36037
     Region          21..326
                     /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 msagsvavvv seqigvpswd lyelsipctv fgkpqsdlad pwydlrlcgt gerpgdtgll
       61 lrtpyglddl agadtvivps vpdscveege plpqalital rrayeggarm vslctgafal
      121 aeaglldgrp atahwmhtal laerypkvrv ddsvlyvddg dvltsaglta gldlclhlvr
      181 rdlgahvanq larrmvvpah rpggqaqfid msvpaaddeg lapvldwarn rldqpltvdd
      241 larraamspr tfyrrlqaat gttplqwlld qrlgrarill estdlpieki gelsglgtan
      301 nlrrhflrhl gtspsdyrra fprttpepnp alpa
//
LOCUS       WP_357640094             221 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent F420 reductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357640094
VERSION     WP_357640094.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..221
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22152
     Region          3..205
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mnvgilgtgn lavalgrawa paghslfvag rdplrskeaa dqigpmakav dptelatqid
       61 vlvvavaweg leaalslvga pegslagkav idctnpvdyt tcelkptsgs aaalvahtap
      121 gahvvkalhl fagaswpyvg pqesapvvai cgdepsaldr aaaliqdlga rpavvgglgs
      181 arqleeaagf vmrvvaagyn prlavpdvdp allraaqttt d
//
LOCUS       WP_357640114             219 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357640114
VERSION     WP_357640114.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13273981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /calculated_mol_wt=23675
     Region          1..209
                     /region_name="PRK13756"
                     /note="TetR family transcriptional regulator"
                     /db_xref="CDD:172294"
     Region          5..>98
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgkltaqaia vraleigdae gldavtirrl atelgvtpma lywhfknkdq llagmadhli
       61 agfapkpadq rpwqeqlrdl mvglirtlrv hpcarsvieq vdvitvpnfl avwnqalgvg
      121 rdagfnrdes clisryllns aiaiadapah hragrenasa vrakliglqs vppetyphiv
      181 emavplvegp dpelydtfgv dlvltgietl acrrlgsss
//
LOCUS       WP_357640116             436 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora parva].
ACCESSION   WP_357640116
VERSION     WP_357640116.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=47795
     Region          8..435
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 maarrsripa tkypverftl dnglrvvltp drsapvigva vvydvgirse pegrtgfahl
       61 fehlmfqgse nleklahfrh vqgaggtfng sthldytdyf etlpsnaler alfleadrmr
      121 gprlteenlr nqvdvvkeei rvnvlnrpyg gfpwltlppv mfdtfpnahd gygsfddles
      181 atvadaadff rryyasgnav lavsgdidva eatelvsrhf gdvparpapq rpdftepdls
      241 aerrtsytda laplpavaga wrvpdpvtdf agylpyvvla evltdgdasr lverlvqrdr
      301 avtslggylg fmgdpfdvrd ptalllqahl ppggdvdkvl rtideeldrl atdgltdgel
      361 artqarmath llrdtdavlg ralrmavleq qrgepgllne lprlvgevte eqvraaaatv
      421 rperraaiev ipggar
//
LOCUS       WP_357640132             255 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357640132
VERSION     WP_357640132.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..255
                     /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=27309
     Region          4..198
                     /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 mtdpilvtgg tgrlgrrlvp rlvaaghavr vlsrkpprde rmyhrdlmmc rgdlitgegl
       61 eaavadtgti ihcatgngha dqdaaralvr aasrtgrphl iyvsivgvdr vdisyyrakl
      121 acerllegsg lpltiqrttq fhelivwmct iqrrlpvimm pagvsfqpvd agevaarlad
      181 lakaspagra pdmggpevra aadlarayar arsnrrpvvs vplpgiggmr gfregshlap
      241 dhavgqitfe qflta
//
LOCUS       WP_357640146             954 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357640146
VERSION     WP_357640146.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 954)
  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 954)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 954)
  AUTHORS   Rosinski,J.A. 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 954)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..954
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..954
                     /product="helix-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=100930
     Region          <6..921
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          897..951
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mvspilvgrd kelarlveli svtspvpava vvegeagigk srlvaellag pavtglrvlr
       61 gaclqirepf plgalvealr graadlgesa lspvagalre llpelaaalp pappplddra
      121 aerhrvfrgl aevltalgpa vlvvedlhwa dgqtveflty lmsvlpgtpp gtlrvvltyr
      181 eeeapavvrg itarlpdair rehlvlppld aaqtrvmasa ilgaeevtae faehlcaras
      241 glplavqell allrtrgtli rweggwarra leeldvpsgv rasvqervaq lsagakemae
      301 rvavlqtavp igllapgeag aidevlgsgl ltdagglvgf rhvlaaqavy eaipagrrra
      361 lhaeaadavr glrpvplgrl ahhlrhagrt eqwaetavea aeqasrlgdd aeaarlladv
      421 lretdppaar raeltvrlgw aalellrppp vadliaaale qdvprplrgt lrlllalhle
      481 rtrtdearig eafaaaaedl tgrpgepgrp glaawamagv grppspvpqd eamswleral
      541 atlpavddpa mrmlvlgkia mifvvigdpr wagltedllr etggrrllrr evnayrsigg
      601 aglfaghhra grrlvtaaie dgaepdlrgr lelrslvvia vadylegswn glaarleelr
      661 ehfgdepher iimdgvgacl aavqgrpeaa ppflfeavat aqtrgqfddl vlplavllrl
      721 aalrgepeaa lavaaevavr weaarlwpva vrtlpaltqa llaagragda adtvarwaah
      781 ldgldaplag pslayargll aatgerwaea aaefaaaada feavparyea aqaheqaaac
      841 lftlddpaaa trlgravtly gelgarwdld raaglgrrwg lrpspaapar ggddhvlsar
      901 qeqvarlaae gltnqeiare lflspktvdk hvsaamrkvg arsrtelarl lpad
//
LOCUS       WP_357640190             514 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora parva].
ACCESSION   WP_357640190
VERSION     WP_357640190.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 514)
  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 514)
  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..514
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..514
                     /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=56234
     Region          1..430
                     /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 mriavvgagf agvsaakvlr qsgfdvtvfe rapdvggvws rtrrypgltt qndkgtyhls
       61 dlpmpahypq wpsgeqvqry letyvekfgl asalrlstev vsaelvndet gwlvtsrptg
      121 aqepltvqry dhlivangif sdplvpsfdg qaafaaaggr vlatgefpdv eaargknvlv
      181 vgygksacdv avpvsevaaq thvvarellw kmprklggal nykyllltrm gealfrylhl
      241 kgferflhgp gnglrqrmvt svgsvatrqf nlralglvpn gsfediarst vslategffe
      301 rvtdgrivvh rdqvitellv ddagrpaarl adgtvlpadl vlcgtgfrqr vpfldeavha
      361 rlqddagnfm lyrqilplgv prltfagyns sffsplsaem aavwtaaylr ggitlppeer
      421 mrdevrarla wmtartngrh argtniipfs mhnidevlde lglnlgsltr arqwllpvdp
      481 gsyrgvtaqm irrtadpvsa isddspikmd kvrr
//
LOCUS       WP_357640218             204 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357640218
VERSION     WP_357640218.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..204
                     /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=22499
     Region          7..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meetrrerkk rqtkqllvst ayrlfseqgy erttvaqits eadvatktff nyfpskedvl
       61 fsdaehyyet alevlaerap degvpelllr tydrviaryl adgplagdre rmevygnlim
      121 svpavqakal hvlfdlqski agafvkafpd eldpisaaaa lgallgavqa atrtcgelhg
      181 hseeeylkag rraveiamrg lgal
//
LOCUS       WP_357640222             144 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine hydrolase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357640222
VERSION     WP_357640222.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..144
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15415
     Region          <29..124
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 marattsirp halaylphgd tsrrrpgpaa vwdamghrdg evlirkpsyg afydtpldti
       61 lrnlgrdtvi vtgtltnycc gttarqayer gyrvvfgadv tatddetrqe pelavlrkgf
      121 alvltaaeie arlaagaaap adrg
//
LOCUS       WP_357640268             451 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome b [Nonomuraea wenchangensis].
ACCESSION   WP_357640268
VERSION     WP_357640268.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 451)
  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 451)
  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..451
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..451
                     /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=48842
     Region          12..393
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mrssvagrrs frfshwsfmf aeiavwsfav llvtgavlml fydpgmtrvt ydgsygplrg
       61 llvsrafdsa mhlslevrgg llirqmhhwa alvfvaaval qllrmfltga frrprtrqwl
      121 iwvallglam aagetgnalp ddnlsggslw lilsvvqsip vvgswvgsll fgtafpgdqv
      181 ipvmyglhlv iplvmaalli vrellvrrhg hsrfvaslpe rrgarplmaa attgmliilg
      241 fgfqiapiwl ygpatpsqis agsvpdwymg fldgalrimp gweltvgght lslavlvptl
      301 vvpglfftal aayptaerll aarrgrpaag rdvldrpret pvktglavag vtfygllwaa
      361 aandqlahqf hltvnavtvf fryaviigpv vafavtrwic lalrqaeret aehgvetgii
      421 vrspdggfhe riappdaadg rrhlaaktav q
//
LOCUS       WP_357640392             424 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357640392
VERSION     WP_357640392.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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 424)
  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 424)
  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 424)
  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 424)
  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 424)
  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..424
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..424
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47351
     Region          1..406
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mlirfrvanh rsicheqdls liatefdegt grrtglqhkg rdvalqpvlg vfganasgks
       61 nllsafqlma eavrdsfadw aktpgtvpre pfkldsasre etslfevdlt lgrdpvryty
      121 gfelsderve aewlhayphg rrnvwfdrea drpesaggef vfrgegfrge rdslvkltrp
      181 nalflsvgat lndpqlsaih rwflndlqlv tpgrdlksst nstrglltrp dragiyeqri
      241 vrllqsadlg itgldtdpet geirlwhrtp dggeapldfr teeslgthaw faflgpmltv
      301 ldrgsillvd eldsslhpal aaevvrvfqd ptsnphdaqv iftthdatll gsavldrpln
      361 rdqvwitvkk rsgetelypl tdakprkeen lergylrgry ggvprvtage ivrelswret
      421 kata
//
LOCUS       WP_357640393            1030 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357640393
VERSION     WP_357640393.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1030)
  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 1030)
  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 1030)
  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 1030)
  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..1030
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..1030
                     /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=112995
     Region          1..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          126..1022
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          775..803
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(819,822..823,825,849,858..859,862..863,865..866,895,
                     898..899,902..903,906)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          819..842
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          847..883
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          894..920
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          934..962
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          974..1001
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 meiqvlggls vqllsrtlrl gtpkqqaifa mlavqpgrlv tvadcidelw adrpprsava
       61 nvlsyaanlr rtfeaspygr gvvvrqrngf rldvppelid vacfqsersa grealevghl
      121 eqarellsra varwqgpmla giplgpvlsa rvlaaeeerl lavelladvq mrsgrgdlai
      181 pllrevtvrh plreptylll mralyeggdh agalvaydei rarlitelgv apgasieelh
      241 reiatpsplp avlfragarp gpasalmhaa ageaaaeqtg qvtpvdhlpr avadfvgred
      301 vllrllaetr rveervpavh iidgmagsgk ttlavhlarr lsdrypdaal fidlyghgdk
      361 nrieparalv tllrqlevpa drvpvefdar velwrrelgr rrsvlvldna asseqilpll
      421 ptepttvvlv tsrrrlthpd vapsqtlpvm tpeesldlla lsvgkarvea epdaaaevvr
      481 lcghlplair lagarlahrr gwrladlagq magdplvlhh laqeqstvtg afaasyeplp
      541 gstkrvfrfl glypgsrfgv paiaaltglt iaearaaldd lvdrnlvedl dstryrlhdl
      601 mrqysielcs gtdssndrrl glarlfdftl eavlkvadll epgvirsqvt hvpsgqvelv
      661 eavgeptaew leveradlvt mvlaaresgf yqhcwqlara lwrfcyirgy fediilthrq
      721 gleaaeavgd idalalmnny lasayvrtgd kqgaldhltr svdlsrnsrd vlnparyran
      781 laavywwsgh laesvklgfe clqdykvygd iggsillpnl glaltamgry eealrihrlh
      841 lawartnsde fhtlnalshi gavrlrmgdv pqairilqas lalrdrtghr yaeaevrndl
      901 giayrglgrv veaqqehela rrlaigsger hveaaalnel grtllaqgrg geavemhqaa
      961 lrlatrishp yeqgralagl adcfaradpa earrhweral aifrrmgvpe rfeaerrlav
     1021 lasttvvsgl
//
LOCUS       WP_357640406             348 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357640406
VERSION     WP_357640406.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..348
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..348
                     /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=37760
     Region          11..348
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 miarhdpqlk sfasdnyagv hpeilraiad angghqiayg ddvytealls vfqrhfgera
       61 qvwpvfngta anvvslramt aqweavicae tahihtdegg apevvggikl ltvptpdgkl
      121 tpelidrqaw gfgdvhraqp rvvsisntte lgtlytpeei aavcahaher gllvhldgsr
      181 ltnaaaaldv plralttdag vdvlsfggtk igllygeavv vlnpeaatgv dyirktfmql
      241 sskmrfvsaq feallsgdlw lrnarqanam grrlaaavrd ipgvevprpv eanavfavlp
      301 revterlqkr frfytwneat gevrwmcafd tteadvdafa aaireems
//
LOCUS       WP_357640414             510 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357640414
VERSION     WP_357640414.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 510)
  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..510
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..510
                     /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=55184
     Region          13..464
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mndrslvgqe vagyyiediv gkggmavvyl aldprlsrrv alkilnpvls vddrfrqrfi
       61 lesrtvasie hpniipiyea nadadgvlyi amryvdgldl rrliydrgal plaqanqiia
      121 qvaaaldaah ahdlihrdvk panillagdh vyltdfgitk hrtsisgltq tdqfigtpry
      181 mapeqinkeh idgrcdqyal acvayealsg rlpfprdndi allwahlaeq ptplsqvrpe
      241 lpievdgvmm ralakspeqr ypsctafvta lrdaisgqpa gppptqqstv rqrrkaasat
      301 sggtvggtag psrlplvvat viaaiaalsl vvllvmtqkg dswaryqstt aapltfeypa
      361 dwtvrthgdl fvvasphaae fesmfvsgaa adwttvnevi tgdadnavgv yvqvsdalsa
      421 sataaqmkam legllpgeiv vdqpvpdrag dsdatrydgs lrdrnsgnrl gfvsyvidrr
      481 pkpllvlyfc aknrcddste grvrqsvhls
//
LOCUS       WP_357640503             317 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357640503
VERSION     WP_357640503.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=33671
     Region          98..231
                     /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 miahiavals lallapatpa aagtaellta qedtlplpgv svkyqekvgd pvrlssyglg
       61 tkstflrakt gntfvnqptl seaavspdaa tvagvpksyr agydsllltd rasgqtrrvr
      121 tvkkplaasy iswsrdgkrv altveqkagg kwrtvgftvv dvvagtartv rpagldesad
      181 fwwspggdlv arfgdglrty rasdgaalrt fagvglptgp edafspsgsr lttwcptrfk
      241 eqlclvnpat gkiagrvavs pemlwgwwde shviavmahq gayrlsvvdl tgkvtrvlag
      301 ipsqtwkasl wmtfrrp
//
LOCUS       WP_357640474             346 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357640474
VERSION     WP_357640474.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=35004
     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 mkerpaevep vasrgrpaal agglvvvfgv lvlaamasva lgarsvplst vldaltapng
       61 sgdhtvirel rvprtllgig vgaalglaga lmqsltrnpl adpgllgine gaalgvtlal
      121 glfglsdptv yvwfafggaa vasvvvyalg sagrsgagpv rlalagiavg mvftavasai
      181 lrmdpqtfdr mrfwltgsla gqtsdvllri apfmvvglvv glllarplnm lalgddagka
      241 lgvavtrtrv ltavsvtllc gsataaagpl wfvglavpha vravvgqdqr wvlpytvlaa
      301 pvlllaadva grliarpgev qvgimcavvg apifilmarr rrlaal
//
LOCUS       WP_357640637             201 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357640637
VERSION     WP_357640637.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 201)
  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..201
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..201
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22212
     Region          5..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 malgknydgq dcsfaktlev lgerwtllvi rdamcgvrrf gdfqahldip kavlsqrlsa
       61 lveagvlerr ryqdapprde yvltpmgrel wvpvlalaqw gerhlaaqgp rrlyhhatcg
      121 splepysvcg tcgrsvplee vevrpgpglr ddartdlvsl tlrsphrmla pipdkmgetp
      181 egrshelggn rvrgraaraa r
//
LOCUS       WP_357640666             189 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357640666
VERSION     WP_357640666.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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 189)
  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 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   5  (residues 1 to 189)
  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 189)
  AUTHORS   Rosinski,J.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..189
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..189
                     /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=21763
     Region          1..81
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 manrpsirql sdpgahkalg hplrqrilrh lgihgpatst tlgralgent gtlsyhlrql
       61 erngfieeip ersngkerww rqisadlrwp pagemdeesq klldeitefk vdqelelarr
      121 ffrdhrryge wakasrglth ltreeldeff eaymellsrf graqedaspg arpvflrfft
      181 mpasedpps
//
LOCUS       WP_357640672             329 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357640672
VERSION     WP_357640672.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=36021
     Region          1..327
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msrptgrvlt llellqsggt rtmaeladrl gvdgrtvrry vdqlidlgip ieavrgrygg
       61 yrlgrgyclp plmlnddeal avllgliagr rtglatatdt asetaaakir rvlperltrg
      121 ldtvleslaf tkpagepvtp dagtlltiad avrhrrpvsi rytdrdgrrs drtlhpygiv
      181 nhsgrwyvtg adpsisenrt frldrvtdar tlpgsfevpa gpdpaqrvls gfatasyrye
      241 vtlrihgtve qirarlpasl asvaeispta dqdpaaerwl rvelraerld wlpavlaald
      301 rpfvierpge lrdlvvalad rlasharrt
//
LOCUS       WP_357640711             374 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357640711
VERSION     WP_357640711.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..374
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39813
     Region          38..374
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mllpgygggs ladlpgalla algvpeparp enarltlapa dsvclflvdg lgadllrahp
       61 eaapflsslt artltagfpa ttvtslcslg tgmtpgehgm lgltlavpgt ghlfnclrws
      121 lpggqnmdpe qwqpaktvyq raaeagvrps yvapaefent gltravyrgv rylaadtvde
      181 riarvhealr ephahvtvyy gdldaaghmt gwgsdewlhq lavvddmaar laeglppgsa
      241 lyvtadhgmv natekvdaeq vpelmegval lggeararhv ytepgaarhv leawaetfhg
      301 kawvvsrqea vdsgwfgprv reewlerigd vvavphdgla iiapsrhrie alftgyhgsm
      361 taaeqnvpll evrp
//
LOCUS       WP_357640715             834 aa            linear   BCT 28-DEC-2024
DEFINITION  CHAT domain-containing protein [Nonomuraea wenchangensis].
ACCESSION   WP_357640715
VERSION     WP_357640715.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 834)
  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 834)
  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 834)
  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 834)
  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 19591576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..834
                     /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=88347
     Region          4..>149
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          121..149
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(122,125..126,129..130,132,164,169..170,173..174,
                     176..177,198,201..202,205,214,217)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          162..194
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          197..231
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          198..808
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
ORIGIN      
        1 msdapcplve aaeaamlrsl vdpehalraa gtvlaaarra gaheaeaval ramaladrel
       61 gdldsaehhl raaiavpgap rervaqarls lvtvrtelgh plqalrvaal awaylrpldr
      121 akldtqrava lahlgrhqea iascdralra lvhapgtvdd rrflagglln rglvrcwrge
      181 weaamrdlta cleisqhagl rhlarlsaan lpflavrrgd iagafhyyre aedtlfgype
      241 rlatmradfa gallaahlpg earamldlav palescgarv alaearlkla qvelltgdph
      301 ralqvgeqaa eelagqerts wlplarevvl rsrlalgpvt pelvsdliac adeledglaq
      361 lpgaaalrlt aaeaalavdd hpaasaqlar ltrhagvder pdepffggrl agewqvpapv
      421 rqhalaleaa lredvpgafr avreglaevg egvecfddps vrahaarage rlaafglsla
      481 vrdgrpddvf ewaerwravt apahgspatd pervraelgs gtlvefvidg esllavlvgr
      541 drvllrwlgg vraveeavvr lryalrrhge rrdwsgsagp dggndlevaa qevdrllfrp
      601 ldaelgdgpl vvvpvgalht lpwsalpclr erpvgvaasa agwlrararq drrgedaprv
      661 aaaagpglth ahaevahvla chrlaaeipa rggrvldalg evdvlhlaah gvfharsplm
      721 sgitlddgll maydlltler apelvvlsac nsgmsrapve gaplglpgtf laqgtscvia
      781 gmvpvqdeaa ravmstfhel vavgqppdaa laaasaktgv yeftcfgagd rply
//
LOCUS       WP_357640806             273 aa            linear   BCT 28-DEC-2024
DEFINITION  segregation and condensation protein A [Nonomuraea wenchangensis].
ACCESSION   WP_357640806
VERSION     WP_357640806.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=30165
     Region          9..253
                     /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 mttaeqsepq gfqvhldvfe gpfdlllgli akhklditev slsqvtdefi ayirsrgpew
       61 dldqtshfll vaatlldlka arllpsgeve deedlallea rdllfarllq ykaykevakv
      121 fsglmaeqal rfprtvqmep qfanllpelv lgigpeqlar iaaraftpka pptvglghiy
      181 eplasvkeqa ailvshlrrl rratfralva dcagtfevia rflavlelfr eaavtfeqve
      241 plgdlhvtwt gadegdvavg ddyeesaekp rnd
//
LOCUS       WP_357640857             319 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357640857
VERSION     WP_357640857.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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..319
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..319
                     /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=32122
     Region          16..319
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mrlspsdpsa strafdllvi gdanpdvvls gaprrlaygq reqlvsggdl vlggsgaita
       61 cgaarlglrv afagrvgdda agrfvldals argvdvthcv vgprptamtv vladgqdrai
      121 ltspgclpdl taddvprgla rhvhvssyfl qpalaaglpg llaeeragga stsldtnddp
      181 vgtwdglagv lpevdvflpn aaeavaiaar laaqplpvek aasveqaaar lgalgplvav
      241 kdgaegalaw eagrivrvpa vpmepvdtvg agdsfnagli aarlrgldlr eclrvavtcg
      301 slstqaaggt aaqptwkel
//
LOCUS       WP_357640874             150 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357640874
VERSION     WP_357640874.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..150
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16573
     Region          3..104
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mqrtnfrema csiartldvi gepwsplilr dvwagvsrfd qiqadlgisr kvlterlnhl
       61 idqgvldrha ydmrpryeyr ltakgaelvd llmvmagwgd kwlageagpp vlyrhhacge
      121 isrvdlrcah cgepmhagdv dllpgpgaag
//
LOCUS       WP_357640916             281 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357640916
VERSION     WP_357640916.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   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 281)
  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..281
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..281
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30547
     Region          4..280
                     /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 mrdapgqqvp vngrtvyvee sgqgqdwvvf eagsgcgrtc wdpvlppltg qarlvaydra
       61 gralsgpttq qlsvddlaad liamteavvp gefvlvahsm gglvarraae rlgsrlrgll
      121 lvdptpetap vydawdqttk kidrmlavtq alsrfrplar lfsgnvrplf sadtyqamla
      181 enftpagtaq trkemqavaa aiprfraqpp qlpkcptivl sasraakgre rqnaairehq
      241 rryaetlpdg ryeavdsahf iqaeqphlva drigrllsrn p
//
LOCUS       WP_357640966             765 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 65 protein [Nonomuraea wenchangensis].
ACCESSION   WP_357640966
VERSION     WP_357640966.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (residues 1 to 765)
  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   3  (residues 1 to 765)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   4  (residues 1 to 765)
  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   5  (residues 1 to 765)
  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 765)
  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 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..765
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=84943
     Region          7..749
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 matlapanpw tlvyegydpa aeglrealct lgngrfatrg atpdglcrtp gtyragcydr
       61 lasrvagrtv vnedlvnlpd wlpltfatpg sdwfhpdgae lleyrqeldl rrgvllrelr
      121 rrddagritr vrqrrlvsma dpalaalett ftaenwsgpl rvraaldgtv tnhgvaryrd
      181 lrgdhltdha tgdedgltwl tattrssrit valaarmdap vpgraerepg rigtehvlha
      241 eegvpvtvtk ivalvtsrdp avhdplsaal rwagqappfg ellaaheaaw erlwerarle
      301 vggpelaqlv hlhvfhllqt lsphtfdldv gvparglhge ayrghvfwde lfvlpwlnlr
      361 fpdislgllr yrwrrlpear aaaraagydg amfpwqsgsd greetqtfhl npdsgrwlpd
      421 vshlqrhvgl aiaynvwqhh lvtgsmtswc adlltdiarf faslavldpa sgryeirgvm
      481 gpdeyhtarp gaaapgldnn aytnvmtvwl laralelgla rpeesarwad itrrmrvdfh
      541 dgvisqftgy adlaeldwgr yrgvrrldra leadgddvnr ykaskqadtl mlcyllttde
      601 lldilrrlgy padpeliprt isyyldrtsh gstlssvvha wvlahadrar swqffaeaal
      661 sdikdvqggt taegihlgam ggtldmlqrc ylgleprpdg lrldpclper lgslslpief
      721 rgrrllvead hertrvdgit lprgaaatip fppliirrpg rvrgr
//
LOCUS       WP_357640979             216 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357640979
VERSION     WP_357640979.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..216
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21794
     Region          56..171
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mpyliaivvl vgalclldll ltlgvvrrlr eqtklidaly eavgtgvlag agdglsagev
       61 vgdfaattvd gasvtrdllp egtvvaflsp dcqgcheqlp evaswaagqd rarvlavvdg
      121 rsgdpaslvt tlspvaqvvv eeapsgvata frvqsfptff qvaaggrlla raprisrlpa
      181 gspavdvags savdvhgspa agiagssewq aeeqpa
//
LOCUS       WP_357641003             578 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357641003
VERSION     WP_357641003.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 578)
  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 578)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 578)
  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..578
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..578
                     /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=58863
     Region          157..576
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdeipdtvss kdrgpffarr lgrgqlvmld lvaglviafv fltsaaaaaq lpswakvalp
       61 lglglpvalr rvwpmpvflf tlalavvaqv tgavtfsyfa payalyvval neragslvpv
      121 saigslsllt vaglvvagtp qavpswvlnl deplmgiaal ggawtigrav yerrlyaarn
      181 aerlaaqavt qerlriarel hdvvthsvgl iavkagvanh viatrpeear dalrvietas
      241 rgaliemrhl lgmlrstsda adrtpapgla gldglvrqar sagievqfea rfnvatgers
      301 vvgsrgedqd dsdgkyvggd gpdgrgvagr gaagrdnddr dverrngidg idhgdtrgng
      361 gggngmsgat addsvtdgtt ahgaggggta adgvrtkgaw vngapvgtva sgpaasdtva
      421 sgtvtsdaaa sgavasdpca dgavvggrap egegiadkrv ggegvggatg avessaarlp
      481 egielavyri vqealtnvik haaparcrvs vlgdgrdvri evvddgpgrr tlpsagaghg
      541 ligmrervmm yggafeaggl pgrgfrvfar lpygedvt
//
LOCUS       WP_357641054             470 aa            linear   BCT 28-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641054
VERSION     WP_357641054.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 470)
  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..470
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..470
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=51174
     Region          29..>470
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtyrlapidt stfaaeraaa gtgvdgggdf tvigsvvqrs darghvtgrt effedvapar
       61 lahlkmhrsa rhharirdvd lsealavpgv lrilthtdip nnlytplkli gvgpddepil
      121 avdkvrylge picavvaete aaalegaari rvvyedlppv fdveealkeg aplvndyhgq
      181 nhfiyeghhc rrlrfgdvea afaradhvfe wryqsapieq apaettgcvv vpqadgrlri
      241 hsdtqacfft ldntalilet pfnklrivgg tvgggfggkv dvvvepvacv aamatdrpvk
      301 fvydraeemq vsspraaeri yikdavmadg riigrkvtly vdagayarht pygttkaaah
      361 lpgpysipnv wadchcvftn rtpssamrgf gvtiadfale sqmdriaral eldplrlrll
      421 nayrdgdlka hrkvaegtal veviqkaaem aghelpeayr rmssttregl
//
LOCUS       WP_357641059             348 aa            linear   BCT 28-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Nonomuraea
            wenchangensis].
ACCESSION   WP_357641059
VERSION     WP_357641059.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 348)
  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 348)
  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 348)
  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..348
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..348
                     /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=38103
     Region          116..344
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 mpryallilp afnrvyadss vrltrseldv fgarglrael sgseervfgg vpyvtfetaa
       61 plaerdvall snlssvyalf gvegsgvege deqpllrplp vrpldrlssd litiqkyagk
      121 tnehftklll nvtalasgkg lgerlsvfdp lcgrgttlnq almygydayg ldvdakdfea
      181 yagfiktwlr nkrlkhtaet vpvrreralv grrlnvtfgp skeavkhgdv qhlamvngdt
      241 lrsreffkpr sfdlvvtdap ygvqhgskgg sglsrsplel lrravpiwae llrpggamgi
      301 awntyggkre elaailtgag leimdypdfe hwvdqaivrd iivatkpa
//
LOCUS       WP_357641080             329 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357641080
VERSION     WP_357641080.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 329)
  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 329)
  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 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   5  (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
REFERENCE   6  (residues 1 to 329)
  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 329)
  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..329
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..329
                     /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=37194
     Region          17..329
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mtstlrpppp apprspqear spaprplrrg rswrqalrrd wqlyslailp llfflvfryl
       61 pmlgniiafr rfkpggsifg eywvglryfr mfltdptfwe vftntlvlga ltllfcfplp
      121 ivlalllnev rarrfkrfvq svsylphfls ivivaamvmq ltsiegtanq lvslfggdpv
      181 aflqkpewfr tiyvssevwq tvgwgtilyl aalttidedl yeaaridgag rlrqtwhitl
      241 pgirptmmtl lilnigsfla vgfekillly npltyptadv vstylfrmgf qssnfsyaaa
      301 iglfeavigl ilvlsanvis rrtvgtslw
//
LOCUS       WP_357641105             121 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641105
VERSION     WP_357641105.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..121
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..121
                     /product="YybH family protein"
                     /calculated_mol_wt=13648
     Region          1..121
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtsteaeilr tvldrwksav dahdpkrvas yftddvifqg lhpygigpes vaeyydsqpi
       61 gmtaaytile trrmaddlvl gylhvdftft drpvvtvnlc vlarrvgddw lidhyqvsrl
      121 p
//
LOCUS       WP_357641108             131 aa            linear   BCT 28-DEC-2024
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357641108
VERSION     WP_357641108.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 131)
  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 131)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 131)
  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 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..131
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14743
     Region          15..121
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mtvhrpepdr dsrewwerva rgefavqrca gcgadrfpar afcpacrsee wrwravppeg
       61 rveswivshq pfvpglatpy vvvmvrlaav pdglvhgnwr ggreprgger vrgvfrrvda
      121 dltlvdwepa g
//
LOCUS       WP_357641111             873 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641111
VERSION     WP_357641111.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..873
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..873
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93928
     Region          <27..872
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 madtagmrll erepslaala eyaaearqga grlvlvsgea gvgksalver fqeelpdarw
       61 swgicdglft prplgplfdv adqrrgalle lcragagree lfrgllhevs epgalnvvav
      121 edvhwadeat ldmlrflsrr lwsapvlvia tyrdegraad dlfrvalgdl asqrptrria
      181 laplsadavg llargsgwea salhrltggn pfyvtevvqa gvtqvppsar davlaratrl
      241 dggsrqvldv aaltgtrves rllesvtgcp psaldellgc glviedgpwl rfrheiarla
      301 vagavsahrg raihglvlta ladlgcddea rmafhaeaag daeavlrhap aaarraawla
      361 shreaaaqfr ralrfadgad astiarlyeg ladeaalldq wedaadaceh alaqwreagd
      421 rlregdtlrr lsrtlwnlvr adqavaaaea avsvleplgp svelawayai fanrrmlqaq
      481 hdaaiglarr aqtiaeglga tdvlsdvlnt maasaaakge dwvggmrral dlalaghhqd
      541 qagrafanfc atyvserqfa eaeplllegl aycderdltt yamhlrseqa tmlertgrwd
      601 eavtlcaeil attplsscsr lcivrklgai harrgepgvw eyldeaaeia drtcepqqiv
      661 pvrltraeay wlegkadhar reaelaaaas dgcdawdlga vavwlrrtgs rrpahgahae
      721 pyrlelggda tkaahawtel rspydaalal ahaprerelr qaleiltglg afsatrvvrr
      781 klrelgarsl pagpraatrg hpfgltrreh evlallcarc tnaeiaaklf isaktvghhv
      841 ssilaklgap srnaaadqai rlglaerepr aes
//
LOCUS       WP_357641115             396 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641115
VERSION     WP_357641115.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..396
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=41555
     Region          8..352
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mtehntshkv vvigggyagt laanrlrmrd dvditlvnpr pefverirlh qfvartgdpt
       61 idygtllgeg irlvvdsvtr idaaaravrl asgrtldydy viyavgstra vrpavpgaae
      121 fafdiaefed aqrlrarlee lpldapitvv gggltgieta aelaeqgrgv tlvcgrtlap
      181 tfsasgrryi akwlsrhgvv vlqdavvsev rpdavvvadg avrtsaltiw tagfgvpela
      241 aasglrtdal grlltdetlt svdddrivaa gdaaapsgqp lrmsgyaagp lgaqaantvl
      301 sriagtepav ldlaftgacv slgrhagirq larkddtavn iyiggrmgaa ikevtckfvv
      361 skrirgeark pgsmswpkgg prpeqpasat rvvtsp
//
LOCUS       WP_357641128             252 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357641128
VERSION     WP_357641128.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26449
     Region          1..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 mnllkdrval vtgssrgiga aiattfaqag arialhgrde aalaavqari dglggeaisv
       61 tgdvtvaddl tqireeildr ygrvdvlvvn agssdsrpmp iediteeswr adidrnltgt
      121 fltvkcflpg mkergtgnii tlssaagrkp sertivayaa akagvqlftq dlaaqvgpyg
      181 iranclapet iltetnqqwl padvqrslae shplrrlgtp edvaraalfl asddsswitg
      241 vivdiaggav lv
//
LOCUS       WP_357641130             128 aa            linear   BCT 28-DEC-2024
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357641130
VERSION     WP_357641130.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 128)
  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 128)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 128)
  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 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..128
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13389
     Region          15..124
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mpvgivhrda ataeffdgta rgellirhcd qcgafsapqa rtcprcgspe lswtaaagtg
       61 svvswsvvht kgappivvai veleeepwlq lqitgaapee vydglpvrva fehpeggeav
      121 pvfrpass
//
LOCUS       WP_357641135             497 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Nonomuraea wenchangensis].
ACCESSION   WP_357641135
VERSION     WP_357641135.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 497)
  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 497)
  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 497)
  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 497)
  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 497)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..497
                     /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=50600
     Region          35..>324
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mpqsgdllrl adavlfpgfa grtppdwlrr rlgeglagva lfsrniadpg qlagltaalr
       61 aenplvlvgt deesgevtrl evaggssrpg ayalgvvdde alteavardl gedlaragit
      121 idfapsadvn anpdnpvigl rafgsepelv arhtrafvrg lqaagvaaca khfpghgdts
      181 vdshhgvpvv agdgvedall pfreaikegv rtvmtghllv psydaelpat lspklltgll
      241 reelgfdgvi vtdgiemaav sgaygiggaa araiaagada icvggerade ataveirdai
      301 aaavtggllp eerladaarr vrelatwaaa ssggsldgas gpgdglglva arravrvtrr
      361 saapvlplsg pasvvelape mnlaidkgtp wgvgeplsrl lpgttvarlt aaeatgaale
      421 rllgeaigrp lvvvvrdahr yawqgealrh llsarpdavv vemglparad lgaahvstyg
      481 sarvcgqaaa evltgrl
//
LOCUS       WP_357641131             342 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nonomuraea wenchangensis].
ACCESSION   WP_357641131
VERSION     WP_357641131.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=35837
     Region          10..336
                     /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 mrtaltslvg crhpivqtgm gyvagarlaa aasragalgv igaatlsvee mtaairrvke
       61 rtdqpfgvnl rsdaddaaer vevlvregvr vasfaqaprr dliarlkdag vvtipsvgar
      121 rhaekvaawg vdavivqgge ggghtgplat tlllpqvvda vdipviaagg ffdgrglvaa
      181 maygacgvam gtrflltads pvpdevkkvy laaretvvtt kvdgvphrvl atpfvagler
      241 lrlarallng arfkrlsgls waamlregrr mrrgreltwa qvlqaantpm llraamvegr
      301 adlgvmasgq vvgviddlpt cqelverima eaaealgrlg rs
//
LOCUS       WP_357641142             298 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357641142
VERSION     WP_357641142.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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..298
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..298
                     /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=32509
     Region          48..296
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mcygygpsrr sllaaglglg aaalaaaspa aaatpphhsg gervppnqis iqlwtvrddl
       61 aqnydatlty laetgypkve lalgyfgrta qqlrqfldgi girassshdg lttdaagldt
      121 kianaltlgq sfmvvpylns tsedelkawa ermniearaa rsaglrygyh nhahefttdl
      181 gggktpwdvl taeldphlvh leidlywavt ggvgrgaadp vrfaldvire apqrvlqfhv
      241 kdraldgdma dlgtgtidfr rifdkhrvme yivendtpdv tprrtaevgy rylrkvrf
//
LOCUS       WP_357641164             519 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641164
VERSION     WP_357641164.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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..519
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..519
                     /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=55754
     Region          7..124
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          240..518
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mftlqalvdr gslelrvlap grpgaldepv twvhntelpd pshyvregel vltnglwldq
       61 vppehfvrnv mkakaggivf glrtetpatp pelvdacreg elplleisia vpftavsqav
      121 admltderkq alvgmvrrgd alataisrga gasgvldvlr rehdlplavv drmarslama
      181 gadlgtdqlh avatgltkrp palevdlgda graalfpvga vgdldaalic lrplrelaan
      241 erealeqtar flslevakqq avqaiemrfa sellemilsg grrsaevpgr lrafgvdpgg
      301 plavcavafa lgetatmhgl aevigeffaa egvpvvvadg tqdvvavlpw rhperdlpll
      361 aqrllngvel rfpgrrpvag lgglaahsae lrprllqsrd tcrvlrrtrt gpsvrafael
      421 gthrlllgsl dvetlrqfsg ellgpmkdhd arrggelelt lrtyldhdgq waatagalhi
      481 hvntlrnrla kiteltgrdv grtedrvdlf laltidamd
//
LOCUS       WP_357641221             407 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357641221
VERSION     WP_357641221.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..407
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..407
                     /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=43849
     Region          4..397
                     /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 misapphtrr lawldalrgl asmvvvfeha lqplwpeara pikavfdpgw ygvlvfflvs
       61 gyivpasler rgsvrafwis rffrlwplft vcvagmalla avgwdslhtw wdsrpvalal
      121 ahagmlqnll yvpnlanvlw tlsyemafyl lltamftlgv hrrstatala faasavlgag
      181 llpvtllsag gagrmltvvv vvtavlaagl aavlrggrrv rqvgavviag tillllavnq
      241 sypgpwqglf ilatmfagta lyrvetgqig hghiawvali pvaglwlara esgvqvaiaa
      301 awltfaagva lrhrtmpswl twlglvsysi yllhpllles vefflpdasa vplavrltll
      361 aavyaallgl caltwrwvem paqrlgrrli sraepraepg leraasg
//
LOCUS       WP_357641238             354 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641238
VERSION     WP_357641238.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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..354
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..354
                     /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=37597
     Region          141..326
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mhrrvallsa valtvagalv pagaaqarsg tgldprpvrw satdssserr nvlqywtqqr
       61 tlaarpldtp aprrgdrsgg ptqgtpwatr gasatitqrt pwtsggtsrv qtasastaqq
      121 garvpnspgl rwtdggavvr ttgrvfftta eggnascsgt avtsanesvv mtaghcvkid
      181 gaahrnwvfi pgfdngrrpf gtwvatrmlt tqqwnanedi nfdiaavvva plqgrtltdv
      241 vggqgvafnq prqrqmfsfg ypaappfdgs rliycsgraf ndtvmtrdqg lrcnmtggas
      301 ggpwfqgfne stglgwlnsv nsfkydfapd fmfgpffgne amavyqaaqn tnat
//
LOCUS       WP_357641282             373 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641282
VERSION     WP_357641282.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..373
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..373
                     /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=38744
     Region          65..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 mvslrpqpkq teqtkqtkqt eqteqpeqte pterqpaggv aatnagrsaw lavclvllav
       61 acvlsivigt kniapntvwn afahftntdd qvlvrelrvp rtalglivga algiagallq
      121 avtrnpladt qilgvnagag lfvvfaigvl gltgiwsyvw faflgsavam ilvyalgsag
      181 srgatpiqlt lagvaigavm egvsagirll kprafdylrf wdvgtlagrp lsiagavapf
      241 vvvglvlala vahslnaial gddlarslgt niararalsm vavtllagaa taavgpigfv
      301 glmvphavrw mvgpdqrwif aytmvcapvl mlaadvvgrv virpaelqvg ivtafvgapv
      361 liwlirrrtv sgq
//
LOCUS       WP_357641280             359 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641280
VERSION     WP_357641280.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 359)
  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 359)
  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..359
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..359
                     /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=36283
     Region          23..359
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mgsgaagssa agsgldfgrr vvvvrgasvs lrfgvrtavv cgvlglaala vgvlalgtge
       61 fevpvgevvr vllggepgpa rlvivewrlp rvllslligm alglsgavfq sltrnplgsp
      121 dvigfntgay tgvlvtmmfv grdyyqtaag alaggllaaa vvyllayrmg vqgfrliivg
      181 iavsailgaa nqwfvikvnl qtavaaaiwg qgslntltwd qvlpvavsva lptallvalg
      241 prlslltmgd daaaalgvgt ersrlaylvl gvaltavata aagpisfval avpqlarllt
      301 rtagialaps avtgalllat sdwlaqrafa ptqlpvgivt vslgglyfaw llarhargr
//
LOCUS       WP_357641290             207 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF47 domain-containing protein [Nonomuraea wenchangensis].
ACCESSION   WP_357641290
VERSION     WP_357641290.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..207
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=21854
     Region          43..>136
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mrsllrdltg rtdrvltgqi itqlgaaatg vwlatasaag eldpatarar maevehegde
       61 araalvgqmr rsltspidre dlfrfsraid dvldavrdfv relhlfaapp dpsyaaplra
      121 laagieqlte aarllpgrpr aaaeaargak kpgvrvayql alaevlaapl tpdtikvtll
      181 ltrldaagts laaavdtlad gvikryq
//
LOCUS       WP_357641304             183 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea wenchangensis].
ACCESSION   WP_357641304
VERSION     WP_357641304.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 183)
  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..183
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..183
                     /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=20796
     Region          4..168
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mseqddrsrf eavyrrtyeq ilgyavrrcs spedaadvva etyviawkri aelpggeagr
       61 lwlygvarrv lanhrrserr rltrhteltd eiehlyaars hhseqhgvde amdmladsdr
      121 ellaltlweg ldpgeiatvl dcsrnaarir lhrarkrfak alektrpsaa gfasrpliek
      181 esg
//
LOCUS       WP_357641323             423 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641323
VERSION     WP_357641323.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..423
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45893
     Region          85..>246
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mrsslqwlsr vltgllmiag avvvpacvaq aqtcsttlph pddygitcvs vdrhlqdngs
       61 elrditmtst aifqasggtp aidplarpit vriylpkdyd parstryrsl yllngggdny
      121 dewttktdlv slveqagayd givvmptggm tgwysdwvgr tdgyfapkwe tyhisqlipw
      181 idanfntiad rsgrglagls mggfgtlkya aahpdvfsvi gafspgidlr gmpaqrtisd
      241 smwasgaaim pltdwgafrv nkyengvlvl dqdkqrryrl eslfgpytst vfngktvddw
      301 psvnpaelvt qgkyapysgr fglyaggcke lpgapgnpqy adghhpapkt caydskahdd
      361 alsvdetilg syasdfdktl tslgvnhryc ygtgghdwns wpddladflq yaygtapayc
      421 pna
//
LOCUS       WP_357641338             154 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea wenchangensis].
ACCESSION   WP_357641338
VERSION     WP_357641338.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=17302
     Region          14..152
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mstkrvheav rwldadeera wralrrmmia iqtrtahdla alglsepdye vlstlserpg
       61 rtstlgeqat kmgwsrsrls rhatrmearg llrrepdpdd grgcylvlte hgletledaa
      121 pahlesvrrh vidrlspadl salediarkl eepa
//
LOCUS       WP_357641342             227 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357641342
VERSION     WP_357641342.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 227)
  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..227
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..227
                     /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=24565
     Region          11..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markaprhae aerndhalle aakkvlavdg ahasvatiaa ragvgiasly rryrskdelf
       61 qhlcalsldq wisaaerglq hddpweglah yigacvefsg gslgplagti avtdemaakf
      121 trseelmrdl vdrahaagvl rsdatamdis llieqlgksp lieqldrqgr adlieaahna
      181 rkrtiaiald glrprhpqlp gtapspalla erwehtptdr trspers
//
LOCUS       WP_357641359             286 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357641359
VERSION     WP_357641359.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..286
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31786
     Region          14..76
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(20,24,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(23,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(30..31,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..279
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 marptgsptv rrrqlaaelr rlredrnlgi eqvaeqldwh ptklsrfeta rraiqpsdar
       61 allgiygvgp aerdallala rearqrgwwh aygpavpewf evyvglesaa sslqiyegef
      121 vpgllqtady iravhrasll dassedieqr vavrltrqkl ltsegapnvs mvmdeavirr
      181 vvggsevmha qlqrlldaad lrnvtlqvlp favgahpamd gafhvlgfap tdpcvvyiey
      241 htgtlylekq hevnrytvmf drlreaalsv dessaliqqv ardlpa
//
LOCUS       WP_357641402             467 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nonomuraea wenchangensis].
ACCESSION   WP_357641402
VERSION     WP_357641402.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 467)
  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 467)
  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 467)
  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 467)
  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 467)
  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 467)
  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 467)
  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 18763457
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..467
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52201
     Region          1..407
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
     Region          209..443
                     /region_name="COG4938"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443965"
ORIGIN      
        1 mitylrlqnf kawadsgkiq fgpitaffgs nssgkttflq smlllkqtae sadrgrvfdm
       61 ggpaslvslg tfnditfrhd sersvgidig wredepfqir steteersai aasddlslst
      121 rvreirnfpv vqrveyglgd lrfsltrsgs gkdeyalesn dypfkhvper pwllpspgkf
      181 ysfpdqvray yqnaaflsdl elqfenlcsr iyylgplrqd parqyiwsgg rpsdvgrrge
      241 lavealiasq adgktkvrgf ieqedgprrt rlitveehva swlkelglih sftvesvddr
      301 gtiyrvqvtr sagstpvllt dvgfgvsqvl pvlvllanap egstvlleqp eihlhpavqs
      361 rladviieaa kirniqvvve shsehfltrl qrriaerdvg rgirlepedc mlyfcqtdga
      421 astidrldld afgnitnwpd dffgnpfeea aamnraarnr andektg
//
LOCUS       WP_357641424             423 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357641424
VERSION     WP_357641424.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=45174
     Region          31..341
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrsprpihal taigglllla gcggggfagg sqakqseggq vsvrmlvnit pnltqaywdg
       61 lvkpfeqanp gidvkieapt gkgvadtlpq qlaagnapdv ietltadetl skqmldltdq
      121 pwtkdtplvk easlngkiyt vgvgvqaqsl vfynkamfek aeidkppttl defdtvmgkl
      181 kaagtlplqt ggefltglql lqlsspsraq ahptwqqdik ggklkagesl lpfleryrtw
      241 idkgyvdkna lgmkyadaet aflsgksamy vmgswftaae akakkdfevg vfpapvdkgl
      301 rypgpqgatm aapymilkst pqkdaavklv rwlvtdpaav ksqlkqdgnf rngvereftp
      361 lekqvqqild sapsgvaqge gygdatlpkg fnaawntevq glyvgkspke vaegvdrwla
      421 grs
//
LOCUS       WP_357641455             375 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357641455
VERSION     WP_357641455.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 375)
  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 375)
  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 375)
  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..375
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..375
                     /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=39381
     Region          40..302
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mwtktvlita fvtsasltgg tayaapatpv ggpalgsrgl vapegvkkpp ktkatsyvia
       61 dvetgqvlaa kdahgrylpa stlktltalt lipklnknlr irpsqnacnq egsavgltpk
      121 atyrvddlfk glmltsgnda amalaevngg laktmremne eakrlqandt vaktpsgldk
      181 pgqsssaydl aliaraglan pdflryistk tanfpapkgk tyqisnhnkl lwryqgmigv
      241 kngwtskalg sfvgaatrgg htivvtvmrh egyfweevgk lmdwgfsvrg kvtpvgqlvn
      301 plpaqapaap qarvsggpvt qvtpahqppl ldtaaqkqtd rtkavgaavi gggllfgvvw
      361 lvygirrrrr ggsgv
//
LOCUS       WP_357641443             131 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea wenchangensis].
ACCESSION   WP_357641443
VERSION     WP_357641443.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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..131
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..131
                     /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=14442
     Region          10..122
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdeqvvvgtw hyvlamhska mcalerelgd rhglgpsefe vldrivhhdr klrlqelcde
       61 vhlsqsalsr vvarlekaal vtrdacssdr rgifvcitpe grarhaaalp tqravlqeif
      121 aeapalpgla r
//
LOCUS       WP_357641471             120 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641471
VERSION     WP_357641471.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..120
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..120
                     /product="YybH family protein"
                     /calculated_mol_wt=13276
     Region          6..118
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mefspalaah lraietrdla gfmatvhqna tvilpngkll tgkdaigefh tawfgdpdws
       61 lqptvirtet ygesalavls vayadldpeg rpyeksyylt lyfaridgqw llvhdqntfs
//
LOCUS       WP_357641491             422 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357641491
VERSION     WP_357641491.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=45972
     Region          38..410
                     /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(148,150,274,276,307..309)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrksarlgaa vfgvvlavsa csagddepga aggqekvtls yamwdnnqkp vmeelgkaft
       61 athpnitvnv qltpwegywt klkaaatgga apdvfwmngp nfqlyasngv lrqleeeitk
      121 dkvdlsvypk plidlytfdg khfglpkdmd tigvwynktl fdakkvpypa ddwtwndfka
      181 aaaklsdpak gvygtaaqlt sfqeyqynti dqaggyvisp dgkksgydnp qtieglrfwt
      241 dliknkqspd lktmtdtfpl qlfeagkiam ywggswnvse faandytkdk vdvaplpkgq
      301 kqatiihgva nvvsaktehp aqawefvkfl gskqaadilg kkgpipayng tqgawvaahp
      361 efklrtflda vayaapfpvs kntaawneae ltyltkawtg eqpvekaate laaamnalla
      421 ke
//
LOCUS       WP_357641500             152 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea wenchangensis].
ACCESSION   WP_357641500
VERSION     WP_357641500.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 152)
  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 152)
  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 152)
  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 152)
  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..152
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..152
                     /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=16941
     Region          17..>122
                     /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 msdqafvpdd ftvpshlatp rfrleplgpq hnaadhaawt gsiehiratp gfrdrkwppv
       61 dgmtleanla dlerhaddfa rrsgftytvl dpatgdvigc vyiypsrrtd hdaavsswvr
      121 adraeldvpv yeavtawlst hwpfgsityh pr
//
LOCUS       WP_357641518             392 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357641518
VERSION     WP_357641518.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 392)
  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..392
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..392
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41756
     Region          1..389
                     /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 mgvldgyrvv dlsiamagpl aamrlgdlga dvikvepvtg ewqrhapagg atgnqvnasf
       61 lslnrnkrsl avnlksdegr divhrlaata dvflqnyrpg vaerlgmdhd tisglnprvv
      121 yvsmsgyges gpyvtrpgqd lllqamsgam lstgrdgdpp apagtyaida itaysafega
      181 laallhrert gegqrvsvnm ldaaiavqmq elsvftvggv pqrrgrephg htyirapygv
      241 fatkdgylal gmprldglav aldlpeladm dghtqrdeit stvarrlper ttaewldica
      301 rhdlwagpvy gyaelvadpq vrhngsfvty dhrtegtvtt pgfpyglsaa ppqvrrgapl
      361 vgehtaeilg elgyppehaa elvekgvlac ad
//
LOCUS       WP_357641530             394 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea wenchangensis].
ACCESSION   WP_357641530
VERSION     WP_357641530.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=41133
     Region          143..383
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrrlrgigrr algtvavgla lfgfglaely vplapyvegd gpdptelsgg wmavltvlla
       61 gyclavaacg typrvavvla gvcfvaqslt pllpespatp ltalvivcft cvavggrhap
      121 miaavsyfvs agiettiand pdwafiifva lavmgpayav rmrraeaerl valaaereaa
      181 arsderlrva relhdivshg vavmvlqaga aqavldsdvr qahesldavq dvgrdvvvel
      241 rrlllvlrae gslerlpslr hldpllsgvr aagvrvdltv dgdlgrvpaa vdvsgyrvlq
      301 ealtnvvkha pgaavsvtid vghtdlrihv vddgprivrr sdgsgfgltg iservelfgg
      361 tattrpvngg gfevrvelpl sgrsaapsrt gasv
//
LOCUS       WP_357641543             419 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea wenchangensis].
ACCESSION   WP_357641543
VERSION     WP_357641543.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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..419
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..419
                     /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=42769
     Region          <35..146
                     /region_name="valS"
                     /note="valyl-tRNA synthetase; Provisional; PRK14900"
                     /db_xref="CDD:237855"
     Region          207..415
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mhhrrlalls tlalaagsaa allpatataa qaqspagasa rpsaqpsvgg pvgglvrgsv
       61 rgqagvpvle qapardqalv rdqataparr qaqapargsa svrprpaqha aadsagerrq
      121 vvrywtearm eaaeplnppn pakgaklspa dvkapsaaaa pstaaptapp psavaptavp
      181 sspaapalqa arnggaawtg ggavvrttgr iffttqgrna scsgsavtsa nksvvitagh
      241 cvklngafht nwvfvpgydr garpygtwaa tkllttpqwd asedvdhdma aavvapldgr
      301 slvdvvggqg vafnqprrrq myafgypava pydgsklvyc sgrafddyll sddlgltcdq
      361 tggasggpwm lafdestglg tlnsvnsfky gfapnwmfgp yfgneaqavy qsaqttgvl
//
LOCUS       WP_357641551             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641551
VERSION     WP_357641551.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=34555
     Region          27..277
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msshpspiti sghelrqrar rqarrqesat awtfitpavl iilglsivpt vwsfllsfqa
       61 ddlvtpsrwv gldnyyaltq dphfgqavrn tllytvlyvp lsivlglala lalnrrirfv
      121 glyrtlfvvp fvisataqgt lfsfildpqf gaanavlhrl gispqgffad paqalpvlva
      181 vslwsglgfc vvvylaalqd vpqplieaar ldgagrwhll rhvtlptltp vsvflvlwqt
      241 inalqvfdlv yvttkggplg attvivyfiw eqafknftag ygaaaayvla valfviaagl
      301 rvirsrerqr legatr
//
LOCUS       WP_357641568             176 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357641568
VERSION     WP_357641568.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 176)
  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..176
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..176
                     /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=18712
     Region          1..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mttaddtrtr ilaaarelfa ergyaatsla diaaavgltk tavayhfhpk drlaaellsp
       61 vagdmlallg ddyadrpafv salvsfavry rsvirlfmed lagddavspv spdseaaair
      121 tfrdgifvkl agedpdaatt vrcwallgal qwgvaktmdl pedeveavll eavrtl
//
LOCUS       WP_357641628             133 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357641628
VERSION     WP_357641628.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 133)
  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..133
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..133
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14328
     Region          35..88
                     /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(38,42,67)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(41,66)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(48..49,60,63,67..68)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mvldphiael lgidlddpev qrenaaidrd mrlietlvgi rrqrgltqsd vaermgrsqp
       61 avsdferlgg dphlstirry alaigvdvfh svsmpgeasq tsstpakiqv cgwepakpqt
      121 sgtasislrr aap
//
LOCUS       WP_357641608             132 aa            linear   BCT 28-DEC-2024
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357641608
VERSION     WP_357641608.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 132)
  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 132)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 132)
  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 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..132
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14078
     Region          20..130
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 msadtatppl pdlpahlagy raacargelv vqrcagcgrw vqlpeaacpw cgggeltyep
       61 vtgtgvvhtf tvvhrsfapg yrgrepyvma wvdlpagvra fghvvgcape evrigmpvrv
      121 tfvdelphwr pa
//
LOCUS       WP_357641637             308 aa            linear   BCT 28-DEC-2024
DEFINITION  M23 family metallopeptidase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641637
VERSION     WP_357641637.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 308)
  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..308
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..308
                     /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=32771
     Region          42..250
                     /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 mdtstrveim raghlgrwaa lagvallasa csqatgvagv saqspatpta saspsvtati
       61 psqtppsqtl psqtlpsqtp tadpqsaetp pkgedpvkip ppklskytya fpvqgcrtty
      121 qrqllvlpkt tiwagkgcaf vapvdgvvde vntlnkwtpt tdvgayregr fvtiigddgv
      181 rylgghldav adglkpgvrv kagqmlgrvg nsgnardtgt nlyfaiswkt gpaywwvrrg
      241 mvnpwdylda wqsgnktlsp keetlkmrsr lgetprcavq casktvtepk kkktrvkptp
      301 tpiivdpt
//
LOCUS       WP_357641711             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357641711
VERSION     WP_357641711.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 191)
  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..191
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..191
                     /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=20568
     Region          9..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgrwepnarg rleeaalely gergyeqttv aeiarraglt ertffrhfad krevlfgggt
       61 lleerlteav aaapdsagpl eavaaaldav gplfqerher srrrqaiila haelrereli
      121 klatlagala galrergvge paaslaaeag iavfkiafer wadepgeadl rqamreafae
      181 lravtagtpg p
//
LOCUS       WP_357641738             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea
            wenchangensis].
ACCESSION   WP_357641738
VERSION     WP_357641738.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..212
                     /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=22277
     Region          14..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msgaappagt grrerkklat raalreaalr lavrhgverv tveqiaaead iavrtffnyf
       61 streealvat laagaealia efrarpgaes vltalreaal rvlrtgdlag pervqalrli
      121 vrapslepqr lavfaaqera laaaiaervp aaagarypal caataltamr lvldewldgg
      181 aasraalrks ldevmaelaa gldrpgvrlv dp
//
LOCUS       WP_357641790             230 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea wenchangensis].
ACCESSION   WP_357641790
VERSION     WP_357641790.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=24959
     Region          1..79
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtadfdglsd pkamralahp arlqilnrlg veesatatev aeiagitpsa asyhlrmlak
       61 ygfvedappr gdgrerlwrt vgkplsvgll pedqpevrda kvalmaafrr eanqeadral
      121 asvetepeew rdatvfdrtr vkvtaeeltg lykairelie pyavrrrert gvpdgaraae
      181 vqvnlfpvit rpvpglpted hglaqrgaea eqaereakga egargegsqg
//
LOCUS       WP_357641861             216 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641861
VERSION     WP_357641861.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 216)
  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 216)
  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..216
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..216
                     /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=23207
     Region          <66..204
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 msrntrrarr wpcalktrlt vlltvpatia raaprrlagk apdttepate ephrptgrpr
       61 rppdpvavrd vlrsalsaag sgravlgevd dallrgtava eiahlvtelv dnaltcsppd
      121 teveirastr egechiaivd qgvgmteger aaanarlrge rrffaaptry lghyvvgrla
      181 erlgvrvwld espphgitar valpgellvp srvngh
//
LOCUS       WP_357641876             360 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641876
VERSION     WP_357641876.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 360)
  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 360)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 360)
  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..360
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..360
                     /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=37857
     Region          166..359
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpqppldhma srpsepvggs rkgvafgvlv raiasrvlri tiaarlsvra iaarppiaai
       61 tsrapvmaia lglsvvlaii ldavvdggpa lavllyclgi aavrlplrhs vpigglaigg
      121 llvegaiygr lgrdlslils aclvflvays vkerraaraa eareavlaer ariareihdi
      181 lahslsaqlv hlegaklllr adktdealdr vvrardlaka gleearravs alredapalp
      241 qalrtlaeef qattdractl qisgtehrlp petelallrt aqealtnvrr hapgspatir
      301 lvyepgscdl ritnpagaer gtpgggyglv gmreraellg gtlsagettd gfhvhlwvpa
//
LOCUS       WP_357641914             453 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea wenchangensis].
ACCESSION   WP_357641914
VERSION     WP_357641914.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=48158
     Region          22..336
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrglaamvrd laartpesre rsvdmwrala iclvvfghwf vvavtyrdgr lsgynaldvl
       61 swldpvtwlf qvmpifflvg gyagsasmas hrasggdgig wvlrrtdrll rpttalfvvl
      121 plvsvaatva gvgsellgha awlasiplwf llayfvlvvl tpwlhalhrr agiaaplamv
      181 vvvavadllr rglhvpvvgq stylfawmai yqlgfcwrdg llrlsrgkal alaagglval
      241 igltvvgpyp vgmvgyntap ptlalmalaa tqtglvlalv paanrwlrrt gpwsvviavn
      301 aviltvflwh mtaaavaaal lfptgvlqqp pvhstawllw rvpwiaacav vlavlvalfg
      361 rielrrsalr paegrgpwrd gatvlglaav laglifvafs gpgyhgptgl swagvlsylc
      421 gaavlrvvrt rpvlpgsgrl sprstpgghv car
//
LOCUS       WP_357641901             285 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357641901
VERSION     WP_357641901.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 285)
  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..285
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31903
     Region          25..77
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(31..32,43,46,50..51)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          101..280
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtgdsgsspt vrrrrlaael rrlrkesglt teqvakrlev aqssvsries grrgikasdl
       61 rllleiygvd gekveelltl arqsrqrgww htygdvvpew fqvligleae aeerrsydve
      121 lipgllqtad yfraylatlp tsfgsddidr kiafrmarqe rmlqddarkl sfvlneaslr
      181 rvaaanmgpq aqfarltels qlphvtlqvl pfsaamhagm gggfvllsft spdpdvvyie
      241 nevsglylee radvdrynlv yehlmakaln pgqsrsfiak lgkea
//
LOCUS       WP_357641947             195 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357641947
VERSION     WP_357641947.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 195)
  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..195
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..195
                     /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=20910
     Region          12..148
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mggrpdevla pedwltdver araarfafep drrsftaahl lvrlcaaavl dtdpagltll
       61 qhcevhgpgh grpyieqaps lgvslshtrg yvcaaagegr vgidaervpp gpfdrllagr
      121 alterelaav ttneelirhw trkealikrg eltldglraa dadvagrhll ewtaegdivv
      181 avitdspaeq fplsg
//
LOCUS       WP_357641953             114 aa            linear   BCT 28-DEC-2024
DEFINITION  PaaI family thioesterase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641953
VERSION     WP_357641953.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 114)
  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 114)
  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..114
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..114
                     /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=11799
     Region          1..114
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mgiefveaga ervvgrmpva gntqpygllh ggasvvlaet lgstgaaiha gadriavgie
       61 inathhrsat sgfvtgvatr lhggrslaty eieitdeqgr rvctsrltcm lrdr
//
LOCUS       WP_357642016            1145 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing serine/threonine protein kinase
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642016
VERSION     WP_357642016.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11600203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..1145
                     /product="WD40 repeat domain-containing serine/threonine
                     protein kinase"
                     /calculated_mol_wt=121540
     Region          14..254
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(14,38..39,67,74..77,85)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,41,43,72,84..87,91,93,130,132,
                     134..135,137,146..147,150,164..167)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(21..22,24..27,29,41,43,72,84..87,91,132,134..135,
                     137,146..147)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(25,91,93,130,132,134,150,164..167)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(146..154,160..167)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          462..969
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          576..612
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          620..657
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          665..698
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <833..1111
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          873..907
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          912..953
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          954..993
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          997..1028
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1035..1072
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1081..1119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mipltpsdph rlgrywlagr lgaggqgvvy eaygeegerv avkvprfddp esrarlarea
       61 aaaarvasfc tariievaep yivsefvpgp nlrqviaehg pyegdslrrl aigvatalta
      121 ihqagvvhrd lkpdniilgp dgprvidfgv areagptttg pamgtpnyma pevlagrgat
      181 aaadlwawgl vvlfaarged aievrepvav igevmdfrpd ttgladplgr lvasaltkdp
      241 aarpsahaal ldligvggdp lsrggalagp lrspaepdlg aiaeelyeel seaeraavpe
      301 vllrmldgdg slrpvtreel peseavsall affeaaglvt stgesyelak paliqawprl
      361 rtwvadnreg lpvhrrlvea aglwdghgrk pgdllhgssl drtlqwaaae rkdltlarre
      421 refldaaakq trsrsrrrgl ltaalavllv aalgglgtae ylrrksgrqr ddalakslal
      481 qaadlresdp qlarlltvag wrlspdlaet rgalyeslsr pasdvftdpy aspssvygln
      541 dsgrtlaavq egrvrlwdvr thglvrefsg vgaavrqial spdgrtlavl egkgvrlwdv
      601 tagtaigatf gggfvtplaq grlafdragr tllvpegtgg aerawdvatr krltagsgag
      661 ldtvdparrv gvvstgghgk velwnlrtgk rlpapwlpak tevtnvslsd dgralmvsen
      721 aprpaerrmr vwtvpgggvi ggryggeadr navfgfgdry iaswtypgel ivwrcagwpv
      781 vlerdlpghv ndvhfdeadr vlrylsdnge idtvdvsmlf dqplamgipe gqallgpgah
      841 tvvitgpgei rlwdvaakrp lgspidvvgr epalafsrdg grlavgdksg trimdahtgr
      901 vldtikvadv gdvafspdgr tlavfpnrpd gtgaplelwn lakgtvtraa vpgpgtlafr
      961 pdgrllvagv epqpidpatg trlpiadglg rlngthafsp dgrlvafsgp drmtlwdadl
     1021 kapvgafpav pgsaiqeiaw spdgrtiaty eegdrvrlwd vpsrqplglv fdgqkkiplg
     1081 egslafsadg gtlysampdg vvrtfpldgg ktaaavcrra grsltgrewq rylpeadrfd
     1141 pcvsp
//
LOCUS       WP_357642080             297 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357642080
VERSION     WP_357642080.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (residues 1 to 297)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..297
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31028
     Region          2..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mievndltvr ygdatavdal tfaakpgqvt gflgpngagk sttmrailgl eapqagtalv
       61 agrpyasler plltlgalld agavhggrta rahvacvars ngigparvde vidrvgltpa
      121 agrriarfsl gmkqrlgiav allgdpealm fdepvngldp egvrwirelm ralaaegrav
      181 lvsshlmaem avtadhvvvv grgrliadta maalaerhrr dvlvhaadpa alatvlradg
      241 gvvraedgla vtglsarrig elafahaipl yeltpreasl eeafmeltdd sreyvar
//
LOCUS       WP_357641987             332 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357641987
VERSION     WP_357641987.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=33876
     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 mwtagalavl avsmvagllg gaadispwqv vlqaldwlpy vhvdsglapv eqgllfelrl
       61 prvlvaavvg gllaiagagy qgvfrnplad pyllgaaaga gltttvvivl vptpvvgipv
      121 aafagavggv flayvlgnta grsggtatlv lagvavtsfl taiqtfiqqf kveqlqriys
      181 wilgdvgggw dqfwlvlpya vvsavlllah grmldvlsvg deeatslgvr agrvrlavll
      241 aaslataaav avsgligfvg iviphvvrrl aggsyrivlp lslicgaafl vladlvartv
      301 iapaelpigv vtmfvgapff vavlrmtrqt at
//
LOCUS       WP_357642161             415 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357642161
VERSION     WP_357642161.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..415
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44281
     Region          1..>80
                     /region_name="PRK13355"
                     /note="bifunctional HTH-domain containing
                     protein/aminotransferase; Provisional"
                     /db_xref="CDD:237361"
     Region          141..202
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          230..405
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manfaerlgl amskrgftga qlaaalteag ipitrayvsq lrtgkqtnpt lqvlralaac
       61 lqvsvgwllg edatdsgave elqlraaaig asaaglsdgs lsvlrgviel araaeglpdq
      121 ppataeipea aapltapqre algdrlrnlr litrmspeev etslgrgaaa igaieegrva
      181 pgpvtverll tlygvtappt reyvlslarg erppswydag svpvwmaaty aleqraslir
      241 tyqtqivppl lqteayaraa ievsgsaglg qtsadaavrl mrsrqallnh gdgpvlwavi
      301 desvllrsia dpetqaaqld rlieyakrpn islhivpidd piflprcgsf tmwrfpeafe
      361 pdvacahaie sdevisdaaa veayhqaftk lsvsttmgde thellyahrd rlshr
//
LOCUS       WP_357642189             139 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642189
VERSION     WP_357642189.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 139)
  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 139)
  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..139
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..139
                     /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=15547
     Region          5..131
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 medvelsell hrvgrrlrhg yahrlaplgv npgqaralra ladadrplrm vqladelriv
       61 prsvtpvvdt leqtglvrre vdpanrrstl vvitpagrem hersrearrq agqdlfavls
      121 edqrdqlkel lgvvdgqpr
//
LOCUS       WP_357642243             448 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642243
VERSION     WP_357642243.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=48751
     Region          170..445
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mfarwsvrrr mtvaallstl vgyfvtavli tplansvltg yriehaagea rrvaagvqrs
       61 apdrmrpvta tedvdliqvv ddhgavrqas prllgyppli rdtstgednr ldttvctnrv
      121 pgvkclivvg yrvpvgstfw tvyayvpavp wyisplyvva vllavlllsa itayvarttv
      181 tralrpvtai ktelaeitat dlgrrvpplp hrdelddlar tvnqtldrle havqqerrfa
      241 sdashdlrtp ltamraqiee amlhpdeadw prtavallss ldrlqaivtd lltlakldag
      301 apglgadvnl aelveeelar rppgkrveln lrpvvvigdp lrltrllanl ldnaerhaes
      361 titvtvderg gwgvleildd gagiapdqre nvfrrftrld asrnrdaggt glglpiarei
      421 atahggtltv edsdtgarfv lqiprvss
//
LOCUS       WP_357642259            2028 aa            linear   BCT 28-DEC-2024
DEFINITION  RHS repeat domain-containing protein [Micromonospora sediminicola].
ACCESSION   WP_357642259
VERSION     WP_357642259.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sediminicola
  ORGANISM  Micromonospora sediminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 2028)
  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 13397747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2028
                     /organism="Micromonospora sediminicola"
                     /db_xref="taxon:946078"
     Protein         1..2028
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=215499
     Region          247..>995
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          700..1778
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mtvadrrate aagvdgvlvs vrpdagagav rvgvdyaafa eayggnfgsr lrlvtlpaca
       61 lttpsvpncr tatplvstnd paartvsaev smaaaagmtv laataeggga ggtyeatdlk
      121 psgswagggn tgsftysypl tvppaasgla ptvalsydsg svdgqtastn aqaswvgdgw
      181 stprsfveqs fascmddpgg saspvktydh cydgpiltla lngsstslvw datkevwkpe
      241 sdngekvthv enanngtgty ntdywrvtlr dgttyefgrn rlpgwasnka etnsvdtvpv
      301 ysshsgdpcy naagfsssvc tmayrwnldy vydahgnams yyykqdtnfy grnkgatdvs
      361 yvrdsylsri dygftdgnay gtppnqvvfn tgdrclsgtc qplnaankan wpdvpfdlic
      421 asgancddfs psffstvrlt siearqynta tsayekvdsy alaqsmpatg datsptlwls
      481 sitrtghdts aggsstpitl psvsftdikl anrvdvtggl pnfyrrrvat ittetgsvis
      541 psyelpvpct apvttdpatn trscypvywt pdgftnptkd wfnkwavtrv tssdptggap
      601 ltatsyeylg gaawhhddne vvkakyrtyg qfrgyakvrt fngdgvndrr tqsetayyrg
      661 msrnnnstvv nltdsaggth edvdelagke lettaylgen grvdsstits ywvsgatatr
      721 srtglsalaa kwvepiktyt rqavtssgtv twrytasens ydantasatl gemkntytyt
      781 vptnaaydqc ttytyapvnt gknlvglvaq tetvsvacgg ftqgspasep gsvntlsaps
      841 tvsrpaqvvk aertfydddt nfsttfpqta aptegdvtmt rtatdytsga yvwqtagrtt
      901 ydsygrakds fdgkgnkstt aytmnavnlv tgvtttnalq qsasttvnpr rgstltatda
      961 nlvvtrqqyd algrstavwl nnratsaaan qkftytvskt gvsavttekl nnsngyqktv
     1021 llydallrer qtqavtpqgg rmisdtfydt rgwtratyng wwddatlptv gmpvsaadlg
     1081 kqvpnqtfnt ydglgraviv eaakngltvs ktttvhggdr ttvvpptggv vkttvtdplg
     1141 rntevreysa kptvatpadt ftgtftvtgg tttvskygyd ghgnqatltd aknnvwtsty
     1201 dllgqvvaka dpdagnssmv ydangnltqt tdgrgktlsy tydaldrktg efassvsnqs
     1261 aanqraawvy dnsnavagvt natgkltttv ayrdgqayts qqkafdvfgn slgvtvtipd
     1321 segalagsyv fghtytsvlg lplidsypak gslpsemvlh gysgvldlpt tlagtnayas
     1381 gvtydawgrv nqqtlgstts aayvtntydt hngrlknqlv trnkttpstv deqayeydla
     1441 gnitrktskr ygastpaetq cygydglarl teawtatddc aatptdaskg mvgntigggs
     1501 aywtswsidv ignrtqqteh glgtaanivt dytydgngqn kphtltsatt ktgttttsts
     1561 sysydgagnt tgrnaaqgnq tltwddagkl sgvtggtsgs nafiydvdgn lmlqkepgkn
     1621 tlylpgqqlt lntgtnavdg aryyelpggg scvrtgsssa ytfavfdhqg tpslyldnta
     1681 qnptwrqysp ygaarggavt apdnrgflnk pmsptgvtiv gargydtalg rfisvdpiid
     1741 ikdplqwnpy ayghnspmvf sdptgmkdca ddpcktysmp tpdggeiihq pggkririkg
     1801 sgkgsqgggg ggkrppapar ctlatpeych pegarkespd dilqkfftgl vpgylspnlt
     1861 cgivgstdrc atyeyfrwgd rmtrelwltt efaniyleid rraasgelgg rqdfhfsdlp
     1921 pgvsrkafar dmlshatkga lgssrimalt gsfdvdwrvv gyesdnpvve yhvqnattis
     1981 sgtrvpglap prgdgnagsg adafpfersv iqsyrfratt cinsacpq
//
LOCUS       WP_357642295             130 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea wenchangensis].
ACCESSION   WP_357642295
VERSION     WP_357642295.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 130)
  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 130)
  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 130)
  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 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   5  (residues 1 to 130)
  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 130)
  AUTHORS   Rosinski,J.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..130
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..130
                     /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=13626
     Region          26..103
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(31..32,36..38,54..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"
ORIGIN      
        1 melleilecs ppltrepldv eqaagvarvf kalgdpvrlr ilsivasrag gevcvcditd
       61 afelsqptis hhlkvlkevg lltserrasw vyyrlvpetl gelsalltlp asgpaggttg
      121 lpaaaaavpr
//
LOCUS       WP_357642310             703 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642310
VERSION     WP_357642310.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 703)
  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..703
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..703
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=76057
     Region          30..696
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(496..497,500..501,503,527,530,537,540..541,543..544,
                     573,576..577,580..581,584)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          496..520
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          525..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"
     Region          610..640
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mqstgseftg dansvvqigt mhgainltsl aralplprql pspaggfvnr aeslaaldri
       61 latgsgtgav savagapgvg ktalvvhwah rvrdhfpdge lfidlggygp saplsadqal
      121 dsflralnva kesipetlae rsslfrslvs grrmlvvldn aadtatvrpl lpassgcfal
      181 itsrsslsgl vtregaarvt levlsssdav ellgqvigva rvaaepqaav rvaelcgclp
      241 lalrvvaera ldrpelalte lvaeleeeqh rldslassed elsdvraafs wsyralsvem
      301 qqafrllglh pgrelcteaa mallnstdqr atkrlldtls aahllegvaa sryrlhdllr
      361 ayakerlree tsakdqalav rrvlswylla adagrrailf yshevplvpr eqlvnplftd
      421 aeaamgwfev erlnilvavn qametgqydi awklpvvadg ffelhsywke wedihrtgae
      481 aarvlgdrlg easnvfalgd adwrggrqes aianyesals yareagdtwl tgfslrglgl
      541 iheemanree arnyfqaale vfrtgglrrg egmallslgk haahlghfde avslgaeavr
      601 vfveindrws eawgalplsr almelsrgae aiealvraar tfdrfkdrrs lamtlaalgd
      661 vhhrqgdvst ahnnwltaae lygtfgenvm aeelrakagd gde
//
LOCUS       WP_357642312             438 aa            linear   BCT 28-DEC-2024
DEFINITION  KamA family radical SAM protein [Nonomuraea wenchangensis].
ACCESSION   WP_357642312
VERSION     WP_357642312.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..438
                     /product="KamA family radical SAM protein"
                     /calculated_mol_wt=48953
     Region          17..385
                     /region_name="EpmB"
                     /note="L-lysine 2,3-aminomutase (EF-P beta-lysylation
                     pathway) [Amino acid transport and metabolism]; COG1509"
                     /db_xref="CDD:441118"
ORIGIN      
        1 milqqtgtrr fkaytskhld ellrragldd eerlkvrava tvlpfrtnay vvdelidwsa
       61 apddpiyrlv fpqadmlpaa dvarladllk aeapnaevqa eanrvraqln phpagqkeln
      121 vprigdepvp gmqhkypetv lvfpkqgqtc hayctycfrw aqfvgdadlk fasddvgrmv
      181 dyisrhpevt svlitggdam imgepvlrry veplleleql esirigtksl aywpqrftgd
      241 pdaddtlrlf ervvaagknl afmahfthpr eldppqvsaa veriigtgat irtqaplirs
      301 inddpavwts mwrrqlrmgm vpyylfverd tgpqdyfavp larayevfrd ayasvsglcr
      361 tvrgpsmsat pgkvcvdgvm evageqvfvl hfiqardpsl vgrpffaryd peavwltdlr
      421 pafgerfpfd psgaalps
//
LOCUS       WP_357642320             280 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357642320
VERSION     WP_357642320.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 280)
  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..280
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31282
     Region          10..72
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(16,20,45)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,44)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,38,41,45..46)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          98..273
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 masptvrrrr lsaelirlre qaglsveeag rrlewsrgrl nkmeankwtr pdlgnirall
       61 dlysvtdsaq reavltlarq srekgwwany qdiwrgslag feaeaslint yedlrvpgll
      121 qtedyatamf kggrvvadtq irrrvearla rqtilhdetp ptlwavidea alakpvggps
      181 vmrqqlrhii emsarpniyl qvlpnsagah aamdgaftil nfpdqndpsi vyietatsdl
      241 yleaaadleh yrlifdlirs salgpdssva rlttlidqls
//
LOCUS       WP_357642332             138 aa            linear   BCT 28-DEC-2024
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Nonomuraea
            wenchangensis].
ACCESSION   WP_357642332
VERSION     WP_357642332.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 138)
  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 138)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 138)
  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 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..138
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14523
     Region          18..131
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mtyaiegwfa vdadgvvllg trcaacgtvc fpprrgscpd prcdgtdmev trlprrgrvw
       61 sytnavyppp apyvaaqpyv pvtlaaveld gagivvlgqv adltvdelev gmeleltagp
      121 ladgplvwmw rrasgaas
//
LOCUS       WP_357642327             269 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642327
VERSION     WP_357642327.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 269)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..269
                     /product="phosphotransferase 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=29372
     Region          19..239
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mifnkigacm daqaskhtie vrsdvvikqy rrldygqper ewralellne yspglapapv
       61 kadleadppt vvmsrldgaa vegpitgqla dalaeavtgi qlaipqrvle rvparaghpv
      121 ellhqvrsww aaavpsdvep avrdafheag swveqptleg llaqpgtpaf gtgdgnlany
      181 lwdgtkvgvv dfefsgrsdr afelaevveh isvwrndaag mtavlerfgl tadeaarlte
      241 crrllalywl lrtreetqsa qaervlall
//
LOCUS       WP_357642348             355 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea wenchangensis].
ACCESSION   WP_357642348
VERSION     WP_357642348.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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..355
                     /organism="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     Protein         1..355
                     /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=38802
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 magievsalh krypdgtvav dhvdlsirdg elfvmlgpsg cgktttlrai aglerqttgn
       61 irigdtlvdd lppadrdiam vfqfyalyph lrtrdnlafp lraeglpkae vrkrvdeaag
      121 lmrlgplldr rphrlsggeq qrvalaralv rrpraflmde pltnldaelr admrteikhl
      181 qgelgttmvy vthdqveams lghriailnk grveqigtpl evydrpaslf caafigsppm
      241 nlievevadg klrsqgglal tpppglprdr rlvagvrpea levtepgaer svparvvsae
      301 wlgdeiiyvv dhdgqrdirv rmpptvrfta dapvglrhtg gpppvydvst eelva
//
LOCUS       WP_357642353             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea wenchangensis].
ACCESSION   WP_357642353
VERSION     WP_357642353.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea wenchangensis
  ORGANISM  Nonomuraea wenchangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea wenchangensis"
                     /db_xref="taxon:568860"
     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=34899
     Region          17..312
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msdsaplttd hpgqvasatp papgrsrrls drwlavafts palllllams vfpllwalyl
       61 sftdysatrg gpaqflwfen ytailtspqv hqralttliy vvgavalqtv lgfaiaylis
      121 rrrhgrgllt tlflvpmmls pvvvglfwrf mldaqfgvin smlgslglgq vewltrqgta
      181 lislvlvdtw qwtpfimlia lagltavpky lyeaasidra sewfqfrtit lplvwpllli
      241 avlfraieaf rlfdlvyilt sggpgvstet lsfhvykvaf lgfntgtasa ygilmvvivi
      301 vltqlylryl nklked
//
LOCUS       WP_357642406             293 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357642406
VERSION     WP_357642406.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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..293
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..293
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29727
     Region          <193..266
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 miilssayaa liavllyaav skardlagfa adiagyrlvp lrltvvaava vvvaelaavg
       61 lltapptrrw gaflaaalfa vflaamasvl wrgmsvgcgc fgdrgligaa tmtrtgllaa
      121 lavmaavags spftpvhllv gavclaltfl aarlvgaver grvgprpgtq wdvtppaval
      181 tsekpgvlya liapacgvcs amlpafvaae qvdvvlvsaa eegevrdyla aqgvelplvi
      241 dpgvfdrhgi pwppyavltd rrgvvlaagg aaepealdal larvpsapgr trt
//
LOCUS       WP_357642476             219 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: potassium channel family protein [unclassified
            Nonomuraea].
ACCESSION   WP_357642476
VERSION     WP_357642476.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=23354
     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 vgrsiaaell enghevllid idpraikids vpraewllad aceiasldea
       61 glnnchvvva ssgddkvnlv vsllakteyg vprvvarinh pnnewlfnes wgvdvavstp
      121 rllsalveea vsvgdlvrlm tfrqgqanlv eltlaedapv vgqragsvpw pndsalvail
      181 regrvlvptn ddpleagdel lfvanqeveq elahllsqh
//
LOCUS       WP_357642487             383 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642487
VERSION     WP_357642487.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 383)
  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..383
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=39835
     Region          147..382
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 matrpqtakk illywmdatv almgfmlsmm vltsaragri svphavaaav cvlavlaflp
       61 lilrdayddr prptaklvag glfaagaval vppsatttgs wemigclwls glslylplra
      121 tacvgaalva ltafyvsavs dqswpyllis ltlsavllsg tmrlwrwlww tireaydsre
      181 akatlavsne rlrfardlhd llghslsvlt lkselaakla tidagkaaae madvgrlaae
      241 slaevqvavd gyrvldldee lagvraalea agarcviear tddlspaart llawavrega
      301 tnvlkhstat rceividggv lemrndgvpa patsgatsga tsgatgagsg lrglaermaa
      361 aggsftaast pagefllraa vpa
//
LOCUS       WP_357642508             294 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642508
VERSION     WP_357642508.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   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 294)
  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..294
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..294
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32215
     Region          5..294
                     /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 mfqhpngrhh qirghrlwae qdgagppvvl laglgpagsh vvfhphfdal aadhrviyvd
       61 lhgrgrsdrp adlgeitfas dvadvtallg eigpahlygf syggliaqai aldhpslvtt
      121 ltlanslhsp emwqlnhani nrelaaqlpe tweriqmlrr sglrstsapm raefaaaapl
      181 irfydpanaa llatepgarn eelyplfcgd dvdfviggqv atipdfrprl kelavplmvl
      241 agrydralyp alqldflrfa prarfemlar sgsfghveep etvlgllcef wrsa
//
LOCUS       WP_357642611             456 aa            linear   BCT 28-DEC-2024
DEFINITION  uracil-xanthine permease family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357642611
VERSION     WP_357642611.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 456)
  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 456)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..456
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47501
     Region          11..448
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mvfgwtkhgd gkhlapgevv kpderltwpr migfgaqhvi amfgatfvfp lvmglspnva
       61 immsgvatim fllivkgkip sylgtsasfv ggvlairavf ggdtpgadai vtgailvvgf
      121 vlalaglavh flgvqiihri fppivtgavv mligfglayv vadvywpkdq wmalitmlvt
      181 fvivvafkgf igrigillgl ivgyalswva drlfgqvpay tdgaltiaph lrvdfsklea
      241 apwfglppfh lpdfkvsavl lvlpaviali aenighvkav gemtrtdvdp yigraiaadg
      301 latvvtsavg gsptttyaen igvmaatkvy staayyiaal iailfglspk fgalvsatpe
      361 gvlggvtvil ygmigllgak iwienrvdfa dpvnmvpiga giilaigpvk qlisgdfrle
      421 giafgtivvv ggyhllrvia grpaeaaatd rgseag
//
LOCUS       WP_357642637             134 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642637
VERSION     WP_357642637.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 134)
  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 134)
  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..134
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..134
                     /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=14928
     Region          2..134
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msrrrlgyll khanlrlaqh tgpalepygv dgrelavlnv ldaadplsqq eaatrlridr
       61 ttmvamidtl egkelvsrrp hpddrrknmv eltprgrdtl reggqavdea eraflaklap
      121 ddaarlrell dkli
//
LOCUS       WP_357642648             288 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642648
VERSION     WP_357642648.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 288)
  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 288)
  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 288)
  AUTHORS   ter Beek,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..288
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..288
                     /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=31787
     Region          24..286
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrqrlrdpvt gllfvlpvlv lflifrifps laaagmsltn wniggewsfv gadnyarlld
       61 daifwtslrv tlvyvavyvp ltllvslgta lllnqvvflr glfrgmlflp yvtsfvlagv
      121 iwrwiyefdg lingvlgkag lgpvafleqs slvlpalavv sawkgfgysm lillaglkai
      181 pgsyleaarv dgasawqrfr ritlpllkpa lffvlvieti safqtfdtvy vmtgggpara
      241 tytliygiyd hgfrsfdfgy aatwgmvlfa lvlivsliqr rfldrgnt
//
LOCUS       WP_357642708             216 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357642708
VERSION     WP_357642708.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 216)
  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..216
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..216
                     /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=23540
     Region          8..144
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpteplsrtr ivaaaidlie regadavsmr riaadlgvgv mslynhvpnk dallngvaea
       61 vlsqieftdd pdahwtdrvr mqarafrqia hghprstmlv vsrqlhsnag llpveralat
      121 lrsagfdgvd avrvlrmfia yivgsllrev gvtptfvppr qhlvnpddvd ptlfpevngl
      181 apllsscdhd adfdfgvell iqaiavlpkr kregtr
//
LOCUS       WP_357642733             159 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642733
VERSION     WP_357642733.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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..159
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..159
                     /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=17253
     Region          7..149
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mfmgegvewg lhcclalawl eeqapvatgq laeifelppa ylkkrlqplv ragilastpg
       61 arggyrlart peritlmdvv saiegsaeaf rcteirqrga gaetparefe rpcgiatamr
      121 raelawrrel aaqtladlia aspagaprrt qrfhqrlgs
//
LOCUS       WP_357642760             324 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357642760
VERSION     WP_357642760.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 324)
  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..324
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..324
                     /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=35292
     Region          12..>264
                     /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 mkdrpagvde ralrdalekw gigavsleya pvgfgdyhwi aadadgprwf vtvadltqkg
       61 qtgdgesalr ramdtavalr eqgldfvvap laaaggetlq llgaryavsv fplvsgrpge
      121 fgdriaager rrtvemlael hrttpppstp vrplripmrg rleeaieasg gvwrggpyae
      181 paralvadra grlrerladf drrvdeasga dlvvthgeph pgnlvmveds pvlvdwdtvg
      241 lapperdlwl vadgpddlar yaeltgrrpd pavmelfrlr waledvalyv eglrsphels
      301 adtreawkal tetvreltdp vskt
//
LOCUS       WP_357642768             225 aa            linear   BCT 28-DEC-2024
DEFINITION  adenylate kinase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642768
VERSION     WP_357642768.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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 225)
  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..225
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..225
                     /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=25608
     Region          1..208
                     /region_name="Adk"
                     /note="Adenylate kinase or related kinase [Nucleotide
                     transport and metabolism]; COG0563"
                     /db_xref="CDD:440329"
ORIGIN      
        1 mrkyvilgvq gsgkgtqstl latdldlvhi svgdifrwhv kshtklgaqv rrlvtagelv
       61 gddlvedvvr erlqqhdwny gfiidgfprs rrqaeffles ydidsvihld lpdeevwrrv
      121 larrlcsrcg mdynliahrp eaegrcdvcg gelvtredda pdalatrlre yhdkidpvve
      181 lfrgkeyvmt vdarddkatv qrnirarlhl ppyvreksgr gvaae
//
LOCUS       WP_357642772             434 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357642772
VERSION     WP_357642772.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 434)
  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..434
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..434
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46518
     Region          17..397
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mnpplttwpt ydkgdvflsp ediaaaieal raqlffrydf rpheetftgl lerrlcevfg
       61 aghalacasg ttaitlslla lqlpagspia cpaftfaatp saillaghrp vlvecdenlh
      121 ldvrdlrrvf degakavvvv hmrgfasdmp eicrlaeeyg alvvedavpa lgarldgryl
      181 gtfghfgafs tqsdkslntg eggflltddp eayaravvys gayegrmarh fpgkvpdvdd
      241 rafpifsfrm deiraalaaa llqrlpdrla ahrrnydyva erladldgia lrqpvapgay
      301 lgealvfrlp gatprecvaf agavaaegvd aralgdrddv nvrafwnwrf llgdnpeaar
      361 slfptsaryv seaidiplsa nldladcdrl vtavrkaaag raltqpnges aaagrapatk
      421 pngesatagr tasr
//
LOCUS       WP_357642802             497 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642802
VERSION     WP_357642802.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..497
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53071
     Region          70..311
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrtgrgtvsv aaglvlvala avgyvlppaf npaplqadht mqalppqpan esrpvvaavp
       61 vhqeeislpa egqtlfgtvr apttpgrhpa mvfvsgsgng srteftpqae flakagvvtl
      121 afdkrtvgyn frdrdfglla ddalrmveym rtrpdvdpar tglwgvsegg wvvpiaaaks
      181 rdvgfavlvs spnvsplrqv awalneqlqr lrapigvrdl ltramggvgf nflrydampa
      241 lrqirqpvla fygtmdpsip fvessqslit alksagndqy tirfmdkadh amrisggpfa
      301 hgyletlanw iiglpgtarp plhvagttpv qrfeasdvpa apwyaggtml glticlaavg
      361 yvagpvaamv vrlrgrrqtp adtnarlwpp irrrlrrmaw tglgllvsvl afitvlvlfs
      421 vnqagawpav lagwlvvrvl avlmlvqevt avaavvaglr eglrpsrwqh vaiagvlggt
      481 glllvaaayy glfafpw
//
LOCUS       WP_357642847             343 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642847
VERSION     WP_357642847.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 343)
  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 343)
  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 343)
  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 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   5  (residues 1 to 343)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..343
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..343
                     /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=37381
     Region          1..231
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          240..318
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maleltftaq daahvrfavs plwevvasvr vvknpaahav lkpwaervrr rlanvdwrll
       61 sdlvpvptts ivgfvsppps tsvpdlevel atmvamaplv regldiwdgp ptralqalha
      121 dpagglerla eeirgywdaa iapywpriss lldgdvlyra rslaegglrh mlsdldtavt
      181 wegetlrlpk tacegvrplg glglllvpsv ftwprvfsit tppwqptiry pprgvatlwe
      241 hresdppqal aavlgrtrar llaeldqpas trelatrldl sepganqhlt alrkagltsa
      301 hrtgryvlya rtavaealla geatsadsvr esdradrgir dir
//
LOCUS       WP_357642857             314 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642857
VERSION     WP_357642857.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 314)
  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..314
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..314
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32585
     Region          75..313
                     /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 mrsvqkilga garitdsrav apltrpsfar fkvsapvaaf vllitsaava ptpdamavas
       61 tpvsanrqap grspgaarpt vvlvhgawad tsswsgevra lqraghtvra vanplrdlts
      121 daqtvrdflr tvsgpvvlvg hsyggsvitn aaagdpdvka lvyvdaaapd vgettgqlsg
      181 sgsalggdpa tlydrsaypg apgkavdlyl kqhvfvrsfa sdlprdtadr lwasqraast
      241 aafmtpskaa awktipswyf iatgdriivp asqramakra hskitefpgg shltlishpd
      301 avtsviedai rsvr
//
LOCUS       WP_357642916             114 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357642916
VERSION     WP_357642916.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 114)
  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..114
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..114
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12470
     Region          30..100
                     /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 mshsrwktlr erklaadfte pedvaearre irlsmalaka vygrrtelgl tqaeladrag
       61 ltqakvsrie gsdtiptlpl laklaealda tlnialdndd tqvsfaghrt trpe
//
LOCUS       WP_357643001             360 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643001
VERSION     WP_357643001.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 360)
  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 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   3  (residues 1 to 360)
  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 360)
  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..360
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..360
                     /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=38874
     Region          3..336
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpsplrvavv gggaiasfah mpafqelpdd ievvavvdat telaqafadr fgvpyasddl
       61 egmlaevrpd lvdvcsppsl havqvaaalr agawvwcekp pclslaeyda mvaaereggp
      121 yaaivfqqrf gsgaqhlrrl iekgalgtpy vahcqttwyr ddayyavpwr grwesegggp
      181 amghgihqld lllellgews evramaarla rdvetddvtt alvrfesgal atvvnsvlsp
      241 rqvshlridl adatlelthl ygyanddwtc tpaehagqid wppaedepts hlkqlrvlvt
      301 dlragrrpra sgrdgrrsle litamykaal tggtvragev gpgdpfyrsl hgetpgwsps
//
LOCUS       WP_357642998             299 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357642998
VERSION     WP_357642998.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..299
                     /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=32490
     Region          3..206
                     /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 mhilvtgatg tlgkavvptl lrtghtvral srqarsgrdv ewvlgdltwg kgiysavrdi
       61 daiihlatfa rkahragsvd vagttvllda akeagvphlv ftsivgadqa atgyledkle
      121 aerliresgi gwtilrsttf hqhldqllre laaaspaipm drtlpwqpvd rsevavyltd
      181 lvaagpergv ieyggpevig mdevvrpwlq arrlrrlllp vrypggrwaa qragwhttda
      241 tplgriswrd ylfpappeps ddfavehtas ptspatqpdl dpnahvyggd egyerptra
//
LOCUS       WP_357643029             408 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643029
VERSION     WP_357643029.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..408
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..408
                     /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=43108
     Region          18..387
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrnflivggg vagasagyfl aesgtvtlle mervpgyhat grsaalfsey fgnpavralt
       61 tasrpflttp ppgfahgpll tprgvltlcp vgaaerfaem ladglsaptp vreidhdevq
      121 rlcpivrsgw ysramlkpaa mdidvdalhq gflrgirarg gqvitsarvr slsrrgglwr
      181 aatdagefaa pivinaagaw adevaalagv rpiglrplrr tafltdlped iglpkdaglp
      241 kdvelpentd lpqgvgaagw pmvtdvadtf yfkpesgrll vspadatpmp pgdvrpddld
      301 vaigverlqr attlvirsvr hawaglrsav addtpvvged pdapgfvwla alggygvqsa
      361 pavgriaaaa atrtsldvay dhlsperthl erhgtptsra aflterwk
//
LOCUS       WP_357643033             764 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643033
VERSION     WP_357643033.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 764)
  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..764
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..764
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=84685
     Region          2..764
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mgrrhevaev ktllaasrtv tligvggvgk trlalrvgle vrrafrdgvw lvelasledp
       61 ellaqvvaea leirdhtacp plqvlvghlr dkqtlvildn cehlvhecav madtllraap
      121 elrilatsrq tlgisgeqml pvptlplpds drprmpaeal mqcdgvrlft eraravlptf
      181 avtednrdlv lricrrldgl plaielaavr lralslqqlh drlddrfrll tagsratlpr
      241 hqtlramidw sfglcseqeq lmwerasvfa dtldleaaea vcsgdgisrd evidlvmglv
      301 dksvflreeh grgvryrlld tirqygrerl tasgqepalq rrhrayyral aarayaqlfg
      361 psqvtwfdrl qlehanlrta ldsfygdpae vgaglgmatd llyhwitsyy lgegrrwldr
      421 glaldtepsg vraralwans wlaiiqadit aastmleesr ilgerlgdel vrgyvalysg
      481 miamyrgete taiklyeeaa arhrstenpv glalalirls lahsylgdss qaislgddcl
      541 avcdtfgeew hkaytmmalg vevwrqgdlr ratelekesl vfnrslddpl gvgvnlevla
      601 wiaeteqhys raarllgile tvwsavgapl sgyghlvryh decesrtraa lgdaafdiev
      661 krgarlpyde algyalqeep pqdekaakge parltrrete iaglvaqgmt nkqiaaalvi
      721 aprtaeghie hilnklgfns raqiavwvgd raraadgerp dsrd
//
LOCUS       WP_357643035             207 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357643035
VERSION     WP_357643035.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 207)
  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..207
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..207
                     /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=22262
     Region          9..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtkrrrvpam apeerratli aatlpllrey gtavstrqia eaagvaegti fgvfpdkasl
       61 vraavmsafd pkpavdalta igtridlrar lreavtmlra gmnananlit gpkelmvddv
      121 efrermldsr rqilaavtal lepdrdrlrr speataqlll mliavsvhrg fgqggefgdm
      181 ddaeivsvll dglllrpspt pstesas
//
LOCUS       WP_357643102             258 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643102
VERSION     WP_357643102.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,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 258)
  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 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..258
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /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=27520
     Region          15..235
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msraadnprs eegdivrlnc vrqtyttgkg sfvalsgvti gcrkraltav igpsrsgkst
       61 llrcasgler pasgsvvldg eeltdlddas ltrlrrdrlg fvfqgsnllp alnvaenial
      121 pgylagrsvd tvlldrviaq igltdhlhdl phrlsfaeqq rvavaralvs rapvifadep
      181 tcaqdndgld qvlgllresa ragqtvvvat hdsriaayad hvyfmaggrv vdelalpptk
      241 aaaermahla mwdrgeps
//
LOCUS       WP_357643078             368 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643078
VERSION     WP_357643078.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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 368)
  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 368)
  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 368)
  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 368)
  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..368
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..368
                     /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=39477
     Region          42..367
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mnpaqdptmt grarhhlrrp slrvqlttly aglvlavvvp mlliagflfg rdrvrvragd
       61 avpppdtaaq qvdaalaita iivmvltvlt awwlagrflr plramtvtaq eisatnlsrr
      121 lglrgpddel tklgrtlddl ferldlsfaa qrhfvanash elrtplaaqr avlqvaladp
      181 easeaslraa ceealglger qerliaallt largqkgieh revvdladvt kgvmlscrae
      241 atrrtitira slesapisgd pdliasmign lvgnalhhnv pdghvtiate ltngrarlsv
      301 gntgptirsq dlrrlfqpfq rlgpqrthta dghglglviv qavaeahgaq ltahprtggg
      361 ldvtilfd
//
LOCUS       WP_357643130             320 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643130
VERSION     WP_357643130.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 320)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..320
                     /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=35473
     Region          49..308
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mttltrgpea parpapasps rgrrrgwvti alfvlpalvl flllvvapil iafyasafkw
       61 ngfgglpttf igldnftrlf gtevfrddvw hlvvlvvltv avqlpialgi amllnqrirg
      121 ralyrlvffa pyvlsevitg vlfslilspd agvanrilgl vglnsdwlad pdtvmlslfl
      181 vmtwkyfgfh mmiylagrqn ipeelieaaq idggtpwrvf rhvtlpllgp tirisvflsv
      241 iytiqlfdlv wiltqggpsh ssetmavtmf efgfkraqvg yasaisvvmf alslvfalay
      301 qrfvmrrdle gattrmgdrr
//
LOCUS       WP_357643133             235 aa            linear   BCT 28-DEC-2024
DEFINITION  sirohydrochlorin chelatase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643133
VERSION     WP_357643133.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..235
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=23657
     Region          <87..229
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mptslppdap vlvlavpgst sgvaaeiaav vrvdnpqiev rltsvtdlad slpsgresiv
       61 vplltwddpi vyaeigkava aagsnavvte algphpllae alhirlaerg laradrvrll
      121 nvsspvdaii lgtvggerav havqatavll asrltlpvva asldsdpgvp vaaerlraag
      181 atrlalapcl igheapaevv eqaatavrag hsealgahsa maelvarayg sqlat
//
LOCUS       WP_357643158             298 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643158
VERSION     WP_357643158.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  AUTHORS   ter Beek,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..298
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..298
                     /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=31944
     Region          20..279
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mvadsgrarp prrggrargw lyvlpalaay lgfaiwpaln tvrlsllnwd gilpatfagl
       61 dnyikifrds alyeailhsl ilivffsfip iavglfmtal lmgkvrrgmt ffrtvfflpq
      121 vlplvavgit wrwlysesgv vnqvldlvgl gaitrawlgd yglalvalgl igtwvmsglc
      181 mmlflagaqk idpslyeaat ldgagayrqf lhvtlpgvrk eitiagvitt iaalasfdlv
      241 ftttnggpag qtnvpgllvy rlafnegdig gasalavvlt viviavvgav ryftrdes
//
LOCUS       WP_357643187             322 aa            linear   BCT 28-DEC-2024
DEFINITION  thermonuclease family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643187
VERSION     WP_357643187.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..322
                     /product="thermonuclease family protein"
                     /calculated_mol_wt=35506
     Region          33..>203
                     /region_name="YncB"
                     /note="Endonuclease YncB, thermonuclease family
                     [Replication, recombination and repair]; COG1525"
                     /db_xref="CDD:441134"
ORIGIN      
        1 makaieqpvp gvtvghallg rskgaaqpvd kivhdgdtin iaadgnfgvr llgvdapevs
       61 felprnpnfp dfpkgfvsid kpawttfltd pfekgyqelt lrtalhnnll grlgpaaapn
      121 haahaapatq alktmmqldi teqgltdetf kirlafayei ldrygrllcy vnrdqrdkpr
      181 pdpynerlla aghvipyfiw pnvdpfvrqe grladavpap gsartvaeag algrarqavr
      241 rareaglglw dhanplavlp felrflaqrr apdryvldls dnarellhpq syfripnped
      301 rlfvnaehap lfgekgwsvp pl
//
LOCUS       WP_357643213             502 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643213
VERSION     WP_357643213.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 502)
  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 502)
  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..502
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..502
                     /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=53879
     Region          112..>203
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkrilipagg ailatgllaa glagtataas dvasdpmaks aadakaiaef wagtnnaalk
       61 aakesnvwds gdvaklqskg gysadskpgs svpigqekkt stkvqnvnmp ktigkvffvn
      121 skgekkwcsa tsvqskyrnl vataghcvyd tatnsdvmsk wvfvpgyyqg ktpfgiyvgk
      181 qafthydfdv yedydrdyaf vtvyngiqlg ggsakqvska dfdkfqgikd akdvaiteae
      241 yqkckdlngg etpdcwaktd skidvvgpdy pgaikaltev akeqydaapt gkangtkapa
      301 atktenvtkt eydaykgpgy rkidskgnft ithyfvknwv kktdikgyyk tvfyivegfa
      361 kdagrlgdvv ggqgvswnqp tgkyvrvfgy paaahpdghk nytgitpkwc ygktskkvvg
      421 saakkieehv alkcamtega dggpwllnys ntkrlgyvng vtstfndqdg nkrvdyissp
      481 yfdgetaavy ksaanvwsgk il
//
LOCUS       WP_357643262              94 aa            linear   BCT 28-DEC-2024
DEFINITION  putative quinol monooxygenase [Micromonospora parva].
ACCESSION   WP_357643262
VERSION     WP_357643262.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 94)
  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..94
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..94
                     /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=9837
     Region          2..>68
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mliiagslev epaareayls gcaqviaqar atagcldfll aadplepgri hvyerwesae
       61 qlaafrgsgp ddgpevavld advrrylisg veap
//
LOCUS       WP_357643303             326 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357643303
VERSION     WP_357643303.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=35506
     Region          2..319
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrflitggag figshltdal largdsvvvv dnlstgrten lalaaghphl kfiqgsvlde
       61 lmvdelvhec dvvlhlaaav gvkliveqpl rclttnirgs evvieaahry rrkilitsts
      121 eiygknssgp lredadrilg spsvvrways takavdeila nayhqerglp tivvrlfntv
      181 gprqspaygm viprlvhqal sgapltvfgd gsqtrcfahv advvdallrl ldleaavgqt
      241 fnigsadevs ildlakrvie htgstsgidl ipyheayqqg fedmtrrvpd ttrireltgw
      301 aprhildeil tevvkqvred rtasir
//
LOCUS       WP_357643353             474 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357643353
VERSION     WP_357643353.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..474
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..474
                     /product="ATP-binding protein"
                     /calculated_mol_wt=51831
     Region          4..337
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
     Region          325..419
                     /region_name="DUF4143"
                     /note="Domain of unknown function (DUF4143); cl24018"
                     /db_xref="CDD:474127"
ORIGIN      
        1 mggfvgrdre lhlldgmlsr vrrggragrp grallmrgrr rvgksrlvee fveradvpyl
       61 fftasaqptv aadlalfvqe vaastlpgak vmqeqqprtw daaltllaaa lpsdqpsvvv
      121 ldempylias dpgfegtlqk vfdrelsrrp vllicvgsdl ammealndyg rpfhqratem
      181 vvpplspadv sdmldlsaad afdaylvsgg lplildewpt gasvreyltd avrdptsall
      241 vsgeralaae fppqsqaglv lraigsgert fsliscaagd lpqaslnral rlltqkrave
      301 vtvplstkps retryavvdp ylrfwlsflg phlseiergr gdltldridr swgswrgrai
      361 epvvrealrr lpsdhlpaea amiggywtrt ndpeidivgv drapvarric fvgsvkwqen
      421 rpfdahdlgr lllhrsrlpg adesvpvvav srsgtavdai rvlsaedllt gyrn
//
LOCUS       WP_357643372             220 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent F420 reductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643372
VERSION     WP_357643372.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..220
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22424
     Region          3..199
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mrigilgagq maealgsgwa rtghevmvga rsqekarnla eaigagacgg dlraaaehge
       61 alllavpals vdgvlaevga adgalagrtl idctnayepd aftdapnsfl laddavserv
      121 arlapgagvv kafnmcaaev wtahagrglg vplcgddera vkvvaglvsd lgfepvragg
      181 lrraryleav svfvvglwfa gydarqmlpp lqeafahsda
//
LOCUS       WP_357643364             154 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643364
VERSION     WP_357643364.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=17374
     Region          3..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mgdprwldea efrawlgyrr mrllldaqvs rdllrdsgls apdydvlssl ssaeghrwrl
       61 tklaermlws ksrlsrhisr meqrglvtre ecetdgrgav ivlteeglra ievaapdhve
      121 svrrhfidll tpeqievlga vaetvlshlg engd
//
LOCUS       WP_357643373             128 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357643373
VERSION     WP_357643373.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..128
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14330
     Region          17..116
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdhhddapfe pygdfvadcp arlavdlfah awlpvvvfal kegpmrpgrl rreiggisqk
       61 vltqtlrrme rcglverrry aeapprveye ltqagkdllv piralgdwaf rhadtvlaay
      121 ddctrtag
//
LOCUS       WP_357643419             320 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643419
VERSION     WP_357643419.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 320)
  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 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   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..320
                     /product="GlxA 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=34234
     Region          2..318
                     /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 mhrvvvlalp nvipfelsvp srifctahgp gdeplyqvit ctldggpvat aadytiaveh
       61 dastlasadt vvipaaagfa ditgreslpp elldalalvr pgtrvvsici asfvlaaagl
      121 ldgrpatthw rhaerfaslf phvrmdsdvl fvddgdvlts agasagvdlc lhlvrrdhgs
      181 eianqvarlc ivppwrdggq aqyverpvpe psaagtaptr awalqhlstp lqladlaeha
      241 gmsrrtftrh frhevgqspg qwllqqrvel arhllettdl pvdrvaeqag fgtaaslrqh
      301 lhasvgvsph ayrrtfravg
//
LOCUS       WP_357643430             580 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Micromonospora parva].
ACCESSION   WP_357643430
VERSION     WP_357643430.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 580)
  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..580
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..580
                     /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=61581
     Region          199..529
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mngsiqsmap atdrptrpis gllstaivvv vgallvhvll etwaqvlsgp tsvdpranld
       61 gsaqwpkqlk tvlylglagl tvvkvavdrl whrfltgadl allvlglvmv laglvndssm
      121 slmgealfvy frgvivfyal raadlnsmmi rrllivvavv vsvnvllalv qmvvgepayr
      181 vlgwvdltws eqsraqglls hpnhlghvlg ltllgfvawl atatdvrrrw wavavvatva
      241 msatqsretl lgvligavvi avvartntrr ilavcllvvl ctvaqiaarp dnraewerri
      301 gnaftsfnhp agsessppap paattakpsp tatarpdggs tasggpktsa kpstspgtsg
      361 sggpggspga atpqpthspa pvreirvlyl qqaakilprq pllgfgigqf ggvvaekdnp
      421 nwhknpkfgp ggfnrygfqa vqvdsfwlhl imevgvlgfg aylvwlfmia kpllartrql
      481 rrtghrpapn vlwgiaalif acivgflsps medpllppll wtvvglawwa arrpapidqk
      541 aggpadttgp agareddtri latdeilaqa rrvrppagfr
//
LOCUS       WP_357643449             277 aa            linear   BCT 28-DEC-2024
DEFINITION  O-methyltransferase [Micromonospora parva].
ACCESSION   WP_357643449
VERSION     WP_357643449.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 277)
  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 277)
  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..277
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..277
                     /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=30696
     Region          122..276
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mdatklrrai artplapvaa fpkrfarvar hdakvlrasa rwlvtsrehh nytyeltkls
       61 rhhltwfvsv vcdipvqqvr ayvaeiesdd alrhhieqat ataarrglad rkvryarrvg
      121 wyaivrathp ahvvetgvdk glgtcvlasa llrnaqeghp grvtsldinp eagylarvap
      181 wsevvdlvig dsiasigald rpvdlflhds dhsrahekre fdavepklap gailltdnvt
      241 stnvlaehae rtgrrflayr espvnhwypg dgigvaw
//
LOCUS       WP_357643452             465 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643452
VERSION     WP_357643452.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 465)
  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 465)
  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..465
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..465
                     /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=47294
     Region          39..>442
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mklrplltgm lalatvsaal vaaqtssads raggpiispa lvaemqrtqr vrsivelhpg
       61 qdgeavardi maasaaariv etakspnffv aelddaclda lrddyrvksv yadelssafm
      121 ddnskfldvs tkvigsdran aagwtgkgat vaildtgide dhpffagrit deacfsstnp
      181 sveavslcpn gqpsqtglga anaktplciv ngvnqcrhgs hvagiaagam vrgapsngva
      241 paaailpiqv ftrinsatac gaagapatpc flsytsdqkl aleyvakaak arhiaavnms
      301 lgggrmytep cdsdpragth kaqfdalral gvapvvaagn sgndgvaspa cvssaiavga
      361 tddsdqiasf snrgamldvf apgvrinssv pggtfaelsg tsmaaphvtg gfavmkqafp
      421 glsvaqvvak lqntgmdisy sseftvvnte rinlasailp pqpav
//
LOCUS       WP_357643455            1056 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357643455
VERSION     WP_357643455.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1056)
  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 1056)
  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 1056)
  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 1056)
  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..1056
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..1056
                     /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=112733
     Region          1..239
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          154..1050
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(830,833..834,837..838,840,870,873..874,877..878,
                     880..881,910,913..914,917..918,921)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          830..857
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          868..898
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          909..937
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfgvlgpls vwtpdgqpvq vpeakvrall adllahrgrp vstdrliedl wgdrppadap
       61 aalrvkvsql rralgdrslv ayrppgylla vdaeavdagl frsllaragq sddarvrqal
      121 ltealglwrg apyaefgdfa raaaarleeq rlvaleelae trlelgdhga laaelaelva
      181 ghplrerlra ahlralyrag rqsealagyg qlrgllaeel gidpapelta lhaailrqdp
      241 aldpptplmd rtrsrlpaph agpphlrppa ppvdpphphp paplgglgds ggpgalagpp
      301 gtnlpaplte ligrdaevae vrsllgagrl vtltgpggvg ktrlaleaaa epgrpfpggv
      361 wlvelasats saspaegvva evvarvlgvr ddlpgsvvdr laaalrtspt llvldncehv
      421 veqvaelaer llraapelrv latsqeslrv pgevlwsvpp lgpeaaarll atragigpgd
      481 dgvaeicarl dgiplalela atrlraltpr llaarlddrf rvlatghrga parqrtlram
      541 idwswellts gervvlrrla vhadgctlea aeaicaepgl dvldllarlv drslvvrtpg
      601 gryrllesva ayslerlsea geteavrlrh arhhadlaer adpglrgpeq rhwlalldad
      661 aanlraaiet slrlgatdea vrlvnalawy wvlrgrlgeg rrtlegvlav addaqarvwl
      721 aglrmlsgqg rapgverlpa aiadparrar aqwflaftly gyddpvvtda lldsalesfl
      781 aladrwgtaa alslrarral lrgdlaalrq dgerglelfr evgdrwgemr aaenlgtlae
      841 itgdyeraad lrrdglrgae elglwsevsg alsrlgrval ltgdldgare lherarqlav
      901 arsdvpleef aevglalvar rqgrldeaer llrrwldwvr evagepgaal ilaelgfvae
      961 rrgdvvaale wqreglavar rvndpraial aleglagara lgghheeaag lldtagalra
     1021 svgaplpeae rgdvdriaas vrtaldrrra tvtdps
//
LOCUS       WP_357643462             252 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Micromonospora parva].
ACCESSION   WP_357643462
VERSION     WP_357643462.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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..252
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..252
                     /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=26774
     Region          11..239
                     /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 migvvqtavs ldvrgvryay pdghvalrgv dlvvprgdrv allgpngagk ttlvlhlngi
       61 lsptegsvsv ggltvtpdra tlaevrrrvg ivfqdpddql flptvaedva fgpanlglrg
      121 aelaarvdea laavgmgehr drapqhlsfg qrrrvavatv lamhpeilvl depssnldpa
      181 arrelaeilr glpvtllmvt hdlpyaaelc ersvildsgr ivadaptntl lndapllarh
      241 rlelpygftp qp
//
LOCUS       WP_357643474             450 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 30 protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643474
VERSION     WP_357643474.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 450)
  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 450)
  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 450)
  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 450)
  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 450)
  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..450
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..450
                     /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=48639
     Region          14..447
                     /region_name="XynC"
                     /note="O-Glycosyl hydrolase [Cell wall/membrane/envelope
                     biogenesis]; COG5520"
                     /db_xref="CDD:444271"
ORIGIN      
        1 mlrgvvavtl lglpiiqspa padppaitvr ervrhqridg fgisqafrrn elvkalgeeq
       61 rreildlwfd rdkgaglsil rlgigsapvg spydqmasiq pedpggpgap pkyvwdgedn
      121 sqvwvakaak gygverfyad awsapaymkd ngddknggtl kpewrqayar ylvqyakfya
      181 regiritdlg ftnepdwtat yasmrftpqq aaefvkvlgp iakgvkglkv accdsfgwte
      241 akaytaaiea dpearrwvrt htghtyaspv dgplptsgnt wmsewnpngs twnenwddgs
      301 gydgftiaga vhdaltlgnv sgyvywlgas rgatrallqi deaagtyhvs krlwalaays
      361 rfirpgavrl dataadpalk vsafrnpdgs qvvevlntgt aavtwqgvyg ratayvtdna
      421 naltaspvtg gtvtlrpral ttvvipgrha
//
LOCUS       WP_357643509             707 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643509
VERSION     WP_357643509.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 707)
  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..707
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..707
                     /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=76245
     Region          8..256
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,31..32,61,66,71..74,86)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,35,37,69,85..88,92,94,131,133,
                     135..136,138,147..148,151,168..171)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,35,37,69,85..88,92,133,135..136,
                     138,147..148)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,92,94,131,133,135,151,168..171)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(147..155,164..171)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mnddrlgpyr llrrlgeggm gvvhlavdpq grqvavkvlr aevagdevar rrlsrevetm
       61 rrarskyiae vidadvtghr pyivtryvag rpldeivkdd gplglpalvr iahgvatala
      121 avhavgvihr dlkpgnvlii dgepvlidfg iaqavdatrl tqtgmfigtp gylapeiieg
      181 qeagpevdvh awagtllyag tgqppfgkgt lemifynita gkadvsaapk elqpllkaaf
      241 qrnpakrpka aelaeqtarm lpkppgsard eistvprsdr snpsielptp qpladkpsyd
      301 istppmtprr lvdgqprrqp pyqgqpqqgs gpnwppqgqp pqpppqeqqy vsllpeqqgd
      361 pyptrrvtpe elrkmqreat sqpwqvsaqn sdqrgsdqrg nnqlsnnqls nshmppgaea
      421 dvptrrvrpd apdvptrrvr peapdygrgn piqpppyipv qgqfppdpqa nrepylphea
      481 qtrrdaygqp dlrtkrepfi paarpgqvlq rsrayglasa mllvlmvmva vvapvlvgll
      541 vlpvvvllra adlaqpelva rrstgsaald vvrvfafpkk laksvgitfa llfyalilgl
      601 pvtllltvfv kmnpynalaw gaaialwtvc agpgvegpgr qmrrtlsslv psrtaamvmv
      661 gvlaagaals lilayssfdn arravwapld vgpvvtqlrg lsgstgg
//
LOCUS       WP_357643476             133 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357643476
VERSION     WP_357643476.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..133
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14721
     Region          16..119
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msvahtqvtp qvggpcgddd cgirevldri gdkwtvlvvv elakgvrrfr elhraipgis
       61 qrmltlttrr lcrdglaert ayptippqve yrltpmgrsl agaiqqladw srehkdamqd
      121 arahwdadhp geg
//
LOCUS       WP_357643606             206 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357643606
VERSION     WP_357643606.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 206)
  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..206
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..206
                     /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=22352
     Region          3..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprprsltpe qlataalavi drdglaglsm ravaqeigms tmglyryvdd rgeleqlvid
       61 rvldtvdpvp pdqdrpwher ieimverlrg vvgshpwlvp liiahrhrsv ailrwsepla
      121 ailaeagldg gervialrsl layvvgaiql eqlgplagag tqviadrael pylsetarha
      181 hdvttdeefr gglalllrgi gggdmr
//
LOCUS       WP_357643549             690 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643549
VERSION     WP_357643549.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=74983
     Region          18..671
                     /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 madptdtrdt gpragtplwa flagitvigf talavamlrl dpaglaelar tplfwvltal
       61 vvlgelrpvm vssatavggt ypstmftfav llhfglpvav lmqavavvmn gvvtrkalhr
      121 vmfniaqstl altsagvvlg lfgivpspaa pwvptgadll alslagiayf avraalvsga
      181 valherrsit rvlkaslgpq slvyvallgl aplvvvvmth sptlvplfva plaavyftat
      241 lsmrrdhqam hdeltglpnr kmlivsteea laearqderv glflldldrf kevndtmghp
      301 vgdrllqmva hrlthsvrpg dvvarlggde favllpsird ahaarevaar lraaltepvr
      361 legmsfdldg svgialypdh apdfelllqr advamylake grtgvelyqp dkdrnsperl
      421 nllgdlrrav dnrelrlhyq pkvgmatgav hgmeallrwh hpvhgqipps efiplaeqsy
      481 lmrqlteyvi eaaleqasrw whsglrvqvs vnisardlld salpeqleag laklrlppsa
      541 iqlevteril mgdqaythet ikalavlgvp lslddfgtgy sslirlqrla vsevkidasf
      601 vqriaesddd yrivrsivdl vrslglssva egvesddvai rltemgcemg qgwlfhkpmp
      661 paeatvwlre hietqpeiey gyrsgvtqta
//
LOCUS       WP_357643610             197 aa            linear   BCT 28-DEC-2024
DEFINITION  O-methyltransferase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643610
VERSION     WP_357643610.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..197
                     /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=20913
     Region          35..194
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mntslasyld slyqlgrdhd apladrllrl rnmtpgaagl vallirvqgs rrvleigtsn
       61 gysaiwfgda vrdtgghlet veidasrvaq araniaaaev adhvtvihad ggevlaaspd
      121 gsvdlvvlda erpayvgywp qlqrvlsprg vvavdnalsh qeqvaafrdl vtadgrfavq
      181 lhevgdgvlt vvrlqqs
//
LOCUS       WP_357643622             251 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643622
VERSION     WP_357643622.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 251)
  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..251
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..251
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25804
     Region          2..243
                     /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 mkrihgllgv vvlialwwll avtvfadgga vptpwavlag mvhdgwgfyg pnttatvsaa
       61 lqgflwgngl aigvallvll vprleavatq lavisycipl laigpivlvv fggeaavvfl
      121 aavsvffttl igallglrsa drtsldliav ygggrlaklr hvqviaalps tfaglkisap
      181 gallgaiige ylgsndqglg vslmisqqqf qvprtwglal vaglvaglgy aivalvarvv
      241 tpwsygrvrs s
//
LOCUS       WP_357643550             332 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357643550
VERSION     WP_357643550.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 332)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..332
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35285
     Region          5..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msavieiegl rktfhslrng rrvavdgfdl lveagqvhgf lgpngsgktt tlrallglvr
       61 adsgrmtvlg epspellprv agqvgaives pqffgnftgh rtlrllarag gvpvsrvdqv
      121 ldlvglydrg ddrvksyslg mkqrlavasa llkdprllil depangldpa giremrdlmr
      181 slaangvtvl vsshilgeiq licdhvtiis rgrrvaagrv devlaghdrh eylvrvaete
      241 ravellhaag ltavvdgeal vvsgvgdptv vsralgeqgl wvgeltplrp dlesvflelt
      301 gayghpsvpr qvddsspprd gavidldrgv da
//
LOCUS       WP_357643624             259 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643624
VERSION     WP_357643624.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..259
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27224
     Region          7..251
                     /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 migrivlrvv gpllpsvviv valwwlslea fgisplvgkr ppqvweylfg sspahreavf
       61 aalgitirda aigfvtgmva avvvamafvl frtveqtfmp vamllrsvpl vvmtplitlv
      121 fgrelvgvav ivgivvffpa lvnvafglrs aspqatdlim aygggrltvl rkvavptamp
      181 svfasarisv pasiigalia ewlatgqgig agilraiggf rydevwadiv vvtavsilay
      241 avvgvveslv larfsdnrd
//
LOCUS       WP_357643675             224 aa            linear   BCT 28-DEC-2024
DEFINITION  urease accessory protein UreF [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643675
VERSION     WP_357643675.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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..224
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..224
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22721
     Region          4..224
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mnraallvlt dgrfpaggha hsggaepavt tgrihdmasl eefcrgrlht sglvaaglaa
       61 taaagydpll ldeaadartp apalrqtarr lgrqlmraar aawpsaelda laaarprgah
      121 qpvvlgltar sagltpldaa caaayetvsg patatvrlls ldpfdaigil arlaadidhv
      181 aaqgvesalc vltegvdalp avsaplldit aeqhaarpvr lfas
//
LOCUS       WP_357643758             348 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643758
VERSION     WP_357643758.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=35470
     Region          2..348
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtttiplrva glswrvrprg vavtlgglal lgllmalnmr igdipmslsq vlggtfdvns
       61 adhfvimelr lpraltgalv gaalalsgai iqsiarnpla speilgvttg asvtvvagvv
      121 asgsayggvs gllstlgipl lallggltga vivyalawrr gldgyrlvlv gigvaavftn
      181 vkywlltvgd vndtgramvw isgslngrgw ehvvpvalal avlvpltllg trsldalrfg
      241 ddtvtalglr mnparalmil aavllaavat asagpiafva laapqvalrl trygqpplls
      301 savvgavlta aadliartaf spielpvgvv tavlgapyli hliwkark
//
LOCUS       WP_357643784             810 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643784
VERSION     WP_357643784.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 810)
  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..810
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..810
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=87521
     Region          4..781
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msepprhnlp aepnrfvgre rdvddlcgll getrvvtlcg vggigktrla lrvaarlvps
       61 ypggvwlvel arltrgelil qeigravgih eegtrplldt vaarlrdtpa lllldncehl
      121 vdqcaqvaae lvaacrglgi latsreplri aselvwrvpp ldlpderhpd aesvllfidr
      181 ataagtrlsq aslgdvirlc raldglplal elaaartsll spgqivdrid grfsllttgg
      241 rtapprqrtl laavewsydl lsakeqvllr rlsvfagsfd lelaeqicad rpiseaeivd
      301 llgalvdksl vlcdeerrry rlletikhya aerlaeaaer evlrdrhlev lcelqlrhfg
      361 temvepdlpw pvrlaaltas rslvddqraa ldwaiesgna plglrlcays tsllpvssvn
      421 paeivgwver llaldltqvp deqiahahay layglegrde larsleyata sltglgadnv
      481 ftscvmhsls vvvllrigrg dealhhaetg lalaiasgdq wnqaaglagl savaltrgrl
      541 reaqchgeea vakarqhghr wllartatql gavaeargdl vkamaqyela vpwleeldgt
      601 ielarclari grvaallhef evarerlaas ltlsrqtgqr qsvarclvsl svlaeaegdl
      661 essvlaaasa talresmgqh satirieell traraklgeg rtatlwsrgr tmspddaarq
      721 vlagerpvpa gpvpdgpvva epvrhsllta reqeiavllt rglsnraiae elvispatva
      781 rhianimekl gytsraqiav waaeqprgsa
//
LOCUS       WP_357643840             286 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643840
VERSION     WP_357643840.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 286)
  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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..286
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30950
     Region          1..280
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 miidihqhlw tgtfvealra rttppyldgw tlildgeppy evdpadhtdr dvtglelalv
       61 slssplgief lppeeawpll dayhegalgl pepfgawast chsepdpdrl akdldrgfag
      121 lqipatalpd drllgvltdr dlplfihpgp aaatpgtpsw wpalvpyvqq mhaswhyfha
      181 vvrprhprlr vcfallagla plhserliar ggtgrglvdp gcfvetssyg praidaivre
      241 lgvdvvvngs dapyatapdp glgeaaahai rvtnprrllg rketrt
//
LOCUS       WP_357643822             411 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643822
VERSION     WP_357643822.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   ter Beek,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 411)
  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 411)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..411
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42833
     Region          28..405
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnstlttdrq derlsgnegl rgaiadvler arggdlgvip vvvgliviwt vlqilnpifl
       61 ssanlvnltl esaatgiial givcvllvgq idlsvgsvsg lsgavlavlf vsnglpiwva
      121 ilaavimgav igwvyaqlfn rfgvpsfvit magllaflgl qlyvlgtkgs inlpfdsglv
      181 nfaqldfvpa wlsycfavia avwlfasgyl haqerrragl sarslsmlli rsaallavla
      241 fvvyylgqtr gvgwmfiffv alvlimhyml srtkwgravy avggnveaar raginvkavy
      301 tsvfvlcssf aavggilaaa rlaaanqssg sgdvnlnaia aaviggtslf ggrgtafgal
      361 lgiiviqsis sgltllnlds sirfvvtgiv lllavvvdsi arksrtshgr a
//
LOCUS       WP_357643942             534 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Micromonospora parva].
ACCESSION   WP_357643942
VERSION     WP_357643942.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..534
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..534
                     /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=57628
     Region          <8..>99
                     /region_name="mnmC"
                     /note="bifunctional tRNA
                     (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase
                     MnmD/FAD-dependent
                     5-carboxymethylaminomethyl-2-thiouridine(34)
                     oxidoreductase MnmC; cl40718"
                     /db_xref="CDD:424349"
     Region          61..533
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 msdqtqsmvs rrgflrtvgi sggagamlat mgamglapsa aasvtpafrp persdftltg
       61 rsgasvvvlg ggiaglttay elgkagyhct ilearhrvgg rnltirggdv etdldgrtqr
      121 agfsdgvyfn agpgriaqwm vtmdycrelg vpvevftnqn adawiynesa gmtapvryrt
      181 akadvygyvs ellakatdqg aldarlsted rerllsflqs fgaiggrssd waytgtsrrg
      241 fsaypgagnd vgtplgtppa lsdvfasnig ryfsfefgyd qamlmfqpvg gmdqiprala
      301 ravgahrirl daevtavtdr gsrvevtyrq hgrqsqitad ycvaalpphl marvphnlgt
      361 avtaaladfp vtasgkigle yrsrwwetdq riyggitetd ldlshiwyps ygfhgkrglv
      421 vgyyntgana raysgltpqq raeravsqgv kihgdkyrse lvtsyshawd rtryiegawt
      481 sprygtagyn lllqpagrvy fagdwlshev awqhgafvaa rsavsalhqr vmag
//
LOCUS       WP_357643888             819 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Micromonospora parva].
ACCESSION   WP_357643888
VERSION     WP_357643888.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..819
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..819
                     /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=87238
     Region          88..>172
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <332..809
                     /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 magrtsqasr rrgasprggt nsrarqpakk trapvrrrta pprpgpavyv gravgalwmg
       61 lahgmgwavr aagrqaasar dldpehrrdg agllmfglal lsavalwlsg agpvgarlad
      121 tirlflgais vvvpvllmig awrlmrqpad pehrgrglig wgsllvstaa llqigqdpvd
      181 tverdfaggl vgagvgglle ravtawvavp llvllllfgl lvvtatpink iperlgllag
      241 glvgapetde evdepvakpa rkrpakrmpp pldpddfedl dgadlqetmv lprkapakvp
      301 asrkppvepp ehspaptrae qlaltglagd ytlppanmls agaaaktrsk andeviaalt
      361 gvfdqfdvda avtgftrgpt vtryevelgh gvkveritql srniayavks pdvrilspip
      421 gksavgveip ntdpenvalg dvlrsraats dhhpmvvalg kdieggyvva nlakmphili
      481 agatgagkss clntllvsil tratpdevrl llidpkrvem tgyegiphlv tpivtnakka
      541 adsldwvvre mdmryddlaa ngvrhiddfn rkvrngeika ppgseremrp ypyllvivde
      601 ladlmmvapr dvedsvvrit qlaraagihl vlatqrpsvd vvtglikanv psrlafatss
      661 ladsrvildq pgaekllgrg dglflpmgas kpvriqgawv tereiadvvk fckdqrepef
      721 rpdvlapaqe skkkidedig ddldllvqav elvvtsqfgs tsmlqrklrv gfakagrlmd
      781 lmetrgvvgp segskardvl vkpdeldevl vglrgdgad
//
LOCUS       WP_357643945             278 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Nonomuraea].
ACCESSION   WP_357643945
VERSION     WP_357643945.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 278)
  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 278)
  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 278)
  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 278)
  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 278)
  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..278
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..278
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30200
     Region          4..263
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mfdspadvte rlaavdylsd daistsvfla aalgkpllve gpagvgktql akavaqatga
       61 qlvrlqcyeg ldearalyew nykkqllriq atsadddifs eefllerpll kairagvptv
      121 llidetdkad veveglllel lsdfqvtipe lgtisavrkp yvvltsnatr elsealkrrc
      181 lylhieyptp ererdivlsq vptiradlae qlartvatlr amelkkapsv aetvdwantl
      241 lalgrdelde ptvagtlgvv lkhasdhara vkelglps
//
LOCUS       WP_357643956              70 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357643956
VERSION     WP_357643956.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 70)
  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 70)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 70)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..70
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7107
     Region          1..67
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mstatytvkg mtcghcvssv keevsevdgv tnvevdlatg lltvdsessi epakivaave
       61 eagyevanqs
//
LOCUS       WP_357643970              79 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357643970
VERSION     WP_357643970.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 79)
  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..79
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..79
                     /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=8868
     Region          5..>79
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mkrftcdelv elltayldda ldpperegvh ahlagcdgcg ryleqfrati vvlgdpppek
       61 lpadlrnrlm safrerrrs
//
LOCUS       WP_357644047             229 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Micromonospora parva].
ACCESSION   WP_357644047
VERSION     WP_357644047.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=24558
     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 mrvaiagagn vgrsiaqeli dnghqvmlie rqpkmlrpdr vpaaewvlad aceltsleea
       61 dvagcdvvva atgddktnlv lsllaktefa vprvvarvnr aenewlfteq wgvdvavskp
      121 rvmaalveea vtvgdlvrlm tfrqgeanlv eitlpptapy vgqplhavpl prdsalvail
      181 rgkrvlvpsp ddpieagdel ifvctaeved dvravilgad svertrgsr
//
LOCUS       WP_357644072             304 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644072
VERSION     WP_357644072.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  AUTHORS   ter Beek,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..304
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..304
                     /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=33452
     Region          3..301
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 merlrkygfv aaflavpval ysvfvispyi qafqisltdw ngyrsrlhyi gldnftrlfg
       61 devfwralrn hgilllvlpl vtvaialffa fllnlgggtr gagkkgiwgs rfyrvvfffp
      121 qvlavavvgv lfkavyrpde sgvingvlvk lgldpvgwlv epdlalwail avmiwqavgf
      181 yvvlfsagma aipkdyfeaa aldgagrarl ffsitlpllr dtiqvgwvyl giaafdgfal
      241 ilvlagdkge pdgattvlpv eiwktaftys kvgyasamgv vlffltvtfa vltlrttrre
      301 riel
//
LOCUS       WP_357644088             184 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644088
VERSION     WP_357644088.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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..184
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..184
                     /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=19802
     Region          44..172
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mkdvyksdfd adpdgslfdp atraamrqft gggdtaalea aaavrtafha iermrahgsq
       61 grglssgamd llmrlgaahe dgvsigelaq sagvssrnvt glvdtlereg lvrrvpdqqd
      121 rrsvlaqita agrdwikafs epsqramtam frdfsaddvt rfrdlclrva dnqhrlaqyl
      181 egas
//
LOCUS       WP_357644089             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            parva].
ACCESSION   WP_357644089
VERSION     WP_357644089.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..416
                     /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=43942
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..379
                     /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(349,351..353,355,366..367,371..372,375,379)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 midelvraea avvscadaaa walserdlia aldathrlqq rlaavqlavv reldgrgvav
       61 aqgassttvw lrerlrldvs aarrlvglaa sldvappavr ealaggtvsv eharviagta
      121 atvaasagae vankavgvlv ewagqfdpal lrrmgtrild hvapdladav aaaalaaeaa
      181 ratrdrhvti seqtggrlrl sgildaeaaa llravidpls apsapddtrc agqrrhdala
      241 dvcrlalrtg elpenggdpa qlvvtidydg larqigggil dvglrltpdt vrrlacdatv
      301 lpavlggagq vldvgrqrrl vtgplrralv lrdggcafpg cdrpprwcaa hhirhwadgg
      361 ptsldnavll cghhhrhvhr sewavrlgdd ghpefvppaw ldpeqlprrn hyhrrt
//
LOCUS       WP_357644110             167 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF1990 family protein [Micromonospora parva].
ACCESSION   WP_357644110
VERSION     WP_357644110.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..167
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..167
                     /product="DUF1990 family protein"
                     /calculated_mol_wt=18121
     Region          2..166
                     /region_name="COG4762"
                     /note="Uncharacterized conserved protein, UPF0548 family
                     [Function unknown]"
                     /db_xref="CDD:443794"
ORIGIN      
        1 maeltypevg strhgplpgg yhhlrhrypl pggcfetasd avlswrlhra agvrmrtdap
       61 ratdgvlvta glgvgparlw gpcqvvwsvd aptlagfgyg tlpghperge eafevvrddt
      121 gavwfevraf slpdrwltra ggpavravqh ayawwlgrtl rrlcagr
//
LOCUS       WP_357644161             523 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357644161
VERSION     WP_357644161.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 523)
  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 523)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 523)
  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..523
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..523
                     /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=55457
     Region          128..383
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrilhsappg wphrrrrlll dvllwavvaa pvgyagispp ysryalpllv gnllvltvav
       61 vasrrqplvs lvlvvlgslv dgnflfaipv fsylagrrsa tagpsimvfv litaggtvln
      121 lgllgagaat wfllasvllf aavfpwlvgr yrrqqqelae agrrhvdalt reqrgaaeri
      181 rlrerariag emhdslghdl slialraaal evaadlddkh rtaaselras vsaaterlhe
      241 iigvlreegg aslrpsgetv adlvdgarea gmavrldaap avaqlpamtg haahrivrea
      301 ltnaaryapg apvdvrltrd gdrvevtvvn dapsagplpa ppsqgsglla laervrlagg
      361 tlaagpraeg gfavravlpa taptpeaigs avevgpmass derqgpaegp vdaerrlhda
      421 rrrvrrsllv alvapvgfal vlslvyypva tagtvldrat fdqlrvgapr selvglprrq
      481 lerpaaadra gceyytdgnf plaeptwrlc ftddrlvske wia
//
LOCUS       WP_357644202             272 aa            linear   BCT 28-DEC-2024
DEFINITION  PIG-L deacetylase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644202
VERSION     WP_357644202.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..272
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29528
     Region          5..233
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mpprtavffh ahpddeallt agtmamlaae ghrvvlvvat agerglaemg pgeelratrl
       61 kelyesaall gcarveclgy gdsglspqgg raeerpddaf idadsekaag klaaileeer
      121 adllsiydpa ggyghpdhvq vhrvgrraae iagtavvlea tvnrdplvrl lklagkfyrf
      181 ppefdvrtfe saysasetit hrvnvrkyak qkrasmsaha sqatggetdr tlavmlkvpg
      241 plyrlvfgte wyvrrdlppg trlshpldqw pk
//
LOCUS       WP_357644255             768 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora parva].
ACCESSION   WP_357644255
VERSION     WP_357644255.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 768)
  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 768)
  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 768)
  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..768
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..768
                     /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=84234
     Region          13..768
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 msrhsggsge lplddeigre qeyvsmlyhr ldelreqaah rltaelhntg gtlqdrsqrd
       61 ssvamyadqv eqfsavengl cfgrldgddd srryigrigi fdttgdydpl lmdwrapaar
      121 pfylataanp qgvrrrrhlr trqrkvtgln devldidsas pgaheeltge asllaalnag
      181 rtgrmrdive tiqaeqdeii raelpgvmvv qggpgtgkta valhraayll ythrrelssr
      241 gvllvgpnat flryisqvlp tlaetgvllr tqgdlfpgvs aqrsepaeta alkgravlae
      301 vlalavrdrq wvpdepleie veretltldp eivraardrv rrtdrphnla ralfdveivh
      361 alaeqvaeri gadplggdnl ldeadraeir relreepeir aaldelwpvl tpqrlladly
      421 adpdriaaaa pmltaderal lrrerggwtp advplldeaa ellgederaa aarrdrirmm
      481 ereyaegvle iargsrsidv edeaeggeil gvtdlidadr llerqeetdr lttaqraaad
      541 rtwafghviv deaqelspma wrllmrrcps rsmtivgdva qtgalsgtps wadalapyve
      601 qrwrlteltv syrtpaeima vaadvlaeid palrpprsvr esgvppwdra vpdgrlaael
      661 vaevtreaag ltegrlgvlv pagrvgelga avtaalpeaa vgehpelesr vvvltvaqak
      721 glefdsvlvv dpdrmvaesp rgrsdlyval tratqrlgvl rptptptl
//
LOCUS       WP_357644330             490 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644330
VERSION     WP_357644330.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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 490)
  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 490)
  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..490
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..490
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=52977
     Region          32..470
                     /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 msalvaaggg afgwawlsst agnvgelpfd rplripplle ggsfdlklqa gvselrpgvk
       61 tgtwgvngph lgptlrvrrg etvapqvhna lpeatsvhwh gmrlpavmdg gphqmiapga
      121 twkptwkidq paatlwyhph lhgttarhvy qglaglflid dehmaklphe ygvddiplii
      181 qdatfdgdgs ltldnfgmsm lpgmdlmgfl gkevlvngtl gpafkvtttr vrlrllnasv
      241 grvyhigfad drefalvatd sglvgepvrl krvllasger veivvdfrpg dqvvlrsyta
      301 elgggtaldr ftggadvfdl mkftapgpla esvavparlt dvpalvvppn artrtfrfss
      361 tsingkemdl aridevvpag avevweltnp stnhsfhihe vsfrvldvng nppaayeagr
      421 kdtvyvppeg hvrllvefgd ytdpkapymy hchmlvhedk gmmgqfvive pgqeshvnpr
      481 lnlkdshggh
//
LOCUS       WP_357644392             528 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357644392
VERSION     WP_357644392.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..528
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..528
                     /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=56916
     Region          55..524
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mgysrrdfls avgvsggaga lfatmgalgl aptaeasake tfdppqqsdf sltgrsakkv
       61 vilgagiagl atayelgkag ydctileald rvggrnwtir ggdrvseldg stqvakfsdg
      121 vylnagparl aqwmltmdyc relgvdlevf tnsnaqayiy hqnmqapvrw rtakadvygy
      181 vsellsratd agaldaalta qdkerliafl ssfgavgnka sgfkysggdr rghsvnpgag
      241 eqpgtllgpv pslsevlasg vgqrfsfefg ydqamlmfqp vggmdaipra fagkigrqri
      301 rlrakvtkit dlpdgvevey edrhgrtqki kadmciaamp phllaktshn lgpdvqaala
      361 tptvtnagki gleyrrrwwe tdediyggit atdldlatiw ypsygygasr gmvvgyynfg
      421 aqadayaalk htdrerraie qgvkihgaky rdelassvsv awklqphieg awvgwpsrqg
      481 ayqllnrpag hvyfagdwls ymiawqagal esarkvvael hqrvlsts
//
LOCUS       WP_357644488             303 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644488
VERSION     WP_357644488.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..303
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..303
                     /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=32663
     Region          <26..302
                     /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 manythrlrq vmtrtfpgit ddlitnvdrn tfrqglltgl adtvhfgrtl tgyritdsgr
       61 vrvefaeggd degdllvgad gvgsavrrql lpnatvkdig lrcvygrmti teatealipe
      121 aishgfswvs desgcgagfa pvrfrsrpag asdylmvtll asqerlgrpd eelfelspea
      181 lwkltleata dwhpelrelf asadsdrffp itiragervd awesgpvtll gdaihtmppt
      241 ggvgantalr daatlagell iaargeqsli davaayervm lprgfdtvda slrmaaqmfs
      301 tsg
//
LOCUS       WP_357644499             355 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Micromonospora parva].
ACCESSION   WP_357644499
VERSION     WP_357644499.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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..355
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..355
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38756
     Region          <90..322
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mghgsvdqqr lerivqefga rwtraaadie tylaaqvada shrevvgpll aasgasgvvl
       61 vggrevaawg dpdvpemafs vtksvvsvva glafddgllv pdqpvhqvvd vaefhgphne
      121 qitwrhllqq ssqwegelwg kptsvdaqsf regtethgtp pgqgwayndv rmnllayalt
      181 llfrrslpev lrqrvmdplg asdrwswhgy rtsvvdidgr ptavvsggah wgggliipar
      241 dlaligqlfl drgthagtrl lsaewvdqsw spcpvkreyg ylwwlnddqv pwpgapttgr
      301 sargnggrhl lwvdpardlv lvshwteepl eliravsrav grsgpvvdep hvtgr
//
LOCUS       WP_357644511             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357644511
VERSION     WP_357644511.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,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 265)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..265
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28661
     Region          15..261
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msippptaqa eqpaihvhgl eksfkqlrvl rgvdidvarg sifallgsng agkttvvril
       61 atllkadggt arvagfdvat qaadvrqais ltgqfaavde iltgrenlvl varlrhlsep
      121 gviaddllrr fslteagsrr vrtysggmrr rldiamslig nppvifldep ttgldpeari
      181 evwqavrela sggttvlltt qyldeaeqla driailhegr ivvngtldel kqmlppaqve
      241 yvekqptled vfltlvgtkt ekeqr
//
LOCUS       WP_357644531             225 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644531
VERSION     WP_357644531.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..225
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23189
     Region          16..223
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mpsespspgm assgaleavl fdmdgtlvdt eglwwqatta vartlgvalg padtpqvlgr
       61 taedvaahll taatsrpgpp eltattpppg apeiarrltd afatrvgggv tvipgalall
      121 aelhaeaipt alvsasprsi vdlvlprldh pfdlvmaved tprgkphpdp yleatrrlgv
      181 eprrcvaied sppgiaaata agcrvitvds rrglpdlhal cdfql
//
LOCUS       WP_357644556             324 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357644556
VERSION     WP_357644556.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=34392
     Region          28..319
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mgntqpsvrp asagraggaa vtpaahrsga rqrrprgglg aeryapyilv apavliivll
       61 rlyplilgvn fsftgdgaqn gtavgfgnyr elfadplfrt alsnvgllvl llpvavaipg
      121 llatfiylrv pghrfyrsvy ffpavlspvi vgaifnllla fdgplnavlg sagvgpvdwl
      181 gdpdiamfmv vgvhiwatfg malvvflagf atldaallda arvdgaslrq vvwhvvipsl
      241 artiqfvfvt tmigmltsmf gllfvmtsgg pegstylpey yiwiqqgqmn rpalasaast
      301 ilfvimlvvg lmqikllera gked
//
LOCUS       WP_357644591             160 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357644591
VERSION     WP_357644591.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 160)
  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 160)
  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 160)
  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 160)
  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 160)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (residues 1 to 160)
  AUTHORS   Rosinski,J.A. 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 160)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..160
                     /product="GbsR/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=17879
     Region          1..151
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mepqeaefvd rmglvmerlg gtrtmgrvya wlmicdpshq sltdlaaqld vsktaistva
       61 rqlegagmie rvptssrehr yqtagggweh vlrvqlggvg fgletldfgl sivgegrrdq
      121 rarleesref fafiehdadg flqrwqdyre ksgeedqsgn
//
LOCUS       WP_357644638             151 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644638
VERSION     WP_357644638.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=16520
     Region          11..144
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 meshqissdr paarvvcvda egrvllvrwh dhirgeaiwe ppgggidpge tpleaaarel
       61 teetglpgsa vrdqwvpvhr dfswlgvryv ktepfylacf pgkapevdpg eltdeearay
      121 lgyrwfaade lphgveppel aeviakltgp a
//
LOCUS       WP_357644670             548 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 27 protein [Micromonospora parva].
ACCESSION   WP_357644670
VERSION     WP_357644670.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=57957
     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          434..545
                     /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(438..441,451,453,456,460..461)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(447,478..479,480,490,492,495,497,499..500)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(464,468,470,474,478..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 mnrttrgrrw gsvlaagill agalvglrap taqaldngva rtppmgwnsw nsfgcninea
       61 lirqtadaiv ssgmrdlgyn yvvvddcwfn pnrdssgniq gdpgrfpsgm kalgdylhar
      121 nlkfglyqvp vdktcaqyfg sypgatgsrg hevqdarqfa awgvdflkyd wcspegsind
      181 qvatfakmrd alaatgrpiv ysinpnsiha ktgpqrnwgd vanmwrtted itnawdtgqt
      241 ngypmgiqni invtvplasy arpggfndpd mmevgrggmn dtemrshfam waimasplia
      301 gndvrnmnaa tqtilknanl iainqdslgl qgtqvsfdgt rrvlakrlan gdvavalfnq
      361 ggstttistt aaaigksgss ftlvdawtgg tssssgtisa svpahgtvvy rvsgggtttp
      421 ppttssayas aasgrcldvp nssttngtqp viwdcngqan qrwtrngqtl qalgkcldap
      481 tnaaagvkvq iwdcnggtnq qwninangti sgvqsglcld vnnngtangt tvilwtctga
      541 anqrwsqr
//
LOCUS       WP_357644696             374 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644696
VERSION     WP_357644696.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 374)
  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 374)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 374)
  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..374
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..374
                     /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=39598
     Region          <189..374
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfvfalphsg rltwplravr laglvvllvt imrtdpglid rrpvvmagll aaasagwllw
       61 lasdwlgrrs lvvalllmgv agaaltgaga gvavafpava lidagarlpp rqvlpitlat
      121 vaatvslrps ppwpylvahv svlvacvllg tfrkqvlqra eqaelllgna eraaqerara
      181 aalaersria reihdiqaha lsalsvqlkv vdalveegae derirvflrr aqeladeglv
      241 etrrailalr dealpleell tglatayadr agkpaeleme aasaelsadv altlyrgvqe
      301 altnarkhap gspvrirlay gthatlsvvs qgpaapvgpg fglrglrera erlggtlsaa
      361 pkgeewhvdv ripl
//
LOCUS       WP_357644739             329 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357644739
VERSION     WP_357644739.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 329)
  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 329)
  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 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   5  (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
REFERENCE   6  (residues 1 to 329)
  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 329)
  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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..329
                     /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=35899
     Region          68..206
                     /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"
ORIGIN      
        1 miwltwrqhr rqalftvlgf aalaallvpi glsmrstfsd lgladcvnql artdvaqttr
       61 etcdagfhrf snqygnlnll avllitlpal vglfwgaplv areveqgthr fvwtqgigrn
      121 qwalvkfglv gasvlvlaig yglgmswwve pltqaaqegr lgmivfdlqg ivpigytlfa
      181 valgifagtv wkrmlpamgi tlagfigvra aveilarphy qaartktfpi egdgppeisr
      241 gdwiltqgvr npdgtmiaed triqcppggk apdgrvcgae lglepgaynw qlyqpadrfw
      301 lfqgietgif valallllyl avrrvrria
//
LOCUS       WP_357644753             349 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Micromonospora parva].
ACCESSION   WP_357644753
VERSION     WP_357644753.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 349)
  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..349
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..349
                     /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=35268
     Region          7..339
                     /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 msvlstlrhp iiaapmaggp stpalvaavs aagglgflaa gmidterlva dvaevrartd
       61 rpfgvnvflp dpggvdeaav qayaerlapq agqrgvslge pvggddaype klaalladpv
      121 pvvsfvfglp draavtalre rgtevwatvt rpdaataaad lgvdavvvqg teagghrggl
      181 pddddygvlp llrltaarcd rplvaagglv dgpavaavla agaaaaqlgt aflrcpeagt
      241 spmhraavag atptaltrsy tgkrargvan dflrqhdava prgypqvlhl trpllaaarr
      301 dgdasmanlw agqahplard lpaaqvvaev sadaraalat vvarsarwg
//
LOCUS       WP_357644768             384 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644768
VERSION     WP_357644768.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=40427
     Region          1..377
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mvrltararl allqtalvli agaaltglty llmrrravft yldptgsdpp gvedlhavad
       61 raqadtlsal lpqaglalvm vtalaavlsw avagrvlrpi raissaarrl saenltervp
      121 vttpadelsa lagtvndmld riqrgiaerd rildsqrlft anaahelrtp lttaraaidv
      181 tldghpsrae llamagdvrd avehmqrvln gllllarsqa grasrqpadl taiaaaalda
      241 aqaraaaadv tvrprlrpap vtgepiller mignlvdnai rynragghlt vdtdtdtagg
      301 ravlrisntg rqippeeagt llepfvhgqg trvrthglgl gltivraitl ahqgriavta
      361 rtggglditi dlphhpatta drpv
//
LOCUS       WP_357644776             567 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Micromonospora parva].
ACCESSION   WP_357644776
VERSION     WP_357644776.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 567)
  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..567
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..567
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=61168
     Region          219..286
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          277..344
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          336..405
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          394..461
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mrffaargnr qyttrliaga alslavigan alltispaea ssingpitrt emldraqnwv
       61 drditytqtg twakdvdgsh tyrrdcsglv smawhlsqsy vtdqfqgsna mwttlgsind
      121 fqpgdamvrs ghielfafwk dkndhtkgay vysfnsdgqt vqnpyannnt gsrgfngwdd
      181 lrtykpirrt gieateptpe pepeptpvad pnvvqlsgdf ngdgrddaam lylhkdssie
      241 lftslgnasg gfgaffgsyk lpanswkwds frtivgdfng dgrsdlgamy yqadgsitmh
      301 talantsggf gaftgsltvp asaswkwdai rltsgdfngd grddaamlyh hkddsielft
      361 slgttsggfg tftgsykipa nawtwdsfrt iagdyngdgr adlaamyyqa dgsitmhtal
      421 antsggfgaf tgsltvpasa ywkwdsvrlt tgdfngdgrd dagmlyrykd esielftslg
      481 nasggfgtft gsyklpansw kwgsfktitg dhngdgrsdv aamyyqadgs itmhtalant
      541 sggfgaftgs ltvpasaswy wdairll
//
LOCUS       WP_357644836             126 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357644836
VERSION     WP_357644836.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14290
     Region          29..118
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtkqlrdss deadlrrads lareifsdva nkwalliiea lgertlrfse lrdevegish
       61 kmltqnlrml ernglaerkv hptvpprvey tltepgqalr atvdlicdwt hqhfghieaa
      121 rrgfgt
//
LOCUS       WP_357644885            1265 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644885
VERSION     WP_357644885.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1265)
  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 1265)
  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 17582184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1265
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..1265
                     /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=132398
     Region          204..585
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
     Region          810..>890
                     /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            870..872
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:239048"
ORIGIN      
        1 mlrglrgrra vatvaavlav salsvpgsra gaevadsgla lgragglavg taggeitlit
       61 gdqvhlravd gghqavtitp apradgsvpn fqvleadgql svipddvaal vpqrldaalf
      121 dvselaedgy daaiplilty dgnttksaip avkqlrtles iggagvsiat hdaarfgaal
      181 aglaagtaar aasplagvsk iwldrkvepv lensvpqiga peawaagfdg tgttvavldt
      241 gidathadla gkvtdqrdft gesvtgdpng hgthvastia gsgaasdgrr kgvapgvgll
      301 ngrvlggdgk gqlswiidgm ewaagekhaq vvnmslgsrv aggplssavs rlsqqygtlf
      361 vvaagndgcd gcvgapgdsa daltvgavdr adqlaafssr gpiavdgsvk pdvtapgvei
      421 taakagggyv tmsgtsmasp hvagaaallr qarpgitgpe lksllmesak pmpgtpadtr
      481 gtgridvgaa lkgavvasag svnfgglveg adksvtmtyr nlgkepvele lkaggpftae
      541 pgevtvpaag qaqvkvtlkg apsgrlreel sasvpggatv rtlltasveq rrvelrvrgv
      601 ardgrnargg ftvlnldegt lvgrvlpgdp aqpcteqksg tgtcllvkpg tysvlghift
      661 mpatqdstat gkplneslvg dpemkitgdt evvldarkav eveirtpdhk tkrnmgaaaq
      721 lawyragekg talrggtnis pggqveerlf iqptrkvtkg tftvatrwrl eapaitltsp
      781 gldlnpqyyd pvsfsdyate ypkldgtall pavdagrgta eeikardlrg klavirrtdg
      841 vpvaaqsnaa aaagarmvai ysdhpgadit sggtgvkltv ptvrltreeg lrlverlrrl
      901 pvpvlakgiv aspyaydlyl rekgrvpdsl ryvvrdrsla riesgyhsql addvtvnear
      961 fvfepwdtss istnrplakt prtqvqyftp dpdlrwsasa gsperhyntm wphvdtprva
     1021 lsspefrsye agervehtwf kqpllpgvnp rnplrregdk lrismqgfvd asgnygdtyt
     1081 stfehgmktd frlyqgdsll qqtnylpsgs vllpveksty rieydvrnea twaklstrsr
     1141 svwtfssehv dagvatvipl ilagidapvd lknqarsakl gvslhrqega arsalkevsl
     1201 evslevsydd gvtwrptrlr akggtdsyea tldrrpggfv slrlkaadve gntfsqevir
     1261 ayaar
//
LOCUS       WP_357644910             131 aa            linear   BCT 28-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Micromonospora parva].
ACCESSION   WP_357644910
VERSION     WP_357644910.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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..131
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..131
                     /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=13285
     Region          1..131
                     /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 mwvgigvfla gglgalsrag idalvkpwws aratgsskaf pastflinvs gafvlgivtg
       61 yavkhtaaga qdfatvvgvg flgayttfst eewhtlgllr knaaveafnv lgslcaslvl
      121 aalglwlgsl i
//
LOCUS       WP_357644973             222 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357644973
VERSION     WP_357644973.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..222
                     /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=23065
     Region          31..131
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mpprphrirp lliiavavlg glctgspaqg aqrepvilvh gwngsptefa qmrtaleqag
       61 yptyaidlpg eenlanaqai adlveqarge hggskvslvg hsmgglsarh ylkslggaak
      121 tlsyismgtg hlgywpacll pagqggqmcp tsgfitqlns gdptpdpvty tlltssldet
      181 rndviagvwc raefagvpha deptspvfid avlsaldgrc ps
//
LOCUS       WP_357644982             399 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357644982
VERSION     WP_357644982.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   ter Beek,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 399)
  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 399)
  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..399
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..399
                     /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=39686
     Region          62..398
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mtttqrtsgp sdasdaagss aaaspagssa agspagssvs paaaglssta vppgesirla
       61 grsllrigpv sllirrravl vaavltvlll lavvlslslg tpyvapadvl ralsgagtpy
      121 dlvvfdlrlp rvvlaavaga afgvagtliq svarnplasp dvigitqgag laatvaltsg
      181 maavlvapta lvggllaaal lfalgarhgl aaqrfvlagv avafgfralt evvmltadpi
      241 dglraqiwli gtlagkgwte aawiagtllv llpvlawagw alnstalddd targvglrpv
      301 arriglagtg vlvaamvtaq vgavdfvalv apqvarrlvr aerpplvcaa llgalllvla
      361 dlagrrlfap tqlpagvlta aiggpylifl llrgrrrss
//
LOCUS       WP_357645039             107 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645039
VERSION     WP_357645039.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=10677
     Region          2..87
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawlllafai aaeviattal klsnglshlg waaivaigyl isfvllaral ktqlevgtay
       61 avwsgagtaa ialigaaflg etltplkigg illiiggviv lnlagah
//
LOCUS       WP_357644990             837 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Micromonospora parva].
ACCESSION   WP_357644990
VERSION     WP_357644990.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=92321
     Region          1..824
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtltaalpts adpdtlfdaf agwakergld lyphqeeavi eivsganlim ntptgsgksl
       61 vaiaahfaal adsrttfyta pikalvsekf falcevfgae nvgmltgdas vnadapiicc
      121 taeilanlal regdladvgq vimdefhfya epdrgwawqv piielpqaqf ilmsatlgdt
      181 trfvddltrr tgrptavvrs aerpvplifs yamtplhetl eelletkqap vyvvhftqaa
      241 aleraqalts vnvatraekd miaqaignfr ftagfgktls rlvrhgigvh hagmlpkyrr
      301 lvetlaqagl lkvicgtdtl gvginvpirt vlftglskyd gvrtrllknr efhqiagrag
      361 ragydtigrv vvqapehvid nekalakagd dpkkrrkvvr kkppegsigw gqptfdrlvd
      421 aepepltssf qvshsmllnv igrpgdafaa mrhlltdnhe epaaqrrhir raiaiyralr
      481 aggvveelpe pdetgrrirl tvdlqldfal nqplsplala tielldaesp syaldvlsvi
      541 esilddprqi lsaqqfkarg eavaamkaeg ieyearlell edvthpkpla elleaayemy
      601 rqghpwvadh qlspkavvrd myeramtfte yvqfygltrs eglvlrylad ayktlrqtvp
      661 edakteelid liewlgelvr qvdsslidew erlrnpsdva evaqahaala drppavtrna
      721 rafrvlvrna lfrrvelaal rrwdllaeld aedgwdydaw adalgpyfea ydsigvgpda
      781 rgpallmieq grerwtvrqi fddpdgdhdw gisaevdlaa sdeigaavvr itdvgql
//
LOCUS       WP_357645080             259 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645080
VERSION     WP_357645080.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..259
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27442
     Region          6..250
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mpepaihvrg ltrtftlakg pvhavrgidl tvrrgeilgf lgpngagktt tvrmlttllp
       61 psgghaqvag hdlladpagv rrrigyvaqs ggldpgcgvr eelitqgrlh rltrrqager
      121 aeelagdlal aelmerptaa lsggqrrrle ialglvnrpq vlfldepstg ldpgsraelw
      181 elvrriradh dttvfltthy ldeadaladr ivvvdagavv aegtpaelks rhtgdpaasl
      241 qdaflaitgr ttagqplpi
//
LOCUS       WP_357645091             495 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora parva].
ACCESSION   WP_357645091
VERSION     WP_357645091.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 495)
  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 495)
  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 495)
  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 495)
  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 495)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..495
                     /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=50600
     Region          36..491
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mttttghlpa laaavlqpgf vgttpppwvc rwlgdglgsv vlfarnvvdt eqvaaltatl
       61 raerpdviva ideeagdvtr lesvhgssrp gnfalgavdd palteavard lgvelaaagv
      121 tlnyapdadv nsnpanpvig vrsfgtdptl varhtaawvr glqaggvaac akhfpghgdt
      181 rvdshhdlpr itadrarlda celapfraav aagvqavmtg hllvpaldpq lpatlsqril
      241 ggllrdelgf sgvvvtdave mravadrygf agatvralaa gadaicigge radeqaarel
      301 rdaivaavis gelpeerlae aakrvgqlaa wtvaarsags aaarsadvgl vaarravrvt
      361 aapgttgalp ltsaahvvef eplrniaiga etpwgiggpl gellpgtstv rygepdvpad
      421 pgagagtrpl vlvvrdlhrh dwmraavhra laarpdavvv elgvpelvtg avhlathsat
      481 rasgraaaev ltgar
//
LOCUS       WP_357645102             763 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645102
VERSION     WP_357645102.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 763)
  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 763)
  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 763)
  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..763
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..763
                     /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=83130
     Region          1..756
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 manrqdalae aldveqgtvs mlygrldaar eraravlrev ygrggalgtr qarverevsa
       61 seqarrlaql egverglcfg ridesggett yigriglrde ehesvlvdwr aaaarpfyva
      121 tasdpgallr rrhlhtrdrt vvglddevfd lermsegerr mlvgeaalla alrrgrtgrm
      181 gdvvatiqte qdrviraslq galvvqggpg tgktvaalhr aayllythrd tlerrgvlvv
      241 gpnpmflryi gqvlpalget qvvmstvgel fpgvrataad gpqaavvkgd armaevvaaa
      301 vrerqrlpeg dlevaldghv lrvpravcva lreraravrl phnmarklfv tellkelara
      361 earaveealr laemewedpe laeplelerd ldevdlalas arlwqepaiy eavqalwpel
      421 tpqrligell aspetlwqvs ppglqwralv rsadapwtvg diplldeaae llgeddsaer
      481 sasrdaegew qeaeryaqev lqstglleeg ifdradvlad rhadtgpdls taeraaadrq
      541 wayghvivde aqelsamawr mvmrrvpars ltvvgdiaqt gsaagarswg evldpyvrgr
      601 wreerllvny rtpaeimrva advlrvvdps qsvpesvrdg eaepravrmg lgglpalvae
      661 elahigegrl avlapdaaha rvaallpggg dleapvvvlt vtqckglefd avivvepaai
      721 maqspmggqd lyvavtratr rltivhengl ppvlsrmsee stl
//
LOCUS       WP_357645109             450 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357645109
VERSION     WP_357645109.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=47441
     Region          40..356
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mslsrtvqva rpllagllla aavlacgtgt gpgggdgktl rvqiptgpla aamqqvgkdf
       61 ekanpgtvvt fegvdsassr gpnvallsss gtpdigylqr stgvwsallk nkqltpleev
      121 wkaagladky sksqvdyytt ngqhygvlye qllinpvyyn kaaftkagip dpidhqvasv
      181 adfesmvgkv kaagyqgfgv ggsspydlgh tldallptav paedydallt nftpgsptnv
      241 kytdpgfvkv lqtiqdwqnk giyqngmlgm dtdqaqglft sgklamlqgg nythaslkea
      301 kpsfemgwfl lppltpgrkt pfdafngdtl vvpvkaanpd lakkflqffm tdkyqvsvva
      361 atgslpvfss ipasslsnlg dlvqqqfels qsvgsvniwd stvpstlgqa fsvpvlqklv
      421 agkltpqqaa rqyqsaledl qsgkvsgasd
//
LOCUS       WP_357645203             335 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645203
VERSION     WP_357645203.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..335
                     /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=34487
     Region          1..333
                     /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 mralvltgpg kaevqeveap laapgevvvd veragvcgtd velftgemsy lrtgrswypl
       61 rpghewtgvv savgegvdgg wlgrrvtgdt mlgcghcdrc raghhhvcad mveigisrgr
      121 pgalaerlal patalhalpd tmdatlgalv epganalraf raaglrpger llvlgtgaig
      181 llvalfarae gveahlmglh tpdvartlgl tgvwtretlp elpwhavvda snapqlpala
      241 ldlveparrv vyiglagtps tldtrdlllr dvtavgilgg saglagaiaa yadasldarp
      301 lvgatvglda tadvlaghrp ddagpgpkih idprl
//
LOCUS       WP_357645261             407 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645261
VERSION     WP_357645261.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 407)
  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..407
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..407
                     /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=44211
     Region          14..402
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(51,58,86..87,94,98,105,236..237,240,244..245,248,
                     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(58,80,82,85,87..88,174..175,184,235..236,239..240,
                     244,288,291..293,394)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mipvvtldpa gtdhhgeaar lrelgpvvrv vlpggveaws vthhalladl ladrrvskdw
       61 hnwtavrdgs iaddwpligm vkvtnmltad grehhrlrkf vtqtltprrv qsmrpriagi
      121 vggllddlps haaadgtvdl rkhfaypvpm qvicelvgvp eeerpelrel vdsifrstta
      181 peevlktqrd iyllldrlva arhaapgddl iseliaaqrd dperltdeel vgtlwlmlaa
      241 ghettlsliv ngarallthp eqralavagg eetwsavvee tlrwdapign fmarypledi
      301 eiagvtipag eailapysav grdgehhgpd aarfditreq rrhlafgggp hlclgaslar
      361 leatealpal frrypglsla vppaalvpvp slfsnsaael pvfltvp
//
LOCUS       WP_357645294             170 aa            linear   BCT 28-DEC-2024
DEFINITION  HIT family protein [Micromonospora parva].
ACCESSION   WP_357645294
VERSION     WP_357645294.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..170
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18588
     Region          33..159
                     /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(58,60..61,68,70,116,124,126,130,132)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(128,130,132..134)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            130
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 madglerlwt phrltyisge drpaegyekp tgcpfcrgpq lppeqslvva rgehvfvvln
       61 lypynpghll vcpyrhvady tdldvpetae lasytqtamr virkvsnahg fnlgmnqggv
      121 agagiaahlh qhvvprwggd anfmpvigrt kvlpqllgdt rdllarawps
//
LOCUS       WP_357645327             384 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357645327
VERSION     WP_357645327.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 384)
  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..384
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..384
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40930
     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 mqqlpldgvk vvdltsvlag pycsyqlmlf gaevvkvelp gsgdlarrlg pddelnrdri
       61 gasflaqnag kksveldlks pagrvafeam vtgadvllen fragvlarlg ydrdrlreln
      121 prliycaisg fgqsgpmsga paydqiiqgl sgmmsvtgtp dtvpmrvgfp vcdtigglma
      181 amaicaalag rhrtgrgsfl dlsmleasis amgwtvsnyl vsgvepepmg dqnataapsg
      241 tfetadgpln iaanqqtqfe tlcrligrpe lpadprfvlp egrkaqrkal naelngalra
      301 rtaleweell sghgvpaarv ltvpqalald qlrhrgflte lsfpdgtdrr ltvtgngvlv
      361 ddeplrppvs pprlgshnee yahe
//
LOCUS       WP_357645355             181 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357645355
VERSION     WP_357645355.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 181)
  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..181
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..181
                     /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=21064
     Region          1..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mredtrsriq eialklfieq gyeatslrei aeelgvtkaa lyyhfktked ivasladlrv
       61 admeellawf rsrsntpetr relllryadk ltnrryleia rfmernqtal rdhpkihrmr
      121 evmleltsei ndpgdplavr isrsmalftl hagkwmaqde klteeeisea alevalrlme
      181 p
//
LOCUS       WP_357645426             312 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357645426
VERSION     WP_357645426.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..312
                     /product="helix-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=34426
     Region          21..309
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mldtsarllr llsllqarrd wpsadlaerl gvavrtvrrd verlrglgyp vhstrgvsgg
       61 yrlgagaelp plllddeeav avavglrtaa ggtvtgieet slralakleq vlparlrqrv
      121 nalqthtvpi tpdgptvaae vltavaaacr dheqlrfdyt grdgvtterk aepitlvnws
      181 rrwylvgwdv drrdwrtyra drlrlrtpng prctpreppg gdvaawverr lghdmwpiqa
      241 rvllyapadq vagrtagvve pvgddtcvlt lrgddlhlia vvvafldldf evlepvelke
      301 rlrglgrrlt tl
//
LOCUS       WP_357645440             262 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357645440
VERSION     WP_357645440.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26478
     Region          4..257
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdmrltgkta vvtgasrglg laivaalrae gmrvvagsrt ispelketga taiavdlssa
       61 egpaeligta laelgeidll vnnvgggdgg egqldgflgf teeqwhqahd lnflsavrat
      121 kaalpsllrq ggtvvnissn garmphagpi vyttakaalt afgkalaeef gpqgvrvntv
      181 spgacrtsmw edpngygaal aakmglehdq llaglpsstg mttgrfvapq evaalvtyla
      241 sphaasvnga dyvidggaik tv
//
LOCUS       WP_357645472             336 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645472
VERSION     WP_357645472.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..336
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..336
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=36799
     Region          25..>188
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mavacpadrr rrpiltkalt amitavflla slatpghaap kptikqlkke laalgkqsdk
       61 liteyyngri ahqkaekaek aaqeklaaaq evydresael rlmavsqytn ggppspatml
      121 stsedpsalm srlalsnhlv dqqsarlsgf aqvrddrkka eeeaaarake lgdqvadlgk
      181 rkdkaeqlik kikdkidkly qapgvrrsdg twvpqlpggs dnitprmrlv ktlvkehfav
      241 pngigcyrai qdggehplgr acdfmlsrgg smptaaevar gneiaawaik nakrlgimyi
      301 iyrqriwhar tgawrtmsdr ggttanhydh phisvy
//
LOCUS       WP_357645528             980 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357645528
VERSION     WP_357645528.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 980)
  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 980)
  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 980)
  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 980)
  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..980
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..980
                     /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=107637
     Region          5..230
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          105..976
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          751..779
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          784..824
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          831..859
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(832,835..836,839..840,842,872,875..876,879..880,
                     882..883,912,915..916,919..920,923)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          870..900
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          911..938
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnasitasrq qtvlamllle annvvplgrl ieavweespp staksqiqic isavrralrg
       61 tglddrivtn pagyqirvae geldlhifnd llseartalr eqrledaasg frqalalyrg
      121 aplsgvdsrl veaaatriae rrlavvedcl elelhlgrhr etidelmalv tehplrerlw
      181 qqlitalyra grqaealaay rsarqasidd lglepseplr llerailngd lepgpvveqe
      241 wpnpiepapp vprmapadip dftgygelvt elgdflrygs ghsdhdsvpv ltitgrggag
      301 kttlavhlah elagefsdgl lftrlgpers hsggvsqild gflralgmpg ssipeglear
      361 aatfrsqiaa srvlivlddv vderqvypll pgspscgviv tsrrrlagip gsrlvevsal
      421 eqrdavellt rmvgserasa eprealrlve lcgrlplalr iaaarliarp hwrmaqlter
      481 ledegrrlde lahggldvrt niaisyegld eqaqrllrrl gllethdfps wtaaplldid
      541 vstasdtlda lvdaqllevv ggfgvdtryr lhdlvrvyar erlaaeetap vrleaarrll
      601 gawlfladea hrilyggdyt vihsraerws lpghlvhdll rdplmwfene raaavaavgq
      661 asqagapdyc wdlaitmval fetgsylddw ratheiallt arqaddrlgt aamlyslgav
      721 diveqrfdda rarltqalev fdeigeargr alalrhlafl drvhgdldqa warysealaa
      781 lhplgdaagt ahilsgmari klewsergsa aellaealrk vtevnstrvq amvlhrlgel
      841 hfedgdltra eeeltkalkl vrgghdrage ahvlhglglv klrqhqhhqa avtlnhgyai
      901 arrngdrlat arfclalarv hrarrdyssa lewasqalgi fdqfhallgr leaekllgqi
      961 rdeaagrhdv reqavlppav
//
LOCUS       WP_357645541             872 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357645541
VERSION     WP_357645541.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 872)
  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 872)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 872)
  AUTHORS   Rosinski,J.A. 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 872)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..872
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..872
                     /product="helix-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=93506
     Region          <9..869
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          431..461
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          807..863
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdstevtird rlrdvfagrh selrricaat drrgsagial igpegvgksr lqteaahrad
       61 parhhvirav ttmatanvpf galaehlpsg llrspftgda lrvaaeallk pagkrrltlv
      121 vddaplldea saalavqlar rgelfllaav rpdrrlprpi adlwtdglae wievgplsrd
      181 dvhqilgeal sgqvegalvq rfweatagna llvrelltaq leanrlvted gmwmlrgpfa
      241 ipswltglid erlaavspec rsamellavt epigpnvlge mvsadvleaa eahglitier
      301 sggqdlarlt ypiygdvlra vtprlrarrw lgqcaslmea sshdpvdlar tvrwqlacgq
      361 rpspentava araarsaldf elagqlaqre laagrgtavi eplgygllfa grpadaesal
      421 sglgrldcdf drarvamvra fnlyfgldrq gpaeallaaa vddvvdpvar rrlvarqall
      481 ralsdapkda lefaagapde peaqvaagla mvfsgrpheg ldllagewpd eapwlsvlad
      541 lgtvhgmlwt aqfaaaeera rtsyeralan rwqfatlvsc llrglvarmr gqlrdqaswc
      601 regisiareq rsnnmlavll gllahsyalt gepdaaastl aeadrldgvs lrllspwtel
      661 nrawvigarh gdaaahaqwt arlardrgsa gfetlalhda arlgaprhaa drlralagqs
      721 grllgksyal haramaegda aalaevsadf aemgspllaa eaaaeeserh rsdgrlamas
      781 taaaralmfm rhcdeiprsp alsalapprl tpregeiael aagglssrei artlvlsvrt
      841 venhlhrvyr klgitnrgel galsvlltrp qt
//
LOCUS       WP_357645558             226 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645558
VERSION     WP_357645558.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,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 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /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=24018
     Region          3..225
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 miiedltvrf gaftavdrvt leippgrivg lvgesgsgks slaravsglv pytgridgan
       61 nvqmvfqdpy asldprmtvg gsvgegvrad ratrraever llglvslpvd larryprels
      121 ggqrqrvaia ralgaapdll vadeitsald vsvqgavlnl vrslrdelgl smlfishnla
      181 vvryvsdvva vmhqgrvves gptervvgep ahdytralle avprlt
//
LOCUS       WP_357645612             487 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Micromonospora parva].
ACCESSION   WP_357645612
VERSION     WP_357645612.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 487)
  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 487)
  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 487)
  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 487)
  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..487
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..487
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=52600
     Region          61..487
                     /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 mvsrrnvmka gatagaaalv tttaaaaarg stppatpahg ahtghrgtah vaaaaapftv
       61 rmpippvqqp iasvgntdfy vvstrkaqae ilpgtrtevl tydglfpgpt frvktgrlav
      121 iahsnhldmp tavhvhggqt psssdgfptd vldpgrsriy sypnkqraat lwyhdhahhm
      181 eaehvfrgla gffliddpaq adlrlpsgny dvpimlrdar faddaslvfe hddfqfrnti
      241 langkpqpyf qvaarkyrlr fvnasnlrtf tlrlgndaev tqiasdggll agptpirsws
      301 ltpgerieiv vdfgafpvgs qvflddavag pvlrfdvnrt atdasrvpdr lstipalpaa
      361 tkeraftlnl npatgqflin gqqfdadrvd teikrnttev wtvtngdtlf giphnfhphl
      421 vqfrvlsrng qppapgeagl kdtisvgpge tvrlqatfgp ylgryvyhch midhsasgmm
      481 aqmkivp
//
LOCUS       WP_357645617             474 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357645617
VERSION     WP_357645617.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 474)
  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 474)
  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 474)
  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 474)
  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..474
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..474
                     /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=49717
     Region          2..473
                     /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 mtdefdvivi gagpagenaa aravrgglta aivedrlagg ecsywacips kallrpvdla
       61 gevgrvpgms lgplevskvl arrdeavahy ndsgqvewik nvpvefvrgr grldgvkrvr
      121 vttrdgqett ervltarhai vlatgstalv ppvpglaeak pwtshevtaa qavperlavi
      181 gggvvacema qamhglgarq ttvlvrggsl larmepftge llaesfaeag idvrthtdvi
      241 rverpepggk vtvhlsdgpp leadellvat grvpataglg letvglaggr svevddsmra
      301 tdveggwlya igdvngrall thmgkyqarv cgdviaarak gsdetllamr diadgygapq
      361 vvftdpqica vgrteaaark agfsvrvvey dlgnvtgayl lgdgyrgrak avvdeerrvl
      421 lgvtfagpgv aellhaatia vtaevpldrl whavpsfptv seiwlrllee gygl
//
LOCUS       WP_357645669             431 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora parva].
ACCESSION   WP_357645669
VERSION     WP_357645669.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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 431)
  AUTHORS   ter Beek,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..431
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..431
                     /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=46557
     Region          29..348
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msdfdpgrrr flghlglagl galgassfls acassasgpt tstgsgavti qsnlsspqak
       61 aameklietf ngqgkgtasl ntiasetfrt qlptyltsan ppdlytwyag svandyaskn
      121 llldvsevwk slddypqslr tlstdasgkq ifvpmnnyww gffyrksnfa kwgvqepknw
      181 teflalcetl kskgippigi glgdtpwvas awfdylniri ngapfhrell agkqrfddpk
      241 vkavftrwre alpyfdpkgk aypfqeatta llagktgmfl igtffadaap kdalgdldff
      301 rfpiidpavp laeeaptdgf fasaktanpt gtkallsyla gveaqeayvk assgivlpan
      361 prakasdspl vakgkamlne akeltqffnr dssdalqpta dtaltkfidk pdqidailre
      421 wqagaekvfk g
//
LOCUS       WP_357645786             478 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645786
VERSION     WP_357645786.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 478)
  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 478)
  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..478
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=50179
     Region          112..478
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mirpplvrgl raqlvlvfll vsalsaltaa altfrqgrta ivervqadal qelrahlgar
       61 apdlpadpae adlrtlalql draagtrgwr talsyrggpl itagaqappl parlraqaas
      121 attalaqrfh haqtpwlava lpviaaarph spppltvyas fslasqqqdv etlaaaarsg
      181 alpvalasiv lallaarrll rpvrqlrtaa ermaggsldt rvdvtgddel adlgrtfntm
      241 aatlqadaaa lrameararr faadvshelr tplaamaavt evldadaasg rlapltaeal
      301 hlvsdetrkl trlvedliev srfdagaavl nldeidlgef iaktlalrhw qdrartdvpp
      361 glrarldprr vdvilanlvg nalrhggaav svliqvrags dqitiavsdd gpgipadllp
      421 hvfdrftkad aartrtdgsg lglaiatena rlhggtltaa naphggavlt ltlprdpp
//
LOCUS       WP_357645789             263 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora parva].
ACCESSION   WP_357645789
VERSION     WP_357645789.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..263
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27281
     Region          10..243
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlglpahvta clfdldgvlt qtarvhnaaw tqtfdeflrq raaasgtpfq pfdpgpdynr
       61 yvdgrpradg vrsflasrgi vlpegnpddp pdadtvngvg nrknvlllqr lrtsgvevyp
      121 gsvhyltaas eaglrravvt asangaevva aaglepllea rvdglvarae glrgkphpdt
      181 flagarllgv dptqaavfed alsgvaagra ggfgyvigvd rvgqadella hgadivvtdl
      241 adlldvadpp tptrtatter gsa
//
LOCUS       WP_357645808              69 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357645808
VERSION     WP_357645808.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 69)
  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 69)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..69
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6949
     Region          1..67
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mstatytvkg mtcghcvssv keevgevagv tsvevdlasg lltvdsesli deativaavk
       61 eagyevanr
//
LOCUS       WP_357645812             379 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645812
VERSION     WP_357645812.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=39942
     Region          60..376
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mirlrkgtvg arftilyagv fllsgivlla ltfvlsdtev stggppqpag dgmtaaqrhi
       61 lqlqrqlgdt eanqsrqlli gsllalvvma ivsllvgral arrvlrplrl itaatrrisa
      121 dnldrrlavs gpadevkdla dtidgllerl easfaaqrrf vanashelrt platmrasld
      181 vavakpgvpt qtlvvgdrlr tqldqvdqll dgflvlaraq hgalaeaavv dlddlvaral
      241 tghaaaiaak rlevttrlra agtrgdaall srmaqnvidn avahneeegw ihaetlrega
      301 evrlivrtgg rvldqrdvdr larpferlgv drtgsengsg lglsivaaia aahggrldll
      361 arpqgglgvs ialpagata
//
LOCUS       WP_357645843             448 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645843
VERSION     WP_357645843.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=48057
     Region          80..448
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 madspllwwr rqglrfrltv vaaavlalal aisasvlltv lnraligtvd dstqqqaqtv
       61 rvqadagtlt spiathdgti vqvidaagri tdvtygadrl vplldarera evlrdgqatf
      121 ldgrpfaisg plrvvvisad hgrtvvaarp igeiqtslgt agrvllvgtp mlivalavas
      181 wvvigrtlrp iaalrrgaae ithtarsrrl pvpesrdevh slattlndml arleeaeqrq
      241 ralvsdaahe lrsplasirl qlevalghpe gqdwpetaeg vmedamrlsr laedllalar
      301 lderggvpar repvdldevv rqtvdrygea rltvcdpvvv rgdaldlsrv ltnlmdnavr
      361 htsskveval tadgvltvtd dgpgipeqdr ervfnrftrl dsgrsrdegg aglglaivre
      421 tvrahgggvh ledaapglra vvrlpvar
//
LOCUS       WP_357645892             293 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645892
VERSION     WP_357645892.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 293)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..293
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..293
                     /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=33136
     Region          2..285
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrrfetrwgi lmalpailgf viftlgpmva sfffsltdwq iggspsfvgl dnytrmande
       61 lfwkslsatt yytlgavplt livsfavaml lnqkarglsl wrtifylptl vpaianvvlw
      121 iwifnpdfgl lnsllrqagl ptsqwvysee maipsliims twgfgntmvi flaglqgvpr
      181 hlyeavsidg ggplrrfwhv tlpmmtptif ynlvvgvvgt fqvfnqayvm teggpnhatl
      241 fyvyylfrka ftesemgyas alawvlfmii mvvtflmfrn arrwvyyema gar
//
LOCUS       WP_357645916             346 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645916
VERSION     WP_357645916.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 346)
  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 346)
  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 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   5  (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   6  (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   7  (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 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..346
                     /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=38583
     Region          38..343
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 maapdriave raanagpagd lpspagsgtt rrrvgrraqn rikhgslrar frrdwqlllm
       61 tvpaigllll fhyvpllgnv iafqdyspyv gvkdspwvgm snfqwlmfdq sfwdatintl
      121 sitmfqlify fplpillail ldsvvrprlr lfiqgivymp hffswvlvvt lfqqmfggag
      181 llaqilrdhg fagvdimtnp dtfillvtae tvwkdagwgt iiflaalaai nphlyeaaav
      241 dgasrwrrlw hitlpglrpv fvlllilrlg dalnvgfeqf flqrdavgrd aaevldtfmy
      301 wrtlltgews ygaaaglvkg laglililia nkvahrfgeq giykrs
//
LOCUS       WP_357645927             435 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357645927
VERSION     WP_357645927.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 435)
  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 435)
  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 435)
  AUTHORS   ter Beek,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..435
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..435
                     /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=47280
     Region          22..347
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 miklrsaaaa lavaaltlta cgsgsdgqqp aasgqprvlk lwhyesaega mgkawaeaik
       61 kfesthpgvt vkfeekgfeq iqktasmvln sdeapdvmey nkgnatagll skqglltdls
      121 eqatkrgwdk llsaslqtta kydergimgs gkwfgvpnyg eyvmvyynkd lfkkngvtvp
      181 ttfeefttal dkfakagvtp istagaeypa qqifyllals kanrawvdsy elykgkvdfh
      241 gpeltyaadt ladwvkkgyi akdsagikae dmatafiggk fpimvsgsww ygrfqteikk
      301 fewgsflwpg nqlapgssgn iwvvpekskn kdlaydfidi tmskeiqnll gnsggvpvaa
      361 dpaaitdpks kelidnfnkl tsqdqlafyp dwpapgyydv lvagvqnlin gskppakvld
      421 eiaqpynenl adlgn
//
LOCUS       WP_357645938             304 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645938
VERSION     WP_357645938.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  AUTHORS   ter Beek,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..304
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..304
                     /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=32628
     Region          40..279
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mssltattaa raatgsrrlp rlspylfiap ffavfaafgv yplvyalrls ltrwrgagea
       61 twvgvgnyvy lltnpdfwas lgnsavmwll ivpvqviagl gaavllanar lrlrglfrva
      121 fiapfvtplv amaqvwivvf dedyglvnhv lglvglpavg wltstawakp tlallflwkt
      181 tgfaiiilla glqavpgavy eaasidgasr wrqfwsltvp lvrrsiaflv vvqtlavfqm
      241 faepyvvteg gpygstttag lylydhisas dlgtgaansf llvllvfgls lgavrllrpk
      301 eevs
//
LOCUS       WP_357645978             358 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645978
VERSION     WP_357645978.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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 358)
  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 358)
  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 358)
  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 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 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..358
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38924
     Region          75..217
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mnehaqrppa eiryagelar lrehdtddrp pgwalslraa rrfvlgdetl gisrkfvgdp
       61 slidrslvtl atnrglmlvg epgtakslls ellaaavsgi stltiqggaa ttedqikysw
      121 nyallvaegp strslvaapl lrgmaegkvv rfeeitrcpl evqdcllspl sdrvlavpel
      181 ggpesmvfaq egftiiatan trdrgvnems aalrrrfnfe tvfpiadfdt elalveaeag
      241 allkrsgvtm pprrdvlevl vttfrelrqg qtargdatdr lsgvmstaea vsvahavglr
      301 gwflrrepgt aadlvsclag taakdnpedl aklrrylerr rhgdqwkaly earhllpg
//
LOCUS       WP_357645942             704 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357645942
VERSION     WP_357645942.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 704)
  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 704)
  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 704)
  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 704)
  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..704
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..704
                     /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=77158
     Region          23..>468
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtpraeyprp hfdrshtwss lngewdfrad adqgwdrtir drtvwdrtit vpfawetpas
       61 gieahwlpva wyrrrvtvpa gwagqrivlh fgavhheatv wvndtevarh vggytpfead
      121 itdalregeq eivvrvsspa dkreiahgkq rsiprddfdg vcftpssgiw qsvwlearpa
      181 thlaalklrp aegldgieve arvegpapat lrlsvrgqat tvevpvsggt aptapqtdgg
      241 tggrvaravl piaeprlwsp edphlyhvda elvsadgtdr vtgytglrri evsgedlyln
      301 ghrlfvrgvl dqgywprtgi tapddaalrr dlelaaaagy nlvrkhlkle dprfvhhadt
      361 lgmliwaepa atgrfsaesv aafeaqiapm aerdgnspai viwglyneew gldwdipgdp
      421 akqdaaaray dllkaldptr pavdnsgwah vktdlldwhy ydesaaswgr tiaallngdq
      481 ddfpvplgpd yvvrkklagt paqplrglpn lnseygtgft svqrgwqlrw qtqemrrhdr
      541 lagyvytemy diehesagll dferrakdla gvdpahvnat ttlvldvvpv apgrdllses
      601 grvtvpvris hhgkdsvsgh lhtawspvfg paparpgtag eraeakpfll gapaevhael
      661 pdgwtsgrlh ialvsdddtv larsavdvdt htapvigddp qarp
//
LOCUS       WP_357645998             452 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357645998
VERSION     WP_357645998.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 452)
  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 452)
  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 452)
  AUTHORS   ter Beek,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..452
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..452
                     /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=48371
     Region          53..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(167,169,292,294,327..328,369)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mtrqhhpaev lgphalsrrg firtaaqagv amglasavsa cggsdggsgg gvtlqlwdtd
       61 trpertanlk klismfeakn pgirinylgl ptdqymqkin taiatrstpd lltpkasdla
      121 alvaqnalap lderlkkagl eqhiseqmlk ssraaapdgk lyltpttsla dviyyradwf
      181 qeaglkppat wadfdaaasr ltdassgrfg ytlrggngff gqfvqmvypr agvstffred
      241 gsstlndpav iaacekyval fgkqtarsdl tadfktmvaq fgnggaamls hsigsypnhv
      301 aalgaekvga vapfpgpdgq vltgwmttgf amfqksehqe eawkflaytm epegnsfwaq
      361 ksgylpgnkt vakeqwvten aamkaaldaa akpgvvtleq pyylpeftai tvtdllpewq
      421 kvlqgsltpr dfltagaaal ttakrkydke hg
//
LOCUS       WP_357646019             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            parva].
ACCESSION   WP_357646019
VERSION     WP_357646019.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..416
                     /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=44906
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..379
                     /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(349,351..353,355,366..367,371..372,375,379)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mlealeqvgd avddcaettl wglsddella sldatqvlsq rlatvqlglv revdsrglav
       61 tqgasstavw lrdrlrlsgr sarqlvqlaa tidaappavr dallngaitv eqgrvvaeti
      121 aalpveagpe vadkatqllv twadrfdpts lgrlgervlt hvapeladra elkalerate
      181 raearrhvtl seqqngevrl sgnldtetas llreaidplc apagehddrt pgqrradalg
      241 eicrlalrtg qlpdnggdrp qlvvtvslde lingvragtl etgtrltpga vrrlacdagv
      301 lpavldgnsq vldvgrqrrl ftgplrralv lrdggcafpg cdrpprwcdg hhirhwadgg
      361 vtalgnavll cgyhhrlihr ddwtvrvaad grpaflppsw ldplrtprrn hyhlrc
//
LOCUS       WP_357646022             761 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora parva].
ACCESSION   WP_357646022
VERSION     WP_357646022.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=80659
     Region          163..757
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpaldlgtdt dtdldadlaa erahlstsra alarmrarae slfatgdqva gdayaaetlg
       61 rtlarrvael addpttplff grldfaeapn ngtptsttpt sttptsttpt satptnatpt
      121 sttptsttpt sttptstgth hlptgstatg npttsdptap dtggdhegrr yhvgrrhvtd
      181 ergeplvldw rapvsrsfyr asvrdpqgva vrrrfgfsng vltsfederl drgeelgtts
      241 riltaeierp rvgpmrdiva tiqpeqdelv radladsicv qgapgtgkta vglhraayll
      301 ylhrerlrra gvlivgpnra flsyiaavlp algeveveqa tveelisrvp vraveapava
      361 alkhdvrmad vlrravqaqi gtptesitvs dgsfrwrigl eplhriveet rreglpygtg
      421 rervqarvvs llqrqaearr aespsdawlr rmsrcrpvld fldavwpalt peglvhglfa
      481 dparlaaaad gllsdaeqaq lvwakpartp katrwtaada vlideatgll erlsgfghvv
      541 vdeaqdlspm qcraiarrse hgsvtllgdl aqgtapwaat dwreslahlg kpdavvvplt
      601 vgfrvpaavv afanlllpal avdvppaesl rrdggldvrt vtdltsatva evraalahdg
      661 svgviaadda vdglraalae agvetatadd vaaaervtvv patlvkgley dhvvvvepaa
      721 ivaaeprglh rlyvvltrav srlavlhvap lpaplvggsa g
//
LOCUS       WP_357646023             391 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357646023
VERSION     WP_357646023.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..391
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40248
     Region          23..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 mdmthpperp gmnertdsqe gggalsgllv adfsrvlagp yatmlladlg advvkverpg
       61 agddtrswgp phaggvatyf lavnrnkrsi aldlrdpadl evaralaara dvlvenfkpg
      121 tmdrlglgys vlsaanpglv ycsitgfgag kgaelpgydl iaqavgglms vtgepdgpgt
      181 kagvalvdvi tglhaglgvl aalrhrdatg qgqrvsvsll ssllsaltnh asgyaaagvv
      241 pkamgnrhps ivpyevfqaa drpiviaagn drqfralcqv lgradladdp rfaantgrva
      301 grevlvaeld rtlgtrtade wfaaltpagv pcgpintlda afafaaelgl dplagdqvan
      361 piglgatppe yrlpppslgq dadwvreilg q
//
LOCUS       WP_357646040             245 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646040
VERSION     WP_357646040.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,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 245)
  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 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..245
                     /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=26489
     Region          <2..244
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mildltdvtv sfttgpplrr trldamrgvs lsvaegetlg lvgesgsgkt ttsrvalglq
       61 rpstgtvrfd grpfprrrkd lagrmqavlq hphwslnprm rigqsvaepl avlgkaagel
      121 vpealeqvgl eagfadryph elsggqrqrv siaralitrp sfivfdeavs aldvsvqvqi
      181 lnllkdlqae ygfaalfish dlgavryvad riavmrggev vetadaetfy sapehpysrq
      241 llesl
//
LOCUS       WP_357646060             158 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646060
VERSION     WP_357646060.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..158
                     /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=17219
     Region          33..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msdatndsgt geaaqdavar swaamcflvl kqedrrkevt dtlgmsffra kalrrllggp
       61 ltmreltarl atekpyttlv vdslerrgyv ersvhpddrr sklvtltpdg vaaaeqaeri
      121 larpprslla lepaelaald rimaklqspa evtseqap
//
LOCUS       WP_357646061             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357646061
VERSION     WP_357646061.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31541
     Region          11..291
                     /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 mgvervpagf teqrarvgqi tmnyvrggag pplvllhgyp qcwhmwrhll pelgrsfdvv
       61 apdlrgfggs dapdggydkk tvaadlhgll dqlglvgdlr lvghdlgtmv ayayaaahpq
      121 rvsrlvlsea pipdesiytf paltsagpgv wnfgyfsldn glpealvngr eslwvekftd
      181 almvrkgsia apdieefagh lrdparvras fayfqafeqd iadnaayrgt kltmpvlavg
      241 aaaslggqva eqvrgyadtv rgeviedcgh wlyeerpdem lallrdflqa t
//
LOCUS       WP_357646086             145 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646086
VERSION     WP_357646086.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..145
                     /product="YybH family protein"
                     /calculated_mol_wt=16238
     Region          5..126
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mnsnesevra llesrvdacq tkdvdrlmsh yssdivyydv vpplqfagsd qvrgnfvrwf
       61 deyagpisle thdltlatge diafanmlhl dsgtrknglq saiwvrstvc crrsgdkwli
      121 thehisvpin penlqawfpp gfepa
//
LOCUS       WP_357646132             996 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357646132
VERSION     WP_357646132.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 996)
  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 996)
  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 996)
  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 996)
  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..996
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..996
                     /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=107396
     Region          1..241
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          124..958
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mkfavlgpld isadaqslpl gagkqralla ellcrpgrpv ppatliqalw gqspprtapd
       61 nlrlyvhqlr rtlghdritr taagyvltlh pgeldadrfe elaeqgrnal sageheraae
      121 llkqaldlwr gpvyaelnlt vglsdhahrl eeerlialen rieadlargt haelvaeltw
      181 lvgehplrer prrqlmlala rsgrqaeala tyrdarrvfa telgldpgae lrrlhqailt
      241 gtlpvefata psdapsprsp aqlpadisdf tgrieqlael tdllgdgppp gpgpmrvyvi
      301 agmggvgktt lavhaahlia qhypdgqlht nlhgaesspa dpaqvlaafl talgvprptl
      361 petleeraav frsrlaerrm livldnaase qqvrplfpgt sgcaviitsr trltglsgaa
      421 vvelsvlhpe qgvqllsriv gadrvaaepe aaaelvrlsd giplavrvag arlvarphwp
      481 ltrlagqltd errrldqfat gdlavrasla lsyvgldpda rrafrllgsl dvpdfagwva
      541 galldlpvaa geelvetlvd tqlvlfsgmd aagqpryrfh dlvrlyarer geledepeav
      601 aaalnrafga wlalaerate rvpgtssaii hgtaprwnsp dgapwdgpav qdpmawfdte
      661 rtaliaairq acslglaeva wdtaccvery fdvcgqfddw rglhervlev clatgnrlge
      721 avirrglmha ttwmetggea maaqyegaer litlfselde erglsdayvl rawgeaargd
      781 maeglrsgqi altlaessgh qsgqaralvc mavaygtrdi kmaivhllrg lelaeklgnp
      841 rfeattlqfl glahahaqef dagleylvra laiyrqirdp lleamglval arlyaghhdp
      901 rarpaaeaae mlsrshrlah hqadalwvlg gvdlaegrid eavahleesv rlwrtrgwqe
      961 flagaladla aaytaagdlp aaaaargeat altgst
//
LOCUS       WP_357646140             601 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646140
VERSION     WP_357646140.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10196292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..601
                     /product="serine/threonine-protein kinase"
                     /calculated_mol_wt=62877
     Region          22..272
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22,45..46,75,80,85..88,100)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,49,51,83,99..102,106,108,145,147,
                     149..150,152,161..162,165,183..186)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,49,51,83,99..102,106,147,149..150,
                     152,161..162)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(33,106,108,145,147,149,165,183..186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(161..169,179..186)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          486..590
                     /region_name="DUF4352"
                     /note="Domain of unknown function (DUF4352); cl13117"
                     /db_xref="CDD:448816"
ORIGIN      
        1 mgqqgrsagt pltpedpsai gpyelisrlg sggmgtvyla kaadgvqval kairrdyttd
       61 pvyrarfhee vsnarkvasf ctarvldhge hdgvlylvte yiegislenh liehgpltps
      121 vlhsaavgva aaltaihavg lvhrdlkpan vmltlggprv idfglarssh vstrhtnagm
      181 vmgtpgwiap eqvfegrtsp agdvfawgsl iayaglgghp fgegdayvma arartappdl
      241 rglpapldrl vaaaihpdpa rrpaakqlll elvgaadepa aqlaatrhls sswnpsefpp
      301 laefphnpqv rqappgwtpp pqahqpsarq pqshqpsshq ssthqpqghq pqghqqtgvg
      361 plpgrgpvph ppaqappppr qapprqapsr qasppgpasq vppslqtgqm ppslqtgqvp
      421 lsahqtgqvp lppgprgpag fpvkrkrsvf tgcvtaivva ivlfvlllav lvwalrspdp
      481 vgadspvqdg klkfavtgtk cpqpakgakq rtcqvsvkvn nvgpearvly pgqqkllded
      541 dalhggtkll dkagaevtpv rigpgqsfsg allfelpkea kpaglelhds glstgvrvsl
      601 d
//
LOCUS       WP_357646148             323 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357646148
VERSION     WP_357646148.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 323)
  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 323)
  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 323)
  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 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   5  (residues 1 to 323)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..323
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..323
                     /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=35137
     Region          <254..310
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mvryeligmd vadlrfavsp lnevvlslra wrdpgrfplq lrwlhaleav rgsldeamll
       61 altdvrlwtp dflnprphsp ltrfddelak lastdptvie rdlravhgat plpeplqgsa
      121 aevlnriida latywrfcfe phwprmrail egdvtfrgrq iaqrglatml sglsdtvrlv
      181 gnvvevrlrs kldyarpana gltlvpslwt tnastpisad eppmilyaar gaatlwepqa
      241 lpapdglagl lgttraglls hldtpasste laarlgvtpt avnqhlralr aggllvgtrh
      301 grsvlyrrsd lgdmlvasaa phs
//
LOCUS       WP_357646157             345 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646157
VERSION     WP_357646157.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 345)
  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 345)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 345)
  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..345
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..345
                     /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=35670
     Region          87..345
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnlvgavvql calvvafrpr vppvysavgg gavslaitay hpltgtrgda tfwllievpa
       61 llaltmlaar raplaalvpg lavstillrm vwpgppslil agcagwslga igvaaaglyl
      121 rsldgnrrra vaqavrdqrl alardlhdfv ahdvsgmlvq aqaarlapel ppriedalrr
      181 ieeggqralt sldrtvhmln epargpapgi dglrdladgf sptvqvnlav eaeqisreas
      241 atvyrvvtea ltnvrrhapr astvdiavtr egnmihiqvh ddggsggqae agdrgdrsgg
      301 grfaglgrrg gfglaglaev lgtvggslsa gphgtgwrvt atvpv
//
LOCUS       WP_357646265             359 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357646265
VERSION     WP_357646265.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=36472
     Region          35..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 marptgsppv arpaglrkrw lvaglfavlv alvagvslgp vslppgsvaa ellnlvpgvh
       61 ldsglterei aivtelrlpr vvlgllvggl lalaggcyqg vfrnpladpy llgvaagagl
      121 avtaaialgg ggrqgtlsgl pmtiplaafa gsllavtmty vlgaaggrrg spamlilagv
      181 avsaflsagq tyllqrnads iqpvyswllg rlatagwhdv llvlpyaalt tvvvllhrre
      241 ldvlavgdde arslglhpqr trylliaaas lgtaaavsat gligfvgiiv phtvrllags
      301 syrvilpmsl lfggaflalt dvvartaaap sevpigvvta llggpffvlv lrtarrvlt
//
LOCUS       WP_357646183             511 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora parva].
ACCESSION   WP_357646183
VERSION     WP_357646183.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 511)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..511
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56294
     Region          84..483
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvstdp rqqppavtst applavpngr hhqsvpqpmp avtpppeppp rprmdfqvvr
       61 elrrelterl tlwqrgreft vdeedterar lavtvvaaya dsvrragtpm aaseerllld
      121 qvtaelvglg rlqtllvddt ieevhilgcd qvritrhggg vdwaepiads daelveilqa
      181 aarragater slstvkptld lqlpdgsrla avflvshrpy avirkhntld vslddlaggr
      241 ndldemidpl lrdflraamr aglnimvagl agagkttvir almneipqde pyvlleesre
      301 llparrrerh ravmsfeare ghgergfdgr pagevtiadl iplslrmgvl riivgevrsr
      361 eivpmlqamt tsrgsmctih artaagvger ivelalahgr emtvdqarrm agnaldlivy
      421 vtvedetaig grkhrfvshv eevigageag rittttvfgp gpdgravprh lpervrdqll
      481 rvgydarllt rwveagagaw rrprqtrlar r
//
LOCUS       WP_357646279             225 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Micromonospora parva].
ACCESSION   WP_357646279
VERSION     WP_357646279.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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..225
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..225
                     /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=22876
     Region          20..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 mrlaalryav ppglpsrtgc dacgapvalt rpwpalgpaa rcghcrarvg pppgtvevav
       61 laavlllavg gpsdgalpal iwwlgwtipa ilvdlavhrl pdrltlpaaa gtwlllgvaa
      121 ldadpahwlr avtggtglal ffastavllg rrgfglgdak lalsvgallg whgwpvllfg
      181 mlltfglsav vslgllatrr anwgshlpfg pflllgtvga vllaa
//
LOCUS       WP_357646346             467 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646346
VERSION     WP_357646346.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=49352
     Region          122..464
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnlvprtlra rliagllvll alscaavgva tsvamdrfll arvdqqiaad gprfaesleh
       61 gedtrgqtrg tfgarlvdgr vthaavvser dgthpglspd deailaalpv ggppqtvdls
      121 klddyrlvat agrdgdvlit glslhgveet lnrlwlfelv mfagalavtg vagalwvrla
      181 lrplqriatt arkvaelpla sgevtlaerv pdtdprtetg qvgaafnrml ghveaalgrr
      241 haveqrlraf aadashelrt plaairghae lalrgdepma dgvrhalgri daesgrmsel
      301 vdellllarl dagrplaree vdlsrlaiea tgdaraagpg hrwrlelped pvtvtgdplr
      361 lhqviasllt narvhtpdgt tvvvavrrlp gavevtvedd gpgvpaglee eiferfsrad
      421 qgrsratgga glglaivrav vvahggsvdv rsspgrtefr lllpseg
//
LOCUS       WP_357646433             269 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646433
VERSION     WP_357646433.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 269)
  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..269
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..269
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28531
     Region          13..267
                     /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 mtaattltrg grstlararv gklirhaigv avfllvwelv srtglvewlp pastclarvi
       61 slafdpeylt dlsstllaav iglplailva vpvglllgtv pvveemtrai veflrpipsv
      121 aliplalflf qpdinakval ivyaaswpil intlygvrdv dplaaetlrs fsfgsaaivw
      181 rvslpsaapf iftgvrlaas itlilaisve yvvggaggig afliqastal ddqamidvia
      241 vlvwsgiigl ivntlllrae rrlfkwrna
//
LOCUS       WP_357646410             177 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646410
VERSION     WP_357646410.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 177)
  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 177)
  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..177
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..177
                     /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=19359
     Region          <58..159
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpdetpdetp getlgdrdsd rdpaqkadgd gdldvnafat aienfnrfyi rlpvleklsf
       61 ttlsvldtla trgtpmrltd ltkteqvsqp gitqlvtrle rdglverrpd psdrravlvh
      121 iteagrqigr srhddrtrhl vpliaqltpe qrqaitdalp gltrlaelgq asaagqa
//
LOCUS       WP_357646434             258 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646434
VERSION     WP_357646434.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 258)
  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..258
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..258
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28134
     Region          2..251
                     /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 miktlvkrlw lvpvvlvawe litravddpf mprptvivsr myemwfsgpl iltdeavdnf
       61 vpsiirlvgs wsvavalgva lgvaigrtaw lsdyidplve faravpppvm fpvflvlftm
      121 gtqvqvativ fgiiwpilln sidgarnvdr lqietatvfg vpaslrlvri ilpaaspkif
      181 aglrlsvsla lilmivselk gatdgigyll asasdrsdmp alwggvvvlg vlgyvlntlf
      241 lmverrmltw hrgarrta
//
LOCUS       WP_357646440             192 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GTP-binding protein [unclassified Nonomuraea].
ACCESSION   WP_357646440
VERSION     WP_357646440.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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=20738
     Region          1..186
                     /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 mdfagsspgl tstkivvagg fgvgkttfvg avseilpltt eavmtdasag vddvsltpnk
       61 ttttvamdfg rvsldrdlil ylfgtpgqhr fwfmwddlvr gaigavvlvd trrladsfpa
      121 idyfeeaklp fvigingwdg nfqhqqeeir ealslnphtp ivrldarvrd svkgtlitlv
      181 ehaltrhsht pa
//
LOCUS       WP_357646461             192 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646461
VERSION     WP_357646461.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=20569
     Region          1..188
                     /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 mdfagssglt stkivvaggf gvgkttfvga vseimpltte ammtdasagi ddlahtpgkt
       61 tttvamdfgr vsldrdlily lfgtpgqhrf wfmwddlvrg aigavvlvds rrladsfpai
      121 dyfeeaglpf vvglngwdgq fahvesevre altlsphipi vrtdarhrea vkdslitlve
      181 halnaraayg sr
//
LOCUS       WP_357646481             192 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646481
VERSION     WP_357646481.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=20638
     Region          1..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 mdfagsspgl tstkivvagg fgvgkttfvg avseilpltt eavmtdasag iddlgmtpnk
       61 qtttvamdfg rvsldrdlil ylfgtpgqhr fwfmwddlvr gaigavvlld trrladsfpa
      121 idyfeeaklp fvvgvngwdg qfqhsedevr ealalsshvp ivrtdarnre svkgtlislv
      181 ehvvrlraap vs
//
LOCUS       WP_357646576             322 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357646576
VERSION     WP_357646576.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=34831
     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 mattsarlls llsllqarrd wpggllaerl nvsprtvrrd vdrlrelgyp irafkgpdgg
       61 yrldagarlp pllfddeqav aiavalqvaa lsgadiqega aralytmrqv mpsrlrhrid
      121 alqvtavgqp ttrpdppvdg tvltaigaav hahevlrfdy astsdasdvp prrvephhlv
      181 twkgrwylva wdldrgdwrt frcdrvsprt ptgprfsprq lpvgdvaayv tarfrgstdt
      241 sawpclgevv lglpaavvat ytrdglveel gpdrcklvqg swswvglaaa lgrfdadiev
      301 igpaglkaaf aglarryaea ag
//
LOCUS       WP_357646582             208 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357646582
VERSION     WP_357646582.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 208)
  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..208
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..208
                     /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=22880
     Region          1..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrrsgaarta lldaaerlfa esgvaevsdr rvaeaagntn hsavryyfgg regllkalma
       61 rhvhdvakqr egmpppedsv lgdirglvep smrvldqlpr pswrarfldh vlhnpttlpl
      121 mreaqdttpq avelreslam rlrhldpevv agrallitri vstttaevea raerngedpr
      181 wpevgdflvd aitgmlsapi srprraeg
//
LOCUS       WP_357646650             234 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646650
VERSION     WP_357646650.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..234
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25659
     Region          15..223
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 meiraatvlp arrepielht adgqtlvgel alpldrppla tlvtfhplpt hggfmdshvf
       61 kkaanrlpal adlavlrfnt rgtssergts sgtfdggege rfdvaaaley aeyhdlphvw
      121 avgwsfgtel tlkwardplv egaillsppl hratdedlda wtefgrplva lvpefddylr
      181 pdearrrfar vpqaevigvd gakhlwvgep yvrivldqiv rrvnpaaapl pvea
//
LOCUS       WP_357646659             389 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646659
VERSION     WP_357646659.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 389)
  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 389)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 389)
  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..389
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..389
                     /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=41611
     Region          151..386
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdairrarri slcvlnvviv mmwigialat vaslasgtvs wlrivpamia livftwlflr
       61 itravlerry ltrevvaaga lavlaaalgg adpfgwgfal lawvsvasig irvwaavgla
      121 vgtavvgtgl gvvtlfmgqp llsilvpydd gavfalgliy aimcallpps nrfwawiytl
      181 avqahegrea htrlavaeer lrfardlhdl vghqlsaiav ktelavrlsa adtvaakaem
      241 vavntltrta lrelrqavrg yreldlsael nsvkgvleaa gvrcelrlpy reppggvapv
      301 fayavreavt nvlkhstasf ceitlrftee eaelsvrndg vvrhqvsdlg sgltgmgerl
      361 adiggkvtar ptgdgefllr avvslplrg
//
LOCUS       WP_357646705             539 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646705
VERSION     WP_357646705.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 539)
  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 539)
  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..539
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..539
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59296
     Region          22..274
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
     Region          <261..519
                     /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 mrvrgndyrm leppetytpt lrvsvivpay gsqdkldlal aglarqtypa glievivvdn
       61 gsspplrlpa erpegtrliv chdpgragar naglaeatgd vihwldsdvv ltpgsieahm
      121 rwhhaapyla vtsyirftda plpselpddl ekafepaeph awivdliert ngltdntqrp
      181 fslhvggats vnarlvavag tmddelilgq dtemgyrlyq agavfvpepk arayhlgptm
      241 rmrdqrpidr vsyafvadri payrwlrshp srqwkvpyva vvvdgtagye qvratvdall
      301 agtmldlsiv vvgpwdslgr erraplkdpd ldlvlvhghy lhegrvrlav sgevdpgvpy
      361 vlrlpagwvp gedslarlld larseglglv nvllheskdg vvaarleras sfararivvr
      421 pdeelddavd dvagvawveg etygfaeeaa ellgrrsayr arlkaeadaa rlakeaerlr
      481 aqvtkwrdea grwrksavel rrdvstlrrq laaanraqqs mkvllattvk ralgkrlrg
//
LOCUS       WP_357646723             436 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646723
VERSION     WP_357646723.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 436)
  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 436)
  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..436
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..436
                     /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=46843
     Region          124..>249
                     /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 mtdledklsr vlsgaahrap qapaglvatv ktrhrrrrar taavraaaav vlvaggvgta
       61 vsalgasaep hpavsatgea kpsadkippp iekvwpqavh kipaklpdgr ayypqlllde
      121 htllvmtgvg dgkrqflwsy dlgtgrprqi aeipptkgsa ifadgvaagg gnivwwasyk
      181 eagsprvari wtvpaaggrp rpvtdvplgn vmkqghingl avtgsdvvfa yekggvyrvp
      241 lsggspqpvk gaerhhilqw pwvgihrgka ifrellnvet gerrdavvka deevrcgvdr
      301 cagvavrykt vkverprdrs gkeikcgtrr cpdtvqtrti lrsfvrdrdg sqehelpsnf
      361 qsgddagler ffkvdlprsg dqgvltlyda dtgrsadlgi rpdargtmai pdggldrlmt
      421 ypiknemyvl dlaaik
//
LOCUS       WP_357646727             439 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora parva].
ACCESSION   WP_357646727
VERSION     WP_357646727.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=47348
     Region          18..381
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mpvvrqpldr lgadpgrrrl lsallgapll asgglagcsd gaatstqdgp velsvfwwgd
       61 anraalteka lqlystrnpr vtfrvtwqga dgyydrlatq agggnvpdli qiddamltey
      121 trrqvildlt drhldlrglp eglirygtve grtmavaagq thavvvfnrd llrelqvpep
      181 ragmswadyi swatevtevs drrvagtmdg sgdyralwlw lraqggefyr gnqlgfgade
      241 liawfelwqr arraratpsa alveqadsge parqlvvsga taasfawshq lpelqrltes
      301 elgivgfpgp pgaqwarasm ywaafrgtrh pdtvadvinf ltnngevgav lgherglnas
      361 savrryaegs itdaaqrraa afgtsiadll gpapapppkg hakvrtllvt aaerirvkrd
      421 gtreatarfl sqaiaalav
//
LOCUS       WP_357646765             146 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357646765
VERSION     WP_357646765.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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..146
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..146
                     /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=14778
     Region          3..146
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mfvsarsdya lramlavaaa gggdgdgdra gelvkaasla evqgiplsfl qgilldlrra
       61 gllhshrgad ggyaltrppe eitvgdvlra vggslttvrg lpaeradyhg vaagltdvwl
      121 avhgaiatvv dsttlanllt haptks
//
LOCUS       WP_357646819             350 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357646819
VERSION     WP_357646819.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..350
                     /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=37988
     Region          1..327
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtdepllrvr gltkhfpvrq glratglvra vdgldfdvrp getlglvges gcgktttgrm
       61 lvrlleptsg siefagrdit hagrrelrpl rqelqiifqd pyaslnprht vgrivamplq
      121 vngikppggi karvqellel vglnpehynr yphefsggqr qrigiarala lrpklivade
      181 pvsaldvsiq aqvvnllrdl qrelglafvf iahdlavirh fcqrvavmyl griveigdre
      241 diyerpqhpy trallsaipd vtqlgpagri rltgdvptpl dppsgcrfrt rcwkaqdica
      301 teepalvprd ggrqatachf pegesastgp agaaavgagt aaqvdeevss
//
LOCUS       WP_357646843             951 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357646843
VERSION     WP_357646843.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 951)
  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 951)
  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 951)
  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 951)
  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..951
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..951
                     /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=102742
     Region          6..242
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          107..951
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(828..829,831,855,864..865,868..869,871..872,895,
                     904..905,908..909,912)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          853..889
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          894..928
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 madaifgvlg pvrarhatgr hirlsgrqra vlatvllnvn ttvsrdrlia avwddpppsa
       61 vanlqtyvaq lrralqpear lhtsgagylf eaapdeldll lfedevrrar vesdpasaar
      121 rlehalalwr grpaedaslg nvmtprltel eerladvrad wadlrlqlgm hdevigalrv
      181 fvaeqplrer awqqlmlala rsgrraeale tyrqarealv telgiepgpe lrllqaavls
      241 gapsanrpeq rgaicqlpad iadfvgrsee ltaiatllrp eitpaalpiv tvtgppgvgk
      301 stlavraahl lredfpdgql ylrlsgaspv pqepgallae vlralrvegd sipdtvaera
      361 alyrslladk avlvvlddaa dglqvapllp gtprcavlvt srgplialpg avavslgvpp
      421 erearelles vaggsrvrde pdaarailha cgrlplavri agarlaarpa wslkdlaarl
      481 avtgapldel alggqnvrah fvasyevlsa parrafrllg laglesaadw svaalmgvpr
      541 reaesavetl alaglvtane vdesgqpryr mhdllrafar eraeaeespa graaallgfv
      601 eeclarlraa aleypppmrp smdtvpppve sarvdggwqr awlhaerktl adavalaepv
      661 taaelaqrla pflvahgffa eaigllenva ertgdthttm lirlvradil tdrrrtalae
      721 pelrllidyf egagdrhava yalatlaice lisgryesal tlvtrslplf eaygdtngli
      781 salvttsgih ldraeydlai atcrrglela adprfadfai rfrrvlgiah felgevetai
      841 ghyeasieas relgwgtger malrrlgqay selgryelaa ttldrcaamf aragdghgqg
      901 mtfyargevs lkqgrpdeal hyfqlcldlv eepiwraraa emverlrhdp a
//
LOCUS       WP_357646846             418 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646846
VERSION     WP_357646846.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..418
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..418
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44401
     Region          70..398
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mthttepkpt atprrpllrr glaaaaglat ltasawltli pgaladatpt paptptpapt
       61 atpiatpylp aptgphrvgt aslylkdssr pdpwvpevka relmvslwyp tearsgqrap
      121 ymtpkeseln lkgskitgvp sdilsktrtg slvgaapagg khslplvvls pgftrsrssl
      181 tglaedlasr gyvvagidht yenyattfpd grvatcaace ldtaenigqk vvenrpadis
      241 fvldqltgph pkwkggalid tsriamagas vggasaagam lkdsriragi nldgnmfvpv
      301 pdsglarpfm fmgqpahqpg gqdttwdrdw knltgwkrwl vlegavhpsf tdldmlarqi
      361 gvnlgstltg trsvdltrky vaaffdlhlr gkrqplldkh strypevafc spptttcq
//
LOCUS       WP_357646915             229 aa            linear   BCT 28-DEC-2024
DEFINITION  PIG-L deacetylase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357646915
VERSION     WP_357646915.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..229
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25402
     Region          6..222
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mrrfdrvlvi sphaddevlg cggliaaqve agaevhvlyl avdgmrhygl dgatsyrqrl
       61 deieavratl gfsyeiaygd mdlterldtl prrelvdlfe ralnerrpdl lllpsfadyd
      121 qdhlavfgag faaarpiaqq fgkwlvptvl lyemskiqwa aepmprstaf cdisahlark
      181 lealrgyksq hrpsphirse esvtalatlr gaeigvthae afgvlrevl
//
LOCUS       WP_357646939             271 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357646939
VERSION     WP_357646939.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 271)
  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 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 271)
  AUTHORS   Rosinski,J.A. 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 271)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..271
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..271
                     /product="helix-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=27653
     Region          100..270
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <210..270
                     /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 mrtvlvcvrt plaaqhltsa aarlglsaiv rtavsdpevm lrlaerpadv vladtaltrp
       61 dsagfvrrvl arapqaavll lgteeseaaa atisagargl iqnvdhdlts avakallllt
      121 apgrasrqrs tdpardaaav ggsgrsgpap rgsgepgwta taadgpagla svpvqrgdde
      181 aeagtgepaa qtdpgrpvpn arpsrasigl terelqvllg maegksnaei grelfvsedt
      241 vktharrlfr klgardraha vaagfraglv a
//
LOCUS       WP_357647004             136 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647004
VERSION     WP_357647004.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..136
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..136
                     /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=14574
     Region          <12..120
                     /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 mragepvrgd qlghrladhy ragrlflagd aahvhspagg qgmntgiqda lnlagkltav
       61 lrdgapetvl deyeaerrpv aeevvafthk mtkiatvgns plrvlrntal raldwipavh
      121 htmamnlsel atadrh
//
LOCUS       WP_357647050             332 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647050
VERSION     WP_357647050.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=36182
     Region          6..332
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtrlprlrig ivgagimgrg haevlsahpe vkitavarra lehaqdatvy pgyrellasg
       61 tvdavsittp dhlhadvmva aaeagvhilv ekpftttved adrsvaairr agviamclfn
      121 hrwvpayaqa kqqmeligep vvgyarkddt ihvptemigw adqttcawfl sshdidlltw
      181 lyddqvaevy atarhgrlrg lgidtpdamq iqarfsrgav atfesawiyp ntfptmvdsy
      241 vtvvgesgvi qldrqkeniq lateksytyp rnmlqrvvhg vpagayrdai hhfvdcartg
      301 aeplisvess rhvtavlaaa hesartgspv kl
//
LOCUS       WP_357647115             431 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora parva].
ACCESSION   WP_357647115
VERSION     WP_357647115.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 431)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..431
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46108
     Region          49..420
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mgvggahalt sgerdvldal ratvavrlqv svvggaegmg dvdllisnal deyarealhr
       61 gqpplsemae hrirqalrns fvgagglqpl lddeaietin ingcdnvqvq yrdgqrarva
      121 avansdteli eqlrdmgarl gaherrfdpd apelamqlpg garlhamqvi sdrvavsirr
      181 hpmvkvsldd lvgmgeltpt madlftglvl arrnivisgg paagkttflr alasaiptqe
      241 rliviedsre lsldpqvhpd mvsmqarqan iegvgefsld qcvraalrlt pdrvilgevr
      301 gaevvqmaka msigvdgsma tvhassssqa llrmttyame ppasyprsaa tsllgeavhi
      361 vvhldrtpng lrvvssvrei vgtdgdqims nevyrpgpgr qavpatrlrd etmdrlvdvg
      421 ldpaaldrdg w
//
LOCUS       WP_357647010             116 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647010
VERSION     WP_357647010.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=12760
     Region          15..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mprshgrraa lvhpdadaid vldvlhalad ptrmtivrtl radperacgt fpvdvapstl
       61 thhfrvlrda gvirqredgn rrwttlrled ldarfpalld tivtaydrqa nssaag
//
LOCUS       WP_357647138             532 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora parva].
ACCESSION   WP_357647138
VERSION     WP_357647138.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 532)
  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 532)
  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 532)
  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 532)
  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 532)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..532
                     /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=54962
     Region          83..503
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mppsepgrsg gtdsalaaqi dllvrpgrrs lglhspaqwp hqeaasepgr iskgivtspt
       61 qlrqvtqsas sssarslpll lsvnqeggrl naldwprvaq lpgnlalgaa gdeglaesag
      121 laigeqlrav gltwnlapvc dtaswpalta vgtrafgsdp eqvgvlaaaf vrglqaagva
      181 atakhfpglg gvsadphhva pvvdrldpga lqpfraavda qvacvmvgsh tvlaldnrpa
      241 lasprvlgvl rdelgfdgvt vsenlsirav hqplggltra avaavaagvd ivmldsevsr
      301 rskqpaeraa avrrraevvq almdavehgv idrqrvgaav vrvqalhrry gltpgsarpt
      361 wqqanasawr aadrvadrsv tvvrgthllp ldvppgkvla lvrvpdaghr radsarhtpd
      421 ylpallaahh rvlqvpvgas vptagpvvvy sydtrtttag lstaareatr ltelgravvq
      481 valgdvddla gspapvlvaa fsphrpsvaa vvqillgdgr srgvlpvcgs pw
//
LOCUS       WP_357647213             262 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647213
VERSION     WP_357647213.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 262)
  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..262
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..262
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28605
     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 msdfttehrl ghreggpavv fmsalfaggw iwehpyryla gagvpvlrth eaicaldrrv
       61 agsierlgda llhacdeagv edlvlcansl gglvaidlag rrperikgiv vsgapgltpd
      121 pdvglsfdrr asvrpfgddf gvrmvsalfh gtepyftraq mdevgtmlrq peamvsmars
      181 lkatrryqvk paldkvrcps lyvwgrhdrm tpvdpwlell agypendvvv veesghipmi
      241 erpaeynavl epfvarcakv aa
//
LOCUS       WP_357647184            2988 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647184
VERSION     WP_357647184.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12828924
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2988
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..2988
                     /product="type I polyketide synthase"
                     /calculated_mol_wt=308861
     Region          1..1406
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1080..2508
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          2309..2782
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(2539..2540,2542,2563..2566,2589..2592,2616..2618,
                     2639..2640,2659..2660,2674,2701..2702)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(2640,2661,2674,2678)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          <2796..2971
                     /region_name="PRK06060"
                     /note="p-hydroxybenzoic acid--AMP ligase FadD22"
                     /db_xref="CDD:180374"
     Region          2805..2890
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 mepvavvgvs crlpqaadpg rfwqllrdgv davtavpegr wpdgsaaayr rggflsdvdr
       61 fdaaffgisp neaaamdpqq rlvlelawea lesarvvpsr lsgsgagvfl gaisndyaal
      121 qdrvganglg rhaytganra iianrvsyfl glrgpsltld agqsssllav qmaceslrrg
      181 esglalaggv nlnllaetta aignfgalsp dgrcyvfddr angyvrgegg alvvlkplsa
      241 aladgdpirc vilggavnnd gggdgltvps rraqeevirl aceragvepg dvqyvelhgt
      301 gtkvgdpiea aalgaaygpd hadgaspllv gsvktnighl egaagiaglv kvvlslerre
      361 lppslnfeta npdipldelg levvrdtrpw pradrplvag vssfgmggtn chlvlgeapr
      421 seygvrsase dtpwvlsars aralsaqaer ltahvgpsag shagpsagsh agpqvgshad
      481 shvgphtgte pgavalallr sralfehrav llgtdrqagl aalaagrlde svitgsvvag
      541 sgaggrrvfv fpgqgsqwpe mardllagsp vfaahaeaca galepfvdya lldvlrgapg
      601 apgfdrvdvv qpalwavmvs laglwrsygv epemvighsq geiaaatvvg alsmpdaarv
      661 valrsraiag iagrggmmsi aapldvvesa irslagdvsi aayngprsvv vsgrlealdd
      721 lgrrltddgy rtriipvdya shsaeveeir devlaalapv rpvsagtlfv stltgepidt
      781 aeldagywyr slrqpvrfaq atrraldhqg glfvecsphp vlgagieeta eeadreaaii
      841 gtlrrgeggp arfrrslaea ytrgaevdwt gpdpvagael velptyafqr erhwpslpad
      901 arrsaaqtlp gdarrsaaqp vpaggggaaa agdasghgpg svggglsrre vrelvltvla
      961 gllgyedaag vepgrtfkdl glesataedl rhrlrsatgl rlptsllfdh ptpdlliahl
     1021 rtllddggsa assaahqsdl atatpaddap adnlvgdpdg dlvggsggdp addadaiaiv
     1081 amgcrypgga dspeelwrlv ssgtdaitef panrgwdlda lfaagpdrsg tsdtryggfl
     1141 hdadrfdaaf fgispreata mdpqqrllme vsweaverag ldpaglrgsa tgvfvgamas
     1201 dygprlhqat gtvdghlltg talsvasgri ayalglrgpa itadtacsss lvaiflamqa
     1261 lrrgecslal aggatvmssp gifvefsrqs glapdgrcka faagadgtgw gegagmllle
     1321 rlsdarrlgh pvlavirgga vnqdgasngl tapngqaqqe virqaladag laaaevdave
     1381 ahgtgtrlgd pieaesiiaa ygadrdperp vwlgslksni ghtqaaagvg gvikmvmamr
     1441 hgrlprtlha deptphvdws ggavrlltep velpddrptr aavssfgisg tnahlileqa
     1501 fepayavset ahagpetthv epetahavse tthvgpesay agsetveapl vwavsaksaa
     1561 aleahaarlr dyatdapqdd lpaaghllar rarfahravv vaadrdelva glaalaages
     1621 haavtsgval pdvrpvfvfp gqgsqwtgma vdllessemf rewmsrcdaa lapytgwsvv
     1681 galragelvg seviqpalfa vmvslaevwr slgvdpaavv ghsqgeiaaa cvagaltldd
     1741 aakvvvlrsq alvklsgtgg mlavalpaee vrlepwadrl wvavrsgpas tvvageldal
     1801 defaaacget vrvrkigidy ashtphvdvl rdellaslae vaprptdvaf cssmaadfve
     1861 ptgldagywf rslrnpvhfe qaigafagdg tplfieasph pvltghiqdt laaagapgga
     1921 tgtlrrddgg rrrlllavaq ayvsgadvdw aavdraaatr aglvpdpprh hvdlptypfe
     1981 htrywinesp raggprhpml davvpvagdd gylltgrlsr galpwladha vdggvllpgt
     2041 afvelaleaa atagcdeied ltleaplplp etgavqvqla vggadaegrr dltvygrtad
     2101 ddearwtrha sgtltvapvv aaaaaaagva atatatatat atgagagaag erlaawppad
     2161 gveidldday erlaergyey gpafqglraa wrvdgdayve valpepvrad aglftlhpal
     2221 ldaalhllvl esaeeagall lpfawsgvrv salgaevlrv riaagegdrv sldihdgagd
     2281 riagvdaltl rpvprhgavt rgpsdaasyt ldwidlavsa mdpaeqrwav vgydefadei
     2341 gaavdapryy dlasltemta gempstvlvp ylpeadaddv pygvrdgiyq aldlvqgwvg
     2401 derfagcrmv fvtkgvfrpg gadvagvvag pvwglvrsaq aehpgrfvlv dvdaatvdwg
     2461 lvaaavaage sqlvareglv areglvaqeg lvaqeglvaq gglvsqegkv lvprlirrta
     2521 dapelfdagt gtvlvtggtg slgalvahrl verhgakdll lasrrgpeas gdlvarleal
     2581 garvtvaacd vsdrdslagl lsgvpaerpl aavvhaagvl ddatveglsa qrldsvfapk
     2641 sdaawylhel vpevplvtfs svagvignsg qanyaaanvf ldvlaahrrg lglpsvsvaw
     2701 glwetadsgm tgalsaadta rlarsgiapl taeqgleffd saitapaelv vaarwdtagl
     2761 raraeagelp pvlrglvrtp rrtaaaanat saptragaag maerlakmae aearvhladm
     2821 vrshvaavla hgsagnvdmd rafnelgfds ltavelrnrl nsdtglrlpa tlvfdhptvt
     2881 alaeylfrtl apaapspedt lrgaverves mltsahgdae airgklvaia qsavtrfgag
     2941 lmtrfgagsn gaaekidsas deeifalidd qtmtsplrss lerpdhgd
//
LOCUS       WP_357647227             399 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora parva].
ACCESSION   WP_357647227
VERSION     WP_357647227.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..399
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43254
     Region          1..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 mstplplddi rvielgqlla gpfcgqllgd fgaevikved pgqgdpmrqw grekpygksl
       61 wwpvvarnkk svtanlrtgr gqdlvrqlia radvlienfr pgtlerwgla perlweinpg
      121 livtrvtgfg qtgpyssrag ygsigeamgg iryvtgdpdr pparagvslg dslaatfacl
      181 gtlvalhqrg rtgrgqvvds aiyeavlamm eslipeyqia gyqrertgtt lpnvspsnvy
      241 ptadgemvli aanqdtvfrr laeamgqael atdekyathg argrwmeqld glvatwsstl
      301 taddllerlh aqgvpagrif rardmledph fasreaivrl thpglgefam hnvvpklsds
      361 pgrvrhvgpe lgehnediyr dllglgddam aslrsagvi
//
LOCUS       WP_357647252             950 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357647252
VERSION     WP_357647252.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 950)
  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 950)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 950)
  AUTHORS   Rosinski,J.A. 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 950)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..950
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..950
                     /product="helix-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=102366
     Region          <6..897
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          884..936
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mamderregl tsledllset vagkgriamv tgaiatgkse llyafaeqaf ehgalpltat
       61 gslaesglpl gvlaqllhna pltqeqraat mnllhegmss qlssdpqaea idhmdvqivd
      121 alcaallels ercplviavd dvhhadrasq lclaylarrv kfaqvmlvfs apdhsahvqt
      181 lfhtevlrqp hcrpirlthl saeevalwvt vragaeaagr faadcyalsg gnrllvtalv
      241 edfqatgapg arygegtvac lrradrrltv varalavlge pasigrllgg gesaviklls
      301 sgdlpggrqa ggetatdrll eegeaavgka iqaltgagvl ehghfrhpaa raavladlda
      361 aeridlhrra aeltyesgap aavvaehllq ashagdpwai svleeaarqa lrddgveaai
      421 eylklawrac vderrrarit ttlvraewri npsapathla eltdalhkgy lgggdtvvla
      481 kallwhghve dakdvlahln elaeldqetv aelaaarpwf rslypsflah lpevsgeqas
      541 saassvvvgr rmesagvlag vltqgpreet vataerilrg srldemtmdt vetallalty
      601 tdrpgkaapw cdafieeaas rrapsrqarl sairaeiglr rgdlaaaayd aqraleiipa
      661 tswgvavggp lgslllagaa mgrldehvrq fnqpvpeaml etrfglqylh gkgrfnlmag
      721 qphqalrdfq lcgelmrrwe ldvpgfiawr tdaaealirl gdheearrli deqlarcgqq
      781 srrvqgiamr llaavsetrh rpmllrksad llqsggdrye laralfdlta ayhangeyrr
      841 agmfgrrarl laaecqaepl tlalnrggkg drtarnspgv tgilsdaerr vaalaaegyt
      901 nreisaklfi tvstveqhlt riyrklnvtr rtelpasltg eesmraqvfs
//
LOCUS       WP_357647263            1134 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora parva].
ACCESSION   WP_357647263
VERSION     WP_357647263.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1134)
  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 1134)
  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 1134)
  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 1134)
  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..1134
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..1134
                     /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=120449
     Region          82..>1133
                     /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 miapdlaawa plaarvlggt peqvsaaaat esfvalggts lqaialvslg qrelradvds
       61 arllsalpla qalagavdfv dtappvvarr paerellpgq rsmlaahlle rdapyhlmft
      121 veadapldpa rvrwalrelt trhealrthf vrdprqariv lsapyeprll hqtlpdddav
      181 ravhdlygpa aarllrpftq ppvvfvltrt grrdlltmlv hhtvsdgwsv glfarefaef
      241 yagdgpaeaa pspdwvgtrl aaqessgald aaltrvtarl dgapwtvtlp tdlppvaead
      301 grgarlrfhl detateattg larecgvtvt svalaawalt vsrragvddl vlgvpaagrf
      361 eagmdrlvgl ctrvvpvrca atddstvref vrgiadalaa avadadvpfe tvvsalgagt
      421 dpgrnplaql gfaahhelvp delvvvdrtw rvheshcgga vfdallylqs wsdrprfale
      481 yatalltaad agelvesfqa avrelaavpd atvrdvttls agqrarlrel gsggtydtad
      541 dvwhrfaaya esagersalv dahtgltlty relhdaaveq srllhghgvr agdavllevp
      601 rsaaeavavl gvlrlgahyv avdrhataew rthlaatvaa rtrlgvgepw pgvvdcplvd
      661 prtpvgadpv eaaptdpart ayvsftsgst gvpkgvvvph ravlrladdp gmfaerpgmr
      721 mlrlsplafd astlellvpl atgdtvvvfp pedptprgla dvlstagvth awltsgvfhl
      781 vadhrpdafa glrqlftggg vvspphvrqv lracrglrlt ngygptentt ftttysveha
      841 datpdplpig gpvhgtdlsv vdasgrlvpp gavgellagg tgladgylgd ptrtdasfvr
      901 hdgvrryctg dlvrwgtdgq lrflgrndrq vkiaghrvep vdverrlraq pgvrdavvfp
      961 tgdpgsgvrl caalkpdpdg ldvaavrrav epdlapyarp qqwvtvaefp ldrngkvdlr
     1021 algalaqpaa ppetsaappd pparvpaqrs aslaefeelv tgawvealgt ddfdvdeaff
     1081 dvggeslrla ivrrllqerl agrtipltdl yrfptvqtla rhlhaqtera gaps
//
LOCUS       WP_357647272             367 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647272
VERSION     WP_357647272.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 367)
  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 367)
  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 367)
  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 367)
  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..367
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..367
                     /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=37500
     Region          3..342
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mssgpvgvai vgagvisdny lrhlssfpdv rvlgvadldt araataareh gvplsgtvet
       61 vlavpeveiv vnltipaaha avalaalrag khvysekpla ldmdeaakvt aeaanlnllv
      121 gnapdtflga glqsaakala agligtpvgv taafqslgpe swhpnpefly qrgagplfdl
      181 gpyyltalva llgpaariaa strrarghrv igsgpkagta favevpthvn alidfagsas
      241 atatfsfdsp irrqtieiig tegalslpdp ntfegpllar gphdaewrel pvtgttagrg
      301 lgvldmarsl ragtphrasg alaqhvleim taigdagedg earrlqttsp tppplpdgwd
      361 phaatlt
//
LOCUS       WP_357647286             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647286
VERSION     WP_357647286.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=33922
     Region          37..313
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtssrpstat spepptaaag rrararkgkg grggnpypyl fyvpagvvyt vvflvptima
       61 fyfsmtrwtl fdstfvglen ftdffaeqnl rigfqntliy avttsalkvv lgmalgvllt
      121 sriklrgflr svvffpvlvs tvavgitfsv llkpdtglvn kalalvgisg pdwlgdanta
      181 llsvalvdvw kgvglatviy iagmmsiprd yyqavavdgg gawhrfrfvt lplswpatns
      241 viilsfiggl rsfdliwtmt rggpgftsdv iasiiykqyq agffglstag nvilfivvta
      301 lvvpltrfls arevaa
//
LOCUS       WP_357647313             234 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357647313
VERSION     WP_357647313.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=24850
     Region          5..234
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtvlrpvrag nafeetverl lqaiklgvva pgrklppere lavqlgisrv tlreairalq
       61 dagyldvrrg ryggafvtya ppppesgdlr rvvadmgtad ltdaltfrma vecgaaavla
      121 aatltddqrs llrdrlaaln kagigdyrrl dtafhlsiae ltgsallata cadarlrvsd
      181 llnaipmlqv nldhsarqhe aivaailagd pegarravae hlegtaallr afls
//
LOCUS       WP_357647360             378 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647360
VERSION     WP_357647360.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..378
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..378
                     /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=39618
     Region          1..>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 mrvlvagagi sglaaargli gaghevvvle qaseprvqgg aitlwhngta ilgdlgvdle
       61 gtgqrltrlc lrtargrrvl efdlaalaer fgsaarvipr gslitllesg lpqgtvrfga
      121 gvaelradgd girvrtqsgq eyggdvlvga dgvhsrvrtl vlgdgpaalt gvatwqgltp
      181 apfdpgsatt mmvgrrgdfg fmgagdglmq wffdvpwspg appedkplem lrrrfagwgs
      241 pvervlaslg dgdaevfpht rhkvprrwgd grcvllgdaa hgmppvmaqg tnqaledvat
      301 lvdcldavpd pasvvgvysa rrrrqaalas tiathslavs gprtlpqgey llrmngltpp
      361 rlatrgfgal lrtlsnri
//
LOCUS       WP_357647386             759 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647386
VERSION     WP_357647386.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 759)
  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..759
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..759
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81715
     Region          24..758
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          581..609
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          652..682
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          687..721
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mssasehlta qltqikelsg lsvralarqa glsssslsry mtgrlvppwe avvalcrvva
       61 rdprplravw veaskagaap sprrndlpad ladftgrete aalveellrt tgavaidgma
      121 gvgktslsvh vahrlapsfp dgglyldlrg ftpgqeplep saalgrllaa lgvahppadt
      181 veraalwrse lsrrralvll dnavdaehvr pllpgagksa vlvtsrnrlv sldgvppvsl
      241 ealppadaas lfgraagvdl teeeavaqvl recgglplal rmagarlrhr pgwtvavlae
      301 rlrdsasrfd svfgmslqql davqrrvfrl lgvlpgadfd apvagaladm tpdrvnavle
      361 elvdahliqe pspgryrlhd lirryaadia aeeepqadaa vhrvlshyla qastydrtlp
      421 lphrkeavpg dpakamawfd teyanliacf daavrlgade vvtelppamr vwffrhrgtd
      481 dqirlleaaa aaaerlgrdr qrasllvdlg faraaagrlt ealaayelae qsdvgddela
      541 galalrtgfv rrdlgdfeaa qarfrlartl fektghrpgr sqalaldgwv tlhlgrhsea
      601 aelaraslal adgparitgl vtlgvalapd npaeslqalh ealrlaeaqh nkawchnylg
      661 valrvmgsld ealehhrqaf elleplaeaq meidflpaya etcraagryd ealalherti
      721 elarklgrph neklareayq vivggvpard dgtdshsrs
//
LOCUS       WP_357647421             131 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357647421
VERSION     WP_357647421.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=13860
     Region          36..113
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(40..41,43,46,49..50,53..54,60,90,112..113,115..117)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(41..42,46..48,64..66,75..78,80..81,84..85,87..88,
                     94..96,101..103)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(64,67,112)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mskqaapftl vdvtadavcc pslaqhrvpa etatllapaf kalgdpvrlq lmsmiasadn
       61 gevcvcdltp afdltgptis hhlrtlreag lvdaerrgtw vyyrarptil rqlaalltve
      121 pvtaaqpaah s
//
LOCUS       WP_357647423             165 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora parva].
ACCESSION   WP_357647423
VERSION     WP_357647423.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 165)
  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 165)
  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..165
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..165
                     /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=17921
     Region          3..160
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mtditvrplr dedaervlai yqagldagna sfeitaptws afdaaklpdh rfvavdaddr
       61 vlgwiavapt sardvyagvv ehsvyvdpaa qgrgiarlll drliisteaa giwtiqsgvf
      121 penaasltlh eragfrvigv rerigrhhgs wrdvvllerr spvvt
//
LOCUS       WP_357647434             496 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF1593 domain-containing protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647434
VERSION     WP_357647434.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10541311
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..496
                     /product="DUF1593 domain-containing protein"
                     /calculated_mol_wt=54968
     Region          23..338
                     /region_name="DUF1593"
                     /note="Protein of unknown function (DUF1593); pfam07632"
                     /db_xref="CDD:462219"
     Region          <340..463
                     /region_name="myxo_dep_M36"
                     /note="myxosortase-dependent M36 family metallopeptidase;
                     NF038112"
                     /db_xref="CDD:468355"
ORIGIN      
        1 mtvatlpaaa eagdfpqegn lprtvvttdm eqddyaslir yllytnevdt egiiyssgkf
       61 hwsgdgkgtp fflpdreytt pqtswrwtgt rtiqdqalra yaevypnlrr hdphyptpge
      121 llskvkigni efedemakdt egsdlirdll ldhdsrplyl qawggtntia ralksiedrf
      181 astkqwprvk aavskkavil asgfqddtya qyiapvwpdi rvenmaagya twgyncergq
      241 gnvrglpadr ayfsgawikq niqigplgsl yrswldgqsm pgdqldifgd peraatgwck
      301 plapydflse gdnvafnpll ktgiqqpenp llggwggrat qttttpnlwt mvsaekdetg
      361 advrnyttlr wagaaqndfa armrwtltpr yrdgnhpptv dihgndtvra rpgsvvtltg
      421 latdpdqdpv tlrwsqyree gsypgtvtit drgrgraavt vpadatpgqt isiilqgtdd
      481 gtfpltrydr vfirvv
//
LOCUS       WP_357647440             317 aa            linear   BCT 28-DEC-2024
DEFINITION  transketolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647440
VERSION     WP_357647440.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..317
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32985
     Region          12..314
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mtalaeqapt fdcrvdfgee laalarader ivavcndsvg ssnlvkfree fpdrlinvgi
       61 aeqdlvgvsa glanagfipf vsaaapfltg raleqikadv aysdrhvvlc gqspgmayge
      121 lgpthhsied lswmravpgl rivvpadpsq trdavrwaaa sglpsyirip rfkvpavtpa
      181 gapfeagrat rlaegddltv iaigtmvsra ldaaallrae gltarvvnmt fvepldvaev
      241 vaaaeqtgai itaeegllsg glgaavakvv aerhpvpvrm lgvptfaptg stsflldhfg
      301 lnaegivkaa realgrv
//
LOCUS       WP_357647464             194 aa            linear   BCT 28-DEC-2024
DEFINITION  response regulator transcription factor [Micromonospora parva].
ACCESSION   WP_357647464
VERSION     WP_357647464.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 194)
  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 11450879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..194
                     /product="response regulator transcription factor"
                     /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=20430
     Region          1..194
                     /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 mirtllaldg alvlgalsfv laaeddirvv aevdrgdavs aavhtqrpdv vvadldvveg
       61 idpgrlggcp llllahphra rrlrgmlcps ravgilrnda aphrvidgir rlarrepvld
      121 adlvvaalrs dgpltsrete vlrltaagap vaevaaslgl trgtvrnhla riarkvgart
      181 rveavrmage agwi
//
LOCUS       WP_357647490             136 aa            linear   BCT 28-DEC-2024
DEFINITION  bleomycin resistance protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647490
VERSION     WP_357647490.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 136)
  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..136
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..136
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=15790
     Region          5..129
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(5..7,36,43..45,47,72..77,82..83,86,127)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(28..29,36,47,49..50,74,109,116,118,122..124,126)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 msrlvpelic sdiqaslafy rllgfkirye rpqerfayle rggadlmleq plsrdrlypr
       61 aeldypygrg inltvevddv dqihttllaa gyemwlplee rwyertvdav gvrqfavqdp
      121 dgyllrisqh lgtrpr
//
LOCUS       WP_357647542             128 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: response regulator transcription factor [unclassified
            Nonomuraea].
ACCESSION   WP_357647542
VERSION     WP_357647542.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 128)
  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 128)
  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 128)
  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..128
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..128
                     /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=13961
     Region          7..>123
                     /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 mgevlgrvlv vdddevirql iavnlslegf evatatdgqd clervldvmp dvitldvmmp
       61 fldgwvtaqr lrtdeatshi kvvlitaraq dddkrrgrgi gvdayltkpf dpaelievvr
      121 dlaagsrv
//
LOCUS       WP_357647534             454 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647534
VERSION     WP_357647534.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 454)
  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 454)
  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..454
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..454
                     /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=50803
     Region          153..444
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqthdvviws irnrkgrakp yqlrwkvgte pkskafltka ladsfradll kaakrgepfd
       61 tltglpasmt ktekaalswy dfcrkyvrmr wkgaaaktre aivdsltvat falladeaak
      121 lskkeiraam qwallprqed evapphlsya vrllqkgtvn vsdladpivv rnvceeltlt
      181 rdgkraaadt tarrrrglnt aleyaidlge ldenslkrvk qkkvardntv drrcvvnpvq
      241 arellvslsy vgswhrargr rlvaffatly faglrpaeai glresdcllp qegwglltle
      301 vtrpssgkqw tdsgtvhdqr glkqreerev rpvpippelv rilrdhlref gmapdgrlfr
      361 nerggvlgas tysraweear rfaltpqqva splagkpydl rhaalstwln agvdatvvae
      421 ragnsvevll kryakcldgr dseinlriea alet
//
LOCUS       WP_357647545             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357647545
VERSION     WP_357647545.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..212
                     /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=22576
     Region          6..>104
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtglrerkka etraalgwaa ihltaergyd nvrvediaea vgvsprtfnn yfsskaeaia
       61 srhldrslrt aaalrerpad eplwvaltqa aleqftrgpe veampspdha qwvagvrtml
      121 aepalqgerl ratalaeael aaavaertat dlatdmyprl vaaaasaava vamqhyldsa
      181 dpptpiehli tdaftqvaag lpapshraap sh
//
LOCUS       WP_357647559             514 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357647559
VERSION     WP_357647559.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 514)
  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..514
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..514
                     /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=54006
     Region          2..514
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mafdviisgg hvldgtgapp yradvaitgd rvaavgrldg aeaasvidas grfvvpgfid
       61 chahgdaavf dpavqlaalr qgvttfvlgq dglsfapgsa gtvayaeryf aavngpltgg
      121 vrsgdglsva ellqgydrav alntayliph gtirydvmgp ssgaptrdel trllahverg
      181 ledgavglss gleylpgrya saaelaalca plaglpyvth mraygeradi gmsevveiaq
      241 rsgtavhish lhgpadvllp lveealtagm dltfdsypyl rgntilamvv lppevpgaep
      301 dralemlssg eldawwpela qtwprltish apglewaegl gmveaaerag laphefcrrl
      361 lietrleagc vtarpdegpe geesvrrvlr hpshtggsdg iyvgghphpr gfgafarflg
      421 rhvrelgdwt wgqaavhlss hparrfgltd rgllrrgfaa dmvvfdpatv tdlatyeapr
      481 tpargvddvl vsgvpvlang altgetpgra lrgr
//
LOCUS       WP_357647606             400 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647606
VERSION     WP_357647606.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 400)
  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 400)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 400)
  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..400
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40783
     Region          <174..391
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnrrgwagfa adaglgvgfa aalafqayri adswggaywq fgcgagavvc glalvrrrgr
       61 lwaaiaglav aaaavvvarl aglpsepgpa malglsvlvg savrvlpaww agavaagggv
      121 vvaggllaaf vfstgsvvav lngaawlaal aaglgprlla arrraiaerv rrnerlelar
      181 elhdvvadhi tsivlqaqag qllarkqpht aegsladiea agsdalaatr rvvgllrdgd
      241 dndeysavsg ptagaagasa ampgaeqlge lvkrfdghgl avrlslpdgd sgwppevart
      301 lyrvvqeslt nisrhapnar hvtvsvardr davrvqvidd appgaahyph rggygligmr
      361 ervealggtl svgprrgagw svlatlpast padapgskrr
//
LOCUS       WP_357647633             206 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent F420 reductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647633
VERSION     WP_357647633.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..206
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21051
     Region          4..196
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mttiailgsg avaraltcrl rdaghelivg srapredsav pvvglreaag vaevvinalp
       61 gpvsvevltg laaelagkvl vdvanatesd argfaaally pggslaeeiq ralpevrvvk
      121 tlntmhesim aqpdrpthpp taflsgndad akkavgglla dlgwaaewvi dlggvetarv
      181 peafmlmvgd lvralgpvpf gmaiah
//
LOCUS       WP_357647648             287 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Micromonospora
            parva].
ACCESSION   WP_357647648
VERSION     WP_357647648.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..287
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..287
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30103
     Region          60..130
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mrrqwlsvgl aalcvavgvp ahawaatsgt taqrtgttav rpvvdmeatv laaqidprrp
       61 dntltpgaks svlaveqalq aqgllnaqwv dgyfgtvtis ayaayqrslg ytglaanglp
      121 gttsltklgq nrytvantig pgakvsrdgy vvnartqaml aqaqrllgyp lvldqgsynp
      181 ggdptsagth dgggvvdiav tgmtaarrta varalrqvgf aawvrnpdqg nwpwhihaaa
      241 indtdlssqa qhqvgdyylg lnglanqgpd dgpqvpirtw eqyqrgq
//
LOCUS       WP_357647690             368 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357647690
VERSION     WP_357647690.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 368)
  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..368
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..368
                     /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=39309
     Region          9..360
                     /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 mrtrvtdmfg ielpifafsh crdvvaavsr aggmgvlgal yftpeeleme lkwiddhvdg
       61 hpygvdvvmp asyegadfap eelvgrlqtm vpaghrqfve nllaahgvpp lssdadagkv
      121 llgwtdvtar pqvetalrhp iallanalgp ppadvvelah shgvkvaala stprhalkqv
      181 evgvdvvvaq gteagghtge istmvlipqv vdavdvpvla aggigngrqm aagmalgaeg
      241 vwtgslwltv eeadtpemak rrileatsrd tvrsrswtgk parllknewt dawesqespg
      301 tlpmplqfml vsdalrrigr sdaaelatfp agqiigimnq vrstrdvmys lmeeyaeate
      361 rlgritgd
//
LOCUS       WP_357647680             298 aa            linear   BCT 28-DEC-2024
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357647680
VERSION     WP_357647680.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 298)
  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 298)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 298)
  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 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..298
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32356
     Region          29..132
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
     Region          171..278
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mpseplvaeh vlefpggyar ttgpvigrfl telrggrivg vrtaegkvlv ppleydpasg
       61 eavteefvev gpagtvtawa wvdeprdghp ldrpfawati kldgadtalv havdagnaka
      121 lrigsrvwpv wrsertghit disyfapevt kivshvrady rlqvggsllt flegvergvf
      181 lggrcpacek vyvpyrvfcp acggpiadql elpdtgtitt yainnlpdpr apevpfvsay
      241 illdgadipm ialvgglpah evrqgmrvra ewvperertk smrnvrwfap tgepdvel
//
LOCUS       WP_357647697             390 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647697
VERSION     WP_357647697.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..390
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..390
                     /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=43154
     Region          4..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 mkeqpagrda aldgiralaa lgvwvlhvgg ntgiiyregm fawmttrlgi avpiffllsg
       61 lllyrpwara viedtpgprp grylwrrlvr vmpaywlvta lalwawssld wtgwvkwlfl
      121 lqnyteqnra pdglyqmwtm piemafylvl pvlawalnvw alhawarggd rpvrllagia
      181 vlpvvslasv vvshvfdqpq lalwlphhli yfaagmamav lsvwikqsev vdalapqllv
      241 lalllyavls telagprtlt lptlsqslwr miletsvavl vvapfalasr hdslrhrvlg
      301 npvtaylgri sysfflwhap vitlyykitg dqpftgdfvk vailtfiasl lvsatsyhlv
      361 eesalrlagr rpapvppppa paeppvvpap
//
LOCUS       WP_357647710             446 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora parva].
ACCESSION   WP_357647710
VERSION     WP_357647710.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=47770
     Region          1..336
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkrrrilatv amlavgtgla acssdeggsd asnctntitk kdlpvvtmwg wypntqlvvd
       61 nfnklnnevq vcwtnvgqgg deydkfqtai sagtgapdvi mveadriptf qiqgalvdik
      121 kygydavkan ysegawkdvs vgdavygvpv dggpmgmiyr kdifdkykit ppktwaeyeq
      181 aaqkvkdagg plfgdfganv pavlmalqiq kgatpftsdp aqpnaigvkl ndqaskdvld
      241 ywgglakkgl vgtqnqftpe yisgvingny atyisaawap gyltgagvgk gqdtgkfava
      301 plpqwdpanp vqvnwggsaf svtkqakkpe laakvaygly adkesltdgw tnqiifplnl
      361 talkdpafvd lkvaffggqq ankevyvpaa dayqgvqyap fgqyyldame kqvsevikgs
      421 itgsqaadrl qedvskyake qgftvq
//
LOCUS       WP_357647714             320 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647714
VERSION     WP_357647714.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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 320)
  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 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   5  (residues 1 to 320)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..320
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..320
                     /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=34608
     Region          243..318
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mahlectped lakvrfglsp msqvvgalnv lcgrsvppgl piwtarvhdr yqrllagnpv
       61 lralsrlhqv tdyapdfycv ppegvdttfe relaavrrmp adrvaadfrl shrerpvdpa
      121 ldvpdaparv adalealwte llapdwprlr allerdivrr agrlavygwl evfgrlgidm
      181 elkeerillg kvsgashrlg gvgvvlipna fgaryvyldp praygltypa hgvaalwerg
      241 spatdglval lgrgraavlt aldspastsq lvaqlsmtlg gvgghlavlr raglvsrtrs
      301 grsvlyrrtp mgdglaqltt
//
LOCUS       WP_357647747             892 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357647747
VERSION     WP_357647747.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 892)
  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 892)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 892)
  AUTHORS   Rosinski,J.A. 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 892)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..892
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..892
                     /product="helix-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=95233
     Region          <4..858
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          831..887
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlkgrqedqa vvdgllenar agrsgalviy gdpgigksal lrsvaeratd lrvlrsvgve
       61 teaelpfaal hqllrpelar aealperqal alkgalglge aagedrflig lgtlsllsei
      121 aedgpllclv ddahwldras adalvfaarr ldaegvvllf aardgfnaqg lperrlgpld
      181 aesaaellte rdphlaeglr srvltessgn plalielprt gdpftpmplp rriqeayatr
      241 iarlpdgaql millaavent gdlgtvlraa erlgigaesl gtaeragflt fadgggltfa
      301 hplmraaavh saafdqrlvv hraladvldd qddrrawhla avalrpdeqv aialeraaer
      361 artrhghaaa aaaleraael ttdpgslarr lteaavaaad aglpdraqal aeraarlved
      421 prsiarlagl rarvafergs vhtahdills gasrvaeldp vaaglmlida grnawqlsdp
      481 rrveeaavrl rrlplrqedg ldtavdavea aaeslghgpa ralpgmrplv ldargiergs
      541 yglrvngafv aglvgefeaq reisaalvee cgalgmtgwl piahvtlaas avylgrfada
      601 kadaseglri ardfgqphrt gylegmlawi aavegddarc aelaarcaeh ftvtgiangv
      661 awsewaqaml dlsrgrhaqa ldrlesalsg pvrhqiqavy faadqveaav raglpdrake
      721 plerlaewag aarldwadav larcrallep gdelfsaalk phgrpleqar telvygewlr
      781 rerrkrdart klraaletfq rlgaapwaer aaaelraage iiaapaafdk laglspqelq
      841 ivrlamtglt nreigarlfv spktvsyhly rafpklgvss rvelarldlg aa
//
LOCUS       WP_357647763             491 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Micromonospora
            parva].
ACCESSION   WP_357647763
VERSION     WP_357647763.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 491)
  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..491
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..491
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=52140
     Region          29..420
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msltelpgtp tpepaptteq pirparrtsp fgalllrlhf yagilvapfl vvaaltglay
       61 ttapqldtil ygdqltvaev gerqlplaeq igaarnahpd gsittvqpgd gdrstkvvfs
      121 lpelgekqht vyidpytaes qgqlttwfgs tpavtwlddl hrhlhlgtvg ehyselaasw
      181 lwvmalggvi lwwrrrgaar aaarhllvpd lstgkgvrrt rgwhattgiw ltvgllflsv
      241 tgltwsryag anfadgldal nartpeists ltagptapae tggghehgaa gaggvvesaa
      301 fdrvlgvard aglsgpveit sakepgsawt vtqvdntwpv nkdriavdpa tdavtarsdf
      361 adwpllakls glgiqahmgi lfglvnqill aalalgllcv ifwgyrmwwq rrptradrra
      421 lagtppargg vrglplwall igvpvsvaig walplfgitv laflvidvvv gavsrrrrpa
      481 atpvspapar r
//
LOCUS       WP_357647835             247 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357647835
VERSION     WP_357647835.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=25591
     Region          1..93
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msvgtdgrgm aelaalladg tragmclall dgrawtagel arragvapst asdhltrlvr
       61 ggllveerqg rhrylrlagp avaqliedla ghapatptpt gslraatata slayartcyd
      121 hlagrlgvlm ydallsvgrl drssglaltp dgwawatglg vpvdvlraar rpvvrdcldw
      181 terrphlaga lgaalcrrft dlgwisrgag ravrltptgr palagalavp ehtldppaap
      241 pptsgra
//
LOCUS       WP_357647868             325 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647868
VERSION     WP_357647868.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=34993
     Region          21..311
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mnieetahvp ggdaardals alraevskav vgqdavvtgl viallcrghv llegvpgvak
       61 tlmvrtlsaa lsldfkrvqf tpdlmpgdvt gsliydakta rfefregpvf tnllladein
      121 rtppktqaal leameerqvs vegdarklpd pfvvcatqnp ieyegtyqlp eaqldrfqlk
      181 ltvplpprdq eimvlerhar gfdprdlsei kpvataqdle agreavskvh vapevlgyiv
      241 dvaratrnsp slqlgvsprg atallaasra wawlsgrayv tpddvkalar palrhriqlr
      301 peaelegats dglldgilas vpvpr
//
LOCUS       WP_357647878             178 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357647878
VERSION     WP_357647878.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 178)
  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 178)
  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 178)
  AUTHORS   Rosinski,J.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..178
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..178
                     /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=19361
     Region          1..77
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          86..174
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(89,102,104,116,119,123,157,159,171)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 migtrirelr sernltvaql aiasgvpsal lrqverdrdd psletlrkia kalelplfsl
       61 fqesdpalva viraearvrv kspsdgityt rvspgrgrle vleghllpgg ssagepwshp
      121 seecvlvlrg rlvvevsgft heletgdscy fdsslphryl ntgteptdfi iaatppsf
//
LOCUS       WP_357647912             402 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            parva].
ACCESSION   WP_357647912
VERSION     WP_357647912.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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 402)
  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..402
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..402
                     /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=40989
     Region          69..344
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mraallaatt savllapvpv gtagasaapt vrcprvpasa asrpprpspp pavpgqrmvg
       61 gaaldttglv vptgvaappk itatswlvad ldsgqvlggc gpheygtpas vqklllaatm
      121 lpkldpkqlv tvteadmdie pgssavglva ggrytvetiw lglllnsgne aanalarlgs
      181 gtdsaagvra mneqahhlga lqthavtpsg ldgrgqftsa ydlaliarac faqptfrrya
      241 lteqtsipaq paqrtkgfei qnenqliyry pgalggktgf tdlarhtyvg aaerggrrlv
      301 vtllgaesap argweqgaal ldwgftlprd aavgrlvepg eltatpsaap salaapgapl
      361 paaasgpars dagwlwsvta lsgatvvalm ggllwrrrrr lp
//
LOCUS       WP_357647996             113 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357647996
VERSION     WP_357647996.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=12477
     Region          13..109
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtthaepsqd asaqlvdvfk alanpvrlqv lqwlrdpehh fpmeqaiadp hevgvcvshi
       61 qaktglaqst vsaymaslqr aglvratrvg kwthyrrdek riaqlvdvlg rsl
//
LOCUS       WP_357647999             275 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357647999
VERSION     WP_357647999.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  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 275)
  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 275)
  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 275)
  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 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   6  (residues 1 to 275)
  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 275)
  AUTHORS   Rosinski,J.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..275
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..275
                     /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=30720
     Region          1..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          108..264
                     /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(109,111,113,122..124,126..127,132,141,148,150,152,
                     154,163,165..166,168,171,177,179..180,209..210,212,214,
                     225,227,229,231,237..241,248..251,253..255,258)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mddafralad psrrrlldrl ndrngqtlre lcdglatsrq avskhlsvle aanlvttvrr
       61 greklhylna apinaiadrw lsrydreraa tladlttale rqamesptfv yttyvstsaq
      121 rlwaaltepa ftrrywggva lvsdwqvgsp vlwqdapdae prdlgqrvlv aepyrrlsys
      181 whgfqpehae hfgwsaeela arlgerrstv tfeiephgdr avrltvihdd fsphsemhra
      241 isgqldgsgg wpellaslkt lvetgepmpe papag
//
LOCUS       WP_357648015             381 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648015
VERSION     WP_357648015.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..381
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..381
                     /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=40794
     Region          18..378
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 miwegafvgi gsvkrperva vigvgvlgas vgwnlsrhga kvvfidagqp gegvtnwsfs
       61 wvnasnktar ksyfdlnvag maayrelart igpdswwhps ghlrwtdgpa aeaklletae
      121 llagwdyqve vytgaevrrr lepaltmpge apvvfypdea wvhgrhlvgr lvgqavasga
      181 ehrfgaavcd igtgtdgsir tvvlsdgsrl dvdtivnaag psashvagli arhlpmrrep
      241 gvvtrigcaq vpvrramhap hieirpdgda smvlhsreid alidtgedpa efgrllhesa
      301 rhvvpeldds rivqtrvanr pipadgypsv gavpsvsgyy eavshsgitl gpvigrllas
      361 eilsgksdem ladfrperfh s
//
LOCUS       WP_357648031             227 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357648031
VERSION     WP_357648031.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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 227)
  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..227
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..227
                     /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=25101
     Region          <15..217
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 msahrkgesd llyrdgrwfl iatcdlpdpr iknpdaflgv dlgivniatt sdgarhsgka
       61 lnavrhrhre lrrrlqakrt ksakrllkqr rrkearfaan tnhviakqiv teaertgqgi
      121 aledlqgird rvrlrkpqrv tlhswsfhql gafvgykaar agiavihvdp afasqqcssc
      181 ghvdrnnrld qacfsctscg faehadvnaa rniaargqtg wavshaa
//
LOCUS       WP_357648071             175 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora parva].
ACCESSION   WP_357648071
VERSION     WP_357648071.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 175)
  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 175)
  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 175)
  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 175)
  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..175
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..175
                     /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=19142
     Region          12..172
                     /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 mrylrsggpa airrprptds defvaaarrs rdlhhpwlaa patpeeydly lrrirrrdsa
       61 gylicdrasg eiagyvnisg ivlgalrggf lgyaaflpys gtghasagia laidhaftsv
      121 glhrleaniq pgnepsrrva rklgfrlegf spdylfidga wrdherwait aptpa
//
LOCUS       WP_357648096             761 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora parva].
ACCESSION   WP_357648096
VERSION     WP_357648096.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 761)
  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 761)
  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 761)
  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..761
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..761
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=76649
     Region          52..>254
                     /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 mdkteillta paaeppaaar pdghsprsrr spawarptla mlllatglly lwglgasgwa
       61 nsfyaaavqa gsvswkally gssdaansit vdktpaslwl malsvrifgl nswamlvpqa
      121 lcgvasvgvl yatvkrwygp aagliagavl avtpvatlmf rfnnpdallv lllvagayat
      181 vraletastr wivlvgvlvg fgfltkmlqa flvvpvfagv yllaaptglw rrvrqvllag
      241 lavvvsagww valvelvpas arpyvggsqg nsileltlgy nglgritgee vgsvggggar
      301 pggggpfsgq tgvlrmfgge iggqvswllp aalvllvvgl llagraprtd rtraglllwg
      361 gwllvtglif slmsgifhay ytvalapaig alvgigvtll wrqhqllptp agvrsgtpaa
      421 aptagtpagd plpasaegaa ggvrgqrwrp laasatlagt lsvtvwwawv llgrspdwhp
      481 wlrttvvvag lvgaalllla srlprrlvpv vlglgaaaal agpvayavqt aatphggsip
      541 sagpfvaggf grggfpggrp pggmelpagg qlpgggqfpg ggqlpadgrd gggqngggqn
      601 gggqngggqn ggqgpgfpgg grnggppggq grstgggmgg lldarepsaa lrellehdsa
      661 dytwvaatig snnasgyqla tgepvmaigg fngsdpsptl aqfqryvadg kihyfigggg
      721 franggssas qeiaawvaqt ftaqtvdgvt vydlgagtea s
//
LOCUS       WP_357648153             142 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            parva].
ACCESSION   WP_357648153
VERSION     WP_357648153.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..142
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15598
     Region          35..131
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msagdlrrrr tnvranvraa pgpcahwnde dadfirevld lvgdkwsvli igtladgpvr
       61 ysdlgdaipg isqrmltltl khlqrtglvt rtsypevppr veyaltdlgr sllstvlala
      121 awsadhhaei rrhqtaydna tt
//
LOCUS       WP_357648182             421 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357648182
VERSION     WP_357648182.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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 421)
  AUTHORS   ter Beek,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..421
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..421
                     /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=44974
     Region          21..346
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mrrrlagiaf lgllaltaaa cgsggsdkqp qaagpvtitm wtraatqaqs erlvkaynss
       61 hknqvkltvi ptdnyqpria aaagakqlpd vfaadvifvp nytsqglfmd itdrvgalpy
      121 kaalapshmk lgtldgklyt lphtldlsvw fwnkdlyaka gldpekgpkt lkefaeqatt
      181 iqqklgkdgk vhgtffggnc ggcyvftfwp svwaagaqvm naegttslnd qpamtevfkt
      241 yhdlyakkvt gptakeeqgp twtgffpkge igvmpmpstt lgtmpagmki gvtpiagpdg
      301 gestfvggds igisstskna daawdflswt vsddaqvevm aknkdvlart dlasnkysae
      361 dprvvlinsl vakgqtpfal rfgqtfndpq gpwlrlarea vfgdaakvpq lnaeitkslq
      421 q
//
LOCUS       WP_357648197             336 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora parva].
ACCESSION   WP_357648197
VERSION     WP_357648197.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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..336
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..336
                     /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=34848
     Region          1..321
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrkcrvglvg aggvaqrhar vlagfddvel vgvtdvapea asalaaqhdg racadvgell
       61 atgldavyvc vppfahgpae eaiieagvpm fvekpvavdl dtaeriadlv arrglrtavg
      121 hhwrylsvld qardlladrp vrmvsgawld kvppvawwsr rdrsggpvve qaahvldlir
      181 vlagevtevt aygngtpppv dgadidsvtt aalrftdgav gtlsaacvlg wkhragleil
      241 adglalalte dglsirdadg erhlpadpea arvavdrafv davrgigddv rvpyaealat
      301 qrlalavads artgttvrla tataptvlas gvtvda
//
LOCUS       WP_357648215             509 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648215
VERSION     WP_357648215.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 509)
  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 509)
  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..509
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..509
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=53822
     Region          78..382
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          350..507
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mkfrplaisv giagllalaa cggpggtkgd salrapassr aaptassgpe lpadakpear
       61 asasaknqsa apeeqkdtsa aqistfaldv dtasytyarr tlqegrwpep gqirpeefvn
      121 sfrqdyaqpr ddgftvhvdg ammpsrnqav lrvglqtras daaarrpanl tfvidvsgsm
      181 aepgrldlvk qslhtlidql apgdqvsivs fsdeatvlas mtplaartel haavdqltva
      241 gstnleaglv tgyeqaakaf rpaatnrvil lsdglanqgs tewrsildrv keyagrqvtl
      301 ltvgvgrnyg dqlmeqladn gdgaavyvst qedadkvfas qlpatielra rdakaqvvfn
      361 psvvegyqli gyenralste efrddtrdgg eigpghsvta lyavrlksga tgqlaqatvr
      421 wqdpdtrnpa etskavdvga ltesvwekap vrlqvdvvaa afavymrdre afgltlptlg
      481 eqarrlagaa edpmvtelag lidkarsvg
//
LOCUS       WP_357648216             151 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine dioxygenase [Micromonospora parva].
ACCESSION   WP_357648216
VERSION     WP_357648216.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 151)
  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 151)
  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 151)
  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 151)
  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..151
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..151
                     /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=16528
     Region          36..126
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
     Site            order(36,38,50,61,63,106,120,122)
                     /site_type="active"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mthhrpepdl ltvaagwadp agwpvalrfd paerwyarla vsdehevwal swlpgqgtdl
       61 hdhggssgaf rvvagvltee tvsagrlrpr llpagagrrf gprhvhqvtn rgadpavsvh
      121 vyrpallrmt ryhlldgrlr vaevaeagrs w
//
LOCUS       WP_357648258             321 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648258
VERSION     WP_357648258.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 321)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..321
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..321
                     /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=34907
     Region          18..319
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 merqtdpppp asladdgtva gprfwhslrf qsraaqvlfl apaviymvaf fgypivknfv
       61 mafqeystst fytgeapwvg fanyaevvss pvfgkamlnt vlftagsiag qfviglalam
      121 ffrrrfplng vlrslillpw lipliasgav wrwildkdng alnrflaaig vasdhpgwlt
      181 stslalvavi lvniwvgipf nltilygglq dipedlyeaa aldgaggwqr fryvtwpllr
      241 pvvsvvlvlg vvytikvldv ilaltgggpa nasqtiatqs yhlsfqqfdf gqgaalgnil
      301 iaislvfaif ylranrravd e
//
LOCUS       WP_357648270             161 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648270
VERSION     WP_357648270.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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..161
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..161
                     /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=17130
     Region          16..154
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msadvprrpt asratdrpgd aspfalglll rqahwraatv msealrpfgi elrhfavliv
       61 lvdrgptvqr dlaaatgsdk agimrvvddl egkglavrks vpgdrrvrav eitpqgvelf
      121 daahvaaepl aerlvadlgs dgseqlrdll trfaypadge a
//
LOCUS       WP_357648307             303 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Micromonospora
            parva].
ACCESSION   WP_357648307
VERSION     WP_357648307.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=32418
     Region          2..241
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilvvggsg ligahvvdvl rerghaattv artaqpgvdh lldvgsasie dlrqvlaghd
       61 gvvyatrtde qrplpkpiyp efrrdnvdpv vrlftaarle gltrgvvmgs yytyfdrlhp
      121 qwrlaerhty ircrleqare graaageglp vavlelpfvf gragdrlpnw agpldrwars
      181 rtplvapvgg saaasarsva evavdaveqa sgadlpvade nlswhdmlar iaaavgrprr
      241 vgrlpagaar aalrlggaaq algrkesgvn pthlgdllla dlfieptsgr pldpalretf
      301 rsa
//
LOCUS       WP_357648315             255 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora parva].
ACCESSION   WP_357648315
VERSION     WP_357648315.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 255)
  AUTHORS   Rosinski,J.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..255
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..255
                     /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=28048
     Region          5..>63
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          92..253
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mivyavgell rqwrkrrgls qldlaiaadv sarhvslvet gkstpsadmi lrladqlhvp
       61 lrdrnqllla agfapryaqr plddialsga ldavrrvlra hepypalvfd rrwnivltns
      121 avdpffahva pdllrppvnl irlgldprgl aslvvnladv ravfrsrvar qlaaapdael
      181 aalyqellsp qpeepaserv dadvvipmil rvgdrelrlf stittfgtpt ditieeiave
      241 syypadaqsa ayftt
//
LOCUS       WP_357648403             464 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648403
VERSION     WP_357648403.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=49573
     Region          9..>259
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtravvlggg fagtlagavl arhvddvivi endhypadpr arrglpqshh shvlvaggar
       61 alrellpgtl eelfargaqh rrlpgdalil aaagwfrrld tgayliscsr glldqvvrqr
      121 algavstwpg tralglvgda srvtgvsvsr egaapetiea dlvvdatgrr skaprwlaei
      181 gvaeieeltv ssglaystrv fqapaelage ipavmlhprp argrpgqgat lfpiedgrwi
      241 vtltgtrgge ppadergfad farslrdpiv adlmaaatpl ggirpyrdts nrrrfferar
      301 lpagfvavgd avvavnpvhs hgmsvaalsm lrldrelarr gldpaaapel qaamtaeaes
      361 swrmalaqda gpagrreata fereiltrrt rallsspela aeffraqtll paraakdasa
      421 vvraltgepd pllttreavm qypvlhawwn altrvrggre pslr
//
LOCUS       WP_357648324             214 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648324
VERSION     WP_357648324.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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 214)
  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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..214
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23067
     Region          4..210
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mlalfdldnt lidrldafkr waaefaadrg lgaqdvawmi eldadgsipm stffthvrer
       61 fglaesadsl wqgyrdrlph lvtcrpavle sldilrlsgw rvgivtngmt dnqsgkihhs
      121 glvdrvdgwa isdaegvrkp spelfeiaah rcgtsladgg wmvgddvekd vaggrgaglr
      181 tiwidrgvsp gqspgadhev sdvleaiall dvgc
//
LOCUS       WP_357648409             404 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648409
VERSION     WP_357648409.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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 404)
  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..404
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..404
                     /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=44735
     Region          21..400
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(58,65,93..94,101,105,112,234..235,238,242..243,246,
                     279,284..285,288..289,291,314,341..343,346..347,349..351,
                     355)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(65,87,89,92,94..95,178..179,187,233..234,237..238,
                     242,285,288..290,390)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 msatgleqaf dptgaqhrrd phplfhrmre rapvyrhapa ngrvswyltr yadvqralhh
       61 pdvgrqldrl pgelaafhrr wendplamvr rnmfnldppd htrlrrlmap afgprtvaal
      121 errihqvvge lvddlaaagd gadlievlal plpilivadl vgfpigdrgr lrgwsddmlr
      181 srdaalvrrt gvafvayvne qlderrahpg pdllsqlvrs teithaelvs svfqlllagd
      241 ettvnligng vlellrhpgq lerlrarpql idsaveevlr fngpvghsrp lfamadveig
      301 psviprgdiv vpvllaanrd pavfhrpdvf digrtpnrhl gfghgihfcl gaalarlqar
      361 aaigalvrrf pglalavdpa elewtpdlfl hgvrrlplll eksp
//
LOCUS       WP_357648425             368 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Micromonospora parva].
ACCESSION   WP_357648425
VERSION     WP_357648425.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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..368
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..368
                     /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=36472
     Region          10..366
                     /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 mvearvaqlt gvyavsalgr gadaqlagvl agvpafgpvr rfdtaarrvt vaatlpevgt
       61 ltdelaaaid eacraagldr egrtgcalll avhggpatga apavlagrla arcglsghtr
      121 vytsacvsas tavadaaaqi trgdvervvv aagylvepdq falfdagral avdgavrpfs
      181 agrrglllgd gvaavvless sgrrrggadp vatvagwgra gdafhpcqpe pggtglarav
      241 ggalrragla pqavgyvnan atgtaqsdaa eaaalrralg ghatevpvss tksvhghale
      301 asgllelvvt alalrhgelp vnagwqgpdd scplnvvthr pqrttathal tlnaafggan
      361 tallvgvg
//
LOCUS       WP_357648428             255 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357648428
VERSION     WP_357648428.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 255)
  AUTHORS   Rosinski,J.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..255
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..255
                     /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=28406
     Region          1..>60
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          91..251
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdqpigellr dwrhrrgltq ldlalqtdvs arhvsfvetg rtipsrsmvl rlaeqldvpl
       61 rgrnrlllaa gyapiyperp lddpdlgkay ealrrilrgh epypamaldh rwnlllanda
      121 mnvflddvdp alleppvnmm rlglhpdgfa prvrnlaqvr gfllprlarq varagdpels
      181 alyeelltyg ddgqaplpdp adialpvrit hrgdelcffs tittfgaafd itlegvavea
      241 yfpaddettr lvgdr
//
LOCUS       WP_357648490             698 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648490
VERSION     WP_357648490.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 698)
  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..698
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..698
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=76494
     Region          4..685
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 miqaergrtv rarprvegss fvgrrhelaa arrglsqarl ltltgtggvg ktrlaqrvae
       61 tlqgtykdgv evvelatlea ghllepvvag alglreagpd pmtalvdhls nkrmllvldn
      121 cehllddcar fvtrllrsap rvrilatsrq tlsvygeqvl qisslsvpgs ghplshiarh
      181 dsvrlfvera asvapgfsld asnaatvarl aqrlegipla ielaavqlra lpleqlarel
      241 derfevlatg spaalprhqt lratmdwsfr lcspaerrlw trlsmfpggv dldgaeavcs
      301 gdgispaevi dlmtglvdks ilvcerwaag lryrmlesir aygcerlspa ekrvlcrryi
      361 dhyrdlvdrh rideivpdqa erylllrqel pnvrvalelc lseprlarvg letasglgsf
      421 wllagalteg rywleralel trtpdsarat alwldsmlal rqgdlaaavp rlrechflar
      481 qpgnedvlpf airtsgvaaf stgdtqrgla lleeslalfr aagdvhgvvl nlyyataygs
      541 tenperavrl geellalsea hhmmvsrgya qlalgiavwn lgdypradal vraaaeltde
      601 indrwclmqc levlawiaga rgeheraarm lgaahslwqa adasptrlwy hakwhercva
      661 qardtlgnra faaifrtgar lgvegvftcd vptcaakd
//
LOCUS       WP_357648564             167 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648564
VERSION     WP_357648564.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 167)
  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..167
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..167
                     /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=18204
     Region          2..160
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 maaaegdhta wdqlesrfgs rmwavaracg lnetdaadav qgawlrllen lhtirepsgv
       61 gawlatttrr ealliirkep pgfpsfdvvh dpdpatavle adgrhllwks vsamhepcrt
      121 llqlvatdmg sqqvamrlgm pvgtvgptri rcleklrtll slqetvq
//
LOCUS       WP_357648587             242 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357648587
VERSION     WP_357648587.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 242)
  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 242)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=26689
     Region          1..>223
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnrtdrlyal vedlraispr crsarelakr fevsartier ditalqesgv piyahpgrkg
       61 gyaidkkmsl pplnftpaea vaiavalsra gdqpfgrqar salrkvvaam pgregelare
      121 larrvrmvtp aaepgaeirp lggegisrai eealqrrrll ridyadakga ltsrdvepgv
      181 flggrggfwy lvawcrlrdd vrvfrldria sasviaercp drplerfatd ipdmfvhgtv
      241 ld
//
LOCUS       WP_357648664             384 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648664
VERSION     WP_357648664.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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 384)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..384
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..384
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40942
     Region          29..365
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrqtlvaaav lavlaasacs apapprsdav saapagpatl paptgphsvg ttvlylkdts
       61 rpdpwnldae arelkvtlwy ptkqrdgqra pymtpkesel llkgtliasa pydtlsktrt
      121 naienaepag ktlplvvlsp gftkpmstlt slaedlasrg yvvagidhty esyattfpdg
      181 hvaeclacds nsdpgfgagl vqgraadvsf vldqlpsrwd gsdridrsri amvgqsiggs
      241 samatmledr rvragidmdg tayaripksg fsrpfmflgs aqhvsggpap twdrdwkllt
      301 gwkrwivltg tehqsftdtp llsdalgikp lpgvlpaart aeltrtyvaa fldhhlksqr
      361 qplldkpssr ypeakfcpat cahs
//
LOCUS       WP_357648629             429 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357648629
VERSION     WP_357648629.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 429)
  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..429
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..429
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48201
     Region          9..76
                     /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(11,15,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(14,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(21..22,38,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mpdyipnvrl rawrnqeqls raqmaekina tpigvaqgla cdeerirrwe agevrwprte
       61 yrlaltqltg kepeelgfsq grqnesrlie arvipadalr aeadlygtme laqqlqasdv
      121 gtgtlealae avdllcrayp vvpagtlrdr tqkrlaqinh llagrltldq hrellvitgw
      181 ltallgcvhy dlgereeaet arraafemgr qvghgelmgw ahemsawfal vegryedvvt
      241 aartgqavag tssamvqltl qearglarig drreadralt rgaevlgslp mpdhpdhhfv
      301 fdhakwifya atcytwladd draeeharet iqmhtrpdgs snapmrvada hidlgiihar
      361 rgdldaavee gnaafdidrr sltdlvhrag dlhhllrqry rrealavefh erfvmarral
      421 tsrrpelle
//
LOCUS       WP_357648666              93 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648666
VERSION     WP_357648666.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..93
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=9831
     Region          <3..80
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mshtasgeag gfvtvevtsl daatayievi ddgtamafpe vrnadagdcg grglwlvety
       61 tarwgvrdeg yrrrvvwaem stkngtpaca arm
//
LOCUS       WP_357648711             253 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648711
VERSION     WP_357648711.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 253)
  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 253)
  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..253
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..253
                     /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=27163
     Region          9..235
                     /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 mnspavnsle vnrlayaypd gtqalfgvdf tirrgerval lgpngagktt lvmhlngilt
       61 aghgsvsvag tpvrkdtlke irqrvglvfq dpddqlfmpt vrddvafgpa nsgvsgaele
      121 rvvkgalerv gmlevidrpp hhlsfgqrrr vavatvlame peilvldeps snldpaarre
      181 laevlrsldv tvlmvthdlp yalelcersl ilsdgvivad gptrelladt ellashrlel
      241 pygfaipapa ehg
//
LOCUS       WP_357648727             289 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora parva].
ACCESSION   WP_357648727
VERSION     WP_357648727.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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 289)
  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 289)
  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..289
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..289
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30787
     Region          32..256
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 marsrkvtvs tdadgrtagw aetdlapvsa pdptgaaffd vdntmmqgas iywfarglas
       61 rnyvttadla rfawqqlrfr llarehagdm slakeaalaf vegwrvneve hlaeeifdel
      121 mapriwagth qlaqrhldag qrvwlvsaap veigrviaar lgltgaigtv aevldgaytg
      181 rlvgdlmhgp akaeavtqla avegldltrc aaysdsandl pllsvvgrav avnpdgvllr
      241 qarqhgwevr dfrtgrravk iavpstaaag lvagavtagl alqrrrrag
//
LOCUS       WP_357648739             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357648739
VERSION     WP_357648739.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19916
     Region          1..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 mprvglnqqt vvreaarlad evgfsqltla alanrlgval pslykhvrga dalaqklaal
       61 ataelatemt taavgrsggd alramadayr gyahrhpgry patqrvpdpa dpehveager
      121 avgavvavlr gygltgddav datralrsal hgfvtleaag gfglprdvnr syqqliasmd
      181 isfrswpgtg a
//
LOCUS       WP_357648766             434 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora parva].
ACCESSION   WP_357648766
VERSION     WP_357648766.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  AUTHORS   ter Beek,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..434
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..434
                     /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=45759
     Region          25..342
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mavfprrrla avalaattal lvtagcgggd eqgdgpitlt vdvfgqfgye qlyqeymaan
       61 pdvkivergt gtnldeyspk ltqwlaagrg agdvvaieeg llveykanpg nfvnlldhga
      121 adlkgnflew kwnagltadg kqliglgtdv ggiamcyrkd lfekaglpte rdavsklwpt
      181 wpdyiatgek fvaaktgasf ldaatntfnt illqtagntt gysyydtsdk lvvdsnpsvr
      241 qawdttmdii dsglsgkygs wseewvsafk qskfatiacp awmtgviean agtgaqgkwd
      301 iaqvpgnggn wggshlavpk qskhqaeaie lakfltsakg qigafkakgp lpsspqaldd
      361 paitgaknay fsdapvgtif gagakslkpv ymgpknqavr tevenavrtv elgqrspaqg
      421 wtdavtnakk aaak
//
LOCUS       WP_357648790             322 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357648790
VERSION     WP_357648790.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=35421
     Region          19..322
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrlisll lllqsrgsmt aselarelev sertvyrdvl alsaagvpvy adrgraggyr
       61 llggyrtrlt gltrdeaeal flaglpgpag emgladavas aelkvlaalp palrdapara
      121 gqrfhldvpg wfretaapqw lpelaravwt drvvelryrr gdrevtrrvq pyglvlkigi
      181 wylvgrvgen vrtyrvdrvt gvevgdehfd rdegfdlagh wreqagsflr tmlraevavr
      241 lspaglrqlr hlvdapfvyd elvaaasepd gqgwvvarlp vesvpvayhq llglgpevev
      301 ldppelrqlf aasadrlaal yr
//
LOCUS       WP_357648794             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357648794
VERSION     WP_357648794.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31501
     Region          36..295
                     /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 mrgfrwpppp dsgprtwgpg pggprtgrpa lpepetelvt tphgvrlerl vtgtgdpvtv
       61 fahglgngia ttrpfgsgvn grkvffqfrg hgrsdspdgp wdyldlardl raiadlgras
      121 rafgaslgag alcrllaesp erfdrlvffl pavldeprgp aareritdll eavesgdasa
      181 vadivtlelp pavrntpagw aylrqrldql lrdgladgla tltdqtplrr igdlaavtap
      241 alvigcagdd lhpvevaerl aaalpqatlh vydrpgvlws eradlreris gflne
//
LOCUS       WP_357648917             109 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357648917
VERSION     WP_357648917.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 109)
  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..109
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..109
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11564
     Region          40..>96
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mspgrnwrev kaeahrlypd ladpqrqaaa daqldayvag hhlkelrksv gktqaevaaa
       61 lgisqarisq iengdldsme letirayaaa lgghvdvtis vgphsvrva
//
LOCUS       WP_357648948             147 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357648948
VERSION     WP_357648948.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 147)
  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 147)
  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..147
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..147
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15440
     Region          45..137
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mtglwvalat lalgsvigvv rlrrdgrvrd taqaddrlvt adlgadlger atlvqfstaf
       61 cqpcratrrv ladvsglvpg vahveidaes rldlvrrldi mrtptvlild sagnivkkas
      121 gqprkadvla alagavshvs sqnadem
//
LOCUS       WP_357648989            1136 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357648989
VERSION     WP_357648989.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1136)
  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 1136)
  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 1136)
  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 1136)
  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..1136
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..1136
                     /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=120458
     Region          6..248
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          135..1103
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mdgdarlrvt llgafqasrg dadlpvpgar sqglivrlal aggraveqgv lvdaiwaedp
       61 pvgaahalqa lvsrlrrtlg sagdvtqvag gyrlnvdaad vdalrfeqla aagrdrlrag
      121 dpnaaaavlg eavtlwgdrp gaeptvvaav apavatwlah asveavadla daelslgrad
      181 aaaarltall aehpvheraa allmdalaaq grqadalaly ervreslada lgtdpgdalh
      241 erhlrllrae rpapaadaar tgpnnlpmpq trpsnlpapq trpsnlpapl tsfigrdgdl
      301 aridtllaag rlvtvlgpgg agktrlavea arrhcheyrd gawmidlasv tepakvgaav
      361 lagiglrgga lfearrrveg galfearsrv esgalsearr rvegsdlveg sdldvlvdql
      421 ggreslllvd ncehlidava hlvaavlsrc aglrvlatsr eplavdgeal vplgplalpg
      481 pndgveqarr aasvrlfter aaavrpgfev dettlpevrr vvrsldgmpl alelaaarlr
      541 tlslpeladg lsdrfrlltt gsrtalprhr tlraviawsw qllseqertv aervsilpgg
      601 vtpasatavc agtavqaaei pellaglvdr sllqlapdpg ryrmletlre ygtdrlaetd
      661 hldtardlaa dhfaklmaqn dprlrgpgql aalrvisaey dntlaalrrr cetgdasgai
      721 tlalnltwyw qmldrypdaa ywlgealavp gggeptpgrd cayaiylihr adtrlgptte
      781 evaddqarlr eladrllayp elpgpcgalt avtlaflqee tavakiarla dgddvwlagl
      841 agmfraqfae nagefdnvra dvaaalacfr qagdrwgqat vlpmraqlrq yddeldgala
      901 dlreaqslag efgslslsde vflhlrwidl hlrrgdtdat iamlgsarer alraaspels
      961 alvdaweaaf rvrlgdldra rdllddaera lhgdttfpgq haralagnvr aslclelgdl
     1021 agaekmlaka ytaalktrdl pimslgavta aalaeahgrh qesavllgaa srlrgahdrt
     1081 dqqvrelsrr graalgeeaf aaaygkgwel dgkaavtavd parprrelgt ahpdpe
//
LOCUS       WP_357648993             220 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357648993
VERSION     WP_357648993.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 220)
  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 220)
  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..220
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..220
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=23601
     Region          1..205
                     /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 mtitlrpgst vmftgdsvtd cqrlesedgl gfgyplrvag ewglrhpdrp vtwlnsaiag
       61 nkvmdlearw qadvldarpd vvsilvggnd vawhtydpdg yvisaeeyaa gydrllapla
      121 eagadlilie tsllpisgsv evgdvhigee erkewraeld pknqvvrela rkygahllaa
      181 dgmfaelaat tgpeywaadg ahptpaghaa laaawlrlva
//
LOCUS       WP_357648998             257 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora parva].
ACCESSION   WP_357648998
VERSION     WP_357648998.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=26941
     Region          49..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 mrdvaaagas tgprvlprnd prqyddlage wwrpdgafam lhwlaearaa lvppatraga
       61 llvdlgcgag llaphlagkg yrhvgvdltr salvqaaehg vsviqgdata vplpdgcadv
      121 vsagellehv pdwpravaea crllrpggvl vldtlndtal arivavriae rlptvprgih
      181 dprlfvdara lvaecarhgv dlrlqgirpq vvgvlawllr raraagtpga vpagrapriv
      241 ptrstavlyq grgvrkg
//
LOCUS       WP_357649009             195 aa            linear   BCT 28-DEC-2024
DEFINITION  GntR family transcriptional regulator [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649009
VERSION     WP_357649009.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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 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   4  (residues 1 to 195)
  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 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..195
                     /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=21333
     Region          <36..184
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 maliartrds ttaaprvlvq ralptepavr gskslflaea erqglkagrr mlyvglepag
       61 dhvaaclrve pgteivarrk mmtandvpvr iatsyfradl fgdtrlaepe fvqpslqsal
      121 talgyafgha eenltarppt pferetlele pgewivqvlr asystedtpv hvleticaan
      181 rhifpigqvs gydef
//
LOCUS       WP_357649025             433 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357649025
VERSION     WP_357649025.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=45511
     Region          16..337
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mnrlaavaaa vtlvagcssg gaqqsaapss sstqkaqkva ltywnwvpgm dkvvavwnka
       61 hpdiqvtsst qaggddsatk fltaakagnp pdlvqaeyqa lpsfvaaeav adiktaadpv
      121 kaqfgegiwg lvtlgtdavy gipqdsgpml lyyredlfkk ygiavpktwq eyadaaravh
      181 akdpkvylgt fsskdpgsfa glaqqaggqw wsisgeawkv aindepskkl adywgglvke
      241 gvidnmpyft pewnkalndg klltwpsaiw apgplssnap kskgkwaiaq lpqwnagenf
      301 sgfwggsavs vsagsknkea aatfatwlns dpealallvk egavypaatk gadllseppa
      361 yfsnvpdfwk qaagfgagar gftfgpnvnv aynafkdafd kaalnktsfs galqsvqdat
      421 vadmtksgfk laq
//
LOCUS       WP_357649064             217 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora parva].
ACCESSION   WP_357649064
VERSION     WP_357649064.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 217)
  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 217)
  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..217
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..217
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21976
     Region          75..212
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mnrrlalavl plllavtact sgtaddepap rpaaaerpsp frdcatlsta ptaatpgsga
       61 stpaspgsgt tapaagkqtl paltlscftg gapvalgava gpavinvwas wcppcrkelp
      121 afqrlseraa gqlqvvgvns rdsrsgaqsi gedfgvrfpm lvdqgealqr elrrnaiplt
      181 lfvaadgqir hvdatgaldd atlaalvrqh lglavpa
//
LOCUS       WP_357649081             399 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            parva].
ACCESSION   WP_357649081
VERSION     WP_357649081.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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 399)
  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..399
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..399
                     /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=43028
     Region          8..395
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mpyphgglar hanlppgerl rvllveddeg daflvgella etnsmidllv atslrearqr
       61 igdvdcvlld lglpdaqgld glrqllemss gaavcvltgr tdehlgvvav aegaqdylvk
      121 gqvdgvlltr alryaverkr adenarrlre velrqaesar lergllpqpl mttdqvavht
      181 fyrpgrhaal iggdffdvvq thpdrldliv gdvcghgvde aalgvelrva wralvlarvp
      241 ddevlpaleq vlmserrlqe ifatvatirl dldanratvr laghppplll sggrvapvpa
      301 pggrllgvrp rrpiaydlef dtddwsllmy tdgliegrvd agderldvpg lsgllgepan
      361 rsvslpelpa wlvgraeqln ggpladdvam llvsrgggr
//
LOCUS       WP_357649077             254 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357649077
VERSION     WP_357649077.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25798
     Region          4..247
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mserlrnkta lvtgstsnig qaiaeafaae gahvivsgrn rergaqvveg irasggradf
       61 lvadldgsve ssqdladrar etlggridil vnnagiypap gttatdektf dkvygvnvka
      121 pffltaavip amtesgggvi inlgswiarl gvplgalyss tkgametltr awaaefgpmg
      181 vrvnavspgv ilppaadeph pgeimmkgtp aggigtpdai ahavvwlasd eaafvhgtvv
      241 dvdggrtgva viaa
//
LOCUS       WP_357649097             204 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649097
VERSION     WP_357649097.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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 204)
  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 204)
  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..204
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..204
                     /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=22159
     Region          6..185
                     /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 mrlnvpalsg asvrlepltm dhapdlaqaa eedrssyaft mvpradqvkd ylqaqlsrqg
       61 lipfaqirvr dgkavgctgl wdvrtwpgrq dpraveigft wlaasaqgtt inaeakllll
      121 ghafevwgvt rvdlktdarn qrsrraiagl gatfegvlrn wspswapgee glmrdsamfs
      181 viaaewpavk aglqerlaty ggar
//
LOCUS       WP_357649146             468 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357649146
VERSION     WP_357649146.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=48274
     Region          4..417
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mdmmtveqng inavpaaerr gtprdlfwpw aganlslfgv afgvyivglg lgvfpaiitg
       61 vigyalsfgl vglvaiagtr sgvptmtlgr apfgyqgnkl pavlsyvsnv gweivlvtls
      121 aqggaailkr vapgipgtta maacfavaal ltivigvygh alimavqryl tyafivltvv
      181 ymilmapklg tsldttagpg gwvgavifam tllglgwvnc gadysrylpa tskppsvalw
      241 ttaggavppm vllvfgvlla ggdpklaqaa gadpvgalaa alptwfllpy lltaiggfla
      301 gaimdiyssg lsmlalgvpi krhyavlidg almvlggyyl lfvstsflat fqaflaiigv
      361 vmaawvavfl vdmwfrragg rsyderllrp gapalnwsgv tslvvasvvg iglitssdpn
      421 iarvvgflms dqmragtfga anigvvvalv lagvlyfais sltprrsg
//
LOCUS       WP_357649153             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357649153
VERSION     WP_357649153.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30397
     Region          6..>154
                     /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 mqdiqthtld ipgvdlvydv rgplpptgah rallligqpm taegftalap hftdrtvlty
       61 dprglgrsvr tdgrsdhtpq qqaadlhali aaldvgpvdl fassggavta lelvathpgd
      121 vatlvahepp inavlpdata aeraragfye ayqakgsgag maafiamtsw qgeftdayfa
      181 qptpdpamfg mtadddgnrd dpllsrnswa vtdyrpdaaa lttaptrivv avgeesagty
      241 tartamglat llgqeavvfp shhggflgge fgyagkpeef aarlrevlda g
//
LOCUS       WP_357649199             901 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent RNA helicase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649199
VERSION     WP_357649199.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Liu,Y.C. and Cheng,S.C.
  TITLE     Functional roles of DExD/H-box RNA helicases in Pre-mRNA splicing
  JOURNAL   J Biomed Sci 22 (1), 54 (2015)
   PUBMED   26173448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Martin,R., Straub,A.U., Doebele,C. and Bohnsack,M.T.
  TITLE     DExD/H-box RNA helicases in ribosome biogenesis
  JOURNAL   RNA Biol 10 (1), 4-18 (2013)
   PUBMED   22922795
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Linder,P. and Jankowsky,E.
  TITLE     From unwinding to clamping - the DEAD box RNA helicase family
  JOURNAL   Nat Rev Mol Cell Biol 12 (8), 505-516 (2011)
   PUBMED   21779027
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 901)
  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   5  (residues 1 to 901)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
REFERENCE   6  (residues 1 to 901)
  AUTHORS   Fuller-Pace,F.V.
  TITLE     DExD/H box RNA helicases: multifunctional proteins with important
            roles in transcriptional regulation
  JOURNAL   Nucleic Acids Res 34 (15), 4206-4215 (2006)
   PUBMED   16935882
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..901
                     /product="ATP-dependent RNA helicase"
                     /EC_number="3.6.4.13"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0003724 - RNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /GO_process="GO:0008380 - RNA splicing [Evidence IEA]"
                     /calculated_mol_wt=96111
     Region          3..901
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
ORIGIN      
        1 msdglpirhv lpellgvldr tgsavltspp gtgkttvvpl alaetglrvl vaeprrlavr
       61 aaakrmgvsy tirgerhtga nplvevvttg vllqrlqrdq elagvdvvml decherhlda
      121 dtalaflldv rdtlrpdlrl laasatadav pwsrllgdap ivrasgathp veivwtppvr
      181 pvapphglrv dpallshvaq vvrqalaere gdilcflpgt geiarvaall sgtlsgggps
      241 gsglsggvev lqvhgqapar vqdavlspgs arrvvlatsv aessltvpgv rvvvdsglar
      301 eprtdhargl gslttvrvsk asadqragra greapgtvyr cwtaaeherl adharpeial
      361 adltgfalqa acwgdpdasg lalldppppa amtaatrtlh tlgalepvpg ttmpsygsdd
      421 dtdqvtgddt drvtgvdagr vtgggtdqat gdgagqatdg gasqvtgdga grvmwrvtar
      481 grrmalvgvh prlaralldl gpraaevval lsdqlpreag ddlveiwrsa rhgrdgftar
      541 wrqevrrltr stpppdrpap ppgrsapppn rqtalqvqqa aspdrremtd dalaglaval
      601 afpervarrr gggylmasgt qaqlaegsrl geakwlavav adrptgsasa rirqavvide
      661 etarlafpvt tedeiawrtp pgerrgdvsa rvverlgaie lsstplknad vreailyglr
      721 tedvltwtke atalrdrlaf chrelgdpwl pmddlaeiae rwlepelsra rrradlerid
      781 vatalkrlip wsrrleevap ervavpsgsr vrvdysggqp vlavklqelf gwtetpriag
      841 vpllvhllsp agrpvavtad lasfwregyr avraelrgry prhpwpedpl taaptrrtks
      901 r
//
LOCUS       WP_357649250             287 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649250
VERSION     WP_357649250.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 287)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..287
                     /product="phosphotransferase 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=30759
     Region          6..246
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 msdakridge liqrllsqrv tgyeplagfa antvaavtle sgaravfkaa aarevevelw
       61 alqsmsergv pvpeviagap daeipylvtr lvsgepgvas lkaasemgrl lravhslpvk
      121 gagffkeasg sppcagegtw adqvaglpdr lgpvadagil tptlfsrcrd lladgtrwdq
      181 pcvyvhgdfh prhvlsvgsr iegiidwadc gaaspwldla rmdfrepglq ramldayfpa
      241 gipldaplhi anhrllymll alvweyecdg dwlhervpgi esalttt
//
LOCUS       WP_357649298             328 aa            linear   BCT 28-DEC-2024
DEFINITION  UbiA prenyltransferase family protein [Micromonospora parva].
ACCESSION   WP_357649298
VERSION     WP_357649298.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001258
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..328
                     /product="UbiA prenyltransferase family protein"
                     /calculated_mol_wt=34870
     Region          18..298
                     /region_name="UbiA"
                     /note="4-hydroxybenzoate polyprenyltransferase [Coenzyme
                     transport and metabolism]; COG0382"
                     /db_xref="CDD:440151"
ORIGIN      
        1 mtvnqleptv rtwdlvvawa rmwrlhfvpf slsaglvgmt appaganaas ivigllfctl
       61 gygvgvvind wfdreadavn apdrpfvtgl inphiglalt ltlsaalmvv aivvaptlal
      121 wsviaigghl vyswtkripm lgnlvngvdm alftvlgava vrpdagwldi pavtwfqtal
      181 vavtfsgfcl vgyfkdiegd rvagyrtlpv aigtrassri avifpvvavi aagtaavaea
      241 dsasayaeiv cwvlliasal gfaqslvtln rapetrayea lvwfirattl fflslgalhr
      301 ptlflvvgvp mmvyleltlr atqssrqa
//
LOCUS       WP_357649308             392 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora parva].
ACCESSION   WP_357649308
VERSION     WP_357649308.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..392
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..392
                     /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=42565
     Region          5..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 mtqqagrmar qlptlnglrg laavtvffsh ttlfgffade riddwwylal srtgsaalgf
       61 ffilsgfvlt wsapdhepnr rfwrrraari lpnhlvvcav filllilvrg gaplwptlan
      121 lalvqswipn efifngvnpp swslsceiff yasfpwvlag irrlnaawlw slaggivaam
      181 lvapafslaf lpaeptytya daafpqfwfv qqfplirmld fvlgiviaql vmrglwirls
      241 lpgaalvtla fygvsevvpl lysvvaamvi plallvaaaa radveghrsp lrgrvtgwlg
      301 dtsfafyllh ilvlygaanm apngfgvaaa lavmngaylv tlglasllhv gverpmmrrf
      361 akprkpaaap aapatptaep lpvatgdgtr vt
//
LOCUS       WP_357649339             303 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649339
VERSION     WP_357649339.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 303)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..303
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..303
                     /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=33107
     Region          3..299
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mlrrsaprte itvkrregrs aylfllpwfa glllltggpi laslflsftd fdllttpswv
       61 gldnyarimd dphfgnavri tmiyvvasvp lsggfallva vllnrpmrgv gvyraayylp
      121 sllggsvava ilwrqifgpd glvndllsaf givgpswist peyaiytlva lhiwqfgspm
      181 liflaglkqi paelydaaav dgagkvraff qitlpmlspi iffnlvlqtv nafkaftpaf
      241 ilsggtggpa dstlfytlyi yqegfgnfrm gyasalawil llvtaaftal afrssrywvh
      301 yad
//
LOCUS       WP_357649316             354 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Micromonospora parva].
ACCESSION   WP_357649316
VERSION     WP_357649316.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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..354
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..354
                     /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=37608
     Region          155..338
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mttigelrtv gsslsyapng gtqviqhpga tyikvhfssl rlaegdyvtv ssrdgkesyr
       61 ydrhlnratg sdyttdgqpg fwamsvdgdt avvtlhssrp argsaatidr fwrgydraei
      121 aahnfstqsv cstdarrdvv cyqnshptey argravarll isggglcttw rvgntnrmlt
      181 nkhcfstqsa vsgsemqfny qcatcgganp gagtkvsgat lykvssggss qldytlfsvn
      241 nfaaiqgfgt lylattatsn gtriyipghg dgspkrlsiy edaqnggtct vrnanyntwn
      301 isyscdtsgg nsgspvlngs hrvialhhlg gcpsnqgaka hliyneiasl idng
//
LOCUS       WP_357649390             305 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357649390
VERSION     WP_357649390.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 305)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..305
                     /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=32933
     Region          10..304
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavrdrtvva satpvrarrs rarlvpllyt apallfyaaf viapwlhslw isfwewngig
       61 vatwagldny reiladpalr lslvhafgli lfysvipicf glvlaalvan vpwkgmpfvr
      121 tviflpqilp lvavgsvwkl ffdddgpfna llravglsdf trawlgdftw aypavgvvgt
      181 wvstglcfll lysgigkidp alyeaarldg agaihefwhv tvpglrrems vaatvtviaa
      241 lasfdvvyvm taggpgestl vpgvaiyrlt ftagqvgtac alavvlsllt cavmfalnrl
      301 trekt
//
LOCUS       WP_357649416             999 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357649416
VERSION     WP_357649416.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 999)
  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 999)
  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 999)
  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 999)
  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..999
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..999
                     /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=108730
     Region          1..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          118..993
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          708..736
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(709,712..713,716..717,719,749,752..753,756..757,
                     759..760,789,792..793,796..797,800)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          741..777
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          788..816
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          828..855
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mefrvlgpve iwsegvrvai ggrqprllla alvleanrpv padrlidliw ehapppsara
       61 tvqtmvsrlr atfrqigasa qlrsergayq lhtdpatvda hrfsalvqqa agssddlttv
      121 elldqaldlw rgeplldvvd dsgrrllcsg lmearwtaae dradallrlg rtrrvvrevs
      181 dqvagqpyrh rlvgqlmtal yldgqtdras evyrnlrtrl hddlglepsr elsrlhqlil
      241 rgdpvlpaer gdalssvphr peelpqdvpg figrtdemth ldqlsggssa ttvwvvsgip
      301 gvgktalavr wahrvraafp dgqmfidlrg fdverppvtp saalgqllgg lgvdsrvvpd
      361 dqdgrvslfr stmagrrill vldnardadq vmplippsgt vlitsrrrlg elvvragars
      421 lllgvlsptd svrllaamlg deavrveaga aarlahlcgh lplalriaaa nlqtsghphi
      481 aglaeeldeg gpltsltvdg adegavtkaf amsyralpta qqrmfrhigl vpggsftahv
      541 aaaiegvapp iatrtlrala sahliehqgg dryrfhdllr qyavdrlvte dddttrhdar
      601 qrllehyrsr adaagrqlip hflrlpgpvp qqsfpdadea lawldaeaan viaainhaad
      661 hghtrfvwql tdalrawfhq rgrraewlsa atralaaaea andltaqasm hlsialahvt
      721 agryeearqh lldglrinah drwpegrtal lnnlsavhqr lgnpraaidc aqrslqlnrq
      781 hrndggeams lanlgfahwq lgalsqadqh irdalacakr sgsryneavl lvdlagirrd
      841 rgdreaaeel ydralvanrd lgyrygeata lsgrallwsm tdraphacad arhavvltqe
      901 igdagteawa reaygrvlla aerpaeaaee hrlaldlarq trfvwceasa lvglaavcla
      961 tgqpdvareh akaalhmane agyrliesrt lgllktlgd
//
LOCUS       WP_357649476             201 aa            linear   BCT 28-DEC-2024
DEFINITION  D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649476
VERSION     WP_357649476.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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 201)
  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 201)
  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..201
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..201
                     /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=21310
     Region          9..175
                     /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 mfeqrrpgav lfdrdgtlik dvpyngdpar vepmqgalea larlrradvp vavvtnqsgv
       61 akglltpdem dqvnarveel lgpfdawaic vhddcdgctc rkpapglvir aaavldvspr
      121 dcvvvgdigr dmeaaraaga rgilvptget rreeiqqaae vaedlsdvad rvlsavdqag
      181 eaarvstgaa vwsplvgwsr w
//
LOCUS       WP_357649505             331 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357649505
VERSION     WP_357649505.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 331)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..331
                     /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=35682
     Region          34..319
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msinatptga dvaadetsga tgqratvptq rggrrkppls enkkaerrlg lllcapaalv
       61 miavtaypii ysvwlslqrf dlrfpdqref iglenyvtvl tnefwwtafg vtmlitvvtv
      121 avelvlgmgl aiimhrtlig rglvrtsali pygivtvvaa fswryawtpg tgylanlfsd
      181 gaplterass laiimlaeiw kttpfmalll maglalvped llkaastdga tawqkftkvm
      241 lpvmkpailv allfrtldaf rvfdnifvlt aggnetssvs mlaynnlirg lnlgigstms
      301 vlifitvaii afvfvklfgt aapgsddger r
//
LOCUS       WP_357649548             322 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357649548
VERSION     WP_357649548.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..322
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..322
                     /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=35298
     Region          33..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavsetvaat ppaatptppa prrrrrgrna aywlyllpga vlfllvigap llgtlylslt
       61 kwsgigdprw vgldnyqqll qddvfwasfr ntvwmlvamv vvptvlglll aavlfdvigr
      121 rfkprtaaal raafylpqvl pvvvagivwg wilrpdgafn slldavglga lrhdwlgdpg
      181 talpavmavm iwvqigypvv vfmaalqrvd pelyeaaevd ganwlhrfra itlpqirpet
      241 fvvaltctia alkvfgpifa ltrggpdnat nvpsyfayyt ffkklqvgyg saismvltli
      301 ivvvagifiw mqarserrdr gf
//
LOCUS       WP_357649607             743 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649607
VERSION     WP_357649607.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 743)
  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 743)
  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 743)
  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..743
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..743
                     /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=81234
     Region          1..727
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mrertqsqlk evlgtgavgt lqnrserdtf agmyasrlar lwaverglvf grldhvdegr
       61 lyigklgitd deqerllidw rapvaqpfyr atpaapmglt rrrhlqtkgr vvigvdddll
      121 dfdtltdedr atlngeaall aalderrtgr mrdivatiqs eqdrviradl ngvlvvqggp
      181 gtgktvvalh raayllythr erlerrgvli lgpnltflry ieqvlpslge tdvllstvge
      241 lypgltatar drpevaavkg dlrmaevier avrdrqrvpr kpvelnlgry tltidrnmle
      301 saknkatrsr rahnqaravf vrsllnalar qaakklgkgl idddeladlr eelrteqpvk
      361 talnrlwpyl tpqrlllgly gsperldyaa saltpqeral lrreggewte sdvplldeaa
      421 ellgeideqv lrasalqaee elaaarqaae hereaelaya revleltgls dvmdaerlae
      481 rqrgegpylt taeraaadra wayghvivde aqelssmawr vimrrvptrs mtivgdiaqt
      541 gsmagarswn qvldpyvagr wrqerltvny rtpvelmeva arvlatidpa leapasvrdt
      601 gaepwsapls alpelvkaev geggkvavvv pdallgelgk visdtvegaa vvsaratrgt
      661 aaldapvavl gvtdakglef dsvivaepdl iasqsprgls dlyvaltrat qrlgvvherp
      721 lsallsgalg glpsrasgpk ngh
//
LOCUS       WP_357649584             415 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357649584
VERSION     WP_357649584.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  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..415
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..415
                     /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=44591
     Region          7..406
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mvdvwgnhqr rpmsaadlvr rlaeppaaer daemlavrla haerlgnmgw aewnlhtgva
       61 twsdhvylif grdredgpir lpdlaahvep gdlgaldqll wsvvqgvepv qaefrirrgg
      121 elrnvrvvle plmapggpeg vhgvvqditg rrraerimse srrqlleare kaaeerhvml
      181 alreailpep vgcldlpctr iavryvpaek tsnlggdwfe aaalpdgrvl laigdvsghg
      241 lpaiahmaql rhaligltmt geppnqllaw lnelvmhrlh ettatavigh ldtasrvftw
      301 sqagnlapil vrdgvagplg qpkgvllgat dqpyglattr lrdgdvlllf tdglverrtr
      361 dideglalat aaacelpgrd ldagldrlla giggpnpedd acllavglgg gqges
//
LOCUS       WP_357649612             411 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357649612
VERSION     WP_357649612.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 411)
  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 411)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 411)
  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..411
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..411
                     /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=43310
     Region          157..407
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnrqpiaval ralwqtvlgp dapverplla rwpgparyaa pvgllaalgl flitltvese
       61 wglpilvall faamtvapll alprrpllaw rltvlallic tfnapadqaw pwtpplalgs
      121 ilvvavvvtr vdrpvlgwvv aistvpvftl vhpnnrvpvl lllgalaivg dlirrnrlsr
      181 ralaaqtels ereqerrgvl eertriarel hdvvahhmsl iavqaetapy rltdvpapaa
      241 aefvaiaasa rdaltdmrrl lgvlrsettg pqtapqpdlt dlgtmvdaar raglsvtlda
      301 eqvdddrvpa pvglaayriv qeglanaarh aagaavrvtv ragasglgvr ventppakag
      361 srpgeagsgh gltgmrerat slggtftagp lpdggyavaa elpydaeggd r
//
LOCUS       WP_357649640             333 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649640
VERSION     WP_357649640.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=36400
     Region          17..313
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msvaedlpde tdaavlrqtl devrrvivgq dhmverlvva llarghclle gvpgvaktla
       61 aatlatvvgg tfariqftpd lvpsdivgtr vfhpsnekfd velgpvfvnf lladeinrap
      121 akvqsallev maerqvtlag vthqlpkpfi vlatqnpies egvyplpevq rdrflfrvrv
      181 phpsaheele ilhrmsvtpp taervldptr lmalqeaaeq isvhqlvady vvrlvmstrs
      241 paeyglgqla etieigvspr atlglvsagr alallrgrdy llpddvrdva vdvmshrlml
      301 tfdaladgvd peqvvrqilh avppplvvwn qnr
//
LOCUS       WP_357649648             409 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649648
VERSION     WP_357649648.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 409)
  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 409)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 409)
  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..409
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..409
                     /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=42657
     Region          154..407
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrwnlprrwa clilggallm pymmagvlts gllqgqsvnm ylpaqlgvfv avlpvvaltg
       61 lflpvralev saaqgllgag vetpprqarr sweerwrtta wytlhlgvgg vasgftlagi
      121 pftvftlavp ffggparllg fdvepgwaal ywpliglavl gavvlvaagg gallarlapv
      181 llgptpgerl aaaerqartl aernrlarel hdsvghalsv vtlqaaaagr vldrdpetar
      241 talaaieqsa raalddldhv lgvlrdgspp peagppqatl adlgdlaatt gadvrpevgd
      301 ltgvpavvsr eayrivqeal tnaikhgqgp vrlavavqdg dlrleitnrp atnggrsagr
      361 sgtepgarsg grgvtgmrer vrllrgdlea gpveggwrvs vrlplrsvs
//
LOCUS       WP_357649657             170 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357649657
VERSION     WP_357649657.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=18121
     Region          26..162
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpaspassrp dptiddeapq rptlgpgpds eltwllhraa qrmhalvgae aerhglslrd
       61 hivlsalhkt gdltqvelgq algmdkttlt aeidrlerme lvarrvnprd rrvrivaitp
      121 kgdaaraava agaeareada vrpipaaeva qlrralylii gsaedpgsci
//
LOCUS       WP_357649720             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora parva].
ACCESSION   WP_357649720
VERSION     WP_357649720.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..265
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27387
     Region          30..251
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpadpravlt rpapepdrtv aygddpnqva dlrlpagagp arplvvvlhg gfwraeydrr
       61 htgplatala aqgypvaqle yrrtgqpggg wpgtltdvlt gvaelpvlaa dalpgrvspt
      121 ppilvghsag ghlalyvaat apatvggvla lapvadlgea yrrdldsgav aallgggpeq
      181 vpdryatadp rmlvpirtra vvvhgsddhq vpaemsrdfv aeasaagsdi slvelpgceh
      241 fglidpesva wpqvlavlrs lhddh
//
LOCUS       WP_357649717             665 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649717
VERSION     WP_357649717.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 665)
  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 665)
  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 665)
  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..665
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..665
                     /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=72088
     Region          2..648
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mstldeerry veqcgaglrr mldaardnvi vgesvagdry saerlgrhlk slakelseep
       61 egppffgrld fggdsvehqg rgyhigrrhi tgehggppvv idwrapvsra fyrasardpm
      121 gvevrrrfgw agteltsfed erlaqgqete srilaaeier prvgpmrdiv atiqpeqddl
      181 vraglaesic vqgapgtgkt avglhraafl lyahrqrler sgvlvlgpnr aflgyisavl
      241 palgevdveq ttlerllgtv avratdspva alvkhdarma evlrkalygr igkpvepvsv
      301 adgsyrwrvg adelrrivdd trreampyai grervrarit elmrrqaesr ghtgnavwtr
      361 kigkaltpfl deiwpavrpe ellcallsdp gpaapiltad eraaitwarp prgyksakws
      421 eadlvlldei agllerprgy ghvivdeaqd lspmqcrava rrsehgsitv lgdlaqgttp
      481 waavswprhl ellgkpeagi valttgfrvp avvvgpanrl laaldvdvpa ttsyrtdgrl
      541 lvtrvtelek gvvaaareal tfegsigvia adadagpltd alwnggldlg erlsvvpasm
      601 akgleydhvv laepaaivea earglnrlyv altravsrld vvhsrplpld vfaaakspes
      661 pdvva
//
LOCUS       WP_357649679             204 aa            linear   BCT 28-DEC-2024
DEFINITION  IMPACT family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649679
VERSION     WP_357649679.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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..204
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..204
                     /product="IMPACT family protein"
                     /calculated_mol_wt=21530
     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 mssyltlsaa iehetearrs rfvcalapar tpaeasafia errhlhpsas hnctayvigd
       61 drkgdddgep ggtagtpmlq altgrgfnev vavvtryfgg tllgagglvr ayssavtetl
      121 dqavpirmip atliqvmvah dqagriendl rasrhpirev sygskvvftv avaddetatf
      181 tdwvatltag raqvtpgnri hvag
//
LOCUS       WP_357649675             192 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649675
VERSION     WP_357649675.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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 192)
  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 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   5  (residues 1 to 192)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..192
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..192
                     /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=21472
     Region          8..81
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mtsdvvldak glralahpvr velvqllrky gpstatrlae rlsvnsgtas yhlrrlaaag
       61 fveedsergn arerwwravh evtrltssdv amqepealma ylrsvaaahs lltqralnel
      121 qtmprpwfda ldishwalrl tpdeaerlre ellsvidryr rdaseetaeg aervslvmhl
      181 lpepagsepd lp
//
LOCUS       WP_357649660             323 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357649660
VERSION     WP_357649660.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 323)
  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 323)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..323
                     /product="helix-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=35365
     Region          1..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrllsll lllqargrmt atdlaaelev svrtvyrdve alsaagvpvy adrgpaggyq
       61 lldgyrtrlt gltaeeassl flaglpgpaa elglsevvas aelkllaalp peprshasrm
      121 rerflmdvpg wyrdaddvph lsevaaavwe qrrlrmtyrr wgqqeverev npyglvlkgg
      181 swyliaapdg qtprtyrvar ilalatlpgg fdrpegfdlg dfwqdysref rermytaeav
      241 ikvapgtdsl laytmgndvi taalaeggep daegwrtltv pieslrharw lllrlgasve
      301 vlgppelral maeaiaelgk iyg
//
LOCUS       WP_357649686             286 aa            linear   BCT 28-DEC-2024
DEFINITION  Fpg/Nei family DNA glycosylase [Micromonospora parva].
ACCESSION   WP_357649686
VERSION     WP_357649686.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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..286
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..286
                     /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=30526
     Region          2..270
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpelpeveal agylrqravg rrvdrleiaa isalktyepa ptevagravv dasrhgkfld
       61 vlfegglhlv vhlaragwlh yreafpsttp lrpgkgpiav rvrlddgsgf dlteagtqkk
      121 laaylvtdla avpgvaklgp dalaadlptf terlrsrrgq vkgvltdqsv lsgvgnaysd
      181 eilhaaklsp faitdrltda qlatlhaatr qvlgdavers lgqraaelkg ekrsglkvha
      241 rtglpcpvcg dtvrevsfad sslqycptcq tggkpladrr lsrlvr
//
LOCUS       WP_357649755             243 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649755
VERSION     WP_357649755.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 243)
  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..243
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..243
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=26068
     Region          10..133
                     /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..25,30,40,43,45,47,49,53,55..56,58,61,
                     67,69..70,83..84,86,88,97,99,101,103,112..120,122..124,
                     127)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mghsfelpqe aevgaspeev waaiatgpgi dswfmgrnev adgvvrtafg qytpestvta
       61 aepparfaha spmaedgrfv ayeflvegre qgsttlrmvt sgflpgddwe aefeamsrgl
      121 emffatlvay lthfrgrtat pvtefgppva dwpraweily galgapghak pgdtvrftpa
      181 glapiegvvy yanaqtlgvl tpdalyrflq glggsmvaah hlfagtgdqg pawnawldhl
      241 fde
//
LOCUS       WP_357649856             883 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357649856
VERSION     WP_357649856.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 883)
  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..883
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..883
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93189
     Region          9..883
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtpdhdwsrs pagrttlpel lrghrraagl tqaelasrag vgvrtvrdle rgrsirpqrt
       61 tvellagala ltgasraafl aaargigadp appdvtsttf avsgnaasaa pagpsvalpp
      121 pvaligrdrd ltelaamlta ergprlvslv glagvgktal atsvahlvas dhpggvagvl
      181 vgegsdgpdv laasmsvlgv arlselvarl agrpallvmd avehapgpva atlhrligal
      241 pslrvlvtgr hpvglpgerv wpvapldvpp peaehsgles wpavalftar laqvrreppt
      301 paelpalaal vrrlgglpla ielmaargrl ldltelldry gdrvldlatp tdasthpgwd
      361 apegltgrts gpdngaagav avtlrdavaf syrllasder aalrqlavfg nrwsvelaee
      421 mladeadrdg tvaidpvpll drfvelglls vrgtgsfrfr lldavrdyav eqaagegelt
      481 cirrrhaevi arlvartasd lvgprlpdav hrldemssdi ssslahaatd dpltalrlaa
      541 cltrwwrfrg rdvagrqwlr rlladprtgd adpllrgwaa lgvarlaaeh gagaeelsta
      601 raaldtfrqa gdvtgelear nvlgtllisv grqeeareqa eallrlaarn grtrdlavaq
      661 nslawheira gdlaaarrrl aavdrlaves geqrlrvlgw anraevarle gwyadavdrg
      721 qraiealhel gdpgrrrrvl gtvglalaqd grvaeasevl aelragsves lparptiprq
      781 rsddatlrwg gpeaglcali egnlalhrgd relaaewfaa atdnagqdrr dvvealvgla
      841 astadptvld rldrvcvetg irllpqesgl lfalvadrdg par
//
LOCUS       WP_357649915             460 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing protein [Micromonospora parva].
ACCESSION   WP_357649915
VERSION     WP_357649915.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Smith,T.F., Gaitatzes,C., Saxena,K. and Neer,E.J.
  TITLE     The WD repeat: a common architecture for diverse functions
  JOURNAL   Trends Biochem Sci 24 (5), 181-185 (1999)
   PUBMED   10322433
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Neer,E.J., Schmidt,C.J., Nambudripad,R. and Smith,T.F.
  TITLE     The ancient regulatory-protein family of WD-repeat proteins
  JOURNAL   Nature 371 (6495), 297-300 (1994)
   PUBMED   8090199
  REMARK    Erratum:[Nature 1994 Oct 27;371(6500):812]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..460
                     /product="WD40 repeat domain-containing protein"
                     /calculated_mol_wt=48985
     Region          52..>345
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
ORIGIN      
        1 mtarlretlh aaaadvpayp vyeralatar rsrrravaaa vvvlvlatlt gavlpltrtp
       61 avdpaagada alpdrialpp lgalhatdrp rlgpasvifs gqarrlqgwd edgivgvvsa
      121 dsdryrifsm gyeapvgeqv ilspdgryva rpaglsdngr vdlidlvtgr trrlhskvtd
      181 svgtnpraws pdgrqlvvdd tvptdptrsg yrrvlsivtl dgerwtqlad aaqqpifgss
      241 vafapgggrl ayqigrtvtv vdpdgrtvst felpaeswla gkgawttdga ltlisrkags
      301 tdwslrrvds atgrdtaplp vpgvtgvtai rllgwgpdgs alvvayqpep lspdrfdqpl
      361 eldqrtaypn vrgvrvlalt pgasaprtvm tapeqilavd vadtvisagr traanppgmv
      421 ggrfwfwgil itvliagiva yrsreglalw lddrrlrrsr
//
LOCUS       WP_357649933             250 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357649933
VERSION     WP_357649933.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=26098
     Region          1..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 mdsrgvlvtg ssrgigreia kifaaggdrv aihhrdspre aeevrsaldg dghavvqgdi
       61 adpeavaafv saaidaldgi dvlvnnaavy lfhdpltvdy aswqriwrrt vdvdllgaan
      121 vswcvarhmv ergrggrivn vasrgayrge peapgyaaak agltamgqsl aialaphria
      181 vssvapgfve tdmaaailte enragveaqs pfgriaqpqe vaaavrylas aeaefvsgtv
      241 ldlngasylr
//
LOCUS       WP_357649935             179 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein [Micromonospora parva].
ACCESSION   WP_357649935
VERSION     WP_357649935.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 179)
  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..179
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..179
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18739
     Region          11..154
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mtdadpdtrt lvllrhakae qgndaaddae rplstrgtad aaaagawlah hgllpdvvic
       61 starrtrqtw hgvamgmtgs ppeggptgpr ptvryepgay dahpeellsl vrtvdpaart
      121 alliahnpgi sllsalfdpe gvddgglrta elavhrspvg wsqwsragap ltarhaard
//
LOCUS       WP_357649948             308 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649948
VERSION     WP_357649948.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 308)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..308
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..308
                     /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=32743
     Region          7..284
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mttiptsags grpsarargg rngslawltv palvffvgfg viplvgvlal sfttwdgigd
       61 ihfsgftswq avladpglph alwvtflima lswlvqtpts illgvflaga qryravlsvl
      121 yfiplllssa aiaitykall dpnfglgagl kiellsqdwl grpglalgvv vfvvswqfip
      181 fhsliyqggv rqipqsmyea aeldgagrvr kffsitlpql kytmitsttl vlvgsltffd
      241 lifvltaggp gdatrvlald mykrgfqanl mgpasaiali lvfvglalsl llrrlgggka
      301 dhsqmega
//
LOCUS       WP_357649994             267 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357649994
VERSION     WP_357649994.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..267
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28137
     Region          1..254
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mapgrfplvv lapgmglnap vfsslaqela shgyvvasit ptysanvtvl hghvvastpa
       61 gkpegdeekt adrvigvwta darfvaahaa aldrdtnlag hvdasrplyi ghsfggataf
      121 qachddpsca gavdldgaly ggvvrtglra palmlggens cvietcradd aenrgmrdrt
      181 rqwlaastgp vwryeiagtg hfnftdyavi ylaapiralf plesidgarg lriqnayvtq
      241 fadqavrhqa spllagarly pevralr
//
LOCUS       WP_357649974             269 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357649974
VERSION     WP_357649974.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=29262
     Region          6..258
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtldpttaer ralitgatag igaaftrrla adgwhlvlva rdearltela aelgsaygre
       61 vetipadlst ddgcatverr laegspvhll vnnagislnk pflrstaede arllrlnvha
      121 vmrltlaavr pmterrngav invssvagfg tampgstysa skawvtnfse svgqstrpfg
      181 vqvmalcpgy trtefhqrag inmsktpewl wlraedvvde alrdlrkgkm vsipawkykv
      241 vvagmrhapr rllqavardt rgrigrder
//
LOCUS       WP_357649996             424 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357649996
VERSION     WP_357649996.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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 424)
  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..424
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..424
                     /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=46437
     Region          10..419
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mvgqevvkrr rghktrldlt raqstlldqq asaaitvwnc lhaywthfpg rrprlaqadq
       61 airqaradfp flavlpaqaa qavlktyrqa wenffnpdhp adrptfkskr rarlavdvpq
      121 vrnmricrls agwgaatipm igrikfrwtk nlpgigknap tgrltgarlv keadgwhlvf
      181 rtetqvtapa phpgpsvgid rgvnvalals dgttrehgpw ltsgerkrlr rlenksarqr
      241 vtrpkktrps nrenhtydqi aglrakakrr atdwqhqitt hladtfgmia vedlkitnml
      301 asakgtieap gknvaqkagl nraiagqawg rtvtlleykt rdrggqvvrv papgtsqtch
      361 rcghrdpaar aktvfactsp tcgwvghadi naainignaa gpavsgrgdl gtarsakrqp
      421 phaa
//
LOCUS       WP_357650005             840 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650005
VERSION     WP_357650005.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 840)
  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 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 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..840
                     /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=87659
     Region          4..814
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mttlsqsrcg lsaveaaerl aadgsnalpv arrvspvvll lremvhffal llwgaaalav
       61 lagmpqlava iavvvvlngg fafvqeyrad ratqrlreli panvvvrrdg rrvliraael
      121 vigdvvllea gdrisadlel aevhglavne smltgesrpa rpregdqaya gtfvvegqae
      181 avvvatgart rlaaiakltr eairplspla vqlgkvvkvv aaiavgvgtv ffglavllgm
      241 epgqgflfai gvtvalvpeg llptvtlsla raaqrmavrn alvrhleave tlgsatfict
      301 dktgtltrne mtvaevwaps ssaaevmrta vlsstgrlsg gkpvgdpmev alhvealrlg
      361 advegqvsrr fpfdparrra svlvdgrlhl kgapdavlpl craapgadde larmsdhglr
      421 vlavargdta eeseleflgl vglhdppred vaeaiwkcrl agiklamltg dhprtaraia
      481 aevgllgpde lvvtgaelpa ddaalgelld qdgvviarvt pedklriara lrgrghvvam
      541 tgdgvndapa lreadigvam gksgtdvare aadlvllddh fativaavel gratyanvrr
      601 fltyhltdnv aeltpfavwa lsggtiplal tvlqvlaldi gtdllpalal gaepanprtm
      661 rgparagnli drrlllrvfg vlgpaqamae mgaficvlll ggwhlgtaps pgllaaasgt
      721 afaavvlgql anafacrses rwvgrirwrt nplllgavav eavlllaflg lppisnllgg
      781 afppaagwal aalaipamil adtahkawka kharedadsp sastrsasvv apsparrqls
//
LOCUS       WP_357650074             415 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650074
VERSION     WP_357650074.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..415
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44425
     Region          24..415
                     /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 mateeateqa seqaseqqhg qgqlrglkvv efahvvagpl agsmladqga dvihveppgv
       61 gdaaramgpt rdgvplwfkv agrnkrsvtl dlhdpdgrqv ahrlvawadv vivtlrpgrl
      121 raweldweav hrinpkavll qisgfgatss radapgfgkv gearsgvvhl tgfpdgppvh
      181 tgfshgdavt glmgayavla alhrrahdpa fdgewidlal feplfrlvew qvithdqlgv
      241 vpgrsgnqla vapaavinty lsgdgdwitv tsatlrsvln vvrllglpee dyattqrqla
      301 grerldqglr awvaargtae cleafadaev vasrvftaed iagdpvyaer gdiitvddpd
      361 lgpvrmqaal phfhqkpghv wrtgpalgqd nalvyrqwlg lgadqladle krgvi
//
LOCUS       WP_357650082             315 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650082
VERSION     WP_357650082.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 315)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..315
                     /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=34861
     Region          13..310
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mttslstara vetppapttr vrqsigeria pyayiapffl ifaifglvpl lftfyvalfd
       61 wnpigehvfi gfgnfsrlfa darfwnaaen tisiwllstv pqlvlalgla hllnharlrl
      121 avffrmsmlv pyitsvaatt ivfaqmfdrd ygllnwllgf vgvepidfkq svwgshvlia
      181 amvawrwfgy ttllylaslq aipraiyeaa avdgaggwkq frhisipslr pvivftivts
      241 tigglqifte pllvsrsvtc gavrqcqtlt lflyeqgfgq fqfgygaaig valfvlvvaa
      301 atlnyvlstr irper
//
LOCUS       WP_357650108             384 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650108
VERSION     WP_357650108.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 384)
  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..384
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=40761
     Region          155..382
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mahpgstryd saarqleqai artgaaarva vglvavvaaa lgavppvsia wlvpmlavdv
       61 vwtalfarlv wrkellptwl aagdvaitia lclsqrhlva rqaledgasw iaglvtmtii
      121 vagvawppkv avptglavsg aylvgarlts ppqdvsitla thvvqilsiv vlmlllrrsa
      181 asadaflres arreitlmve rlrredelrq vgsihetslh tltmvglgty dgpsptlrgq
      241 aasdlsalek lrdtpraapg sialdallde vaervtglev hrsltpetvp gevaesfara
      301 vtealanvar hsgvrqaell ssrrdgeirv evadegrgfd qdrlppdrfg vrgsildtmr
      361 slpnggaqis sggqgtrvsl wwrp
//
LOCUS       WP_357650111             231 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-binding response regulator [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650111
VERSION     WP_357650111.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10361220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..231
                     /product="DNA-binding response regulator"
                     /calculated_mol_wt=24698
     Region          12..123
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Region          47..212
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Site            order(100..103,105)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381085"
ORIGIN      
        1 mgqqhlagsv tvalvedhqv vvdgvrswfs ppgpvrlvaq gstiesvrgv aadvlmldln
       61 lngtlvvdrv aelcgggqrv ivfseheepe ivravldaga safigkgrat rescletile
      121 vaadkpsmtp pmaqaiatde gphrpqlsdk eraallfwfq smskasvaar mgikertvrq
      181 yidrarvkya aagrpaptke kllicaiqdg lvrpdevtvy tslaarseea t
//
LOCUS       WP_357650120             387 aa            linear   BCT 28-DEC-2024
DEFINITION  CdaR family transcriptional regulator [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650120
VERSION     WP_357650120.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..387
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..387
                     /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=41630
     Region          9..121
                     /region_name="Diacid_rec"
                     /note="Putative sugar diacid recognition; pfam05651"
                     /db_xref="CDD:461704"
     Region          82..385
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msqpwppvlt ptlaqgiagd tsdiigfnvl itdpdglvig sgdtrrigsf heasvevmrt
       61 lksaahsaeq arrlqgvrpg itlpiiidgr algtvgitgs parvqrfglv vkrqteimlq
      121 esmrlrsrll lertvedllr diarfdpdvv npedlvarag elgydlraer tavivdvgeg
      181 apshdgsgir smllrairet fsgsqdlvaa mtssrfaalp rlpagtdlrs lclplaghir
      241 qriglrvgig lgvaadsvpg lhdsyedaat alrlgprvha daqvhaigdl rvhqllaaap
      301 rrarsrfagv staglrarpd wpmlrqtvia ycesgfnlvr aaaalnihrn tllyrldkis
      361 qlsgrpaddh rarlalylac vadqiep
//
LOCUS       WP_357650123             298 aa            linear   BCT 28-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Micromonospora parva].
ACCESSION   WP_357650123
VERSION     WP_357650123.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  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 298)
  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..298
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..298
                     /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=32765
     Region          9..282
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 meaapakter aavaerllts tlrtsydptv eidwdaphvp gaywlppqrs slygtplwer
       61 lseeqrvelt rhevasaasa glwfetilmq mlireyyrad ptsrqaqyal tevadecrhs
      121 imfgrlieam gcpvyrastv dhhlgrflka tasgprmyaa iliaeeilda fqreimades
      181 lqplirmvsr ihvveearhv rfareelaaa vaatgpvgma yarllvgraa ytianrlvhp
      241 dvyaavgipp avgraaaran phwqatlrws aarvhanlag vglvagpgrl lwaragli
//
LOCUS       WP_357650028             226 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Micromonospora parva].
ACCESSION   WP_357650028
VERSION     WP_357650028.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 226)
  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 226)
  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 226)
  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 226)
  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..226
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..226
                     /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=22890
     Region          1..226
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrirpllavl stalvgalgv tsaasaapvs pliiggstvs sapwaaavls ngsftcsgsv
       61 iaaqwvltar hcisgtmsvr igsvnrtsgg vtrtvsatyt rydlalmrls stvststvsl
      121 assnppinst nsiygwgmtc ysgcsastql ktatvrvtsn svtdayggqa irstringna
      181 wrgdsggpqf yngqqvgvas tadgssiqny gsvaynrawi tsvagv
//
LOCUS       WP_357650132             922 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650132
VERSION     WP_357650132.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 922)
  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 922)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 922)
  AUTHORS   Rosinski,J.A. 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 922)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..922
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..922
                     /product="helix-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=97439
     Region          <2..844
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          849..906
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrmwerdrew hcvetllrtv eggaagtllv dgepgagrtr llteaaraag errvsvlqgg
       61 pgelgelipc gmlyqaldlr fepaaggdpg dsrartlerl rsgleeratg pvlvvlddlh
      121 wadpmtlmvl ralhhvlasr sigwllsrst aveqgqaafl fdlleregaa rvelaplspe
      181 avvglmtetl gappepalla laggaggnpl lisellaglr degrlaagad givlphayvp
      241 hrlrmvvrhw idalstgarn lvetvavlgr sfspeqatsl lgttpaallp lveecmaagi
      301 laatpqgltf rhelvrlvva trvpqpvrha lldqlgvrtn vetasrppev yaepasrlpd
      361 vyagatsrsp dlsapgsgdl validaaiag grlqeaerlv nggladrdpa gnvaelrcll
      421 sdimyltgri eealrqaetv lavpdlpghv rdravlirly altrlrasgt pareyacevl
      481 eggarygpaa qvaalvvlav teweegrfte alayaedarq lagteesyvh rydsllvsae
      541 llmnvhrlde arailreara dmsadnhltw tadasalear aelaagrfad avteaekald
      601 latalgtplp amvanavlat valrrgdlra asryvadiad fadvadvagg aggaggagga
      661 gggggpltgh prhtlltaqv aevrdgplsa mtlltdlpvp carlrsmltm dptasawmvr
      721 valaaddrpa aeavvaavea lsaanpgfaa lvasaaharg lldgdcdalg raaertddaw
      781 arasamedlg tallatgrhe eaagsldral aiyqdigsvr dlarvrqrlr gmgvrhrhws
      841 yaerpvsgwd slteternis llvadgwtnr riaeqtfisv htvafhlrhv yrklqinsri
      901 elvrlvvsqg rvesgpsgva ga
//
LOCUS       WP_357650144             299 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora parva].
ACCESSION   WP_357650144
VERSION     WP_357650144.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 299)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..299
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..299
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31041
     Region          81..279
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mssptttrpr svagratrfv laavlaaggv vagstgaaqa agpyergpap ttaileasrg
       61 pfatasqsvs slsvtgfggg viyyptstse gtfgaiaisp gytaswssis wlgpriashg
      121 fvvigietnt rldqpdsrgr qllaaldylt qrssvrsrid ssrlavaghs mggggsleaa
      181 ssrpslqaav plapwnldks wselrvptli iggesdsvap vathsvpfyn sipasaekay
      241 lelngashff pqttntptar qmvawlkrfv dddtryeqfl cpgpsgsaiq eyrntcpsa
//
LOCUS       WP_357650192             915 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357650192
VERSION     WP_357650192.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 915)
  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 915)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 915)
  AUTHORS   Rosinski,J.A. 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 915)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..915
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..915
                     /product="helix-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=97638
     Region          <20..914
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          851..904
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrraivgrde vfdrawqhlg rsgpvlvegp agigkselwr alvghatrag wlvlscapte
       61 aeaelpyaal adllrpladr vaalagpqra aaevvllsgt vreavdtrvv gaatrsllea
      121 attgshpgtl vavddapwld rpseralrya lrrvaglsvl vsrrrgqgds edvplglddg
      181 rhgnrldrve lppldvgalh hvlrdqlgvt ltrpmlvrva reaggnpllt ievvramqrl
      241 prhpspgddl pvaasmhhll advvaglppp srdalrlaal ltvptlvdls aagvpaaald
      301 apeeaglivv tptgvrfthp vhaaavragi psgvrrrlhr rlaelvadpd erarhlalct
      361 tapdpvvaet lagaaerwhs rgapdlaadl herasqltpv edrallgrrr laaarcrlds
      421 gdlpaarqaa esvaadftgd lraeslllra vvawssgeag qaaveigtra laaarpgsav
      481 agrvhahlav fddhteaara haeaaaalld grdgehdlla aallllffqe vrlgraprtd
      541 lleralrleg depawlastv paiwwksidd aqrardrlhr mlaraeargd eplqhellsh
      601 lgeaellagr wdtaerhiaa ardlgdqlgs glvaetwlaa lldahrgrla eatrvaesgl
      661 rlaeeldddw crrihqqlag fvalsagrma eaaaaytala atidarglve plamrfepdw
      721 ieacvgagdl draaaalqrl ndrhrrlprp wtilgtarar vlldsatgrd pgpaldalta
      781 ardavppdvl pldrarclfv agmahrrsrr klparqalea avaeftaiga aafaerarae
      841 larvggrapt prhltptedr varlaargrt nraiadelfv spktveanla rvyrklgist
      901 raelgaamtr aeaqt
//
LOCUS       WP_357650208             267 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357650208
VERSION     WP_357650208.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (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
REFERENCE   4  (residues 1 to 267)
  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..267
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..267
                     /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=29520
     Region          8..263
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          182..263
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 matspagshv sawrpavagv aevfhahfvd hayprhihev wtllivddga vsfdldrhrh
       61 galrtsvtll pphvphdgss atpdgfrkrv lyldtsalda eligravdep dladpqlrdr
      121 ihhlhralaa tggefeaesr lafildrlrr rlrqhppvdg qpagrglavr lrelldartv
      181 egvtlgeaaq llhahpthlv rtftqvygvp phsyltgrrv elarrlllag qrpvetavaa
      241 gfydqahltr hfrrylgvsp arypars
//
LOCUS       WP_357650215             329 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650215
VERSION     WP_357650215.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..329
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=33445
     Region          12..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 msstiglrig gallavvals acsvkgggag dgaaypskav eftvptepgg stdlvtrala
       61 ksiekplgkp avvvnkpgan gkiagkdvfs skpdgyrvav mpqslfaigp lmvqdpdaik
      121 lddmtfikgl avedyalvvp agspykslkd llaagnlkyg ttgagtgsql sqallfgvak
      181 vkatpvpfdg gaptitavlg gkvdaasvqi aeaakhvqsg klralavfgt krvealpdtp
      241 tatesgydvv vdqrrfvagp aglpadvrdk lagaidkaia tpeygellks nyigrwevgg
      301 devktqltka qgefaaltkk lgidltgqq
//
LOCUS       WP_357650229             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            parva].
ACCESSION   WP_357650229
VERSION     WP_357650229.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..416
                     /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=44739
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..371
                     /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"
ORIGIN      
        1 mvvelsqaed aiaacadtai walsegelia aldtahrieq rlasvklali reldgrgtat
       61 thgasstavw lrerlrltip aarrlvdlaa ildtgnpgvr daladgritm eqarviadtv
      121 dtvrtaagpe aadkslgvlv ewagqfdptl lrklstrild hvapdiadaa aeaaldaear
      181 ratrdrhltv stladgrlrl tgvldsetag llraaidplc apsgpddqrt pgqrrhdals
      241 dvcrlalrtg elpehggdpa qvvvttsydg lirqlgsgal dtglhltaea vrrlacdaai
      301 lpavlsgagq pldlgrqrrl isgplrralv lrdrgcafpg cdrpprwcda hhiehwadgg
      361 ttsldnavll cghhhrhlhh sdwtvrltgd ghpefvppaw ldpeqlprrn hyhrrt
//
LOCUS       WP_357650243             254 aa            linear   BCT 28-DEC-2024
DEFINITION  YqjF family protein [Micromonospora parva].
ACCESSION   WP_357650243
VERSION     WP_357650243.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..254
                     /product="YqjF family protein"
                     /calculated_mol_wt=28095
     Region          17..244
                     /region_name="YqjF"
                     /note="Uncharacterized conserved protein YqjF, DUF2071
                     family [Function unknown]; COG3361"
                     /db_xref="CDD:442589"
ORIGIN      
        1 mppepvdhap rqafpwavlr qrwedltflh wavdpalvap llpagtrpdt lhgvsyvgli
       61 gfrmvglgfg rgpgvpyfgt fsetnvrlys vdddgrravv frsldasrlv pvlvaratlr
      121 lpylwssmrl ardgdrrtyr crrrwpgpag atsrmvvrvg eriveptpld hfltarwglh
      181 traygrtlhl pnwhpswplh rcellhldde lvaaaglpap vgppvsvlys pgvgvrfgpp
      241 vaarlraagp praq
//
LOCUS       WP_357650246             164 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650246
VERSION     WP_357650246.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (residues 1 to 164)
  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 164)
  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..164
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..164
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18426
     Region          27..127
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 medgtlkslg ycgdtdgdyd ilqwdtredc evrqildrva dkwsllvial ldrrslrfte
       61 lrrmidgvsq rmltrtlrhl erdglvsrtv hptvpprvdy eltslgvtlh stiralvtwt
      121 eahqneiaaa rtaydarvra eeqaaeaaaa eraeiarnal sgih
//
LOCUS       WP_357650248             418 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650248
VERSION     WP_357650248.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11923260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..418
                     /product="TetR/AcrR family transcriptional regulator"
                     /calculated_mol_wt=45305
     Region          25..191
                     /region_name="mycofact_TetR"
                     /note="mycofactocin system transcriptional regulator;
                     TIGR03968"
                     /db_xref="CDD:188483"
     Region          211..>340
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtstspgari tggadkterr rrlrqaaltl feqrgfaavs iddiaaaagv srrtffnhfd
       61 tkaaalfdpa pgeaaqvadl laqeigtdpw valtralkay laaefrtvst rrrilagqpe
      121 lsrfllvani hfeesildwl gsrgitglsa rtmssmalsc vresvmawds eagpaqlfei
      181 ldqmfalaea gtaairaapa artdtatdkt tpkagqtrsr illtaerlfa ehgvfavsnr
      241 qiseaagqsn naavgyhfgt kagllraive hhttlmerir eqllrargds tdlrdwvacv
      301 vlpftehlss letptwyarl aaqimtepql relaaaglqd apnfytvvgg lhrclpalsp
      361 elrrrrddma rtllvhtcah rehtlpadad aaraawsgta aelidaiegl ylapateh
//
LOCUS       WP_357650250             607 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650250
VERSION     WP_357650250.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 607)
  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 607)
  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..607
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..607
                     /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=67860
     Region          88..553
                     /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 mdhsspppah ftvaelgfdp dvlraryrhe rdrrlrpdgn aqyqgargef gyyaadpyte
       61 raerepvrdr vealvvgggf gglltgaelr eagvddirml deagdfggtw ywnrypgihc
      121 diessvylpl lekagylptm ryapgeeirr havaiaelyd lyrdtmfhtr vtqlrwddaa
      181 aewqvrtdrg ddfraryvvm sagtlvqpkl pgipgietfr ghtfhtsrwd ygytggdqng
      241 alhkladkrv avvgtgatgi qviphlgrds qqlyvfqrtp ssvdvrdnrp tdpawaaslk
      301 pgwqrermen fltvvtggla eqdlindgwt starlqrhll agtvdtdllp erreyldeia
      361 dfqkmnqira rvdeivgdpv taellkpwyr ymckrptfsd hylqtfnrpn vtlvdtadhg
      421 gitamtesav vvgeqeyevd cvifatgfev gvsgivsgal pvhgregaal ldtwrrqgpr
      481 tlhgfyshgf pnlfhlgplq nasavnfvhi lqeqathiga vvaearrrgi avvepttdae
      541 dawvttirel apdnsrfqae ctpgyynneg kprpvsqtyg pgpvafhdll rrwrtqggld
      601 evlagnr
//
LOCUS       WP_357650304             402 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650304
VERSION     WP_357650304.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..402
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..402
                     /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=42477
     Region          8..398
                     /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 mteqgvgrvl vigaglgglt lahalvragl dvrvyeaddg sgerfqgyri glaepgltal
       61 raslpqrlye mveatsgglt gpgllfdeql tvlsrdldgp vegsravdrq vlrrillgdl
      121 gdrvthgkrl tgvaegagvr sahgtegagg svtarfadgt qatgavlvga dggnsvvrrh
      181 lvpevglves dlcgamgrtt itdrflrlvp grgtmvkgre vtlmlgrmqf drepsaaaad
      241 lvpgldmpyr dsyvrwvllv ppghpaatdp gsagedarel vleliegwhp dlrdlvrsad
      301 msavgrskiy drpmppwpvg ritllgdsah ltlasggnga ntamqdavrl sarlaeahrg
      361 erdllsalga yqddllergn aavqfgkeal krfvpprpqe tr
//
LOCUS       WP_357650314             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650314
VERSION     WP_357650314.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..212
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..212
                     /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=23152
     Region          4..195
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 maekqqqgae trdrlidaaa etirsqgyag tsaraiakaa evnsalvfyh fggvdallla
       61 aldrsseqrm aayrqavdqa ksleelveta saiyradleg ghitlfsemv gasiarpelr
      121 aeitarsdpw idfieqaler viggsplarl lpprdlayaa itfylgvnlf thldadrtrt
      181 ealfnlaerv aprarlltmr lpgrrgndkp kk
//
LOCUS       WP_357650387             985 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650387
VERSION     WP_357650387.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 985)
  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 985)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 985)
  AUTHORS   Rosinski,J.A. 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 985)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..985
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..985
                     /product="helix-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=105290
     Region          <80..939
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          925..977
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mthvsdegml lipggtlisa tptdsatahd rpgqkrsvnr gdsysgsavr syleagfagr
       61 dlgskrswlh maanqpvral fgreseqrrl gdfvdgvrrs ggamlvrgea gigksallld
      121 tagiaaargm rilrtvgves ethmpfaglh qvllplrtei gelpapqrda lgaafgltda
      181 rvpdpflial aalnllgeaa arspvlllve dahwldrasa dvlafvarrl esepivllaa
      241 irdgfpspld gaglpellld rlddsaatal ldacgttltp tvrtrllrea agnplalvel
      301 piaaetqggk gplppgwlpl ttrleqtfta rmsglpsilr tmllvaalnd stalseilda
      361 talitgvpvt addlapavtv rlvdvhetgv sfrhplmrsa iyqgasisqr havhaaladv
      421 ltgrpdrrlw hraastprpd etiavelett arsvrgrgdl lsavaaleha arlsenpahr
      481 cerlvraaey aaemgrrdiv grllgegerl qpsaqqrarm vwiretfedg irddsaaahs
      541 ladlaesmaa qgdvdlalkl lssaslrcfw ahadersrqr vvtvaeglpv ddldgrlltv
      601 lafaapierg qvvierlrhl aahptgdrla arllgssalm vgafdlseef caaslpalra
      661 qgrlsllard lgaqawsaar ladlslaipa aeeaarlahe tsqplmhama qasgavlaal
      721 rgeqdrvesl avaaeqvalp igarpvlatv qharglaalg egryadafdh lrrvhdpadp
      781 afhlalrcfs iaeladaavh sgqsravagi igeletvalt tpspslhadl ryaravlade
      841 aaaepffdaa lgadlrrwpf vrarvqlayg ewlrrqrrta esraplrtar etfdalgvip
      901 wserarqelr asgessrsrs seardvltaq elqiaqmaad gltnreigek lylshrtvss
      961 hlyrifpkla itsrsalsta lrvsa
//
LOCUS       WP_357650362             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357650362
VERSION     WP_357650362.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33002
     Region          7..289
                     /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 maenavrhrt vdvdgiaify reagpvdapv vllphgypss sfqfrhllpa ladrwhviap
       61 dypgfgysal pdpdrfaytf dahahllqrf vdtlgltryv iylqdygsqf glrlamaapq
      121 rvaglviqng diypdqhgpk yeplkrfwrd ptdegregla aaisedgfrg eflgelpdrl
      181 tdrvspdlwr lsgalvtdpr rhdawlrlla dqgstvawfp rqqeylrthr pptlivwgph
      241 dgympqgaar aylrdlpdad lhlldgghwl lethldevvr lvrdfldrlq p
//
LOCUS       WP_357650436             385 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650436
VERSION     WP_357650436.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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 385)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..385
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..385
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40704
     Region          32..365
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrhllavaag lvvlaasacs apipprsaap satptgpatl paptgahpvg ttalylkdts
       61 rpdpwnldad arelkvtlwy paeqrdgqra pymtpkesel amgrygiagi pddtlsktrt
      121 navkdagptg rklplvvlsp gftnpmstlt slaeelasrg yvvagvdhty esyattfpgg
      181 rvaeclacds dtdpgfgagv vagraadvsf vldqlpsrwd gsgridrsri amvgqsigga
      241 samatmvkds rvragidmdg ttyaripksg fsrpflflgs aqhvpggrdt swdrdwkllt
      301 gwkrwlvvtg aehstftdas llagalgikp aygvppaara aeltrtymaa fldqhlrger
      361 qplldkpspr ypevklcapd kktca
//
LOCUS       WP_357650465             389 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650465
VERSION     WP_357650465.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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 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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..389
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41398
     Region          47..375
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mtvqsirarl lavpltaclt vtavastttt atatatgkpi ptairlelpr ptgpnavgrd
       61 ilhlvdsdrk dpwvpdsgpr qlmvsmyypa rsatgdpapy mttaeaasll rrkapgvelp
      121 petvsatrty artgapakhg ryplvvlspg lglprasltf laedlasrgy vialvdhaye
      181 ssgttlpdgq titcaplcdq pkppeggqat itknrtkdvs fvidelagrh pvwknarmia
      241 pkrigmaghs lggdaaaatm avdkrvragv nldgtfhpav tldrpflllg sqadhipgkd
      301 dtwdaswpkm sgwkrwltva htnhtsftdl tilqkavgts apddlspqrs leltrgyvga
      361 ffdlhlkgkk qpllngpspa npevafhnp
//
LOCUS       WP_357650475             151 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650475
VERSION     WP_357650475.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 151)
  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 151)
  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..151
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..151
                     /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=16211
     Region          2..139
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msttpgpsda srlyrrylsa vmlhghasak acdlgatdly alnilelagp mtpgelgart
       61 glttgpttrl idrleqagyv rrvpapddrr kvivepigkp aeldqvmapa rqkvgailag
      121 ysteqldvlf dyfdraahay qeaaellrsd s
//
LOCUS       WP_357650478             339 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora parva].
ACCESSION   WP_357650478
VERSION     WP_357650478.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..339
                     /product="phosphotransferase 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=36731
     Region          9..279
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtavsptqqs ltsadvayll gasfgpgtgv rdagpltggg yatvwwalld dgrrvvlkla
       61 psaetpllry erglcaaedr yfrlvaerap qvpvptvlwh gtdpaygewl vtellpgrsl
      121 fdlaeaggav ddgparydlg valaalhqvt gdrfgydggr aagatwraaf tamldellad
      181 aadwdvrlpv tpqrlhellg rhadvldevr rpallhfdcw dgnvlaapdg dgrlrlcglv
      241 dgerflygdp lldlvsprlf qrveddpehp llrgyqatap rplvldgsar rrlafyrlhl
      301 yllmtvemps rgmtaqshpg ryaqltalld eevaalasg
//
LOCUS       WP_357650477             147 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650477
VERSION     WP_357650477.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..147
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..147
                     /product="YybH family protein"
                     /calculated_mol_wt=15776
     Region          2..123
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtttidlaai rtvlqrsqda wnrgdgaayg acfsddatdv tfvgtvyhgg aeigrahqal
       61 fdsflkgthl vmeileirry gadaavvvtr gevakgtpkk lgklatytlv readgqwria
      121 avqktkhkgl meavsfkfqp atkpaah
//
LOCUS       WP_357650507             382 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40 repeat domain-containing protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650507
VERSION     WP_357650507.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Smith,T.F., Gaitatzes,C., Saxena,K. and Neer,E.J.
  TITLE     The WD repeat: a common architecture for diverse functions
  JOURNAL   Trends Biochem Sci 24 (5), 181-185 (1999)
   PUBMED   10322433
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Neer,E.J., Schmidt,C.J., Nambudripad,R. and Smith,T.F.
  TITLE     The ancient regulatory-protein family of WD-repeat proteins
  JOURNAL   Nature 371 (6495), 297-300 (1994)
   PUBMED   8090199
  REMARK    Erratum:[Nature 1994 Oct 27;371(6500):812]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..382
                     /product="WD40 repeat domain-containing protein"
                     /calculated_mol_wt=39428
     Region          <115..339
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
ORIGIN      
        1 mssrmsaalt glalavlaag cadpaadrvs lagapqplas sltvvpssps pmvssgpvrh
       61 plpmatslae pmatgaplaa tgpprffvsa rtpltyfpgr sktavftpvp pavhnaetga
      121 fianiplppg vesswhlvaa ardnrtfava gwtepknpei rfflvrlged grpgkpvait
      181 qtdpddlmmv ydlaisadgt rlaystplig ggakisvldv atgrrrdwkt saysmvtgls
      241 wapdgrslac vlggralasl dlarlgadpe gaapriiknv sgvmliesva htpdgsaliy
      301 asghivervp vaggpaqvla rpelppgasl slrfsvdgtg ehllyvhnwr ayrvgladga
      361 vtsvpitvdq rpgegdppra aw
//
LOCUS       WP_357650510             221 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650510
VERSION     WP_357650510.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..221
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23482
     Region          5..98
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msrsygqycg laqaldvvgd rwnllivrql liaparyrel ldglpgvatn lltdrlrdle
       61 tagvverrla eegnaivyal tpwgaelrep ieglirwstp lmargpggdr fqadwlivgl
      121 ralltgrmaa rqasrvgiav dgrllqvrat gsgievalhd ggdldavvra easivlglaa
      181 galtlddalg lievegdeva vrglfqeggr ntavrdrgpa l
//
LOCUS       WP_357650556             262 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357650556
VERSION     WP_357650556.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25946
     Region          4..243
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrcdglvavv tgggsgigla cvraftaaga rvgvldlels glpedpgvlg vradvsdras
       61 lstavaavaa afggvdilvn nagisavgtv eeddderwsr vldvnvsgva rtsavalpyl
      121 rrsssaaivn issiaatvgl prralysask gavhaltlam aadlvtegvr vncvapgtvd
      181 tpwvarllag aadptaekrq lasrqptgrl vtadevaaav vylaspatgs vtgsslpvdg
      241 gmsglrlpap arpapdrges ga
//
LOCUS       WP_357650567             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357650567
VERSION     WP_357650567.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=35201
     Region          16..292
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msavitprtd tpeapaavpe dsawsrwtne hrkwlfaapa mtfvavliif pvawtgylsl
       61 tdaegsvrae sefigiqnyl dvltdtdrfw pavwrtvlft gvvlffevil gmaialllwr
      121 pfrgekwvrv aillplvatp vavgmmwrli fdpnigmanq llgwigigpq pwlagqhsal
      181 pttmfidiwq wtpmvvlill agltslsdep qeaaridgas swqrfrhvtl pllmptviva
      241 illrgidalk tfdilyatkg rgggsfheve tlnvyaygls fdyndygvss tvliifflii
      301 igvmwaltyr kkglgr
//
LOCUS       WP_357650600             980 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650600
VERSION     WP_357650600.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 980)
  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 980)
  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 980)
  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 980)
  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..980
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..980
                     /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=104996
     Region          1..244
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          168..980
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          733..761
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(734,737..738,741..742,744,774,777..778,781..782,
                     784..785,813,816..817,820..821,824)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          772..802
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          812..839
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          846..879
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          891..921
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvrfrllgpm riqvngspvr itapkqrtvl amllaraghv vpirslvaev wderpprsav
       61 anlrtylmql rkllpdeerl vtsdvgyllr agpqeldlle fealsargrq alakrdtsaa
      121 eqaytqalal wegtaaedvp lgptlrevva rltnnylgvv eehadiqlal grnelaatrl
      181 revirqyplr erlhgqlmta lyrcgdvvga ldafgaarrv ladelgidpg pdlrllqqai
      241 lrrdtallaa grdsaavpvd dgrprprllp raplvfvgrs aerahlhtvl ygetgapmig
      301 psagppaaal egpggagppv valhgpggag ksalaltvah gvsdrypdgq lyvdlqgstp
      361 glpplrpaev lgrflralgv ppgdvpaapa eaathyqsll adrrvlvvld navgaaqvtp
      421 llpagggcaa lvtsraaltt mdavplavgm ldevesvrll rllagpervs aeaeaaaqia
      481 rscgfhplal riagarlagr pdwslarfge rlgdqrrrld elqaadlrvr tcfevgygtl
      541 tstakaafra fgvlevpevg veltaaltdv dqttaeaald eltearllep vgdgrfrmhd
      601 llrlfaaela avhdtpqera ravgralewy ldrlrrlqtl lqphlmpagg genasdvglp
      661 dlaaavrwld tdlpclvaaa vqaakgkpag fvieltalik aiamksgywr eletiarlai
      721 evarrdgdrv aeaatlatlg llewksgrpe aarallhral dlwravgerg eeglalhnlg
      781 wlcmrtgdld aaldhigagl lllethrpnr vglvshnlge vllrlgrhte avdrfeqclt
      841 irradrdlyg esitlaalgr ahclldqrdk alavlaealv hceatgnred qwevllsrse
      901 irlrqgdpaa amadltrvle lttkigdayg haaclrqlar araalgdpra aadagkaagl
      961 fadpatrcdp vlerlltarl
//
LOCUS       WP_357650741             338 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650741
VERSION     WP_357650741.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Rosinski,J.A. 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 338)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11972933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..338
                     /product="helix-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=36995
     Region          12..269
                     /region_name="YrhO"
                     /note="Sugar-specific transcriptional regulator TrmB
                     [Transcription]; COG1378"
                     /db_xref="CDD:440988"
     Region          <283..338
                     /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 mpsesptlpd platlgldpa qtalytavlr lhrttrtela eamdgpvdkv srqlddlvrl
       61 gvideqsgey larhpaaalg rliaerldrl aeesrridsa lgsirglird ydvghdyqng
      121 afrvemvsga dvlyesvvgm avqsqsppmr lltaipdert madfvrkfad pwidaqqrkl
      181 lnvravipvs tltlpgvrdq ltrllatggt vrtldrvpsw fmtagpdaag lpalwggnlp
      241 dhaynfylvr tpivvgmlrs lfeelwgrav plpwgrrgeg vvqvlrlaaq gmcddsiarq
      301 lgisirtvra rfadamvqlg aqsrfhagve aarrgwls
//
LOCUS       WP_357650771             404 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650771
VERSION     WP_357650771.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..404
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..404
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42982
     Region          167..396
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtaedatlkv irkngpeggk lrrriiivtv svllvalvgg afgvawwgsd faikpdhhfn
       61 thpdhsnvvl evkrvgsgen vvigspnayt rrrgtyrmvw ggveakigdv vagsagsver
      121 pilsgpapsv gttvdvtgvm isdpksslgl dysevsvrte lgpapawyvp asgstwviav
      181 hgqnarrnam vaipifhrlg lpvlaityrn degapasadg lmhygeseyr dlesavryaq
      241 skgakrvvly ggsmggmivg qflarsplag vvtatlldsp llsmpmvaaf ggehygvpap
      301 aiwlsnkity wrsgvdmdql dlinhppatk pptllfagls dteappamdr afvaaakkah
      361 wpveyaefpg aehseswnsd paryekavtd fftrtvvaae rgsa
//
LOCUS       WP_357650770             100 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora parva].
ACCESSION   WP_357650770
VERSION     WP_357650770.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 100)
  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..100
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..100
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10422
     Region          15..89
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvrlpltpae vergqrlgal lrrargersm lltaldagvs petlrkiesg riatpafpti
       61 aaiadvlgls ldavwseint sdagadlprp ahvagerlas
//
LOCUS       WP_357650789             339 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Micromonospora parva].
ACCESSION   WP_357650789
VERSION     WP_357650789.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 339)
  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 10167525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..339
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=33088
     Region          3..146
                     /region_name="SRPBCC_5"
                     /note="Ligand-binding SRPBCC domain of an uncharacterized
                     subfamily of proteins; cd07823"
                     /db_xref="CDD:176865"
     Site            order(3,5,7,16..18,20..21,33,41,43,45,47,62,64,74,76,
                     91..92,94,96,106,108,110,112,126..130,132..134,136..138,
                     141)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176865"
     Region          <143..259
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mkitnefava vpierawavl tdlpglapcl pgaqltgvdg diyqgrvrvk vgpvvsefag
       61 tarfvekdda ayhgvigakg rdsrsagaas alvtaqlrpd gdrtvvsvdt dlkisgrlaq
      121 fgsgmikevs gkllaqfvan leaklatdrp dpavpaprpg pegvastpdp vatasaaava
      181 ttpdtaavap spvepslvga ptkpssaepp tpvespsapg spvppststs asesasasas
      241 aggsptgsts vtsaaepeal veapsasgss vppspstsas asasaggspt gstsvtsaae
      301 pealdllsia gasvtrrlvp vvvglvalga viawlvarr
//
LOCUS       WP_357650779             290 aa            linear   BCT 28-DEC-2024
DEFINITION  SIS domain-containing protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357650779
VERSION     WP_357650779.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Bateman,A.
  TITLE     The SIS domain: a phosphosugar-binding domain
  JOURNAL   Trends Biochem Sci 24 (3), 94-95 (1999)
   PUBMED   10203754
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454870
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..290
                     /product="SIS domain-containing protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31063
     Region          6..288
                     /region_name="AgaS"
                     /note="Fructoselysine-6-P-deglycase FrlB or related
                     protein, duplicated sugar isomerase (SIS) domain [Cell
                     wall/membrane/envelope biogenesis]; COG2222"
                     /db_xref="CDD:441824"
ORIGIN      
        1 mtthteaeig sqpecwrrav anvpvdalpr pgervavvgc gtswfiamay atlreraglg
       61 etdafaasea ptgrsydrvl altrsgttte vlellrrtda rttaitadpn tpvmtaaddv
      121 ivldyadeqs vvqtrfattq lamlraslge dltqaiadae qavaaplpae ltdaeqfsfl
      181 gigwsvglaq eaalkmreas rswteaypam eyrhgpisia gpgrvtwmlg tapeglreqv
      241 eetggtffqt gldpmaelir aqrvavaraf argldpdepl hltrsvilss
//
LOCUS       WP_357650844             250 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357650844
VERSION     WP_357650844.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=25298
     Region          9..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mptpspdlrv alvtgstlgi gravavrlar tghevvlhgr dhersakaaa evaaetggrt
       61 dtvhgdvadp aavsammrev hrrhgrldal vinagghaas llgmmhsdvv srlfhvnalg
      121 athtlqaavk llrrgtdpav vlvssvmgrk gapgqavysa tkaavlgltl aaakelgpqg
      181 irvnavapgy iqtdmlstld draradtiaa tplgrlgtag dvaaaaafll sadacfitgq
      241 vigvdgglvl
//
LOCUS       WP_357650920             376 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357650920
VERSION     WP_357650920.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=40403
     Region          125..376
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mdlstgqpwp vsrhwrytgw llaavwlffl nvplatalhq pelwrrilgv aalvvfgvgy
       61 vllfqwarkl rqslrpipvg raraglalll avglaslpga ggdwlatlvy vaaaavfllp
      121 pwealavval cavtpvlasw lvtgweaehg ivfavllasf amfgvsqlaq rnselraaqq
      181 eigrlavaee rartardlhd ilghsltvva ikaelagrll dvdreraaae iaevealara
      241 aladvrqtvg ayrevslaae vagarsalaa agiaadlpve lpelpeewdr lfgwavregv
      301 tnvvrhsgar ccvirvhpdr veisddgrgp stpdasghgl vglrerarrl davvtvgrrp
      361 tgdgfllrvh tpeear
//
LOCUS       WP_357650934             280 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome c biogenesis CcdA family protein [Micromonospora parva].
ACCESSION   WP_357650934
VERSION     WP_357650934.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Williamson,J.A., Cho,S.H., Ye,J., Collet,J.F., Beckwith,J.R. and
            Chou,J.J.
  TITLE     Structure and multistate function of the transmembrane electron
            transporter CcdA
  JOURNAL   Nat Struct Mol Biol 22 (10), 809-814 (2015)
   PUBMED   26389738
  REMARK    Erratum:[Nat Struct Mol Biol. 2015 Nov;22(11):939. doi:
            10.1038/nsmb1115-939b. PMID: 26581523]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..280
                     /product="cytochrome c biogenesis CcdA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=28533
     Region          1..168
                     /region_name="CcdA"
                     /note="Cytochrome c biogenesis protein CcdA [Energy
                     production and conversion, Posttranslational modification,
                     protein turnover, chaperones]; COG0785"
                     /db_xref="CDD:440548"
ORIGIN      
        1 mtgalllalt agmlgavnpc gfallpayls llvagtsdtr gavgraltaa agltvgyvlv
       61 fgafglalap lagwlrprlp wltvalgvll lvagcwllag rrlptpgwsa raprltrswp
      121 smalfgaaya laslgcaiap flaivvtslq agstgqglal fgayalgmgl vvavaalgva
      181 lvrdglvarl rvagalvprl sglvlllagg yvawygwyel rlaagrrdal hdpvirvaaq
      241 aqraladald rmgpavllaa latlllaalv akrahrprrp
//
LOCUS       WP_357651019             239 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357651019
VERSION     WP_357651019.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24449
     Region          25..237
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrevvvtggg tgigyavaaa faaagdrvti tgrrehvlke aasrlgadfl pfdaaspaav
       61 kvaasrlper vdvlvnnagg ntnldrrqsd dlldvaegwl anlnanllsa vlvttallpr
      121 fakggriiti gsiaargtgs gsygaakaav eawtadlaaq lgprsvtanv vspglvvdte
      181 ffrgrlteeg irarventrn grpgtpsdva dsvvflaspg arhltgqvlh vnggaylgr
//
LOCUS       WP_357650941             393 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Micromonospora parva].
ACCESSION   WP_357650941
VERSION     WP_357650941.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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..393
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..393
                     /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=41821
     Region          4..391
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mavertydvv lfgatgftgg ltaeylarha paglrwalag rnpqrlaavr drlaavdpal
       61 adlplltadv tdadslrvva enarvvastv gpyihhgepl vaacaragth ylditgepef
      121 vdlmyvrhha eatrtgarlv hacgfdsvph dvgvwftvkq lpadvpitvd gyvraggrfs
      181 agtyhsalta fsrtgqasra arerravepr padrrvravp grlarsaelg iwtvplptid
      241 pqvvrrsaaa rpeygpdfry rhfaavkrlp tvlvgaaglg alvglvklpp srrwllgrla
      301 sgqgptaqqr asswfrvrfv gtgggqrvvt evaggdpgyd etakmlgesa lcltlddlpp
      361 tagqltpvaa mgdalldrlv ragltfrvle rsa
//
LOCUS       WP_357651022             290 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Micromonospora parva].
ACCESSION   WP_357651022
VERSION     WP_357651022.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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..290
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..290
                     /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=29414
     Region          3..260
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mvdllvlggl gvdvrvrvpa lplpaadsht vepielrign tgagvalaar alglrvlvvd
       61 tlgadpagel vraaltragi pavlaenpdg trrsvnlvdp ggrrtslydp rpwrggppfs
      121 apelaalvrd arhvhlsimd wavpllpavr aasaagaals tdlhdwdgen tyhrpfadva
      181 dlvlmsgvrl gdrasslagt laprtvlvtr gadgaelfpg dgtvtpvppa tapapvvdtn
      241 gagdafaagl iaarlrgepl adaaryaarv aaaacahdgm eypsgllpgg
//
LOCUS       WP_357651053             153 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357651053
VERSION     WP_357651053.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 153)
  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 153)
  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..153
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..153
                     /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=16417
     Region          14..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msddsdestl grietevall mrfgeatrra tgtaehrvld raayvilrhl adagpqnvsa
       61 laarlnldgs tvtrqvsalq rdglitrtpd psdgrgtvis ptpaglqrma avqaartrly
      121 gdmladwsae dratlaallg rlnqalinrn rpr
//
LOCUS       WP_357651093             133 aa            linear   BCT 28-DEC-2024
DEFINITION  TadE/TadG family type IV pilus assembly protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357651093
VERSION     WP_357651093.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..133
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..133
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=14109
     Region          5..>40
                     /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 msqnrrrerg smavetvmla pvfllflmfl agagrlveaq gevngaarda araasvrrsf
       61 gdageaadrn vkaaldgrcq spavslagsk weeggqvqae vtceldlsfl gfsgtkrmtg
      121 tsvvpleqfr rte
//
LOCUS       WP_357651102             143 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357651102
VERSION     WP_357651102.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 143)
  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 143)
  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..143
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..143
                     /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=15775
     Region          4..143
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mpladdavea raqgwrtlaa lhariedrle ralqkehels vseytvldvl grqdgwhmrm
       61 qqlaravvls qsattrlvtr lenrgllsry lceddrrgiy tevtpagrel laqagpthdt
      121 vlkevlaeaa elpelaplaa via
//
LOCUS       WP_357651049             182 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357651049
VERSION     WP_357651049.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 182)
  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..182
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..182
                     /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=18737
     Region          2..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mradakrnyd livtaaseai ardgayasle eiarsagvgs atlhrhfptr wsllqavfgg
       61 cvhnlaarag dllaasdald alttwlhevt ayatttrgla dsllnepaee sgtcgatlva
      121 agepllrrav degsvrpdit madlmilang islaaqpmga akasqlltla lqgigspdrg
      181 rs
//
LOCUS       WP_357651117             398 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora parva].
ACCESSION   WP_357651117
VERSION     WP_357651117.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..398
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44147
     Region          4..395
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mskpthaela rvvrdhagql aaslvhlvgd fsaaedlvqd aieaalthwp vegiperpaa
       61 wmytvarrrg ldqirrdqrh rrklalvawp vepppddrlr liftcchpal praaqvaltl
      121 rvvcglstaq iaraflvpes tvgqritrak rkisdaaipy ripseddlgs rltevlaviy
      181 llfnegylst ggdraqsrdl addaeflaal lhqlmptepe vagllalirl hrarasarfd
      241 rdneivqlqh qdralwdhrs iaaagrlvaq aaarkrpgpy qlqaaivach aeagrweetd
      301 wtqiavlydm llrlapspvt rlhraialry vsgpsialte vdaltgelnd yhlfhatrae
      361 llrdlgdttq artaderala latnpaersl lrhrlnwa
//
LOCUS       WP_357651156             102 aa            linear   BCT 28-DEC-2024
DEFINITION  putative quinol monooxygenase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357651156
VERSION     WP_357651156.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 102)
  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..102
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..102
                     /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=11534
     Region          2..86
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mfglmvrftc kdeasattfd tlvgetieai rrhepgtivy ashrvdgqpl qrifyelyqd
       61 rdafdaheqt ehtrrflaar dellasvevd wldllsgkgt ts
//
LOCUS       WP_357651175             398 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357651175
VERSION     WP_357651175.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 398)
  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..398
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..398
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43213
     Region          2..70
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 meyqralgrr iaqerkrrgl sqaelarlvd rsvawisqve rgvrkvdrms vlekvaetld
       61 vplselaaea pvvaatneem pgtaglrlvl sgshslqatl hatpvpaidq lkpqvdhawe
      121 lthqsryvel tellrglvpt lesavrsapa erqaelfell avtyqacaas laklgepdaa
      181 wiaadraisa aeragnpllm aagafrlgfv flgarhfdqv eetartaaea lwfltdqgsm
      241 eamslwgglt lqravaaarl nqadmayehl sraremaarv gegrndynte fgpanvalhe
      301 vavavevgda ghalrvgaav etsslsaerr arlaidlara haqrrqvdea vtqlleaesi
      361 tpeqvrnhri vrqltsdlls mqdqaspelr elaervga
//
LOCUS       WP_357651183             670 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357651183
VERSION     WP_357651183.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 670)
  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 670)
  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 670)
  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..670
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..670
                     /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=72404
     Region          13..666
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpahqlapdi padvlaaeqs hlaesraalq amrlhaqsls adaagdwvsq qilqslldkr
       61 vaaladhpdt plffgrldrs adddlpptiy vgrrhvhdgn srplvidwra pvsrafyqas
      121 padpmsiarr rrfgyhggal tafedeplge ggdigsskil tdeierprtg pmrdivatiq
      181 pdqdeivrat ltqtvcvqga pgtgktavgl hraayllfth rerlarsgvm ivgpnrafls
      241 yissvlpalg evkvdqttva gllgehatpe dpmvsalkgd armaavlera lwlhivkpee
      301 gvvyskgayr frvadyevre ivaslrgttr ygpgraalaq rlahmvlvrm eqrgespddr
      361 vqdavarskp vkqlvdavwp klvpqqvlfk llsdsefltk aakddlspde qqmllwqkpy
      421 rgwksakwsa adaalldelg dliertpslg hlvvdeaqdl semqlralgr rcrngsatvl
      481 gdlaqgttpw stsswetvlk hlgqdegevt eltlgfrvpr evldyaarll psiapalapp
      541 rslrpgvgsl tvrpggavad aaleamareg sigvivpdal vaevsrqldg lahavldsdt
      601 teehrllivp atlakgleyd hvivvepadi vaaeprglar lyvvltravt sltvlhgkal
      661 paqlsaqpav
//
LOCUS       WP_357651189             132 aa            linear   BCT 28-DEC-2024
DEFINITION  group I truncated hemoglobin [Micromonospora parva].
ACCESSION   WP_357651189
VERSION     WP_357651189.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 132)
  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 132)
  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 132)
  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 132)
  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 132)
  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..132
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..132
                     /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=13870
     Region          14..124
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(16,21..22,25..26,29,59..60,63,92,95,99,102,113,116)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(30,39,42..43,46,50..51,54..55,57..59,61,69,71..74,
                     77..78,81,83,87..88,91,116,119,123)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(32,35..36,94,97,101..103)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mtvteetapa shydriggas svkaavelfy dkvladpela gyftdvemag qrrhlalmlt
       61 vvlggpneyt grglaeahqp lnitvehyak vgehltatlt elgvpadila dvqtvlgqvq
      121 gqvvaaenrs gv
//
LOCUS       WP_357651200             205 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357651200
VERSION     WP_357651200.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 205)
  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..205
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..205
                     /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=22522
     Region          1..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtrstrerii dealrlfaer gysatsvaei eaasglspga gglyrhfksk yevlaaaine
       61 haartrtqva eslaqlgdme tsadlemrls hlcraglakv reeseltrvf frdlsqfpel
      121 vavvregllq pmfdaittwf raqpeyedak vdwngiaavl ggsvvhyrlf qetvgevpgh
      181 aekdqfvtaw vrlamgllps papvs
//
LOCUS       WP_357651225             260 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357651225
VERSION     WP_357651225.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..260
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27474
     Region          1..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 mhlaydqsad tgaavvclpm fstsraatat alhpalagag lreiyldlpg hgdtpahcpp
       61 tsqavldtvc awldhhvdtp vllaggsyga ylaagiarqr pdlvrglllv cpgvtiarhs
      121 rtlpdnppld tptgwldaap talhahldaa lghrtpavva tvlaalnsgg pgdatfqqel
      181 qtgpdyalpd edadvvfhgp vtvitgrqdg ivgyadqfra mrryprgtyt vidaaghylp
      241 yeqpallrsl tqdwlrrtrd
//
LOCUS       WP_357651241             157 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357651241
VERSION     WP_357651241.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=16324
     Region          12..137
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mstvptlngq vigqahyatr allertiapl gvefhqllal nvlangpveq aqltqritst
       61 lkvderevrr vlttlvdadl aqsdpdtatr lrltdagrav qariadavag isarlyadip
      121 paeasaaaqv ltlvtqrana elaatehtga gnasiaa
//
LOCUS       WP_357651239             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357651239
VERSION     WP_357651239.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=16279
     Region          19..135
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mdhaapqspa glhttpswll nqtashagrl lsegfaahdl rgyhyrllat lteegpasqa
       61 dlgrrcgidr sdvvatindl agrglvvrap dpadrrrnvi svtdagadea rrmaatverv
      121 qadllaplst dereqltrll trllrhhsrh
//
LOCUS       WP_357651289             517 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora parva].
ACCESSION   WP_357651289
VERSION     WP_357651289.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 517)
  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 517)
  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 517)
  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..517
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..517
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54701
     Region          34..310
                     /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 msepatdidr phrsapsppt arqpepgart rgpwlvaaat satllllagr ygyhrdelyf
       61 llagrhldwg yvdqgplvpa larlldtiap gnlvvlrtps allaggavll vaaiarelga
      121 grgaqlvaav laalsgivla sghllstttv dllvwllaaw cavrllrtgd srwalgigla
      181 lgvgmlskll pallavglvv gvliagprrl lrdrwvlaaa gvtvllaapn liwqashgfp
      241 qlgvaasisg gdssysgrld aftlqfviis pyavpiwiag lvallrrpaw rayravgwaw
      301 lvvvgivlaa ggkgyydapl llvltaagav vtvawasrgs lwwrrgllal gvvpfllpnv
      361 vlllpvlpad rlpgfvvdvn ydagetigwp afadslaavh nglppeersr avvltanyge
      421 agavarygpd ralpraysgh nsmvdfgrpp adadvviavg werpdqlstw feqctlagrv
      481 dqrvevdnde nggpihvcrg lrrpwaqiwd tevrhtg
//
LOCUS       WP_357651355             111 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: antibiotic biosynthesis monooxygenase family protein
            [unclassified Nonomuraea].
ACCESSION   WP_357651355
VERSION     WP_357651355.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 111)
  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..111
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..111
                     /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=12299
     Region          3..107
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msvvkinvlt vpaemreele rrfsnragmv esadgfewfe llrpvegtdq ylvytrwrse
       61 ddfqtwqqgq afqrghaqag aaqghghgqg paasgsqlws fevvqsaspk s
//
LOCUS       WP_357651387             239 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357651387
VERSION     WP_357651387.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24139
     Region          3..234
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtrtvlvtgg tsgigravae lfaadgaevy itgrrpdtve paakelgvhg iacdatmpdq
       61 ltelgdrldg pldvlvntag glpetppagt pplaalaaew qssvstnvlt avlttaavrd
      121 kltagssiis igtigaergg gsygaakaal aawnamlaae fgprditcnv issgyvtgtn
      181 ffgggmtear hqalvdetll krpgtpsdia qtvfflaspg ahhitgqtih vnggafttr
//
LOCUS       WP_357651385             169 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357651385
VERSION     WP_357651385.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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..169
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..169
                     /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=18276
     Region          22..162
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtddapspae iaaawqrerp gtptdsieiv tpiwrlakmf addrarvlra agidaatldl
       61 lsvirrsgpp ytlstrelas rtlvtagais qrvaraerdg lvrrapgitg rksvnvsltd
      121 eghmliersv dsvlsreasl vadlpkeerd tlvdllaklt anvqrrqgl
//
LOCUS       WP_357651389             230 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357651389
VERSION     WP_357651389.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 230)
  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 230)
  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 230)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..230
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=25233
     Region          <1..214
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 misrdirefa hvnkaqaipd lialvaarag gqvvlahiaq glgldvatvr tylayletvf
       61 lvatapawsn nlssrvthap ktyvtdsgla ahlmdvdaes llapghpalg glletfvfae
      121 llklstfarr hvtvrhyrdr eqreidfile rrdgtvvgie vkasatpkse dakhlrwlrd
      181 klgdrfragy vlhlgatnlp sgdriffspl silwnhmgpd tvtpslpsrr
//
LOCUS       WP_357651394             965 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357651394
VERSION     WP_357651394.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 965)
  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 965)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 965)
  AUTHORS   Rosinski,J.A. 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 965)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..965
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..965
                     /product="helix-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=103536
     Region          <7..913
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          902..955
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 masdvdtapl vgraelvqtv rsallgdgah gqtaavfltg esgvgktrll geigdrlrer
       61 gavvltgscl digdasplhp llqalrrfdt evsasparts savrgllqmf adetagpdga
      121 gallervsrg lhliaegrpl vlilddlqwv drstrqllly llaglgdlql svlaavraes
      181 lqgahplrrv ltelrrlrtv rvldlaplgr adtetlasav vgrtlsadaa eqvwqrsggn
      241 pfvieelard lrdgrdglse tlreifldrv dalpqhahav vhavaagvep vqhwllaevl
      301 rmpedeliaa araavahrll vgaddgyrlr hrlvaevlah ellpaersgl hrryaealtt
      361 apgelhqarl ahhwrlagep aralpaavaa aqeaerlhgy aeahrhwsaa lqlaaepgps
      421 tvdrvellen aaeaahhcge haralallee lvalrggeps calhirrary laaagrsala
      481 eeeyqralka edcsprdrat aaarlaelll hlgryadage rarealalae nvagsttevv
      541 lassalgfsd afledpdagl avmrdaldta eragqpedva caylhlaell tgplnileeg
      601 vvvarrgaer vaelglgrtw gtrllaiain glfrvgqwae aekvvavalr hrpsgadave
      661 lllarcrlsv gygdieaagr dldavatlla gggarhvipl ltlrsglamw egrhdvarqa
      721 vqrgltesrs ddvmilsalv whglraeaea hasrtvevdp tavrrlrdva drmarksaga
      781 arpvrsvveg flalcaaevs rldgsdpelw avsaaewdrr nhpypaaysr lrqaeallar
      841 rsrlatagkl lreayrvaqg lgavpltsei relagrarvs lderdaatgt rgapaeasdd
      901 eltaltarer evlalvaegl tnkeigqrlf isertigvhv shifdklqvr trvqasaiql
      961 rnqrg
//
LOCUS       WP_357651401             333 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357651401
VERSION     WP_357651401.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=36167
     Region          16..316
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mletsarllr llsllqthre rsgvelaerl gvtvrtvrrd igrlrelgyp vhaiagapgy
       61 rlgagtdlpp lllddeeava vavglrtaag gsvsgieets vralaklerv lpsrlrhqvh
      121 alqsmtvpmg ragsvvdpas ltaiaaacrd hetlrfdyrt hdgeesvraa epyrlvhsgr
      181 hwylvgwdtd radwrtyrid rlslrtpngp ryvprdppds dlaaymsrsi ssapyryqgr
      241 ftmyapaevv aehmqattgt iepinersca lssganhlde lavwvalmdi dfevheppel
      301 vdrirvlstr lataagsspa gsspagsspv gpa
//
LOCUS       WP_357651461             923 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357651461
VERSION     WP_357651461.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 923)
  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..923
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..923
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=97551
     Region          9..849
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mvagadispr eaevlelvga hlsnaeigar lyisvrtves hvssllrkle vpdrralaqr
       61 apepagagps hpapvlpasl tsfigreser aeltemikah rqvtavgpgg vgktrlasav
      121 aaqaageysd gvwfvdlvpv tdpgmiaaav agalglgeqp grdmtasvva aladrhallv
      181 ldncehvvdg atlllerllv tcprvtvlat srarlmvpfe rvyqvpplsl tvdgesdava
      241 lfmeraaavg wpldpplrdq iaaicerldg malaielaaa ryptlgldgi taalshplrm
      301 ltggsrader hrsvraaldw shtllepadq allrrasvfv apftaaavae vagseeglva
      361 dglarlaeqs llvvaaspgg tqyraletir qygterlaea gelidarsrh lrwcltraag
      421 lkavrvdwra rfdavaddlr aalawaadrp eqrtdaydla rhlaeltftr hltgesqrry
      481 eqaaaltadp aagasmlrqa aavagcrtig ddmyrlrraa adaarssgds agaaadlata
      541 atiafrfstt fvrlpsreet lalitearel agddpaaqaa valaeaavlt dafgaaqgpp
      601 gnavpetiar aeravelthr tgdplaesaa ldaltgaqsw agdtfataat arrritllss
      661 lpispagthe lidalgmvte aalgagdvpg arrwarqlad hpslaevghr atcrllmvda
      721 lagnidevlt gsvrfldawr ragsparsll rpaaaavami hglradhdaq rewqevlnql
      781 gtplehtygy gavfdailll hrgqapeale rmtpeprqvw kwvtwiwhhw yvalrteaav
      841 lagspdardr laearttvag npvadamver aqalldndqe rllatvaafd tagcryqsar
      901 tlvlaggdha argaaaladl gla
//
LOCUS       WP_357651507             283 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Micromonospora parva].
ACCESSION   WP_357651507
VERSION     WP_357651507.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 283)
  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 283)
  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..283
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..283
                     /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=31744
     Region          40..231
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mtggarrqvt drlrrgvrta rawgraarpg epgplpdflv igaqrcgtts lyhhlaahpr
       61 irvptgkelq yfsvhhargv rwyrghfprl apgertfeas pyylfhpsvp arvaatlpqa
      121 rfvvllrdpv qrayshylht rsygaeplsf adaldaeeer lagatrsgpd spaahralrn
      181 hsyaargrya eqldrwfahv prerihvart edlhadpagt ygdivrflgl paftpdaftr
      241 htrrvdpgvs eltpalrerl serfaphnar lasllgwsdp wpd
//
LOCUS       WP_357651517             303 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Micromonospora parva].
ACCESSION   WP_357651517
VERSION     WP_357651517.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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..303
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..303
                     /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=34480
     Region          5..256
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mlslvvgtgr cgstlvqell srhpavgfvs glddklarln pkgrfnglly rrsaprpagm
       61 tslrhsrrll ergrlrvaps eayhlldrqv lagfsrpcrd lvaedltpfv srrlraffde
      121 riarqgcqql vqhvtgwprt gllhaaypdl rvvnvvrdgr avanswlqmg wwdgwrgpds
      181 wiygplpsdl reewiesgrs fpvlaalgwk mlmeafaqar lrhpadqwld vryedlveqp
      241 reqagrmldf lglrwstafe kgfsrydfsv graeayrdel spaqvtaier vlekplaewg
      301 ypv
//
LOCUS       WP_357651709             332 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357651709
VERSION     WP_357651709.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..332
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=35689
     Region          1..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 mkvttprltq hvltvagrds gepvlfvhgn vssgafwrdt maalpeayrp lavdlrgfge
       61 sdpepvdatr glrdysddls elidrlgler vhlvgwsmgg givlrllrdr pgtvrsvtlv
      121 npvspygygg tegadgrlth adgtgagaga anpdfvsrlk agdmsdespt sprsvfrsty
      181 vknpvpdedf yvrsmltthv geahypgdpv gsarwpgvap gkhgvlnala pthfrlddlh
      241 eidpkppilw irgaddvivs dtslfdlahl grlgvvpgsp gttaqpmvtq travldrygr
      301 yreavltecg hsphlerpad fqrlladhla es
//
LOCUS       WP_357651710             381 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora parva].
ACCESSION   WP_357651710
VERSION     WP_357651710.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..381
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41324
     Region          3..377
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mdetllrnlt psvlgilvrr gidfaaaeda vqdalveavr vwpvdpprdp lgwlttvawr
       61 rfldaarada arrrredlvd eepapgpapc vddtlalyfl cahpsltass avaltlravg
      121 glttrqiaha ylvpeatmaq risraertvs glrfdrpgdv atvlrvlylv fnegysgdvd
      181 laaeairltr qlaaaidhpe vagllalmll hharraarta pdgslvplae qdrsrwdtrl
      241 iaegveilqa alardqlgef qaqaaiaalh adaptaaetd wvqivewyde lvrltdnpvv
      301 rlnravavge adgpraglma laalddtlpr yaavaaylhe rdgdlataar ryaeaarqap
      361 nlaerdhltr qaarlnalgr r
//
LOCUS       WP_357651746             147 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            parva].
ACCESSION   WP_357651746
VERSION     WP_357651746.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..147
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16255
     Region          18..135
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mttttaaqkr aqakveydaf laqcpsrkli driadkwvtl vlaalnsdgs hrfgldcagq
       61 prpmrysels rllagvsqkm ltqtlrsler dglitrtvvp tvpvtvtyel tdlgislhhl
      121 mrglkgwaet hmddvlanra tydnrda
//
LOCUS       WP_357651780             501 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357651780
VERSION     WP_357651780.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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 501)
  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 501)
  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 501)
  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 501)
  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 501)
  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..501
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..501
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54922
     Region          13..333
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 meeslptkpd hvvdrdrewd llaefltdpd pamrlgivsg rrrhgksyll qalseqvggl
       61 yvtavreegr lpairrfsda vaahaglrpg slrltdwrdv lsnaldvtar sshpllvide
      121 lpyllqhspe ipgllqqlyd erqrgarpga gsgprlilcg samsvmhell sgtkplrgra
      181 vvdlrlgafg yrdsrafwri ddpltalkvh avlggapgyr pvaarphpdd gfdawltrtl
      241 ldpgravysr aeteyllred pritqhtlyy diltaiaqga ttpskigaal erprnavayp
      301 lgvlestgyi rreqdilrsr hpvitladpv irfnqlitlp qaaaveqgfa eqvwqqaapt
      361 fnskilgphf edlardftrr yahtllpggl pgsvgtteva dqagrtkhev dvialaager
      421 pqalrarial lgeakataar rgtgdlerle riralladqg ydtagttlal yslhgfhpdl
      481 vdlagrrddl llvdlltlyg s
//
LOCUS       WP_357651802            1028 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Micromonospora parva].
ACCESSION   WP_357651802
VERSION     WP_357651802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1028)
  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 1028)
  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..1028
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..1028
                     /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=110702
     Region          146..881
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mrrrgwkwgs lgvvaalaag gtawvwlryd fekvnwtwgv vagfiavyvl ldqvfrgata
       61 glaeaaahrr aaadelveli rrdptdeall rtvdepyplp vrwrtapdrf lpswraigrs
      121 saavpvdlag gngtlwscyr rvpsgrllll gpagsgksil alrmarelpv hrepdapvpa
      181 lvaadswdpd regfhdwlvd riarrypqla aghprrdavl rdlietdlvv pvldgldevp
      241 edrliaclde lnalptqrfv ltcrtsvyer yltqgeklrg tavvmleppa paevadylvd
      301 aaplhqvdnw tavattlgda pqltaalstp lmvamarsaf dqpgtdprdl vplarergqr
      361 sveddlltra vdaalrsrrg sqglrrweph tarryltfla ahlesldvre frwwqlanaq
      421 pgpfwalvag artaaavwla ltlsadalta taqvvthppt rnllddlvre tdtlaitafl
      481 lagvvalvrg sgragretpr rvafvgglrs frdglldglf ggailalftf gfltafapta
      541 qlialvdrvp glpqwpdpvr aavmvgllgg afravraglr vdvaapapel gatsvvetve
      601 adraasvasa lasaatgvlr llvvvaalrl tgvlsavppl palvwagvgl glgwwlhrrg
      661 ggawmrfalt raalavrgrt phrllaflay aetvgllrdg agayrfrhgr lqsrlaagsv
      721 sarrgsrlre efgvelagag ywpeafgvfa dvtqaraasi ghaddltvaa lrrallagaa
      781 agewtrlasl lalipppsep tpsavqrqrl aqliaddapv teliaaaeel draatgvtpd
      841 lasvtrpaah gvreflavlh hvngdveaar thldllraaa dqdvgepapv gagllasmlv
      901 dagepasalv vchhelllad eppdrvdlll laetwrwsve vmrrntdeqa elrrriravl
      961 agrrdqprri elgrrevael glqlchavie hqtlgplava asrrlvavla epaivvrtvn
     1021 rsapmwya
//
LOCUS       WP_357651834             403 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora parva].
ACCESSION   WP_357651834
VERSION     WP_357651834.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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 403)
  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 403)
  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..403
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..403
                     /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=42334
     Region          16..285
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mpgdrvdtgr savsgatppr vaviganghg rwhrrviapl hdagrlrlva lvdvrpvedd
       61 paapvppgva vftdhramla atrpdvvvic tpphthltia rdalatgadl llekppvlsl
      121 aeheelawal taagrvaqvg fqalgsaalt altdalaagr lgtvtgisti aawqrpdayy
      181 arspwagrrs ldgrpvldga lanplahavm qclaiaeala gatpwpvaie veryrvrpie
      241 vedtavlrvr fragppvlva vtlaaeefva gevvvtgttg qavleyptdr lrlpgdvvtr
      301 rvpgrlglle nllahrvdpv gvpliaplar tapftallda lrpapeprll dgdlvttlge
      361 ggqrvrhlrg vvdvlrrsae rgalpselav pwasaayrae lag
//
LOCUS       WP_357651966             171 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357651966
VERSION     WP_357651966.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 171)
  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 171)
  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..171
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..171
                     /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=19436
     Region          6..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 myrrretrre qlvaeitnnl rrysvdaqqv shafanlhgl nptdlnalla vmdaellgdp
       61 itpgrlgeql nlssgsvtal idrleraghi rrdrdtvdrr kvllhyahqg mtlareffrp
      121 lgertdavmd rfsedelavv hrfmaemses lrthrdavra arpesprrpt g
//
LOCUS       WP_357651992             227 aa            linear   BCT 28-DEC-2024
DEFINITION  TVP38/TMEM64 family protein [Micromonospora parva].
ACCESSION   WP_357651992
VERSION     WP_357651992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..227
                     /product="TVP38/TMEM64 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23561
     Region          12..218
                     /region_name="TVP38"
                     /note="Uncharacterized membrane protein YdjX, related to
                     fungal oxalate transporter, TVP38/TMEM64 family [Function
                     unknown]; COG0398"
                     /db_xref="CDD:440167"
ORIGIN      
        1 miravrrllr qpsavrfall vlligacgll lllvphpdpe qlplvadrlg dlapvaailg
       61 galllvalvp rtfitlaaga ifgplegagy algaallaaa igftvgrllg refvaervrg
      121 rlarldgwfa rqsvlgvvtv rllpiagfgl vsygygttga rvlpflagsv iasaptafgy
      181 aaigaavssp gevnwyaaap aslgliaslv lvgqwwraer rrrrmpv
//
LOCUS       WP_357652024             372 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357652024
VERSION     WP_357652024.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 372)
  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 372)
  AUTHORS   Rosinski,J.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..372
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..372
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40536
     Region          8..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          190..289
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mmeeqgwrev grrvadarkt rglsqdelag qlglertavt kietgrrhin slelvrlaev
       61 ldrplhwfva tppaaiisrr aatadqrcdp nsdyaiedia ydlsvlvgar algpnpakga
      121 lssvgpgsed wvveavatea rrllgadags plydladlve gvglfcysls lgkaaadgay
      181 aevdglgvav ingdleagrr rstlahelgh hlfgdaysag wgtdtsaiek aidcfavnll
      241 fprkgvtqqw rslreahdlr saaiiisahy riswtaalrq lktfeliskd dyraldsrsp
      301 tradylecnl riteeleppy vatgisaaai rayrshklsa erviemlrgq ieiddlpard
      361 eipldalrge lr
//
LOCUS       WP_357652128             260 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357652128
VERSION     WP_357652128.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..260
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26944
     Region          104..257
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mraiigsigl vlvlagcggp vspmtapatp lqsrptlrnt pntpntpntp tpaqkvtgpn
       61 vsgcfttadg kiftygddlp gvitgkgavg vvityerngn vctwrplsdr lvaagyrvll
      121 yarksseypd evavamakrl skekgvrrlf lvggsigata svpaaerlgs rmagvvalsg
      181 avaedeaakl tvpllqigse ndayggakdl qrthdaatka pdnelhvikg eslhasalfg
      241 sphgpevldr iiafidrhkg
//
LOCUS       WP_357652214             475 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Micromonospora parva].
ACCESSION   WP_357652214
VERSION     WP_357652214.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=50791
     Region          27..475
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mtipyptiqp tpaiaavtpp sgaprprvtf lgtgylgaty aicyaelgye vlgfdvdadk
       61 iaklnagqvp ihepgldell rrnlaagrlr fstdiaetad fgdvhficvg tpqradgmga
      121 dlsyveasvt glaqhltrka livgkstvpv gtaewveqlv dkhtpegldv evawspeflq
      181 egfavddvlr pnrivvgvks ewangmlyaa hkgvfdlaat edrevplvvt dfataelvkv
      241 aanaflatki sfinamaevc eaaggdvtql arsigydpri gnrflqaglg fggaclpkdi
      301 rafqaraqel gagealrflh evdlinlrrr trvlqlaadl lgrrsgpagp dfagtriavl
      361 gatfkpntdd vrdapalava allqkagadv hvydpqgten arravpelty easmneavtd
      421 adlvcvltew adfrnadpva lgefvkgrkv vdgrncldpa lwtqagweyr gmgrp
//
LOCUS       WP_357652235             205 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora parva].
ACCESSION   WP_357652235
VERSION     WP_357652235.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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 205)
  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 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..205
                     /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=21187
     Region          66..180
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mpdtvitgpt aqptnpeaya alhadatall egwqptspda agardrtlal laagpvamsr
       61 qhrpghitas alvldatgsr vllclhgkfg rwvqlgghce ptdetlvaaa lreateesgi
      121 aglridpvpi dvdvhqvqcq ggsahhdvrf avlappsave qvsdeaealg wfpadqlpep
      181 laggtvqlva palaalrrsp lrlap
//
LOCUS       WP_357652245             330 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357652245
VERSION     WP_357652245.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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 330)
  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 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   5  (residues 1 to 330)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..330
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..330
                     /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=35851
     Region          <151..240
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          246..318
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkarltfsvn glaetrfavs pmweivtssr vlaaaavpep hgdwadqvrp rlaaagldrg
       61 wladmippig hlpdflnpap atacpdlsee laaieatdpe qvrrdldcla aerdgrlssr
      121 lrslhrtprt ylprivaeie vywglaiapy warirsvlea difhrgrqva eqgtaqalde
      181 lhhtvrwadg glhlvqrhca itrietgagl llvpsafawp rvltrsvase ppqlayparg
      241 igalwerrth ermealaavi grsralilte ldspasttel arrsglsaag vsqhltalra
      301 agltsthrag rsvlyartgl adalltaqkm
//
LOCUS       WP_357652275             354 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357652275
VERSION     WP_357652275.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  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 354)
  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 354)
  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..354
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..354
                     /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=37833
     Region          60..352
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mswtprrrvl lvgllallag pvlpamgkwl agvtwiwgqq fcdlpvpgls tvcadvrpta
       61 falplvavil vtvsalaalw fgaawclrpv adlagpighl gpqnlghrir prgrdelarl
      121 sraidemmer vsagyegqrr faanashelr tplavqrtli evgmartlsg eqlelltsql
      181 letnernerl iegllalses dqglrsripq rldtivegvl agyvdrarea gvtidthlvp
      241 rvvvgervll erlvtnlven gikynrpggs ltvvvsgvpa lsvvntgqpv paeavaglfe
      301 pfrrlardrt sqgggaglgl aiarsitqah dgiiaarpae hgglrvdvql pavt
//
LOCUS       WP_357652307             258 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357652307
VERSION     WP_357652307.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 258)
  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..258
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..258
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27026
     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 mnkvistdgt piaydrtgeg paviligggp tdrsvnapva dlladgftvy nydrrgrges
       61 gdtepyaver eledlqalit eaggsamvyg tsgggllaih aaahglaisk lalwevpyil
      121 pgtrpavpad yrdqqfalre qgrygdmlel ffleavlmpe efvagmkasp fwegmgatap
      181 alaydaelag dfslpteqla altvpaivid gatipwisaa aeaiatalpn prrrtltgqp
      241 hnvdpaaiap vlaeffaa
//
LOCUS       WP_357652341             301 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357652341
VERSION     WP_357652341.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 301)
  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..301
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..301
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31199
     Region          49..292
                     /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 mprklkaavv aalcitvvga gvtgcdddsm dnwdplaatt hkadagrisg tkkinvagrs
       61 vnvscsgdpa kgkpvimlmh gggdgldkma alqktlskkn qvcsydrlga gasdrpdgpq
      121 dfssigkilt gvldrvagdg pvvlaghslg gliaaryapd hqdrvkglvl mdatpptmvh
      181 ditkaipesa kgpaaevraq nlaifqgqnp eklvipdgka rsagnipvev iqhgkqylaa
      241 iptygprleq awsagqrkwl alssgsklst atdsghyiyv dqpdvavqai qrvtsaaeds
      301 p
//
LOCUS       WP_357652358             376 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora parva].
ACCESSION   WP_357652358
VERSION     WP_357652358.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..376
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..376
                     /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=40571
     Region          3..311
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrnryldllr slaivrvvvy hvtgwatltl vfpamsvmfa lagslmaasl trsgpaavgr
       61 rlrrllpslw vvavvfvpam lftglpvspr vllwlfpvad ppanhwgala lsviwylrdy
      121 lwfvfaspva fwlfrraplp tllapylllv mievgiypap pvlrefglyf gawllgfahh
      181 agmlrrlsgw llyplalala vgggawivgh pgprgydlnd nhlgnalwsa afilivlgra
      241 pagvswlgrs rlveravtvl nrraltvylw hmpfvvaltp lvdvvgwshq dpvglairvl
      301 lvfalvglvt lavgwvedva arrrpelips gsappadeaa qpcgdtsdga gttggravvp
      361 aqrvtgeeas vtlnag
//
LOCUS       WP_357652367             276 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357652367
VERSION     WP_357652367.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31127
     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          92..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mhnidpepal kgprvefgth lreyriaark rqkevaamlg wsvskismve rgqrpadedf
       61 araadtalsa dggllsrwre tvehasrwpv wlarlveieq qadtlrlwqp livpgmlqtp
      121 eyaraifrgk pattpdever nvtarlerqh vlqrdngptv wvivdevvls rpigseavma
      181 eqmahlaald ecprinvrvl prnswlttgl qgafvlasgp gmpdmayles itlsqitads
      241 ervreiksry emlhnealpr raslqlirem aeqwtt
//
LOCUS       WP_357652384             309 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate ABC transporter permease [unclassified
            Nonomuraea].
ACCESSION   WP_357652384
VERSION     WP_357652384.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..309
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..309
                     /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=33696
     Region          1..300
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtvaipsaar prrgrntlyv wlfltptvll ygaftvypia gsyiysftdw ngfdaspsfi
       61 gvanyrevla dpmfwssfrl tltfmvfavp vqvlatllla ivlnsprmpl rklfrtalfl
      121 pvvtttaivg vvmqfvfdpa sgpvnlalre aglapdgidf lgqsssalgt tiavyvwkwf
      181 gitlvywlaa lqtvpnevye aarldgagal atlrhitvpl lkpflviitl lsieaslqvf
      241 dlvltmtggg pfysteviev yiyrwafaat iprlgyasaa avlfglfvcl vgllqllamr
      301 atrrtrsaa
//
LOCUS       WP_357652388             486 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357652388
VERSION     WP_357652388.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 486)
  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 486)
  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 486)
  AUTHORS   ter Beek,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..486
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..486
                     /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=51568
     Region          39..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 msgmtrrgfl aaagtlaaat atggcgaggg ggagaggnsl twwdhqnqlq kakaevfakf
       61 akspggvpvq ytyynpakmg qalqlakqsg qlpdirtnag lnlpaaalva agwaqpldls
      121 daakaqvkds lieglhvfdg kiyafpifsh qtystvtwfn telvaragld pdappktyde
      181 fraaaravqs kgggqsygwv wnigmpirlg dqvhdlaqaa gfagggglry qtgeyayhad
      241 eyldviefli slrqdkvvvp ganswlddva rarwtagiaa yyfdgpwcpg valkdtpgfg
      301 dklgvgpilv pdagttvaty hvpqpgdywl spttkkasaa nkllsdyfat eeysrtiagt
      361 msqpprdisv vdqssahpay kkligwfkes vflapepiag nkdlqrvqve skpvtpglgd
      421 ivqgaltgdv sdvraaltkl ssdsakqrdl aiaaakskga qvslddyafp nwkprtdylk
      481 pmyakr
//
LOCUS       WP_357652497             268 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357652497
VERSION     WP_357652497.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 268)
  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..268
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..268
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28515
     Region          2..>154
                     /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 mhntlevpda rlyyevrgeg pvvvlvgapm dtesfapaae llaadhtvlt tdprginrsp
       61 lhdpgqdstp qsraddlsrl lthldagpaa vfgssggavt alafaeahpe qahtviahea
      121 plvdplddre qlyagtddli atylagdvtg awrkfmaqaa ipipddaigm mfggerdpqq
      181 vaderrwfah emratiswrp dfaalraast rvvigigeds agqlcdrtsi alaaglgiep
      241 tmfpgghigf vddpksfvtr lhavlyes
//
LOCUS       WP_357652526             609 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora parva].
ACCESSION   WP_357652526
VERSION     WP_357652526.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 609)
  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..609
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..609
                     /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=60831
     Region          11..262
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <282..496
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <405..>511
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mltrgvllgd ryrlgervat ggmgavwrgt dvllerevav kvllpslvad pefttrfrae
       61 armlaalrhp gvvpvhdvgq avlddgsqvd ylvmeyvege plsarvravr rldpattmsv
      121 laqaadalht ahlagivhrd vkpgnllvka dgtvvlvdfg iarsrhmagl taanmvlgta
      181 symspeqatg qpvsaatdvy algavayfcl agqppfhgdn plavalrhaq eepaalpadt
      241 ppavaavvar alakrpedrf gsaaelaaaa adardatlas ipvsarppwa laaptpgvaa
      301 saapavplpa apapavaatp paaamsegpa gpmsagpagp vsagpaalra aasvaaeptt
      361 apkptredti pggptnrrlp llvgagavvl valavavtvv alrlgadqgp adqpaalage
      421 tavaatdgpp pptdatttap rpsttpgasr tattgpsgsp vdpatsgdpa rtpvpggpps
      481 atassrptps rtpssrpnpy taaqacgsgy qvidsatltg gdgqrkgrvf llyhagtgtn
      541 cvvtlkdtav gaksaasayl evqgrarstd sgsfdyyagp vrasaagtcv kwggstggvs
      601 ygsgfehcd
//
LOCUS       WP_357652528             447 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357652528
VERSION     WP_357652528.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=47166
     Region          20..338
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mgsripraar lvaavvaigl aaacgggssa pagtaasgdp aqpvtltfws wvpdiqkavd
       61 afntahpgik vkletitpgp dggyakmlaa vkagnapdva qvgydslpsf lvngalqdvt
      121 eyakddaakf vdwqwqtgvf gdkvyaipqa sgpmgfyyrk dlftkwglea pktwddfaaa
      181 aatirkkdks ayistfaanq apwmislaqq agqqwfgteg dawkvtidnp dtrkmaaywq
      241 kmldgklvkt eadmsnawyk dlqtgsvvgw iggswgdaii rgnapgtsgk wavapmpqwa
      301 gaaqftsasw gggsasailk gtknpgaate favwlnsape svntllsagy gwpsvkdtsk
      361 ipnlqkddtv fpfyggqniw evfkqadaav atdwrwppvs dalyasltdn akaavqgdgt
      421 ltdafaktqq amveqlkakg lnvvtgg
//
LOCUS       WP_357652560             217 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357652560
VERSION     WP_357652560.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 217)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..217
                     /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=23539
     Region          8..>92
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          69..213
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mgkltavaiv eraleigdae gldtvtirrl aadlgvtpma lywhfknkdq lligmadhli
       61 lgfgvkggdd rpwrdrlrel veglirvlrt hpcaknvleq vdqsavpsfl avwdgalgla
      121 rtagfsaeec cliskyllqs aisiadapvh frsrhtseei aeivrvkrlg leslpadqyp
      181 nlvemagpmv egmtagfyds fgvdlvisgv ealaarr
//
LOCUS       WP_357652564             129 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357652564
VERSION     WP_357652564.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 129)
  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 129)
  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 129)
  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 129)
  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 129)
  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..129
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..129
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14107
     Region          10..129
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mttqhrdaal spseqatirq lldadrqrte triavlghdr ddmvqsaaqs asddehdpeg
       61 tstaferahi ealldqaqth lvdldlaver lhdgtygica kcgqriaier lmilpaakmc
      121 vgcaahhrr
//
LOCUS       WP_357652696             373 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357652696
VERSION     WP_357652696.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..373
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..373
                     /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=40466
     Region          8..339
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mserserten dvlvevrdlk vhfpikrgvl fdrvvgqvka vdgvdlsiar gktyglvges
       61 gcgkstlgra llqltpptag evsfdgvelt tlppgklrgm rrrmqmifqd pmssldprqn
      121 vesilteglq thgigtdrtd rrriigetld avglprwals ryphefsggq rqrigiaral
      181 vlgpelivad epvsaldvsi qaqvvnllde lqdslgltyl viahdlavvr hisdtvgvmy
      241 lgalveeaps drlyneplhp ytralmsavp vpdpdvedrr erillagdlp spanppsgcr
      301 fhtrcpwaqp trcaderpvl reiggsrvac hfaeqiasge lrphgvsaqi vrpegegdap
      361 gvvsaptepg syv
//
LOCUS       WP_357652724             361 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Micromonospora
            parva].
ACCESSION   WP_357652724
VERSION     WP_357652724.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..361
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36650
     Region          51..359
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mtirrsrlra avtggivllv aavgvvaavg fgggadggra qagsappata tvtrqtlads
       61 etadgelgyg ttrtatakls gtvtalaatg stvrrgkaly rvdneavvll ygglpayrtl
      121 apgvdgadva qfernldalg ytgftvddey tgatadavrq wqedlglaet grvepgrivy
      181 aerevrvdgh qadvgdltqp gqavltytgt srvvaveldv ddqrlakrda kvsvrlpdgq
      241 tvagtistve tvvqagtaga ngqtgdaetk ievtvavtdp kaltgfdras advtftvser
      301 rdvltvpvaa llalaeggyg vqvaeggtsr ilavttglfa ggrvevtgtg ltegatvvvp
      361 t
//
LOCUS       WP_357652728             386 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357652728
VERSION     WP_357652728.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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   4  (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   5  (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   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 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..386
                     /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=41340
     Region          62..384
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkrltirarl tliygglfll agvvllavty vlvdqrmpqp fgvklrdlpv ptatpgsgsg
       61 qniemlrslv eqaqdeakrn aleslltqgg ialvvvsava iafgwllagg alqplhqvtd
      121 tarriagadt agrglheria ltgprdevre ladtfdemle rldrsfdgqr rfvanashel
      181 rtplalnral velavtrpda saetrrlges llavnerher lidglltlad seneltertp
      241 vdlaevcaht tdqaggqapg vrvrralapa ptsgdpvlle rltfnlvena lrhnlpadgw
      301 vevrtglveg rptltvtntg pvvpgydvet mfqpfrrlsr ervvgargfg lglsivrava
      361 rahggtaeaq prpggglvvt vtlppa
//
LOCUS       WP_357652742             418 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora parva].
ACCESSION   WP_357652742
VERSION     WP_357652742.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..418
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..418
                     /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=44388
     Region          12..390
                     /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 mstaaaptip qtsvtdrlpa ldalraigav avvghhigfq taatmntpwg gwlarldvgv
       61 aiffvlsgfl lfrpwalnaa tgqarpragr ylwrralril paywlavlvc livlpqnrpa
      121 sagdwirhlt ftqiyetgql rsglsqtwsl atevafylil pliavlavgr swrpvrtvvi
      181 vcggllvtag wlallgvgwl snglhtmwlp syaawfgagm alaaahvalr tgtapaafrv
      241 lddlasapia cwaaavalma iattpiagpr dltgptaaef avklalylai atlilipvaf
      301 ggrtrakeif aaesarwlgt vsyglflwhp lvieliylid drplftgglf ntfaltmlfg
      361 liyatvsyyg verplqvlgs qrrkrpasrg qasgtpavdv aapavaastv tpaptvgt
//
LOCUS       WP_357652798             217 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357652798
VERSION     WP_357652798.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 217)
  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 217)
  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..217
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..217
                     /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=22732
     Region          5..194
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 msvtiaeell llayseeegk qlisgsqldp alggailael ainervalsg kkvsvedatp
       61 lgddeldaal triaqegker kpdwwvqrlh stklrrrlli rlaetgvlae ergkvlgvfp
      121 ttrwpeadgs veaevrqrvs gvlagaepdg rtavliavmh aakldrkafp gadkarikei
      181 aegdwagdav aktiaainsv iliaatgaai gagtags
//
LOCUS       WP_357652806             327 aa            linear   BCT 28-DEC-2024
DEFINITION  ketopantoate reductase family protein [Micromonospora parva].
ACCESSION   WP_357652806
VERSION     WP_357652806.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 327)
  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..327
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..327
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33695
     Region          1..297
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mryviigaga vggtigvrla qadrdvtvva rgahldairt rgltlrqpdg evtarlaavd
       61 rpgdqplpad tvliltvksq dttgalaawv dapvvgggta gerlplvtaq ngvaneraal
      121 rlfadvhpvc vwlpathldp gvvvangyph pgmlhigryp agaddtdrai aadltaagfv
      181 apvradvlrw kygkllsnlg nglqallgrd ipdalaervr aegvaalaaa giahtspaee
      241 kaergdlvgq rpvagearsg gstwqslarg tgstevdhln geiallgrlh gvptpanvav
      301 qravrraare riaagafpla elekmia
//
LOCUS       WP_357652837             160 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357652837
VERSION     WP_357652837.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 160)
  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 160)
  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..160
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..160
                     /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=17329
     Region          11..>109
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 melitlqdvp lgrllvvagh lvgqrwnryl aeehgltqag mitlmtlarh gelphrkvae
       61 kgfvrpatlt givdtlerdg lverqrddsd rrsirlaitp agrervaalg almhsgrplt
      121 svdadpakaq virefllevi gsgddprmtg rptgaedpac
//
LOCUS       WP_357652896             871 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Micromonospora parva].
ACCESSION   WP_357652896
VERSION     WP_357652896.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 871)
  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 871)
  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 871)
  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 871)
  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..871
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..871
                     /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=89038
     Region          36..843
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mttiggrdgi lvdpvdrdvs vgldaaeaaa rlratgpntv aapprqpvta rvlrqltdpl
       61 valllaaaav taalgdypdt aviflvvlvn tvigvvqevr adraiaaldq laaptarvvr
      121 dgrelvvpaa divrgdlvrv eagdvvpadl slveasrlhl desaltgesv tvgrvagdea
      181 lagtvvtigr atgtvlrtga asalgrisal vagtrpagtp lqrrlsalgr vlglvavvvs
      241 glvfaigvvg grpvvdmait avslvvaavp eslpavvtla lalgarrmaa ahaiprqlha
      301 vetlgsvtvi asdktgtlte grmavqqavt gdgarygvtg sgyaptgtvh rdgeavavpd
      361 rlrqlaragl lcndaalspp dderpewgav gdpleaalva faarcgldpq atrtawprva
      421 ehpfdqaqrr mvtvhrscdq rylvvckgap esvlgaplld atdeeiaelt stahrlateg
      481 lrvlavaaal tetvpdpasp tglrpvglva vgdplregap rvadsfdtag vrlllitgdh
      541 patataiggr lglwragdpl angdddeaah pdtrifartq peqkldiiag lqargevvam
      601 tgdgvndapa lrradigvam gggtevarqa adlvlvdddl stvanaigeg rriydnirrf
      661 lryalsggva eilvmligpl fglpvpllpa qilwinllth gvpgvalgae paepgtlrra
      721 prspqesvlg aglgrdvllt galiaavvlg agvlaahrel pwqsvvfvvl glaqlgvala
      781 vraprpagtr sgnpgllvav avsallqvgg vllaplrdll gtealtpsvl lacaavsvlp
      841 glvlrltrss atdadrgddg tngprprtvr p
//
LOCUS       WP_357652904             361 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Micromonospora
            parva].
ACCESSION   WP_357652904
VERSION     WP_357652904.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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..361
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..361
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=38747
     Region          64..238
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          161..344
                     /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 matllaigta kglflatstd drrsweitgp hfpmtgvyav aidtrrstpr llagmtsshf
       61 gpsvatsddl gaswdepdqa pvafpadtgv slgrvwqltp agpdepdvvw agtepsalfk
      121 stdggrsfel vrslwdhphr pqweagfggq avhtvlphpr drarllvams tggvyrseda
      181 gaswtpgntg irayfmpdew pefgqcvhkv ardagnperl yaqnhhgvyr sdddgrtwss
      241 iaeglpsdfg fpmvahpgra gtvwtfplva dgerfptdhr crvfrsadag gkweplsvgl
      301 pegpfypavl rdamcaddas pggvyfgtrs gsvfasrdeg dswsavaahl pdvlcvraae
      361 v
//
LOCUS       WP_357652915             951 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357652915
VERSION     WP_357652915.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..951
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..951
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=100750
     Region          <4..925
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mfetrrplvg rtaelahlsg lldarrqwvf vsltgepgig ktrllgafad larergimai
       61 agratefers apygivqdal adahqhpela ghldglrall sretgtgdla gldrhrrfre
      121 mrqgvermga ssrllvlmdd vqwaddasve vidyhirhpp ntsavivlac rtgelprgla
      181 rsltsanvvn lplgplsaae adtmlagqsa ppgrrqlsrp grrrlyersg gnplfleila
      241 tlpdtpaadl aevtgagala gvkgsgvlte vtrtdaldrl ivaelagldp drqlvaqaaa
      301 vagddlaaaf vaavsgldlp tveaaldelv rrrvlgtagr alvfrhplvr aaayqlagps
      361 wrraahrraa ehllargasd vrravhmeha igvgdadgaa llvsaagavs vnapataarw
      421 fraaleaspa datpelrvsl aaalgvsgrl eeargllhel vregganrdq avgllsamqr
      481 slgrleeara lltgelarvd dsagrpsllv elaaidllqg qwdsaadnas qaldqpdqas
      541 pqrehtsaar pgtsasavtl lavaelyrcr fpdgyrllar aktfmdaltd relcddlgvv
      601 aplawgefiv dhhddalrhl arglqvardh grdnvvpllh aaramvrsal geieaalada
      661 eeaeeiarhl gsaemlafah vvksrpllwq agpeaaaplv eevlhgpgmr sawwrtiadd
      721 vvsevlmsvg rtedcrrfla arvggdpsgv gpgaasvfar raraeaargd mtaagqwyer
      781 avavvasgap parsadveaa raalamaadr pheaeaaare aveclvtarl pvgegfarml
      841 laevsadagd irtaqeqlgq akalfarvga awpaaqagrr qrgtvahgag grlsererei
      901 velvgegltn rqigerlyls prtvethlah vfrklgvntr aalarrsagr w
//
LOCUS       WP_357652950             822 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357652950
VERSION     WP_357652950.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 822)
  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..822
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..822
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=88334
     Region          23..819
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          611..639
                     /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"
     Site            order(652,655..656,659..660,662,692,695..696,699..700,
                     702..703,732,735..736,739..740,743)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          690..720
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          731..758
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          771..798
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msdqwlpsga hhtshgspga felaraaaea qtlpelagvl rqlrrrearq qgetlltyrq
       61 laaktgwsrg iigeyfagni lppperfdvl irllgatpae qgvlatardr veerrrrpnr
      121 ehaatgrsvv raraggprta ttsprfpvpr qlppalpgfv gratqlaqld aecagtvagg
      181 ddavapvtvl tlsgtagvgk ttlavnwahr vagrfpdgql yvdlrgfdst gtvvtavevv
      241 rgflealevp peripthlpa qvglyrslla grrmlvlldn ardadqvrpl lvgspsclvl
      301 vtsrnrlagl iaadgarpig vdllstaeaw qllarrlgad rlaaepqavd eiiercarlp
      361 lalavlaarg aekpefplav laaelraapr pldsfdagda gtdvqavfsw syrsltpaaa
      421 rlfrligchp gpdigfaaaa slaglprdqv prllaelaha hlvtehapgr fgahdllray
      481 aaeqverlep aparraairr gldhylhtah aaalllqpgr dpvtlaaaap gvvpeeisdl
      541 aaalawftae ypvllaavah arrtgfdgha wqlawtlvdf lqrrgrwpdl avaqrnalag
      601 aqrsgdrpgq anahrdlarv lsrlgrvnea arnyrqalti faelgdhtgq arthrafgam
      661 ldglgrhaes leqseralal yrsaghvage asarnavgwa yaqlgryppa lshcrealal
      721 lrttgdrhge antwdslgfi harlgehraa idcfqralgl yrrvsdryde adtlsrlges
      781 rqavgdaaga artwrralgi lddlghpdae rvrdllvrat qr
//
LOCUS       WP_357653029            1074 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Micromonospora parva].
ACCESSION   WP_357653029
VERSION     WP_357653029.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1074)
  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 1074)
  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..1074
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..1074
                     /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=112142
     Region          112..570
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mrrrqrralt agvlatalvt agltaqpana qptpptpgta gtftlitgdr vsldaagrpq
       61 iqrgpgraam rfvsnredgh qyvipvdamp lvrdgrldrr lfdlttlaef gyddraaelp
      121 llvaypenta arartattgg agrvradlpa ahalavradr ddrvtlwasl trgtpsartl
      181 tagvthiwld gkrmvsldrs vpqigapaaw qagfdgtgvt vgvldtgida nhpdfaghlt
      241 evrdftgggd psdsvghgth vastivgsga asggryrgva pgakllvgkv cattecqdsd
      301 iitgmqwlap rtrvvnlsvg gddtpgldpl etavqelshq ygtlfvvaag negkpksvss
      361 pasaddalav aavdaddqra yfssrgprig dnhikpeisa pgvdivaaap ggdyatmsgt
      421 smatphvagt aailagqhpd wtgpqlkaal mdsakptged tlyeqgagrv diaravaqpv
      481 aadiaaidfp vqrwphadds pitqvvgyrn tgttavtltl aiapapagml tvrpttlvvp
      541 aggraeavit vdtrvdapdg vyqgaltatg agdlrvrtpf alnreiesyd vrldhtgrdg
      601 kpateyttva anlatgefst lavtpgggvl rlpkgryaly stihegsvst llaqpvldvr
      661 gpvtealdar gakpvaltvp qhdaaptsin vsanwddglr ypgvqlsgls fadlffgrig
      721 pavtapefta tlgvglarpg rdgtfrnspy tydlayvrqg dmftgltrkl spknlatvra
      781 tyrsqssttt atrfhrasgp ggsgpigsnt pvdlpfkgve yyntdggvvw tstflegdnl
      841 taqdstfaag rtytqtwnaa pfgpsvaqap tlsplgyagr dgdtisiasl plfgdasgrp
      901 asrddqpvri rllrdgkeig ssdspwaeft vpagratyrl eaavtrgapd tlstsvsvaw
      961 tftsahttsp erlplttarp tpvlddtnta rigrvmafpv tldrqagska tpnrtlsvsa
     1021 sfdggrtwta lpvlrnvavi shprragfvs lrlaatdtag ntvtqtiqra yris
//
LOCUS       WP_357652980             113 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357652980
VERSION     WP_357652980.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=12110
     Region          26..103
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(31..32,36..38,54..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"
ORIGIN      
        1 meplqilecs pplareplda eqaagvarvf kalgdpvrlr ilsivashag gevcvcdind
       61 afelsqptis hhlkvlkdvg lltaerrasw vyyrlvpeal aelsgllntp vtv
//
LOCUS       WP_357653145              58 aa            linear   BCT 28-DEC-2024
DEFINITION  CopG family ribbon-helix-helix protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357653145
VERSION     WP_357653145.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..58
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..58
                     /product="CopG family ribbon-helix-helix protein"
                     /calculated_mol_wt=6412
     Region          4..>48
                     /region_name="PutA1"
                     /note="Predicted transcriptional regulator, contains
                     ribbon-helix-helix (RHH_1) domain [Transcription];
                     COG3905"
                     /db_xref="CDD:443111"
ORIGIN      
        1 msnkpttvrl tdeqkaglda igkredrsrs wliskavdey iarhlrsekt ttnggepq
//
LOCUS       WP_357653086             111 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357653086
VERSION     WP_357653086.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=11844
     Region          12..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdsdkeplar aeaeeyaswf kaladatriq ivsllarrrt pmnvgeivaa sgvgqstvsh
       61 hlkilaevrf vlvekqgtss lyrineacvs cfptaadvvm gkpvpaaptc e
//
LOCUS       WP_357653168             164 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357653168
VERSION     WP_357653168.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 164)
  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 164)
  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..164
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..164
                     /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=17503
     Region          7..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mnvvniddpr ltamgllsev qaglaarmqp vfgaaglsei dfetllrlgr spreslrmsd
       61 laaqtglsts gvtrvvdrle rdglvarvac avdrrasyat ltdagrekle vvlprhledi
      121 dkcltsllsa keleaflttl rtvrdvvrpc atagavegec paqp
//
LOCUS       WP_357653205             277 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357653205
VERSION     WP_357653205.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 277)
  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..277
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..277
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30678
     Region          1..263
                     /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 mtvlevpgac lyyethgsgp lliliagasg tadsfrmlag hltahytvai ydrrgfsrsr
       61 ldgpqdyerr letdtddvrr liehlgdepa tvvgvssgav ialqvltrhp avvrrlvpye
      121 ppavrqlpdg qrwvdfffgv ydlyqrsgie pamaqfreet faesdrqama hapknatnaa
      181 ywfehelrqy plvdldldtl tahadrivpa sgrespgypc yevnvelgkk lardvielpg
      241 ghigiitqpa qfatelihal rraeqedevd isqshgs
//
LOCUS       WP_357653248             460 aa            linear   BCT 28-DEC-2024
DEFINITION  phenylacetate--CoA ligase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653248
VERSION     WP_357653248.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 460)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..460
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50761
     Region          11..421
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mkesvprllq darrtrrhhe watvqrrrla eiveyartrs pyyrdlysgl ppraddsatl
       61 pvtelpvtdk kalmahydqw atdrevtlar arafaadpql aggrfldryl lvttsgttgn
      121 paifvkddrd iavnyalsmr mmgswldlad itrilagggr maivaatngh flvsagaarm
      181 rahrlqrkai rlfsvhtpld alvealnqfr palllgygsv lnmlaaeqes grlriapvvv
      241 epagetltsg dyqrmarafe akvrdtygas ecpfltegca ygwyhvnsdw alvepveady
      301 sptppgrrsh tvlvtnlanr vqpilrydlg dsvlqrpdpc pcgnplpaiq vqgrvanvlt
      361 fatgrgevvi aplmlntlvd rtpgvqlyqi vqtspatlri rmrpspgads etvwravrdg
      421 isglladhkl dhvileraee ppqqspggky raviplkdfa
//
LOCUS       WP_357653282             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653282
VERSION     WP_357653282.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 190)
  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..190
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..190
                     /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=20385
     Region          11..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meaqvtdarp rdraatrqrl leaarmlfge ygyeqvtvrm iasaadania lvgryfgsks
       61 glfgevlage ptvravvegd raglprrlae yaagrmshdp etpilrsler sagdpeiqal
      121 vrerlhtavl epiaallggp dahtrarmat avflgigsvr rligpetpsp advdrltavf
      181 elclgletrp
//
LOCUS       WP_357653322             237 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653322
VERSION     WP_357653322.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 237)
  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..237
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..237
                     /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=26373
     Region          12..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msanaerlrd prqraeratr ildvaadlll rhgyrrvtid dvaegagigk gtvylhwktr
       61 eqlfsvvfar evlyamdelr qalrqepetc llrnfarayf laitdrpllr gflladphll
      121 gkltsspdta rderhgtmar dylnllteyg llrddmrade igyayqatfe gflraegdap
      181 tggpeqradl lartvqrafe seaaipdarl rdlaaatvtl lsglidadra esgipea
//
LOCUS       WP_357653335             561 aa            linear   BCT 28-DEC-2024
DEFINITION  murein biosynthesis integral membrane protein MurJ [Micromonospora
            parva].
ACCESSION   WP_357653335
VERSION     WP_357653335.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Kuk,A.C.Y., Hao,A. and Lee,S.Y.
  TITLE     Structure and Mechanism of the Lipid Flippase MurJ
  JOURNAL   Annu Rev Biochem 91, 705-729 (2022)
   PUBMED   35320686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     gene            1..561
                     /gene="murJ"
     Protein         1..561
                     /product="murein biosynthesis integral membrane protein
                     MurJ"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=56389
     Region          20..>399
                     /region_name="MurJ"
                     /note="Lipid II flippase MurJ/MviN (peptidoglycan
                     biosynthesis) [Cell wall/membrane/envelope biogenesis];
                     COG0728"
                     /db_xref="CDD:440492"
ORIGIN      
        1 mnrpaplaga grlagaaali avltvasrla gfgrtavftw vveqsdlggm yviantvpni
       61 vfeivaggal aslvvpllag avaaqdrrav aattgalltw tvsllvplav lvavfadpii
      121 slisegrsaa elaagarmlr vfapqlplyg igivltgvlq ahrrfawpvi apllssltvv
      181 vvyvafgaaq grgvsvaqvg rsgelllsgg ttlgvvvlsl slliplrrlr lrprfgyaft
      241 ddarariggl atagavtvaa qqvallvvln rvsggptgsp qvfnlaqaiy llpwavlavp
      301 lavasyptla tasaagdedg yrrtlssavr gvllfsclga aaligtaqpv aalfypdnpa
      361 steaaiigfa pgllgygvfa ilsralyarg dtrpatvait lgwlvvpava lplaallpta
      421 drvlavtsan svgmlvlgal lllavlrgag rralagagra gaagglggvl aglagwgltg
      481 wlapsdggtp tiaaafgqgm lsgvlvgvvf lavvwfvdrr dvqpllagvl rrlgrrgpsg
      541 gaptpgadaa ergdgketat r
//
LOCUS       WP_357653342             400 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357653342
VERSION     WP_357653342.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..400
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42745
     Region          21..380
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mirtrrtava vlltltlpls vatavsmslp aaaasstnrs dvrlaiphps gqydvgrdtl
       61 hlvdgkrrdp wvpragarel mvsmyypagt ggsaapymtm dearlllkgq kldtlfkael
      121 ladtrtnard garpvggrhp lvvlspgftl nratlttlae elaskgyvva lvdhayesyg
      181 ttfpggrtlt cvacetveqa psdeeekqll gkaaagraad isfvidqltr tggqapvwkr
      241 wkmidpqrig aaghslggna aasvmaadrr vragvnldgt ffapvpnagl gkrpflmlgt
      301 kaqhspdstd tswprdwrrl dgwkrwltvt gsghftfidl pilggqagit dptaplpgtr
      361 sgeittayvg affdqhlrge hqqlldgpst anpevlfqnp
//
LOCUS       WP_357653379             204 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653379
VERSION     WP_357653379.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..204
                     /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=21222
     Region          16..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 merreradaa rnrrailaaa eellrehppe evsvervala agvgkgtvfh rfgsrvglmq
       61 elmserahtl eqavvegppp lgpgaparer lvafldavva matrsaglia aheharltqk
      121 agggtrlanp iyvswhrhvs aliaearpdv daelaghvll gtlhtepiss llhagesarv
      181 aatlgdlarg llgdaggplk aggg
//
LOCUS       WP_357653403             256 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357653403
VERSION     WP_357653403.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..256
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..256
                     /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=27375
     Region          <32..139
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 merqlishia hadhpiaspi seanllrllr raklpsgari ldlgcgaavw svrllelygd
       61 atadgvdlsd agfadarrma aeagvadrlt lhhgsattft aaepydlvlc vgathafggl
      121 tpsmeaiggl lapgglalvg egfwerppgr eieaeigeya dlpgtvaqae sagyhtvyah
      181 vsergewydy ewswtgtlid walrhpgddg daamaaaleh rkmwldgyrd llgfvtlllr
      241 rccsdapdgr rvtegv
//
LOCUS       WP_357653432             425 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653432
VERSION     WP_357653432.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 425)
  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 425)
  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 425)
  AUTHORS   ter Beek,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..425
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..425
                     /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=45501
     Region          6..332
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mnfssrkkiw tvallaatvm tsagacgggd kadsgkvelr fsywgsdsrq klteqvikkf
       61 eeknptinve gdfsdfnnyy eklatkvaan dapdvmsiei rglgeyagrg aladlagkvv
      121 ttdldqqala agnidskqya ipsgvntfsm lvnkatieka kqkvpddksw twddwinlak
      181 qisasgggit gaeynynpaw lqifaaqrge klydgkklgv spetlkawwg ihqqliqtkg
      241 spdaakssel iaggveqspl gtnagatgmw wsnqlggltk asgqeltllr mpkvkeatts
      301 gmflqpsmfy tiaaksehpa eaakfidfmv ndpdaasill sdrglpinak vlatvkdklp
      361 avdqktlgfi devrselspi aappkgalqv ddilkrvtee vvfakttpda aaqkfltean
      421 aalag
//
LOCUS       WP_357653448             324 aa            linear   BCT 28-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653448
VERSION     WP_357653448.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 324)
  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..324
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..324
                     /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=35367
     Region          160..265
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mlitvsqahl sgenemsvds rrdierypsq tglrgfirrr pllsffvlan lmswaawtpy
       61 ilsatglgil dftmpsvlgt tqfvgvlpga ylgpifaafv vtavadgkag lrrwvgrmmk
      121 wrvswvwylg tavgvpaaii vaglamsnnd ihvppvavlv aylpslllqm vttglaeepg
      181 wrdfalprlq rkfgplgatl ilgplwgfwh vplflsewgg wpnltwltvg efiafasifs
      241 vivtwvfnrt geslpvvmvl hvsvnnfmsl ayanmfpsia taqqashvtl lasstvaiii
      301 lvatrgrlgy rkveepapea thqs
//
LOCUS       WP_357653496             149 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357653496
VERSION     WP_357653496.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 149)
  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 149)
  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..149
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..149
                     /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=16736
     Region          1..144
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtrwldddeq rtwrdfltat qlvnealdrq lqreagmpht yymilvalse apersmrmse
       61 lanraqssqs rlshavarle ergwvrrrpc eadrrgsfaa ltdegfaala aaapghvaev
      121 rrslfdiltp eqlgqlaeic aavrntlep
//
LOCUS       WP_357653397             300 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653397
VERSION     WP_357653397.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 300)
  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 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   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..300
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..300
                     /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=32049
     Region          2..292
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrvgvtgasg fvggavcraa vargwqvygf grrateipgv tyriwdltgd erpeldldal
       61 ihcagsvtdw gppaeiwran htgtanamaa fpyarfvhvs tasvydprrp tvmareheap
      121 vsryvnayga skaaaerlve gravilrpha vhgpgdttll prvlravrgr rliavgdgrq
      181 rvsltsvsnl aqacllavtg plgtynvtda epvvlddalr avlrekgida tplylprhla
      241 hglavisetl ahalatisep rltryavghl avertldita arerlgyaps ptsfrgaasw
//
LOCUS       WP_357653541             840 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Micromonospora parva].
ACCESSION   WP_357653541
VERSION     WP_357653541.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 840)
  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 840)
  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 840)
  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 840)
  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 840)
  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..840
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..840
                     /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=91934
     Region          117..838
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mshdvvppae gtvhptgdad gsvtdrtgda parvtgtgng sgrasgespv rptsgppsae
       61 aspgadgvvv pfpidagidp spsggfglsn aptgrrvrar larfnapwqt sqvsevlepl
      121 iashrdnhpk adarllqraf dtaarwhsgq yrksgdpyit hplavatilg nlgmdtttlv
      181 aallhdtied teytldqmra dfggevallv dgvtkldkvk lgdaakaeti rkmvvamakd
      241 prvlviklad rlhnmrtltf lprpkqeqka ketleilapl ahrlgmntik weledlsfgt
      301 lfpkryeein rligehqpqr eallrqvtqk vqtdlkaaki kaettgrpkh lysiyqkmiv
      361 rgrdfndiyd lvgvrilvdt vrdcyaalgv ihanwqpvpg rfkdyiampk fnmyqslhtt
      421 vigptgkpve mqirtyamhr taefgiaahw kykehkgtqi vgppahidem twlrqlldwq
      481 reaadpsefl dalrfdlssq evyvftpkgd viplptgstp vdfayavhte vghkcigarv
      541 ngklvplest lsngdvieif tsksetagpt qdwlgfvksp rartkirqyf nkerreeaie
      601 agkdaivkam rkqgmplqrm ltsdalmsia rdlhladvas lyaavgdsqv saqsvvqklm
      661 aayggeegaa ediaetavat rpprsrqsss dpgvvvrgvs dvwiklarcc tpvppdsvfg
      721 fvtrsggvsv hrddcanaed lraqservve vswkltsast flvaiqveal drhklladvt
      781 rvlsdervni lsatvtttrd rvavsrfsfe madpkhlghl latvrkvdgv fdayrvtsga
//
LOCUS       WP_357653560             205 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357653560
VERSION     WP_357653560.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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 205)
  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 205)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 205)
  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 205)
  AUTHORS   Rosinski,J.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..205
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..205
                     /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=23064
     Region          18..91
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mendgdapra alrevridkr qvrvlahplr mrlvgalrvk gpatattlae llgtntgats
       61 yhlrqlaevg lvvedpdrgs grqrwwqaah dvtnwepsdf dddpdaraai ewiqgdqvrh
      121 lvehaerwfa tqhewspawr dgfgmgdifm tipparleel kaevwqvler yhreaepvdt
      181 aapvdpearp vqvflaaypl ldgpq
//
LOCUS       WP_357653663             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653663
VERSION     WP_357653663.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 191)
  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 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..191
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..191
                     /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=21000
     Region          33..173
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 memtviascp fgqtkwidrl vkffgmlrrm gnredllaga krcliergwa rttvrdiasa
       61 agvshaaigy hfgskdallt qalvqavdel gdelarraps dkpeqrwqtl idsftthral
      121 wvaqleaavq aerspevreh lakgqrqgre glggsvplal ltglmlqwlv dpdhapsgad
      181 vitelrslrh l
//
LOCUS       WP_357653618             114 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653618
VERSION     WP_357653618.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11457519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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]"
                     /calculated_mol_wt=12730
     Region          1..77
                     /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 msasddrssa wtflthharv lleiarnpqa rmrdiaagig iteravqgiv tdlhqagyls
       61 rdrvgrrnhy sinldehfry pteaglpirl lidmftqhdl pgrpaspqpp epqp
//
LOCUS       WP_357653720             166 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family winged helix-turn-helix transcriptional
            regulator [unclassified Nonomuraea].
ACCESSION   WP_357653720
VERSION     WP_357653720.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 166)
  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 166)
  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..166
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..166
                     /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=18433
     Region          24..162
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mneepqdevd rlvaawrter pdldveplqv lsrvsrlakh ldrarraafa ehalepwefd
       61 vltalrragk pyelspgali ratlvtsgtm tnridrlaqa glvrrrpdpe drrgvlvslt
      121 esglarvdaa fagllrrehd llaglpltdq rtlsallrtl lapfds
//
LOCUS       WP_357653762             350 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653762
VERSION     WP_357653762.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 350)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 350)
  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..350
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..350
                     /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=38230
     Region          105..347
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          263..345
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mvnhamhdgg avsdtmkgtv sphlarllvr agiaagldrs rlvgvpglav ldedgiript
       61 atilriwelv sgpvwaaggs dkvmelwqpg algvwdylfs asntlgdafr maarrftaia
      121 dpadrltvtr hddgvtvawq gpyrdypeya miaefvpyml lmlassgagr rltpvwvglp
      181 rrpatapkrl aalydtrrve yeaahpsvtf aeadidarlp radpalaail dnhahlstaa
      241 arpvrgwldr fhaalesava dgppgldqva qrlamsprtl qrrlrdegss wreeleklrq
      301 rrvdrllret tlsvesiaar vgftdpralr raihrwyghg paairasgpt
//
LOCUS       WP_357653767             260 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357653767
VERSION     WP_357653767.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 260)
  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 260)
  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 260)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 260)
  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 260)
  AUTHORS   Rosinski,J.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..260
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..260
                     /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=29361
     Region          2..83
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          116..249
                     /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(117,119,121,130..132,134..135,140,148,155,157,159,
                     161,170,172..173,175,178,184,186..187,202..203,205,207,
                     217,219,221,223,228..236,238..240,243)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mslearamds vfkaladptr rllldrlreh ngqtlselce rlnmarqsat qhldvleran
       61 lvtvvrrgre rlhylnpapi heieerwisg fdkprlrals aiknqaeeya mttaptyvyv
      121 tyirasaeqv wqaltdadlt arywghanvs dwqpgstweh rrvdgsgvid vvgrviktep
      181 ptrlvitfdd apdaesprep svvtflveph qdivrltvth enlpnqemlt gisqgwpavl
      241 anlkslletg evlpqapwdm
//
LOCUS       WP_357653775             296 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653775
VERSION     WP_357653775.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 296)
  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..296
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..296
                     /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=32238
     Region          11..>203
                     /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 miyvktpltr eireavaltw gvtgegeger lhggeesaay rldghvirvg pawraaaese
       61 wchaiarhaa aslpeavapl paaegrtviv mggrpiscwp yvegawpdsg ipaqreagar
      121 llarlhrsla gfrpgprpvp afqesglygd ppqdaaelad pdldrwlaaf haehpvrhpl
      181 hgdyytgntl ardgrivavl dwdetfvgap elelaaaale wgddlagpse efvaayheag
      241 gtaarldgks laqlvrhklr rehayfhkav rsgvthdead veyhrgrvel fhrlrp
//
LOCUS       WP_357653808             202 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653808
VERSION     WP_357653808.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 202)
  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..202
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..202
                     /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=21341
     Region          9..185
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msdtepgrrr daagtreeil gaavvefteh gyaragvrqi aeragvtamm inryfgskeg
       61 lfaeavdrsf glptvvaqgp dglasavars laertgpeae rldpfllmlr sasdpvagpi
      121 vrrgieahvg arfaqliggs eadvraqlgl alvsgiwllr avvgtgalva vdnerladll
      181 armldpitre sdvepdaehr sd
//
LOCUS       WP_357653891             233 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357653891
VERSION     WP_357653891.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=25881
     Region          4..198
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 msevtrpsls daltermlel irtgghrpgd rlpstrelsq rfavttptlr ealrrleatg
       61 aiemrhgsgi yvgadierlv lpnpnmremh aaqllellga riviepplaa maaaratgee
      121 lvalqrvlea aarhlrgqda elhdtnmtfh ratarlagns vlhevvdsll tvhgpeqrei
      181 lqifddrrrd ydehlailea ieahdaaaae ermrahlvdv ktvieqrlqh ppk
//
LOCUS       WP_357653911             536 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357653911
VERSION     WP_357653911.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..536
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58603
     Region          16..521
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mahvevghlt yvlpdgrpll ndvsfrigeg vkaalvgpng agkttlmrlv agdlqpvags
       61 vassgglgvm rqfigsvrdg stvhdlllsv appavrqaae rleraelvmm erddekaqmr
      121 yaqaitdytd aggydievlw dtctvaalgv pydnvkyrdv atlsggeqkr lvleallrgp
      181 dqtllldepd nyldvpgkew leqalretpk tvllvshdrq llanaadriv tvesgniwih
      241 gggfatyaea rkarnerlde lrrrwdeeha klkalvnmlk nkaryndgma apyhaaqtrl
      301 rrfeeagppe etpsdqnism rlkggrtgkr aviceglelt glmrpfdlev wyaeriavlg
      361 sngsgkshfl rllageqigh sgvarlgarv vpghfaqtha rpdllgrspv eivmneharl
      421 kneamkalar yelagqiaeq rfdtlsggqq arlqilllel sgatllllde ptdnldlasa
      481 ealqagldaf agtvvavthd rwfaadfdrf vvfgadgtvy essepvwdea rvvrpr
//
LOCUS       WP_357654023             127 aa            linear   BCT 28-DEC-2024
DEFINITION  RidA family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654023
VERSION     WP_357654023.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..127
                     /product="RidA family protein"
                     /calculated_mol_wt=13166
     Region          1..126
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mtrtvitten apslpaplsq girkgpvlqv sgqlpfdpdt gevvgtsvae qtaqtlrnvn
       61 avlkaggadl advvmlrvyl tdpahladmn eayaaavgep fparttvymq lppgllvevd
      121 alavldd
//
LOCUS       WP_357654102             202 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654102
VERSION     WP_357654102.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 18527488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..202
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21112
     Region          15..81
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          103..201
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mveqdgnaae pqhgddlaga fggnvrrrre eagltleqls tqssvsraml skvergeksp
       61 tigvasriah aldaslsdli gapaaaasgv aivmrkndrp vfrdpetsfe rhmvsaapga
      121 ggaemvvhyl paqvstgllp ayppgtekql vvlegtltva iggisetlnt gdslffqada
      181 dhgfanrtna pceyimvisr rt
//
LOCUS       WP_357654107             241 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654107
VERSION     WP_357654107.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=26216
     Region          24..>241
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtdfapadgd pagrtlllle llaarpswsa sdlagrlevs trtlrrdvar lqrlgytves
       61 rpgpgghyal rpghrmpplv fqddevvalv aalrmvegil agdaahrala klsqvlprrl
      121 rtvldaaaag senvggelgg vepstlavll raadqdlvlr fgyrdrhgav srrrveavrc
      181 lyargrwyvl ahdldagdwr vfrldrvrep eegepgsgdr grpaedlatw latdfgrrse
      241 g
//
LOCUS       WP_357654121             364 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654121
VERSION     WP_357654121.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..364
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=38781
     Region          19..331
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mmsrtvvivg ggyggsvvak aldaeadvvl idprdafins agslraltqp dwahnmffpy
       61 dqwlrrgtvv rdravsvdpg gvtlasgrrv eadflvlatg ssyaypakpa sdstpdvldd
      121 llrthkelag servlilgag pvglelagei kevwphkhvt ivdpaedllp afpaemrdel
      181 rrqldelgid lrlgaglsap pttgagqagt ftvtttasee itadlwfrah gvrinsdyla
      241 dgrlttrnpq gqvpvtetln vrgyehvyai gdltdvaeak magyamqhge vvaqnilaqs
      301 rgeqpattyr plphpmillp lgprggvgql ptpdgpavvp aetvsaykga dlftgrfteq
      361 frav
//
LOCUS       WP_357654137             373 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654137
VERSION     WP_357654137.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=39734
     Region          1..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 mqktiaivga glggltlarv lqahgvaati yeseasattr aqgglldihv etgqvalraa
       61 glydefltlv rpgedakrvv drhgtilfdm padpgsarpe vdrgelrrll idslapetir
      121 wghklasirh rveggydltf vdgsatradi vigadgswsk vrplltpakp lysgicfiei
      181 alasggqdcr asvaaigsgt lmavapgkgi iahryadghv hgyvalnkpe ewmrsidfgd
      241 psaglrqlad efdgwspllt afvtqsdael wlrpiyalpv glnwdrvpgv tlvgdaahlm
      301 spfageganl amydgadlas klveqpdvev altgyeerlf lrssdvagrs aknleiffgr
      361 eapqsvvtlf dhs
//
LOCUS       WP_357654187             178 aa            linear   BCT 28-DEC-2024
DEFINITION  RICIN domain-containing protein, partial [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654187
VERSION     WP_357654187.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19228254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         <1..178
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <1..37
                     /region_name="XynA"
                     /note="Endo-1,4-beta-xylanase, GH35 family [Carbohydrate
                     transport and metabolism]; COG3693"
                     /db_xref="CDD:442908"
     Region          47..172
                     /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(64..67,77,79,82,86..87)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(73,105..108,116,118,121,123,125..126)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(92,96,98,101,105..107,116,118,121,125)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(146..150,159,161,168..169)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 twgvrdsdsw lganatpllf dgngnkkaay tavlnalngg sttpppgggd agqikntasg
       61 rcvdvpnsst tdgtavqlwd cngqsnqqwt qstagelkyg dkcldaggtg ngakiqiysc
      121 wggdnqkwrv nsdgtivgvq sglcldavgg gtgngtglql ytcwggsnqk wtynagta
//
LOCUS       WP_357654171             311 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654171
VERSION     WP_357654171.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..311
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33643
     Region          26..311
                     /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 mtpvtqrqpf gegsparrsq atdrvrhrtv qagglevpil eagsgplvvc lhgfpdhaas
       61 wtgildrlaq egywavapaq rgywpggaap dgsyritstg qdvlalieal greqadligh
      121 dfgaaaayaa tsldprrvrk lvtmaaphgr qlmtslvtdg dqqrrswymf ffqtamaeaa
      181 velddfafid rlwrewspgy elpdaeraal ketlgapgvl teilgyyrql ftppadeaaq
      241 alearafgal tvpslylhga ddncfsvels dgmddlfang lerivipgag hfphleqpkt
      301 vadhilgfln g
//
LOCUS       WP_357654231             370 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654231
VERSION     WP_357654231.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..370
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36608
     Region          36..337
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mtngalsvll lggvafayaq lgtgqvaset ttrtvtagrg tvtasvsasg avessksral
       61 tfgtsgtveh vyvkagdkvr kddilarldd aaaqeslsaa ratynsavdd gtstaqlyaa
      121 yikarnayre aqrtaaatvl rapfggtvta vngavggssn gsgtssgtsa tqstgqsgqs
      181 gsqsgsgsgs gfidladtgk lqlvgtftes dvsklkvgqa atvtfdalpg vtatgkvtqi
      241 epvaatsnnv vqypvtisft kvpkqvrlgq tttvevvtge aenvisvpst aistsggqnt
      301 vtllkngqqv rtpvevgvqg aslteiksgl segdqivppa ttttgtgnnq rqggfgggfp
      361 ggggvpgggr
//
LOCUS       WP_357654298             205 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654298
VERSION     WP_357654298.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 205)
  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 205)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..205
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..205
                     /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=22920
     Region          18..196
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mrsenepsgq karsfieear raqivasaie viaesgfaga slariaqhag iskgvisyhf
       61 agkdelmeev vnqvysaide hvrvrmegqe satdllrtyi laiaehmrah rtqlralgei
      121 yynlrtadgr prygfkanee tyaaleriyr agqaggefrt fdvrvmavtm ssaidnmfgy
      181 wvtypdhdld ahareladlf eravk
//
LOCUS       WP_357654312             476 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654312
VERSION     WP_357654312.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 476)
  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..476
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..476
                     /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=49043
     Region          16..258
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,42,44,73,89..92,96,98,135,137,
                     139..140,142,151..152,155,170..173)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,42,44,73,89..92,96,137,139..140,
                     142,151..152)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(26,96,98,135,137,139,155,170..173)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(38..39,65,70,75..78,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(151..159,166..173)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 matplapddp aslgayrlag rlgkggqgvv ylahssdgea vaikllstgd eetrarlare
       61 ldalesiasf ctarvldasi dgprpyvvse fveglsladr arergplrgg elerlvvgta
      121 talaaihaag ivhrdfkpan vllgpdgprv vdfgiaraeg aatltsglig tpaylspeqi
      181 agspaspasd vfawaatmvf aatgrspfga dtvpavlhrv lhadpdlsel pprlrglmas
      241 clakdpvhrp tardlmvslv npmsnpgage rtgpraaalt tdvskrnrsr gllvgavaav
      301 lalvaaggtl lwinraptgt aaqrsstltp sqstttqept qeptstaqas atektaaekk
      361 pqsgslkipa afagkwsgrt tstnpldsdg aavtidlktg qstarwtekd savsctgkit
      421 ltrvagtelt sslqpdtidc iagtvwltld ggkltyvwrd vpgpglveet gdlnrg
//
LOCUS       WP_357654336             228 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654336
VERSION     WP_357654336.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..228
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23977
     Region          6..196
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtnaqtiegv vfdldgviie sehlweevwr dfsesrglpw elsdtlavqg mssiewagyl
       61 aghvgapgda evardycvtg lvgrirrgea ellpgarelv tsvsarvpia lassaarqai
      121 davldhhdla glftatvsse evprgkpspd vyleavallg ispdhglave dssngiraay
      181 aagllvvgip natyppkpea aaladhlaad hvdarefila rlaegarr
//
LOCUS       WP_357654358             836 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora rifamycinica].
ACCESSION   WP_357654358
VERSION     WP_357654358.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 836)
  AUTHORS   ter Beek,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 836)
  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 836)
  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..836
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..836
                     /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=86134
     Region          1..830
                     /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          607..832
                     /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 mlklagqmlr hrkgsavatl lamtagvlil mslgvlvesg lrftaapqry aaadvvvanr
       61 ditltsttlg dqetttvvlp eggtvpaemv drirqlpgva tvvadrtvpa ilpngaatgh
      121 gwsstavtpy rlttgvrptr dtevalderl aasvapgdev pvlvngsart yrvsglvrha
      181 girpdphapp avfftdahav vlhprlgrvd avavlaepga artvvadvrr laaeagvkay
      241 agderglleq sadqaaslll vqlgsvfggy vallvmfvva gtiglavrhr rrdlallrav
      301 aatpgqvarl vlaevgllsl lsvvigvpag wltsrwlhqe lvdrafipdt fpvrgggwaa
      361 vavavatvtv aagaaliaar rtvrirptea lgeiavesgr ngplrlisgf valaggvili
      421 altgaakgta algpamgllc lfvlavallg pwinrtaarl lapvlrrvwg dsgylaaanl
      481 ranaqgmvtv ltalvlsvgf ggsvwflqdn ldkqivaenr ggmlaqqtvv satglpdtml
      541 aqirdipgvl aatgvrntsi ipdgaaegad aqaidpegvd ltmdlkvrsg sladlrgsam
      601 aastlqaesn gwrvgdqvtv rlgdgtpadl rvvaiydrgf afgdvtvvkd vvaghtavag
      661 yerilvrsep gedvsaalge vvgrypgssv tstadvsgql addlalsawl nklligimvg
      721 yaalaaantm vmaalargre lallrlvgvt gkqvkrmvha eqtgllgvsl liggaiaavt
      781 lmsivhtltg qlvpyvpplg wvsiiggttl lalfttilpv arllrvppva gigike
//
LOCUS       WP_357654363            1049 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357654363
VERSION     WP_357654363.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1049)
  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 1049)
  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 1049)
  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 1049)
  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..1049
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..1049
                     /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=112310
     Region          4..245
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          111..1049
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          749..785
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          836..864
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(837,840..841,844..845,847,876,879..880,883..884,
                     886..887,910,919..920,923..924)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          874..904
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtwrllgpve avvrgervpl grpqqravla ylllnanvvv saeqlaealw ggalptrara
       61 qvqvcvsrlr rltraagipe tihsdsggyr lelagddldv vvfsgmtaaa rryadsgehe
      121 raatllrqal alwrgpalag asaafvpaav aglhdkrlaa sedlfdaefa lgrhaaavap
      181 lrelvtgnpw heglavrlmt alagsghrae alrvferirr lladelgiep garlaeahvr
      241 vlrrqlppgg paspvretgt aprpaqlpag lstftgrgda latldtmlsr argsdalavv
      301 aivgtagvgk talairwahr vrhlfddgql fldlrgyspg aatapsdals rclralgvpp
      361 tqvpddvdea tdlyrsvlad rrvlilldna rdtahvrpll pggagclviv tsrdrlggla
      421 aghdaqrlsl dvlspqeate lltrvigadr vagqrdalae lardcahlpl alriaaadlh
      481 grpdervggy larlrtgdpl tvltvrdddq tavrsafaas yrtlpprlqr lfrlfglvpg
      541 cdvtaesaaa mlrcgtgeaa dllsriadah lvqertpghf gthdllgryv telaetgdnr
      601 etlgdllswy lfsvyaaadr lcpqvlrvpt rlpapvgppm rfathvdala wldahrhnlv
      661 avtrhaahre lhafawslad alrgylwlgm httqwsevar iglaaaradr heqaeaaarl
      721 slaalhwrle rfpeaiddyq lallaakrsg wrdgeaaalg nlgpvfrmtg qpgealrvme
      781 qalavnrrng rtagvavnhn nlglvcadlg rlraaaehhh aaltlahqgg atssralils
      841 nlgvvhhllg rsddalrtlt ealelheqtg srgrattlca larvhgdrge hrraadlarq
      901 aldlartpae prvealalhi lgvvegktgt llnalrtart tadryieadv tvslaeidep
      961 aapswchaal sitrrcgyll legralaara aaeyragdlt aawrsarlaa rshaltghqp
     1021 gteridklia llasehlpdt adglpvedr
//
LOCUS       WP_357654369             325 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654369
VERSION     WP_357654369.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 325)
  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 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   3  (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   4  (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 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=34830
     Region          133..320
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <261..320
                     /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 maeitlnvrq lqafaeigyq aaggggggac gamaalrrvv pvdayefvaf dpasgrhhsv
       61 vsdghrridg daaeeytgle vyrtamatra pvpmpepgte ryfrrhlapy gwraglttpl
      121 flaegrytgl lhlaareafp eltgslvaav apmlahvtdl trcvidpvgl pagflaaafd
      181 rlgvrrevpg vdrsaalwde paiaglaraf idsrelsrrg lwldrdgrwh evrvlragvg
      241 fqgslqgavv aerpcslpye ltgrevdvlt rvaagdsnpq iaaalvlsvr tvtthlehif
      301 aklgcdsrtr lttkalaegl crldv
//
LOCUS       WP_357654377             374 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora rifamycinica].
ACCESSION   WP_357654377
VERSION     WP_357654377.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=40143
     Region          69..371
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mgrepgpsvr lkltlsyagf vvlaggllla tvwvfllryv pevidapatp tpapggsrlp
       61 apvmfvpnrs dllrafapra vavlalllff gllggwflag rmlapltrit ratrmaahgs
      121 lshrirlegr ddefrelsda fdsmlerles hvaeqqrfaa nashelrtpl avsralldva
      181 rrdpaagrgd lidrlhtvnq raidlteall llsrgdrgvf trervdlsll aeeatetllp
      241 laerrrttld vsggaactsg spelllrmvt nlvqnaivhn lpaggtvsvh tgvhgdtsvl
      301 rigntgqrlp pelvptftep fqrgtervrt eehagvglgl aivhsivrah agtldlapdp
      361 rggllvtvrl pgtp
//
LOCUS       WP_357654385             617 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora rifamycinica].
ACCESSION   WP_357654385
VERSION     WP_357654385.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=65747
     Region          18..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 msdrpdaggl ddrhrpgveq fvtawavalh rahyvpisae hrhrivtgla drlvtavlae
       61 saepghghri gadlvaagfg spealggtia vigsrfldel avgadpvhaa rlnslladla
      121 agfsaaahdr tlraqetvrl aaltartkae ealrvsearf rrfathdtlt glpnltlfte
      181 qlgrlsaaev pvdrvgvccl dvddfaavnd vlghqvgdll lreiadrlga ltdrridlva
      241 rldsdrfail vrdttctedt ikiadqalaa vaapyrvngt evpltasagv aeatvadgga
      301 aalmraseia lhwakadgka tlrqfdpdrs nadaaryrls aampaalrrg efvaayqpia
      361 dlstgrlagv ealarwqhpr lgllsaarfi elaertglvv plgsqlleqa crqasrwqrv
      421 qpglyvsvnv svrqlhqngl agavsqildr tglpphllql evteqavidl sgvvtetlaa
      481 lmtigvrivi ddfgigyanl anlrslplhg lkldasltrs stqptrwpga rrpgtddefl
      541 stvvslghkl glvvtaegie taqqarqlas tgcdngqgwh fgrpvpphei tagivarqhr
      601 ettprdtglp vvplrrp
//
LOCUS       WP_357654399             449 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654399
VERSION     WP_357654399.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=47960
     Region          36..352
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mtpptprprr rwtmaaalav altatvaacs sadtpssgss atgaasgpvt lqvwtwnlkg
       61 ndprakaiid kyhqenpnvt vklsevggta dtaskllaad qagdtpdvvq veyrglpalv
      121 vagavkdvta dvadvksgie pniwalttfn nqvygvpqdi gpmmftyrkd lfdkygakvp
      181 ttwaeyakaa eqihkkdpea yiasfsaaql effaaqaaqa gaqwwsndgk awkvgidsep
      241 slktadfwed lvkrdlvkve plltpewnaq indgkllswa aaawapnvih svapdtaakw
      301 esaplpqwtp gdpavpflgg saflvpaksk hakeatafaa wlgasdegsk lqlsldiypg
      361 gnagrqatls heppklmpqq kdfyqvadqv iknttipvtw gpnvnvsqta fgdalnkaal
      421 nkssfrevyk atqqavvadl qksgytvtk
//
LOCUS       WP_357654456             766 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Micromonospora rifamycinica].
ACCESSION   WP_357654456
VERSION     WP_357654456.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 766)
  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..766
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..766
                     /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=83804
     Region          69..539
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mtgphppgee trldpgrgga gwdrsdepat eldpgrvrpd drepateldp grvrpgsrdv
       61 ppwgrrlpdr lgtrfqvlre lstggegdly vvqeratgld rvlklyraga gpdpqvtgyv
      121 resrrsrhiv elfeadtadg hhyeimeyla ghtaaelrrr hpggldpall ttllgqitea
      181 laelhaagiv hrdlkpsnll vrtldpieiv lvdigisryv ddvealtrnr dtgtiryrpp
      241 efiaggvisp aydwwslgit lfelatggqi laglgddval nvryttgmld vsavtderfr
      301 llcrglltpd pdrrwgtdqi rswlagdsps vaatstapap gtphaadrpy ryldvdywyr
      361 pelamaltet wqtatallfg adptpdqrlg ewlrqfpdrp ktrtrgrrps rdvrllarlq
      421 aidparppvy rneniavdrl yglaaqalns vgssadvvad lwafdllpvl sagsaapgls
      481 ggqglrevrd rwrrehrhlt spaslsavad aearaelrrl lrdeaprfha ltllaavate
      541 dqrqavrrdl tqraqqveep wfatlvaqpr hlwlayalap faestaerka aeeeaararr
      601 ewlrrteair ewsrrqnrpr alalavggvc alvvvlaamv gigdavdvvp dativdawfa
      661 vvaatgvalt fesllawtig grfraysllv saavtvgrla rrvtgrqaal avvggvlvga
      721 glltaylpvv tpvavavlmv vwtigrylaw ldevarerad iaaags
//
LOCUS       WP_357654520             197 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654520
VERSION     WP_357654520.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  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..197
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..197
                     /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=21537
     Region          11..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msdrpaqglr erkkaktral iqkealrlfr eqgysattve qiaeaaevap stvfryfask
       61 edlvfndqlp pfaealsaap adlspisavr valrevtaar tdeeiaegve reklmfsvpe
      121 lwaasltnvs galrsmqeil arragrdasd peirnitgai agvifavwfd wvkedskvdg
      181 paeidkalah leeglrl
//
LOCUS       WP_357654538             399 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654538
VERSION     WP_357654538.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  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..399
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..399
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43619
     Region          2..81
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mdvqqeiger iararrrrgl sqavlsglvg rseswlsqve rgqrsvdnht vinalaeilg
       61 lpldeltakk saamtrydaa pgirrammgy dglsssidsr laegsaeslv wlqheirrvn
      121 alyqatryde vgrrlprliv atelgsrhap agarrayqtl rsltyhcatt tlrrvsepel
      181 awvaadrsla aaeeadrpll vavsayrlgy vlirlheter alrlvlgaad slrrsprslp
      241 vlgalylvav taaaaaydra gvqdflaqar qaaetigedr ndfwtafgmt nvaihevsaa
      301 vefgdarrai stgeslnlsa latglvgrra qvhldlaray avqrkdaasv nmllqaerls
      361 pelvryggrp rdlltqllkr ehqastpelr plahragiv
//
LOCUS       WP_357654555             181 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora rifamycinica].
ACCESSION   WP_357654555
VERSION     WP_357654555.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 181)
  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 181)
  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 181)
  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 181)
  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 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..181
                     /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=19208
     Region          6..157
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mttlrlrpeg padagpvrrv laaafarpdg ttpgevtlvd elrgsaswlp elamvaeygg
       61 evvgyalltr vrveadrarv dalvlgpvav aphrqraghg tavvqaalea atelgerlvv
      121 vlgdpayyrr fgfsradrmg lvspwsglge pwqalvlppe vshapppprg evvfpppwsr
      181 v
//
LOCUS       WP_357654562             119 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357654562
VERSION     WP_357654562.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..119
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13237
     Region          25..101
                     /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 mmghsrwety kakrlremea daqshseyeq agrdlelgdq lreirkrrgl sqkivaersg
       61 msqpalsrie ggggipdiat llrlgaamgv rfrvelvvdd dttteieplt vhhrqlana
//
LOCUS       WP_357654609             402 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654609
VERSION     WP_357654609.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 402)
  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 402)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..402
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43720
     Region          26..399
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrillvgagg vgsavvpiaa rrdffehivv adsqqsraar avagvddprf saisldaadr
       61 vavaaalreh rcdvlfnavd prftmplfea alaagadyld mamslsrphs srpyempgvk
      121 lgdeqfarde ewrardrlal vgmgvepgla dvfaryaadh lfdgideigv rdgsnlvvdg
      181 ydfaptfsiw ttieeclnpp vvwedgrwht tepfsepevf dfpegigpve cvnveheevl
      241 lvprwiparr vtfkyglgee figvlktlhk lgldsadkir vggadvaprd lvaaslpdpa
      301 tlgdrmhgkt cagtwvkgtg kdggprevyl yhvvdnawsm reygsqavvw qtavhpvval
      361 ellargawkg tgvlgpeafd avpfldllte ygspwrirea aa
//
LOCUS       WP_357654577             418 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654577
VERSION     WP_357654577.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  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 418)
  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..418
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..418
                     /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=44990
     Region          1..406
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mvtlaivgag srgtsyarha vesggarvva vadpvesrra rhpgatpyad wrelaalprq
       61 adaviiatqd adhvepavrf aelgydille kpmavseddc raivaaaers daifavchvl
      121 rytpytralk alldagrige ivsiqhlepv gwwhqahsyv rgnwrrsdes tfmllaksch
      181 dldwlvhltg rqvtkvssfg glqhfrpehr pegaadrcld cavedacpys akriylplag
      241 keawplnvvt ddvsergvle alrtgpygrc vyacdndvvd hqvvnlefeg gitvaftmta
      301 ftpaahrqtr ifgtrgsieg dgdrltvtdf ltggtdtidt rptgdatagg ghgggdealv
      361 aafltavrtr drapilssps eslhshliaw aaersrlrge ivdvtpgavs psaeaspr
//
LOCUS       WP_357654651             257 aa            linear   BCT 28-DEC-2024
DEFINITION  CoA transferase subunit A [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654651
VERSION     WP_357654651.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..257
                     /product="CoA transferase subunit A"
                     /GO_function="GO:0008410 - CoA-transferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27918
     Region          2..226
                     /region_name="AtoD"
                     /note="Acyl CoA:acetate/3-ketoacid CoA transferase, alpha
                     subunit [Lipid transport and metabolism]; COG1788"
                     /db_xref="CDD:441394"
ORIGIN      
        1 msveevaaev esgmtvgigg wgsrrkpmal vagllrsnvr dltlisyggp dvgmlcaagk
       61 vrrvvapfvt ldsiplephf rrarqggtie fteydegmfm fgllaaahrl pflptraglg
      121 sdvmrvnpdl rtvrspyedg eelvavpala mdvalvhlnr adrrgnaqyl gpdpyfddly
      181 akaaarcfvs cerlvdtadl lkegpvqsll isrsmvsgvv eapggagfta cepdygrdeq
      241 eqrryvdtpw eefhdpa
//
LOCUS       WP_357654641             125 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654641
VERSION     WP_357654641.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 125)
  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 125)
  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 125)
  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 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   5  (residues 1 to 125)
  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 125)
  AUTHORS   Rosinski,J.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..125
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..125
                     /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=14009
     Region          5..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msdviwaalv dphrravldl lrerdrsvte lvdelgvtqp taskhlrvlr aaglvrvrkd
       61 aqrriyaidl epiaeldqwl apyrrlwndr ldtlgrhlde tdtgantntd tdigadisad
      121 igkes
//
LOCUS       WP_357654656             147 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654656
VERSION     WP_357654656.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 147)
  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 147)
  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..147
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..147
                     /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=15837
     Region          4..135
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mgmpaeerlg ldikraeqel iaakqvavrp agltvpqyat lyvlaanpgi saaalaracl
       61 vtpqamtvvl knlearglve rtphpwhgnv letrltdagr aalekadera vrieqaiade
      121 ftteerdtlr sllrrcgtai drassql
//
LOCUS       WP_357654681             501 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Micromonospora rifamycinica].
ACCESSION   WP_357654681
VERSION     WP_357654681.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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 501)
  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 501)
  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..501
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..501
                     /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=52635
     Region          5..495
                     /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 mnaplrrvgv vvmvlfgllf anlnwiqayk adeyrnsdyn grvqvaeyer rrgnieaggt
       61 avatsketgg klkfqrsypa gtkyahvlgy kpvnlgdtgi erlendflag tsdallgnri
      121 kdmftgdesg ggnvllsisk raqdtayeql rnnrngvkrg aaiaidprtg avqalvsmps
      181 fdpnplvdhd tnaasaaynk yeqdpdgplk nralsetlpp gstfkiviaa aalengvgkd
      241 teipagpswt pptsgtpirn ahpsicpeaq vtlidavtes cntgfaqlgv rlgadtvkek
      301 arqfgfeqdd ltvgqlgegg lpvaasrtgd mqnpdggtdp aalaqssigq nnvrmtplqg
      361 aliagsvank grqmrpylvk qllgpdrtts yynaqprelr qpvsgqvadd lrdmmvsvvr
      421 ngtgssaaid gytvggktgt aqsapgrpdh gwfigfaldk ngnavsavcv eleqadsggs
      481 aeaariggki mqaaiadagg r
//
LOCUS       WP_357654687             226 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora rifamycinica].
ACCESSION   WP_357654687
VERSION     WP_357654687.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=23943
     Region          6..201
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mapltladel vllayddegv nrlgrphldy glsgavllel alagrvevvd drlvvtdptp
       61 tghqvldaal aevaadgrrr rpkdwisrla kglpdrvlag lvdagvlrre sdrvlllfpr
      121 trypsptgae pvaetaarqr mvdalladgp veartaallg ltravgldrk lfrelpkerl
      181 kartteiaag dwasaatkka ieetqaaimt attvatsaai igatss
//
LOCUS       WP_357654695             267 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654695
VERSION     WP_357654695.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=28073
     Region          7..265
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 magseltnvk sprvkaarrl akrafreqdr kflaegpqav realklegvt lelfataeae
       61 lrhpelitda tlkgiplhra sgevmaelsq tvtpqgllav crlvhvpldd alsgdprlva
      121 vlahvrdpgn agtvmraada agadsviftd asvdpyngkc vrasagslfh lpvaigtpva
      181 aavrqlrerg lrvlaadgag khtlddvdls gptawifgne awglpeevla eaddvvrvpi
      241 ygqaeslnla taaavclyss araqrvp
//
LOCUS       WP_357654699             203 aa            linear   BCT 28-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357654699
VERSION     WP_357654699.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 203)
  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 203)
  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 203)
  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..203
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..203
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=21426
     Region          1..203
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mrirpvgrha llldcdhpgq veqwraelwr rraagelsat eivpaagtvl ldgvpdpesa
       61 aariagwtpa pvtttagtat veiptvydge dlplvaghwr ltvpqvvrrl adtefrvafc
      121 gfapgfgylt glppryavpr lptprprvpa gsvalagpya giyptaspgg wllvgrttlt
      181 lfdvaadppa tltpgtrvrl vtv
//
LOCUS       WP_357654727             729 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654727
VERSION     WP_357654727.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=81074
     Region          2..726
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mnpvleplfr tvrathpkad lrliehaydv aayhhrdqkr ksgdpyithp lavatilael
       61 gtddetlcaa llhdtvedta ygldelrgdf gdtisslvdg vtkldkvkfg daaqaetvrk
      121 mvvamsrdir vliikladrl hnmrtmrylp ehkrhqksre tleifaplah rlgmntikwe
      181 ledlafamly pkrydeiarm vseraprrdl flqeviekvs gdlrdakira lvkgrpkhyy
      241 svyqkmiard vafddiydlv girvlvdsvr dcyaalgtih arwnpvpgrf kdyiampkfn
      301 myqslhttvi gpegkpvelq irthamhhra eygvaahwky keevgapgpa gkvkpgsdma
      361 wlrqlldwqk etsdpgefle slrfdlsvse vyvftprgqv valpegatpv dfayavhtev
      421 ghrcigarvn grlvplesrl gngdtveift skspdagpsr dwlkfvksgr arnkirqwfs
      481 kerretaiea gkeaigramr kqglplqrlm sgesllalar dlrypdvsal yaavgeghva
      541 aqtvvqklva siggvdsaee diaetslptr lrgrprggga gvvvagdsdv wvrlskcctp
      601 vpgdeivgfv trghgvsvhr adctnivqlk sqpdrlvevs wspgddsvfl vaiqvealdr
      661 prllsdvtrt lsdqhvnils asvttsrdrv avskftfemg dpkhlghvlk avrniqgvfd
      721 vyrvsgast
//
LOCUS       WP_357654767             176 aa            linear   BCT 28-DEC-2024
DEFINITION  HIT family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654767
VERSION     WP_357654767.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 176)
  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..176
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..176
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19101
     Region          40..166
                     /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(65,67..68,75,77,123,131,133,137,139)
                     /site_type="active"
                     /note="nucleotide binding site/active site [active]"
                     /db_xref="CDD:238606"
     Site            order(135,137,139..141)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238606"
     Site            137
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238606"
ORIGIN      
        1 mhdqagagep dnfqrlwtph rmayikgegk ptgtgaddgc pfdaipkmsd eeglivarge
       61 vvyavlnlyp ynsghlmivp yrhvpdydll dgaelvelae ftqravralr kasgaqgfnv
      121 gmnlgqvaga giaahlhqhv vprwggdtnf mpvvaqtkvl pqllrdtrel ladawd
//
LOCUS       WP_357654798             274 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654798
VERSION     WP_357654798.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 274)
  AUTHORS   ter Beek,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..274
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..274
                     /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=29802
     Region          1..269
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 msepllrane ltkrfvtrgp lgskaefvav dgvsfdvrag etlavvgesg sgksttarmv
       61 arltepsagt lefegedita akgsalaryr anvqvvfqdp fsslnprhtv erilmaplvy
      121 qgipptggkr aharelmerv gldpdhsqry paqfsggqaq rigiaralav rpklvicdea
      181 vsaldvsvqa qviellrrlq aesgfsyifi ahdlavvrqi ahrvavmskg kiveqgpvdq
      241 vfgdpqdpyt rtllaaipri npewdrrrre gspr
//
LOCUS       WP_357654841             451 aa            linear   BCT 28-DEC-2024
DEFINITION  LVIVD repeat-containing protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654841
VERSION     WP_357654841.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..451
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=48748
     Region          50..429
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          75..109
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          116..167
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 mifgkvrvaa acaalllaaa csagpqgdpg gedpseetvs taqptgdakt spnvklvahv
       61 prtaplngam dwntdlafqg dyayvgnfgg fsiydisdpt kpktvsqvac paqqndvsiy
      121 gdllilside prsdescast tksraweglr ifdvsdkknp kyvsavatdc gshthtmipd
      181 getlyvyvss pgpepesdtc ppphellqvv eiptkdpkaa kvvarpnffp dreetgagch
      241 ditaypekkl aaaacfgdgv lldisdpvnp kmlqrvrdee nfqlwhsatf nndatkvvfs
      301 delgggsapt cdrdtprtkg adaiydltng qlerrgyfki preqeqdenc vahngsllpv
      361 pgkdimvqsw yqggvsiwdf tdssnareig yfdppafngv agswsayyyn gyiyssdirg
      421 gldvieikdp ltdpakqvkm ddfnvqtqks y
//
LOCUS       WP_357654852             133 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357654852
VERSION     WP_357654852.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 133)
  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..133
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..133
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15229
     Region          12..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(16,20,45)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,44)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,38,41,45..46)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mvtptiqrrr lgnalrrare aagknqdeaa evidsagski srlelgqsgi rltdlkllld
       61 fygvppeeae plrelaragr qrgrwtgyrn vvpdwfrqyl dleadaaeir wyqsehprhp
      121 pdralhpgdh rrr
//
LOCUS       WP_357654932             530 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654932
VERSION     WP_357654932.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..530
                     /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=54507
     Region          2..530
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mstltgtggl irlilrrdrv rlpvwyglva llvigvagsv aaaypteear qaflhttngd
       61 ptqlmmigpi ydssaaglaa wrvrgqaall ialaslflvi rstrgeeeag rsellgstvv
      121 grhaaltaal tvaftaglvt alavalglmg qgmpaqgslv mglsvaaagw vfaalaglaa
      181 qltessrtaa glaatalail yavraiadle ksswvswlsp fgwtqrmrpf agdhywpllp
      241 vigltlllva aayrmsarrd lgagilpsrl graeaapglr tslalawrlq rgtllswaia
      301 stafgaglgg aaqsaaeqln asealrgmie rmggggrpad gffafviylm sqvitvyaiq
      361 atlrlraeet sghadviltg pvgrlrwagg hlavvaagsa ivlaglglgm glvsglstgd
      421 vggeiarllg asltrlpsvl vlaavpvlvy gllprlaavv ayvalglclv lefavellha
      481 dpsiltvspf aqtpglpvae ftmtplillt lvaalltavg laafhrrdlg
//
LOCUS       WP_357654936             401 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357654936
VERSION     WP_357654936.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..401
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=42753
     Region          34..377
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mtthretgtv tphrvlilga gyagmaaaiq laartkgred vqvtlvnpqe rfterlrlhi
       61 satgqqvaem nipellegtg arfvrgwvtg meadakivri dddrvlhydt lvyglgsvad
      121 tvtvpgveey aytlnsaqda evlaerlarl grgtvvvggs gltgveaaae iaerhpqlnv
      181 vllgrqepga amspkpkayl qsalarlgvq vrsgievvkv lpdsvelagg esvaadavlw
      241 tsgtrvspla aaagltvder grivtdaklr svshpdvyav gdaaairqgy gvmhgtcqgg
      301 mptgvhaavs ivraldgkrt kpfrfgyyht pvslgrndav vqfthpddsp rrvhltgria
      361 arykeavtas pwptygrmkk mpasgafwpr ggrftrvrgv r
//
LOCUS       WP_357654953             969 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357654953
VERSION     WP_357654953.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 969)
  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 969)
  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 969)
  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 969)
  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..969
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..969
                     /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=106057
     Region          8..251
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          154..969
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          821..849
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(822,825..826,829..830,832,856,865..866,869..870,
                     872..873,902,905..906,909..910,913)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          854..890
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          901..929
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mssegrlrat frvlgpvelq tatgrvvltg kqgalltill lsanrvvsvr rlaeslwgep
       61 lpsspssrvr tlisnlrrtc vtagddlirt qrpgyvvrla pdqldlaryl draaqareaa
      121 argdletavs cydealslwh gapllgidgs fvqaevarle elrleavegr ssamlamgrh
      181 aeavtgltav iadhplreaa hgqlmlalhr sgrradalav yrrlrerite elgleperel
      241 qrlhqrilts dtalentaqe tsdvtpetsd iapeaprhqp rpvvspvprq lpappphfvg
      301 rereraeldr ltrdpttnsl aiaaisgtgg mgktslalhw ahdnanlfpd gqlyvnlhgf
      361 dpsngplpaq valrhflgsl gvpaaaipag eqaqaglfrs lvagrrlliv ldnardvaqv
      421 epllpgspgc ivvitsrnhl pglnatrgas liglnaltra etrrllgrhl gesrisadpd
      481 svavlvehsg glplaisvlt araamhpgfp lsvlaaelss pstrldalha gdlgtdlraa
      541 ftasyealda atarlfallg lapwpdvslr saaavaglpt srtrmllhdl eaanlihqhr
      601 pgryrthdlv rlyaaerars drpdqertea ltrlvdsyvr tacagdrlly pnrpfvsrif
      661 perspdefed aaaawawfed eqssliavqq lavrlgmdaa vwrlawamdt yhkrcqheir
      721 ieswqtalaa aerlghsgtr afvhwylgya yaqapraddg lehlmlafkl feqeddlagq
      781 ahtshtlgfa wlargrpeha lphvenalrl qrelrdplwe analsaagwc haklghypea
      841 rsyceqalel frkyedlnge satldslgyi ahwagqrdqa ldyygrclel rdrlgntyqg
      901 adtlvrigev qhetgrttaa rdawqraldl yhkqhraaea envqekirrl aerpsaaagp
      961 sgpaapadr
//
LOCUS       WP_357655094             158 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655094
VERSION     WP_357655094.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 158)
  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..158
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..158
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17222
     Region          4..152
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mrtlivlrha kaaqvpgled serplthrge rdakragdev ralglapdlv lcspslrtkr
       61 taelafpeva vsyerdvyqa ypeellalvk ltdpeletvv lcghnpgvhe laialaggdy
      121 gfrpgsfavi rteadwvdlw pgeaqlitrw dpkgeisg
//
LOCUS       WP_357655098             315 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357655098
VERSION     WP_357655098.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 315)
  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..315
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..315
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34927
     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          101..282
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvddgssvpr rhlgrvletl rveagmtvdg aaealgfsrr klwqieagrs avsrtdvrdm
       61 ceryaarpel adtlvtlagq trakgwwhay gdplprwcep yvslaaearr lreyadgmip
      121 vllqtreyat avcrqradlt evdrdrliev rlrrqrvlrr lptaprlevv laeavllrav
      181 gdpgvmvaql rhlveashlp qvslrvvpla vgsyraalag pfmlldfppv srvepdppvv
      241 yrefltgaly ldrasevaey eqawagldav avghdesrrl ietisaevhg crtgaahplp
      301 smirttrtvp sapye
//
LOCUS       WP_357655106             798 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357655106
VERSION     WP_357655106.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 798)
  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..798
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..798
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=86504
     Region          16..797
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          507..535
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(508,511..512,515..516,518,548,551..552,555..556,
                     558..559,588,591..592,595..596,599)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          546..576
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          587..615
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          621..655
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          667..693
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          707..733
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mserdgqept prhvnrseld gpadlvqard vfggvhfhgd aadreppprq lpgdvrgfvn
       61 rivelsaldr ltgdgdgdrd aqvtlsvitg tagvgktsla lrwahrarhr fpdgqlyanl
      121 rgydpgeptr peavldrflr algvpaaaip tdredrealy rsrladrrvl lvldnaatar
      181 qvrpllpgsd tcltivtsrs mlsglvtrdg grrltlpmlt eddavallrt vtadhragdd
      241 pdelielarl carlplalri aaeraagrpf mplgdliqdl rdesalwdal taeddeeada
      301 vrtvfawsyr glstvparlf rliglhpgpd fsvpavaala gvptaqvrqp ldalvtahlv
      361 eqhasgryql hdllrayavd qvrqfedeen rlealrrvla wylhsadaal artlpfnrtv
      421 plqppagvvp lafaspaead awfdgerdnl vaatriaaet dlsrvawqla ailrsvfmhr
      481 nafdgwftta riglaaarsl gdrrgeaeal eslgkahfqa rqldeaaehh raalairrdi
      541 gdehgtavsv nalgllglrh rrltealahf tdaltrferl gsrrwqalll snlaetryel
      601 gdpaqavell eralavqrei adrgqegnsl fflsmalrel grvgeaeaai gralaiaeda
      661 gspvwlahwl veqarvlcas grpaealeaa hraatiqrrl gdrsreamal dgageayles
      721 graeeavafh lraaathrgl gdawhlavsl anlaaalvga grpgeaespr reardllagf
      781 ddaravallg sldaagds
//
LOCUS       WP_357655139            1041 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357655139
VERSION     WP_357655139.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1041)
  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 1041)
  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 1041)
  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 1041)
  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..1041
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..1041
                     /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=111562
     Region          9..258
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          136..985
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          776..803
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          808..844
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          855..889
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(856,859..860,863..864,866,896,899..900,903..904,
                     906..907,934,937..938,943..944,947)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          894..928
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          933..963
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtgqsgeggl rfavlgpvra wrdgtevdlg tplqrsilam lllregravt ptemidavwg
       61 edappralga lrtyvsrlrt vlepgraars rpelltsvgr gyalrlpdds ldltrfergi
      121 heaeaarrag rpreaaeglr aalslfegep lagavgpyte hqrdrlverr isvvetlmdl
      181 dlelgehaav vselialtae hplrerlraq lmlayyrcgr qgdalavfte trdalieelg
      241 iepgheltal hqrilsadpt lavaevaeed apeeraptld lprpaqlpaa vsdftgrtdi
      301 agrlrtllss kpaegvpvaa icgiggvgkt alavhvahaa ddlfpdgqly adlrgytdea
      361 tgpesalgaf lralgvpsdv iperlaersa lyrsllaerr ilvlldnahn aeqvlpllpg
      421 ssgcaaivts rhkladlpsa rlfdldvmdp dealtlfasv agaervaaeh gaamdvvaac
      481 gflplavriv aarlaarpsw tvaslvprlt deqrrldemr vgnlaveatf algygqldta
      541 qarafrllsl pngpdfsvga aaavlsmsaf asedlleslv daslleapap gryrfhdllk
      601 lfarrtlekt erpqartmal rrllgfylas aqsahrlaye gsmiadnlqv dgsglsfnsv
      661 neavawlvae gdslfaainq aaatarapep llpagdllva mepllesgth trefdqgtra
      721 vlatakrigd agselraryv lgrvlfasnk ltqaeeqfri vhelsverae kvvtgevmna
      781 lavvvgrqrr haealtwfes amgwyrengv pagealvlsy sardhlglgr pedaitaaek
      841 glaifteigs gagtararyh lgivlsrvgr iaeavhhhae claffraskq rvweqrvcsr
      901 laetfiaakr ypdavrhaee alvvsreigh pygealslmv lgealegmgs atrsldclrq
      961 afeifsllga peagdlkvrl dkapatgsvv epvvspvvep epvvgpivrp vvepvvstva
     1021 epvvstvvsp dvepvvgpve p
//
LOCUS       WP_357655140             540 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora rifamycinica].
ACCESSION   WP_357655140
VERSION     WP_357655140.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 540)
  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..540
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..540
                     /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=55013
     Region          9..255
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(9,33..34,63,68,73..76,88)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,71,87..90,94,96,133,135,
                     137..138,140,150..151,154,163..166)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,71,87..90,94,135,137..138,
                     140,150..151)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(20,94,96,133,135,137,154,163..166)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Region          <197..431
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mtgdwrlsgy tpvrqlgaga sgrvllathd atgtpvairy lpaalgddpa frlafreqar
       61 llvdvdaphv crlfeyaesh aaaaivtelv ngvtlrhllr ahgptgpeaa lrvlkgslag
      121 laaahargvv hrdhrpenvl vgvdgrtklt gfglapatgg ghgvprhlap eqwtgapaep
      181 agdiyaatat ffecltgrpp yggpdlatlr aqhaaapvpt gptpaplhdl lrhglawcpa
      241 drpqpaeifl aelehtaars yggdweergr rqlaervall aaslpfpdgv pvpaavsvat
      301 ephatrrggt rsalvgvglt avlltgvvgv tyaarrpgpv tladgaavpg ataavtrsaa
      361 plaaapaitv vppepsrspt paatttdpap tttasrptaa tttrgrtpgp tpaatpvspl
      421 lppdvfaptv savdassaiv epqgcpetvt sttvtarvvd draggdllrv vfrytldgvv
      481 rtvgmdqtgp dtfrgtlgdl pvpasvtrip veviavddag nasapagpiv vsllstctsg
//
LOCUS       WP_357655149             155 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357655149
VERSION     WP_357655149.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 155)
  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..155
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..155
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17355
     Region          9..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnvafqvnnc siertldivg ekwtflvlre afrgvrrfad mqaitgaprq vlsarlarlv
       61 deglmrkepy repgqrqrde yrltekgrdl ypllvalmhw gdkylagdeg ppvllthrdc
      121 gapieqhfrc adghevvgpr evtalpgsga elkta
//
LOCUS       WP_357655153             491 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora rifamycinica].
ACCESSION   WP_357655153
VERSION     WP_357655153.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=53729
     Region          1..437
                     /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 matehvdvli vgaglsgvga achlrrecpg rtyavfearg aiggtwdlfr ypgirsdsdm
       61 ftlgysfapw tdpkaiadgd ailryvrdta rrygveehvr frhrvlragw dsatarwtvh
      121 arredtaeev vltcdflyac tgyyrydagy tpafpgvery agrvvhpqhw padldltgrr
      181 vlvigsgata vtlvptlaqr aghvtmlqrs ptyvlalpsr drladalrrw lparlayplv
      241 rgknvlvgaa syqfsrrapk ltrsllrrav rrllpvgydv drhfsprydp wdqrlcvapd
      301 gdlfaalaag rasvvtdtvd tftpagvrlg sgdelaadvv vtatglrlla lggmtlsvdg
      361 tdvdpgrtva ykgmmlsgvp nfaltvgytn aswtlkadlv atyvcrllrh ldatgqqvvt
      421 pvapadgels plidlrsgyv vrslhtlprq garapwrlyq nyprdvllmr ygrlvdegvr
      481 fsratagapa g
//
LOCUS       WP_357655261             230 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357655261
VERSION     WP_357655261.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 230)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..230
                     /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=24674
     Region          18..>130
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          79..224
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mtvwdrpepp ppappldrgr ivatavalad eggleavslr kvaarldvgp mrlygfiatk
       61 rdlldlmvde vhaeilperp pgdwretlrv haertrqaal rhewladllg grptlgphgl
      121 avtearlaal dgladldtvl cavatvsayv tgairrevad lraeratgls trewqrasgp
      181 hltrmlatgr fpalsravhd gtdtdagtsf atglewvlda vaarltrpgv
//
LOCUS       WP_357655288             306 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655288
VERSION     WP_357655288.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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 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 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..306
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33914
     Region          4..284
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnfnslgtrc agdlylpevs gpvpglvlgh sgvmvkeala ffapyfvkag favlaidyrt
       61 vgasdgeprg qdyperqved frsavsylrt rpevqperig vwgvsiggsv aaqaavldrr
      121 ikcvvvqsps vwngwryldr llgragvhal rdsldedwqr rneggqsarv phltldhksv
      181 qdtpdmstql fpryrnektl dstehmltfa penlihrlap tpllmiangg wdpyhmleea
      241 qsafdkagep krlevlpydv lglytgpgle eamalaidwf dlylrrtrla ditptptfes
      301 vtamtp
//
LOCUS       WP_357655435             276 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655435
VERSION     WP_357655435.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 276)
  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..276
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..276
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29521
     Region          12..276
                     /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 msplpvrqra lfsadgtqig yqtmgagpgl ivlggalrta qdylplasal arsftvhlve
       61 rrgrgasgpq gaqyalgkev edlravqaet garlafghsy gglviletar sfqvfdriav
      121 yepgvpaghv ptgwmapyre rlaagdpyga fvhfirgsgg apafmaklpy wylrmalrvg
      181 frgpswqrmr plleanlaeh eqvaaqqgrl aafsavtasv lllcggrssr asreefdavr
      241 dtlpdvtlet ldglnhfgpe gksavvvaer alaflr
//
LOCUS       WP_357655436             594 aa            linear   BCT 28-DEC-2024
DEFINITION  IucA/IucC family protein [Micromonospora rifamycinica].
ACCESSION   WP_357655436
VERSION     WP_357655436.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 594)
  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..594
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..594
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66135
     Region          12..589
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnpaasvahl npatwtranr llvgkalaef aherlihpap tddgrwavrt ddgtveyrft
       61 arrfaldhwh idpdsitrhr gdedlppdav dlclelraal gltdqvlpvy leeitstlag
      121 tafkldrpav saaelaradf qaietgmteg hpcfvanngr igfgvheyha yapetgrpvr
      181 lvwvaahrdh atfssaadld yptllrtelg pdtlarftgt ltdagldpdd yllipvhpwq
      241 wwnrlavtfa gevarqrlvc lgeapdeylp qqsirtffnv tnphrhyvkt alsvlnmgfl
      301 rglsaaymea tpaindwlve lvaadpvlag tgltvirera avgyrhpqye aatdryspyr
      361 kmlaalwres pvpglapgrr lstmaallht drdgrslaaa liaesglpar rwlrrylday
      421 lvpllhsfya hrlafmphge nvilvlhdgv vervifkdia eeivvmdpda dlpplvqrvr
      481 aaipddeqll tiftdvfdcf frhlnavlaa eevldeddfw rtvadcatdy aagvphladr
      541 lrrhdlfape ftlsclnrlq lrnnqqmvdl adpsaalqfa gtltnplarh appr
//
LOCUS       WP_357655449             127 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655449
VERSION     WP_357655449.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..127
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..127
                     /product="YybH family protein"
                     /calculated_mol_wt=13649
     Region          4..125
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mmrqlaerpe dvpavfaerf ntgdaaavae vyesgavfvp epgspltgqe ahaanerfls
       61 lglpiavrpr hvytagdial livdwvidgt drdgrpvhie gtatdvarrg qdgrwlyaid
      121 npfgvkp
//
LOCUS       WP_357655474             749 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357655474
VERSION     WP_357655474.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..749
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80916
     Region          16..749
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 meqipgtpes pslgsalrah rvaaglsieg ladrcgvsvr aisdierdrv rrprrrtltv
       61 lfdvlavpdd errrlaeaas grpvggelpg ppryfsgrvt elrtlgdiar rpsgdrqqat
      121 alvvtgpagv gktslvlras adlapefpdg rffvdlrgmd dvptppgeal hrllralgvp
      181 eqripaglad ratayrsalc erralvvwdn aadetqvrpl lpgagrslvl ftsrrrlsgl
      241 dtaqwlsvep lsaadstaml raiarsapdt dpaaltelar hcghmplalr vtgqrlseep
      301 glsvqelnrr fsgeqarlrv idagaagiht alslsyrrlg adlrrtfrrl slmpgpdfgp
      361 dpvaavtdvp aeqaerrlea lvesglvaav padryglhdl vrdfaidrmt veepgstgpl
      421 rtsslrwwla rttaagrhfe pdgptsltef rdraaaaawl daergnwfaa lrsaaaeglh
      481 gpvveavdal hwfsdsrvhl dlwpevfrls aasaarlddp rteavhlnyl swaqaicqre
      541 yassvatagr aldravragd paqqgwally aasghtglge heaalrqrqr awvllrraad
      601 peglpqamas vgssllalgr paealrvhrr trgllrdprh piaafaratt daltcrrigd
      661 dlaalgrwpe cvaarreava rlrasampat ealasvelae alrrtgqtrd apahlrraie
      721 laeecddpdl agraatllae ysrdhpaeg
//
LOCUS       WP_357655527             463 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655527
VERSION     WP_357655527.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 463)
  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 463)
  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..463
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..463
                     /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=51510
     Region          152..433
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mktsyhvkfw eirpnksatk sgktisytvr wtvagreksk tyeksaqakn wlsdlrqaak
       61 ngepfdietg lplsmikake artvldfvra yvemkwphaa sksrdsmsda lstvlpaltk
      121 etpgrpdakv lrgalrkyal lpegkrpatp pdmaqairwl esasldvqdl netkvirpal
      181 dalalcldgt kagantvkrk ravlhnvley aveleelpsn plhrvkwspp kttetvdprv
      241 vvnprqarel lvavtyvgkr grgrrgrgqr lmamfacmyf aalrpgeavs lrkddcylpl
      301 kgwgrltldv srpevnrqwt dtgdaheqrg lkhrgetdvr vvpippelvk ilrehiaefg
      361 vgedgrifrs erggvvasta ytevwqearm lalmpgqvas plvrrpydlr haavslwlng
      421 gvpapevakr aghgvdvllr vyakcidgqe eivnqrieda laa
//
LOCUS       WP_357655569             313 aa            linear   BCT 28-DEC-2024
DEFINITION  complex I subunit 1/NuoH family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357655569
VERSION     WP_357655569.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 313)
  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 313)
  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 313)
  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..313
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..313
                     /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=33883
     Region          1..313
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 mldvvlrfaa ilvvflvlpl ivgqtehkvm ahmqsrlgpm yaggfhgwaq liadgvkfaq
       61 kedvipaaad rrifmiapgv alvpyllvli aipvdqglvg vdldlglffv lavmgigvlg
      121 simagwasan kysvlggmra aaqlmsyelp lvlaassvam aagtlsipgi vsawqwwwlp
      181 wqaiggvvff laglaelrrp pfdmpiaese iimgpmteyt gmrfalfmls eyvgivvlsf
      241 lttvlflggw hgpllagwvw tlvkvfvlaf lviwlrvsfp rlredqlqkl awvvlvplal
      301 aqlaltgvvk vlt
//
LOCUS       WP_357655533              98 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Nonomuraea
            sp. NPDC050680].
ACCESSION   WP_357655533
VERSION     WP_357655533.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 98)
  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..98
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..98
                     /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=10537
     Region          5..>63
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msttveltrf kvrpeqaeam laarpamlad frgdregflg arlvqlpgde wldvvewrsa
       61 edfavsrakg anlpgiaaff gtiaelvsae egvladaw
//
LOCUS       WP_357655594             221 aa            linear   BCT 28-DEC-2024
DEFINITION  PaaI family thioesterase [Micromonospora rifamycinica].
ACCESSION   WP_357655594
VERSION     WP_357655594.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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..221
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..221
                     /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=22699
     Region          <141..219
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mivesryngp pgsgnggwsa gvfagaydad rpvevtlrrp ppldtpltlt dgdvydpdgq
       61 lvaevrpagd ppapvppvdp atadaasagy pglrdhpfpg cyvcgpdhpd glrifpgrlp
      121 dgrtaaawrt prrvtaptvw aaldcpggwa viapgrpyvl griavtldal pgpgegcvvt
      181 gavvsaegrl avvhtslygd tgrllgrara twvalppapr p
//
LOCUS       WP_357655607             322 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655607
VERSION     WP_357655607.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..322
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35937
     Region          20..230
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtsrsphvrs saslvgraep pigvgmpvyn gepylegalr svlsqkgvdf elviadncst
       61 dgteelcrel artdprvryl rrernvgita nhnkvvhetr geffsyatsd deyhedrlal
      121 lsaalrrhps aaaaisgvee idetgqtigt wrdtaptdqp dpvarlrhrl dnydetmhfy
      181 glmrretllr arpleailpa drvmisglal lgplvvvdel llrhrnhpgs nsqvnharaf
      241 rarempgdqr fflpnveegr allrvirnap ltrrqrlray aalrpwlrrn avsmarnvah
      301 saidvargpr gplsssppre ss
//
LOCUS       WP_357655686             379 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655686
VERSION     WP_357655686.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 379)
  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 379)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 379)
  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..379
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..379
                     /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=40479
     Region          145..377
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrglirsvwd eprppnpapr gwrdwalvgv lvavallega lrpdlpwrgl svivtaglat
       61 tllwrrsrpl lmiaiafgam tpvplltggy spetytmvfl lllayslfrw gsgreavigl
      121 tiilvkicfs mvfdypgpsd avggvtvvfl tlalgvafry rakarmreld qvkllereql
      181 ardlhdtiah hvsamairaq aglataasrp saatealhvi eaeaaralae msamvrvlrr
      241 dqpaglapgr rvtdlqqlag pghsgpsvdv eisgdvddlp psvgaaiyrl aqesvtnarr
      301 harhatriqv rltaddtsvh lrvsddgdss lirpaaspgy gligmierad llggtcvagp
      361 npdrgwsvta vlprtgsap
//
LOCUS       WP_357655698             160 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655698
VERSION     WP_357655698.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 160)
  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 160)
  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 160)
  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 160)
  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..160
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..160
                     /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=17586
     Region          1..160
                     /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 mdielrewca ddaptvlraf qapdmagqas wpivslqdav gwiaswpgag hafavtlfgq
       61 vvgnvavtgi dghdngwvsy wtvpeargrg vaaaavvelt rwafrergly rlelghrinn
      121 pascrvatka gfrpegierq klrydgrryd verharlatd
//
LOCUS       WP_357655782             196 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF4190 domain-containing protein [Micromonospora rifamycinica].
ACCESSION   WP_357655782
VERSION     WP_357655782.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13262498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..196
                     /product="DUF4190 domain-containing protein"
                     /calculated_mol_wt=19694
     Region          <1..115
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Region          114..174
                     /region_name="DUF4190"
                     /note="Domain of unknown function (DUF4190); pfam13828"
                     /db_xref="CDD:433508"
ORIGIN      
        1 mqpgnpgqdp ygqqpphdpy gqqpapgqpq dpyaapqapy gqqppapygq qppapygqqp
       61 hdpygpqpts gqpygqpdpy gqpvgkdpyg aqpygaasyp gagypapqgq qntlglvsli
      121 lgiasiplvc caflgipvgi gavvtgwlgm qkanqglagn ggqakaglic gavavglgil
      181 lvllnivgsf tlptsp
//
LOCUS       WP_357655732             471 aa            linear   BCT 28-DEC-2024
DEFINITION  TldD/PmbA family protein [Micromonospora rifamycinica].
ACCESSION   WP_357655732
VERSION     WP_357655732.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..471
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /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=48445
     Region          31..467
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mtgpgdtgat eldvaarvve lvhqvagpta qaevtvvrhd laltrfansf ihqnvaesgv
       61 rvrlrvhvdg rtatgggslv dadglralvg rtlaavrlcp pdpawpgltp psavhsngll
      121 deatagaepa araervrdfv davggleaag ycrtsyrsga fanslgqsaq grtteaamdg
      181 iarldgadgv arlcagrldg ldgtalgtra aakaraaadp velppgryev vlepaavadl
      241 lqnlawygfn gkrhaerqsf arpgtaqfdp avtliddpty ggampfdleg tpcraltlve
      301 agttravahd rrsaagagtt stghgapggs tfgpvprtvr llgragagda gpaptggvsg
      361 avadtdtaal vapmtrgllv sdfwytrvld pkslvvtglt rngvwlvedg vptravrnlr
      421 fteaypralg pgavlglgrw pvrqpdrtdg gwweapplrl aswnftggas g
//
LOCUS       WP_357655851             276 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357655851
VERSION     WP_357655851.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 276)
  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..276
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30572
     Region          5..83
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mpessritte iaailrrers aqrltqqqla dragtsqsav ariergqrvp giplverlfa
       61 algrqlavtv eeldshldar mdalatrsla dridelgldr lsdrlgdlph lltggsaall
      121 qgapvpadav eiavrwrdsa rftawleaay gqrwnarwre fgglylapee pgehywstry
      181 geiraqmcde lpaaievrhg ersyrvvplv tveltdpqaa allrryrrrs adhraipdgp
      241 tptndpasvh drrsadnrds addpasaagp rprtrr
//
LOCUS       WP_357655963             322 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655963
VERSION     WP_357655963.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 322)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..322
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..322
                     /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=35551
     Region          15..312
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtdrdrspak raperaghsr ervrgiervw llvflapfll lylgftiwpl iatiyysffd
       61 wsgvgpiddf vgggnygtil adplfwlsvv ntlvfalltt viklpislla ailltrkwlr
      121 gkrffrtmff apliipvama glvftyllnp sngalnailr dlglvdqgfd vfanrwsalv
      181 vlvlvsiwqi fgqymiywia alqnvpeevy eaaaidgage wkkltritlp mirpvaviia
      241 llglvnamhv fglvvtltag gpgtstyvvs yfiyqnafgs vpfaygyasa aallfsviaf
      301 vlvsaqglav rraqrlrkey gv
//
LOCUS       WP_357655985             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357655985
VERSION     WP_357655985.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32458
     Region          30..284
                     /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 mtektsanev tglresygda qqtarddrtm rhftirhdgv tlpvtrggqg rplvlcpgln
       61 stqaglhela ellrrdhdvl tfdlrghgla saadrysfea flsdlaavma elgrldpdsa
      121 ptlvgyslga dlavhyaaeh pgtvaelvli dganpvpepf ltetllpefr amwedlatrq
      181 esergtarqv lltaqeildl nieidtvrsr ildryrkidr pislimstsm agdsgeghap
      241 rfnqnwragv erlvrdqphl vtswldadhq lvfthapeia qiirstrrpg gqats
//
LOCUS       WP_357656002             453 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357656002
VERSION     WP_357656002.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 453)
  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 453)
  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 453)
  AUTHORS   ter Beek,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..453
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..453
                     /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=47545
     Region          9..363
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 marrvrpgrs gaalviamgt laaacaapgs dsprpqatsa stmsaapacg tapitmngyf
       61 etgfplpkal tteftkqhpn vtwniredqf avitqnaprv ladnppdlmr lpqvselvkd
      121 nllknldgya tafgwgkwpa sqlqqlrlgp ggrprgegsl yalglnfsmt gvfynkklaa
      181 qvgmsappat laeldavlak aksagitpiv qfnggatggl afplqnlmas ygppqpindw
      241 ifqkpgatid tpsnlraaqh lerwikagyf qkdvnavdya tmmsrfiggk glfmfdgdwe
      301 sgnldkqmag nvgfslmppv qaggkraams apltfgiaan aknadcaaff lnwvatdkra
      361 reigvevggs rpmgpadaym pavksgtvta gtlaagadia kdngamdfia natgaiyaks
      421 wtpqlqklva gqqtpqellk svqadyagql egn
//
LOCUS       WP_357656114             644 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357656114
VERSION     WP_357656114.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..644
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=70086
     Region          <168..271
                     /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          400..641
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpfwrspist tdvarssrrl gwpialdgqv wwtedrpdqg grttimhraa dgtcrellpe
       61 pwsartrvhe yggrpyavtp egdvifacla dqrlyllkdr agrtdradla dreglsdlad
      121 radladregl ndlaeradep vpltpdgdry adllvrddqv wcvrerhtdd gkttravvsi
      181 pigggetrew vtggdfyasp aispdgrhla yitwnhplmp wtgtelrvtr lsdgtswtvg
      241 ggpaesvlap swkddghlyl isdrsgwwnl yqtglhdlsp kplhpleeef awppwtlggl
      301 pyvvlgdgrl avlhgrgdlr lglldpqtgr ltdldppgdg wdpalaadgt gvtgiaygaa
      361 vpkslirvdt vtgqaetlrr dvdelpdlac lptprpvemg hrvhgflypp snpaaedsee
      421 appyvlfvhg gptahegtal dlekayltsr gigvldvnyg gssgygrayr drlkgqwgvv
      481 dvedtimaae wlvaegladp griavrggsa ggwtvmaacc rsdvfaggvs yygvsalapl
      541 hahthdfesr yvewlvgped prlyaerepl alvdgvscpm lllqglddpv vppeqsaafa
      601 dalaergvsc tylafegesh gfrrtetrat alaaelafyq qifs
//
LOCUS       WP_357656045             218 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357656045
VERSION     WP_357656045.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 218)
  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 218)
  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 218)
  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 218)
  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..218
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..218
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23069
     Region          2..209
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtvdavvfdl dgvivdsepv weevrrayva arggtwqpdt qrrlmgmstg ewaeylsgel
       61 gvdrsagqva tevveemarr yavrvplidd adlvvrrlaa rwplglasss ptrliaaala
      121 aadlaaefrv tlstertarg kpapdvylav aerlgvdpar caavedssng vrsaaaagmr
      181 vvavphglyp ldpdaaelaa vvlpsvhdlt pevvdrlg
//
LOCUS       WP_357656190             426 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357656190
VERSION     WP_357656190.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 426)
  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 426)
  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 426)
  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 426)
  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..426
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..426
                     /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=46373
     Region          4..323
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mstryafvgl ghraqmyvda llgdwrdtgt ivglcdvnqt rmnyyverig eqvpcfapde
       61 fgkllelada vvvttvdath aryvvaalda gldvivekpl tidaegceai aaaaernpgk
      121 lvvtfnyrys prnsavkkli segaigdits vhfdwaldti hgadyfrrwh rdkansggll
      181 vhksthhfdl vnwwlaaape lvfaqtdlrf ygqalprgpr pargqgapgl gtdpfildis
      241 tdehlkrlyl daehedgyir dqdvfgpgvt iddnmsvlvr yanramltys ltahapyegy
      301 rvvfngtegr ieldvlerpw tpehaaidps aagkehmaga geklilhrhw qepeeiaieq
      361 gegghgggdr lllddvfrgp gddplgrpag yrdgirsvlv gvaatrsagt gapvrlaadg
      421 trlvga
//
LOCUS       WP_357656205             337 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357656205
VERSION     WP_357656205.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 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   4  (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
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..337
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..337
                     /product="helix-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=36878
     Region          21..313
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mvntsarllr llsllstrss wtcadlsaql evaertvrrd iarlrelgyg iesemgpwgg
       61 yhlgpgtsip plildeeeal avavglrtaa fsgvsgsdqa alsallklrq vlpariadrl
      121 geldaaftht arpddsqisp allldlatac rrgertqlty rdragttstr rvdpyrliyt
      181 grrwyllayd ltrqdwrtfr tdriidatat gqatalpdpp dpaqmvstgi alrpyparvt
      241 irlavpadea rrlvpptvgv hhpdgddati idiggpdadg laryllslgr plqilhpeev
      301 rqafltrtqq llkdnqwhkh ppitdtatcs dgccqpp
//
LOCUS       WP_357656218             160 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357656218
VERSION     WP_357656218.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 160)
  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 160)
  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 160)
  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 160)
  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 160)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (residues 1 to 160)
  AUTHORS   Rosinski,J.A. 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 160)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..160
                     /product="GbsR/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=17834
     Region          1..158
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mteispdeaa fvdrlglffe mvggprtmgr iygwlmicdp pqqsltelaa algvskpsis
       61 tvirpmqegg lverlpsstr ehryritpgg ftrvlqvqld rmgagaeaae fglsvigedr
      121 peqrdaleel rdfcafsate vhdefmrrwa dyraakrrgr
//
LOCUS       WP_357656228             250 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357656228
VERSION     WP_357656228.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=26243
     Region          1..241
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 merltnktvl itggtsgigf atarrlldeg ayvvitgrdq arldtaaegl ggervlpvra
       61 dvsvdadldl lmrrvetwrs aldavfanag iadfrpeftp kdfdhtvgin fkgvfftiqk
      121 alplmgdgga vvinaswtlh rglpaasiya askaavhnla rtlgtdlapr girvnsvspg
      181 yietemyrsa idpdaetrit aevplgslgh pddvaaavaf lvsddasyit gqdlvidggl
      241 vgaaplglrl
//
LOCUS       WP_357656255             309 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357656255
VERSION     WP_357656255.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..309
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..309
                     /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=33867
     Region          10..305
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msddaiarpa avagggrpsr lrrdgraaaf faapsmiglt lftlfpivls lvmaffrwpa
       61 vgertftgve nfttlftdpv frrallntll fvvlylplnl vvsvglavwm gprikgrkal
      121 rvvfflpvvt pmvanaivwr miyqpnglid gslyaatgth apnflgeqgw amfavvamsv
      181 wqgfgynmlv fsaaldaipr hlleaaqidg agpwrqffri mlpmispalf fastmtlits
      241 fqvftqpflm tgggpgmdte tlmmfvfdkg fsiyqyglas agawilfvli lgvtavqfag
      301 qrrwvtydv
//
LOCUS       WP_357656276             696 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc ribbon domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357656276
VERSION     WP_357656276.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 696)
  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 10591252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..696
                     /product="zinc ribbon domain-containing protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70216
     Region          3..23
                     /region_name="zinc_ribbon_2"
                     /note="zinc-ribbon domain; pfam13240"
                     /db_xref="CDD:433054"
     Region          <180..419
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          439..458
                     /region_name="zinc_ribbon_2"
                     /note="zinc-ribbon domain; pfam13240"
                     /db_xref="CDD:433054"
ORIGIN      
        1 miicrecgnh ngdadtfcgs cgsflewtge ktvpkipvet vqeaerefrq kptllqriag
       61 viapapggsp vnegvvrvgd ptgrgsgplg gppgvrpgpp glgppgvrpg ppglgppgvr
      121 pgpsglgpsg pvppgarpgp pgvrpgppgl sppagrpgpp glgpsgpvpp garpgppgta
      181 pvggrsgppg vgsaggrpas aaprppgarp grpglpgdlp aggsagaggp vaaagapava
      241 apprrlpppp pgvpaarlpd raartglpas gppgervvpp arptadgpgd sdtpadeass
      301 thdlpaagas spadgtpvgp pqtastgavv psrrlppppp gvagatlptv prkpvapsmp
      361 vrrdtraaph tsalvapdgs adpvrpgapt tggragarpg atttatatpe evspqavrpr
      421 vatvgnraat rrrqpgdlic gecgegnapt rrfcsrcgds lrsaevvrrr wwqrllprrg
      481 prvtaagarp gtpgggrpgg vggvlhsiyq rsnavaavll faigvayliy pplreringa
      541 vsgpvtgard wadrkinprf vavrpvqvtg gasvrdhgpe lsvdqyrnth wqvrwdrekp
      601 ptvtlrfaae vdlerlivta gtaedytash rpktlhlvys tnrsdtltve dtgepqtltl
      661 dgadgvtsvq iqvtdvhrae kgtdvavsef effare
//
LOCUS       WP_357656290             154 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357656290
VERSION     WP_357656290.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=16611
     Region          1..139
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msknvdgqig tvaalvrstf lvnavyansa reygltqqqg qllcvlmaqp ygmselgttl
       61 glakssltgl vdrsernglv qrrpdpqdsr avrvaltprg aklvdefyte tcrrveelts
      121 gfapaeldtl aallgrvvad nkvptvfmep drpr
//
LOCUS       WP_357656308             810 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357656308
VERSION     WP_357656308.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 810)
  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..810
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..810
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=86677
     Region          5..809
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          598..626
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(642..643,646..647,649,679,682..683,686..687,
                     689..690,719,722..723,726..727,730)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          642..666
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          671..707
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          718..746
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgetgrdalr afaeelrrlr qlaggpslnt lvavaarrgr plarstlsdk lnakslpdrd
       61 fvadflgacv ayaeqtgirl pagladparw eaaywrmlga adaaraedrl aaaraergrp
      121 edtgsvppaa gpggripfvp rqlpaavrhf tgrsaplaal tallteppgp pgtvpvstiv
      181 gtagvgktal avywahqvad rfpdghlhvd lrgydpespa lspaeavagf lealavpper
      241 ipaalaaqaa lyrslladrr mlvlldnard adqvrpllps spgclvlvts rnhlpglvaa
      301 egarplplgl lspaegrell srrlggdrva aepeavdriv aaaaglplal aivaaraaty
      361 pefglarlaa eltatrgald afssgeanvd vravlswsyr glepvaadlf rvlgahpgpd
      421 vsvaaaasll avstaevrrp lavlnranll tehtpgryvl hdllrayave lamatdsarl
      481 rdaalrrlld hylhtayaaa lllhkhrddi alpaaspgtt avvpadrdea wawlaaehra
      541 llaavdlaae hglpthawql awsvntyldr vgawqdqsha qqvalwaata agdrdgqara
      601 hrnravaclr lggydqardh lerslrlyae lgdgvgggrt elnlgilaer qgdhrraldh
      661 aqrahrlfaa aghaqgqana lnnigwyhiq lgdharaldy cgralaqqqr tgnryweaha
      721 wdslgfahhq lgrhrdaldc yrhalalwre tgeryyesvt lmhlgdshra aaddaaaraa
      781 wrqaldvldr lghpdaaqlr qrlgetrpap
//
LOCUS       WP_357656318             529 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357656318
VERSION     WP_357656318.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 529)
  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 529)
  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 529)
  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 529)
  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..529
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..529
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=57435
     Region          55..529
                     /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 mredltrrrv lgiggalglm aatglsasaa larrpsitga elrsavplpp pfhvplpipa
       61 vlapvstsgg adryeitqra asaeilpgvr talwtyggtf pgptiesrrg rpitvthhne
      121 lpvptvvhlh ggrtpaasdg yptdlvlpeg wpaatthmgh gsahvmhdpr aavtqltrdy
      181 tfpldqrpal lwyhdhrmdf tapaiwrgla glqivrddae dalglpsgrr elplmiadra
      241 fagdgslayp aldptlrerp gvldayiagv lgdvilvnga pwpvheadaa ryrlrilnas
      301 narhyeleav gddgrpldlv qigadqglla apvthrllpi apaerydvii dftglpvgsr
      361 vkivnrlgsg rtrdvmafri arkatddsri patlstdlpg wrrseavrtr efsfrtgrmr
      421 gdhgwliggl pfdparsdvt vglgdvevwr lvadvhhpvh lhlvgfrvls rsgrpplpyd
      481 aglkdtvslr pgesveiitr fdgyrgrylf hchnaehedm gmmanlevi
//
LOCUS       WP_357656329             263 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357656329
VERSION     WP_357656329.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..263
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28066
     Region          9..255
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mttqqapaiq vhgleksykd lhvlrgvdfd varggvfall gsngagkttv vkilstllka
       61 dagsarvhgf dvatqaadvr esisltgqfa avdeilsgre nlvlvarlrh lknsgqiadd
      121 llarfsltda garkvatysg gmrrrldiam slignppvif ldepttgldp qarievwqav
      181 kelaaqgttv llttqyldea eqladriail hqgriivngt laelkqllpp akveyvekqp
      241 tledvflaiv gadgkhhhaa tna
//
LOCUS       WP_357656485             288 aa            linear   BCT 28-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357656485
VERSION     WP_357656485.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 288)
  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 288)
  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..288
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..288
                     /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=31213
     Region          <11..138
                     /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 malaspaaaa nrptwrwpld ghprvlrhfa pppepwlsgh rgidlaaaps tsvvaagpgi
       61 vrfagplagr gvvtiehtdg lrttylpvna svrryqrvtp gtrigviert tghcreaclh
      121 wgllrgshyl dpllllgrah irllpywnld apdtaalstq pppsstellh pspagmapst
      181 attattrllt spprssrapa pgttvsseps wpaaatpafr laarsaskpa iavislstlf
      241 salllftlmr rhrstrtqhp raargqhrkq qrnrpprkrr rrarptkr
//
LOCUS       WP_357656459             294 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357656459
VERSION     WP_357656459.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 294)
  AUTHORS   Rosinski,J.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..294
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..294
                     /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=31391
     Region          31..>82
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          106..272
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mqasgqlgef lrsrrsrlsp eeagvatygg rrrvpglrre elallagvsa syyarleqgq
       61 atnaspevld alsralrldd terrhltgla aghrrpaarr ppperidpav rqlvaalgdv
      121 pvlvlgrrld vlawntagha lfaghldpav vdrpdrrpnm arlvfldaht rdlyvdwptk
      181 aravvatlrm asgqhpadpl laalvgelav rspefaagwa dhrvkaggaa gytmrhpvvg
      241 eltvtqqtlr tgddqavvva ttapgspsqa amtllvhaav tgratvrqpl ptyg
//
LOCUS       WP_357656526             533 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357656526
VERSION     WP_357656526.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..533
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..533
                     /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=55434
     Region          9..533
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msdasalpsh advviigagh nglvsavlla ragldvlvle aaeviggaar tenpfpkvpa
       61 lrhstgsyll glmppellaa ldvripvlrr dphyflptpg gpgapyllfg sdtaatrrql
      121 teffspadva addalqaela qlradlapaw lteplpveqt aeryvrprlr qvfvdlvrgs
      181 vadhlarfdf rsellvsmya vtdglsglna gpddpgtghn flvhnmcrlp gsdgtwmite
      241 ggmgtvsrtf aeaaraagat iltgarveav tlsggaasgv rladgrevaa evvlgacdpy
      301 rlmelvpdga lpaelgarmt avrrpgttfk lnlaltglpr fsclpadaps pfgstihllp
      361 gsaslvgagg aspmaalram wadvqagrlp deptiewylh ttvdpslsdp aghhssalfv
      421 qsvpytlagt dwdtalpgyv trlveicery apgtgdliad avplpppgie ahfgitgghi
      481 hhvdntvsft drmpyatgid gvyagsagch pagsvigaag hnaarrilad lgr
//
LOCUS       WP_357656556             106 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Micromonospora rifamycinica].
ACCESSION   WP_357656556
VERSION     WP_357656556.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 106)
  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..106
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..106
                     /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=10986
     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 mavvkinaid vppgasaele krfaaragav enspgflgfe llrpvagesr yfvytrwese
       61 eayqawaagp sraahaggpg ggqqrpvatg asllefevvq qvtgkg
//
LOCUS       WP_357656563             306 aa            linear   BCT 28-DEC-2024
DEFINITION  proteasome assembly chaperone family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357656563
VERSION     WP_357656563.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..306
                     /product="proteasome assembly chaperone family protein"
                     /calculated_mol_wt=33525
     Region          15..262
                     /region_name="COG1938"
                     /note="Predicted ATP-dependent carboligase, ATP-grasp
                     superfamily [General function prediction only]"
                     /db_xref="CDD:441541"
ORIGIN      
        1 mldphelyql tddlpdlgqp vliqaltgfv dagnasrlar eqlltsldar tiatfdvdql
       61 fdyrsrrpvm tfvedhweey dapelalhll ndddetpfll ltgpepdlqw erfvaavgav
      121 aarldvrltv glnsipmavp htrptgvtah atrreliagy epwlqrvqvp gsvghlleyr
      181 lgqlgrdalg faahvphyva qteypaaaev llasvsrstg lllpndslrs aaevvrveid
      241 rqvaqtdeav alvkaleeqy dafargrgek nllaaetgpl ptadelgael erylaeqtrp
      301 gdtpnp
//
LOCUS       WP_357656585             166 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357656585
VERSION     WP_357656585.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11441181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=17813
     Region          1..165
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mtliqpvset dlpavaeiya hyvtesvatf detpldveaw rlkaaaiaea glpflvakqe
       61 dggvlgfayc gryrpkpayr htvedtiyls pgatgrglgr lllgeliart getdarqmia
      121 viadggdpas lklhaafgfa eagrlksvgf khgrwidtil yqlelp
//
LOCUS       WP_357656610             835 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357656610
VERSION     WP_357656610.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 835)
  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 835)
  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..835
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..835
                     /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=93018
     Region          14..817
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 megvsllvdr lpeeidadpd aifdafvswn sergltlypa qeealievvs gsnvilstpt
       61 gsgkslvaag ahfaaltrdv rtfytapika lvsekffdlv svfgtenvgm mtgdasvnpg
      121 apiicctaei lanvalrdga aadigqvvmd efhfyaepdr gwawqvplle lpnvqfilms
      181 atlgdvamfe rdltrrtgrp tsvvkhterp vpliysyrmt plhetleeml rtgqapvyvv
      241 hftqaaamer aqslmsinms tkaekeaiat liggfrfttr fgralsrlvr hgigvhhagm
      301 lpkyrrlver laqagllkvi cgtdtlgvgv nvpirtvlft alskydgnkv rrlrarefhq
      361 iagragragf dtigyvacqa pehdienaka lakigddpkr rrgyarkkpp egfvgwseet
      421 feklqtaepe plnsrfkvtn amllavinrp gdcfqamkhl ltdnhedrkw qrrhisqaia
      481 iyrsllaggi veqlteadeq grrarltidl qedfalnqal stfalaafdl ldhdspsyal
      541 dmvsivesil ddprqilsaq lkkargeava qmkadgieye ermeqlaevm ypmplddlll
      601 gayetyrhgh pwvgdytvsp ksvvrdmyer amtfadyiqf yelarsegtv lryladayrt
      661 lsrtvpehlk tedlidliew lgelvrqvds slideweqla npeealerna qleakvrpvt
      721 antrafrvlv rnamfrlvel caiekedelg elapdvdwga aldayyadhe eiftdadarg
      781 pallrieeed glwkvrqtik dpagdgdwgi daqidlagsd eegravvhvq glnrl
//
LOCUS       WP_357656695             397 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357656695
VERSION     WP_357656695.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..397
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42333
     Region          16..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 mrreefyrea rddldgplhg lsvldvtkvw sgplatslla dmgadvvrve lpygrdgevp
       61 peipgtglsw fretvnrnkr svgldlrqpa greaflglvr dadvvvenfk pgtldgwgvg
      121 yadcrrvrpd vvfvsitgwg qfgpdvdrpa ydpvvqaasg wmalngdpag rpvraptfla
      181 delaglhaav galaalahrd rtgegqhldv amldsllass cglltlaatg apparwgnet
      241 dfavpsnvys crdgevylsv aldkhwrala etigrpelah apgygrgaqr rgnrvevdal
      301 vadwcrgrtv devmaafraa hlvaervrtl aevaadpqvs ardmlqptvl hngtvapltg
      361 pavkfsrtpt rirrgapaag adsrdvlpgt apdpdgp
//
LOCUS       WP_357656663             242 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357656663
VERSION     WP_357656663.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 242)
  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..242
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..242
                     /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=25714
     Region          8..183
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mddrlggdec liwrcpvapv pgplsalldd aerarartla heqararfvt grvvarllaa
       61 rhadtaprdv vfsstcrhca gphgrlevht atgvlhvsvs hsaarvvvai argtvcgvdi
      121 ervalrggri pvsalstaer rvlaslpeqr rlagfirywt rkeavlkatg dglvlspadl
      181 tvsapdapac llswanrppp htevhlsdla vgdgyrgala tlgrpltvve cdvdprekas
      241 hl
//
LOCUS       WP_357656775             948 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357656775
VERSION     WP_357656775.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 948)
  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 948)
  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 948)
  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 948)
  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..948
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..948
                     /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=102287
     Region          1..246
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          129..948
                     /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"
     Site            order(727,730..731,734..735,737,767,770..771,774..775,
                     777..778,807,810..811,814..815,818)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /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"
     Region          846..872
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          886..914
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfavlgpvr vwraaaevdp gsrqqrlila lllaragrpa titdfvallw gerpprsavn
       61 ivhlhlgglr rlfepglppr apgrwlagda agyrmvvgad eldllrfrel arrartvddp
      121 teafatylra lelsrgpcag aanltsrpva dfeavdneya dlvgeaadla lragtartvl
      181 pvlrrvagqr pldeavqarl lltlaaagqq aeavtryqel rdrlsddlgi dpgrelqeay
      241 rkvlrqgdsd pagpsgkpar dedpgpggll vspaqllpdl phftgredsl rralavihgr
      301 aaalrivvve gipgvgkttl athlayrvad efpdgqlyad lrgldpdaal apgevlqafl
      361 halgvrgpdi pandlarsgl yrsvlaerrv livldnvrda dqvrpllpga pgslvlvtsr
      421 yslaglaath gadvltldvl sepeardllv arlgpgrala drralaeivt lcgglplala
      481 vvaartmarp grplaavare lhetrgsldg fdvddphsdl ravfswsyrg lgpaaarlfr
      541 llavhpgpdv tlpaaaslag lpvraaravl gelvrgrlvt errpgrygth dliaayagel
      601 lratdtvadr daaadrllgy yrraayaanr hinpeidaep pglpdgtvde npatgaeavd
      661 wfvaerevlr svmrqaidrg rvyeawqlel tvqgyyqrdg wwqewatvvr ecldaasdag
      721 dpagaaemlr slagahfylg dstsalalle ralvlfgelg nvsrealtlr nlgevsfavg
      781 dydrstachh ralriaestg drmaqldvlc rlaetryevg drassfetid ralalseqld
      841 rdsrrgechl rranlhlrer qyvealtdwt aaeevstaig hrvmmirakl glgdtyhamg
      901 drsaartawl aalslsddad pgqadpgqea girrrlaelg hrtddlaa
//
LOCUS       WP_357656768             225 aa            linear   BCT 28-DEC-2024
DEFINITION  trimeric intracellular cation channel family protein
            [Micromonospora rifamycinica].
ACCESSION   WP_357656768
VERSION     WP_357656768.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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 225)
  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..225
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..225
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23091
     Region          9..207
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mstsfqvalw iqllaaglgg lqgalfaage rdrridvlgv ivigltmslg gsllrdvvln
       61 qppvvvwqnw ylpvagvsav lgmalhpvfa ratwvitvld avvmglfgai aaskalslgv
      121 geagalvvgv igaigggmlr dvilglpvsi lrvgtlyava agagvgvlvl ltafgtrtpl
      181 aglgcvvvta svrlaairfr wtfpeqravr lrrgkdpqpa rrptg
//
LOCUS       WP_357656787              99 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357656787
VERSION     WP_357656787.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..99
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10885
     Region          12..>90
                     /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 mserkawtdk raeimsrpga gaayeaarir felgeavrlr reelgltqse laeraglqqp
       61 avarfeaggt mptipmlerf aealglrltv qfqplreas
//
LOCUS       WP_357656789             169 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357656789
VERSION     WP_357656789.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 169)
  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..169
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..169
                     /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=18357
     Region          12..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mradarrnrd rileaardav aergadapme liarragvgv gtlyrrfpdr gmllaalaeq
       61 yvhelmdald havtaepdaw sairafvvys vekgrgaiav alagasapqa rqalvrrlde
      121 lvllaqadga mrsdvgtddl mellnvfach pdvipkrflp lmldgldrr
//
LOCUS       WP_357656814             394 aa            linear   BCT 28-DEC-2024
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357656814
VERSION     WP_357656814.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13559706
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..394
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /calculated_mol_wt=41071
     Region          14..>66
                     /region_name="3HCDH"
                     /note="3-hydroxyacyl-CoA dehydrogenase, C-terminal domain;
                     pfam00725"
                     /db_xref="CDD:395588"
     Region          110..384
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mtvqehgiaa ghvlllryln raailcgqdy vtgsdidtam rlgcgltagp lamvddigrd
       61 rvlelmaaaa vppapllttr awpgrpdrds prsgrpaape pvaaavpssv givgsgtmav
      121 giaqalvvhg lrttlvarrd eraemarrgv aaaldkavar grvapatage aagrlrtsva
      181 lddladcdlv veavveeeda kravfaaldr vcrpgtvlat ttsslsvadc aaatgrpadv
      241 vgmhffnpas vmrlvevght phtaprttgv aralarhlgk vpvccpdrsg fivnyllfpy
      301 lndavgmver geagvaeldr emeeahgfpl gpfalldtig ldvslailrr lhqqfgdpat
      361 rpgamltrlv aegrlgrkta agfhaqrpgr gaar
//
LOCUS       WP_357656764             233 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357656764
VERSION     WP_357656764.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   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 233)
  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..233
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..233
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24155
     Region          2..233
                     /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 mkptivlvhg afaesaawsg visrlqaagh rviaagnplr sltadaaavs allasiddpv
       61 vlvghsygga vatnaavghd nvralvyvaa lapdkgenvp dltgrfpgat lgahlyevpl
      121 adgtadlyvr pecyhelfaa dlpfdrsdva aatqrplnsn altegsgepa wmtvpswfvy
      181 peldlaiplg tyrfmaeran aresvevpga shalpmsrpq avadvilraa aav
//
LOCUS       WP_357656816             476 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Micromonospora rifamycinica].
ACCESSION   WP_357656816
VERSION     WP_357656816.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 476)
  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..476
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..476
                     /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=49857
     Region          23..474
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mttaelsdaa dpgtddprap ltrlarladp gslrlfgphd avragharig gspvvlfctd
       61 atraggslgv eestqivtai dravrdrlpv iglwhsggar ltegiqsmdg vgrifaaiir
      121 asgrvpqisv vlgpaagaaa ygpaltdmvv madagrmfvt gpdvvrsvtg eqidmeglgg
      181 veahgrksgv vhvaaasete ayaatrhlvg vftrpgwfdl ssvtddaglv dvlpasarra
      241 ydvhpliarl ldgpgdeepa flelqprwar nivvgfgrla graigvvann plhrggclds
      301 lsaekaarfv rtcdsfgipl lvlvdvpgyl pgvnqewggv irrgakllya fgeavvprvt
      361 lvvrksygga yiamnsrslg attvltwpda evdvmgpeaa vgilhrrtla aapeadrerl
      421 rrelvtehrr isggtrrgla lgmidevidp aasrrriaev lataaagrgs hgnipl
//
LOCUS       WP_357656833             208 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357656833
VERSION     WP_357656833.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 208)
  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..208
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..208
                     /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=22703
     Region          16..>141
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaepgprry dslrratqar etraeiagaa rrlfvsqgwa attvrdvare agvsvptvya
       61 aygnkagltq aladaadlsa dvsqqlaele aaasdprrql aamaaydrrl feragdvial
      121 vreagrtepe laalyrdarr rgdetrvqvf sswpagvlrh gldvpsavdv yaamctidvy
      181 ttlttergwp pdriqrwwse alarella
//
LOCUS       WP_357656924             173 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357656924
VERSION     WP_357656924.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=18636
     Region          34..151
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 milrsratgr avaykvfyrl pvtvrrrlvr lagpkyvvga vtlvrdsead gagrllllrq
       61 ppghswtlpa gllqrgeapv vgaarelhee sgvrlspdrl rpavpnalvh trgwvdmvfe
      121 vevpasttil kvdgaevlea swhplddlpr lsratanllg hygigphagq pat
//
LOCUS       WP_357657002             257 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657002
VERSION     WP_357657002.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 257)
  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..257
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..257
                     /product="ABC transporter permease"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26877
     Region          3..249
                     /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 mtrarllrgv vgaagflaag elvirfglsr elvfpppsai lyeavlllad rdflmgaltt
       61 ltnwalgllv avavavpagv llgaltpmer avrplleflr pipsvaiipl aillipvdel
      121 mkvsvivyas vwpilintly gmhdvdplak dslrsfgfgr lavlgrvslp saapfvatgi
      181 riaagialii avsaellagg vaglgvfvvq agsgnrtdli maatfwagaf gllsnvalqa
      241 aerrlfrwhr vrtgavs
//
LOCUS       WP_357657047             172 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357657047
VERSION     WP_357657047.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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..172
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..172
                     /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=18946
     Region          1..85
                     /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 msdvvftapa vddlrrigpd avpkvlkkil llldnpeagy plggeltgfr klvvgrntwr
       61 vvyritedks veicevwavg eradaevyae atarvreaga drpevvqlgq vierlgtlad
      121 hirvveappr epvpdwladr lihtvgmare dvaaldlqea vdlwaeyrsk ps
//
LOCUS       WP_357657072             395 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657072
VERSION     WP_357657072.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 395)
  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 395)
  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 395)
  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 395)
  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 395)
  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 395)
  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..395
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..395
                     /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=41962
     Region          106..388
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtaptlrgrl tlvygtlffv agltllgvty llfnqqleqk tvsiivrggg pgsldsdtgs
       61 ldgdramnwm kqqqtllrga attslltqga ialavvgcaa agvgwviagr vltplrqvte
      121 tarriaaapv aerglheria lngpadevke ladtfdtmve rldhsfdgqr rfvanashel
      181 rtpltlnral velamhrrta sadvkqlges lleinarher lisgllllar aeheigdrsp
      241 vdladvvshv vaqataeate skvtleeaag paptsgdall lerlvhnlve ngirhniddg
      301 tgwvratsri ahdgrvevev sntgpavpsy eiptlfqpfr rlgpdrvvta ksaglglsiv
      361 rsialahgge vtarprdggg livtatlppq spahr
//
LOCUS       WP_357657088             168 aa            linear   BCT 28-DEC-2024
DEFINITION  (2Fe-2S)-binding protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657088
VERSION     WP_357657088.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 168)
  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..168
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..168
                     /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=17782
     Region          11..168
                     /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 mtriipegnv vtlrmrvngv trslelepwv slldalrerl gltgtkkgcd qgacgactvl
       61 vdgerinacl alavqyedrd ittiegithp iqqafiehdg fqcgyctsgq icsaigmlae
      121 hgagmpsavt epgasglsea eirermsgnl crcgayngiv daikevar
//
LOCUS       WP_357657113             595 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Micromonospora rifamycinica].
ACCESSION   WP_357657113
VERSION     WP_357657113.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 595)
  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 595)
  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 595)
  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 595)
  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 595)
  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..595
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..595
                     /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=65916
     Region          44..>592
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mdvdaghgaa lggalpaqpg elplarrlrs llswpasdgd pvtqlvrthr gihssadasv
       61 lrraytiaen mhrgqyrksg epyithplav aqicadlgmd tttlvaallh dtvedtrytl
      121 qalsedfghe vahlvdgvtk fdkafygkaa eaetirkmii aagkdvrvli ikladrlhnm
      181 rtlgvrsaas reriarktqe vlvplcdrlg iqtlkrdldd vvllhlepde harlaryvhd
      241 rpgwdayldd vvaqakvalr rsrvdaevsv rprhlysiwk dtvagghtvp ydlprivivv
      301 dgpatdcyaa lgavhgrwrp vpgrfkdfia spknnlyrsl htsvcgpqdh tvemlirtre
      361 mhrcaeygva adfrfprasg etsntdrlsw lrrvldweqe apdpaqflqs lrcdlaeaqi
      421 qvvadgrqvv lpagatpvdl ayelgtergd hclaaringr laplaselde gdvveiytes
      481 daesgfeatv aprgprrewl dfvksphaqm qisrwftdht epgisiadkv rlgratigla
      541 lrkhdrglas dlpllrlsee lgypdletll vavfdravep dtvvrqlidl vdhrq
//
LOCUS       WP_357657216             324 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657216
VERSION     WP_357657216.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 324)
  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 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   3  (residues 1 to 324)
  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..324
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..324
                     /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=35344
     Region          1..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 melrqlryfv tlaeelhfgr aaarehivqs alsqqiqrle reldvrlldr sthhvdltta
       61 gaaflvearq ildhvsraaq vartaaasap tlrvgiidag ydtmpqilre lhrnhpgiti
      121 hqveagtpeq yrqladgrld iaighasqtp aevtsnlirl dplgvlvpdd hrfadldgvp
      181 vaaladelll lgeesqtpel nqfvlalcrs aglaptlyeg tvessraaad lvlqhrcvhc
      241 vpssfrssnr pgttwrplsd pathypwsll whdanpsphi aividiarrl aerldwlepv
      301 apaaepasge gasaatsrrs ddpl
//
LOCUS       WP_357657223             180 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357657223
VERSION     WP_357657223.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (residues 1 to 180)
  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 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 18527266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..180
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18549
     Region          1..78
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          84..178
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 mnghdaeigs rlrrlrearg islsalarsa gigkatlsgl elgtrnptle tlyavagalg
       61 lpltalvlep gappaeavhv pgaavtatll evfeeptatf ellrmsvrpg ivqhspphap
      121 gvtehvtvya gvlragpadv pllaapgehi swqadvphiy savgpeeava tllirsprqp
//
LOCUS       WP_357657237             370 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase 5 family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657237
VERSION     WP_357657237.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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 370)
  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..370
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..370
                     /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=40341
     Region          4..322
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
ORIGIN      
        1 msarfgvnyl prenwwyawa edddtfaedl hqiaslgfdh vrvqclwplf qpnplwvspr
       61 alrrlvhlld raaengldvc vtvldgwlsg fdfrpgwlke vdpftdpeav naaellvgav
      121 araveghpal wcvdvanepn vlmkhlkage geawaarmlr aaraaavpvt vgvdhvpwms
      181 ddapigrafl agacdlipvh awpyftgala rvgeerawai pdhlsqvara tpgaadkplw
      241 iqevgvsplw ltdvavedfa ermlrraaai pglgavtwwa shdisrrftg fdeleyglgl
      301 idaegrtkpi gsrvaevvae lrdrppvpsa aepaivlptg rapdiafaeq wfahmgasag
      361 paielersas
//
LOCUS       WP_357657337              95 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357657337
VERSION     WP_357657337.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 95)
  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..95
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..95
                     /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=10117
     Region          3..>92
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mvdiarqlls qllsghlapg trlpserqls etlgvgrstv realkaldvl giievrqgdg
       61 tylrqstssl lpsaiewglm lgqpqvldli easkp
//
LOCUS       WP_357657381             303 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657381
VERSION     WP_357657381.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 303)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..303
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..303
                     /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=32284
     Region          9..301
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mslrlvppva rvsgkgqrwa eartggllal paavyflvfw lvpfvaavyl sftsydfagt
       61 pewtgldnyr rmlgdpgfwn sarvtaayti asvvpsivlg laiavplskp grynaflrgl
      121 vmipaamplv atsmvwsvif adkglanali glvgvgpkpw ltdeglalwa lvimttwkhl
      181 glfviiltag lqglplsvfe aaaldgagpi rvfyritlpl lrrtllfvlv iavvgamqsf
      241 vpaflltkgg pagatevlpl ylwatgfgfe rmgyasaiam vllvamlals lvqfrvlrgg
      301 edg
//
LOCUS       WP_357657388             230 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357657388
VERSION     WP_357657388.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 230)
  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 230)
  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 230)
  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 230)
  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..230
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..230
                     /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=23131
     Region          4..229
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msavlvagsd ggigracvaa veatggaafg vdlaggidit tpghvekala qatavhgris
       61 gvvhavgmsg rslgdggvve ctdtawhevh rvnhesvfrl lraaipamge ggsivvigsa
      121 lgssldddfr tvayasakga liplirtaar eaaphgvrvn lisaglvatp msrraqtsea
      181 ikaklpslmp lgaelcqpee vaqavlwlls pssgrttgav ipvdggwhlr
//
LOCUS       WP_357657393             275 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657393
VERSION     WP_357657393.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..275
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28224
     Region          43..239
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mklvvaaivv llglvarpaq aadtieahyk vagpwavata dapgyklyyp adlgaggvkh
       61 piitwgngtn avptqysgll nqlaswgfav vastdmttgt gsemiaaaqy liarntdsss
      121 vfygkldvtk vgavghsqga ggsvntatks gglidtvvpi alpapiwvss gdkfyvdqla
      181 cpvlfvsgan dtlispnsal qtyygqvpga aakaqlkgad hntiqgtggg flgyvtawlm
      241 yqlqgdtyar gafagttpel ntnagwqnqv eknlp
//
LOCUS       WP_357657485             110 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657485
VERSION     WP_357657485.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   4  (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
REFERENCE   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..110
                     /product="PadR 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=12029
     Region          8..104
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrqmqeptfl iltalaagpq hgygvitdve risdcqvrlr agtlyaafdr lqeegliaed
       61 reeivdgrvr ryyrltgdga arlaaeaerm rrhaqaatar lraigsagta
//
LOCUS       WP_357657489             202 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357657489
VERSION     WP_357657489.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 202)
  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..202
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..202
                     /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=21610
     Region          12..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnqsaprrgr grpavltrer ivaaaieild aegldaltmr rlgtqlgvaa mslyrhlpnr
       61 davlaavvdh lfaeavidld agtpwpeala rfadsyrrml lghppavpll athpvdidlg
      121 lellaglldr feaaaiprqa altaiqsvav yvlghalaqv gtppgttaae sdvtaaafyd
      181 ewfktglram vsgferqldq er
//
LOCUS       WP_357657494             345 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657494
VERSION     WP_357657494.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 345)
  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 345)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 345)
  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..345
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..345
                     /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=36533
     Region          73..338
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrngailavv agvslvnglh ldhipvwrql lfavvavvay lhgrhlpvrr dwlvlgvvai
       61 pgvvelgvsl wdgvgglmam alfavlpwla grfrrqqael veagrqrvgq lereqqytae
      121 rvklherari aadmhdslgh elalialrag alelaadmne tnreaaaqlr asavtatdrl
      181 rrtigllrds ggaptdppde sietlverag ragmavtlyr dersavlppl ldraahrvtq
      241 esltnaarya pgaevrvtie rdadmvavtv tnapslteaq stggggtgla glrervrllg
      301 gtleagptgp gaanrpgagd gsriggftvm arlpwpkesd tgdna
//
LOCUS       WP_357657551             514 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora rifamycinica].
ACCESSION   WP_357657551
VERSION     WP_357657551.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 514)
  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..514
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..514
                     /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=52453
     Region          17..266
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(17,40..41,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,78,94..97,101,103,140,142,
                     144..145,147,156..157,160,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(24..25,27..30,32,44,46,78,94..97,101,142,144..145,
                     147,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(28,101,103,140,142,144,160,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(156..164,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <280..442
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mpdvtplttr dprqagpyel vgrlgsggqg vvylgrddqg rwvavkvinv dlrqhpkaks
       61 qfakeiaaar rvapfctaqi lfadvdgdlp yvvsefiegv tlqrhvreqg pisgnalhrl
      121 avgtatalaa ihqsdvvhcd lkpdnvilga dgprvidfgi araldvtetm tdrimgtapy
      181 maperfrdde vgpasdvfaw agtiafaagg qppfrtgpva avmhrvlhdp peltglsgpl
      241 avligqcldk dhrmrptaqe vllrllgrdt hpgtavplqs vlragtdaaa tqqlprtlst
      301 vapvsppvap aapdgpvpaa vdpwptmstv lpaptdpapp dpatappata wptptspata
      361 whgptgtata gptptspata wptptgpata gpdpagaatp pggrtavpap dhpgrpapav
      421 tpstgrdgfg rrlrrqwadp wgvstaiflg algtaagyva ttavgtaaav gsvtlvvvyg
      481 vrllvaaalp psaapdgppa attgpggpap rtda
//
LOCUS       WP_357657605             416 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora rifamycinica].
ACCESSION   WP_357657605
VERSION     WP_357657605.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..416
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44895
     Region          2..403
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mtgtpavedl lrvhapqvla tlvrrygsfe tcedalqeam laaavqwpre glpanprgwl
       61 ttvaarrwte awrtdaarrr rertvaaltg pgpepvcavd dtltvlllcc hpslsrasqv
      121 altlravggl staeiarafl vpestvaqri srakqrirvg gaefrppaag dhparvaavl
      181 evlylifneg htassgpalt rveltseair ltrqlhrrlp ddpevtglla lmlltdarrp
      241 artrpdgslv plaeqdrsrw drsaiaegva litrtladar vgpyqlqaai aavhdeapra
      301 edtdwpqllg lynllrhiap gpmvtlnriv alamvdgpev alaeltaaqa dhglvgnhrt
      361 qvvrahlldl vgdraaarrc ylsaaqatls vpeqrflhlr aarqpdlprp ptggaa
//
LOCUS       WP_357657623             264 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357657623
VERSION     WP_357657623.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  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 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   3  (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   4  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..264
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..264
                     /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=28536
     Region          2..216
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilmtgaag kvgtllrprl ardgrtlrls dlhsletapg eemvtadlvd eaamaeamkg
       61 vdavihlggq srehpwadiv ranmdglhvl leaarregve hlvlmgshha agfhtrpadg
      121 velpdyafpr pdtfygvskv vmealgslyh drfgmnvtvi rlgtcneasg dtrglatwis
      181 pddlarlvea altapgyhvv wgvsdnarrw wsleearsig yvsrddsegq aaaliaeqge
      241 pdlseplher aggvftlrdl ggkw
//
LOCUS       WP_357657626             308 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657626
VERSION     WP_357657626.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 308)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..308
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..308
                     /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=34312
     Region          47..306
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtstltqars rtetprrrpk rmrrrgtlia waflspalll flffkfipmf eglrmsffei
       61 ryvgdrwvgl dnyatimtdd afvsaiwhsi vlalgttags lllgllfall iegparylwf
      121 irtaaflpvv ttmaavaevw rimyhpadsg mintilgwit ldpqpflase hssllsimgm
      181 siwrgtpydm miflaglvgv drtlyeaaav dgattwhrlr hitlpalrpv fwilftlaai
      241 rglrvfvevy vltnggpngs sevlmtliyk lgfqkgdlgt asaggivlfa atllltvltq
      301 vmrrrqna
//
LOCUS       WP_357657638             323 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357657638
VERSION     WP_357657638.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 323)
  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 323)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..323
                     /product="helix-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=35310
     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 maatsartlk llsifgigat ltaeelatrl gasvrtvrrd idtlrelgye ieavrgargg
       61 yrlgratrlp pvvfdedqav aaavalqtvp tvlsgirens aralatlqqa mpvrsrihae
      121 aftvsaarny wefpaapida dvirviggai nrqhivrvdy tgedepttlt lephdlvvwa
      181 arwylvafqp dadrwramrv drleprmptg rtfdrrdvph sdpvafvmst hdrgdtpaew
      241 pcrgsalval papvvarfap ggstvehdtd srcrltlgaw swaglaglll tfdaditgie
      301 paelrqalrs lrtridealr ctt
//
LOCUS       WP_357657681            1017 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357657681
VERSION     WP_357657681.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1017)
  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 1017)
  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 1017)
  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 1017)
  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..1017
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     Protein         1..1017
                     /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=109307
     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          118..1011
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mefrllgpve vwngdhrval ggpkpralla alllragqvv sidrlvhlvw gahapdtarg
       61 lvqtyvsalr rtlggdliet rppgylvrld rgvldvqafe hfaddgrrav aearhedaar
      121 slraaervwr gpaldgvgea lsadaarlte lrltvvderi avelqlgrqs evavelaslv
      181 aahparermr ghlmtalyrl grssealavy edgrkalaee lgidpgpdlr alhqailred
      241 vallgfvpla qpvseehgrv ipaqlpadvp dlvgraaliv dltrlldmnh tappvlvisg
      301 kggvgksava vhlarqaghq ypdgqlfadl rgttdspata eevlsrflra lgipytaqpe
      361 saqdradlyr sllerrrvll vlddarserq irpllpggtg cavlitsrgr lsglagahlt
      421 dldvldtega lallgsvlga drlaaepdaa aeivrlcgll plavrtagar latrrhwtla
      481 tmagrlgveh rrldelvagd vavrasvgls yrlldqraqt afrrlgllgt pdfpswivap
      541 lldipaddad dvverlidaq lidhvtidav gqsrfrlhdl lrvfaaecse vcdtaaarda
      601 aitrtlgswl qliieigsrv psgevelrrh yasahpvddh vakrvmadpe awleaetpal
      661 ivaveraacl gldvaacdla talsfsrvfs anrmaewhss haaalaatrr agnrlgeaal
      721 laglgqihys ldhfdqvreh lsqaltifie agdrrgeava laglggacre qcrlreglgl
      781 lsrsaelfrl lgddigigat crlsaaihle lgeydatwpl ldqaltayrs adsgrgealt
      841 vrtrslvhra lgdyaragrd stealamlra sgeqlmiafa vqswakveir rgrggaclps
      901 lvdaldvcrn hldrygealm lrtigelhla egeldlaeah liesvaisre lgtalpaara
      961 rrdlaailsa rgdgtaeaml ataleifseh eareftelth taaaclpplr rpqttgl
//
LOCUS       WP_357657707             426 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC050680].
ACCESSION   WP_357657707
VERSION     WP_357657707.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=45542
     Region          1..364
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkqrvwwsvl latglavagc gsaarteaps ggdsqpkqhk lvvwdwksge paaaayieka
       61 kadfaqrhpd vtvefvaqpf dqyytllgta vqsnkgpdvm lfngggqird rvnalvpldq
      121 yvsedksrla gwdafskdgk tyaapvtlqg hpiyynkaly ekagldpanp pktwdefvad
      181 caaikkatga acfalgnkeg fgiqffmsgl gsgiltpqey ddwiagkrdw tsphvkrife
      241 lwkdandkgl nneganstam ftdifrvfet nkaahiiglm sdvghwkdfa eflppdkigi
      301 mpapvvtgga tpslpydggi gyavakwtkd pklaadlvrs ltstdaltaf yakagaiasd
      361 ttidvsqagp avaaivpeik tgkpalhval ssktldlmgr lsqqllsgsa tvdkavrqla
      421 asdrks
//
LOCUS       WP_357657709             328 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC050680].
ACCESSION   WP_357657709
VERSION     WP_357657709.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC050680
  ORGANISM  Nonomuraea sp. NPDC050680
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC050680"
                     /db_xref="taxon:3154630"
     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=34707
     Region          33..323
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpigssspqv rparsgrvga atmkrrghlg gvhasarsts rgpraerlap yvlvapavli
       61 ivvlrlwplv lgvnfsftgd gefngtpvga snylellgdp lfrtslsnvg llvlllpvav
      121 aipgllatfi ylrvpghrvy rsvyffpavl spvivgaifn lmlgfdgpvn ailgaigagp
      181 idwlgdpgia mftvvgvhiw atfgmalvvf lagfstldas lldaarvdga slgrtiwhvi
      241 ipsltrtiqf vfvttmigml tsmfgllfvm tgggpegsty lpefyiwhqq gqmnrpalas
      301 aastvlfvvm lvvgllqigv lrragrqd
//
LOCUS       WP_357657752             289 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357657752
VERSION     WP_357657752.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  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..289
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..289
                     /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=32532
     Region          10..275
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mlgedtegsl vaisdlhigy aenralveal rptsprdwli vagdvadtva diewalglla
       61 qrfdtviwap gnhelwtppa dpvtlrgvar yellvrrcre lgvvtpeddy rvwrgpggpa
      121 lvaplfllyd yswrppgfdt reaalaeaye tgivctdefl lhpdpypsrq ewcaarldat
      181 arrlaardpa lptvlvnhwp ldrhptevlr ypifaqwcgt datadwhrrf aaaavvyghl
      241 hiprttwkdg vrfeevsvgy prewrprrlp pgrvrrilpa pegtpltaw
//
LOCUS       WP_357657754             145 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357657754
VERSION     WP_357657754.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..145
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15209
     Region          26..121
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msapntdvrs lvvtalptpv padeydgcpv tgllrllgdk wsmlvlvllg rrpfrfnelh
       61 raiggisqrm ltrtlrgles aglvlrevhp tvppsvgyrl tplgqsllgp lsgladwavd
      121 neaalaaarr pvaaatssgp nrpag
//
LOCUS       WP_357657809             393 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357657809
VERSION     WP_357657809.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..393
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..393
                     /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=42069
     Region          3..298
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrnryldllr flaivrvvvy hvtglatltl vfpamsimfa lagslmaasl drsggsalrr
       61 rlrrllpslw vvavvfvpam lltglvftpr vllwlfpvtd ppanywggla lspiwylrdy
      121 lwfvlaspla lwlfrraplp tlaapylllv aieagilptt savprdfgly fgawllgfah
      181 hdgmlrrlag rvlvpvavll agaggawils hpgprgydln diplgnalws aafilvvigr
      241 apaaaawvdr nrifgrlvti tnrraltvyl whmpfvvalt plvglvgwsp rdpwglairv
      301 vlvfllvgvv tllvgwvedv aagrrpellp gghpdpapdr rgpvaggrpe papgplpsrp
      361 gtvspgtgag agraaavpgp qvpepgtaea qar
//
LOCUS       WP_357657832             510 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357657832
VERSION     WP_357657832.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..510
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53817
     Region          3..341
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 msrrlvvldv vgltprllah mprlravaee gfsaelgtvl pavtcsaqat lltgeppagh
       61 givgngwyfr dlgevllwrq hhalvggekv wqaarrvepg ytvanvcwwy amgadvdwtv
      121 tprpiyyadg rkepdcwtdp pelhdtltea lgtfplftyw gpgagltssr wicraaeril
      181 adqapdltlv yvphldydlq rfgpsspraa aaaaeldavl aplldaaraa datvvalsey
      241 gitdvsrpvd vnrllrtegl lrvytqdgme yldpwtsraf avadhqiahv yvkdpadvaa
      301 vaklcaglpg vaevldaegk aaagldhera gelvlvaepd awftyyywld darapdfarn
      361 veihrkpgyd paelffdpaa pgaakrragv alarkklgmr ylmsvvglda garavrgshg
      421 rlpadpadgp vllcsdpsla rdsfaatevk allldlaglg gataatggpa agtagpvpse
      481 aadpdagaag stagapsstp tgppgaegrr
//
LOCUS       WP_357657877             576 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora rifamycinica].
ACCESSION   WP_357657877
VERSION     WP_357657877.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 576)
  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 576)
  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 576)
  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 576)
  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 576)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..576
                     /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=57476
     Region          70..554
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mgrvpisprr agvavaalta llasgcageg qvpapalsgp aptasptvav ptatdpvara
       61 aalagtlgde dlvgqvlmpy aygssattvt pgsaagnqal agvdtpaemi akyrlgglil
      121 vgfsaddpts gnqsttnvdn paqvrklttg lreaagklaa gpapflvgtd qeygvvtrit
      181 dgvtilpsal aagaaddpar teaawkaagt elaamgvnld fapvadvlat rstvigsrsf
      241 gadpkraaaq vagavqglqs agvaasvkhf pghglsaads hqevpvvaqp raeldsvafp
      301 pfragidaga mavmsahldv tavdpgtpat fsrrlltdvl rgelgfqgvv itdgmnmppa
      361 kryppgeaav kallagndli lmtpnvgqay dgllaalrdg slprerlvta vtrvltmkfr
      421 ladrptpams tldgaphraa aaelaaaavt qlrggcgqki tgpvsvttsa grdrtrqtlt
      481 aaltaagvrv vpkggtrvhl vgygdgpkdl aagaavtvam dtpyvlekat sptllatyss
      541 srasmtalag vlagkakptg rspvpltglp attctg
//
LOCUS       WP_357657971             326 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora rifamycinica].
ACCESSION   WP_357657971
VERSION     WP_357657971.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 326)
  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 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   3  (residues 1 to 326)
  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 326)
  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..326
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..326
                     /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=34034
     Region          1..243
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrvgvvgcgr hatsvllpal vqlgldvaav carrlssaqa aaarfgaraa yadpaemlrr
       61 egveavvacl ppqvygevvr acvdarvpvf aekpgaggsa eagrlaalsa eagvpvmvgy
      121 mkrfapayrq artaiadpsf gapslatftf vmgdmgvgid gylvdnpvhh ldlarfllge
      181 lhdlhvtrgr sdggrhalsv aaraesgavv slqlgttgsw qqhnesvevf gsgssvlvdn
      241 vdtcvlrppe gperrwrpny sipdqvnttv dtmgfgpalr hfqdvvrgta scesdlrsaa
      301 rtlalvdvig drlglgrqap pgeafg
//
LOCUS       WP_357657982             976 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Micromonospora rifamycinica].
ACCESSION   WP_357657982
VERSION     WP_357657982.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 976)
  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 976)
  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 11437895
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..976
                     /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=107499
     Region          133..943
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 msalpfvlrh pvavipsdka aeqlaragiy dpavlvdqlg rlatagalpa rmeverdrlv
       61 vysqrwkvgf ylsgreraal kladvsplsf kdqeqllkga lllrcapgwh tfphvrdvgs
      121 pyrvpwaelc htwerlgvtg savpalpahh ggfldlltev ieavrdieia kqqedlalpy
      181 rrvdsareer rsargvyvfh llrpcalaqg alvyvtdqpd lrgrvlrvrd rdrevtvrfd
      241 gvvdfarlpq qgalgvlpgd rvhrarlaav qtlrdreatn phllthlvdr qlapyrpdvt
      301 aqpratldgd qlrafqsalt vpdlllvlgp pgtgktttit emvavsaarh qrvlvtshtn
      361 ravdnvlerl payvravrvg nedamtahar glmvevqvet lrreilatte gsmsrltpft
      421 aaddaagrwm sflttqlgea qladtevqal saeltaamdr avrplaaqla taeqehrttr
      481 aeleqlgere hgarqrlaev rrraaggpla flfrwqqgwr errlstvreq lavavreagr
      541 aeqayaeira qadaiaaadp evgsraaard aaaeardkfl tevtraaemv ratlrpvvpv
      601 stgtpvdlpg wmalhqklta alalarsrar lldqwraevt eaeqdlhrel lryadvvaat
      661 cigtattall agldfdlaiv deagqistpd llvplvrarr avlvgdhhql ppfldhevas
      721 wadslpsgta psnagqirdl lrrsaferly qgvgdanrvm ltvqrrmpev larfvstsfy
      781 ggvlrtehra grrdplfhsp mamidtsdrp areraertpp avdafeqggy lnelearliv
      841 rlltrhadhy gswavivpfr aqvkllaell tkelganava envgtvdsfq ggerdlivyg
      901 ftrsnqhgni gflkelrrln vaitrarrqi vlvgdtttlt nardpgfaal anslvvhlga
      961 fgerrpsrei eeklng
//
LOCUS       WP_357657975             375 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora rifamycinica].
ACCESSION   WP_357657975
VERSION     WP_357657975.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 375)
  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 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
REFERENCE   3  (residues 1 to 375)
  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 375)
  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..375
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..375
                     /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=39777
     Region          10..371
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mgddiarapa dpvavamvgn gfmgrahtlg lvvagllvpd lppvelrsis grdpdrtrrs
       61 aaqyryreaf tdwraqldgp glsavdvvlp telhhaatma aigaghavlc ekplaataad
      121 ayemwqaaea agvvhqcgfn frfapavrla hdlvaageig qvvafdgsfl esiglpehda
      181 ddvavwpppp qdgallglgp hildlalwfa depttvqaqr gklnpspavl ddffsgtlqf
      241 rsgahgtvrg srvaggvtse crftvtgtkg alrwesprln elwsitpghr atvievtrpt
      301 dpfmamwwpe pghpvswtet fthqaahflr avaggtsvre saadfedgyr callvealst
      361 aadsgrptaf arpeg
//
LOCUS       WP_357658091             538 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357658091
VERSION     WP_357658091.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 538)
  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 538)
  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
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..538
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54762
     Region          70..532
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpaehgpaar ppvpvggrpp agagparrap glpgpavpks agdgragsga aagepsggaa
       61 aggevwpqpv lrllatggdr pvfedgdriv datgmwalvr riasglraag vgpgtgvalr
      121 lgvtpeafaa viaafavgar vsglrpelpp tplerllgsd dallvddarl aalvdtpddg
      181 tplvaagrpt diaritwtsg stgnpkgcaq tyaamsaawa aypdrwppai aalaprlgry
      241 lvfgslssqv mleygiltla aggtlvaarp pgfpgmitrh ratasvitvg klhqlvrdqr
      301 trpvdlsslr alvvsgsplt asrlaealdv lgpvvfhgyg qtetgmiamv tpaellarpa
      361 tlasvgrapa vvdlsirdad grpaaegely vrtpaqatay wadpvetadv ftdgwvrtrd
      421 larldadgyl hlfgrvrdvi ivnanlvyag piervlaadp svaeayvvsr pddvtgeavh
      481 ayvvpaaghe pdaerlrarv aaalgaaavp ttvaviaavp vgpsgkpdkr algtpgqs
//
LOCUS       WP_357658163             287 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357658163
VERSION     WP_357658163.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..287
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..287
                     /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=32242
     Region          7..258
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mttslvpevr lvagalgaev hgvdlntltd egfahlhrll lqhqvvfvag qtgltpeahi
       61 afgrrfgeve lhpylprlpg hpeivvidse dggkvdvwht dmtfhqsppi asilhlvqlp
      121 etggdtmwtn qckvyealsa pmrdlldglt avhvirigne ftsraehpvv rvhpetgrrs
      181 lyvnrlftsh ipqlsrnesd alleylfgfs egpqftcryr wrvgdvaiwd nrvtqhyain
      241 dyqgvrrgqr itvlgdhptg daprwdhyva apgqrywpdr vnavdny
//
LOCUS       WP_357658176             763 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora rifamycinica].
ACCESSION   WP_357658176
VERSION     WP_357658176.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 763)
  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 763)
  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 763)
  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..763
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..763
                     /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=82990
     Region          10..761
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mgpdklrhhd deigreqeyv smlygrldal reqagnrlad alraggggtq qdrsqrnsal
       61 rmyadqvkqf savaqglafg rldgtdgsrr yigrigifdn dsdydpllmd wrapaarpfy
      121 lataanpqgv rlrrhlrtrd rkvtglndev ldiesasptg heeltgeasl laalnagrtg
      181 rmrdivetiq aeqdriirad lagvlvvqgg pgtgktaval hraayllyth rqqlstrgvl
      241 lvgpnatflr yisqvlptla etgallstpg dlfpgvnarr aepagtaavk gravlaevla
      301 aavrdrqwvp depleielpq revllldpat vrlarervrr tgrphnlara qfdieivhal
      361 adqvaeriga dplggdnlle eadraeirre lreepevtaa ldrlwpvltp qqflddlyas
      421 periaaaapm ltdaerallh rppgdgwtpa dvplldesae llgederaaa arrerlrsfq
      481 reyaegvldi argsrsidve ddadggeilg vtdlidadrl lerqeegdrl ttaqraaadr
      541 swafghvivd eaqeltpmaw rllmrrcpsr smtivgdvaq tgalagtpsw aealepyvaq
      601 rwrleeltvs yrtpaevmav aaevlagidp alrpprsvrr sgvppwdrtv aadrlaaelv
      661 eaanreaagl degrlgvivp agraaelaga vlaalpeagv geqpelesrv vlltvgqakg
      721 lefdsvlvvd pdrivaespr grsdlyvalt ratqrlgvlr pas
//
LOCUS       WP_357658216             611 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora rifamycinica].
ACCESSION   WP_357658216
VERSION     WP_357658216.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 611)
  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 611)
  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 611)
  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 611)
  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 611)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 611)
  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..611
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..611
                     /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=65985
     Region          45..515
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mntyrrgwtl rrrvlallav vgllliglav aeaavaaknr aytdtlltrt gplrvqgqel
       61 lnvlldqetg vrgyavsgnr adlapyeqgv rqerdvaati adlgrdypai mdalrtaqqq
      121 aadwrrtvae pviattgssg taagqalita qarqqfdqir asvgdlqaai laerekgard
      181 iertgnmlvm llivaavvvv iagtlmllsl ermvirpltg laqqvrevaa gdyqhhiags
      241 gppefrrlad dvdvmrqkia kdlaevraar eniewvnsql qkqaeeltrs nrdleqfayv
      301 ashdlqeplr kvasfcqllq rryagqlder adqyiafavd gaqrmqrlin dllafsrigr
      361 lttgfvdvdl nrvmadvssq tepgrqyada eltwselpvi rgeeplltnl lvnlvsnsvk
      421 frrpdvpprv rvsarlvdae weitcqdngi giepefadki fvifqrlhak daypgtgigl
      481 aivkkiveyh ggrvwvdtdq aegtairftl parpedveaa katadadata dataptdgdg
      541 ttttgtddpa ttgpddpats drpvgeppvp vgevagdgpt vgrqpaggrh edppggppgq
      601 gttggtkerv g
//
LOCUS       WP_357658278             850 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora rifamycinica].
ACCESSION   WP_357658278
VERSION     WP_357658278.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 850)
  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 850)
  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 850)
  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 850)
  AUTHORS   ter Beek,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 850)
  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 850)
  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..850
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..850
                     /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=86812
     Region          12..850
                     /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 mvratlksll arkvrlllsg lavvlgvmfv sgafvltdtl grsfdavfad ayegvdvnva
       61 gkprvalsem qgeqvpatvp aatvqrigav agvaeatgvv ttdgaqligs ngkvvtsfgp
      121 pqlgsnwqge sdlvklregh epraddeivv naalaqagkv kvgdrvgvlt plvpkqtftl
      181 vgifgysgdr dsiggvneva fttpvaqrll lgepdvftnv tvraadgvsd atlrddvart
      241 lggdfevktg aqlsadasas lkeglsffnk illgfaaval lvgtflilnt fsiivaqrtr
      301 elalmraiga sgrqiigsvv leavaiglia svlglgagig igallayvfg nlaggltlag
      361 igvpasavvg sfavglvitv vaallpalra arippiaamq dvanpdrplt rvtvtggvit
      421 gigavllflg lsgnagdntl pvilggvlfa figvalltpl isrpvvsllg avfawsvpgk
      481 lgrlnsgrnp rrtaitaaal mvgialvtgv tvildsakgs igalaqdtik aelvisgast
      541 gprpasfdpa vltkvaalpg vqladgeygd mgmvdgkvtw laassdvtal qrifgaktta
      601 gdisrlgpdq mlfssdaaes rgisvgsrvt vqasrgeprt ytvsgiyess eltspvqlpp
      661 qavkdfaipk pnqgfiqlap gtrvadvqpr vealladspe vsvadrdafi eqqtgsldsl
      721 ltmiqillal aiviavlgiv ntlalsvler trelgllrai glrraqtmrm itveavvisv
      781 fgallgivvg vglgaavvra lkddgitdli lpwgqmglfl llaavigvva avlpairaar
      841 invlgaiahd
//
LOCUS       WP_357658406             260 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357658406
VERSION     WP_357658406.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 260)
  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..260
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..260
                     /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=27595
     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 mfprpsrlae vlrdggvalg sltllqepai geilgvlgyd flvvdtehaa adeqsvlamv
       61 raagsagttp lvrlrrieek dllwsldsga ggvvlplvet gaqaveaarl thyppvgdrt
      121 lcsaaraagh gtargdfdry ltwagrnttv valvetpagl anlddilaad ldvlmlgrad
      181 lsvklglgyq pthpevekha iafvervvaa grvagmlays aeearrwidr gvrfvvysqp
      241 emllsdayrr ardeilggas
//
LOCUS       WP_357658407             387 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357658407
VERSION     WP_357658407.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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 387)
  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..387
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..387
                     /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=40600
     Region          64..>255
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrglrttltl agarwlwrrh rrsrestpvs agrsgaella wgaaaaalga gasalserrr
       61 arrmngrvvl vtggsrglgl qlarefgagg asvvicargr edldravael tgrgvealgv
      121 vcdvtdpeav dsllddaver fgrldvvvns agimrvgpqr tlpddafvqa mdvmfwgpfh
      181 lsraamermr grggtivnvt sigaylsvph llpysaakha waalsegmaa esggsgvrvv
      241 tvvpglmrtg shrgvvfsgn pereyawfal aagapllsvs aeraarriva aaasgrgflv
      301 ispiarigla vhgvapgltq agmrlvgrll pdapehveer sgseaadsri grlvgvvaal
      361 neragrrmnq ssraeerrrd vdsgkdg
//
LOCUS       WP_357658514             324 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Nocardiopsis alba].
ACCESSION   WP_357658514
VERSION     WP_357658514.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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..324
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..324
                     /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=33114
     Region          98..323
                     /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 mstpsvlmas pvlwsvvaaa algalglivg rgtgrlvhlf gpadadvavs srpaehagpe
       61 nppgqdgatp gpghpegape rgsrppvegp redpgpappr cphcrtalrf vrglpvpver
      121 eilgdgrcpg cgrpiashlp tvvvtgalfa ltvpllahqp avwspfgaaa vlwlialgvv
      181 lcaidlrvmr lpdalvgpay pvagallaaa vllppagpdl ergahaligl vlvavlywfl
      241 wrihprglgf gdvklsgltg lyagwaagpl gamvgvlwaf vsfslvglal lllrrvtrse
      301 plplgpfmia atlatvftga plvp
//
LOCUS       WP_357658528             427 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nocardiopsis alba].
ACCESSION   WP_357658528
VERSION     WP_357658528.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 427)
  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..427
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..427
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45034
     Region          10..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 mttspepstt daplplagvr iadlsrvlag pyatmlladm gaevvkieqp grgddtrswg
       61 ppyaapteeh eaahspgeaa yflsvnrnkr slavdlkdpe glaavqelca ssdvviqnfr
      121 pgvidrlglg yerisernpa vvycsvsgfg peheptgrpg fdivvqaesg lmattgpaeg
      181 paskvgvalt dvltglnaav gilgalmrar etgrgeevsv slinstlsal vnlaqqslvt
      241 dreparvgna httivpyqvf ptadaeivva agndalyrrl caaidrpdla edprygtnpd
      301 rvahrdalid elskvlrsrp adhwmtalvd agvpvgrvrg vldalrtadt sgddvlrtvd
      361 hptagpleqv ragfrmagtp vpmaappllg qhseeiltel gltperiaal vergavqrtd
      421 vrpdtte
//
LOCUS       WP_357658530             702 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora rifamycinica].
ACCESSION   WP_357658530
VERSION     WP_357658530.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 702)
  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..702
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..702
                     /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=72352
     Region          12..269
                     /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..37,70,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 msdvpsqlva dryrllsplg qggmgrvwka rdevlhrdva ikelvpppsl tdderremre
       61 rslrearaia rlnhvnvvri fdvlrtdgdp wivmeyvask slqdtlaedg pvsparavei
      121 glgvlgalks ahkagvmhrd vkpgnvllgt dgrvvltdfg latipgdpnv trtgmvlgsp
      181 ayiaperard gtagpeadlw slgatlyaav egkspyarps aigtlaalat eplpparnag
      241 plkpvltgll rkdpaerita evaermlrra agkrakgisl ldgvrrpgpn gpreprapvv
      301 paqggtggki ssslaaaagi atgtaaakaa aaraaakaas gdaaaddsaa artttagaas
      361 tdgtatvvtd apavggdata tipagvdagp ttkvtpptga daapagtvea tegpssdava
      421 vaadddaatg stvappartd radppapgnp tavldapvgp pagvasvpay dstppdnrrr
      481 nllvgalvav llvglalavp lltrsdepdd gpapagptsa aassvaptsa paappptsaa
      541 ptptptpsas psadpnalpe gwemfkgptf svplpkgwrr svrsdsvtvt epggvrelli
      601 qwtsspkkda vadwreqeps rrnfvsnyqy ldikacggyr tcadwdwles rdntrihvrn
      661 rgfvtatnrg fairwevaak dwnanldnfa litsrfvpdr qn
//
LOCUS       WP_357658548             262 aa            linear   BCT 28-DEC-2024
DEFINITION  PhzF family phenazine biosynthesis protein [Nocardiopsis alba].
ACCESSION   WP_357658548
VERSION     WP_357658548.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Blankenfeldt,W. and Parsons,J.F.
  TITLE     The structural biology of phenazine biosynthesis
  JOURNAL   Curr Opin Struct Biol 29, 26-33 (2014)
   PUBMED   25215885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..262
                     /product="PhzF family phenazine biosynthesis protein"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28299
     Region          3..262
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
ORIGIN      
        1 mpeyrvvdaf terplagnpa avlvlsdeyp dvwaqgvaae fnlsetafar ridsdeadye
       61 lrwftpvaei dlcghatlat ahaltqleve gpyrfstrsg iltverrdgr lwmdfparpa
      121 aeveapeglt ealgatpvwt giggnndllv eladedtvrs lapnlgliea lpsrgvivta
      181 rgsgeydfvs rffapkmgvp edpvtgaaht vlapywaerl drtgfrahqa srrggdlelr
      241 ltgervligg havtvatgel dl
//
LOCUS       WP_357658634             526 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nocardiopsis alba].
ACCESSION   WP_357658634
VERSION     WP_357658634.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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   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..526
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..526
                     /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=57927
     Region          5..120
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          216..526
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mqisellavk glrlrflsge eharrdirwa yttdllepar ylrggelvlt gmmwhtrped
       61 setfvssivs agslavgagr algeippdli eacrahdipl ieiptetsfg avteevlrsl
      121 tqrrfttiae trdrhrrlma evasgadfps afssaatqag leawvissgg rhiassgapl
      181 pvedrerlaa qaltwsafpr tlrfpeegen graitvlpvr arethslagw wmvvagdhrd
      241 wseeehetva elvsigvlar sraeeraltt arhleglprl laaqrfdeva elmrgaeggs
      301 vpedrahvvv savmlpdprv pdlsrrvlae lvadhpaavv tgdndalaii pveggdhdir
      361 rrgeeirnel vhrahvldag lldyrlvvgl ssaargitel rgaavearha rrlaelrggr
      421 srviagaeid shelllasvp eevqtsyrer llgpliaydr dhrsdlvetl erflahsgsw
      481 qrcaaamhvh vntlryrigr veeltgrdls slehrvdlfl alklrd
//
LOCUS       WP_357658659             449 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Nocardiopsis alba].
ACCESSION   WP_357658659
VERSION     WP_357658659.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 449)
  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..449
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..449
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=45992
     Region          107..172
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mkyrialppl lavamitaag cgattdlsda rpangeaapv pidvdgdgyg dlpisgvlgd
       61 pedgepyvgv llggedglsp drsvlltaad ldlpeasapq tvletgdldg dghtdlivaa
      121 dddgylvlgg pegptgpaip lpwlstgven gmaavslavg dmdgdghtdv avldqvqgsp
      181 idewesryhr gpfdaegept etrdlplpee awdaelasfd adgdayqdli lisgrdespa
      241 tdlilrsgpd gpaeevvget plshtrasgd idgdgiadll igisgipnne pgyedelrpg
      301 yvdtllgseg yldaepirld rdgegmpgda edgdgfggel lvgdvdgdgf ddvvamsgpg
      361 ysyeeaflll ggpeglrgtg tdpltvpsar dgsfgphalm dydgdgyadl llstvfpamp
      421 gasgeyalyl ggpdgfsaep dttfdtadl
//
LOCUS       WP_357658682             999 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Nocardiopsis alba].
ACCESSION   WP_357658682
VERSION     WP_357658682.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 999)
  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 999)
  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..999
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..999
                     /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=107304
     Region          <116..>254
                     /region_name="DUF1631"
                     /note="Protein of unknown function (DUF1631); pfam07793"
                     /db_xref="CDD:429661"
     Region          267..971
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mrvlhgvwsg gtltiwaege ahadrppgvh pfaaglpdlr dlvdrlgidp sspaateptl
       61 flpggaeapa rsdstdttps eprpwrvpal elspadadll lcalanpssv algpalahlg
      121 avhafaerlv gagcvlpdlv gapprarwrp apsdtaeehl aalsatlppa atahltardr
      181 adadrlcvla plelltdava rrlstgrgrp setedvppsp earlaaaltg srtrvdeeta
      241 aalrgplrew rsrvrgagra rllfvlrepe pegphhgprp wtlefwvrst tdpglrlple
      301 qvwsgeggaw lpedvastal adlrraarhy palgrvlgal apdrltmdtl gaqdfvgtha
      361 arlaaagfsv vlpewsgrdg lglrmtvdep pkrrgrggvs psdlvdvsfe allngpenea
      421 pltgeelael aelarlkrsl vrvrgrwmev dpesvasale lmrrsgrgrm rrdealrtai
      481 gvaetaplpv tdvvadgplg alldggakae prpmgtpagf egslrpyqdr gaswlrflge
      541 lglgavladd mglgktvqll alltderadg papgptllvc pvslvgnwrr eaerfapglr
      601 vhvqhgpdrp sgnalarivg hcdlvvttyg vvardaeels gmpwhrvvcd eaqalknhdt
      661 rqaravrslp aatrialtgt pvennlgelw svmefanpgl lgasadfqrt vadraeaegg
      721 egegtdlvrr ltgpfvlrrl ktdrsiiadl pdkhqmrtwc tltpeqasly kavvdemger
      781 maeadekerk glvlatmsrl kqicnhpaqf lgdgsalagr sgklerleai lgeavaegdk
      841 alcftqyarw gerltpylrs rlgvpvlwlh ggtsradrer mterfqtmag pavfllslka
      901 agtglnltaa nhvvhvdrww npavenqatd rafrigqrrd vqvrkmvcvg tveervdemi
      961 erksaladga vttgeqwlsg lsvedlrevv rlapeavag
//
LOCUS       WP_357658732             165 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nocardiopsis alba].
ACCESSION   WP_357658732
VERSION     WP_357658732.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=18393
     Region          <60..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 merhnpgrrr tadhlyasal slartgetfd rlrglqgveg ealllvleas radgrsgvte
       61 sepitpgrlg relrlpsasv tavvdrlerg ghlrrvrdtg drrkvlllpt eeaerahtty
      121 wgglderive vmerfspeel sivdrflrga tavtegyrae reehp
//
LOCUS       WP_357658744             210 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nocardiopsis alba].
ACCESSION   WP_357658744
VERSION     WP_357658744.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 210)
  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..210
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..210
                     /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=22415
     Region          9..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprtpeqhra mraatrervr taairlfcrr gyagvdmrai aaeagistgs iyrhfatkde
       61 lyddlvaeaa tglrtlarsf tdtdlvvepl rgfvevflad lsrdtgavef yllmnqvfas
      121 gveagperga avedllrahr evtgavvtli ergrgrgrgl trpapaaela tcffatlggl
      181 amtrsalgea fvapsvatvt gillveetta
//
LOCUS       WP_357658771             320 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nocardiopsis alba].
ACCESSION   WP_357658771
VERSION     WP_357658771.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 320)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..320
                     /product="phosphotransferase 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=35186
     Region          11..258
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mnddpprrsr ealnrlvaaa glpsvtsvrp ingdgdgldn hlvkaeltdg ravvlrrsrv
       61 esaspesrig flrangvttp elyaadgega slwefvpgrt laeavetgta tdtvwrrtge
      121 alaevhgvvf paplqgpidv daltlrpvdp veelhtslhe saawverehp hllealrrve
      181 gfvaeraaei raerptvthg dinllnivvt ddeavrlidw dfptvrypla elaafdehay
      241 lhgleglpra ffegygravp edlllayrav gclgwlssdd wrewdetpdl pgpararlra
      301 wherllawad rlpdlvkalg
//
LOCUS       WP_357658781             323 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            rifamycinica].
ACCESSION   WP_357658781
VERSION     WP_357658781.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 323)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..323
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..323
                     /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=34012
     Region          26..298
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtsalgsapt grdgtgtspg ratrpssara hrprwaragg tgwlfvlpav lmyavfvlrp
       61 laltiqysfy nwngigvarw agldnyvtvf tdgdllkiig nalvlivffs fvpvalgllv
      121 aslvrrittg afgtvvrtvl flpqviplva agiawswlls snglvnqvlr avglggvara
      181 wlgdfdtalp avgvigawvl lglctillvt gmskidpaly eaarldgagp vreffavtlp
      241 slrqeigvcl tvtiiaalas fdivyistsg gpglqttvpg leiyrlafsq rqvglasala
      301 vvlmllvllc vlpiqrltrg dkp
//
LOCUS       WP_357658790             321 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nocardiopsis alba].
ACCESSION   WP_357658790
VERSION     WP_357658790.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 321)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..321
                     /product="phosphotransferase 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=34362
     Region          20..237
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mmpepgatsh pldqhrdpsd aafvrglaae vaaryggelt rmrrangysn atwvgdgiav
       61 riahtpvdma reaalvralp revahpeilg egvaeghgwi vtaevrgrnl yeawptltpa
      121 eqrqaihqlw araqivhdas pslktyvash ggfvpetlgd atasagraga alglssaqrs
      181 rfheiiegyf raapmveqvv dhgdlalmna lwdgevvall dfefavlgpv eidlcrlvye
      241 acvseegtyv dseagaaave iaarhmdpth gralirgaav ldqlrdfdiw laqgggedwn
      301 pgrlltalid ddggylapll k
//
LOCUS       WP_357658819             175 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardiopsis alba].
ACCESSION   WP_357658819
VERSION     WP_357658819.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 175)
  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..175
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..175
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19213
     Region          22..>74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msvenkeaqv dqdadslcve skkalgvhlk rlrkvaglsg yrlsgvdqst vsrietgrir
       61 pshelltrll dayeadqegr eqaylfwdqa qlplqtrrrq vegirpawgq aarpacgptl
      121 lagasaaeda aryltraqwa gnsqsrrnal lddaegrlvq vlaalhaart rtper
//
LOCUS       WP_357658866             340 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Nocardiopsis alba].
ACCESSION   WP_357658866
VERSION     WP_357658866.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 340)
  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 340)
  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..340
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..340
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=35767
     Region          15..326
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mysptsrpad srtgkrnrra lmasmavapl ilagcgandg eypsdsieyi vpynpgggad
       61 pvgrqfvqml eteldangnv invpggdeav gitqlanada dgytlglgts ggfvaqplvt
      121 geaqyetptd ftplakmsgt pyglfvspds eyetlddlie aakqnpgdiq istparmgnp
      181 afviyfleeq advevslvtt aggtgeaale vmsgrldavv gnasgqlglv esgdlralay
      241 sgpedysdfl pdavrfdeag yeipftsdym tmapaglded iasalreasd aivtseewee
      301 wargqgtlph vatgeeldty lediqagieh gielgndren
//
LOCUS       WP_357658883             390 aa            linear   BCT 28-DEC-2024
DEFINITION  epoxide hydrolase family protein [Nocardiopsis alba].
ACCESSION   WP_357658883
VERSION     WP_357658883.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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 390)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 390)
  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   5  (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 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..390
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44067
     Region          11..120
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          82..385
                     /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 msrptddvev feahtsesdl edlrarlasa rfpeaetvan agpgphrweq gvpladlvel
       61 vdhwrtgydw rafeerldri gqfrttidgl rihflhrrst radaaplvlt hgwpgsiaef
      121 idvvdeltep edpnapafhv vipslpgfgy sdkptttgwg tekiaaawve lmgrlgydgf
      181 lahggdwggn ittilggrfp ehvlgihttf aqgppgttmd glttverewa egthhfwrhr
      241 aayakqqatr pqtigyslvd spvgllawil dkyaewsdte dspfetisrd rilddvtlyw
      301 ltrtgasaar iyyeshdsld pelrvdvpsa itmyprdter yprpwarery rqivrwrepe
      361 rgghfpslev peyfvedlre glaavlaarr
//
LOCUS       WP_357658993             449 aa            linear   BCT 28-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Nocardiopsis alba].
ACCESSION   WP_357658993
VERSION     WP_357658993.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 449)
  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..449
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..449
                     /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=47231
     Region          6..389
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 mtgpidvavv gagpaglata haltaagrsv rvleaaeavg grmrtlrvdg hlvdtgaemi
       61 psanaypatw rlirelglda dpsaiprvrg alsvwwagra rrnagrplgl ltgmglapaa
      121 rldlarllgr lggadldpeh pergdltdvs vadllesahp qvrerllgpl asgffgwple
      181 raaaapfaah lvasgstahw rtyrdgmdtl praladrldv rtdhpvtrvv eeadgvrles
      241 prgdltagav vlavpapiam elypgiggve rayleaceya pmlrlslfld tpmaprgrgr
      301 gfavlvsddp llsvvtvdhd khsgraprgr gllslvaspr gvrelaeapd hevtrrltes
      361 aerllpglgg hvrgavahrf rhglplpgpk alaaraafva rppaavdyag dwislrpcse
      421 gavasattat ervtaflaaa repirieet
//
LOCUS       WP_357659017             349 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardiopsis alba].
ACCESSION   WP_357659017
VERSION     WP_357659017.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=34589
     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 mtttgtrpae pagigavrrp rrlrvlglav lvlvvlglmc vsvavgtrdv gwdaivaalg
       61 gsvegfdeaa vakrvprtll avlagaalgv agavmqgvtr npiadpgilg vnmgaslavv
      121 vgmasfglas athfvwaavv gggitavfvy vvgslgrgga tplklalagt avsaalasfi
      181 saivlprndi aggvrswqig gvggatydsl tqvlpflvag falclacarg ldmlalgddl
      241 aaglgerval arggaslgav tlcgaatavt gpiafvglvv phvcrlltgp ghrwlipfsa
      301 lggaalltaa dvvgrivarp aqidvgivta ligapffihi vrrqkvrsl
//
LOCUS       WP_357659028             164 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardiopsis alba].
ACCESSION   WP_357659028
VERSION     WP_357659028.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 164)
  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..164
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..164
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18024
     Region          10..>65
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mdqdadslct eskkalgvhl krlrkavgls gyrlsgvdqs tvsrietgri rpshelltrl
       61 ldayeadqeg reqayllwdq aqlplqtrrr qvegtrpawd qaarpacgpt llagaraaed
      121 aaryltraqw agnsparrta llddaegrlv qvlaalhaar trtr
//
LOCUS       WP_357659068             234 aa            linear   BCT 28-DEC-2024
DEFINITION  histidine phosphatase family protein [Nocardiopsis alba].
ACCESSION   WP_357659068
VERSION     WP_357659068.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 234)
  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 10001383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..234
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26195
     Region          1..150
                     /region_name="PhoE"
                     /note="Broad specificity phosphatase PhoE [Carbohydrate
                     transport and metabolism]; COG0406"
                     /db_xref="CDD:440175"
ORIGIN      
        1 mttcfvrhgr tsyssrhlvn gdprvpvpld degilcarrs rslvremgir tcrtssfprt
       61 rqtadllleg ndcprsvdac ldepdygmfe grsfleyasw lkeygptarp pgsresqhea
      121 llrmlegcar lpflsaprmv vahgfllsal nwchsrhsqs gfplflpeas yleplvvsdr
      181 cllgwvklls eevhrgpcsn egrgapqiss eddrtvlhpp rtvrtpleen efda
//
LOCUS       WP_357659144             362 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora rifamycinica].
ACCESSION   WP_357659144
VERSION     WP_357659144.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=38524
     Region          6..>53
                     /region_name="PRK10083"
                     /note="putative oxidoreductase; Provisional"
                     /db_xref="CDD:182229"
     Region          59..360
                     /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(66,68..69,72,136,141,174..179,198..199,203,220,
                     245..246,248,268..269,295..297)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mrdtvvvvsg pgqvelaeqe agepgdgair vrtrysgvsa gtelscvkgt npflnvtfdt
       61 tlglfrpgga stpypvtrlg ymqvgevvqs rtpaiavgtv gamtyghrtg hvadplaerf
      121 vplpgdldpm lgiyvahmgp icangllhaa adlcgtdvrs lgdgvrgrrv avvgggvval
      181 ltalfakrhg aasvvvldpt pqrrqvaeal gletldpead dpavllktrw hhsagdrgad
      241 vvfqcrgqaw alhlalrllr pqgtvidlaf yqggaeavrl geefhhngls lrcaqigrvp
      301 rglaptwdre rlsaetidll rrygdlirqh lisavvpfea apalltdlae rrrqelqvvl
      361 tc
//
LOCUS       WP_357659161             405 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardiopsis alba].
ACCESSION   WP_357659161
VERSION     WP_357659161.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=43132
     Region          165..400
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 malsrylpfd arpvlgartg aflvflamaa lwsldlrtvl ssrritdwmg pphsamdfap
       61 visgavcvvl vllvlwpprg hwttfvvgaa vplvvittsv llwplpkgtf gypivasegv
      121 gmvvaaslva lrgrvwqmpv vatlvflavc sdylrepyvl daenallvav lglapglylr
      181 wravdrdarv rriraeerla iardlhdvva hevtgivvrv qalrhvadrr pemvrealpe
      241 iekaggrale smrgmvsrlr gpeeaplapd paeglaalaa paspgrpevs vhadadvadl
      301 pvevgtailr iaqesvtnal ryargadrvt vvvesdddtv llritddgrg gartggpsgg
      361 ghglvgmaer arilggtlsa gpdgfgqgwt vraeipvsge rertr
//
LOCUS       WP_357659188             223 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357659188
VERSION     WP_357659188.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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 223)
  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 223)
  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..223
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..223
                     /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=24158
     Region          3..217
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mtrvtilgat grsgsavlel lpphtritat lrrpgdrsrl patereitev vvdvedpasl
       61 rravadadvv vnavrmrgdi dpsalvelhe rvveaadpss gpapfivtvg gagslrlpdg
      121 trfwqspafp ertlprgrah arlrdhleeg rdgekwayli pppafdpdgp rtknhrvwpg
      181 aadesafler sigyvdfaea vcaaveerwa gtrlvagpet rrv
//
LOCUS       WP_357659189             446 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardiopsis alba].
ACCESSION   WP_357659189
VERSION     WP_357659189.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 446)
  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 446)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 446)
  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..446
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..446
                     /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=47579
     Region          189..446
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrrdapalpe tidagqsppl gptsrlsswi daaltragfr gafgrdlllg vfvalvstal
       61 lysfvlfarv eetpfspasv stlvaltvvq slalclrrra pllclaivva tqigmtlllp
      121 adasaqgpap fiaaytcgtl lpvkrlvral vtitvlfgvc gavfamppfa slappalvtd
      181 pamagisqvv tavlvfgvag ligndvsmrr ryvhqerirl vererervhg alraertrma
      241 relhdiaahh lsgmvvqaga aekladrdap elaptigwir rqgketlenl rmvvgalrdp
      301 geypgggrge aagesdapvp gvavldrlve terelgvevs lersgpdlel ppvadvmfyr
      361 vaqealanar dhawgapvrv elargerevv lrvdndpgve reerakasrg lgligmrera
      421 dlvgatletg ptetggwsvr lvlplr
//
LOCUS       WP_357659228             683 aa            linear   BCT 28-DEC-2024
DEFINITION  bacteriocin-associated integral membrane family protein
            [Nocardiopsis alba].
ACCESSION   WP_357659228
VERSION     WP_357659228.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468666
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..683
                     /product="bacteriocin-associated integral membrane family
                     protein"
                     /calculated_mol_wt=73385
     Region          102..622
                     /region_name="COG4652"
                     /note="Uncharacterized conserved protein, DUF1430 domain
                     [Function unknown]"
                     /db_xref="CDD:443690"
ORIGIN      
        1 mpdrtlsfay tacvvfavlv afllaataer tiyvlddael iwitendgth atdevartvq
       61 evadahgaai gysvldvdep sskahmylav sdpdsryadw lrdgypsfgr gftvqthpit
      121 dfgrvgpngy yllfgapeae palraalaeh glheapgtrt trlwhffsdg pllhlvvial
      181 lgtmtatgag vllgsrehav krlhgwsrtr vllselvria rlwavvlpvt ailtlillwf
      241 ynggnqfgfh arltvlflvv ftlpclvvha calalsrtvg ilpalegrlp vlgalvaina
      301 vripalvltl vvlgtvvsta qsvrdqrsgl evyerygdts rpalsadygw adaeavdgll
      361 gpwlrrvdvt gdmvlsvlls pgeflpvgad ppvmdtpilv vndgylraee vlsptgeryg
      421 pdesvrlllp gpaleheadl rqgaagwlam ngeegreppr ietapladdr svfvygaqer
      481 lggtsplved pvlvvlpagr vlsdsgyvdh msarqtifpd pdvvetfrse dpwaaryism
      541 vetlatsahr tydltsgilr dsllnlvgag aillltamaa cvvhvrvhaq rifarhlcgh
      601 sfltthrrll avetaialgf vgwtvldvlr tgagphdlap lsapdggagp lhavgivlls
      661 laltlgtlll fhrrivregs sqa
//
LOCUS       WP_357659263             286 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            echinofusca].
ACCESSION   WP_357659263
VERSION     WP_357659263.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..286
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31356
     Region          13..76
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(19,23,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(29..30,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..282
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mplptspvir rarlgaelrq lrrrealtle qvcdrlgwas tsklsrielg qsrpdladvl
       61 dlldvyevpp pqrdalivia rdaatsrgww kalgemgerq rtyaeleaga asivdwqpav
      121 vpgllqtpay arlriaagrl ldpaldvdad vraralrhev lrradppryt allaeaacda
      181 gdtppqvwre qlrhlvdlag lphvtirllp rgvaarggaq pltpyscysf pdpadprtvm
      241 lealttdvrl atavdvdrye rltgwlleaa lgpeetvaal nrlavd
//
LOCUS       WP_357659292             280 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardiopsis alba].
ACCESSION   WP_357659292
VERSION     WP_357659292.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 280)
  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..280
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..280
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30810
     Region          9..64
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          89..268
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mrrlgrllrr areesnrspt eaaklvgwsl pklgrleaae trrikpddla alaelysvga
       61 dtlamwqela aqakergwwa kyrksgiftd dlpdfeseas airtyepqvi pgllqtpeya
      121 eqilregqaq ddgaiaarvd arirrqdilh rhqppeywai idesalrrgm agfpevmvdq
      181 ikhllrmatr sgvtiqvlpy tagahaassg sivimdyaea vdpsivyves yaaslmmeep
      241 aeinrvssvf shvsasalsg aesaeflrai lteaesgsdv
//
LOCUS       WP_357659336             303 aa            linear   BCT 28-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Nocardiopsis alba].
ACCESSION   WP_357659336
VERSION     WP_357659336.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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 303)
  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 303)
  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..303
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..303
                     /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=34959
     Region          13..285
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 msaartpeve ptdrediakr llrgsakasy dplvqidwda plkdlwgmrp ervslygthl
       61 wdrlteeqrr elsrlevast matgiwfeti lmqmlvrhay hndptslhvq yayteiadec
      121 rhtvmfakai erlesrayri dplahalgrv fkalahgpli fggalfveei ldrlqremmn
      181 desiepvvrs tsrihvieea rhiryareef hrdwrrrgpv nraysrlvlg vvayfsatrl
      241 vhpkvyarvg ldprearrva rrnprfidsk telsrkvvst ldtagaisgi grhfwrragl
      301 lgr
//
LOCUS       WP_357659367             273 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357659367
VERSION     WP_357659367.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 273)
  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 273)
  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..273
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..273
                     /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=28362
     Region          23..272
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mllkdriaiv hgaggfvgga varafaeega rlfltgrreg rlaavaeeig rlggpepgia
       61 rldvtdpeev grhadsvvsa agrvdivfna vsygdvqgap lermpfdrfa apvttalaaq
      121 fhpvraaarh maergsgvvl tvvghgppsp elggtrvawe tveamyrqwa celgsrgvrv
      181 awlrtggfae svagadayge dlkvivegre vplssrsdea ttereldela rstvlgalpt
      241 ladaghaavf lasdrarhvs gaalnltaga vid
//
LOCUS       WP_357659460             202 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Micromonospora
            echinofusca].
ACCESSION   WP_357659460
VERSION     WP_357659460.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     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=21718
     Region          4..175
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mnveqirqay gsvaelyiel fgttqqvdpd dlafigrhla grpgpvldlg cgpghitgyl
       61 rslgvdatgi divpefiaha raahpdgryq lgsmrdldvv dhsvagilaw ysvihvppqd
      121 ldgvfagfrr amspagtlvl gffdgdevaa fdhkvvtayr wpvdevserl aragfkeveh
      181 vrrpsdgthr phaaiaaiat eg
//
LOCUS       WP_357659501             472 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Nocardiopsis
            alba].
ACCESSION   WP_357659501
VERSION     WP_357659501.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=49189
     Region          1..455
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdqllemadl vsgiiwgpfv liplllgvgv fltvrlgliq lirlphamwl afvrrkedas
       61 vegdishyqa lstalaatvg vgniagaala igiggpgslf wmwvigifgm atkyseallg
      121 vkyrradakg eqsggpmyyl kygikgglga tlgvafavfg aiaafgigng tqantltqqv
      181 tsvtplpawl vglllmiiag svilggiksi grvasalvpi miigyvgicl ivlavnwaal
      241 lpalqlvfsd aftgtaatgg fagagimlai qmgfargifs nesglgtggi aaaaakttqp
      301 vrqamvsmtq tfidtiivvs mtcmviivtg vwqtdnagdg slltsramse glsvidpalg
      361 aagtyivais vgvfafstll gwayygercv eflggrkfvl pyrlvfiaii yvgsvaslda
      421 vwlfsdiang lmalpnlvgl lllspvivae trkffghpnw rdpdvvmedv rs
//
LOCUS       WP_357659537             319 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Nocardiopsis alba].
ACCESSION   WP_357659537
VERSION     WP_357659537.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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 319)
  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 319)
  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..319
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..319
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35217
     Region          36..302
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mtiyesaent kspttpgiap rplpvftdrd fwrggeldlg aylervglsg egpppptldt
       61 lvavhrahla tipfenvhll ldrpvpldvp sltdkmvrhh rggycyehgl llaavldrlg
      121 ftvtaltarv lvgaegrprp sthallrvdl dggswlldvg fggglleplp lvdgyqvsqd
      181 gwdlrldlit evgaeewllr sfdgeewqnl ysfsmaanlp qdyvifnhyl itdprspfgn
      241 rlmvartvgg tryaltnttl tidrvgadra dpsgatlere vreltvsevg kvlheifdir
      301 ldqeeratve drvrgfldt
//
LOCUS       WP_357659601             248 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Nocardiopsis alba].
ACCESSION   WP_357659601
VERSION     WP_357659601.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=26752
     Region          8..210
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mekrhaiwls epsaaaveia hlagygtvvl diehglfdla aldwliplir skgmsviakv
       61 lgpergpiqq aldfgadiva iphvesaaha ekvcgyakfp plgdrsfagg rtsdfrgfnd
      121 ewvtrqdtgt rcypmiedas afeqieeila lpavdgifig psdlslrrdr gaytageadl
      181 adlrhlaraa gaagkpwvlp awsdaekrla veenaetivt tmqygallsg ftgaletlre
      241 ienelrsr
//
LOCUS       WP_357659615             264 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora
            echinofusca].
ACCESSION   WP_357659615
VERSION     WP_357659615.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 18601864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..264
                     /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=28073
     Region          26..150
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
     Region          <86..228
                     /region_name="arsM"
                     /note="arsenite methyltransferase; PRK11873"
                     /db_xref="CDD:237007"
ORIGIN      
        1 mthpvwadgr ayeayvgrws rpvageflrw lavppgrrwl dvgcgtgvlt stvlavadpa
       61 yvagvdssag faayaraavr ddraafqvgd aralplpdrc vdvvvsglav nfvpeparav
      121 aefarvvrpg gvaaayvwdy aggmelmrhf wdaaalldpa vaerdegrrf avcdpdslrg
      181 lwtdagltav alrpvdvptv fadvddywtp flggqgpapt yvasltardr arlrdllsar
      241 lpvapdgsir ltarawavrg tapa
//
LOCUS       WP_357659660             274 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardiopsis alba].
ACCESSION   WP_357659660
VERSION     WP_357659660.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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]"
                     /calculated_mol_wt=29818
     Region          34..162
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mhvrssstpa sdhprspaaq fattdrlsdy wrfywavaea qigrwlpttp srlldlsgpd
       61 fqgtpravaa ghdvvtllps vdaavrrplt lvngravvpp rpsrrgrlrh vvgdsallrs
      121 fadasfdgvi adnrvlsrhl ateasmaeva rvlrpggral fcvdsvvlgm allaeqdywp
      181 elshapsadv llvpwpdgsi trcftaeqlt emvaeaglel ewvkprtvls astvemmldr
      241 dprsmsrlve melhaaesdd yvgvhliasv vkhg
//
LOCUS       WP_357659674            1025 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Nocardiopsis alba].
ACCESSION   WP_357659674
VERSION     WP_357659674.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 1025)
  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 1025)
  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 11437895
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..1025
                     /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=110632
     Region          57..909
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mrslqddeqi ghagsytpvg gtigdepeag sgvgaaslrw krsvdvsrth sflaytrscl
       61 hreavhrhea tvgrldsdvh acmpagpell lsgarealpl heegarvarl agrhgqalry
      121 gyplvvlgeg tgddrialpl fvvdvrpvee pgerdrpgtp slravgtpdv nvallarigv
      181 tdpedlfelr trlrsgapdp ihrpaavael aaktrillsr leiervddid plgtrgrplr
      241 pvrgahntav lyragpggrp egepfepglp eglladldpt dpegldpdav pgtalepllg
      301 srpearapre rpqrerrrsr srareeavse paapeivpia asplgqaqye vlraamgeql
      361 tvaaappggg vhdlvdtvvr tavaegqrvl icchgesdid evlaradtsp ehpvvraggv
      421 aearrltril vrdtglppaw itdpgepver eddlvgswnr irevweamdd vasgghvlad
      481 lasergrdiv rgwnpeslft perggpeywl hraeraiagg lgglshrsav rrelgvttdp
      541 eslarlcsva rmesewreav errtrrapln eltaildeam eehrragalr lssvtgprlr
      601 rgraavvnrl eslnwndggg rpamgdlldi lpawicrtdq aralpsgpgs fdlvivvgae
      661 rtrvgellpv lyrsvralvi gdpahpgpat alepeeerra latagldaee lderglrhgt
      721 gsalraaarg asatlwldeh dgapeplasv aseycyggri avrtephpgd epvvdwrdva
      781 gdceaapgss yvnrdeayrv avvvdeldrt lpeewtltvv aplqpqvall rrllrqcvlr
      841 rrvrvggpel pvdgttdvtv lspmltadap aiaerrvmgm ghlwssvltr trrrlvvvgd
      901 rahwaagrgp ltallvrdge gglglaeepr ddpatvalve alraagtevv vrprvrgwat
      961 dlvvrygarr vvvlldrepd gpalrrllar gealdrgved lvvivpawrc ladprtlvee
     1021 ilsac
//
LOCUS       WP_357659678             255 aa            linear   BCT 28-DEC-2024
DEFINITION  RluA family pseudouridine synthase [Micromonospora echinofusca].
ACCESSION   WP_357659678
VERSION     WP_357659678.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 255)
  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..255
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..255
                     /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=28761
     Region          14..239
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mttfswselr rrpvyeddhl lvldkppgis vmgerhtdsl tdlaaaagep vhwvhridkv
       61 tsgllllart psahasltrq fadrgadkry lawvegarlp ergtidlplr pgrkgtiria
      121 gerdairyda drrrfelpes avdrskpsyg srtdfatalv sgdrtllvlk pvtgrrhqir
      181 vhlawlgfpi vgdplfqrgq peqrtylhsw gceitcdwrd eprtrfwapp geefldvfad
      241 grkphlddal etlag
//
LOCUS       WP_357659679             334 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Nocardiopsis alba].
ACCESSION   WP_357659679
VERSION     WP_357659679.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..334
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..334
                     /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=35943
     Region          1..332
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 midlrsdtlt rpteemrram asaevgddvw gedptvrale eetaallgre aalyvpsghm
       61 anqlglyvst rsgeevwahe hhhligdeqg aavvlsrvlp rlysgdpfpp qellekwitg
      121 lgdvhradpa llwlentftg rvvpleeqrr vtdfahehgl lahldgarlw naaielgvdp
      181 arvaegfdtv svcfskglga pvgsalvgdv dtirrarrgr kllgagmrqa giiaagalha
      241 lrhhrerlae dharaavlae rlsglpglea vartnmvllt taggeaarya eafaeegvra
      301 lgggdrirmv lslevtdsdv ekaaeaitra vsrl
//
LOCUS       WP_357659686             185 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nocardiopsis alba].
ACCESSION   WP_357659686
VERSION     WP_357659686.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 185)
  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 185)
  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 185)
  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..185
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..185
                     /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=20067
     Region          44..181
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 meviadaaqi isytrmkcss ngtwtihhvf tseeqvmtra aptidvcvll tredgcvllg
       61 erkgtgfadg qygipgghle sgesvpqgaa remkeevgvv idpddlvcah vahhlgsegk
      121 trigfffttt rwqgspvnre pelcsglswf dpaalpenti pyiatiidri rsgqtfsahg
      181 wdrah
//
LOCUS       WP_357659688             426 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardiopsis alba].
ACCESSION   WP_357659688
VERSION     WP_357659688.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 426)
  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..426
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..426
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46131
     Region          <65..94
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mvgtghtdss afdvvlvpld vtykvvfvpt sphigpqlar lrrrraltqd elaasavvsv
       61 dvvrrleqgk rtsarlstld slaralgctt adllaldqke gasgggprve eirhalttpe
      121 vlgliepvee epvcleelrg qmqrvwalyq dgfyaqvalr lpevlaqarl lgresvgdeq
      181 veaegllata yqaaagvtit lghpdlsfla veralnaarf sgselhhasa vnflswvyrr
      241 sgrlsdaehv atraaeaiep pwsgassshl avfgsllvna agaaartkhv nrcrdltsia
      301 rsaaervgsd hvdrwavfgp gvvamtavnd avelddldta rrfidqvptv egvpsswrar
      361 yllnvaltht rhrnyqqaie alaeahrvas ewaryhpqsr vtaqillerg ygrkapnlvd
      421 iaqhda
//
LOCUS       WP_357659689             256 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora echinofusca].
ACCESSION   WP_357659689
VERSION     WP_357659689.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..256
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27574
     Region          24..254
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtagadaaag aarevglvrp rslpgaalrl vcfpyaggga svfaswpagt gpdievcavq
       61 lpgrearfgq rpfqdvrtlv saveaslggl ldepfalfgh smgalvafef arrlaarrrr
      121 apahlfvsar paphlprpwp rahllpddql idrvrqiggt paqvladarl mrlvlpvlra
      181 dfavndghvh rpgplldcpv talggrddpe aspraltawq rhttgpfrlr lfdgghfylr
      241 ehrdellrvv reslvg
//
LOCUS       WP_357659695             260 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357659695
VERSION     WP_357659695.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26894
     Region          5..260
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 midprlagrt vlvtggsgnv gaaiarafaa qgarvaihyl aqdpsspagi ewahvtpaeg
       61 eaarlaeelg ngsfavsadl sepegpvrll revversgai nvlvnnaahc elpddidtlt
      121 haslerhyqv naiapavlta eavrlrrgda llcvvnittd aarafpgqtg ygtskgalea
      181 ltrstaldla argvrvnava pgpvqtgwmd ddllarveei vpmgragdpe diadavvyla
      241 shqarwvtgq vlqvagghal
//
LOCUS       WP_357659702             208 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357659702
VERSION     WP_357659702.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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 208)
  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 208)
  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..208
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..208
                     /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=22313
     Region          2..207
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mriaivgatg rtgkevvrla mrdghhvvav vrnpnrlndl rptevrvadg ldvtalseai
       61 qeveavvmcv gpvkgeradv lsaaittlie amgnagverl vaitasgwlv dgddplsrfl
      121 akpilaralr eenaafasae rsisasplew tivrppmlkd gpatgsyrqr rdgnvrwhys
      181 mrradlaram ldvledptav rstvavtg
//
LOCUS       WP_357659730             471 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora echinofusca].
ACCESSION   WP_357659730
VERSION     WP_357659730.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     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=49085
     Region          238..461
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 maeptaaspp prhrpgrtlt sravlvtcav alvsvlvtai vavplavrgv errdqealaa
       61 qarlaaevlr prletgrtad eerlirqlda qgvdaylirg gvaerpglpp rvvrrvaegr
      121 nvstrrpldg rrtliegral pggdglvltr srptapwrqv vpslwlplla glaagvaagl
      181 llarrlarpi rraadaaarl ragdravrvp veppdevadl ayalnglaaa latsegrqre
      241 fllsishelr tpltairgya ealadgvigp adaagagrtv laeaqhldrl vsdllalarl
      301 eaadfplepv pvdlarlaad agrtwadrca avgvpfrvea pdaavpaytd pgrirqvvdg
      361 llenalrvvp pgapvvlavr pagadpaggv vevrdggpgl tdddlavafe rgalhqryrg
      421 vrkvgsglgl alaaglvrrl ggevaaghap eggaaftarl ppdpyltrts v
//
LOCUS       WP_357659737             297 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nocardiopsis alba].
ACCESSION   WP_357659737
VERSION     WP_357659737.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 297)
  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..297
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..297
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32066
     Region          3..281
                     /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 mamistdktr lsydeagdgp avvfahagia drrmwdhqft nlsrthrvir ydqrgyggsa
       61 dhegpvphhe dlldlmdale igsatlvgas fggayavdaa laaperveal alvcpgmsgh
      121 rwtgeflres reailaavpp drlatyragd avvlpedvaa maeaqarfmv lgpdrspedl
      181 pleawdlsll mlrelfarrw sspanepawp erpavdrlge itvptlvvkg lsevaavqev
      241 adlymegipg arsltmpdtg hlpsverpge ltaalaefld eevspssttf grdtsrr
//
LOCUS       WP_357659806             430 aa            linear   BCT 28-DEC-2024
DEFINITION  ParA family protein [Micromonospora echinofusca].
ACCESSION   WP_357659806
VERSION     WP_357659806.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 430)
  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 430)
  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 430)
  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 430)
  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..430
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..430
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45686
     Region          <36..>145
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          169..420
                     /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 mhddgrhddp rvtgspgdpv sretdypnwa pggasfrppg wdaaappsda eavgpehpat
       61 raapdvprag npaggrvipi rrnasasarf elpvpqqpap dsvpdatpep vpvtdttaap
      121 gasaaeaayv sretptreed dpplameamr avqilnpsge vtmprpertr vmcvanqkgg
      181 vgkttttvnl avalalhgnr vlvvdldpqg nastglnvph htgvpdvydc linsvpleev
      241 aqgvegipnl wcvpatidla gaeielvsvv aresrlarai aaypghfdyv fidcppslgl
      301 ltvnalvaaq evlipiqcey yaleglnqli nninlvrqhl npkldvstil ltmydrrtrl
      361 adaveqdvrn hfgdkvlqav iprnvrvsea psygqsvmty dpgsrgatsy feaaqeiaer
      421 gvkepvgrna
//
LOCUS       WP_357659836             876 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora echinofusca].
ACCESSION   WP_357659836
VERSION     WP_357659836.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 876)
  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..876
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..876
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=91561
     Region          14..874
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtpdhdrspq pggrtglsal lrghrlaagl tqaelasrag vgvrtvrdle rghssrpqrt
       61 tvellasale lagparsafl aaargpvpaa gpvtpggapp arvdldhhag tpaplpppva
      121 lvgrdrdlve laglftdghg prlvslvgla gvgktalals vvhavarehp ggaagvlige
      181 gsdaadvlsa svavfgvarl seltarldgr aalllvdaae rapdavaetv hrltgavpsl
      241 rvlvtgrhpv glpgervwpv apldvpppgs erkgpaalgd ypavalfiar ltqvrreppg
      301 paelpalaal vrrlgglpla ielmaargri ldlnelldry gdrvldlats sgaadrpgwd
      361 trdpgrpesp raavaetlrd avavsyrlla pderaalrrl aafgnrwsva laeemladpa
      421 dtdgtvvvdp vplldrlvel gllsvrgsgp frfrlldavr dfaaeqatga geltairrrh
      481 aqvvarlvar tapelvgadl paavhrldev sgdissalah aavddpltal rlaaalsrww
      541 rfrgrdvpgr qwlrrlladp rtadvdpvlr awaslgvarl aaehgagaee lpaarealaa
      601 freagdvtge leartvlcal lialgeygea rtqaetvlal avrhgrvrdm avaqnnlawh
      661 dirvadlaaa rrrlatvdrl aaqsgeqrlr vlaranlaev srlegryada vdqgrrvvaa
      721 ladlgdpghr rrvlgtvgla laragrsaea vavlaelrpp pgppaprlge awppgrlpgv
      781 tpgvrpedgi caliegnlal hrgdrelaae wfaaaaaaga ggqdrrdvve alvglaassg
      841 dpvvmdhler acrqsgvrll pheeellras tasrng
//
LOCUS       WP_357659892             347 aa            linear   BCT 28-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Nocardiopsis alba].
ACCESSION   WP_357659892
VERSION     WP_357659892.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 347)
  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 347)
  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 347)
  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..347
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..347
                     /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=36872
     Region          2..182
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mtdsrvrdal asvsedyytr aedgglirqs ssveaitaml erldvspgmr vleigtgsgf
       61 sgallgelvg esgsvvsmdv vpalverakg lhsrrgadni rvvtgdgvag mpeqapydrl
      121 vawaagdrlh rtwadqcvtd avlvvpitla avlranaivr arrtreggle adrlwsggyv
      181 emypeeltqw lvpprgvqaq atdaegnpww isgtwidegd rhvaqrlvet lasearvege
      241 llasgesced frtylyatas aglsmiglga rgwapghata esaavvlgdg glltaggpes
      301 alelkrraee wrssgrpgag sliptleevr dgwfvrsrgm rssvaea
//
LOCUS       WP_357659991             227 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Nocardiopsis alba].
ACCESSION   WP_357659991
VERSION     WP_357659991.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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 227)
  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 227)
  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 227)
  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..227
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..227
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24773
     Region          69..223
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mnknltisls ilailavvit lgvfaysgsd geeasgprps apeapptasa ellvrddsry
       61 ldrveeaqvt vvefldfece acyaqfpvme riredyegri dvviryfplp ghansrpaaa
      121 aveaaaqqda ldemyvrmfe tqpewgesre sqaelfigfa edlgldvdef tevmespete
      181 arvqadfddg velgvqgtpt ifvdgvrtss mpsyeelssr idaglge
//
LOCUS       WP_357660009             600 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Nocardiopsis alba].
ACCESSION   WP_357660009
VERSION     WP_357660009.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 600)
  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 600)
  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..600
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..600
                     /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=64316
     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 mtlppgtand ltlvdllrrn arehpdlpal sgpsrdgrgr ttltwervha tvtslaagli
       61 dlgirpgdra llmmgnrpeh wladlallha gavpgsvyst sspeqiahia rhgrarlavv
      121 enptvaavwe pllrdpatpl eflvvvdgpd lerghlsyed lvgspdtrgt eglhepgpdd
      181 latvihtsgt tgapkgvait hravlaqaia ldrsvgvpgh pdhvcylppa hiaervlgly
      241 lpllrashvw mcpeladlpa tlarvrpphf lgvprvwekl avavrlvmag lsederaavd
      301 aarriaterl ahvergdtvp eeleegyrra raevltplla glgldrlila agasaplppd
      361 lvrfwaglgv vimdawglte svgvatmnvp spggfrlgsv grplpgielr tgedgevflr
      421 gdslfegylr edgtidpavd degwfatgdv grvdedgflw itdrkkeliv tsggknvspa
      481 lvenalkehp ligqafvhgd grpypvallv ldpevtpvwa vsrgvdpgpd paghpeivae
      541 veraveaana rlsrpervkr hrllagewgp gsgeltpslk irrrvvaery ageidalyee
//
LOCUS       WP_357660030             263 aa            linear   BCT 28-DEC-2024
DEFINITION  glutamate racemase [Nocardiopsis alba].
ACCESSION   WP_357660030
VERSION     WP_357660030.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..263
                     /product="glutamate racemase"
                     /EC_number="5.1.1.3"
                     /GO_function="GO:0008881 - glutamate racemase 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=27015
     Region          1..246
                     /region_name="MurI"
                     /note="Glutamate racemase [Cell wall/membrane/envelope
                     biogenesis]; COG0796"
                     /db_xref="CDD:440559"
ORIGIN      
        1 mrialidsgi gmlstaaalr aarpdadlyl smdpdhmpwg prtpeevigr alagaraatr
       61 avaedggrld avvvpcntas vhgldalrae yepgvpvigt vpaikpaaaa gtpiavwste
      121 attrsayqrg lvetfasnle vtpvacigla eavesadprr iadavdyaae ltppevrgvv
      181 lgcthydlvg qrisealggr aalftaadav aaqtlrrigt aeppsaragr vrvlasgrpa
      241 elpaaalnyp agrslldgtr adr
//
LOCUS       WP_357660057             254 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357660057
VERSION     WP_357660057.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26192
     Region          19..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 madtrrlavv sggsggigra vvlslaeagd evvalgrspe rladladtar ergfhvatrv
       61 gdltdpatve slaetlgpvs vlvnnagdah sasladtdld lwrhhldana tsaflltrel
      121 lpgmlrrdrg rivfvastaa htgsrytaay taakhavlgl arsvaaevas ggvtantvcp
      181 sfvrtplter sisriaertg rdperaeral aastplgrli epeevaaava ylasplagav
      241 ngqtltidgg dtqr
//
LOCUS       WP_357660091             153 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nocardiopsis alba].
ACCESSION   WP_357660091
VERSION     WP_357660091.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 153)
  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 153)
  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 153)
  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 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..153
                     /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=16495
     Region          13..120
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mymgnstgdr pstplhsvsv agavvredgr lltirradng rwelpggvle laetpeegvr
       61 revweetgvh vqvsgltgvy kntargival vfrcapsggd prpsdestav awltpeevae
      121 rmsevyairl ldaldpsgph irshdgkrlv qar
//
LOCUS       WP_357660172             278 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357660172
VERSION     WP_357660172.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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   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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..278
                     /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=29685
     Region          4..203
                     /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 mtapvlvtga tgntgrhvva gllaegipvr amtrdperaa lpagaeivrg rttdpedvaa
       61 aaegasavyl vwpgtddeae gaaevvealg grvprvvyls aqgaeeggvw gavetlvrrn
      121 vpewtflrvs glatntllwv egvrrgvvee pfgrarrslv hekdvaamav ralvdpdhvg
      181 raytvtgpes igqaeqvrvi geiigretrw veqspeeard glvervgeef adqllshwsa
      241 nvdvvepvsq dvprvlgrpa ltyrewvgdh radfapeg
//
LOCUS       WP_357660203             278 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nocardiopsis alba].
ACCESSION   WP_357660203
VERSION     WP_357660203.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   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 278)
  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..278
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..278
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30010
     Region          13..278
                     /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 mgrikvgten stdielhyed kgagrpvlli hgyplsgdsw egqipallda ghrvitydrr
       61 gfgrsdkpsi gydydtfaad lhtvmetldl rdavlvgfsm gtgevaryls tygsdrvaka
      121 vflaslepyl aitddnpdga appsffegvs eavkkdryaf ftgfyadffn ldenlgtrvs
      181 eeavrnawnv aagagpiasa aapltwptdf radiprvdvp alivhgtadr tlpidatgrr
      241 faealpaaey veiegaphgl ltthtaevne illdflgr
//
LOCUS       WP_357660190             293 aa            linear   BCT 28-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Nocardiopsis
            alba].
ACCESSION   WP_357660190
VERSION     WP_357660190.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 293)
  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..293
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..293
                     /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=29986
     Region          150..>230
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mflgmvtetp sthpvppspa pahspdpsrt tavdprglta flvisfafsw tawwlgprll
       61 dggdptpavl vggfgpmvaa ilvtaatkgr agvgalfrrh slrhrggiap yaitalvvla
      121 iagsaalpvy lgtasveeea lkaalmtvpv qfllialvgg gneelgwrgf alprlqgslp
      181 plaanvvlga iwavwhaplf evagtiqsev yfpayallcv gltvvlghvf nsarggvlaa
      241 vvahaavnvv aglkgmlvgd paglfevsav llvavvltla trgrlglrrp ads
//
LOCUS       WP_357660202             181 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora echinofusca].
ACCESSION   WP_357660202
VERSION     WP_357660202.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 181)
  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 181)
  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 181)
  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 181)
  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..181
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..181
                     /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=19662
     Region          4..175
                     /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 mypitipgrv itlrdlrpdd aadalaivgd nrvtqwlsfd srdqaatvam vegavaraql
       61 tprneyylav adtsdrmigf arlgltghqa aklgyaigad hwghgyatda astivdygfr
      121 elrlhritaa igpdnaasia vakrlgmrye grlrdhvytn nawrdsllys ilapewsgtt
      181 g
//
LOCUS       WP_357660217             284 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Nocardiopsis alba].
ACCESSION   WP_357660217
VERSION     WP_357660217.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 284)
  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..284
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..284
                     /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=29691
     Region          1..>59
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtshpdveal affaedlldp deersvadhi etcatcattl ddlagvsrtl agtpapampr
       61 dvtdllddgi araaaeraan eatdgtehea ppveenrpat vvpftpkrrg lglprlmmva
      121 aasvfviggg tavltnvlse dradqgvass plteesesdp ditrsystea lesgtvytee
      181 rlaeqasrvl amteegesgt gpgvqtlssd lpagaqecvt lyeeatgsrv tllddalweg
      241 gsesgerawv lfvrdadgas vvvldptcar ggdvteqvla eerl
//
LOCUS       WP_357660366             349 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Micromonospora echinofusca].
ACCESSION   WP_357660366
VERSION     WP_357660366.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 349)
  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..349
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..349
                     /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=38343
     Region          5..348
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mvlgavaepp vrrgsdyaql srrisgagll errpgryvtr itltlgvfaa gwaavglvgd
       61 swaqllvavf lavattqvaf lghdaghrqm frrrgpseai glltgnlavg lsygwwvdkh
      121 nrhhanpnhe dedpdvgaga lvwtyeqaaa trgfgrrlar rqawlffpml llegfalhva
      181 svqaivgrds dgrfrtpmrh rrvealllvl havgylgall lvmsplkall fvavhqglwg
      241 lymgcsfapn hkgmpmptad ddldflrkqv ltarnvrggr lvdvalggln yqiehhlfpn
      301 mpranlrrar pivraycaeq gipyaetglv esyrqalahl hevgrplrg
//
LOCUS       WP_357660341             269 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardiopsis alba].
ACCESSION   WP_357660341
VERSION     WP_357660341.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..269
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30257
     Region          9..>62
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          85..265
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 makpdpawkq fgrhmrshre aldlrqvdia kkigvvgscy sswetgsrkv dekyvnslde
       61 hlkaggriae ewekahrqvk tpfrfaelsd leaaatqird fqplvfpgll qteeyaramf
      121 edifpgmpsa sieelvqtrm drqriledep rplvlflige tvlrqqvgar gpellkkqae
      181 ralqdledgk vrvqiipqas grhygsggaf rlytfadeps vasaeymtge avisdkeryq
      241 ecvttfgllq gealseaatl qmlremvgr
//
LOCUS       WP_357660399            1007 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nocardiopsis alba].
ACCESSION   WP_357660399
VERSION     WP_357660399.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1007
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..1007
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=108437
     Region          111..1006
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrvdmlgplr vevdgrstgv ggprlralla rlalepnrvi ghrtliedlw pegevgapes
       61 pmvalhslvy rlrralpepe avcsepagyr lalpddsvdl rlferlarqg reelragrha
      121 kaveylsral asrrgeplsd iprlpfveaa alhleeiglg avedraeass llpgvespsv
      181 aelerlaaah plrerlrtll vaalaaegrr aealvayevh rarlaeelgt dpgpelralh
      241 lrvlreehar patpappars grrtplstfv greaerrlve erlaehrlvt llgpggvgkt
      301 rlasvaasdv dvrahvvelg pvtdpelvph tvaaalglrs pvdpvadivd alsitdtllv
      361 ldccervvda aaalavelle rcpgsrvlat srepldvpge alcpipplpl eaarrlftdr
      421 araarpdlra seeevdricg rldglplaie laaarlrsmt vealaegled rlgflaggnr
      481 lapphhrdlr gvvawswgll idteraaaer lsvfpqsftp sdgervgvra stlyslvdrs
      541 lverdgdryr mldtireygn erlvenggsr eardahaecf ldlaeradpy lrgpgqttwp
      601 drlavdhdnl ltalghlrdh gpqekalrlg atlglfwair gdhatavfhl rsllgvsdgr
      661 gngenglrna vravyllnat fagaltdart vvgpppddst pvgafvaall amaesrtteg
      721 raalephlsh pdpwtrgtlw parafldgts gdiargshdv ehavrafret gdhwgsslll
      781 mslayarsas gdaeeatall dealalsral gthhgqrvwa amahvdaget grardlleev
      841 vtdatsvrrt alarvcladl aryegdleka sglldmadra ggekdpsesa lyhsaaghla
      901 aatgdldear rhlrvafvla dampdlpmla qvsvgtadvl rrgseperga rvagaahavr
      961 ggpaprhpdv vrltrelsah rahydraall sveealallr eehgrae
//
LOCUS       WP_357660430             447 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora echinofusca].
ACCESSION   WP_357660430
VERSION     WP_357660430.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     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=47059
     Region          12..430
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtataqaapr alpplgpnrr lklpkqaert lgngltviav rrpavplvev rlwmpfgrah
       61 largamlaqt llsgtrtmss vriaaelqkv gggltagidp drlmlsgagl vtgldrmlei
      121 laevltdasy pnddvaterd rlvdriqvar sqpahlarta llrrvygthp yavqtpepea
      181 vravrpavlr tlhaqrvhpa davlvlvgdv qperaldaae kalsgwngag htadlppapp
      241 lepgplllvd rpgavqsslr ialpavprth pdhaalqlan lifggyfssr wteniredkg
      301 ytygghsvve hsvagsvlva aadvatevtg pallettyel grlatlppge deleqarqya
      361 lgtlqlgist qaglasltsa yagsglrlef laehaarlak atvadvaeva arylaparaa
      421 tvvlgdaeri gpqlaalvpv tteparp
//
LOCUS       WP_357660425             455 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Micromonospora echinofusca].
ACCESSION   WP_357660425
VERSION     WP_357660425.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 455)
  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 455)
  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..455
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..455
                     /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=48814
     Region          1..445
                     /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 mtdiprravs rtaklaalpl gfagrtvlgm gkrvtglasd visaeiqqrt aeqlfsvlgq
       61 lkggamkfgq alsvfeaalp eeiaapyrqa ltklqeaapp lpaasvhkvl aeqlgpdwrd
      121 rfvefddtpa aaasigqvhr avwrepgygp sgapntrdva vkiqypgagd alladlkqls
      181 rlggmfraiq pgldvkplla elreriteel dyeleaesqr afaaayaddp eihipavvsa
      241 sprvlvtewv egtplaeiir egteeqrdea grlmailhls apqragllha dphpgnfrll
      301 adgrlgvidf gavarmpegt pepigriagl alrgdadgvv aglraegfig steeidaqav
      361 ldflrpmlep iaadefrftr awlraeatrl asprspayql srqlnlppsy llihrvtlgs
      421 igvlcqleak apyrgvlerw lpgfapstgq pstgd
//
LOCUS       WP_357660504             337 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora echinofusca].
ACCESSION   WP_357660504
VERSION     WP_357660504.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,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..337
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..337
                     /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=37222
     Region          1..332
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtenilevrd lvkhypvtrg vvfkktighv kavdgvsfdl kagetlgvvg esgcgkstla
       61 rvlmnlekpt ggsvhykgqd isklsgpalr rlrrqiqlvm qdpytslnpr mtvgdligep
      121 feihpevapk asrrdkvkel ldlvglnpeh ihryphqfsg gqrqrigiar alalrpeiiv
      181 cdepvsaldv siqaqvmnll eklqgelgls yvfiahdlsv vrhlsdrvav mylgkiaeig
      241 tedeiyerpt hpytqallsa vpvpdptvrd nkaiirltgd vpspvsppsg crfrtrcwka
      301 qdicaeqvpl leirpgsdhp sachfaekre ivqthem
//
LOCUS       WP_357660514             386 aa            linear   BCT 28-DEC-2024
DEFINITION  thioester domain-containing protein [Micromonospora echinofusca].
ACCESSION   WP_357660514
VERSION     WP_357660514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10551059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..386
                     /product="thioester domain-containing protein"
                     /calculated_mol_wt=38830
     Region          71..185
                     /region_name="TED"
                     /note="Thioester domain; pfam08341"
                     /db_xref="CDD:462437"
     Region          <184..344
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <305..>357
                     /region_name="PLN02983"
                     /note="biotin carboxyl carrier protein of acetyl-CoA
                     carboxylase"
                     /db_xref="CDD:215533"
ORIGIN      
        1 mfgqrgrrwa rialatvagg alalgavapa aaadktgvak svkgsnvtlm lngqpkstga
       61 lalkidgklv pafcidyhtn vaidgkykeg twdesqvknl gkvqwvlthg ypnadaakll
      121 aaagatapak adadkllyfg tqtaiwnfsd gvklgdwvdn skllgknqyd vvkkvhdylv
      181 anatdqpepk aelsvdpasa katvgekagp ftvkgpagei tvaadggsav daegkpvttt
      241 tnggqfwlva dgagevkvtv saqdsvsfgr vflftgeraa qklilggstg atvtakaeaa
      301 faaaptesps psapaespsp sapaespsps apvdspapst spasgggdlp ltgspiaasi
      361 aagvallaag avavllfrrr klrfta
//
LOCUS       WP_357660539             259 aa            linear   BCT 28-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Nocardiopsis
            alba].
ACCESSION   WP_357660539
VERSION     WP_357660539.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..259
                     /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=26524
     Region          122..222
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mtagtapeea pdtgasrrgi valvvwllvs svgavgllav qpligldmev lspvmfapai
       61 galtawvfvr ggvprfgtav sggpfviavl lslaasaiyf lwvslvrgaa peipgavagv
      121 pvalmilaqa lgalgeeigf rglllhglnr wttwpisavv tgllfgfwhv qyyglpplef
      181 lvfvlgaval tltmaavmvg sfwqrmtict iihtganlal aftggdhval ttfggamvva
      241 avvivptall lrrkggtag
//
LOCUS       WP_357660545             363 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora echinofusca].
ACCESSION   WP_357660545
VERSION     WP_357660545.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   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 363)
  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..363
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..363
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=38934
     Region          74..363
                     /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 mtsrsriplp rtgharaavg alaavgvaaa glaagvater alvrklkadp adpyagevfg
       61 dqrhdesfrl empdgtdihv evveptrpvp gnptvvlvhg fcldmgtfhf qrkllaerge
      121 hrivaydqpg hgrsgrletg eydltalgrt lrevidrtap egplvlvghs mggmtimafa
      181 elfpelfgdr vvgtvlmats ggllaetklv apallgrvga pvlhmvgnvt ryggpvidra
      241 rrsttnvawl ltrkygfgtr hpsaalvsyv etmnsrtsad tvtrylrtla thsrfpalaa
      301 ladtpvlvvv gdkdmitpvt hseeivrrlp haefvkisds ghvvmlehad evdaalvrfl
      361 eal
//
LOCUS       WP_357660640             203 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardiopsis alba].
ACCESSION   WP_357660640
VERSION     WP_357660640.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 203)
  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 203)
  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 203)
  AUTHORS   Rosinski,J.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..203
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..203
                     /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=22101
     Region          6..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          90..176
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(93,106,108,121,124,128,162,164,176)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mdhdldqald avgprlralr lqrgttladl sestgisvst lsrletgdrr palelllpla
       61 raygvtldel vdapptgdpr vhlrpvnrhg mtvipltrrs ggiqafkmvl spgggrevpd
      121 pqshegydwl yvldgrlrlv lgehdlvlap geaaefdtrt phwfgtaddr pveilslfgt
      181 qgerahlrar prrgqgrdeg ssa
//
LOCUS       WP_357660657             326 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora echinofusca].
ACCESSION   WP_357660657
VERSION     WP_357660657.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     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=33928
     Region          17..>68
                     /region_name="MDR"
                     /note="Medium chain reductase/dehydrogenase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cl16912"
                     /db_xref="CDD:450120"
     Region          52..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(63,65..66,70,129,133,153..158,177..178,182,194,
                     209..210,212,232..233,259..261)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mtgearafwl rtpgrgeirp mplavpgpge vlvrsrysgi srgtetlvfa grvpadqyaa
       61 mrapfqegdf papvkygyln vgvveqgpae lrgrtvfclh phqsayvvpa eavvpvpdav
      121 pparavlagt vetavnalwd aaplvgdrvs vvgagmvgcc vaallarfpg vrvelvdtdp
      181 traqvaaalg vgfappqeat ggrdlvvhas ataaglqrsl ellrpegtvv elswygdrtv
      241 alalggafhs grltvrasqv gavaparrds rsfadrlgla ldlladpafd alltgesrfa
      301 elpdvlarlt agslpalchl itydge
//
LOCUS       WP_357660670             323 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nocardiopsis alba].
ACCESSION   WP_357660670
VERSION     WP_357660670.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 323)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..323
                     /product="phosphotransferase 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=34765
     Region          7..>236
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mcvvggrtdp gaivavaara lggrgravgv erlrggtrkg vyrvrveggr dvvvyvwgra
       61 ehrwpeaave regpfadpdg ldlflgaarv legagvrvpa vewverdhpg pgvdmavved
      121 vpgpdlegll ardrragmrv verlgpvlet maslrgsgwg rvsgavrgeg acerlvlera
      181 lrdlaegarr rpdlaavrgr vergvveaaa rveprrrygl vhgelgpdhv lvgaggepvl
      241 idmegtmffd vewehvfvrl rfgdlyrsle vpgldgarlg lyawaqrlsl vagplrlleg
      301 gfadrrvleg iveaqmgwig ahv
//
LOCUS       WP_357660683             400 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nocardiopsis alba].
ACCESSION   WP_357660683
VERSION     WP_357660683.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..400
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43308
     Region          <36..270
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mvdllraera rarrerevvv adpalrgpga svsevddgla lsflcchpsl svtsqvaltl
       61 ravgglttaq iahahgvdea tmgtrigrak rrsaeagarf tlpvgdraar avavmrvlyl
      121 vfnegytasa geelsrvdlm aeairsarml raalpeeaea agllammlll wsrraartga
      181 dgvlvplkeq drslwdveai eegralldgv wnrgeagryq veaaiaavha ssevadragp
      241 vrlarvvava raygaerglt lldelgrrhr wgmirwsvgv svwcapicrr wsgtpmpprs
      301 sigrpprwap igwrdvicws vpivcaevgr grprvrverg aavvfgwggr scvstgatra
      361 sippsgrtar scvnrrwwkg rrvrrirpgc ggsrragwsr
//
LOCUS       WP_357660707             458 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357660707
VERSION     WP_357660707.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..458
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48186
     Region          1..457
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msgvveelra algeglvvtd pevmegyahd eaewapyegp vavvrpreta dvaavvrica
       61 drgvpvvarg agtglsgaan sgrgwvvvsf ermnrvlavd pvqqsatvqp gvvnddlrar
      121 vsldglwypp dpasspwsti ggnvstnagg lccvkygvtr dyvlgmevvt gtgrvvrlgk
      181 ttakgvtgyd laglmvgseg tlglvtevtl rlvplrtgve htvvgyfdsl tdagravaav
      241 saagvvpsal elidrfclqa vdewknmgls aegevlllar sdlpgesgra eaerilecfe
      301 keravyavrs tdedeaealf aarrlaypal erlgpllted vcvpkasvpt mleaierige
      361 rfrtrignia hagdgnlhpl fivpagdeea keraqrafee ivdealamgg tvtgehgvgl
      421 lkmrgaadel gpdvvamhra ikgaldpkgi lnpgkvfv
//
LOCUS       WP_357660713             350 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nocardiopsis alba].
ACCESSION   WP_357660713
VERSION     WP_357660713.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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 350)
  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 350)
  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..350
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..350
                     /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=37315
     Region          1..346
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrmgvvglrm glhlarwaer mgievvagcd hdpetarhad relpgmvlve hwrdlltagl
       61 davvlandfd ahaplaiafl ehgvhvlset aacvspeegr dlvaaaeast atysfaenyv
      121 llphtrllre svesgelglp dlieadylha mapeavqgli gdpshwrgri pptaycthsl
      181 spilaitgam pvevtafpvd tneprlasvm avrlstgala ltrngflqge seshwsqisv
      241 rgdlgmaesl rapgerswsv rvrheawavp egrvreeerl tapllvdgap vdrgaegtvl
      301 lfqglrrtve egapppvgvr eavaaslvgv agarsleegs vpvavplpwa
//
LOCUS       WP_357660722             541 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora echinofusca].
ACCESSION   WP_357660722
VERSION     WP_357660722.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..541
                     /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=54385
     Region          2..540
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 msaftgtgrl arlvlrrdrv rlaiwvlgtp llgyalagsv kefypdeaar vgyagtsass
       61 lvarafngpi agtdlgavvv aetyvtlall aallstfavv rhtrqneetg raellgasvv
      121 gryalltaal lvivaanvaa tvllaaalag aglplagsva aaaaicgvgv aftgiaavta
      181 qlsvtsrgan alaaaavgis fllraagdvl geqtdgglrv vsawpswlsp lgwgnqvraf
      241 ggerwwtlal paalllagva layalaerrd igaglvaprr gpatatpgll spaglawrlq
      301 rgallgwaig vavlgfsmgi agdefnamie enpaaaeais amgggarlid aylaamlglf
      361 altigayvvq allrtrtdet dglleavlat avgrtrwlvi qvaaatlgal alvllggltt
      421 glgyglvagd plgravelgg aalvrvpall vvvgvvtalf gllprwsaal swaalivfll
      481 lgqlgavldl pqaalnlspy thvpsapavd pavlplavlt avaaallaag magfrrrdvp
      541 s
//
LOCUS       WP_357660799             325 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora echinofusca].
ACCESSION   WP_357660799
VERSION     WP_357660799.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 325)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..325
                     /product="phosphotransferase 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=35531
     Region          7..259
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mdgaragltv delrpvawaa fgrgrtllsv erltggtkkg vyrltlddgs tgiayvwhpt
       61 edywpaqaal epddpfghat gaglfeaahr eftaagvrmp rllltptagl lpgevavvqd
      121 vrggtlqdlr rrdprraevv larlgdavrs mharrrdryg rpgldgptpg rpveriildr
      181 alrdlteaaa rveriaavrd rladalaerc aavaprsryg lihgelgpdh vlvderdrpv
      241 lvdiegavfl dvewehafle lrfgdaypal avdgldgnrl rlyrlatyls lvagplrlld
      301 gdfpdragml aivehnitrt ldqla
//
LOCUS       WP_357660807             248 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Nocardiopsis alba].
ACCESSION   WP_357660807
VERSION     WP_357660807.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=27388
     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 mdlpriftir esehrihnpf tpdklatlgr slrlpagtrv ldlaggsgem lctwardlgf
       61 tgtgvdistl fteqararav eldvadrvef vhgdaaghvs dtpvdlaacv gatwigdgva
      121 gtvellqrsl rpggmmlige pywrltppde etakachatg pddflslpgl iesfgdlgyd
      181 vvemtladqd swdrysaaqw ltmrrwldan pddemavqvr eelttepary trytreylgw
      241 gvfalmrr
//
LOCUS       WP_357660826             382 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357660826
VERSION     WP_357660826.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=40428
     Region          13..367
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mdvivvgggi vgtsaafhla gkgvstalvd aahagqataa gtgivfpwpf pwddpreqef
       61 klraaehypr lmaelaedgh pagyevvggl svdregddsg fdlldtlsrr pefstmgrve
      121 rlapgeprah fplipedygg vyiegmarvn grtarsalfd aaeerglryf kgdarllwng
      181 hrvtgvrvgt edleadtviv aagawstell avtgvdlgvh pirgqmthfs lpgrdtrswp
      241 vvrfgerdyy vsaaapdrvv tggtvepeag fdrrvtasgl lenlstalev lpelgeatvv
      301 etrvgfrpgt hdgrlslgpi erlpgvvvat gagsqgltfg pfqglvaarl amgrdpgvdl
      361 safvpdraqs ptwgrpggtr qg
//
LOCUS       WP_357660893             338 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptidase [Micromonospora echinofusca].
ACCESSION   WP_357660893
VERSION     WP_357660893.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..338
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36977
     Region          24..337
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 matdlhaaat vvdgstviel sdahldrirr ggvtavnhtv trpyadtvta lrevnrcrrw
       61 idehsddvll altvadiera kaegkeavif gpqdtemigv dldllgtfyd lgvrilqlty
      121 qrqnllgagc geetdsglth rgrrfvqamd elgilvdvsh cgertgldam easakpvvvt
      181 hsfcdamsph iraksdgylr slaeqggvig ittlsgflyy peepsrrpdl arfvehvsrv
      241 vevagidhva iatdydetwt epmriaqlks iaqskskehq nllgdfgwte rraigmddaa
      301 dfpnfteall nggfspadvt kilggnwlrv ygqtwkpa
//
LOCUS       WP_357660963             344 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardiopsis alba].
ACCESSION   WP_357660963
VERSION     WP_357660963.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=34601
     Region          25..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 mkgfgipfgw llggaaalfv aglfgisaga asitaadvfr hllsllpfgg vetplterqe
       61 allmelrlpr vvagaivgal lataggayqg vfrnpladpf llgaaagagl gatmvmvfgq
      121 dlfgdpralv pvaafvgala gvasayllga taggggtaal vlsgvavssf lsaaqtlvqq
      181 mgvdqlqriy awllgglgrg gwddvrlilp yalvglgvll lsgylldmla lgddkavslg
      241 lnpalvrgav iaaaslataa avsvsgligf vgivvphivr rlvgsnyrai lpvtiligaa
      301 fmitvdivar tvvapaelpi gvvtaflgap ffvlilrttr hrgt
//
LOCUS       WP_357661049             525 aa            linear   BCT 28-DEC-2024
DEFINITION  GMC family oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357661049
VERSION     WP_357661049.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..525
                     /product="GMC family 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=57650
     Region          8..519
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msneetvydy vivgggtags vianrltedp gttvcviegg pddrnlehvl rlrdwlsvld
       61 geldygyttt eqpngnshil hsrarvlggc sshntlisfr pfaedldewv aagaegwdna
      121 tvqsyadrik cniipiaekd rndmvkdwvs saseaanvpv iedfnaltsh gdgfsggagf
      181 lsiaydpytg yrssasvaym hpimdvrenl tvlletwvgr ilfdgdratg vtattkdger
      241 itvkarhevi vsagaidspr llmlsgvgna eelgalgies qhdlpgvgen lqdhpesiim
      301 wettrripen tvmdsdaalf vrrhegddpr pdlmfhiyqi pfddntkrlg ydspedgyav
      361 cmtpniprsr srgrlyltsg dpeakpaldf ryftdpegyd eqtivdglki arevaetepf
      421 kswikrevap gpkvrtdeel seygrraaht vyhpagtcrm gavddeaavv dprlrvrglk
      481 glrvadasvf ptlptpnpmv mvlalgeraa dliredrrae egear
//
LOCUS       WP_357661030             355 aa            linear   BCT 28-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Nocardiopsis
            alba].
ACCESSION   WP_357661030
VERSION     WP_357661030.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 355)
  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..355
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..355
                     /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=38299
     Region          192..276
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mdreedrstp tpppepaegl pptgidptgh vpsapvgapa ptprrrgprp vppgvpyhrv
       61 laderrriwr giaalvllfg gmlafsfgft ilgslvdmal grpsvllggd eftpatqasa
      121 liglallvpw smliqrwlyg vkgaslhsvl svfrpavfgr aflmilpiwa vymtvfsmft
      181 pmpegvwrps dlvlmfgivl lltplqsage eygfrglafr vaaswgkgpr aalllgvavs
      241 gllfmlahfa ldpwlnlyyl tfgvtlalit wrtgglevav vvhavnntia flltlvtrsd
      301 lvegmdrsvg agsaimlvpc vllilitivv wartretgpa ltpserethe aprer
//
LOCUS       WP_357661070             185 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora echinofusca].
ACCESSION   WP_357661070
VERSION     WP_357661070.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 185)
  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..185
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..185
                     /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=20436
     Region          5..169
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mgppkkrdeg wftglyvaey anvvryglrr ladsdasael aqevfvvawr rrdevpdrsl
       61 pwlygvarrl lanhwrsrrg apdvlpiagv dlarvasssg adttvgvadv raalailsel
      121 dqeilrligw eeltvseaaq vlgctrataa vrlhrarrrl aeamsdrpaq srhrlvlatt
      181 treel
//
LOCUS       WP_357661076             306 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Nocardiopsis alba].
ACCESSION   WP_357661076
VERSION     WP_357661076.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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..306
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..306
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33154
     Region          103..267
                     /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 mmtttpaprp dsdrsgddrp treqalkaae qawmeheqel grealrslkp wkgkaqrqdk
       61 vlltvalllp alllltlplr plfiadhpla lalitgshaa vgaasafigv gqggalwvvi
      121 lagvigkiki dwifwwlgrr wgrgivnfli qgergrrfad rletmnpwvm ralvplsylp
      181 gvpagithvi agangmrlhv ymllnalgaa fvtsivalvg hssgqtgvdv vllidkyalw
      241 imlalifgma lyptftasrd qkarktaale kaateydaet arleaegrst estiaptapt
      301 geenpr
//
LOCUS       WP_357661128             140 aa            linear   BCT 28-DEC-2024
DEFINITION  YchJ family protein [Nocardiopsis alba].
ACCESSION   WP_357661128
VERSION     WP_357661128.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..140
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..140
                     /product="YchJ family protein"
                     /calculated_mol_wt=15509
     Region          13..136
                     /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 mvkhgsrlrq slpadspcpc grsrtyalcc grlhsgeska ataedlmrsr ysafvvgdee
       61 ylsrswhpdt rprdvgvdad tvwrgleilg stegtpfhde gtvefraryr eggrdgeihe
      121 nsrflrhgga wvyldalggr
//
LOCUS       WP_357661129             213 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora echinofusca].
ACCESSION   WP_357661129
VERSION     WP_357661129.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 213)
  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 213)
  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 213)
  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 213)
  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..213
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..213
                     /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=22551
     Region          3..213
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 msnivvfgag gtagsritae avgrghrvta avrrpeatsy lppavtvvtg datsersvre
       61 lapdtdamvv aigggehdlw ldaarnlvga lrgmpgapri ihvgggstll tpkgtrylde
      121 pdfpedyrda algqadaldf yrssadgvtw tyvsppplef hpgertghyr tggdepvadh
      181 egrsvlsyed lavaivdeie qprhenarft aay
//
LOCUS       WP_357661147            1162 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora echinofusca].
ACCESSION   WP_357661147
VERSION     WP_357661147.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1162
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..1162
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=123812
     Region          <2..889
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <865..979
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
ORIGIN      
        1 mdprydeavi grehpaallr aevdrvtash gglvlvtgep gigkttlvta aagearrrga
       61 lvlgaacwds dsapgywpwv qvlrglrrss ddwavaresa epglaallge atggtagept
      121 dgdadeatgg pagddrveqe efalhdavtt alvaasqrrp vvvvlddlhw adpasmrllr
      181 faaqhtwfer llligtyrda evespdhplr ellmplvaka ttltltglsr devaalmtrt
      241 agrapdagll devhrrtggn pffveqtari wradgrvgai ppgvreavrr rlaqlpaavv
      301 ealtaaavlg refhrqvlaa yagtpaaqad rlldravtar lvvsrgggrf afvhdlvret
      361 lydalpdder rsrhaalvra vdrapalaer lipadlarha hlagahldps raadllvaaa
      421 rdaggrlavd esvvhfrral evaedpagrv kimielgqll hhagggdear rllaeavtla
      481 vavddpvvla rvalvvhsrh adgsrrvpdp egvvreayrr ligesagavp vstlvtdlia
      541 ateslarrgh ddealtfslw arhdttwglg sardraaita eirdvarrgg daetalwata
      601 lrwvallelg dpryhdefat fvagarrgdv rhraaatmdd aiiaafrgdf aradelfgel
      661 tglgewdhsd fafmghhlrw srlhlqgrsd dalldelssa gyphpellrg itavecgdtg
      721 salrlvtgie aagtaypgav splwlrlrag vaaatrdprr caevrqalrp hrgqwmsalf
      781 gcdlsgpvdh wlalvdvaqr rwddavagfs aardsadrlg arpwsvlara aladaltgrd
      841 gpgdaaaaaa lreatardat dlgmhqvtrr ltgaeeagap paghsgallp vtgpvpdrvg
      901 gpqvavvwpp gpqaaargph epraaigpre pgvaigprep gvaigprepg vaigprvsag
      961 avvaqpsggr qapageqapg raygfrrdgp vwqlayagvv vhlpdakglr dlhvllsrpg
     1021 vdvpavelld ptagpelvaa rrmggdpvld deakaryrrh lerlddeidr aaergdrrrm
     1081 adldaergal laelraaagl agrsrrlgde aerarktvta rirdalrkld qrhpalaghl
     1141 rdtvstgstc rylppdpvpw rl
//
LOCUS       WP_357661157             445 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardiopsis alba].
ACCESSION   WP_357661157
VERSION     WP_357661157.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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
REFERENCE   3  (residues 1 to 445)
  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..445
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=48416
     Region          163..418
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnerlrewne nlgllvrrhg mwwwrrrari adwfyalftl pfsglmmlag ttsgiglfsk
       61 pfaalmvapi gapepgpaaa wtavatlfal fvipgtlasa tmlwrrsspr wlliagailm
      121 igygdpiplm vglysypaff sdrkvltgwf algvlstalv ynasvtgfvm avivfllvpv
      181 faglwigtrr elierleera erlereqhmm aeqaissert riaremhdvv ahrvslmvlh
      241 agglevsatd drtveaagli rttgrealae lrgilgvlrd eggetaptap qpvlddlerl
      301 lgewrgagme vrreesgdpr plpvqvqrta yrvvqealtn aakhatgavv dvhlyyaadr
      361 lelevsngpa pgvvnppprs gygltglser valaggevsa gpcsdggwrl railplgemd
      421 endapvpnte veeegsegdp htpgr
//
LOCUS       WP_357661163             256 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Nocardiopsis
            alba].
ACCESSION   WP_357661163
VERSION     WP_357661163.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 256)
  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..256
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..256
                     /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=27627
     Region          11..196
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtlgstplrp tvwwahissa ndrlvrllne eelarntrfr lqtdrdrhll gralartala
       61 ertgvpasev afelrcrsce dkartgadgg dpsphgkpvp vgpatgweis ishsgewvvl
      121 amaegvpvgv dvervseard ldglaaytla esearawral peedrseaff gywarkeall
      181 katglglsgg lrrvsvtpps drarlvaweg ggapgtawlt dlerdpgyrs alavltdrpv
      241 eptvhpaert aallrg
//
LOCUS       WP_357661234             466 aa            linear   BCT 28-DEC-2024
DEFINITION  LURP-one-related/scramblase family protein [Nocardiopsis alba].
ACCESSION   WP_357661234
VERSION     WP_357661234.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 466)
  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..466
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..466
                     /product="LURP-one-related/scramblase family protein"
                     /calculated_mol_wt=50522
     Region          9..192
                     /region_name="YxjI"
                     /note="Putative phospholipid scramblase YxjI, Tubby2
                     superfamily [Lipid transport and metabolism]; COG4894"
                     /db_xref="CDD:443922"
ORIGIN      
        1 mhaplftapv llieqprhly ateghyevld esgrplayvn ehmnarshrr gphrphrftv
       61 ydtgghpllt ldkpwdrgrp hiqvtgphge pyggivqdra fagsrfrlcd prghtvaeir
      121 gdwkgwdftl ldragieiar vgkehpgllg gffttedrya lefaydlpwp lrrlvlaaal
      181 tidvllhere pefyhshyad frrypeygyr prhhwhhprr gymiarrrrp pllvhhtfrp
      241 vrrrgyvpvr eravesrggy rtfssrseap srsagagraa tprvdrrggg gfasrseaap
      301 rrssgfasrs eaaaprrdrt sgasrsespa sgaaarrerq rrsgaarqsa sgkrvgagrq
      361 gtaaksagsp rgggssnrvg glfgggssgs rsssgssars sssrggasrs sfskaaskrs
      421 ggfssrssgg rssggasrss rssgrssggg rssggrssgg ssrrnr
//
LOCUS       WP_357661268             240 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardiopsis alba].
ACCESSION   WP_357661268
VERSION     WP_357661268.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=24962
     Region          1..92
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 metervapgl akiaalladp tragfclall dgrawtagel arhvgvaast ttghlnalva
       61 ggllvqerqg rhryvrlasp eiaelverla algpeaapps pslrarsrgr hlalartcyd
      121 hlagrlgvli teamiergll segrglaltp ageewsaelg latapgarrp avracldwte
      181 rrfhlagala aafcshafss gwivrtgvpr avmvtpegse afgtlfglps dalsapegta
//
LOCUS       WP_357661286             435 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Micromonospora echinofusca].
ACCESSION   WP_357661286
VERSION     WP_357661286.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 435)
  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 435)
  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 435)
  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..435
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..435
                     /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=47421
     Region          44..428
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(82,89,117..118,125,129,136,262..263,266,270..271,
                     274,307,312..313,316..317,319,342,369..371,374..375,
                     377..379,383)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(89,111,113,116,118..119,202..203,211,261..262,
                     265..266,270,313,316..318,418)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mapreavasg hvtvagpaag cpvtggtata pvfdptaarh rpdphpllhr mraqapvyrh
       61 qaprsgrafw yvtryadvqr allhpqlgrq ldrlppnlat vhrqatgdpl vmlrrnvlhl
      121 dppdhtrlrr llapafgart matidrhvrr vvaeltdama pargpvdvie alalplpvlv
      181 vaevlgfplh drdrlrhwsd eiarsrdprr ahragvefts yltkviaerg eatgddllse
      241 lirahrdggw lsraellggv fqlllagdet svnlignavl ellrhpdqla rlraapdlid
      301 saieevirfn gpvghtgqly aladveiggt viprgdvvvp vllaanrdpa vfadpdvfdi
      361 grhpnrhlgf gygihfclga alarmqaraa vgtlvrrfpa lrlavdpadl rwtpelflhg
      421 vrqlpvllqp tsgev
//
LOCUS       WP_357661337             703 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Micromonospora echinofusca].
ACCESSION   WP_357661337
VERSION     WP_357661337.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..703
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..703
                     /product="PhoX family protein"
                     /calculated_mol_wt=74849
     Region          47..697
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msdrprllpl lgatrhgsrd amtclyrcgn acdhpvpnts dnayfgdvvn aevsrrglvr
       61 ggavgalvlg fggavagaap aaatpaapvv peaagfarpa ggvgngaltf kpvppntlds
      121 lvvpngydha vvmrwgdpvv pgapefdlha qtaaaqarqf gynndfvgvl pldgrrrall
      181 vvnheytned lmfpgftgqd alsveqlria maahgmsvve lervdgtgqw rpvtkgrrpy
      241 nrrvtalatk feltgpaags ahlrtaadpk grtvvgtlnn caggvtpwgt vlsgeenfnq
      301 yfvggdavae evkpklaryg vttttrypsg srkwerader fdlakhpnea nrhgwiveid
      361 pydpesrprk htalgrfkhe ganvivarsg hvvaymgdde rfdylykfvs dkkfmkgnsw
      421 varrhnltll esgtlyvakl detsageidg sgrlpsdgaf ngrgrwirlv sgnrsyvdgm
      481 taadvltftr lagdkvgatk mdrpedveps lltgkvyval tnntdrgkag kpaadeanpr
      541 nlnkhgqvle lvedrgdnag etfawslpiv agdpadpstf fagydktkvs piscpdnvaf
      601 datgnlwist dgnalgsndg lfatavegpe rghlkqfltv pvgaetcgpf itgdnrsvfv
      661 avqhpgelig asvenpasnw pdgdfakpgv vvawrldggp igs
//
LOCUS       WP_357661387             253 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Nocardiopsis alba].
ACCESSION   WP_357661387
VERSION     WP_357661387.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     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=27872
     Region          <17..142
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 msshalppyh rdlsfhgpls deraarlvrs lgllddrhvv dlgcgwaell lralatspsa
       61 tgfgidlhee dirqgraaar ergldervel vvgdvaawkg gpadvvfnig ashvwggepv
      121 thtenaltal adlvrpggra lfgecfwrrt pteeeyaame gtrgtrgqyr plpdlvdlal
      181 dhgfrlgsls eagvdewdvm engialaree wllnspdapd feevreradr mrrfrthgar
      241 dtlgfayltl irv
//
LOCUS       WP_357661322             299 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Nocardiopsis alba].
ACCESSION   WP_357661322
VERSION     WP_357661322.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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..299
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..299
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33838
     Region          22..163
                     /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 mlvdedpeka yqhaayarrk asrlstvrea sgiaaytvgk wqealadlra arrmsgrdnf
       61 lavmadcerg lgrperalei asdpaagnld tadrielriv aagarrdmgd tkaalaelqv
      121 pelkerrarp yvarlfyaya dvleelgrtd dareyfaras svdregvtda derlavlegv
      181 elvdidvedg ivwtdveedg gseefveapr drrndsedrg dqgeerresd drrdereddg
      241 grddseerpe pekrpdseer sesedrsede trddrpeeev reapsedegr eddrdrdrd
//
LOCUS       WP_357661411             335 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardiopsis alba].
ACCESSION   WP_357661411
VERSION     WP_357661411.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 335)
  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..335
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..335
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36727
     Region          16..70
                     /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          103..279
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 middrgpvvh qallihrlve lrrgngltqe kvarslewsh aklmryeggt qvlpkadlda
       61 lldlygvlgs gqgrklqeig rrardkpwwy phrhalsvee ryyvglemga arirqcapal
      121 vpgllrtrdy ahalcamvdp ggevdrlvdv lmgrqgvmlt rspvpeqvyv ldeavlrrvv
      181 ggrekpgvmv rqlhhlvers asvqlrivpe eaglhfgvlg gftlfdfddg lppvlhtehr
      241 grvvaskkee dvhsyaeafe glveehalda rrslaliehh srrlqsrgga spdtggegae
      301 spgngvgeap agagadqepv pprhlqitnd rtspp
//
LOCUS       WP_357661466             218 aa            linear   BCT 28-DEC-2024
DEFINITION  O-methyltransferase [Nocardiopsis alba].
ACCESSION   WP_357661466
VERSION     WP_357661466.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 218)
  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 218)
  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..218
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..218
                     /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=23910
     Region          39..214
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mtdallgylr gisppedpvl gelrelteal pggrlmllmp gqgdflamlv rltgarrile
       61 igtytgystl cmaralpeeg rivtcdinrk wtdigaefwe ragvsdrvev rigdaaetva
      121 elraeqdepf dlvfvdadka gypgyfentl pivrtgglmv fdnvlffgrv adpehrdddt
      181 agirtlndll radhrvevsv lpmadgmtla rkrpeags
//
LOCUS       WP_357661503             987 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardiopsis alba].
ACCESSION   WP_357661503
VERSION     WP_357661503.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 987)
  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 987)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 987)
  AUTHORS   Rosinski,J.A. 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 987)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..987
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..987
                     /product="helix-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=107456
     Region          <10..946
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          918..986
                     /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 mgamplisdi spvfvgrrdq lrlladqaer arsggsetll vggeagvgks rlvsefvetr
       61 trgavfvgac lqlgedglsy apftavlrqv lrdlgrevfe taapggigef arllpelgea
      121 prdrrenrgi lfeqllrlfg glggeegvti vledlhwadg atrdllvflv rnldrpgvqi
      181 igtyrsddlh rshplrrllp alerlpgvgr ihlepltree vaaqarairg ddltpsqids
      241 lyrrsegvpl yvealasaet cpteedpdlp dhfrdlllep lhrfdetaws vlhavaagai
      301 gggvehetly havglperel eaalrvlvda nvlragrtdy rfrhallrda vhgeilpgph
      361 arlhlrfaql ideypdtvps erraaeqahh yqaahdlpra lqaawwaavr agealafdee
      421 lamvervldl wdrvpdarer vqnrsraqvv draagaalds grpkralell dtalaelpee
      481 peddetrmlr avllrergqa lsqgvrdggl pdlvralemh pphmpgyarl laalakesrl
      541 aradreetpd qrlltrllra glgpralaer aidvatreet adprgevdal ivlggllmee
      601 gdieggrplm ergtlravel tdpilearga gnlghhlrel grheegmevl rsslarhdrl
      661 gwasvhrafn hqnvaeilfe mgrlgearel sdhtvtaate rvrvhcvltv qaraaaaqgd
      721 leaarratgs kgdrsmlnah rmnvlqlhal aavdtslaeg dpeealglsr tlldrtaler
      781 fpgytwplle amaeaarqgd dpkvaervls vaertdvvgs impaysasia alvaetvgdd
      841 agplwkrave aweplpmply lararlreae vgaardrdla vcrvrqvyat avecgaspla
      901 asaeglarrl gvgvsdeapt prtpagltar etevlrllae gatnariaea lfispktasv
      961 hvsnilakld vpnratagah arrlgva
//
LOCUS       WP_357661527             440 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora echinofusca].
ACCESSION   WP_357661527
VERSION     WP_357661527.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..440
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..440
                     /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=47715
     Region          1..>181
                     /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 matgsavvig asmgglltar alteayervt lvdrdllper adsrrgvpqg rqlhvlltrg
       61 rqafeellpg isaelaargv ptvdlheqvh wynnghrmrr apsplfalgv srplleqvvr
      121 ervaalpgvr ivsdcevagl tttvdrrrvt gvrlhprdge pttvaadlvv daggrgtrsp
      181 vwlaelgyrp apeervkvgv tyltrtyrre phhlegllga ltnavpgqpr ggivavqeqg
      241 rfavalsgml geeppaddeg mtafaetlaa pqiaellrta qpegppatmk fpasvrrrye
      301 rlrrfpagyl vvadavcsfn pvygqgmtva alealllrrl lrrspdrlar rffrgaarli
      361 dgpwsiavgt dlrfpevpgr rsprvrlvna yvgrlhaaat rdpalgaafl rvvnlvdppt
      421 rllsppvllr vlrgapapar
//
LOCUS       WP_357661565             534 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Micromonospora echinofusca].
ACCESSION   WP_357661565
VERSION     WP_357661565.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     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=56110
     Region          10..499
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msspgaesad avvvgaghng lvaanllada gwdvlvleat atpggavrsa evtapgylsd
       61 lyssfyplgy aspvlrglgl dryglrwrhs pdvlahllpd graavlnrdp eataasleaf
      121 apgdgkrwlh ayddwrqvae pmletitrpf ppvrgglgll rrlrvsgalr larrlvvpvr
      181 klgdelfege ggpallagca lhtdlspeea gsgvygwlla mlgqqvgwpv pdggaqkitd
      241 alvarlterg grilygahvd rvltargram gvrtvggtlw rarravladv papalyldlv
      301 gaaalpprlv edlahfrwdg stlkvdwals apvpwtnrav atagtvhlga dldgltsyaa
      361 alarkeiprd pflllgqmsv adpshsppgt eslwsythlp frrqwraedi aahvermeqv
      421 leeaapgfrs lvigrhvagp adleagdpsl vggalgggta aayqqlflrp ipnlgradtp
      481 vdrlflasas ahpgggvhga pganaaraal ardraltgpl yaagidaahr avyr
//
LOCUS       WP_357661598             684 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Nocardiopsis alba].
ACCESSION   WP_357661598
VERSION     WP_357661598.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 684)
  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 684)
  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 684)
  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 684)
  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..684
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..684
                     /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=73683
     Region          13..675
                     /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 mkdpigtrdi gprvgtplwl ymagttfaga llfgastfel gldqlfllgq epliwvllcm
       61 ivlgeltpia mpgqapgngv ptslpftfal vifyglpvaa llqcvattvs gvvrrhaphr
      121 tafnaaqyvl tlgvadavlr lvlpeivivp avpagaelia ialagaasfv vnrtlvlcav
      181 amhervplrq vmfkglrqqi yvnavlisls pliviamths vlyvplfafp lgalyacvll
      241 lvkrdhqanh deltglanrk lltvrahrei lrarqqgsrv glllldldrf kevndtlghp
      301 tgdrllvtla rrlthsvrpn dlvarlggde faillpqvrd ndsarevalr lrgalaepvr
      361 ldgmdfdlqv stgialypdd apdfpllmqr advamyvaks grtgvesydp gkdrnstarl
      421 smyselrrgl adgalemryq pkvaladgrp iglealarwr hpvrglltpd efmpviehsn
      481 lfraftvqvl ditlarlslw reegltlpvs vnlgvrelld pdlpdtvaaa lrehgvpadr
      541 lileisertl iadaetdaaa eaaarlralg vgltlddfgt ghftlaqlag lpldevkihd
      601 sltarlsdea sggrtvvraa ialvrelgmr ataegvrnae maraaaesgc haaqghhfse
      661 plaprdvppw laahgtgapa hpra
//
LOCUS       WP_357661700             336 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora echinofusca].
ACCESSION   WP_357661700
VERSION     WP_357661700.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     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=37257
     Region          17..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtvqldarpp vapaprtgrr ppamrfsrld tkyspylfia pffvlfgvfg aypliytfwv
       61 slhdwdllgs dhpfvgleny srlladadfw havvntlgif vistipqlla alwlanllnr
      121 qlrarttfrm avlipnitst aavaivfgvl fgrefgmvnw lldlvgidai awksnrfasw
      181 vaistmvdwr wtgynalifl aamqaiprdl yesaaidgag rarqfwsitv pllkptiift
      241 viistigglq lfteprlfhs gtnpirggtl resqtvtmym fenafaphyn fgygsavawl
      301 lfaliavvaa invlllrrlg gakppkgdak skegar
//
LOCUS       WP_357661701             307 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardiopsis alba].
ACCESSION   WP_357661701
VERSION     WP_357661701.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (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   2  (residues 1 to 307)
  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 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
REFERENCE   4  (residues 1 to 307)
  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..307
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..307
                     /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=33430
     Region          34..278
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          195..278
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdplstllrd tradcavfdr sflrgpwsvp vkgeeerfgl villggdgtl tpeggdplhl
       61 gardvaviap gtdfvvsgrg vdleaegagr vtlltvtyhl hrhrlerlae ilpptlvvpd
      121 eagscpllev ivdefvherp ardilltrsl dllllavvre wferdevnap swlrasndpv
      181 vgralralhe epgrrwtvad laarggvsra sfarrfnelv gespiaylta wrmtlasell
      241 lepgatvdsv srrvgyadpy gfseafrrhl glrpgahrdl ltaggkgrga grvgdrplge
      301 dfedqts
//
LOCUS       WP_357661709             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora echinofusca].
ACCESSION   WP_357661709
VERSION     WP_357661709.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   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 265)
  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..265
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..265
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27575
     Region          4..264
                     /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 mtkievngal layddtgsgt pvvllhagia drrmwreqvg plaarhrvia ldlrgygdse
       61 lpptpfahhd dvaglldald lpraalvgcs fggavaidta lahpervsal allgtaasgh
      121 ewseeandlw eslvgevdpe dfaasaagev rfwvvgpgre padvdpalla fahemdqral
      181 aaelalsavd vaeldppaig rlgelrmpvl vgagaadvpd isrladriaa eapnavrlpd
      241 vpdaghllpl erpapvnaal ldflp
//
LOCUS       WP_357661744             526 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Nocardiopsis alba].
ACCESSION   WP_357661744
VERSION     WP_357661744.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..526
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=58946
     Region          82..516
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 madaddfplt gnafrsdwfe rqqeaaarhr lipqrdweal akdikggael hlpgtawyda
       61 nyrpqnhfys ylrpagivri ldqakihdlt dpqglvntav grvvrwardh kmriavrsgg
      121 hsyagfsatt gllidfggqq tvyepttdnk itfgtgmqgr wlypalrdry pnayiptgrc
      181 ptvaigglal gggagfldrk wgltcdqmlq stmvtadgkv lvcdaqhekd lfwairgagq
      241 gnfgihtsfq fqgqplptag nggiatffki twniedafpl idlvqnivee kdeefdkieg
      301 rlgistyglk keeieknlnt niigiyhggk defedlfepl ikgpvspvev eivegplaef
      361 lsesyafqti psvkytsksg vvdrpfspda aqkiidwvkr wpgsahpteg ggvalftlgg
      421 ainrkapdet affhrrgiff fnidasfaee dprqgavlnw aqdfyldmre hryisehcyq
      481 sfpdrsladw eyayygtnyp rlqrikahyd penffryaqs irpatg
//
LOCUS       WP_357661760             193 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nocardiopsis alba].
ACCESSION   WP_357661760
VERSION     WP_357661760.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 193)
  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..193
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..193
                     /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=21194
     Region          12..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msggvssrpr lradaqrnaa qirraaidaf qgrgltvple evakaagvsk atifnrfggr
       61 iglidavieq vvavelraiv drtrsiddag erlayyvtai rdlqyrqpaa ndtmlqvype
      121 arslmeicri ageineelis asrasgalrp eftvddlhal vhdnalalkh gplprredyd
      181 rrtvflldgm rar
//
LOCUS       WP_357661979             481 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora echinofusca].
ACCESSION   WP_357661979
VERSION     WP_357661979.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 481)
  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 481)
  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..481
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..481
                     /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=50182
     Region          <175..475
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 maglslrtrl vlilvallal vsvaiggitt valrhflidr vdeqlapmra apgwggpapv
       61 ewprggtggp dariprglpp gtlaaevvdg rvvrawilag reeqavpakd laeladlptd
      121 grprtrelgg rgdyrvvarq lpggtvrvlg lplsgvsetv wwlvvaqagv atagllvagg
      181 agalivratl rplrrvaata grvselpldr gevalsvrvp aadtdprtev gqvgaalnrm
      241 lghvgavlaa rqasetrvrq fvadashelr tplaairgya evarrgrdev ppdvahalrr
      301 vesesarmts lvddllllar ldsgrplave pvdlsalsvd avgdahvagp ehrwrldlpd
      361 vvvrvpgdpa rlhqvlanll anarvhtppg ttvtttlrva gdaavldvad dgpgvppalr
      421 aevferfsrg dssrsrahgs tglglaivaa vveahhgsve ldsrpgrtvf tvrlpgvttd
      481 a
//
LOCUS       WP_357662023             304 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nocardiopsis alba].
ACCESSION   WP_357662023
VERSION     WP_357662023.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..304
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32897
     Region          14..293
                     /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 mlddsaayvd gpwshrtvsa agarfhvaet gegplvlllh gfpqfwwawr sqlvalaeag
       61 yravavdlrg ygasdktprg ydlvgsaqdm agliralgaa daivvghgvg glvgwtmasy
      121 hpesvralav lsaphprraa rvllsggpgv shmlraqipi lpehrlltdg cvrvgellda
      181 wsgpgwphae teeryrlafa ipkvshcsle yhrwifrsrw rtdglryalr mrtplripvl
      241 qlhgsldpvc ppkvarasgg lvrgpylwkp vegtghflhe espnevneal vgwtseigta
      301 vgdg
//
LOCUS       WP_357662061             417 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent RNA methyltransferase [Micromonospora
            echinofusca].
ACCESSION   WP_357662061
VERSION     WP_357662061.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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..417
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..417
                     /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=43732
     Region          14..410
                     /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 mspqedgrgl eeaervevtv gavapgghcv arvhgqvvfv rhalpgervv aevtevhkgf
       61 vradavsvle aspdrveqpc pyakpgrcgg cdlqhvapaa qldwkvavvr eqltrlgglt
      121 daeldalgvr vealpggplg wrsrvryavd gagragllkh rshevvpidr cliahpaire
      181 lpvlaptgar wpdadtvetv astggdvavt avadgvphpv sgpervreva agrewtlpvs
      241 sfwqvhpaaa dtlvdavlel vdprpgeraw dlyggaglfa aalagrvget grvtlvesaa
      301 qgvaaarenl rdlagvevvp arvetalarr ritgpvdvvv ldpprsgaga rvvrdvvaag
      361 pravayvacd paafardvrt faqqgwrlaa lrgfdlfpmt qhvelvgllv ppdgaar
//
LOCUS       WP_357662134             412 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Nocardiopsis alba].
ACCESSION   WP_357662134
VERSION     WP_357662134.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..412
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..412
                     /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=42872
     Region          12..>72
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          55..391
                     /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(68,70,233,253,322)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mtgsrtlyrd ltlidgtgaa pvedaavlve dgeiayagpa adapataped tveslggrtl
       61 lpgfidthvh fgfadgrala tnnaeisrsl hafesaerms vtldagvtga rdlggadagf
      121 rvaqerglir gprlsmalrl mshtgghadf tlpsgfnahd cehtaaeiad spqearvstr
      181 rlirdgadvi kvcatgglss psdgptdegi geeeiaaiva etakhggrpv aahaqgavgi
      241 rnavrggvas iehgylidde gidlmlergt flvptlttfd fedrihlmsr ksietkralt
      301 detyervsha vargvrvamg tdagisehgr nlrelaqlvr vgltptqaiv agtrnaaelv
      361 gvadragtve agkvadlvvc dgdpladisl lgdrdnvvlv vqggkvvkdt ra
//
LOCUS       WP_357662251             363 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardiopsis alba].
ACCESSION   WP_357662251
VERSION     WP_357662251.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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
REFERENCE   3  (residues 1 to 363)
  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 363)
  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..363
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..363
                     /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=37244
     Region          21..361
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mnetltsvrp dtaapfrprd tlawrspkgr lsflmrprtl vvclalvavt fvtlvvsvsv
       61 gdyeiplpvv pgaligqger ldvffvqgvr lpraltaigv gaalgiagav fqslsrnalg
      121 spdiigftsg aatgavfail vvgasrvvvs lgaiagglvt aavvyllamr ngvqgyrlvl
      181 vgigvsamla svrdymmtra dltdalgaqi wmigslnnrg wgeaaavwig vallapvlla
      241 lgrrmrfmel gedtarglgv ptrstqvial avasaltgaa iavagpigfv alaapqlarr
      301 ltrtggttlv gsalmgatll vvadlvalra laptqlpvgv vtavigggyl iwllytewrg
      361 gra
//
LOCUS       WP_357662252             354 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            echinofusca].
ACCESSION   WP_357662252
VERSION     WP_357662252.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 354)
  AUTHORS   Rosinski,J.A. 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 354)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..354
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..354
                     /product="helix-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=38121
     Region          15..306
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrpaarggs rasadrlarl lnlvpyllar pgielaeaag dlgvterqlr edlellwvcg
       61 lpgygpgdli dmafdgdrvt itydagidrp lrltpdeala lvvalrmlae tpgvtnreav
      121 eralakieha agdlvaapie vrlpadtrrv eelrsavesg ralrityyta ardettervv
      181 dplrmlmvgg rayveawcrr aeavrlfrad ridavtelde ravvppqarp hdltegvfrp
      241 spdlplitlr igrgerwlte yypcerveag dgdhwlvslr vtdlgwarrf vlglgpdvav
      301 vapvelaeqv raaavaalda yaspapaapr gpagvaatar avspadpavt vgtq
//
LOCUS       WP_357662262             217 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Nocardiopsis alba].
ACCESSION   WP_357662262
VERSION     WP_357662262.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 217)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..217
                     /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=22347
     Region          15..192
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mavhetgaar sygmiselya dfaagafead plgrsmidvl aksvaasggg pvldagcgpg
       61 hvtaylrgsg veafgvdlse glvelartrh ggirfevgdi galeaeggsl agvvsnysii
      121 hspperlavi maefarvlap egylmvafqs hedpgagvet fdhqvamayr ygvdhvlaea
      181 aavglveqar lvmapgldar rgfsqahlll rkagadl
//
LOCUS       WP_357662314             724 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora echinofusca].
ACCESSION   WP_357662314
VERSION     WP_357662314.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 724)
  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 724)
  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 724)
  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 724)
  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..724
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..724
                     /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=78818
     Region          38..720
                     /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 maavpepggd dlsrsgaqry aaewaravrr lgfvplsaae terllhlhtv rlaqallaep
       61 fsalpaeevg ralveehlte prvldwsvra lgdrfaarvl sgrahrdeta ervaalqggl
      121 aagfaralrd rtfaqqeria rsawqarddv eqalrdsear fravfvgaat gigiagvdgl
      181 iidvnqafad mlgysieelr qtdvaalfhp ddaagmwely qeliegkqdr arvekryyrk
      241 dgsvvwtdls vslirhddgr prftvamied iteryelqqr lrfqalhdpl tglpnrtlff
      301 etlgrvfdva dasrrvgvcf ldldgfkavn dslghdlgdr llvviarrla dcvagrghlv
      361 armggdefvi lvddgagidd avrvaevala avsapvrige hqlavsasig ivecpvggts
      421 aselmkaadt tlywakaegr grwavydper gardiarsal aaglpaaldr gefvvhyqpi
      481 vsllegsmla vealvrwqhp elgligpdrf iglaeetgli vrlgewvlrq acrdaeawrr
      541 efpraqlvvs vnlaarqadd pgivdtvada ltstglpadl lqleltesav mgtageplrs
      601 lhrlatlgvr maiddfgtgy snlaylrrlp ihclklagpf vegirgedad atadhrderi
      661 vdalvrlaha lelwvtaeav etgvqaerlr alrcdtgqgr ffgppapase iterlraedr
      721 gata
//
LOCUS       WP_357662321             416 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Micromonospora echinofusca].
ACCESSION   WP_357662321
VERSION     WP_357662321.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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 416)
  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 416)
  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..416
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..416
                     /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=44651
     Region          1..409
                     /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 mayllgvvlf alailvsvsl heaghmltak afgmkvtryf vgfgptlwsf krgeteygvk
       61 giplggfcki vgmtpqdddv dpadepramw rfpvwkrtiv msagsithfa lavialwiia
      121 isaglpnpqf psteaeirke pavialskcv vpentlrect tadpaspaaq aqlrdgdrit
      181 aingtpiddy gqllttlral kpgdtaqiay vrdgqpatts tvlaqtqrpp lddpkgqvap
      241 vaalgvglvp stptritygp vgavgatadf tgdmavntye amkripqkvp alwaaitgee
      301 rdidtpisvv gasrlggeav endawllffm lfvslnffig vfnllpllpl dgghiaiawf
      361 erarswlyar igradpgrvd ylklmpltya viliggvftl ltitadvvnp itlfsr
//
LOCUS       WP_357662391             339 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardiopsis alba].
ACCESSION   WP_357662391
VERSION     WP_357662391.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
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   Wintjens,R. and Rooman,M.
  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 339)
  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..339
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..339
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37755
     Region          16..70
                     /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          103..279
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 middrgpvvh qallihrlia lrrsngltqe kvarslewsh aklmryeggt qvlpkadlda
       61 lldlygvlgs gqgrklqeig rkardkpwwy phrhalsvee ryyvglemga arirqcaptl
      121 vpgllrtrdy ahalcsmtdp ngevdrlvdv lmgrqgvmlt rspvpeqvyv ldeavlrrvv
      181 ggrekpgvmv rqlhhlvers asvqlrivpe eaglhfgvlg gftlfdfdeg lppvlhtehq
      241 grvvaskkee dvhtyaeafd rlieehaldt rrsraliehh arrlqdrtrt spdtgeeetg
      301 trakgvgsfp tedllavsep rppppplfsa gfgvevgse
//
LOCUS       WP_357662419             338 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora echinofusca].
ACCESSION   WP_357662419
VERSION     WP_357662419.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 338)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..338
                     /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=37475
     Region          34..319
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mstpradpat prpgrdpgat asrrdrphep gpwrtrlhrf dvryvpylli apffllfaaf
       61 glfpivfngv valrhwrldd ptltgwagle nfrrlftddd ffnalsntfg ifllstvpql
      121 llalivasll nrklraqtwi rvgvllpyit pvtastlifs vvfardtgia nwalsllgig
      181 gtepidwrsa kwsswvaiat mvnwkwigyn allylaamqs iprdvyeaaa vdgagpwrql
      241 writvpmirp vviftvvlst igglqlftep mlfdanpalg lggddgqwqt vaqliykvgw
      301 rdlnlgyaaa mswalflvil lvaalnallt nrlgggnr
//
LOCUS       WP_357662420             219 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardiopsis alba].
ACCESSION   WP_357662420
VERSION     WP_357662420.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 219)
  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 219)
  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 219)
  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 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   5  (residues 1 to 219)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..219
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..219
                     /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=25079
     Region          21..103
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msetpedpne agrrpleveg ealrglahpl rarildelhm rgpatatllg erlgessgst
       61 syhlrqlfry gfiendpers ggrerwwrfr pagwrmrgge llrgpstrea tegilaryyg
      121 grrerldrwh rlvderpddp gvrrwrraae dsvahvrmtp eeteefgrdl qdfirerlrp
      181 fqgrtaedrp gaepvelqtd lfpnltgtda dpedgpsar
//
LOCUS       WP_357662429             390 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora echinofusca].
ACCESSION   WP_357662429
VERSION     WP_357662429.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 390)
  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..390
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     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]"
                     /calculated_mol_wt=40694
     Region          152..378
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlspqrcalv rlwrvglwlc gtvlvvvgtt kvrpddgera vdalahlava gacaavavsw
       61 rwpvqaagav tvtlllyngr hypdgpvlla glvvlyglgs vrsrrlaygf aagtavvvva
      121 agalvdggpg vvdlafvgwa aaavfaadav rgvrerrlaq eertrlrtqa rqrdeerlla
      181 eerlriardl hdtvahamat invqagmagq vidsrpdlar ealevvrgvs gavldelnam
      241 vrvlragder splcpvpglt dlaalarste lagtpvelrv tvppgrvarp valaayrivq
      301 esmtnvtrha vgararvtvt yddadglrva vmddgggagr pggrvgligm reraastggc
      361 lvvgprpdgg favtahwpaa aaravegadr
//
LOCUS       WP_357662432            1099 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nocardiopsis alba].
ACCESSION   WP_357662432
VERSION     WP_357662432.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 1099)
  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 1099)
  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 1099)
  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 1099)
  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..1099
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..1099
                     /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=120390
     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          131..1079
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrfsilgplq vhdaagapvg vggarlrall vslllhpgrt vgverltdti wgwdetpaaa
       61 gnalqalvsr lrralgeear ihgdgsgyrl eiapeqvdlh vfeasagsgr ahltsgrpae
      121 aeaalveals lwrgpalsdl targraedva lrlaeihrta eedllearld lgrytealpe
      181 aeavagrdph rerpiellmr alagggrvae aldayeafra rlaeelgldp sprlrrvhln
      241 llrgetapap entiernvrp saapsvrlpr pltdfvpren evgatverls gsrtvtligp
      301 ggagktrlaa esaetlaern pglvsggvrw velapvgqgt dlhqvvadtl elreyavira
      361 ntgaahldpa ervashlgdr pfllvldnce hliaeaaalt esllarcpgl rvlatsrepl
      421 gvpgevllpv ppldlppegd dlerartrsa vrlfteraea vrpgfrvsqd nlahvvritr
      481 eldgmplale laaarlrmmt pgqlaerltd rfrlltngsr salprhrtlr avvdwswell
      541 deaerrllrr lavfpggagl eavervgsdp geeaeggvlg rdvwsvlfal vdkslvvaen
      601 pvrddappty rqsetvraya lerlaesgee ervreahary vvdlwrradp elrgpeqasw
      661 larlgtaidd chaafrwave rrdaelaldl veytqwywal dggrsrnhrw aeatlelvge
      721 evprgretay amclfsldeg vergregila llteverllr ageretgrhp slalclvyga
      781 itdgrvdgpw rvrleeeleg addpwtrall ylmtamldat fgeigrsrer aglalegmra
      841 lgdawgqcna laqlvdvcfh tdpercgdll segiglaers glrgivalfr ilraqtlvel
      901 griasaeedl etvtgtplek ehlvtfrmtr vmwlqaagrq eearrlvdet epvvvglggl
      961 apiyiepawr gltadvalsd gdvarawkea grawwlagrg lstykseile ifarivvdsd
     1021 peravlllgh aatlrgglps rrprtlrlge rlvevlgear farlwsegvd tptpeasarv
     1081 gewlerivpd dvemdtwar
//
LOCUS       WP_357662453            1126 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora echinofusca].
ACCESSION   WP_357662453
VERSION     WP_357662453.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1126)
  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 1126)
  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 1126)
  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 1126)
  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..1126
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..1126
                     /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=122270
     Region          25..1101
                     /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 mtepsnarre lmrrllagds tgeqpirrrp agtqplplsf gqqrlwildq ldadaaayna
       61 svvfqvagdl dadlldravr tvvarheilr tvfrrqdgqp vqvvrpdmpv pirhddlrav
      121 aepgrseaar klaadeaavp fdlergpllr lrlirldaad wrlcltmhhi icdgwsldvl
      181 vdelsaafsa laagdaprlp elpvqyadya iwqreqlrgp gldrllahwr grlagaptvl
      241 qlptdrprpa vqsfrgatvp lvlppdvvrq iqavckqrqv tpfmlllagf kallarysgs
      301 advvvgtpvg hrrhtalepl vgffvntlvl rtavaggssf adlldgvrat aldafehqdl
      361 pferlveels perdlsvnpl iqvlfvlqna pagarrlgaa sltatdpdtt takfdltlsl
      421 eslgdeivgr ieystdlfdr ssaqriadsy vtlvaaavae pdrpvdrlpl ltadqehrll
      481 rghndtvaef padtclaqlv eaqvartpel tavscgagsl tyrqlnaran qlarlllrhg
      541 arpdrlvgif ldkslhaava ilatlkagag yvpldptypa ervghmltds aatvvvtrsa
      601 llpalaeitt evrtldmdtl ddaldalpdg dlppaarpdd layviytsgs tgrpkgvmmq
      661 hralvnllaw ygrvlrprar ilqfsslsfd asfadlfftw ysggqvvmig drddlspagv
      721 lralaeegie ravlpaamfh plaeeyarrr palprlrelv snaeqleltp mvremfaalp
      781 gcvlhnhygp sethvatght mlpgeawpsh vpigrpisns tlyivdrhlr pvpqgvvgev
      841 ylggtavgrg ylhrpdltaq rylpdpyatq pggrwyrtgd larylpdgvv eflgradqqa
      901 kirgfrvelg eveaalveap gvrqavtavh efapgdrrlv ayltgvsedg psvgevrrsv
      961 rqilpeymvp ssyvvlpefp ltpsgkvdrq slpapersrp dlgsvpvapr taterllagf
     1021 waevldldap qigvhdgffd lgghsllatr lismindayg telglkrvfq hptpagfaal
     1081 ladqlgedva dlvsatvlev asmsaegver gltaatggev egeklp
//
LOCUS       WP_357662456             925 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora echinofusca].
ACCESSION   WP_357662456
VERSION     WP_357662456.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 925)
  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 925)
  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 925)
  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 925)
  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..925
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..925
                     /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=96822
     Region          4..>893
                     /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 mryptdttrl ldepqrgrwl raeaatragg gvstvglavr ihghldaavl reaahrtvaa
       61 ypvlntaygl tggepadlgp vahslafeer dlgvrpaalp talararrdl lapidpavgp
      121 nlrlglsrla ahdhvltlaa hrvvadrrsl svllgrlgqt hrallsgapv pappdggayd
      181 aawsadgrae erlwfwrarl agvpertslp adrpgpvdaa rgahrlsvpa aaltslrrss
      241 qgagpgtell alfavllary agttqvtmgi pvdlrtdlgq eavgpfedta ilcldvpaaa
      301 alpevlrltr aalddverhg rvpydwllpr lrpdlpietd pyvqvrhtpa rpdplpavag
      361 wrielldags tptegelnlv agqegrgvae lvypaarfap stvarmarhl gnlatsaaah
      421 pdrpvtrldm lsadertlil sgwargrppa tgaariatgt pgaprpclhe lverhaertp
      481 davavvdagr swtyaelnaa anrtahrlma lgvgaerpvg lclergaeli gaalatlkag
      541 gafvpldpth ptqrlrhild etavaavitd rrsaervraa tsavmllvdd dppaavpgev
      601 ppgnpagrat peslayvlyt sgstgrpkgv lvshgalvgr cgwehdldgp tdrlvmlqss
      661 hvtfdaalwe ifapltgggt vvtvqhgrea daahvndllr rhgvtvagft ptllaallsd
      721 gafagvslrr lvsggevltg dlaarvlsgv dadefhnlyg ptetcvdatg hrvtapvrrg
      781 tgvpigrpvp garayvldrh lqpspagvpg elfvggagla rgylgapast aerfvpdpya
      841 gtpgarmyrt gdrarfraed galeylgrld eqikirgirv elgeieaalv ghpavtaaav
      901 vvtgrstaga ppsapnptap ngapr
//
LOCUS       WP_357662470             391 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Micromonospora
            echinofusca].
ACCESSION   WP_357662470
VERSION     WP_357662470.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 391)
  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 391)
  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 391)
  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..391
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..391
                     /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=40521
     Region          3..387
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mtgtgtiavh gddglspgaa vsppivqsat fsaesdeqfa alatetrghg fytrygnpnh
       61 aqvaavvael egvqagmvta sgmgaistia lallsagdhv vvqrstyggt tslvtgllar
      121 fgvaftqvdq tdneafaral rpqtrlvlve tpsnpllelt dlaavielah andalvavdn
      181 tfatpvnqrp adfgadlvwh sgtkylgghs dlsagvivgs adlvdrvwqt aivtgstlgp
      241 idawlllrgi rtlslrverh nanalalara veghpavrrv rypglpthpq helagrqmtg
      301 fggvlgvelh dgraaaalld glrlakraas lgsvstlvvh prsmwagivd aeqlaaagia
      361 eglvrvstgi edtedlvadf laaldtadrp r
//
LOCUS       WP_357662639             321 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Micromonospora echinofusca].
ACCESSION   WP_357662639
VERSION     WP_357662639.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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..321
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..321
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33609
     Region          <42..182
                     /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 makpvaetva rhlvatgqli dedpaealah alaarrlasr iaavreavgl aayhagewqt
       61 aiaelrtyhr msglqshlav ladceralgr peraidlfrg adrekldqav atellivaag
      121 argdlgqkda avamlqvpel tsetaepwta rlryayadal lavgrreear ewfsraadvd
      181 aegetdaaer lleldgvvie gdeedeepae evasgpgapg avparpdadl tgdaeptddd
      241 addrdddedd rddedddedd deddeqdeaa vaavpaddls ddeltddeag svaagstgdd
      301 sgaragggea tasggsdaaq r
//
LOCUS       WP_357662471             340 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nocardiopsis
            alba].
ACCESSION   WP_357662471
VERSION     WP_357662471.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis alba
  ORGANISM  Nocardiopsis alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (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   2  (residues 1 to 340)
  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 340)
  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 340)
  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 340)
  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..340
                     /organism="Nocardiopsis alba"
                     /db_xref="taxon:53437"
     Protein         1..340
                     /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=35826
     Region          21..327
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mgtaprydps eqsfsdlsge rvlvfggtgf lgrhvcaalr sagarvvtvs rnapaggtpd
       61 dsvpmdlasa teaelvrlvh dhaprvvina agrahggeps ellavnaeav erlahalpaa
      121 pepprlvhlg siheygtgev gtgfledgpt rpvgayaaak lratlaviea vrtrgldgtv
      181 lrignvvgpg aprqsllgtv ahslaeaaer artsgerprl rltplraqrd fvdvrdvaea
      241 vlaaatapla svrgrvvnvg cgraipvrqa vermialsga pldiverase tgrsdprwqr
      301 mdigaagell swrprrdler slsdlleear rsrarrttae
//
LOCUS       WP_357662652             140 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora echinofusca].
ACCESSION   WP_357662652
VERSION     WP_357662652.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 140)
  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 140)
  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..140
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..140
                     /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=14905
     Region          4..137
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 malpngpvta sseaeavlfd lvdvydraye aaaaelslsp aqacvlgrla errgmgalae
       61 elgcdasnit qivvrlealg lvarepdprd rrarlvgrtp rgdevnqrfa eaftfartav
      121 grlspdeqdq ltallrkalg
//
LOCUS       WP_357662703             374 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora echinofusca].
ACCESSION   WP_357662703
VERSION     WP_357662703.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 374)
  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 374)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 374)
  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..374
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..374
                     /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=38930
     Region          128..373
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgtgrsgvpa gvrdwvvavg vaatllvagl sgdrpdagpl gyallvaggl alaaarrapv
       61 avlavtglcv vghqavgldv pavaflfavy aavraghrvv tivaavamla alplaalarp
      121 sdlsvgealv rsrgalelaw lvaagaagea lrqaerrade aertreeaal rradeerlhm
      181 arelhdtlth qisvikvqae vavhlarrrg epvpeallvi qeagreaare lratlealrd
      241 dgrtpphgla hlpelvrrar msgldatltv agrrqdvpva vdrtayrivq esltnvarha
      301 aaatasvrvd yrpdalairv dddgratpda ppvpgigllg mrervtalgg rlraeprneg
      361 gftvhaelpv ggta
//
LOCUS       WP_357662753            3649 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Micromonospora echinofusca].
ACCESSION   WP_357662753
VERSION     WP_357662753.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13759389
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3649
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..3649
                     /product="type I polyketide synthase"
                     /calculated_mol_wt=378044
     Region          2..30
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          32..1422
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          1235..1685
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(1443..1444,1446,1467..1470,1495..1498,1522..1524,
                     1545..1546,1568..1569,1583,1610..1611)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(1546,1570,1583,1587)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          1704..1789
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          1807..3184
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          3006..3464
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(3217..3218,3220,3241..3244,3269..3272,3296..3298,
                     3319..3320,3342..3343,3357,3384..3385)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(3320,3344,3357,3361)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          <3469..3647
                     /region_name="PRK06060"
                     /note="p-hydroxybenzoic acid--AMP ligase FadD22"
                     /db_xref="CDD:180374"
     Region          3483..3568
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 madeaklldy lkrvtadlhq vrqrlrevea geqepvaivs mscrfpgrvr spedlwevva
       61 sgrdvvsdfp edrgwdlgsl ydsdpeqsgt sytrqggfvh dladfdpgff aisprealam
      121 dpqqrwllet swealeragi dphslrgsrt gvfagstgqd ygtvlmgaaq gleghlmtgn
      181 agsvvsgria ytfglegpav tidtacsssl valhlagqal rqrectlaiv agvtamctpa
      241 afvefsrqrg laadgrckaf aaaadgtgws egvgvlvler lsdaqrnghp ilavvrgsav
      301 nqdgasngls apngpsqqrv iqqalanagl aaggvdvvea hgtgtrlgdp ieaqallaty
      361 gqdrgnsapl llgsvksnig haqaaagvag vikmvmamrh glvpptlhvd eptpevdwsa
      421 gevslvteat pwpavdrprr savssfgvsg tnahtileqa papqqppsaa apvverpvvp
      481 vpvsardaag laaqatrwae riaadetlrp ldlgfssvts rssldhravv catgredlla
      541 glralaagqp sgtvvagqag grgslavlfs gqgaqragmg relyagfpvf aaaldevcvy
      601 ldallprplr evlfapegsa eaalldrtvf tqaglfavev alfrlvesfg vapefvgghs
      661 igevtaayva gvlsladaca lvaargrlmq alpagggmla vaadeaavve siagstdrvg
      721 iaavngptsv vvsgavdald evervwrerg vrtrrltvsh afhsplmepm laefrtvldg
      781 lafsapslpv vsnvtgalad adeirtadyw vrhvreavrf adgvaalrsa gadtfleigp
      841 qsvltamvge ilpgddvvla vaaqrkdrpg aqgllaglae lhthgvavdw qpwfagtgar
      901 rvdlptyafq hqrywpeaga gwtgdvtafg lrpaqhpllg aavgvahaeg flftgrlarr
      961 thpwisdhvv fdtvllpgtg fvelalqaga hvgadhvrel tlesplilpe tggvdiqlwi
     1021 gpadetgcrs vslhsaqdge ptegerawtr nasgvlasgp avpsgpvgws dlttwpppga
     1081 tevgtddlyl nlaaqgydyg psfialrsaw rrgddlfael alpeapaaea ggyglhpall
     1141 daalhtlglt tpagepsgad mppgygrlpf swndvalhga gaaaarvrvs htgpdsisll
     1201 ltdvtgapvi svgslvlrpv sadqlrtasg ggteslfrve waplalpagp atvdwavigd
     1261 aaaltdavaa tgtavtayad ltalatamdd gtdapgvlvv pfldpptsad vpravaevth
     1321 ralavlqqfl addrytasrl vvltsgavat ewdtdltdla gaavigllrs aqsenpdrfv
     1381 lvdvddiagc aaalvpavat depqvvirag vaagarltrv pavveppaap fdgdgtvlit
     1441 gatgtlgqlm srhlvgtygv rhliltsrrg raaggvaelc aelealgvsv tvaacdvadr
     1501 gavaellagi paehpltavi haagvrddgv issltpermd gvlrpkvdaa whlheltadl
     1561 dlkafvsyss laataggpgq gnyaaanafl dglaqhrkar glaaltlawg lwadrsgmtt
     1621 elddvhlnri srsgvaamea eeglalfdaa crttdaalvp arldlaamkv qfaggtippl
     1681 yralirtpar aaaattgasl vqqlaglgea eraaalveiv rgqaaavlgy pdpaaieprr
     1741 afsefgfdsl tavemrnrln nafgmrlpat lvfdyptphd laaflgteia gtpvpvrptt
     1801 tavsvgddep laiigmacrl pggvwspddl wrlvvdgvda isdlpadrgw dldslyspdp
     1861 dapgtfyarg ggflsgvdkf dpgffgispr ealamdpqqr lllettwesf esagidpadv
     1921 rgsstgvfvg tsgqdygsll ayspeaaegy mltgmtssvi sgrvaytfgl egpavsldta
     1981 cssslvalhw agqalrrgec dmalaggvmv matptafvef srqrglaadg rcksfaasad
     2041 gtgwsegvgm llvqrlsdar rqgrtvyavv rgsainqdga sngltapngp sqqrvirqal
     2101 asarlstadv dvveahgtgt tlgdpieaqa llatygrerp adrplllgsi ksnighaqaa
     2161 agvagvikmv qairhgmvpa tlhvdepsph idwtsgavel atqsrpwpav drprraavss
     2221 fgisgtnahv iieqadapie avapaepapg lvaadvvawp lsarskgals gqaarlaeyv
     2281 rgrgevdpaa vgwslattrs vfdqraavva stvedllagl dalasgspag nvvagtvash
     2341 gagavfvfpg qgaqsarmaa glvgrtpvfd arlaecqral vpyldvdlvs vltgddeswl
     2401 ervevvqpvl wavgvalaav wqhagvspaa vighsqgeig aacvagilsl edaakavalr
     2461 sraltvlrgt gtmasidlsa eavaerlpaf pgvgvaavng psivvvsgpp qpvadlveac
     2521 qadgvrarli pvdyashsaa vqdvaeqlra dladvtprqg hirlvstltg dwvepasmta
     2581 dywyenlrqt vrfdaavrva vaaghttfie isphpvltmp vtailddsgv tghtlgslrr
     2641 gdddatrllt nlatahtigl pvdlttvlae tdivalptya fdhqrywvep plhraqdvss
     2701 aglqdaghpl lsatltfpds ermvftgrls vrthpwlgeh rvmdnillpg tafvelatya
     2761 geqagcptve eltllaplvl pelgalqvql mvgdrdddgr rsvqlysrpy rdgsdeilad
     2821 vawtchatgl lgpqpadaap afdlgvwppp gatrveaddf ysgieatvfg ygpafrglra
     2881 awtrddevfa evelpadhha eagrfgvhpa lldgalqams iggflgrmgd gadasvprlp
     2941 fawtgvslla agatalrvrv aaagevgvsf qvadatgapv lhvdslimrr vsgdslgaar
     3001 sgrheslfqv dwpvlpvptg pvpaatrwva lgddlalsaa ceaagarvrt dvgldslgdl
     3061 laggepapea vivpigdvgd ptdpalagqa ratthrtlaa lrtwladdrf adsrlvlvtr
     3121 davaageqqt vnlrqapvwg llraaqlehp grcqlvdldd tpdsaaalaa avasgepqla
     3181 vragqvrtpr lgrvpagvep lpggidpdgt vlitggtgvl grilarhlat thgvrhllla
     3241 grrgaaaegi ddlvaelaga gtevtvaacd aadpdalsal lagvpaahpl tavvhaagvl
     3301 ddgvlesmtp ervdavavpk idaawhlhrl tadadlaafv lfssaaatlg sagqsnyaas
     3361 nafldalaah rragglagis lawglweqas gmtghlgddd vrrmaeqgaa glateqalnl
     3421 fdaawrldaa avvpmrldvg tlrgqaeagt lapmlralvr vplrrsvdat garsggvqls
     3481 qrlaglagpe rlkvvldvvr aniaavlgha gadavdpnrl ftdlgfdslt avdlrnrlng
     3541 lsglrlpatl vfdyptptal aekltseiaa daapstqplf qgidtvesll nsipldpaar
     3601 arftarmqdl lakasdlaag paaepdrpdl dsasddeifd fiskefgis
//
LOCUS       WP_357662761             724 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora echinofusca].
ACCESSION   WP_357662761
VERSION     WP_357662761.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 724)
  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 724)
  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 724)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Kannan,N., Taylor,S.S., Zhai,Y., Venter,J.C. and Manning,G.
  TITLE     Structural and functional diversity of the microbial kinome
  JOURNAL   PLoS Biol 5 (3), e17 (2007)
   PUBMED   17355172
REFERENCE   6  (residues 1 to 724)
  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 15505478
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..724
                     /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:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=78425
     Region          <65..131
                     /region_name="PknG_rubred"
                     /note="Protein kinase G rubredoxin domain; pfam16919"
                     /db_xref="CDD:435653"
     Region          132..393
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(132,156,160,185,190,195,197..199,213)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(139..140,142..145,147,161,163,193,212..215,219,221,
                     264,266,268..269,271,285..286,289,302..305)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(139..140,142..145,147,161,163,193,212..215,219,266,
                     268..269,271,285..286)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(143,219,221,264,266,268,289,302..305)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(285..293,298..305)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          408..722
                     /region_name="PknG_TPR"
                     /note="Protein kinase G tetratricopeptide repeat;
                     pfam16918"
                     /db_xref="CDD:435652"
     Region          548..573
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          578..605
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 mtvdrdcaqr ncpgavdedg fcrlwghecl gaggadvgga avrppeadpr pprtasrpwe
       61 rpavlptarp hdpltavvsq avvpehsryc gntrchrhrg prlprvagfc pdcgtrysft
      121 ppladgdlra gryriegclg nggvgwvfla rdedmdgawr vlkgqrnped reavaafvae
      181 rqalialnhp rivtithalr pesdrdggyl vmeyvnggtl eearstagpg ggscavdvaq
      241 algyavqild afeylhdqgw lycdlkpenv mrvggqgtnd piklvdfgaa rridntvspa
      301 wgtvgytape verlgpagps vrsdlytvgr tlaaltlvpr stevtrippg adllrlpvpa
      361 rldpflrlla rataaepedr fasaaemreq vrgvrrqvgs atdgvprptr stlfspstca
      421 falhtdraal dvveimlglp vplvdgtdpa agflaslgaa dpaeliellk tapqrtaqvt
      481 yravrahlaa grvaeagpll agfpedlrdw alwwhrglva lvgrdaatar rrfeqvygwl
      541 pgevstrlay avaceldgdp rtaadhyrgv wdadpgvvga afglarclla tadarsaada
      601 llrvpessra stvavtcavr illdapddgr rldaaldaaa ivdklppfge reeveahilr
      661 ialdcdlteg rhddrrlfgh rldedalrra ferrcrsrar rtadrreria lvelanayrp
      721 vtww
//
LOCUS       WP_357662903             379 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357662903
VERSION     WP_357662903.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 379)
  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 379)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 379)
  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..379
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..379
                     /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=40416
     Region          122..378
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrrdilaava afavgavmlv gdayfhrrgv plwftavpla ltcagvavrr raplaclalg
       61 vaavtidvay tgpslpttlv ftdnlysaal ygpvrasrwl lgvtttaavi igavigmler
      121 swlalaiygv qvslvlvvpv ttamvlrqqr dqaaaerara eqvahlaeld rgaaivaert
      181 rmarelhdmi anhfsaiaiq stavlsrkdl dagavqqima sirensvqgm aemrtmigll
      241 rqegedndat trprladaad lverarqagm etvmtvegtp ydlpvsvdla gyrivqealt
      301 namkhgddrv evvityaqgl vsvvvdnpln eartqlpgag agligmrera tlvggafeag
      361 pyeekgwrvr atlptehal
//
LOCUS       WP_357662839             279 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora echinofusca].
ACCESSION   WP_357662839
VERSION     WP_357662839.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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 279)
  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 279)
  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 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   6  (residues 1 to 279)
  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 279)
  AUTHORS   Rosinski,J.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..279
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..279
                     /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=31463
     Region          1..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          108..263
                     /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(109,111,113,122..124,126..127,132,141,148,150,152,
                     154,163,165..166,168,171,177,179..180,209..210,212,214,
                     224,226,228,230,236..240,247..250,252..254,257)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mddvfralad asrrrllddl nrrngqslre lcagldmtrq svskhlavla aanlvttvrr
       61 greklhylnp vpinavaerw idrydrervr aladlrtale repmdsptfi yttyvnttpe
      121 klwtaltepa ftrrywggva lrsdwrvgsp vlwqdepgge frdlgqrvlv aepfrrlsys
      181 whgfqpehaa hfgwsdeela arlgerrsrv tfdiapyggf vkltvthedf spgsemyrav
      241 sgqldgsggw pellaslksl letgeplpep rpesataqg
//
LOCUS       WP_357662913             399 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Nonomuraea dietziae].
ACCESSION   WP_357662913
VERSION     WP_357662913.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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..399
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..399
                     /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=42967
     Region          144..294
                     /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 mrteedlvha lrqaaerapq pdlsaalgvr rrrrtrrrta saalavaavi gvagvgttia
       61 rdvftsgggd gvavapvdgp sevrasmqas aeaesrpqeg tpiekiwpka iftmpaknad
      121 gwryrpitgv satevmlnae safekagaie iydsesgtfr kvtdvpttpg lkraypqdaa
      181 fdarsvvwwv natdvreiwk aplaggearl vatykgehqg ieaiavkgkh iywseedgtv
      241 wrllaeggap ekiadglhli dwpwasdase rehrknqtkv vnletgetrq itaaagakgl
      301 rcgptwcvae glvqrvdgtg lrkadvsfhm sgypvldryv stgtsvldle tdswvafpkn
      361 pdnwwgsgts sapstitywg atkgekpdqf rmvnlaaaq
//
LOCUS       WP_357662919             355 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Actinomycetes].
ACCESSION   WP_357662919
VERSION     WP_357662919.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetes (high G+C Gram-positive bacteria)
  ORGANISM  Actinomycetes
            Bacteria; Bacillati; Actinomycetota.
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   Wintjens,R. and Rooman,M.
  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 355)
  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..355
                     /organism="Actinomycetes"
                     /db_xref="taxon:1760"
     Protein         1..355
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38949
     Region          13..76
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 msgrgrsalq rgevtgylfk liresipltq eqlaadlgvd rvtvqswesg rrpftavplg
       61 qaitvrhrlr rldanpvlla alddaaeadf ilaavldeqv drsdvaehpl gwsvlthrlt
      121 dlilwavlgq tpafakglpi ahprrgpvas gptlpvdeqr tffanlhvla eraaagrdps
      181 vllhrqacfl agmdptrtaa gwltksttra lpmtafrtws plwpdarsvv tslanqgdpe
      241 plrdfiahah pddaceraal nysaywvgei pyhhrddsfm pgplagwhgs illrhliqrl
      301 epghpfvdln ihnvwallaa rrglaldspa atralldrci plldsdrtsa rrsse
//
LOCUS       WP_357662941             319 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora echinofusca].
ACCESSION   WP_357662941
VERSION     WP_357662941.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..319
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..319
                     /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=34483
     Region          59..317
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msdlpliqad raapplaaaa tptggrrrrv rllsrtdrvv valmvvvpll lvvglvwlpa
       61 gatvllsgtd wdgigpvsdi ewvggrnyad vvqnyppfvp avqnnllwla alfavatpfg
      121 mflavlldke lrgtrfyqta lylpvvlsla ligfvwqlly srdqgllnav lgtgvdwygd
      181 pdvniwavlv aagwrhvgyi mllylaglkg vdpslreaaa vdgasegrtf fkvifpvlrp
      241 iniivlvvtv ieslrafdlv wvinkgrngl ellsalvtqn vvgeasrigf gsalatimlv
      301 vsllfitvyl atvlregrr
//
LOCUS       WP_357662967             214 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357662967
VERSION     WP_357662967.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 214)
  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..214
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..214
                     /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=23304
     Region          8..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtgtrplrad aarnrdkllv aatqvfgerg idapleeiar ragvsigtly nhfptrqaff
       61 daifperlaa ldrmaaqala dpdpwngfvg fldalfalqa qdhglndala rrfpvtsevn
      121 dachsgltql driierakes gqlrddfepq dlatlvwams qvireameaa pqawrrclaf
      181 fldglradaa hpiavpaltt vqlaeaaras anra
//
LOCUS       WP_357662986             365 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora echinofusca].
ACCESSION   WP_357662986
VERSION     WP_357662986.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     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=37905
     Region          18..363
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 midylvmggg iagasaghhl aaygtvvlle meqvpgqhst grsaavfsey yggsavralt
       61 rasrgfltap ptgfaehpll tprgvlslcp pgsedafeea lrdgaevdpp areidvadlp
      121 rhcpvvrpew crramvkpav rdldvaalhq gylrgvraag grvvcgarvr rlrrsgggwq
      181 vttdagefta rvvvnaagaw adevaaaagv rpvgltplrr taflvdapag vpagdwpmvn
      241 dvdgsfyfkp esgrllvspc dttpappgda rpddldvaig adrvqaattl eirrvhqpwa
      301 glrtaapddv pvigpatdap gflwmaglgg ygvqtspaag allaaltvda pppvdptpfs
      361 psrfp
//
LOCUS       WP_357662992             287 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357662992
VERSION     WP_357662992.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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 287)
  AUTHORS   ter Beek,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..287
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..287
                     /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=32158
     Region          4..286
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpgqrwytpy lfalpalalf gvffvwpalt aiqlsfmeyd vvsppefvgl dnfvkmvgds
       61 tfwtatlnsv lfliglfpll vvaplllavl vnqklpgirt frmlyylpvv tsmvavavaw
      121 eyvfhqqgvl nwiltgagll dqpiqylldp fwalpalilv egwksmgfym miylaglqti
      181 dsslyeaarv dgasawqrlw ritvplmipy iavaitmeml damqaftsvy vmtrggpqda
      241 tltlgyyiws agfehydmgy asavglvlwv mmiamamlny ritkgrs
//
LOCUS       WP_357662995            1042 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora echinofusca].
ACCESSION   WP_357662995
VERSION     WP_357662995.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1042)
  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 1042)
  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 1042)
  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 1042)
  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 1042)
  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 14997958
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..1042
                     /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=112233
     Region          55..533
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(185,188..193,195..196)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(188..189,309..310,331..336,357,424,436,439,527)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
     Region          559..615
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
     Region          662..927
                     /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 mragdtvsva avpvsdgptc rctatpaaaa vgtpyddrpf lavpgmveer vdrhphrrav
       61 sfrgrsltyr elddlangva aalagrgvrr gdvvpvllad glelpvvdla lmklgaafvp
      121 vdpgwpadrl haslrvvrpr lavvrgtgpr pdtgdvpclp vdldeitptr rrpgvpigpa
      181 dliygiftsg ttgtpkcaln rhdgianrlr fmtrhfaatg devvlqnsrh tfdssvwqmf
      241 wplttggrtv vpveggfldv ertvrtiade tvtmtdfvps vlgalvsvld rdpaarrava
      301 slrnvivgge eidpwavhrl velvpgvavt ngygpteasi gmifhtvars dgdvipigrp
      361 idncyaavvd delrplppge tgeiviggvc lgegylgdaa rtaevfvpnp lpaipgarly
      421 rtgdlgrvap dgrlhfagrr dhqlkvngvr ieageietaa trlagvrqak vllareprgr
      481 slalflaadp evtepqvrah lrrllprthv prhvvvrdal pltgngkvdr qaleawldht
      541 fadrtrpsaa paeartlper vlgvfrtvlg rpdldpdtdf ldaggdslqa ldvvtalgad
      601 qslrvgvqdl fthrsaarla ralavrlraa dpaetedelv erdakipadl pvrpvgrrra
      661 prtvlvtgat gfvgarlvhe llattdvrvl claraaddae atarvvrala erglwrpghd
      721 lrlhgyaadl grpalgltpq awdrlahdcd lvlhagalvn flfdyrahra anvlgtaell
      781 rlcltgrpkp lhhvstlgvl dseaarhpqp lpetydpala vpptsgysrs kwvaeryldd
      841 arrrgatitv lrlgevmpaa ddghpnpral thlllaachr lrmrpdapvr sdwtpvdwaa
      901 rrivatvvdp rqwggtlhvl hpvsvdftdl plggadalpr vscgrflagl reaagegdrd
      961 aavllalfpp gagadeerlr avfatlltdn prlfrrdgca elerrrgftd hrlgpsvgay
     1021 rawlgehegr eadrlllpag pg
//
LOCUS       WP_357663119             305 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357663119
VERSION     WP_357663119.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   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 305)
  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..305
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..305
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33908
     Region          14..299
                     /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 mpdesfvhmd gpwthrsvha ggtrfhivea gegplvlllh gfpefwwtwr hqlaslpeag
       61 yravavdlrg yggsdkpprg ydlptlagda tgliralget gaivvghdwg gllawtmavt
      121 dpksvhrlva vsaphplrlr galltdpfgq lrasgytlgf qlpflperrl trddgklvgq
      181 llddwsrpgw peqdtarvyr eafgiptvah caleyhrwfa rsqvrpdglr yaramrteve
      241 aptlqlhgal drcilprtaq gssryvaapy rwrllegtgh fpheeapevf daellawlad
      301 pepdr
//
LOCUS       WP_357663236             320 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357663236
VERSION     WP_357663236.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   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 320)
  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..320
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..320
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=33668
     Region          34..315
                     /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 mtawkvaagv lagvaigaaa rvrrapepqp lrgrtltvtt pdgvrlavev depespacav
       61 vfahgwvlnr hswhfqreal agramlvsyd qrghgdstpg ppdcctieql gedlhaviss
      121 vvppelpvvv vghsmggmtv mglaaahpel fgprivgaal vstssgrlae styglpglfg
      181 rlaprvtprv msalrdplit pvttlpltry mafgpraehl rfvnrmvaat paavmagffh
      241 gmavhdklaa lsalgevptl vmvgehdrlt plvhshriae alpsarlvvv rgaghmlale
      301 rpsvvsaels allercrsgs
//
LOCUS       WP_357663264             189 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Nonomuraea dietziae].
ACCESSION   WP_357663264
VERSION     WP_357663264.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..189
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19594
     Region          47..189
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrakphalal vallavsgca gnvggqpqag dtrfvagdgk vtvfpaadrk aapvvegvtl
       61 dgarasvaah kgkvvvlnfw aswcgpcrae apvlkdiyak tkaggvefig idfkdrqada
      121 laferteqpg ypsifdqpgk valsfqgtvp paaipstlii deqgrvaara lgavkyndll
      181 kavtqvrde
//
LOCUS       WP_357663338             198 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Nonomuraea dietziae].
ACCESSION   WP_357663338
VERSION     WP_357663338.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..198
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21153
     Region          1..197
                     /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..32,70,74..75,78..79,91,95,102,
                     105..106,111,134,138..139,141..143,145..146,149..150,
                     153..154,169..170,172..174,176..178,180..181,183..184,188,
                     191..192)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(137,141,144..145,147..148,183,186..187,189..194,197)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(158..165,171,174..175,178)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 migvyvpgds llhrlpawak vlglvvsctv lvllgsltal agfiayvaim ylvsgvgfaa
       61 awaqirplrw fapvlfvmqf vlvgldaavt stlrivlava laglvtlttr fadmmtffer
      121 cfgplrrvgv dpfrvsllls ltvrsvpvis alatrvreaq rargvswsmr afaiplvvsa
      181 lrhadalgea lsargldd
//
LOCUS       WP_357663322             922 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Micromonospora echinofusca].
ACCESSION   WP_357663322
VERSION     WP_357663322.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora echinofusca
  ORGANISM  Micromonospora echinofusca
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 922)
  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 922)
  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 922)
  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 922)
  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..922
                     /organism="Micromonospora echinofusca"
                     /db_xref="taxon:47858"
     Protein         1..922
                     /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=93554
     Region          40..856
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mwdspdggep rgvpvpadts trpaaglsaa eaaarlradg pnaavapprr hlggrvlhql
       61 tdplvallla aavvtavlrd ypdtavivlv vlvntaigvv qevradraia aldqlaapta
      121 rvvrdgrdmv lpaadlvrgd lvrveagdvv padllldeaa rlsvdesalt gesvpvarsa
      181 geeasagtvv ttgratgtvv rtgaasalgr italvastrp aatplqrrla glgrmlgfaa
      241 vvlsglvfvi gvvggrpvvd mavtavslvv aavpeslpav vtlalalgar rmagaraipr
      301 rlhavetlgs vtviasdktg tltegrmavq havtgdgsry gvtgsgyaph ggvhqrgapv
      361 avpddlrrla ragllcndat lapptderpe wtavgdplea alvafaarcg ldpertrsaw
      421 prvaehpfdq elrrmttvhr scdqrylvvc kgapenvlaa plvdasaeei aeltaaahrl
      481 aaeglrvlav astvvdappa dparpvglrp vglvavgdpl rtgaadiags fddagvrlvl
      541 itgdhpataa aiggqlglwr egdpvvrgdd gdparahpqa rvfartqpeq kldiiaglqs
      601 rghvvamtgd gvndapalrr adigvamggg tevarqaadl vlvdddlstv aaaigegrri
      661 ydnirrflry alsggvaeia vmllgplfgl avpllpaqil wvnllthgvp gvalgaepae
      721 pgtlrraprs psesvlgagl grdvlvtgal iaavvlgagv laahwdrpwq svvfvvlgla
      781 qlgvalavra prprgarhgn walpvavavs allqvagvll pplrellgte plgaaellac
      841 aavsvlpglv lrlarrpagg tptgvgtdaa gtdaagtdaa gtgagteaag tdaagtgagt
      901 eaadarwlai rdqgptgrda rp
//
LOCUS       WP_357663366             158 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357663366
VERSION     WP_357663366.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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 158)
  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 158)
  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..158
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..158
                     /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=17462
     Region          1..158
                     /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 mrlrewtagd adrvleafrs edmraqsgep irtlddavrw iegwqdrgha faveldglvv
       61 gnvavtgidr hgngwvsywt taqargrgva araagllaew afterglfrl elghrtnnpa
      121 scrvavragf vaegiergkl lydgvrydve rharlatd
//
LOCUS       WP_357663472             112 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357663472
VERSION     WP_357663472.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=11849
     Region          3..94
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 memasdielt daargflkam asetrqqilm lfsggieltv nevaermsla qsatsthlat
       61 lrdggvltsr rewkavyyra dparigrals dlqaslqacc ppsdcppsgg cg
//
LOCUS       WP_357663492             363 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea dietziae].
ACCESSION   WP_357663492
VERSION     WP_357663492.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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..363
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..363
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39824
     Region          <8..53
                     /region_name="CysS"
                     /note="Cysteinyl-tRNA synthetase [Translation, ribosomal
                     structure and biogenesis]; COG0215"
                     /db_xref="CDD:439985"
     Region          142..358
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mseaprhvte laerrvkara vrdyaaadvl rqeieqagwq vrdsadgyel tvkppfeqwp
       61 svrsvpvsam tetekkkggg ldkinpaael gfsgdpaqtg dpgddmlhaq rtwdaslatn
      121 rldtagvdle rqrveisgvt asvgvivdgw addmrrcles ilehtsapil aldlgnvhga
      181 gealhelaer hperitawhv aeqphwqggt agwgaartkl mqldtadvhv lletstvleg
      241 daltplvkav kdgavaagwk gvdpgendte wnesgpgrvr allgylmavr rgaalrafpe
      301 kvryyrnadl vlslalegpl vvpderlpvr qerhhgyhdv speyrerear rnyeavlrml
      361 rss
//
LOCUS       WP_357663478             223 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357663478
VERSION     WP_357663478.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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 223)
  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 223)
  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..223
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..223
                     /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=23056
     Region          2..223
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mkltvfgasg gvgrhlldqs lakghdvtav vrdpaklngq pvrvvrvadm ataevstllp
       61 avegadavls algppnnaaa gvasrgtkai latmraagar rlivvsaapv gttpspgrpn
      121 pprydpgdgp flrflvypiv kaalrpqyld lavmedavrd sglgwtvlrp vqltdkpmtg
      181 ayrtavgqnv pggryvsrad vahamlaald rpetveqvig man
//
LOCUS       WP_357663503             102 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357663503
VERSION     WP_357663503.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=11288
     Region          10..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrvlpqpaae diqltevlha lsdparlevv trlaverelt crgvgdeigl hkstmshhyr
       61 vlresgvvss rqegrqkfmt lrrddldarf pglldsvlga tl
//
LOCUS       WP_357663521             148 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357663521
VERSION     WP_357663521.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=16550
     Region          5..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mrwlnedeqs twqafglasr llvdrldrdm qaqagmpity yellvllsga pertarmsdl
       61 akwtnskpsr ishavnklee agwvrrehfa gdrrgwlavl tdkgqaalea aapghvasvr
      121 ehlvdlltpe qlkqlgdisr vllshltr
//
LOCUS       WP_357663537             181 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357663537
VERSION     WP_357663537.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 181)
  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..181
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..181
                     /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=19512
     Region          13..>105
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meradaarnr arileaaagl frakgapnvt mddiakaagv grgtlyrrfp drasiavall
       61 dehervlqek lirgepplgp gapaaermaa fyaamvelle ehahlilgse vgrsrfetga
      121 ygfwrvhvrs lldgvrdada lvdtllapla pdvytyqred rgltpsqisa alarlaravv
      181 t
//
LOCUS       WP_357663543             331 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357663543
VERSION     WP_357663543.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 331)
  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 331)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 331)
  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..331
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..331
                     /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=34456
     Region          82..318
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrlftnaatg vaalvlllal pfarrrvlaa arrlagsdpg dlrlvawlfv hgvtgpaall
       61 gvvvmlsalg viwtlrtaet smavtltlsl smlaivslaa gfghlatraq arladlllnp
      121 darvrelada qaaelrrier dlhdgaqarl isirmtlgla rsapdpreli eeawesagqa
      181 ltdlrdlvrn ihppvladrg lvgavqaaal lcpvpvrldl dlegrpeapv esalyfaate
      241 alsnvakhsg assawvrlty adgvlrltvg ddgrggadaa agtglhgitr rlsafegtlt
      301 vhsppggpse limelpcals spkislssgt g
//
LOCUS       WP_357663591             141 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system VapC family toxin [Nonomuraea
            dietziae].
ACCESSION   WP_357663591
VERSION     WP_357663591.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006427
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..141
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=15550
     Region          5..138
                     /region_name="COG2402"
                     /note="Predicted nucleic acid-binding protein, contains
                     PIN domain [General function prediction only]"
                     /db_xref="CDD:441958"
ORIGIN      
        1 mtatlldtgp liavvdrddk hhascvrlle elegplllps tilieagwti nrhmgpavha
       61 qfldlvteef elvdllpadv rrmaelvrly kdarldpadv svvaiaerlg vtqiatidrr
      121 dftlirpqhv safillpetl a
//
LOCUS       WP_357663687             165 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Nonomuraea dietziae].
ACCESSION   WP_357663687
VERSION     WP_357663687.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..165
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17137
     Region          47..153
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mpflvaavvf lgllclfnlv ltlgvlrrlr ehtaelarln ersmfmpydp avlvgrplpe
       61 aaagarlvgf fdvgcstche rapqfaeaag kqpalavitg dgakvddlva vvggvssvit
      121 gdeaasltha lgveafptfl wadqegtvaa ahtelselpv vatar
//
LOCUS       WP_357663690             957 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357663690
VERSION     WP_357663690.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 957)
  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 957)
  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 957)
  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 957)
  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..957
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..957
                     /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=103418
     Region          1..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          118..957
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          710..738
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(711,714..715,718..719,721,745,754..755,758..759,
                     761..762,790,793..794,797..798,801)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          743..779
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          789..817
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          823..857
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfrllgpmr iqvngspvri tapkqrtvla mllaraghvv pirslvaevw derpprsava
       61 nlrtylmqlr kllpdeewlv tsdvgyllrv gaeefdlfef ealsargrqa larrdlgaae
      121 eaftralalw dgtaaedvpl gptlrevvar ltehylgvve ehadvqlalg knataatrlr
      181 evigqyplre rlhgqlmval yrsgdvvgal dafgaarril adelgidpgp dlrrlqqail
      241 rrdtallapd rdipavpvdd grprprllpr apmvfvgrsa elghlhtvly ggagpsvvtl
      301 hgpggagksa lalkaahgva drypdgqlyv dlqgstpglp plppaevlgr flralgvppg
      361 dvpaapaeaa thyqslladr rvlvvldnaa gaaqvgpllp agggcaalvt sraalttvda
      421 vpiavgmlde aesvrllall asqervsaea eaaaeiarwc gyhplalria garlagrpdw
      481 sltrfgerlg dqqrrldelq aadlrvrtcf evgygtltst akaafrafgv levpevgvel
      541 aaeladvdpt taeaaldelt earllepvgd grfrmhdllr lfaaelavth hapeertrav
      601 graldwyldh crrlqallqp hllpvsggar atgvdlrdlp tavrwldtel pclvaaavqa
      661 akgrqggfvi elmalikaia mkngywrele tiarlaieva rrdgdrtaea stlatlglve
      721 wksgqaeaah dllrraldlw revgergeeg lalhnlgwlc mqtgdldaal dhisagllll
      781 eargsnrvgl vshnlgevll rlgryteavd rferclsirr adrdlygesi tlaalgrahc
      841 lldqrekalv vlaealarce etgnredqwe vllsrseirl rqgdpaaaaa dlvrvleltt
      901 kigdvyghaa glrqlarart alddpraaad adkaaelfad patrrdpvle rlltarl
//
LOCUS       WP_357663724             270 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357663724
VERSION     WP_357663724.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 270)
  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..270
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..270
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28218
     Region          1..262
                     /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 melaferrgh gpplilvhgi ghhwqawlpv mdrlaasrdv iavdlpgfgr sqglppgtpy
       61 taesladave sfcamldvre phvagnslgg yialelasrg vvrtataisp agfwsraell
      121 wcqsvlramr asaeggaaeg sgapgsgals rllgseplgf lgagllvahp srlgrvalaa
      181 gtealasapg fnetldsftg mmppappksp itiawgehdr lllrrqavra arwsnqrvkl
      241 lkgcghvpms ddpelvakvi leasdprspa
//
LOCUS       WP_357663742             736 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357663742
VERSION     WP_357663742.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 736)
  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..736
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..736
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80524
     Region          3..734
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mergnlpvdv tgfvgrrael kevrrllrra rlvtltgvag vgktrlamra ahsarrafdd
       61 gvffvdlsgl hdpglieaai adalrltdqt artdeevlta hladkrlllv ldgtehlver
      121 caqlvelllk ssrglkilva grqalevege hllpvpsltl sdavalladr araatgcfav
      181 taenealvrk lclrldlipl aielaavrlr alsveevveg ldhrfklldl ggprhqplra
      241 aigwshelct pderllwarl svfsggfglv aaesvcsder lprpaiadlv gtlvdksili
      301 reeseggvry slidsvreyg aewlgrlgaa etdalrarht dfylrlaran eadwfgprqq
      361 aifsstrael gnlraafers ldaheqaldm aatlwfywvg cgqlregrhw lgralsaape
      421 ptsarmkalw vagyvcvlig esdsgmrfle ecrdhgdqra vayavhrlgc aaliaddhdh
      481 avplfteave ryaklgvlec nvlmacvela ivlafrgeld scaelcgqvr drcervgeqw
      541 vlsyvdyvea yaawakgarg ralslalrsl rvshrfhdlv givlavelva llraeagepe
      601 vaavlqgaag aiwrsvgpll fdsrhfnrph licaeqaere lggrvyaaay argrrlglde
      661 avsaaaggre praelpltrr ewevaqlvae glsnremaeq lvlskrtvda hvehildklg
      721 fssraqiaaw vaslps
//
LOCUS       WP_357663757             233 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaD family protein [Nonomuraea dietziae].
ACCESSION   WP_357663757
VERSION     WP_357663757.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..233
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=24456
     Region          1..226
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mttlgaglkl tlfalltsac aamlaltisg atvapaqvyr glftdatglr pgddvrvagv
       61 rvgrveeisl ygtqaevafs vrrstplprg vvaairwrnl agrrylaltp gsdasgylkp
      121 gervaatrpa ldvtalsngf rpllkairpe dvdtlsrqiv qvlqgeagtv esllghissv
      181 tgpladrdav irsvidnltv vladitgrdd eygslidnlh alvkglsger trv
//
LOCUS       WP_357663792             309 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Nonomuraea dietziae].
ACCESSION   WP_357663792
VERSION     WP_357663792.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..309
                     /product="phosphotransferase 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=33802
     Region          13..239
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mndeinppaa gvrlpwqdvp ealrlqiadf lggrvveavt qtggfspaaa vrlrtehgrr
       61 afvkacgssp npdsirayrw eaaiaaglpa dvpaprllts fdtgdwvalv fediegrppa
      121 mpwrddelrr vldavgklsa rltpspveap tfserhkdaf tgwrrlleed ttgldpwalr
      181 hldtlaeles gwaeaaegdt lvhadlradn llltedqvyv vdwpwacvga pwidvmamlp
      241 svrmqggppp qdlfdfpdpa vtavlagltg ffvwngrqpd ppglptvraf qraqgvaale
      301 wlrhrtgws
//
LOCUS       WP_357663807             310 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357663807
VERSION     WP_357663807.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 310)
  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 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   3  (residues 1 to 310)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..310
                     /product="GlxA 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=32413
     Region          1..308
                     /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 mdivilayhg vrlmdvtapl evfgtaagfg apyrvrlcsp gggpvttstg vsllaeppvt
       61 sahtlvvpgs pglpahgara elleavsavs arrvasvctg afvlaeagll dgrratthwr
      121 haatlasryp aievepdaiy vrsgevltsa gvsagidlsl amveqdmgad larevardlv
      181 vflqrpggqs qfsvasrtpr prhdplrgll dqvaadpgad hslqsmaars gvsvrhltrl
      241 fhervgrtpa ayvesvrlea aqalldsget vtgaavrsgm gsdeslrraf lrhlgvtpsa
      301 yrarfrtsls
//
LOCUS       WP_357664075             451 aa            linear   BCT 28-DEC-2024
DEFINITION  LVIVD repeat-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357664075
VERSION     WP_357664075.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..451
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=48626
     Region          36..429
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          60..94
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          101..156
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 masrlgrvlv lagaaltlva attpaqaesa dkilksanve hvanlpkkga ftgpdafnsd
       61 lafqgdyayq gnyngftiys ikdpakpkvv sqvtcegaqn dvsvkgdllf lsvddsrdsd
      121 scksdygtpt skkswegiri fdisdksrpk yikavetacg shthtlvpdk sgksvylyvs
      181 sympadiype ckpphdrisi vkvplkkptd akvvsrpvlf peggneqqsg lllptsgchd
      241 itvfpsknla agacmgdgvl mdisdrerpk vtatvtdenf afwhsatfnn tgtkvvftde
      301 lgggasatcn atigpkrgad avfdivdgel vhksyykipr hqdssencva hngslipvkg
      361 kdimvqawyq ggvsiwdftd ssapkeigyf ergplkprss ggswsayyyn gfiyssdiqk
      421 gfdvlrisdk ltdpaakvrl silntqtqlp f
//
LOCUS       WP_357664017             437 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Nonomuraea dietziae].
ACCESSION   WP_357664017
VERSION     WP_357664017.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=46957
     Region          4..437
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mpyrltvigt gylgithaac madlgfdvlg ldvdvdkirr lqsgelpihe pgleeilrrg
       61 lesgrlrftt syeeaaafgd ihflclgtpq khgeyaadvs yldaavesla pyldrdclvv
      121 gkstvpvgta arlaaklarl apvnagaela wnpeflregf avqdtlnpdr ivigvaseqa
      181 ekilrevyep lgevpmvvtd yptselvksa anaflatkis finamaevce ashadvqqla
      241 qalsfddrig grflnpglgf gggclpkdir afmaragelg adqaltflre vdainmrrra
      301 rmvdlarela ggsfrgctvg vlgaafkpns ddirdspald vavtigeqgg qvtvydpial
      361 dnarkahpel sygesaldav rgahvvlllt ewkqfidldp eelgaavatr kivdgrnald
      421 aetwraagwh yralgrp
//
LOCUS       WP_357664133             311 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357664133
VERSION     WP_357664133.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 311)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..311
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..311
                     /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=34159
     Region          2..287
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mpprasglpn waipyvllvp gllviaglll ypmvqlviis fqkfgiaqir gkaaewvgwa
       61 nfekvlatei fwtslrntvv fasiavtltl vvgtavgvll hklgkkmslf vvigcmfawa
      121 ippvaqaaiw rslfdadsgi vnwalnllpd wlsqavfgra dwtgepwlnd aftvyvvlvf
      181 cvvwagfpfi avsvlaglkg ipnelyeaar vdgsgawrtf rkitlpllkp vfavltvlsi
      241 iwdfkvytql hillngptnr eafnlsmyav aeafkpppkm gtgaaisivl tiilliitvf
      301 yvrqivkqee m
//
LOCUS       WP_357664140             460 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357664140
VERSION     WP_357664140.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 460)
  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 460)
  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
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..460
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=48557
     Region          5..458
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 msvtlpdllr eraeadparv amtvhgagsl tfgewerrsa gvaaglgvep gdrvglvfgn
       61 gdwleyavaf lgvvragava vplsdrlaga dveamlahcg asrtlrpgal pfaegaapdp
      121 prprdlaqil ytsgttgrpk gvaashanla ygcggrrrpf thsahlahaf pigtnagqwm
      181 lvnaldahpq vvtlprftpg rfagliehyr agtvflvpam aiemlsarvh hrhdlssvll
      241 lgsaaaplps qvavelgaaf gnatianyyt steaapaqtv mlfdpdrpas vgrpasggav
      301 kiatakgdpl pprvtgevwm rspavtrtyy gdaqasgevf rggwvrmgdl gyldddgyly
      361 lvdresdvik sgaykvstih vedvvhqhpd vveaaaygvp hptlgkavev avvgsvahee
      421 lriflkgrla phelparivt ldalprnqgg kvdkrrlrhd
//
LOCUS       WP_357664194             134 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357664194
VERSION     WP_357664194.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 134)
  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 134)
  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..134
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..134
                     /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=14964
     Region          4..127
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mqllvkhvrq aketalaevg iqdfefetlh rlvsrssrqa tpselaselm lspagmtgrl
       61 dtlekaglvr rvrseedrrr vdveltdtgh elwaaamavr ataeaemlra lapeerktld
      121 ellkrmlisv eart
//
LOCUS       WP_357664291             175 aa            linear   BCT 28-DEC-2024
DEFINITION  LGFP repeat-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357664291
VERSION     WP_357664291.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..175
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..175
                     /product="LGFP repeat-containing protein"
                     /calculated_mol_wt=18713
     Region          30..>95
                     /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 mrravtlgla atlalagavt paqaktsaca iqpygligdy wrtmggengv fgcpkatekg
       61 iansngrrqs fangqiawsp dqggrmivaa ygkdgkavvr wgptnpfhyd yfeilvrsth
      121 langtytqrt gqrirgsasf hgpdgyftfr vrgcddkplg dvcrqgwsis vstya
//
LOCUS       WP_357664297             292 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Nonomuraea dietziae].
ACCESSION   WP_357664297
VERSION     WP_357664297.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 292)
  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 292)
  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 292)
  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..292
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..292
                     /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=28392
     Region          120..>292
                     /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 mnglgeprgp dfrsgalpgl qqgppppspv adgrvaaapr grllvtaalv aaltggaagv
       61 agarliegse papaalprvp aaqapgqgqn qgqgrtpaqg lsataaqvlp svvsvetrrg
      121 sgsgfvidgs ghvltnahvv glstsatvvl ndgrrlsatv vgedededla vlrvgdasgl
      181 tparlgrsse lavgdqvlai gsplglsgtv tagivsaldr evglggsskr tavqtdasin
      241 pgnsggplvn argevvgvnt aiatsrgggn igigfaipid raapiaesii rn
//
LOCUS       WP_357664306             380 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357664306
VERSION     WP_357664306.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 380)
  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..380
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..380
                     /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=40528
     Region          18..379
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 matfvivgag lagakaaqtl reegfdgevv ligaeeerpy erpplskgyl lgkserekif
       61 vhppywyadq eidlrlgvtv tgialdahev alddgsrmsy dkllittgas prtlpgqayt
      121 lrtvadseal kagfaaggrv viigagwigl esaaaareag cevtvvepep tplhrvlgpe
      181 lgevfasvhr rhgvdlrlgv saeaveadgv rlgtgerlpa dlvvagvgaa pnvnlareag
      241 levgegiltd aalrtshpdv yaagdvaesy hplygrrlrv ehwanalngg paaarsmlgq
      301 evvydrvpyf ytdqfdlgme fsgdttgydq vvtrgeelef iaywlregrv iagmnvnvwd
      361 vvddiqrlir sggplpspqg
//
LOCUS       WP_357664342              69 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Nonomuraea
            dietziae].
ACCESSION   WP_357664342
VERSION     WP_357664342.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 69)
  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 69)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..69
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6886
     Region          1..69
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mststykvtg mtcngcagkv ktqignvagv sgidvdlatg hvtvtsagqi ddvrvveave
       61 eigyeavlv
//
LOCUS       WP_357664349             147 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora chersina].
ACCESSION   WP_357664349
VERSION     WP_357664349.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=14774
     Region          3..135
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 myvsaradya lramlavada agstgdggsg agelvkaasl aerqdiplsf lqgilldlrr
       61 agllhshrgn eggyaltrpa adisvgdvlr avggaltsvr gmpadhagyh gvaaglrdvw
      121 lavdgaialv vdrttladll adraaas
//
LOCUS       WP_357664376             382 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357664376
VERSION     WP_357664376.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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..382
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..382
                     /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=41394
     Region          1..355
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 msvpvvlvsg lhaearstlv drllaehpgs vavhhdlgev gagrverivr dasgvldrql
       61 vrlahgcvac tvredlipel laraaggapl liaelwdsve pravaealaw hedaahalrv
      121 tgvltavdae gltedlccde rlatrgkraa adderylaev ltrqieyatg ivvsgadqed
      181 ielaltvlgh lvpttpadvl tlpqvtgrrv dvemlaarvd pataqlpcqa htgeistvvw
      241 hrlrplhpqr lfdavdelvt qtvrsrgrfw lanrhdrlla wdavagivsi edagpwlval
      301 peaawelvsp arrmaatldw ndilgdrvqh lvftgpnldq erilslldsc llteqealag
      361 sdvwadypdp fafvldlket ta
//
LOCUS       WP_357664388             356 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357664388
VERSION     WP_357664388.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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 356)
  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 356)
  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..356
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..356
                     /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=37822
     Region          1..355
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrvgvigaha srgwaraahl palsslpdye itavastsqe sahqaadvwg akhaftdpqe
       61 liahpdvdlv tisvqlprrd glveaaisag khvysewpla rsaeaaerlh tlaeqagvrh
      121 avglqsrhhp aigylrdlva dgkvgevmsa sltyslsspe vwsmryadlf dhtkgvnhla
      181 vvgghsmdmf gsavghftei satlatripr itlqetgeqi tvtspdqiaa vgllesgaaa
      241 svhimtggpr gegflievhg ragrlvldsa ddslvgpeft lsfsdgpggt vvlsvpdryy
      301 pmpsdappav rnvhqvyknl aagipsepdf rtavrthrli daikrssttg erqrlv
//
LOCUS       WP_357664439             292 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Nonomuraea dietziae].
ACCESSION   WP_357664439
VERSION     WP_357664439.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=30538
     Region          42..286
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mfkatrrrsa vlaalvaagl alapaataaa taaapgagyp aiiggravte pysfmvsfql
       61 rsepghhcgg sliasdwvvt aahckglmkp grtqvrvgsl hkekggvvts vkrvvthpgw
      121 rqrgghgedn qsdimlvqld rkvplqpirv addpgkvsqp trvigwglvc edgedpacep
      181 rqlqeldtvr vsdgkcsdla rgaelctgds rgraasacng dsggpqvrmv agrweligat
      241 srdgddyedr rdggagcstn pdggpgvgiw tdvthyrtwi dkivgaelhd as
//
LOCUS       WP_357664409             125 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357664409
VERSION     WP_357664409.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 125)
  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 125)
  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 125)
  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 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   5  (residues 1 to 125)
  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 125)
  AUTHORS   Rosinski,J.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..125
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..125
                     /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=13051
     Site            order(25..26,28,31,34..35,38..39,42,72,91..92,94..96,
                     98..100)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Region          25..96
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(26..27,31..33,46..48,57..60,62..63,66..67,69..70,
                     76..78,83..85)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(46,49,91)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 maindggrcv sadiaaglpp aaalfhslad ktrlrivarl argearvvdl tgelglaqst
       61 vskhlaclrd cglvdyraeg rqsfysltrp elmdllasae qllsatghav alcpmpglae
      121 qprps
//
LOCUS       WP_357664444             306 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357664444
VERSION     WP_357664444.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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 306)
  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 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
REFERENCE   5  (residues 1 to 306)
  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..306
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..306
                     /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=32744
     Region          2..302
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mnvllagatg tlgsvlvrhl laaghtvlgi trsgggarrl aeagavpvva dmmdrealla
       61 aldgrqadav vheataitgl plfhralyat dalrdrgtah lleaaklvga hrfvtqsffl
      121 gygyrdhgea pvteerpfae pgqgafdphm rsmraneeqv fgtpgiegis lrygmfygpe
      181 astrklmdmt rkrmlpapep agtvslihie daasatvaal ergvagrpyn vaddhpvrfd
      241 dyvralaaaa gapaplrlps allrpmpymy vlmvgtrirl sserakrelg wapaypsyre
      301 gltfst
//
LOCUS       WP_357664453             113 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357664453
VERSION     WP_357664453.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=12139
     Region          1..101
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msgpvaaqdv lalfaqtrpl ftalgderrq eiivfllest dprsvgeiaa hlnlsqpaas
       61 hhlkilrdar lvtvrrsgtq rlyalnaady pqlltplrdl atlivscata spp
//
LOCUS       WP_357664463             382 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357664463
VERSION     WP_357664463.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 382)
  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 382)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 382)
  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..382
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..382
                     /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=41697
     Region          132..382
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mhdpteyqpp ldrlgtalry lfaalpllfy gillvsmgdr apsaqdlprs mlldmglgai
       61 alvlmrwrrr wpwqvalata lltvisftat apacvayvsl cthrrwrqlv pvavvfwlcl
      121 vastrwqgpg qltvfygvvg alalggltvl glhlrgrrdl aasrraaera aqlqrveqaq
      181 laerltiaqe mhdvlahris llsmlaggla yrkdltaeqt revalaiqen ahqslnelra
      241 vlgtlrresv veapqptlah ldtlfdevra agqqvevdda ihdrdllpaq tarhtyrivq
      301 ealtnarkha pgsrvtaelr grpgddlrit vsnpvppgtp agpggklglv glaerarmag
      361 gtmshavrng rfvldarlpw ka
//
LOCUS       WP_357664468             125 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            dietziae].
ACCESSION   WP_357664468
VERSION     WP_357664468.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..125
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12820
     Region          17..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maprpgtpvr gsttgrpima amdllgrrwa lriiwelrdg pvgprtllsr cqglsssvly
       61 qrlgeltsaq vvasssdgye ltplgaslgh alaplgswat twaealsprg statsqpppa
      121 gggda
//
LOCUS       WP_357664461             237 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357664461
VERSION     WP_357664461.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   ter Beek,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 237)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..237
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24778
     Region          2..234
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 miefnnvskv ykevkalddv sftvepgsvt gflgpngagk stamrilagl srptsgsatv
       61 lglpygeldr pafrvgtlld agaqhpgrtg reiltlgaiv lglprsrvdd ildlvgltar
      121 qgrqtvggys lgmrqrlgig hallgrpeal ildepangld phgiqwmrgl lrdlagsgcs
      181 vllsshllhe veqvadrivm idrgrvlaqg tvgelsggrg leqafldlta nagrsta
//
LOCUS       WP_357664498             309 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357664498
VERSION     WP_357664498.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..309
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..309
                     /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=33766
     Region          12..307
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mslltrtegp vrravpapsv grmrwwtpya flapylalfa vfmvvpigfg fwtslhewdi
       61 nlpakpfvgl gnyadlfdpg svdgsrfwta mratgiftva svpilivlpl avallmngrf
      121 rgrnvyravy fapyvlgvav vgfvwrylld gniglvnhyl gldvqwttdv ppvwialvgv
      181 tvwwtlglns viflaglqdi prelheaamv dgasawhrft avtlpglrpv tvfvvnatil
      241 asanmfgqsy litagapadq tktaiyliae tglrqfdmgt asamsfvlat flmlasalvf
      301 gafrdrrtp
//
LOCUS       WP_357664530             253 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357664530
VERSION     WP_357664530.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=27878
     Region          28..153
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtalsnlvrp dvyprsslyd pawlvgldmg pnplwlledl sadlelkpgm rvldlgsgmg
       61 atsvflaref gvevvaadlw vaadtaaavf aeagvadrvq avnaeahalp feresfdaii
      121 sidsyeyfgt adgylayitr flkpggqlgi atpgmtreir elgaipphik alvgweaiaw
      181 htaqwwrfqw eitelvtvts arlqrdgwnd wllwaracle hrpdgreaae qtiamletdq
      241 geflsfalvt ark
//
LOCUS       WP_357664532             171 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357664532
VERSION     WP_357664532.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 171)
  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 171)
  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..171
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..171
                     /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=18615
     Region          33..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mndhrelrhl dpatgaaven aaaalvavwa ssrqtaatkv ssiqmqallt ierhqevnla
       61 rlgealgalp sstsrlcdrl eatgwvrrsv spddrrelti gltpsgkall eelrarrrdd
      121 laqvvdempp earkallrgl raftaaadrv taqrsdrsdd nwtiiagrfl a
//
LOCUS       WP_357664616             370 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora chersina].
ACCESSION   WP_357664616
VERSION     WP_357664616.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 370)
  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..370
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..370
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=39664
     Region          24..313
                     /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 mkpaalwpdh llpahhvppp wpgrnvrldg tvtyvrdtpa tapgaepaly vhglggssqn
       61 wtdlagllad rldgqaidlp gfgrsepgrr ytvpafadrv vrwiehsdrg pvhlfgnslg
      121 gavtvrvaal rpdlvrtltl ispalpfldf rrslqgrmlp llaiprgerl aawrlaqlap
      181 evmaqqvmea ciadltrise qrrleaveei rvryeaahya aayvrtfrgl vssflraylp
      241 gsgslwrlas avrvptlvvg grqdrlvdvr vapqaarvip dsrlmlldgv ghvaqlevpr
      301 tvaravlall aeaspagspp ggdrtsaaqp gaergpgevg arsateraeg qaseliaetg
      361 esgrrrdmag
//
LOCUS       WP_357664621             382 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora chersina].
ACCESSION   WP_357664621
VERSION     WP_357664621.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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: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=41589
     Region          149..284
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            order(177..183,205..206,232..234)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mpepldaals evrallldpa ltravaagrr rgqrpsvvra elrpvtlkgg prlqistsdg
       61 arpytrnvap gaeagtavda llaepfgnwh vetadstiql rvtksgeaqv hraaasrpap
      121 epgghdrakd wlldpgdpif aeiggsaakr rqvdaflral aatlpddltg plrvvdlgcg
      181 nayltfaahr ylsqrgldvt lvgvdvredq rrrntelaer lgwadrvsfv agtildaqve
      241 papdlvlalh acdtatdeal aralrwdarw vlaapcchhd vaaqlrarpa prpyelltrq
      301 gilrerfadv ltdalragll rlhgyraevv efvdsrhtpr nllirarrtg saptgdqrae
      361 yrelvdqwgv tprletllad ra
//
LOCUS       WP_357664645             727 aa            linear   BCT 28-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Nonomuraea dietziae].
ACCESSION   WP_357664645
VERSION     WP_357664645.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 727)
  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..727
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..727
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=76764
     Region          14..725
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtqtastgta gpetagrvqq gvgesagrpd atlkvtgefa yssdlwlegm vwgvtlrsph
       61 asawirsidi gpalaiqgvl avlthedvpg ekfyglehkd qpvlaidqvr yqgepvalva
      121 aehpetarra aaaivvdyev reavtdprla tefvrrqpvr vgdtfeaevv vtgeyevgmq
      181 dqaflgpesg lavpaedggv dlyiatqwlh vdrdqlapcl glppekvrls lagvggafga
      241 redlsmqvha cmlalrldrp vkivygrees ffghvhrhpa wmryehgatr egelvyvkae
      301 illdggaycs sspavvgnaa slgvgpyevp nvdivatgvy tnnppcgamr gfgavqacya
      361 yesqmdklaa acglspveir vrnavsqgsa latgqiidsp apladmlrel eamplpaaat
      421 sdlrdlpggv sqtthgegvr rgvgygvgik nicfsegfdd ystarvrael iggephvtvh
      481 taaaevgqgl vtiqaqiart elgiervnva tadtrvgsag sssasrqsyv tggavkaace
      541 avrerfnglp aalalekfgp ieetreyrhr ptypmdpvtg qadshtqlal cvhravvdvd
      601 velglvkvve laavqdvgki lnplalegqi hggsaqglgl almeeiqvre gkvlnpsftd
      661 yliptildmp pvrlsilenp dpaapyglrg agepptlsst paivaavrda tgvaltrvpv
      721 rpehlvg
//
LOCUS       WP_357664694             177 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora chersina].
ACCESSION   WP_357664694
VERSION     WP_357664694.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 177)
  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..177
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..177
                     /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=19429
     Region          27..177
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mgsqpsapag padvltrsrd tpphlpfeqf yrdhvdrihr alalavgdta vareatdeam
       61 arayarwdrv rrldnpggwv frvglnwats wwrkvrrerp paedrhpaaa apdpaglaar
      121 salellplsr rtvivcrvll dlstaetaav ldltegtvrs rlsrglaelr aalaeee
//
LOCUS       WP_357664755             328 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora chersina].
ACCESSION   WP_357664755
VERSION     WP_357664755.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=36698
     Region          18..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavqldarpp vqpahrvtrp frgvrlsrfd tkyspylyva pffllfgvfg iyplvytfwv
       61 slhdwdllga ehpfvgldny sqllgdpdfw hsvvntlgif vistvpqlll alwlanllnr
      121 qlrarttwrm avlipnvtst aavaivfavl fgrefgminw lldhvgvdai dwkanrlasw
      181 vaistmvdwr wtgynalifl aamqaiprdl yesasidgas rsrqfwsitv pllkptiifa
      241 viistigglq lfteprlfns gtnairggpl resqtvtmym fenafaphyn fgygsaiawl
      301 lfaliavvaa invlllrrlg ggarkeds
//
LOCUS       WP_357664716             464 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Micromonospora
            chersina].
ACCESSION   WP_357664716
VERSION     WP_357664716.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..464
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46397
     Region          78..463
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mgrvartpsp rlpaarrprl vtallavval tgataascgd drsavtvaqv grsavtevid
       61 apatvtaraa atltapadgt laslrvqpgq rvargqvlav idspsardrl tqarealraa
      121 kragrgvggg dlggrrrdtd raateafaaa rkaagkigdp qlraalllqv esaqeqyasa
      181 araadravsa vqrgvaglns avgalstaqr lqaqqaydla katvdaltlr apipgvvqpg
      241 gtraatptdl tgllgaagga vpgldpsalg aagqggppag vddavpaggr vtagtpvltv
      301 vdtgqlglla evdetdvllv raglaatvel davtgatyda tvrsvdmlpt ssarggvtyr
      361 vrlglgagrl gegeaapapr pgmnavvhlr vreaadavav pasavfnadg rdavwllrdg
      421 kadrvpvtvg vqgqdlvqiv sgvragdriv vrgadqvhdg qelp
//
LOCUS       WP_357664811             391 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357664811
VERSION     WP_357664811.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 391)
  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..391
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=42490
     Region          145..391
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnveyrwllp svllgdpdeg rparrstrdw vvdilifllt cglvwltlpd legegralrv
       61 teqvlgglsc aavwlrrrwp vtlslvatvf ssyfvmvgga avvalftvav hrpfkisglv
      121 laanlitlap lalwrpdkvl gplwmavfgt vlalaafgwg ivvrsrrqlv htlraqaqva
      181 gqearrlere riaremhdvl ahrisilslh agalefrpda ppeqvaraag airdsahqal
      241 qdlrevigvl rqpgdapdei vperpqptla dldelaeesr ragmdvtltv eagqeppasl
      301 grnayrivqe altnarkhap gapvrvsvtg gqgegltiea rnkigwpssi pgagsgligl
      361 teraelaggr lehwrtpegd fvlkawlpwp t
//
LOCUS       WP_357664913             993 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357664913
VERSION     WP_357664913.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 993)
  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 993)
  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 993)
  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 993)
  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..993
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..993
                     /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=107739
     Region          1..244
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          110..993
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          705..733
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(706,709..710,713..714,716,746,749..750,753..754,
                     756..757,780,789..790,793..794,797)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          744..774
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          779..813
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(866,869..870,873..874,876,900,909..910,913..914,
                     916..917,946,949..950,953..954,956)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          866..893
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          898..934
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          945..972
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfgilgplr vgdgestita grdrtllaml llragrmvpv eelvdaiwee rppatartql
       61 qicvsrlrqr fvalglpsem ivtdpvgygi rvapsdldae vfaqsveagr savdagqpae
      121 asrhyraala lwrgsalsgi asrsvrrraq aldeqrltvl eecvevelrl rraadlidel
      181 sesvernplr erlrgqlmla lsavgrqada ltvyregrri faeelgiepg talqelhqrv
      241 lagdlavtap qrpapspvra lpraisdftg rqdtlarlvk eieehdarih lidgmagtgk
      301 ttlavhlaaa lagrypdaqv fidlhghser epvtpaaala allrqlgvpa agipadader
      361 aalwrselsg rraivvldna asavqvapll pngpdcltli tsrrrltgld ggrpsslavl
      421 dpdeavella rvvgvdrvaa epeaaaevvr rcghlplair lagarlahrp rwrvrdladr
      481 laagrnplie lsvgersvgq afdlsyaqld paaqrlfrll gvhpgaffdh qvaaavtdlp
      541 ladaqdlldg lvdahlleep dpgrfrfhdl vrdfarqlld gagrpgerae avrrlldhhl
      601 haayaisrem epaasraalv lpepprpdlv tvcvtegpaw fdrnrstlpa lvrlaagegl
      661 lahcwqlarv swyflfsrgh ldelidthtv glraaercdd eaavattrny lasglfrlgr
      721 fpeaidlmeg alqirrrlgd regeatvrrn laiaygadwq lapalahlda aldlarstgq
      781 paavaallnn qvvvllawgr yaeaqavsrr hlalgrevgd lnsvrnaigh lgaararlgd
      841 lsgalrflrl alrlkrregn rfgegevlne lgvierklgr peaaaalhre aliavtasgd
      901 rvlgclsrnl laralleqgd vrsaldlyrr vlrdavrlra rheeaealag iarcqrptdp
      961 aaarshatra ldllrqldap erdevaalla elg
//
LOCUS       WP_357664951             384 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357664951
VERSION     WP_357664951.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 384)
  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..384
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=41278
     Region          145..383
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 midlrgitdl wrrcdvvvrd lpfglllava sllpalhgkg tqvgdlparp fdaaafvvia
       61 leclplavrr rwpavclalv slgfvldqlr gyhvlasnam pialisagah lerhrrvtvv
      121 llsmayvpla lalgrlgate rvegyvvfyl alalawgiga rlrstraaea errrhvaeat
      181 raaertriar elhdvvthhv tamvvqaeaa ryltaapdrl datlsavtdt grraitdlrh
      241 mldllkadhd tdvsmpsage lrtlveqtrq agqpvefaee grpaesagsa efvtyrvvqe
      301 altnalkhah gsptvvrvry gekeisvevs tddpgsravs pggsgrglag lrervdalgg
      361 efsadrqasg gfvvraripa esrs
//
LOCUS       WP_357664960             377 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357664960
VERSION     WP_357664960.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=40739
     Region          4..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 mnttptpria iigagpggli carilqqhgi taavydrdag paardqggtl dlhadngqia
       61 lreaglleef frlarpegqe mrqmdpagti lfhhvpeqge rfkpeidrgr lrdllldslq
      121 pgtvrwghal rtvsgpaegp rqlhftggtt ieadlvvgad gawskvrrav sqatprysgv
      181 sfleawfhdv atrhpdiael vgqggaaaad gdrglfaqrn sgdhirvyii qrvpadwita
      241 sgltpqatdg iralllaryr dwsprlrqli tdndgpyvdr pifalpvpha wehnptvtll
      301 gdaahlmppl gvgvnlamld acelalaiah hdtideaiha yektmlprst emaqlldgaa
      361 dellstelpd fatadnq
//
LOCUS       WP_357665017             326 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357665017
VERSION     WP_357665017.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..326
                     /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=35721
     Region          3..326
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtllelsgle khfpvrggfp irrqigrvha vdgvdltvha gqtlglvges gcgksttgrl
       61 aarlleptag rvlydgrdis hasrrslkpi rpeiqmifqd pysslnprht vgaiirgpmd
      121 inglnpkggr earvrellei vglnpehvnr fphefsggqr qrigiarala leprlivade
      181 pvsaldvsiq aqvvnllgrl qrelgiaflf iahdlavvrh fsqrvavmyl griveigdrt
      241 slyesprhpy thallsavpe vavdgggrer irltgdvpsp idppsgcrfr trcwraqekc
      301 alttppltrl qgdrdghlta chfplp
//
LOCUS       WP_357665025             229 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora chersina].
ACCESSION   WP_357665025
VERSION     WP_357665025.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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 10130767
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..229
                     /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=24403
     Region          34..189
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mtrppgwldp lldrlgtara edftrlatpe sggresavlv llgeepaagp dvlvlqraat
       61 lrnhagqpaf pggaadpeda dasatalrea neevdldpas vtvlaelpkl wipvsdflvt
      121 pvlawwhdph pvhprepaev ahvarlpiae lvdpenrmrv rhpsgwigpa fsvrgmlvwg
      181 ftagvlntll emggwarpwp rsrvvelppt gtapapsagt davdespvr
//
LOCUS       WP_357665043             533 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Micromonospora chersina].
ACCESSION   WP_357665043
VERSION     WP_357665043.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 533)
  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..533
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..533
                     /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=57139
     Region          21..531
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mstldsaidp sspthranre allerlaele stldraragg gekyvtrhhr rgkllpreri
       61 ellldpdspf lelspvaayg tdfpvgastv tgigvvegve clvvandptv rggavnpwal
      121 aktrrageia lanrlpmvnl vesagadlpt qaeifipggr vfrdltrlsa ariptvsvvf
      181 gnataggayv pgmsdytimi rdrsqvylag pplvkmatge vtddeslgga tmhatrsgla
      241 dflaederdg irlarqcvrr lnwrkqgspp rnpvpqppky dpeellgias adlkvpfdpr
      301 evlarvldgs efdefkpnyg talvtgwgel hgwpvgvlan argvlfseea qkaaqfiqla
      361 naadtplvfl qnttgymvgt eyeqrgiikh galminavsn skvphltvnl gasygagnyg
      421 mcgrayeprf lftwpnaksa vmgpaqlagv lsivarqaaa argrdydeds daamrmmveq
      481 qiesqsgalf lsgrlyddgv idprdtrtvl glclsaihsg pvkgadgfgv frm
//
LOCUS       WP_357665053             359 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357665053
VERSION     WP_357665053.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 359)
  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 359)
  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..359
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..359
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=39752
     Region          5..354
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mrdlaatmtg fartlraagv gaghertqnl lralghldva rredvywagr ltlcatpddl
       61 prydrcfaay fggkraargl traatvtrhl aggegegerg qeavlatasp vevlrqrdva
      121 alseaeraev hrmlallrgr rerrlsrrla psrrgrldqr rtirealrkg dvarlrhrdh
      181 ttrprkvvll vdvsgsmapy aetvlrfaha martepratr vysigtrltp isvelrhrdp
      241 gtalaevsra ipdwsggtrl geelrelltr tsvrgaivvi asdgwergdp allgeqmarl
      301 arqarrviwv nphkghedyq pltggmraal pfiddlvagh slaafeelse rlsharrpa
//
LOCUS       WP_357665107             247 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            chersina].
ACCESSION   WP_357665107
VERSION     WP_357665107.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=24771
     Region          5..246
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtgvldgkva lvtggsrgig aavalrlare gadvaltyer radraaelve qikavgrral
       61 avpadsadpa aaraavdrva gefgrldvlv nnagvfltgp vtelgsdeve rtiavnvrap
      121 fvfaqaavgh ltdggrivni gsnvaeravf pglalysmsk tallgltrgl arelggrgit
      181 vnlvnpgptd tdanpadgpn adairgftal gryaapaeia avvaflagpd ggyvtgatin
      241 adggftg
//
LOCUS       WP_357665159             312 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357665159
VERSION     WP_357665159.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 312)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..312
                     /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=34059
     Region          25..302
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matipleaeq rrtappprrr gptsnraagi flapfavlfv vfflvpitya vnesfyqvkr
       61 sglgfgtper vfagldnfta vfadgsfmng igrlllfglv qvpimlglal vlallldsas
      121 arfkrffrlt yflpyavpgv iaaivwsfly tprispladl lpfdflsdsv vlwsmanivt
      181 wtwvgfnmlv iyaalqsips slyeaaeldg aggwktawyv kvplvrpslv ltgvfsiigt
      241 lqlfnepmvl sritpavgkd ytplmrslqv aldnndygqg taialmlavf aaglsslfir
      301 lsawltargv nr
//
LOCUS       WP_357665164             580 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Nonomuraea dietziae].
ACCESSION   WP_357665164
VERSION     WP_357665164.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=63977
     Region          10..326
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mrnftidgda frldgeefrv lsgalhyfrv lpeqwshrlr mlramglntv etyvpwdlhe
       61 prkgefqrle elaafldaaa vegllaivrp gpyicaewdn gglpswltae lglrartrda
      121 eylshveryf eevvpliaer qvtrggnvim vqveneygsy gsdalylrhl tddlvahgie
      181 vplvtsdgad dfyltggavp gvlatvnfgs epeaafaklr ehrpegplmc mefwcgwfdh
      241 wghghvtrdp adaadtleri laagasvnly mahggtnfgt taganrvgel sdgeyrpttt
      301 sydydapide rgaptekfwr freilsryns dipdlpplpe plpatrvplt gsvglrdald
      361 qlagpsvtaa lppsfedlgl thglvlyqve vpgprrpyrl rvrgvhdrah lyvdgeqaav
      421 lerggeepvl evagparlev lvesmgrtny gpalgerkgl mapimhdrqy lhgvtarpvp
      481 lrdlpalpyg eglsaavpal frgeleverp adgflalpgw gkgyvwvngf llgrywdrgp
      541 qrtlyvpwpl lraganeivi leldragepa leirpaaelg
//
LOCUS       WP_357665166             289 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357665166
VERSION     WP_357665166.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=31261
     Region          37..280
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          193..276
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mldgrermae dfrrwmhylt pgpahrrlgl vclgvghleg rlptvgpral dhhvavvvtq
       61 gkgwfsqage epvevvapsv lwllpgvrhh yaphddtgwt ewfvdftgpa atayqdlgfv
      121 davspvtplt taepaahgig riahairrgs pylevetsal vhevlvalrh arvdedaagd
      181 pvltglarda clpisvaeha rrlgmtvadl rvvvrrlagc spkdyllsir ltrakdllag
      241 selpiasiar rvgyddpayf triftrragl ppsefraqqh ggpasagls
//
LOCUS       WP_357665365             363 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea dietziae].
ACCESSION   WP_357665365
VERSION     WP_357665365.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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..363
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..363
                     /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=37960
     Region          121..360
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrqlaiaass gvllmlpmft gtshavaapp dyvyaeplak sdaemrkvae ywkperlkda
       61 dsyspatpgt kssapsssps sspssapsss agsvvtngvs rqaaardiqp tapvkggaak
      121 tigkvffqlg gkeywcsasa vaaknrslva taghcawdpr lgksanwifv pspgkdgdap
      181 ygiyvgstlh mhedwaaigd ydydyafisv hhgfrwtted gkavmkdvgr lednvggqgl
      241 tvgkktgnqv aafgypagaq pdgsqpfngr tlkscegktk rtvnptrnlq ygvllagcdf
      301 sagasggpwm lgyrastglg vlngvnsltw nldaaakyda vsspyftptt fevydqaand
      361 att
//
LOCUS       WP_357665386             239 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357665386
VERSION     WP_357665386.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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
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 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..239
                     /product="PadR 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=27403
     Region          19..97
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          60..>191
                     /region_name="PHA01972"
                     /note="structural protein"
                     /db_xref="CDD:222842"
ORIGIN      
        1 mspvfghgrl rlyllkllee sprhgyevir llqdrflgvy spspgtiypr larleeeglv
       61 thevvdgkkv fsitdkgrde lnsrldelad leqeitdsvr diarevkedv retvkslree
      121 ltamardvkr nsreqqaadl krlkdqqkrq wmdhaahwqd qgerlsrqwr svwsevwsdl
      181 ggagdnrael daelgellad fvatvreqas dsrltrekle qcraaldeaa arirdslrg
//
LOCUS       WP_357665457             281 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357665457
VERSION     WP_357665457.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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
REFERENCE   4  (residues 1 to 281)
  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..281
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..281
                     /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=30919
     Region          25..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          190..272
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mthdwsrywr spdkpleamh ahfvrhvyhr hshdtysfgv tedgaqafkc rgsahtsaag
       61 mvmafnpddp hdghaadqlg ftyrilhigt elvadaledt tgrrtglplf aepvlddpll
      121 arslhalhla llggasalrr dellratlaa mvrrgsrslg apdarrpapg gtaliaervr
      181 nrlddshldd ltaadlaesa gcsrftvyra fqtvygmaps dyqrqlrlrt arrliaeglp
      241 lgevaaqagf adqshltrwf trtygvtpgt yrestdprpa r
//
LOCUS       WP_357665506             315 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357665506
VERSION     WP_357665506.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 315)
  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 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   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..315
                     /product="GlxA 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=34020
     Region          2..315
                     /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 mhrvvvlald gvipfelsla srifgtargr yevitcsldg gpvrtdadfs iavehdagvl
       61 atadtvvlpa aewfgdvrgp adlppaliea lstvrrgarm vsiclaasvl aatglldgrp
      121 atthwahaee fqrhfpevrv apevlfvddg dvltsagaaa gvdlilhlir rdhgsqvanq
      181 varrcvvppw rdggqaqyie rpvpepassg tadtrqwalt rlhepllldd magharmsrr
      241 tftrrfreev gmspgqwlig qrvelarhll essdlpvdqv aeragfgtaa slrqhlhavv
      301 gvsphayrrt fagra
//
LOCUS       WP_357665536             188 aa            linear   BCT 28-DEC-2024
DEFINITION  flavodoxin family protein [Nonomuraea dietziae].
ACCESSION   WP_357665536
VERSION     WP_357665536.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..188
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20381
     Region          5..181
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 maerrflflm gsarpggnte alaraaaehl pegagkrwlh lddlplppfr dvrhadggvh
       61 papvgnervl leatldatdl viasplywyt vsastklyld ywsawmrvpg vdfrkrmagk
      121 ttwaisavsd ddlavadplv gtlrlcaeyf ggrwggallg fgnrpgevan dhdaltrakt
      181 ffttratg
//
LOCUS       WP_357665562             257 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Nonomuraea dietziae].
ACCESSION   WP_357665562
VERSION     WP_357665562.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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..257
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..257
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27072
     Region          6..251
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mgefarvevs dqiatirldr pkmnalngqv qreiaecara vdadqgvhav vvyggervfa
       61 agadikemad rsyadmvahs rtlqdcftal arvgkpviaa itgyalgggc elalcadfrv
      121 agesaklgqp eiqlgiipga ggtqrlprlv gparakdlif sgrhvsaaea leiglvdrvv
      181 pdvdvytaal ewaatfvggp tvalraakqa idqglevdld tgleierlqf sglfatddak
      241 igmhafteks kpkftgh
//
LOCUS       WP_357665563             322 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora chersina].
ACCESSION   WP_357665563
VERSION     WP_357665563.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  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 322)
  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 322)
  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 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   5  (residues 1 to 322)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..322
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..322
                     /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=35602
     Region          1..236
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          242..315
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maitlrfgaa dllrcrfais pmletlsalr llspregvgp hrrwldtldt rgldlrpial
       61 lqprrgytpd flspppvsph arfedelaav aatdldrvra evrrsladtp gaaesatgrl
      121 llgdpavvlq tlvslvkqaw evlvepvwph vrglldadvg fqtrrlaegg ldrlfaelhp
      181 rlrwnngvlt reygddehrd lrgeglalvp safkwdqvvv ivdppwqptv iyparglgtl
      241 wqplstdrha algrligrtr aallfnldep astttlahrh alaagtvseh lsvlrdagfv
      301 sgerhrheir yrrtplgeaa lr
//
LOCUS       WP_357665576             769 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357665576
VERSION     WP_357665576.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 769)
  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..769
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..769
                     /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=78641
     Region          8..252
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,31..32,61,66,71..74,86)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,35,37,69,85..88,92,94,131,133,
                     135..136,138,147..148,151,168..171)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,35,37,69,85..88,92,133,135..136,
                     138,147..148)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,92,94,131,133,135,151,168..171)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(147..155,164..171)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mnddrlgpyr llrrlgeggm gvvhlavdpq grqvavkvlr aevagddvar rrlsrevdtm
       61 rrvrskyiae vldadvtghr pyivtryvag rpldevvkqd gplelpalar vahgvasala
      121 avhsvgvihr dlkpgnvlil dgdpvlidfg iaqavdatrl tqtgmfigtp gylapeiieg
      181 heagpevdih awagtllfga tgqppfgkgt lemifynita gkadvsaapr elqpllkaaf
      241 qrnpskrpka adlaeqtarl lpksakvvde vstvprpdrp gsrpvtdpad vptpaippar
      301 pplgqpslsg pyggaapmsg agapgsqefv sllgnqapsg pstgghgpvg pstgghgqpg
      361 pggptgpgsg ghgatgpgsg ghgpsgsgpa gehattggdp wptrrvtpee lrqmreeggv
      421 pahpwdvptr asteppssrp wpgnqaghsa phvppgapnp pggfpsagha ggfpasggqs
      481 pgfptpggqa sgfpaqggqa ggypgappyp rdgdiptrrv rpdapdyprg aqqpygqqyp
      541 qashpahdpe twrepripga rpglalqrsk aygvagamll vvmivlavla plivsavaip
      601 favllraadl aqpqlnarrs tgsaaadvlr vfaqpaallk sigitvalvp yalilglpvt
      661 llltvlvhsm planalawgg aialwtvcag pgveapgrqm rrtlaslvps rtvamvtagv
      721 lavgaalslv lalgtvpesg rksvwapvdv spltdrlmdl rgkagqggg
//
LOCUS       WP_357665621             324 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Nonomuraea dietziae].
ACCESSION   WP_357665621
VERSION     WP_357665621.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..324
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=32955
     Region          1..322
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mqlrilatia alsiaaltgc gdqgtggsgg tgalrimapa avgggwdqts rtaeqalksv
       61 dpqrkvevfn vpgaggtigl aqlagekgng nmlmtmglvm vgaieqnksk vtladttpia
      121 klteeyeivv vpadsplktl adlvaawkad pakvsvaggs aggtdhilag lmakaggvdp
      181 kqvnyiahsg ggealnallg nkvtigvsgv gefaehvksg klralgvssp sridsvdapt
      241 lkegglnvel anwrgfvapg glsdadkksl tdlvtkmhds qawkdavakn gwidafqtgq
      301 qftdylnaeq trvkaviaem glvs
//
LOCUS       WP_357665671             212 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Nonomuraea dietziae].
ACCESSION   WP_357665671
VERSION     WP_357665671.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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 212)
  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 212)
  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 212)
  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..212
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..212
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22597
     Region          57..207
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 merrgrskmv gafvalavla gmliiaglpk gsaaqdvklv rradgsmlla rpganapvld
       61 lfedfdcpfc kelhetsgrr leqmvgegkl avvfhtvtif tdepsrsnsi raaaaarcvp
      121 sanwlafrdk lygmqpaphg qatgytveel vaagrsagvt dagfeqcvts qrhagkhled
      181 nariridgtp tllldgrpir dlsaieqqgt sv
//
LOCUS       WP_357665726             391 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            chersina].
ACCESSION   WP_357665726
VERSION     WP_357665726.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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 391)
  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..391
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..391
                     /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=43296
     Region          1..379
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mklvvqvkll ptteqatale atlracnaaa cdvaqlardv gcyrnydlrr hvyqgiktdy
       61 glgaqaaqhv ikkvadayat ltanlkagry gkpgskrrsr veanpvrfrw daaqpydarm
      121 lswqqdartv siwttagrlk nvaytgspaq lkavatsaig esdlvhrdgm wflyasieva
      181 eappyepdgf lgvdlgiani aydsdgnrya gtrlngyrrr qlrlrarlqq kgtksakrll
      241 arrtnkearh aananhrisk tivteaartg rgiavedltg irervrlrkp qrvtlhswsf
      301 hqlggflayk arragvplvq vdprytsqtc hgckhrdkrn rpdqetftcr scgvvahadr
      361 naalniaerg veswgavnrp hvaspcsqrg v
//
LOCUS       WP_357665745             166 aa            linear   BCT 28-DEC-2024
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Micromonospora
            chersina].
ACCESSION   WP_357665745
VERSION     WP_357665745.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 166)
  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..166
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..166
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17715
     Region          24..>120
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mtlapggrpt dptghgaggi rgftvlydah cplcraarqw lasraqlvpl efvpagsaea
       61 rrrfpgldhd atlrdltvva dtgavyagdg awfaclwala dhrataerla rphllplarr
      121 mvttasavre lvreprpdpg ygddddradc addrcgrpeh rgdgpg
//
LOCUS       WP_357665773             299 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357665773
VERSION     WP_357665773.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..299
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..299
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=32510
     Region          30..>175
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mrsgrravla atlvallatp lphvaaadpd sqsklrkltk qatalntvyr gtiesledtr
       61 lsakratera anlkaalaaa rvevtqiaqt tyiqgpvdga slftsggepy qvlgqaanma
      121 ylaaertstl nrveamvada qkakkdadek iddlerdikk mqskrrdiek llakygiqqp
      181 gsasgltqrm itlrdevmrn fpmfygvgcl rvgdpgehgk gracdfmmsp ggsmatganl
      241 argdelaqwl iangsrygvm yiiwkqryyd irtgggwdmm snrggvtanh wdhvhvsvf
//
LOCUS       WP_357665778             201 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora chersina].
ACCESSION   WP_357665778
VERSION     WP_357665778.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 201)
  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..201
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..201
                     /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=22016
     Region          13..189
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtvpsqgpep pgeddlatrf rdgdeaalre aydrygravl hlatttlanr sdaedvtqat
       61 fvaawlgret fdpakgslig wllgigrrkv vdrirvatre trvvetvkql pepvstdpdp
      121 dtvvdrlvva delarlpdeq rrmlelafyd dlthqqiatv tgvplgtvks hirrgmqslk
      181 rrwevdgaap gprpaglsga r
//
LOCUS       WP_357665799             282 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357665799
VERSION     WP_357665799.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10005476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..282
                     /product="amidohydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30552
     Region          81..279
                     /region_name="LigW"
                     /note="5-carboxyvanillate decarboxylase LigW (lignin
                     degradation), amidohydro domain [Carbohydrate transport
                     and metabolism]; COG2159"
                     /db_xref="CDD:441762"
ORIGIN      
        1 msidvhqhlw ttsfiealra rsrppyldgw tlildgeppy evnpadhdar dttdlelalv
       61 slssplgief lppeeawpli dayhegalkl pepfgawaat chsdvdparl aadldrgfag
      121 lqipataepd drlldvlter dlplfvhpgp aaatpgvpgw wpalvpyvqq mhaawhhfha
      181 vvrprhprlr vcfallagla plhterliar gggrgqvdpl cyvetssygp raidaivrel
      241 gidvvvngsd apyatapdpg mgaaaahair vanprrllgr ke
//
LOCUS       WP_357665812             427 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            chersina].
ACCESSION   WP_357665812
VERSION     WP_357665812.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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 427)
  AUTHORS   ter Beek,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..427
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..427
                     /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=46351
     Region          1..337
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkrswthwar aatvgavslv mvaacsgkst tggsdaadgq itlkinfwgd fglqdlkary
       61 eadhpnikiq lnsgeynaqh edlqkklvag ngapdiaaid egfmvqfrsq sdkfvnlldk
      121 gagsyegkyl pwkwkqslsa dgrtqiglgt dvgglamcyr tdlfkaaglp terdqvsalw
      181 pdwdkfievg qrytaktnkk fidagtnlfn pilgqqqvgf yndqeqlqmd ggpkvafdyt
      241 vkavqaglsa nlvsfqadwd kgftsgafav lacpawmlgh ikdtapgtqg kwdiaavpgg
      301 ggnwggsflt ipkqgkhvde aykllewlva peqqieifkk vgnlpsqpal yadpaiadfk
      361 npffnnapvg qifprmaqgl tpqylgkkng ptrvavenvi rrvenkslkp daawgeavke
      421 adkaars
//
LOCUS       WP_357665814             337 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora chersina].
ACCESSION   WP_357665814
VERSION     WP_357665814.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 337)
  AUTHORS   ter Beek,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..337
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..337
                     /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=37901
     Region          27..331
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msttraapas psrraaperg rsggddrrlt wrnrlyrfdm rympylmiap ffllfivfgl
       61 fpllfnavvs lrnyrlddpt lpywagvenf srllgdedfw nalyntfgif llssvpqlll
      121 alvvasllnr rlraqtwwrv gvllpyvtpi vastmvfsvf fsrdfgmanw vlglfglgga
      181 ddpidwradk lhswiaiatm vnwkwigyna llylaamqsi prdvyeaaai dgagpwkqlw
      241 ritvpmiqpv vlftvilsti gglqlftepm lfdpnaqaat ggpngewqti aqliykvgwk
      301 dlnlgyaaam swalfliili vagvnylvtn rlsggrk
//
LOCUS       WP_357665862             529 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nonomuraea dietziae].
ACCESSION   WP_357665862
VERSION     WP_357665862.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 529)
  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..529
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..529
                     /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=56046
     Region          5..527
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mnlellirga lvadgtgapl rpadvgvaga rvvlfprdpa vpeerdaarv idaeglvvap
       61 gfidvhthsd avtllgergr elaaapvrmg vtteicgncg sslfpalper vpalrrssra
      121 gfggdipifq dygafmeahr qvprsnhlts lvghgtlrag vmgyedrpat areletmcal
      181 ldealaagaa glstgliytp gtygdtaevv alarvaaryg rpyvthlrde msrveealee
      241 aveiarasga alhvshhkta grhgwgrter tlpriaalre qglditcdvy pytegstsls
      301 amfppwandg gteallerlr draerermrr aiaegvpgwe ntvgnggwdr isvagatghp
      361 evegrtiael ggdpfdaaae lllaeqgevt iishsmredd vlrvlasefa migsdgvpkp
      421 grphprlagt fprvlgrysr dqalfpleta vhkmtgmaae rfgldgrgvv rdgahadlvl
      481 ldprtvadga tytdpllppt glaavvvage vavedgtlta rrpgrilal
//
LOCUS       WP_357665902             196 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357665902
VERSION     WP_357665902.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=21786
     Region          9..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 mtaklpspvv lenavvrlep ltydhvpdlf lagggddevw rwlsvptprt aeelasvaae
       61 viesptyaah avvlresgra vgwttyldvp gfdqsveigw twygravwrt avntsckvml
      121 idhafdvvgy nrvqlktdnl ntrsqaairr iggvhegtlr rhrprldgtw rdtvvfgild
      181 dewpahrdrl tqatsa
//
LOCUS       WP_357665973             283 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Nonomuraea dietziae].
ACCESSION   WP_357665973
VERSION     WP_357665973.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..283
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..283
                     /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=30252
     Region          29..225
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mtrgarepip grypvtfgev ellrdldrqh gwmlskdgvp qsyvdledpt yldfeyvrlm
       61 advidvlpdg plncvhvggg actipryvaa trpgsrhivv epdaalvelv rsqldlrsvp
      121 klkvrlqggl eavagiwdds tdllvldaft gatmpvelat aeymadlarv lrstgtllin
      181 ladgkglafa rrlvatvrgt frhvalladp gvmrgrrfgn livaaspael pvdlltrraa
      241 ggltqarcvy gealtnfvag appirqgdav lapvpppavf gle
//
LOCUS       WP_357666006             268 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357666006
VERSION     WP_357666006.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27423
     Region          5..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 mdlqlsgrva vvtgaskgig latvatllee gasvvavsrk sspeldalag prlthaavdl
       61 mdpegpaaav eravevyggl dilvnnaggp ppgvklprfa fltptdadwl tmfefnlfav
      121 vravraaiph llargggsiv nvttgavrqp gpmnvdyqaa kaallnvska lseeyapqgi
      181 rvntvspgpv rtawwteegg aadilagatg sdrdsvmdtv apqmmnlstg rlvepqevad
      241 viallasprs asttgsefav dggflkgi
//
LOCUS       WP_357666032             172 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Nonomuraea dietziae].
ACCESSION   WP_357666032
VERSION     WP_357666032.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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..172
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..172
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=19092
     Region          <18..171
                     /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 mrhlaivipd ptraslfglp ywlivavgav alfgafqayy wighklgdtl yesrfgrklp
       61 rerirsverv vekwgalavy acfwvpvlrh tlpwvagalr isypwyvvas algcltwvpv
      121 tsfalysvlw gwlelaahsp laaavaavil isgvaafvvw rrrrksekal aa
//
LOCUS       WP_357666134             271 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357666134
VERSION     WP_357666134.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 271)
  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 271)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..271
                     /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=28561
     Region          1..199
                     /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 mivvtgatgn vgrelvrvla dagervtavs rqpapvppgv rhspadladp aglrtalegs
       61 dalfllvage dpqaildqar sagvrrvvll ssqgagtrph iyrhpaafee avresglewt
      121 ilrpcgfdsn ayawaesiqt hrtaaapfae vglptidpad iaevaavvlr qaghagrtye
      181 ltgpapitpr eraeaigaal gapvrfdeqt reearaqmla fmpepvvdgt lailgeptpe
      241 eqkvspdvel llgraprafa dwaarnvaaf r
//
LOCUS       WP_357666171             592 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Nonomuraea dietziae].
ACCESSION   WP_357666171
VERSION     WP_357666171.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 592)
  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 592)
  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 592)
  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 592)
  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 592)
  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 10147745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..592
                     /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=64284
     Region          29..479
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(150,153..158,160..161)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(153..154,269..270,292..297,320,375,387,390,473)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
     Region          496..569
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mhaehrefra ewleesiaar fwavvaehpd riavlgeegp ltyaelaqev ravaaavhga
       61 srvgllvghg prmvaailgv ltagatyvpl dpayprarle smselarpel vvtvpehkdl
      121 ltgdlvdlts mppapdfrpv tvdpsspayi lftsgstgrp kgvvqthrga lfqirthtnn
      181 lrirptdris vvssfsydma vtdgfsalln gaavvpvdlr lhglgqlrea lvagqvtiyh
      241 stptvyryll dslsegevls nvrvvilgge evvrhdlarf qrhfpassvf vngygateis
      301 fvaqnhltaa emgddpvvpi grpldgveie lrphpaegei virspylagy lgaaerdqar
      361 fgvdpdgmrf yrtgdlgrwh pdgrlaylgr ldrqvkirgh rvelgeieav latlvpraav
      421 vtrevrgeph ivayvlgddt sglrerlaev lpdfmvpaei vavdtlpltp tgkidtaalp
      481 dphpgptpar avnlpaqeae lateiaavwr avfdvrevdw ersffdqggh sllmakvqqr
      541 leavlsrrip lttlyahptv aslahhltag eagapsdapa traalrrqrr rs
//
LOCUS       WP_357666148             208 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357666148
VERSION     WP_357666148.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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 208)
  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 208)
  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..208
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..208
                     /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=22373
     Region          2..208
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mrftvfgatg gtgvhfvrqa ldadhdvdav vrrpdavsdr hpglvvyegd vtrpdtlkep
       61 ingtdavifl vgphstgpct vyssgghnvi eamraagarr ilavtaalvd qpndtllqra
      121 trrivrrvfr eaqadrlvfe qelresgldw tivrpprlve gagkgvyrta fdtgvrgglk
      181 ltksdlakal lsmapdpath ghtvdiay
//
LOCUS       WP_357666184             374 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora chersina].
ACCESSION   WP_357666184
VERSION     WP_357666184.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..374
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..374
                     /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=39628
     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 reasrsarsq ggsldlhpes gqraltdagl
       61 agrfrsearp egeehrildp sgrtlvhhtp ppgsfsgrpe idrralrdll ldslpadava
      121 wrhrlvavtp rpgggfgltf dgghradcdv lvgadgarsa vrplltdaal spvailvels
      181 igdadrrhpd laelvgpgnl wcigasqila aqrlgdgsir vgislppddr hldafrsrra
      241 lldlfdgwdr rltalieagd gppiprriea mptgthwahr pgvtligdaa hlmppvgega
      301 nqamldaael aaelagnlad pdaaiqayek amfarvhpia emsarvqamm lspsaaediv
      361 rfftprptep apad
//
LOCUS       WP_357666190            1293 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Nonomuraea dietziae].
ACCESSION   WP_357666190
VERSION     WP_357666190.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1293)
  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 1293)
  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 1293)
  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 1293)
  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..1293
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..1293
                     /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=141483
     Region          3..1283
                     /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 mtaleleday pltalqsgml fhsayqedsa tyhdvftlil rgpyqsdtfr aalrevmarh
       61 svlrtsfdlt gfdepiqlvw qdveppvqel dfsgfedpgq rlsiwreqek hrpfdweapp
      121 lfravihhld tdefaltlsf hhaildgwsv asmvtelldr yaaglqgvrq apavpppstf
      181 rdfvarekea vaspqteefw rdvladapmt alprlpgyrt gdaedtvsha vplddqlveg
      241 lervarqarv plrtvllagh lrvlalltgd tdvvtgivth grpeheaaeq vlglflnsvp
      301 vrvrtdvpsw eelikrvfaa evaflphrly plfemqrlsq rsplidvlfd yrdfhvyqdl
      361 gpggviqvvq seffeqtnlp lsanftwspq agglelklky ditqfsadqv vragehyrrv
      421 fakiaedpaa dpreseklld advasvegwn atgaarefva lpdvvarrva sspdapavwd
      481 gswmtyaefg arvrglaavl reqgvrlgdv vgvclprgad livavhavma aggaylplep
      541 dypderlsfm vsdagarvvi tgepgrfpgs vvvapsesad gpvvglkipp sapayllyts
      601 gstgrpkgvl vsheaianrl vwmgeafple addrvvqktp ftfdvsvwel fwplmegagl
      661 vvappgahld aaalvelmra hsvsmahfvp smldavmevp dldvpslrrv vcsgealpas
      721 lvarvhsawp gvevhnlygp teaavdvtwh acrvgeertp igapiratri eildadlrrv
      781 pvgtagelci ggvqvaqgya arpgltaerf vpdpygrpga rlyrtgdlar wlpdgevdyl
      841 griddqvkvr gmrvelgeie avlaqhpgvq aaavrpvggv laayvvgtae peelaaflrq
      901 rlpdhmvpss fteldrlpvt angkldrkal pdpapvarap yeaprdelee tlagiwaeil
      961 gverpgirdd ffdlgghsll alrlalrmrq algreipvat vlaaptiaql tealadegdn
     1021 pisrgrvvpl rtagnrpplf lihalggqvf ryrplaqhlg ddqpvyaipa hgltegdsvq
     1081 ttidemaeay agyirelfpa gpyfvggfci ggnialevar rlrkdghdvp yvflawssae
     1141 epvvgstled dtalmvhala ggatsldpre lslmepaerl laivnaatke gqlrtestdl
     1201 dqiqryvevf ranahavgry khdtfdgpai llipeednap pdedygwraf vpnletglip
     1261 garfsalynp yvtrtanawr rwmdrglehr arh
//
LOCUS       WP_357666195             226 aa            linear   BCT 28-DEC-2024
DEFINITION  FMN-dependent NADH-azoreductase [Micromonospora chersina].
ACCESSION   WP_357666195
VERSION     WP_357666195.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 226)
  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..226
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..226
                     /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=24735
     Region          1..182
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mphllhldts arrtshsral saafadawra arpdatytyr dlaaspvpvi geawteicdh
       61 althgitdpg rlaegvrtpa qreawsvaep llaelvsadv lligapmynf svpaslklwi
      121 dqvtfpratl dlkvvvtgar ggsyapgtpr epfdhheryl rnffhghfqv ddvtfvnaef
      181 vnstvdptld hrreayrrsy adarqaaaal areaatpaas tsrrpp
//
LOCUS       WP_357666300             347 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase [Nonomuraea dietziae].
ACCESSION   WP_357666300
VERSION     WP_357666300.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 347)
  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..347
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..347
                     /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=36795
     Region          36..347
                     /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 mtpdvrdeir rpaagptqgp adggisrtai gegewaralr liqeadeval achispdgda
       61 lgsmlaaaka ltamgkrvva sfgdrrfvvp rllrflpald lltvpsafpa epdlmitfda
      121 stlerlgvla atagkarevi vvdhhasnqg fgtvslidpg vaatavlaee lirrlgqpld
      181 rdmatllyvg lstdtgqfrh ssttpaahqm aarlvaaglr tdeiarelwd rspfaylkvl
      241 aaalervvle dglvwtyish adraayglpy deiegvidvi rrtdeadvav vlkqdddgaw
      301 qvsarskgga dvgaistalg ggghcyaagf tshdsveetm arfkeml
//
LOCUS       WP_357666229             153 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357666229
VERSION     WP_357666229.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 153)
  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 153)
  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..153
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..153
                     /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=17098
     Region          1..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msetrwldae emtawqaflt ashlldrrie eqlksaaglt hpqfeilail saaperrmrm
       61 telarkvvvs ksgltyqvgq lekrglvert tcpdddrgvl avltveglrh lekiapghve
      121 vvrrflidll sreelatias amhkaqqamr pst
//
LOCUS       WP_357666304             328 aa            linear   BCT 28-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357666304
VERSION     WP_357666304.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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..328
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..328
                     /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=36249
     Region          97..325
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 msryallilp afnrvygess irltrselaa fadvseveet riggvpyvtf eadspdlall
       61 snlssvyaif giegdllrpl emtpldrlss dlitiqkyag ktnehftkll lnvtvlasdf
      121 pldarlsvld pmcgrgttln qalmygyday gvdidgkdfe aytgflrtwl knkrlkhtae
      181 tvpvrrdral vgrrfnasfg lskesykage tqqvtvvnad tlrsreffkp rsfdvivtda
      241 pygvqhgska ggglsrspld lidkavpvwq ellrpggaig iswntyggsr ddlariltah
      301 glevvalpdf ehwvdqaivr dimvarkr
//
LOCUS       WP_357666318             561 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357666318
VERSION     WP_357666318.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 561)
  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..561
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..561
                     /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=59080
     Region          19..132
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          240..561
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mdvlgrglap gelamrlkdl vqddhlalkv ltghdlldrr vrgvattdlp dpsrfvkpge
       61 lvlteltwht gadsakefvd rlgdvaalvc gtalkvpptd lidvcahagl plltlpvdvp
      121 fsqltehvlr aliaelgsnp rrpyggrrrl astlvdggsl tklvdtvage ldvpcwvmsa
      181 tgrvivgsqp lhedsrarla htfltarflp gmvddlsvfp iskgvphria nwflayrgeg
      241 aqgdsedviv elaalvaler srmeaahrie rrvldqllql lesgdadlpg lvsrlhtlhv
      301 etehgllvva ltaggpevsv avldellrpl apgivtasha pgswgsagtg asgpgspgtr
      361 apgpgasgsg aagsgaagsg yagsageava lvplagnsaa elaehlvrga rileaglgee
      421 rislgvssvt tgpaglngli eearharsla slgtgkvsvv tgddvsshrt llaaipdplr
      481 rsfrsrllgr leaydatnqt elletletfl eesgswaata drlhvhvntl ryrlkrieel
      541 tgrslnswde rvdfllalrm r
//
LOCUS       WP_357666324             196 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Micromonospora chersina].
ACCESSION   WP_357666324
VERSION     WP_357666324.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 196)
  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..196
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..196
                     /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=21335
     Region          2..162
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtrigiiigs trpgrngetv arwvheiaaq rddaqyelvd ikdfnlphld emappslgqy
       61 tqphtlrwae kiasydgyvf vtpeynhsts galknaidfl yaewnnkaag fvsygsvggt
      121 ravehlrlvv aelqmadvra qvalslftdf enfsvfkpgd hqvgavntml dqlaawsgal
      181 ahlragttma tpqsga
//
LOCUS       WP_357666325             449 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nonomuraea dietziae].
ACCESSION   WP_357666325
VERSION     WP_357666325.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..449
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..449
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47316
     Region          1..441
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 meqrgielvp aserygrprd llflwagttt tvftvvygti vvamglsfwq avaaivignl
       61 lafplvgfss iqgmqhgtst maisraaygn kgarvlgffg wlnmvgfeag gmvmitlagl
      121 tllkqagveg eglglkvaiv liaaviqlil plighaavmk aqkyltwvfv amfvvmailv
      181 apkanltagg sadfatftla vmlvmsgggl swaplggdys rylpvdssrk avfgyaflgg
      241 fvpylllmil gaavatvvtn asdpisglpg alpswfvvpy llltvvtlfa anttdlyssg
      301 lnlqaagiri krwaavvldl ifcviitfva itsdsfntml naflglvvvw lapwagiyvt
      361 dwlrrrgvyd aaslfdesgp gqirwaglia qavgmvaagl wlnssvyvgw lssatggsdf
      421 sifagfvvag ivyaaldrra vpvkelaha
//
LOCUS       WP_357666381             896 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357666381
VERSION     WP_357666381.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 896)
  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 896)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 896)
  AUTHORS   Rosinski,J.A. 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 896)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..896
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..896
                     /product="helix-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=93601
     Region          <3..896
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          838..895
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrgrdgecra irhlldrpeg galllhgepg sgrsallaya rrhagervvl aaagladeat
       61 lpyaglqrll dpvldradsl pdpqrrvlrr alagggcpaa rrlalatavl allaaaardr
      121 pllctmddvd sgdpetaetl avvarrlhrl pvallltags aaaadgipth rlspldeeqc
      181 aalladrrpa ppptavaadl aavscgnpqa lvdladaltp gqwhgeeplp aappadgalg
      241 aayrahldrl ppdtrrvlll aaldpdgdpa tlaraartag lavealapae aagllragpa
      301 gvtfpspltr tmieavapla drraahllla raldgrplrr alhraaatdg pdpaladele
      361 aaatddadpa gaaaalrraa elsddparta eravaaarca wtaghpdqar rllsglpadp
      421 vaagradllr gemqlrcdap ttavatllaa agavapadrg aallglvrag eaicltgdhy
      481 ryaevarqar alrrpgdppd vellttfaag vgatlrgdhe qggpalrrvv vlggrltgpa
      541 ltpaalicga vagllvavdg aahrladrav elarargdrs vlpralelra vaeywlgrha
      601 taaetaregl aiaratgqrt garvhlgila vlaavradrs tslariaeig dgatpgsrpy
      661 ayaqwalgvl dlvdgrhada aarleslart gtargqvlvq vmatpylvea aahdggrpta
      721 alavfdrwas staspsrral sarchallap rgsaeaeref rtalrlhptd tdrferarte
      781 llfgrelrra rrprdarayl hraretftll gatvwaeqag aelraagesv gsshrppaql
      841 ltgqqlhiar lvaegatnre iasrmslstr tidhhlrnif hrlgvrsrte larlfa
//
LOCUS       WP_357666485             412 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357666485
VERSION     WP_357666485.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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..412
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..412
                     /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=44665
     Region          32..410
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtrarkeqld agggwgglpp vqaadedtlg erirvmrdrv sirwrltlty galffmagav
       61 llvamhlivr svldslsftl rlpagsppsl adwlneqsel lannntnavl eylvrqsvmv
      121 ligvgilali lgyfvadral rpvaqmtata kklsesnlah qridlkgpqd elkeladtfd
      181 amltrlnvaf dtqrrfvana shelrtplti nrtvleials dpeasedlka lgrtllevna
      241 rnekliegll llarserela vrkpvdvrev aqtaveqlap faaesdvtft tdlsaaptvg
      301 dpvllersis nllenavkyn vqengkvwir tgmadgalvv qvantgqhvp ayevnslfep
      361 frrlhadrvd sakgsglgls ivravvqahg gnvaavprdg gglvvtirlp gr
//
LOCUS       WP_357666496             120 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora chersina].
ACCESSION   WP_357666496
VERSION     WP_357666496.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=13406
     Region          3..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhafdvlgdp vrrrilella egeqpagtvg atvqrefgis qpavsqhlkv lrdhgfatvr
       61 aqgtrrlyav dpgplrelde wlagfrrfwt pplaalatel argrrerrlr egnseerntp
//
LOCUS       WP_357666542             420 aa            linear   BCT 28-DEC-2024
DEFINITION  cellulose-binding domain-containing protein [Micromonospora
            chersina].
ACCESSION   WP_357666542
VERSION     WP_357666542.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10456332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..420
                     /product="cellulose-binding domain-containing protein"
                     /calculated_mol_wt=42355
     Region          38..136
                     /region_name="CBM_2"
                     /note="Cellulose binding domain; pfam00553"
                     /db_xref="CDD:425748"
ORIGIN      
        1 mrisharlap vvaafatlaa avvvtplvag paaaaqgcqv dyrptvwpgg ftatvrvapg
       61 dtalngwtvg wtypgdqrit gawnavvgqs gatvtarnaa wngsvpagga tefgvqgtvg
      121 paapaptgft lngvpcngap pgsttappsp sgspttspsp tvspspttsp sptvspsptp
      181 ttspsptgqp pagcagavlc dgfenqtgsa psgdwtvvhp dcagtgaaav dtatahagsr
      241 svridggggy cnhvfvranr dlsavgavry grlwvrhtta lpadhvtfla mtdaadgnrd
      301 lrmggqngal qwnrasddat lpeqspagva lsvplptgrw sclefmvdgs sgqlrtwldg
      361 aavagltadg vpthdvdgqw ygrtwrprlt dlkigwesyg gaadtlwfdd valgatrigc
//
LOCUS       WP_357666505             615 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357666505
VERSION     WP_357666505.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 615)
  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..615
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..615
                     /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=64318
     Region          13..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(13,37..38,71,76,81..84,96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,79,95..98,102,104,141,143,
                     145..146,148,158..159,162,179..182)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(20..21,23..26,28,41,43,79,95..98,102,143,145..146,
                     148,158..159)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(24,102,104,141,143,145,162,179..182)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(158..166,175..182)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mgdpsgsrli ggryllaeel grggmgavwr ahdqvldrpv alkqvlvpgw mseqdreraf
       61 ervlrearat arlrnpyvit ihdvvvdegh pwivmellsa sslaqvlers gplpehvvad
      121 igvkllgalr aahaagithr dvkpanvlll ddggvvltdf giahvanspt ltatgmlmgs
      181 paymaperle gepageasdl walgatlyta vegappyamd spvavmaail mrephpmrrg
      241 rrlrpvvegl mrrspkerlt leaasaalav vagrrhgeea rrregsrala llvrqdqidp
      301 dpptdplraq pqdldlpsee apdppvprvp dapgsttppa edapasstpg vrdargssap
      361 gvrdargssa pgvrdargss avpeaadplp gpvpplspvg tagvevlrea saeaarergs
      421 aregggatav vvrglrfgav tsatlgvlay avprvarrmg tevtllapgt allvlfaava
      481 llavvlprdl lpdsgvnatl tralpfvafa gylggyqtgt gahvstslay allaawaatt
      541 sartwrrsqa aaavgaaata cmaaltvahl widlagrsal ttrllealpe ltaaawtlht
      601 awawwtarrq gqgrf
//
LOCUS       WP_357666551             419 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357666551
VERSION     WP_357666551.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 419)
  AUTHORS   ter Beek,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 419)
  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 419)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..419
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42840
     Region          30..406
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mskllandea iitavrqpsi gnsarayqer vrggdmgalp avlglvvlct vfallrptfl
       61 tpvnfanlft qggqitviam glvfvlllge idlsagfasg vcaavlavtl tdmgmpwyvs
      121 vlaailtgvl iglmlgvlva klgipsfivt lagflafqgv llvlleegtn isirdetila
      181 vanrnlppml gwglflvgvg gyaavqivrs lkrsrrglva dpasliaarv gtmaviagla
      241 vyvlnlersr npalvsltgv pivvpivlal lvvwtfvlrr tafgrhiyav ggnaeasrra
      301 ginvdrikis afvicsgiaa vggiiaasrg asvdpntggs qvllyavgaa viggtslfgg
      361 kgrvmdavlg gaviavidng mglmgygssv kyivtgsvll laagvdalar rraaaaglr
//
LOCUS       WP_357666569             104 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357666569
VERSION     WP_357666569.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=11540
     Region          7..97
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtalhptreq iqlvevlaal ghpvraqivr tlsaqppdte mfcgsvlpdv pkstltnhwr
       61 vlreagvivq rpegrklfit lrrddldarf pglldlvvqe sham
//
LOCUS       WP_357666580             276 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357666580
VERSION     WP_357666580.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=29224
     Region          1..275
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkpalnqwtt krwtvaeavd gcvrhgleai glwrqevaaq glaesvrlvr daglrvsslc
       61 rggfltsgsk ealddnlrai deaaelgaac lvmvvgglpg vpagqapskg fsrdlagara
      121 qvaealsvla pyagergvrl aleplhpmyc adravlstlg qaldlaspyp ssqvgvvvdt
      181 fhvwwdpsvy eqiarageri asyqvcdflq plpsdvllgr gmmgdgvidf apltkavlka
      241 gytgdievei fnadvwaadp dtvmttmker faalia
//
LOCUS       WP_357666117             265 aa            linear   BCT 28-DEC-2024
DEFINITION  GtrA family protein [Micromonospora chersina].
ACCESSION   WP_357666117
VERSION     WP_357666117.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..265
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27572
     Region          55..185
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 msrqmagmvr matsdagclp qphwqagrrr rcsgstipsm lkplrrcsar vrvgrstsgs
       61 farfilfggg vglaasiavs vlatlmpwaa analitvist ligtelharf tfaagrrarw
      121 rqhvqsagsa taaylvtsaa vlvlhavqps asirweqavy lsasglagag rflvlrlhvf
      181 ahgappapts trsapaphra vfgpfggcls lttgggrrta rrrqagvtal arpprrppav
      241 garrpgsrrp agsdgpcssg rlsgr
//
LOCUS       WP_357666642             296 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357666642
VERSION     WP_357666642.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 296)
  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..296
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32957
     Region          25..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(30,34,59)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(33,58)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(40..41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          111..291
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 meaaenvrpl spakgggptv lrillgaqlr rlrmakgisr edagyairas hakisrlelg
       61 qvsfkerdva dlltlygvsd pddrarlidl arqanqpgww hkysdllpsw fevyiglega
      121 asiirtyenq fvpgllqspd yaravislah drapagemer rvalrtarqq rlkgerpvsl
      181 wavldeavlr rtiggaevmr aqvehlieas elpnvtvqvm pfdrgghaaa ggpfsilrfp
      241 epelpdvvym eqlssalyld klaesehytk vmdrlsvqad tpaesrrfle rlrkiv
//
LOCUS       WP_357666613             231 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora chersina].
ACCESSION   WP_357666613
VERSION     WP_357666613.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  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 231)
  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 231)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..231
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23769
     Region          55..229
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtepapphrq peegyrhgrl tarptavaap gpagpaelpd paggppalrh vpaggtgpyr
       61 lvlllhgagg sarqgldlll pladahrlll lapqalassw dliaegygpd varidallag
      121 tlgaypvagv tvggfsdgas yalslgltng dlvdavlafs pgfaaplvth grprvfvshg
      181 tddrvlpvdv csrrlvprlh tlgypaeyae fagghevpae irrravdwlv g
//
LOCUS       WP_357666651             495 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Nonomuraea dietziae].
ACCESSION   WP_357666651
VERSION     WP_357666651.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 495)
  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..495
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..495
                     /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=55263
     Region          95..336
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mvevaaergk rsssrtseeg agwrcqqigs ykglrpntdt fswfhprtlw rsrneilagl
       61 fgdpsgevrr rwveeqrarg vdgdfrirpg vgkafsflll gdpgegddsq yavvpgmlhv
      121 gegtsfavia sdvvyptgag neycdkffrp ykdyqapiya ipgnhdwydg lggfmrvfcd
      181 applkprpdr glrallwrks erideqalae arelrgapsq qavqpapywa iesesllivg
      241 vdtgikgaid aeqtawlrrt sldprpkili tgkpiysrdv hkpsaleggg tiddivrdpa
      301 hryvaaiggd vhnyqrypvr vgdrviqyiv sggagafmha thtigrvgva gvheddfkcy
      361 plrgdslsfy sqlyakrlrm rwlfltpaea acimadrikn tpirqidpav titrrmrwaa
      421 rvlgawpmpf rlpvgsvfhr ylselsdwdt ppffksflhl evtpsrltir cfaatgclpq
      481 eldppledev sisll
//
LOCUS       WP_357666652             980 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357666652
VERSION     WP_357666652.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 980)
  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 980)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 980)
  AUTHORS   Rosinski,J.A. 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 980)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467563
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..980
                     /product="helix-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=105084
     Region          <7..920
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <918..978
                     /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 masdvdtapl vgradtvaal rsallddvap gqtaavfltg esgvgktrll aevgerlrdg
       61 galvltgacl digdasplhp vrqalrrlda dlteartssa vrgllqvfde etpgpdgaga
      121 llervsrglh lvaagrplvl vlddlqwvdr strqlllyll aglgdlqlsv laairaeslq
      181 gahplrrvlt elrrlrsvrv vdlapldrag tdelaaaiag tplppeaadq lwqrsggnpf
      241 vveelardlr dghdglsdtl revflarvda lpqpahavvh avaagvepve hwllaqvvrl
      301 pedqlieavr eavahrllvg addgyrlrhr lvaevlahel lpaeraalhr ryaetltsat
      361 aelhqarlah hwrlagepar alpaamaaar eaerlhgyae ahrhwsaals ladtpaavlp
      421 dggrpepvev draellthaa esahhcgeha ralalleela adpagpptca lhirraryla
      481 aagrsapaea eyrqvlaaad ctprerataa ahlaelllhl gryaeagdqa realrlaaev
      541 egaasevvla saalgfseay ledpdaglav mrraldtaer sgrpedvaca ylhlaelltg
      601 plnileegvv varrgaerva elglgrtwet rllaiatngl frvgqwaeae kvvaaalrhr
      661 psgadavell larcrlsvgy gdveasdrdl eavatvlagg garhvlpmli lraglamwqg
      721 rhdqarqavq rgltesrsdd vivlatlawh glraeaeasa srtvevdpna vrrlrevver
      781 vtrksgkaga pvryvadafl alcaaelsrl ddgrgdpelw araatewdrr nhpypaaysr
      841 lrqaeallar rsrvatagkl lrqahetaqa lgavplseei rtlagrarvp leeapaatrp
      901 aprpraaapa aptvdelevl tarerevlaa vaegltnrei gqrlfisert igvhvshifd
      961 klqvrtrvqa saiflrnrpe
//
LOCUS       WP_357666688             379 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Micromonospora chersina].
ACCESSION   WP_357666688
VERSION     WP_357666688.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 379)
  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 379)
  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..379
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..379
                     /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=37781
     Region          9..378
                     /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 maerehlrit gvhaisalgr gadallagvl agapaftpvr rfdtigrrvt vaatvpevgt
       61 ladeltdavd racraagldr thragaalfl athggphslp arpagggdta pevpalaghl
      121 arrcglggrt rtyttacvsa stavadaatl igrgdldrvv vaagylvepd qyalfdagra
      181 laadgavrpf sagrkglllg davvavvles araaavrgap tvatvagwgr agdayhpcqp
      241 hpeghglara aeaalrragl paaavgyvna natgtpysda seaaalgrvf gaaagripvs
      301 stksvhghal easgllelvv tvltlghgkl pvnagwlgpd dscpldvitd aprpaptpha
      361 ltlnaafgga ntallvsap
//
LOCUS       WP_357666734             311 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Micromonospora chersina].
ACCESSION   WP_357666734
VERSION     WP_357666734.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=32142
     Region          1..297
                     /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(30,241,244)
                     /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 mitvvgeslv dliedpsgva aahpggspan vavalgrldq patlltqlgd daygrllrah
       61 lagsgvrldp aslsdlpats vartrvgadg qagydfdidw rsfpqraltd vgagsdclht
      121 gslatvlapg addvlalvqd rrattmisyd pncrpslmgd patvlrrvee lvaasdvvkv
      181 sredlawlhp grahervgre wlergavlvv vtggergawa atrhgevrvd alpvrvvdtv
      241 gagdaftagl laalaqrdll gaarraalda adpatiagvl rhaarvaawt cgrkgadppt
      301 raqltalplp a
//
LOCUS       WP_357666792             246 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora chersina].
ACCESSION   WP_357666792
VERSION     WP_357666792.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 246)
  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 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   5  (residues 1 to 246)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..246
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..246
                     /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=25505
     Region          19..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mttrtdgqal aglaalladp tragfclall dgrawtagel arsagvapst asdhltrlir
       61 ggllteerqg rhryvrladp svaqlvedla grapapatpp rtlraasaqa slayartcyd
      121 hlagrlgvlv hdallargvl drsgglavtp agvawltdlg vpveplraar rplvrdcldw
      181 terrphlaga vgaalcrrfl dlgwtargtg ravrvtpagr palaaalald padlappsrd
      241 sgpara
//
LOCUS       WP_357666851             191 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea dietziae].
ACCESSION   WP_357666851
VERSION     WP_357666851.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 191)
  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..191
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..191
                     /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=20457
     Region          7..143
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtpkgplrma viigstregr vgesigrwfa araelrddla vsvldladya fpccfpavat
       61 pamrafsrav agaeafavvt peynrsfpas lkqaidfayd ewqakpvgfv sygsgsdgfy
      121 aieqlrtvfa glhtvtvrdg vgidllgggv ddggrpydtd ertlavttml dqllwwglal
      181 raaratrpfa s
//
LOCUS       WP_357666891             469 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Nonomuraea dietziae].
ACCESSION   WP_357666891
VERSION     WP_357666891.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=50616
     Region          25..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 msdplsereq apaalnlvaa aaepylgsln erpvhdhsad hlldqlegpl seegegtmaa
       61 veqllavgte astqtsgprf fhfvvggatp aaqaadwvts lldqssglhl tsplaaraer
      121 ialdwlkdlf glppayggvl tpsatfanlt glacarqwwg erhgadvtsq glaglprmpv
      181 laggyihpss rkalqmlgvg rdgvtvcard eagrvdlaam erelvalegp avivgnagev
      241 ntggfdpian ladlaeryga wlhvdgafgl faaasprlrh lvegverads itadghkwln
      301 vpyesgfafv rdqdlmfrsf gawgahylps dvnynnlgpe ssrraralpi watlraygrq
      361 gyarlverhh dlalrlaeav ekapdmella pvplcvvcfr yrpegrpeee lddlnrrlga
      421 alladgrvya gtttyqgmta lrpaivnwrt teadidyfwe vlreladrl
//
LOCUS       WP_357666897             319 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Micromonospora chersina].
ACCESSION   WP_357666897
VERSION     WP_357666897.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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..319
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..319
                     /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=34833
     Region          101..248
                     /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 mtelnrrall ratalagaaa atglagglta aapaaaaest evvngpwlvt gsagllqinp
       61 ghttpqvlls raydattspd gryvavndlr yegetgssls lydrvtgevr kvisdpfgvs
      121 yewptwspdg tevalvvdre tlvavnvatg arrvlvqght myrphwsrdg smivmqwisr
      181 seghqlrmle latgrvrrvy qpeegerfgw pvfmpnserv vfctnrwyrd vdlplgedsl
      241 asvridgtgl kkltdeprly lspvfspdgr ycaalsvppt neypdggnii vstsgfgeqw
      301 wipgdeydds mrvdwarai
//
LOCUS       WP_357666923             217 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357666923
VERSION     WP_357666923.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22762
     Region          5..185
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mrspvvfdld gvlvdsepvw eevrrafvae hggtwrqetq srlmgmstge wsaylaelgv
       61 rlppeeiarg vvgqmaeryr hgvpllpgak eaverlaagr plglassspr alidvvleat
      121 glgaffgatv steevaygkp apdgyleaas rlgvdpsdcv avedssnglr sahaagmrvv
      181 avphplyppa pdalalaagt aktldeltpd lvdslpr
//
LOCUS       WP_357666911             264 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora chersina].
ACCESSION   WP_357666911
VERSION     WP_357666911.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..264
                     /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=27761
     Region          4..206
                     /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 mnapilvtgg tgtlgrlvvp llrdaghpvr vlsrrggrpa dgvehvtadl ltgagvdpav
       61 rgvdtvlhla ggpkgddvat rhlvdaarra dvrhlvfisv vgadrvplaw lrskrdaera
      121 vagsgvpwtt lraaqfhdlt ltmvekmakl pvvpvpgglr lqpvdareva armvelalga
      181 paglvpelag prvygldelv tgyltavgrr rlrlpvrlpg ragrayrngd nltrpgaslg
      241 vrtweaflae rlrqpavear ggaa
//
LOCUS       WP_357666967             355 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357666967
VERSION     WP_357666967.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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 355)
  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 355)
  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 355)
  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 355)
  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 355)
  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..355
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..355
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38564
     Region          74..212
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
     Site            78..85
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(79..86,151,195)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            147..152
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            211
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mttvlrphae ddhaeelall akeddrarpp gwklspwavt tyllgdgdri spkyvgarri
       61 vevavatlat drallllgvp gtaktwlseh laaaisgdst llvqgtagta eeairygwny
      121 arllaegpsr aaltpspvmr amaegriarv eeltrmpsdv qdalitalse ktlpipelne
      181 evqarrgfni iatandrdrg vnelssalrr rfntvvlpvp ataeeevdiv trrvaqlgrs
      241 lelpetttgm aeirrvvtvf relrdgvted grtkvkspsg tlstaeaisv ltnglalaah
      301 fgdgvlraad vaagivgavv qepvsdqvvw reyletvvre redwrdfyra crevs
//
LOCUS       WP_357666980             321 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            chersina].
ACCESSION   WP_357666980
VERSION     WP_357666980.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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..321
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..321
                     /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=34973
     Region          49..317
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 marnridrrt llrglagstv avsaaslaga apagaddggc grlipqghvg iqlysvrdki
       61 aqvgfaavfe elsrigyrev efagytqgsv gaitpeqirr llddngltaa gshrglndfr
      121 tnleweleva eilgmpaigt aqaptgdrti vgyqraaaef nawgaaaaar glklyqhnht
      181 iefafatdrp dvrlydlfle ltdpryvfle mdilwaygga rkypgfrpvd yvnrhpdryp
      241 lfhvkdgvpl pdpqqgnsya dvefgagvip faeffgelkg rgrfeflweq dsapgaqpnp
      301 pgslgaaers yqrmidlrga r
//
LOCUS       WP_357666981             135 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357666981
VERSION     WP_357666981.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 135)
  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 135)
  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..135
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..135
                     /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=14595
     Region          5..135
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msvtrevval faevaarynd gyeaaaaarr ltalqakalv llareplpmr rmaelfrcdp
       61 snvtgivdrl errglvsrep gaadrrvknv tltpaglgvv eelrgvlgfa geplaalsea
      121 ereqlrdlla rmlgr
//
LOCUS       WP_357667043             252 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357667043
VERSION     WP_357667043.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26078
     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 mrltgkvaii tgaaggigsa taarfaaega avtcvdvrad aamelaerig gdtygigadv
       61 aspednarvv aetvrrfggv dilhanaavq imgritdttp dqwdrlhavn lrgvylgvqa
      121 vlpalrergg gsivitasll givgdpdmpa ygamkgglrs mtralaaahg pdgirvntic
      181 padvetelle dffafqpdpe aarreltgry plrrfaspgd vanaalflas desayitgtd
      241 lvvdggllar iy
//
LOCUS       WP_357667083             300 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357667083
VERSION     WP_357667083.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 300)
  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 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   3  (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   4  (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 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=31838
     Region          108..295
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <236..295
                     /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 mdqitlsaca evgfqvagrk gahgamralr rvipldayef vafdpvtgrh tslvsdgltv
       61 apapsepppe agrepyameg allasygwrr glttplllae grytgllhls aadfpphapa
      121 lmaalsptla hvtdltrcvi dpvglpkgfa avafdragvv rdvagaersr vlaedrsmaa
      181 yardfldsre lsrrglwqdg ngrwrevrvl ragvgshgal qgavvaerac clpyeltgre
      241 vdvltrvaag dsnpqiaaal vlsvrtvtth lehifaklgc dsrtrvttka laeglcrigl
//
LOCUS       WP_357667209             850 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357667209
VERSION     WP_357667209.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 850)
  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 850)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 850)
  AUTHORS   Rosinski,J.A. 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 850)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..850
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..850
                     /product="helix-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=89896
     Region          <1..808
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          790..846
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlhgrdkece rvgrliegar egrsaalvir aepgtgksal ldhaaeereg lrvlraggie
       61 teselpfatl hqllrpllgg ldalpepqad alrgalglar segrdrflig latltllaeh
      121 apllclvdda hwvdraslea llfaarrlda egvvlifatr amerdvlaaa glpqlpladl
      181 dreaalsvll ehapglrdhv rdriveesgg nplalielpg mdqdllsagp lplphrlqea
      241 yqeritalpp dtrtlllama aedlaaalra tglslaalap aeqaglvedg afrhplvraa
      301 ayqgasfaer vavhralard tgahrrawhl aaaatgpdee vaaalertaa qagqvsgyae
      361 aaaalehaar ltpatrdrvr rltaaatlta dsgqsdraam lidqarrlgg asaelvrlha
      421 rvefehgspe aawrllldag pellieaarv awsvgdsagl lavrerldpg paamvtgvve
      481 llsgdpgagl dlirrhagla ppregadglq isataldlls gdlvsardsl lrlaadlrsr
      541 gaigwlpgvl avlaetelll grarettate alriaqdtgq lrhashargl lafaaalrge
      601 dlagagsgtg dtgrggsggd gsggegawvg raqamldlgr grfeaaldrl dllahrphgv
      661 yfvpdqveaa vrsgrahlap iarfeswara sgqpwaravr hrclallaee peehfeqsva
      721 csdlpfqqar srllygewlr rsrrksqart qlraaletfe qtgtaawaah araelraage
      781 aaappaddll aaltpqelqi vrlaatgatn keigaqlfls pktvghhlyr afpklgvsnr
      841 telarlslfa
//
LOCUS       WP_357667213             693 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357667213
VERSION     WP_357667213.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 693)
  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..693
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..693
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=76385
     Region          2..691
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mpaeltsfvg rtrllanlkr hlsdentnlv tvtgiggvgk srtvlrlahq vrgqfedgvw
       61 fadlarlqda gmvkntiasa lgvadqsarg eseslsewva nrnmllildt cehliegcae
      121 lidellqanp nlkvlatsrq slhlpyehvv pvpplavpge dphenmftne svqlfaarsg
      181 avvpdfvlde hnigsvaelc rrldgiplai elaavrlral svdqilgllt drfsllagas
      241 rtalprhqtl raaigwshel cepaerllwa rlsvfagdfe ldaarfvcsd drlpaeditd
      301 lvtglveksi llirsdhagv ryklidtlae ygeewleklg esqrlrhkhl ayylslarrs
      361 edawsgprqi ywfvrmrqeh dnvrlaleha lrtpgesrma lellsslwfm wiccgfvreg
      421 rvyleralra npdpskerck alwvlsyvrs aqgdsvgale aaekcsseav lvgdsravil
      481 askmqgtaal lqgdlqkasa llgmaiefnt gnkelnpgll paivelpivl ttqgelyeae
      541 sllvdvlqvc kergelwvss yaywalsmpl lasnrldkal esaqeglrik rhfhdtvgsm
      601 mvletmarim vglnqpdraa rvlgalhqnw raaglpmlga pfltsehera vkecqktlge
      661 eayrrafdag tkldldeats lalddldagp apv
//
LOCUS       WP_357667224             879 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357667224
VERSION     WP_357667224.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 879)
  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..879
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..879
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=97447
     Region          103..878
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          615..643
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(616,619..620,623..624,626,650,659..660,663..664,
                     666..667,703,706..707,710..711,714)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          648..684
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          702..728
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtregdlpae lrsallehat ggrgmsirwt arqdwrrpyl iglnhprrgc vvtgplrlte
       61 deprprrrrr vwaapvaaga aagaasvlaa sleweippva kigvtglaav lvgvttwatt
      121 atsrnepkpr pedplwrppd qwppspehft grtealaelr kvfsarrgan elapplvvsv
      181 ygrggvgksa lmarfgqeia dwfpdgrlya slrgirpdev ligflralgv rlttdpggle
      241 elrrlwltwt kgrriligld nvddaeqvka lipaepgcav vvtsrqplfl mnaydtqlsv
      301 fseaqgvell arlaggarvv edlasakeiv kicdylplai nicggrlatr sswslrelag
      361 rladerrrld qlelartvdk svrasvqlsy ddctgiqrrl lrllssltsp dvpgwvagel
      421 lgisvldgad qlealvdvql aetsgadqtg amryrlhdlv rlfaaeleed rrdaaiervl
      481 ygyrrraeaa aqarwpqdwg rtgrvgdleg qaqasdwlna erlsliamin qarsmglwel
      541 vfglgrafcs ichslraywt dwgeiaeitv eaarrmgdrr algialldrt avnagdgave
      601 aleiftelge swwaaramrt igmrlfndgn ldraqgylig aitafkgeed ywwmartqrn
      661 laelrlaerr peearelled alevfkrdgn ryseaqtlra ygevlaaqar glrregdlka
      721 aadlftkagf sldragemfr srgelweear clraagevgd ptnglreleq vkraeeilaa
      781 lgdswgqart hlsagralar lgrkaeaete llrsvaafee lgdqwwmars lrylgethld
      841 ardrdaavpp lerareiyrs lgneagmrrt lellrraes
//
LOCUS       WP_357667227             373 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357667227
VERSION     WP_357667227.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..373
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..373
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40379
     Region          84..365
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mlqrsvddla irlgrpllle drfqrviays eqdgamddir rdsilrrhtt pevrgflhaa
       61 gileateplr tpgapalgll prvcvpvrhd galmgflwfi dagpamsaad ideartaaaa
      121 lavalfhesl aegmashrel eavigvlsgd pdasraliea gfpqalavta lvatplaaep
      181 seaarlaleq gmltvrrrlg glhlvrydha tllttssspa eevhaamalp vvvgvgrprp
      241 slaeadasya ealhaaqvaa rvpglgrtve wtrlgvyrml thvpradlhp glerlladaq
      301 hlplletlet yldlagsava tsrrlrlhrt slyyrlqrve elaetdlkdg gerlslhlsl
      361 klarlsgryr prf
//
LOCUS       WP_357667260             790 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 65 protein [Micromonospora chersina].
ACCESSION   WP_357667260
VERSION     WP_357667260.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Nakamura,S., Nihira,T., Kurata,R., Nakai,H., Funane,K., Park,E.Y.
            and Miyazaki,T.
  TITLE     Structure of a bacterial alpha-1,2-glucosidase defines mechanisms
            of hydrolysis and substrate specificity in GH65 family hydrolases
  JOURNAL   J Biol Chem 297 (6), 101366 (2021)
   PUBMED   34728215
REFERENCE   2  (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   3  (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   4  (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   5  (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   6  (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 11446212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..790
                     /product="glycoside hydrolase family 65 protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88418
     Region          9..764
                     /region_name="ATH1"
                     /note="Kojibiose phosphorylase YcjT [Carbohydrate
                     transport and metabolism]; COG1554"
                     /db_xref="CDD:441163"
ORIGIN      
        1 mireraypve pwhvretrld mdvlaqsesv falsnghvgl rgnldegeph glpgtylnsf
       61 yelrplpyae agfgfpesgq tvvnvtngkl irllvddepl dvrygellsh ervldlragt
      121 lhrelhwrsp agrdvkvrst rlvsftqrav aaihyeveal egplrlilqs elvanetlpp
      181 qsrdprvaav lesplqaeee lttddgglli hrtkvsglrv aaqmahdvda perttveseg
      241 yedwvrttig cvlkpgqtlr vvkyltygws srrslpalrd qvgaalaaar ldgwdglrre
      301 qreyldefwd aadvrvegdp evqqavrfgl fhvlqagara errpiaakgl tgpgydghaf
      361 wdtemfvlpv ltytqpgavr dalhwrhstl pqaqerartl nlagaafpwr tiegpessay
      421 wpagtaafhi aadiadalrr yvlvtgdqal eeeiglellv etarlwrslg hhdrtgrfhi
      481 dgvtgpdeyt avkndnvytn lmaqrnllta adcamrhrdq aldlgvteee aaawrdaasa
      541 mhlpydpeiq vhgqvegftr lqewdfehtp pekyplllhy pyfdlyrkqv vkqadlvlam
      601 hwrgdaftgp ekmrnfnyye rrtvrdssls actqavmaae vghpelahry lreaalmdlh
      661 dlnentrdgv hmaslagawi alvagfgglr dhdgtlsfsp rlpsrlsrle fslqwrgmrl
      721 rvdvrphqtt yslrnggpdt vvelrhhaep irvtaaqpvt vpvppahpsg pqpeqppgra
      781 pllhlpenms
//
LOCUS       WP_357667281             260 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357667281
VERSION     WP_357667281.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,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 260)
  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 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..260
                     /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=28160
     Region          <2..253
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mtviqaerlr kvygeavave evsftveege slaivgesgs gkttvarmll gletptsgti
       61 tvcgrpraag rvsskerrrr areiqivfqd pyssldklqr igdviatsls lhfsltpael
      121 rrrtlelles vglaerhaam lpkqlsggqr qrvaiaraia veprvlvlde avaaldvsiq
      181 aqilnlladl rapggmsyvf ishdlavvnq isdsaivmhr gavvergpta dllrepqedy
      241 trallaavpr pgwkpsrrvt
//
LOCUS       WP_357667310             396 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora chersina].
ACCESSION   WP_357667310
VERSION     WP_357667310.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..396
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=41497
     Region          5..396
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mdearldrar rtsvaqtagv igivlllvga lmfvltsrqe sraldaglte vlaaaedvdd
       61 pppgqflarq rpataavevt rsaspelvri lngavgrppg ryetgagddr rvrvlvarra
      121 dgsrwavaad laplrrrqgq lavallvael aglagalvaa allarravap lataltlqrr
      181 fvadashelr tpltvlhtra qmlarrarsq padrltdqld qlvadtralg evvedllvsa
      241 aaehqplpdt evdlaevare vvasmsayar ehqvelrlea agparvrgar talrraltal
      301 vdnavghttd gghvtvtvtr rdgrvaaava ddgvgldpae adrlferfah gtagagrrfg
      361 lglalvqhva rahrgaveva gapgrgatvt lvlpaa
//
LOCUS       WP_357667313             463 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357667313
VERSION     WP_357667313.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..463
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..463
                     /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=51337
     Region          32..407
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnltkdfang gvsfwyrqig iperraalpg srdydvaivg ggytglwtay ylkkeqpdlr
       61 iailekefag fgasgrnggw lsaefagsre rhakargrqs midlqhamfa svdevirvad
      121 aegidadihk gglihtatnp aqrrrlheel delrawgyge qdlrllerde reerlrvaga
      181 ldatysphca riqpaklavg lagvvaglgv diyegttvtq ikpreaitdr gvvraeyiir
      241 ategftagie gqrrqwlpmn ssmivteplp advwkhlgwe grellgdeah ayiyaqrtsd
      301 driaiggrgv pyrygsrtdd rgatqkwtve slwrmlvklf paaadariqh swcgvlgvpr
      361 dwcstvhldh stglgwaggy vgsgvtttnl agrtlrdlvl rrdteltglp wvgrqvrqwe
      421 peplryagvq liytlfraad rrendrgtst sgyarlanli agr
//
LOCUS       WP_357667403             388 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Nonomuraea dietziae].
ACCESSION   WP_357667403
VERSION     WP_357667403.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..388
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40943
     Region          50..383
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mdgkppqpmv payggsslad lpgsllaalg vpsrdqdara agsdnlldla padrvclflv
       61 dglgaellra hadrapflss atarrltagf psttvtslcs lgtglppgeh gmlgmtlavp
      121 gerhlfnclr wtlpkgmppm dpsewqpaet vyqraaragi tpsyvgpaaf egtglteavy
      181 rgvryvpadt veervagvka mlagprahvt vyhgdldatg hlvgwgspqw ldqlelvddm
      241 aarlaetlpa gsalyvtadh gmvnavekid aqatpalseg vamfggeara rhvytekgaa
      301 ravleawrev ltgkawvmsr qeavdsgwfg pdvrrewmgr igdlvavpyt dcvilasath
      361 pieaafvgyh gsmtaaeqlv pllevstr
//
LOCUS       WP_357667491             955 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Nonomuraea dietziae].
ACCESSION   WP_357667491
VERSION     WP_357667491.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13307259
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..955
                     /product="glycoside hydrolase family 3 protein"
                     /calculated_mol_wt=103207
     Region          1..822
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
     Region          840..946
                     /region_name="CBM6_xylanase-like"
                     /note="Carbohydrate Binding Module 6 (CBM6); many are
                     appended to glycoside hydrolase (GH) family 11 and GH43
                     xylanase domains; cd04084"
                     /db_xref="CDD:271150"
     Site            order(856,867..868,921)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:271150"
ORIGIN      
        1 mkrallalal vvsisafttd ppvyqdpskp laervedllg rltpdekisl lhqsqeaipr
       61 lglpyhkngt ealhgvgwsn dhgdgwkqkf asgtifpqav glastwnpel iervgaatgd
      121 evrgyaaenp elwgtqvwap vvnllrdprw grneegysed plltgaista ygkglsgddp
      181 vylktapvlk hylannneyq rsltssnlpp rvkheydeaa fkpaisadaa tgvmgsynlv
      241 ngrpntvnpd qdevvrtwtd kvlynvsdaw apqalyqven yypdeptsya atlkagqdsf
      301 tvdgmdtapm tasikaaler glitqadidt avrhvlsiri rlghadpggg pyakitkevv
      361 dspahralnr rtaaeamvll rndgrlpldq katksvavvg plqdrlhrdw yggalpyqvt
      421 pkralaeraq vtgldaldrv alrhtatgky vtasadlaqa vtvgadrtaa aqwdltdwtg
      481 gvstlrnaas gklltgnggt llansdepdg wfvqqqfrfe kqgdgsyliq yagyevnesw
      541 wsipepyltv radgtvamga kadaarfame vvsdgvkqav eaakgadaav vvvgshpfva
      601 grevhdradl tlgasqlrli eavqranpkt vvvletsypv tvtakallwt thagpetgha
      661 vadtifgean pagrltqtwy pssdlpdild yditktgmty lyhrgeplya fghglsyttf
      721 gyqglkvtkd gqvsvkvtnt gsragdevvq lythqqrsrv vqpvkqlrgf qrislrpges
      781 revrftlkke dlalwdvtrg rwtvesathd vlvggsssai rqratlqvag eripprelsk
      841 ptraidfddy kgvrlvdlsk ergeavggsa ggwlafkdsr lgaaftaqva svtggsvevr
      901 lgspkgrllg tlkapatgdv ytyatamtpi tpvrgvhdvy lvftgdvrvg tftla
//
LOCUS       WP_357667516             186 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora chersina].
ACCESSION   WP_357667516
VERSION     WP_357667516.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 186)
  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 186)
  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 186)
  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 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..186
                     /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=20333
     Region          48..180
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mrdeiralvd altpgdelet rhraaalawl agtadifrre kprtpsphlv ayfllrdead
       61 gavllvdhrk agmwlpsggh vepgedpaqt vrremveelg vpavfapvlg erpafltvte
      121 tvgppeerht dvslwyvltg srdqklipdp aefrgvrwwt paevaaapag tvephlgrml
      181 akvsrg
//
LOCUS       WP_357667518             297 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Micromonospora chersina].
ACCESSION   WP_357667518
VERSION     WP_357667518.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 297)
  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 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   3  (residues 1 to 297)
  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..297
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..297
                     /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=32078
     Region          7..291
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 mleryeietf ltlaeelhfg rtaerlrvtt grishvvrkl errigaplfe rtsrvvrltp
       61 igahlaeelr plvagiedav qravdagrgl agelrvayvg estapvllra valfterhpd
      121 cvvhvheapl attrsslrdg sidvliasyp fdgmangpal lherrvlava adhplagaes
      181 vslevladhp vvqypavtsa afkrdrtpdr tpsgrsvpqg pagtsfseml alvamgrgvl
      241 pvgeqtrhyh arpdlayvpi hdappirrgp vwlasntttr vrefvraavd anpapaa
//
LOCUS       WP_357667562             512 aa            linear   BCT 28-DEC-2024
DEFINITION  GMC family oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357667562
VERSION     WP_357667562.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..512
                     /product="GMC family 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=55954
     Region          1..511
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 meydfvivga gsagcvlanr lssdpsvtva lveaggqddk leirmpvafs klfrtdydwn
       61 ystakqqela grelywprgr vvggssslna qmwvrghrrd ydqweipgws ydevlpffqr
      121 aerrtggnag gvygeagpih iselrspnpv thaflracee lglhrlpeln gpsnegyspt
      181 pvtqrrgrrw saadaylrpa lkrpnltlit garvervvfe grravgvehd ggaqvrvrre
      241 vilsagaigs pyllmrsgvg dadelrqssv pvihelpgvg rnlqdhlasa vymscprpit
      301 ltkqaetign llrylvlgkg mlttnvgeav afirtaeqep apdielvfap gfffehglta
      361 ptehgltiga vllqpesrgr iglhgrdvvi dpgyltaead lrrlvaglrm arrlfataal
      421 gpyatapmap yqgqeseeel aqwvreraet lyhpvgtcrm gldeesvvdp elrvrglegl
      481 rvadvsimpt vnrghthapa imigekaasm lv
//
LOCUS       WP_357667610             267 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            chersina].
ACCESSION   WP_357667610
VERSION     WP_357667610.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 267)
  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..267
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..267
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30029
     Region          12..71
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          83..261
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mesaptaeli raqlrrlrlk aelsqeefgk lvhfsgsqvs avelgqrpld rfflkradev
       61 lgtgglltsl lklaerdgqp swlrpwleae rqaqqlrcyq ptlihgllqt enyaravirt
      121 ddmisddevd rrvaarmdrq svlfqsdppk ylavleeavl rrvdesfrgl maeqighlid
      181 caerphihvh lisaevsmhv glvgplslar grdggwvghm ehqlggvvvd sdedvaills
      241 rwesvrseal srqqsielmk dvrtsws
//
LOCUS       WP_357667621             259 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora chersina].
ACCESSION   WP_357667621
VERSION     WP_357667621.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..259
                     /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=27313
     Region          2..208
                     /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 mrvlvtgatg rlgrvalprl rdeghtvrav srrargdvgv ewvaadlatg eglaaavdgv
       61 eavlhlassp drrthqidvl gtrrlvlaag hagvghlvyv sivgvdrvpl gyyrhklaae
      121 qvvaagpvpw svlratqfpe fledllrsas rlgpvlgdpa vlaqpvdpge vagrlaamla
      181 agptgrieef ggpevlryde avrawraarg srrpllpvri pgrlgrelra ggltttatpt
      241 gtrtwadhla dtyggtgrr
//
LOCUS       WP_357667624             193 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Nonomuraea dietziae].
ACCESSION   WP_357667624
VERSION     WP_357667624.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=20074
     Region          1..189
                     /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 mivlasaspa rlallrsagl dpkvivsgvd eeavtailps dlalklavak atavaeglte
       61 glvigcdsil eldgrpygkp atgeealtrw rmmrgrtgrl ltghcvidaa tgrraaevgs
      121 tvvrfgtpse qeiaayvatg eplkvagaft ldglggwfve siegdhgnvl gislplvrsl
      181 fdelgyavtd fwr
//
LOCUS       WP_357667639             327 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Micromonospora chersina].
ACCESSION   WP_357667639
VERSION     WP_357667639.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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..327
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..327
                     /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=35689
     Region          41..261
                     /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 midkpgvder llaaevaaaw avevadlvfm pvgldgsawa yrvvtsdggr yflklrrgef
       61 nrsavllpgf lrahgvrqvv apvdlpgggt crefgdhqll lypfhdggsl wsrgltdrqw
      121 iqygeflrrl havtpsadia allpvetyrs sagerlrtvs geaaasetlg afwerygaal
      181 hrlsetvddl asrvtrgrhv ichadihpgn liadgdgplh vvdwdgpila paerdlmfvh
      241 sqdfgdhpin ahraalfrrg ygpwepdqtl lsyyrserhl ddvaaflrsi ldpgaspesr
      301 andlhcltri aeavadpgya nggarat
//
LOCUS       WP_357667694             847 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora chersina].
ACCESSION   WP_357667694
VERSION     WP_357667694.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 847)
  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 847)
  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 847)
  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 847)
  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..847
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..847
                     /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=89998
     Region          141..810
                     /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 mrggghdvtr tlardtgtdr rllllvglvv ftagisvlvs lrliaghglv tqanvtravt
       61 laflvavaat vnvririrat thgiswtdaa tvvglavapv pwvivatglg vaiartinrl
      121 ppiklafgia kemtlaaagg lvllaagwtw pwsgsigrsl palvlayltv vvldellmfp
      181 vlafatgtsi lnrfrqqldl rlasvlarfs vvlstllilr inptflvvvp plvlslhlan
      241 ssrvrsraer eawqrlartt dalnvvdldq vlttavtqat elfsadevdi elreegrlvr
      301 gaggvitfrg pagtpsgieg svlttrlegh dqtadigvlr lrfagpvels ereqytlrtf
      361 asalctavrn aqayaelari adehayaath daltglsnrr hlldegteql tnrhadgvta
      421 lvlidlnhfk evndtlghga gdrvltqvad rlraaarpdd lvarlggdef avllrglpap
      481 aiaahraeal laalhepldl dgmrisveas ggiavapasg gmpellrrad vamyqakrag
      541 qriatyaptr dtadlgrltl ggelpravad heftvnfqpi vdlgsgevig aealarwhhp
      601 thgmidplrf leaversgll pafaeaildq aliaagswrd agfdlpvsvn vsprslldar
      661 fpgavlarlr ahdlppdrlv leltetltls qldvvdrvls rlrdsgvrla lddfgtgyss
      721 lsllsripvh elkidrsfvt amestaeaaa virstldlgr sldltvvaeg vesepqrral
      781 welgcaagqg hlfarplpsg tllaalqrga ggrpgalapp lhdagavirl pgrrtgggrn
      841 rtatpap
//
LOCUS       WP_357667696            1015 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357667696
VERSION     WP_357667696.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1015)
  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 1015)
  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 1015)
  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 1015)
  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..1015
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..1015
                     /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=110802
     Region          1..246
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          122..1007
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          843..871
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          883..911
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(884,887..888,891..892,894,924,927..928,931..932,
                     934..935,958,961..962,968..969,972)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          916..952
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          957..990
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 maevrllgap eawcgstrlp lgtpkqqlvl amlalhggrv vttdalvdel wpeqpprsav
       61 anvrtyagnl rraferqngp tivrlpggyr idltdeqvdv prfehlvdaa atawsrgave
      121 sadallaqte rlwrgplvag lptgpvlaar raaldeqhls aielrarlel qlgrtrsaia
      181 fltdhvvahp yreqahalla raryadgdpv galaavrrae avlaeqlgie pgielrtlhq
      241 alldgepivt vppaadtgaa saagrtepta gtpasgnhlp rmvsdfvgrr elterlitei
      301 aaadgrtspv rvidgmagsg ktafavhlay rlagrypdaq lfidlrghae svpvdpadal
      361 tallrqlgvp agriptdhds raelwqrelr grravivldn aaggdqvrpl lpagpgsvvl
      421 vtsrrrlstg dvgppvplpv ltpaeavqll artvgeervg kepeaaaevv rrcghlplai
      481 rlaggrlahr pawqvadlad rlsaegtvlr qlaveqqtva raftasyepl aepvkrlfrl
      541 vsvhpgnrfd apmaaaladl pldrtewmld dlldqhliee igpgryrlhd lmrqysaels
      601 rgpaerrdrd daagrlldhv lhevarraqs ldplalrahl rldpprrpdl lghsappdve
      661 wleqersdlv alvrfaehvd lygygwrlar alwrfcymrg yfdeilvthr tgltaaersg
      721 draaqavmhn ylasaytrtg syldslrhle vavaisrelg dhgnehryra nlvvvhwltg
      781 dparsvslgr qllrdwpggv dpvpslpnlg yalttlgrya ealrahrqhl flgrcqgsgy
      841 hisnalghia svenrlghha kavrlitasl rlrdrtghrf geaearndlg iayrhlgrld
      901 aareqhelal dlardsgerh vqaavmndlg ltltesgrtg aavaahrsal alatriahpy
      961 eqgralaala dhlgederde alrfrqrala ifrrigaper tdleqrlspt angrg
//
LOCUS       WP_357667731             275 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora chersina].
ACCESSION   WP_357667731
VERSION     WP_357667731.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..275
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27917
     Region          30..256
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpadprdvlt rpapppdatv aygdhpdqca dlrrpagdgp prrlvvvvhg gfwraeydrt
       61 htgpmaaala alghpvaqve yrrtgqpggg wphtltdvla gvaalpglaa aalpglvaaa
      121 ppilvghsag ghlalyvaaq apatvggvla lapvadlaea yrldldsgav aallgggpae
      181 fpdryatadp sslvpartrt vvihgaldeq vpvamsrswv aaaraagspa tlvelpeceh
      241 fgliapdsaa wpqmvaalrs lhddlqgida aslsr
//
LOCUS       WP_357667861             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357667861
VERSION     WP_357667861.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   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 291)
  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..291
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..291
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30977
     Region          41..284
                     /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 mstprflslp pgvvevqiet pqgsfaalea splsgvierl pallvpgltg skedflaimq
       61 tlaaanrrvt aidmrgqyet qgpddptayt cpalgndvda iamaigeggp vhlvghsfgg
      121 lvtreavidg rtkfasftlm ssgpsgivgr reqagraiml elpefglehv witryepeal
      181 sggvpdeivs flrkrlfann ptglatmaeq vldqpdrtde lrqievptlv lygehddgwp
      241 pevqaemaer lgaeavvvpg avhspaveap ettaaaltrf wnaaetrkpa f
//
LOCUS       WP_357667872             129 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357667872
VERSION     WP_357667872.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 129)
  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 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..129
                     /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=13232
     Region          6..123
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 mrvncvgaii lddagrllli rrghppaegl wsipggrvea gesdaaalrr evmeetglvv
       61 tvgplvgave rpgpagavyv irdylatvea gtlapgddaa aarwcapadl allpltdgll
      121 daltswkvl
//
LOCUS       WP_357667880             627 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357667880
VERSION     WP_357667880.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 627)
  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 627)
  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 627)
  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 627)
  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..627
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..627
                     /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=66217
     Region          7..256
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          136..>620
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mgaavftvri kvlgpvaafr dtteiplgps rqravlgyla lhpgqpvpvg alteavwgdd
       61 apvsgdqlvr tyvarlrqvl epdtaprart nviasvpggy rldvppdrvd asqfqqllgr
      121 argrqaagap heafelldaa lglwqdptla dlggllaspr hltalradwv daglrhvavg
      181 lslgqasvvl pvaeqlaave plqeavqary lealtrsgqr aaavhhyltv rarlraelgv
      241 epgpelrrmy aallhagdep gpgveppsra gpdepdrrpg wrgpgpaigp ligreddvar
      301 catllvahra vtivgpagcg ksatglavae rvaaafpdgv atvdaaeard cgevlrllae
      361 tlelpgpnad plravadqrm llvlndvehl garagemveh alhrcprtam lvtsrrrlgl
      421 aheavfrlap lplpgtdapd alpdnpavrl fvhraglvrp gfrlapadav tvaricrgld
      481 glplaielaa aclytdsldg vlrrvddpld elrpqrrghp qhhrslraal hrslaalapv
      541 draclarlag gdrcfsrdea aarcaglvpp aqlgavldrl vdeslldarp gsggpryrll
      601 rtvalaaatv pesgehqafh gmvgnqp
//
LOCUS       WP_357667883             219 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent F420 reductase [Micromonospora chersina].
ACCESSION   WP_357667883
VERSION     WP_357667883.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..219
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22520
     Region          3..195
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mtvgivgrgr mgrglaeavr qaglhpllvp gradprrvad lldgaalvvl avpfpaavef
       61 lrgpagrrgr grtlvdptnp vfceppmvpp grsggellae laadraagpd hpaegwrvak
      121 afntvpagvl arcrvnglpv slpvaadhpa alrdvfalar algfapldag girtarhlea
      181 ltgllmavsd rqglrgqvsi higvpsgdrt vrepacrag
//
LOCUS       WP_357667849             299 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357667849
VERSION     WP_357667849.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   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 299)
  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..299
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..299
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32025
     Region          31..273
                     /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 mtepiehwpg rmigdvhvrs tpegaaaeqa vfvhglagsa tnwtdlmgel rdlvtghaid
       61 lpgagyspap edgdyslsah aravialmeh tgpahlfgns lggavavsva atrpdlvrsl
      121 tlispalpdl lprygparva aaatprlgew vadrlrllpa eqrinasfam cyadatlvhp
      181 srlreaveel rrrdglpyag raligsargi vaeylrlgeq nlwrqaarvt aptlvihgrr
      241 drlvrpatar ralrtfpqvr mvllrnaghv aqmevpaava aearrlilet rlgnaplpg
//
LOCUS       WP_357667893             623 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora chersina].
ACCESSION   WP_357667893
VERSION     WP_357667893.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 623)
  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..623
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..623
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=67090
     Region          120..>606
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mkrqlsvtvl gtvqvhdgta pvdlgpskqr allallalqv genipvgsla lalwgdnppp
       61 sgshllhtyv arlrraleps sprhartnvi assprayrlq lyadqvdltr frrlaeaare
      121 lvrrdrrsaa fellvaavam wtdpdltdlr allpgeeava alrrewvtvc ldlvtlglel
      181 drpaevlata ehlaaaeplh eavqarhltv lartgrraaa ldrfagirar laaelgiepg
      241 peliaahrel rdgptaarpa vpppgcvasr prppwrgprp gateligret dlarmtglla
      301 dhrvvtvagp agcgksalal aaarrvhagy adgvlsvdla aartpddvtr eirrllrlpe
      361 rgglprllad rhlllvldnv dhltdscagl vddvvqvgrr vsalvtsrep lglayesvwr
      421 lpplpalatg pdgvrgmpav qlfarraaqa rpgfevgake vgtvavicgl ldrlplavel
      481 aadrmadesl dellrrlddp ltalrrpdrr grpahqtsls aalqrsldcl tpaerwcfvr
      541 lgalprlfgl devdrvcgaa pwwrvrtsvv ldglvakslv tvrhhagrpt yamlrtvhqf
      601 aarllagelg qygstpalsa rvg
//
LOCUS       WP_357667899             173 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Nonomuraea dietziae].
ACCESSION   WP_357667899
VERSION     WP_357667899.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 173)
  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..173
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..173
                     /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=18236
     Region          6..>66
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mshlgerlsa lvdgelrhae reralahlaf caecrrevea tralksrlrs ldgpsmpadl
       61 tmsllrmgep gdpvpprerp fptfggvplp gprsiappdn rprgflggpa gpgrsrrrpa
      121 yvavgvvsaa valgtlfvva gqdqgpsvap pvevfkqvhk ttvpysnpps atp
//
LOCUS       WP_357667967             353 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357667967
VERSION     WP_357667967.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..353
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..353
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38050
     Region          20..340
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mktpyvvaaa lslsllaspa haetakpslp eptgakkvgt tslhlvdter rdpwnqeaaa
       61 relmvslwyp aarsggkras yltkeesaav lkdfdvppea ltatrvparv tappsrarlp
      121 lvlmspgftm pkatltslae dlasrgylva avehtyesva ttfpdgrttt clacvrgqdg
      181 akvaqgrvad lrfvldqlmr rdlvdrsria vvghsmggns aahtmladpr fkaaanldgt
      241 fapvvpkldk pflmvgttkh vpdgkdttwr qswanmtgwk rwitvagadh ssfvdyavlr
      301 pqlglpapel dgaralkitr aylaafldth lrgrdeplld gpstaypevr fdk
//
LOCUS       WP_357667981             383 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nonomuraea
            dietziae].
ACCESSION   WP_357667981
VERSION     WP_357667981.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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 383)
  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..383
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..383
                     /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=41417
     Region          12..382
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtahglpemp plllieddag daflveellq evekpptitw arsiaearqr fsrdiqcvlv
       61 dlslpdadgm ealrqvlama pdvavlvltg lndahvgiaa vaegaedflv kqdvdarlla
      121 rairyaierk radlahqrli qseltgrent rleygllpvp llpqgpvahq crylpgrqrs
      181 llagdfydtv qgpdgaihtv igdvcghgpd eaalgvalri awrtltlagi hgnealqtld
      241 tvlkherrsp eifttlctat idptlrhatm hlvghpppvl iregrldvvr ggpsgpplgi
      301 fpdvawraid vplgeewsml lytdglteat igggpdllgt dgllriideh ggidldriid
      361 rvteinreal sddlaavlis rkg
//
LOCUS       WP_357667978             894 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357667978
VERSION     WP_357667978.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 894)
  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 894)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 894)
  AUTHORS   Rosinski,J.A. 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 894)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..894
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..894
                     /product="helix-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=93425
     Region          <1..858
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          831..888
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlhgraeeqa qidrlvdgar egrsgalvlr gpagigksvl leyaalratg mrvvrgvgie
       61 seaalpfaal hlllrtgldr ihalpdaqvr alsaalglrd appesrflvg latlsllsel
      121 agdggllclv ddvqwcdeas vdalafaarr lgaegvamif aarpdlpvtg lpehrlagld
      181 dtaaaallpa dlppqvrerl vqesagnpla lielpaalta eqrtgrlspv gampvaeriq
      241 esflaqmaal peaaraallv aaaegsgela tqvaagaplh gleaaersrl igingtavsf
      301 rhpliraaay qsasvsrrla vhraladali sstspdaadr riwhlaaaal gpdegvarql
      361 eeaagrartr gghaavaaay qraaeltvdp vrrsarlaaa alaasdaglt draaalaasa
      421 tpdvddpami valtqvrahr evelgtplaa griildaavr vaardpeqat wllveavrca
      481 wfagdaplag qaatalhelp atgsplvgqa vglarllagd lagglpltgg aldpsgfagl
      541 gvpgltftag aalatgraal ceelteriva dcrrsgmigw lafalqdqgf aqglqgryge
      601 aratldaglr latdlghehr vihltcclaw vlahqqdvag craraedgvr raddrklvla
      661 aslgrwalgr lelgqgnada alerleripp tgfgalaaad lveaavrsgr peragepler
      721 yltwarhvrq pasdavalrc ralveqdeah faaavrahdg ddqpyeqart rlaygewlrr
      781 arrradartq lraaleifdr lgaeswarra rtelratgdv paaprragdp lsvltaqere
      841 vvrlaaagas nrdiaaqlfl sprtvgyhly kafpklgits raqlatlagv aaae
//
LOCUS       WP_357668038             947 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357668038
VERSION     WP_357668038.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 947)
  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 947)
  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 947)
  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 947)
  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..947
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..947
                     /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=102485
     Region          3..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          135..946
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          738..766
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(739,742..743,746..747,749,779,782..783,786..787,
                     789..790,819,822..823,826..827,830)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          777..807
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          818..846
                     /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"
     Region          898..926
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 matiqvrllg pvdvtegdra rpvpglrrka llaalalhag davhpdllid ivwngtppat
       61 aknslqrhis ylrgvlggra aiavrphgyv ldlppeatdl hlaqrliges rhpaepaera
      121 valraalalw rgrpladlag lrwldeqaer laglelsare alldarlalg ehaslvpela
      181 rladehpyhe qihhrlmlal yrggrqvdal aayqrlrtal atdlgvdpsp alcrlhaail
      241 rqdadlappa mgeparvtga pagrpapsgp vpaqlpmavr gfagrrpela rldallraar
      301 tsradqpgtl piavvsgtag vgktafavhw ahrvagefpd gqlyvdlrgf adhgcpvdpa
      361 aairsfldaf gvpaqripve ptaqaalyrs mlagrrvlvv ldnardaaqv rpllpatpgc
      421 lvlvtsrtel tplvvsegah pltldllstq esrellagrl gadrlatdpg avddliarca
      481 rlplalavva aravtrpdfp latltaelrr aaeepdaald pfdggdlatd iravfswsyr
      541 tltteaarll rllslhagpd iaapaaasla grsaalvkpl laelarahll gelapgryac
      601 hdllhryaae lahthddaga rqrarhrmld hylhtadgaa rlldphrdpi tdsahepgtv
      661 ptvlasytea lawfraerlv llaavaqatr tgtdrrawql awtlldflda haywhdlaav
      721 qdlamtaarr lrdrrgeaha hwglararak lgdhedarrh fqralelfeq tgdrtgqaht
      781 rlnlawvldr qgryaealph arealalyqa lghvagqadg lnaigwylth lgehrqalgh
      841 crraldlhqr tgdrrraaqa wdslghvhgn lgdheratec yrnalaltrq lsirydetiv
      901 lthlgsarra agdreearaa wrhalaileq lnhpdaeavr vqlagls
//
LOCUS       WP_357668161             394 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora chersina].
ACCESSION   WP_357668161
VERSION     WP_357668161.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   ter Beek,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 394)
  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 394)
  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 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..394
                     /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=39999
     Region          9..393
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mrsrlraadl lpvstvglrs rpgraalsil gvaigiaavv avlgvtrssq sdvlaridrv
       61 gtnlltvsng ktirgeearl pvtastavar tdgvltsaat amldvriyrn drmpagrtgg
      121 lsvraadpal latldgalvd grflnaatag ypavvlghya atslgirrvt gnpqvylghh
      181 wytvvgimap velapeldas aligasvaad qfgydgrptr ifvraqtert devagllgra
      241 anpahpeeva vsrpsealta rlavtggatv lllglgaval lvggigianv lvisvlerrg
      301 eiglrralga trrhiaaqfv veslllgagg gaagvllgat vtyvmsvvrg wqmlvpaaai
      361 gaglaaalli gglagvypal raarlspata lrta
//
LOCUS       WP_357668197            1002 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357668197
VERSION     WP_357668197.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1002)
  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 1002)
  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 1002)
  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 1002)
  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..1002
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..1002
                     /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=107417
     Region          8..255
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          146..1002
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msrdneptvs fgvlgtvelq vagrpatpla pavrallarl vlaagrvvsa daltdalwge
       61 rppsdatnal qlrvsklrra lvaagaggdl lvtrapgyql vvavdavday rferlleaar
      121 sattgdgpaa alarfdealr lwrgpaladv gdadwalaea arleelrlga vedrlellle
      181 agrqaeavad leqlvathpl rerlhrllml alyrggrqad aitayhalrh rladelgidp
      241 apelqalaea ilrqqvpapa paappaappa rtaaappart avapplpvpr apqrgdlprr
      301 lasvigrqdd vrrvldrlre trvvtltgpg gvgkttlale varraddtla drvhlirlaa
      361 lpsgtdlpea vagqlgvpag gpgaaataal vawlgadral lvvdncehvi deaaelveqv
      421 vaacpavtvl ttsrealavp getqlavapl gvpdgpadla rlgdspaval fvdraravrp
      481 gfvldettap vvadicrqld gmplaielaa arvkalppge iaarlhdrfa lltagartse
      541 arhrtlratl dwshdllsea errllrrlav frggwdlaaa eqicafdgla adevldllfr
      601 lvdrslvvpd pttgrfrllv tireyaaarl aeageteaar drhlthfteq aerygphars
      661 dgdawarlte ehdnfraaid rcldrrdgvd aglrladalf lfwnygprye gvraltalla
      721 agiptpaara aalqrigllg vyyptaqtra aardsvlafe rlgdpvntat srlvvawegq
      781 ydgdpdryra mvaqavrerg dtddpwwhgt vhyvealldl rtgafersae qwarslewtr
      841 kagdlllpag ilahlgialr eagrpdeaia tleeaaaear rnpsphataf tlvqlahtrl
      901 drgevdgvta mlaeaddtar rsgnprcqaw sawgrariry adgdaagaad ecrraldllq
      961 erefpwarrr lwflaadaas aagrpqeada arraaedlta er
//
LOCUS       WP_357668539             134 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357668539
VERSION     WP_357668539.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 134)
  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..134
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..134
                     /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=14248
     Region          36..>107
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdvlsvklg telhkcspsl ptrvadapap pcspwralle elgpealtmd atakrarvtr
       61 rtvylhfpar adllralydh vaeveglads irpvlsapda italdracwr shgpspmppt
      121 clgrsklppp aagp
//
LOCUS       WP_357668591             307 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Micromonospora chersina].
ACCESSION   WP_357668591
VERSION     WP_357668591.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 307)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..307
                     /product="phosphotransferase 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=33417
     Region          8..241
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mdlshlgapi gpmvrvhggf anrmyrldtd qgsfavkeln lldrrwtyra edvfrferaa
       61 faagipmpep isashdtlvh rwvegekvpe apvspayafe vgeilariha ldvawtdvsi
      121 edptardwpe laaratatgq pwageltsrv etflaiahfv dtcerpgpvv lthrdihpwn
      181 llaregrpvv ldwelsgmld lsgelgstal slakgpgfdd iepaifrsvl dgyvagggal
      241 ppsgpswfvf misgwlghtr wnilrclagv eastgpdlal shesvrngvr glpdlfgrlp
      301 efeallg
//
LOCUS       WP_357668593             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            chersina].
ACCESSION   WP_357668593
VERSION     WP_357668593.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..295
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32382
     Region          35..>82
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          118..281
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdnrddvrqe vreflttrra ritpdqvglp ttgsrrvpgl rrsevaaiag lsveyyarle
       61 rghvagassg vlealaralq ldeterahlf dlaraadgip tsgrprrrta tkaasrlslr
      121 walaaikdgv afvrdpqqnl latnalgraf yspvvgdggr lpnlarfqfl dptsrdfypd
      181 wdlfaemcvg imraeagrdp hdrglqdlvg elstqsetfr rlwadhnvrt hgagtkrfhh
      241 pvvgeltlay eelaitaepg lvlmiytaep gspsaerlrl laswaapadv pvrnl
//
LOCUS       WP_357668637             360 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea dietziae].
ACCESSION   WP_357668637
VERSION     WP_357668637.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..360
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..360
                     /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=41042
     Region          3..327
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrdkyvdwlr alslitvvvw hwaftilqws pegpsptspl gftsglwilt wlfqvlplff
       61 yvggyvhlls wnracergtg igafvwrrik alaipgltlt giwigigagm tmlfdipwmw
      121 rvvllvlspl wflivylvli allpvalwlh rrydvlaliw lggaalvvdv irlrygvewv
      181 gwlnmiliwg lahqagffye rvvvlprryd vailwtglfg lfglvysgly pgsmvgvpgd
      241 klsnmapptf vivcllifqi glvevlrptm ervlerprwk rvnetinrfa lplflfhttg
      301 maialglwwg lfgfpsadpr pnlmwwlerp faivgpllct lpviylfsrr krvdrapapa
//
LOCUS       WP_357668677             481 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-amylase [Micromonospora chersina].
ACCESSION   WP_357668677
VERSION     WP_357668677.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 481)
  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 481)
  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 481)
  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 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..481
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52469
     Region          38..387
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(82..83,86..87,122,125,180..183,213,215..216,
                     218..219,241,243,248,304..305,310)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(124,185)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(215,241,305)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          393..479
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 mhrrrcrsaa lalglvasll vpttvaappa aastpgskkv ivqlfewnwt svanecttvl
       61 gpkgygyvqv sppqehvkgn qwwvayqpvs yriesrkgtr aqfqsmvntc hnagvkvivd
      121 avvnhmsgqd nggtgwagst yghydypgty gsqdfhycgr ngnndivnyg dryevqncel
      181 vnladlktes dyvrtrlaty lndllslgvd gfrldaskhm paadiaavkg klsrsaylvq
      241 eviygagepi qpteytgngd vhefrygkdl armfnserla ylrnfgeswg ylpggsavvf
      301 tdnhdtqrdg gvltyrdrge yalanafmla wpygtpavms sytfsnkdqg ppsdasnkts
      361 nttcysgwec ehrwrvianm vgfanatqga gvanwydngw qhiafsragk gyltlndedf
      421 aitgrsfytg lpagrycdvi hgdfsngscs gpmitvdang wfaatvnahd aiaihigakl
      481 s
//
LOCUS       WP_357668669             110 aa            linear   BCT 28-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Nonomuraea
            dietziae].
ACCESSION   WP_357668669
VERSION     WP_357668669.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 110)
  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 110)
  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 110)
  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..110
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..110
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11868
     Region          1..109
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 makqiqeili ddldggeane tvsfaidgas yeidlsvdna kklrdalspf qqaarksgaa
       61 aarrrvrggt rsmsreksse irqwakahgl pvsergrias tvvekyeaah
//
LOCUS       WP_357668756             145 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357668756
VERSION     WP_357668756.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 145)
  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 145)
  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..145
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..145
                     /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=15602
     Region          16..140
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msdrgellsa talttfrlng qflevseela rpagltasww qvlgavlhep lpvagiarvm
       61 gmtrqgvqri adllvergla eyqpnpahrr akllrptpeg raavekitpg haalaarlae
      121 elgeaewaai lealqrlsaa ldrlq
//
LOCUS       WP_357668777             359 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357668777
VERSION     WP_357668777.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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..359
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..359
                     /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=36671
     Region          1..358
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mirvgvvgas gwagashlpa laglaefevt avattnqasa draaaahgvr hafadagala
       61 ahpdvdlvvv svkvpehakv iraaldagkh vfsewplgvn adeareltea ataagvvhav
      121 clqgyhspga rfvgdllaeg rigalesavm vaagdplgga tirpelawst dpalgqsilt
      181 imaghflatl drvaggltev sarlprlhdq vlvagtersi psgvpshvll hgllesgaha
      241 svtvhggdra vpdgfllkfa gakgtltvtp vqpgmfmhwa dweitldgep lavpesyrsa
      301 psgipsgpaa svagvyleia ravsegrpph pgfdtalrlh rllatiersa stglpqeis
//
LOCUS       WP_357668813             179 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea dietziae].
ACCESSION   WP_357668813
VERSION     WP_357668813.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 179)
  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..179
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..179
                     /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=20026
     Region          5..160
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mpnpherfia lyntyqarvy gyaasraghq laeevvsetf lvawrrlnsi pehaqlpwll
       61 rvarnilrdn frqaarrasl eaelrtwmde aaadvgehat ervavlrals glseadkeil
      121 tlttwhglst teaaqvlgct kaaffvrlhr arrrlqsaid vtgttasrkp vtvpgrklr
//
LOCUS       WP_357668332             290 aa            linear   BCT 28-DEC-2024
DEFINITION  LLM class F420-dependent oxidoreductase [Micromonospora chersina].
ACCESSION   WP_357668332
VERSION     WP_357668332.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..290
                     /product="LLM class F420-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31896
     Region          9..235
                     /region_name="F420_Rv1855c"
                     /note="probable F420-dependent oxidoreductase, Rv1855c
                     family; TIGR03560"
                     /db_xref="CDD:274648"
     Region          <238..290
                     /region_name="dnaE2"
                     /note="error-prone DNA polymerase; Validated; PRK05672"
                     /db_xref="CDD:235553"
ORIGIN      
        1 mrlglhywnf stpadpstma gtlaetaria eqagvsafsv mdhyfqmeft tsaeepmlea
       61 yttlgyvaar termtlgvlv tgvmyrypgl lakivttldv lsggrarlgi gaswydreqr
      121 glgvpvvpva erferleetl riclqmwsdd ngrfdgrhyq laetlnvpap isrphppimi
      181 ggggekktlr lvaryadacn lfgnspaeva hkldvlrehc aaegrdyeai dktvlvmrpp
      241 lpdvdafvae vaeyaalgvt evqtmpdrhp vefarelaeq rvaarlaela
//
LOCUS       WP_357668827             214 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357668827
VERSION     WP_357668827.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 214)
  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..214
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..214
                     /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=23139
     Region          16..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrvtatgpdp edltararir daamqhfaeq gferatirgi aetagvssgl vrhhfgskqg
       61 lreacdahla kmirrlndev rsghaldran pvatahaamg pyqrylaral vegsaetvfd
      121 qmvelteewl aeadekrpdt pdvdrrarat vgtamalava vlhkhvsrgl gvdlytpegd
      181 lllartlidi yshpmlsved aaevraaldn lspg
//
LOCUS       WP_357668834             312 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357668834
VERSION     WP_357668834.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 312)
  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 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   3  (residues 1 to 312)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..312
                     /product="GlxA 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=33872
     Region          5..309
                     /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 mpkfrsvaay apqgvtalgl givneifnrs gfdfaicaer pgtlrtdlgl plpvehgldt
       61 laradlvlal pgmefradpp qavlsafrda yargamiaah cvgtflpaaa gllddleatt
      121 hwrfatdlaa rhpavrvrpe slyidqgrli tgagavagid lclylirreh gaatanriar
      181 dlvttpyrsg gqlqylpapv addgdderls eviawaranl drrisvddla sralmsrrsf
      241 arrfkaatga tphawllaqr lnlaeellet tdlpveniah hvgygsaavf reqfalrrgv
      301 pprdyrrafk qg
//
LOCUS       WP_357668846             258 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357668846
VERSION     WP_357668846.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 258)
  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..258
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..258
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27398
     Region          12..253
                     /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 mmnglphlsi gqgpplvvll ytpraadpeg parwsmtrml rpfaehftvh vvirppglpp
       61 dttmaelaav yagaieatfe epvkvlaist ggsvalqlaa dhpglvdrla lggtaatlgp
      121 vgrraqrayi erarqgkrps palaevvtds aigrrllagl lwlsdgggad htdavtmlna
      181 edgfdlrgrl gdiraptllv qggedvvypv elarqtvegi pdarlivyqg rshngtftdr
      241 rfardtlafl krtpplgp
//
LOCUS       WP_357668862             269 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357668862
VERSION     WP_357668862.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..269
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29265
     Region          7..269
                     /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 msyleladgv plyyedhgsg pavllihgwt mnstfwgqnv galsasnrvi tvdlrghgls
       61 gktddghtls qyardicall qhlqvsdvsm vgwsmgtavi lsyvqqfgcd llrsaafvdq
      121 sprfldgegw dfpllggyst ndlavfaqgv ryarpsvikp fiaacfaetp pdevidavya
      181 ettkmatsaa lsiwydmaya dlrpvlpels vptllmygar skifpgdlde wlagrlpkaq
      241 varfdhsgha pfseesdkfn etlgaflrs
//
LOCUS       WP_357668892             276 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora chersina].
ACCESSION   WP_357668892
VERSION     WP_357668892.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 276)
  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..276
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..276
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29150
     Region          28..271
                     /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 mrpsppgrfg paelrlalaa prpaagltse frlvgglrth trrsadpggd atpvvlvhgl
       61 avshryltpl alalsathpv yvpdlpgfgl terpgraydv prhtaflaew laayrlgpvc
      121 llghsfgaev aaalaarrpd lvralvlagp tsdpaarsrr gqigrwlvdt vreakwqapi
      181 llrdvldarp wrvfatlshs vrnsieadlv rvtaptlvlt gardpvvpag wrtdaarlvp
      241 dartaavpga ahnvattapg pvadairgll apvlrr
//
LOCUS       WP_357668905             370 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Micromonospora chersina].
ACCESSION   WP_357668905
VERSION     WP_357668905.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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..370
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..370
                     /product="LolA family protein"
                     /calculated_mol_wt=38409
     Region          44..259
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 msvlknravl rwlvpvtagv avigggaavg tfaagadpal pprtaaqlle dlrtsrldgl
       61 sgtvvqragl glppiaelag kaggnelasl vsgthtirvw yagpdrqrla lvdtlgerdv
      121 lrngrdvwtw ssrdnaashr tlpaegkdld tapatpadaa dralaaidps tavtvgrsat
      181 vagrsvyelv ltprdrdslv hqvrialdak ehvplrfevl adgsdepafe vaftqvdfrt
      241 pdadqfrfnp ppgvkvtees agdghgpagk rpagrsedrp dvrtvgtgwt tvlvakidaa
      301 gdatggkpge atgpdaeals kllgglqrvs gdwgsgrlls gklfsvlltd dgrvlaglvt
      361 perlyqaakg
//
LOCUS       WP_357668898             318 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora chersina].
ACCESSION   WP_357668898
VERSION     WP_357668898.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..318
                     /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=34907
     Region          58..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msdlpliqad ravpppaatt ttrgrgrrlr llsrtdrvvi tlmvlvplll vvglvwlpaa
       61 atvllsgtnw dgigplgeid wvglknyddv vniyppfvpa vqnnllwlaa lfvvatpfgm
      121 flavlldkel rgsrfyqtal ylpvvlslal igfvwqliys rdqgllnall gtqtdwygdp
      181 nvniwavlfa agwrhvgyim llylaglkgv dpslreaaav dgssetstff rvvfpvmrpi
      241 niivlvvtvi eslrafdlvw vinkgrngle llsalvtqnv vgeasrigfg salatlmlvv
      301 slvfitlylf tvmredrr
//
LOCUS       WP_357668922             229 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357668922
VERSION     WP_357668922.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 229)
  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 229)
  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 229)
  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 229)
  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..229
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..229
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24968
     Region          27..217
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mslssdtapv vahdrrihqp sgperyvffd vdgtlidald nqrrvwrmwa arhgldpdev
       61 yrvalrtrpl etfaavapdr dphtslavlh elededvrsg vytafdgase llhglppgsw
      121 alvtsnyahr vrgrflrtrl pipevivdaa aveqgkpspa pyllaaerfg vtpehclvve
      181 dapsgvqagl ragmtvwnvn tpvavgeahr hfeslrdavs dilafvsgg
//
LOCUS       WP_357669018             390 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Micromonospora chersina].
ACCESSION   WP_357669018
VERSION     WP_357669018.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=39638
     Region          3..388
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mtgfgtaavh gddglvpgga vappivqsat fsaesderft eiateprgsa fytrygnpnh
       61 aqvaavvael egaetglvta sgmgaistva lallsagdhv vvqrstyggt tslatgllpr
      121 fgvactqvdq tdagaferal rpetrlvlve tpsnpllelt dlaavvasah aagalvvvdn
      181 tfatpvnqrp lslgadlvwh sgtkflgghs dvsagvvvgp aglvervwqt aivtgstlgp
      241 vdawlllrgi rtlplrverh nanalalara leghpavarv rypglpshpq halarrqmag
      301 fggvlgvelt agragaaall aglklakraa slgsvstlvv hprsmwagiv daaqlaaagi
      361 sdglvrvstg iedtadlvdd flaaldrapa
//
LOCUS       WP_357669096             277 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora chersina].
ACCESSION   WP_357669096
VERSION     WP_357669096.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=31293
     Region          5..248
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mtgalfavsd lhvsyaenrt vvdglrpesg ddwlivagdv gevfadiert lrqlrdrfar
       61 vvwvpgnhel wthptdpvtl rgkarydalv gmcrelgvlt peddypvwhg dggpvtvapl
      121 fllydysfra pgtnskeesl raayaagvvc tdemllhpdp hpdreswcwe riaeterrla
      181 dvdpalptvl vnhwplvrqp tdvlwypefa qwcgtdrtad whlrhraava vyghlhiprt
      241 thydgvrfee vslgyprewg rrggeprpmr rilggaa
//
LOCUS       WP_357669155             203 aa            linear   BCT 28-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Micromonospora chersina].
ACCESSION   WP_357669155
VERSION     WP_357669155.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 203)
  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 203)
  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 203)
  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..203
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..203
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=21244
     Region          1..202
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mrirpvgaha llldcespeq veawraelwr rraagelsav eivpaaatvl vdgvpdpavt
       61 aariagwtpe gvaatagave vrvptvydga dlpavaehwg vdvpavverl hrtefrvafc
      121 gfapgfaylt glpaelavpr latprtrvpa gsvalagpya giyptaspgg wllvgrtdlv
      181 lfdvhddppa rltpgtrvrl vsp
//
LOCUS       WP_357669213             213 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357669213
VERSION     WP_357669213.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=22902
     Region          14..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpnptdappl agrraqaarn davileaara vflddpkapi aavaeragvg isalyrryas
       61 kedllrklcd dglrrfiaaa eeaaaepddw safagflagv vdadvhsltv hlagtftpte
      121 emsraavran elveglvera rkagrlrpdv vaqdvgllle gcaairvpdp ertrqlrrrh
      181 lalllaglaq aepplpgppp aagefdwrwk rre
//
LOCUS       WP_357669030             300 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Micromonospora
            chersina].
ACCESSION   WP_357669030
VERSION     WP_357669030.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 300)
  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 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   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..300
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..300
                     /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=32461
     Region          11..297
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msdheavvpr rvvvtgaagk lgravvahlr avgvdvlavd raggrdprdv dgefllvdlt
       61 dygqvveaft ggadehaggv gavvhlaavp apglqpnavt fannsaatyn vfaaaraagi
      121 krvvwasset vlglpfdtpp pyapvdeeyp prpestysln kaleeemarh fcrwdpdlvm
      181 vglrfsnvmd vedyaafpsf qadprlrrwn lwgyidvrdg aqaveralah drpgadvfvi
      241 anadtvmnrs saelmaevyp dvevrgelge hetllsidka rrvlgyeprh swrdhvdpag
//
LOCUS       WP_357669237             281 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357669237
VERSION     WP_357669237.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   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 281)
  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..281
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..281
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30793
     Region          4..276
                     /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 mpdielsagr idytdtggsg etvvlvpgla fdesvwqavv ddlradfrvv vpvlpigghr
       61 rpmrpeadls aqgvadvlae fmerldlrdv tlvqndagta qllvgvrdar igrlvltsce
      121 alenyppgvq grtlhaaskv pgglflllqs frvpflvrmr tslggmakrp ipyelvrrwy
      181 gplltdaevr rdfakfcgsv ekdtylraae rlrgfrgpal vawgaedrmm ppetgrrlaa
      241 llprgeyvei pgsrtlipld npgglcaelr rfiketstar t
//
LOCUS       WP_357669221             298 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357669221
VERSION     WP_357669221.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  AUTHORS   ter Beek,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..298
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..298
                     /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=32102
     Region          33..298
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 madtavlpar rvgretaapp rrrrrgrltp llyvlpalif yaafvivpwv hslwislwew
       61 ngigvatwag lanyievftd salrsslvha fgfivfysvl pigiglvlaa lvaatpwkam
      121 plirtilflp qilplvavgv iwkwiysadg plgldsswlg dftlaypavg lvgtwvstgl
      181 cfllllsgig kiepslyeaa kvegcgpire fwhvtvpglr keiavaatvt iiaalasfdi
      241 vyvmtgggpg yttmvpgvqi yqlvftagrv gtacalatvl slltcavmyg lnrltrer
//
LOCUS       WP_357669333             360 aa            linear   BCT 28-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Micromonospora chersina].
ACCESSION   WP_357669333
VERSION     WP_357669333.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..360
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36452
     Region          80..232
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 mgasqrsavr rtgqvltglg alvvlcavlv ggpvallafa gnplpdhlpt laevgtalts
       61 rddgqlflra lavvgwfgwa tfafsvlvel lagalrrpap rlpgmrrqqr aaaalvgsva
      121 lilaaspaaa saatlaapqp vaaapavvap qaghtapqag aaqaalaapp vraasvttsp
      181 avyrvakgdy lgevadryld dfdryrevar lnrladpdri rpgqllrlpe gavdagarrh
      241 atgrlvvtpa gpsrpapgpa tapggggass ttpkgkpsph ptgrdttptv eapagqqpam
      301 stgasratve dginrplais avlavasivg aqigavlglr rrpvprttvr dlmvgrhrrd
//
LOCUS       WP_357669344             475 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357669344
VERSION     WP_357669344.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 475)
  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..475
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..475
                     /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=49728
     Region          8..249
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,31..32,57,62,67..70,81)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,35,37,65,80..83,87,89,122,124,
                     126..127,129,138..139,142,158..161)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,35,37,65,80..83,87,124,126..127,
                     129,138..139)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,87,89,122,124,126,142,158..161)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(138..146,154..161)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <219..392
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
ORIGIN      
        1 mtpsfigpyr vvrplgeggq gvvylatapd grpvavktlr egfagddrfa keiaaarrve
       61 pfciaqvlda slsgrpyivt eyvegpslqe agrhlgadlq rlaistatal aaihragvvh
      121 rdfkpanvll grdgprvidf giaraagsal tvtssvvgtp symapeqvag aevgpaadvf
      181 awagvmvfaa tgtppfgrgs lpevirrvqy deplldqvpd alrpivaacl dkdparrptm
      241 qdvlfqliga rpparsapag rrrrpalvag aaalavtcva gatwgaaelw ggpgthasvp
      301 tdtastgsaa lpakgrspaa tgkrptprpg ksrtsakprs tptvsrtsep tgrptsrpms
      361 sptsrptgsr saepsqgtgg vssvslrpeg irmsgcwrnd lniyvdvkas grfsyrwlvn
      421 gqnrgrheaa sgdkvvlpsi twqgagsyrv vfevitpssv rrsvtveicd syegw
//
LOCUS       WP_357669390             226 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora chersina].
ACCESSION   WP_357669390
VERSION     WP_357669390.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=24618
     Region          10..183
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtasipqlpl rdelfllghh ddtgqphlhr qalalgmagg vlidlflagr itldsyddhp
       61 aadrwlrvns ehpvgdliad taltaihhsr tiptmkaflr sfaddlyert raglvaagil
      121 rhtarrrlgg lvradtylat dtkwavvara rlrylaagre qpdnhtaala glvavlgltd
      181 hlyldddttt ltthlktiae qhhrpvreit aavdaavgdl atatyr
//
LOCUS       WP_357669596             383 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora chersina].
ACCESSION   WP_357669596
VERSION     WP_357669596.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=42615
     Region          1..380
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mertsigiil ngvtgrmgyr qhlvrsllai reqgglpard gsriwpeltl vgrneaklae
       61 iaarhgltsy ttdldaalad dshqiyfdaq vtaqrekair aaieagkhiy tekplaeglt
      121 gslelarlaa argvkngvvq dklflpglrk lkrlvdsgff gqilsvrgef gywvfegdwq
      181 daqrpswnyr aedgggitvd mfphwhyvle qifapvtavt ahiathiper vdetgqtyra
      241 taddaaygif elaggitaqi nsswavrvyr delvefqvdg thgsavaglr ecriqhrgat
      301 pmpvwnpdlp vtenfrdqwq svpdnedfdn gfkvqweafl rhvvdgdpfp wdflagvrgv
      361 qlaeaglrsa regrrieiee irl
//
LOCUS       WP_357669628             373 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Nonomuraea dietziae].
ACCESSION   WP_357669628
VERSION     WP_357669628.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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..373
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..373
                     /product="LolA family protein"
                     /calculated_mol_wt=38311
     Region          <97..262
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 msrgklvrwg vpmaavavig aaigagpvia avsgdpvlpe rsaqqllaea aaavqkdglp
       61 pmsgtvleta slglpalpqt asagspiall sgsheakvwy gsrdqfrlav pgpmnetnvi
      121 vngdqtwvwd sqsntatrvk iapgaektht apptgpsmtp qqaaeqllsk vgehsvvsvt
      181 sntqvagrpa yelvlapkea gslvqdvrla ldgetyvplr vqvyakgsae pafevgftqv
      241 tfsapapenf tftppagakv eektlgfskd eekrdfaege vktvgagwtt vavlptpkip
      301 aapsqgqreg qgqgqeaaaa ldtvlrsatp vsgawgsgkl iktklvsalf tddgrllvga
      361 vtpeeltkaa gak
//
LOCUS       WP_357669630             448 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357669630
VERSION     WP_357669630.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=48182
     Region          132..447
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 madsplarwr rrslrfrlta laavalvlaf avsastlmtv lgrslmdtvd ettrqhaqav
       61 raqadsgtlt dpittqdgti vqviaangri thgtygadrl vpllpahdrr raqshegawf
      121 rdgapygipg plrvvvvsgd dgitvlaarp vaeiqksltv agrvlfvgtp llvaflagas
      181 wliigrtlrp iaalrkgaae ithtarsrrl pvpeardevh slavtlndml arlegaesrq
      241 ralvsdaahe lrsplasirl qlevalghpe gqdwretaeg vledtlrlsr laedllalar
      301 lderggrlar nepvnleevv rqvverygea rltacepvvv rgdaldlsrv ltnlmdnavr
      361 hatgkveval radgeltvsd dgpgipeqdr ervfnrftrl ddgrgrdegg aglglaivre
      421 tvrahggtvh ledaapglra vvrlppaa
//
LOCUS       WP_357669651             173 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora chersina].
ACCESSION   WP_357669651
VERSION     WP_357669651.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 173)
  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 173)
  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..173
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..173
                     /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=18879
     Region          8..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtqprwlnpe eqrlwlaflr mrraidvaid gqlaeaglsp adydvlapls qsgkalrvrd
       61 laaqigwdrs riahqlrrme qrglvvrsgs ttdrrgtlvh ltdlgrtait taapghvetv
      121 rrvlfdqldq heltqlttia ervadaaglt gisrtggpap raaahegrqg lep
//
LOCUS       WP_357669682             294 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357669682
VERSION     WP_357669682.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=31857
     Region          3..288
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mnrrvkaapy lfltpaivlf tlflalpicy tfylsmrrvk vsglglgkgs rqeifvgldn
       61 lsaavtdgel wagwlrvlgy galvlvvmlg lallfallld sahvrlarfs riaiflpyav
      121 pgvaatllwg flylpslspl ralldvdflg attvtysman vavwggvgfn mlvlytnlra
      181 iprelyeaar idgatetqia lrvkipilvp aiilttvfsv iatvqvftep ttlrpltnti
      241 sstwsplmkv yrdafvtgdl ysaaatsivi aavslvlsfg flrvvrgraf gees
//
LOCUS       WP_357669698             427 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357669698
VERSION     WP_357669698.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   ter Beek,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 427)
  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..427
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..427
                     /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=46802
     Region          1..326
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mstvvldkvt kvypggylav drlslraedg eflvllgpsg cgkstllrmi agleevthgd
       61 lwldgqlanh laprdrdvam vfqngalyph rtvrgnmafp leiskadpal vrervtelsk
      121 alhidetldr rpgtlsggqr qrvamgraiv rqpkiflmde plsnldagmr telrmeissl
      181 vrslgvttiy vthdqvealt ladriaimnr gvlqdvgtpg qiyndpataf vaaflssqql
      241 nllaatvhtp qnqyvlldfg phqlvipwsd prayaisqht ggqiivgirp dglapvqesy
      301 egpsfygrvr aleyhghewl ayvecgvpav avpeppdprq nangndgggg glramvrrmf
      361 gsepdehaqq eqvghnlrdg hhrradlivr lgvrpawrtg daakigvdvt rlmlfrldgs
      421 ridpprr
//
LOCUS       WP_357669742             319 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357669742
VERSION     WP_357669742.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (residues 1 to 319)
  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 319)
  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..319
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..319
                     /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=33368
     Region          1..239
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 madlawgiaa tggiartvga viaaepgmrv aavgsrdrgr aaqlaatlga esaygsyadl
       61 cadpavdvvy vatphaqhle vaeaaiaagk avlcekplaa sladaermvk larqagvflm
      121 eamwmrfnpl irgllteerf galrsvqasf gfvlpyqeeh rlwnpvlggg vlldlgiypf
      181 glaqlllgep aethltgsla psgvdaevga lltyeggara lldtslispl antatvvgtg
      241 lradiaapfw apqritlsgp gfeteehvld palngyagei revrealaeg rtesaimpld
      301 eslammrmle earvrlgar
//
LOCUS       WP_357669755             300 aa            linear   BCT 28-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Micromonospora chersina].
ACCESSION   WP_357669755
VERSION     WP_357669755.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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 300)
  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 300)
  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..300
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..300
                     /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=33067
     Region          10..282
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 megtptgfpr eavatrllaa svrtsydpvv didwsaphvp gaywmppers slygtslwtg
       61 lseeqrvelt khevasaasa glwfetilmq mlirhyydad ptsrhaqyal tevadecrhs
      121 imfgrlieam gcpvyradpv dhllgrwlka tatgprmyaa iliaeeilda fqreamades
      181 iqplirmvsr ihvveearhv rfardelarq veaagpvgla yarvvigraa ysitrrlvnp
      241 rayaavgipp aagvaaaran phwratlrws aqriaehltd lglvagpgrl lwrragligd
//
LOCUS       WP_357669811             849 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora chersina].
ACCESSION   WP_357669811
VERSION     WP_357669811.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 849)
  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 849)
  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 849)
  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 849)
  AUTHORS   ter Beek,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 849)
  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 849)
  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..849
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..849
                     /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=87019
     Region          21..849
                     /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 mfratmksll arklrlllsg lavvlgvmfv sgafvltdtl grsfdavfsd afsevdvnva
       61 akpkvalsev egeqvaaplp asvvdrvkav pgatdvrgvv nadgarligs ngkvvtsfgp
      121 pqlgenwlge sdllklregr apqaddeivv nvaladaakv kvgdrvgvlt lapkkeftlv
      181 gvfgysggrd svggvnevaf ttpvaqqlml gkpdvfsnvt aqaadgttpe alrdevaral
      241 gtdyevktgk qladdasasl keglsffnki llgfaavall vgtflilntf siivaqrtre
      301 lalmraigas grqvigsvvl eavavglias vlglaagigv gallaylfgk laggltlagl
      361 gvppaaviga favglvitvv aallpalras rippiaamqd vatpdrpltk vtvggsvvta
      421 igagllflgl gghagdntla tilggvlfaf igvalltpli srpvvallgt ifawsvpgkl
      481 grlnsgrnpr rtaitaaalm vgialvtgvt vildsakgsi salaedtika elvisgaqag
      541 prpasfdpav lekaadipgv qlvdgeygdm atvngertwv aassdvaale rifgakadag
      601 disrlgpdqm llssdtaksr nlsvgstvtv qlsrgeahty tvsgiyessq ltnpvvlppq
      661 aatdfaipqp iqgfvqlapg tsvdavqpqi erlladspev svadraafik qqtsqldtpl
      721 rmiqillala iviavlgiin tlalsvlert relgllraig lrraqtmrmi tveavvisif
      781 gallgvvvgt glgaavvral kdegitdlvl pwsqmvtflv laaiigvvaa vlpairaari
      841 nvlgaiahd
//
LOCUS       WP_357669822             468 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357669822
VERSION     WP_357669822.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..468
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48401
     Region          60..280
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mnrflvtiaa alialaaptt aaqaapvpdg lvskevsftg gggltlhgtv lspgqssagr
       61 pglvlvhgag tgtprtklmt eatefarrgl svlvydkrse gyslfersys tladdalgav
      121 kalraqpgvd pakvgvwgls eggwvaplaa grssdvafvv lvganahqpl rqqawavsag
      181 lrkagvsgtl adrtvptmyr aiadgglfpe pwfdplpmlg rvrqpvlavw gthdlltppa
      241 etpplmagal arggnghvtm rmfagadhaa hqspdggvtr lpalapgyad lvgswveqva
      301 egraprtqdt vrgprasqas ltvetpppaw wesapvqtaa lvlfvvafla ypitalvrri
      361 rgtsvpsgra prvlafsgla vslggfgyvm yllmtggkla apgpvlagrp vlwlllqala
      421 vtaavatvlt alawrrasgr servrlgvla aggavmipwa fywglllp
//
LOCUS       WP_357669831             205 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357669831
VERSION     WP_357669831.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 205)
  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..205
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..205
                     /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=21970
     Region          18..146
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msqdmglrer kkrrtreali taamelfrsq gyeqttvaqi aaaaevsvrt fflhfpaked
       61 lvmaevserv algvrvfeqp lpgehltdll lravnqmith tgdtdlvsgv aysrvqlivs
      121 vpdlqarmlr rlaeaqtlia dalrracpea ldpiaaaavv gsvvgavtaa aavsvsredp
      181 pervvaamrr aaglavgdfr aligq
//
LOCUS       WP_357669835             349 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357669835
VERSION     WP_357669835.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 349)
  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 349)
  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 349)
  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 349)
  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..349
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..349
                     /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=37157
     Region          1..305
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnvvlagahg fgrwhlqnir rlglrlagvc dlvpledadg dldgvpqssd ldwllrrtga
       61 qvtiiatpih thadlartal argshvllek ppvrtieefe nlseavaesg ltcqvafqsl
      121 gshavsavar liadgavgqv rgisvtgtws repgyyeraa wagrreagdg altnpfahgi
      181 atalclagse rlgevaevea elfhahpida ddtsslrvrt tggtvitvav tlcaereadp
      241 yvrvhgdrgr itlwytrdev rvgegpvvsy grddllenlv sgaeplvpla rtgaftqvma
      301 ailtardplp ipsvlvgerr vvqgvdelva ssadrlalfs eigppwear
//
LOCUS       WP_357669844             319 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357669844
VERSION     WP_357669844.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (residues 1 to 319)
  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..319
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..319
                     /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=34787
     Region          1..293
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
ORIGIN      
        1 melrqlryfv tlaeelhfgr asarehivqs alsqqiqrle relgvrllnr sthhveltps
       61 gaallvearq ildhvgraah aarsasvspp alrvgiidag ydsmpqilrd vqrrhpglti
      121 hqveastpdq yrqladgrld igigrasqtp phvtselirl dplgvlvpdd hpfaetdgvs
      181 varladepll lgedtqtpel nqfvielcra agftptvyeg tvqstraaad lvlqhrcvlc
      241 vpssfrsssr pgtvwrplve patrypwsll wlagepsaqv aavidsarrl arrldwlagg
      301 erpaareept avgsgdepa
//
LOCUS       WP_357669899             338 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora chersina].
ACCESSION   WP_357669899
VERSION     WP_357669899.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..338
                     /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=36992
     Region          1..325
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtepllkvrg lakhfpvrgg fragglvrav dgvdfdvrpg etlglvgesg cgktttgrml
       61 vrlldstsgs iefagrdith arrgalrplr qdlqiifqdp yaslnprhtv grivamplqv
      121 nrinppggik krvqellelv glnpehynry phefsggqrq rigiaralal rpklivadep
      181 vsaldvsiqa qvinllrdlq rdldlafvfi ahdlavvrhf chrvavmylg kiveigdrdd
      241 iytrpqhpyt rallsaipdv ttlgpagrir ltgdvptpln ppsgcrfrtr cwkaqercat
      301 eepalvprdg gnrltachfp etgsgldvia eagtdart
//
LOCUS       WP_357669887             327 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357669887
VERSION     WP_357669887.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=35964
     Region          14..309
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrllsll lllqahgrlt aaelarrlev svrtvyrdve slhaagiply geaghaggyr
       61 lvdgwrtrlt gltaeeadrl lfaglpgpaa elgyqsvvat lqlklraalp ppladradrl
      121 qqrfhldtpg wysdgdpspy laaaaeavwr ehrirvryrs wngevtrvle pyglvlkggr
      181 wyvvaarpdr aepatyrvnq ildltpldep fdrpefdlpa wwrahvvafr aglhrdeati
      241 rlsprgrerl revasdtvva avdasagppd aagwvravvp ieslthahgd llrlgaevev
      301 lspstlrdrl aetatalaal yhppapr
//
LOCUS       WP_357669914             387 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Nonomuraea dietziae].
ACCESSION   WP_357669914
VERSION     WP_357669914.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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 387)
  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..387
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..387
                     /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=41514
     Region          9..383
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mnddwicgrl gedapwalga vnppvfensl ftfetagdla eaikdedery vywrgtnptv
       61 dlaqrklaal eraerakcfg sgmgaisati sslvsggdhv lvlgaiygpt tqflrylekf
      121 gvththvgdp agldsairan trvlyfesps ymsyrlvdip avtawasghg lvsvmdntws
      181 tplfqkpltm gvdlvihsls kyvgghsdlv ggvvagstel irpialteyq lygaamsphd
      241 aakvikglrt lpvrmaahqe rglavaafld rheavravhh pglashpdhe lakrqmtgfs
      301 svfgleldtd erqvvaafld rlkvfrigvs wggfeslvaa paltteesvr vtmgipvglv
      361 rlsvglepag tlvedlalal egvvrla
//
LOCUS       WP_357669974             366 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357669974
VERSION     WP_357669974.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 366)
  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 366)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 366)
  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..366
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..366
                     /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=38915
     Region          121..364
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrktaylalv vavfqviash gaqagqtdrl rvdslgtvll lvgpvailat rrfpitslaa
       61 tlvatsvfma lgypygpvfl spvillfktv aegrrkvawi asaitaayfl vystwlvdrp
      121 aagawhvlai vavmllilaa gevarfrreg raeharvaee esrrqaseer ltmaqelhdv
      181 lahnislihv qastalhlld ddpsqarpal ttikaaskev lgelrsvlnv lregaprspt
      241 agldrvgelv ersgmdvslk qvgsrplpsq veraayrivq esltnaarha pgakvtvrle
      301 ylpaelvitv gdtgpttpav lseegsgngi pgmrerasal ggtlvagptg tgfqvearlp
      361 lpeete
//
LOCUS       WP_357669983             548 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora chersina].
ACCESSION   WP_357669983
VERSION     WP_357669983.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 548)
  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..548
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..548
                     /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=55799
     Region          8..259
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(8,32..33,62,67,72..75,87)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,70,86..89,93,95,132,134,
                     136..137,139,149..150,153,167..170)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(15..16,18..21,23,36,38,70,86..89,93,134,136..137,
                     139,149..150)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(19,93,95,132,134,136,153,167..170)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(149..157,164..170)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <202..533
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 msgwqlsgyt pvrrlgagas gsvvlathda tgtpvaikyl vrdlgadssf rtafreearl
       61 lgeiddrhvs rlyeyvesph gaaivmelvn gvslrqmlra hgpttpeaal cvlkgslagl
      121 aaahahgvvh rdykpenvlv tgeglsklad fgiampvgqg sdttvsgtpr ymapeqwtga
      181 paspacdiya atatffeclt grppypgpdl fslreqhasa piptdpapap vhellrhgma
      241 krpderpqpa qvfleildrv agagygedwe erglrelarr aallaalwpf pdgaggatsl
      301 asttlgetag rggrfrrgra rtalaagala aallvggagy syaahddpvt aggptgpava
      361 dptttagpap atptgtpapt vtatpsapat psatpsatpg gsrsatptrs pvrtsapapt
      421 pststspppp pdvtaptvgg vaadpgqlep ngcpygykta tvtatvtddr sgpaalkvtf
      481 aytlegvtrt gsmasagrgv frgtlgplpa pkqssripvq vtavdaagna ttsaspvyvt
      541 lynyctpg
//
LOCUS       WP_357670000             512 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nonomuraea dietziae].
ACCESSION   WP_357670000
VERSION     WP_357670000.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 512)
  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..512
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..512
                     /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=53262
     Region          2..511
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mtfdvvisgg rvldgtgapa fradigitge ritavgrleg adaaqvidas grfvapgfid
       61 chahgdalvf dpevqlaalr qgvttfvlgq dglsyapgsa atvnyatryf aavngvhpfl
      121 dgaasvadll agydrataln tayllphgti rydvmgaspd aastselaqm lahvekglad
      181 gavglssgle ylpgrnassa elaalcrplg alpyvthmra ygggagvgma evveiarssg
      241 tamhvshlhg padvllplve salahdvdls fdtypylrgs tilamvvlpp qvpaaevdra
      301 ldvlesssla dwwptldglw prltvshapg eewaegltiv eaavrkgvsp sefcrrllvd
      361 trleagcvvg rpdegpegee svrrvlrhpa htggsdgiyv gghphprgwg afarflgthv
      421 relgdwtwee avvhlashpa rrfglsdrgl lrqglaadvv vvdpatvadl atyaaprtpa
      481 sgisevlvsg alvlsdgalt grtpgralrp ts
//
LOCUS       WP_357670005             340 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357670005
VERSION     WP_357670005.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..340
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36219
     Region          80..339
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mtrsplaall laaltataca ttqpqserpt ataqprserp tatapfqsqr pdataaatrp
       61 ssgvpstrpg glavldeera grlvrltvds palkatakve lllptawrpg trwpvlylld
      121 gccrrggpaw vsdgradevt rdakaivvmp eagyagfysd wlegpqwetf hltelrhlve
      181 rryggtgrra iaglsmggfg alsyaarhpg mfraaasfsg lvnvsredve yltdqsgddp
      241 gklwgdgvae hnptalvrql rgipvhvscg ngepgpldag ntprdggeaf ieaenrafvr
      301 aaeaagvkvt anlygpgthr wpywtreler alpmllgsls
//
LOCUS       WP_357670008             536 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora chersina].
ACCESSION   WP_357670008
VERSION     WP_357670008.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=58290
     Region          17..519
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 msstaaastt ataergarmt tsrrlsvmml gmtvlvlagg gvggvalsht atvsnrladr
       61 ispartavsr letglleqva avrgyvitgd pellrpyedg vaaerataqr ardlltdepe
      121 arreldaala laerwraeyp trliaarrag tsaaelapvv rrsrlafdaa qaaltglear
      181 ldrvqaagra dldraralrd llfvailatl llssivisvl vrttvlrpld rlgasvrrva
      241 ggdfehrltp egpadiarlt tdvetmrqrv vdalntsrrh rdaleqqtae lrrsnedleq
      301 fayvashdlq eplrkvasfc qmlqrryadq lddrarqyid yavdgatrmq nlindllafs
      361 rigrvyrddr evdlaatftq aesnlsetia eagaeiaadp lpvvhgdptl ltmlwqnllg
      421 navkfrspdr pprirvavte dtagwefava dngigidpry adkiflifqr lhprgaydgt
      481 giglaickki veyhggtlrl ddgyadgarf vftlpkpapa vsvpeqagel tqvapg
//
LOCUS       WP_357670070             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora chersina].
ACCESSION   WP_357670070
VERSION     WP_357670070.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=35385
     Region          22..309
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mattvtppvp grrrrtplar rearwayvfl apwivgflvf tagpmvaslw lsfteydvin
       61 aprwtgldny rqlvsdpqva rslgntvyya alhvplvmli slglalllkr vgrwqgffrt
      121 vfylpvmtpa vavgilflll lntqdglinr glavfgidgp swttdpdwvm pgivlmslws
      181 lgstviiyla alqnvprdly eaadldgaga warfrhvtlp misgslfftl ivntiaslqm
      241 ftevytmyfg nrqtqgsfss daasfyvihl freafqflhm gfasamawll fliiliitav
      301 qvklsnqfvy yegedr
//
LOCUS       WP_357670097             318 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Nonomuraea dietziae].
ACCESSION   WP_357670097
VERSION     WP_357670097.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..318
                     /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=32567
     Region          3..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(37,247,250)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(190,218,245,248..249,252)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtvavlgecv adaftdpdha rhgelalrvi pgggpanaav alarlgtgar ylgrvstdpf
       61 grlfterlta sgvdlswvvt aaepstlava tldgegrasy sfhaegtadw qwtaeelaav
      121 dlggvaavht gslalvrepg aarieeflar arpsatismd pnirpllvdp gvyreamprw
      181 aaladivkvs eedlahlgsp dafcadlhaa gvrlvlvtrg adgvtasldg ermdvaapvv
      241 evvdtvgagd aftagllhrl dslgrlggri stlgaaelrd alafavrvaa ltctvaganp
      301 pwaaaltsvg tirpngea
//
LOCUS       WP_357670036             148 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora chersina].
ACCESSION   WP_357670036
VERSION     WP_357670036.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 148)
  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 148)
  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..148
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..148
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15471
     Region          55..132
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mqpprltgvl vlvavlaaat vfgwwrrrrd grlravspaa aaphraalaa lgvragavtl
       61 vqfsapvcap craarrvled vagrldgval levgveehld rareldvwrt ptvllvdgdg
      121 rivrraagvp dradllaala pltagara
//
LOCUS       WP_357670138             337 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357670138
VERSION     WP_357670138.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 337)
  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 337)
  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..337
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..337
                     /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=36035
     Region          10..332
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtfdtvtedr plraviagag figrqwatel llhpdvslvg wadidpskvp ggrgvpafgs
       61 vaemveavrp dflvngtvpa ahhevtlaal ergvsvlsek pmavtfeega dmvaaadrar
      121 rlfmvsqnrr ylpglvayrr tvaelgqlai ltsefyipyk svkfledlph pliqdmaihl
      181 fdaaraisga dplsvycesf rpaaswytga csataifems gglryvfsgs wsapglqtsw
      241 tgswraigar gtavwdggsv igaegvtpve lepdpsqard rfqglawale efvgalrtgr
      301 ppqgeghdnl aslamvtsal esalrgerik cplygat
//
LOCUS       WP_357670121             451 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357670121
VERSION     WP_357670121.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=47910
     Region          9..380
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mtsrlvrwsv vsmslamals acargtggea apmatgtyds ratfqgtltv mgiagideia
       61 ttriekaeas lggagvklie gdldiqqfls svasgsppdi vyanrdqigt fasrgaiipl
      121 tacvqgerid tsmydkpais qvtfggelwa vpefnqvqit manaalleka gltvqdvngt
      181 dwtkitaatp kllkasgkig fdsklpeflp lwakangael lsadgrkaql ntpqvveale
      241 favgvydaqg gfakvkavrd sadffgkgnq fakgelgamp meqwyvnvln dvsprtpmaf
      301 dtfhdkqgnt iayssgsawa ipkgskdpea acrfaktmtl vetwkaaaqa rlakrkaegk
      361 pftgvltgnt kadaeirkmv tsggrpwddg vkavyeaseh tftlpanpad tefkkawqda
      421 vnrvlngqqe pkaaldqaqq eaqaaldraw g
//
LOCUS       WP_357670232             316 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora chersina].
ACCESSION   WP_357670232
VERSION     WP_357670232.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 316)
  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 316)
  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 316)
  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 316)
  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 316)
  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..316
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..316
                     /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=31723
     Region          44..314
                     /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 mdtehterae daaldaysrv vtgvaarvlp svaallvrtp rgagagsavv igpdglllts
       61 ahvvqgardg saafgdgtet gfrvvgadpl sdlavlraer atvepvelgd adrlrigqlv
      121 vavgnpmgla gsvtagvvsg lgrslpardg rvtrliedvi qtdaalnpgn sggaladsag
      181 rvvgvntava gyglglavpv nattrqiiad lttdgrvrra wlgvagvpvp lppeitartg
      241 qrrglrvvev vpgspagtag lylgdvivaa ggrpvqdgqg lqrlmlgpai garlpvtvlr
      301 rgafvdviav ptelgr
//
LOCUS       WP_357670270             757 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357670270
VERSION     WP_357670270.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 757)
  AUTHORS   ter Beek,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 757)
  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 757)
  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..757
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..757
                     /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=79166
     Region          125..363
                     /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          513..>670
                     /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 mragarwira dlrarrgqav ltvatiaaiv aalitaatll edstnpwrgl fsqtngahlw
       61 vhtkerpqvv alreidgvtq aagpyrtapv tlleegrkap aalrampvtp pevarpvvae
      121 ggwltssqpd gavversfar slglgvgspv tvtalsgarh vlyvrgiads adqgfypewt
      181 pgliwvlpek ldrvepelgr sewvtglrla dpestqfvsq rvvvmldeev qrvytwrevr
      241 dameldnrll gtllalfgiv glvaaalala naaggrvlsq lrdlatlksm gftrgqvagl
      301 llvehgalgl lgialgvlpg wlvtwlvldr tavalvplva itagtalvvl vavglpawrg
      361 srtppipaap sapprghlsr laklallvrl ppalvlgard afsrrvpafl ttfglavpmm
      421 mitiglgvwa tldnflahpe qvgqhaqllv rpvkltpeea kraaqldpgv revypgadvd
      481 alvpgvarsi rvraiggsga pypfpvaegr myadrgeava gqglldllkv kigdrvwlsv
      541 ggtplivriv grtvepdldg qvlslgvdsl aakdvvppef wglalkkgad padvrdrlla
      601 asgegleiqr vvnpaerlsi iravivaliv vlaliglanl ltasalglrd haldlavlka
      661 mgltprqvma tlvtgtgvlv vlgvvlgtaa gsfvvtslid lqghtsgvga gigrppsalt
      721 ltvavtgavg aalavallpa rraaraqlgt ygfnanq
//
LOCUS       WP_357670303             327 aa            linear   BCT 28-DEC-2024
DEFINITION  ketopantoate reductase family protein [Micromonospora chersina].
ACCESSION   WP_357670303
VERSION     WP_357670303.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 327)
  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..327
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..327
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33697
     Region          1..311
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mryviigaga vggtigvrlg eagrdvtlva rgahldalre rgltlrtpdg tvtsrlpava
       61 gpddrplpad tvlvltvksq dtaaalaawv dapvegggta gerlpivlaq ngvanepaal
      121 rlfarvhpvc vwlpathlep gvvvanghph pgmlhlgryp sgaddtsrai aadltaagfv
      181 apvrddvmrw kygkllgnlg nglqallgpd vpeplaarvr aegeealaaa giphtsgeee
      241 aaergdrvrh rpvdgeerag gstwqslarg agsaeadhln geivllgrlh gvptpaneav
      301 qaavrravre ripaggfpla eleklvg
//
LOCUS       WP_357670308             299 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357670308
VERSION     WP_357670308.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=33092
     Region          17..297
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 masvgrrpps rrgrearrnl taygflvaal icfgvfswyp mvrevllslq ennfvdaprw
       61 vgldnfetvi edpafaqawi ntaaftglal ligyvipfca aiilnelrha kaylrfvvyl
      121 pvmlppavsv llfkwfydpg pglfnqilgf fhlpglawld stdtalislv ivstwmnlgs
      181 gtliylaalq tipselyeaa eldgagmfkr irhvtipqtk lillvmlllq iiatmqvfie
      241 pfmltgggpe natvtvaylm yqyafnfgnf gggsamglml mivlivfsav ylrvsrent
//
LOCUS       WP_357670354             416 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357670354
VERSION     WP_357670354.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=43407
     Region          1..325
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkallaaglv ilagatacgg gegtaggakq ddgtvtldwe mwagseeeka qldhvaqlvt
       61 qqhpnirikl rtapfnayft klqtefaagk qacvvsmqsl rlgayadlle pltapegfap
      121 asldalkmdg kqlalpydls pmllyynkda fakagvaepk agwtiadfek aakalstggk
      181 sgfgmsfsdl htlslllsyn gagpvtdevk lqmdsqpmvd avtwyaglga sksasvpags
      241 aeagwgetqf ingnammavd gswnigstik dakfkvgiap lpagsggskt yvansgfgva
      301 kgcpykeeai kavsvlsgke aqaylagqgr gfparteqqp ayeeflvkqn qdkaadvqaa
      361 mssvkeglag gvplfttknw ddvsklmaqh llqvytgaqs akeslttiqq qgargq
//
LOCUS       WP_357670343             304 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357670343
VERSION     WP_357670343.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  AUTHORS   ter Beek,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..304
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..304
                     /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=32133
     Region          21..303
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mirsrsssas araghppgep rrvaflyllp afavyavfll ypigravhls lfdwdglslg
       61 twagldnyva ivedeglraa fghalvlvlf yavgplvigl tlaailnhak vrglgffrtv
      121 vflpqvvamv vvavawrrvy apdgtlngll galgldsltr gwlgdhafal pavgvvgtwf
      181 etglvtvlll agmsrippel yeaarldgag alreffavtl psvrgeiava ltltviaalr
      241 tfdlvyvttr ggpgnstsvp syevyhrafg lgqvgsaaai gvtltvvifa isfvinrvad
      301 revs
//
LOCUS       WP_357670317             583 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora chersina].
ACCESSION   WP_357670317
VERSION     WP_357670317.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 583)
  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 583)
  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..583
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..583
                     /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=60907
     Region          1..447
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          516..582
                     /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(539,548..550,557)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            549
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvirac rdaglasvav yadsdrdalh atladeayal ggdtaadsyl
       61 ridklidvaa ragadavhpg ygflsenadf aqavidaglt wigptpqair dlgdkvtarh
      121 iaqragaplv pgtpdpvgna devmafavdh glpvaikaaf ggggrglkva rtmeeiphlf
      181 esatreavaa fgrgecfver yldqprhvea qvladqhgnv ivvgtrdcsl qrrhqklvee
      241 apapfltqaq rqqihdsaka icreagyhga gtveylvgad gtisflevnt rlqvehpvte
      301 etsgidlvre qfriadgekl rftedpaprg hsiefringe dpgrnflpap gtitalrlpt
      361 gpgvrvdtgv aagdviggnf dsllakviis getrtealer arraldemvv egmatalpfh
      421 rlvvrdeaft aepftvhtrw ietewdntvp aftaaagaae gpaeretvvv evggkrlevt
      481 lpaglgggta aaapaakkpa rrgggakaga aaggdtlasp mqgtivkiav adgdtvaegd
      541 lvvvleamkm eqplhahkag tvsglsaevg avitagaaic tia
//
LOCUS       WP_357670383             279 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357670383
VERSION     WP_357670383.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 279)
  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..279
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..279
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30217
     Region          4..279
                     /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 mdfftsydgt elachmfgeg ppavclpggp mqasaylgdl gglsahrkll mldlrgtgrs
       61 avpeeaasyr cdrlvddvea lreylgldrm dllahsggtn latlyaarhp ervnklvlis
      121 psvmavgiti tedvrrktar lregepwfpa tfaaleavma gqatgdtwqa iapfwygrwd
      181 etaqahkaae aeqrnseaaa ifgsegafdp datraaltrf tspvllftge vdlnspppvm
      241 selarlfpna elvvqaragh fpwlddadrf vattttflr
//
LOCUS       WP_357670376             534 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase [Nonomuraea dietziae].
ACCESSION   WP_357670376
VERSION     WP_357670376.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 534)
  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 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..534
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56554
     Region          1..534
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mdtllvagat vitpdghaea lavrggrieh vgtvaecraa lgrvdeelal dggvvhpgfv
       61 dahchpvmyg qalawvdcrp eaapdldtlv sllaetarrl ppgapvrgfg yehrrlaerr
      121 hptahdldrv atdrevylmn asghggvvnt yalrqygita gmadpvggri grfdggepng
      181 elwdaacdll tgldgvkirn hgpnfhlsep adimiehvrr aqevflaagv tsvgdaqvsr
      241 reletylwar dedvlrlrvs ayltsallgt aadlglagel gddrlriagv kfyadgtlgg
      301 wtayfpdgya adcchhgqly hspeeyteli grahrlglqt athaqspyai gmvldaveka
      361 gppygmrhri ehsglptdeq igrmaelgvi pvmqpqhhlr tgdgtitavg elghrynpag
      421 lcaaagvpvv fssdapvaqp dpleavaaaa trttvlgtvl ggpelrmsvp dglrahsiaa
      481 agalrrehav gslepgklad favmdgdptt aepaelssir vtqtwiggri awsa
//
LOCUS       WP_357670385             239 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357670385
VERSION     WP_357670385.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=24792
     Region          1..>217
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnrtarlyal veelraaapr pltiaalatr fevstrtvqr dlqtlmqtgv pvrttpgrgg
       61 gwsidpemtl ppihltadea saltaalaaa dastpyasaa rtaalkivas magpaaaaaq
      121 elaarivtlp thgdsairta veqalannmv lrlsytdaag hesnrvvepa glltadgrwy
      181 liawcrtrra grgfrldria aaaptgeqah phdltelllg saaagavqpt alasltppp
//
LOCUS       WP_357670482             487 aa            linear   BCT 28-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Nonomuraea dietziae].
ACCESSION   WP_357670482
VERSION     WP_357670482.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10167365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..487
                     /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=51380
     Region          4..427
                     /region_name="ASKHA_NBD_FGGY_SePSK_AtXK1-like"
                     /note="nucleotide-binding domain (NBD) of Synechococcus
                     elongatus putative sugar kinase (SePSK), Arabidopsis
                     thaliana xylulose kinase-1 (AtXK-1) and similar proteins;
                     cd07783"
                     /db_xref="CDD:466801"
ORIGIN      
        1 msgvwvgldl gtqsvralav tgegrvagmg trkltshreg erheqdpeqw whatalacae
       61 aladvpdaev rgvavdatsg tvlladtqgr pltpglmydd traaaqvdki nevgdhvwse
      121 lgyrrmqaaw alpkllwlld eygrsgvrll hqsdfvnrrl vghevptdls salktgahli
      181 eedwpsdvla tlgvpgetlp flvrsgtvig tvcaaaaelt glpegtpvia gatdgcaaql
      241 gagaltpgsw nsvlgttlvi kgvtrelvrd plgavyshra pdggwlpgga sstgsgaiar
      301 dfpgrdldel taaaagrepa rplayplvsa gerfpfvapq asgfllgeva deaehfaall
      361 qgvafverlc fdyldqlgap vdgaltltgg atrsaywcql radvlgrqvt lpenaepalg
      421 mavlaaspgr rvadvaaemv rvratidprp gsadrfdday lrlvdelarr qwlpaeiaah
      481 aherttr
//
LOCUS       WP_357670479             412 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357670479
VERSION     WP_357670479.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   ter Beek,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 412)
  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 412)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..412
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42759
     Region          29..408
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mtgletptdl kderligrqg lrgaaeglld rvrggdlgvl pvvigliviw svfqalnpif
       61 lssvnlvnlt lecapvgiia lgvvvvllvg qidlsvgsvs gltsavmavf fvdrrlpvwl
      121 ailaaivigc aigwvygqif nrfgvpsfvi tmagllgllg vqlwmlgakg sinlpfdsgl
      181 vafaqlafvp vwlsyvfvvv aaaglfasgy aharrrrqas lsavstqllv arsvlvligl
      241 gvvvwylnqt rgvgwmfvlf lalvlvmhyv lgrtkfgksi yavggnaeaa rraginvrav
      301 ytsafvlctt laavggvlaa arlaavnqss gggdvnlnai aaaviggtsl fggrgtafaa
      361 llgivviqsi ssgltllnld ssfrfmvtga vlllavavds varrsrvshg ra
//
LOCUS       WP_357670496             796 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Nonomuraea dietziae].
ACCESSION   WP_357670496
VERSION     WP_357670496.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 796)
  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 796)
  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 796)
  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 796)
  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 14311966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..796
                     /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=88249
     Region          26..647
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          632..715
                     /region_name="Mannosidase_ig"
                     /note="Mannosidase Ig/CBM-like domain; pfam17786"
                     /db_xref="CDD:465505"
ORIGIN      
        1 msvyrpldrg wtvtavssev aienvpatvp gcvhtdllaa gliadpyldd nedrlawigr
       61 tawryetdft vdddgfdrad lafdgldtva tvtlngerig avanmhrsyr fpvrellrqg
      121 rntlavqfes pyqhaeaqra vsgdrpspyp epyqfirkma cnfgwdwgpt lvtsgiwrpa
      181 alhtwstarl aqvrpevtld grdglvrihv sveraadvpi tltatvagaf ararlapgac
      241 eavlemrvse pdlwwprgyg pqplspltvv leetgqtwrr nvgfrsirld ttadeqgsaf
      301 tlvvndvpvf vrganwipdd cfpagltrer laerfaqacd anvnllrvwg gglyesddfy
      361 dladelgllv fqdflfacaa ypeddplaae vaaeareqvv rlaphpslvl wignnenfmg
      421 hadwgwrehl adrswgagyy ldvlpgivae ldpsrpywpg tpysgddsrh pnapehgtvh
      481 iwdvwnerdy tgyadwrprf vaefgfqgpp thatlrrsvt hgpltadssh qkaddgqlkl
      541 lrgldghlpp patfddwhfl tqlnqaravs fgverfrslm pscmgtivwq lndcwpvtsw
      601 saidgegrrk plwyalrrvy adrlltvqdg alvavndspe pwsgelelvr rsltgeplak
      661 esarvrvppr svsrialpph vagaadpsae llvaaldetr mirffaedvd lalppagfea
      721 gvrpvadgyl vtvtartllr dltllpdrld pdatvddmmi tllpgeravf hvrssldldp
      781 tsltcapvlr cvndgr
//
LOCUS       WP_357670507             261 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Micromonospora chersina].
ACCESSION   WP_357670507
VERSION     WP_357670507.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 261)
  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..261
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..261
                     /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=27088
     Region          1..>76
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 msradhmdva ayalgvldpq daerfeehla tcwacaaele tmvpvvglls gidgeamaal
       61 eqthtdpall drtlmavrrd rkrtrmrqvl aaaaavvvfg glsgagiagv fggddgkrip
      121 qaeptltapi tappspgpta sgpgvggneq egdqhdatdp gtgvkttmwl askeygtqid
      181 lqltrlpgpr tcrlvvvrkn atsevvstws vpgggygtnt nqlplelsas tsaplkdiqk
      241 iqvqsvdvng iasplvtvad l
//
LOCUS       WP_357670342             225 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora chersina].
ACCESSION   WP_357670342
VERSION     WP_357670342.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=23286
     Region          15..201
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mtgvalaeel lllayddetg katmprisld lgmaaavlve lalagriaya dgnlavldpt
       61 ptgepiaddv lariaadtph tpsswvqrlr hglrdrilgd lcgrgvvrdv detelgfihv
      121 hrypvadasv eadirqrlad altvgqvpde rtaalatlva vlrmepalgl tgtaaadagk
      181 rleeiasgag fsgtvsldds vvrpsvslvi aalaeavdaa lgkrp
//
LOCUS       WP_357670583             254 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357670583
VERSION     WP_357670583.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26304
     Region          7..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 mdyerlfrld grravvigag sgigrqaala laahgaqvvc adrdlpaaee targcggsav
       61 lldvldteav retaaaagav dvlvftaatn vrkrlldysg eefqrvvdln lrasfevlra
      121 fgagmvergt gsiigfasir aavtepgqgv ysatkaglvq llrtaaaefg psgvrvnaia
      181 pgvvetplts qikndpawyd ayaaksalgr warpeemaga vvylasdaat fvtgsvlyvd
      241 ggwtavdgrf nppn
//
LOCUS       WP_357670602             420 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Micromonospora
            chersina].
ACCESSION   WP_357670602
VERSION     WP_357670602.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 420)
  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 420)
  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..420
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..420
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=44023
     Region          258..415
                     /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 mpeldftglk daayrgfkpq fenvvavarr rrrrrrvltv ataamvlags gvavaarpda
       61 pappsvgvgg vrtpdfipvp ggtpspgtdq gvatgrpvag dldhiylrws ecsgcrirwa
      121 gtedrgrhwr tgdlpasvng tldlravgpr tvvarsvprs apdnryaewv astdggsnwr
      181 rvqprtveal pagwpvlslr tgptdeplva vdpatgdvaq lnrrstlhna mlvesvpaea
      241 glwvsgftge riaaddriig tggavevsrd ggstwsrhaf pddlaasddv ggpavatrdg
      301 rtvyaigrvr gslvvwrsad ggatwtraag taavgdrtir aalrpdgvlv vqagisared
      361 plmlassdgg atwdrtalgp gadprpvpgg fvqtgwpdsk gvwlstdgat wswldppelp
//
LOCUS       WP_357670609             213 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Micromonospora
            chersina].
ACCESSION   WP_357670609
VERSION     WP_357670609.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=22966
     Region          9..192
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 miepnwltet raaydtvavd yarlipdvle gpldrgmlaa faelvgpgrp vleagcgtgr
       61 itahlrglgl disgvdlspg mlevarrdhp elrfevgsmt aldlpdgala glvawysiih
      121 lppellpgvf aefhrvlapg ghllvavkag derirleqay ghtvsydvyw lpperlveql
      181 taaglavhat lvreaeeldr gpqafllark adr
//
LOCUS       WP_357670569             412 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent RNA methyltransferase [Micromonospora
            chersina].
ACCESSION   WP_357670569
VERSION     WP_357670569.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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..412
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..412
                     /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=43047
     Region          13..407
                     /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 mtapartgle eaqrveltvd avapgghcva rvegqvvfvr halpgervva evtelhrgfa
       61 radavevlta sadrveppcp yakpgrcggc dlqhvtpaaq ldwkatvvre qltrlggltd
      121 dqidalgvrv eplpggplgw rsrvryavda agragllkhr shevvpidrc liahpaiqdl
      181 pvltpsgtrw pdadavetva stggdvsvva faegaptpvs gpaevrevaa grdwtlpasg
      241 fwqvhpaaad tlvgavldll dprpgetawd lyggaglfaa alagrvgdar vtlvessqdg
      301 vdaaranlad lprvevvaar vetalarrrv tgpvdvvvld pprsgagapv vrdivaagpr
      361 avayvacdpa afardvrtft gagwrlaalr gfdlfpmtqh velvglflpp qd
//
LOCUS       WP_357670614             356 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea dietziae].
ACCESSION   WP_357670614
VERSION     WP_357670614.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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 356)
  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 356)
  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..356
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..356
                     /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=37146
     Region          1..342
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtgiaivgcg nisqqyltnl tsfpdvrvva cadldverar avaeeygvpv ageveqvvnh
       61 pdveivvnlt vpaahaevaa qviaagrhvy nekpltlepa agrelleaae aagvrvgcap
      121 dtflgaglqt varslaagdi grplsaitll qgpgperwhp speflfkpga gplfdmgpyy
      181 ltalavlfgp vtrvaangsr ahaqrrigsg plagtvfdve vlthvsalle feggqrattv
      241 fsfdsplsrg dfleltgtea tlaapnpndf tgpvrlrrtg apdwtdlpvk gatagrglgv
      301 lemaqaiaeg rphrasgela lhvvevmtai ltsaeesrfv pvtstftppd pwdatv
//
LOCUS       WP_357670650             197 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357670650
VERSION     WP_357670650.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=21231
     Region          3..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..181
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 mgragltadr vtlagaelad evgldhvtms avarrlgvkd aslyahvrnl edlrgriall
       61 aadektiria edtagragkd alvafanayr ayahehpgry tatqipiqid pelaarapgp
      121 rraveltygm lrayaldepd ltdavrlvrs tlhgfislea aggfaharpa edswvrclda
      181 lhtllerwpa hhegdpt
//
LOCUS       WP_357670686             203 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357670686
VERSION     WP_357670686.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 203)
  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 203)
  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 203)
  AUTHORS   Rosinski,J.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..203
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..203
                     /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=22405
     Region          6..80
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          91..176
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(93,106,108,119,124,128,162,164,176)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mdsdlsqald avgprlrvlr rqrettladl saatgisvst lsrlesgarr ptleqllpla
       61 rahgvtldel vdapptgdpr ihlrpvthhh itmvpltrra ggiqaykivi pagsprkepd
      121 pqthegydwl yvlngrlrlv lgeqdlvlsp geaaefdtrv phwfgaadae pveflslfgr
      181 qgerahlrar pksrnpperp ekr
//
LOCUS       WP_357670652             279 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357670652
VERSION     WP_357670652.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 279)
  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..279
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..279
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29342
     Region          4..279
                     /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 mtdpaigrlr vegatlhyev rgkgplllli pggtggaasf dgvaddlaad ytvasydprg
       61 ltrsplddpe ahqrvaqhad dafqlmells pdaparvagc ssgaivalhl ltahperier
      121 vvaheppvve vlpdaaehra llarvkdtfh rdglmpaaae faaglrrpga dpvaaqaate
      181 pppqatarag rtmadmpyfl grivpsfmay vpdvdrleal sdrlvlagga dsrgelpyrp
      241 aaflaerfgt elihfpgght glsthpaafg ellrkvlga
//
LOCUS       WP_357670722             395 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora chersina].
ACCESSION   WP_357670722
VERSION     WP_357670722.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..395
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42750
     Region          1..393
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mlaatarvag dldvaeecvq daylaalaaw ardgvpdkpg awltatakrk aldvlrrekv
       61 frskmpllve paeaemteep agdavpddrl rlvftcchpa lareaqvalt lrlvcgvatg
      121 diaraflvte ttmaarvtra kkkiaaarip yrvpdaaelp erldavltvi hllfttghta
      181 ptgsglvrad lvdravhltr mllalmpdep evrgllalll ltdarratrt daegrllvle
      241 eqdrsrwdra aiaegntlvl gafrtgrvgr yalqaaiasl havapsyaat dwpqvvrlyd
      301 ellkrwsspv valnravavs mvdgpaaala evdllaadpy lagyhylpai radllrrlnr
      361 aeeaadayra altlvdneae rafltarlte vtppr
//
LOCUS       WP_357670756             378 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357670756
VERSION     WP_357670756.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 378)
  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..378
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=39709
     Region          124..376
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mhglmrsvwn eppppdppar vgrdwalagv lvpvavlegf lrpdlpwrvl avavtvalvp
       61 tllwrrtrpl pmlaiafgvt svvalltggd agetytlayl lllvyalfrw gsgraavtgl
      121 almlvslgls iavgrigpad avgagavlva aialgtafry rararqreld qvkllerehl
      181 ardlhdtvah hvsamairaq aglataasrp dsaiealrvi eaeaaralte mnamvrvlrr
      241 nepvdlapgr gigdlprlag rdpsgltvdv elsgdlddlp psvaaaiyrv aqesvtnarr
      301 harhatrvev rvaadatsvr lrvsddgdda grqsgssgyg ligmieragl lggtcvagpd
      361 pdrgwtvtav lpragtat
//
LOCUS       WP_357670785             112 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl carrier protein [Nonomuraea dietziae].
ACCESSION   WP_357670785
VERSION     WP_357670785.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 112)
  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 112)
  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 112)
  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..112
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..112
                     /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=11343
     Region          10..86
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 msmspagqdr adevagtvld ivadmtgrdr galgldddlr arlgageddl nalavvvsae
       61 fdidleggev pdtvadlvae vrrraaegdg sadsplqpll rgletaraaa gv
//
LOCUS       WP_357670823             329 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357670823
VERSION     WP_357670823.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 329)
  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 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   3  (residues 1 to 329)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..329
                     /product="GlxA 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=35056
     Region          6..329
                     /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 msagsvaviv pediavpswd lyelslpctv fgkpqpdlad pwyelrlcgt gqadpgglav
       61 pglalrtpyg ledlvgadtv ivpsvpdacv edgaplppal vsalrdayda garmvslctg
      121 afalaeagll dgrratahwm htaqlaeryp kvqvddsvly vddgdvltsa gltagldlcl
      181 hlvrrdlgah vanqlarrmv vpahrpggqa qfvdlsvpat dddgmapvle waranldqpl
      241 tvedlarqaa msprtfyrrl qgatgmtplq wllnqrlsla qsllestdlp iekvgelsgl
      301 gtannlrhhf ikqvgvspsd yrrafprta
//
LOCUS       WP_357670973             338 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357670973
VERSION     WP_357670973.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Rosinski,J.A. 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 338)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..338
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..338
                     /product="helix-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=36742
     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 mpktsarlls llsllqarrd wpgallaerl dvsprtvrrd vdrlrelgyp itafkgpdgg
       61 yrldagtelp pllfddeqav alaialqiat tagagieeaa vralntvrqv mparlrrrid
      121 tlqvtaverp sirpepqvds rvlmalsaav hacevlrfdy apasppgvdd ngvrtpprrv
      181 qphhlvtwgg rwylvawdld redwrtfrad ritprtptgp rfsphelpgg evaaflagrf
      241 rgsggsgdwp crgevildlp aaavsgytrd gvveelgpdr crlvlgswsw tglaatigrf
      301 dadievvgpa elkqafahla grytraatdv rgsgpalm
//
LOCUS       WP_357671005             304 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357671005
VERSION     WP_357671005.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,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 304)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..304
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32153
     Region          2..217
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mislrglskr ygdrmavdel tlevrpgavt gflgpngagk sttmrmilgl drptagtali
       61 ggvpyhrirn plrkvgalld aralhpgrsg hahlvamars ngiprgrvae vletvglgea
      121 arkragalsl gmsqrlgiac allgdpevvm fdepvngldp dgvrwvrhlm rsladegrtv
      181 fvsshlmsem qltadhlvvl gkgrlimdap laeviarssl tavvvrtpha adlsvrlsat
      241 gvavervgen elvatgvaie rvgdlaheag irlhelrtre asleqayqel tassveygaq
      301 kagv
//
LOCUS       WP_357671098             693 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357671098
VERSION     WP_357671098.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15774079
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..693
                     /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=70315
     Region          10..650
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          16..252
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,41,43,72,88..91,95,97,134,136,
                     138..139,141,150..151,154,170..173)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,41,43,72,88..91,95,136,138..139,
                     141,150..151)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(26,95,97,134,136,138,154,170..173)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(37..38,64,69,74..77,89)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(150..158,166..173)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          456..514
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          525..584
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          591..650
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
ORIGIN      
        1 mpvplkmgdp krlgdyelsg rlgeggqgvv ylgtlgeesf avkllhgpvg eeqaaflrev
       61 elakhvarfc taqvvdagfd dgrpyivsey vdgpslsrev alagprsgga lerlavgtat
      121 alaaihragi vhrdfkpqnv llgpdgprvi dfglakalda aatvsgrgvg tpaymapeqi
      181 tasaitgavd vfswgatmcf aanasapfgq dsvapvlhri ltaepelgrl dgrlgalveh
      241 cldkdprnrp tsrelllall gagdevpaev lrsppphilr vdpyplaepe atgaaegyll
      301 pesrgrvpsg asparasrsa ggsgpaavrs dprgsvvpwp rvpgddgghp swpggdgrtp
      361 eathpgrwvg paanraslav sgallvsaav lvavlvpalq sseappmsva eptrvtssap
      421 aspqdqqgsg kikdtptsik rqpspppsva lvtysvpslv gmdrsaavra ikdaglvvgt
      481 vserdsarsp gevlgstpgg gtkvargtrv dlevaagprv pagprvpala gltreaassa
      541 laaaglrtgk itqscselps gqvisskpga garlapgrtv sllvaqqgar vppvvglpra
      601 eargslkaag favrqkaqiv ddpdvvnsvl gqsvspgtca rpgrtvvitv gvagqsfpdp
      661 septlppdsa eppagaeptp tpaptdeesp pen
//
LOCUS       WP_357671135             510 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora chersina].
ACCESSION   WP_357671135
VERSION     WP_357671135.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=54293
     Region          33..494
                     /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 mslpgatvpa psagagpava rdhlftarsl dryrtvlaeg vervarrvat adrpftgagp
       61 ddlaprvaav dldrplgdpg aaldelhdvy lrdavyfhhp rylahlncpv vipallgeav
      121 lsavnssldt wdqsaggtli errlidwtag riglgpaadg vftsggthsn lqalllaree
      181 traraglrpg pealsrlrvl tsaaghfsvq kaarllglgp davrtvdtda qrrmrpdala
      241 reiahcradg llvmavvata gttdfgsidp lpqvadicaa agvwlhvdaa ygcgllvspt
      301 rrhlldgieg adsvtvdfhk sffqpvsssa vlvrdgrtlr hatwhadyln paraveqrip
      361 nqvdkslqtt rrfdalklwl tlrimgadgv galfdevvdr ageawhllda dprfevvtrp
      421 alstlvfrwr paglaadlvd danlyareal aasgaalvag trvdgahhlk ftllnpettg
      481 ddvaavldli aehagwyart rtadeltpvg
//
LOCUS       WP_357671167             238 aa            linear   BCT 28-DEC-2024
DEFINITION  YqjF family protein [Nonomuraea dietziae].
ACCESSION   WP_357671167
VERSION     WP_357671167.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..238
                     /product="YqjF family protein"
                     /calculated_mol_wt=26671
     Region          5..234
                     /region_name="YqjF"
                     /note="Uncharacterized conserved protein YqjF, DUF2071
                     family [Function unknown]; COG3361"
                     /db_xref="CDD:442589"
ORIGIN      
        1 mrapasprva rpvmyhrwsd itfvhwrfpp dvvqalvpgs lkvetfdgta wvgltpflme
       61 gvrapgtpal pwlsrfpetn lrtyvrdarg rsgiwflsme agrlpaalgg ragywlpyfw
      121 sdmsvrtdgs lrryrsrryw pgpagarcdv dvetgpdlae derdelahfl tarfrlftvv
      181 agrlasaeve hppwplrhar larldqdlvr vaglpapdqa pllhaspgvp vrvglwsw
//
LOCUS       WP_357671199             536 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora chersina].
ACCESSION   WP_357671199
VERSION     WP_357671199.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 536)
  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 536)
  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 536)
  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..536
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..536
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57117
     Region          47..>234
                     /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 msrperdpgr wrpaldrpal valllgvagv gyrlvltllt lptsnsdeat fglaalhiat
       61 gnerpvflyg qrymgmlesy laaplvgwag aswpvlrlpl lalyavflwl ayrltrrlfs
      121 pwlatfvvgl lalgservvr dqltavggrp evkpavlamv liavalgerr vrhrwlatgl
      181 fgllagvalw sdwlivpyla vagllllwaa prdlvgwpgv llvvgfvlgv apmvkdnlva
      241 pegqdslsvf reistkdgat ptlaerlhgg llegvplasg lcpmdgcarw aqwfgllypv
      301 llvaaaglal vafrratdpa artravaila lvvgaaltll ayvrsplaat dplgnsryls
      361 vlqislpavl wplwraaaha vrataggaar lagalaglvl aalvaatlag tvafvadaps
      421 lraeerqard ladavrragl revygdywtc nrlifntgea vvcavldgdl spgqnrypay
      481 wkrvgraarp gyvvavgssa erglrrmlgd radaavvaev ggyrvyhpda avrpwr
//
LOCUS       WP_357671277             157 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            dietziae].
ACCESSION   WP_357671277
VERSION     WP_357671277.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..157
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16659
     Region          4..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mlgrtydtqv csaaralevi gerwsllivr dalfagatrf adfqrlgiat nilakrldsl
       61 vdsgilerrs sgeqpdragy avtrkgldla pviitltqwg drwaapdgpp ivyrhtdcgg
      121 aiaeqttcss cgqvtdlaqi hvvhgpgmpg apstdvv
//
LOCUS       WP_357671278             253 aa            linear   BCT 28-DEC-2024
DEFINITION  sirohydrochlorin chelatase [Micromonospora chersina].
ACCESSION   WP_357671278
VERSION     WP_357671278.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..253
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=25438
     Region          7..245
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mrpahltaep pvvlvahgsr dpraaaatra laravaaarp gvpvlpswld htdpgpaavl
       61 rdlaaaghpr avlvplllta ayhrkvdvpa avaaarqgga dievrvtdvl gpadgtvdsr
      121 llaglrrrla eaepggvdav vlaaagtrdp rargsvgrma aalgaelgvp crvsyasaap
      181 pgagvavsrl raagarrvav aayflapglf hdavrseaer agavavaepl tdlseladlv
      241 lrrvdavpvg spv
//
LOCUS       WP_357671302             463 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome b [Nonomuraea dietziae].
ACCESSION   WP_357671302
VERSION     WP_357671302.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 463)
  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 463)
  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..463
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..463
                     /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=50833
     Region          15..408
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mrslsakrrs fqfshwsfmf aeiavwsfvv lavtgaalmv fydpsmsqvt yggsygplrg
       61 lfvskafdst mhlslevrgg llirqvhhwa alvfvaaval qllrmfltga frrprtrqwl
      121 iwvtllalgm aagetgnalp ddmlsggslw limsvvqsip fvgtwalsll fgpdfpgdrv
      181 ipvmygghll iavvmaalli arellmrrhg hsrfsasvst rrgarplmal atigmliilg
      241 fgfqiapiwl ygpakptqis agsvpdwymg fldgalrimp gweltlgdyt lslavlvptl
      301 vipgvfftal aaypmaerfl vsrrsrrdal grpkttsrmp rvtgahdmld rprdtptkta
      361 iavagitfyg llwaaaandq iahqfhltve avtiffrfav vigpviafti trwiclalqq
      421 tdhhvvehgv etgiitrspd ggfherlapa rqesreptvt sgr
//
LOCUS       WP_357671286             185 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357671286
VERSION     WP_357671286.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=20296
     Region          7..177
                     /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 mfavslgdga elrplepwqa eellahmdrg refvgqhvgl advvsdldsa rgwlqsyadr
       61 aaadtgrlyg iwldgllvgg vlfrvfdagm gtceagcwle paaagrglvt raarviidwa
      121 irergmhrve wqvsskntps invarrlgms rdgvlrensl hrgvrqdtei wsvlatewra
      181 thsts
//
LOCUS       WP_357671319             178 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357671319
VERSION     WP_357671319.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=19014
     Region          22..160
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 madhptspae iaaawqrerp gtptdsieiv tpiwrlakmf addrvrvlra agidaatldl
       61 lsvirrsgpp yrlstrelah rtlvtagais qrvaraerag lirrspgetg rksvavsltd
      121 eghalversv dsvlgreasl vagltavera tlgklleklt idvqhriata epsrtsgs
//
LOCUS       WP_357671327             350 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Micromonospora chersina].
ACCESSION   WP_357671327
VERSION     WP_357671327.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 350)
  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..350
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..350
                     /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=38394
     Region          4..349
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtsstltapa arrgsdyarl srrvataglf drrpgryaar igitlgafla gwavvvavgd
       61 swwqlplaal mavattqvaf lghdaghrqm frrrgpseva glvagnlavg lsygwwvdkh
      121 nrhhanpnha dedpdvgaga lvwtyeqata trglsrwmar rqawlffpll lleglalhva
      181 svralvgrep dgrwrtpvrh rtveglllaa havgylgllf avmspgrall faavhqglwg
      241 lymgcafapn hkgmpmptae ddldflrkqv ltsrnvrggr fvdvalgaln yqiehhlfpn
      301 mpranlrrar plvraycaeq gipyvetglf esyrqalahl hevgrplrag
//
LOCUS       WP_357671328             386 aa            linear   BCT 28-DEC-2024
DEFINITION  epoxide hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357671328
VERSION     WP_357671328.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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 386)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 386)
  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   5  (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 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..386
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43863
     Region          5..110
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          85..>201
                     /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 msedvtpfhl dvpepvlgdl rerltrtrwp eeetvddwsq gvplgylrel crywaedydw
       61 raterrlnal pqfrtsidgf gihflhvrss hddalplilt hgwpgsivef lkvigpltdp
      121 tayggdarda fhvvcpslpg ygfsdkpdrr gwgveriada wirlmarlgy drygaqgadw
      181 gttittligr qdpdhvagih ltpplappdp ttfddltdae aaaltalqqa qetedgysle
      241 qstrpqtigy glvdspallc awiiekfraw tdcdghpena ltrdelldnl mfywlpgtga
      301 saarlywesf khvqrlftae ttdlvtvptg ctifprenpr psrrwaekrf idirhwnepd
      361 kgghfaafeq pelfveelrt ffrlvr
//
LOCUS       WP_357671372             445 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nonomuraea dietziae].
ACCESSION   WP_357671372
VERSION     WP_357671372.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..445
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..445
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45723
     Region          5..438
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msdaalttel sdeglarddy alqrvppsar ygwvtvaiqr fgmlsalsqf llgatlgmgm
       61 tfwdavlait lgavilevva iaigiagmre glsttvlarw agfgrygagi vgmviaicll
      121 gwfgvqsavl aqglasllgg ppvwawsima glavtaivvh gfagmawtaw itvpaflala
      181 gwaitvelsk qslgalvast ppgpalslae gativaggfi vgavispdmc rwnrsaadvv
      241 kqtvlgitlg eyvvalvgvl lahalrtgdv iaivtttsgv vgtivlitat lkindwnlya
      301 aslgmtntlh tafgkrtnra vvtvalgvig tglaaagild hlidffvllg vaippiagim
      361 vaeyyvvrrw rpaldtsras galpdtapgw apaalviwla saligkyvaw gipalnalmv
      421 afaayaiagr lgltgaprde narva
//
LOCUS       WP_357671341             279 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            chersina].
ACCESSION   WP_357671341
VERSION     WP_357671341.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 279)
  AUTHORS   Rosinski,J.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..279
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..279
                     /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=30775
     Region          26..>79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          107..267
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mgtplgdfvr akrdslqpes fglpgrgrrr spglsraeva trsgisveyl trieqgrdrn
       61 pshsvlhala dglsldager hhlrylakit gggcpghrpp appnrevrpt vretlrllep
      121 gvafvtnrlg dvlaytegfa lvmgaaglld adppnltryv ftdprarsvf pdwdqvadeq
      181 afdlwlgpsa essewfrvql apvagpeftr rlqrhlpppq vplrldhptv gelrwhrekl
      241 elpstdaqel vvllpadeat aqaverlrhr rhgalravg
//
LOCUS       WP_357671379              71 aa            linear   BCT 28-DEC-2024
DEFINITION  tautomerase family protein [Nonomuraea dietziae].
ACCESSION   WP_357671379
VERSION     WP_357671379.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..71
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..71
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=7507
     Region          2..61
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mplinvkiie dvfteaqkae mvtkltdamv siegenmrsv twvlveevks gdwgiggktl
       61 ttadvkalaa g
//
LOCUS       WP_357671408             269 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357671408
VERSION     WP_357671408.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..269
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28150
     Region          5..>156
                     /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 mktdtlevpg arlyyevrgs gpvlllipgg ptdagvfagl aaaladrhtv vaydprgnsr
       61 stlselpged lldlhaddaa allalfgeep advmgssggg ltgltlaarh pkrvrtlvah
      121 eppvvellpe aarqreisae vydtyvqhgv gpamrrfmev sglggtaeam pppppeaqev
      181 marnldffla htwrafdgft pdfdalrsgg arvvvgvgeg segqlahraa lalaarlgap
      241 pvvfpgdhgg fgerpeefad llhqvlrgs
//
LOCUS       WP_357671330             131 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357671330
VERSION     WP_357671330.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=14853
     Region          4..98
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mttdtlsrvf aaladptrrd mvarlsggda tvsqlaepyr mtlqavykhl rvledaglvs
       61 rpqgpqprsv hlevqafdlm dtwieryrsr aelryrrlda vlaeikgaed eqdhrdshrd
      121 rpevadhpdd s
//
LOCUS       WP_357671436             145 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357671436
VERSION     WP_357671436.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 145)
  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 145)
  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..145
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..145
                     /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=16161
     Region          8..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mekylaathp phivallyea ylrlsdvvfq agkeidprir pahsavffhm ehdgirlskl
       61 aekaqmtpqa mgelvddlek lgylrrvpdp adrraklivf tdrgddalra gyaaiddler
      121 rladllgedg rsglhaaltr vindf
//
LOCUS       WP_357671573             149 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357671573
VERSION     WP_357671573.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 149)
  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 149)
  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..149
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..149
                     /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=16456
     Region          1..141
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mseeladrlv evfdlvgply rraqrkveqd apieglsvgv ravlnmlreh gpmtvpqmgr
       61 aqalsrqfvq rmineaaarh lvefvpnpah krsslirlte qgraaitavi dreravlgql
      121 ggdlsdaeva vcirvlsrll qfldhvdvd
//
LOCUS       WP_357671576             614 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Micromonospora chersina].
ACCESSION   WP_357671576
VERSION     WP_357671576.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..614
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..614
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=64866
     Region          193..>286
                     /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          361..571
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mslaedfaal svedavrast sfdqlragdg alywletrpe aggrgavtrw rpgegtrsis
       61 pegfdvtssv haygggtfav vedtlwcige aglyrsgrss dqlelitrgr fgdltvgdge
      121 llavreseqg deivgvslag rtqvravvas tsflgaprqg pgllawvaws erdmpwdace
      181 vwvapylpgg digsprkvag gsnesalepr wgpdgalyfm sdrsgwwnly rwngdaieav
      241 gpiagecaae pwelgyasyd fladgriamv vqegprhrlv vvepdgavrp vnvpytsikp
      301 ylaaqgmtvs ligssptaap qvavvhladg hprlevvars ehaelseaqv stptelrigv
      361 pggrevvalv ypptgsaadw caplivrahp gptascllrl dwqaqfftsr gfavvdvdyl
      421 gstgygrsfr eslygrwgld dvddcaavad hlvetgravp gqvfirgasa ggytalhavs
      481 kdgpfaaata vsaivdpgrw aetvprfqra hatrlrggag rvraatvrcp vlfihgtade
      541 vavvedvrel addlaalgvr hellllpdvg hyvatssrag aaleaelahy rsvtaaavvg
      601 sgdhraasgs csrt
//
LOCUS       WP_357671575             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357671575
VERSION     WP_357671575.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..212
                     /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=23744
     Region          7..128
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mptrtgrppr israeimaaa lrvieeegvd mltmrrlare vgstamaiyr hvrdkeelll
       61 lllddyaagi prpelpeepr ervvaaamam hkavsgcpwv vdvlraddlm svealwyper
      121 ivdaavragl tmeeavdayr iiwrytvgei ggraaarrrr ekggstyrer vfaeldaeef
      181 prlskvagrw eeltardtya kgvralvngl lp
//
LOCUS       WP_357671582             208 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora chersina].
ACCESSION   WP_357671582
VERSION     WP_357671582.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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..208
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..208
                     /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=22977
     Region          3..195
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mlladeffli ahddqtgrpr lhpsaithgl aaallgelaa agrvsfdrgh lyvldhrppa
       61 dalqhlildr lvgepqhtat rtwlsyvaat aheevarrlw qagkvepqqq rrflrtvtvh
      121 vptdmnvaaw swarlstklr qyeeldsfdl alagiaascr ldqfildgap yavgahlrrl
      181 laaapqpmre lladldtaig htilshrt
//
LOCUS       WP_357671610             192 aa            linear   BCT 28-DEC-2024
DEFINITION  RICIN domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357671610
VERSION     WP_357671610.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..192
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21210
     Region          50..>160
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(63..65,76,78,85..86)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(114..115,127,129,137..138)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mtpvsllrrl tcliaaagls lglassaqat tmlkadpnpa vwswvdenrt ykidnvvtgg
       61 hlvpegwgln steglpiysa vsdagngwkf qqrrhsdgwa yhqiknihtn rcikpgplgg
      121 lnrtlviqva cntsdssqyw rverspynrd evqfvnhssg eafrpwtdvn vdqwvfltnp
      181 gvratywald av
//
LOCUS       WP_357671590             300 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Micromonospora chersina].
ACCESSION   WP_357671590
VERSION     WP_357671590.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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 300)
  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..300
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..300
                     /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=31801
     Region          16..269
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mastvwfvgv stgkslihea fpiwmgdlgl dvrlvgrdvp laapgeayra lmtelagsdd
       61 vlgavitthk vavlrqagdl vdwldplaae cgeinalrre tgrlagfard pisigrvvde
      121 iwpdgehvvc lgaggsaial grhllarpvp pnrlmftdcs gaagrhlqav lgpwaesrrv
      181 rlevhigagp wdhlvasgpp gtlvvnatgl gkdrpgnpls pvaqfppaal vwdlnyrgdl
      241 amlrqarahd glvvhdgwql fchgwaaalg pildlpneld tagrfamlta plrarpdacr
//
LOCUS       WP_357671614              90 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            dietziae].
ACCESSION   WP_357671614
VERSION     WP_357671614.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 90)
  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..90
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..90
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9838
     Region          <3..73
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mqlgggphrf tqleraiegi srrmltvslr nlernglitr tvypdapprv eyattalved
       61 iraplealat warhagpvia aarkaydssr
//
LOCUS       WP_357671624             119 aa            linear   BCT 28-DEC-2024
DEFINITION  cupin domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357671624
VERSION     WP_357671624.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 119)
  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 119)
  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 119)
  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 10004899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..119
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12882
     Region          1..94
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
ORIGIN      
        1 mskdpavtnp elykvifend rvrvleyrdr pgdrtvahqh pdsvmytlss frrklsaggr
       61 evavelpagq vrwldaqehs genigdteth sifielkepg pakeggagdl lgpsgggsr
//
LOCUS       WP_357671635             331 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Micromonospora chersina].
ACCESSION   WP_357671635
VERSION     WP_357671635.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 331)
  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..331
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..331
                     /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=35580
     Region          2..242
                     /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 mdavdlarrf alggaarlsd gpvargrqga vwrletadgr wavkvpfhqs gedevrlatv
       61 fqeaaysagv ptpqvrrtte ggvfatvggr qvrlyewvdv kapdrclnpg lvgavvaaih
      121 rvpvtepgpl dpwyrepvga drwdqlvqql vearapfagq ladlrdelva leswieppqt
      181 lrtchrdlwa dnvlptadgg vcvidwensg padpsqelgc vlfefaradp graraliday
      241 reaagpavvn rpghfsmlia qlghitevaa tdwltpnars pkradsaawi gevldephtr
      301 elldsllaav cgdatpsgqp pdthagdrav p
//
LOCUS       WP_357671634             217 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357671634
VERSION     WP_357671634.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 217)
  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..217
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..217
                     /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=23021
     Region          24..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtrrtrgtsa gldrarivaa avalidrdgl erfgvrrlae elgvdpmsiy hhikgkaall
       61 daiseavlte vaaaaddasl gwqevtrrta hayrslayrh pqvfpllvtr aqtspaaiia
      121 lerlviamre aglpdqvvad apmllfgfln ghllartsag pdgptpvpaf dpeayptmaa
      181 laplwadfgs aaefdrmlds vldgikgqat argtgtr
//
LOCUS       WP_357671668             374 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Nonomuraea
            dietziae].
ACCESSION   WP_357671668
VERSION     WP_357671668.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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 374)
  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 374)
  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 374)
  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..374
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..374
                     /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=42134
     Region          15..372
                     /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 mttsspatts sviptlpghy ytdqelfare qknifeamwf cvvrssdlpk pgsfktvqvg
       61 sesilvtrar dktvraffnv crhrgaqlca eesgevkraf qcmyhawtyd ldgkliaapn
      121 ltkmadldrv eyglvkvhvr ewlgyvwvcl adeppsfeed vlgavterlg alelidnydv
      181 aglevgrriv ydvkanwkli ienfmecyhc atihpeltev lpefadgyaa qyfvghgaef
      241 geeirgftvd gsegldripg vsedqdrryy aitikpqvfi nlvpdhvivh rmfplavdrt
      301 vvecdwlylp gvvasgkdld ksvelfhrvn eqdfeacerc qpamgsrtya kggvlvpseh
      361 higafhewvq drig
//
LOCUS       WP_357671662             390 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357671662
VERSION     WP_357671662.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 390)
  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..390
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..390
                     /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=40511
     Region          1..383
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mntvcvvgas laglltaral rgqgytgrlv lvgeerhrpy drpplskdfl rgaigeadla
       61 legegeelda ewrlgvaata ldavarrvtl sdatsiradg iviatgasar tlrgsrglag
      121 vhtlrtldda ralrrelgsg rrlvvigggf igaevaatac elgldvtlve sgpaplagvl
      181 gapmaeaiat lhegrgvrlv rgayvteltg agrvdgvrla dgthlpadvv vvgigaipnt
      241 swlegsglel gdgvlcdegg gtrvpgvvav gdcaawfdpa qgghhriehw tgarqraava
      301 attllsggta rpeparpayf wsdqfdikiq fighaghads vtveegdlaa hsflavyrqg
      361 erpvavlgvn qvrlftrwrr hletapvqag
//
LOCUS       WP_357671680             662 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357671680
VERSION     WP_357671680.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 662)
  AUTHORS   ter Beek,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 662)
  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 662)
  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..662
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..662
                     /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=69780
     Region          47..326
                     /region_name="ProW"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4176"
                     /db_xref="CDD:443335"
     Region          382..647
                     /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 mttvavvaar lparryllla vlalwvlgwa vfggrdtlnl ggaeltplht slnegmdaid
       61 dsrnsnpffl yfinyirlfl desvtfvqal isqpsfgrpl pvlgwlgvva lataiawlwg
      121 ngrvalltaa gllsfgvlgl wqesmdtlal tltavvfsla vgiplgvwag lndrfnrlvt
      181 pvldfmqtmp tfvylapltl ffligpasat vatmiyaipp airitshgir qvshdtleag
      241 aslgatgvqs lrhvrlpmak qtiivgvnqt imaalsmati aalidapglg ktvlkalqtl
      301 dvgtafnagl aivimavvld rvtsaasrrv eadrragrlr gtrrrrlela gafgvvavlg
      361 ylsytyvwaa efpvqanlgs yvrqaadags lwvqdnlaay tdalknvltn tllnpfekll
      421 ttspwwlvla vgvavallvg svraalvtaa gllvlvllgl wqdsmvtlas tlvatilvmm
      481 lgvvlgvwmg rsdrvdtvlr pvldagqtmp afvylvpilg lfgptrftai iaavvfaapi
      541 aiklvaegir rvspttveaa isagtgtwql iskvqlpmar sgvtlaasqg liyvlsmvvv
      601 gglvgagalg ydvvagfsqh qlrgkglaag laivvlgivl drvmraatqr advaahggvt
      661 hr
//
LOCUS       WP_357671715             167 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea dietziae].
ACCESSION   WP_357671715
VERSION     WP_357671715.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 167)
  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..167
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..167
                     /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=18559
     Region          1..148
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mddseaqlta lytrhyrsvl syvllraeqq taediasetf liawrkldrv pepplpwllg
       61 varnllrtqr rsrlrgqtlm erlaelapae dvahqvaerq aalnalagls erdaeavlla
      121 swyglspaea akiagcsart fnvrlhrarr rlanalglta ltfqeqs
//
LOCUS       WP_357671746             511 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nonomuraea dietziae].
ACCESSION   WP_357671746
VERSION     WP_357671746.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 511)
  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..511
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..511
                     /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=53498
     Region          1..511
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mhdlllrdgt vhdglggvpr hadvavadgr vaavghdlgp arrvidvtgl lvspgfvdph
       61 shsdtvpfle epqpfkllqg vtteivgncg fscgpvdpes lsfmpaelag aafatlgdyl
      121 daaeaagpsn nlgvlaghnt lrlaaagmsa eitpnrlarm celaaqsfea gavglssgle
      181 yvpgayadle elvalalvak rwdlpyathm rseseglada ldeaiavakr agvrlqvshc
      241 kasgravhga sammldklaq arragvdvra dvypylafgt mlvavlppia ceggeqallk
      301 rlgdpaeraa lralaedpat gtgvgfwrel hpsdvqilih ndpgiegrrl sdlggdpwea
      361 lcdlvrldpq asgvfhtmhe rdlaafladp lisigsdngp pvgpthprtf gtfptylgty
      421 vekedmpeai rklssavaaq fglagrgwlg pgaiadlcvf dpvtighagt yespgvrptg
      481 vehvfmagrq vvadgeftgg rhgrmlrrga r
//
LOCUS       WP_357671726             153 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357671726
VERSION     WP_357671726.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 153)
  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 153)
  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..153
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..153
                     /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=16440
     Region          10..150
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mhhgtsssqa ppaadvterl gyrlkraaaa lrgamdgalr eygltvpqya clelldqrpg
       61 lsnaelargt fvtrqsmnvv lrglqdsgli trpattdrgr alpahlteeg hrrlaaarsv
      121 vyaidqrmtd avperrlael ladldhmtaa ldg
//
LOCUS       WP_357671788             328 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Micromonospora
            chersina].
ACCESSION   WP_357671788
VERSION     WP_357671788.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..328
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35579
     Region          4..328
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mttqmsdrld dvlhagqvgg lhavvavrgg rtvleyygag edfawgdslg vvefgpetlh
       61 dirsvtksvt mllygialge glvpppaepl lrlfpqypdl avdpqrarlt vehaltmslg
      121 lewredlpyn spanaeiame lapdryryil erpileppgt rwaysggata llgrliadgt
      181 gqslpqyaqa mlfaplgigs fewmtgtdgv asaasglrfa prdlarigel vlaegtwdgh
      241 rivpadwirt mlqprlqttw gaqygyhwyv esieghqmva gmgnggqrlf vlpdlgltva
      301 vtagnyddpd qwrtpltvlg rvilpama
//
LOCUS       WP_357671765             279 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora chersina].
ACCESSION   WP_357671765
VERSION     WP_357671765.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 279)
  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..279
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..279
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29035
     Region          1..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 mttveangvt lgiehfgdat aplvllaggt tmlswpdalc ealarggrhv vrydlrdsga
       61 sttvdpeapa ytlrdlaada aalareldhr pahlagigvg gmaaqvaald hpdafsaltl
      121 vgtrpvapgp vdddlpdhdq atmgrlfsra mpdwsdraav agfaaegaev lgddpvaara
      181 taerrwdrtp gtepavqman hlgtvfakld ctprwrerls elaiptlvvh grrdpffplg
      241 ngealareip garllvlera ataipdaaag evaaamlal
//
LOCUS       WP_357671808             289 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357671808
VERSION     WP_357671808.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 289)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..289
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..289
                     /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=30794
     Region          12..286
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mikrfsalsp swlfaapall vyavvvlyps vagvlyaftd wsgigegmsf vgaanflall
       61 ddeqamgslg ntllltlaiv vvqnglglll algvhaklks rallrvvffa pvvvspvmva
      121 flwkyvynpd psaglngllg levdwlgdps ialwsiagmv vwqyagysmv iflaglegip
      181 aelheaamid gagtlqrfry vtwpllapal tinlmlstig glklfdqvfa atnggpgyat
      241 etlstvlykq afvfgkfgys taialvlalf vaavslvqiy ylrsrevaq
//
LOCUS       WP_357671828             116 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357671828
VERSION     WP_357671828.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=12526
     Region          7..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msfrhpdrdq irienvlsal gnplrlavir vldaggehnc ggvlnllgvt skstmthhwr
       61 vlrdsgviwq qpsgrenllt lrrddldary pglldailag avrdgsdpae psplsa
//
LOCUS       WP_357671880             120 aa            linear   BCT 28-DEC-2024
DEFINITION  5-carboxymethyl-2-hydroxymuconate Delta-isomerase [Nonomuraea
            dietziae].
ACCESSION   WP_357671880
VERSION     WP_357671880.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790028
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..120
                     /product="5-carboxymethyl-2-hydroxymuconate
                     Delta-isomerase"
                     /calculated_mol_wt=13067
     Region          2..118
                     /region_name="HpaF"
                     /note="5-carboxymethyl-2-hydroxymuconate isomerase [Amino
                     acid transport and metabolism]; COG3232"
                     /db_xref="CDD:442464"
ORIGIN      
        1 mpqitveysa alddaferra falavhttag alidsdpdsf ktrfhrieeg vigdgaaaha
       61 mihvevailp grseetrrll gqtvldlavr hrkdvaeltv qttvevrelt aghyhkqvsp
//
LOCUS       WP_357671871             269 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora chersina].
ACCESSION   WP_357671871
VERSION     WP_357671871.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 269)
  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 269)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..269
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..269
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28377
     Region          53..264
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mahlltrrtl lgaaagvaga avvgglaarq laeprpgpap avpdapagde rlirirsgar
       61 drevdfwtav pegygdgrgl pvclvlhgas atprdygrfg larfltdavr rgappfalag
      121 atggrlswrr sgdddpqrmv reelptwcar rgfdssrlav wgwsmggfga lllaeaypgw
      181 lravaafspa vrpgdavfag vdrlrgtpvg lwcgrqdnfl kdvralaral pepparaawa
      241 dgrhnfaywg tvipdafalv gaaltppka
//
LOCUS       WP_357671881             596 aa            linear   BCT 28-DEC-2024
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Micromonospora
            chersina].
ACCESSION   WP_357671881
VERSION     WP_357671881.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..596
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=63273
     Region          4..285
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
     Region          313..592
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mareftsvgv vglgtmgagi vevfarngid vvaveisaaa vergratltg stdravakgk
       61 laeadrdall arvdwqvgld alhsvdlvie avpehldlkq rifaeldrvc kpeailatnt
      121 sslsvteisv attrpnqvig ihffnpapvm klvevvrtvv tsadvvadve alcerlgkvd
      181 vtisdragfi anallfgyln havsmfesry atredidaam klgcglpmgp lalmdligld
      241 tayeildtmy rrggrdrrha pvplikqmvt agllgrksgr gfytyerpgs pvvvpdehtp
      301 vttggaladg araiakvgiv gsgtmatgii evfakagyev isvtrgaeks akvceavkts
      361 lnkgvvrgkl seedrdaalg rvtwsatldh ladvdlvvea vveelsvkka lfasldeick
      421 pgvvlattts slpvidvama tqrpadvigl hffnpapimp lveivqtirt sgetsatara
      481 vcaalgktgv vcgdrsgfiv nallfpylnd avkmleasys taddidyamk lgcgypmgpf
      541 elldvvgldv slaiqrelyl elrepgfapa pllehlvtag ylgrksgrgf rdhtkr
//
LOCUS       WP_357671890             187 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea dietziae].
ACCESSION   WP_357671890
VERSION     WP_357671890.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=20523
     Region          2..165
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mpslkiivas trptrigrti gdwvdahavr hggfdvelld laevglpfld epedattgry
       61 vhqhtklwsa aidaadafvf vmpeynycfn aplknaldfl yrewahkpvs fvsyggmsgg
      121 mravemikpv vvklrmvpag navtifrrtm ldaegrviad qdladsadgm ldelgrltda
      181 lwamraa
//
LOCUS       WP_357671900             201 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357671900
VERSION     WP_357671900.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 201)
  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..201
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..201
                     /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=21995
     Region          5..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnlkaergaa trdrvlgiat rlfsehgydg tsiemvlhes alsrgalyhh fagkdalfea
       61 vfeavetrig reiaatvtsg asaeqalreg slawirlagd kviqrivlid apsvlgwekw
      121 relearhafg mlkrtlratr avreeyleih ahmllaaine iallvartgq teqaeraved
      181 flsrlldger pgrgsgaarg l
//
LOCUS       WP_357671961             266 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Micromonospora chersina].
ACCESSION   WP_357671961
VERSION     WP_357671961.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..266
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27466
     Region          1..242
                     /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..34,73,77..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..215,221,223)
                     /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..222,226,228)
                     /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 misvepvaap gaplarrnpv aklaaalvft lilvatldpv apaiaiavel avlplfgvry
       61 gvlarrawpl lagaggilvt lvlfaadrsg rvlveagpvl vtegvlvtal glvlrmlava
      121 lpgilvfatt dptdladali qnakaparfa igalaafrlv plleeewrmi smarrargvd
      181 agrnpiaklr lfgstafall vgairrgtrl avamdargfd agtprtvarr qrftradall
      241 vvaagtlaaa altvsvllgt frplig
//
LOCUS       WP_357671986             178 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357671986
VERSION     WP_357671986.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=19493
     Region          25..154
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mttdephdgv dviisqwqkv rpdldcspme iigrlsrvsr llerairdnf svygiepwef
       61 dvlatllrsg pphvlsagel staamvssaa ltnridqlek kglvdravdp ahrrrvlisl
      121 tdqglslvnr lvehhvaner rlleglssad rdqmpvllrr llvslgdtgp dtsatgss
//
LOCUS       WP_357671992             326 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357671992
VERSION     WP_357671992.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..326
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..326
                     /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=34081
     Region          1..326
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkpfdyqraa dprsavaals rqseamylgg gtnlvdlmrl gvatpavlvd vtratsdaie
       61 essgggllig aaarnsdlaa hpvvrrrypm laqavlagas gqirnmatvg gnllqrtrcs
      121 yfqdiakpcn khrpgsgcpa regdhrnlai ighssscvat hpsdmavala algasvhveg
      181 vegtrtvpmp glhrlpgdep erdtvlepgd litavelpal pfaarsryrk vrdrasfafa
      241 vvsvavaldl adgvvrdcri alggvahvpw ratlaesalr gapataeeft raadlelaga
      301 rplpdnafkv plarnvlvrv lgelas
//
LOCUS       WP_357672026             418 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea dietziae].
ACCESSION   WP_357672026
VERSION     WP_357672026.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 418)
  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   2  (residues 1 to 418)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..418
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44293
     Region          1..409
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mtdlihapag tlrgigagga vtaflgipya raerfaaprp rrwdsvldaa rpglaapqpr
       61 msrlervigp ggelhggelr qgenclslnv wapggsglpv lvwlhgggfl tgsgaqawyd
      121 gallaergrm vvvtvnyrlg algylyltpe fapanlglld qiaaldwvkd nisafggdpd
      181 ritlagqsag alsalalsgh pagrelfrqv ilqstptgvq pysigdaaei gqifldvlgl
      241 rssdaerlrt lpladllaaq eqvarrtaqp mgvtppfhlv aaddvpadlt tgapeempml
      301 igttrdeara ffpqagaglt arlfrdgslr laeqvrpayv yqfdwsapgs pfgachclel
      361 pfvfgnlevw raspmlagae paqldrlvad vqsawtgfvy rgspgwpafp hvqhitlt
//
LOCUS       WP_357672011             182 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357672011
VERSION     WP_357672011.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 182)
  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..182
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..182
                     /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=18885
     Region          2..>107
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marspsalrg hildsalqlf atqgykgasl hdiaqvagcs kasllyhfvs keailaellt
       61 pageglaald arlsglegee aaeaavtgfv dlamrfrrev kvlfqdipvl aghpalgavp
      121 aivarlmaam vegstepkal itaymvigav avtcaadvpv edddlraeli qgalrtlgrq
      181 pr
//
LOCUS       WP_357672083             152 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357672083
VERSION     WP_357672083.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=16986
     Region          26..149
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maqeeghdva gaadavradi rswptgrlls maarlvesrf hdfleahelt haglialhhl
       61 aegplaqrel arlsrvtdqt msrtvehlrr agyvgkgpde rdrrrvlvri tpsgaevlah
      121 areeergsdr llgavdeydr freqlirlit iv
//
LOCUS       WP_357672114             395 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora chersina].
ACCESSION   WP_357672114
VERSION     WP_357672114.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=41611
     Region          1..373
                     /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 mrsavvvgag lgglatagal arsgwrvtll eradrvrpet tavvlwpngv ralralglga
       61 gldaiatplp dggvrrpdgh wlvqprptpa ermpvvvhre dlhdaliagl gdqvelrtgv
      121 tvrtvraapg erpavgdgrh tveadlvvaa dgtdseirrq lapetavvss gcaawravip
      181 wyrapqlpdd qpvhgetlga gyrfvaaslg drgtagasrr ggiywvataa gaprpeppet
      241 qlallkrwya gwpapiatll datdpadvvq qeirelrplp raygfpagpg gvvllgdaah
      301 ampphlgqga clafedaatl sallresrlp davtaydrlr rpraatmvrq trrmsavlqt
      361 rgrlalrard aalgtisprl rntaataaas whppa
//
LOCUS       WP_357672141             271 aa            linear   BCT 28-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Micromonospora chersina].
ACCESSION   WP_357672141
VERSION     WP_357672141.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 18498059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..271
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27906
     Region          53..154
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          <111..257
                     /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 mllrtilaat aavtvllvpa taahaeptsa aattvaadtg ttaeattaea avganpvivv
       61 ggligisiay epiaarlrad gyrvsiyqlp glgfgdires aralssyvdq vraatgaakv
      121 dlvthsqggl vsrwyvkflg gadkvdryvs lgspqqgtyv aniinflglg scagivacqq
      181 msigsnfltd lnagddtpga vrwttvrtwq delvrpvdna aladgatnvl vqawcplriv
      241 ghlglildgt tytivrqvla gaairpncfa l
//
LOCUS       WP_357672143             519 aa            linear   BCT 28-DEC-2024
DEFINITION  GMC family oxidoreductase [Micromonospora chersina].
ACCESSION   WP_357672143
VERSION     WP_357672143.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..519
                     /product="GMC family 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=55243
     Region          1..519
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mdgfdyvvvg agaagcvlan rltedpgtrv llieaggwdr spfvrvpkaf srlmddprta
       61 whypatigpg rretwqrgrm vggstsingm iwsrgaaadw dalahlgwgw stmgpvferl
      121 aehpvrvsva tgtdplceem vetgaelgwr rvddldagdg erigyvtati hagrrvtaad
      181 aflhpvrerp nltvavdtva lrvlvddgra vgvrvahrgr eaehrasaev ilaagalatp
      241 qllqvsgigp adtlraagvp vlldrprvga glrehrpipv qyrltgpggy naalgsplgq
      301 araalryllt rrgplalpvm dvaahvksrp eldrpdvhll mapfsaapar pgralelere
      361 pgliclgtvt rpdsegslai tgpdprtppe ivanyfatah drrvavdalr rmrelfatgp
      421 iakriaaetl pgaavqtdee iveaarlhgy cgyhaigtca mgpddehvvd pqlrvrgvtg
      481 lrvvdasvlp vmvsgwtsap vsalawraad lilgrtata
//
LOCUS       WP_357672169             250 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            chersina].
ACCESSION   WP_357672169
VERSION     WP_357672169.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=25439
     Region          1..246
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mndeqqrtvv vtgagtgigr atarafavag arvlavgrra apltetaagh pliralvadv
       61 tdadaparvv gaaletygrl dvlvnnagia gggplaglde paarrqldtn llapirlaha
      121 avepltasrg vivnvitttv gqrawpgssv yaagkaalds ltrswavela prgvrvvava
      181 pgaidtpige hqglspdqra avrrwqldrt plgrigrped vawailrlsd paaafvtgvv
      241 lpvdggalva
//
LOCUS       WP_357672171             193 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357672171
VERSION     WP_357672171.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 193)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..193
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..193
                     /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=20920
     Region          3..185
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpppnpqrrd hladaaitvl aeqgsrglth ravdtaaavp pgttsryfrt rdallngvie
       61 rithrlgerv daytvrpisp adleealvav lttmltdsrh dplalfelhl estrnprlrh
      121 tltdalhgrs dlivrqcraa gidisqddam llemsvlgil ftalttgvpe spgepirtav
      181 rallahhqtp tat
//
LOCUS       WP_357672210             191 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora chersina].
ACCESSION   WP_357672210
VERSION     WP_357672210.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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 191)
  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 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 191)
  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 191)
  AUTHORS   Rosinski,J.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..191
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..191
                     /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=21219
     Region          12..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mekptvrhvt dsrvlaalah plrrrlmdvl kvygpcpvgl laertgqapa nvshhlkvla
       61 aadlvleape lardrrerww rlrdpavrws ntefdadpaa ravadaassl nldrhvalvr
      121 awhaapdeah aawgdgpfst dkwlhltpde laqlsrevte lfarwaerpa pddgqrrepv
      181 flfahgvpgq p
//
LOCUS       WP_357672242             201 aa            linear   BCT 28-DEC-2024
DEFINITION  LGFP repeat-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357672242
VERSION     WP_357672242.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..201
                     /product="LGFP repeat-containing protein"
                     /calculated_mol_wt=22013
     Region          51..>116
                     /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 mntakrsart aciyavavvl aplaipsgga paiastsacd lglvaprgsl vgdywrsrgg
       61 qnsvygcpvn tetgfadrrg srqqfqngqi awspnmgegn llriyakngk inlrwgttsr
      121 dwdffhvrwv ieadpkrqaq rrvkretaws gsygfnpypg vshgghlkev ftfwfqgcdr
      181 gtfssdcgaw snvpvyivwt s
//
LOCUS       WP_357672229             197 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357672229
VERSION     WP_357672229.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  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..197
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..197
                     /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=20999
     Region          7..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mngtararqr eetrrtlvre srrlfaargy gavglseivr aagvtkgaly hhfdskaelf
       61 ravveqvqqe vgrrvaegad amddpwdqlv agceaflaag adpevqqiml idgpavlgwn
      121 ewramdeaas ashladalaa lveagvianq plaplthlls gamneaalwl asstgpndla
      181 dtqaalvrml eslrvrs
//
LOCUS       WP_357672385             319 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea dietziae].
ACCESSION   WP_357672385
VERSION     WP_357672385.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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..319
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..319
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34022
     Region          1..195
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mitvviptig rsslreaipe gvpvivvedt grkgpaaarn agwraaatpw vvfldddvvp
       61 gegwlealtk dleslpedva gsqgrievpl prdrrptdae rntagladae witadmayrr
      121 aalekvggfd erfprayred adlalrmrea gfrlvrgerv trhpvrddgf wasvrfqrgn
      181 addalmrrvh gpewrsliga ggllprhaat talgltalal aaaralscan nregrgvral
      241 lggrglrggr gvrgagaggv walglaaagw agltakfawe riapgpgtpg evvrmvvtsv
      301 aippaaclhr lrgelrvrr
//
LOCUS       WP_357672491             243 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Nonomuraea dietziae].
ACCESSION   WP_357672491
VERSION     WP_357672491.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 243)
  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 243)
  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 243)
  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..243
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..243
                     /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=25797
     Region          9..236
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mnepapptsv tvltgagist dsgipdfrgp qgvwtkdpaa qamvsidsyl adpqvrrraw
       61 qarrdhpaws aepnaghral vllersgllr slvtqnidgl hqkagstrvi elhgtifeve
      121 clscglltpm revldrqepd ppclrcggiq kahtisfgqs lkeevlreav taarecdlfl
      181 avgtsltvqp aaglcgeald agaglvvvna qptpydafad lvidrpigea lpalvrelid
      241 arg
//
LOCUS       WP_357672493             292 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea dietziae].
ACCESSION   WP_357672493
VERSION     WP_357672493.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=32129
     Region          <116..247
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mrppphilvv ngikvrrpvf llgaphsgad llaralkrsp gfhltmgrqs vahvvhafar
       61 rpsiarssga vrvmrdslae swqvlpgscg hcplpcreag gvtgsgpcvs taavtrfgda
      121 spdllysaev llqafpdarf vqlirdgrdv tadmvndpdc lawfkpsmls ddtefpnafl
      181 gvnrdehrdr wksmptagkc alrwrsavrl satlrrdlpt dqlltlryed lalspgetlt
      241 slssfletrv skvsmygmrv pevgswrarl rsadrelvek vareeltrlg yq
//
LOCUS       WP_357672532             263 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Micromonospora chersina].
ACCESSION   WP_357672532
VERSION     WP_357672532.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..263
                     /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=27721
     Region          19..214
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mesdaealei vvdparptgr tllaagveqs yvdvtdprhl hfeyvrrmaa vvdlaappgr
       61 plaalhlggg altlprwlaa trpgspqrvi erdpavvdlv rrdlppappe vvveigdard
      121 avtaapagay dlvladvyra armprhvasm efaaavarvl rpdgvflvnl tdlpplahtr
      181 tqvatlravf advclvadrr mlrgrrygnl vlaaatrpdr lpvrrlvara agdpvpggvl
      241 hgatldafva garpatdatl agg
//
LOCUS       WP_357672545             227 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357672545
VERSION     WP_357672545.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..227
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..227
                     /product="helix-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=24245
     Region          1..216
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mtssiepgse rstrarvarl ilehgpvtav algerlgltp aavrrhldal ladgmieprt
       61 vrprgqrgrg rpaklfaitd agrsafehay ddlagsalrf laermgeeav tefarsqveg
      121 llqrlepvmr tvpedqrvqv laqalsadgy aasatkaksg gdqlcqhhcp vahaaaefpq
      181 lceaeteafa qllgtpvqrl atiahgdgvc tthvspvrik esketgr
//
LOCUS       WP_357672636             201 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora chersina].
ACCESSION   WP_357672636
VERSION     WP_357672636.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=21208
     Region          37..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 mgkptrwvte tkpghsqwyv drfrrlaaeg adlagearll dtlvppgari ldagcgtgrv
       61 aaalaerght vvgvdadpvl idaaradhpg prflvadlad ldlaaqgepe pfdaavvagn
      121 vmafvapgte ravltriaah vrpdgpvvvg fgtdrgyplt eldadavaag lrlehrfatw
      181 dlrpwhddae favtvlrkpa s
//
LOCUS       WP_357672670            1039 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora chersina].
ACCESSION   WP_357672670
VERSION     WP_357672670.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1039)
  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 1039)
  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 1039)
  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 1039)
  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..1039
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..1039
                     /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=109784
     Region          8..1033
                     /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 msqewtfpas faqervwman qldagspvfn vsipwrfpag vdadtasdvv nrvvarheal
       61 rthlreddgt lvqvvrahep vplpttdlrh lpeserlaaf eeiraelart pipldtpplw
      121 rarlvhigds walvfvvhha vfdshsavlf haelaafcaa aqagadpavp elpiqyadfa
      181 vwqrdqlagp eldrqlafwt ghlagappvt nlpldrprpa qlgfagdevr fdlpdglldr
      241 vgrlaagaaa tpymvllagf aallsrisgd tdvvvgvsta grdtpelapl igmfvnpval
      301 rcdvsgdpsf aallgrvrdg lvdamehgqt pfqkiveavd pqrdpsvqpi fqtalnyipd
      361 sgldpvelgt tkddlafdit agecrlvyrt alfdrataet vvrryvallt aavadpertv
      421 aalplltdae rdlvlgawnd tahevpaatv vdevqrqaaa apdatalvcd gvpltyaeln
      481 taanrlarll vsrgagpetr valalprsce lvvamlavlk sgaayvpvdt gypagriayl
      541 ledaapalvv atpdtaalvp gdalvldgel gadqpdgdlt dadrrsplrp ehpayvlyts
      601 gstgrpkgvv vehravtayl awarhtylgl agvallhspv sfdltvtgll gtltaggtir
      661 laaidepaar aggrpaflkv tpshlplldg elsptadlvi ggealtgeql agwraahpdv
      721 avvneygpte atvgcvaari apdepvpsgp vpigtptwnt rallldaalq pvppgvvgel
      781 yvagaqlarg yhrrpgltae rflpcpygpp garmyaagdl arwrpdgsld ylgrrddqvk
      841 vrgmrielge veaallahpd vraaaaavrt dggeptlvgy lvgpahedsv raelarelpa
      901 hlvpaalirl dalpltpngk ldraalpapa aaapaedayv aprteaeslv aevyaeilqv
      961 ekvgalddff tlggnslrgm ramariraev dvdlpmralf sspvvadlaa qieeriaael
     1021 dglsdsevaa llaaeeess
//
LOCUS       WP_357672674            1069 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357672674
VERSION     WP_357672674.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1069)
  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 1069)
  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 1069)
  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 1069)
  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..1069
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..1069
                     /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=113718
     Region          1..233
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          143..1047
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrfgvlgpte vsgvpvrgag lsgllvllal eagrvvsvdr lvealygpsg tvnalqsqvs
       61 rlrglvgvpl elgpagyrlv vdplevdahl fthtvavarr asspgerarl lrealglwrg
      121 paladvltlp faeaeaatle elrlsavedr veadlltgca plaelvselg elvrrqplre
      181 rlrgqlmlal arsgrraeal evfeearrtl aeelgadpsp elaalhvsll rdeppsvvas
      241 paasadplav ghlpaaavst aalgaasalr praprprlts fvgrdhelrl vgellgrgrl
      301 ltlagpggag ktrlaveaae aahglgevcf velapldpgs dvalavlial glpygrsepp
      361 gplsaarqdp sasmslprge ppvdalvtal ghhrvtlild ncehlvepaa lladrilaec
      421 prvrvlatsr eplnidgeqv lpvsplprpp hdldleqare hpavrlladr aaavrhgftv
      481 tgdnlepvlr icraldglpl aielaaarlr altpsevaar lddrfrlltg gsrtalprhr
      541 tlravvawsw dlldpaertl aarlsvfvsg ttaeaaervc ggdldllsal vdksivqadg
      601 grfgmletvr afcaerlaes geqqrvrqah aehytrmaaa aeselrgpdq lrrlaelaae
      661 hgnlraalrw aidtgqaema lrltadlwmy wwlrglrheg allsaevldl vgpeptegla
      721 edhimcalqm vttgrpleea rerldnaerl argmtepprh pliamvrpyp aiasgdytll
      781 lpallaatta sdpwsrafar lllgylrlga geveagehel rlaldtfrma gdrwgvgqam
      841 lqlselsgwr gehkeaiama eealeviapf gatedtallm srrgaelara gdvaaaqvel
      901 eraasmarrl pgseaeaiat yglaelarlg gdparately laamagceah wlgahetrgr
      961 iliglgrveg egarlreayd llvdvldlpg asgaveamae lalregsaar aafllgaavs
     1021 lrgaaltdgp dvvrtagear rvlgdaafer syqrgcstpr dqitdllpf
//
LOCUS       WP_357672748             274 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357672748
VERSION     WP_357672748.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   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 274)
  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..274
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..274
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29123
     Region          3..266
                     /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 mnkvmsadgt aiaydrrgsg palilvdgam cwraqgpsgp ladllkqhft vytydrrgrg
       61 dshdattyqv ereiedlral ideaggaahv ygissgaala leaanaglpi tslalyeppf
      121 ivdgtrppap adlltqtqtl lasgkrgdav klfmtkginl pglvvammrf mpawsklksv
      181 ahtlaydlti mgerqlghpl ptdrwtaltm pvlvadgaks ptwirngarq ladvlpgaeh
      241 rtlpgqthmv kpealapvlt affsghdapp psra
//
LOCUS       WP_357672690             824 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Nonomuraea
            dietziae].
ACCESSION   WP_357672690
VERSION     WP_357672690.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 824)
  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 824)
  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 824)
  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 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..824
                     /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=89780
     Region          47..816
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 msdtpfgsff gdpfrgfeql sgrvfggmda wpptrpsvqr vdvgrllses arqllaravq
       61 iaadrgapdv dvldvlaaat eedpgrallm sagadpgklr erveslsqsr tpgeapttfs
      121 paakravlda qrvsralgas yigpvhllla laanpdstaa rllaeqgvsa gelqtatiae
      181 pergatpkde tpaldeygrd lteearkggl dpvvgreeei eqaievlsrr tknnpvlige
      241 pgvgktaive giaqrivngs vpdtlkdrrv valdltgmva gskyrgefee rikkvidevr
      301 rhsdeivvfi devhtlvgag saeggmdaan ilkpalsrge lhviaattid eyrkhiekda
      361 alerrfqpvl vpepsvedtv gilaglrday eahhqvritd daldaaasls dryiadrflp
      421 dkaidlmdqa aarvrlrart paadvrelee rvaslrrekd qavagdefdr akeltseidr
      481 lrpelenarh ghdtvpevtm adiaevvsrr tgipvsqlte qerdrllrle qhlhervigq
      541 deavtavaea vrraraglsd phrpigsflf lgptgvgkte laralagalf ggedhmvrid
      601 msefgerhtt arlvgappgy vgyeeagqlt eavrrrphtv vlldeiekah pdvmnlllqm
      661 lddgrltdgq grtvdftnti vimtsnigaq lilhggddve erlmdllkat lkpellnrid
      721 etiiftrlgs eqlrqivdll lektrqrlrg qgielrvsdq akdwlaehgy qpefgarplr
      781 rtvqreldnr lsslllggqv kegdtaevdv sggglevkva aqta
//
LOCUS       WP_357672744             115 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357672744
VERSION     WP_357672744.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=12581
     Region          14..97
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgrtpphpev pqfdlqqile alvdpvrrsi vtqletaged ikcggfgiqv skstathhfk
       61 vlreaglirq yyvgtsrmna lrraemdeaf pglldalttp qarradpavq arstl
//
LOCUS       WP_357672752             399 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea dietziae].
ACCESSION   WP_357672752
VERSION     WP_357672752.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..399
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43884
     Region          4..399
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 msqlegvfre eygravavlv rafgdidlae davqdafaea tkrwpstgtp pspagwiitt
       61 arnraidrlr ressrderha qaalmasgde tdqvegpvrd drlrliftcc hpslataaqv
      121 altlrllggl ttaeiasafl vpeptmaqrl vrtkgkirda ripyriprea dlpdrlravl
      181 svlylifneg yaasagdrlv reelcaeair lgrllaelmp depevwglla lmlllqsrra
      241 arttpdgrlv plaeqdralw nhdliaeghq ivrrclqrdq pgpyqiqaai navhsdgppt
      301 dwrqilalyd qlllftptpv valnravava eiegpavale lvddldlggf hlfhairadl
      361 lcrmgrdaea lrayaaaiel tanaaerafl raraeaiar
//
LOCUS       WP_357672756             219 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357672756
VERSION     WP_357672756.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 219)
  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..219
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..219
                     /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=23158
     Region          26..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaskpdgrt araratrarv taaatelfva agygatsvna iaaragvgeq tvyyafgtkr
       61 avltaaldva vagddepipt lerawvreal aepdpaeqir rqvegagaiy lraaalldvv
      121 rsaaasdpdl aevwadnvdr rltvlrvfae alaakgalre eltvedaadi alaslspety
      181 tllvhgrgwp harwrrwatg alvhqlttra crngtgafv
//
LOCUS       WP_357672770             117 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357672770
VERSION     WP_357672770.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=13097
     Region          1..92
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 myvrvvvnsv qqrltaisep nrfrivellr dgpqsvggiv dalglgqpqv srhlrllaea
       61 gvvevtkraq qriyrlhpes mrelsgwvqg favlwsermd rlgsfldddc vpdeanq
//
LOCUS       WP_357672825             262 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357672825
VERSION     WP_357672825.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 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   4  (residues 1 to 262)
  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 10248791
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..262
                     /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=28140
     Region          4..105
                     /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(5..7,21,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133382"
     Region          112..254
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mdllpigqfa rlsrlsvkql rhyadlgllp pahvdddtgy ryyhpsqarq alsigllrsl
       61 dvplaviaqv lsgttgalgq vrddldselr rrrrtlsale kvmadglpsa qvrvveesar
      121 lvavtgeqaa ddldvgrats acvarllaah lqqanpqqsa prliglfpvd lnepitveva
      181 lesgapvtga tsrllpggrf aqathigpyd qisltahall swcaernhpv rgpirevyas
      241 dpattpadql ithlqvplee dq
//
LOCUS       WP_357672857             260 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357672857
VERSION     WP_357672857.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26932
     Region          1..259
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mgpltgrtal vtggsrgigr aivqrlaadg asvvftyasa eaaarrvaae idlevgalrg
       61 sadggawpvr ldltdlddiq rlfataftaa herfpepgld ilvnnaaiaa drpisevtea
      121 dydhamavna kgvfftiqha lphlrdggri inlstvsttw pspgealyta skaaveqfsr
      181 vaakelagrg itvntispgp tdtdllreat teqerqavat mtplgrlgtp advaavvafl
      241 agpdsgwvtg qnihvdggli
//
LOCUS       WP_357672917             287 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora chersina].
ACCESSION   WP_357672917
VERSION     WP_357672917.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 287)
  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..287
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..287
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30526
     Region          2..281
                     /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 mptflgsdga qlhyddlhsg dserlllial aggaarhpsy lgdlaglser qhlivphlrg
       61 vgrsplpdtv evasfwrqae dierlrvylg lehvlllghs agtrlaisya aqfpgrvagm
      121 vlltppagyl vdvpsdadel idsrrgepaf daalaawtag pdadddadfn awqpqvaplg
      181 yaawgaaeqa haavgrysfa anrayfsvdp pqdlaarlge vtapvlvvgg addcitgiap
      241 vialaklfpa gesvmiercg hypwveqpaa frqavdrfll ryptpds
//
LOCUS       WP_357672912             157 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357672912
VERSION     WP_357672912.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=16629
     Region          <41..148
                     /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 mrlgccsarw ssapatsgsd ltpasglpav wcspglpast andalvltgt irwptvidnh
       61 nrsahiglgl lpsargkgyg tdvvavlchy gfvvrglqrl qietladnaa mlrsaerngf
      121 vregvlrssa wvmgefldev llgllvhdwk ptskayl
//
LOCUS       WP_357672943             479 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora
            chersina].
ACCESSION   WP_357672943
VERSION     WP_357672943.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 479)
  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 479)
  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 479)
  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 479)
  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..479
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..479
                     /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=49801
     Region          3..477
                     /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 manttydvvv igagpvgenv adrvvqgglt aavverelvg gecsywacmp tkallrsata
       61 lraarrlpga reavtgdlva savlrrrdaf asnwsddgqv swldsagial yrglgrisad
      121 rvvevigedg astsltarha vvvatgssal vpdvtglrea apwtsreaaa asevpgrlai
      181 igggvvasem atafanlgsv vtvlardgvl pqaepfager vtqslreagv svrlgaeavs
      241 vsrgadgtvh ltltdggqve adellvaigr tprtqdigld riglkpgawl tvdhtlrvvd
      301 edgslvgdgw lyavgdvnrr vllthqgkyq aravgdviva raggepvdds rwgrhvatad
      361 eravpqvvft dpeiasvglt aaaaeaaglr irvvdydlaa vagaalhvdg yqgharmvvd
      421 edrqvivgct lagpdvaell haatiaivge vqidrlwhav pafptisevw lrlleaygr
//
LOCUS       WP_357672948             154 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357672948
VERSION     WP_357672948.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=16596
     Region          1..137
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mskhvdgqig avaalvrstf lvnavyadsa reygltqqqg qllcvlmaqp ygmselgavl
       61 glakssltgl vdrsernglv erkpdpqdsr avrvaltrqg akladdfyte tcrrieelts
      121 gfaaeeretl aallgrvvtd nkvptvflep grtr
//
LOCUS       WP_357672974             386 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora chersina].
ACCESSION   WP_357672974
VERSION     WP_357672974.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=42168
     Region          50..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 mtqamderai aapttnpvqp gqrpelprqa gapepaagaa parrprllvl dglrlgaalm
       61 vvayhlvgdk igvwdasaat nfgpvhslak ygflgvqlff iisgfvicms awgrsvgdff
      121 vsrvvrlypa ywfavlltaa vlvavprgpr vqprevvgnl tmmqdflgir hldlsywtlt
      181 vemcfyiffa vlvarglsyr gvvafcaiwt vaslivpklg npwltnvvaa nhssyfiagi
      241 alylihrfgp slllwsvvgl swlvaltrlp nlaqardvaf aptavivtlf flvmaavaln
      301 rfawvkagwv atagaltypl ylihqtvgla vieraqdlmp pwvlitalva alllaawlih
      361 rlierpvarw mkrqlsasmr qvreas
//
LOCUS       WP_357672990             162 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357672990
VERSION     WP_357672990.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 162)
  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 162)
  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..162
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..162
                     /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=18025
     Region          23..162
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msseqdpidv ileqwrrerp dldlsamgvf srlaqasrlv esaveqvfrr hglrpgefdv
       61 laalrrsgpp ytlipselsd vlmmsragmt nridrleaag lversldpad rrsfrvaltq
      121 egrevidatl tehaanlatl atrlteqeaa tldtvlrrml ar
//
LOCUS       WP_357673004             815 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Micromonospora chersina].
ACCESSION   WP_357673004
VERSION     WP_357673004.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 815)
  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 815)
  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 815)
  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 815)
  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 815)
  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..815
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..815
                     /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=89294
     Region          92..813
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 megtvhptgd adgsvtersg gnpparvtgp gsgpdgladg gavvvpfptd tgadpspagg
       61 falsnaptgr rvrarlarfn apwqtsqvse vlepliathr enhpkadarl lqrafdtaar
      121 whsgqyrksg dpyithplav atilanlgmd tttlvaallh dtiedteytl dqmradfgge
      181 vallvdgvtk ldkvklgdaa kaetirkmvv amakdprvlv ikladrlhnm rtltflprpk
      241 qeqkaketle ilaplahrlg mntikweled lafgtlfpkr feeinrlige hqpqreallr
      301 qvtqkvstdl kaakikaett grpkhlysiy qkmivrgrdf ndiydlvgvr ilvdtvrdcy
      361 aalgvihanw qpvpgrfkdy iampkfnmyq slhttvigpt gkpvemqirt yamhrtaefg
      421 iaahwkykeh kgtpvvgppa hidemtwlrq lldwqreaad psefldalrf dlssqevyvf
      481 tpkgdviplp tgstpvdfay avhtevghkc igarvngklv plestlsngd vieiftsksd
      541 tagptqdwlg fvksprartk irqyfnkerr eeaieagkds ivkamrkqgm plqrmltsda
      601 lmaiardlhl advaslyaav gdsqvsaqsv vqklmaaygg eegaaediae tavatrpprs
      661 rqssadpgvv vrgvsdvwik larcctpvpp davfgfvtrs ggvsvhrddc anaedlraqs
      721 ervvevswkl tsastflvai qvealdrhkl ladvtrvlsd ervnilsatv tttrdrvavs
      781 rfsfemadpk hlghllaavr kvdgvfdayr vtsga
//
LOCUS       WP_357673008             232 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357673008
VERSION     WP_357673008.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 232)
  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 232)
  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 232)
  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 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   5  (residues 1 to 232)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..232
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..232
                     /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=24155
     Region          3..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msaqglasfa alladptraa fclalldgra wtagelarta gvaastaseh lskmveggll
       61 aeerqgrhry vrlrdaataq lvedlaarvs psaathttlr aasaasalar artcydhlag
      121 rlgvsvtdal lshglldpgf slsasgaawf eelgialtas rtrpmarpcl dwterrphla
      181 gtagaalcrh alevgwvtri ggqralkvtd sglsslarll eipsdtlrps pn
//
LOCUS       WP_357673024             564 aa            linear   BCT 28-DEC-2024
DEFINITION  murein biosynthesis integral membrane protein MurJ [Micromonospora
            chersina].
ACCESSION   WP_357673024
VERSION     WP_357673024.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Kuk,A.C.Y., Hao,A. and Lee,S.Y.
  TITLE     Structure and Mechanism of the Lipid Flippase MurJ
  JOURNAL   Annu Rev Biochem 91, 705-729 (2022)
   PUBMED   35320686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     gene            1..564
                     /gene="murJ"
     Protein         1..564
                     /product="murein biosynthesis integral membrane protein
                     MurJ"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=56766
     Region          19..521
                     /region_name="MurJ"
                     /note="Lipid II flippase MurJ/MviN (peptidoglycan
                     biosynthesis) [Cell wall/membrane/envelope biogenesis];
                     COG0728"
                     /db_xref="CDD:440492"
ORIGIN      
        1 mtkpapvava grvagaaali avltvvsrla gfgrtavftw tlaptdlgga ylvanyvpnf
       61 ifeivaggal aslvvpllag aveagerrav adttgalltw tlsllvplal lvalladplm
      121 gllghgldaa qqeagarmlr vfapqlplyg vgivltgvlq ahrrfawpvi apllssvtvi
      181 vvylaftaae grlarvaevg rggelllsgg ttlgvvvlsl slliplrrlg lrprpgfrfp
      241 adararvggl avagvvtvaa qqialvvaln qvtygrtadv gvynlaqtiy flpwavlavp
      301 vavaayptlv asraagdera yretlapavr gvvlfsllga aalagtavpv ghfffdpada
      361 gtaaagiagf apgllgyglf avltralyar getrsatvat algwlsvpal alllgrllpl
      421 adrvlavtla tsagmlllgg lliaavrrsa gpaalagvgr agaagllaaa vaalggaata
      481 rglagltdgt pttaealaqg mlsgvvvgal flavawltda rdlrpllaav trrlgrrrpp
      541 gggdgpradq hpgergdgke tvss
//
LOCUS       WP_357673134             387 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Micromonospora chersina].
ACCESSION   WP_357673134
VERSION     WP_357673134.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..387
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39584
     Region          37..384
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mtgpavgpld rvaprygggs ladvlpsala llgvpgaadl lglaprlagv rrvavllvdg
       61 lgwyqiptaa pyaptlagla atvgvpltsg fpsttptslv slgtgtpsgp hgvlgftvrv
      121 pgtdrvlnhv dwagdpepsa wqpvptwyer araagvavtv vsrpefagsg ltlaanrggd
      181 yrgaagadpl aermlaalaa gpgptlvsgy hpdldrhghl tgvdsapwrl aaaevdrlla
      241 rlvdglppda allvtadhgq lnvpdghrid ldtdprlrag vrvvageprv rylhvepgat
      301 advvaawsav ldgaarvltr aeamatgwfg pvpeahlgri gdvvvvcrdt yavvatrsep
      361 pmasrlvayh gadtaaemti pllvvrg
//
LOCUS       WP_357673157             524 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase [Micromonospora chersina].
ACCESSION   WP_357673157
VERSION     WP_357673157.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 524)
  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 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..524
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53584
     Region          4..519
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mtnpstlyrg gvlhcpadps atallvrdgr iawlgadada paadrvvelg galvtpafvd
       61 ahvhatdtgl alsgldlsgv rsasglldal agfaaalpad avvlghgwde sswaepalpd
      121 aaaldraagg rkvylsqasi hsalvstall aacpdaaaaa gydpsgwlrr dahhvvraaa
      181 fasvtraqrv aaqrralaha aslgiaavhe cggpdisdee dftgllgisg agvpevygyw
      241 gellgaakar elgavgaggd lfadgalgsr tahvsaayld gepgacghgy vsaeqvrdhl
      301 ldcaahglqg gfhaigdaai gtvlegfaqa aqkvgvdrlr aarhriehae imskrliagf
      361 veygivasmq pafdrlwgga grmyesrlgl srslesnpmg amhgvgvala fgsdspvtpl
      421 dpwgsvraaa ahhnpvqrms vraafaahtr ggwravhldn egvlalgapa tfavwdtpag
      481 verglpvlqa edpeargadd ptplpvcrat vlrgdviyqe gsle
//
LOCUS       WP_357673218             344 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            chersina].
ACCESSION   WP_357673218
VERSION     WP_357673218.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=37742
     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 mrasrlvsll lllqtrgrmt aqeladalev svrtvyrdve slgaagvpvy adrgpaggyr
       61 llegyrtrlt gltapeaeal flagmpgpaa dlglgpvvaa aelkllaalp deladrggra
      121 rqrfhldapg wfrhpeatph laalaravwe drlvemryrr wraprevtrv vaplgvvlka
      181 grwylvarcd gqlrtyrvga vldvvvsder herpadfdla dywrewtery erdvyrgrar
      241 irltvaalef mpyvfppems raaraaagep gpdgwlettv piesvkhaht ellklgaeve
      301 vlepaelrdr ltatahalar lypvapetpa gvadtptapa atsp
//
LOCUS       WP_357673237             398 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Nonomuraea dietziae].
ACCESSION   WP_357673237
VERSION     WP_357673237.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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..398
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..398
                     /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=44005
     Region          69..365
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 makiligkye atiypegngy tgaislgfgp dgkrqrlkrk grtkaevktk lieaakelea
       61 gvkssdtytv reavedwlsk glkgrsegtv sklttlarkh viplignekl krltadqvda
      121 wmdglaghls trtlgevhai lkratrqaqa rdlvmrnvae lvqtptgkeg rpskaltqeq
      181 adavleaaea splhayvvls lttgirteea ralrwdhvva wdktakgwrp vteagfkher
      241 faiyvwraer vggdtktrks rrtleiskla aealrqhhtr qaavrlkagd awqehglvfc
      301 tsvgtpmdah nvrrsfrsit rqakvgedwt prelrhsfvs imsandvple tiadlvghag
      361 trvteavyrk qlkpvitkga etmnavfgdg krrkrksa
//
LOCUS       WP_357673307             530 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357673307
VERSION     WP_357673307.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 530)
  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 530)
  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 530)
  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 530)
  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 530)
  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 530)
  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..530
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..530
                     /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=54598
     Region          143..521
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mhrrllavlv plavllvaal gvplsvsvae remqetyvdr lndvgrfasl aetalstgrt
       61 ealhqelary relygipvav idpsgavllg pagayqeaar aepalprivt aalagarsep
      121 sgewapwdds alvvaepvgr dsevvgavvt isdlsktrcr ilvrwarlag lgllplialv
      181 avawpvsawv lrpvreldaa ssrisqgdlt tradaeagpv elrrlagsfn tmmdavenav
      241 qrqrafvsda shqlrnplts lrlaveslep hlradgdgrq vydvavdelk amqrmlnslq
      301 asarmesirt vspvdldavl atrvdrwral tatagqtltv dvppglrlle psgglgsild
      361 elisnalrls daqvvevtar avpgghvggv caghgggaga ghgggvcvgh gggegaghgg
      421 gvcvghggga raghgdasaa ggvvtiavrd ngqgmdaser aqaiqrfwrs prhqnvpgtg
      481 lglaicadlv gaaggelrle eglprpdgsg hgfaavvalp vvprvasssv
//
LOCUS       WP_357673345             380 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357673345
VERSION     WP_357673345.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..380
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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]"
                     /calculated_mol_wt=39732
     Region          3..>56
                     /region_name="NagA"
                     /note="N-acetylglucosamine-6-phosphate deacetylase
                     [Carbohydrate transport and metabolism]; COG1820"
                     /db_xref="CDD:441425"
     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(54,56,205,225,294)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mpairarrlf dgrellgerv vhvtdgkitt vtldgpadld lgdvtllpgl idchvhlvfd
       61 astdpvghlr essdeevldr mreeaartva agvttvrdlg drgylalrla eklgvtegpe
      121 ilasgppitt tgghcwflgg qadgvegvra avreraergv hvvkmmvtgg emtpgsfshl
      181 rqyglaelca aveeahahgl piaahahage giadalaagf dtiehcsfmt ehaaehdeti
      241 iarlaasdvi vsltaglvpt geppppgiak rmpgimaavr alhaagtafv igsdagigpg
      301 kphgvlpyga rmlvdlgyap ldvlrsvtsr aaracrvadr kgrimqgyda dllavggdpl
      361 adisalqrps avfrmgrqvr
//
LOCUS       WP_357673354             344 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Nonomuraea dietziae].
ACCESSION   WP_357673354
VERSION     WP_357673354.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 344)
  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..344
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..344
                     /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=38499
     Region          1..339
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtdvpvtvea rgsdfarlar kinqaglldr rpfyyalrls lvaaafvggw vafvlvgdsw
       61 wtllvafasa vafaqlalva hdlahrqvfr nrrpseiagr iagnlfigmg ygwwtdkhtr
      121 hhanpnhedh dpdvspaviv wsveqaervk glpkfvarrq awlffplltl egwhlhvasf
      181 kslakesmrh rgleaallvl hfvwffglif tvlpfgkavv ftlvhqavfg vylgctfapn
      241 hkgmpiltke deldflrkqv ltsrnvrggw ivdvalggln yqiehhlfpn mptpnlrkak
      301 pivmahcael gvdylesgli ssygqalrhl hevgeplrkv kara
//
LOCUS       WP_357673363             371 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Micromonospora chersina].
ACCESSION   WP_357673363
VERSION     WP_357673363.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora chersina"
                     /db_xref="taxon:47854"
     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=38549
     Region          34..371
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mgvgtdelyp aerlaaaqra taaagldall ltpgsdlryl tgydaheger ltclvlpaeg
       61 eptlivpvle rpgaeaapga gyrivdhadg tdpwplvraa lpgpvaavgl adrmwaeqvl
      121 alratlpdaa qrlasevlre lrirkspaei aalaeagaai davhrrmgew lrpgrtevev
      181 aadiaaaira aghvrvdfvi vaagpngasp hhgtgdrpir pgepvvvdig gtmpsgyrsd
      241 ctrtyvaggp apaeftdyya vlheaqraav aavrpgvtae aldavardii taaghgdafl
      301 hrtghgigld theepyvvag nprpleagma fsvepgiyla grhgariedi vvcttdggqr
      361 lnttptelia l
//
LOCUS       WP_357673372             226 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357673372
VERSION     WP_357673372.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 226)
  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..226
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..226
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=23729
     Region          3..224
                     /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 mnlvlvhgtg gdpatnyghl vdgfadvrhv itpdysqitg elsvdqlash vtadlpdepy
       61 dlvgfslgav vaaaiaagdp arvrrlvlia gwvdnsdfrl hlgfstwarl aatdptsfga
      121 fgplvafspa fvsamgedat kdtpppgtvs qieldarvdi rdrlplitap tlvvgcsqdh
      181 lvpvsnaral hegiagssya eldsghvvll erpaeittli rdfils
//
LOCUS       WP_357673393             398 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357673393
VERSION     WP_357673393.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..398
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43707
     Region          <182..389
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrgdlsdarr lwdsvpsgia halrpgtakl sdevieeiqt ripeyarpsd eiyikvvrla
       61 veeaigrfld riedpdapwd pepfrmigrg eategrnlep lqtamrlgar vgwrrlteia
      121 eplglspqsl ydlgeaifvy ldqladaaae gfdearahaa gemerrrhrl ldlllsqppa
      181 aaeaisdlak aagwrlprtv agvalddqng tpslppdilv gldrpqpcll vpdpngpgqp
      241 qmldkglrgw raaigpavpl eraatslrwa tealelarrg vlpggrgplr csdhmatliv
      301 fkdeelvgal aasrlaplah lrpsqqdrla etllawlryg rgagevaarl hvhpqtvryr
      361 lrqleelyge qlgdpdirfe leivlrarqa aregarps
//
LOCUS       WP_357673398             201 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357673398
VERSION     WP_357673398.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 201)
  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..201
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..201
                     /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=21677
     Region          5..>95
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnlrdrkker trqllsdtai emflaegfdr vavadiaaaa evskptlfry fpakedlvlh
       61 rfadhqgepa rvveeraede splralrrhf lrglderdpv tglcdlpevl afqrlvfgtp
      121 slaarlveyg tadadalara lggpapglva aqviavrqvl ardnvaaisa grsadevype
      181 aveaadtafd llshgaagrg y
//
LOCUS       WP_357673408             486 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Micromonospora
            chersina].
ACCESSION   WP_357673408
VERSION     WP_357673408.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 486)
  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 486)
  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 486)
  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..486
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..486
                     /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=53652
     Region          27..408
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 magefvvlvv lgvvvprrrd paaprvvhrt arvglrvtag qrrrcfgllr sagdvwacvl
       61 evngwrrrrr dapltsyqel crelsvsgps tfgeldstga rsvlrrfsda wfaaakrrkd
      121 gdlsarfprr rrglvpvrwy hgtfaldgar vriptargaa plwvrlartv pypveqvrsv
      181 tllceggrlf lditaevpal tyragegpdp arvagvdlgi ihpyavagpd gagllvsgra
      241 iraehrmhla dtkarcrava rrapkpgqkg srrwrqyrrr awqvegrhrr rvrqaqheaa
      301 rqvvswavrq rvgvlrvgdp rgvldldagr rhnlrlrqwq igrllqvltd kavlagitvh
      361 lvdergtsst cpacrrrmpk prgrtltcph cafsghrdlv aaatiatrtp gggtttptpa
      421 rvpgvvthrr agrhlpgagr srrdprrpsr aargsvgprr papppggesl aqkarihnth
      481 rtpger
//
LOCUS       WP_357673454             205 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357673454
VERSION     WP_357673454.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 205)
  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..205
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..205
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=22339
     Region          5..201
                     /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 mgepidvngt rmwverrgrg pdvlliagls dpaeawqaql dgladryrli afdnrgagrt
       61 plpqgplsvp lmaddaaall raldvpaalw vytprahadg tvermieeal afphqqsvea
      121 fqrqfeafet hetldrlpei avptlvlage idratppllg revaegisga vfevlageah
      181 qpfqevpdef narvdafwre vdgrg
//
LOCUS       WP_357673481             310 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357673481
VERSION     WP_357673481.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 310)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..310
                     /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=34094
     Region          23..306
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtltaapprt tptpapgppr rrlryagtva vfllpslipl vlftlvpmag slwvslhewn
       61 liepmrwvgl dnygevladp rtraaflhtl tfiagylplv yagglglaml lnramggrni
      121 fraiyflpvi tswvvvalmw kwllnpasgi vnwalgllgv egpgwwtdpt wampsiilas
      181 awkdlgfvmi illaglqaip neyheaarvd gasawqrfrr itlpllspst ffvvvislin
      241 gfqvfdqvhv mtgggpggat evvveqvyrl tfqygragaa salswllfav vllvtliqvr
      301 vqrrwvnygy
//
LOCUS       WP_357673493             492 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea dietziae].
ACCESSION   WP_357673493
VERSION     WP_357673493.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 492)
  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..492
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..492
                     /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=51201
     Region          11..265
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,103,139,141,
                     143..144,146,156..157,160,177..180)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,141,143..144,
                     146,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,101,103,139,141,143,160,177..180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(156..164,173..180)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <228..455
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mlgsgttlnd ryrlttrlgg ggmgevwrad davlgravav kvllpalmed prfaqrfqne
       61 aramatlahp gvvdvydcgt celgdgrrvs flvmefidge sldrllrrsa ltpeetmrlv
      121 aevadalaaa heqgivhrdv kpanlmirpd gsvtltdfgi ahsasggqlt atgtvlcsag
      181 ycapeqasag titpavdvya lgvvayqclt gelpfdgetp vqiifkhlra pvpplpedvp
      241 agprvlvgra lekdperrwp sasdmaaaar haaahptasi wssaappaae pgrspatqrp
      301 aadsseadlp lepgagqepg sapltagpat rpadlkrggr rralvmaaat vtalvatvaa
      361 vgwtwfrqpe plqsvrrdqp vplpvvgrtv evrlpvkqgq trpptstikd gkvvpsapas
      421 svgpttpkps apatppaspp qeptkeptpe psaepstqps pqeptaeptt npptpdpqtg
      481 pgdvqcikap cp
//
LOCUS       WP_357673519             263 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357673519
VERSION     WP_357673519.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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]"
                     /calculated_mol_wt=28130
     Region          24..250
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mgltmaegvp raalrpyvtr lcayrerydr pltrteaavp gavlilafga pmqvggarlt
       61 sftgglgdry tvtrisgpte gvevlltpfg arrlfgvpmr eltnlvlpvd dllpawsrta
      121 gerlaalpss aerlalaesl latrilaapp pdplvlwawe rlvasggsvs vaslarslgw
      181 shrhlvarfh dqvgltpkas arvirfdram gllreglsls dvavscgfyd qphmnrefra
      241 magatpgqir prpqvslgad las
//
LOCUS       WP_357673539             398 aa            linear   BCT 28-DEC-2024
DEFINITION  mechanosensitive ion channel family protein [Micromonospora
            chersina].
ACCESSION   WP_357673539
VERSION     WP_357673539.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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 398)
  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 398)
  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..398
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..398
                     /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=43261
     Region          117..345
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mqtylvtaaa alaaaavall lvevvhrvtr rlgrrsllmt eltdhshrsf qvtatvlavq
       61 lavrfttlya vgspgrqlvl halvlaliaa aawlvasllv vaedtalarf rvdvpnnrha
      121 rrvrtqvvll rrltiavivv lalgvmlmtf pavrgigagv ltsagvvgvv aalaaqsllg
      181 nvfaglqlaf sdavrlddvv vvegewgrie eltlsyvvvq iwddrrlilp tsyftstpfq
      241 nwtrteaavl gtaefdldwa ipvqamreel rrlcegtelw dgrvcvlqvt datgglvkvr
      301 alvsaadags lwdlrclvre qlvawvrdqr ptalprlrae vgdtagsppw qavqprrpvr
      361 rqpdtevpdd arvfggsddg earseafvgr eehadarr
//
LOCUS       WP_357673556             197 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357673556
VERSION     WP_357673556.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 197)
  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 197)
  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 197)
  AUTHORS   Rosinski,J.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..197
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..197
                     /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=21544
     Region          8..84
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          101..175
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mddasgitat laevgprlkr lrtergltli vlaeatgisk stlsrlesgq rrpslelllp
       61 iahamrvpld eligepeved prvrgvpvsr dgqtvipltr qpgglqawkt iipadhdepd
      121 lcthdgyewl yvlagrvrlv laehdlllgp geaaefdtrl phwfgstgdg pvevlnlfgp
      181 qgerihvrar prprssr
//
LOCUS       WP_357673604             266 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357673604
VERSION     WP_357673604.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..266
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=27140
     Region          5..266
                     /region_name="COG4132"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443307"
ORIGIN      
        1 mrrslgalpl lvfvglafgi paiamvagaf spgldnlalt lqggyllall nsvklsavva
       61 glgavlgtll aqavvtsrst alreavltas gvlanfggvp laffwvatlg nsgvvsgllg
      121 lpsgslfsfw glalvylyfa vplmvlviap aldglrpqwr eaaanngatt whywrhvglp
      181 vltpgllggv vllfgsafaa yatasamgag tvlplvtlki aaalsgdvqt gfenvglals
      241 ldmvlvaalv mavylplqkr sarwlq
//
LOCUS       WP_357673685             395 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea dietziae].
ACCESSION   WP_357673685
VERSION     WP_357673685.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..395
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42543
     Region          4..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 mtsladirvi daatlfagps aammlgdfga dvikiehprr gdpsrghgaa kdgvglwwks
       61 lsrnkraaav dlskpegqei lrrlvresdv lvenfrpgtl erwglapddl lalnprliva
      121 rmtgfgqfgp masrpgfgtl aeamsgfasm tgepegpptl pplaladgia glamsyavmv
      181 alharertgr gqvvdmaiie pimgllgpqm taykalgvvp rrtgnrsssn aprntyrtrd
      241 grwlavstsa qtiaervvtl vgrpdlvaqp wfssgagrve hveeldeavg swiaardaee
      301 vvarfeeaqa aiapiynvkd iaedpqyaal ntfvelpdee lgsvtvqnvl frlsetpgev
      361 rwtgrplgrd tdevlgeldy tpeqikqlre ngvia
//
LOCUS       WP_357673613             346 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora chersina].
ACCESSION   WP_357673613
VERSION     WP_357673613.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 346)
  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 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   3  (residues 1 to 346)
  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 346)
  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..346
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..346
                     /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=35888
     Region          5..321
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mracrvglvg aggvaqrhar vltgfddvel igvtdvapda aealagthga rtfrdvdell
       61 aadpdavyvc vppfahgpve eavidagvpm fvekpvavdl etaervaalv errglltgvg
      121 hhwrylhvve earqlladrp vrmvngawld kvppvawwar rdrsggpvve qaahvldlvr
      181 llvgeatevt aygdgtpppv egadidsvta atlrfasgav gtlaaacvlg wkhragleil
      241 adglalslae dglticdadg erhlpadpdg arvavdrafv davrgigddv rvpyaealrt
      301 qrlalavaes artgravalp tgpaarltaa vadatpaeat gvtvda
//
LOCUS       WP_357673686             596 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Micromonospora
            chersina].
ACCESSION   WP_357673686
VERSION     WP_357673686.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora chersina
  ORGANISM  Micromonospora chersina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 596)
  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 596)
  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..596
                     /organism="Micromonospora chersina"
                     /db_xref="taxon:47854"
     Protein         1..596
                     /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=64044
     Region          38..572
                     /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 mttssgasrr qvlavaaaaa tapliagapa eaaskpsktw dltvlgtsdt hgnvynwdyy
       61 rdaefddskh ndvgvaklat lvnqiraerk gratlvldag dtiqgtplat yyakqepite
      121 tgathpmana mnvlkydavt lgnhefnygl pllatwigql gfpalaanai nektgkpafl
      181 pyvikevalg gydsptlkvg ilgltnpgva iwdkanvegr lvfadmvata akwvpvmrer
      241 gadlviisah ggdsgtssyg pelpnenpva liaeqvpgid ailfghahne vpqkfvtnka
      301 tgaqvltsep skwgqrltrm dftvtkvkgr wqvvaksatt lntntvvedp avlaavrgqh
      361 dktvgyvnqv vaqsteelst vesrykdtpi ldfinhvqae vvskalagta yaglpvlsqa
      421 spfsrtavfp agdvrirdva glyvfdntle avvmtgaevk ayleysakyf ktwaagetid
      481 lpnindpnvp dynydvisgl eydidiakpv gqritrlvlp gtdtpvaada qfvvavnnyr
      541 rsgggnfpgi vktqvynqqq eirqllidwa qakgeirpgd ffvdnwklvr egvpvf
//
LOCUS       WP_357673703             780 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357673703
VERSION     WP_357673703.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 780)
  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..780
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..780
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=86369
     Region          <50..779
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            order(501..502,504,534,537..538,541..542,544..545,568,
                     571..572,581..582,585)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          532..562
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          567..601
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgvasrgwei rglsaeltsf vgrrceiaev krlladsrlv tlvgvggvgk trlalrvadd
       61 vrrafrdgvy lvelaalerp dllvqavtea leiadlstrp qlevladhlr drqtlvvldn
      121 cehllhdcav maetlvrsap dlrilatsrq vlgvageqtm vvpplplmdg dmsrppgkss
      181 eqsdavrlfa eragavlpgf avtddnreav vricrsldgi plaielaavr lraisveqll
      241 arledrfrll tvgskvvlpr qrtlralidw syllctaqeq llwarlsvfs gsldlegaeh
      301 vcsgdgiate eildlviglv dksilvreeh rsqvrfrlle tirqygrdrl hesgqedklr
      361 rrhrdwyqdl vlraqhdwfg pdqvtwyarl rtehgnlrta ldfclavpge aesgltiaaa
      421 lryywiaads phegmswfnr llagdgrptp arawalcvka rlavlqsdft aaatlldecg
      481 elarrfddlt itgsatyvag laallqqdls raltllskal dcgrrtddqi gvvnsliyla
      541 ttrsllgqsd qaveqfeecl aiceprhenw frsytlwtyg ievwkrgdtr ravemereal
      601 rlkepfddhl gialcieala wmscgdgdge raalllgalq eiwrsfggpl fgylaehhdt
      661 ceraargilg argfeaafrk gtglslaeal eyairkdape secqrrsspl trremeiarl
      721 vaqgmsnkai aaalviaqrt aeghvehilv klgftsrvqi aawvsrqepg ddqslsgdap
//
LOCUS       WP_357673701             693 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357673701
VERSION     WP_357673701.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 693)
  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..693
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..693
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=75876
     Region          3..693
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msrtgrrpaa gidppmevpr fvgrrrevsq arrmlshtrl ltltgvggvg ktrlaarvae
       61 tlgrtykdgv etvelatlea gdllaptvaa alglreagpd satmlvdyla dkrmllvldn
      121 cehlledcar lveqllrgaa rlrilvtsrq tlrvsgeqvl tvpslsvpdh ghqpsdiarh
      181 davrlfvdra asvwpgfsld agnaaslarl aqrlegipla ielaavrlra vpleqltrev
      241 eerfdvlarg sptglprhrt lratmdwsfd lcspaeqrlw arlsmfpgga dldtaeavca
      301 gdeidladvi dlltglvdks vlvgeqgqag vryrmlesir aygyerldps earalrgryi
      361 dhyrevvegh ridrivpdql eryrllrrel pnvraalemc lsepstaveg letatamwly
      421 wlldgslteg rywlerglel vpgavgaram alwvdsmlal rqgdlavamp rleechtmar
      481 qagnegvlpf airtsglaaf stgdaprgla lleeslalhr atgdidsvaf nlyyaavygs
      541 medparaarf geellalces hhasmsrsha qlalgiamwn lgdcrragal vseaaefaqk
      601 indrwtltqc levlawtagv rgdheraart lgaahalwqv vgttparlgy harwhercae
      661 qsrrklgera fmaafrdgar rglepgvisa lda
//
LOCUS       WP_357673749             359 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357673749
VERSION     WP_357673749.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..359
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=38700
     Region          64..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          159..341
                     /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 msdallavgt rkglflarst gggpfevepi qfstvgvhsv aidargetpr llagieyghf
       61 gpsvmysddl gkswqeaqkp piafpektga tlekvwqllp spsepgvvwa gtepgalfrs
      121 ddggitytlv eglwehphrp qwqpgggglc lhtilnhptd pkimgvaist ggfyrttdgg
      181 lsweaanqgi rapflpegqq ypefgqcvhk vslhparper lflqhhfgvy rsddfggswt
      241 digsslpsdf gfpvvvhpdr pdtlyvlplh admdrtpvgh ryqvfrsdda geswqahgeg
      301 lpqgpvyasv lrdamtasha giffgtrdgs vygsrdggdt wsevashlpd vltvraavl
//
LOCUS       WP_357673825             196 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea dietziae].
ACCESSION   WP_357673825
VERSION     WP_357673825.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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: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=21718
     Region          8..196
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mahyfeeqpq aasrpssvdl vlpdlhlrle tdrgvfsper idlgtrvlle svpappqegh
       61 lldlgcgygp ialtmasrap satvwavdvn rrsleltern akaaaldkvr pahidevpgd
      121 vrfvaiwsnp airigkqamh emltrwltrl tpdgvaylvv qkhlgsdslq rwlsdqgwqa
      181 treasraayr ilkvtr
//
LOCUS       WP_357673974             417 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Nonomuraea dietziae].
ACCESSION   WP_357673974
VERSION     WP_357673974.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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 417)
  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 417)
  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..417
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..417
                     /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=44441
     Region          12..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(22..23,26..27,30,63,113..114,116..118,121,140,
                     143..144,147,224,227..228,231..233,236,259,263,319..320,
                     324,328,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mwrrfrsfdh svqllmlnql tinigfymlm pylaghlsag lgmaawavgl vlgarnlsqq
       61 glfllggtla drlgyrpvii agcllrtagf allgfastlp lllaasvmtg lagalfnpav
      121 rayvahdage rrveafalfn vfyqagillg pliglalmav dfrlaclvaa aifalltvlq
      181 vlalppcrte ttqagaqtgv qagvladwra vvtnrpfllf tlamvgsyvl sfqvylalpl
      241 elgdtravgl lfvvsaivav tgqlritdwa rrrwtarqai argvalmals ftplmlygfv
      301 deslrvpavl actvlltlgt tltypfemdt vvalcagrmv athygfynti agagiavgnv
      361 vvghmldegt srawltltgv gmvsalavsl lrdgdkpvsr llpwarqrrt sststls
//
LOCUS       WP_357673972              97 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea dietziae].
ACCESSION   WP_357673972
VERSION     WP_357673972.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 97)
  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 97)
  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 97)
  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 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   5  (residues 1 to 97)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..97
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..97
                     /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=10772
     Region          4..79
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(8..9,11,14,17..18,21..22,25,55,74..75,77..79,81..83)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(9..10,14..16,29..31,40..43,45..46,49..50,52..53,
                     59..61,66..68)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(29,32,74)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 meaaveafrm lsdatrlrlm wllstgefdv gslataieta rpsvsqhlak lrlaglvqtr
       61 regrrvlyra rdahvralin ealfhadhev sgiprhd
//
LOCUS       WP_357673992             170 aa            linear   BCT 28-DEC-2024
DEFINITION  GntR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357673992
VERSION     WP_357673992.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 170)
  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 170)
  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 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   4  (residues 1 to 170)
  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 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..170
                     /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=18701
     Region          <1..153
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtarglearq ellrvdtita apeiaaqlgl dedaevivrr lmftvegepv qrtdgyypss
       61 mfaatpvsea lrvrggvaay iedqmgrris qfverlsmrm pvpeeiamlk lgpgvpvvhv
      121 qrlardtegv pvefldsvvv gdryifeyvi dvdasedgav ptelrprnti
//
LOCUS       WP_357674004             369 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357674004
VERSION     WP_357674004.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 369)
  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 369)
  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 369)
  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 369)
  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 369)
  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..369
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..369
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40579
     Region          76..219
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mlrapaetky aeeldylesi dqghkpfswr lsprmvrifv lgsersdgld reipqkwfgd
       61 rsfversivt lasdrgllli gdpgtgkswl aellaaaicr nstmvvqgta gttedhikys
      121 wnvsmviakg qsresmipsp imtamekgvi grfeeltrst sdvqdalisi lsekyvsipe
      181 lgegednivf aqpgfsiiat ansrdrgvnd lssalkrrfn fvripvvtnk kseaeivrfr
      241 ttellrrhqi dldvpptlld illqsfadlr agaasatsdd qklesalsta eqigvledai
      301 lhsqffgdst lraatlassl vgslarrtpe dlailnkywh gvveprskkd ggewpefleg
      361 grqaiatls
//
LOCUS       WP_357674017             231 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357674017
VERSION     WP_357674017.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   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 231)
  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..231
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..231
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=24482
     Region          3..231
                     /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 mdviliagfw lnasswdgvv paleatghrv haltlpglas vdddrtgigl adhvaavvkv
       61 iddidgsvvl vghsgggaia haavdarpdr varvvyvdsv plgdgdvind elpvvdgeip
      121 lpdwsvfgae dltdlddelr erfratsipq pvgvatdkqv lrdprrydvp itvitceypa
      181 etvreltang hpytaelakv rdvkivdlpt ghwpqftkpa elgaaiveal a
//
LOCUS       WP_357674034             315 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Nonomuraea dietziae].
ACCESSION   WP_357674034
VERSION     WP_357674034.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 315)
  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..315
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..315
                     /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=32797
     Region          1..>78
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtgdthydle ilaelaegll daataeqvre hlavcdpcge lladlaavre vlaatptpam
       61 pmgvamridq alareaargg ldlldgpdwe eltrqtpepv rlgtaaddgd lvpayssgra
      121 asghgysghg asghsgsgrr pgarrpagqr ppaqrspgrr rwgmplvaaa aaavvvgtag
      181 istgllaggs dpspgrslla qpqpsvsqpa lsymvtdtdy nwssqdlkqp lstflgaapg
      241 skdaggvdpk vsacvervaa rsnlrpftvd qsefngqeal iiaswkdqaa lrvrvdvvdp
      301 fkcknivkpt lgrwk
//
LOCUS       WP_357674094             338 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357674094
VERSION     WP_357674094.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..338
                     /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=37282
     Region          1..329
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 msetllsvqd lrmhfpihkg llrrqvgavk avdgidfevl kgetlglvge sgcgksttgr
       61 lvtrlleptg gkivfegkdi thmpqgrlrp lrrdmqmifq dpysslnprh tvgaivgapf
      121 riqgikteqg tkkavqdile lvglnpehyn ryphefsggq rqrigiartl alkpkliiad
      181 epvsaldvsi qaqvvnlled lqneldltyv viahdlsvvr hisdrvavmy lgkiveiadr
      241 kslytspmhp ytnallsavp vpdpkaraer erirlqgdvp spinpppacr fhtrcwkaqe
      301 vcrtvepple qlasghrvac hfpenaptvt papetita
//
LOCUS       WP_357674176             170 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Nonomuraea dietziae].
ACCESSION   WP_357674176
VERSION     WP_357674176.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 170)
  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 170)
  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..170
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..170
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17419
     Region          48..156
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 msyltaavvl igllcvfnll ltlglirrlk hvggasaghv gppialrpgs pvgefaavtl
       61 dgeqvshetv eglvgffsag cepchklipg ftaqaralgr envlavvage daeavealsp
      121 varvivedfe gpvagafqnt wtpalyllgs nhrivaaggr medlplasta
//
LOCUS       WP_357674141             419 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nonomuraea
            dietziae].
ACCESSION   WP_357674141
VERSION     WP_357674141.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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 419)
  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..419
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..419
                     /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=45136
     Region          22..414
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mggpqaplps sddrrpggpm taaellqqlt dqlrrresae tlsvqlahaq rlgnmgwaqw
       61 nlrtgeavws dhvyvifgrd paagpvglse ladhvepadl stldqllwav gegvepvhae
      121 frirrggevr nlrvvleplv gagettgvhg vvqditgrrr aerimsesrr qlieareraa
      181 eernvmialr eailpepvgc ldlprtrvav ryvpaekaan lggdwfeaag lpdgrvllai
      241 gdvsghglpa iahmaqlrha ligltmtgqa adqllswlne lvmhrlhdtt atalighldt
      301 ttnvftwgqa ghlapilvrd gtakqldspr gvllgavceq pyelasielr pddllllftd
      361 glverrtrdl deglalalsa arelpvydld agldqlvasi ggpnpeddac llavgildl
//
LOCUS       WP_357674211             448 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nonomuraea dietziae].
ACCESSION   WP_357674211
VERSION     WP_357674211.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..448
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..448
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47250
     Region          23..448
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mthvidpkha evpltldeap pktlgvldqg afwanlgvsl lgfsfalfli npllddnpls
       61 mtaavtatvv gslvgtamvg laaipgaqtg qpamvllrgl fgaklsyvpt vlniiqmlgw
      121 gafelwvism gaqaifgdav pyavwvliag aittgltiyp lgairlirrv vtigviistv
      181 wfavvflrsa papaggswda fapavdfvia lsvswvpvaa dyarhsrssr aaftgvvggy
      241 tiaqvaclai gvyavaiagh davlndpttv fgpfvaaplg alffgilvlr etdqsfanvy
      301 stamslqnlm prvdrrvfsv aigvltigva llvdvnsysa flsiigavfv pmlgvlvvdy
      361 fllgrattwd tsehapsrwp mvapwalgfv twwllaapsq igwwaaiwdg artalgftrq
      421 pwmsaalgaf lvaglvtlai glvrrsrr
//
LOCUS       WP_357673941             290 aa            linear   BCT 28-DEC-2024
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Nonomuraea dietziae].
ACCESSION   WP_357673941
VERSION     WP_357673941.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..290
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=32208
     Region          <212..255
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mktlsreirk tveqtkaahk ivkdarrkha kavqlrnlga lvlvmrhdrk iqptmrlaai
       61 grdawqamlt dasipstlpq wspehavkvi ekavadiaai gveeqqaren rvrgvlalsq
      121 atvdgekltn vdvgeltelg kvmvgkdlkh aeewgftepg agntsesagm vpvavmaerl
      181 gvshkrvldr meyarenslg vprtstaasr vllvdeeefa awwvqhrfhw laakdlaerw
      241 gvpyeavker lrtakakgtd pvstnfgrri fyepasvdew gtqygyaprs
//
LOCUS       WP_357674234             238 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea dietziae].
ACCESSION   WP_357674234
VERSION     WP_357674234.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..238
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25231
     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 mtdtavivpa kdeaerigat vtaalqlpgv dlvvvvddgs tdqtgrvara agarvvrhsr
       61 nrgkasames gaeavrllda avprnllfld adlgetaraa aalvepvrag eadmtiavfa
      121 trvklgghgv vvrlsrdgik rasgfsatqp lngqrcltre afeaarplah gfgvetglti
      181 dlvrkgfrvv evevemahra tgtdwhaqlh rarqlrdvar alatrepvir dnlaklrs
//
LOCUS       WP_357674315             329 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357674315
VERSION     WP_357674315.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 329)
  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 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   3  (residues 1 to 329)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..329
                     /product="GlxA 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=35986
     Region          4..315
                     /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 mrrhvvavav tsgmptfela vpcevfgldr sdivdpwyel rlcaagpgpl ltsgglqiht
       61 phtlddliea dtvvvpacar avqtspppsl veavrkahel grrivslctg ayilaaagvl
      121 agrpatthwm nagdfthrfp evrfepavly tddgnvltsa gtgaavdlcl hllrrdhgaa
      181 vanevarrmv vqphreggqa qhapllvqpe nsddlapvlq wardhldepl tvsqfartan
      241 lsertlarrf hdklgttplr wllqqrvrla qelletsdep veriarrtgf rtaanlrhhf
      301 grvtgmtpqt yrhvfraraq raaealpgt
//
LOCUS       WP_357674377             197 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea dietziae].
ACCESSION   WP_357674377
VERSION     WP_357674377.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  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..197
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..197
                     /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=20954
     Region          2..150
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mirvaviigs trpgrngeav arwvhdlavr rgdaefeivd lkevglphld eamppsmgvy
       61 ehphtrawae tiasfdayvf vtpeynhsis galknaidfl yaewndkaaa fvsygsaggv
      121 ravehlrlim gelgvadvra qvslslaadf enfsvlrpaa greagvtaml dqlvawagam
      181 kalraagdya aasvgds
//
LOCUS       WP_357674417             266 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357674417
VERSION     WP_357674417.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   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 266)
  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..266
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..266
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28508
     Region          4..266
                     /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 mdgtrrevva gdgvrlvcwd gggpgraivl lhglagasge wravadrlgp awriivvdqr
       61 ghgdserrpg dvsraayvad vvevigalgl gpvvlvgqsl ggnaallvaa ahpalvrglv
      121 lieagperpd pggprkigew ldswpvpfpd reraadflgg gsvgrgwase leeteeglwp
      181 rfdrevmvas laaacrrsyw tewqqircpa lvvlgekgii glqesdrmrr lrpdlpivvi
      241 dgaghdlhle dpqalyeqma gflrhl
//
LOCUS       WP_357674420             270 aa            linear   BCT 28-DEC-2024
DEFINITION  segregation and condensation protein A [Nonomuraea dietziae].
ACCESSION   WP_357674420
VERSION     WP_357674420.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=29988
     Region          8..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 mtsteqqgfq vhldvfegpf dlllgliskh klditevsls qvtdefiayi ksrgpewdld
       61 qtshfllvaa tlldlkaarl lptgevedee dlalleardl lfarllqyra ykevtkvfsg
      121 lmaeealrfp rsvpmeaqfa nllpelvlgi gpdqlariaa kaftpklppt vsvghiyqpl
      181 asvreqaail vqrlrrmrra tfrtlvadce gtfeviarfl avlelfresa vtfeqveplg
      241 dlhvtwtgad dgdvsvgddy eesaekaade
//
LOCUS       WP_357674432             133 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357674432
VERSION     WP_357674432.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 133)
  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 133)
  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 133)
  AUTHORS   ter Beek,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..133
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..133
                     /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=14204
     Region          16..>96
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mailtearpr aarrakgirn rdgwwaaffl gpqltllavf llfplgfavv lafmrwdglg
       61 qkewvgldnf aaqlsdpefg aavwntvkla lltapfglal alliavalns vkgggstacc
      121 tscrwspars psr
//
LOCUS       WP_357674469             608 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357674469
VERSION     WP_357674469.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 608)
  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 608)
  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 608)
  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 608)
  AUTHORS   ter Beek,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 608)
  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 608)
  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..608
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..608
                     /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=65924
     Region          84..601
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mavltkvepp pppqkrrrll yrlrvlrhdp taalglilvv vlaylvvapl vavlsdafrl
       61 qygdevhagq qpgewtgyyl wrvfrsqvse llfwepllnt lvislgtvlf alvvgggmaw
      121 mvtrtnvpgr kwlagalvvp ymlpswtfsl awltlfkndr aggqvgvlqa qgiatpdwla
      181 ygplpiivtl glhyypfvfl lvgnalrrid aqledsaril gaprrvvirr ivaplmlpal
      241 ssavllvvgr vlgtfgtpyv lglpadyrvl stglyqsird rstgvasvlt avivivgvli
      301 vftdarllre hrrfvtvggk gamdrlsdlr rwrwpafalg gvifvlsvlv pvltlllssl
      361 trtpmdlstf tlsywfaesl pgavgfphgv frgtelwtaa wnslrivgva svicavagll
      421 igyvvvrgsa priagflrqv sflpylipgi afaaaslslf avargpvpal ygttfllilv
      481 mavthlpyss rsgiaamtql grepeeaaqi agaswwqrmr riifpiqkga lvtgivlpfi
      541 sglkelsivv mltttgtell ttlsiglvdy gytqlanavv lvialvsftm tyltqrltks
      601 slasglga
//
LOCUS       WP_357674561             298 aa            linear   BCT 28-DEC-2024
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Nonomuraea dietziae].
ACCESSION   WP_357674561
VERSION     WP_357674561.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 298)
  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 298)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 298)
  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 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..298
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32328
     Region          29..132
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
     Region          171..278
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mpsdpltadh vlefpggytr ttgpvigrfl telrdgrlmg vrtaegrtlv paleydpatg
       61 epvtdewvev gpagtvtasa wvhepreshp ldrpfawali rldgadtall havdagnpka
      121 lppgtrvrpv wraerrghit disyfapevt kivspvstry rltaspsltr flegvrdgvl
      181 igcrcatcek vyvpyrlscp ecgnpiagev alpdtgtvtt fainnlpdpr apevpfvsay
      241 illdgadipl ialvggvpah qvrqgmrvra ewvppeertl smtnirwftp tgepdvel
//
LOCUS       WP_357674573             358 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Nonomuraea dietziae].
ACCESSION   WP_357674573
VERSION     WP_357674573.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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 358)
  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 358)
  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..358
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..358
                     /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=34483
     Region          76..358
                     /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 mrmivasaaa aallisgcsg sisratppas tpapspaspa ssapasassp haleaeyerv
       61 iqevlpsivq intkvglgsg ivydsaghiv tnahvvgeat emevtlatgg tarparlvas
      121 fpagdlavik vsdpnglapa rfgdsaklrv gqivlamgnp lglsgsvtng ivsalgrtvs
      181 epqdggapga tianaiqtsa ainpgnsgga lvdlsgqvig iptlaatdpq lgggaapgig
      241 faipsntatd iaaqivkdgk vtnsrraalg iagrtvigpe gtpvgvgvvs vtrgggaala
      301 giaagdvivs vngtdtptms alseilasqk pggqakvevv kpdgstgtvt vtlgelda
//
LOCUS       WP_357674577             933 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357674577
VERSION     WP_357674577.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 933)
  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 933)
  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 933)
  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 933)
  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..933
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..933
                     /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=99564
     Region          4..242
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          121..919
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msarfgvlgp lrvldgggae vtpgpakhra llvallmsag qtvthdrlvt avwgaeppas
       61 aeavlrvyvs alrktvegir tvpggyllav dpeevdalrf ermvaharra raagraieav
      121 dalaqalglw rgraldgieg elrrahavpl eelrlaalee rveldlelgr gaeligelra
      181 lvaayplrer awaqlmhalt qagrrsdala ayqeargtlv aelglepgpe lreahervla
      241 eelgrsvpne tppdiadftg rqavldwies alpapgaapv hlvlygpaga gksalavhaa
      301 arldlpdgrl haslrdrapg avledllrsl gcpdgavpss ldervrlyrs lvagrrllvv
      361 lddatseaqv rpllptgagc ltlvtsrspl fgleaarayp ldvleageav amlariigad
      421 rvaaepdqah rivrlcgalp lalriagsrl arrrgwtleh ladrlgderg rldelsagdl
      481 avrsslalgy ralsgderll lrrlgalssp dfapwiaval vgrdggrgme slaeggllqe
      541 rgldrygwhd ltrlyaaerl aeeegpasav lagaageild rarrarelml paepgsgltl
      601 shtverdlat arlaesarwl aaersfmvaa vgdlhrarld eaawrlafyl tplfelgayh
      661 ddwrttaalg lesarraghr hgealllrsl adlhraegrl eeaaealraa lpltergeva
      721 rttlrlglvy raqdrlsdae rcfteclaaf gsgqgggadp rgsadalral gelradeels
      781 rraldlyrql gdprgeaatl ldlaalclag rrtkearela eraaglsrrl gdrlpaasas
      841 lllagtarae grpeaaraaa tealaafesh gdrrgtarak laiaaaaldl deidgavdal
      901 acimgefdal gdrrglveaq elarearrrr glr
//
LOCUS       WP_357674611             220 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357674611
VERSION     WP_357674611.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..220
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23579
     Region          15..214
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mgvddepgvd dergrvrava lfdldgtlid terrnrviwq mlldnhqldh dvaifmgrrg
       61 rdvlpeifpd hdveqliaev fsyddhpglp dvapvpgaae lvrkvaaygs riglvtsarr
      121 ewaetrldqv gvrslfevlv taedveigkp dpagfllaaa rlgvdpddcv vfedsvagis
      181 aakaagmkcv avatthaged ladadlvvad ltavgwppfs
//
LOCUS       WP_357674606             206 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357674606
VERSION     WP_357674606.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..206
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22699
     Region          2..198
                     /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..12,115..116,144,168..169,172..173)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            139
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mvkgvlidwg gvlttsmsea vatwiesdrl dgdhyrtvmr ellrqesavh alergeitav
       61 eferelaarl rtvdgtppla dglltrmflg fqrvdamydm llkartagik tcllsnswan
      121 eyprdgwdei fdavvisgei gmrkpeprif qhalgliglt gpecvfiddi evniaaarsl
      181 gitgihhidp dttiaeletl lglplr
//
LOCUS       WP_357674617             371 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357674617
VERSION     WP_357674617.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=39304
     Region          38..362
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtsrqlarrs lqtrlalaya agiyaagvmv lvfvdvplat ihaatpagha ssseiaetgp
       61 gislpqlltg savalvilip valalgwyva grflhplrai tatarvisag nlhqrlglge
      121 ptdeltelgh tlddlltrlq tsfdaqrhfv anashelrtp laglrtllev aladpdadtd
      181 tlrsacqeal algghqerlv qallalatse rgvtrwdhld lahvvegvlv srrdqaaerg
      241 idlaehlkpa vtagdprlie slvanlidna irhndehghv qittqtsgtq valtvtnsgp
      301 avphnqiqrl fqpfqklapd rhgrhdgygl glaivnavtq ahhatlttsa rpegglsvtv
      361 rfghgshpnp p
//
LOCUS       WP_357674748             383 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357674748
VERSION     WP_357674748.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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 383)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..383
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..383
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41605
     Region          26..369
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrktstalla taalliapav ahadpapkat felpaptgph slgvrevhlt dqergrelmi
       61 svwypamrgs eprapymrpk taayfdgaaa amglkpgqvd waavsthart garpkgrwpv
      121 vlyspgwgsl rtlgtstved laskgyvvvt vdhtheapmv efpggrleta kpaqgddylr
      181 agmetrrqdv rfvldrlssl dglgramdls rvgmfghsfg gdtaaevmat drrvdagadl
      241 dgwlaydvdg nqptraatdg tarpfllmgs sgstgdgrpr shltspawks fwehssgfkr
      301 dllmpeamhy sftdlqaflp qldeqlevvp evrakrigtv dpgrsvasqr aylsaffdqt
      361 lkhrpqrllr gesaehpdvt fvr
//
LOCUS       WP_357674786             241 aa            linear   BCT 28-DEC-2024
DEFINITION  MIP/aquaporin family protein [Micromonospora rifamycinica].
ACCESSION   WP_357674786
VERSION     WP_357674786.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..241
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24122
     Region          5..221
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mdaarryaae llgtlllvfv gvgsavfarv qggvvvvala fgfvlvalvy aigplsgahl
       61 npavtlgvll sgkitvvgav ayavaqfvga aaggfviwal vrwggvadqt galgtngygv
      121 hingggtavl etiltflfvl vvlvvtsrve hagfaglaig lalaavllvg itldgtsvnp
      181 arsfgpalfe ggtalrqlwv fvvfpllgga laalvaplvl rqsprlrrgp eapdpaapqp
      241 g
//
LOCUS       WP_357674818             186 aa            linear   BCT 28-DEC-2024
DEFINITION  SOUL family heme-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357674818
VERSION     WP_357674818.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10521978
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..186
                     /product="SOUL family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=20527
     Region          2..183
                     /region_name="SOUL"
                     /note="SOUL heme-binding protein; pfam04832"
                     /db_xref="CDD:461449"
ORIGIN      
        1 mteqqpyrvl grhpgfelrr ypahlvvelr idggfaaagn aafrplaayl sganrsrrrg
       61 gtagpvmrev gservamtvp vvqeegdrpg nwrvwfvlpa rltpatvpep adpritvrei
      121 peqlaaavrf agrwtdrafe qratalgrav adagltpsga iryarfdppw kpwflrhnev
      181 vlpvve
//
LOCUS       WP_357674848             334 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Micromonospora rifamycinica].
ACCESSION   WP_357674848
VERSION     WP_357674848.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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..334
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..334
                     /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=35390
     Region          96..332
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mtskpifgrr grvgvagava alvtatlagv aqqpataapg tvatyvvagt aaerqavlay
       61 wtpqriadlk tpsaqvppva kpdgapwtra gavsrtvgrl fftdhgedas ctatvldsan
      121 rstvvtaahc vnntdliged nrwsanvlfv pgyrdgrapy grfvgrlsva pstwllndqi
      181 eslydsydqa fvvlhpnsdg rrvqdavgaa qrigydvpga rvvhqfgypr assdearegl
      241 peytgerlay cagraveqqp tedwpeppgq wgtecvmggg ssggprfahf drhtglgtvv
      301 gdnshgyvpg krylvgpqfs tavtrplfqr aqhg
//
LOCUS       WP_357674862             271 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357674862
VERSION     WP_357674862.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  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 271)
  AUTHORS   Rosinski,J.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..271
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..271
                     /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=30312
     Region          4..>66
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          93..266
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mkveqpsrvg vllrewrqrr rlsqldlanl aetsarhlsy vetgraqpsr amvlrlseal
       61 diplrerntl llaadyapay resgldeeym ssirvaidtm ltahepypav lvdrlwnvla
      121 gnramavlmd gipphllepr pnvfrlalhp dglasrlanl devrtlflqr llrqvnatgd
      181 ealrslyeev rrypapmsge rdetgegehg pspiqvplri rtpygelsmf stmatfgapa
      241 dvtlselaie lfypldefst kalhalgers s
//
LOCUS       WP_357674884              94 aa            linear   BCT 28-DEC-2024
DEFINITION  putative quinol monooxygenase [Micromonospora rifamycinica].
ACCESSION   WP_357674884
VERSION     WP_357674884.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 94)
  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..94
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..94
                     /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=10166
     Region          2..87
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mfivagslyv dpaerdtyla scvevirqar sapgcvdfai gadlvepgri nvyerwesdd
       61 ellafrgsgp ereqvaairg aevhryrisa vaap
//
LOCUS       WP_357674909             354 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357674909
VERSION     WP_357674909.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 354)
  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 354)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 354)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..354
                     /product="GlxA 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=37563
     Region          6..325
                     /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 mtlvphrigv laldgvvgld lgtpaqvfga ardadrrply tvdtctpggr pvrssagfrv
       61 lpdhgldlla tvdtvvlpgl hgsapmtdgt idpavtaalr aayqrgarim sictgafala
      121 aaglldglpa tthwayadrf rrlhptvdld pdvlfidagr vltsagvaag idlclhvvrs
      181 dhgsavanga arrcvvppwr dggqaqyier pvprtpasgt satrqwarqr lhepvtlrel
      241 aaharmsvrt ftrhfrsetg lspaqwllqq rtdharllle ttdlsveqva rragfgttaa
      301 lrqrlhtrig vspsayrrtf rragsgtrpd gpppapapgp apssgglrlv aehp
//
LOCUS       WP_357674933             127 aa            linear   BCT 28-DEC-2024
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Nonomuraea dietziae].
ACCESSION   WP_357674933
VERSION     WP_357674933.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 127)
  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 127)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 127)
  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 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..127
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13934
     Region          5..110
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mipgwfdgth llgtrctscq avsfpphhgf crdprcegee lveerlsrrg tvwsytnacy
       61 pppapfvaae pyvpvtlaav elererivvl gqvkglaved lrvgmelelt egtladgpsv
      121 wmwgppr
//
LOCUS       WP_357674960             679 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea dietziae].
ACCESSION   WP_357674960
VERSION     WP_357674960.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 679)
  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 679)
  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 679)
  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..679
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..679
                     /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=73683
     Region          13..679
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpghqlapdi ptdvlaaera hlaesraalr amrkhaqsls sdaagdwvsq qilqslldqr
       61 vaaladhpdt plffgrldra teedleanle grlkagdelp atiyvgrrhv hdggsralvi
      121 dwrapvsraf yqaspsdpmg vvrrrrfgyq ggdltafede plaeggelgp skilteeier
      181 prtgpmrdiv atiqpdqdei vrsaltqtvc vqgapgtgkt avglhraayl lfthreklar
      241 agvmivgpnk aflsyissvl palgevkvdq ttvaellgsy daperpevaa akgdarmakv
      301 leralwlhiv kpteglvytk gvhrfrvady evremvaslr gttrygpgra alaqrlahqv
      361 lvrmeqrgds pddrvqdava rskpvkqlve svwpkltpaq vlhrllsdpd flaaaarsdl
      421 sqeeqellvw skpqrswksa rwsaadaall deladliert pslghlvvde aqdlsemqlr
      481 algrrcrngs atvlgdlaqg ttpwstrswk svlqhlgqea gevteltlgf rvprevldya
      541 aqllpsiapd laaprslrpg lgslsvrqdg qvleavreal aregsigviv pdslvetvse
      601 elaglphavl gpdsteehrl lvipatlakg leydhvivve padivaaepr glarlyvvlt
      661 ravssltvlh akplpaqla
//
LOCUS       WP_357674968             486 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357674968
VERSION     WP_357674968.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..486
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=52709
     Region          6..486
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mteqtlgrla eeswnrfddh eavfyegewh rshtlaqrar rvtgglieag vgpgdrvvvm
       61 matspdvgvv yqavwaagav vipvvflvga delrhilsds gatavvtspe lletvqaage
      121 girvfvdtee leqaehgplp rdpsdlaavm ytggttgrak gvmlshgglw qvakdafdla
      181 yqpgvtraiv pvplshaygl ivtiagmhap epqqavlmrw fdpkaflsla aeqrvqygtv
      241 vpsmlqmlla epledtplpd lrhltcgaap lgrdvlrefe rrmpgvqile gygltetsav
      301 ttfnppgrrr pgsvglplpg ytitirddeg eeveagdige icvagrslml gywggldspi
      361 vdgelrtgdi gcmdddgyvy vvdrkkdlii rggfnvfprd vedalnahpd vvmsgvvgrp
      421 dplhgeevva fvqlrpggea seeelvawar ervgrvkypr eihftdhipv tsvlkldrka
      481 lrarll
//
LOCUS       WP_357674984             320 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora rifamycinica].
ACCESSION   WP_357674984
VERSION     WP_357674984.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  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 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   3  (residues 1 to 320)
  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 320)
  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..320
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..320
                     /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=33589
     Region          1..243
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrvgvvgcgr hatsvllpal vqlgfdvaav carrlssaqa aaarfgaraa yadpaamlrr
       61 egveavvacl ppqvygevir acvearvpvf aekpgaggsa eagrlaalsa eagvpvmvgy
      121 mkrfapayrr artaladpsf gapslatftf vmgdmgvgld dylvdnpvhh ldlarfllge
      181 lhdlhvtrgr sdggrhalsv aaraesgavv slqlgttgsw qqhnesvevf gsgssvlvdn
      241 vdtcvlrppe gpeqrwrpny sipdqvnttv dtmgfgpalr hfhdvvrgta scesdlrsaa
      301 rtlalvdvis erlgpdrpvg
//
LOCUS       WP_357674986             267 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357674986
VERSION     WP_357674986.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 267)
  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 267)
  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..267
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..267
                     /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=28483
     Region          1..264
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqvscstigf galpiedalg riaaigftev eigvlgdfcp hldplapiae tvarstalfd
       61 rcglrpvaln sapriygddp adpdqllrva drllelaagl rcelildvge redtdaglrr
      121 aaavageafr rgrdrygvtv sveaphrgmn aqtvpealrl leiagedalg itydtshatc
      181 ggvpaaeglr ligdritriq ardhrggdvh htpgdgeydw palarflvan prpvclelef
      241 dgrltadqva aesgrgrefl hrlvpsp
//
LOCUS       WP_357674992             342 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 9 protein [Micromonospora rifamycinica].
ACCESSION   WP_357674992
VERSION     WP_357674992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 342)
  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 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..342
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37123
     Region          32..333
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mrlphtpgla krsfqhlryr tgmirsvhaf rrepveritl vvpdslgdia insaitrair
       61 lrgvpaeitl ltdrkyesav afnrdydava lldgytdkpp waltyqdqla aakaltpmmd
      121 alvlcqpgaw cdalwsryhs ldiqyrlsgt ppalrrlprl tvpagaaeav rplrqravgr
      181 tafiapgaft lkfgaagerf ftelaarlvg agwqvfwnga eapspaggpp ggagsvvavg
      241 hlplaevval asgcervvca rsgladvitf ctpelpqyvl yprtrypysr rpvrecyslr
      301 amggvnvces ensldteadl saelaavgqw lesprkhtes tp
//
LOCUS       WP_357675061             384 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357675061
VERSION     WP_357675061.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 384)
  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..384
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=41194
     Region          <191..384
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfgkirawsq rhpqlvdslw laplvglcvm taisytslgr apiglagyla lstallvplf
       61 wrgshprvvf aivsltsffq wlasvdafpa naavlvalys vvtrcasrwa laaglvselg
      121 iflalmqwgt vslstffgct vfvvtiwltg lyantrhryl egleeraera ererdhqarm
      181 aaaaeraria relhdvvahn vsviivqadg agyaidsdpe qarravqais ktgrealaem
      241 rrmvgvlred gpggadytpq pglaqleelv rgsglpvdlr vtgapqelpe geqlavyrlv
      301 qealtntlkh ggpgaralve meygmhelvv rvtddgrgaa appspdghgl lgmrervsmy
      361 ggavqaaprp gggfevlarl pvaa
//
LOCUS       WP_357675064             329 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora rifamycinica].
ACCESSION   WP_357675064
VERSION     WP_357675064.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=34993
     Region          22..316
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtrpattvep tagpddarta lhrlraevak avvgqdavvt glviallcrg hvllegvpgv
       61 aktllirtva aaldldskrv qftpdlmpgd vtgslifdpr taaftfregp vftnlllade
      121 inrtppktqs allevmeerq vsvegarrpl pdpfivaatq npveyegtyp lpeaqldrfl
      181 lkltvplpnr deelgvlrah hagfdprdlg aagvrpvaga adlaaareav grvhvaesvl
      241 gyivdlcrat rvtpalelga sprgatgllg takawawlag rdhvtpddvk atarptlrhr
      301 lrlrpevele gvgvdavldt vlatvptpr
//
LOCUS       WP_357675065             815 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357675065
VERSION     WP_357675065.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 815)
  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 815)
  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 815)
  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 815)
  AUTHORS   ter Beek,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 815)
  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 815)
  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..815
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..815
                     /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=83884
     Region          3..815
                     /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 mirttlaglk ahklrlllts vaitlgvgfi agtfvltdti qagflqkvta dagrvavavl
       61 psqggqlpeq vlekvrgidg vtgaqglvrg sapllgadgk avgdlptsai svsdrttite
      121 gvapsgdaea ivdtntaraq nfkvgdtvav ldqkgakhdf rlvglfdvgl dqelgytgav
      181 gfttataqlm tgekgyreid vtgadpaalk qaiaaalggg yelktgtela aalsksngve
      241 lefitlglli fgliammvaa lviyntfnil vaqrtkemal lrcigatrgq vfgsillesv
      301 vvgllssvlg latgyglgag amallrafda plptgmaatl aprtiaiglv vglvvtvgaa
      361 llparsatav apiaalraqv eeqtfraglv rvllagllll agvgattmav mmepgsqapl
      421 fiamagcslv flavlvlgpv lvkplsalvg wipgrrfgvp grlavdnsgr nprraattti
      481 altigvtlmt lisvitastr vsmaakldsq fpadylitaq ardasiprsi geglrgrpel
      541 dsviqlrets amlgrnetmv gtfagpaaik slgpgevais gslakewglr egspvelrtk
      601 ragtvtlkvs qlldsesllp evtvtarsyd eyfgrtpdst vyvkikdgvd pdrtrkmvea
      661 ataahptlqv isstdvrgqy ddaldmtlmi vtgllglail isllgiantl slsvhertre
      721 sallralglt raqlrrmlsv ealvlgliga lvgitlgiaf gwaavrtmmd gatlivpfaq
      781 ialfvvlsgl agvvaavlpa rkaarasivg slaag
//
LOCUS       WP_357675136             359 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357675136
VERSION     WP_357675136.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 359)
  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 359)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 359)
  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..359
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..359
                     /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=38629
     Region          127..358
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msdrrteyer lrratmwsva ggallpwvgl fwtatapdpp ppwqlvvaaa asavftvvyw
       61 raaritvtgv harteviitg llallvfimt repefagamt alawgalagl hvsrftavmm
      121 iviataacaa fqphavvfya vtismvvwln rfqfwfwtvv kaslegrdaq aklavteerl
      181 rfsrdlhdvv ghslsaiavk selaarlasg paaeemmevr rlareslkei rsvvrgyrtv
      241 dlnaelrsvr avmeaagisc alelpetalg devstllawl vresstnvlr hsaatrcrik
      301 vastggwvel tvsndhpkpp agtagsglag mservaahgg altagqsdgq ftvraripa
//
LOCUS       WP_357675209             333 aa            linear   BCT 28-DEC-2024
DEFINITION  YeiH family protein [Nonomuraea dietziae].
ACCESSION   WP_357675209
VERSION     WP_357675209.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..333
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..333
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32756
     Region          6..332
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 mpltasappv agrllpglal taaavavalv vnrlvpmlsp avvavalgaa lantagigas
       61 vapgvrfasr tvlrtaivll glqialpdvl algwqpiavi alatgltfti tpligrrlgl
      121 spgtsllvat gvsicgaaav agmheatgge ggvsddddaa galsvvvlyg talivllpli
      181 aswlglsarq lgvwtgasvh evaqvaaiga atggavlava vtvklarvvl lapivalttl
      241 rtglsrrrst plvplfvlgf llmvavrstg lvphavtdma prisglllaa alfglgtgid
      301 arkllrggra lllgaistal isaislalva llv
//
LOCUS       WP_357675219             317 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            rifamycinica].
ACCESSION   WP_357675219
VERSION     WP_357675219.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..317
                     /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=34862
     Region          45..305
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mtepsgpgpg gvrrtgrrpr pgrrralavf ltpslllfll lvlapilvas yaslykwngf
       61 glpenfigld nytrafgdpv frgdlwhgli livlslvvql pvamglamll nqplrgrafy
      121 rviffapyvl sevttavlfn lvfspnrgfg daisrflgad agavfadpdt vlyavflvvs
      181 wkyfglymil flaarqnipk elneaavtdg asawqafrlv tlpllgptir isvflsvigt
      241 iqlfdmvwvl tgggpihase tmavtmfqyg frrfevgyas aisiimflls lvfalvyqri
      301 vlrrdtegal tvqgdqr
//
LOCUS       WP_357675296             478 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nonomuraea dietziae].
ACCESSION   WP_357675296
VERSION     WP_357675296.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 478)
  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   2  (residues 1 to 478)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..478
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49869
     Region          3..457
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mrnavvktgq glvqgfdqdg iisfrgipya aapeaalrfr ppapptrwdg vrdatafgaa
       61 ppqlppapgv ppiwrpgdgl dcltlnvwsp dlggaglpvm vwlhggtwkv gassmphydg
      121 vtlarsgvvm vtanyrvgfe gfghlpgipd nrglrdqiaa lrwvqdnasa fggdpgnvtv
      181 fgqsagaasi ayllaapaad rlfqqaiaqs vpaghrdrde agritatlaa aagvpatweg
      241 laglppeail avqdtpltgp eaggsafgpv idgelvtgpp wagsgararh vnlicgfthe
      301 eyrglapggp pqgvdpavva aslglgpdaa tayrqadpdg tdaglftvmm sdalvrmptt
      361 wvaeahakag grtwlydfaw qspaigaghg vdvpftfgng dsryaarllg spppaefaal
      421 sgqireawts faatgdpgwp pfdldhrrtr iwdatprddv ypltdsyriw rqsahspr
//
LOCUS       WP_357675297             186 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine hydrolase family protein [Nonomuraea dietziae].
ACCESSION   WP_357675297
VERSION     WP_357675297.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..186
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19936
     Region          5..177
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mtttalivgd lqagivdnyp faagvlpvme rvlpaaraag ipvifirfgl rasgrdvaag
       61 nqlisalhgv gtlfheespe tlvhpriepl preavvlkrr asafagtdld lllraqrids
      121 ivltgvatga mvaatlydaf drdyrltvls dacadeepdv hdflinrvfp argaevltsh
      181 ewiarl
//
LOCUS       WP_357675338             257 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357675338
VERSION     WP_357675338.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   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 257)
  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..257
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..257
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27054
     Region          1..257
                     /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 mhsaqvlpdg srirwveipg veptlvfvhg lgassapyfa paaahpalag rrslmidmlg
       61 fgisdrptdh aytleehada laaaleqaav gaadvvahsm ggavaitlaa rhphlvgrlv
      121 ladanldptp lpqtkrpgss giavyrteqe fldhgwketm dfvgpqwaat mrlagpealy
      181 rsamnllrgt vptmrenlek lpisrtflyp aadgpradte sltaagvcvm aipdcghnim
      241 ldnldgfaha vadalsa
//
LOCUS       WP_357675328             381 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea dietziae].
ACCESSION   WP_357675328
VERSION     WP_357675328.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 381)
  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 381)
  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 381)
  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 381)
  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..381
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..381
                     /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=41459
     Region          57..380
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msirlrfgla cggvflliga lvlaglylvv rqtleprtgl mtpefintqn gffgkgsrgy
       61 eitaeraavv rrvyqsdala nvrtygaliv lggaaaavgl gygaagwglr plravtrtar
      121 rvaqghdltg rigykgssde leelasifdt mlgrlarsfd gqrrfvanas helrtpltin
      181 rtlvdvavrr peatddvkrl geslllvnar herlidgllt laegehsvld rrpfdltdva
      241 ehvldavage aaerevtihr lldtaptage avlverlvqn lvenairhnh vkgevwvttr
      301 qraeqvelvv antglqvppy eieaifepfr rlhgdrlrsd rgsglglsiv rviaeahhgt
      361 vaarpreegg ltitvelpvq h
//
LOCUS       WP_357675345             260 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357675345
VERSION     WP_357675345.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26779
     Region          1..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 mtdlkgktal vtgaargmgr aiaqrlaadg alvavhysrn adaaretvat ieraggeafp
       61 vqaefgtdgd vrtlltglta glggrpldil vnnaacgnqd tvragsidrl tpgqfdevfa
      121 invkaplfli qatlplmpdg grivnissla trvalpsqia yamtkgalev msrtlanalg
      181 argitvntvs pgstdtdvtd tlhnpeirti ltdltalgri gqpadiadav aflasddarw
      241 itgnvldatg gaylgpmwar
//
LOCUS       WP_357675372              84 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea dietziae].
ACCESSION   WP_357675372
VERSION     WP_357675372.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   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 84)
  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..84
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..84
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=8960
     Region          <1..>50
                     /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 mraiardqve vmralgyerf avaghdrgar cayrmaldhp eavarlavld ivptgrpsaa
       61 ptwtspsaig cgpswrrlsr cpsg
//
LOCUS       WP_357675428             221 aa            linear   BCT 28-DEC-2024
DEFINITION  O-methyltransferase [Micromonospora rifamycinica].
ACCESSION   WP_357675428
VERSION     WP_357675428.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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..221
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..221
                     /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=24372
     Region          45..221
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 maqqteftea llnyvrrvsl rddeiladlr retatlpmgr amqimpeegq llallvrlta
       61 tslpvvevgt ftgystlcma ralppggrlf tvdiserwpm iaapywerag vadridvrig
      121 aarevmadle selgpgavdl vfidadkagy pdyyeaalrl vrrgglvvld ntvffgrvld
      181 eehqdrdtat irelnvslla ddrvdlamls fadgltlavk r
//
LOCUS       WP_357675463             283 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357675463
VERSION     WP_357675463.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=30590
     Region          <169..279
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrsarrlgtg pgftvdavtc vddhrrwspp evgddyrlvl vrtgrfrrkt geiaslvdpt
       61 taylgvpgee erfahpaggd vctslslspa lwrsltgdgr rklrptvyvd arvelahral
      121 ltaarsgdqq falaerllal lsavlvqsss ehadgsvttg skarlvtvar aerlvtaare
      181 aiaaehpaae glvplaellg aspyqlsraf sremgvslth yrnrvrvgra lerledgets
      241 laalavelgf adqahltrtv rrhlghtpta lrrlltgrpa ner
//
LOCUS       WP_357675452             144 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea dietziae].
ACCESSION   WP_357675452
VERSION     WP_357675452.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 144)
  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 144)
  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..144
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..144
                     /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=15609
     Region          2..136
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mterrdlaam lqplvkslia aelrvleehd ismwgyvvls alddspirtq aalaeaigad
       61 ktriistldr lqaaglisre pdpedrrarl lsitqdgrsa rraaqadiqa nedrvlatls
      121 aadrqaflra aqalsamphe eivg
//
LOCUS       WP_357675483             349 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357675483
VERSION     WP_357675483.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=35327
     Region          1..349
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mritvigsgi vgagaayhlt lrgadvtvvd ggrageataa gagivcpwvd hedddawyrl
       61 tlegarhyav ltesvgharv gallvaedpa elepvralla aryaeapemg evrevarpse
      121 lfppldpkls allvpgaarv dgrvvrdgll rsavrrgatv hqgsasltgd gvvtvsggar
      181 leadavivaa gawtgqvcgp lgvdlpvfpr rgqivhatme gadssawpiv lprrgpyllg
      241 fpggrvavga tveeagfdpr itvaglnevv aaglavapgl agatltetrv glrpvmatgr
      301 pviarvsdrv vavtglsayg ltagpfagll aaglalgekp aldlapfav
//
LOCUS       WP_357675495             330 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Nonomuraea dietziae].
ACCESSION   WP_357675495
VERSION     WP_357675495.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..330
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..330
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=36593
     Region          19..>193
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mavaapgdrr raplrvllav glavslpmtv pasgghaepk ptpkqlrkel salqknsdkl
       61 iaeyyssrhe lqkvekaeks arerlrvaqa dyeresaqlr lmaseqyisg gtgaigvmfg
      121 eidlnglalv eamaaeqgar lqgftevrdr hqrarteakd radelsdrik elekqkkaae
      181 kvigkikdri drlyptpgvr rpdgswvpql psgpdnitpr mrlvrnliae rfgvpygigc
      241 yraiqdggeh plgracdfml srggampsaa evrrgneisa waiknaqrlg imyiiyrqri
      301 whartgawkv msnrggttan hydhphisvy
//
LOCUS       WP_357675504             238 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357675504
VERSION     WP_357675504.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 238)
  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..238
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..238
                     /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=26501
     Region          5..>112
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msqleradri ldtaqdlllr wgyrrvtide iakragvgkg tvylhwrtrd elflavgare
       61 avamieavta amradpaeia lhaymrrffl eamrrpvlra lftrdtetld rflssparqp
      121 legakllasr eylgaladng llredlrped ldyslptiaf gffaieplll kaialsleek
      181 adqladvlrr tygpaappst arfaaaapkv veiferlale yravaygttr kgepehgs
//
LOCUS       WP_357675537             362 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora rifamycinica].
ACCESSION   WP_357675537
VERSION     WP_357675537.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10169599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=38806
     Region          78..360
                     /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(136,141,174..179,198..199,203,220,245..246,248,
                     268..269,295..297)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mrdtvvvvsg pgqvelaeqe agepddgair vrtrysgvsa gtelsfvkgt npylnvtfdt
       61 tlglfrpgav stpypvtrlg ymqvdevvqs rtpaiavgtv gamtyghrtg yvadplaerf
      121 vplpdnldpm lgvyvahmgp icangllhaa adlcgtdvrt lgdgvrgrrv avvgggvval
      181 ltalfarrhg aasvvvvdpt pqrrqvaeal gletldpead dpavvlktrw hhsagdrgad
      241 vvfqcrgqdw alhlalrllr pqgtvidlaf yqggadavrl geefhhngls lrcaqigrvp
      301 rglaptwdre rlsaetidll hrygdlirkh lisavvpfae apalltdlae rrrqelqvvl
      361 ac
//
LOCUS       WP_357675539             379 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora rifamycinica].
ACCESSION   WP_357675539
VERSION     WP_357675539.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 379)
  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 379)
  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 379)
  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 379)
  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..379
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..379
                     /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=38436
     Region          1..321
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mrtcrvglvg aggvaqrhar vlgsftdvdl igvtdvarea ataladahsa rvfadidell
       61 aagpdavyvc vppfahgpve eaviaagvpm fvekpvavdl dtaervaalv eekglrtavg
      121 hhwrylhvve qarelladrp vrmvngawld kvppvawwav rdrsggpvve qaahvldlir
      181 alvgeavevt aygdgspppv dgadidsvta atlrfangav gtlaaacvlg wkhragleil
      241 adglalslae dgltirdadg erhlpadpdg arvavdrafv davtgagddi rvpyaealrt
      301 qrlaiavaqs artgrsvtlp tgpaalapat ggipaggvsa ggvraggvpg ggvragdvra
      361 tdvraggghg vpagvtlda
//
LOCUS       WP_357675567             184 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357675567
VERSION     WP_357675567.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..184
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19661
     Region          2..146
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          77..174
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 mtterltrag aeladevgfd qvtlsalarr fdvqvaslya hvrnsgdlrt riallaldel
       61 avraadalag ragrdalaal ggvyrdyare hpgrwaaaql rldpdtaaas aggrhaeltr
      121 ailrgyhlge pdqthavrll gsvfngyvnl elgggfahsa pdteqtwtrv ldaldallrn
      181 wpap
//
LOCUS       WP_357675575             404 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora rifamycinica].
ACCESSION   WP_357675575
VERSION     WP_357675575.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=41121
     Region          112..372
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mllldlsglg yllfgtrtgq sptgaqwala gtaflvalva hrrplvnlta qtvllvaaia
       61 avddttinqv gaswgllelt mrsrrprtgw vaagvlgvva afnpgghgak gvagtvfgvl
      121 vyvglpllag tvvrtnrela rqaeqrrrad qlrresesra aradersaia relhdvvahh
      181 vasmvlrvgv arhvltdpdp rvgavfddvh atgtaaladl rglvavlrdp daahgdaalt
      241 siepsalpta lgaavdrarq sgvtveaevd pavgaldavr glavlrltqe altnvvkhag
      301 aatrarlsvs vvgdavhwev addgrgwtpa tvppggghgi tgmrervevl ggrldagpag
      361 agwrvrtvlp arsspsgssp agsspsgssp agsspsgssp vgsa
//
LOCUS       WP_357675582             225 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357675582
VERSION     WP_357675582.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   ter Beek,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 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..225
                     /product="ABC transporter ATP-binding protein"
                     /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=23589
     Region          3..222
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 miikgltvrf gaftavddvt levpegrivg lvgesgsgks tlaravsglv pytgeivdgg
       61 gvqmvfqdpy aslnprmtvg asvaegvrrp apadverllg lvslppqlas ryprelsggm
      121 rqrvaiaral gasprllvad eitsaldvsv qgavlnlvrg lraelglsml fishnlavvr
      181 yvadeiavmr egkvvehgpt qqvvetpahp ytrdllaavp rlpap
//
LOCUS       WP_357675588             527 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357675588
VERSION     WP_357675588.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..527
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..527
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56156
     Region          223..522
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mttrpraslr rilddlgstv ldvaaspggl dtevtgvhiy dpldelmlps gglllgvgve
       61 gaehicdlle aakagsgivv kqpvavderv rakvletgva llgltraasw sqvaallrsl
      121 laegdlteag qsppddlfsl analcallda pitiedrssr vlafsgrqde adpgriatvl
      181 grqvpesyqr mldeqgwfrk vyqnpgpvyi plseslprva iavrsgdeil gsiwaavrep
      241 lskqrewali daakivalhl lrqrvgadtr rrlqadllst vleggkdaae aagrlgvase
      301 rlcvlaaqla ddqidaaqse sgrqrfcdal alhvgaihpk aaaalvgsva yavlpmhasg
      361 eeearavrva qsflsrvgpr hnanigvgrl aadlgevars radadrslrv lrsrgvagqv
      421 agysdvhfea lllrlgdlaa aeqqtptgpy qrllrydaeh gtelaatlga yldsfgdvna
      481 aaaavhvhsn tfryrlrrlt eisgldladp earlaamlmm rifgrrh
//
LOCUS       WP_357675620            1566 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Nonomuraea dietziae].
ACCESSION   WP_357675620
VERSION     WP_357675620.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1566)
  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 1566)
  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 1566)
  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 1566)
  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 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1566
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..1566
                     /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]"
                     /calculated_mol_wt=166879
     Region          9..1361
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <1450..>1543
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
ORIGIN      
        1 mdhghspgdt diaiigmagr fpgatdigtf wrnistgves ftrfsdedlv sagvdpatfq
       61 qpnyvrsrpi ledirgfdag ffgynpreat ladpqqrifl ecvwealesa gyaapqgrgs
      121 vgvfagmnis gylltrlraf emgidtsalm igndkdslat nvsfrldlng psvsvqtfcs
      181 tslvavhlas eslrrgecdm alaggvsvri pdrigylwee ggqespdghv rtfdaegrgs
      241 mfgdgaavva lkrlsdavtd rdtvlavira sainndgamk fsylapsidg qrrcvsaala
      301 ragvdpadvs yveahgtate vgdpmevaal trafgaterk qycvlgsikp nvghldrasg
      361 vtglikvvqs lrhelipgtl hyrspnpeid feaspfrvta eptpwprtgd rpriagissl
      421 gmggtnahai iteapppaer parprrwqil pvsarsaaaa erscarlaeh legsaddlgd
      481 vaytlqagrk vfnhrkvvva dstagaaall adpagplgrt datvgrqvgf liagvgeqyp
      541 gmvaglyaed pgfradvdec lavlgltepg qlsdvftpag rtsdgagdla rllgraggda
      601 prsmteahlv qpavfvaeya larrlmrwgl rpevmigysl geyvaaclag vlslpdalrl
      661 vayraklits qpegamlavs anerrltavl geegsrdldv avrtgsqvvl agpvaaveaa
      721 aarllearig hrrletthaf hsrmlapvag eltawiadni tlcppslpyl snvtgapate
      781 elvtdpgywa rhmcetvefg agldhvlgip elalaeigpg qslgaltrgh pacergrwpl
      841 ivttlpaagd pqdagaalat avaklwltgv pvdwtalhdd dgvgwapgri plpsypfehq
      901 eywleidesa lgggtpafde sdpksiakay prlpdtrwih aplwrettpr ppmpqeaarw
      961 lvytdaglad elaapllahl aatggeavli rpgeafavgp dgirvrpgsp edavaalrel
     1021 sgrdwaperi vhlwnadgdr pvgeclrrgl htlvafarac gdlglhgwtl divtsgahrv
     1081 hpgdrvhaag gtllgptrli pveyprtrtr lidlgpgcgt rgllaelrae padqvvalra
     1141 grrwipdyet ldatvieqap paarvrqggv ylvtgglggi glamaerlae qyrarlvllg
     1201 rtpvppleew asilaggnaa gevlrrlegl rrleaagsgv vtvagdvsra edvrravdaa
     1261 lehfgelngv lhcagvpavg lmqfktvadm ervlapkvag tlalaevlre vpvdflalfs
     1321 sttsatggga gqvdycaana fldsfalsdp lpgvtvtsid wcewtwngwt dgldnydegs
     1381 rqyfewyren fgltfdqgwq tllrvlasge phvvastqdf apmvamsrrs sieshqatvk
     1441 kirdafgrhp rpdlstayve pqspaeeaia gvwtealgle qvgvhdnffe lggnsllgme
     1501 iiaevrkale lsylpphily qaptiaslae aaragqeage qpaeareqqr sriaqrrnml
     1561 rsgrts
//
LOCUS       WP_357675628             264 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Nonomuraea dietziae].
ACCESSION   WP_357675628
VERSION     WP_357675628.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..264
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28705
     Region          26..264
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtvhdltgdd vlvrwlpfrt ltgaepgalp lyclphagga asafrmwqrk lpgvavqpvq
       61 ppgregrhke ppylhmsela sdladvvlad veltsagrry alyghslgal vafelvreir
      121 rrggpepvhl fvsgadaphv tyepgppvsg mtrpevvall rrlggtpewl ladpdalemi
      181 lpavqadftv ketylyleep pldvpisafp sasdprvapa kvarwrdqtt apfalhpfdg
      241 ghfavfeqaa rtqrllaqal lpwv
//
LOCUS       WP_357675662             759 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357675662
VERSION     WP_357675662.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 759)
  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..759
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..759
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=82068
     Region          3..755
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          552..580
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          592..620
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(593,596..597,600..601,603,633,636..637,640..641,
                     643..644,673,676..677,680..681,684)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          631..661
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          672..700
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          712..740
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msedlarrlr qvreaggrsl rdlerslhvs ssslsryltg qavppwsvvv glcqaagvdp
       61 rplrplweag krgprlgpav tvarndlpyd istftgrqee laavlaaara ervvaidgmg
      121 gvgkttlavh aahrltsdhp daqlyldlhg ftpgrdpvep gealrillaa lgvpsgripe
      181 tveeraalwr selamrravv vldnvagqaq vrpllpgags sivlitsrrr lvglgdaypv
      241 sldvlgprea adlfgkalgd araqdspale evlrrcghlp lvlgvaaarm rhrpawtlet
      301 laeylregdl gtagvlsmsl rdldegqhrm frllglapga dlsvhaaaal aevssstarr
      361 lledlvdasl vlenvpgryh qhdllrelar gaaeerdekr ealtrlldhy vraaatatnl
      421 lypsgahlrp avpagepfar padalrwldg eranlvtagt yaaeqgwpeh avllartlyp
      481 yldghahhae slplygrale aarhlvdrgg evhllnewms mnarqgrydh vhddakhard
      541 lareigdryg earalnalgd mhwrerddlr aeerfrasle lfrevdagtd vaivlgnlgl
      601 vagrqgryde aeralrqala gfaalglpgg qgtiranlgq iclwqgrpae alehyreale
      661 hhrgldypsg eadalngmga aarhlgevtq avedhraala maveagdpar qaaaheglar
      721 ahreggerdl srehatgald iyvrmglpga ddmrafltg
//
LOCUS       WP_357675672             104 aa            linear   BCT 28-DEC-2024
DEFINITION  putative quinol monooxygenase [Micromonospora rifamycinica].
ACCESSION   WP_357675672
VERSION     WP_357675672.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 104)
  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..104
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..104
                     /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=11574
     Region          2..80
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mivifssmsi nparrpdlda emaewlvata qvrggasiyk ymtdpadpsk vyvfqswpdd
       61 nsfatwtqqp afqellekfr ldesitdvea vifegcthtr ggpl
//
LOCUS       WP_357675706             266 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Nonomuraea dietziae].
ACCESSION   WP_357675706
VERSION     WP_357675706.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 266)
  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..266
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..266
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29293
     Region          29..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 mrklliclvl lltacgaarq eslmdddelv vairsdvpli sfkgqdgsyd gfnidvakdl
       61 vsrlgkrirw leikagdqlt vltdgradlv fahmsvtper kkvidfagpy hvdfqdiavr
      121 padkgvirdv rdlkgrkicw vrgtniaqri vderrveaiv vpapdynvcl emikdgrida
      181 istnsqilag lltkpgvdlh lvgatfneqr tsigvrkgdv dgceelnrai tqmyqdgtah
      241 mlldkwfgks gidlsvisvp qfegcs
//
LOCUS       WP_357675807             310 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea dietziae].
ACCESSION   WP_357675807
VERSION     WP_357675807.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 310)
  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 310)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..310
                     /product="helix-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=33699
     Region          19..310
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mletsvrllr llsllqsrpd wpgrelaerl dvttrtvrnd ierlrilgyt vesttgtagg
       61 yrlgagaalp plilddeeav avavslhaaa sgtvtgieet slraltklqq mlpsrlrhri
      121 dalgaatvsv agrgptvdae tltviaaair dheqlrfdye ghdgtasart aephrlvytg
      181 rrwyllawdt gradwrtfra drihprtpng prftprrpps daathvvrgv astawrypar
      241 vrlhappaql sellpptagl lhddgvletg geslhnlaaf lgtlgvpftv ldppelrdll
      301 hslatryana
//
LOCUS       WP_357675719             290 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357675719
VERSION     WP_357675719.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   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 290)
  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..290
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..290
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31396
     Region          11..289
                     /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 mgdgrvpagf teqraqvgdv sinyvrggrg ptlvllhgyp qcwrmwrall pelaatyhvv
       61 apdlrgfggs dappdgydkl tvaadlhgll tglgladdir lvghdvgtmv ayayaaahpd
      121 avsrlvlsea pipdesiytf palteagpav wnfgffsltn glpeelvtgr earwvdrftd
      181 simvhkgsig padieeyarh lsdpahlras fayfrafaqd vadntayrrn plpmpvlavg
      241 aaasldgqva dqvrryartv dgrvvadcgh wlfeerpael talllpflrd
//
LOCUS       WP_357675815             704 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Micromonospora rifamycinica].
ACCESSION   WP_357675815
VERSION     WP_357675815.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..704
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..704
                     /product="PhoX family protein"
                     /calculated_mol_wt=75259
     Region          47..698
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 msdrprllpl lgatrhgsrd amtclyrcgn acdhpvpnts gntyfgdlve gevsrrgvvr
       61 agavgalvlg fggalagaap agaapatpvv pevgdptapq rgvgsgaltf kpippnqldt
      121 lvvpngydhs vvirwgdpvl pgaprfdlhg qtaaaqakqf gynndfvgvl pldrrgkral
      181 lvvnheytne dlmfpgftgl dnltveqlrt amaahgmsvv elervdgsgq wrpvgqgrrp
      241 ynrrvtalat kfeltgpaag sawlrtaadp kgrtvvgtln ncaggvtpwg tvlsgeenfn
      301 qyfvgadaap aelkprfdry gittaaryps gsrkwerade rfdlakhpne ahrfgwivei
      361 dpfdpesrpr khtalgrfkh eganvivard krvvaymgdd erfdylykfv sdkkfmpgds
      421 wvarknnltl lesgtlyvaq ftqtsaaeid gsgklpadga fngsgrwikl vsgnrsyvdg
      481 mtaadvltft rlagdkvgat kmdrpedvep slltgkvyva ltnntdrgka gkpaadeinp
      541 rnlnkhgqil elvedrgdnt aesfawslpi vagdpadpst yfagydktkv spiscpdnva
      601 fdatgnlwis tdgnalgsnd glfatavegp erghlkqflt vplgaetcgp fitgdnrsvf
      661 vavqhpgeit gasvekpast wpdgdyakpg vvvtwrldgg pigs
//
LOCUS       WP_357675830             224 aa            linear   BCT 28-DEC-2024
DEFINITION  urease accessory protein UreF [Nonomuraea dietziae].
ACCESSION   WP_357675830
VERSION     WP_357675830.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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..224
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..224
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22697
     Region          4..224
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mnraallvla dgrfpaggha hsggaeeavt agrvrdvagl qefcrgrlht sglvaaglaa
       61 aaaagydpll leeaadartt apalrrtsrr lgrqllraar aawpcpelda laaarprgah
      121 qpvvlglaar cagltpldaa yaaayesvgg pvtatvrllr ldpfdatavl arlasdidhv
      181 aaagaeaaqr vhtdgpaalp avsaplldit aeqhaarpar lfas
//
LOCUS       WP_357675867             227 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Micromonospora rifamycinica].
ACCESSION   WP_357675867
VERSION     WP_357675867.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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 227)
  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 227)
  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..227
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..227
                     /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=22752
     Region          1..227
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrlrstlavl ttalagvlat aagataapag pqpiiggstv ssapwaaavf sngsftcsgs
       61 viaaqwvlta rhcvsgtmsv rvgsvyyasg gttrtvsasy trndlallrl astvtntpvs
      121 lassnppvgs tntiygwgmt cysgcgassq lktasvqvts tnatdayggq airstringn
      181 awrgdsggpq fyngrqvgva stadgssiqn ygsvaynraw itstagv
//
LOCUS       WP_357675922             494 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357675922
VERSION     WP_357675922.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 494)
  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 494)
  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 494)
  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 494)
  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..494
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..494
                     /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=51195
     Region          22..493
                     /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 maepelvdvv vvglgvggee vagrlaeagl svvgverdlv ggecpywgcv pskmmiraan
       61 alaearrvdg lagsaqvrpd wapvakrire eatdtwndra avdrftgkgg rflrgsgrld
      121 gpgrvrvgdq vfqarrgivl gtgtrpsipp idglagtpyw tnhqaievae lpatlliigg
      181 gaiglelaqv farfgvgvtv leasgrvlal eepessevaa aalradgvei atevkiervg
      241 hdddtftvya gdrsfsaekl lvvtgrrahl eelgldtvgv datqrylpvd drmhvtdeiw
      301 avgdvtgega fthiamyqas ivvadvldha rraeggpdas gtasvvggam gaasavggsm
      361 gaagpsgaag tvpradyral prvtftdpev gavglterqa rerginvqvg ftelssstrg
      421 wihqgepggf ikviadadqg vligatsvgp aggevlsalv vavhaavpvs qlrhmiyayp
      481 tfhraiqsal ndls
//
LOCUS       WP_357675951             242 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Micromonospora rifamycinica].
ACCESSION   WP_357675951
VERSION     WP_357675951.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 242)
  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 242)
  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..242
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..242
                     /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=24270
     Region          30..240
                     /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 mffvrrlaat lavvpvlraa varyavppgv adrtgcpgcg apvgldrplp algptarcpr
       61 crgrigaapl avealslvav avlalvdgav aervalawwl gcavplvlvd lavhrlpdrl
      121 twpaaagtwa llgvaalaga gagpwlravt agvalglafa attlllgrrg fglgdaklal
      181 gvgallgwqg wgvvvtglvl tfllsalvsv allatrrvgw sshlpfgpfl vagtcaalll
      241 pa
//
LOCUS       WP_357675959             156 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357675959
VERSION     WP_357675959.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 156)
  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..156
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..156
                     /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=16890
     Region          1..132
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mservewglh ccltlawigd dhpmpaarla ewfalppayl tkclqaltra gilqsvpgar
       61 ggfrlarppa evtvlavtva idgadnpfrc teirqrgagv dpaapefrvp caistvmhra
      121 dlawrrelad htladllaaa paeaaertrr halrpr
//
LOCUS       WP_357675971             295 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea dietziae].
ACCESSION   WP_357675971
VERSION     WP_357675971.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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 295)
  AUTHORS   ter Beek,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..295
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..295
                     /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=32770
     Region          6..292
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mraivqrtlg lawvvpalvl vgvfvylplv qnigfstlkw diysgdqeyv gldnytklld
       61 dpifwssfgn nllyavisiv fqvfgallla aliesirsdr wrrslraiyf ipsaisltva
      121 gllfyfmyep nlgplnhafq avglglfdqs wlgqestamf aiigmsqwqg fgystllfav
      181 aiqripsely gaaaidgtgp irrfihvtvp lvremtglmt mvtisgafqv fnevmvmtsg
      241 gpnnstqvmg twlyrsgfvr nnfgyaaaia tlifvitlgi amaqlwvtrr rrvew
//
LOCUS       WP_357675987             184 aa            linear   BCT 28-DEC-2024
DEFINITION  chloramphenicol phosphotransferase CPT family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357675987
VERSION     WP_357675987.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008105
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..184
                     /product="chloramphenicol phosphotransferase CPT family
                     protein"
                     /calculated_mol_wt=19991
     Region          1..172
                     /region_name="COG3896"
                     /note="Chloramphenicol 3-O-phosphotransferase [Defense
                     mechanisms]"
                     /db_xref="CDD:443103"
ORIGIN      
        1 mrgdsmvivl nggsssgkss larslqellp dpwlafsvdt lvdampssci tftpdgevhl
       61 gprfgeleda wmagvatmvr sgarvilddv flsgpasqer wrvpltgldv lwvgvrcdpe
      121 vaarrererg drptgmarsq atmvhegvvy dmevdtsfms addcaqliak wmnrqtgeta
      181 heph
//
LOCUS       WP_357676050             540 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Nonomuraea dietziae].
ACCESSION   WP_357676050
VERSION     WP_357676050.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..540
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..540
                     /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=57932
     Region          73..540
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mprtaalral qriaadhhaa rrlgmpveev rglgrrellr raalaglgat afaatpaaal
       61 advvadapkp plrpariavv gagiagltaa ltlrdagaep vvyesntrvg grmytqrslw
      121 lngqtseigg elidvehkkm lqlcrrfglg tvnfagsgpn gaeevlhvng hyyprsqada
      181 dfkemyqdlh adlmaagevm wnnatpegia ldnmsirewi dsrvpggyas dlgrfldvay
      241 nveygaette qsslalvlll gyqpnpghfn vwglsderyh ivggndqlpq aiaaslpsgs
      301 vrtgwrllav ranadgtqtl tfdggrtvta dhtvltvplp ilqsldlsra gfdarmtnll
      361 rdarmghvtk lnmqfstrpw lgtgpwdgvs agdcftdqpw qqcwdttkaq agatgvliqy
      421 gggaaaraln pstafpthtd pyvrtlagsv ldgidtvfpg tkaqwngraq lsawhknpha
      481 lgaysywpvg ylhryagyeg vpqgnvhiag ehtsydfqgf mnggateger aaneviaklr
//
LOCUS       WP_357675989             451 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-binding oxidoreductase [Nonomuraea dietziae].
ACCESSION   WP_357675989
VERSION     WP_357675989.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..451
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=47096
     Region          1..449
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 miealvkalp egrvltdpdv vdsyardrtf lepgkalgvv lattrdevvt tlrwatehrv
       61 pvvprgagtg lagaataseg sivlslakmt airelnpade yavvepgvit adldraareh
      121 glmyapdpss yeistiggnl atnagglrcv kygvtrdsal glevvladgr ilntgrrtvk
      181 gvtgydltgl fvgsegtlgv itsatvrlrr aplappatia aefgslreaa aavsaiiaag
      241 cqpslmelld ratlkaiddw rnigledstq amligqsdas dgqamaammq qlceangasf
      301 valsstpeet edligirrma yqakerlgac lvedvcvprs alpgmisaie aaaarhdvmi
      361 ctvahagdgn lhpvfifdhg tveppanvwa aadevfkaal emggtltgeh gvgllkrrwl
      421 alesgpvaae mqqgikrvfd plgilnpgka i
//
LOCUS       WP_357676077             271 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea dietziae].
ACCESSION   WP_357676077
VERSION     WP_357676077.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     Protein         1..271
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29200
     Region          11..257
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtankvqgpv irvqgleksy kelqvlrgvd fdvargsifa llgsngagkt tvvkilstll
       61 kadagtarvh gfdvatqpad vresisltgq faavdeilsg renlvlvarl rhlkdpgkia
      121 ddllnrfslt dagarkvsty sggmrrrldi amsligdppv ifldepttgl dpqarievwq
      181 avrelagqgt tvllttqyld eaeqladria ilhqgriivn gtlaelkqll ppakveyvek
      241 qptledvflt lvgdngkngd vrqishastd k
//
LOCUS       WP_357676154             994 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357676154
VERSION     WP_357676154.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 994)
  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 994)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 994)
  AUTHORS   Rosinski,J.A. 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 994)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18732957
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..994
                     /product="helix-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=107392
     Region          <7..938
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          933..989
                     /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(934..936,949..951,959..960,962..963,965..969,980)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:99777"
     Site            order(945,947,949,980..982,985,988..989)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:99777"
ORIGIN      
        1 mpeesvfvgr adelgllrrr laevgrgkar tvlvggepgv gksrllsefa lqargfgahv
       61 lagtceerfg sptpygplie alemfgrehg earavelggs ayqkltvffd lgsdsmgapq
      121 qvflaarrml deigskapvv liledlhwad pstldlvrhl gqaspegrrl llvgsyranp
      181 prgellwqlf agttflrrte rfelapftla emrellaagr vdpklaarcl rwsdgipfya
      241 eqllaagalt grdedvelpp dirsvmlarl selsedalrv lrvaavagra msrrllrtvs
      301 glpaetlrda lqecfdrqml vaeheddvyr frhalmrevv yqqtvrdtrv dlhvamaeal
      361 aadsrlclse gsavaeqagh wyqagswpqa lgsavqagqv aartlafasa qvqfdralgl
      421 wrqvedpqtr agvthpqlla eaaeaarwsg hldralelvg raidapdhgr dpgrlgelhe
      481 rratylweag rrteygaafr qaatllaesp psavkarvla gialahlqag hyqegrdtad
      541 aalalatevg aeaergralg isglalgmlg dpegerrlrr sleiarsaqh iedllrayan
      601 lglilehagr lresatvtsq gleearrldl agsrqgvlla nnssaalvll gewadaekii
      661 teasldrspa eslyprltla eikvaqgafa qahqllasie nvehgedprf lgplhavrae
      721 lalgegdpvr aadevsrgva avrrgenale llrlfalgmr caadraatdp qgatavgdrl
      781 aglardvvrr ssttaagqlt aelrqlvalc taerqrigrt dsalgwkrva vgwaeldrpy
      841 paayarwrqa laalaaadrt aaqaavrtaa qaadktavpt gdraaarepa rdayriahgl
      901 garplaerie elapkigltl gerpvparlp hrltpaefev lrmlyegmda ariadargvs
      961 lrtvqtqltk iyrklgvhsa tgavalarre gffd
//
LOCUS       WP_357676215             207 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357676215
VERSION     WP_357676215.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  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..207
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..207
                     /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=22158
     Region          2..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mradalrnqe avlaaagrlf daavdpdevs mdaiaaaagv gkgtlfrrfg draglvlaly
       61 erraehlrtm tlralsqggl askdgpasqd ghdleggpaq ralallvatv rfkqanrvlt
      121 lalendgsrs pyrtaayehw hrlltalvie argpeqadyl ahvllgavrs dlvehlrpqs
      181 aqqwheglra lvqgllgsag paprqqh
//
LOCUS       WP_357676241             387 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acetylglucosamine-6-phosphate deacetylase [Micromonospora
            rifamycinica].
ACCESSION   WP_357676241
VERSION     WP_357676241.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Hall,R.S., Brown,S., Fedorov,A.A., Fedorov,E.V., Xu,C.,
            Babbitt,P.C., Almo,S.C. and Raushel,F.M.
  TITLE     Structural diversity within the mononuclear and binuclear active
            sites of N-acetyl-D-glucosamine-6-phosphate deacetylase
  JOURNAL   Biochemistry 46 (27), 7953-7962 (2007)
   PUBMED   17567048
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hall,R.S., Xiang,D.F., Xu,C. and Raushel,F.M.
  TITLE     N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate
            activation via a single divalent metal ion
  JOURNAL   Biochemistry 46 (27), 7942-7952 (2007)
   PUBMED   17567047
REFERENCE   3  (residues 1 to 387)
  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 10788057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..387
                     /product="N-acetylglucosamine-6-phosphate deacetylase"
                     /EC_number="3.5.1.25"
                     /GO_function="GO:0008448 - N-acetylglucosamine-6-phosphate
                     deacetylase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0046349 - amino sugar biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39882
     Region          3..378
                     /region_name="NagA"
                     /note="N-acetylglucosamine-6-phosphate deacetylase
                     [Carbohydrate transport and metabolism]; COG1820"
                     /db_xref="CDD:441425"
ORIGIN      
        1 mpadrvltgr dpvsgtplav tvaagritgi gpgpaqetrf lcpglvdlqv ngfaghdlna
       61 dgltpqtvva lthtlfasgv ttfvptlvta ahdritralq aisaarrtdr lvehaipyah
      121 legphispqd gprgvhdatw vrppslsefa dwqaasgdlv gmvtlsphfp eaadytaalt
      181 grgvhvavgh thaepaqita vvdagarlct hlgngahavl arhpnylwtq laderltagf
      241 iadghhlpad tltamlrakg pdrsllvsda valaglppgr yrtpigdave lhadgrlvqs
      301 gtpylagaar gladgvaqav taarlslgea vrlatgqpgr fvggrgtvtv gapadllrfd
      361 wvpgastlgv dtvlvlgqev gppratr
//
LOCUS       WP_357676238             335 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora rifamycinica].
ACCESSION   WP_357676238
VERSION     WP_357676238.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 335)
  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 335)
  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 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   5  (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   6  (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   7  (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 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..335
                     /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=36439
     Region          22..334
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msgapapdvp aegevlarrv rtamvedpap arvrgasrrq rlrrdltlvl lmlpalayfl
       61 vfhygalagn liafldyvpf lgitgsvwvg fdnfsemfrd pamwqatwnt veisalqllf
      121 ffpaplglal llhsltggfv rkfvqsvvyl phfiswvivv alfqqvlgga gvlngmlgdh
      181 glstidvign pdmfkplvvg qviwkdcgwg miiflaalhq vdeqlyesaa idgagwwrrl
      241 whvtlpalrp iialllilkl gdilstgfeq iylqrasvgp aaaevldtfv yftgvangdw
      301 gyaaaaglfk gvvgallvys ankvahrlge sgvyr
//
LOCUS       WP_357676290             302 aa            linear   BCT 28-DEC-2024
DEFINITION  transketolase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357676290
VERSION     WP_357676290.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..302
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32066
     Region          40..290
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mrdafvasat rflddprtti vladisadaf aaaarrypaq vvnvgireql migvagglal
       61 tgqrpivhsy apflveraye qikldldhqg vgavlvsigg sydraesgrt hlapadvali
      121 dtldgwtvhv pghpdevpdl lrdavcgqhs tylrlslrsn araypqaggl qvvrdagpga
      181 allvavgpvr ddalaavadl pvtvaythrp rpfdvtglrt lagsevivve pylagtstrv
      241 vaealadrph rllslgvgra elrrygtaed hdrwhgldpa glrraiaafl tpgdrtpgep
      301 vr
//
LOCUS       WP_357676248             274 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora rifamycinica].
ACCESSION   WP_357676248
VERSION     WP_357676248.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 274)
  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 274)
  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 274)
  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 274)
  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..274
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..274
                     /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=29256
     Region          22..274
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 migtenthvd qileylnvre lapgtrvval aggaterneq lrahggveri vdaptellgq
       61 vdaviitdrh gglhrehavp flaeglpvfv dkplacsvad aeaivavare hdalltsysa
      121 lrwipdteal vaelptvgtp qvvvttgpad easpyggiwf ygihsvdval rlvpgeigev
      181 rversvetvi arvrvgdtlv vvnlvrpeei arvpfhamvv grtgiaarpl vlddwyvapg
      241 leaflrmvgt ghppigyddl lrpirvldav aaal
//
LOCUS       WP_357676309             394 aa            linear   BCT 28-DEC-2024
DEFINITION  homogentisate 1,2-dioxygenase [Micromonospora rifamycinica].
ACCESSION   WP_357676309
VERSION     WP_357676309.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..394
                     /product="homogentisate 1,2-dioxygenase"
                     /calculated_mol_wt=43864
     Region          1..390
                     /region_name="HmgA"
                     /note="Homogentisate 1,2-dioxygenase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3508"
                     /db_xref="CDD:442731"
ORIGIN      
        1 mpyyrsvgev prkrhtqfrq pdgtlyteel mgqegfsads sllyhryppt aiiaaeeftp
       61 pghtrlpnhp lkprhlrthk ldgagadpvl grrhllandd vrigyaladr psplyrnatg
      121 declyveagt lrlessfgal dlvagdyavi ptstvhrlvp tgdtpvrllt ieatghigpp
      181 krylsargqf lehspycerd vrgpdapllv dgtdvevlvr hrartatgta wtrhvyahhp
      241 fdvvgwdghq ypwafsihdf epitgrlhqp ppvhqtfagp nfvicsfvpr kvdyhpdaip
      301 vpyhhhnvds demlfytggn yearrgsgie qgsislhpsg fthgpqpgaa ersigvdffd
      361 elavmvdtfr pldlcdaave cedpgyawtw nrrp
//
LOCUS       WP_357676357             232 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357676357
VERSION     WP_357676357.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=24649
     Region          35..190
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msprppswld plvdrlgtar aedftrlttp eeggresavl vllgeqpgsg pdvlvlqraa
       61 tlrnhagqpa fpggaadpgd adaratalre aneevdldpa svtvlaelpr lwipvssfvv
      121 tpvlawwhsp hpvhprepae vahvarlpva elvdpanrmr vrhasgwigp afsvrgmlvw
      181 gftagvldal lemggwsrpw pwsrvvelpp tgatpapsag teeadelagp rt
//
LOCUS       WP_357674201             485 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Nonomuraea
            dietziae].
ACCESSION   WP_357674201
VERSION     WP_357674201.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea dietziae
  ORGANISM  Nonomuraea dietziae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea dietziae"
                     /db_xref="taxon:65515"
     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=51177
     Region          8..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 mngtlkraav aclvmfgllm lnvnylqalk aeelrsdarn irnyfdrydv qrgritaggt
       61 ilaqsvekkk gdfrfvrnyp dgkvfahvtg yfspesesai essenrylds thpdlllrrs
      121 idlftgeptr ganvevtinp kaqkaaheal sasgkrgavv alnpktgail tlvslptydp
      181 nvlsgtdkpt vfgaynkldk dktngplvnr ainrtyppgs tykvltaaaf leddssrdgq
      241 tivpapqvld lpnttadlpn sggaacgggq vplvyalers cntpfgkigm dlgydrmaeq
      301 aakfgvgqpl tipmgvsksd vgpkedqaal aqasigqrsn qmtplqmami aagiandgkv
      361 mkpylvqkit dakndtidea epeelseavs setaaklrqm mvsvvnngta sraqisgvev
      421 ggktgtaqtv qgkaphawfi sfapaqdpqv avavivesgs agtdasggqt aapiakavme
      481 avlnk
//
LOCUS       WP_357676455             423 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora rifamycinica].
ACCESSION   WP_357676455
VERSION     WP_357676455.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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..423
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..423
                     /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=46719
     Region          60..397
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgfvrktsag tyracwrdpa ggqksksfrt kreastylte vegslnrgty vnphagrlrf
       61 gdfaqqwlat rvveartter tvsmlrthvl pkwgdwplgk vdfmsvqewv tglgrdlapt
      121 tvakcyqlls milrtavqar liatnpaegv klprdrsrdv kpvtisrgdf lgrllpavpp
      181 rhraivstaa gaglrwgeca gltwssvdld raslrvvqva eethggivlr pypksragvr
      241 tvplpgflla alrelhttad dpdprtlvfr drvgrplrrs nfrrrvwlps lvragllgqv
      301 vaigphryra vwpdrdgvew saeftterea vacvaaraag gmrfhdlrha yatwlvtdgv
      361 pinlvqrvmg heqasttlnr ythtpddyaa rvleafdgsa asllppaget psvghpdeed
      421 del
//
LOCUS       WP_357676509             195 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357676509
VERSION     WP_357676509.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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 195)
  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 195)
  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..195
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..195
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21228
     Region          9..176
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlplppgdfr aylfdcdgti vdsmpvhhla wraaldewgc dlpedlfyaw ggrpvadivv
       61 dlnarhglam pvelvarrre dayqsflpql tavpgvlahi eqayrrvpfa vvsgstresv
      121 tasltalgll drfdalvcae dyarakpdpe cyllaarlld vppeqclvfe dtdlgvaaat
      181 aagmasvrvp ppwqr
//
LOCUS       WP_357676516             303 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora rifamycinica].
ACCESSION   WP_357676516
VERSION     WP_357676516.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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..303
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..303
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33022
     Region          18..>128
                     /region_name="WcaE"
                     /note="Glycosyltransferase, GT2 family [Carbohydrate
                     transport and metabolism]; COG1216"
                     /db_xref="CDD:440829"
ORIGIN      
        1 mnrpldlgtt gefrrprrld vliptrnrpa elavtlagla aqlgvpgfgv vvsdqsddkp
       61 ayahpaaatm vrvlrhrghp vlltrrlprr glaehrayll grsaaryvlc ldddvwlepg
      121 tvqrlvtaig elgcgfvgna vhglsyaddv rpdthrhyee wtgpvvpelv rpgtpqwqrs
      181 eihpaanllh iqqqvdlppg awraykvswi ggcvlydraa lvdsggfefw rrvpenhqge
      241 dvaaqlavla ryggagvlps gayhlesptt vtdraveawe vvaadparrt tarpahadss
      301 rpa
//
LOCUS       WP_357676628             278 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357676628
VERSION     WP_357676628.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   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 278)
  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..278
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..278
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=29271
     Region          2..274
                     /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 mtehlsiagn nlayevsgrg plvvlahgig dsrhsyrfla palagvgyrv asvdirgcgd
       61 sslgwdgysr tdiagdlvav vrhlggpavi igqsisggaa tiaaatapdl ingvielapf
      121 trvqpfdlgg lmrvkrfrsg ysqmaqvmvl grlaswkkyl dvaypvkpad waaeltriea
      181 klnepgrmkv lqamcrtspt dagaqlanvt cpvlviegsl dpdwadprae gekiiadlpr
      241 glgelaiieg aghyphaqtp dqvlalarpf ldktlana
//
LOCUS       WP_357676715             397 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora rifamycinica].
ACCESSION   WP_357676715
VERSION     WP_357676715.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 397)
  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 397)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 397)
  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..397
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..397
                     /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=41368
     Region          129..396
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrmpgwagsg rpgrdlalag aslvgglavy gvglqpqfpw apdvpracfl lpllavsvav
       61 glrrvatrtg lavgtvavla daalgvsvgg tviytqvlyd tcvygpprvr rwllrvtvgl
      121 svgstalgll vwgwrgagvg vpfallgvlp vvtgvsvrqy rdqaaaerar aeqtarlvel
      181 drrqavlaer armarelhdv vanqlsaval hatavlaapg ldrpqveaal rviressvqg
      241 maemrqlvgl lrepsvdpvq eatrvrlael drllarmaaa glrvrttvag rprplpvgvd
      301 laayrivqes ltnalrhgrg taeltvaygp tevvvtvenp vrsdgsgvat agaglpggga
      361 gligmrerat lldgeftggl rdgcwrvrat lptgasa
//
LOCUS       WP_357676818             383 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine desulfurase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357676818
VERSION     WP_357676818.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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 10003004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..383
                     /product="cysteine desulfurase family protein"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=38936
     Region          5..376
                     /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 msahpvylda ataaplhpva rqallaaldd gwadparlyt tarraaqlld aareataatl
       61 gvrpdevsft psgthaahsa vlgglagrrr sgatlvhsai ehsavlhaag rhvaaggtat
      121 svpvdrlgrl deaawsaavh spgvalaali gashevgtvq pvagaaaaca aagvplhvda
      181 aqlvgrvpvp agwsvltasa hkwggppgvg llvvrkgtrw espwpadere fgrtpgvvnl
      241 pavvaaaasl raaaadaaae aarlaplvdr irarvaadvp dvevvgdpvd rlphlvtfsc
      301 lyvdgevllh aldrrgfavs sgssctsstl rpshvleamg vlshgnvrvs lhrdtteadv
      361 erfltelpgi vadlradagv vgl
//
LOCUS       WP_357676833             829 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357676833
VERSION     WP_357676833.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 829)
  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..829
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..829
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=89238
     Region          15..829
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          613..641
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(614,617..618,621..622,624,654,657..658,661..662,
                     664..665,694,697..698,701..702,705)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          652..682
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          693..721
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          733..760
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          773..801
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msdqrgpagt rqpaagavrp apeahrldtd aqtvpdlagl lrqlrrrear qqgetpltyr
       61 qlaartgwsr gvigeyfagn ilppperfdt lirllgatpt eqgalatard rveerrrhtd
      121 pdhpapgrsa rttvrtrsgg tragtpaarv pvprqlppal pgfvgraaql dqldtgctgh
      181 dmpgragpts tmvlsgtagv gkttlavywa hrvadrfpdg qlyvdlrgfd stgavvtpte
      241 avrgflealg vppdrvpthl saqvglyrsl ladrrmlvll dnardvdqvr pllagspncl
      301 clvtsrhrla glitaegarq itvdllstge awqllarrlg adrltvepaa vdemiercvr
      361 lplalavlsa rgaahptfpl ativaelrea prlldsfdgg dtgtdvqavf swsyrnltpp
      421 aarlfrlfgc hpgpdtgvaa aaslaglprs rtarllaela hahlltehap grfaahdllr
      481 ayaaelaerl epaedrqaav qrgldhylht ahaaalllqp grdpvvpvaa rpgvvpedla
      541 dhgralawft aeypvllaav sqagrngfdg hawqlawalv dflqrrgnwp elavaqqaal
      601 agarraadlp gqanahrdla ralnrlgrvd eavehyrqal alfgglgdht gqarthrafg
      661 amldglgrya ealehaqral alyraaghla gqasarnavg wafarlgryg paldhcsral
      721 allcstgdrh geantwdslg fihdrlghhr qaircygral vlyrrigdry deadtltrlg
      781 gtrqalgdlh garrtwrral aifgeldhph aarvrdlltr paaegtaad
//
LOCUS       WP_357676880             860 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora rifamycinica].
ACCESSION   WP_357676880
VERSION     WP_357676880.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 860)
  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 860)
  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 860)
  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 860)
  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..860
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..860
                     /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=89647
     Region          195..857
                     /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 mtdapllrrp psapvvssvl aallvgaglt galpplaava lagvvgcapv vgrllrlaaa
       61 ggrdrrsrlr rraaalldva vtvaaltvav splapagwrv gvavaglgaa tatyaaglfl
      121 lpghsrltpr arlrrgvdvl glgtallfag wvlvpsgpvp pvvravtvlg aaglagllvs
      181 aladrrrrpg aarcrvgaat vlaglaglva leayrapava lltlvpllvg galltaagma
      241 rvsagdppgp agpppawprv tapaavatva aaghlavvgg fsatavllgl avipplvgre
      301 lisatddrrw adrlaareay frtlvsggrd lilvlddrlr vhwlsaager wfglrqgdvr
      361 glaladllhp ddapgvltrl aappedggpp llvarmragd gawreiestv sdqrdvpeva
      421 avvlhvrdvg drrrlerelr rvaatdpltg lanrqellrv lgervgppga lllvdvlggg
      481 ptqdgpgpgv dgdalmatta rrlrdvvgsr dlvarlsgae favvtdaasv payalgerll
      541 aaltepwpvp sgmarlrvav glaeltgggp qdvlrqadla rrravqlgrn rvewydvcle
      601 eqlvrrldle relpgaaarg eldlvyqpvl aladrrpagi eallrwrspv lgtvlpaell
      661 pvaedlgllg elgrwvldra crqladwsyg grelwlavnl tlaellapdl vprvatvlag
      721 hgvpaerlvl eiaepglgad lsmvvarlag lramgvrtal dsfraehasl trlrrlpidl
      781 lkvqpqpvgp degarplidv vvglgerlgv tvvmaelese pdvdratrag crygqgfala
      841 rpataervea yfaefpsafr
//
LOCUS       WP_357676906             287 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora rifamycinica].
ACCESSION   WP_357676906
VERSION     WP_357676906.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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 287)
  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 287)
  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 287)
  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..287
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..287
                     /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=28344
     Region          112..>286
                     /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 mavqtglgep rgpwflspdl gpdgrhrwdv pgpgedpsrr rwrgrlwtaa avvalstvsg
       61 aaaggwvagq dgagptaasa apvpaelvta aqktvpgvvs vlvgggvagq sasgsgfaid
      121 neqhivtndh ilakgnggav tvempdgrry aadvvgrepg sdlavlkvps aaglaplpla
      181 kprstrvgep vlavgsplgl agtvtagivs alnrqvrlgt srrsavqtda sinpgnsggp
      241 lvnargevvg vntaiatldg sgsigigfai pidqvqqtad tiigkgg
//
LOCUS       WP_357676913             306 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357676913
VERSION     WP_357676913.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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..306
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..306
                     /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=32689
     Region          31..284
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtwdepaarr vlrppadyrl tasvraltfs pydpcariaa gtfrwatrtp agaatltlrp
       61 eggeliaegh gpgadwvver adaiaglrdd ltgfaglaaa hpvvagvaar hrglrmpatg
      121 qlfprvlrav leqkvtgqea yrayaatvrh faepapgpfg plllppdaat vaatpywvfh
      181 rfgveqrrad tlrraaalad rlercvdsae atrrltaipg igpwtaaevv rigygdpdav
      241 svgdyhvpnt vawalagear gddarmlall apfrghrgrv clllaaagiq aprfgprmpv
      301 rsfarf
//
LOCUS       WP_357676940             398 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357676940
VERSION     WP_357676940.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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 398)
  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 398)
  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..398
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..398
                     /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=41658
     Region          6..391
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mprevrdvvf vdgvrtpfgk aggmyantra ddlvircire llrrnpqlpp drveevavaa
       61 ttqigdqglt igrtaallag lpktvpgfav drmcagamta vtavaggiam gaydiaiagg
      121 vehmgrhpmg egvdpnpriv aeklvdpsal vmgataenlh drvphvtker adtfalasqv
      181 ktakayadgk lqadlvpvai rddeggwgla tadeaprets laklatlktp frphgrvtag
      241 naaglndgat aslladeata relglpvamr lvsygyvgve pevmgvgpip stekalriag
      301 lgiediglfe lneafavqvl afldhfgiad ddprvnpwgg aiaighplas sgvrlmtqla
      361 rqfaehpevr ygltamcigi gmggtviwen pnweggdk
//
LOCUS       WP_357676955             181 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora rifamycinica].
ACCESSION   WP_357676955
VERSION     WP_357676955.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 181)
  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 181)
  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 181)
  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 181)
  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 10006981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..181
                     /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=19234
     Region          6..157
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mttlrlrped padagpvrrv laaafarpdg ttpgevtlvd elrgsvawlp elamvaeygg
       61 evvgyalltr vqveadrarv aalvlgpvav aphrqrvghg tavvqaalea atelgerlvv
      121 vlgdpayyrr fgfsradrmg lvspwsglge pwqalvlppe vshapppprg evvfpppwsr
      181 v
//
LOCUS       WP_357677010            1490 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Micromonospora rifamycinica].
ACCESSION   WP_357677010
VERSION     WP_357677010.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1490)
  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 1490)
  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 1490)
  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 1490)
  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 1490)
  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 1490)
  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 20187797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1490
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..1490
                     /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=151684
     Region          <79..606
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          616..1455
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mttlgrvagr ilpsvpvppl vggvsrgvgs aagrlarvag ltrrrvwsrd grhhievhgv
       61 cqdggdrlar qvevalqrlp gvawarvnap sgrvvvavve pkprlrdlid tvarvervcp
      121 hepdpeippp hppedgprtp rtlgalasda lgltisaatr ilpftpvpge vaglltavdl
      181 hpklhdlagr glradpraev lfplaeavvq gltggwagiv ldgaqrivqw gearaqlatw
      241 traepgltgd pdravarspg vrrpcprpdg pveryvstml atgaaagaaa wpvagpkraa
      301 alglaalpka pgsgregyaa qlgrilarrg viamdrsvlr eldridtvvl daavlgsarg
      361 vladlaplag tdtgevagra falfdpdhpd dvheadgwrl gpladldaad pgdtpdserl
      421 raaggpllgl vhggsltavv rvapepapgv dalptaarha glrlvvagad tqrygfadav
      481 lpggdrlaes vralqrdgav vmlvsgdrva lagsdcglgv aapeelppwg ahllvgtdlr
      541 ipallieaag aarrmtgqni rlamagtglg algaftaaap qlpgrslaav ngaaalafan
      601 gvwrarrlpd ptdtpmpatt awhlmpaatv lhqldtgpdg ltdaeaqrrh radpaattgt
      661 vglfrafvde lanpltpvla agavlsatfg slvdaalvgg vvggsalvga vhqrntdral
      721 agllsrsavt arvlrdgaer vtaaedlvpg dvvsvrpgda vpadcrvlta dgleadessl
      781 tgeslpvgkg agpvvaaala drtsmlyegt tiatgrgtav vvatgtrtes grslalarqa
      841 ppeigvearl grltrsaipl aagsaiavag agllrgvplg qtaataanla vasvpeglpf
      901 lvsaaqlaaa rrlaehgalv rnprtiealg rvdvlcfdkt gtltegrlll agvgddgrfa
      961 avdrlddglr rvlaaglrat pyaadpqelp qhtdravryg arragvseqt gasgwsavgg
     1021 lpfepsrgyh atvgrtadgl llsvkgapet vlprcgswrl pggrdeplda arrdrlhaal
     1081 adragaghri lavaecraga eavtddevrg lvfvgflala dgvresaapa vrrirqagvh
     1141 timitgdhpa taaaiaatis peadgqrvvt ateldeldda algerlartd vvarctpahk
     1201 vriiqalqrc grtvamtgdg andapairla dvgialgqrg tpaaraaadl vvtddrleti
     1261 iatlvegram wssvrhalsi lvggnlgeia fsvlsaavtg rsalngrqll lvnlltdlap
     1321 alaiavrppd sdhadgllre gpdaslgdtm treiglraaa ttlgatagwt varwtgrerr
     1381 agtvalvslv gtqlgqtvla ggtsptvlas taasvgvlaa vvqtpgvsqf fgctplgpvg
     1441 wgiaagsalg atfangaltr lveqlpaarp daagghhgpd aagqagghgg
//
LOCUS       WP_357677014             261 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora rifamycinica].
ACCESSION   WP_357677014
VERSION     WP_357677014.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 261)
  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 261)
  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 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   4  (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   5  (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   6  (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   7  (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 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..261
                     /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=27593
     Region          2..202
                     /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 mrvlvtgagg tlgravlprl rtdgftvram srrprhdpaa dwvvadlgsg aglagavagm
       61 davlhlasha gggarthrvd vlgtrrlala aasagaghll yvsivgvdrv pvpyyrhkla
      121 aeqvlaagpv pwtvlratqf pvfldrllra asrlgpvpgd pavlaqpvdp hevaarlaer
      181 lttgpltgie eyggpqvlrf deavrawraa rrshrpllpv rlpgrlgrel ragglttsvt
      241 ptgrrtwaey ladtyggpdr r
//
LOCUS       WP_357677021             267 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357677021
VERSION     WP_357677021.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 267)
  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..267
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..267
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29968
     Region          12..71
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          83..261
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 meseptaeli raqlrrlrlh aelsqeefgk lvhfsgsqis aielgqrpfd rlflkradev
       61 lttgglltsl lrlaerysqp nwfrpwleae rqaqqlwcyh ptlvpgllqt enyaravira
      121 ddmlsddeve rrlavrldrq gvlsrsqppk liavveeavl rradesfrgl mvqqiahlle
      181 cvdqpnvsvh vipaevsthv glagpftlal gndsgwvghl enqlggttid kdgeltilia
      241 rwesvrseal phnqsallmk evmtsws
//
LOCUS       WP_357677019             244 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Micromonospora
            rifamycinica].
ACCESSION   WP_357677019
VERSION     WP_357677019.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 244)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..244
                     /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=26450
     Region          5..147
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mrqdeiwdae aarhydtpgt gmfaaevlgp tvdrlaalag egpalefaig tgrvavplaa
       61 rgvpvtgiel sapmiaqlrt kvdaqtipvv agdmatavap geyslvylvy ntianlltqa
      121 eqvacfrnaa rhlgdggrfv ielwvpelrk lppgqqavvw hsepgylgvd tydvlvqhvv
      181 shhfrfagsr qaelfrtphr yvwpaeldlm aqlagfvles rhadwaggef taesrshvsv
      241 yrlp
//
LOCUS       WP_357677042             293 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357677042
VERSION     WP_357677042.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 293)
  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..293
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32535
     Region          14..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..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mserrsptir rrrlgaelrr lrdgagitie vvaeqlecsa skvsrietgh tsatprdvrd
       61 mlriygvvga eseelvqiar earqkgwwhp hrsvlvgayv gleaaagsiw tyeqqvipgl
      121 lvteeyatam iqaarpelsa dqvqqrvrvr lgrqslltqd dpvdlrvvld eavlrrpvgg
      181 davmrgqlrr lvevaelsnv tlqvlpfevg ahagmdgpft ilgfpdsvdp dvvyaenatg
      241 glfleksdel qkykfifdqi qaaaerpees iahiaelaee plwkwrprgs prt
//
LOCUS       WP_357677101             295 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357677101
VERSION     WP_357677101.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   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 295)
  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..295
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..295
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31096
     Region          36..>180
                     /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 mrgfrwpppp dggprtwgpg pgaprtgrpa lpepetelva tphdvqlerl vtgvgepvtv
       61 fahgfgngia ttrpfgsavt grrvffqfrg hgrsdappgp wsyldlardl ravadlcgat
      121 rafgaslgag alcrllvesp drfeklvfll pavldrprgp iaqqrltdll davaggdasa
      181 vadvvalelp psvrntpagw shlrqrldql lrdglaagls elveqsplpd vaalagvtap
      241 alvigcvgdd lhpthiaael aaalpaatlh vydrpgfawt dradlreris tflnd
//
LOCUS       WP_357677125             137 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system VapC family toxin [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357677125
VERSION     WP_357677125.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..137
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=14174
     Region          22..132
                     /region_name="VapC"
                     /note="Ribonuclease/mRNA interferase VapC, contains PIN
                     domain [Defense mechanisms]; COG1487"
                     /db_xref="CDD:441096"
ORIGIN      
        1 mtrasatpgg tlvldsegla kavlrdrtvt awlalaradd lrvitsaatl vevvhprvnr
       61 palewtlsrl vvepvtepia rhaatllsda glhghkyaid amlsatalaa pgpvtvltsd
      121 pedlaalcgg rvtvikv
//
LOCUS       WP_357677131             225 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357677131
VERSION     WP_357677131.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 225)
  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..225
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..225
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25572
     Region          3..104
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mgssyhqfcp vakavellde rwtllvirel vcgterfnel rrglprmspt llsrrlhqlt
       61 hagiverhvk dndvryvltq aghelrpvve alaawgirwi gelgdedldp klllwdmhrn
      121 vdqtavpdgr tviefrfpda ppnsrrwwlv itcdevdvcd tdpghavtvt vtagvrsmve
      181 vwrgnlswsd alrlhavevq gpeairravp rwftlpewas vprpa
//
LOCUS       WP_357677161             189 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677161
VERSION     WP_357677161.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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..189
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..189
                     /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=21141
     Region          38..175
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 meptneleag vshdtdpees tvewqvartq aehgpdfdpd lltltltfyr amsafdraga
       61 aelavhglsv sqfnilnvlh radrplnmge lalaisirpa nltsvidglv qrsfverrin
      121 pddrrsylia ntetgerfla eflpshwryl ealiwrldge drrtltalla klrdsietar
      181 vdkgqvvst
//
LOCUS       WP_357677170             962 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357677170
VERSION     WP_357677170.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 962)
  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..962
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..962
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=103690
     Region          44..920
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msprihlpsg wvtfvftdie gstrlaqllg pdyrpvlweh rrllrdtlaa tdgaellteg
       61 dsfflafpda aaaltaclta qralsthdwp npeaaprvrm glhtgyaepr dgeyaspevh
      121 raarvaaaah ggqvlcsast arladpmpag aalldlglhr lrgfddrerl fqlvapgler
      181 qfprprtaea lahnlptqvt sfvgreterg eldllirrhr lvtvvgagga gktrlaveva
      241 sgqveaypdg vwfvdiaavt dpglvafaia avlgprpepg rpivdtlveh aalrrmlvvl
      301 dtcdaqpaac aevisrllag gvgvrvlats reafglpgev vwripplavd pqpgrtesda
      361 vallldrtaa arggrppewt eaadlrrvvq rldglplaie laaarlrvls asqlaarldd
      421 vlgtldagrg vpeppvdrgw agnqqdtvdl vaaasgqspp spahravqrs aterhltmqa
      481 tvtwsyrtlg prasrllrwl avfagpvdla tvewmlgdds ldplsvlvdk smmlaerhas
      541 gstyrmldpi rayaarrlve tgeehaardr hvawaqhalh rahlgadgrp vtlslyaldp
      601 lagelraalr wsatggsara glrlaggldq wwrerglsre arlwlfrlyg riaetgeaip
      661 eaelaaayhl hslhagadge fgeelrfsqr aeaaarqagd agllarvlag ravplidmeq
      721 fteaericre vidwadeqgv sgdallasyn laellwrrga lteaaellga vrlveatrpv
      781 ergrrsvdml lgmvalarrd lvaahehllv alrarmghgy hgracdtvna vavrcalgge
      841 pltaarlfga aqatrarlrg tpgifgtywl erqadlrrvl gdaafdaayg eggelgldea
      901 aalafavehp dmaadsvrfr ttgpvmpgpv mpgpmtprpm tprpmtprpi srrdadrree
      961 wa
//
LOCUS       WP_357677175             197 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357677175
VERSION     WP_357677175.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  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..197
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..197
                     /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=21931
     Region          9..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdiqvglrer kkaetrqavh eaalrltveh gfdavtveai adaanisrrt fsnyfagked
       61 avlygeeeli rvlvervrar paserpwqam rgaihdvyre vgtpdqgwaa rtrlarkhps
      121 llarqlanha alerelaevv taragtgdtg giqprlmaaa flvtlrvsth lwieeqqarp
      181 lnevmdefld qmalpfa
//
LOCUS       WP_357677217             249 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxymuconolactone decarboxylase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357677217
VERSION     WP_357677217.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11628473
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..249
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /calculated_mol_wt=25283
     Region          7..225
                     /region_name="ahpD_dom"
                     /note="alkylhydroperoxidase AhpD family core domain;
                     cl00460"
                     /db_xref="CDD:469777"
     Region          <162..231
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtgflgvppp taegrqvfde dvaevgyvmn lsrlwayrpa llnglfdlmg etgrvhgldl
       61 rgrgvlvaac asalgdsycs lvwggrlaae tdpltasavl redddhlslk qpptagghlt
      121 dgggladggg ftdgagladg gdlavggglt dgggladggg ltdgeramar warkvardps
      181 gtcaedvrsl reagfddaqi faitvfvalr iafstvnaal garpdaalrs ttpaavldav
      241 tygrpiaev
//
LOCUS       WP_357677210             444 aa            linear   BCT 28-DEC-2024
DEFINITION  TrkH family potassium uptake protein [Micromonospora rifamycinica].
ACCESSION   WP_357677210
VERSION     WP_357677210.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 444)
  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 444)
  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..444
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..444
                     /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=47723
     Region          8..439
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mrrflrhpvr lvpfgflvai vigtgllmlp watsahrytp lvtalftats avsvtgmnvt
       61 dtpnywngfg lvmitvltqv gglgiltgaa lvslavtrql glrnrllvqa estdygigdi
      121 rrllmhiagt vfgcelvmti vvtgrlwlty hyppgralws gvfhsvqafn nggfslyseg
      181 lvafardpwv alplslgaiv gglgfpalfe afrqrrrpgr wtvatkltiw gslvllatgf
      241 vgllvaewan pftigtydtp gkvlaaftqi alsrtggfdv invstlsees ypllialmfi
      301 gggsastagg ikvstffllg fviwaelrge pdvtvgrrri avasqrqalt vallsvalvt
      361 vgtlwltvlt tgvrfndtvf evvsafsttg ltiglaerls wsgqlvltvl myigrigplt
      421 lgsaialntr rrlyrypkeq pvvg
//
LOCUS       WP_357677220             823 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677220
VERSION     WP_357677220.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 823)
  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..823
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..823
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=89133
     Region          21..820
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mesdplraag vtpresqifw lvgdrlhnre iadslqvser tveshvssll rklggssrla
       61 lvdaavrlra rrepgtvlps plssfvgrar etddllglvg ahrlltltgp agtgktrlal
      121 rlaqsvttlp pavlvdlasv ppgddveraf adalgvsgde rrlrslirea laegrhwllv
      181 dncehvtgta aalladllat tghlhvlatg hgplgvagev vyeipplplp eevddppavl
      241 gaaagqlfad raaavspgfe vtpgnarhva micrrldglp laielaaari rffspaella
      301 rlddrfallt dgaqgrhrtl eealqwsydl lggderllfe rcavfpgefd ydtaaqilay
      361 pplgsadlvr lfprlldrsl isrrrrdett eyrlldsvrq fahrrlvsrg aagtareqha
      421 rhhlrhgval ladlrgrdqa gamrwfdrhw adlrtamrwa ldrpdtvaaw eflagvgtgw
      481 eilgargelf gwidrllerp lpdgslgvra avtcsvllay qdtgraltfa eqayeragdd
      541 tgpdralall algwvkmyge rrasaighle lavssfellg ddwhraltms alghatagta
      601 tcltltaqaa dlfgrlrdhv kranclnqma iraiedhsrl ddaalwlaea grlarlsgne
      661 herlhaevfr arldqhhgdh atartgytal lgqfrrigdr rctarcllgl graaasdgdh
      721 glarrhlteg lelavglgdp ravmtglcll aecdhatgrf eraatllgaa erldpelrah
      781 llpgnalhas lrdelgaaal aaalatghrt plpdllsser igr
//
LOCUS       WP_357677268             392 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677268
VERSION     WP_357677268.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=42084
     Region          161..386
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mshrawaava ssalvlalll lpvspaigll aavpaaigwa fvvawailrp sigtggswwt
       61 alpggaslaa tgfahatgyr gstdagmwgl vevaallvll tlvvrwnrgr glwvsgivta
      121 vaqiawisrf ipdedvgavl agcalwglgs asavviggyp rfaarrterm veaeksrqkr
      181 qlerdlhdyv ahdlsgiiaq aqaaqfvrds dperllaalr rveeaglram ssmdralell
      241 sgddpgsaet keeirrpdmr aveslvesfr qvsedvdvrl lvdgdvatlp revsetayrv
      301 tmealtnirr haknrawvrv evrmdpsggl flrvenaapr gpsrsliprr rggtglrevr
      361 artealggtl sagaspsgwr vsmnvpsrrt pr
//
LOCUS       WP_357677384              75 aa            linear   BCT 28-DEC-2024
DEFINITION  tautomerase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677384
VERSION     WP_357677384.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..75
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..75
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=7619
     Region          2..61
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mplvnvkvie gvfteaqkae iitavtdamv gvegeamrpv twvvveevks gdwaiggkpl
       61 ttedvkalaa gapag
//
LOCUS       WP_357677387             263 aa            linear   BCT 28-DEC-2024
DEFINITION  ACP S-malonyltransferase [Micromonospora rifamycinica].
ACCESSION   WP_357677387
VERSION     WP_357677387.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Marcella,A.M. and Barb,A.W.
  TITLE     Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as
            templates for engineering
  JOURNAL   Appl Microbiol Biotechnol 102 (15), 6333-6341 (2018)
   PUBMED   29858956
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..263
                     /product="ACP S-malonyltransferase"
                     /EC_number="2.3.1.39"
                     /GO_function="GO:0004314 - [acyl-carrier-protein]
                     S-malonyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27753
     Region          1..262
                     /region_name="FabD"
                     /note="Malonyl CoA-acyl carrier protein transacylase
                     [Lipid transport and metabolism]; COG0331"
                     /db_xref="CDD:440100"
ORIGIN      
        1 mgsglfaqfp ettaladeil gysieelctr dpdrklrdtr yaqpavfvan allgrqrvae
       61 qpddyrfyag hslgeynalc aagmldfeta lrlvrrrgel maditgggms avqgvpaafv
      121 qralretgls gvhianfnad tqttiagdrv evavaakaig alpgarvvpi nvsgpfhtpl
      181 masvepelrt alescafttg sgtvvssvtg avfpadqgae lltrqvstpv dwvravatlr
      241 algvtqfdev ngstlsalvn rir
//
LOCUS       WP_357677400             392 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357677400
VERSION     WP_357677400.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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 392)
  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 392)
  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 392)
  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 11468631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..392
                     /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=43792
     Region          25..372
                     /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          189..372
                     /region_name="RHO_alpha_C_2"
                     /note="C-terminal catalytic domain of the oxygenase alpha
                     subunit of an uncharacterized subgroup of Rieske-type
                     non-heme iron aromatic ring-hydroxylating oxygenases;
                     cd08886"
                     /db_xref="CDD:176895"
     Site            order(197..198,202,205..206,209,211..212,216,293..294,
                     329..331,333..337,345..348,359,362,366)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176895"
     Site            order(206..207,209..210,212..213,217,261..262,264,272,274,
                     283,285,315,318..319,323,327)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176895"
     Site            order(206..207,209..210,212..213,217,261..262,264,272,274,
                     283,285,315,318..319,323)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176895"
     Site            order(212,217,327)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176895"
ORIGIN      
        1 mtpdspstid hisagyhpdp alsmslhada ytdpkwfdvd qraifarswq wlchveklre
       61 pgsyvtgtva gmpivavrde agalrafynv ckhrahellt gsgvrrsivc pyhawnfdlt
      121 grlrrarntg dmpgfdtstv cldqiqvtef ggmvyvnldp taaplneqag dlqaeieara
      181 pdvakltlar rltytiasnw knvvdnflec yhchvahkdf vslvdmstyr vttygiyssh
      241 maqagkadns aydvtgatvt ehavwwlwpn tcllrypgrg nfmvlqiipd gpertheiwd
      301 fyletaepne aeldsiryid evlqvedial vesvqrgmrt paftqgkivy dpngsglseh
      361 alhhfhglvl dayrhelers gsapmkeitp ap
//
LOCUS       WP_357677430             152 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677430
VERSION     WP_357677430.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 152)
  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 152)
  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 152)
  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 152)
  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..152
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..152
                     /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=16724
     Region          15..>122
                     /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 mndhalvpdd favppylvtp qfrleplgpq hnpadhaawt ssiehiratp gfpdggwppv
       61 ggmtleanla dlqrhandfa qrrgftytvl etasgevigc vyiypspsee hdadvaswvr
      121 adraeldvpl yeavtawlst hwplgtlnyh pr
//
LOCUS       WP_357677468             156 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677468
VERSION     WP_357677468.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 156)
  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 156)
  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 156)
  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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..156
                     /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=17417
     Region          10..146
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mtkiplrrft aralpidddg rvlllhgfdp aepgrrywft iggaleeget lqeaaarelh
       61 eevgirapad eftgpygttt iefffdqyai vqdqtffavr vgrvevsfeh meeiekatti
      121 ehrwwsaeel dataeaffpe dlasilrkit gggapa
//
LOCUS       WP_357677484             560 aa            linear   BCT 28-DEC-2024
DEFINITION  NuoI/complex I 23 kDa subunit family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357677484
VERSION     WP_357677484.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 560)
  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 560)
  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 560)
  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..560
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..560
                     /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=57275
     Region          59..188
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
     Region          <200..545
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 maagyrpvla yigcgpmlwi tspkpvdscg kpgdrvscsf tcaakcamml nmgripgvgl
       61 akglsitlrh mlrksvtqqy pevkpalppr srgvialvee nctscmlcar ecpdwciyid
      121 shketipape ggrprqrnvl drfaidfalc mycgicievc pfdalfwspe feyaegdirn
      181 llhekdrlat wvptvppppa hdpgaeppke ltaaprrpga aparpassrr prpdtpappa
      241 strqpvddtt steqrppgtp dkhtpapstp ettssgtsis gtstpettss gsstsgtsis
      301 ettspgssts gtsisettss epltsgtass gpitsgtsts gslpsgapas gaavpgtats
      361 etapsgsapa ettsaetvss egaasedeps gavtsgdvsr gtassetaap atasqdqras
      421 eaegpesgas egtmseaegp gtgtaerams eaegpgtgta eramsearge aagsetggep
      481 sgagpdrtpp serpqngpss tgkpaeeels tasgeprpdp gskeqtagpr prrrrmadpr
      541 sirppgrldp dgtreseeds
//
LOCUS       WP_357677541             386 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677541
VERSION     WP_357677541.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=40754
     Region          1..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 mgarlsgldg irglaalfvv lhhcwllsfp gfpadtgpgw agwllyghfa vvifialsgf
       61 slavsparsg wrldslrrfa rrrawrilpp ywaallfslv vawtlvpqpg qpvptgktvv
      121 vyglllqdvf gspspngalw siaieaqlyl vfplmllavr rlgavamlga vtavvlavgl
      181 lapavppvet lmrltpqfav lfavgvvaar vvrtpsrlpl hwaallaavp vlaliavkgs
      241 ewtvagffwv dlalapaagl llaavaggrp rplvalldtr pvrslgsfsy slylvhapiv
      301 valnhflvap rlgpgvprfl vllavagpas vlfargfaav felpfqrhrs gpalraaard
      361 rlrsrrgpga ragdrtggqa gprags
//
LOCUS       WP_357677564             192 aa            linear   BCT 28-DEC-2024
DEFINITION  dTDP-4-dehydrorhamnose 3,5-epimerase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357677564
VERSION     WP_357677564.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 192)
  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..192
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..192
                     /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=20523
     Region          3..172
                     /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 mdplsvegaw vhaprvhtda rgafheafrt vglphpfdla qincsvsrrg vvrgvhfadv
       61 ppgqakyvmc vagrvvdvvv dlrvgspgfg rweavtldas epravliaeg lghafmavse
      121 ratvvylcsr pydperehgv hpldpglgig wpadveplls ekdataptla eavaagllpd
      181 yqvcrsfyst ph
//
LOCUS       WP_357677605             497 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677605
VERSION     WP_357677605.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..497
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51095
     Region          64..307
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrrilpavav aaclltgpat aatasptpaa apapapapap astptagtda sgvvpadlsa
       61 aevsfrgggg lamhgtvlsp agaktarpgv vlvhgagtgt praklmgeav efarrglsvl
      121 iydkrsegys lmrrsystla ddalgavaal rsqpgvdpak vgiwgfsegg wvapiaaars
      181 adiafvvlvg ansqsplrqq twavaaglrk agvsgalvdr aehnlyrvia dggmfpepyy
      241 dpeptiaalr rpvlaiwgvh dlltppkesp pgfvsalekg gnrhytirff adadhaahlt
      301 pdrgvtrlpe lapgyadlvg swigevtagr ppvaqtsgpa paqdsptlpt eppawwesal
      361 mqavalvllv agfaaypvva lvrrlrrrsl apvtraarll saggtavvlg gfsylfylvt
      421 tggklaspgp llagrplvwl vlqalsvacv vaavltaraw rraggsvpcg ervrlglllt
      481 gglvfvpwsl ywgllip
//
LOCUS       WP_357677590             268 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            rifamycinica].
ACCESSION   WP_357677590
VERSION     WP_357677590.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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 268)
  AUTHORS   ter Beek,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..268
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..268
                     /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=29189
     Region          1..261
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavslylaft rydiftppew vgldnfvrmf tddpvflrsa kvtleyvlig tpvklvaala
       61 vamllnsvtr gsgffrsafy apsligasvs vaivwramfa gggpvddslr ifgietggwv
      121 gdvdlaipmm vilmvwqfga pmviflaglk qvptelyeaa evdgagpvhr fwkvtvpmls
      181 pviffnllle tihafqvfgs afvisngsga pagqlnfitl ylykrgfadl qmgyasaiaw
      241 ivllvvavia lvmfrtarsw vyyagdnr
//
LOCUS       WP_357677607             187 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677607
VERSION     WP_357677607.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 187)
  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 187)
  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 187)
  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 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   5  (residues 1 to 187)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..187
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..187
                     /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=21804
     Region          13..80
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkdddrllld dparlkalah pmrrlmlrhl nvhgeatstt lgellgaktg ttsyhlrqle
       61 kygfieeipe rstgrerwwr kadvprdirl ptpdqlaped rpvlaefhrl gmeedlelfn
      121 rfpeayrrdp dwakgsrglg rmtkaefhdf yeayielltk yshrhedapp darplyirlf
      181 alpaded
//
LOCUS       WP_357677608             485 aa            linear   BCT 28-DEC-2024
DEFINITION  rhamnulokinase [Micromonospora rifamycinica].
ACCESSION   WP_357677608
VERSION     WP_357677608.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 485)
  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 485)
  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 485)
  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..485
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..485
                     /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=51229
     Region          7..453
                     /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 msavvdvaav dlgassgrvi vghlgagrmt lteayrfpnv pvrvggtlhw dilglwrgvl
       61 dglraagpvt sigvdswavd yglldaagal lgnpvhyrda rtegvaerva grvgeqrlya
      121 ttglqrlpfn tlyqlvaaag tpqldtadrl llipdlityw ltgrlgaelt nasttqlydl
      181 srrawatdlm aevgipatlf pplhapgvri gpvrpdlelp gtpqvvavas hdtasavvgv
      241 patgerfayl scgtwslagv eldtpvltea srranftnev gidgtirylr nvmglwllqe
      301 slrtwgtadl pdllrraade palrsvvdpd dpvflppgdm pgriaeacrq tgepvpdsra
      361 atvrcmldsl alahrrvvrq aqelsgrqvd tvhlvgggar nellcqltad acglpvvagp
      421 veatalgnil vqaraagavr gdlpalrall retqhlvryd prrdraaawa aadgrvggsg
      481 rgtaa
//
LOCUS       WP_357677627             497 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677627
VERSION     WP_357677627.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 497)
  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..497
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..497
                     /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=53155
     Region          25..128
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          240..470
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 maltlsqlla esvleltlvt psspdllqrp vrwvastelv dptpflrgge lllttgafid
       61 addhqawqaf irrlkaarip avgfgcglth hdvpralvec ataadlplla vpysvpfvri
      121 sefvadaiia drfkdmgras nlaaelaklv sngapiaall rqiaeeikge aaivdidgsv
      181 msswpthhel qpdlvlqgla tngttgyfav pldqagahdh ilvgrsemav etvrmamnsa
      241 atlvaidltr rlqeepssat rmaavlaglt dwttptatlv ralrvagfds daptvvlvah
      301 pnpafsagys lrlrlaveqv lpvvrsvrsg emlvllaqgg sgdatgtvle vlrrempsrr
      361 ivvagparda eeirmvlasa ramiapeqat pvrarafdlt sivaaaagrg gqhaarevlq
      421 plidydakvn gellhtlrty lrldarqhlt akalhlhrnt lryrlaqigk lldadldsld
      481 tllicnlacr mydaagg
//
LOCUS       WP_357677654             533 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677654
VERSION     WP_357677654.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 533)
  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 533)
  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..533
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56762
     Region          237..433
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpadaphrtq rrlsprelav iaslgtmilm acvwlwavss vpteakgvma mvggvsaall
       61 agataavvhy saagrrsreq arwasarltr lerevlqmae eslpalgrqv rggvsvadal
      121 srvaqppegp lrhllkaaan eldvlerert maqasrsame aeisrvtset lpdlvkriqa
      181 drmsvtaalt evrrpvhsql rdllgeaarq lgegerrgaa vmaacagaaa rvqaqatsll
      241 arlrgleely gdqeevfadl leldhriaql srladniall sggrsgrrwt rpivmesvlr
      301 gamgrvgayr rirlhststv avagyaaegv mhalaelmdn aatfsahgse vhvyvdeeda
      361 gvvitiedsg lgmrprerhh atklvsepld lrtlsgtrlg lavvgrlvdk ygltvsfrps
      421 arggtgvvvl iprllitqpr sdttappaie pssrpavtas vaaaiptqeg paeenedllp
      481 rrrrgqtlae agralqapva kpvregrdsa arfaafrqag argrgtspdp gds
//
LOCUS       WP_357677798             181 aa            linear   BCT 28-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Micromonospora rifamycinica].
ACCESSION   WP_357677798
VERSION     WP_357677798.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 181)
  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 181)
  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 181)
  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..181
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..181
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18800
     Region          23..>156
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mpiltmpldg papptgatgp iqdrydrqvr afgphvqrrl aeltvavvgl ggvgsqvvqs
       61 lahlgvggll lvdpdtvaat nlnrligakp advaraatkv tvaartvrti npqvrvrgia
      121 gsildpvvwq qmrpaevivg avdghaprwa lnrlavsvrp llsrrrsrag tgtppgaarl
      181 p
//
LOCUS       WP_357677823             276 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677823
VERSION     WP_357677823.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 276)
  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 276)
  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 276)
  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 276)
  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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..276
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29546
     Region          88..266
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mkilpaiavl ltgcatsaeg paagtdtgta dpavvrtdag avrgtatgty rlyqgiryat
       61 aarprqdphp epdrgrpagt aqwlavtyda vlcdldgvlr rfdhtvqaei earyglplmk
      121 tafdpallvp atlgrvtere waesivvalg gderarrava efvevpfrvd eevrlllara
      181 qermpvvlvt namdtleehl erlgltyfad dvvssarvgv akpdrriyei aaeragaape
      241 rclfvddrla nvegaralgm tgvhfrtaad laaalg
//
LOCUS       WP_357677844             386 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677844
VERSION     WP_357677844.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..386
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..386
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41788
     Region          86..371
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 madlqrtvde laarldrpll ledhlqrvva yseqsgamdd irrdsilrrh ttpevrawlr
       61 asgidgaslp lrtpgapdlg llprvcvpvr hdsgllgflw fidapvmsdt qvaeaaaaap
      121 glalalfhes latglashre leavtglllg ernaalqlie agafpqaqpv tvlvarplaa
      181 epdqalrlal eqgllalrrr lsghhplhlv rydhavllta gpaaspeelh aampvpvavg
      241 igrprpalaa asgsyvearh aaevaarvpg lgrslewtrl gvyrmlthlq qhelhpglep
      301 lladahhlpl letletyldl agsavatsra lrlhrtslyy rlrrveelar tdlkdggerl
      361 alhlslklar lsgrylprds rpptpt
//
LOCUS       WP_357677855             698 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora rifamycinica].
ACCESSION   WP_357677855
VERSION     WP_357677855.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 698)
  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 698)
  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 698)
  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..698
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..698
                     /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=75905
     Region          10..692
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mrgnsaldns tasaaiseeq efldqatarr dkladqlltg lsvealdale rarlrmlrqq
       61 yeelrrateg lvfgrldgld gtvrhigrvg lrddeddepl lvdwrapaar pfytatavdp
      121 qglarrryir tagstvvgvd depldgtltt dlvgegalla aldqrrtgrm staistlqre
      181 qddiiraeag gplvvqggpg tgktvvalhr vayllfahpt maeqavlvlg psprfleyig
      241 qvlpalgeta vvaatcdtll pgisvgrdes ralaeikgra lwqpaledyv asllprardl
      301 klrwegefyv ipaatvaqal aavrgrpyhq arrvfteqlh hilaeavvdq realmnemee
      361 gfedilarvd rsmrydpgaa agsdadglls deevddlrqr iaanvaiarf veawwptlda
      421 etllrdllad edllarfalr lsaaeiaavv aepapwassd iplldavadl lgdsdapqqq
      481 gefiadrarr qrgwvyghva vdeaqelsem qwhmvvrrcp srsitavgdi dqaeaahrht
      541 swaqavqavl gdrwtpaelt icyrtprevm eltapvlrra gshnapprav rasgispwer
      601 tvtpaelgda aaeavrelre rwhggtvgvi apvgriaelq aavdddvpvl saaqskglew
      661 datllvdpdg itaeprgwng lyvaltrctq elgqlvla
//
LOCUS       WP_357677873             370 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357677873
VERSION     WP_357677873.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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..370
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..370
                     /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=41158
     Region          1..362
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkfvvqvrlf pepaqeaala dtlrlcneaa nlvsriawet kvfrnydlrl haygelknmg
       61 lsaqpaqhvi kkvadayvtv kaqvkaklrk plakpigfrt daaqpfddrc lswqveertv
      121 siwttggrmk gvrfgcsekq atalaayrkg esdlvhrdgm wlliatcdvp dtdvtepdgf
      181 lgvdlgiani attddgkrys gkhlnavrhr drelrrrlra kqtksakrll karrrkesrf
      241 ardvnhvisk sivteaertg rgvaledlsg irdrvrlrkp qrvtlhswsf hqlgrfvayk
      301 aaragvaviy vdpaytsqgc sacghidkrn rpsqetfact scgfaehadv naarniakrg
      361 vagwavshaa
//
LOCUS       WP_357677884             199 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357677884
VERSION     WP_357677884.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 199)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..199
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..199
                     /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=22396
     Region          9..193
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mtpgfsrlrr edllktacev iaergfghtr tldiaraagv sqallfyhfe tkdrlfaqaf
       61 dyaarqhret laeierlerp pldrlrtllr rcspngspdg wrlwidawae amrsqdleet
      121 srgldeqgrt vlrgiiedgv asgdfvcanp edaawrifsl idglaihthv hprtlsrrri
      181 thlvrtaaaa elgltptdl
//
LOCUS       WP_357677885             559 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Micromonospora rifamycinica].
ACCESSION   WP_357677885
VERSION     WP_357677885.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..559
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60644
     Region          16..550
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mgyvdvaavg hilpdgrelf advsfrvgeg akvalvgpng agkttllrmv agdlpvrtga
       61 iarsgglgvm rqfigmigde stladlalsl appalrdagr rladteqamr aaelrgkyst
      121 aagkaqlaya dalaawgeag gydaevlfdt vtttvldlpw easrdrpvrt lsggqqkrfa
      181 lelllrgtde vllldepdnf ldvpgkrwle qrlresaksv lyvshdrell arsadrvvav
      241 eggsawvhpg gfaswhdart arharldelr rrwdeehqkl relmlmykqk aayndglasr
      301 yqaaqtrlrk feeagpppvp pkdqdirmrl aggrtgkrav icerlelegl typfdlelwy
      361 gdrvavlgan gtgkshflrl larggsdpdp angpvdgaaa lapvahggav rlgarvrpgh
      421 fsqthdrpel maktlvealw rgdehregmd rhaamaalsr yelagqgdqr fgtlsggqqa
      481 rflvlllels gatlllldep tdnldlasae aleagltafa gtvvavthdr wftrsfdrfv
      541 lfrgdgdvve tpepvwdvg
//
LOCUS       WP_357677904             499 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677904
VERSION     WP_357677904.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 499)
  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 499)
  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..499
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..499
                     /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=55634
     Region          3..457
                     /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 mgpkvaivga gfgglcmaiq leragidsyt vfekagdlgg twrdnsypga gcdipshlys
       61 ysferygswt rrypeqpeil gylehcadky dvrrkirfns evvsavfdga ewqvstappa
      121 aatrpitgsp teppaeppme pltesfdmvv msvgqlnrph lpdipgmsdf egtsfhsarw
      181 nhdhdltgrr vavigngssa aqfipriaqr vehlsvfqrt pnwvipkpda tfgpiarlaf
      241 hyvpglqray rewiyryaea tlypalsqgw svgllkqral rhlrdqvpdp alrakltpdy
      301 ppgckrvvid stfypaltrp nvdvvteklv ritprgveta eslhevdtiv yatgfrttef
      361 vapirvvgrq grdlaeqwrg gaaaylgisv pnfpnlflly gpntnlghns iifmlecqvn
      421 himaclpyis tlgpmevrpe amaawtrrld tamsrmvwgn gcqswyktae grvtnnwpgp
      481 tplyrrltam pprrayrpv
//
LOCUS       WP_357677977             219 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357677977
VERSION     WP_357677977.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=23363
     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 mriaiagaga vgrsiasell enghevllvd idpkaikidt vpraewllad aceiasldea
       61 gfndchvvva stgddkvnlv vsllakteyg vprvvarinh pnnewlfnes wgvdvavstp
      121 rllsalveea vsvgdlvrlm tfrqgqanlv eltladdapv vgqragsvpw pvdsalvail
      181 regrvlvpsd ddpleagdel lfvanqeveq elahllsqh
//
LOCUS       WP_357678026             420 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678026
VERSION     WP_357678026.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 420)
  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 420)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..420
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42724
     Region          17..407
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mskvkelpge alvtaassps ianssrayve rirggdmgal pavfglvvlc tafalarpsf
       61 ltainfanlf tqgaaitvia mglvfvlllg eidlsagfts gvcaavlavt ltdmgmpwyv
      121 avlaaivsgv vigtmlgtlv akvgipsfvv tlaaflafqg lalvlvnegt nisindpvik
      181 aiaqrnlppa lgwalyaacv aayalvqivr srkrarrglv sepisliaar vgalavigga
      241 avyvlnlers fnpefasltg vpivvpvilt llvvwtfvlr rtafgrhlya vggnaeaarr
      301 agiavdriri safvicssma avggiiaasr assvdpntgg ssvllyavga aviggtslfg
      361 gkgraldail ggaviavien gmglmqygas vkylvtgfvl llaagvdala rkraaaaglr
//
LOCUS       WP_357678030             552 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 27 protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357678030
VERSION     WP_357678030.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 552)
  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 552)
  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 552)
  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 552)
  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..552
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..552
                     /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=58038
     Region          46..308
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(53,88..89,130,164,166,199,218,222)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          320..395
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          428..551
                     /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(439..442,452,454,457,461..462)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(448,481..484,494,496,499,501,503..504)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(467,471,473,477,481..483,494,496,499,503)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(524..528,537,539,546..547)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mfrrrvallf pvllaaslgt avvtgavvls gappaqalen glartpqmgw ndwnsfgcnv
       61 netlirqtad tlvssgmaaa gyeyvniddc wstkqrnasg dlvadpvkfp ngmkaladyv
      121 hgkglklgiy ssagtttcag ypasinyeqr danlwaswgi dylkydncgd hlgrngqqry
      181 tamrdalaat grkilyslcn wgqesvwtwg aavgnswrnt gdiggnwnsi mgildqqvgk
      241 dsyarpgawn dpdmlevgng ptetesrahf slwallnapl lagndlrtms aatrtiltnt
      301 eviavnqdwg grqgykisds gdlevwrkpm ssggvatvll nrgggtatvs ttasalglgs
      361 assyavrdlw ahstststgt isasvpahga amflvtgggt pppttppptt pppttppptt
      421 pppgtttavr nvsagrcldv ngatqtngaa aivwdchgqa nqswtstssq elrvygtkcl
      481 dvnnagtang tsviiwdcng qsnqkwrfnt dgtvtavgsg rcldlvgngt angtrtqiwd
      541 cngaasqrws rg
//
LOCUS       WP_357678034            1082 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357678034
VERSION     WP_357678034.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1082
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..1082
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=114747
     Region          1..1062
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 magllsgegg hrtrpegalr lqilgplrar rggveldpgp rqrayllvll laraggpvst
       61 telidlvwgd dapasavnvi hkyvgalrrl lepglppraa gsylhrhptg yrlsasaetl
      121 dlmafrehvg aatahlargr dgaaldayvr alalwrgpag dghphrpgav alfsaldgef
      181 ltaavtaael avasgqphqv laplrlaatm aplhepvqag lvtalaaagq qaqalavfra
      241 vradlaeqlg vdpgpvlwqa yhrvsgrast ppaprtpagg glvgragela alrhataaaf
      301 aggtglvlvq gepgvgktrl lreataeaeq rgalvvwghc ldgggtpsmw pwvqairgil
      361 dglpaaqrdi pvgrelgsll eprpdvlaap vlpdngfpfr lfeqvvaiva aasaqrptvl
      421 alddlqwgds aslhlvghla trlpggtali galrdraptp gsalsrmlat vsrlpghqrv
      481 hlgnlneaev aelirretga aptadatrgi lsrtggnpff vrelsrllad rprgragvpa
      541 tvrdvvvdrm sgldagtrdl lriaaligrd velgllaraa gldldgcler lepvqalgml
      601 esrpddpfsl rfahdlvrea vtattrptqv gqlhlriada lertptgatp aqpdrggpea
      661 etvaerlghh lwsagllaep artvralvga grhaagksal dvaerrlraa vqvartagla
      721 egelsalaql tavlgmrsmy gfsvtdller aehlarglgl ereaasflys rwaalvqave
      781 ldrsaplarr lrrrgeesgd pwvlacglha wglqqwdyge igeairwldr srdmifdipr
      841 rdedpvrhdl qllmaamlae vttlhgavad grtlldgied lagedpymvt vwacaatria
      901 vivgdpalal rasgrgiavd pgfsfvflgt yqrlarcwal avtgrdpign adrarqliaa
      961 hlldpprsdv aawhgllaem liaggaveaa ataldradfy lescgqrhpe glllllrarl
     1021 lqargepvev vraaaerara vsadrgaflh thraerllae latrparrrr paaggcrper
     1081 rr
//
LOCUS       WP_357678053             305 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357678053
VERSION     WP_357678053.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=32245
     Region          1..302
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mslslnqwtt rrwsvaeavd gcvrhelaav glwrekvaeq glaetvrlvr eaglrvsslc
       61 rggfltgsgp pgeedrrafa ralddnrrai deaaelaaac lvmvvgglpg vrpgeplpas
      121 svshepaadg sapgppgfsr dlagarerva ealevlapya gergvrlale plhpiycpdr
      181 avlstlgqal dlclahppeq vgvvvdtfhv wwdprlfddl araggriasy qvcdylhplp
      241 adallgrgmm gdgvidfgpi travtgagyt gdveveifna dvwaadpdev vatmkaryaa
      301 lvpvg
//
LOCUS       WP_357678103             125 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357678103
VERSION     WP_357678103.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..125
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13712
     Region          18..114
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msqyehtcli rgdggrtira ildricnkwt llivatldgg alrftelhqq ipgisqrmlt
       61 ltlrhlerdg lvsrtayaev pprveyaltp tgkslippal alagwaiehv phieasralh
      121 qdksg
//
LOCUS       WP_357678118             319 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora
            rifamycinica].
ACCESSION   WP_357678118
VERSION     WP_357678118.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 319)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..319
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..319
                     /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=34691
     Region          59..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 msdlpliqad havaspapta psrggrgrrl rllsrtdrvv itlmvvvpll lvvalvwlpa
       61 latvalsgtd wdgigplgdi dwvgarnysd viniyppfvp amqnnllwla alfvvatpfg
      121 mflavlldke irgsrfyqta lylpvvlsla ligfvwqliy srdqgllnav lgsqtdwygd
      181 pnvniwavlv aagwrhvgyi mllylaglkg vdpslreaas vdgasetstf frvifpvlrp
      241 iniivlvvtv ieslrafdlv wvinkgrngl elisalvtqn vvgeasrigf gsalatimla
      301 vslvfitiyl avvmrenrr
//
LOCUS       WP_357678163             762 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678163
VERSION     WP_357678163.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 762)
  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..762
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..762
                     /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=80434
     Region          27..283
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(27,51..52,85,90,95..98,110)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(34..35,37..40,42,55,57,93,109..112,116,118,155,157,
                     159..160,162,171..172,175,192..195)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(34..35,37..40,42,55,57,93,109..112,116,157,159..160,
                     162,171..172)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(38,116,118,155,157,159,175,192..195)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(171..179,188..195)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <193..496
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 maadrvlsgp gaegnasqsq grligrryrl mspvgrggmg mvwhahdvll dravavkeli
       61 lpfgldntgk qiahrrmlre arsaarlthp givtvhdvve edgrpwivme lvrawsleqa
      121 vrqsgplpvi qaaeigirvl dalrhahaag ilhrdikpgn vlltadrvvl tdfgiaaieg
      181 dvtitqtgll mgspayippe rlsgqpitqa adlwsfgatl yaavegrppy egpdaiavlg
      241 avltqdptrp qragallpii erllrknpae rltaeqvsea lervlhahgs vrprtpetqp
      301 slptqadstp mallppfdas sgpmpsrive tpsgpvrvpy dpasgppdtp damsspsggq
      361 fpppprpdgf daftshsgpl rapespsgpl rlpeppagar ppfggpagag dpamppfggp
      421 sgphptlepr elgdpsgphp vpnpprelga psgshpipnp prefggpsgp hpvqspppgp
      481 ggpggptgph svpdrpagpq pilplttdsr avpwplatdd dlrdhsrals rdvprsrlaa
      541 rpsvpdrttr srrrpeaggg nawmrdgrpt arlilasvaa vgtvavaial vassrspepv
      601 vstplasasa saqplqaavp dgytkhtppg fsaavpdgwk ltasageatf tgpkdsglri
      661 lveqttpqpd gglselgree adggregyiq vqlqatqfrt wkaadweyty tlpngvpmha
      721 ltryvtiddd taykitfdmp eltwddqaks rkvfldtfrq tt
//
LOCUS       WP_357678211             288 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678211
VERSION     WP_357678211.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 288)
  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 288)
  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 288)
  AUTHORS   ter Beek,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..288
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..288
                     /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=31820
     Region          2..286
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mrhrlrdpat gllfvlpalv lflifrifps lgaagmsltd wniggewsfv gadnyarlld
       61 dvnfwlslrv tlvygaiyvp ltllvslgta lllnqvvfmr glfrgmlflp yvtsfvlagi
      121 iwrwiyefdg linglldkag lgpvafleqt slvlpalavv svwkgfgysm lillaglksi
      181 pasyleaatv dgasawqrfr sitlpllkpt lffvlvieti safqvfdtiy vmtgggpara
      241 tytliygiyd hgfrsfdfgy aatwgmvlfa ivlvvsliqr rfldrgnt
//
LOCUS       WP_357678212             596 aa            linear   BCT 28-DEC-2024
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357678212
VERSION     WP_357678212.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..596
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=62517
     Region          4..285
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
     Region          312..592
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mareftrvgv vglgtmgagi vevfarngvd vvaveisepa largratlar stdravargk
       61 laeadrdalh srvdfqvgld alhavdlvve avpehldlkr rifaeldrvc rpdtilatnt
      121 sslsvtdiav atnrpqqvvg lhffnpapvm klvevvrtvi taaevvddve alcarlgkva
      181 vtigdragfi anallfgyln havslfeary vtredldaam rlgcrlpmgp lalldligld
      241 tayeilntmy rrggrdrrha papllrqmvt agllgrksgr gfytydkpgs skvvpdewtp
      301 aatpadadga revtrvgvig agtlatglvg lfgragyqvv svtggaeesi giggavrdsl
      361 deevrrggld gadrdaalar itwaatldql advdlvveaa tggpgveqtl fasldeickp
      421 gvllattcss lpvievamat tgrpadvfgl hfvdpaaavp lvevvrtvrt saeatatara
      481 vcaalgrtav vcgdragfvv dallfpylnd avrmleagya tadgidhamt lgcgyptgpf
      541 alldaigldv alaaqralyr esrepglapa pllehlvtag ylgrgtgrgf rdhtgr
//
LOCUS       WP_357678247             182 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678247
VERSION     WP_357678247.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 182)
  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 182)
  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 182)
  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 182)
  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..182
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..182
                     /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=20365
     Region          10..177
                     /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 mssstylaqg prvavrrlcl qdheqllplh resvemyrsw mpgapittye afrdylkrfd
       61 epghegfvfc lrgtgavvgr vninnivrgt hqcgtlgyas yasttgrgym teglglimgl
      121 afgelglhrl eaniqphntp slnlvkrlgf rregyspafq yingawrdhe rwaitaemae
      181 dt
//
LOCUS       WP_357678288             194 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357678288
VERSION     WP_357678288.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 194)
  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..194
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..194
                     /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=20402
     Region          3..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mirraprthg eilaaaarrf avtgykgtsl qdiarevgcs kaavlyhfgg ketllaelma
       61 gpisvlceld erisslsgaa aqraaaegfv dlavrfrgei allrgefpel laqpafahiq
      121 riserlieam tgpdggqdar vaalvllagi aegcgafadi pdeelrpall avaqrvlvtp
      181 appppptpdh qhqd
//
LOCUS       WP_357678334             268 aa            linear   BCT 28-DEC-2024
DEFINITION  Fpg/Nei family DNA glycosylase [Micromonospora rifamycinica].
ACCESSION   WP_357678334
VERSION     WP_357678334.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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..268
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..268
                     /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=28886
     Region          2..268
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpeghtihrl aarhaelfag dkviasspqg rftegaavls gtvldgteay gkhllhhhad
       61 ertlhvhlgl ygrftdgdge ppvpvgqirl rlasdrhwld lrgptacell tppevaalrd
      121 rlgpdplrad adpdrayari rrsptplaal lldqsvvagt glifvtealf raglrptlpg
      181 rqltpggwaa lwadlvalmt lavargridt vrdahlpgam grparvdrhg gevyvyrrpg
      241 epchvcgspv srsglagrnl ywcprcqp
//
LOCUS       WP_357678361             110 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357678361
VERSION     WP_357678361.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..110
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12490
     Region          1..96
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrealdrvgg kwsigillaa spgpvrfsel errvegisrr mltltlrnle rdgllhrray
       61 ptvppkveyr atpmamelye plvaltawaq rhrsaisear aaydrehdrp
//
LOCUS       WP_357678382             418 aa            linear   BCT 28-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357678382
VERSION     WP_357678382.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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..418
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..418
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43371
     Region          7..388
                     /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 masltavarg glagvtgatt salaqfllvv vvtrafsaeq agafftatal vlmaagvarl
       61 dagnglvyfi araradeylg vsgyiraall psvivalvat valyprlgpl alavpvmvaa
      121 dillaatrgf gamrptvfld gmllpagqll lvsatavvaa pgrlpvawal pylpvlvlaa
      181 tslrgrvprt rylpgtardl wrytaprsva gaiqavfqrl diviiallgg paqaavytaa
      241 trfkvvgqla nqglaqavqp rlvraladge lararelyqv ttvwlvmltw pvwlgyaala
      301 pwllrlfgse ygsavpvalv laatmmvata cgmvdvvlta aghttaslln lvaataitia
      361 ldvalipahg algavlgwsg gmlaknllpl wqlhhryglr pfgrhslgal rirswaaa
//
LOCUS       WP_357678538             226 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Micromonospora rifamycinica].
ACCESSION   WP_357678538
VERSION     WP_357678538.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=23949
     Region          6..201
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mapltladel vllayddegv nrlgrpqldy glsgavllel tlagrvevvd drlvvtdptp
       61 tghpvldaal agvaadgrrr rpkdwisrla kglpdrvlag lvdagvlrre sdrvllvfpr
      121 trypsptgae pvaetaarqr mvdalladgp veartaallg ltravgldrk lfrelpkerl
      181 kartteiaag dwasaatkka ieetqaaimt attvattaai itttts
//
LOCUS       WP_357678571             380 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678571
VERSION     WP_357678571.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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 380)
  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 380)
  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 380)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 380)
  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..380
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..380
                     /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=41842
     Region          <21..375
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mslhplpppk kptglgrlpv arwfiatgva atlalvggiv ltivmidavr eanprpavev
       61 qldrlnvalv vlfvvavaga lgltfiiqfa vlrpiaqlte qvrkvaagdf dhrlqvdrpa
      121 elaelsshid amrrrvvaaw rtaedqadel rrsngeleqf ayvashdlqe plrkiasftq
      181 mleqrygdql ddrakqyihy svdgakrmqs lindlldfsr vgrvtgervv tdtgealrla
      241 ldnlsaaied tgasvtsdel pkvignrlql tqlfqnlven avkfrsdlpp rvhlgvrrag
      301 emwefscsdn gigveakyad riflifqrlh prdvypgtgi glalcrkivd fhggqlwldg
      361 dadglgttfr wtlpatgeae
//
LOCUS       WP_357678670             332 aa            linear   BCT 28-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357678670
VERSION     WP_357678670.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 332)
  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..332
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..332
                     /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=35262
     Region          186..283
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mqenpgpqip ygprppewpa ahpyppapqp tpwflptprg arydqlartp darlwrqivg
       61 titvaggfll igvfvvvaga vvatmagisa pmrvgryfgd pvfemvvlll sialvlplvf
      121 gtaalvqrrr pgtlssvagr lrwswllrfi algvlalalg qaaqvvalvl tgeeaselfg
      181 wvgwsaflpa lvaivllvpf qaateeylfr gwvlqafgah lrnpvwgili gagifaslhg
      241 ytwvglidvf afgvvmgwla vrtggleaai alhvvnnmva fglsaaagkl eealqqgavp
      301 wqslagtvvq lgvftvgvly lskkrsisti sg
//
LOCUS       WP_357678683             333 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Micromonospora rifamycinica].
ACCESSION   WP_357678683
VERSION     WP_357678683.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 333)
  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 333)
  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..333
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..333
                     /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=36003
     Region          119..332
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mppqrhvqgq sparpavfrr varrlltvva avavgagmla vpasaaptpe eieaaldkqw
       61 eqleptiesy nkvraqlkvn rkksaelqkk ieplalqsel algrvgdlas ryyksgpsqe
      121 lsallttskp gtlaaqltil drlaaeqrke veavlvvrrk ydaekqklda liaaevqqek
      181 dlatkktkin aeikrlqaam pkstvkvngc ptingvlssa artairvacq qvgdpyvwga
      241 tgpnsfdcsg ltqfaykaag islthftgaq wnegkaisrs earpgdlvff fsdlhhvgly
      301 lgndmmvhap rtgkpvqvts inympvagfr rpg
//
LOCUS       WP_357678701             299 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678701
VERSION     WP_357678701.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   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 299)
  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..299
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..299
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=31905
     Region          31..290
                     /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 matepiphwp grtvgavhvr stpggapeqa vfvhglagsa tnwtdlmdel kdvvtghaid
       61 lpgaghspaa adgdytvagh aravielmeh tgpahlfgns lggavsvkva adrpdlvrsl
      121 tlvspalpdl lprygpfrva aaatpwlgew vtdrlrllsa eqrvnaslam vwanvsavhp
      181 vrlseaieel rrrddlpyav qamlgsargi vaeyfrrgad nlwshaarvq aptliihgrh
      241 drlvrpamaa kagrtfrqvr lvllpraghv ammempgvva fearrliaet rlgnaplas
//
LOCUS       WP_357678712             265 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Micromonospora rifamycinica].
ACCESSION   WP_357678712
VERSION     WP_357678712.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 265)
  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 265)
  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..265
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..265
                     /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=26811
     Region          1..249
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mnrwrsligr taaamvaita gslvltapat aapiadpaps vvggtraaqg efpfmvrlsm
       61 gcggalyspr lvltaahcvn rtgtntsita tlgavdlqss sriqvksnyv yrapgyngsg
      121 kdwalirlat pvtsqatlpi atstaydsgt ftiagwgaar eggaqqryll katvpfvsda
      181 scsasypgdl iaaeeicagy asggtdtcqg dsggpmfrrd aanawiqvgi vswgdgcarp
      241 napgvytqvs tfassiasaa aslgg
//
LOCUS       WP_357678783             312 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357678783
VERSION     WP_357678783.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 312)
  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..312
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..312
                     /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=34735
     Region          39..278
                     /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 mkdrpqdlde hdlrpvlsew giqpaaldya pvgfgdyhwi atdtdgrrwf vtaadlrlke
       61 qdgeaalrra mdtadalrel dfvvapvrta hdetvrlvga ryavsvfpyl dgvsgffgqe
      121 ltpahrgqvv dllarlhgaa pparcpvlrp epalralleq aieesdqswe agvfaraaga
      181 lvaghaaglr rrlaefdhla rkvdrselvv thgephpgnl mwsgdrcllv dwdtvglapp
      241 erdlwmfaed laryedtsgr rpqqaalafy rlrwalndva ifvdqfrrsh ertpdteqaw
      301 aafagtveel ta
//
LOCUS       WP_357678800             279 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678800
VERSION     WP_357678800.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..279
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29581
     Region          59..229
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mvvtlacgtl alspaahaag pyergpdptd sileasrgpf stsqqsvssl svsgfgggvi
       61 yypndtsqgt fgaiaispgy taswsslswl gpriashgfv vigietnsry dqpasrgrql
      121 laaldylved sstavrsrid asrlavaghs mggggsleaa ddrpslqaav plapwnltkn
      181 wsgirvptmi iggesdsvap vathaepfye sipassekay melngashff pqttntptgk
      241 ymvawlkrfv dddtryerfl cpaplrsdie eyrdtcphs
//
LOCUS       WP_357678831             398 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678831
VERSION     WP_357678831.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 398)
  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..398
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..398
                     /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=42341
     Region          3..397
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mirslivvgg gqsaavairt lrrrgydgsv lligeehvpp yqrpplskey lageaepgel
       61 tlldpgwcaa ndvelrlgvr aesvrgpevr laggatltad alliatggrp rrlpgleger
      121 vrylrtvada drlrddlkpg arvivvgagf vgsevastal argaevtvle clpnplqril
      181 gdeigracaa lqrasgvdlr tgvtvtgyae tgqgavvttg tgetaegdvv vvgagmvpnt
      241 ealdgfaldd gvlvdehcrt svegvyaagd varhyhplyg rhvrvehfdh asahgmaaak
      301 nllgratpyt aphwfwsdqf drnlqyagha drwdeivvrg sldeldfaaf ylregrleaa
      361 fgmerggeva varqliaarv tpdprvlade dadltdml
//
LOCUS       WP_357678851             361 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease [Micromonospora rifamycinica].
ACCESSION   WP_357678851
VERSION     WP_357678851.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 361)
  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..361
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..361
                     /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=39967
     Region          125..192
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
     Region          <250..>352
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
ORIGIN      
        1 mpywlesdsf gdepvwdvla ggnadlvdhl qaaycrlkak ashtrkngyl teqtaqrsar
       61 rrkwldllct tvldeqplih rpgddcsclg dtwiegyayr lhnflrrnps sseyernraq
      121 kadlrsaplk amvysrdags crycrsgpls akagrsrdrr kvltfdhvdp dipagadgan
      181 lvvacgrcne hkgrrtpyea dlvllpepta aeriawadrg qvlndipdqr pitdetaseh
      241 rsdadpnsep itdrsddrng dpidnpteev cpnngdeqpe qrtprfegga gegrvgprad
      301 hpgprrhpth ptqparapda pdvyhrrsra papadpyiwp pgsvpanptp ptgghhrddt
      361 p
//
LOCUS       WP_357678872             114 aa            linear   BCT 28-DEC-2024
DEFINITION  GerW family sporulation protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678872
VERSION     WP_357678872.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..114
                     /product="GerW family sporulation protein"
                     /calculated_mol_wt=11703
     Region          1..>37
                     /region_name="YtfJ"
                     /note="Uncharacterized spore protein YtfJ [Function
                     unknown]; COG3874"
                     /db_xref="CDD:443082"
ORIGIN      
        1 mnimelleqs kdaatvkrvf gdpiqqgdvt vipvarvgqg ggggmgsgkg ehaeqggggg
       61 yglsatpagv fvlkdgdvsw rpavdvnriv lggqvvavvl lltvraivrk rrrr
//
LOCUS       WP_357678901             325 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357678901
VERSION     WP_357678901.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 325)
  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 325)
  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 325)
  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..325
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..325
                     /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=34191
     Region          18..323
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mttgtrvaav raamaeagld alvlrpspdf rflggrhgpy lvvtadalae tadpgrllpa
       61 gvrrvgvdpe mrvrelfala ieaelvpaav vleplrlrke preveaigra agaaeavlgq
      121 vrelawfgat eramaarlrm llletgceev lslrvaageh tarpdhlpde rvinpgdall
      181 vslcarwdgy caevarvfav aeppedfeam ysvvlaahga alrsvgrsat aaevavtird
      241 vidgsgyghf aaarfgrgig lghdegpelr pgdgtalepg mtlclepaiy vpdlfgarla
      301 dvvactpdgp laltttphal hvldr
//
LOCUS       WP_357678966             264 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357678966
VERSION     WP_357678966.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..264
                     /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]"
                     /calculated_mol_wt=28635
     Region          33..158
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mdavythghh esvlrshrwr taansaayll phlgpetnll dvgsgpgtit adlatrvghv
       61 tacevteeal altraelaar gtanasfava dvhalefadd tfdvvhahqv lqhvgdpvra
      121 lremrrvtkp gglvaardsd ysafawyprl paldewlaly qrlarangge pdagrrllsw
      181 aqaagfthit ptsstwcfat pedrawwggm wadrilhsam arqalstgta tpatlrrisd
      241 awlewsgtpd gwlsilhsei lcta
//
LOCUS       WP_357679012             181 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357679012
VERSION     WP_357679012.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 181)
  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..181
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..181
                     /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=20987
     Region          1..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mredtrtriq eialrlfteq gyeatslrei aeelgvtkaa lyyhfktkdd ivaglvdlrv
       61 aeieellawf raqprtpear rqlvlryadq lkrsrymeia rflernqtal rehpkllrmr
      121 evmlelttrm sepgdplatr isrsmalftl hagkwmahde tlsedeitda svevalrlle
      181 a
//
LOCUS       WP_357679031             483 aa            linear   BCT 28-DEC-2024
DEFINITION  argininosuccinate lyase [Micromonospora rifamycinica].
ACCESSION   WP_357679031
VERSION     WP_357679031.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Baruteau,J., Diez-Fernandez,C., Lerner,S., Ranucci,G., Gissen,P.,
            Dionisi-Vici,C., Nagamani,S., Erez,A. and Haberle,J.
  TITLE     Argininosuccinic aciduria: Recent pathophysiological insights and
            therapeutic prospects
  JOURNAL   J Inherit Metab Dis 42 (6), 1147-1161 (2019)
   PUBMED   30723942
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Erez,A., Nagamani,S.C. and Lee,B.
  TITLE     Argininosuccinate lyase deficiency-argininosuccinic aciduria and
            beyond
  JOURNAL   Am J Med Genet C Semin Med Genet 157C (1), 45-53 (2011)
   PUBMED   21312326
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415011
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..483
                     /product="argininosuccinate lyase"
                     /EC_number="4.3.2.1"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004056 - argininosuccinate lyase
                     activity [Evidence IEA]"
                     /GO_process="GO:0042450 - arginine biosynthetic process
                     via ornithine [Evidence IEA]"
                     /calculated_mol_wt=50955
     Region          7..449
                     /region_name="ArgH"
                     /note="Argininosuccinate lyase [Amino acid transport and
                     metabolism]; COG0165"
                     /db_xref="CDD:439935"
ORIGIN      
        1 mselttyqrh hlaptydhhv ghlypamvra sqahvvmlte qglipaerga rllrglaalr
       61 adgspapafd gsfedtyyll ektlaqacgm paseldvqma rsrndldagv frmllrdqll
      121 gvldrvlatg ttaldaadry advvitgyth rrpaqpttig halagyaeal ageaamyadv
      181 idqlnvsplg scafagtdld iaparvaell gfdglvtnsy eavagadhlv rvgtlnaqal
      241 atgarlartl mdwltwqwva tpgdftqgss impqkrnpvv lehlvsmaga saadaasvln
      301 nvgaawweds nnattdvqvr lwdsndradr ffalvggfla eleplhpptr eeivasgatt
      361 taaadaltrh gvpfraahsv vgrlvragap dtwtaegvra aadgltdrlt ddavadliaa
      421 avhpalvldr vqvdgpgaaa vraqvatlrv aftgvadrlv atrdrlarad ealdtvaaev
      481 agr
//
LOCUS       WP_357679057             352 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357679057
VERSION     WP_357679057.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..352
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..352
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=36836
     Region          11..352
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mrvgtttrll aavvttlalg vssapltpav aapatrlaap gdddeggtpa lrdqldaask
       61 gwvdakaale rstkrqqeld gqlksieaql vvqtgkvgqi agaayrtgrl gpmsallnsn
      121 spggfmdraa aletvaared qelrtmletr dqatrtraav sreiteqrkq vatmgkrkeq
      181 aeralavaaa dkpaatsrds gssdgtsssn akgaprnsdg swpsescsvn dptpangcit
      241 prtlnalnqa kaagftryvs chrpsgsgeh pkgracdfaa qkngfggvas ggdrtygnnl
      301 aayfirnadr lgvlyviwfk riwlpssgwk aysggngdps sdhtnhvhls mi
//
LOCUS       WP_357679088             208 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora
            rifamycinica].
ACCESSION   WP_357679088
VERSION     WP_357679088.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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..208
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..208
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21376
     Region          81..208
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrsssypsng pegrpaarla vavalagtll atsacavgpt taqpaaevav pvatassaap
       61 tptgaptptg apavvpdalr ftaktldgta fsaatlagrp vvlwfwapwc atcasqawtv
      121 aeiapkyrdt vpivgvaglg eqkamrsfvt efelagttqi ddragalwrr feiveqstfl
      181 iidregkvvh qgfldgedlt rrvaalag
//
LOCUS       WP_357679135             395 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357679135
VERSION     WP_357679135.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..395
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42128
     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 mmslaglrvi daatlfagps aammlgdfga dvikiehprr gdpsrghgaa vdgvglwwkt
       61 larnkraaav dlsraegqei lrrlagrsdv lienfrpgtl erwglapedl lelnprlivg
      121 rmtgfgqfgp marrpgfgtl aeamsgfaam tgqpdgpptl pplaladgia glamsyaimv
      181 alrareatgr gqvvdlaiie pilgllgpqm tayralgvvp ertgnrsssn aprntyrtrd
      241 grwlaistsa qpiaervvtl vgrpdlvgqp wfatgagrvr hadeldgava gwiaerdade
      301 viarfeeaea avapiydvsd iakdpqyaal dtfielpdee lgevtvqnvl frlsdtpgev
      361 rwpgrslghd tdevlgelsy gpaeiaelre qgvva
//
LOCUS       WP_357679163             208 aa            linear   BCT 28-DEC-2024
DEFINITION  IMPACT family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679163
VERSION     WP_357679163.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..208
                     /product="IMPACT family protein"
                     /calculated_mol_wt=21909
     Region          3..197
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 maspfltlks svehetearr srficamapa rsveeaaafi agrrrlhpga thnctayvig
       61 qrlqkgdddg epggtagtpm vqalvgrgfn dvvavvtryf ggtllgaggl vraygsavte
      121 tldradtvrm vpaklvrvsv ahdqagrven dlrasrhpih evgygqavdf tmavgddeld
      181 afedwvatlt agrarvtvag dihvpgps
//
LOCUS       WP_357679179             264 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Micromonospora rifamycinica].
ACCESSION   WP_357679179
VERSION     WP_357679179.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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..264
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..264
                     /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=29313
     Region          <23..256
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdepspseie wlaeyvrtrv varrnarggr saaehliaal rclyrravad gfiaaadnpa
       61 vkvakprrla strravadar laeinavaag tgddpvldsl llrlhtetac rrggalalrp
      121 vdldpdqcli llrekgdtvr wqpvsptlmr hlqrhaeerh apargqllry rngqpityrr
      181 ydhlwvrige hlpwvwvqqi sthwlrhttl twvernfgya varayaghad sggdagtttt
      241 yvraslqeva salaaltnep hpla
//
LOCUS       WP_357679220             410 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679220
VERSION     WP_357679220.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..410
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44312
     Region          3..410
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mstveqllre lapqvlgvlv hryeqfdace davqeallda avqwpeqglp dsprawlitv
       61 agrrltdqvr seharrrree tvaarvpade svlpapgder asdqddtltl lflcchpals
      121 qasqlaltlr avgglttaqi asaflvpeat maqrisrakq rikatgvpfr qppeperadr
      181 lrvvlhvlyl ifnegytats gpdlhraelt reairltgal rrllpadgev agllalmllt
      241 darraartgs ggrliplaeq dralwdrrai aegvalvtea lstspvgpyq lqaaiaavhd
      301 eapkaeetdw pqilalygvl aglddnpvvr lnhavavamv rgpragldll dglaadaris
      361 ghhrlasvra hllemtgdvd aavagyreaa rlttslpeqr ylegraarls
//
LOCUS       WP_357679257             158 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679257
VERSION     WP_357679257.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..158
                     /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=17320
     Region          4..142
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msvnnerddl irritetqrs lgrafaqhqs plfasnltmr qlkvivilai ngsasgqela
       61 tglgvglgtv tgivdrlvaq glvsrhedph drrvrrvelt dagvklieei ndarleqydl
      121 imrhldtdtl raldmvirri ravadelfgp pkgsgcdg
//
LOCUS       WP_357679266             395 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357679266
VERSION     WP_357679266.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..395
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40417
     Region          48..392
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mtgvpraglp apgadplavv apcygggsla dvlpsalavl gvpgavdllg lapglagvrr
       61 iavllvdglg wyqlptaary aptltglaat vgrpltsgfp sttptslvtl gagaapgahg
      121 vlgftvrvpg tnrvlnhidw dgdpdplhwq pvrtqwqrar aagvavtvvs rpeyagsglt
      181 laanrggdyr gaagvdalar tmlaalaagt apalvsgyhp dldrhghlsg vdsapwriaa
      241 agvdgllarl vdglppdaal lvtadhgqld vpaehrfdld tdlrlragvr vvageprvry
      301 lhvepgavdd vlatwsavlg paarvttree lvaegwfgpv gedhlhrvgd vvvtcrdtya
      361 vlatrseppa asrlvayhga dtavemtvpl lvvrg
//
LOCUS       WP_357679273             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679273
VERSION     WP_357679273.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,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 265)
  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 265)
  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 265)
  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 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..265
                     /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=29148
     Region          6..265
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 mdevfrslrl yvllqrasar gamqyrlnav igilsgalwq gtgfafiwvv mhtfpslagw
       61 glaeiaflyg lrltahalvm ipmmsvndih wvvrngefdr fllrplnplv qlmgnrmgva
      121 qfgdllvgag llvvagqnvq vswnawliaf cflaivggal ieaafflalc slalrmidtf
      181 alrvfvddif skfgsypmki fggvtewllt fvlpvafvay vpasvvlgkl dnpwalagpl
      241 lgvvlavlay lvwrrqldhy qsvgh
//
LOCUS       WP_357679277             188 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679277
VERSION     WP_357679277.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 188)
  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 188)
  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..188
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..188
                     /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=20387
     Region          24..170
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mkdvkiyesd sdgllydprv raamtqftds dgdlltfeag aavrtanhav ermrahgsqg
       61 rgvsagaldl lirlnssehg isigelaraa gvssrnatgl vdtlehdglv rrvpdpkdrr
      121 svlaeitpag rawmeafrrp sqlamramfh gfapeelvvl rdlclrlaan qhrlaalkdg
      181 vsslkemr
//
LOCUS       WP_357679330             378 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679330
VERSION     WP_357679330.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=40778
     Region          18..372
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mqfgrrrlrl rltllyclvs vvssavllvi myalasslnl glvrplsgpp arplpypgpp
       61 gagdggtaph vralsaemlv lpgvalaima vfslllgwli agrmlrpvlt mterlhqise
      121 rnvherlslp gprneltdla dtvdgllgrl etaldahkrf vanaahelrt pltveralle
      181 eplidpaasl esfranferl laitdqrgrl leslltlsgs edahsrdepv dltgliektl
      241 qdrapdvkrr glrvqsalrp vrisgdqvll ahllanlcdn aihynvpggt veigvrreag
      301 rvvlsvantg qvippdqvdr lfepfqrlhr taddghhglg lsivraiara hkanltavar
      361 pdgglavdia fptitpgp
//
LOCUS       WP_357679394             263 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357679394
VERSION     WP_357679394.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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]"
                     /calculated_mol_wt=28497
     Region          8..253
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mstlglamve atpspalrpy vtrltayheh yerpvtrsea ampgavlilg fgaptevdgr
       61 pvtsfagglg drftltrtse paegvqvflt pfgarrlydl pmrhltnvvv pvedvlgpwa
      121 raavarlaet pswtdrlala drllarrilt gpelgpevpw awarllgsgg alrvsrlads
      181 lgwshrhlva rfhdqvgltp kaaarvirfe raarlvragt piaevaascg fydqahlnre
      241 fralgdltpg qirprpgkpp rad
//
LOCUS       WP_357679403             145 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679403
VERSION     WP_357679403.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=15984
     Region          7..138
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 megvdrraar vvcldgqgrv llmhwhdrvs gkaiweppgg glepgetple aarrelteet
       61 glpgsvvedv wvevqrdfrw lgvryvttep fflarfdeag pevdpgaltp eeseaylgya
      121 wlesmpdgve ppelaevvak ltgrr
//
LOCUS       WP_357679476             370 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora rifamycinica].
ACCESSION   WP_357679476
VERSION     WP_357679476.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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 370)
  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 370)
  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..370
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..370
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40069
     Region          34..330
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 maqpttpdap tpngtppetp pavttpaqda tlleralfei krvivgqdrm vermfvalla
       61 rghcllegvp gvaktlavet larvvggefa rvqftpdlvp adimgtriyr qssekfdvel
      121 gpvfvnflla deinrapakv qsallevmse rqvsiggqth rvpdpflvma tqnpieqegv
      181 yplpeaqrdr flmkivvgyp tdaeereivy rmgvaapepa qvfsaddlla lqrkadqvfv
      241 hnalvdyavr lvlatrspae hgmpdvarli qygasprasl glvratrala llrgrdyalp
      301 qdvqdiapdi lrhrlvlsyd aladdvpadh vvhrvmstip lpsvaprqqa ssapppvsgp
      361 paggwpgqrp
//
LOCUS       WP_357679491             310 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357679491
VERSION     WP_357679491.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=31418
     Region          5..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(35,249,252)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(189,220,247,250..251,254)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mgyavvlgea lidlldaece grpvfrqaig ggplnvavgv arlggtaqfv gslgddvlag
       61 rirdflaaag vgligavtva apttlavtth tgaepdfrfy gdppsyglla addldvalve
      121 gadvlycgsi vllspptlaa arrawslapg lrvfdpnvrp rllsgpaela glrevvvefa
      181 agahlvklsg adaallwpde pvegvaaylr elgagtvvvt lgadgalvaa gpdpvrvpap
      241 kvravdatga gdsvmaalva ellvdgepta padwhrrvaf alrvaglvce spggavampt
      301 rdevrrrfgd
//
LOCUS       WP_357679510             274 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679510
VERSION     WP_357679510.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 274)
  AUTHORS   ter Beek,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 274)
  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 274)
  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..274
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..274
                     /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=28488
     Region          4..274
                     /region_name="COG4132"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443307"
ORIGIN      
        1 mttrsrgwlg alpllafyaf vfgvplvall vgaftsqgrp tlenmrqslq ggnltsmags
       61 vqvsavvall gavlgtflay avvtsrftal rqsvltasgv lanfggvpla ffwvatlgns
      121 gvvsgllglp sgalytfwgl vvvylyfsvp lmvlvmapal dglrpqwrea aagngatawq
      181 ywrhvglpvl tpallggvvl lfgsafaaya taaamgagtv vplvtlkian altsdvligq
      241 envalalsld miviaglvma vylplqkrst rwlr
//
LOCUS       WP_357679516             202 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679516
VERSION     WP_357679516.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..202
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20670
     Region          6..185
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mpsevpravl fdmdgtlvdt etlwwqatet vagsmgvalg padephvlgr miedvaaylv
       61 eaaepgagal aevarrltda fadrvgrgvd vvpgaldlla gltaqgipta lvsasprsiv
      121 dlvlprlghe fdlviaaedt argkpcpdpy leaarrlgvd prrcvaveds ppgiaaataa
      181 gchvlianpv sglpglhams vs
//
LOCUS       WP_357679574             306 aa            linear   BCT 28-DEC-2024
DEFINITION  proteasome assembly chaperone family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357679574
VERSION     WP_357679574.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..306
                     /product="proteasome assembly chaperone family protein"
                     /calculated_mol_wt=33564
     Region          15..262
                     /region_name="COG1938"
                     /note="Predicted ATP-dependent carboligase, ATP-grasp
                     superfamily [General function prediction only]"
                     /db_xref="CDD:441541"
ORIGIN      
        1 mldphelyql tddlpdlgqp vliqaltgfv dagnasrlar eqlltsldar tiatfdvdql
       61 fdyrsrrpvm tfvedhweey dapelvlhll hdddetpfll ltgpepdlqw erfvaavgav
      121 aarldvrltv glnsipmavp htrptgvtah atrreliagy epwlqrvqvp gsvghlleyr
      181 lgqlgrdalg faahvphyva qteypaaaev llssvsrstg lllpndslrs aaevvrveid
      241 rqvaqtdeaa alvkaleeqy dafargrgek nllaaetgpl ptadelgael erylaeqtrp
      301 gdtpnp
//
LOCUS       WP_357679596             837 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Micromonospora rifamycinica].
ACCESSION   WP_357679596
VERSION     WP_357679596.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=92034
     Region          1..824
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtltaalprs adpdtlfdaf agwasgrgld lyphqeeavi eivsganvim ntptgsgksl
       61 vaiaahftal addrtsfyta pikalvsekf falcevfgae nvgmltgdas vnadapiicc
      121 taeilanlal regaradvgq vvmdefhfya epdrgwawqv piielpqaqf vlmsatlgdt
      181 trfvddltrr tgrstavvrs aerpvplifs yamtplhetl eelletkqap vyvvhftqaa
      241 aleraqalms vnvctraekd miaaaignfr ftsgfgktls rlvrhgigvh hagmlpkyrr
      301 lvetlaqagl lkvicgtdtl gvginvpirt vlftglskyd gvrtrllkar efhqiagrag
      361 ragfdtigrv vvqapehvid nekalakagd dpkkrrkvvk kkppegsigw geptfqrlve
      421 aepepltssf qvshsmllnv igrpgdafas mrhlltdnhe daaarrrhir ravaiyralr
      481 aggvveqlde pdetgrrvrl tvdlqldfal nqplsplala aielldvasp syaldvlsvi
      541 esilddprqv lsaqqfkarg eavaamkadg ieyearmell devtwpkpla ellhaayemy
      601 rqghpwvadh qlspksvvrd myeramtfge yvqfygltrs eglvlrylad gyktlrqtvp
      661 edakteelid liewlgelvr qvdsslidew erlrnpsdva daalahasle ervpavtrna
      721 rafrvlvrna lfrrvelaal rrwwdlgeld gasgwdadaw aealepyfea ydgigvgpda
      781 rgpallmieq grekwtvrqi lddpegdhdw gisaevdlaa sdevgaavvr vtdvgql
//
LOCUS       WP_357679774             546 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679774
VERSION     WP_357679774.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 546)
  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..546
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..546
                     /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=56764
     Region          11..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,89..92,96,98,135,137,
                     139..140,142,152..153,156,168..171)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,89..92,96,137,139..140,
                     142,152..153)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,96,98,135,137,139,156,168..171)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(152..160,165..171)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <347..515
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mhgdaqwgvp gyssirelgs gsagrvvlar rdhdgaevav kylsdelrad vgfvarfrhe
       61 arllgtlrsp hnarlidyve tgagaaiime lvngvslrev lrsegptgpe aalvvlkgsl
      121 qglaaahaig vvhrdfkpen vivqgdgtsk lvdygiavra gedasaagtp pymapeqwsg
      181 apaapstdvy aativffecl tgtrpyrapn laalarqhqs apppveevpg plqglvergl
      241 akdpigrpps aeafltelea iateaygadw eqrgrrrlar laglllvlfp sapdappevq
      301 tslaethfrt pskllsklss kvligtacag vvitaavvtv gafdddttlr aqtsqvtpst
      361 vapftgdpvt eepleepvee ptpsaeettp eptpepptpe pttstsaapp pmtsssptpr
      421 psrtrtpkpt ptatettgkp attspvitgt ldeppttatq ptatpttaap ptfrpptrsp
      481 gtpapeptpt rtgddggeit ptpvpedegp graaatllav glvtsgavpv tlavkrrmag
      541 rhrrks
//
LOCUS       WP_357679640             334 aa            linear   BCT 28-DEC-2024
DEFINITION  dTDP-4-dehydrorhamnose reductase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357679640
VERSION     WP_357679640.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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 334)
  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 334)
  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 334)
  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..334
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..334
                     /product="dTDP-4-dehydrorhamnose reductase family protein"
                     /calculated_mol_wt=36474
     Region          34..311
                     /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(39,41..44,64..65,86..89,109..111,113,128,150..152,
                     175,179,194..197)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187564"
     Site            order(129,152,175,179)
                     /site_type="active"
                     /db_xref="CDD:187564"
     Site            order(152,175,196,211,220,226)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187564"
ORIGIN      
        1 mspatdtvrp drvprrrsdh ladpsgdhrs ptrrvlvvgv tgmlgyavlr elgddpdldv
       61 hglarsiadr adrfpphllt rivpavdvtr fgqvrhlvde lrpdvvvncv gvikqrpdvq
      121 davhtvtlna lfphqladac aqvgsrlvhv stdcvfsgrr ggyregdlpd ppdlygrskl
      181 lgeatgapal tlrtsivghe ltthrslvdw flaqrgqvrg ftravysgvt tvefarllrt
      241 vvlprpeltg lyhvaaapia kydllrlvae vygwrgelvp ddgfvcdrsm radalarttg
      301 yrppswpdmi aamhaardrw agdparpgla gvpl
//
LOCUS       WP_357679879             243 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357679879
VERSION     WP_357679879.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 243)
  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 243)
  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 243)
  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..243
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..243
                     /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=26452
     Region          44..218
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mpddtweppl illavdlvil tlrggrlnll vvrrgiepfi graalpggfl aderedilsa
       61 arrelreeag ltdiphleql gtygdpdrdp rgrvvsvahl avvprlpepv sgtdaaaaew
      121 tpvedvlaar vplafdhlri vvdgverars klehtslata fcpevftlte lqqvyeavwg
      181 tpldprnfyr kvqgtkgfvv pagppratgt grparvyrag prrnlyppmi rtvptvaagg
      241 der
//
LOCUS       WP_357679916             538 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 27 protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357679916
VERSION     WP_357679916.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=56573
     Region          33..317
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(40,75..76,117,158,160,195,216,220)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          330..404
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          411..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(427..430,440,442,445,449..450)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(436,467..470,480,482,485,487,489..490)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(454,458,460,467..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 mavlaasatv aagtaltpas pasaapgspa vrpplgwnsw ntfgcninea kirgaadamv
       61 nsgmraagyq yvvvddcwqa ttrdaagnlr sdpvrfpsgm kalgdyihsk glkfgiyqap
      121 reetcaqyfn alggatgaln heqqdattfa swgvdflkyd wcspwgtlnd qiagftkmrd
      181 alratgrpiv ysinsnsahs ntgpsynwsn vadmwrtted itdrwstgcr adcfmgvtei
      241 ldvqaplaaw agpqhwndpd mlevgvrgtf tptqnrahfs mwammaapli agndittmpa
      301 dvrdvltnpd vlavnqdsag rqarrvrdfg etevwaktla dgsgavalln rsgstatvst
      361 taaeigmpaa gsytladvwt kasrntaaai satvppngvv myrvrtgsst pttsfslrgv
      421 gsgrcldllg gaptdgvrav iwdcnggntq ivtaasgqlr iggkcldaeg ngtangtrvi
      481 lwacgtgtnq qwtsqadgti rggqsgkcid vdqagtanns alvlwtcsga snqrwtri
//
LOCUS       WP_357679912             272 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357679912
VERSION     WP_357679912.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=29182
     Region          7..272
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mkvheyvtda adprltdytr lrdvelrksl eaerglfiae gekvirrava agypirsvlt
       61 arrwldplad vlgdaqvyia gdevmtgiag fqvhrgalas marlplppld tvlsgpspgp
      121 rrilvledlv dhgnvgaifr caaalgvhgi vlsprcadpl yrravkvsmg avfsipyarm
      181 ddwynglarl reagyqtlal tpdqsatsld tvkmtdrval llgsegdgls srwlheadep
      241 vcipmspaam eagvdslnvv aaaaiachgl mr
//
LOCUS       WP_357679952             294 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Micromonospora rifamycinica].
ACCESSION   WP_357679952
VERSION     WP_357679952.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=31082
     Region          43..221
                     /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"
ORIGIN      
        1 mpeptgvihd igyqrytgpr lgrrhvfnal ylhglrtvfg lgrsakakif pwlvvgivtv
       61 vaaglaavrs qlgevvmtya qfadamswlv iffvavaape lvsrdlrsgv lplyfsrplp
      121 rddyalakll almsalwlll ggpqlvmflg aafttktglr gvwnelldll pgllyaglwa
      181 vvfaaigllv asltgkrafa aggivavflm ttpivgvlsi lpsravnela flaspstlvg
      241 gvgtwalgdl lvpegqnadi ligdfgpvya iaavllvaac tallllryrk vaaq
//
LOCUS       WP_357679982             297 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Micromonospora rifamycinica].
ACCESSION   WP_357679982
VERSION     WP_357679982.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 297)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30460
     Region          11..291
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 msdpqltyrd pvavlglgpm gralaatlis agipttvwnr tphraealva rgataaptvt
       61 gavraaalvi tclrnpaavd svlaghddwa grtvvdvtts rpdearrlsd wadghrvhlv
      121 kgailtptpt igtpaaitlw cgsrpafdaa lpalttfggt pthlgtdpga aaaydmalld
      181 lfgtavsglt hafalasaeg iaprsfarya agiapmlgem ttrfadqlte erfpgdrstv
      241 asahsgithv ietaethgid savlraarsv iaravtaghg edglaqlarf ltparsa
//
LOCUS       WP_357680014             388 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357680014
VERSION     WP_357680014.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 388)
  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..388
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..388
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42346
     Region          1..>60
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          21..>117
                     /region_name="CheA"
                     /note="Chemotaxis protein histidine kinase CheA [Signal
                     transduction mechanisms]; COG0643"
                     /db_xref="CDD:440408"
ORIGIN      
        1 mpyvdprfga qlralragqg lslralgqlt hrgkshlhdl etgakaptpe tarhldevlq
       61 aggtlarlve apvdhdaeag ellarvrasd vsaetlvrie aavddlasay aktrpvdllp
      121 mvrrqlayvg rlldgrgtla qrrrlvvagg wlavlratvh idllqrsaad ahlstatala
      181 dhgghpeiha wcletqawer ltrgdyrral dlaqqaqraa prgssaqiqa taqeariwar
      241 laevrrtrea ldrlerltan lpvperaehh yrydptkala yaattlswag dpaaeqlart
      301 alaeldprgd ggdrprrsas arldlamall aadrpdeasv vatdavrsgr vvpsnwwrar
      361 evlrrveptg taeaaafrem yeahrpar
//
LOCUS       WP_357680088             425 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora rifamycinica].
ACCESSION   WP_357680088
VERSION     WP_357680088.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..425
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45913
     Region          3..411
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mrppavedll rvlapqvlga lvrryghfdt aedavqeall vaatrwpvdg lpesprgwlv
       61 tvaarrltdl lrseqarrrr eddagravpa grwlapaadh pdpgddslvl lflcchpalp
      121 paaqialtlr avgglttgev araflvpest marritrakq rvrdsglpfa lpdaaarqar
      181 ldavrqvlyl vfnegyasta gahlrrvdls teairltrml hrllpadpev tgllalmllt
      241 dargparvgp sgelvpmaeq drrrwradqi aegvalvsav lprgdvgpyq lqaaiaavhd
      301 eapraedtdw aqivalyevl mrisdgpvva lnhavavama rgpaaglrll dtlaadqria
      361 ddprwyaara hllersgdpv garrayehaa rrsmnlprqr ylygraarlp drppagaapt
      421 dpggg
//
LOCUS       WP_357680094             215 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357680094
VERSION     WP_357680094.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22425
     Region          2..165
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlfdmdgtlv dseklwdial yelattyggt ltaaarrami gtsmaasmrl lhddlgqper
       61 dqqvsaewih arilelfrtg lrwrpgaltl lravraagip talvtssgre lvevaldtlg
      121 rgsfdavvcg devdsakphp epyltaarll gvpigrcvai edsptgvasa laagaavlav
      181 paevplpptd gvhqveslta adlellaall geppa
//
LOCUS       WP_357680126             437 aa            linear   BCT 28-DEC-2024
DEFINITION  lipopolysaccharide biosynthesis protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357680126
VERSION     WP_357680126.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 437)
  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 437)
  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..437
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..437
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44285
     Region          26..381
                     /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 mrrllhlvpp gtlavgggla llglasyvhl avaghaldla dysslsvlws ivftlgigvf
       61 ipveqevarv vaarrsqglp pgpvlargav vatvvlallv vatlagrral tdrlfagddt
      121 mvvvligalv amavayttrg vlsglqlfpw ygtqlgvdgg lrialvaglg vsgvtdpvwy
      181 gavlvvapll svlvtlppvl ravgggvpva wgtllrglgl ltvssllsqv vvnvgvinar
      241 lldpadvata gallsalvlv riplfvfgsm qasllpglat tattgdvagf hgllrralgv
      301 vtalgvtgal gavalgpwlv hrlfdapgvl ghgdfawlav gtlaylwamv lgqallaldr
      361 hraqavswti gvaallavtv vpapvalrve layavgsvvv aatmavlllr rgarpatptp
      421 irplddvvap gvsggir
//
LOCUS       WP_357680141             395 aa            linear   BCT 28-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Micromonospora rifamycinica].
ACCESSION   WP_357680141
VERSION     WP_357680141.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 395)
  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 395)
  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 395)
  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..395
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..395
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42216
     Region          33..252
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mtgdryarla diewwdqdev rgahavvaga galgnevlkn llllgwgtit vvdldrveag
       61 nlsrsvlyrp sdvgaakvda vvraagelnp dcridviadd lrvglgagll hradvvlgcl
      121 dnvtarvalg qlagqagvll idgglttweg alrlylppdg pcyvcgltdd dlrdltlrhs
      181 clayrvraes argipttptv aatvgaamvq qamrwlsrdr hdmtvpighe lrfdlaydrf
      241 wqvgipvnpd cplhptpvlp aatpassgad rwvdildrwr aaladgevvl rlplpvlrgw
      301 tcpgcgrqda vhrahpgdrp ercpacaaev aldlvdqidg tqqwhrlspy atgfprwswv
      361 eaygggearv felaepagpd saaaappgra gkdgd
//
LOCUS       WP_357680165             333 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357680165
VERSION     WP_357680165.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=36401
     Region          15..305
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtrpaarggs rtsadrlarl lnlvpyllar pgievaeaag dlgvterqlr edlellwvcg
       61 lpgygpgdli dmafdgdrvt itydagidrp lrltpdeala lvvalrmlae tpgvanreai
      121 eralakiena agdlvgapva vrlpgenprv qelraaverr ralrityytv ardesterti
      181 dplrmlmvdg rayveawcrr aeavrlfrad ridavvelde paavppqarp hdlrqgvfrp
      241 spdlplitlr igrgerwite yypcerievd gdrwvvslrv tdlgwarrfv lglgpdvtvv
      301 apvelavqvr aqaaaaleay atpvlpagag tar
//
LOCUS       WP_357680163             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357680163
VERSION     WP_357680163.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=36154
     Region          4..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 msrsrterlv nlvicllstr rfltaaqiaa tvpgyehdpe dareheafqr kferdkaelr
       61 elgvpletgt asvfdtepgy riahreyalp diplepdeaa avgiaarlwq haglaaaass
      121 glaklraagv dvdpqatlgl epmvtvdpsf apltaaardr revtfdyrvp drdaptrrrl
      181 qpwgvvcwrg rwyvvghdrd raatrcfrls rvvgavrvtg apgayepphg idlishvarw
      241 sgpvertgra tvlaatgraa glrrwavqsv pgpdgdrlvl pyadpeslag qlvgygpdvr
      301 vleppevrda viqrlkeiaa rhdelavtgg ar
//
LOCUS       WP_357680206             533 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357680206
VERSION     WP_357680206.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 533)
  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..533
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..533
                     /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=57094
     Region          12..268
                     /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..37,60,75,80..83,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,78,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(23,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mpgqgdskia gryrvlralg qggmgtiwla hdelldrqva ikevllpqsl deagraealq
       61 ramreamaaa qlrhpgiiti hdvlqqdgrp wivmellrgr dlkeavaaeg pwaperaael
      121 glrvlealsv ahargiqhrd vkpanvflsd dgrviltdfg iarledqati tesglligsp
      181 gfiaperlrg erggpesdlw slaatlyaav egqapytgts plsvlrdalt lpprppqrag
      241 hlgpvlmqmm areprqrpvp qaaeqmlrrv aeggqavapl apagrasrap ilagavvvaa
      301 aaaavafvvl rpgdqppepg pssmpaaapt tvrttsetlp eatpeatpea tqmpeperta
      361 rftaavdlca lltprqvgql vpgagkgerg gdscewatrg kglqvlvlsn sqlpdrwsge
      421 vedaeeqyin trnsrgregs ritwswpeig ldksitqprr nvqdlkgigd eafsyelvnp
      481 aghpehvtlv frlsninvev thvdidkigk daalreatrd aarrlakald gqe
//
LOCUS       WP_357680216             309 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357680216
VERSION     WP_357680216.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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..309
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..309
                     /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=31460
     Region          6..294
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 msdrglliig dvvtdvvamh gapvlagtdt aadimlrpgg sgantaawaa hlgadvrlla
       61 klgydssewh ttelvrtgvr phirvepghp tavviamvdk sgersmltnr gaggristed
      121 wdrsmldgvg hlhlsgyvlf aepglelarl amseaaaaga gisvdpastg plrefgvarf
      181 lretaaagli ipnldealll tgaptparaa eilserygta vvklgpqgal vatggrilat
      241 aeaapakvvd stgagdafaa gyltaqlkga heaaalqagc qagatcvalv ggrpryglev
      301 nrlypihtd
//
LOCUS       WP_357680219             343 aa            linear   BCT 28-DEC-2024
DEFINITION  YeiH family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357680219
VERSION     WP_357680219.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..343
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..343
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34500
     Region          2..343
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 mpfadrlpgv vaalaavvla lvanrfvpal spamvavvtg alvanlwgid erllpglrfv
       61 arrvlrvaiv llglqisvpq vlalgwqapa iaavatgvtf tltplagrrl glppgtsllv
      121 aagvsicgaa avaamrqsaa atdddaagal svvvlygsaa ilvvplaaaw lglsnpqlgv
      181 wtgaavheva qvaaigsatg vlataitvkl grvillapii alttmrrrrs pahvatwsgp
      241 erdpgsapag rrwsgpaara pvvplfvagf lamvalrgtg lvpslvtevv pevtnilmaa
      301 alfalgtgid arklvragrv mvlgaiatgf vttvsltgvm ilm
//
LOCUS       WP_357680235             283 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357680235
VERSION     WP_357680235.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 283)
  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..283
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32403
     Region          10..72
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(16,20,45)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,44)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,38,41,45..46)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          98..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtsfqqarid lgsqlrqlre tahlsgkela erlrwqpskv srlenarqtp teddvvvwaq
       61 avhaapettd elirqaiall erhdgwkqrh rsglaaiqed irdlesktkl frvfepnivv
      121 gllqtaeyag hvfrkvkrly sapdqidtav rirmqrqeil ydrnrsfrfv vhesalrtrl
      181 tppdvmqgqf drllavstlp nvefgvipfg aelpasping fwifnealvi vgtmtkdlll
      241 rdpddiafya rafddyakaa efdeagrdvi irildeyrkq tph
//
LOCUS       WP_357680346             107 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357680346
VERSION     WP_357680346.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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..107
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..107
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11752
     Region          1..104
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mttelhdqae qhrltmlrqt ltdqfavqta rlteltadtg dpaeahtraa llaatrqsld
       61 hlagalrrla egsygrcerc qvaipaerle vlpqarfcvp cqqktrg
//
LOCUS       WP_357680424            1029 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora rifamycinica].
ACCESSION   WP_357680424
VERSION     WP_357680424.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1029)
  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 1029)
  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 1029)
  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 1029)
  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 1029)
  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 10147902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..1029
                     /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=109601
     Region          <8..>942
                     /region_name="PRK12316"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237054"
     Region          36..492
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(148,151..156,158..159)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(151..152,267..268,284..289,314,381,393,396,486)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
     Region          959..1017
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
ORIGIN      
        1 mdgavwgrpe tkadvvsgav rldmgearrr aralastlla rgldpsaesp vavclprsad
       61 lvvaylavam aggviapidp tlpelrrrdi lrqlrpafai aaptvadafa vdcavlapda
      121 wsgvtgadve aarsaldvpa pddralymif tsgttgvpkg vvctaanleh llrwslddhd
      181 fgdgarisvt vspgfdvsiw ehfvafaada slhvvddelr ldpqalraaw arhdvthsfv
      241 spqlaeelva ldwtgqptsl relyaggdrl rkrppatlpf plvnlygpte ctvistggvv
      301 rpaddtnadt ypdigvglpg lsiavvddel rpvpagtrgq lciggpqvtr gylnddelta
      361 ekfrllagpd gvtrryyctg dqvtenpdgt lqfhgrtdgq ikvggvrlei geieaaltah
      421 pavdravalt vthprsgnlr vastvvtgtg itareikdwv aarlpraavp asvlfrermp
      481 lthngktdmr alraeheaal rdavatvdea vdggtdtddh ayvfpvnqeq rslwflwhva
      541 prsprynvta afvvegalde arlrtavgsv vrahpsvvas fregrdgale lvaeakarha
      601 ggelvqvfdp vanlaaamrt adeqynepfd lltgplmrva lipvaqadta vlqlvlhhtv
      661 adgvsiqgll ekitesyhgr alparparvd eqppgvdtpp gvvafwegrr dtyrplrlrr
      721 efdpeladgs avevrstgrl gerlreaavr ahttpfrlml tawiiaagrw tgqdaltvgv
      781 pahgrsssda ssvgmyvntl pvtvplrdld fadvlaavet elavtdehha pfsviaragr
      841 sasplafdiv nstfslelpl rlgigdratr mqprldscpy plsvfadpls gdevnvfaqf
      901 grgcvdaaev rgmvaaflaq lahqadatpd rpgvaarprr redeapaaap vgpstaalaa
      961 vtqawesvlg lanlppdadf felggdslaa lrivgqlsaa gyplsladff rcpsiaeqas
     1021 tmggddghr
//
LOCUS       WP_357680431             217 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357680431
VERSION     WP_357680431.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22937
     Region          37..170
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mgigrslhdh akhgdgggvi nhprayevla eigfigrrrr vfaglaalte irpgekildv
       61 gcgtgylthl lapvtgpagq vtgvdpsasm vghagrhapr ncsyqvgegq dlpfpdasfd
      121 vlvstlavhh mpssaralav qemfrvlrpg grlliaefhp panrlaahlm svlvgpamrp
      181 smpellaelv paagfqvkde grvkplmyyi kavrpaa
//
LOCUS       WP_357680489             291 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357680489
VERSION     WP_357680489.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 291)
  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..291
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..291
                     /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=30688
     Region          1..>89
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtgdthydld ilaelaedll dagtarrvre hlavcdpcge lladlaavre vlaatptpam
       61 pmgvalridk alaaeaeshg arrggvglae tpdwdelmrd spwerpaetp epvrlgvvsd
      121 dgtivpagrr aarrrrwamp avaaaaaaav vgtavlsngl lasgggggse iqveagapsp
      181 akeelrarsy altdsghnys dqelrqpleg flapapiing gspdvdqvdt cvskvatrsk
      241 lqayavdqgq yngqeaiiva swkdkasgrl ridivdpfnc knlrkpmlgr w
//
LOCUS       WP_357680578             380 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357680578
VERSION     WP_357680578.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 380)
  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 380)
  AUTHORS   Rosinski,J.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..380
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..380
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41353
     Region          3..82
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          192..293
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 madidartlg erirearkra dlsqedlgha vgiertvmnk iesgvrkvta leladiaaai
       61 gvrmstffee pvpalvahrs sqgldtadsq vdtlltkfag evefvaslgv delgldgaea
      121 varagitqps nnaeaealaa qardlmscpa aepinrfver vadigllafs qdigkdtada
      181 gsvllprggv clvnshmkvg rrrlalahel ghyliadtyt vdwrvadhsd qvvplesrld
      241 rfarafllpa aavapqweek avrsgeraaa iylasvfrvd matlatrlke lgladgekva
      301 svrryrttqa divemglnvp peeltgttvp rpfaravlrl vrderisrer aldllqgtfd
      361 egdlpqirqr radeiwrfvs
//
LOCUS       WP_357680626             566 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357680626
VERSION     WP_357680626.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 566)
  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 566)
  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
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..566
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=58920
     Region          7..478
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
     Region          <436..>564
                     /region_name="alpha_am_amid"
                     /note="L-aminoadipate-semialdehyde dehydrogenase;
                     TIGR03443"
                     /db_xref="CDD:274582"
ORIGIN      
        1 mtggrtvpgl lrrraadtpg avalchpdgs sltfagwdra adalaaelva dglrvgqrva
       61 llfderewfg yaiafcgvlr aggvavplst rlsprqlvdr vtatgavgti reggtvptgl
      121 ggwqrglarp gggatpdrst pddaaqvift sgtegsakav vathgnltyg hdtapgrrhl
      181 ahsrhflhaf plgtnaaqtm lltglaaapa alvvprfdaa evcaaveefr vgtlflvpst
      241 arellasgep hrrdlssvvl vgttgdilpa pvaralgaam pnatvvntys steaapartt
      301 mvfdsrrpha vgrgavrvtd dagrevdpge vgqvwirsda pprryldgdd tatfrdgwtr
      361 tgdrgrlddq gylhlvdrds sivhsggtki sslaveqalh ehadvldcav vgipdpvlge
      421 raaavlvtra gtvpadlrgf lagrlstpei pqrvvcvdal prndggkvvk rslrdlfrpd
      481 gsapapapqt averqlagiw atvlgvaavg rdddflalgg nsmsvlrlar lvsdqfavat
      541 pvsalfarpg lveqaawiaa rlsgpp
//
LOCUS       WP_357680604             155 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357680604
VERSION     WP_357680604.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 155)
  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..155
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..155
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17319
     Region          8..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnvpfrvdnc siertldivg ekwtflvlre afsgvrrfad mqastgaprq vlsarlarlv
       61 degllrkvpy repgqrqrde yrltekgrdl ypllvslmhw gdkylsgeqg ppvrlthrdc
      121 gapveqhfrc aeghevagph evtplpgsga klksa
//
LOCUS       WP_357680636             208 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357680636
VERSION     WP_357680636.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 208)
  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 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   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
REFERENCE   4  (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 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=22207
     Region          45..208
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          147..202
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mngraqtyir tpdpistagi taalrgraei evvpaqmita etvgvvaadt ldhdtldvlr
       61 avrrlgcrrf vlvaavesds alipavelgv ralasraeat ghrlaqlvvs tasggaampp
      121 evlgllvkqv trlqqtvlap rgidvnglsv reseilrlva dgmdtrevat rlsysertvk
      181 nvlhditsrf qlrnrthava yavregli
//
LOCUS       WP_357680662             362 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora
            rifamycinica].
ACCESSION   WP_357680662
VERSION     WP_357680662.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=37198
     Region          22..356
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msgpglklrp sghgtrlvir srgsrlslrv hlraliagaa llltalgval vnlssgdfpl
       61 pvsdvlrslv gqgdpgtdfi vhelrlprvl itllvgtalg asgtifqglt rnplgspdfv
      121 gltvgaatga livlllfngt gfqvaagaiv gclatsvaiy llafrrgvqp frlvlmgvgv
      181 salldsfnsf liyrsrldea iaaqvwligs vngpgwteva lvavavavll pvalhqgryl
      241 dmlalgdeta mlhgvpvers rvvlalsgvg laagataaag piafvalaap plaarltrsp
      301 nagilpaasm gaalltasdw vaqrilpedd vpvglvtaal ggiyltwllf herrnrgqga
      361 qr
//
LOCUS       WP_357680786             379 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357680786
VERSION     WP_357680786.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 379)
  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..379
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..379
                     /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=40338
     Region          3..375
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mirdivvvgg saaavtaada lrqyghegti tivseerhtp yvrpplskgm lkgtetpesv
       61 lmpplradid frprtravgl drerrrvlld gdeelpydgl vvasgararr lraedadefv
      121 vrdlddalrl raalagagsl lvvgggflgm eiastarglg levtvvdrdp plvrqfgsfl
      181 aehmtraald egvrivrspd gvellggdri tgvrtsgget leadvvvsav gdlpnvewla
      241 gsglgdpagl lvddrcrvap givaagdvva rvstrtgrpr rtphwgsaid qartaaqall
      301 kgdeappyrp apyfwteqwg fdikicgevq pgsaaeilfg amsersaliq wtrdgapvaa
      361 atvnhrmplv klrrlatsv
//
LOCUS       WP_357680758             365 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357680758
VERSION     WP_357680758.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   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 365)
  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..365
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..365
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=39208
     Region          76..365
                     /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 msavsrfrvp rprtaagrva gvvgaavgva aaglaagvat eralvrrlka dpadpytged
       61 fgaqrydeay rlelpdgtdi hvevveptrp vpghptvvlv hgfcldmgtf hfqrkllaer
      121 gdyrivaydq pghgrsgrle tgeydlaalg htlrrvidrt apegplvlvg hsmggmtima
      181 faeaypelfg ervvgtvlma tsggllaetk lvapallgrv gspvlfmmnn atryggivid
      241 rarrstsnva wlltrrygfg tpkpspalvs yvermnsrts adtvtrylrt lathsrfpal
      301 aalsgtpvlv vvgdkdmitp vvhseeivrr lphaeyvkiq dsghvvmleh agevnaaler
      361 flaal
//
LOCUS       WP_357680819             246 aa            linear   BCT 28-DEC-2024
DEFINITION  sirohydrochlorin chelatase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357680819
VERSION     WP_357680819.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..246
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=25109
     Region          1..233
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mtptlvlaah gtraeagert lsdlagvvra arrrhrvels yleisrplla dvlsatpgra
       61 vlgsaacavp gpvvvvplll tggyhvrvdl psviaehrpd alvapplgph rllttalarr
      121 lahaglrsad avvlgaagss dpaaladvra aahqlavrls rpvtaafasg gapsldeale
      181 rvrpgpatrv aiasyllapg ffhdrlvvag adlvseplga dpdvaalvwr rfdetaaala
      241 gravsa
//
LOCUS       WP_357680843             146 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora rifamycinica].
ACCESSION   WP_357680843
VERSION     WP_357680843.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 146)
  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 146)
  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..146
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..146
                     /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=16066
     Region          3..135
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maddpstpvd lmraltraer llarrigavl ategltveaw rvlcrladgq ghpmsevste
       61 eslppgtltk ivdqlvdqnl vhrridpfdr rrirayltpr ghreqdrida lvraelagil
      121 ddaaltgqlv dlaarlgprr hpartg
//
LOCUS       WP_357680862             372 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357680862
VERSION     WP_357680862.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=40562
     Region          10..355
                     /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 mhqpnrprha rgdgrlaeld llrfiaalav lafhyfvaya svwgdrpael fpglaplagl
       61 gilgvelffv isgfvilmsa wgrgvgafar srlvrlypay wlsllavagl yaftgakald
      121 pklsageylv natmfqrlfd vtdaagvyws lwvelrfyll mailviigvt ygrvlvfcgi
      181 wlvaafgael lgndllnqiv mpryapyfia gmalylihkh gsawlpwlyv vagwamslhs
      241 alervhgrik lagfknmpvg dvsviititv vfaamalval gvlrlrpsri ltalggttyp
      301 lylfhsvvav alvpplvsrl dpwlvatitt laavllsylv yafaerpiqr llkprgtaap
      361 aaaarrervp sa
//
LOCUS       WP_357680874             303 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357680874
VERSION     WP_357680874.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 303)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..303
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..303
                     /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=32623
     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 msaadaaglg rgravgfvlp alvligvflv fpaiwtiylg ltdyrltgla aanpqvvgld
       61 nytaalrdpr flgslwltvv yvggsailgq aglgfalawv lrtrtgwvrr ivegvvllsw
      121 ilpstvvgfl wfalldrddg tlnallntpg fgwlldypll sivvfnvwrg tafsmmlyaa
      181 alenvppshl etarlagasv fqqlrdvvlp lirrhiltnl llislwtfnd ftpfvltggg
      241 pegrseilpi yvynvalrgg qlgvgaaisf lillinlvfa ltylrllrgr rgqepapvgg
      301 ppa
//
LOCUS       WP_357680941             158 aa            linear   BCT 28-DEC-2024
DEFINITION  Lrp/AsnC family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357680941
VERSION     WP_357680941.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..158
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16826
     Region          1..135
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 meeidrrivt llardgrmsf tdlaretgls vsavhqrvrr lekrgvirgy aaivdhdavg
       61 lpltafvsik pidpaapdda pdrlahlrai eachsvagde syilkvrvas pvaledllqq
      121 irasanvstr ttvvlstpye hraadvageg gvagqdgp
//
LOCUS       WP_357680943             441 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357680943
VERSION     WP_357680943.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13307259
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..441
                     /product="glycoside hydrolase family 3 protein"
                     /calculated_mol_wt=46344
     Region          <74..292
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
     Region          324..437
                     /region_name="CBM6_xylanase-like"
                     /note="Carbohydrate Binding Module 6 (CBM6); many are
                     appended to glycoside hydrolase (GH) family 11 and GH43
                     xylanase domains; cd04084"
                     /db_xref="CDD:271150"
     Site            order(336,347..348,404,435)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:271150"
ORIGIN      
        1 mnvldhleav pavtaeplag hgntlfrlvd dadaatwltv dvvesgaeaa arlaatadva
       61 vvvvgdhplv ngretedrtd lalapaqdav vraaraanpr tvmvissgyp vswpdhdvpa
      121 vlwsshggqe yghalaevll gdadpegrlt qtwyrsagel pdlldydiva adatylyyrg
      181 vplfpfghgl syatfdytsl avsvagdgga atvtvtntgs rpgtevvqfy thqrrsrvkq
      241 plrrlrgfer vrlapgesrt vtlsfpvadl afwdvtrgrf vveaaphrlm agrsatdlrl
      301 sapfqiggpa ggesipprrg plravdhday davafvdagr vsgdavrsea egawilfgdv
      361 efagaasgvi eaesteggvv tlrlgdplhg palgalpipp tgryaparvt aelaeatgvh
      421 dlhvvfeneg itlstlnvag a
//
LOCUS       WP_357680965             196 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357680965
VERSION     WP_357680965.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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: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=21612
     Region          8..196
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mahyfseqpg apsrpgvvdl vlpdlhlrle tdrgvfsper idlgtrille tvppppregd
       61 lldlgcgygp ialtmasrap eatvwavdvn rrsveltern araagldkvr svhvddvpdd
      121 vtfnaiwsnp airigkpalh emltrwltrl apggvaylvv qkhlgsdslq rwlgeqgwqa
      181 sreasraayr ilrver
//
LOCUS       WP_357680992             411 aa            linear   BCT 28-DEC-2024
DEFINITION  mechanosensitive ion channel family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357680992
VERSION     WP_357680992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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 411)
  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 411)
  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..411
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..411
                     /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=44606
     Region          <177..346
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mqdyletiaa aataaaiall lvevahrlir rlgrrshlmt eltehvhrpl qvagtvvavq
       61 favrwttgya vgtgwrqavl hilvlgvvaa vawlvaallv vaedtalarf lrvdvpdnrh
      121 arrvrtqvvl lrrltivviv vlavgvmlmt fpavrgigag vltsagvvgv vaalaaqsll
      181 gnviaglqla fsdavrlddv vvvegewgri eeltlsyvvv qiwddrrlil ptsyftstpf
      241 qnwtrteaav lgtaefeldw svpvqsmree lrrlvegtel wdgrvcvlqv tdatggaitv
      301 ralvsaadag slwdlrclvr ehlvgwvrdq rptalprtrt elgdssgslp wqwaqprrpa
      361 rrrsdgevpd darvfggshd gdarseafvg pdteargdam vgaengadvr r
//
LOCUS       WP_357681000             253 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357681000
VERSION     WP_357681000.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26473
     Region          9..250
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mseyldelfs lhgrralvtg gssgigyama eaigragadv vivarrqgel dktverlrrh
       61 gvtasslsad lgdrdavkrv caaageidil vndaannirk pmaelteddy eqtiavnlta
      121 pyllgqhfgp rmaergwgri invgsqqtvs afgdsgvyga skaaiagltr sqaeawsarg
      181 vcvntiipgf vltpltepaq aipgrveqla arhmtgrngv padfagaavf lagdasafvt
      241 gqmlfvdggf fvh
//
LOCUS       WP_357681044             506 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Micromonospora rifamycinica].
ACCESSION   WP_357681044
VERSION     WP_357681044.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 506)
  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..506
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..506
                     /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=51923
     Region          9..453
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mtplttrdpr qagpyelvgr lgaggqgvvy lgrddqgrwv avkvinvdlr qhpkaksqfa
       61 keiaaarrva pfctaqilfa dvdgdlpyvv sefiegvtlq rhvreqgpis gnalhrlavg
      121 tatalaaihq sdvvhcdlkp dnvilgadgp rvidfgiara ldvtetmtdr imgtapymap
      181 erfrddevgp asdvfawagt iafaaggqpp frtgpvaavm hrvlndppel tglsgplavl
      241 igqcldkdhr arptaqevll rllgrdthpg tavplqsvlr agtdaaatqq lprtlstvap
      301 vsppvtpgap dgpvpvavdp wptmstvlpa ppaptgpatt ppatawstpt ppathwsgpa
      361 dpapastgtt ppatawtgst ppaqtwtgpa gpatppggra avpapgrttp drpvpaatpp
      421 agrdgfgrrl rrqwadpwgv staiflgslg taagyvatta vgtaaavgsv tlvvvygvrl
      481 lvaaaltpsa apdgpppgrp aprtda
//
LOCUS       WP_357681074             106 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357681074
VERSION     WP_357681074.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 106)
  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..106
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..106
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11483
     Region          33..>88
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mnsgyvrwnd iraehverag geevveagkr ellaevvghr laevrrarsl tqqqvadrmg
       61 vtkgrvsqie qgkisgqdvl aryaaalggr lhqaiyfddg diaaia
//
LOCUS       WP_357681123             399 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357681123
VERSION     WP_357681123.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..399
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..399
                     /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=42818
     Region          3..297
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrnryldllr flaivrvvvy hvtglatltl vfpamsimfa lagslmaasl drsggsalrr
       61 rlrrllpslw vvavvfvpam lltglvftpr vllwlfpitd ppanywggla lspiwylrdy
      121 lwfvlaspaa lwlfrraplp tlaapylllv aievgilptt savprdfgly fgawllgfah
      181 hdgmlrrlad rvlvpvavll agaggawils hpgprgydln diplgnalws aafilvvigr
      241 apaaawvdrn rtfgrlvtit nrraltvylw hmpfvvaltp lvglvgwspr dpwglairvv
      301 lvfllvgvvt llvgwvedva agrrpelvpg grpeqipgrr sssppgtisp gtispgtisp
      361 gtalpgtasp gtvspdsgrv aavpdprvpg pgavearar
//
LOCUS       WP_357681148             313 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357681148
VERSION     WP_357681148.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 313)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..313
                     /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=34193
     Region          1..310
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mmvstrvapp rrwrgegvra llwlspwiig iavffvypll stvyfsfhry dlftlefvgl
       61 dnyryafsda rvlqsalntl wlvvfmvpaq vlfalgvaql lvklkigggi lrtifylpsl
      121 vpmvagtvaf vyllnpatgp vnqllarfgi tgpdwfgsaa wakpsltlla lwgagntimi
      181 flaalldvpr hlyeaaaidg agswrqfrsv tlpvispvlm fsavtgviya vqyftqamia
      241 srvasgatds agttftpgyp dgslltlpqh lfhtgfrdws mglacvhall lfavamlftl
      301 illrqfsrae gts
//
LOCUS       WP_357681194             488 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydroorotase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357681194
VERSION     WP_357681194.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 488)
  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 488)
  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..488
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..488
                     /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=53320
     Region          7..484
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
ORIGIN      
        1 masfdvivtn vgvvrhdrpe petadigvld grivrvapgl dpagahtvvd gggklafpga
       61 vdahqhwgiy nplavdtete sracaqggvt saltymrtgr yylnkggpyd eifpevldas
      121 egrsyvdyaf hlapmmrrhi deipalvrdh gvtsfkvfmf ygshglhgrs adqnaflmip
      181 egerydyahf efvmrgiqaa rerfpelage islslhceta eimsaytqmv eeegrltgle
      241 aysasrpphs eglavsiasy lahetglpti nllhlssaka mdaalrmaea fphidfrrev
      301 tighlladit tasgiggkvn pplrpredve alwahlldgk vdwvvsdhac crdeqkfgep
      361 rddvflaksg fggaeyllpg lisegsrrgl sygdvarlls wnparrfglr tkgaiaegld
      421 adfclvdpds twtvraedse stqeytpfeg feltarvtdt flrghrvled gkvagdpqgr
      481 ylarpvtg
//
LOCUS       WP_357681243             294 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357681243
VERSION     WP_357681243.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..294
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32231
     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          99..285
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mrethsstvp rrqlgrlltq lredahlsid aaageldcsr qklwriergl tsaktpdvrv
       61 lcelyratpd qasvllglae vsraegwwha hgsavpswfs pyvglenvas siryyhaelv
      121 pgllqtpgya talfqhnrpe lgeeerrkav sfriqrqgll arrlppaptl tvvlseavlr
      181 rpvpgrsvma dqlrhllavg erhnitirvl plaagpplaa eagtfvlldf ppsvlgspse
      241 pptvyveglt galyldqpae iaayervwqg ldslaldaqq stelidairg eche
//
LOCUS       WP_357681325             308 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora rifamycinica].
ACCESSION   WP_357681325
VERSION     WP_357681325.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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 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
REFERENCE   4  (residues 1 to 308)
  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 308)
  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..308
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..308
                     /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=31599
     Region          1..251
                     /region_name="fabG"
                     /note="3-oxoacyl-ACP reductase FabG; PRK05653"
                     /db_xref="CDD:235546"
     Site            order(12,14..15,17,36..38,89..91,140..142,155,159,185,
                     186..187)
                     /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 msldgkvaiv tgsgrglgla yaqelarrga avvvndvdae ataeavatig asggravavt
       61 apvgptetae elvsaavehf grldilvtna gvlrdtvlwk msdddfdtvv nvhlrgtftt
      121 vraavrhlrq aggggriici gsptgqrgtf gqtnyaaaka givgmvrtwa lelkragita
      181 ntvvpvaata mtatvpyfaa avraeadgep mpaffrhdlg fgtaadvagl vaflasdaaa
      241 qvtgqvigvg gdrlqiwthp eaaltayreg gwtydalvqa wpatfagaaq svgerfpelp
      301 arfqpatp
//
LOCUS       WP_357681399             202 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357681399
VERSION     WP_357681399.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 18527488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..202
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22178
     Region          7..84
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          78..188
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mteseitrlg vriqayrkmr rmtvrglaad aqaspsfisq lergqtsasi gmlrrisval
       61 gitvadlfnd ddevghrvlr rserpelpmr pgtrkylisq rplqnlemya gefdpgastg
      121 depfthgdsq eillvvrgev tlrlglddae tghrlgpgds veyrtsvphr vindgpetae
      181 viwvvspptp strtplpplp rg
//
LOCUS       WP_357681453             362 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357681453
VERSION     WP_357681453.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 362)
  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 362)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 362)
  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..362
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..362
                     /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=38810
     Region          129..360
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 maivpfsplm lgglsltagv laltvpvhrg ladsgyvfag savllvllav harfvlgtla
       61 rkgvgwwlva vqawltylpl pfvgpawipm sgllsgalll vayrtrsfvp aalamacgpv
      121 llathsealt hagwavtapl lglvefalit laaqahwlsa arsdvihrav alerrrftrd
      181 lhdlvghrlt vlvlktqlir rlvhehdeka gqevdetlal lralasdvra vahggqrssl
      241 etelssaral lesvgvrcqv rvscrdlpre vavalthtlr egvtnvlrha aarecviqll
      301 erdrvvslsi rndgvlpprq pkdggqglan ltervavlgg rletatfhgg hfsftvhipi
      361 nq
//
LOCUS       WP_357681468             583 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora rifamycinica].
ACCESSION   WP_357681468
VERSION     WP_357681468.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 583)
  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 583)
  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..583
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..583
                     /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=61401
     Region          1..456
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          516..582
                     /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(539,548..550,557)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            549
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvirac rdagldsvav yadsdrdalh ttladeayal ggdtaadsyl
       61 ridrlievar qsgadavhpg ygflsenadf aqavtdarlt wigptpqair dlgdkvtarh
      121 laqragaplv pgtpdpvada aevtafaveh glpvaikaaf ggggrglkva rtleeiphlf
      181 esatreavaa fgrgecfver yldrprhvea qvladqhgnv ivvgtrdcsl qrrhqklvee
      241 apapfltaaq raqihdsaka icreagyhga gtveylvggd gtisflevnt rlqvehpvte
      301 etagvdlvre qfriadgekl rftedptprg haiefringe dpgrnflpap gaitalrlpt
      361 gpgvrvdtgv ragdviggnf dsllakvivt getraeaier arrvldemvv egmatalpfh
      421 rlvvrdpaft tepftvhtrw ietefdntvp aftatagpad paapretvvv evggrrlevt
      481 lpaglpggtt taapttrkpt rrggganaga tvggdaltsp mqgtivkiav adgdtvaegd
      541 livvleamkm eqplhahrag tvagltaevg avltagaaic tit
//
LOCUS       WP_357681528             253 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357681528
VERSION     WP_357681528.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 253)
  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..253
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..253
                     /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=26253
     Region          66..252
                     /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 mdsvrspewp vaplgglaan sasarygqpv ggpptpaqhp papppyrppa vpattapvpt
       61 trtgaaaapp ipvklliagg fgvgktttvg aiseiapltt eaemtsagig vddpglgsak
      121 ttttvamdfg cvtidrslkl ylfgtpgqhr fgfmwddlar galgalvvvd ssrlddcypa
      181 idfferaglp fvvgvntfdg rlthelgair walaigdhvp lvqfdardrl svrdallvvl
      241 draldravre kgv
//
LOCUS       WP_357681469             101 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357681469
VERSION     WP_357681469.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..101
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11349
     Region          16..94
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 mshprhalde iihapvrlsi mamlaaaetv efrflrdtie vsdsllskhi htlekagyvr
       61 vekgfvgkrp rtwlaltdqg rsafqdytsi lrqitegppr p
//
LOCUS       WP_357681539             336 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357681539
VERSION     WP_357681539.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   3  (residues 1 to 336)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..336
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35312
     Region          5..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msavleiegl rktyksrrrg vrnaldgfdm rveagqvhgf lgpngsgktt tlrtllglir
       61 pdggrmailg hevpaalptv agqvgaives pqffphftar dtlsllagag nvpavrvdev
      121 lelvglrdra gervktyslg mkqrlavasa llknpkllil depangldpg giremrtlmr
      181 tlaesgmtvv lsshilgeiq licdevtiis lgrrvaagpv eqvlaqhshg gvrvrldaae
      241 dlaaaadllg ragvavtrhp dhlmlagvdk patvsrllae qhlyvselap vsvdlesvfl
      301 eitatapvpg qhrqvdqsak igepghaggt tggwga
//
LOCUS       WP_357681552             367 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357681552
VERSION     WP_357681552.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 367)
  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..367
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..367
                     /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=38502
     Region          134..364
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrsltkgpll lgavlggavt allglvfllp alpfarrtav reaarrlavl evrrlrldpa
       61 alglgaarpd gqelrylaar lpvgvlggmi galllyglgw agllawtwgr glpvdgmppt
      121 apllgyaala gsvllflnls glvgvhvler rlalrmlapd ptealrrrit elaesragvl
      181 aavdserrri erdlhdglqq rlvalsmlag rarrgrpell aqvheqaqqa lvelrevawr
      241 vypsgldslg ladalagvae ragvpvkvvc elsarpprav etvsyfvvse avtnaakhar
      301 agavtvevre hgrmvvvrve ddgvggadta ggglsglarr vaaldgrftv tspvggptti
      361 eaellcg
//
LOCUS       WP_357681581             278 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357681581
VERSION     WP_357681581.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 278)
  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 278)
  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..278
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..278
                     /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=31066
     Region          14..126
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
     Region          148..262
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 medrpattat hepvgrllrr vysrftaaav rddpqardyv vldtladqda dsqhelaerl
       61 ginrtimvrl vdrlqdagyv trtrnpanrr syvlsitdeg rrardamrqa vaerdarita
      121 sltpaerrrl nellslllpe peplqttafl vaqahyrlrr mgdallsgvg lrtrhfgslt
      181 aidelgpcpq qqfaqrldit epaaaqvvde lvqlglvarg rdphdrrrya leltdlgrqr
      241 lvvvhdalgr lqaevldvlg adgerelral larllpeg
//
LOCUS       WP_357681560             119 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357681560
VERSION     WP_357681560.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=13363
     Region          3..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhafdvlgdp irrrilella dgelssgevt tvirgefgis qpavsqhlrv lrdngfasvr
       61 aqgtrrlyav epaplqevdl wlerfrgfwe qrldalatel argkrerrsg dvpsrnenp
//
LOCUS       WP_357681712             472 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357681712
VERSION     WP_357681712.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..472
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..472
                     /product="PhoX family protein"
                     /calculated_mol_wt=49954
     Region          1..469
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mdrrrflara tvamaagiag pfagvacage rggakpvrgy gplrpvadlr dgkvrlhlpd
       61 gfgyrsfsaa gqkfsdgsav pgrhdgmaaf aaprgtaylv rnhevngpvg afgdqdkayd
      121 rmagggtstl rvtrygevmr sgpsltgtmm ncsggpmpwk awvsceetvn gpdvrddfsg
      181 gdnsqltrkh gyifevpvlg aatakpirsa grfahesaaf dptsgalylt edcfgfasgf
      241 yrylppenpv kagrildggr lqmlavkgsp redlsagqrp gavystswvd iddpdptftg
      301 rpsneeavqa vgrqgrakga aifsrlegai hhqgtvyfvs tqggapvpda pvpdgfgkgh
      361 gqvwayetws grlklayesp rssvldlpdn vtasprgtlv lcedgdgdny lrglsrqgei
      421 fdfcrlapia gdpgaefags tfgpgghtly vniqsrhgms faiwgpwhrg af
//
LOCUS       WP_357681751             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357681751
VERSION     WP_357681751.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 190)
  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 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..190
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..190
                     /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=20766
     Region          7..190
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 marqnlarra alvdaaievl aqegargltf ravdaqagvp tgtasnyfan rddlltqagg
       61 riyerlrpda atmrllqega rdrervltlm ralvdrisaf rsgylallel rleatrrpel
      121 ravlterira dvdanvaghl esglpgdats vlllylalnw liverltlpd vfteeeihgl
      181 vaaavervip
//
LOCUS       WP_357681802             245 aa            linear   BCT 28-DEC-2024
DEFINITION  YqjF family protein [Micromonospora rifamycinica].
ACCESSION   WP_357681802
VERSION     WP_357681802.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..245
                     /product="YqjF family protein"
                     /calculated_mol_wt=27122
     Region          8..244
                     /region_name="YqjF"
                     /note="Uncharacterized conserved protein YqjF, DUF2071
                     family [Function unknown]; COG3361"
                     /db_xref="CDD:442589"
ORIGIN      
        1 mqiepvdpap vqtfprtllr qrwadltflh waadpdlvap llpagtrpdt ldgttyvgli
       61 gfrmvgvgfg rgpavpylgt fwetnvrlys vdqtgrravv frsldasrli pvlvaritlg
      121 lpylwsamrl dhdgdlrsyr crrrwpgpag ttsrmvvrvg apisrptple hfltarwglh
      181 traygrtlhl pnwhpqwplh raellhldde lvtagglptp tgppvsvlys pgvpvrfgpp
      241 tpvst
//
LOCUS       WP_357681886             178 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357681886
VERSION     WP_357681886.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 178)
  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 178)
  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 178)
  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 10130719
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..178
                     /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=19836
     Region          46..172
                     /region_name="NUDIX_ADPRase_Nudt5_UGPPase_Nudt14"
                     /note="ADP-ribose pyrophosphatase, UDP-glucose
                     pyrophosphatase, and similar proteins; cd03424"
                     /db_xref="CDD:467530"
ORIGIN      
        1 mrwtvhserd lyrdqwvhva sadvelpdgr hldhriirta apgaglavvt dnkvlliwrh
       61 rfitdtwgwe iphgsirpge dpadaaarea eeetgwrper pirplvysqp spglmtsehh
      121 iftanaatyi gspkdsfesd kvewlpladi selinkrqiv agttlvally llaghptg
//
LOCUS       WP_357681945             379 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357681945
VERSION     WP_357681945.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 379)
  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 379)
  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 379)
  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..379
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..379
                     /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=40543
     Region          1..376
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mdraydivlf gasgftgalt aaylaknagp evrwalagrn rakleglgid apilvadatd
       61 paslaevarq arvvvttvgp ylkygeplva acaeagthyl dltgepefvd rvhvryhama
      121 qrtgakivha cgfdsipydl gvlytvnqlp egvplrisgf lraslrmsgg tlhsgltifs
      181 rplqmiaagt qrrsaepgpr grrissragg lryvggwalp mpsldpqvvg ysarlldryg
      241 pdfeyrqyya vrrlpaaisa vvgagalvtl aqlppardwl msrlqpgegp speqrakswf
      301 nvtflgeggg drvitevtgg dpgydetakm laesalclaf ddvperagql ttasamgthl
      361 idrldragir frtrtatrs
//
LOCUS       WP_357681959             329 aa            linear   BCT 28-DEC-2024
DEFINITION  YihY/virulence factor BrkB family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357681959
VERSION     WP_357681959.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..329
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33999
     Region          22..291
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 msglteriea vkargrrlve swrvrrpsvd hlirtvqryq vqsgdrlaga vtyfaflsff
       61 plvalafsvl gfvlsndqna idaltkavne qlpgiagqld isgiaqakat agiigllgll
      121 yaglgavdal rgalremsmt tvpplnffvg klrdlvslvl lglsmlasvv vggfatqata
      181 tvvnfltlda talntaglfl aglvaglgad wlifvivlgw vappvgsfry vargallgav
      241 gfgllkqlag lllshtlgnp lygtfavivg lllwinfsar lvlyvaawta taglsppptp
      301 spipssgspq egappgrsps sppgeasaa
//
LOCUS       WP_357682020             239 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357682020
VERSION     WP_357682020.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24441
     Region          16..237
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrevvvtggg tgigyaiada fislgdhvti tgrrehvlke aagrlgcaav pfnaaspvav
       61 qeavtslper vdvlvnnagg ntnldrqepg dlmevaesww anlnanllsa vlvttallpr
      121 igkggrvvsi gsiaargtgs gsygaakaal eswtadlaaq lgpkgatanv vapglvvdte
      181 ffrgrltdeg irarventrn grpgtpadva dtviflasrg arhltgqvlh vnggaylgr
//
LOCUS       WP_357682037             310 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Micromonospora rifamycinica].
ACCESSION   WP_357682037
VERSION     WP_357682037.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..310
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34105
     Region          13..198
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mteattaghh qpvtvviatr drpgllerav aavldqdypg pvecvvvydh tdlrelavdv
       61 pagrslryvr nthrqglpgg rntgvdeata aliafcdddd fwlpaklrrq vellaqrpda
      121 aaascgirle gpgiakerql draevtlpdf vedrimevhs stilirrstw daigpvdedl
      181 pggygedyew llriaghgpv vivpevlvvv dwhggsfffg rwativeatr ylldkhpela
      241 gsrtglarlh gqiafalasg rrrreavrel grvvrlnpre krvlvtvpvv lgllsgervl
      301 rlaqrrgrgv
//
LOCUS       WP_357682172             407 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357682172
VERSION     WP_357682172.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..407
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=42426
     Region          2..>296
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mphrivvlga gytgaiaagr lakrlrredv aitlvnaepd fvervrmhql avgqnlksrp
       61 fsdmfagtgv elrlakvtgv dvdrktvali dangagliap gsgaeelayd tlvyalgsgw
      121 naqgvpgtae hayeiasrpg alrlrerlar ldagqtvvvv gggltgleaa teiaearpdl
      181 dvalaarggl gdwlspkgre hlrkifgkrg itvhehtavt gveadrvata ggmaipatvt
      241 vwttgftvht iakatalevt gtgqivvdrt mrsvshpdvy avgdaamaig pgdkplrmsc
      301 asgtptawqa adaiaarltg gklpnapiry fnqcislgrk egliqyvtad dravqavltg
      361 rlaavykelv cktaawgvan ptlglptrrr rvtgdraeag savkava
//
LOCUS       WP_357682174             238 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357682174
VERSION     WP_357682174.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   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 238)
  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..238
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..238
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=25282
     Region          1..228
                     /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 mvpaladhhh virvdlpgcg qsppalsydv pvqagrvaav lddlglrqva avghssggyt
       61 atalaeqrpd lvrslalist gpsldallpq plllrallap plgpllwprr sdamirrais
      121 atcarpvdip ddlvadvrgt tyrtfrtvlr rntayiaqrg vpdrlaalev pmlvifgtad
      181 rrwepssahq ydavpnarve llpgvghipm feapeatsel llgftattad sppvipea
//
LOCUS       WP_357682288             428 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357682288
VERSION     WP_357682288.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..428
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43883
     Region          112..419
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mksphkaall rramavavat laaaaattcp atattagtga tgagtahaet arakttaats
       61 raettvaqai sgargrpltv rplkggaalp saartwsvty vsegatgtri avsgtvavpk
      121 ttpppggwpv iswahgttgt advcapsrdd englahdyls smrptldawv argfavvqtd
      181 yeglgtpgeh pymngrsaan tvidivraar rvdhrvgrdw fvaghsqggh atlftaaasd
      241 agkglrlrga vsiapggwgl sqlvpyaqhn lpvpvdvlaf lptvvigasa vepaadpeei
      301 ltdemrplla aartacvaqv ravaastpvg qvirtgadta pltaylrtqe pvgirvkvpt
      361 lvaqgthdal apkqstdlmv adlcrqapki tyriydgadh raavprsfdd alafvrtila
      421 gqtpattc
//
LOCUS       WP_357682350             367 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357682350
VERSION     WP_357682350.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=37345
     Region          28..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 maghgdasgg gpgvagqvld tpltrlvgvr hpvvqtgmgw vagprlvsav anagglgvlg
       61 satmtldela aaikevrsrt gapfgvnlra dasdaadrid llirngvkva sfalaprrel
      121 iarlkdagvv vipsvgarrh aekvaawgad avlvqggegg ghtgavattl llpqvvdavd
      181 ipviaaggff dgrglaaala ygaagvamgt rflltsdssv pdavkqtyls msetvvtrqv
      241 dgmphrvlrt glvdglersg rvtgmiravr naarfkkisr mswaamirdg lamkhgkelt
      301 wsqvlmaant pmllkaamvd grpdlgvlas gqvvaliddl psceeliggi vaqaagvirg
      361 lganltg
//
LOCUS       WP_357682363             372 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora rifamycinica].
ACCESSION   WP_357682363
VERSION     WP_357682363.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..372
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..372
                     /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=39858
     Region          1..365
                     /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 mrhriavvgg gpggltfarv lhrhdhpvtv lerdrapdar ppggtldlhe glgqlaldka
       61 glragfeals rpegqamril dpsgtvlrdw rprpderanp eidrgqlrdl lisgldvrwg
      121 revtrvvpgt gdgalvhfad grqetfdlvv gadgarsrvr pavsavtpry tgvtsvetsl
      181 ddvdtrhpdl arligdgsvs aygvnrslta qrnsgghvkv yakfrapldw hagwdladve
      241 avrtgllalf egwaapvldl lrhgsafvhr pfhtlpvsht wthvpgvtll gdaahlmppl
      301 gaganlamld gaelaesiva apddldgavr gfeermwvra grwaelttag lerlvsadpa
      361 eavalfdevq ps
//
LOCUS       WP_357682401             491 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora rifamycinica].
ACCESSION   WP_357682401
VERSION     WP_357682401.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=53836
     Region          1..437
                     /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 matehvdvli vgaglsgvga achlrrdcpg rtyavfearg avggtwdlfr ypgirsdsdm
       61 ftlgysfapw tdpkaiadgd airryvrdta rrygveehir frhrvlragw dsatarwtvh
      121 arredtadev vltcdflyac tgyyrydagy tpdfpgvery agrvvhpqhw padldltgrr
      181 vvvigsgata vtlvptlaqr aghvtmlqrs ptyvlalpsr drladalrrw lparlaypvv
      241 rgknvlfgav syrlsrrapg larsflrraa rrrlpagydv drhfsprydp wdqrlcvapd
      301 gdlfaalaag rasvvtdtve tftpdgvrlg sgeelaadvv vtatglrlla lggmtltvdg
      361 advdlgrtva ykgmmlsgvp nfaltigytn aswtlkadlv asyvcrllrh ldatgqqvvt
      421 pvppadgels plidlrsgyv lrslhtlprq garapwrlhq nyprdvllmr ygrlvdegvr
      481 fsratagapa g
//
LOCUS       WP_357682491             426 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357682491
VERSION     WP_357682491.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ogura,T. and Wilkinson,A.J.
  TITLE     AAA+ superfamily ATPases: common structure--diverse function
  JOURNAL   Genes Cells 6 (7), 575-597 (2001)
   PUBMED   11473577
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421745
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..426
                     /product="ATP-binding protein"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45910
     Region          14..408
                     /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"
ORIGIN      
        1 mpawrlrdfh dddldraiql wdqdrqadds ppvfpisevm aaaragefai vavvgddmvg
       61 mavaqaqger awitlvalsg mwrnrgigsa ligelerrlr gqgirrisal rppgatgtta
      121 lensgfltra glifyekveh lgasdaglla elggrvlprg lwdslggmep eketierriv
      181 lplaepalae rygvtppkav ilfgppgtgk tsfakavasr lewpfvelfp srlasagagg
      241 latslrdafa dlaeletvvl fideveeiag vrsgvavdpg hgvtnellkl ipgfrdhtdr
      301 llicatnsvr sldpaflrpg rfdyvipvgp pdavaraaiw qrylgpaagg velhrlvaas
      361 emftpadief aarkgaqaaf erevvhrlga pastedylaa iadtrptltd qalarfredi
      421 ehyvrm
//
LOCUS       WP_357682493             852 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357682493
VERSION     WP_357682493.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 852)
  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..852
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..852
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=89971
     Region          9..849
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          558..586
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(559,562..563,566..567,569,599,602..603,606..607,
                     609..610,639,642..643,646..647,650)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          591..633
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          638..666
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgddvddfav llrahrtrrr ltqealaela gissrsvgem ergngrsprp gtlehlatal
       61 elsgeereef vsagralfwa srarptgssa prrapagaad pppwtlpadl sdfvgrgdel
      121 allgealdpa shrarlavis gppgvgktal avhaghrfaa rfpdghlyaa lrcvtgdpak
      181 pldvmahllr llgldgsalp tdvdacagll rarlagrril lilddatgyh qvepmlppeg
      241 vavvvtsrmp ltglpgvtam dlrplpdpva vellcqvaga ervraepsaa adlvaacggl
      301 plalritgar laarphwmlg tlterlader rrldelrhgd lavrpglqlt yrgltpaaar
      361 afallgalsv psfpewpvaa lldvgpaqga aaleelldar lledlgldqa gqsryrfhdv
      421 trlyaqerre aefdqtawrd alaraatgwl alarhaqdhl dcerfhlddr sghpatvade
      481 ravavatgrp vewfeaerea lavlvsacae aglahaargl agcgadfyel rayygdwrra
      541 mesglaacrr agdrpgeaam lrglggclve lddleaavst lraaralake mgdpagaama
      601 rkdigfvlsl sgrlneaeld lrdaaeelgr agrkptkvma ltslgfvqrq qgdlagavat
      661 irdalrvars cgdrfahafa lrglagalva cgqareaelt arqaaalfar igdrigaaqs
      721 lrvlgealaq edsrlaeaeq tlaaaaavfr egghawglal telslgeiev rrgsteaagr
      781 lrrslefwte eqvpalrara lvslasaaeq agdpaargll teayglyqel gspaaaelaa
      841 rlglpesaas pa
//
LOCUS       WP_357682508             200 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora rifamycinica].
ACCESSION   WP_357682508
VERSION     WP_357682508.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=22276
     Region          5..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 mdgpvvlrpy rrsdavawsq vrranqawls pweshlpgsw neanspaafr yvhadqrrsa
       61 rtgegmpfav clreggqerl vghlnvgsiv rrafcsgyvg ywvdsraagr gviptamala
      121 vdhafgpggl hrvevnirpe nkpsrrvvek lgfreeayhv rymhidgawr dhigyamtse
      181 eaaadgglla rwhrlrhdvg
//
LOCUS       WP_357682550             422 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357682550
VERSION     WP_357682550.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 422)
  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 422)
  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..422
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..422
                     /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=45076
     Region          113..>325
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mpysdattpt drylsreivv esrdegllla elkgfvagep egdhvlgltr irldsldrfp
       61 fdpeldarmr deagttarga dpsdldrvly hlrdrfqrtt qwvprmakir myaegtpytg
      121 ggtgdpqela agtevviepr esyqgprvri gildgalyrh pglaghylad ssvfgatdht
      181 dppatlghav hlagivarqa pgadlvirqa ldasnevdsw tlakamvrfs gevdllltsl
      241 ggatwddkrp fvleraesrl dcvhvasagn wgkvvrpgpy psptrdsaif paalpgviav
      301 galddeggra dysqsgpwms lmapgahdgl fleraallar nshgalvant drkpvnfggv
      361 arwpgtsasa ayvagalaav amaqgtslqe aaetvlsghp glaqeipqvr girpyspdrd
      421 ry
//
LOCUS       WP_357682644             475 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357682644
VERSION     WP_357682644.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=50574
     Region          27..475
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mtipypniqp aptispvtpp sgaprprvtf lgtgylgaty aicyaelgye vlgfdvdvdk
       61 iaklnagevp ihepgldell rrnlaagrlr fstdiaetaa fgdvhficvg tpqradgmga
      121 dlsyveasvt alaqqltrka livgkstvpv gtaewveqlv gkhtpddlgv evawspeflq
      181 egfavddvlr pnrivvgvks ewanamlyaa hkgvfdlaat edrevplvvt dfataelvkv
      241 aanaflatki sfinamaevc easggdvtql araigydpri gnrflqaglg fggaclpkdi
      301 rafqaraqel gagealrflh evdlinlrrr trvlqlaadl lgrrsgpagp dfsgtriavl
      361 gatfkpntdd vrdapalava allakagadv hvydpqgten arriapelcy epsindavsg
      421 adlvcvltew adfrnadpvv lgelasgrkv vdgrncldaa lwtqagweyr gmgrp
//
LOCUS       WP_357682740             345 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357682740
VERSION     WP_357682740.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..345
                     /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=37475
     Region          12..336
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mtgpaspakv rgetilavde lvkhfpitrg vvfprqvgav ravdgvsftl rrgetlgivg
       61 esgcgkstla rvlmrletpt sgratlegrd llsasggelr rlrrnmqmvm qdpytslnpr
      121 mtvgdiigep fdihpdaapk gskrgrvqel ldvvglnpeh vnryphqfsg gqrqrigiar
      181 alalrpeviv cdepvsaldv siqaqvinll eqlqdefgls yvfiahdlsv vrhicdrvav
      241 mylgrivetg teeevyerat hpytqallsa vpvpdpdard atdiirltgd vpspadppsg
      301 chfrtrcwka eeicaredpp tvprpadphp sachfaalrd pqggg
//
LOCUS       WP_357682761             185 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora rifamycinica].
ACCESSION   WP_357682761
VERSION     WP_357682761.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 185)
  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 185)
  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..185
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..185
                     /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=19396
     Region          4..>107
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 maadpsdpar lgtrlrhlwe lldgdvaavh adlgltgmrp ryapvliald rlgpasirtl
       61 aeatgvthsa asqtvarmvt dglvtlapgv darqrivtst drarellpvl raedaatara
      121 argleaelay plsrlvdeal aalrrrsmrq riadvapdlv athradggpa agasgdrpqp
      181 pgdrn
//
LOCUS       WP_357682800             275 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora
            rifamycinica].
ACCESSION   WP_357682800
VERSION     WP_357682800.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 275)
  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 275)
  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 275)
  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 275)
  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..275
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..275
                     /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=27491
     Region          4..258
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdlglkgrva lvaggssgig lacakefaae gaqvaicgrd pdrlaaaere vaqvasgrvs
       61 atsvdltdpd aarrwvdava adlggvhvlv agggsppvgt atgfgvedyr aavdrvllpa
      121 valataalph lraagwgrll fvasetacvp igplvlsgvt raalvrfaqg lavdvgrdgi
      181 tvnvlapggv rtppmeraaa rlatdgdvea rlramghhsa lgrlarpdev aavaaflase
      241 rasfvtagvh lidggaaatg pdlphltgvr kdtya
//
LOCUS       WP_357682567             820 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Micromonospora rifamycinica].
ACCESSION   WP_357682567
VERSION     WP_357682567.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 820)
  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 820)
  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 820)
  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 820)
  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..820
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..820
                     /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=91120
     Region          9..>636
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtcttlhegw rlranggpap dvlagrdipa qvpgsthldl maaglipdpy ldsneasltw
       61 mhrvdwqyat afqasapgvg eqvelvfdgi dtiatialng vvlgrtanmh rgyrfdvret
      121 lreghneltv tlgaaltyae qaesqlgwrq rayphpynai rkmacsfgwd wgpdlqtagi
      181 wkpvrlerwd tarlaqvrpl vavdadgtgr vevhlevera adrdytavvt vagreertav
      241 agnaahvtvl vpdarlwwpv gygeqplydl tvtlladaea vdtdrrrigf rtvtvdtepd
      301 gtgtpftfvv ngtrvfakga nwipddhllt rvtperlarr idqavganmn mlriwgggiy
      361 etddfyaacd ergvlvwqdf pfacafysee eplwseveae arenitrlva rpslvlwngn
      421 nenlpaytdw kgwresldgr swglgyytel lpalvtaldp trpyapgspy spgdlppnda
      481 pygtrhewdv wnmldythyr dhlprfcaef gfqgpptwat ltrwirdqpl tptspafllh
      541 qkahdgngkl drglaphlpv pddfeqwhwa tqlnqarava fgiehfrsww pytagalvwq
      601 lndcwpvtsw aavdsderpk plyyalkhaf aprlltvqpr hgrptlvavn dhdqqwtgtv
      661 saarqtltgg ilatvempld vaprsvalld ltddlltpvd prsellivag ggirvhhqfa
      721 edrdlaydpt pftaevtpvt ggyrvdvrat syvrdlalla dkvapdavvd dmlvsllage
      781 thtftvrtaa sladpsalrh prvlrcanaa araeerpdkd
//
LOCUS       WP_357682806             433 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora rifamycinica].
ACCESSION   WP_357682806
VERSION     WP_357682806.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..433
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..433
                     /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=45406
     Region          17..427
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mattpapgdv pgrgdpdvlv vgagvaglfc awflrraglt vtvvdrgevg dpaacssgnt
       61 gfvgtqgaap laepgvpakg lrwlldpesp fhvrprldre lltwlwhfrr hcterqarag
      121 fevlldlkqr slailrevca hdelagtlta rgmvlacktp egyaqaratv paavargvpl
      181 rvldpaelar lapgvefava gallneegaa lripaflvaf arllraagve iltgtevrgf
      241 htvdrqvrav rtsrgdlrpg evvlaagvws vacarqlgvg lllqpakgya vtvdsgpatp
      301 tlpvllsegk vavmplgdrv rlagtleltg ldttvsprrv agilrtvrsy lpamdtggqv
      361 qvwtglrpct pdslpligrl gsyrnvsvat ghghigmgla paggrllaql vtgtppdvpt
      421 atfavdrhrr ghr
//
LOCUS       WP_357682809             234 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357682809
VERSION     WP_357682809.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..234
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25780
     Region          15..223
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 meiraatelp arrepielht gdgltlvgel arpldrppva tlvtlhplpt hggfmdshly
       61 kkaanrlpal adlavlrfnt rgtssdrgts qgafdkgege rydvaaaley aefhdlphiw
      121 vvgwsfgtel alkwahdpav egavllsppl rrasdddlda warfgrplva lvpefddylr
      181 peearrrfar vpqaevigvd gakhlwvgep yvrvvlneiv krvnpaaypl pthv
//
LOCUS       WP_357682814             254 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357682814
VERSION     WP_357682814.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25745
     Region          4..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 mgafdlsgkk alvtgaskgi graialayae agadvalvsr saarlaevak eveahgreav
       61 vipadltdrd qaagavhgai dalgrldivv nnaggsnflv efkdlrlsgw dklmrlnlds
      121 amavchavap hllergagsv invasaaalg apllapyaaa kagvvaltks lavewaragv
      181 rvnalcpgwt atdlnrnlwd deaasastia gvpmhrwgsa eemahpavfl aapasaymtg
      241 qvlfvdggmt atag
//
LOCUS       WP_357682829             386 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357682829
VERSION     WP_357682829.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..386
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41008
     Region          6..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 maeetpgrtg plhgvvvadf srilagpyat mlladlgaev ikvegpggdd trtwmppvrd
       61 dvstyylgin rnkrsialdl kdpddlavah rlaaradvli enfkpgglrr faldydtvaa
      121 gnprvvyasi sgfgtgagag ypgydlmvqa isglmsltgd pdgppyragi svfdvmaglh
      181 asigilaalh hrhdsgrgqh vevnllssal sglvnhssgy vaggvvpfrm gnahpslfpy
      241 eplpvadgel iviagndgqf rrlcqvldlp elvddprftr nqdrtanrea lrpllverlr
      301 rrtrdewftd lmaagvpcap intidggval aerlgldpvv tvgegaaavp girhpitlsd
      361 tparygtppp aldehgeeir awltgs
//
LOCUS       WP_357682946             399 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357682946
VERSION     WP_357682946.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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..399
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..399
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=43309
     Region          54..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          55..87
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          95..121
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(97..98,101..102,104,128,131..132,135..136,138..139,
                     164..165,168..169,172)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..186
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          196..226
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          231..259
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrslvlacgv vlagalaftt vavsapeqrq eqqaapftet lqarlkrlpg dyrgwarlgm
       61 eyvdqtritg dpsfyakaeg alataarlap eddavltgqa vlaagrhefa davrlanrai
      121 dvnpysapah gvladaktql gdlrgaekav drmlslrpgv paftrasyaa elrgdrdrar
      181 eflqdaedda flpadrayar hylgelalhs gdlrtagewy gkalqaypay tpalagqakv
      241 aalggrltea ltlyervvqr lplpqylieq getrmkaglt adwtllraqr ellrsagvrd
      301 dltwaefead hgdpalavrh araeyarnpn lvaadalawa lfqdgkpraa lryarkatst
      361 gwhhpligyh rarieqalgl parvdpafdp slpalgrfs
//
LOCUS       WP_357682958             274 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357682958
VERSION     WP_357682958.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 274)
  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..274
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..274
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30116
     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          90..267
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mssgpdlsfa vppevafgre lralrhaqgw sldafgkrig ysgtmvgyye rakrpvpeaf
       61 vakaeevlgl sgelvtlwka vnpqtapkwf rqwpkiesaa rtlrswepll vpgllqteey
      121 asavlraepg vteeqikdal etrlrrqaif srptpptlva videgilhrp iggksimydq
      181 lthllalmdh pnitiqvvpl avganggllg gfavahrpga pdaayletag ngqvtdrvee
      241 veaislrhdt irawahplhv trdviremiv ryeq
//
LOCUS       WP_357682991             409 aa            linear   BCT 28-DEC-2024
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357682991
VERSION     WP_357682991.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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 409)
  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..409
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..409
                     /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=41746
     Region          74..347
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrvrgrtaaa iaalllspvg vpagavaavg avttgpcapv paasrpprpv pprtdpaart
       61 vggpalatra qvrptgtrvp pavpaaswlv adldsgdvlg gcgpheygtp asvqklllaa
      121 tvlpkldprq tvtltpgdld iepgssavgf aeggryriet lwlglllksg neaanalarl
      181 gggpdglpgg lramnaharq lgalqthavt psgldgpgqf tsaydlalia racfadatfr
      241 rydttreati paqpalgeka fpiendnqll yrypgalggk tgytdlarht yvgaaerggr
      301 rlvvtllgae vldrrgweqg aalldwgfgv prgaavgrlv npgeltagps atavtpppla
      361 aaggpgrldp pghpwsrplv avslaavvag lagllfalrh rphdgrrrr
//
LOCUS       WP_357683022             201 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357683022
VERSION     WP_357683022.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 201)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..201
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..201
                     /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=21850
     Region          2..198
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 maqrksrtdr ridlieaarr aiirhgvdgv qlshvaeeag ltsgavlyhy pdlsellvea
       61 qhagmerfye qrlrqlatit dpvtklattv rsglptgpld pdvrllnelg gaagrnrmyg
      121 vlltslydrq vsmyqsildt gaalgvfrls gdsltiarnl valedaygyr itarhpligp
      181 aeaaelilsy artatgndlv h
//
LOCUS       WP_357683088             448 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora rifamycinica].
ACCESSION   WP_357683088
VERSION     WP_357683088.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 448)
  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..448
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..448
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47038
     Region          54..429
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtlittrpgp gnarpyrfpt vvrrdvaggr vvaahlpgqt lavallllda gagrepvgke
       61 glgavlakal eegtvqrdat gfalaveglg telatgldwd sfqvsvqvpv drlvaavrll
      121 aeavrtprld pddvrrvrdd eatalrmdwa npgpradavl radlfgaanr wgrplygdpd
      181 svagldvedv tvfhsewflr pgtlivagdl drlnldalga aafagtgggp verggpievp
      241 lpagrriilv drpgsvqstl rlghpsphra hpdhvpmtla gtvlggafts rlnhlirevr
      301 gytygirgdf assrrfgrfa vssgvqtavt apalveavge itrtraggvt edelavarsw
      361 ragqlsvelq spraiasalt tlvvhdlpdd yharlreell aadvaqvsaa aathlhpdal
      421 tlviegdagl irddlvasgl gevtdhag
//
LOCUS       WP_357683141             502 aa            linear   BCT 28-DEC-2024
DEFINITION  M28 family metallopeptidase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683141
VERSION     WP_357683141.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11978080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..502
                     /product="M28 family metallopeptidase"
                     /calculated_mol_wt=51987
     Region          51..>96
                     /region_name="PRK12893"
                     /note="Zn-dependent hydrolase"
                     /db_xref="CDD:237250"
     Region          109..>205
                     /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"
     Region          230..483
                     /region_name="M28_SGAP_like"
                     /note="M28 Zn-peptidase Streptomyces griseus
                     aminopeptidase and similar proteins; cd03876"
                     /db_xref="CDD:349873"
     Site            order(276,288..289,320..321,349..350,401,404..405,421,
                     448..449)
                     /site_type="active"
                     /db_xref="CDD:349873"
ORIGIN      
        1 mrfslmkgvt aviaalalpl alaspanags lddgfakllv kqvkgtnvtk hlnalqaian
       61 anggtraagt pgydasrdyv adklreagyk vtldpidfve gwtennpptl eipgqktyap
      121 nedfftfqps pagdvtaqvq gvdltlpptp tptstsgcet sdfagfvpgn ialiqrgtca
      181 faakirnagf agasgiivfn egqpgrtdaf pldigewrag vpmvfadfav gnelaatpgt
      241 tvrlkvdatl qlgtnhnvia etrggdpgkv vmvgahldsv pvgpgindng sgsaaileta
      301 lqmknfpvkn kvrfafwaae eigllgsdqy veelpqaqrd rikvylnfdm vaspnyaykl
      361 ydgddsdgeg spagppgsaq iekqleaffd grglahvgtd fdgrsdygpf iavgipsggi
      421 ftgaegikta eeaalfggta gvaydvcyhq acdttanvna taldvnadai adstaryafn
      481 lgsipardda aaaariavks ag
//
LOCUS       WP_357683146             472 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683146
VERSION     WP_357683146.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=49369
     Region          3..394
                     /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 mnlpdtgatv eellaevarl kehdlpvrgg qvtayvydtg rgevheaaar ayfemlevnc
       61 ldptafpsiv emekqvvgav adllggghgv ftsggtesim lavkaardaa rrdrpnlvlp
      121 vtahpafhka ahylgvavrp vpvdlgtyqv lvpavkeaid edtvlvvasa psypqgvvdp
      181 ieevaavaaa anvpchvdac vggwllpwlr eagadvppfd lsvpgvtsls cdlhkfgyap
      241 kgasvllfad pamrrkayfa saawpgytii natvqssrsa gplggawatl ralgrqgyve
      301 lgratlraat rlregiaeip glevlgrgds sliafrgtdv dvftladear argwflqpql
      361 syagipanlh itvtgvtlag veamlqviae saeaarlrgp aelpeglvdl iagldldald
      421 datfaelaas vgvdlrpgag qpemavvnav ldalpaatre ailvrflsvi yq
//
LOCUS       WP_357683167             291 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683167
VERSION     WP_357683167.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=31605
     Region          4..286
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mqvpapleye ratsvdhaig llerlgdsar lvagghsllp mmklrlatpe ylidindlhd
       61 qlgyikvess qirigamtrh relleseala etfpifrdae rviadpvvrn rgtlggslcq
      121 adpsedlsav cttlgascvi rnrdgervvt meefhrgpye tavgdaemlv eirvpirrng
      181 ssayekverr agdwaivsag aavwlddgvi sdarvglaav gpnttglpav sealrgreps
      241 eevyrlagdl aaqhcspatd mrgsadykrh lameltrral rrsvarlngr v
//
LOCUS       WP_357683183             409 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683183
VERSION     WP_357683183.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..409
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=43924
     Region          18..401
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 msgsrptrpa mlpgvdraaf aaslavrlrq rgvpvgltgv edfvraldva qprslpelyw
       61 aarislvrrh seieifdeaf aaifdsvgpa ldpharrrpl artngsddaf vplpdaragg
      121 ddagglpwtt lpavvagaeg pdgstavpel lpsdaeglad vpfeelgdre cellgrwlee
      181 aaadwptrra rrfrvsprgr aiavratlar srrtgwepfr larkrpvvrs rrvvmlcdvs
      241 qsmqaqasay lhlmralavt vdaevfafat tltrltpvla hrsaaaavgl atervtdrfg
      301 gtriatnvra llashhgakv rgaivlvgsd gwdgdppeel gaamdrlsrr ahrviwmnpr
      361 aaapgfeprv asmaaalpyc dlmlpahtfg slrdvigavg gvagsrfrw
//
LOCUS       WP_357683224             507 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora rifamycinica].
ACCESSION   WP_357683224
VERSION     WP_357683224.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 507)
  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 507)
  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..507
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..507
                     /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=54525
     Region          1..507
                     /region_name="COG3920"
                     /note="Two-component sensor histidine kinase, HisKA and
                     HATPase domains [Signal transduction mechanisms]"
                     /db_xref="CDD:443125"
ORIGIN      
        1 mstlrdlaee htklrpadid hlhriagdwq llsdlsfadl llwvpvdddg tflcvaqvrp
       61 ttaptayldd qvgrivggpe vahlevayrq griwregdpv wygdvparhe aipvrlrtae
      121 geageviavv grdtnlstar tpsqlelnyl ttaddlaqmi adgtfppprh pgettsaprv
      181 gdglvrldag gkvtyaspna qsayrrlgya shlvgedlak lhrrlasdpl dgteaangil
      241 aalrgegppr reidargatm ltralplmpa gvpigalvlv rditevrrrd ralitkdati
      301 reihhrvknn lqtvaallrl qarrvampea rvaleesvrr vasialvhet lsmssdeave
      361 fdgivdrvas aatevaatev svgmrrtgsf gvlpaeiats lvmvlnelll navehgfppv
      421 eeggetaepd vrpevvvsah rhrkqlhvsv tdngrglpae fdadrggrlg lqivralvtg
      481 elrgsielrp gptggteavl vlplaka
//
LOCUS       WP_357683233             236 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683233
VERSION     WP_357683233.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 236)
  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 236)
  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 236)
  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 236)
  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..236
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..236
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25690
     Region          1..203
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 myeavlfdmd gvvvdtehsv tefwqrlars egfsiapddl erhvyghrad htlrelfpsv
       61 spdrygevyr rlrenqeslr ytaipgvlrl laelsdarvp valvtgaqdw kaaevlgqld
      121 laetfdvlic addvalgkph pacyllaadr lsaaigdclv fedaisgvts avtagaacva
      181 lapphraaqv ieagastver dferisfdpy ehllrvggqt gfgfaaares rylran
//
LOCUS       WP_357683269             312 aa            linear   BCT 28-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Micromonospora rifamycinica].
ACCESSION   WP_357683269
VERSION     WP_357683269.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=33412
     Region          1..311
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mrdiavfsgt ahpdlaaeic shlgvplhpv rvsrfandcl evqlqancre rdvfliqplv
       61 ppvqehlvel llmidaarga sagritvvlp hyayarsdkk daprisigar lvadlltsag
      121 aqrvlamtlh spqvhgffsv pvdhlhalre laahfrgrel gntvvvspdl gnakeaaafa
      181 rmlgtpvaag akqrfsddrv tistvigevd grdvivldde iakgstviel iahlrernvr
      241 sirlacthgl fssgalarls atdgvceivc tntvpipqek rvpklevlsv apalaeamrr
      301 ihngesvsal fg
//
LOCUS       WP_357683372             316 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683372
VERSION     WP_357683372.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 316)
  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 316)
  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..316
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..316
                     /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=35608
     Region          6..202
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mpdfliigvp kagttalhaa lhrhpdlfls pvkepkyflt dgpppteggp gdaetyrehv
       61 wrredyealf aaappgtltg eatpfylydl aaqrrireav pharlivilr dpverahsnw
      121 thlwsaglep igdvvracae eerriaagwa hfwhyvglgr ygeqlahlft vfpreqvlif
      181 ryrdlvdrpa etldricafl gvrrglltvl pkenvtahpd asprhallss frrrvpssla
      241 apiekllqhr gdsrrpltwe qrqrlipyfa advqllqrvt gqdfggwlrp rersgglvgt
      301 rppgqrqsrn grpppa
//
LOCUS       WP_357683306             224 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357683306
VERSION     WP_357683306.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 224)
  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..224
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..224
                     /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=23751
     Region          2..168
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mrdtvriwtv parvtpdela ryhavldage rsraaalada atrdrftvgh galrllvgri
       61 ldvpperlrw srgrhgkptl adpgggpqts lsysadlval avgghrpvgv diqhlapgld
      121 pvglasrffa teearqvasg ttagvradrf arlwarkeav vkaaggrlwp nlampvhrgd
      181 lvrcadpvgv hrvtdvvtpa gyriavaltg daryvvescr glag
//
LOCUS       WP_357683429              97 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Micromonospora rifamycinica].
ACCESSION   WP_357683429
VERSION     WP_357683429.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=10677
     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 mvlevaliev tpgheddfaa ayaqahaiiv avqgcrsvrm trgiespsrf vllvewdsvq
       61 aheqnfrgte afdrwralig phfaapprve hfvdvpa
//
LOCUS       WP_357683435             309 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Micromonospora rifamycinica].
ACCESSION   WP_357683435
VERSION     WP_357683435.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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..309
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..309
                     /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=32256
     Region          124..309
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 melepgreal vrvavatlwt dpgatrpvdr palavpsdtd gwitgmdatq rvgdcvlsql
       61 llgervlvta vppggwaevv aveqaaprrd prgypgwlpa aqlapapptr drrtpdgdpp
      121 aplvvdavst dlraapggpv alsgvvlgtr lpalgpavgg wrpvrvpgrp dplwvpevdv
      181 aglpavapsa ddvlavaarl rdvayvwggl sghgidcsgl vhlawrrfgv plprdaddqa
      241 avttpvpage erpgdlyffa rpgrgihhvg lvtagsgprm lhacyrqqrv laeplppdrv
      301 atlvgahrv
//
LOCUS       WP_357683450             709 aa            linear   BCT 28-DEC-2024
DEFINITION  MMPL family transporter [Micromonospora rifamycinica].
ACCESSION   WP_357683450
VERSION     WP_357683450.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 709)
  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 709)
  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..709
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..709
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=72893
     Region          50..691
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mslftrvars rlaawltvva aivvgavvfg lprpdnpapv sttglsaqwq stqverlqdq
       61 lpqrdvqpai vvvsrddgaa ltdadraavt drsaalgrla vggqvsppqv spdgtvalla
      121 vpldtaggqq avadevaqvr davgglpggi tvavtgapaf tadltkvfeg aditllavta
      181 gvvallllit yrspflwivp livvaateql tlravetivp avginlqega vtgiasvlvf
      241 gaatdyalll iaryreelrr dedrfaamra avrrtaepil asggtvvlgv ltlllseqet
      301 nralavacat gvvfamlsal fvlpavlvif grglfwpfvp rvggparegk lwgrlgaavv
      361 rrpvpvaala tlllaglalg glgirtglse teqfrvepea vagaqtlara fpagttqpva
      421 vltnpaaapa vtrvaaavpg vasarpgpag gnvaqvdvvl tdepgtpasd ravealrdav
      481 aavpdsappa vegvdppdga lvggtvaaty dsdeantrdl wlilpiilvl vlavlvlllr
      541 gllaplllvl tviasffasl gaawllfdhv lgfpaldsgv lllafvflva lgvdyniflv
      601 traredarva gtrdgmlsal rvtggvitsa gillaavfav lgvlplillt qigiivclgv
      661 lldtllvrtv lvpalafvlg drfwwpgrih rdaptdavpa artpaaard
//
LOCUS       WP_357683518             215 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357683518
VERSION     WP_357683518.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..215
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23098
     Region          <46..204
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mplllldldn tlldragpfr awaegflaei gapatdidwl lsidadgltd rwdiadaird
       61 ryalripsid lveelhdgvv gytrldplva calriaddag wlpvvvtngs vrledakirq
      121 tgldryvadw viseeagvsk pnprifalaa qrarlplrga wvvgdspesd iggaaavglp
      181 svwlhrgrsw tdtrfaptrt vdsliaavsv vlagg
//
LOCUS       WP_357683600             338 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683600
VERSION     WP_357683600.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 338)
  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 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 338)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..338
                     /product="GlxA 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=36384
     Region          21..326
                     /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 msagsvavvv seeigvpswd lyelsipctv fgkpqsdlad pwydlrlcgt gerpgdaapa
       61 dsglvlqtry glddlvgadt vivpsvpdsc ieegkplpqa litalrrayd ggarmvslct
      121 gafalaeagl ldgrpatahw mhtallaery pkvhvddsvl yvddgdvlts agltagldlc
      181 lhlvrrdlga hvanqmarrm vvpahrpggq aqfidvsvpa eddeglapvl dwaraqldqp
      241 ltvhdlaqra amsprtfyrr lqaatgttpl qwllfqrlgr arillestdl pvekigelsg
      301 lgtannlrrh flrhigisps dyrrafprtm pesspsal
//
LOCUS       WP_357683603             294 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683603
VERSION     WP_357683603.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 294)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..294
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30517
     Region          8..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mktdrqavtv vglglmgsal agalldhghp ttvwnrsehk arplvdrgag laatpreaie
       61 asrlivacvl dyealhtvle pvagslsgkv lvnltsgspe qahkfaawag shgadyldga
      121 imttppgvgs pemmflysgp rvvfeahrst laalgdplhl gtdpglasly daallglmws
      181 tmtgwlhgaa lvgaektpaa vftpiairwl tavagflsay apqvdagryp gddatidvqi
      241 aaidhllhaa eargvdnalp ellksvmera kaaghgsdsy asvievlrep adgr
//
LOCUS       WP_357683631             517 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357683631
VERSION     WP_357683631.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..517
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55319
     Region          6..501
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mstaniaaml agnarrfgda dalvfedrrw thrqldddvn alaagltaeg vgrdsrvaiv
       61 adnvpeflvl slalaklgav fvplnyrlta gelarllaha rvgavatvpe faalttaala
      121 dlpqvrrfal epiddgwtdv rslvaahrga rvadaaldda alqrivytsg ttslpkgvll
      181 thgnvnmnmh aqivelglrp tdrilnvapl yhvggtdlpg ygiwhvggcm vlhrrfvpaa
      241 vlraigaeri tgmvvaatml dmvrresaav aadlssvrwl ifsqvtaalf gvarglfpna
      301 rliegyglte tcsgltylda ahqeskqgsv glpvpwvqvr vvdpagddvp vgadgevvar
      361 gpkvspgyld dpaataaafr dgwfhtgdig cfdadgylyi rdrlkdmirs ggenmssaei
      421 envladhplv laasvvaaph pvwqevpaaf vvarpgltpe aligharqrl grfkvpkeiy
      481 lvpefptnps gkvlkrslre lrstlrpdwt ydaarrd
//
LOCUS       WP_357683683             293 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357683683
VERSION     WP_357683683.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=32220
     Region          8..281
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mtdtlvelal tplgphfaar vpgfdldrat daelaavraa lvahkvlffp dqrldddgqv
       61 rlgrrlgelt ashpvvggvd eahpevyald sadngfadvw htdvtfvarp plgsilravt
      121 lpprggdttw adsqlaydsl aepvralvdr lvavhdgnre fgyylahrrg grgsvwedev
      181 vtrldpvehp vvrvhpetgr rgifvnpgft shvvgvseae sraildllya hltkpehlvr
      241 hrwrpgdvvm wdnrstahya nrdygsarri vhritlrgdg prgpgdlwrp paa
//
LOCUS       WP_357683711             359 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683711
VERSION     WP_357683711.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=38000
     Region          25..355
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mtdvfspshk dvheqvvfca dahsglraii aihntalgpa lggtrfypye seqaaltdvl
       61 nlargmaykn alagldlggg kaviigdpgr dkseallray grfveslggr yitacdvgty
      121 sedmdviare srfvtgrtla hggagdssil tafgvfqgmr asaeqvygtp slhgrrvgve
      181 gvgkvghrlv ellredgadv vicdvseqav ervrqrrpev dvvadaealt sadldvfapc
      241 alggaldddt vdklrakivc gaannqlahp gvekqlaerg ilyapdyvvn sggviqvade
      301 iegfsmerar akaaqiydtt lkifaiaaee gvppaaaadr laerrmsevg rvrgiwlgh
//
LOCUS       WP_357683775             289 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357683775
VERSION     WP_357683775.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 289)
  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..289
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..289
                     /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=32567
     Region          10..253
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mlgedtegsl vaisdlhvgy aenralveal rpasprdwli vagdvadtva diewalglla
       61 erfdtviwap gnhelwtppa dpvtlrgvar yellvrrcre lgvvtpeddy rvwrgsggpa
      121 lvaplfllyd yswrppgfdt reaalaeaye tgivctdefl lhpdpypsrq ewcaarldqt
      181 arrlaardpa lptvlvnhwp ldrhptevlr ypifaqwcgt datadwhrrf aaaavvyghl
      241 hiprttwkdg vrfeevsvgy prewrqrrip pgrvrrilpa pegtpltaw
//
LOCUS       WP_357683787             517 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357683787
VERSION     WP_357683787.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..517
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55471
     Region          12..508
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtngadpstt yvhdalelfa gfgdrealvg dgrrltypqv aaevrglaha ltghgvrpgs
       61 avlvmlgnav egpllqlalh llgcrtmwia pvtsrreide fvrlarpdvf vhhahapdgl
      121 ggqiaaslpg vpvlrlgvel tadappvelt aevpvpesfl qtsgttgtpk lvhhresfyr
      181 qvlalaadfr aagfpllrhl shspmwlasg qittlfnlft ggvlflrqqw dpaafiatvd
      241 aerltstfvt ppmlyevldh palpgadfsa mfmfnvgagp aaparlrqai arfgpclriv
      301 yglseavvic aqpgltedpa hpqrlgscgr pygdvtveir dadgralpag tdgevwvrtk
      361 lsfhgyhgqp eltaetlvdg wvrtrdighl dddgflylvd rlqdriltrq rswpiysrpi
      421 edvlaghpqv raaavigvpd pvagelpyay vvrtagatvt gaeliglvta elsdtwapga
      481 vefldalpln rsakvdkral rdryaagrpv dpvgsls
//
LOCUS       WP_357683848             370 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357683848
VERSION     WP_357683848.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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..370
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..370
                     /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=41056
     Region          66..364
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mneeqrrmaa dpqyraqvtr rrllaasaga aavlgaaglp vlqtkgpara dgkwqvdpli
       61 ptqnrgiily svrdriaaap ddsgvpygfe rvlaslaqmg ykeiefagyn qhtsilgrqi
      121 tpteirkild dnglvangth asinaatfqq qldiaeelgm knigtgsdpt nsayqsdwda
      181 aadlwnelgr qakerkmrly thnhdvaysf lldsgpldan gkptrssgvr rleyffaktd
      241 pkyvyfecdi ywayvarhkh ttytnsagqq ktslfdpiln varrskrfpl fhakdgnrnt
      301 alpngyemip lgegdinfqq ffqtigesdf hhanwemdta pggtanpgqs ldfarlsyan
      361 madltiyhnd
//
LOCUS       WP_357683803             112 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Nonomuraea
            sp. NPDC048916].
ACCESSION   WP_357683803
VERSION     WP_357683803.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=12425
     Region          3..105
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msivkinvlt vptemreele hrfsnragmv esadgfewfe llrpvegtdq ylvytrwrse
       61 ddflrwqesq dfqrghaeaa gsgqghghgr gpaasgatlw sfevvdsagp kg
//
LOCUS       WP_357683943             484 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Nonomuraea
            sp. NPDC048916].
ACCESSION   WP_357683943
VERSION     WP_357683943.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=50783
     Region          <75..483
                     /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 mniplrrval vcgamffsll anityvqtvg arglyadprn erallarfgh prgdiltyeg
       61 rtivrsresr rgpyeyrrvy tdgemyapvt gyvslhqaag ieqaengvls gddpgmrmrr
      121 lvrdgevdga dvrltirqrv qwaayqslrs aglpgaavai dpatgailal asypsydpna
      181 ystlnpdrla rvdhdlsldp grpllnrale rsyppgsaft vvtaatalas geytpesrls
      241 gparlplpgr pdhlsnpggr pcgdgtpsla rafrrscdta fadlglrlgq dslrdqaeaf
      301 gfgagdlaip lrvvpstlpr eldragtalt aagrhlerat plviamlsaa vandgvmmrp
      361 ylvqdvrlpd gsiinrgdat pyrttlaapl arqlasmmta vtrpggtgta aaiagvevaa
      421 ggtpaafsgi rpatgagprd havftafapa dapevavgvv lehappgdsa aipiaravlq
      481 aals
//
LOCUS       WP_357683970             414 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357683970
VERSION     WP_357683970.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   ter Beek,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 414)
  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 414)
  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 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..414
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43194
     Region          33..387
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnttvngttt drqderlqpr eglrgaisdv verarggdlg vipvvvgliv iwsvlqilnp
       61 vflssanlvn ltlesaavgi ialgivcvll vgeidlsvgs vsglsgavla vlfvsqgmtv
      121 wvailgsvim gavigwvyaq lfnrfgvpsf vitlagllaf mglqlyvlgs kgsinlpfds
      181 glvnfaqlaf vpdwlsytfa vvtagwlfat gylharerrr aglsskttsm lvirsaalla
      241 vlvfvvwylg qtrgigwmfv ffvgmvlvmh yllsrtkwgr avyavggnve aarraginvk
      301 aiytsvfvlc ssfaavggil aaarlaaanq ssgggdvnln aiaaaviggt slfggrgtaf
      361 gallgiiviq sissgltlln ldssirfvvt gvvlllavvv dsiarksrts hgra
//
LOCUS       WP_357683975             443 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357683975
VERSION     WP_357683975.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 443)
  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 443)
  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..443
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..443
                     /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=47826
     Region          1..440
                     /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 mtdiprravs rtaklaalpl gfagrtvlgm gkrvtgiasd visaeiqqrt aeqlfsvlgq
       61 lkggamkfgq alsvfeaalp deiaapyrqa ltklqeaapp lpvasvhrvl aeqlgpdwrd
      121 rfvefddtpa aaasigqvhr avwrdpetgv srsaavkiqy pgagdallad lkqlsrlggm
      181 fraiqpgldv kpllaelrer iteeldyele aesqrafaaa yaddpeifip avlsasprvl
      241 vtewiegtpl adiiregtee qrnaagrlma tlhlsappra gllhadphpg nfrllpdgrl
      301 gvidfgavar mpegtpepig rllglslrgd adavvaglre egfvkptepi datalldyir
      361 pmldpvaqee frftrawlra eatrlaspks pafqlsrqln lppsyllihr vtlgsigvlc
      421 qleakapyrg ilerwlpgfa pva
//
LOCUS       WP_357684023             375 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357684023
VERSION     WP_357684023.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 375)
  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..375
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..375
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39802
     Region          1..>63
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          2..>151
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrdntqeqlh rlrslrtvag ltieelavrs gvsartiggi erhrircphq gtlralgaal
       61 gldgadagql ratgeqvagv tglpgvtahf tgrrddlawl arqlrrrpvv qliglpgagk
      121 talavqaatd laerfpdgvw flgpvadata atiarrllsp pdaaahrsda aaigayrdll
      181 rrrrilvlld dvrddrqigp llppdalgvt litgrhpltg lpvtdrrlvp plpaadarta
      241 ltamvdgtap taavaalaag cgglplalrv tanrlltrpq wsaqwlidrl atpervldal
      301 vagdlsvrda fertyaglpe rarravrllt rpvgpaaaea glldlaergw vtagrehrye
      361 phplvrafar vaagt
//
LOCUS       WP_357684025             768 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora rifamycinica].
ACCESSION   WP_357684025
VERSION     WP_357684025.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 768)
  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..768
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..768
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=82884
     Region          16..759
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 meqipgtpes pslgsalrah rvaaglsieg ladrcgvsvr aisdierdrv rrprrrtltv
       61 lldvlavpdd errrlvgats grpaggelpe ppryfsgrat elrtlgdlar rpsgdrqqat
      121 vlvvtgpagv gktslvlras tdlasefpdg rffvdlrgmd dvptppgeal hrllralgvp
      181 eqripagled ratayrsalc errtlvvwdn aadesqvrpl lpgagrslvl ftsrrrlsgl
      241 dtaqwlsvep lpaedstaml raiarpgpat dpaalddlar hcghmplalr vtgqrlseep
      301 glsveelnrr fsgeqarlrv idagaagiht alslsyrrlg adlrrtfrrl sltpgpdfgp
      361 dpvavltdas gaqaerrlea lvesglvaav padryglhdl vrdfaldrmt aeepastgpl
      421 rtsslrwwla rttaagrhfe pdgpasptef rdraaaaawl daergnwfaa lrsaaaeglh
      481 gpvveavdal hwfsdsrvhl dlwpevfrls aesaarlddp rteavhlnyl swaqavcqre
      541 yagsvatanr aleravragd haqqgwslly aasghtglge hraalrqrqr awvmlrraad
      601 peglpqamas lgssllalgr ptealrvhqr trsllrdpry piaafaraat dalncrrigd
      661 dlaalgrwpe cvaarreava rlratampat ealasvelve alrrtgetrd apaylrraie
      721 laeqcddpdl agraatllaa csrndltgdg dqvpaatrak artsgcgs
//
LOCUS       WP_357684033             580 aa            linear   BCT 28-DEC-2024
DEFINITION  amylo-alpha-1,6-glucosidase [Micromonospora rifamycinica].
ACCESSION   WP_357684033
VERSION     WP_357684033.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..580
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..580
                     /product="amylo-alpha-1,6-glucosidase"
                     /calculated_mol_wt=63541
     Region          214..558
                     /region_name="GDB1"
                     /note="Glycogen debranching enzyme (alpha-1,6-glucosidase)
                     [Carbohydrate transport and metabolism]; COG3408"
                     /db_xref="CDD:442634"
ORIGIN      
        1 mtvapsgpef siqdipfsyr gswlnispvv aektyaddlh lvshqtglhp vlrlapdagt
       61 tvvatptllt whradgriea gyqgpdtlri rgrglglria aaapvltpfs gtylyrdpvd
      121 gsavftsyet grryrvtvls galrgtggve algpadrwld lpadqpweia ieeyatarrp
      181 yaqgvpfdrl cherraefaa fvdavapwrs vdtpaaelaa yvlwsatvdp agfvtrpavl
      241 mskhwmdkvw swdhcfnaia laagdpelaw hqfqlpfdhq dpagalpdsi thsevlhnyv
      301 kppihgwalg hlrrrlptpp draalaqtyd rlsrwtrfwl darrvpghal phyqhgndsg
      361 wdnattfddg rvletadlaa flvsqlrcla dlatelgepa ggwsaeadrv raallrelwd
      421 gerftarsph tgrlrasrsl ldlmpvtlgt elpapvtaal argieshltt hglateptds
      481 adyladgywr gpiwapstvl vedglrragh tgiadeigrr flalceksgf aenfdaetga
      541 glrdraytwt assylilaag qqerrgapvd grstrtepar
//
LOCUS       WP_357684061             396 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684061
VERSION     WP_357684061.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 396)
  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..396
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..396
                     /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=41524
     Region          2..389
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 msrrvliaga smgglraaer lraagftgei vavgdeahlp ynrpplskea lasevtheav
       61 afrlrpavad vtwrlgvpia aadlragtvr ladgaepayd glvvatgmrp rrlpvpgpra
      121 grhvvrtled ardlraelrp garllvvgag figcevaata ralgasvtvv apeavpmrrp
      181 lgddlgaalr rrheargvvf llgrtvaafl gdgrvtgael sdgtrldadv vveavgsaan
      241 tawldgngld lsdgvlcdna mrvegrpgvv avgdvarfpn prydgvarrv ehwsiptdta
      301 rraaatllad lglaepdpap faplptfwsd qydlrvqsfg vpalgeddir ilegdldgev
      361 avgyhrdgel vgvvliglap avaryramlm rtptaa
//
LOCUS       WP_357684072             204 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Micromonospora rifamycinica].
ACCESSION   WP_357684072
VERSION     WP_357684072.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..204
                     /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=21042
     Region          13..156
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtghgtrvet tlllgsprag srtagiavrl veelslalaa egvelagpdv vdlaeigagl
       61 plrasrsvpl gpeteralgl vrrsgllvvv sptfkgtytg llklfldmlp vdglagcvgv
      121 gamtagwakh rgagdqylrp lltelgavap vpclsilede fedvpavvaa wsrrwapalg
      181 avarhlrhdl sapevhpltg aras
//
LOCUS       WP_357684090             172 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684090
VERSION     WP_357684090.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=19255
     Region          1..163
                     /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 mtltpvgpeh aeglyelvtd pevrrltgsh aefdrdtarq wyltrgerpe rldlaitagd
       61 ayvgeivlne ldaanlacnl riallgsrvf grgygteait lvldhafttt plhrisldvh
      121 afndrarhvy kkvgfveegv rrdallwdge whdsvamsml rtewlprses la
//
LOCUS       WP_357684142             106 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Micromonospora rifamycinica].
ACCESSION   WP_357684142
VERSION     WP_357684142.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=10552
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mayvflliai saevagtsll katqgftrlw ptvglalayl lafgmlalav rdipvgvaya
       61 mwsglgtaai vaigaaflge plslskvigv gliiggvvvl nlggah
//
LOCUS       WP_357684146             381 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357684146
VERSION     WP_357684146.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 381)
  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..381
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..381
                     /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=43288
     Region          24..363
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtviqhkpvn piahlsaedi eilgkeldai rdrvlaerge sdaayirkvi rtqrtlemss
       61 ravllfslfp pawvigtagl tvakilenme ighnilhgqy dfmrdpkihs ttwewdhvsp
      121 aeqwkhshnq lhhtytnvlg kdndlgygim rvdedqkwyp mhlgqplwnf vnacffeygi
      181 aaydlelgrn lrkgrhktpe frarlravgr kirrqvlkdy vihpllsgps flstlaatft
      241 anlirnlwsh svimcghfpn gvetfsktsi egetrgewyl rqmlgsanis gsrlmhimtg
      301 nlsfqiehhl fpdlpskryq eiapqvralf drygltyttg plpkqvasaw wkvirlslpn
      361 rgaarpatde rparalaasg v
//
LOCUS       WP_357684147             129 aa            linear   BCT 28-DEC-2024
DEFINITION  YkvA family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684147
VERSION     WP_357684147.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..129
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..129
                     /product="YkvA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14105
     Region          27..122
                     /region_name="YkvA"
                     /note="Uncharacterized membrane protein YkvA, DUF1232
                     family [Function unknown]; COG3339"
                     /db_xref="CDD:442568"
ORIGIN      
        1 mrawliglav gvvcvvacwg vlvvlarrlp pgtardlaaf ipdclttvrr lrrhpqvprr
       61 araaivfagv wvaspidlip eflpvigpld divvvalalr yaarqvprev lleawpgepr
      121 lllrligqr
//
LOCUS       WP_357684189             216 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684189
VERSION     WP_357684189.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 216)
  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 216)
  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 216)
  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 216)
  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..216
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..216
                     /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=24024
     Region          12..187
                     /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 mrhwplfdls vttprlelry psladldela eraaegvhet gtmpflvpwt daepeerars
       61 tvqyhfrqwa efgparwsvd fvavlagqvv gtqgvsaadf pvlrevksgs wvgqrfqgrg
      121 lgtemraaml hlafaglgae yatteafedn paslavteks gyrddgvtrh vrrgevavtr
      181 rfrlartnwt pmegvrihgl eaclplfgle klqrae
//
LOCUS       WP_357684205             397 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357684205
VERSION     WP_357684205.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..397
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42424
     Region          16..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 mrreefyrea rddldgplhg lsvldvtkvw sgplatslla dmgadvvrve lphgrdgevp
       61 peipgtglsw fretvnrnkr svgldlrqpa greaflglvr dadlvvenyk pgtldgwgvg
      121 yadcrrvrpd vvfvsitgwg qfgpdvdrpa ydpvvqaasg wmalngdpag rpvraptfla
      181 delaglhaav galaalahrd rtgegqhldv amldsllass cglltlaatg apparwgnet
      241 dfavpsnvys cldgevylsv aldkhwrala etigrpelar apgygrgaqr rqnrvevdal
      301 vadwcrsrpv devmaafraa hlvaervrtl aevaadpqvs ardmlqptvl hngtvapltg
      361 pavkfsrtpt rvrrgapaag adsrdvladp apdpdgp
//
LOCUS       WP_357684247             222 aa            linear   BCT 28-DEC-2024
DEFINITION  ComF family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684247
VERSION     WP_357684247.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 222)
  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 222)
  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..222
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..222
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=22643
     Region          2..215
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mlsalldlvl pqpcvgcgat gaslcdrcla glfaaparrp psprppglpd cwsaadysgp
       61 vrqaivayke rarmtlagpl aealaftvas arpgadgfal vpvpsarral rarghdpvgr
      121 laalaarhlr rlghgaevrd vltpgrrvad qaglsagcra anlagslrav tpvegpvvlv
      181 ddlvttgstl aeaaravrag gaevlfaatv aatrrrsckp lr
//
LOCUS       WP_357684263             447 aa            linear   BCT 28-DEC-2024
DEFINITION  LVIVD repeat-containing protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684263
VERSION     WP_357684263.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..447
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=47914
     Region          31..425
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          56..90
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          97..152
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 masrfgrala vigavlalaa spvhasdgvk tsanvkrvan vpkqapfdgp eaygtdlafq
       61 gdyayqgnyh gftvydiknp akprvvsrvt cpgaqndvsv qgdllflsvd eplrddscra
      121 ghgsetskaa wegirifdis dksrpkyiks iktacgshth tlvpdkkgka vylyvssydp
      181 garypgcrpp hdrisiikvp lkkptaakiv srpvlfpagg netqpgllap tsgchditvf
      241 pkkdlaagac mgdgilmnis drerpkvtnr vtdanfafwh satfnnagdk vvftdelggg
      301 igatctkgfa pergadavyd ieggelvhks yykipraqts mencvahngs lipvkgrdvm
      361 vqawyqggvs iwdftdsanp veigyfdpap lkpanlggsw sayyynghvy ssdiqkgldv
      421 lrvsdkrlgs agkvrlkvln aqtqyap
//
LOCUS       WP_357684303             444 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Micromonospora rifamycinica].
ACCESSION   WP_357684303
VERSION     WP_357684303.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=46916
     Region          27..430
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 msaltsnvra lpalgptrrl klprqaerrl gngltviavr rpavplvelr lwmpfgrthl
       61 argailaetm lagtatltat riaaelqtvg gglsagvdpd rlmvsgaglv tgldrmleil
      121 advltgasyp adwvqterdr lvdriqvaqs qpaqvvrtal lrriygrhpy avqtpepeqv
      181 ravrpaalrr lhadrvhpae avlvlvgdvq peraldaaek altgwtgdsr gadlppappl
      241 epgplllvdr pgsvqsslri alpavprthp dhaalqlanl ifggyfssrw teniredkgy
      301 tygphssveh svagsvlvag aevateatgp allettyelg rlaslppgpq eleqarqyal
      361 gtlqlgistq aglaaltsay agnglrldfl aehaarlakv tvddvaevaa rylaparavv
      421 vvlgdaerva gplaaltpvr tesa
//
LOCUS       WP_357684352             529 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D family protein [Micromonospora rifamycinica].
ACCESSION   WP_357684352
VERSION     WP_357684352.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..529
                     /product="phospholipase D family protein"
                     /calculated_mol_wt=59251
     Region          13..412
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
     Region          270..410
                     /region_name="PLDc_vPLD1_2_like_2"
                     /note="Catalytic domain, repeat 2, of vertebrate
                     phospholipases, PLD1 and PLD2, and similar proteins;
                     cd09105"
                     /db_xref="CDD:197204"
     Site            order(375,377,390,392,403)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197204"
     Site            375
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:197204"
ORIGIN      
        1 maiedwflta eeranpvsgl pvwttgnlae plihgaayfd rlvsevealg agdhlfftdw
       61 rgdpdermrp dgptvaqifa raaqrgvvvk gllwrshldt lsyseaenrs lseavraagg
      121 evlldqrvrr ggshhqklvv lrhpdaperd iafaggidlc hsrrddaehl gdpqplamsp
      181 kygprppwhd vqlairgpav galdttfrer wtdpmpldse nplaylrdrf rgsdlspdpl
      241 pdqpadpppc gthriqvlrt ypavrprysf apdgertvar gytkavrrar rliyledqyl
      301 wstevaelfa ealrdnpdlh lvavvprypd vdgalalppn mvgreqalsl ceraapervh
      361 vfdvenragg pvyvhakicv vddvwasvgs dnfnrrswth dselscavld etrderspvd
      421 pagqgdgarv fardlrlrlw rehldrapdg addadlldpa saveaitsaa dtlqrwyddg
      481 rvgprpqgrl rphrperlpw ytrlwalpay rlvydpdgrp lharrkgtw
//
LOCUS       WP_357684349             440 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357684349
VERSION     WP_357684349.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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 440)
  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..440
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..440
                     /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=46619
     Region          32..429
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 msaaassqer laflndastr igstldlaqt crevldvavp rfadtggimv qerlitegef
       61 pvrpkdgsal vrrvatavav dnpwdwntaf pvgevavypp llpqgqamat aktvlvprle
      121 qvvgdenaqa fgrpiiarll pgcsflvtpl vargnvlgff vlvrratsep fqdgdialae
      181 elaartaici dnarlygrer rtaltlqsal lptglqkspg leigyrylpa gdlahvggdw
      241 fdviplsddr talvvgdvmg hgiraaatmg qlrtatqtla sldldpgell frlnrvaqhl
      301 dsdqlatcvy atydqatgal aiasaghvpp vlvepsglae tvpvvpgppl gvggerleic
      361 eatmpaggml alytdglves rdrsigdgia dlcslltgpp reiericdli vkaqrpadkr
      421 ddialllaka mpveqtaplr
//
LOCUS       WP_357684360              58 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357684360
VERSION     WP_357684360.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 58)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 58)
  AUTHORS   Rosinski,J.A. 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 58)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..58
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..58
                     /product="helix-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=6702
     Region          1..58
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mntlaklwtv edvatflgvp vatlyqwrhq rtgprghkig rhlrylpedv mswvqdqe
//
LOCUS       WP_357684390             416 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Micromonospora rifamycinica].
ACCESSION   WP_357684390
VERSION     WP_357684390.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..416
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44930
     Region          2..403
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 mtgtpavedl lrahapqvla tlvrrygsfd tcedalqeal laaavqwpre glpanprgwl
       61 ttvaarrwte swrtdtarrr rertvaaltg pgsepvsavd dtltvlllcc hpslsrgsqv
      121 altlravggl staeiarafl vpestvaqri srakqrirag gaefrlpaae drparvaavl
      181 evlylifneg htvssgpalt rveltaeair ltrqlhrqlp ddpevtglla lmlltdarrp
      241 artrpdgslv plaeqdrsrw drpaiaegva litrtladap vgpyqlqaai aavhdeapra
      301 edtdwpqllg lynllrhiap gpmvtlnriv alamvagpqv alaeltaaqa dpglagnhrt
      361 qvvrahlldl vgdrtaarrc yllaaqatls vpeqrflrmr aarqpdhrrl ppggaa
//
LOCUS       WP_357684472             316 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357684472
VERSION     WP_357684472.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..316
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..316
                     /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=34523
     Region          1..316
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mravlvvnpk atttsersrd vlvralrsqv dlsvrytrrr ghatdlarea aqegvdlvvt
       61 lggdgtvnev vnglmtaepp tirtggspad rlpalatvpg gstnvfaral glprewadgt
      121 smileglrlg rsrtiglgra ddryftfcag fgldaavihr veqarrrgrv sspslyfrst
      181 lshyflgahr rhpaislerp gepaegelgt viiqntapwt ylgdrevnpn peasfdlgld
      241 vmalrqlrva sttrtvtqfl srhpdphgkq vlrlhdleef tlvsarpqaf qldgdylger
      301 hkvrftsvsg alrvic
//
LOCUS       WP_357684479             638 aa            linear   BCT 28-DEC-2024
DEFINITION  molybdopterin molybdotransferase MoeA [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684479
VERSION     WP_357684479.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..638
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=62989
     Region          134..575
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 mrntstpalc raaptyapma paprtatftd tsvlasycaf giqygkmpvk eppmtvaghe
       61 pdlkpgthac ggatgpadld gsggidnagg adgpveqvgp velveqagpv gpvgpvgwev
      121 arriaagaar pravveaplp eaqgcrlavp lralvavpga dvaamdgyav agpppwrvag
      181 qvlaggrpyg dplrageave iatgapvpmg ttavlpyeda vllpapdaaa pacedagspp
      241 gagrtvpceg agrvpgvgrm mpsredagsp pgagrtvpye gvgrvvrarg eiaagrhvrr
      301 rgediaegav vlepgavvtp vvlglaaglg hdvlrvrprp avtvlvtgde vvdaglpepg
      361 rvrdaigpfl pglvewaggr vtggirlpdg adplraalaa sagpraaaap raaagplgat
      421 apraapdgaa ssggvalsdg aeaddagsag dgmggvvdvv vvcgassrgp adhlravlae
      481 lgaevlvdgv avrpghpqll arlragplvv glpgnpyaal gaaltllvpv lgrltgterg
      541 retgalagpv gahphdirpv avlrtgaags vrahphdtrl vavrrtgggv vpvghdrpgs
      601 lwgaaladal avvppgwnge rvellelpgg ldrpfttg
//
LOCUS       WP_357684492             728 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional polysaccharide deacetylase/glycosyltransferase family
            2 protein [Micromonospora rifamycinica].
ACCESSION   WP_357684492
VERSION     WP_357684492.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..728
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..728
                     /product="bifunctional polysaccharide
                     deacetylase/glycosyltransferase family 2 protein"
                     /calculated_mol_wt=79175
     Region          92..286
                     /region_name="CE4_SF"
                     /note="Catalytic NodB homology domain of the carbohydrate
                     esterase 4 superfamily; cl15692"
                     /db_xref="CDD:472828"
     Region          372..718
                     /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 mgeppvragr rrvvgsprrr ravpppswil lgtvlsllag vllvgayana sfapdrrqst
       61 ggqrevptsv vtggpiisas semvrsyrlp prtialtfdd gpdpvwtrev lrvldthqvk
      121 gtffvlgsqv arhpgvarel adgghqlgvh tfthpdlael pgwrqrleya qtqlavasat
      181 glrtslvrfp ysshpgaidn qdwpvltaag dlgyltllnd tdsqdwslpg variienaap
      241 egdsgavtlw hdaggdrsqt vaaldrfipm mqqrgyrfvt ateglnlafa aagvdhrmda
      301 avpasaadrw rgrmliwavq gaddmltvfg glfvvvgllt vgrtsvlfvl agrharrrrg
      361 rdwswgppvt apvsvivpay nekegiaaav rslaggdhpg gmevvvvddg stdgtadivd
      421 alglpnvrvv rkpnggkpsa lntglalarh dlvvmvdgdt vfepdavrrl vqpfadpqvg
      481 avagnvkvgn rrsliakwqh ieyvigfnld rrlyetlrcm stvpgaiggf rrealryagg
      541 mtddtlaedt ditialgrag wkvvyeetar awteapatig qlwkqryrws ygtmqamwkh
      601 rrsvfdrgas grftrrcmff lslfgvllpl lapvidllal yglffldrqa tavawlamlg
      661 vqtatavvaf rldrerlgvl wvlplqqfvy rqlmylvlvq avvtavtggr lgwqklrrtg
      721 lepavrsg
//
LOCUS       WP_357684506             251 aa            linear   BCT 28-DEC-2024
DEFINITION  phasin family protein [Micromonospora rifamycinica].
ACCESSION   WP_357684506
VERSION     WP_357684506.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008148
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..251
                     /product="phasin family protein"
                     /calculated_mol_wt=24239
     Region          1..102
                     /region_name="PhaF"
                     /note="Polyhydroxyalkanoate synthesis regulator phasin
                     [Secondary metabolites biosynthesis, transport and
                     catabolism, Signal transduction mechanisms]; COG3937"
                     /db_xref="CDD:443138"
ORIGIN      
        1 mqdawrayle lalglteapr kraqdaarrl agtggatavq lqalaeella tgaanrealt
       61 klvrfevdra lgavglatad evaeltrrvh elerqlreak ngpvpvragd aapdttapst
      121 tapsttapst tapattapat tapattapat tapattapat tapagdaavg gaagaaggaa
      181 gepgaapspr avakkavark avakkavkka vpkpvaadps agsgtpagdp apssrpprka
      241 apgrgssgga g
//
LOCUS       WP_357684556             310 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684556
VERSION     WP_357684556.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 310)
  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 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   3  (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 10003067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..310
                     /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=34331
     Region          1..307
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 matitteapr gapgtpgwvr wvndhrkwlf aapamtfvaa llvfplawtg ylsltdaegs
       61 vraesefvgf qnyldvltdt trfwpavgrt atftgvallf emvlgmaial llwrpfkgqk
      121 wvrvaillpl vatpvavgmm wrlifdpnig manqvlgwfg igpqpwlage htalpttifi
      181 dvwqwtpmvv lillagltsl seepqeaari dgastwqrfr hvtlpllmpt vtvaillrgi
      241 dalktfdily atkgrgggsf hevetlnvya yglsfdynky gvsstvlilf fliiigamwa
      301 ltvrrkearr
//
LOCUS       WP_357684561             298 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora rifamycinica].
ACCESSION   WP_357684561
VERSION     WP_357684561.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   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 298)
  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..298
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..298
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=32248
     Region          12..294
                     /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 mtsttipgfd yrhvtvdedv rlqvavggvg rpivllhgfp qthlmwrhva tdlaadhtvi
       61 cpdlrgyggs dkpaerdgdt yakrtmaadv valarelghr qfalaghdrg alvairagld
      121 hpdavthlas ldvlptldtw dilhgvdaav afhlylmalp pglpeqliga spdaffgyfl
      181 dvwardpqai ppdvraeylr asraavpsiv adyrasagvd lthdradraa gnrltmpvtv
      241 vqqdwgaalg fdaaarwraw tadlehhtts aghfmaeeap tevvtvlrrl larsrtgr
//
LOCUS       WP_357684566             505 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684566
VERSION     WP_357684566.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 505)
  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..505
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..505
                     /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=51314
     Region          28..255
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(98,100,137,139,141,157,175..178)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(153..161,171..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <289..502
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mrpltvgdpv iigrylllgr lgtggmgvvy laehprgglv alktphavhl kdptlrarfa
       61 eevafsrriv pfctaavved gtdrdrpylv seyvpgpals qvvvargplt pdlaygvglg
      121 vaaalvavhd aglvhrdlkp gnvllstagp rvidfgiard vdttaahtqa gqvmgspgwv
      181 sperltggpa vpasdvfawg clvafaatgc hpfgggepdv larrimveep rvegvpallr
      241 paveaalake padrpraael lrallaaggv gdpwdlreav agvleeiwtp vpyppgagrv
      301 rlapppddrr ptapkrgsra kgganlshas faalatvsia avtviaasgg ggdvrigggs
      361 qlpdipaavq shspratads tlrppatstg gvpasagtet patpatptvw vtqtrtrgps
      421 taldptperq tgspppetrd pggqgdgdpc aspaarrran aarrgcpqpt tsittipqdg
      481 pgespgpsst psvpqtpsat atgss
//
LOCUS       WP_357684624             217 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684624
VERSION     WP_357684624.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 217)
  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 217)
  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 217)
  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 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   5  (residues 1 to 217)
  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 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 18445957
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..217
                     /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=22967
     Region          1..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          110..213
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mggqrlyeaf asvakalasd rrleliella qaerpvedla raaglgvtsv snhlqvlkqa
       61 glvatrrqgt rvfyrlaged vaalwvllrq vgsahlaeae raraaylgpg dtdqltreql
      121 qqrlaagqvt vidvrpgvey aaghipgals lpldelldrl delpaegliv aycrgaycvl
      181 aheavrvlag rghgaarlad gmlewrlagl pvaiaga
//
LOCUS       WP_357684632             212 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357684632
VERSION     WP_357684632.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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..212
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..212
                     /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=22810
     Region          39..156
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhhpdpagae iearqakped gaathapvrr lrraerreqi ldaatrafaq agyaatgldd
       61 vaaeanltra mlyrhfdska dlyravldra ctrlgeatgt ddfdddaipa lmrsaaadpd
      121 gfkllfryaa repdfrelid titaasreva hrnlarvipa gpwldwaanl ipaltieavi
      181 awldagrpdp gqaadriaqa vhgvmaaarp as
//
LOCUS       WP_357684638             428 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684638
VERSION     WP_357684638.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   ter Beek,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 428)
  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..428
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..428
                     /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=46449
     Region          1..423
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mssvvldnvt kiypgdhlav drlslkasdg eflvllgpsg cgkstllrmi agleeitege
       61 lwlggqlanh lpprdrdvam vfqsgalyph rtvrgnisfp leiaksdpam arervtelsk
      121 alhidetldr rpgtlsggqr qrvamgraiv rqpklflmde plsnldagmr telrmeisal
      181 vrslgvttvy vthdqvealt ladriailnr gvlqdvgtpa qiyndpataf vasflnsqql
      241 nllaatvrtp qnqyvlldfg ahrlviswsd prayaisqht ggqvlvglrp dglapvpesy
      301 dgpsffgrvr aleyhghewl ayvecgvpaa avpeppdqrg rsdgqaggag glggmmrrmf
      361 ggreeeshqd qeqvgqnvgg gfhrradlvv rlggrpvwra gepakvavdv nrlmiftpdg
      421 aridpprr
//
LOCUS       WP_357684640             252 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357684640
VERSION     WP_357684640.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 252)
  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..252
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..252
                     /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=28010
     Region          4..234
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mstrppayqs laaelrgqil agvlkpgdrl pvepelsaah gvsrstarea lrllasqdli
       61 stvrgvaggs fvvtprpeqv seylhaslnl ltvdtqitvd qlletrelle vhatgraalh
      121 rteedltglr atlfdpwqlr peemyepnka fhtrllhasg npllevvarp vfqvlderfl
      181 rqrapgrfwh evdhdhreiv arvaardeag areaarahld rlrttylaid rarsqpragv
      241 sdgedrsgrr pe
//
LOCUS       WP_357684730             284 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684730
VERSION     WP_357684730.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10790449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..284
                     /product="sugar 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:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30907
     Region          15..283
                     /region_name="MalG"
                     /note="ABC-type maltose transport system, permease
                     component MalG [Carbohydrate transport and metabolism];
                     COG3833"
                     /db_xref="CDD:443045"
ORIGIN      
        1 mtarrrrgre drgplasial hatlllavgv alfpvvwlil tslkprdgwl stelqlfnds
       61 sldnyarvlg gtqfplwlln salvaalttv lgvflaattg yavsrfrfpg lrsvmwlllv
      121 tqmfpvavli vplynlmaal gllnqipglv iaymtiavpf cawmmksyfd tvpreldqaa
      181 mvdgltpfga fwrvilplar pgiavtaffc fmtawgevgy atifmsqenk rtlgvglqqf
      241 vgqhwsdwgl mtasavliai pagavfllvq rhlitgltag atks
//
LOCUS       WP_357684758            1340 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora rifamycinica].
ACCESSION   WP_357684758
VERSION     WP_357684758.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1340)
  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 1340)
  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 1340)
  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 1340)
  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..1340
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..1340
                     /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=146556
     Region          25..1318
                     /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 mdiarsehhp ssasappaps lapsradapg arsaplsdlq yayllgelgn fqlggpalff
       61 eeyacqeldv rafsaalhql marhemlras fdeagllhvq delpvpltyr slrgqpeqvc
      121 rrlltrnrer cydegpprra ghapfeifvf aldthivvqv carllaidgf sgeifaqelr
      181 allngeslpp lrytfreyrn ecerrtdgda herarrywld rldslpaape lprrrttsdp
      241 sprlvrrvfk ltpeqwtsla arirknrltg tmvlgtafce vlrhwsknad ftinimygdr
      301 lpfhpevdkl ignfsstllm ecrqspgdtf ldrarawrrq llqdmahssf ggvsvirqln
      361 qrtgnarnal mpvvftsmlg vgepdsgvfl ehlgwqrleg rvrtpqvald hqafvagnal
      421 vttwdsaddl ypagmiddmf aayrsllvrl atedaawete sfdltpaaql kireqvnnta
      481 aparvatmhq lfeeqaerqp drpaviaegr eityaqlcdr anavaaelve agvrpgelvg
      541 vqalrgahqi iallgvllag aayvpvsprw prrrreqvae icglrvllad rsvqgeepya
      601 gartvdiata iarqdgaaap avevspdsla yviftsgtsg apkgvmishg svvntlvdin
      661 erfglsprdr vlavsdytfd lsvwdvfgml aaggavvvpt agqerevthl yelcqatgvs
      721 vwnsvpayla mfvefvrtsg rsplgelrla mvsgdwvpin lgaelaeiap haacaslgga
      781 teasiwsnyh pvpvrvpphw isipyghplr nqrfqvldar lrdrpdwvpg elfiggrgla
      841 vgylgdeelt aasflvhprq qeriyrtgdw arywpdgtle flgredpqvk vngfrvelge
      901 ieaallahpa vsdaavvtrt dgravslvaf vasqtpagel apqlsehlts rlpdymvprs
      961 idvrqrlplt angkvdrrel aeraagvgaa phvgddaprt gterglatlw qellevpevg
     1021 rsvgffaygg ssllaarlmn rieqqfgrrl platlytsgt iaelaavlda gchpeptrsl
     1081 vvlsdnghrp lvlvhpvggd llcyrpllae lgeryrvlgl tapspaqpgv tieelatryl
     1141 aelapelgge ppdrplrlag wslggvvaye marqlqrqgr rcavllidpw vgcgghptvd
     1201 daslvraflh nlvgtpveva sdpcapnaal etlrrtwasp ppqlkeltsw syaelqamyg
     1261 vfeantrall rypivaaegv evdvveasrg lvgpasgyls plrhaaaqlp vrlhmleadh
     1321 ftvvdgehag avarlidgmr
//
LOCUS       WP_357684861             303 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357684861
VERSION     WP_357684861.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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..303
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..303
                     /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=34638
     Region          4..257
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mlavvvgtgr cgstlvqell srhpgvgfvs gvddklsrln lagrfngply rrsaprpagm
       61 tslrhsrrll ekgrlrvaps eayhlldrhv vagfsrpcrd ltaedltpyl grrlraffda
      121 rierqgcrll lhhvtgwprt gflragypgl rvvnvvrdgr avtnswlqmg wwdgwrgpen
      181 wflgplptdl hreweeydrs fpvlaalgwk mlmdrfaear aahpegqwld vryedlladp
      241 raevarmldf ldldwspafe rgfgryrfha grqaayheel gdaqlaaver vldkplrqwg
      301 yrd
//
LOCUS       WP_357684869             313 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357684869
VERSION     WP_357684869.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 313)
  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 313)
  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..313
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..313
                     /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=34578
     Region          4..>61
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          65..245
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 madpagpvph ptpaddtpad pasiastpat tapigstptd pappggraag mpavdsragr
       61 pqgpiflvgc qrsgttmlrl vldshsrvsc gpetrfltdm rrivgrdwer larfgfprey
      121 wlgriadffg giqtdyarsr gktrwadktp lyalsidfla evfpdaqfvh virdgrdvvv
      181 shrkrfgyws avkcvvkwpr yirvaraaga rlpagryhel ryeetvtdpe kamrglfefl
      241 gepweagvld ydgkqhdvag kytaeadrrr aaagtdapiy gsrvgtyrre ldpflrvlvr
      301 vfsgatlrel gyr
//
LOCUS       WP_357684967             172 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684967
VERSION     WP_357684967.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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 172)
  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 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   5  (residues 1 to 172)
  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 172)
  AUTHORS   Rosinski,J.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..172
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..172
                     /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=19328
     Region          11..>65
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mswekdelvp lralanplri rivslltgas msatevarel diahasasyh lrqlaeagfl
       61 eqvdehpppg grgrprrryr ydlssgmrld rsgrrllhda mftdlarrle qardqrmsmd
      121 aevwldrsvw eevvgligqa vamvhdkarp prsadsvkvs mtalllemgd dr
//
LOCUS       WP_357685027             470 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685027
VERSION     WP_357685027.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 470)
  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 470)
  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..470
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..470
                     /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=51138
     Region          15..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 mphfpehple pgpdetrkmg eavlglvedf iralptmpaf dldgaqqlat dlrerapehg
       61 tplpellqtv aaaatkgats agpgylayip ggglysaala dflasalnky vsvwnlapvc
      121 aqlewtairw lcdlfgypeq argiltsggs lanfsaivta raarlgedfl dgvlyvtgqt
      181 hassakaaml agiprrnvrt vptldtlamd plaltrliee drraglrpfl viasagttnt
      241 gaidpldqla tiarserlwl hvdaayggpf qltdrgrdll sgieradsit ldphkamflp
      301 ygtgallvrd gallreahhl sadylqdlga eeeipnfsey speltrdfrg lrlwlpiklh
      361 glaafreald ekldlagyay dslreagfev pweprlttva frwvpergda dafnaallkh
      421 vndagrvfls stlidghyml risvvsfrth rdrvdealha irtardaltt
//
LOCUS       WP_357685007             427 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685007
VERSION     WP_357685007.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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 427)
  AUTHORS   ter Beek,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..427
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..427
                     /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=45225
     Region          12..334
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mnsssrkkmw tavvvsaalm tgagacggds ggeaaggdkv qitfaywgsd arqklteqvi
       61 qkfeeknpai dvegdfsnwd syyeklatkv aandapdvms ieirglseya grgaladlsg
      121 kvpsadldqq vltsgqiegk qyaiptgvna fsmvanpsvl ekakqklpdd aswtwdqwig
      181 lakdisgagg vtgaeynpnp awlqifaaqr gekmydgtkm gvsaetvkaw wsihqrliet
      241 kgspdaaksa eigatgpeqs llgtnagamg mwwsnqlnal skssgqeltl lrmpkaegas
      301 ssgmflqpam fytasakteh saeaaklidf lvndpdaagi llsdrglptn akvlaavkdk
      361 lppvdqktlt fieevksels piiappkgal qmedilkrnt eellfgkatp dqaaqkflse
      421 anaaiag
//
LOCUS       WP_357685013             264 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685013
VERSION     WP_357685013.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  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 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   3  (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   4  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..264
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..264
                     /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=28368
     Region          2..220
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrilmtgaag kvgtllrpll aregrtirls dllpleagpg eevvtadltd eaamteamkd
       61 vdavihlggq srerpwadiv ranmdgthvl leaarregvr qvvmmgshha agfqtrpasg
      121 gdlpdyafpr pdtfygvskv vmealgslyh drfgmnvtvi rlgtcneapa dtrglatwis
      181 pgdlarllea altapghhvv wgvsdntrrw wsleearaig yvsrddsevh agpllaehge
      241 pdpgeplhdr aggvftlnel ggtw
//
LOCUS       WP_357685076             135 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora
            rifamycinica].
ACCESSION   WP_357685076
VERSION     WP_357685076.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 135)
  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 135)
  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 135)
  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 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   5  (residues 1 to 135)
  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 135)
  AUTHORS   Rosinski,J.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..135
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..135
                     /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=14201
     Region          37..104
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(38..39,43..45,61..63,72..75,77..78,81..82,84..85,
                     91..93,98..100)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mskqtaasep tadppccppv teqrmpaeaa avlapafkal gdpvrlqlls miasapggei
       61 cvcdltpafd ltgptishhl rtlreaglvd aerrgtwvyy rarpvllrrl aallavptap
      121 agddpprpgp raecr
//
LOCUS       WP_357685078             165 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora rifamycinica].
ACCESSION   WP_357685078
VERSION     WP_357685078.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 165)
  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 165)
  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..165
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..165
                     /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=17863
     Region          5..160
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mahptvrpmr atdadrvlai yqagidagda sfettapdwa afdaarlpdh rfvavdgddt
       61 vigwiavapt saravyagvv ehsvyvdpaa rrrgvarlll dtliasteaa gvwtiqsgvf
      121 pentasralh qragfrvigf rervgrhhgr wrdvvllerr spavn
//
LOCUS       WP_357685181             534 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Micromonospora rifamycinica].
ACCESSION   WP_357685181
VERSION     WP_357685181.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=55613
     Region          6..499
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mispgtdtad avvigaghng lvaanllada gwdvlvleat aapggavrsa evtapgylsd
       61 lyssfyplgy aspvlggldl prygltwtha pdvlahllpd graavinrdl drtaasleaf
      121 apgdgdrwrh ayadwaqvsg pmldaittpf ppvrgglgll rrlrvggalr larrlvlpvr
      181 rlgaelftge ggpallagca lhtdlspeea gsgvygwlla mlgqqvgwpv pvggaqritd
      241 alvtrltarg grisyraevd rvltaggram gvrtvggatw rarravladv papalyldlv
      301 gaallpprlv edlahfrwdg stlkvdwals spvpwtnpav agagtvhlga dldglttysa
      361 alargeipas pfllvgqmtt adpthspagt eslwaythlp frrdwraeei arqvermedv
      421 leaaapgfrs rivgrhvagp aeleqgdpsl vggalgggta aayqqlflrp ipglgradtp
      481 vdrlylasas ahpgggvhga pganaaraal ardravtggl yaslidhahr tvyr
//
LOCUS       WP_357685195             258 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein [Micromonospora rifamycinica].
ACCESSION   WP_357685195
VERSION     WP_357685195.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..258
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28252
     Region          16..252
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtatlendlw vrrfhpapss airlvalpha ggsasylfpv sralspgvev laiqypgrqd
       61 rrhepvldtv aglvdgvfga lrpwldrpva lfghsmgavl ayelglrlqr etgqppvrlf
      121 asgrrapsrt rderyvhtrd dagvlrevar lsgsdprvlg dpellpmilp alrgdyrave
      181 tyraeegrrl dapitvltgd sdpmttvdea rdwrlhtsae cdvrvyqggh fflnehaadv
      241 irligaelgr plpessag
//
LOCUS       WP_357685199             943 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357685199
VERSION     WP_357685199.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 943)
  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 943)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 943)
  AUTHORS   Rosinski,J.A. 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 943)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..943
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..943
                     /product="helix-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=101284
     Region          <3..878
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          854..907
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mefversrel dilrdlysgs atgrgrvalv sgpgatgkte llrtfaehve sagglvlsaa
       61 csraerllpa avmgqlfhsv plpaetlrrv gafvepaatt vegaadigav rgmcaelldi
      121 ardrplvllv ddvefadett lqtllylqrr ltaaqilvvl tespqpqpfn pefraeltrh
      181 acfcniqlsp lseegvaell agwtdrdtav alapayhris ggnplllhal gqdrraagav
      241 dgtgpvvgdq fgqavlaclr rwdpailema hglallgdla spvllgrlla skptrvqwvl
      301 dalttsglls ggrfrhpaar aavlhdlapd alaemharaa ellhaegapa saigghllaa
      361 gglaepwait vlqesathal aedrvddave slklahemcd daprraalta mladcrwrvn
      421 paavsqhlqs qrdalraghl serhavallr yqlwhghrqd aqetlrhlrd vrqrldaatt
      481 aelagcaewl rlhfpvafae ldaapgfpst atparsdgsl gsatpsltav ltdgvtdevi
      541 araeqvlgsh llvdvglesa lcalqtlvya drmdravhwc dvlgaeagar gattwhails
      601 dvrshialrq gdlplaerfa realdalsph nwgvaigspl snlllakigm dkldeaeaql
      661 khvipdaird twfwplylra rghlhlaggr vhaaladfet cgqlatqwgl dlptllpwrg
      721 dlaqvylrsg rpdrargmvt eqlsrpgaan artrgislrl lgsaldvkqr vetlrqaanl
      781 lqeagdrfql flalaalssa hygrgefnts rvvarsatql akdiqaqalc rrllpgndpv
      841 ggdeadaape heelsrlsda eqrvatlaal ghtnreigkk lyitvstveq hltrvyrkln
      901 vrrrtelslg lpmdatgsgl lavapsgaer swpqwestav qas
//
LOCUS       WP_357685214             279 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357685214
VERSION     WP_357685214.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 279)
  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..279
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..279
                     /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=31631
     Region          5..248
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mnagiyavsd lhvaypenrk iveslrpaad gdwlivagdv aelfadvtwa lkllserfak
       61 viwapgnhel wthsqdpvrl rgearyqaiv rqcrelgvst peddypvwtg aggpllvapl
      121 fvgydysfre pgvtskeqsl arahaagvvc adevflhpdp ypsrdawcra rvtrtearla
      181 dcdpavpkvl vnhyplvrmp tdilrypefa qwcgteltad whrrfhartv iyghlhiprv
      241 twhdgvrfee vsvgyprewr hrtrldswlr pvlpapaqv
//
LOCUS       WP_357685228             401 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685228
VERSION     WP_357685228.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 401)
  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 401)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..401
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43534
     Region          48..399
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrillvgagg vgsavvpiaa rrdfyehivv adsqqdraaq avaavddprf sairldasdq
       61 aqveaalreh rcdvlfnavd prftmplfea alaagahyld mamslsrphp repyvktgvk
      121 lgdeqfardg ewrgagrlal vgmgvepgla dvfaryaadh lfdsideigv rdgsnlvveg
      181 ydfaptfsiw ttieeclnpp vvwedgrwrt tepfsepevf dfpagigpve cvnveheevl
      241 lvprwiparr vtfkyglgee figvlktlrk lgldsadkir vggaevaprd lvaaslpdpa
      301 tlgermsgkt cagtwvkgtg kdgsprevyl yhvvdnawsm aeygsqavvw qtaihpvval
      361 elvasgvwkg egvlgpeafd avpfldllee ygspwamrea a
//
LOCUS       WP_357685250             161 aa            linear   BCT 28-DEC-2024
DEFINITION  LysE family translocator [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685250
VERSION     WP_357685250.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..161
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=16993
     Region          <1..81
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
     Region          108..>158
                     /region_name="PRK13042"
                     /note="superantigen-like protein SSL4; Reviewed"
                     /db_xref="CDD:183854"
ORIGIN      
        1 mltallnpkg vllylslmpq fidagggvpi glqltvlgvl hvlgcgaiyg litlaaarag
       61 haptttpkaa rrmtavsgav lppgrrrgdp ehtlrslvrv ivkrkkgapp pepqtnhpkv
      121 cptethppet rtnkpdrapp rtepdqtppt kqtrrsvntg p
//
LOCUS       WP_357685258             254 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Micromonospora
            rifamycinica].
ACCESSION   WP_357685258
VERSION     WP_357685258.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 254)
  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..254
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..254
                     /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=27822
     Region          19..239
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtareitlna stppawarrp tnlatavtae lverivrgvh ppgsplppep alceafsvsr
       61 tvvreavkil qekglvqvrq gsgtivtpps mwdmldelvl aatiaeddsl tilddlvatr
      121 rvlesdmanv aarladratv drlralvdrm delvddqvay hehdrafhdv imqasgnria
      181 rgvvrslesq vvntarymgr serslcvasn qghrriyeri aahdpdgaae amvthiteaw
      241 lvrrsgpdta rlar
//
LOCUS       WP_357685260             422 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357685260
VERSION     WP_357685260.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     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=44590
     Region          19..360
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkqrtvisav lvaalalagc gsaagtrssp ggsagklvvw dwksgeptaa aylqkakadf
       61 akkhpdvtve fvaqpfeqyy tllgtaiqag kgpdvilfng ggqlrdrtda llpldeyvae
      121 drqrlagwea ftkggktyag pvtlqghpiy ynrtlydkag ldpakpattw peflancatl
      181 tqrtgakcla lgnkegfgiq fflsafgtgv ftpqeqddwi agkrdwtsph vkrifalwke
      241 tqdaklnsdg anstamfnds faifqsakaa hviglmsdvg hwkdfsefvp adklgvmrap
      301 vvvpgatpnl pfdggigygv akwtkdpkva adlvrsltst dalksfyada gaiaadttid
      361 vsqggpavtt ivadlktgkp alhvalsskt ldlmgrlsqq llsgsitvde avkqlaasdq
      421 ag
//
LOCUS       WP_357685281             704 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685281
VERSION     WP_357685281.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15774079
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..704
                     /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=71054
     Region          10..676
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
     Region          16..287
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,76,78,107,123..126,130,132,169,171,
                     173..174,176,185..186,189,205..208)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(22..23,25..28,30,76,78,107,123..126,130,171,
                     173..174,176,185..186)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(26,130,132,169,171,173,189,205..208)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(61..62,99,104,109..112,124)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(185..193,201..208)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          488..546
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          551..610
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
     Region          616..676
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
ORIGIN      
        1 maqplrtgdp rrlgayelsg rlgeggqgvv ylgtrgeash geqdygeerr geerqdderr
       61 geersgegry geeryavkll hgsvgderaa flrevelakh varfctaqvi eagfddgrpy
      121 ivseyvdgps lqrhvaltgp pvggaleria vstatalaai hragivhrdf kpqnvllgpd
      181 gprvidfgla raldaaatvs grgvgtpaym apeqitasav tgaadvfswg atmcfaanas
      241 apfgqdsvap vlhriltaap elgrldgrlr eiveacldkn prnrptsrel lldllgdpga
      301 vpaevlrspp plivrvppat afaspgsvpg svpgsvpgsv sdsasvaqpe atgapggyrl
      361 pgpvssgehp ppgspatsag mglgvvhgtg psfaevettr rtgqafnrag lavsaallvs
      421 aavlvtvvvp afrsdgppra agptaittap agtltrpdak ateksgrtpe trgpsseppa
      481 rvpagvrvpa lagldraaai ralkraglat gtvtqvdsgr evglvlttqp vagalvskga
      541 avglrvsagl pvpvvaglqr kaaeaaltga gltvgavtas cstqptgqvv sskpeagsrv
      601 aggarvalvv srqgaavpsv tgkapaaara elraagftvt rqgrmvtdea qvgtvlaqsv
      661 aagacarpgs gvvitvgvea qtdpdpteps eppatqspep paeg
//
LOCUS       WP_357685344             281 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            rifamycinica].
ACCESSION   WP_357685344
VERSION     WP_357685344.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 281)
  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..281
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..281
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31272
     Region          18..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          100..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtvsptvrrr riarelrqlr eragmtldva arqldmsksn lsrienaqig ikprdvraal
       61 alyqvtgdda ealieiarga qqrgwwqnys dvlpewfefy vgleaeaesl rtyeaesvpg
      121 llqteayare mfrrtageeg lerkvaarlr rqevlhrqsp pvdlsvvlne avllrpvggp
      181 avmaeqlthm trvaqspnvt chvlpfasgg hpamstpyvi ltfadaadns vvyldnltlg
      241 laleevghvr gytlvheelc rmaldpaesl trleeasrhf a
//
LOCUS       WP_357685373             318 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Micromonospora
            rifamycinica].
ACCESSION   WP_357685373
VERSION     WP_357685373.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         <1..318
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          64..305
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 ggadagpagt gtgptgtgaa ptgtgaaptg tgtaptgtdt gpapadlyvi agalfgyvda
       61 lagaaaegfl deqrdtaqdw atlrrrlvtl lvqpdppaeg vlhaaaeaar wplpatvavv
      121 svhgtdaehl arsigagava tvigdavrvv lpeprtpgrt egarqalagr raafgpavar
      181 hrarlsyrls rralvlhqrg algpdpvvsc ddhlltllta wepglaghla dtvlaplagl
      241 rpttrrtlae tlhgwlrrqg qvvavaedlh thpqtvryrm rqlralfgpa lddpdarlvl
      301 alalrsrptg gadhsdag
//
LOCUS       WP_357685446             176 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685446
VERSION     WP_357685446.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 176)
  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..176
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..176
                     /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=19498
     Region          3..142
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgrpsdtkar iqavarelfv eqgvrdtslr qiadrlgitk palyyhfasr ddlvrsiiqp
       61 lvedmegfva grrpgearhl ledyfellwr hrevtvmvvr elstlthldl ggrmfewrrr
      121 livlllgpdp ipaahiratv alggmadctv eyaslpmeev kdaaveaaaa alglap
//
LOCUS       WP_357685376             285 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Micromonospora rifamycinica].
ACCESSION   WP_357685376
VERSION     WP_357685376.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..285
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..285
                     /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=30462
     Region          31..226
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mgrrrgddri vvpvdtgrae lvpdpdrprs wtlllddapq shvdladpth lefeyvrrlg
       61 aaldliappg aplrvlhlgg galtlpryvq atrpgstqrv vevdgalvel vrrelpwpad
      121 prlrvrvada raalesgrda gydvvvadvf agartpahlt saeyagqvar vlaptgwyla
      181 nladgpplrh traqvatvrs vlpraalvgd aavlrgrrhg nlvlmagrve ppvpeltrra
      241 agdwfpgrvl agdeldrfva gaavvtdada tdslppppgi fsvrr
//
LOCUS       WP_357685501             396 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora rifamycinica].
ACCESSION   WP_357685501
VERSION     WP_357685501.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..396
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..396
                     /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=41414
     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 mrsavvvgag lgglavagal arsgwqvtvl eradrvrpep tavvlwpngv ralqvlglga
       61 gldaiatplp dggirrpdgh wlvqprptpa drmpvvvhre dlhdaliagl gervelrtgv
      121 gvdsvradag erpgvgyngr fveadlvvaa dgtdsvlrrq lapeasvvss gcaawravip
      181 wyratlpgdq pvggevlgag yrfvaaslge rgssggsrrg gvywvataag aprpepprtq
      241 lallkrwfag wpapvgella atepadlvqq eirelrplpr sygfpvgpgg vvllgdaaha
      301 mpphlgqgac lafedaatla sllresrlpd avqaydrlrr praatvvrqt rrmsavlqtr
      361 grlalrarda algtlsprll sgaattaaaw rpppss
//
LOCUS       WP_357685460             511 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685460
VERSION     WP_357685460.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 511)
  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 511)
  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..511
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..511
                     /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=55548
     Region          4..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(173,176..181,183..184)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(176,293..294,315..320,398,410,413,424,504)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(176,217..218,265,267..268,271,293..294,315..320,398,
                     410,413,421..424,485)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(217,267..268,271,293,421..423,479,485)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mlnlstvleh sarttpdgta ivfgdmrlpy smidtvarqv anllvsrgig kgdkvalacp
       61 nlpyfpfvyy gilkagasvv plnvllqsre iayhlddsda kalfcfegtp elplgeraka
      121 gfeasegceq ffvlpatpla teseygesfw aaldgmpaef etvqtspddt avilytsgtt
      181 gqpkgaelsh qnmlmnamvs demfprtegg dvtlavlplf hsfgqtvvmn sgfrrgaalv
      241 lmprfepgda lalmrkegvt lfagvptmyw amltkihaeg aevprtlrva iaggasspve
      301 vlrdfeetfg igilegygls etspvasfnq lgrptkpgti gtpiwgvemk lidgdwkpid
      361 gegpgeiavr ghnimkgyyg rpeataevmr dgwfrtgdia trdadgyymi vdrakdmiir
      421 ggfnvyprei eevlmtheav slaavlgvph dshgeeikay virtpgatvt eqdlitware
      481 nmaaykyprv vefrdalpmt atgkilkrel r
//
LOCUS       WP_357685523             237 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685523
VERSION     WP_357685523.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 237)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..237
                     /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=25415
     Region          36..>78
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..221
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 madllwgira egsrgpkpml tldriadaai giadaeglta vsmqrvsael gftkmalyry
       61 lpgkkelvav iveralgepp dlqdmtwrag lrawahalla ahlrhpwtle avmlprpvgp
      121 nelswmeaal allvdtgltg aerldifavl tgqvrviahq aratsrsedh fltaigdvlt
      181 khadrfpala rtvaeatmsa agqnqafdfg lerildglqa liegrgdsvr tglgdvp
//
LOCUS       WP_357684980             163 aa            linear   BCT 28-DEC-2024
DEFINITION  CinA family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357684980
VERSION     WP_357684980.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 163)
  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 163)
  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..163
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..163
                     /product="CinA family protein"
                     /calculated_mol_wt=16696
     Region          1..150
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mtqaaevlsl lmgraatvav aesltgglig arftsvsgss kafrggvisy atdlkhtlla
       61 vpedllereg avhpevaeam algvarvcga tyglavtgva gpepqdgrpv gtvfaavsgp
      121 ggrlwrrels lkgsrerirv ktvdeavdll asvlkpnkge qfg
//
LOCUS       WP_357685591             222 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685591
VERSION     WP_357685591.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 222)
  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..222
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..222
                     /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=24100
     Region          8..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvtvavraer anatreqile aaerlfaehg vsavsnrqis etagqgnnaa vgyhfgtkad
       61 lvraivrkha grveilranl laeigdsaea rdwvgcmvrs ltdhlavlgs ptwyarfaaq
      121 vmvdpalrdi videaltspt lqrildgmnh clpelpaevr aerydmarql mvhmcaerer
      181 alaegrptpr pswhaaangl idaivavwla pvtpgqaern vs
//
LOCUS       WP_357685615             274 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate deacetylase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685615
VERSION     WP_357685615.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..274
                     /product="carbohydrate deacetylase"
                     /calculated_mol_wt=29771
     Region          3..272
                     /region_name="ChbG"
                     /note="Chitooligosaccharide deacetylase ChbG, YdjC/CelG
                     family [Carbohydrate transport and metabolism]; COG3394"
                     /db_xref="CDD:442621"
ORIGIN      
        1 mtrrvvitad dlgrepgtte vivallaegh vtattlicvs aaaeqaanqv relgvlprvh
       61 vtltserglp rwrplngaas lvdpdgtlsd dplalgarge ardvireada qlhwmrhrgl
      121 tpqaadshag tlyglhgrsw laealewcar hglafrlprd pepyfggplp prlaaahera
      181 valadalgvs ipqtiatnrr sahelgayer lrddylrrla alpegtself lhpsredavt
      241 gpdgivrtwe arllrdpvwh naleservev vggw
//
LOCUS       WP_357685622             215 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685622
VERSION     WP_357685622.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 215)
  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..215
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..215
                     /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=22950
     Region          8..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marrtqgrsa gldreriaat avalvdrdgl erfgvrrlae elgvdpmsiy hhikgkaall
       61 damseavlae vavtaddtsh gweetarwta hgyremayrh prvfpllatr aqtspvalsa
      121 lerlvtamrk aglpdqvvad aplmlfgfln gyllavlsge pdgagdlpai datayptmat
      181 lmplqagfgs laefdrmlgt vldgirhraa qsgsp
//
LOCUS       WP_357685707             347 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685707
VERSION     WP_357685707.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 347)
  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 347)
  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 347)
  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 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 347)
  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 347)
  AUTHORS   Rosinski,J.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..347
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..347
                     /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=37863
     Region          1..231
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          248..312
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mgleltftaq daanvrfavs plwevvasvr vvknpaahav lkpwaervrr rladvdwrll
       61 sdlvpvptis ivgfvcppps tsvpdlevel atmaamaplv qegldawdgp rtqalqalha
      121 dpagglerla eeirdyweaa iapywprira llegdvlyra rllaegglrr mlsdldtavt
      181 weeeklrlpk avcegvrplg glglllvpsv fawprvfsit tppwqptiry pprgvatlwe
      241 hrecdppqal aavlgrtrtr llaeldqpas tkelaarldl sepganqhlt alrraglasa
      301 hrtgryvlya rtaiaetlla gdaspipgsh gypragitel ldpprph
//
LOCUS       WP_357685718             213 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685718
VERSION     WP_357685718.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..213
                     /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=23088
     Region          5..196
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 msavnraafl reflrspftv gavapsgepl adlitspipr dgdplvvelg pgtgaftgai
       61 qqrlagrghh laielnqrfa dllaarypqv dvsvadarhl rekltdrgld hadvivsglp
      121 waafapglqd dllcavthal aphgvfttfa ytytrwappa rrlrhslger fdevvvsrtv
      181 wanvppafvy fcrrprvpaq trplipdgra cva
//
LOCUS       WP_357685761             667 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-ketoacyl reductase, partial [Micromonospora rifamycinica].
ACCESSION   WP_357685761
VERSION     WP_357685761.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rifamycinica
  ORGANISM  Micromonospora rifamycinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172469
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Micromonospora rifamycinica"
                     /db_xref="taxon:291594"
     Protein         1..>667
                     /product="beta-ketoacyl reductase"
     Region          2..465
                     /region_name="KR_1_SDR_x"
                     /note="ketoreductase (KR), subgroup 1, complex (x) SDRs;
                     cd08952"
                     /db_xref="CDD:187655"
     Site            order(229..230,232,252..255,280..283,303..305,326..327,
                     349..350,364,391..392)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187655"
     Site            order(327,351,364,368)
                     /site_type="active"
                     /db_xref="CDD:187655"
     Region          487..571
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          589..>667
                     /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 mvgglryriv wkpllvgdph pltnrwllia dpetadsala adieaalvrr gaevelltvd
       61 pladrpllae llagtmnrat pisgavsllg lvseahpeyp avgmglvssl mlvqaigdag
      121 ldlplwtvtq laaaavpqev pdafgaqvwa fgrvaalelp drwgglvdlp sapdarmldq
      181 lggilnradg edqiavrasg iygrrvtraa daarrswrpr gnilvtggtg slggrvarwl
      241 arngaehlvl vsrrgarapg aaeleadlrt lgaevtivac dvadraalag vlaahppsav
      301 fhtagvlrdg vidalvaghi devfrpktva allldeltre qeldafvlfs svtgvwgngg
      361 qaayaaanaa ldalaerrra aglpatsiaw glwggggmae gigeqnlnrr gitamdpdrg
      421 iaalqqaldr ddvtvtitdv dwptfatrha elsagrlfdg vpearnalda rkadtessta
      481 glsqrvtgmp daerqrfllq tvraeaaavl rhekvdaias trafkdagfd sltalelrnr
      541 lnsvtglnlp stvvfdhptp stlatfvedl llgasteetp vvpaavpide piaivgmacr
      601 ypggadtpek lwdlllaead vigpapddrg wdvdslfdpv rgvvgksyvr eggfvydagf
      661 fdaeffg
//
LOCUS       WP_357685806             355 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685806
VERSION     WP_357685806.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 355)
  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 355)
  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..355
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..355
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=39579
     Region          5..354
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mdelaatvtg fattlraagv gadherarnl lkaldhldvt sprdfywagr ltlcatpddl
       61 prydrcfeay fggrkatatr vstttvtrht aagdgerdde gtaapatasr tellrhrdva
      121 rltdseraev hrmlsmlksg rarrrsrrfe ashrgemdqr rtirealrkg evarllrrah
      181 ttrprrvvlf vdvsgsmapy setllryaha lvrsepratr vysvgtrlts itaelrhrdp
      241 gtalnevsrt ipdwsggtrl geelreyltr ysargaivvv asdgwergdp ellgtqlarl
      301 srqayrviwv nphkgyedyq pltggmraal pylddlvagh slaayaelse rlaha
//
LOCUS       WP_357685817             623 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685817
VERSION     WP_357685817.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11601498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..623
                     /product="serine/threonine protein kinase"
                     /calculated_mol_wt=62195
     Region          12..308
                     /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..37,65,70,75..78,90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,73,89..92,96,98,135,137,
                     139..140,142,152..153,156)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(19..20,22..25,27,40,42,73,89..92,96,137,139..140,
                     142,152..153)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Region          249..>447
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
ORIGIN      
        1 msdeapslva gryrldelig sgpmgevwra ydtradwtva vkllgaqaag aatrevlkrh
       61 aqavakvihp nvamvldvgd rdgapflvle fltgeslgee laargplkiv dvcdlvgqaa
      121 agldaahrag vvhgqvspgs frragsgvlk vvgfgladqp paadavryra peladgraad
      181 asadlyalgc vcyellcgrp pfdgappest ppdapgtsas gtsasgasas gasapgtsas
      241 gtsvhdgpgt sggpagpgma raaggpvpps rhrpevpael drlvlallsg dpagrpagge
      301 avrralaaia rprpqappms gpmpgptgpt gsmsgpmsgs mpgsmsgpms gsmpgsmsgp
      361 msgpmsgsmp gptsgsmpgs mpgsmpgrms gsmpgsmpgp mpgsmpgsmp gpvpgsvspl
      421 gmaaayqgpa prggdtaiye afpgeppasn kklfvqlgva vavivtvtvg mmawggsggs
      481 pvaapassap aatapptvpa ssapaerptp ttgpsevttl retgapnpka tlrdtvppgg
      541 wlkwlsefdk avtaqeamgs ieprtarkah dkirkaarrf adgredsgrd qlrdvmrdla
      601 kaqdkgdvat sgpladflsd wrl
//
LOCUS       WP_357685851             129 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685851
VERSION     WP_357685851.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 129)
  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 129)
  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 129)
  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 129)
  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 129)
  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..129
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..129
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14089
     Region          13..129
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 maavtqtatp smwseeelae vrgtlkteid elntdilrhe seiasgdvtq gagddqadag
       61 aktyererei altlnardlv aqneraiari dagtygvces chkpigkerl qafpratlcv
      121 ackqreerr
//
LOCUS       WP_357685966             127 aa            linear   BCT 28-DEC-2024
DEFINITION  PTS-dependent dihydroxyacetone kinase phosphotransferase subunit
            DhaM [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685966
VERSION     WP_357685966.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..127
                     /product="PTS-dependent dihydroxyacetone kinase
                     phosphotransferase subunit DhaM"
                     /calculated_mol_wt=12050
     Region          4..>94
                     /region_name="DhaM"
                     /note="Phosphotransferase subunit DhaM of the
                     dihydroxyacetone kinase DhaKLM complex, contains PTS-EIIA,
                     HPr, and PEP-utilizing domains [Signal transduction
                     mechanisms]; COG3412"
                     /db_xref="CDD:442638"
ORIGIN      
        1 mvgivlvahs aglaaetaal argiagaeap vaaaggtedg glgtsvdlie ralasvdqgd
       61 glvlipdlgs svltarllae pgrveladvp fvegaiaaav saaagaplad vlaaaadawt
      121 yrkvsgp
//
LOCUS       WP_357685915             630 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685915
VERSION     WP_357685915.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=63837
     Region          34..603
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msgllivasf aasaalgaqv pgdvlmvaaa vvagwgiavk aaralmarvv gidllvsvaa
       61 vgavvigeyw eaaavtflfa vghalenatl srtrsalael vavapevavv lrdgdqvevp
      121 aasvatgetv lvkngakvpv dgvvidgtga ldeasitges iplekitgdq vfagtvsmgg
      181 flqvratgvg adttlariih rveeaqdaka rtaafmdrfs awytpaiivl alvfglatgd
      241 vvlaltllvi gcpgalvisi pvaivagigr gakdgilikg gefletsari davaldktgt
      301 ltegrpyltd vvpldeawsr advlgwaara eagsehplar pivdaaraeg ldvtglpeat
      361 epvpgkgiva tldgrrvavg nlalhedegv pyaaaagvvd glaaagrtpm vvavdgrlag
      421 vvavadrvrp daarmvadlh aagvrrlvml tgdtrrvaea vaaqvgvdev hagllpedkl
      481 evvrdlqarg hvvamvgdgv ndapalatad igvamgaagt gvaietadia lmkddllklp
      541 ravslarrtv svmrqniaia lvtvgallag vllggvtmai gmlvhemsvl vvignamrll
      601 rrrgtpqngg satgptsnqs eardtdrqpa
//
LOCUS       WP_357685952             263 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357685952
VERSION     WP_357685952.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..263
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28279
     Region          6..248
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mptggfegai fdvdgvlvds phemawkeal relmegpwad vrdqsewsdd rftpevyqrv
       61 msgkprmsga laglehfkvp daearietya alkqellirl ieaerfkayp dalrfvlavr
      121 dagiptaaas ssknaglflr qirldtfaee eglaydfvrp gltlldffda dmsgrdvahg
      181 kpdpeiflna aaalsagpgq cfvvedavsg iqaakaggma algvaradda hlltaanadl
      241 vvttldevev palsghrlar rrp
//
LOCUS       WP_357685999             374 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357685999
VERSION     WP_357685999.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 374)
  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..374
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..374
                     /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=38940
     Region          25..367
                     /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 mrtaiterlg vefplfafsh crdvvaavtn aggfgvlgai aytpeqldte ltwideqvgg
       61 rpygvdvlvp gkidasaldr darladfipe rhrdfvthll skygvtgpgq plggsadefg
      121 rrvtaagatg lidvalkhpi gliasalgpp ppemvaaare agvpvaalvg tveharrqva
      181 agadlivaqg teagghtgei atmvlvpqvv davaplpvla aggiasgrqm aaamalgaqg
      241 vwcgsvwltt eeaetspavk rkmltassld tvrsrsrtgk parqlrsawt eewdsgqesp
      301 gplpmplqml vaegtmarvt aaaergepga lelanyfvgq vvgqmkqvkp arevvyemvs
      361 efadaverla rlsg
//
LOCUS       WP_357686065             144 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686065
VERSION     WP_357686065.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 144)
  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..144
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..144
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16599
     Region          8..135
                     /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..80,90..91,93,95,105,107,109,111,121..129,
                     131..133)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 maedprairl dqflahppak vwraltepdl iarwlmpndf rpevghrftf ttkprkavgf
       61 dgivhcrvle lerekllris wsdgkaadwt vtwrlepegh gtrlfldheg fdpddelqqm
      121 srrimgggwr sshirafadv ldtl
//
LOCUS       WP_357686066             108 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686066
VERSION     WP_357686066.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=12355
     Region          <25..85
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtadhvfaal asparrellr llldegaqpa grlaerfdmt rpsvsehlkv lrdaglvaet
       61 rrgrerhyrl epaplmeird wltpyerfwr erlaglstll demddddg
//
LOCUS       WP_357686069             111 aa            linear   BCT 28-DEC-2024
DEFINITION  PadR family transcriptional regulator [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686069
VERSION     WP_357686069.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (residues 1 to 111)
  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 111)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (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
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..111
                     /product="PadR 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=12136
     Region          1..99
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mnpdalrghm dalllsvied eplhgyaiie alqersggal svptgtvypa lrrlerighl
       61 tsewatvggr rrrtyrltgs grkhleeers awhefastig nvlrpgvrpa g
//
LOCUS       WP_357686086             424 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686086
VERSION     WP_357686086.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=44727
     Region          162..420
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 misavmnpla lalfrgeadp ppprsrrlsp avpgrlqvia pfqrfdlvlv adlllawilf
       61 atasgevvtg yasagesywe glpylaalai aapvvlrdrw plaawrtavv llpfsihvgi
      121 tikspggmpy tagatimyll vlysvsvrcd rritfatwvv tvlalwiihp dsvalgtvmv
      181 tvavvfgynv rvrrtatarl veeerrtqva egaqavlaer sriarelhdv vahhmsviai
      241 qaeavplkae gdpaqleagl aeiralslea iaelrqvlgv lrdqdgridt aplpgldrid
      301 dlvaharaag lavllkrpgs ldglppavgv sayrivqesl snamrhapga tvavdiardd
      361 rdlrlrvang pgvspggapg aghglvgmre rstllggvle agptpgggfq vtarlpiagt
      421 eetg
//
LOCUS       WP_357686109             467 aa            linear   BCT 28-DEC-2024
DEFINITION  diaminopimelate decarboxylase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357686109
VERSION     WP_357686109.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 467)
  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 467)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..467
                     /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]"
                     /calculated_mol_wt=49762
     Region          16..458
                     /region_name="LysA"
                     /note="Diaminopimelate decarboxylase [Amino acid transport
                     and metabolism]; COG0019"
                     /db_xref="CDD:439790"
ORIGIN      
        1 mtvtdlshap ealahapdgs vtfdgvslae laarhgtptw aisasqlrln yttlhaalsa
       61 rlsrpviays mkannnravv qtmaglgaal dcsseyelal avsagvpagk viingngksr
      121 ayltaairlg vwqinvdsia evdriraiar slgvtvpcav rlklsyarll rsdpsyertl
      181 riaegkfgss tqsgdaeavv raivaseele faglthhagf pgyradftae rqlmhqarca
      241 eeivefahll rrrmgivtpr lnlggglrsg rsvylstpgn ggdgefrtlp tpdeyaeaia
      301 aglagadwdp ivqfetggfh vgnavlllag vqdvkdvtrp rerryvtldc amtmftgrgl
      361 nrvgfpllvv ghgpgaaphp lpvelvgptc aydsiaedvs lpavregdlv allnqgayce
      421 vlstqfngfp rpavvhlddg dvrlvrrret ladiwaresa aldlwpg
//
LOCUS       WP_357686118             187 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686118
VERSION     WP_357686118.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=19440
     Region          1..156
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mriigiaasl hagsfvnrll kavggelppg vhfgcwpdla evppytpgpp pepvagllrs
       61 ldeadalvlt apehsllpae lthtlgwlsa fgalagkhva vmsasaracg amwaqaelyk
      121 elsaagavvm ggelvispsc phfdekgrli arylrdqvld vvrqlcpvsv gqpafgepvl
      181 repalsa
//
LOCUS       WP_357686189             206 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357686189
VERSION     WP_357686189.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 206)
  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..206
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..206
                     /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=22412
     Region          6..144
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvgirerkkq rtrraliqaa lrlfdekgye ettlaeiaaa advstrtffs yfaskedvlf
       61 fdaaariett lalvatrrpd eappellmri vraglawtve dqdfrpedvr lrmrlvmtvp
      121 alqaralhll fdnqlrltra lreaypgelg pveaaaavga lagatklavv aslnrdgsle
      181 qaaeaalqaa eitvrglasl grpaar
//
LOCUS       WP_357686157             281 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357686157
VERSION     WP_357686157.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 281)
  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..281
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..281
                     /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=30136
     Region          26..273
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mfrrlglvlt pvlailavtv padaasrpvi vahrgasada pentlsalap asrsgadmve
       61 vdvretrdha lvlmhdttlt rttdaesvfp grapwrvadf tlaeirrlda gswfgrasrg
      121 ervptlgeal ramsrsglgl lleiktpqly rgiearvage lrrnpswpga grlvvqsfdw
      181 gsmrtfhrim pdaaigllgt pspgelpgla dfadqvnppy qdvtaeyvrl vhgqgmavft
      241 wavdepgdae rvifdgvdgv itnrpgmlrs vvaddadlra a
//
LOCUS       WP_357686197             389 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686197
VERSION     WP_357686197.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 389)
  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..389
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..389
                     /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=40994
     Region          4..386
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mnvrhvvvvg aglagvrsve alrgrgfgga itlvgqerhr pydrpplska vllgdadssf
       61 vdsdlaalev dfrpgvtats lrpgavvtse gelgydglvi atgaepvmlp gdgpqhvlrt
      121 lddalelral lvrgarvavi gagwigaeva saarragcav tvieagpapl aqavgaeiga
      181 rtlhwydgid lrlntmvgsv deggvrlagg efvradvvvt gigvrpavew ladadidlhn
      241 gvvtderlrt slpgvvavgd caawwsrrfg vrlrvehwdt alsapdvaaa tllgeeavyd
      301 pvpyfwseqf ghmlqyaghh qagtrllyrg gpagkwsacw ltadgalaav lavdrprdlv
      361 qgrriiadgr rldterlvdp dvslrdcvv
//
LOCUS       WP_357686211             384 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686211
VERSION     WP_357686211.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11461692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=41516
     Region          <135..378
                     /region_name="LytS"
                     /note="Sensor histidine kinase, LytS/YehU family [Signal
                     transduction mechanisms]; COG3275"
                     /db_xref="CDD:442506"
ORIGIN      
        1 mlttacvvls sltfvlgygl arlaraprrg prvperrckd eatfttlhia amaapalrtg
       61 lhrdsarkav rhlhallgty avaitstdaa lawdgpctde vltyartala agraqvfage
      121 pygavvvplt vdgkivgala afddelsagl vrtvtevarw vsgqlelael dssrrralea
      181 emralraqis phfvynaltt iasfvrtdpv rarallldfa dfaryalrra hdfttladel
      241 tcvdryllle rarfgdrlrf slqvapevlp vpvpflclqp lvenaikhgm gsrggsgevr
      301 vvardagpea hisveddgag mdpeharrvl dddprregng iglanvdvrm rqiygegygl
      361 vvetalgagt kvrlrvpktq fssl
//
LOCUS       WP_357686221             300 aa            linear   BCT 28-DEC-2024
DEFINITION  lactonase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686221
VERSION     WP_357686221.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..300
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..300
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31396
     Region          4..299
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mkclyiggyg pgiltigdgl trlaspsfla ahptlpvlya agelaqgwlt alttegglkp
       61 lderssdgds pchvavhpsg tllavanygd gtaglhhlgp egaftgkpiv lrhegsgpvr
      121 drqegshahq cvfhedllhv sdlgadeirr ytldgtplep lrlapgtgpr hmafagsrly
      181 vvgeldgivt vidgesrqga pasrregvnq pshlavadgl vyvgnrgpnt isvlraddls
      241 pvaevssggd wprhfaidgd rmyvanqhsd avtvfalkdg vpeptgqaye vrspscvlpc
//
LOCUS       WP_357686226             155 aa            linear   BCT 28-DEC-2024
DEFINITION  Dps family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686226
VERSION     WP_357686226.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..155
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=16945
     Region          8..153
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 makitgplsg dakntvaeal qgalvdlidl slvtkqmhwn vigshfrpvh lqldevtsla
       61 rrhadviaer aaaiglnpdg rsttlgkstk ltqpergwie dgkviatmsd ildgigqrmr
      121 erveateepd pvsqdliisv aqdidkqrwm fqaqr
//
LOCUS       WP_357686259             399 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686259
VERSION     WP_357686259.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 399)
  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 399)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 399)
  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..399
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..399
                     /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=42683
     Region          150..399
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mserreheyh walpsvllgd ggdgpparrs trdwivdvvm flaacgltll taseltgvpr
       61 plviveqvag vlacaavwlr rrwplgfalv ttalssclal vggaavvglf tvavhrpfri
      121 sgpfvlfslv alvpyvllrp dpdlgpagel ilgvaivltv fawgivvrar rqlvwslrqr
      181 aiiaagearr lereriarem hdvlahrism lslhagalef rpdapaeeia raagairdsa
      241 hqalqdlrev igvlrhpasp qddpvpdrpq ptladlpalv eecrragmev slsmpgpapq
      301 evpqglgrna yrvvqealtn arkhaggapv avtvsgapge gltvevrnpl wagrssripg
      361 agagliglie rvelaggrlk ygaapegdfr lrawlpwtp
//
LOCUS       WP_357686261             270 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686261
VERSION     WP_357686261.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,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 270)
  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 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..270
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /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=28636
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msavrcdgiv qiytaqdvev valrdvdlvi epgetvallg psgagkstll wllagllrps
       61 agrlwldgve vgrldqrrld rlraahigmv lqnparnvig yltaaqnvaf aqravrtdrr
      121 rvrdllarvg ldgadgrpag rmsggeqqrl avavalanap rllladepts qldtasggrv
      181 idlikgaaer dgttavvvth dlavgealsr tvtirdgrvg aegrrgedfv vvgregavqv
      241 ppeyhhllpp gsmariepie dgvtlrradp
//
LOCUS       WP_357686290             266 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686290
VERSION     WP_357686290.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..266
                     /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=28773
     Region          1..256
                     /region_name="ModF"
                     /note="ABC-type molybdenum transport system, ATPase
                     component ModF/photorepair protein PhrA [Inorganic ion
                     transport and metabolism]; COG1119"
                     /db_xref="CDD:440736"
ORIGIN      
        1 mhvvelegvg vrvvgkalls dvdwqveyge hwvilgpnga gkttllslaa avrhptegtv
       61 svlghrlgrv dvrslrrhig lvassqrlid eelleeegat ahtvvltght gtsaplwdry
      121 gdaeheralr lladlgckdl adrpfrvcsq gerarirvar slmpdpavll ldepfagldl
      181 paredliaav edlaatrpvl ttitvthhle evpstttham lmcdarvlaa gpvadvltps
      241 nlsdcfgral hvdrldgrwy aravrl
//
LOCUS       WP_357686365             493 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686365
VERSION     WP_357686365.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 493)
  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..493
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..493
                     /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=51452
     Region          5..113
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          226..492
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrirdllaad elsltlltgd pgrefhtvhi tdlpepgryl sggelvltgl mwrhtpadsa
       61 rfvaalveag vaalgagrar lghipadvvs aceeaglpll dvptevsfrt iaelaaprlt
      121 gdvrdalgrh rrlvaavaeg aglpelfelt aaelgitgav lsatgevivg avddparlar
      181 ayltasrlpc pagrhtvfgv gsghraagwv lacdgdlmdr adlgyelaac valersrmee
      241 grrverrlae rlvmaaltga dpaelnaglr tcgigatepy avahvtvprv gagrgpdpaa
      301 lggpvaeell grevvaaaga dgavalvplr gttvaglaer lrhgvevlsa lpdghvcvgl
      361 sgeltgaaai kggveeagha rrlaearsgg vvtsdeiyth alllatvpgd vrrsfagrll
      421 gplvdydrrh qselvrtlgt fldcagswna caermhvhvn tvryrirrve dltgrdlsam
      481 adrvdfflal rag
//
LOCUS       WP_357686371             210 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357686371
VERSION     WP_357686371.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 210)
  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 210)
  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 210)
  AUTHORS   Rosinski,J.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..210
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..210
                     /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=22013
     Region          36..103
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          119..207
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
     Site            order(122,137,139,151,154,158,192,194,207)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380339"
ORIGIN      
        1 mdrvrqaeri dfwseqvgng sasegvreps dligliagai rreraragls ltelarragl
       61 akstlsqles gagnpsvetl walgtalgvp fsllvdpprp dvrvirageg pvahseqagy
      121 aatllascpp narrdvyriv arpgtprlsa ahppgttehv vlssgralag paeeptelgp
      181 gdyvtypgdt phifqalrag ttavfvmehl
//
LOCUS       WP_357686375             477 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686375
VERSION     WP_357686375.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..477
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..477
                     /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=49707
     Region          1..477
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msadavvvgs gpnglvaaim laragrevll leaaerfggg lrsaeltlpg rvhdlgatvm
       61 amalaspalr glglegrgpg qvefvhpava aahplddrpa vlvhrdagrt ceglgvdgaa
      121 wgatvgaaar agfplvdllv kplgpwrpep rafaaaarfg vaaalpattf arrvlrtveg
      181 ravfagmaah svldlrspit sgyglllasl ahlvgwplvk ggsqvladal varlrglgge
      241 avaghrvrrl delaglgaet ivldvtprqf lemadlpary rrrleryryg pgvfkldwal
      301 dgpvpwrdpa vaaagtvhlg gtleeialse aevaagrhsp rpyvllvqpy aadstrgght
      361 lwaychvpng spvdmtgaie tqieryapgf rdrvlarham gpadleawnp nlvggdiggg
      421 laglgqflrr pvwspapwrt plpgvflcsa stppggavhg mggwqaarla trpaarr
//
LOCUS       WP_357686376             348 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686376
VERSION     WP_357686376.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..348
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..348
                     /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=37732
     Region          12..348
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mtprhdprlk afasdnyagv hpdilraiad angghqiayg ddvytealqd vfqwhfgeqa
       61 hawpvfngta anvvslramt ahweavicae tahintdegg apevaggikl ltvptpdgkl
      121 tpelidrqaw gfgdvhraqp rvvsisntte lgtvytprev aeicahaher gllvhldgsr
      181 ltnaaaaldv pmralttdag vdvlsfggtk igmlygeavv vlnpsaatgv dyirktfmql
      241 sskmrfvsaq feallsgdlw lrnarqanam grrlaeavrd lpgvevprpv eanavfavlp
      301 kevterlqkr frfytwneat gevrwmcafd tteadvdafa aaiaeela
//
LOCUS       WP_357686390             319 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686390
VERSION     WP_357686390.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..319
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..319
                     /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=32401
     Region          8..315
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mlagllggaa dispwqvvlq aldwlpfvtv dsglapveqg llyelrlprv lvaavvggll
       61 aiagagyqgv frnpladpyl lgaaagaglt atvvivllpg lpgglplaaf agavggvfla
      121 yvlgntagra ggtatlvlag vavtsfltai qtfvqqfkve klqriyswil gdvgggwdqf
      181 wmvlpyaavs avllilhgrl ldvlsvgdee atglgvraar vrlavllaas lataaavavs
      241 gligfvgivi phvvrrlagg syrivlplsl vggaaflvla dllartviap aelpigvvtm
      301 fvgapffvav lrmtrqaat
//
LOCUS       WP_357686428             294 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686428
VERSION     WP_357686428.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 294)
  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 294)
  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..294
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..294
                     /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=32014
     Region          <116..247
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mrlpphilvv ngikvrrpvf llgaphsgad llvralkrsp gfhlttgrpc vahvvyafar
       61 kpsigrgsga vrvlrdalae swqvlpgacg qcaepcreag gvtgsgpcva tgeitrfgdg
      121 spdllysapv ldqafpdaqf vqlirdgrdv vadmladpvc lawfkpvmla qhtefpndfl
      181 gvnrdehver wktmpaagks alrwrsavrl satlrqelpa grlltlryed lvhkpaesva
      241 altefletrv skvalygtra pevgcwrtrl rpadlelvek varqeltrlg yltg
//
LOCUS       WP_357686484             293 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686484
VERSION     WP_357686484.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 293)
  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 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   3  (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   4  (residues 1 to 293)
  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 293)
  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..293
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..293
                     /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=31727
     Region          <3..292
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mtalvsfdrv feildlkpmv aerpgaepvs ggpvtiefdd vhfrypsaee vslaslesva
       61 rqdtgpsqpv lkgvsftakp gqlialvgps gagkttitsl vsrlydvneg avrvngldvr
      121 datlaslres vgvvmqdphl yhdtieanlr yarpgasdee lwealraaqi gdlveslpdr
      181 letvvgdrgy rlsggekqrl alarlllkap rvvvldeata hldseseaav qralktalag
      241 rtslviahrl stireadeil vvqdgriaer gehdellrrg glyaelyrtq fsr
//
LOCUS       WP_357686541            1160 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686541
VERSION     WP_357686541.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1160)
  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 1160)
  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..1160
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..1160
                     /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=129207
     Region          179..1109
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mrrrtlgyed avrilggesa vlrafgwlsg agltvasagg selalslfdl kgeverlsqd
       61 avstvrrrvg gltrfersel leaahvvivi aafftalddl dgelrttlnt ttlelvraeq
      121 aalatgrpvq ggriaelvev lntpgnlpdm gahwrqtpll ayyqtlarrl lefgpgtaaw
      181 dgadettrlr waagletdlp rlattryerm lrqlasdype vafwahqagv rvlldelkaa
      241 rqdvtetgtk laglarmvrw maqgrapdal rsalsteyra qvdrpltdpd avpdgvrlpk
      301 lrevyvnpsy rrltglgraa eqpeqvseag wrnaelgddl etflvqhlis paatkaplvv
      361 lgqpgagksl ltqmlaaqlp pddylvvrve lrdvsadadi qhqieealqk itrvehewqt
      421 vsascapalp vvlldgfdel lqasntvhyd ylekvkdfqd rgarhghpaa vivtsrtava
      481 dqvrypresv vvqleeftda qvrrwierwr aanpqralnt eealvhgeia rqplllfmla
      541 lfhadggelq gkigqtelye slfsrfaere vdkrgrhlge rdrrmliare lylmsmvafs
      601 mfnrssqsvt deglardlaa lpfggdprrr dtaldtaqev agrfffklfv hrnqaveght
      661 lhrryeflhs sfgeflvgrw iadelvrvag qllknaddpi pvapddtrlr tlvsfavlag
      721 rarvveviad rfrarsseel velrallirl frecmdsrap ellspayepv rlgvparfav
      781 ysanlctllv haagalaard psltrislae lgfhedldea srsffaitrs whahlnrksw
      841 hamldvirvt dssgsrdfhl sswnvaeipg egpnsasdll agltvrtnpp vlpgtwvgqv
      901 fretalldse tqhrmlttll pfleaaglfr gtefpigssg alamellvhr rpfdavsrsd
      961 cyielldrep epnigfarlf lgalrnepar vqalvvtraw qeferlawah itafldalrd
     1021 clvsqfeapp pwsfhprftd pidvhnycal lgfrevphhf dvrdlacllv lrdlmglgtl
     1081 dqvealcqav phweppghqe lvqvalwaam aerdlvaygp psinlsreqa erldevapgy
     1141 ltgiselatl wrqenpvvir
//
LOCUS       WP_357686545             392 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686545
VERSION     WP_357686545.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=41650
     Region          143..390
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mqdrvkdrvk arvkarvrlr ktdtliavav ltlgvvgtyg rlsdsglter pldafgltli
       61 tvaslalawr riapipvgmi avgcgiayyg alypgifaaa paliatytaa tlgrrnlava
      121 lavtlavgvg vlvalsdtdp epgglsllsg wlvaavvfge vtrnrrayln eveqraieae
      181 rtreeaalrr ageerlwiaq elhdtlthai svinvqtsva lqllerdpgl artalravke
      241 sgheamhelr atlgvlrqae ldgqeaglar lprlveraea aglpvkmvvi gdrrelppev
      301 draayriaqe aftnvlrhag pasitltiay apemitlrve ddgnndagta ehgmgligmr
      361 eravavggsl vtgprpeggf avqtelpvgt lt
//
LOCUS       WP_357686569              84 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357686569
VERSION     WP_357686569.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 84)
  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..84
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..84
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8923
     Region          23..>74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mvrppltpee rlrgerlgll lrqargersi vevasaagms aetlrkietg riatpaffti
       61 aalaevldlp ldhlavrlap gvpt
//
LOCUS       WP_357686582             184 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357686582
VERSION     WP_357686582.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 184)
  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 184)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..184
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..184
                     /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=20589
     Region          7..176
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mtphtpppqe rgrrrratll taavdllteg gfaavthrav arrahlplaa ttyyftsrdq
       61 llaeafaqlv qtelttirtw itdhgltala dqiattdrhr qlglwelyvh agrdpvlqqi
      121 arrwtdgcvq liaetlhqpp ghprvrllyt tvstlwleql veqrpldetr tllaiaiena
      181 sppt
//
LOCUS       WP_357686625             293 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686625
VERSION     WP_357686625.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..293
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30933
     Region          3..215
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mkievrdltk tfgsisavtd lsfdvgegtv tgflgpngag ktttmrmmlg liaptsgtat
       61 fggrrysdlp rpsaavgavl dsagfhpaht ardhlrvyar mgrygaarvr hvadltgvsa
      121 fagrltstls tgmrqrlsla tallgdpqvl lldepsngld pegiawlrhl vrelaadgrt
      181 ilvsshvlge vehmadrvvv irdghlvtta pvtelygpat vlvrspqadl faagltkagt
      241 rversrpdll rihglstaei aaaatsrgit lheitperpt leqaflhltg gpr
//
LOCUS       WP_357686628             377 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF1648 domain-containing protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686628
VERSION     WP_357686628.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..377
                     /product="DUF1648 domain-containing protein"
                     /calculated_mol_wt=40471
     Region          1..364
                     /region_name="COG4194"
                     /note="Uncharacterized membrane protein, DUF1648 family
                     [Function unknown]"
                     /db_xref="CDD:443348"
ORIGIN      
        1 mipllillal vtclmwmlpa ltrptlpfgv rvgvqrvgdp avisarrlya rlvvvvavla
       61 aaisipallv tgssvvigla atvvivadll lyhrahltvr aakhaggwaa drrqavtvdt
      121 tfrtdpvrvp wlwglpamav llltaglgwa rygelpatlp lfpgygtass krepttllsa
      181 fqpviyqviv tlivlavvmv vlrarpdlda arpkgsarry riylrgvaam sllsaaclnl
      241 slflaalplw eivtstivwq vavcvplval lggwlawevk vgqaghrlpa lpgeeredsg
      301 idqrdddrhw flagavyvnr rdpallvhar lgsaswtlnl ghpiawllig vlavalavfa
      361 vlalagvvdp pqrhnlf
//
LOCUS       WP_357686649             256 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357686649
VERSION     WP_357686649.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=26768
     Region          1..248
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msefggkval vtggsmgigr avidrlaggg asvvfcgadk daefdsehvt gvvadvrrag
       61 dmrdlvdlav trhggldivv tcagvqrygt vvdtpedvwd evldinlkgv yltckaaipw
      121 irargggsiv lmssvqafss qtrvaaytas kaalngltra maldhapdgi rvnvvcpgsv
      181 dtpmlrwaad lwrgelsqde qvaqwgrahp lgrvgrpeev aelvaflagp hssfitgaeh
      241 rvdggllarn paalpe
//
LOCUS       WP_357686631             525 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686631
VERSION     WP_357686631.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 525)
  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 525)
  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 525)
  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 525)
  AUTHORS   ter Beek,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 525)
  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 525)
  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..525
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..525
                     /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=54716
     Region          14..483
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mtshlgrrlg ralrvtgrps rplllalsvv tvavalvpvv ylgvrtaeag warigeellt
       61 vrvawlafrt lglaavvtag clvlgvgsaf lvvrtdlpar rlfavlaalp lavptyiagf
      121 awrstvdgfe gfwaaalvlt lcsypyvflp vaaalngadp aqeevarslg rspwraftgv
      181 tlrqirpalt ggallvalyv lsdfgavsiv rtdtftraif vafdlgfdrt galvlssalv
      241 altmlilage tasrrrgary ahlggarrqp arlrlarlrr pavvalvala glslgvtavs
      301 lthrmiqgvs rpgawaevva amgnslwlsf agaaltmlla lplgllsaka pgplattldr
      361 laylshalpg lviglslvsf gvtlayplyq ttwllalgya alflplavaa vagaaaqapp
      421 vlddvarslg rgplsvlrtv tlpltlpgig agaalvfltc mkelpatlll rptgtdtlat
      481 elwthttvaa yaaaapyaal lvalssvptw lltartgilt repsr
//
LOCUS       WP_357686813             429 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357686813
VERSION     WP_357686813.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 429)
  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..429
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..429
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48303
     Region          9..76
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(11,15,51)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(14,50)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(21..22,44,47,51..52)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mpdyvpnvrl rawrnqenls raqmaekina tpiglaqrlt cdeerirrwe agevkwprte
       61 yrlaltqltg kepeelgfsq grqnesrlie arvipadalr aeadlygtme laqqlqasdv
      121 gtgtlealae avdllcrayp vvpagalrdr tqkrlaqinh llagrltldq hrellvttgw
      181 ltallgcvhy dlgereeaet arraafemgr qvghgelmgw ahemsawfal vegryedvvt
      241 aarmgqavag tssamvqlal qearglarig drreadralt rgaevlsslp mpdhpdhhfv
      301 fdhakwvfya atcytwladd draeeharet iqmhmrpdgt snapmrvada hidlgivhar
      361 rgdldaaveh glaafdidrr slsdlvnrag dldrvlrqry rretlvqefr erfstarhal
      421 trrnpelld
//
LOCUS       WP_357686842             474 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686842
VERSION     WP_357686842.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 474)
  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..474
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..474
                     /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=49608
     Region          26..472
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtvldnrvvt sgsdqepvdp rdpvvrlsal ldegslrlit pedksgvlaa mgrvegvpvv
       61 afcsdarfqg gamgsegceh ivhaydvavr ervpvigiwh sggarlaegv eslhavgrvf
      121 asmtkasgvv pqisvvvgaa aggaaygpal tdlviladsg rifvtgpdvv rsvtgeevss
      181 aalggpephs krsgvvhivt ktetdallra rqlasllghq grvrasdtde idfssllpes
      241 arraydvkpl vnglldepgi elhpkwapni vtslgrlggr tvgviannpm rlggcldats
      301 aekaarfvrm cdafgvplvv lvdvpgylpg vgqehdgvvr rgakllhafa easvprvtlv
      361 trkayggayi amnsrslgat kvfawptaei avmgavaavr ilkrrdlaaa peeeraeleq
      421 rlarehekla gglsrahelg videvidpre trgaiakvla qatpargahg nipl
//
LOCUS       WP_357686846             883 aa            linear   BCT 28-DEC-2024
DEFINITION  CHAT domain-containing protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686846
VERSION     WP_357686846.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 883)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..883
                     /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=91558
     Region          80..106
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          115..146
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          129..841
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
     Region          152..180
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(153,156..157,160..161,163,195,200..201,204..205,
                     207..208,234,237..238,241,245,248)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          193..225
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          233..262
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtrsrdrgsg aasgrrppvp vgsphppppa gapgdtkplv qaaeaavlrs ivdpeqalya
       61 grtvlsaaea cgdveaavva lramalgare lgdlqaaerh lrraiatpka pserlaqarl
      121 slvtvrterg hplqalriaa lawaylspld rakldtqrav alahlgryqe aiascdralh
      181 alvaapgtid drrflaggll nrglvhayrg dwdsamrdit aclqiarhag ldhlarlaaa
      241 nlpflavrrg dlagafghyr aaedalfgfp erlatmradf agallaahlp gearelltla
      301 vpdleasgal valaearlkl aqvelltgda rralavaera ereltaqdrv swlplvnevt
      361 lrarlmlegp spellaelva cadeletgsa laasaaalrl lsaetalavd dhpmasaqla
      421 hltshvppha pwvpagarlt slsseaqarh lgqvsqipap vrqhalalea slqedvtgaf
      481 ravrdglaev gsqmdtlddp svrahaarag erlaafglsl avrdgspaev fdwaerwrav
      541 aapahargma dpdqvraalg pgalvefvvd dtsllavvit germvlrrlg glgpiteali
      601 qlryalrrss lgdgawaggl vgpaaeeler lllrpieael gdrpvvvvpa gvlhtlpwga
      661 lpclserpvs vaagatawla arrhgpvpst ppvvaaaagp glahagaevg rvlalhprgr
      721 evagrtgavl dalttadvlh laahgvfhar spllsaitle dgplmaydll glsrtarlvv
      781 lsacdsgmar tpaegaplgl agtflargtt cvvagmvpvr dedalavmtl fhellatgrp
      841 pasalasaaa ktgvlgfacf gagdqpvatg lagsatqldh ept
//
LOCUS       WP_357686848             375 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686848
VERSION     WP_357686848.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..375
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39702
     Region          21..370
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mvenaplipa yggssladlp rsllaalgld ehnvlgiqpa qriclflvdg lgaellraha
       61 dvapflasag sttltagfpa ttvtslcslg tglppgehgm mglmlavpga gylfnclrwt
      121 lpdkmvmdpl twqpattvfq raaaagiass yvapgafegs glteavyrgv rylgadpvee
      181 rvervrqalr eapayvtvyy gdldavghmt gwgseewlrq laivdqmaer laetlpggsa
      241 lyvtadhgmv nasdkieads vpaltrgvam lggeararhv yaedgaagev ldawretlag
      301 rawvvsrqea vesgwfgprv raewlprigd vlavpytdla itaptvhrle aaftgyhgsm
      361 taaeqyvpll evstr
//
LOCUS       WP_357686851             297 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686851
VERSION     WP_357686851.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 297)
  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 297)
  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..297
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..297
                     /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=31001
     Region          3..297
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mtrvvvvgdl mtdavarary alarasdtpa vvtmhgggsg aniaswlave gaevafigrr
       61 gaditgrnrd melmgygvda rlvmdperpt gtcvvlvthk gertmlsdpg anaalspedl
      121 prdlfngggh lhlsgytlin egsrdaglaa ldmahrsgms itvdcassap lertgaepfl
      181 ewtsgakllf anidqakvlt grddpeaaak vltawfpqvv ikmnsegalw fgngrpdpir
      241 vaadpvdrmv dgtgagdafc agflpswlag kppaeslasg crlatkailh lgarprl
//
LOCUS       WP_357686890             117 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686890
VERSION     WP_357686890.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..117
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..117
                     /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=12419
     Region          <1..>59
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mgsllrcvql pgvggdtcwa ntclayetls pslqrlcdel tavhditmsm rdvdeeghrq
       61 gapvrpgggp gevaadraar asactprpda rrcsstaarr rdrpgsptar trrcrpc
//
LOCUS       WP_357686913             285 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686913
VERSION     WP_357686913.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   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 285)
  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..285
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..285
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=30027
     Region          3..>154
                     /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 mntltvpgat lhyevggsgp vlllicggvy daagyaalak rlsdrytvvr ydrrgnsrsp
       61 ldgppehqsi evhgddahrv lsavgvtgea pahvfgnssg gmiglelatr hpeqvrtlvv
      121 hepplfellp drdhwraimr dvdeafqkeg aeaagrvlaa glqmsggeqg ddaeripggg
      181 pgseagsepd petmammarl gkntefflgy evppfstyvp dlatlrasqv rvlpavggas
      241 kgeppyraav vlaerlgasp vvfpgdhggf glhpeefaar lhevl
//
LOCUS       WP_357686923             472 aa            linear   BCT 28-DEC-2024
DEFINITION  xylulokinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686923
VERSION     WP_357686923.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 472)
  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 472)
  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 472)
  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 10167394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..472
                     /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=48345
     Region          3..431
                     /region_name="ASKHA_NBD_FGGY_BaXK-like"
                     /note="nucleotide-binding domain (NBD) of Bifidobacterium
                     adolescentis xylulose kinase (XK) and similar proteins;
                     cd07809"
                     /db_xref="CDD:466809"
ORIGIN      
        1 mtlvagvdss tqsckvvvrd aasgrlvrqg raahpggtev hpshwwtall raveeaggld
       61 dvaaisvagq qhgmvcldes gdvvrdallw ndtrsaaaaa alvtelggpa awadavgsvp
      121 vasftvtklr wlaehepeha rrtaavclph dwltwrlaga lglprsdwad apppaldrlt
      181 tdrgdasgtg ywspatgdyr tdllkaafgs vpllprvlgp vadaapgspv rvapgtgdnm
      241 aaalgvgtrp gdvvvsigts gtvfavsdap sadpsgavag fadatgrflp lvctlnaarv
      301 mdaaarltgv dldrlgelal qappgagglt lvpylegert pnlpaatgsl hgltlatatp
      361 ahlarasieg mlcgladald algstperil ligggarsea vrriaptvfg rpvlapppge
      421 yvadgaayqa arlldeevhw steeaapyea paepairhry aaarphvldr sp
//
LOCUS       WP_357686972             323 aa            linear   BCT 28-DEC-2024
DEFINITION  ketopantoate reductase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686972
VERSION     WP_357686972.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 323)
  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 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   3  (residues 1 to 323)
  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 323)
  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 323)
  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..323
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..323
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34714
     Region          1..288
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mryivigaga vggtigarlf qgghevllva rgahyealrs gglrlftpgs aetltipatd
       61 tpvpprdddv lilatksqdt italdpwprh vpvvcaqngv enertvlrrf grvygmcvwl
      121 palhlepgtv aahghprsgm lhigrypqgv delsqqiaad laksgfvala tpdvmrwkyg
      181 kllgnlgnal ealserapgt eslhervrae gtavleeagi pystpreere lrgrqvelmp
      241 iegiergggs swqslarssg sieadylnge ivllgreygi ptpvnevlqa eanrfareql
      301 ppgsmplerl talidersas gsr
//
LOCUS       WP_357686963             513 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357686963
VERSION     WP_357686963.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 513)
  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 513)
  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 513)
  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..513
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..513
                     /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=54861
     Region          131..513
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtsphaalaa tfapgeaavp aamrftrevm tawavggmls iaervagdlt eqvvsepfev
       61 iwkhfgdavq velrqrntsh gdpkapsvgv eewgitysgd srvhwarltl pgsvdrvvse
      121 wqeetskgph wlgfladasd llagtlnpdm vpaiiaqivv prlaswcavy tadtasgplr
      181 laylwhadea ridglrqelt amdvspvdsq vtasmhlgds qvlaipltar grglgmmclg
      241 rsdrfgddvi qfaediarra alamdnarly aqqaaanral qrsllppnep evpgldygvv
      301 yepageanev ggdfydlfka sddswrfaig dvcgtgpeaa avtglarhtl rllaregygv
      361 aavlgrlnqa ileegerarf ltllhgditp vdtglevrlv saghpealrl kpsgvvepvt
      421 tpqsllgvfh evvfesdtvh ldhgdvllav tdgvterrsg hrlldddggl akllaecagl
      481 saravaerir rgvadyasep saddlaivvl rar
//
LOCUS       WP_357686975             198 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357686975
VERSION     WP_357686975.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 198)
  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 198)
  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 198)
  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 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   5  (residues 1 to 198)
  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 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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..198
                     /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=21851
     Region          6..98
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 maatemslmd epdrlrvalt pirrellarl repasavrla aeldlprqrv syhlkvlerq
       61 glievveerp rrgfvervmr atanaflvdp dvlasaadve agfhgiadrh aaehlvevaa
      121 gtvrhvtrma aeadrqgvrl ltftleaevr faepgdvhrf tdelaeavsr vaarydtpgg
      181 rpyrlvaggh paprkepe
//
LOCUS       WP_357687092             346 aa            linear   BCT 28-DEC-2024
DEFINITION  YncE family protein [Micromonospora parva].
ACCESSION   WP_357687092
VERSION     WP_357687092.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 346)
  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 346)
  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..346
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..346
                     /product="YncE family protein"
                     /calculated_mol_wt=35542
     Region          9..>136
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <218..329
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mqirrgftla faaltagllv gavpghaqaa aaptvtplpm ktvgdvvsag drvfvsggrs
       61 stdvvvtsat gavvgtlsgl pgptdlllsa drrtlyvalp naiaafdtgs liesarydtg
      121 agecpsslal tgrylwfgyg cdqwggnigq idlgrqparl tthvaeqdfh dfplltaagq
      181 nrsvllagqp glspasvyay sigtagtltt lrtnawsalg snlrdialdp tgttlytaag
      241 apyevqafpf adistpsaty ptgaypnave vsrdgtriag gadasydpdv fvftpdgtel
      301 arfelgdels pgalawspns arlyavaydw tgvnqatlhv lpvpaa
//
LOCUS       WP_357687099             454 aa            linear   BCT 28-DEC-2024
DEFINITION  sialidase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687099
VERSION     WP_357687099.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 454)
  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 454)
  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 454)
  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 454)
  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 454)
  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 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]
REFERENCE   7  (residues 1 to 454)
  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 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..454
                     /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=47682
     Region          <146..>235
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mtvvavivll lndhllkqah pgfvtgklsd faglivappl lalllwrrad laatlltgal
       61 ftlvkttetg aetashlwtl vagpsrvlad ptdllalpal glawwvrrrs lradsgrwra
      121 lvttplavla vaatsaaspp psadsvqadd rrivvhldda yesdtgvrgl vsedggvtws
      181 ewylrrdrpp qsaacvprqa qrcyhvldgr avaesddggt twheswkpaa drpdpeagqr
      241 pddrprpral avqarsgghv vvvangvdgi lvrdvsgawr qagwpqfvsg vvppepmdpv
      301 reerriafff aitvllgamg vglrqlrtpy tifamvglgg llytvleald dgpgfapgkl
      361 llggsvtlig ilmcvvlaaa grtrptaalv glgaaplvyg svygpfhgwt qgvpdsygva
      421 vaaavvltag vvaaggalir rdaylagsst srpt
//
LOCUS       WP_357687113             240 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687113
VERSION     WP_357687113.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 240)
  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 240)
  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..240
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..240
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25458
     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 msdtavivpa kdeadrigat vtaalalpgv dlvvvvddgs tdqtgkvara agarvvrhsr
       61 nrgkaaames gaeavrlldg dvprhlvfld adlgetagaa aaliepvreg radmtvavfa
      121 trvklgghgm vvrlsrdgir ratgfaatqp lngqrcltrd afeaarplah gfgvetglti
      181 dllrkgyrvv evevemshra tgtdwraqlh rarqlrdval alaarepvit qnlnklrpkr
//
LOCUS       WP_357687117             371 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687117
VERSION     WP_357687117.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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..371
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..371
                     /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=38372
     Region          130..365
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 msatvvndlg vivavtaglg llvallgvgv mwrlrtrsia mmlgvvmvvs ivatlagvva
       61 itlkmiidgs vrdivlsvvv vgglvglgva fvlarrvvge srrlvaavrd lpfvaprglp
      121 aelqtiantl qeanareral egarrelvaw vshdlrtpla gmramaeale dgvvadpetv
      181 gryhaqikle verlsamvdd lfelsrihag alrlsrtrig ladlvadtla gaeplarakg
      241 vrltadatea vpveadagal gralgnlvvn airhtpsdrt vvlraavdag maclsvsdsc
      301 ggipdddlsr vfdvafrgea artptkdgga glglaiaqgi veahdgmidv vndgpgcrfe
      361 irlplvggpv g
//
LOCUS       WP_357687143             292 aa            linear   BCT 28-DEC-2024
DEFINITION  Fpg/Nei family DNA glycosylase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687143
VERSION     WP_357687143.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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..292
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..292
                     /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=31192
     Region          2..276
                     /region_name="Nei"
                     /note="Formamidopyrimidine-DNA glycosylase [Replication,
                     recombination and repair]; COG0266"
                     /db_xref="CDD:440036"
ORIGIN      
        1 mpelpevesl agflreqavg rtilgvdvva fqalktfdpp vsalggltvt gvsrhgkfld
       61 ldcdglhlvf hlaragwlrw rddlsgakpv rrgkgplavr vrlapddegl apgfelteag
      121 tqkrlavyvt knpdevpgva algpdpldes ftvatlqgiv ggnrtqikgl lrdqkiiagi
      181 gnaysdevlh aarmspfkia atlteaqvad lyeaivstlr daverahgla akdlkaekks
      241 glrvhnrtgq pcdvcgdtir evsfadsslq ycptcqtggk pladrrlsrl lk
//
LOCUS       WP_357687145             201 aa            linear   BCT 28-DEC-2024
DEFINITION  TenA family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687145
VERSION     WP_357687145.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..201
                     /product="TenA family protein"
                     /calculated_mol_wt=21915
     Region          1..199
                     /region_name="TenA"
                     /note="Aminopyrimidine aminohydrolase TenA (thiamine
                     salvage pathway) [Coenzyme transport and metabolism];
                     COG0819"
                     /db_xref="CDD:440581"
ORIGIN      
        1 msiaerlhav grplldaqla hptvvgigrg dlpepvfrsw leqdylflhd yvrvfarlaw
       61 qapaahlgdl vdlahatfhd eldlhrslsa gfgadlegar kgpacaayts fllesaadyg
      121 dglaalypcm wgystlgril aenppaepry rawvdtyadp gfaalarrig emideadpdp
      181 araealfveg mahelafwdv p
//
LOCUS       WP_357687244             139 aa            linear   BCT 28-DEC-2024
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Micromonospora
            parva].
ACCESSION   WP_357687244
VERSION     WP_357687244.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 139)
  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..139
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..139
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14636
     Region          5..121
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 metstfvydg dcafctscaq fierriptsa rvvpwqfadl galgltvaec eeavqwvgad
       61 garaagpdai akllaasgpl wrvagaglri ppvraaawpl yrwvarnrhr lpggtaacsl
      121 pqearerlyg pagrpstga
//
LOCUS       WP_357687250             318 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Micromonospora
            parva].
ACCESSION   WP_357687250
VERSION     WP_357687250.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..318
                     /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=34140
     Region          6..307
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 maavgrprrs clavpgssvk mlgkaqglpa dqvfldleda vaplakpdar knivaalneg
       61 dwagktrvvr vndlttpwty rdvievvega ganldcimlp kvqtaeqvhw ldllltqiek
      121 tlglevgrig ieaqienaag lvnvdaiaga sprvetiifg padfmasinm kslvvgalip
      181 dypgdpyhyi lmrilmaarm hdkqaidgpf lqirdvdgfr evakrsaalg fdgkwvlhpg
      241 qidaanevyq paqadydhae lildayehyt seaggklgav mlgdemidea srkmalvvaa
      301 kgraagmsrt ssftppqq
//
LOCUS       WP_357687278             375 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687278
VERSION     WP_357687278.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 375)
  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..375
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=39151
     Region          <176..374
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstgrsgvpa gvkdwaiavc vaaallvtgl sgpnsatnld llgyallaag glalaarrra
       61 pvpvlavtgl cavgyqaagf dvpavaylfa vyaavraghr tvtvaasvtm laalpfaalv
      121 sglhntgeaf aqargaleia wlvaagaage alrqaerrae eaertreeta rrradeerlh
      181 iarelhdslt hqisiikvqa evavhvarrr geqvpealla iqeagreatr elratlqalr
      241 dddttpprgl dhvpelvera rsvgldatlt iegqrhdvpa avsrtayriv qesltniarh
      301 aaaatasvqi dvrpdalair vdddgkatpg tapvpgvgll gmrervtalg grlraeprgd
      361 ggftvqaelp vdqts
//
LOCUS       WP_357687315             314 aa            linear   BCT 28-DEC-2024
DEFINITION  ketopantoate reductase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687315
VERSION     WP_357687315.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 314)
  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 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   3  (residues 1 to 314)
  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 314)
  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 314)
  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..314
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..314
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31810
     Region          5..311
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mtagrigvlg aggmgsafaa flaraghdvv ligrggehar aiadrglvvr ppgetswsvg
       61 ldvalhaadl ppasldavvi ltktydtspa arsvvpalap ggvavslqng lglasrlaav
      121 fgeerslvga ttvgaallsp grisisgata tgetftcmge mdearggrra aglvgalnaa
      181 glpathtpqv seqiwrklal avmspvssvl rltvgqvwat aegrslvrqm fdevvavasa
      241 qrvildpdda wahasrvfeg tgehytsmca dvmngretel ssmagavhrl aaergvpapa
      301 hgfvlgmlga lgvr
//
LOCUS       WP_357687320             487 aa            linear   BCT 28-DEC-2024
DEFINITION  multicopper oxidase family protein [Micromonospora parva].
ACCESSION   WP_357687320
VERSION     WP_357687320.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 487)
  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 487)
  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 487)
  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 487)
  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..487
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..487
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=52758
     Region          61..487
                     /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 mvsrrnvmka gatagaaalv tttaaaaarg stppatpahd ahtghrgtah vaaaaapftv
       61 rmpippvrqp iasvgntdfy vvstrkaqae ilpgtrtevl tydglfpgpt frvrtgrlav
      121 iahsnhldmp tavhvhggqt psssdgfptd vldpgrsriy sypnkqraat lwyhdhahhm
      181 eaehvfrgla gffliddpaq adlrlpsgny dvpimlrdar faddaslife hddfqfrnti
      241 langkpqpyf qvaarkyrlr fvnasnlrtf tlrlgndaev tqiasdggll agptpirsws
      301 ltpgerieiv vdfgafpvgs qvflddavag pvlrfdvnrt atdtsrvpdr lstipalpaa
      361 tkeraftlnl npatgqflin gqqfdadrvd teikrnttev wtvtngdtlf giphnfhphl
      421 vqfrvlsrng qppapgeagl kdtisvgpge tvrlqatfgp ylgryvyhch midhsasgmm
      481 aqmkivp
//
LOCUS       WP_357687355             843 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357687355
VERSION     WP_357687355.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..843
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..843
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=88733
     Region          <10..841
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 midggedktr gggsptpvrp erlrgpvefv grtaelarlr rlvatppcli llegepgigk
       61 srlvaellae lpgrhlvgec ddvpepfplg vlldairgnt erpgplspva galapllpel
      121 advlpdappp ltdpaaerhr lfravaavla alspatllle dlhwadpatc ellaylsthp
      181 vdglavllta rtatpgsstp ihdalartpp wsvtrvalsp ldaddvrrla artlrlddpp
      241 qqltaalldr tagipfvvee vlrtlaergg dpladdsvpf vlrdvllwrl rpldeatrev
      301 lgaaavlgmt pdqrilaavl sldrvaigaa ltaahragll hdagdglrfr hdlarqvvyd
      361 llpresrewl hlrvarvleq elprpvaqla hhyrragsga dfvrnaeaaa dlatergdda
      421 taasfllqtm dvaelprpvr vrlaaklgrs aidglsqaea ipvlerllad rrlppgarge
      481 lglvlgrmlr qqgealrgyt eieravpylr aprrkapala vlaapdtvvg rhvddhlarc
      541 teaeaaaaas gdpgshlavr iaraslllel gdpaawaiit elrasielad rpreharacl
      601 nwaqgalhag hpaqaealla agralvdetg yerlaslvea tqlsldratg rldglaerlg
      661 rlvasaermp vtlldarael atvlaltatt anagstnaaa anatatnagt anagtaaglg
      721 drtggldvve aaeralrevv adarrvgaiw plvqalsala rltvtrqpde avrhateals
      781 vvrgkgilaw aadavlvlae aaaaqgepar aaaavaelea giagrdtpla raalrrcrel
      841 vpa
//
LOCUS       WP_357687339             253 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357687339
VERSION     WP_357687339.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25807
     Region          1..248
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mkdirgtsil vtgggsgiga gvartlverg arvtisgrre hrirevaael gpaclavpgd
       61 vtlaadrerl laaaiehgdg ldtlvnaagn myrgalaeld earmldlyhs nvvgpvqlsg
      121 lalpalresk gsiiffgsvh tqrafpgasp yaatkgales ltgvlaselg sqgvrvncvr
      181 pgavfteine raglgtseea harlqglaga halgrigtte evaeavvyla caewvtgsil
      241 tvdgglalgv tha
//
LOCUS       WP_357687384              88 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357687384
VERSION     WP_357687384.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9519
     Region          10..78
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mppaenpeha ievhldrlle ergmtvvela dkvgitnvnl silknnraka irfstlskic
       61 evlgcqpgdl lsftprstva aqaeirdp
//
LOCUS       WP_357687383             401 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Micromonospora parva].
ACCESSION   WP_357687383
VERSION     WP_357687383.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..401
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41893
     Region          32..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 mttswpspgg sapaddpgaa ghhgprpaad ggplagvrvv elaslapapf gcmvladlga
       61 dvvrvdrpga pgagrlaapt ggplqrgrrv taldlksptg vadlltlver advlveayrp
      121 gvaerlgfgp qvcqarnprl vyarmtgwgq dgplaaragh didyiavaga leplgrager
      181 pyapmnllgd fggggmllav gvlaallere rsgfgqvvda amvdgsallt sflhgllgtg
      241 lwaaprghnm fdggapfydt yatadggfma vgamepafya vlltgldlad dpdlpaqydp
      301 sgwdelrrrf tarfaertrd ewtaifadld acvapvlapg eahqhphnaa rgtfvevdge
      361 iqpapaprfd rtppkrptpa pdphrdamrv eeiltgwphr t
//
LOCUS       WP_357687399             217 aa            linear   BCT 28-DEC-2024
DEFINITION  dienelactone hydrolase family protein [Micromonospora parva].
ACCESSION   WP_357687399
VERSION     WP_357687399.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 217)
  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   2  (residues 1 to 217)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..217
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22218
     Region          1..211
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mdeqrstvmv pigeaqlpad ltlpaqpvgv vlfahgsgss rhsprnvsva rtlndsglat
       61 vlvdlltpve devdartael rfdigllasr lagivdwlat grpagdvptg lfgastgaaa
      121 alvaaasrad rvaavvsrgg rpdlagdala qvraptlllv ggldeevial neqalaelgd
      181 vgelrvipga thlfeepgtl eqvadqagaw ftthlsr
//
LOCUS       WP_357687413             149 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687413
VERSION     WP_357687413.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 149)
  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 149)
  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 149)
  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 149)
  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..149
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..149
                     /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=16855
     Region          2..147
                     /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 mlrdtadddv arlreiaeap dvakwwgpvd efddmlaitl dgevigaiqy eeiddpmyrs
       61 agidiflgpa whgrgygqea irvlarwlig erghhrltid paahnevair ayervgfrrv
      121 gimrayerdp vtkrfhdgll mdlladevn
//
LOCUS       WP_357687417             218 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687417
VERSION     WP_357687417.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 218)
  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 218)
  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 218)
  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 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   5  (residues 1 to 218)
  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 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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..218
                     /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=24350
     Region          15..99
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkailhieye ylghmtqere slndpkamra lahparlail nrlsvggsat atevaeiagi
       61 tpsaasyhlr mlakygfved apargdgrer lwkatdkplm igvlpddrpe vreakdlliq
      121 afrreaeeea qraltgydqe sqewrdvirf nrtllrvdaa emarlneeie kllqpyiary
      181 rsaeaapsga riaeaqvnlf phverivpgl ptedhdag
//
LOCUS       WP_357687453             359 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687453
VERSION     WP_357687453.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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..359
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..359
                     /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=37891
     Region          1..>221
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkialvgcga vtqavyvpll srrrdlfevt avcdlsrtla davgdrlgap grytaldrml
       61 adggfeavvm lasgshgeav rqalaagysv lcekplaltr aevaalpegr lmvgymkqyd
      121 pavrraeevl aelggaavvr svevsvlhps gesqlafanl tqardvdpdl laslraaedg
      181 lvsralgeaa pasvralygv algsichdls llrrftgspa eishvetwgp apgsieisgp
      241 lpvagrfair whyledypay retvtihhds gslelvfpap ylmnapttlt vvspgesrte
      301 wrdvteafev qlaafhayvn dgkppltdaa ggledivtaq rvaaryavqh glpiggeaa
//
LOCUS       WP_357687462             504 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357687462
VERSION     WP_357687462.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..504
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..504
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53091
     Region          2..466
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msnniteiet ygidripdad raarpfdlfr vafggantfa tcvlgafpil fglsfwqgla
       61 atvlglvvga lilaplalfg plngtnnavs ssahlgvhgr ivgsflsmlt aiaffsisvw
      121 ssgdalvgga hrtvglpatd fsygvayalf aglvlvvcvy gfrfmlfvnk iavvaaslmf
      181 vlgafafagd fdpaypgmla dgdplfwpsf igaalivlsn pvsfgaflgd wsryipastp
      241 rskvmaaafm sqiatilpff fglatasiia vkaaehmdpa apnyvggllt iaptwyfvpv
      301 clialiggms tgttslygtg ldfsslfpgf trvratvfvg tlsivfifig rfaanltqsi
      361 stfatliitc tapwmvimml gyvtrrgwyd pdalqvfnrr qrggrywfth gwngrgltaw
      421 ivsagmalmf vnlpgqfvgp lgdlaggvdi slpvglgvaa vlyltllavf peprevhgpa
      481 gprlvraadt pvppivavat epav
//
LOCUS       WP_357687477             236 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Micromonospora parva].
ACCESSION   WP_357687477
VERSION     WP_357687477.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 236)
  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..236
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..236
                     /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=24668
     Region          1..>60
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtrcefaydd gayvlgalap aeraayerhl ggcascreav aeiavlpgll grldpagleq
       61 ilpppapprv pallaearqr rrrerradrr ryalttlaaa glalvvgvgt aavlprpvap
      121 spqaqgtpgp qvsmvsmrpv aaagpvhadi glvgtkwgtq vtmrcgydar tsygkaypfr
      181 lvargpngat eqigswlaap gddlsftgat rftdaeltsv elqkadgtpl ltyavp
//
LOCUS       WP_357687504             416 aa            linear   BCT 28-DEC-2024
DEFINITION  HNH endonuclease signature motif containing protein [Micromonospora
            parva].
ACCESSION   WP_357687504
VERSION     WP_357687504.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..416
                     /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=44652
     Region          41..333
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          325..379
                     /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(349,351..353,355,366..367,371..372,375,379)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mlealaqvsg avddcaetal walsdddlla sldatqvlgq rlaavqlglv reldgrgvav
       61 aqgasstavw lrerlrlsgr sarqlvqlaa tidaappavr dallggamtv eqgrvvaeti
      121 aalpveagpe eadkatqllv awadrfdpts lsrlgervla hvapeladqa elkalerate
      181 raearrhvtl seqqngqvrl sgnldtetas llreaidplc apagkhddrs pgqrradalg
      241 eicrlalrtg qlpdnggdrp qlvvtvslee lvngvragtl etgthltpga vrrlacdagv
      301 lpvvldgnsq vldvgrqrrl ftgplrralv lrdggcafpg cdrpprwcdg hhirhwvdgg
      361 vttlgnavll cgyhhrlihr gdwavrlaad grpeflppsw ldplrtprrn hyhlrc
//
LOCUS       WP_357687522             464 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687522
VERSION     WP_357687522.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..464
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..464
                     /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=52319
     Region          33..407
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mdplkalada erkpywldsp arpeprprld getdadlvvv gggfsglwta lmakerdpsq
       61 dvvllegrri gwaasgrngg fcmatlthgl pnglerwpde ldrlermgvq nldeiertle
      121 rygvdcsfer tgelnvatep wqlealhehl dviaelgldy vpldreqira eidsptylgg
      181 fwdrrgcamv dparlawglr evclrlgvrv yerspvrsma ddgstirlrt phgvatgrrv
      241 alatgvfppl lrrlkhflvp vydyalmtep lsreqlaevg wrnrqgvgds anqfhyyrlt
      301 dddrilwggy davyyngglv kpeydqrdet fvklaehfat tfpqlaevrf thrwggvidt
      361 csrfsafygq ahggrlayav gytgmgvgat rfganvmldl lsgerterte lrmvkekpvp
      421 fppepvrsgv iqltrwsiaq adrhqgrrnl wlrtldrmgl gfds
//
LOCUS       WP_357687590             871 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357687590
VERSION     WP_357687590.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 871)
  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 871)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 871)
  AUTHORS   Rosinski,J.A. 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 871)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..871
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..871
                     /product="helix-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=93686
     Region          <2..834
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          808..862
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrsqfeqssa gagrvvmvsg gvasgkttll ndlldeataa gavtlsatga pdeqriesai
       61 idqllansst pvtgaakpyt alglcdtlqg larerptvic vdgihyadet svrillqlqr
      121 rirsvkllmv lsrpewprgs pagfdlqhrc ygvrlaplpe qtiaamldaa ghnhsglaar
      181 lhalsggnpm fakaavddhl eglghdgrav agpayaqavw aflhrsedhl ldvatalavl
      241 gecgdaelia kltgidadav vdvlavleqg gllaggwfrh pdaptavlrn lptterirlh
      301 raaaelkyre aaaatevasn lvsagetsae wslpilrraa eralmaddia fatrclelgl
      361 saasdeaeqr sihlsivrst wrvnpsgvlp hisalaaaad qgeldqagcl allrhalwhg
      421 drqnalrahe llhtgpgpid pqidtavkla fhwhfgqdlp qvkssdfath pgaapwnhta
      481 hsltqtwrqg ssdttkasae rvlrnsrlgd ttleaiamai salahggncd raqwwcgrla
      541 kearqrgats wqamiealra avvlqrgevt kaaelarsal dmlsepnwgv sishplttll
      601 madiaagtfa saaetlrrpv pdamletvgg lwflracghf ylatkrplaa igyfhkvqrl
      661 mrtreesmpl lvpwrsdlae atlrlgnrti ardlanqqie lahssnpfah glalralala
      721 gtpaegsrsl leraaksfqq aghqlelnrt lkviaqlqnp ererlnglaa daieaprpvp
      781 asrlmvaqda rpepvaredg rseraesvtl seaelrvaql aalghtnrqi srrlfitist
      841 veqhltrtyr kldirgrsal ahelgyaris i
//
LOCUS       WP_357687597             511 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaF family protein [Micromonospora parva].
ACCESSION   WP_357687597
VERSION     WP_357687597.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 511)
  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 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..511
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56311
     Region          84..483
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mrfepvstdp rqqppgvtst applavpngr hhqsvpqpmp avtpppeppn rprmdfqvvr
       61 elrrelterl tlwqrgreft vdeedterar lavtvvaaya dsvrragtpm aaseerllld
      121 qvtaelvglg rlqtllvddt ieevhilgcd qvritrhggg vdwaepiads daelveilqa
      181 aarragater slstvkptld lqlpdgsrla avflvshrpy avirkhntld vslddlagar
      241 ndldemidpl lrdflraamr aglnimvagl agagkttvir almneipqde pyvlleesre
      301 llparrrerh ravmsfeare ghgergfdgr pagevtiadl iplslrmgvl riivgevrsr
      361 eivpmlqamt tsrgsmctih artaagvger ivelalahgr emtvdqarrm agnaldlivy
      421 vtvedetaig grkhrfvshv eevigageag rittttvfgp gpdgravprh lpervrdqll
      481 rvgydarllt rwveagagaw rrprqtrlar r
//
LOCUS       WP_357687611             318 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357687611
VERSION     WP_357687611.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..318
                     /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=35197
     Region          21..318
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 maitavpetp rkpgrppspy sarpqrtslg rkvrdnltgh afligavlcf vvfswypmvr
       61 givmsfqrtr rgettwvgwd nytriiadps fwpawkntly ftglalvlgy avpffvaill
      121 nefrhgkgyl rilvylpvml ppasalflfk fyaydpseag lfnailralh lptsqwmqsp
      181 emtmpamvva stwmnmggav liylaslqni pgelyeaael dgagiwrrir hvtipqtrli
      241 lalmamlqiv atmqlfiepl ilangagaed satsvayliy qhgffqndln gaaalgviml
      301 valagfsavy vrltakqd
//
LOCUS       WP_357687675             214 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357687675
VERSION     WP_357687675.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 214)
  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..214
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..214
                     /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=23018
     Region          13..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msptsgktlg grraqaarnd evileaarav flddpkapia avadragvgi salyrryagk
       61 egllrqlchd glrryvaeae aalaepddwa aftgflgriv dadvhsltvh lagtftptee
      121 mgrdavrage lasalvdrar aserlrpdav vqdlglllea caavrvpdpe rtrqlrrrql
      181 avllaglstv pdadplpgpp paagefdwrw rrre
//
LOCUS       WP_357687677             381 aa            linear   BCT 28-DEC-2024
DEFINITION  epoxide hydrolase family protein [Micromonospora parva].
ACCESSION   WP_357687677
VERSION     WP_357687677.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 381)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (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   5  (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 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..381
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41875
     Region          6..111
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          70..>219
                     /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 msdtairpfr veipqtaldd laarlgrtiw padlpgagda ygmstervra lvdrwrdefd
       61 wravearlna hpqfvteidg erihflhvrs srpdatalvl thgwpgsvle yldviaplte
      121 ptdpdapafh vvipslpgfg fsgptrnagw nrfriarawa elmnrlgyds ygavgndags
      181 miapelgrid pervlgvhvt qlfsfpsgdp aefaglsead qaalghlqwf yenkfsfnqv
      241 hsqqpqtlaf gladspvgll awnaqlfdes ldadftlanv alywftgtaa sairlyweda
      301 hageppagpt ttptalvmfp gdfqsirrfa erdhanivrw taydtdvdgr gdvgghyaah
      361 qatkvlvtdi seffaslrqp n
//
LOCUS       WP_357687701             500 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687701
VERSION     WP_357687701.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 500)
  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 500)
  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..500
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..500
                     /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=54738
     Region          111..>209
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkrillpagg ailatgllaa glagtaqaqs dvasdplakt eaqaaetldf wsksnyaalk
       61 kavafnpdal evkkiksggg yssdtkpgss apigeekkaa vktqnvnlpk tigkvffewk
      121 dgnlywcsgt siqsqyrnlv ataghcvydi agndevvskw vfvpgyyqgk apwglyigkq
      181 afthydldvy edfdrdyafv tvyngiggtl nkpkqvtkae fdaykgekfa kdvevsrdef
      241 rkgrldpkta eyywrqpgvp sevvgpdypg aevskkevtk evydaakvgk gtgfkfgepv
      301 teqvtkteyd aykglgtkse dkrgnyfits yyvqewfkpg tdkkffrtdf fivvhevkdv
      361 grlgdnvggq gvawnqpggk yvrtfgypag phpdgnkpyt gvtpkwcygk tnknvlqvps
      421 rkveehqsfr cavtagydgg pwlykysnak rlgyvtgvts livdtdgnsr ydtitsphfd
      481 getaaiykaa aaswsgklip
//
LOCUS       WP_357687744             883 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357687744
VERSION     WP_357687744.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 883)
  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..883
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..883
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93107
     Region          9..880
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtpdhdwsrs pagrttlpel lrghrraagl tqaelasrag vgvrtvrdle rgrsirpqrt
       61 tvellagala ltgatraafl aaargvgaep appdvtsttf avsgnaasaa pagpsvalpp
      121 pvaligrdrd ltelaamlta ergprlvslv glagvgktal atsvahlvas ahpggvagvl
      181 vgegsdgpdv laasmsvlgv arlselvarl agrpallvmd avehapgpva atlhrltgal
      241 pslrvlvtgr hpvglpgerv wpvapldvpp peaehagles wpavalfttr laqvrreppt
      301 qdelpalaal vrrlgglpla ielmaargrl ldltelldry gdrvldlatp adasthagwd
      361 apegltgrts gpdngaagav avtlrdavaf syrllasder aalrqlavfg nrwsvelaee
      421 mladeadrdg tvaidpvpll drfvelglls vrgtgsfrfr lldavrdyav eqaagegelt
      481 cirrrhaevi arlvartasd lvgprlpdav hrldemssdi ssslahaatd dpltalrlaa
      541 cltrwwrfrg rdvvgrqwlr rlladprtgd adpllrgwaa lgvarlaaeh gagaeelsta
      601 raaldtfrqa gdvtgelear nvlgtllisv grqeeareqa etllrlaarn grtrdlavaq
      661 nslawheira gdlaaarrrl aavdrltves geqrlrvlgw anraevarle gwyadavdrg
      721 qraiealsel gdpgrrrrvl gtvglalaqd grvaeatevl aelragsves vparptvprq
      781 rsgdatltwg gpeaglcali egnlalhrgd relaaewfaa aadnagqdrr dvvealvgla
      841 astadptvld rldrvcvetg irllpqesgl lyalvadrdg ptr
//
LOCUS       WP_357687768             166 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357687768
VERSION     WP_357687768.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 166)
  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 166)
  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..166
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..166
                     /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=17588
     Region          9..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mserpdgvdp laleqqvcfa lsvaarsvva vyrpllepmg lthpqylvml alwqhaplsg
       61 rdlsrllqld pgtlspllkr leaagylrre rdpsdersla vtltasgaal rsqaelipaa
      121 ivarlglpve dlqhlhavlt rligaanrpa aaepgtepdv aaqasa
//
LOCUS       WP_357687771             226 aa            linear   BCT 28-DEC-2024
DEFINITION  orotate phosphoribosyltransferase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687771
VERSION     WP_357687771.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 226)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..226
                     /product="orotate phosphoribosyltransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004588 - orotate
                     phosphoribosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0046132 - pyrimidine ribonucleoside
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=23684
     Region          76..>199
                     /region_name="PyrE"
                     /note="Orotate phosphoribosyltransferase [Nucleotide
                     transport and metabolism]; COG0461"
                     /db_xref="CDD:440229"
ORIGIN      
        1 mtttpasqga ttdspttdlr tadfpmadlr tadlraadfw svlardemra fqtdeerrae
       61 lladvvaaaw gsdgqfvdad qfltkptvlr rlasiladrv psdadrligr ephslvlgta
      121 laletglplv variagsptg kelvcsgelh pgervlvveg vtgtgasavq avrlarrrga
      181 tvvgvlaavd rdagaaarlg glavmldnlf ddvelraaas rgresr
//
LOCUS       WP_357687699             494 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687699
VERSION     WP_357687699.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 494)
  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 494)
  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..494
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..494
                     /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=53922
     Region          106..>197
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
     Region          <313..455
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkrllvplaa lglsaatlsl paaatptwis dplapkaada ysnasfwlda ngaalrkatq
       61 yrldakdvpk lvrpqtqtgd gkpgmtaptg akpvatkvkn vnlpktigkv ffldrkgdyr
      121 wcsatsiqsr hrnlvatagh cvyehgedvf akwvfvpgyy qgkapygvya gayaftaydl
      181 dtyddydgdf afvavhngfr lagekkvtfr efkawqgdkw vkpheitaae yakcqldlge
      241 cwsegkdtpa dkvgpdypga vlekeevdgk tykdaktgkg ngfklgepvt vpitkaehda
      301 ykglgtkgdd krgnysltty yvqkwvkpgt srkyympeyv iglakdagrl gdvvggqgia
      361 wnqpmnqqvm vfgypsaphp dgdrpytgtt pkwcsgktgt ktyqvnmfkv ethqvlkcsm
      421 tggadggpwl lkydnnkrtg yvngvtslfh dqdgndridf issayfdgev advynkanya
      481 etksvvgpng elpn
//
LOCUS       WP_357687802             185 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687802
VERSION     WP_357687802.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..185
                     /product="YybH family protein"
                     /calculated_mol_wt=21245
     Region          1..146
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtnqasdeeq ilrlhrdwyy snfniniplm rtvfpvgden flmfnlndhp yfgvddlanl
       61 wsfyartdrw glcedyvvrv dvagdmgyvv segvypswvv rddegnplpe eipvvfnyrs
      121 teiykrddge graewrmwhf hcstrpadde apaaktekds aavrglgntp ystgartdys
      181 eytas
//
LOCUS       WP_357687807             845 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora parva].
ACCESSION   WP_357687807
VERSION     WP_357687807.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 845)
  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 845)
  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 845)
  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 845)
  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..845
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..845
                     /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=90109
     Region          150..805
                     /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 mpsqaqsdqe dhqrltliig vivvaasvvc alslmamlar ppatvtevat vvaliamiav
       61 atmvkarvri rstthsitwn etaivvgvav apapwvvlct aigvavafav lrlpaikmaf
      121 sigkntlvaa gagltlvsld wvwppdtftd fadliapial aylaatllde iiaipviaia
      181 sgssirqqfr tnwdlrgvgv alrflvtict llllqadlrl lvavpplvls lhlaystrir
      241 srteqqawqr larttdalnv vdldevltta vtqaaelfsa devemelreg grtvrggtgg
      301 itfdgptgtp tdvdgtiipa pleghdrtvd vgvlrlrfrg pvqlsereqy tlrtfasalc
      361 tavrnaqaya elarvadeha yaashdaltg lanrrqllde gteqlstrha dgvtalvlid
      421 lnhfkevndt lghaagdqvl vqvadrlrga apasdlvarl ggdefavllr glpapavaah
      481 raetllaalh epfeldgmri sveasggisg apsnggmael lrradvamyq akragqriat
      541 yaptrdtadl grltlggdlp ravadhefvv nfqpivdlgt gevtsaeala rwhhpvhgli
      601 dplrfleave rsgllpafae aildqaliaa vswhdagfdv pvavnvsprs lldarfpgsv
      661 larlrahdlp pdrlvlelte tltlsqldvv drvlsrlrde gvrlalddfg tgysslslls
      721 ripvhelkid rsfvttmess aeaaavirst ldlgrsldld vvaegvesep qrralwelgc
      781 vagqghlfar pmpsgtllaa mqrgsggrpg tlaaplhdag avirlsqnrr qtgrsrpdrl
      841 phlpa
//
LOCUS       WP_357687827             286 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357687827
VERSION     WP_357687827.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..286
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..286
                     /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=29459
     Region          6..280
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mslagalprs ylfvpgdapg klakalgrga dalivdleda vppegkeear savvawlrsg
       61 letggaqlwv rvnsghlrva dvrelagipa ltglvlakae daaevatvae llsaagdddt
      121 llmplletag sildareiar aprvhrlqig evdltadagl lpgpdeaela wprgmvvlas
      181 aaagidppvg pvsrltgdpe altlstervr rqgfvgraci hpaqlpivhq vftpsdeeia
      241 earevlaafe rataagsgvv ldsqglmlda avirlarrtl gtvsag
//
LOCUS       WP_357687841             413 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357687841
VERSION     WP_357687841.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..413
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44798
     Region          1..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 mkpledvrii aveqygagpf gsvhladlga evikiedpra ggdvgryvpp ygeeedslff
       61 etfnrnkrsl sldlstpagr rvfedlvkvs dvvysnlrgd vpkkigityd dlkhlnpaiv
      121 ccsltgfgmt gprskepgyd yilqglagwm dltgepdgpp tksglslvdy sggfvaaial
      181 laglhaarrd gvgmdcdvsl ydtalgllty patwhlnagf tpvrtrhsah pslvpfqafe
      241 asdgwlvvgc akekfwarla kvvghpewae pgsrfgtfad rqrnsaellp lleeifgrrt
      301 vtewlevlya aaipcgpind vaqameeeht karglrvtte hprfgtveqi aspvrvgdqp
      361 asyrraplrn edfelvvrdi agydeatvge ltaqgafgdp ekvpglqaea sar
//
LOCUS       WP_357687879             416 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687879
VERSION     WP_357687879.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Paget,M.S.
  TITLE     Bacterial Sigma Factors and Anti-Sigma Factors: Structure, Function
            and Distribution
  JOURNAL   Biomolecules 5 (3), 1245-1265 (2015)
   PUBMED   26131973
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..416
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45125
     Region          2..412
                     /region_name="COG4941"
                     /note="Predicted RNA polymerase sigma factor, contains
                     C-terminal TPR domain [Transcription]"
                     /db_xref="CDD:443968"
ORIGIN      
        1 miapdledll rdqapqvlga lvrryghfdt sedavqealv aasvqwpkdg ipdnprawli
       61 tvasrrltdl lraeqarlrr edtvarwtlp gerlapaadg papesddtli llfmcchpal
      121 spasqialtl ravgglttse iaraflvpep tmarrvsrak krvkdsgipf rlpsgperag
      181 rlgavlhvly lifnegyast sgpslhrtel saeairltrv vhrllpgdpe vagllalmll
      241 tdarrpartg pdgelvpmae qdrrlwnadh iaegvalvtd alprgtpgpy rlqaaiaavh
      301 deapsaeatd wpqimalyev lmriagnpvv alnhtvavam vrgpragldr laeleaderi
      361 aedhrlhavr ahllemagdh akaresyeaa agrttnvrqq rylraraahl apdagp
//
LOCUS       WP_357687895             231 aa            linear   BCT 28-DEC-2024
DEFINITION  RICIN domain-containing protein [Micromonospora parva].
ACCESSION   WP_357687895
VERSION     WP_357687895.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..231
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24318
     Region          115..>193
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
     Site            order(157..158,168,170,177,179)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
ORIGIN      
        1 madprddlta ivdevrrvat lpgaqalrqr sdrrrrrraa vgaaglavva vaagtalsqi
       61 rndvetpdag pagqvappvv psatasagpq eilggrrqvq itlpgmrgat laidsdgdqv
      121 rattdqgidd ralwvlrpeg dryrillasg atevcmtvvh dtapgsvrgr acdaaastql
      181 fridqvpdgs ysifqgrryv qvvdgtnalv pdlpeglttt yefedrgpap r
//
LOCUS       WP_357687941             359 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357687941
VERSION     WP_357687941.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=36438
     Region          35..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 marptgpapv arpaglrkrw lvaglfavlv alvagvslgp vslppgsvaa ellnlvpgvh
       61 ldsglterei aivtelrlpr vvlgllvggl lalaggcyqg vfrnpladpy llgvaagagl
      121 avtaaialgg ggrqgtlsgl pltiplaafa gsllavtmty vlgaaggrrg spamlilagv
      181 avsaflsagq tyllqrnads iqpvyswllg rlatagwhdv llvlpyaalt tvvvllhrre
      241 ldvlavgdde arslglhpqr trylliaaas lgtaaavsat gligfvgiiv phtvrllags
      301 syrvilpmsl lfggaflalt dvvartaaap sevpigvvta llggpffvlv lrtarrvlt
//
LOCUS       WP_357687949             225 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Micromonospora parva].
ACCESSION   WP_357687949
VERSION     WP_357687949.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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..225
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..225
                     /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=23019
     Region          17..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 mrlaalryav ppglpsrpgc dacgapvglt rpwpalgpaa rcrhcrarvg pppgtveaav
       61 laavlllafg gpsdgalpal iwwlgwtipa ilvdlavhrl pdrltlpaaa gtwlllgvaa
      121 ldadpghwlr avtggtglal ffastavllg rrgfglgdak lalsvgallg wygwpvllfg
      181 mlltfglsav vslgllatrr anwsshlpfg pflllgtvga vllaa
//
LOCUS       WP_357687956             175 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357687956
VERSION     WP_357687956.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 175)
  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..175
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..175
                     /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=19026
     Region          7..175
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkrtdadacv larvadgdta alaelyerya eplfaflfrl agdrgtaeei lqdtmlavwr
       61 sagtfqrrss astwlfgvar rqahnrlrla appaaaelye qadalpgpee lavggdwlda
      121 vlaglpptqr evavlhfvvd lahqdiaevl ripvgtvksr lhlartklre slngq
//
LOCUS       WP_357688074             340 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase enzyme family protein [Micromonospora parva].
ACCESSION   WP_357688074
VERSION     WP_357688074.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 340)
  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..340
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..340
                     /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=36126
     Region          15..289
                     /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 maqdvvrqvv ervragfglr lstmervnhg adqharlwla qaadggryav klsgggtpag
       61 lvvtahlagq gvpgiaaplr svdgrlsidh dgrrlsvvpw vsdqraldgp mtgahwrayg
      121 evlaavhavp vteelsrllp mggaaypsiv tatravaerl rdpdpgdlad plvaelagvw
      181 savadrlrfl treverraag qrgrpgshvv chgdphlgnl llgadgqvwl idwddavlap
      241 pecdlmfvlg gvlafapitp dqqravlagy gttkvdrarl awflavrald disdwtrqal
      301 dcdagaadrg raarivrglv splglvslad aalrdldrqr
//
LOCUS       WP_357688080             464 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora parva].
ACCESSION   WP_357688080
VERSION     WP_357688080.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 464)
  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 464)
  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 464)
  AUTHORS   ter Beek,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..464
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..464
                     /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=48610
     Region          6..346
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 msapprrila ttvilaltas tllacgddep dsnskkitvw sledvadrvt atkaiiadft
       61 artgiqvdlv tvnedqfpsl iaanaaagdl pdvvgsvsla girtlagnel lhasanaevv
      121 dklgrqtfsp raleltsddg rqlsvpsdgw gqllvyrkdl ftaaglpapd tyeritaaaa
      181 rlntggvagi taatapsdvf tqqtfehlal angcqltdds gavtldspqc veafrfygdl
      241 irtssvkgaq dvdttratyf agkaamviws pfildelagl rndakptcpq cqsdpgflak
      301 nsgfvtaikg pngtepaqyg eisswavldg avtdpaksfv eymlgdgypr wfgmspegrf
      361 pvrkgtpaep eayltawnts qagvdakkpl advygdevla tlrrspdtfg rwglsqgqgk
      421 lvgamlgelp vpkvlgdlva gkadaaatan rakkdvdaik agvn
//
LOCUS       WP_357688093             198 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357688093
VERSION     WP_357688093.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 198)
  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 198)
  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 198)
  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 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   5  (residues 1 to 198)
  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 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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..198
                     /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=21911
     Region          16..>81
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mslknpygdf eitepqalra lahpvrlail drlqrhgpat atglsphvga tpsvvswhlr
       61 hlatfglvvd aegtsskrer wwqaaargfr fnlpddaegq aagrqlrgem fartaeapqr
      121 wllhdeprld tqwrgvsgvs dtsfvatpee lqrleaaiee liapyvrrkd ddmspadart
      181 vrmlryllpe pgddpaas
//
LOCUS       WP_357688185             303 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Micromonospora parva].
ACCESSION   WP_357688185
VERSION     WP_357688185.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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..303
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..303
                     /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=34549
     Region          5..256
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mlslvvgtgr cgstlvqell srhpavgfvs glddklarln pkgrfngply rrsaprpagm
       61 tslrhsrrll ergrlrvaps eayhlldrqv lagfsrpcrd lvaedltpfv srrlrsffde
      121 riarqgcqql vqhvtgwprt gllhaaypdl rvvnvvrdgr avanswlqmg wwdgwrgpdn
      181 wiygplpsdl reewiesgrs fpvlaalgwk mlmeafaqar lrhpadqwld vryedlveqp
      241 reqvgrmldf lglrwstafe kgfsrydftv graeayrdel spaqvtaier vlekplaewg
      301 ypv
//
LOCUS       WP_357688225             507 aa            linear   BCT 28-DEC-2024
DEFINITION  gluconokinase [Micromonospora parva].
ACCESSION   WP_357688225
VERSION     WP_357688225.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 507)
  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 507)
  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 507)
  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 10167328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..507
                     /product="gluconokinase"
                     /EC_number="2.7.1.12"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046316 - gluconokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0046177 - D-gluconate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51856
     Region          7..478
                     /region_name="ASKHA_NBD_FGGY_GntK"
                     /note="nucleotide-binding domain (NBD) of gluconate kinase
                     (GntK) and similar proteins; cd07770"
                     /db_xref="CDD:466790"
ORIGIN      
        1 mqperrvivg vdvgptaara vafaldgtar hvatraypli epvpgwrvqe pdvlvaatla
       61 atsacvagta gaevvalals sarygligld sammpvtpll sgrdtrsaea arellssgqs
      121 relhrltgtp vhpmnplckl lwfarhepyl ctttrwwvgl kdyvvhrltg mlvtelssas
      181 gtgmfdvhrr awssavldla gvsdnqlppv lpttavlrls paagravglp sgtpvvvgag
      241 dgplrslgaa atghavgglt lgatgalrtv vgapctdaae tfscaalted awvvrgavgn
      301 ggnvvrwagr vlgddsptsa lldlaariap gsdgvvmlpy lwadpaapeg cgppgaflgl
      361 rgehsrahlv raavegvclq lgdvrdrlae mtpigsvrlt ggafrsalwr evmaavldcp
      421 vhvagaadqv tlgaaalglf aightadlqt avtqldpgag gdrvtvdpal attyrglrtr
      481 lpalvtvagr lgeildastg lsaparp
//
LOCUS       WP_357688240             666 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688240
VERSION     WP_357688240.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 666)
  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 666)
  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 666)
  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..666
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..666
                     /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=71906
     Region          13..666
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpahqlapdi psdvlaaeqa hlaesraalr amrahaqsls adaagdwvsq qilqslldqr
       61 vaaladhpdt plffgrldrs adddlpstiy vgrrhvhdgg srplvidwra pvsrafyqas
      121 paqpmdvvrr rrfgyhggrl tafedeplae ggeigpsril tdeierprtg pmrdivatiq
      181 pdqdeivrag laqtvcvqga pgtgktavgl hraayllfth rerlarsgvm ivgpnrafls
      241 yissvlpalg evkvdqttvp gllgehaape dpavaavkgd armatvldra lwlhivkpee
      301 glvftkgayr hrvadhevre ivaslrgttr ygpgraalaq rlahqvlvrm eqrgespddr
      361 vqdavarskp vkhlvdavwp klapaqvlyr llsdpeflsk aarhdltpge qqlllwpkpy
      421 rgwksakwsa adaalldelg dliertpslg hlvvdeaqdl semqlralgr rcrngsatvl
      481 gdlaqgttpw stnswetvlk hlgqdqgevt eltlgfrvpr evldfaarll paiapglaap
      541 rslrpgagsl svrqggdvva avrealgreg sigvivpdav agrvsesltg iahtvlgpds
      601 tedhrllvip atlakgleyd hvivvepadi veaeprglar lyvvltravt sltvlhhkpl
      661 paqlta
//
LOCUS       WP_357688258            1031 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357688258
VERSION     WP_357688258.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1031)
  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 1031)
  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 1031)
  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 1031)
  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..1031
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..1031
                     /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=108886
     Region          3..240
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          151..994
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          895..923
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(896,899..900,903..904,906,936,939..940,943..944,
                     946..947,970,979..980,983..984,987)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          934..964
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          969..1002
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 merarfgvlg plrveggqvp gpakhralla allvsagrvv pierlmalvw ddrppasaep
       61 vlrvyvsalr klvdgittap ggylidvppd dvdchrferl vgqartarea graaeavsvf
      121 kaalglwrga aladvessvl rrlhavplee lrltaleerv aldlslgrga evvgelrglv
      181 aayplreraw arlldalcqv grrsealeay qearrtlvee lglepgaelr eahrrvlsse
      241 aapapsrrmp inetppdisd ftgrahvlsw itaaaaaqtr tpapgaagsd aageraagsd
      301 aagsgtagsg taapgaagag agrapvalvi hgppgcgksa vavhaatgld lpdgrlyasl
      361 garppgavle dllrslgcpd gvvpaalder vrmyrsltag rslllvldda adeaqvrpll
      421 ptgpgsltlv tsrsplagle aarayelgvl dpdeavamla gvagrarvaa epeaarrivr
      481 lcdglplalr iagsrlarkp gwtldhlagr lgderrrlde lsagdlavrg slalgyrglv
      541 dperrslrrl galsapdfap wvlgadlepl aeagllqsrg ldeagqeryg whdltrlyaa
      601 erlaeeqtap agaepggrag aqlggragge sdgraggepg gragvesrgr rgaeqggrag
      661 lgggsvgwre arrrvlaeia gevldrtrra rtalvpaepg sgqtvartae gmmetgrlra
      721 earwlgaerr flvatvgdfh dvglyeaawr lafyltplfe lgahhddwha ttatgldaar
      781 aaghrqgeal llrgladlhr aegrpeaaaa alraaqplve gldlaritlr lglveqrpea
      841 aeralarclr vfeeagdqrg radalralga vrrdlavlea slaayrelgd prgeaeslld
      901 laglhldarr haearecaer rlrvnrrlgd rlpeaaslll lariarsegv pdaaegfare
      961 avetferhgd rrgtgrallv laearldlde idgavevitr amgefdvlsd ihgraeaerl
     1021 arearrrggr p
//
LOCUS       WP_357688268             354 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688268
VERSION     WP_357688268.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  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 354)
  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..354
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..354
                     /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=34903
     Region          71..353
                     /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 mrkmvagiat aalltgcaai gpagtaspts patsasatps aaasqqslea ayeqvitkvl
       61 psivqintet glgsgivyds aghiitnahv vgeatrmtvt latggaarda rlvksftagd
      121 laiikvndtk gltpakfgds sklhvgqvvl amgnplglsg svtngivsal grtvsepeep
      181 gspgatiana iqtsaainpg nsggalvdla gqvigiptla aldpnlsgga apgigfaips
      241 ntatdiagqi vrygkvtnth raalgirgst iiggngrpdg vgvvgvekgs gaqkagirag
      301 dvivsidgkd tntmaelaey lttrkpgdqv kvevrhpdgn tetivatlgr lpge
//
LOCUS       WP_357688279             990 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357688279
VERSION     WP_357688279.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..990
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..990
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=106114
     Region          <34..966
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mvaplsfdir rcfgivrpip lecagrrlvc vmtpglesas ssprfvgrrp qlarigraqa
       61 tvlsrrwqmv cevvgepgig ktrfvhealq rcgptipwav gtcspdergv pfhvfrhaft
      121 egqslrhevr agqpteetwa esvaavpaap artsdarrfr tyqlarrlig laardglvlv
      181 lddlhwadas stgliahllr ypvpaplllv lvyrprqmat pmpfgppvpa ehadaeptsh
      241 drielhplsv aevgllhphv dqvelraryd lsggnpgyla vlpsgptsts adpireaqga
      301 rltdaavavl rrewvdlppv eltclragav vdapfttdll aevaqvpasv avevswrlar
      361 ldlfrrvpgt grfafrhpvl rmavaqdtda awqvkacara ltalvelgap ptdraryaer
      421 llslpnggwv drcvtvlcra aqevrretpd lairwlrlal walrptaglt rrrqdvslal
      481 aqitgetgdl aesrallqei vplfpadpdg rraqavalwa rverllgnya eaaaisrrel
      541 aalpagagpa ggyrlateig vagilaghpv tglpdmlggd lggsgadras llavsslaaa
      601 hdgalddarg lleagarivd alpdrdmrdh pdcftalgls elylerqada arhldrgltl
      661 vrashrddgl cqlllgrsqv ayhggqlnta ialateagiv arrigshhll sfalafeaea
      721 tawrgglrdd dravalarsa vgiatdlttw cgrtaatala taallsgdpa tcaelvlsag
      781 gdsrlsqlqt slrprwyell caaalatgev adaerqarla mteadqvglr gqrgfaesay
      841 gevllargef raalphlqta adlfrtggmv lrrslalasl araaeaadqt alaararrra
      901 lelagwcate rvglrlarpv gprevaaltd rewhiarlaa tgatsrligr qlnisprtve
      961 ahltriyrka gvasrsalva wvarlddtdr
//
LOCUS       WP_357688316             212 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688316
VERSION     WP_357688316.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 212)
  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..212
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..212
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=23104
     Region          6..212
                     /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 matfalihgg ggsardwqlv gaelrqrghd tvavdlpied esaglgdyad tvvravgdrg
       61 dlvvvahswg gfvaplvcdr lpadllvlvt amipapgepp tdwwentgfr svemddpiav
      121 flhdvpaela aealtwgreh aekallepwp lerwpdvptr fllcrddrwf ppafmrgvvr
      181 drlgvtpdei dgghcpmlar pgaladrles yl
//
LOCUS       WP_357688336             484 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688336
VERSION     WP_357688336.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 484)
  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 484)
  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..484
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..484
                     /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=54087
     Region          6..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 maepgiviig sgfagigmai klkeagyhdf vilekaadlg gtwrdntypg cacdvpshmy
       61 sysfalnpdw srmfspqaei wdylracvdr ygiaphfryg kqvvsleydd gdrawevata
      121 dgetlrtnav isgigalhip sfpeipgrel fagpafhsae wdhsadltgk rvavigtgas
      181 aiqfvpqiap ragkltvfqr tppwihpkpd faippwmkra lrlpgtaral rnglywlles
      241 ralgftvdpr lmkvheklar ghlesqvpdp elrrrltpgy tigckrilis sdyypaltrd
      301 nvelvtdgvs eirrhsivdv sgaehetdvi vygtgfkvte slqdqrivgr ngvkiqeawq
      361 dgietyygig tagfpnlffl lgpntglghn svvfmiesqi ryvidclrll srtraraldv
      421 rpeaqrafgr rllerldplv wnsggcdswy ldeqgvnrti wpgftfeywa rtrkvkpgay
      481 eliy
//
LOCUS       WP_357688339             420 aa            linear   BCT 28-DEC-2024
DEFINITION  Gfo/Idh/MocA family protein [Micromonospora parva].
ACCESSION   WP_357688339
VERSION     WP_357688339.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..420
                     /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=44855
     Region          34..414
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msitlaivga gargaayarl aaattratia avadpdparr ialadefdvp aerrfaswed
       61 laaqprlada vivatpdrah vepvvafaer gyaillekpm aplpeqaeri vaaavdndvl
      121 lavchvlryt pysrtlkrll dsgrigaivs idhlepvgww hhahsyvrgn waveaesssm
      181 llakschdid wlghligrpv rrvssfggla hfrpenrpag aagrcvdcpv erscaysair
      241 iyerflgdpv heawplgvlt ddvsadgvrk aledgpygvc vytgrndvvd hqvvnleyeg
      301 gitvaftmta ftaldfrktr ifgtlgsieg dgrtlrvhdf ltdtvetidl dpdgdasaad
      361 ghggadaalv eafiaavttg drslvtsgpe vsisshrvvw aaeqsratgs vvelipatpv
//
LOCUS       WP_357688351             509 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357688351
VERSION     WP_357688351.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 509)
  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..509
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..509
                     /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=53133
     Region          2..507
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mafdviisgg rvldgtgapp yradlairgd rvaavgrldg aeaatvidar grfvapgfvd
       61 chahgdaavf dpavqlaalr qgvttfvlgq dglsfapgsa atvayasryf aavngplteg
      121 pltvgellgg ydravainta yllphgtiry dvmgpspaap trdelarmia hverglaega
      181 aglssgleyl pgryasaeel aalceplggr pyvthmrayg aaagvgmsev veiatrsgaa
      241 ahvshlhgpa dvllplveda lardvdltfd typylrgnti lamvvlppev pgadtgrale
      301 mlasgeldaw wpqlaetwpr ltishapgla waegldmvea aeraglapae fcrrllvetr
      361 leagcvtarp degpegeesv rrmlrhpsht ggsdgiyvgg hphprgfgaf arflgqhvre
      421 lgdwtweqat vhlashparr fglagrgllr dgfaadvvvf dpatvadrat yaaprlpaag
      481 vddvlvsgvr vldggeptga tpgralrps
//
LOCUS       WP_357688403             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357688403
VERSION     WP_357688403.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=16643
     Region          14..144
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtrgagvtts gatvaafaya vdasldgwlg dnyrvgltef ralvvlhqep hkelrvndla
       61 qrvslnqsst trlvsrleak glarrdlcqg drrgvyafit eqgqalarev repyegrire
      121 llreapthfr hldvrqlgda lseiqtlirs
//
LOCUS       WP_357688374             127 aa            linear   BCT 28-DEC-2024
DEFINITION  RidA family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688374
VERSION     WP_357688374.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..127
                     /product="RidA family protein"
                     /calculated_mol_wt=13497
     Region          3..125
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mvkkqlktta gaaprgsysq glvvgdfvyt sgagpidprs gevvgddvaa qthqvmrnlg
       61 ailaahglgy ddvvkstvhl qhlkrdfaay davyksyfte pypvrttvgs dlmdilveid
      121 fvahksg
//
LOCUS       WP_357688427             222 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent F420 reductase [Micromonospora parva].
ACCESSION   WP_357688427
VERSION     WP_357688427.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..222
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22887
     Region          4..200
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mttvgfigsg aigstiarla veaghqvvls nsrgpetlae tvmelgsras aatsgeaaaa
       61 gdivvitvpv kafphvpaap larktvidtc nygperdgpi peldseslts selllrylpd
      121 amvvkafnni ffkhllslar pagaadrsyl pivgdsaqak vavtefiesi gysvldagpl
      181 aaswrqatgt pvwgtpygpy snekgqpvge dviraalaaa tr
//
LOCUS       WP_357688434             428 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357688434
VERSION     WP_357688434.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=45806
     Region          19..428
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msdelgvtgt pafvrgspcd vavigagmvg lstawflqea garvtvyerh hagagsswgn
       61 agwltpglta plpepavlry glravlsars pvylplradr dlwrfllsfv fystarrwrr
      121 gmaayvplne rcldafdala aggvsavttp aepflacfar erdsrgllde leqmgdagqd
      181 vtfrpvtgqv vrsmepvlsd rvgaavqifg qrylnpsefi psladavrar ggrildnsev
      241 tglqpattdv rvtgpfgqqr rhdavviatg aafgelaarf gvrrpvqagr gysfsvpver
      301 mpagplyfpa qrvactplgs rlrvagmmef rrpadeldpr ritavvdavr pllngvnldd
      361 rrdewvgsrp ctpdglplig ataaprvfva gghgmwgivl gpiigqlvaq avlkgevpae
      421 lapfdplr
//
LOCUS       WP_357688433             188 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357688433
VERSION     WP_357688433.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..188
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19438
     Region          54..188
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mraksislvl laalaagcag npggqpqagd trfvagdgkm qvfaaadrqa apavegptld
       61 ggtaslaahk gkvvvlnfwa swcgpcraea pvlkdvaakt kasgvefigv dfkdrkadal
      121 aferteqtgy psifdqpgki alafqgtvpp aaipstliid kqgriaaral gevrytdlmn
      181 tvtkvrde
//
LOCUS       WP_357688447             418 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            parva].
ACCESSION   WP_357688447
VERSION     WP_357688447.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  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..418
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..418
                     /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=44289
     Region          29..405
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 misdadlptm pptgmpsgla npasspttae pavllieddp gdalltrell sdsgisnrft
       61 qasslkeaaa apttpdcvll dlhlpdcqgl ealgrvlhrw pdaavvvltg lddaatrtaa
      121 vaagaqdylv kghidgallg rtiqyaiqrr ravvterqlr dsrmqasent rlqrgllptp
      181 lvtdpalavv sryvpgrgrs llggdffdlv qdedhtlhav igdvcgngpd eaaigvglrv
      241 gwrtltlagv ekaarmrlle qvlvaerpre smfatactir vvpdrsqvii vsaghpaplv
      301 itpgsadpap irhhlglgmf pgrgrwqesv vtlpagagll lytdgvyegf sedgtrlgee
      361 rfielaatls tvtepgdflt alldkirrsd dgrhsddtal lyltwpagad aapigpdr
//
LOCUS       WP_357688464             287 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688464
VERSION     WP_357688464.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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 287)
  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 287)
  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..287
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..287
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30416
     Region          32..253
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mrrrhqaeae iageaaaaaa vtappaepdl qaaaffdvdn tmmrgasiyh farglatrgm
       61 fttsdlfkfa vgqavfrlrg nenpdhiava retalafvag akvddvvrlg eeiydevmad
      121 riwggtrala qshldagqrv wlvtatpvel arviaqrlgl tgalgtvaes tdgvytgrlv
      181 gdllhgpaka eavralarre gldltrctay sdsandlpml slvghavain pdselreyar
      241 qqswpvkdfr tgrkatlaal piaagvgava ggvaagmalr rhyrstq
//
LOCUS       WP_357688580             372 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688580
VERSION     WP_357688580.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..372
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..372
                     /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=40133
     Region          43..354
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mpdtsppvrr slflhapirr rprvmleqml alvddstpad gpegpvavle rrlaellgke
       61 salffpsgtm aqqtalrvha drrgrrtfaa hpqshldvwe eqgynavhal rmrrtgdlhe
      121 lmtaadlaai geplaavvwe lpqrdiggll pawddlceqv alvratgaaa hldgarlwea
      181 qsyyrrpfde iaalfdtvyv slykslqgvr gavlasdaat vevarvwrqr lgggirdawp
      241 lalaalvhld tlaeqmpayr ehaiaiaaai nadgaaracp dppqtplfhi hlpadrrave
      301 ragqailaeh giqlwgrvrs asdpgrcafe vsvgenamef apdevvalih dllaraapaa
      361 svpsggsaar pa
//
LOCUS       WP_357688568             200 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357688568
VERSION     WP_357688568.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=21825
     Region          9..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvekhglrer kkqrtrqali eaavrlfedr gydrvtvaei adaaevsprt fflhfqaked
       61 vllantdvri dlalqaiaer raeeplpevl vramdhmian twehdlpsgl aalrarlvas
      121 vpalqarllq ryltaqaela qalqrafpgr ldtitasalv gamvgavsas altalqrgdg
      181 pdevrnamrq amalvarsvt
//
LOCUS       WP_357688631             541 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora parva].
ACCESSION   WP_357688631
VERSION     WP_357688631.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 541)
  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..541
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..541
                     /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=58277
     Region          9..260
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(9,33..34,67,72,77..80,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,75,91..94,98,100,137,139,
                     141..142,144,154..155,158,176..179)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,75,91..94,98,139,141..142,
                     144,154..155)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(20,98,100,137,139,141,158,176..179)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(154..162,172..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <212..414
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mhqlliagry rlldlvgtgg mgrvwlarde mlhrdvalke vvppswlaet eraelrlrtl
       61 reartaarln hpnvvrlydv vhdrdspwiv meyvpsrsvq qiisaegpls pprtarigla
      121 vlaalraaha agvlhrdvkp hnvlvaddgr vmltdfglat fdggdgtmtg pgtvlgspqf
      181 vaperaregv sdartdmwsl gatlyatveg qspyarssam atlsalatep pdpmrragpl
      241 rpvltgllqr dpwrrltave vepllrsaaa spdelagpar saaveavrsa grastphpve
      301 ptppwgepat ptprpqrrpv rrrrlialgg aaaallvagg vtltlvdrhd ertppsgsgg
      361 gaptsrpaaf acasspppta tpvvsvsppa daryrlpegw twhddptgfr iaapvgwarw
      421 negpvtcfrr ssgsrvlsve agparadpva ywkaeesrlt tsaalpgyrk vdisamdife
      481 ggavwecrwl nalgvavhsf rllintspgr sytvswltee fdwqvnaayl pmirqsftpt
      541 p
//
LOCUS       WP_357688635             322 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate ABC transporter permease [Micromonospora parva].
ACCESSION   WP_357688635
VERSION     WP_357688635.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  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 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   3  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..322
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..322
                     /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=35195
     Region          22..316
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 mavsetvaat apaatptppa prrqrrgrna aywlyllpga vlfllvigap lvgtlylslt
       61 kwsgigdprw vglanyqqll hddvfwasfr ntvwmlvamv vvptvlglll aavlfdvigr
      121 rfkprtaaal raafylpqvl pvvvagivwg wilrpdgafn slldavglga lrhdwlgdpg
      181 talpavmavm iwvqigypvv vfmaalqrvd pelyeaaevd ganwlhrfra itlpqirpet
      241 fvvaltctia alkvfgpifa ltrggpdnat nvpsyfayyt ffkklqvgyg saismvltli
      301 ivvvagifiw mqarserrdr gf
//
LOCUS       WP_357688658             210 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357688658
VERSION     WP_357688658.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 210)
  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..210
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..210
                     /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=23146
     Region          11..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msdvkrpnkr aqkanetrqr ilaaalelfv rdgygatnlq dvadkagvav qtiyfvfgnk
       61 rallkelvdv tiagddepva tmdrrwyrda laadtahdmv rayvtgttsv lervapigkv
      121 legavasdpe vaalwphsvn pryvvqreaa ealvakpdar aqlsaqeaad llfgllspel
      181 yllfvqergw prerweqwvg qtlrtqlcsg
//
LOCUS       WP_357688672             433 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Micromonospora parva].
ACCESSION   WP_357688672
VERSION     WP_357688672.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 433)
  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 433)
  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..433
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..433
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46738
     Region          4..331
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtllpatarq idtqvaqaqi dgrtpslvlg vvrdgalvhl atagehprpd adlqyrvgsi
       61 sktmtatlim qlrdagqlsl ddplerhlpg taagaltvrq llghasgmqr epegdwwers
      121 agtdlaglld glnadkiayp phtayhysnl aygllgglle rltgtrwadl ldervfgplg
      181 mrrttyaate pyargyvvhp whgtlreepr tdtgamapag qlwstiedlg rwaafladpd
      241 psvlaagtlt emcapvvisd ldswtgghgl glelyrdger vyvghggsmp gyvaalavhr
      301 ptrtavvgfa nsygfpittl grrvltsvld aepalpqpwr paaatptaer aelagrwwwm
      361 gipldlrwda gdlvahvrge rvsrftaegp drwrgrsgpe ngeilsvlrd dngratavdi
      421 atfvftrspd eap
//
LOCUS       WP_357688686             377 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357688686
VERSION     WP_357688686.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..377
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40298
     Region          4..340
                     /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 mtgsqpqlpl hgvkvldlst llpgplatlm ladagadvvk lerpgrgdem rtyeprfgea
       61 sanyavlnrg krayvtdfkd paqrdrvlel aaeadvvleq frpgvadrlg lgyqhvravn
      121 pdviycsisg ygptgpratr aghdlnylae sgllgvatds tgspslpvtv ladiaggtyp
      181 avvnillalr qrdvtgdsvh lqvsithnlq vlaygyfath qagggwprpg aelltggspr
      241 yqvyetadhr hvacaaleqk fwsrlvelve ldpkfhddhg qeqavisala erfasepadh
      301 wrsvldgedv ctvvvatwde avqanlvdid apervsapgt qdsfgtlpsp isptlrqgpg
      361 tvpypaladl gdespws
//
LOCUS       WP_357688718             157 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688718
VERSION     WP_357688718.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 157)
  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 157)
  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 157)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..157
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..157
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17020
     Region          44..>157
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkaiiplwed stqeaihghe tflqeipaar nvrlirnvta psltvytpdp svaartgvil
       61 cpggsfhtlp hwedleingv agrlaghglt vfvlryrlap tpradeefmr lassspimda
      121 vkaqsrvard dafqalrvvr erasawgvdp grvgmtg
//
LOCUS       WP_357688743             282 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Micromonospora parva].
ACCESSION   WP_357688743
VERSION     WP_357688743.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 282)
  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 282)
  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 282)
  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 282)
  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 282)
  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..282
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..282
                     /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=30411
     Region          15..260
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mprvrqnrpv pvheitdpdd driadyralt dvelrtrwep phglfiaege lvlrralrag
       61 yparsylvda krtdqladld tgdapvyaat pdvlqratgf hvhrgvlasf hrrplptaae
      121 vlatarrivl ledvnnhtnl gaifrgaaal gidavllspt cadplyrrsv rvsmgevfam
      181 pyakldswpg gldqvreagf tvlamtpapd avpiqrltpa qreraalllg aegpgltvaa
      241 qaasdvrvvv pmrrgvdsln vaaaaavafw elgrddppfg ge
//
LOCUS       WP_357688761             559 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Micromonospora parva].
ACCESSION   WP_357688761
VERSION     WP_357688761.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..559
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60574
     Region          16..550
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mgyvdvaavg hilpdgrelf advsfrvgdg skvalvgpng agkttllrmv agdlpvrtgv
       61 varagglgvm rqfigmigde ssladlalsl appalrdagr rlgeteaamr aaeahgkfsn
      121 aagkaqlaya dalgawgeag gydaevlfdt vativlgqpw davrdrpvrt lsggqqkrfa
      181 lelllrgpde vllldepdnf ldvpgkrwle arlrestksv lyvshdrell aqsadrvvav
      241 eggsawvhpg gfaswhearv arharldelr rrwdeehqkl relmlmykqk aayndglasr
      301 yqaaqtrlrk feeagpppvp pkdqdirmrl aggrtgkrav vceqleldgl typfdleiwy
      361 gdrvavlgan gtgkshflrl larggtdpdp angpvdgaga lapvahdgva rlgarvrpgh
      421 fsqthdrpel msktlveilw rgdehrtgmd rhaamgvlsr yelaaqgdqr fgtlsggqqa
      481 rflvlllels gatlllldep tdnldlasae aleaglnafe gtviavthdr wftrsfdrfv
      541 lfrgdsevve tpepvwdvg
//
LOCUS       WP_357688810             369 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            parva].
ACCESSION   WP_357688810
VERSION     WP_357688810.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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..369
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..369
                     /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=40638
     Region          85..363
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mpdhtapdat ptgrlsrrsl laasagaaaa igaaglpvla tgtpalanpk sklrveplip
       61 aknrgiilys vrdritaapd dsgvpygfer vlarlaeigy keiefagytq steilgrqit
      121 paeirkildd nglvangtha tiqpatfqqq ldiaeelgmk nigtgsdpts saykaewdaa
      181 adiwnelgrq arargmrlyt hnhdaaysfl idrgprdaqg rqtrssgirr leyffeitdp
      241 ryvffeldiy wayvarhkhq kyinpagqev tglfdpiltv adrttrfplf hakdgdrdts
      301 vpngyqmtpl gdgdlnfqqf fqtigernfh hanwemdtap ggadnkgqsl dfaatsyrnm
      361 sdltiylek
//
LOCUS       WP_357688821             175 aa            linear   BCT 28-DEC-2024
DEFINITION  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase [Nonomuraea
            sp. NPDC048916].
ACCESSION   WP_357688821
VERSION     WP_357688821.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 175)
  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 175)
  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 175)
  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 175)
  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..175
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..175
                     /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=19221
     Region          4..169
                     /region_name="Adi1"
                     /note="Acireductone dioxygenase (methionine salvage),
                     cupin superfamily [Amino acid transport and metabolism];
                     COG1791"
                     /db_xref="CDD:441396"
ORIGIN      
        1 mtedgdvlvr tseptriaae lagrgvafer welkgpgdpl tayaqeiaal rqaggyrlvd
       61 vvrlhadevd pdtaraarak fldehvhded evrffadgsg cfylhlgdrv yavvceagdl
      121 lsvpsgtrhw fdtgaaprft avrffqeedg wladftgdti arriptldel leatp
//
LOCUS       WP_357688847             425 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688847
VERSION     WP_357688847.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..425
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..425
                     /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=44587
     Region          20..423
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mtivvpsmtp apitpgrqal dsalhqlgqa sehlglddgl rlmlatprrs ltvsvpvrre
       61 dgrldvvqgf rvqhnvsrgp akggirfhps tdldevtala mwmtwkcalv gipyggakgg
      121 vavapetltt relerltrry vneilpligp ekdipapdvg tdeqtmawim dtfsvnagys
      181 vpgvvtgkpm alggslgrag atsrgvqiva lsalgrspeg vtvavqgfgk vgalaaqyls
      241 dagctvvavs dvsgavhass gldiadlraw vaetgsvqgy rhadaldrde lfeldvdllv
      301 paalegvita anaprirarl ivegangptt peadeilagr gttvvpdila naggvivsyl
      361 ewvqnmqays wsaaevemrl rdlmesayge vkslaagrgl tlrqaahvig vgrvaeahqm
      421 rglyp
//
LOCUS       WP_357688857             229 aa            linear   BCT 28-DEC-2024
DEFINITION  LacI family DNA-binding transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357688857
VERSION     WP_357688857.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K.
  TITLE     Parallel evolution of ligand specificity between LacI/GalR family
            repressors and periplasmic sugar-binding proteins
  JOURNAL   Mol Biol Evol 20 (2), 267-277 (2003)
   PUBMED   12598694
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Nguyen,C.C. and Saier,M.H. Jr.
  TITLE     Phylogenetic, structural and functional analyses of the LacI-GalR
            family of bacterial transcription factors
  JOURNAL   FEBS Lett 377 (2), 98-102 (1995)
   PUBMED   8543068
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..229
                     /product="LacI family DNA-binding transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23905
     Region          <4..229
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mladtaeshr rvvqhvetrq vdgvvlvrpd gagplaerla rtevpvvllg rpaiaslvpy
       61 vdvdnvggar aatahlldrg rrnlgiicgp mdlvdvqdrl tghrnalrqa glhpllapag
      121 ldresgaaaa rrlmaehprl davlatsdhl aigalqaagq aglrvpedla ivgfgdgdaa
      181 sattpalttv rvpvteqala larlllsrld grhttsvvlp arlvvrett
//
LOCUS       WP_357688920             303 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora parva].
ACCESSION   WP_357688920
VERSION     WP_357688920.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 18123688
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=32454
     Region          13..199
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          230..295
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mievrfspdd lsrvrfahsp laelvasswa lrkptkywmh rpwreraerl lpdaglepll
       61 avlrssngyv pdfltpigaa pnlaaelrav agtdpslvrr qldragaprl tadelvaqlh
      121 ryftlliapd wprlralala dirrrtllaa eqggrtllre lhplirwdga alrvavgttr
      181 pagldgrtwt llptsfsgpt vhaiwegdag palcyppagl gdlwaappps aalgallggt
      241 raaalsllda plstgelaam lglapatash hlttlrdngl ivgvrqgrvv ryartvlgdq
      301 lvg
//
LOCUS       WP_357688949             431 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357688949
VERSION     WP_357688949.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 431)
  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 431)
  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..431
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..431
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=45994
     Region          <19..243
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          373..418
                     /region_name="VWA_3_C"
                     /note="von Willebrand factor type A C-terminal domain;
                     pfam18571"
                     /db_xref="CDD:408355"
ORIGIN      
        1 mgdqptftlh idqnkylstd grevhailti gstgavtttt asvpaeaaev iivdtsgsms
       61 ggkirearqa aatavqslrd gvffavvagt dtarviyphg rqmarasrat rteaqnaigr
      121 ltanggtsig qwlllagdll aahpnairha immtdgqnne radvfaaala rcegafvcds
      181 lgvgadwapg elrkvaeall gtfdfvrnqg dladffrkit qtsmsktvae lamrvwvpqt
      241 atlkfvkqvs ptlldltgkr tdvnpltgdy ptgswgaeer eyhlcvevpp gqvgseirag
      301 wvkllrpdtq evlasgnvla qwtddlaast qinrkvahyt gqaelheliq dglsaraagq
      361 vdvatarlak arqlatesgr sdtarlldkv vevdphsgta rlrrnvdkad eieldtgsvr
      421 tsrlrkdgeg s
//
LOCUS       WP_357688987              70 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy-metal-associated domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357688987
VERSION     WP_357688987.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 70)
  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 70)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 70)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..70
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6968
     Region          1..68
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mstatytvkg mtcghcvgsv keevnevpgv tnvevdlatg sltvdgdgav dparivaave
       61 ragyevagrs
//
LOCUS       WP_357689027             381 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357689027
VERSION     WP_357689027.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 381)
  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..381
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..381
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39493
     Region          1..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 mdrgplsgvr vvelggqgpv pfcamtladl gaevitvrrp gpaaptnphn pvidrgrrfv
       61 avdlkspdgv avvrrlagra davlegfrpg vlerlglgpg hllaenpalv ygrmtgwgqd
      121 gplaqraghd inyialtgal hgigqaggpp vvpvnlvgdy aggalylalg vtsallsara
      181 tgrgqvvdaa ivdgvaalms ivyglsaagr wtgergvnll dggapfyrvy rcadgehvav
      241 galeepfyld lldgvglggr ddlvtgrldr srwpaieeal stafaaypra hweavfagrd
      301 gcvtpvlsar eaqhhphlaa rgtyvdghaa paprfsgtpa agaphvepre cdvralladh
      361 dlspseidrl ladgvvapal w
//
LOCUS       WP_357689029             294 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357689029
VERSION     WP_357689029.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..294
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..294
                     /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=31848
     Region          1..293
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mrpyksllfv pghrgdwvdk avragtdavi ldledavpeh lkaearqtva esvarlhaeh
       61 pevgvlvrpn algtphvgrd laavvrpgld alllpmiyta edvvrydalv gyfeseqdgl
      121 dagsvhlvpt letarsvanc eelavatprv asllvaaakg adiareigfe wtlegletlh
      181 lrsraliacr aagithpicg iwqdvsdldg lavfsaqnhr lgfrgqvllh pshvrtinat
      241 ygldeqeldr yrrmvaafea aeaegraavl fegehidiah vqtarrlleh agrs
//
LOCUS       WP_357689035             506 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357689035
VERSION     WP_357689035.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..506
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55913
     Region          4..503
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mrtiadflrl nrrrypgrta vvddtsrvty aeladrayav adglladgvr rgdtvgilag
       61 nsvfvaevyl gvlcagavpv mynwrwatpe lvfglndsra qvafvdqewa gtmraaqdtg
      121 ellhlrrvvv egagyegylg epvepeltgd mdatnvimft ggttgfpkgv mlsersavgn
      181 glneiidtdm ehsdvtllia pmfhaasllc wfvphlmlga tsvlmrrfde rqvgevvqre
      241 gvtngflvpn mvrrllaagv ftdydwsgyr rmyvggaifk lpdktavrda lphvriyyqy
      301 glteggpivt rlrpedmfre didgsigref lltevrlrav dgdeevppgv vgeitvrapn
      361 imdgyfgrpk etaevlgedg wlrtgdlasr dengyfyyhd rskdmiktgg envysaever
      421 vlythpaise aaiigvpssk wdeevcavva lkkgarldag elqewcrghl agykipkria
      481 fvppehipvn dsgkimktrl rsmglf
//
LOCUS       WP_357689109             730 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357689109
VERSION     WP_357689109.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 730)
  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 730)
  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 730)
  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 730)
  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 730)
  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..730
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..730
                     /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=81162
     Region          2..727
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mnpvleplfr tvrathpkad lrlieraydv aayhhrdqkr ksgdpyithp lavatilael
       61 gtddetlcaa llhdtvedta ysldelradf gdtigslvdg vtkldkvkfg daaqaetvrk
      121 mvvamsrdir vliikladrl hnmrtmrylp ehkrhqksre tleifaplah rlgmntikwe
      181 ledlafamly pkrydeiarm vseraprrdl flqeviekvs gdlreakira vvkgrpkhyy
      241 svyqkmiard vafddiydlv girvlvdsvr dcyaalgtih arwnpvpgrf kdyiampkfn
      301 myqslhttvi gpegkpvelq irthamhhra eygvaahwky keevgapgpv gkvkpgsdma
      361 wlrqlldwqk etadpgefle slrfdlsvse vyvftprgqv valpegatpv dfayavhtev
      421 ghrcigarvn grlvplesrl gngdtveift skspdagpsr dwlkfvksgr arnkirqwfs
      481 kerretaiea gkeaigramr kqglplqrlm sgesllalar dlrypdvsal yaavgeghva
      541 aqsvvqklva siggvdsaee diaetslptr lkgrprgggg agvvvagdad vwvrlskcct
      601 pvpgdeivgf vtrghgvsvh radctnvqql keqpdrlvev swspsddsvf lvaiqveald
      661 rprllsdvtr tlsdqhvnil sasvttsrdr vaiskftfem gdpkhlghvl kavrsiqgvf
      721 dvyrvsgagt
//
LOCUS       WP_357689130             871 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Micromonospora parva].
ACCESSION   WP_357689130
VERSION     WP_357689130.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 871)
  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 871)
  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 871)
  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 871)
  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..871
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..871
                     /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=88874
     Region          36..843
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mttiggrdgl lvdpvdrdas vgldaaeaaa rlratgpntv appprqpvta rvlhqltdpl
       61 valllaaaav taalgdypdt aviflvvlvn tvigvvqevr adraiaaldq laaptarvvr
      121 dgrelvvpaa divrgdlvrv eagdvvpadl slieasrlhl desaltgesv tvgrvageea
      181 lagtvvtvgr atgtvlrtga asalgrisal vagtrptgtp lqrrlsalgr vlgliavavs
      241 glvfaigvvg grpvvdmait avslvvaavp eslpavvtla lalgarrmaa ahaiprqlha
      301 vetlgsvtvi asdktgtlte grmavqqavt gdgarygvtg sgyaptgtvh rdgeavavpd
      361 glrqlaragl lcndaalspp ddersewgav gdpleaalva faarcgldpq airtawprva
      421 ehpfdqaqrr mvtvhrscdq rylvvckgap esvlgaplld atdeeiaela stahrlateg
      481 lrvlavaaal veavpdpvsp tglrpvglva vgdplregap rvadsfdtag vrlllitgdh
      541 patataiggr lglwragdpl angdddqaah pdtrifartq peqkldiiag lqargevvam
      601 tgdgvndapa lrradigvam gggtevarqa adlvlvdddl stvanaigeg rriydnirrf
      661 lryalsggla eilvmligpl fglpvpllpa qilwinllth gvpgvalgae paepgslrra
      721 prspqesvlg aglgrdvllt galiaavvlg agvfaahrdl pwqsvvfvvl glaqlgvala
      781 vraprpagtr sgnpgllvav avsallqvgg vllaplrdll gteplapsvl lacaavsvlp
      841 glvlrltrss atdsdrgddg tngprplavr p
//
LOCUS       WP_357689163             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357689163
VERSION     WP_357689163.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=35874
     Region          7..314
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mshpagrvla llellqtrhr staadlagql gvdertvrry attlvelgip vtadrgrhgg
       61 yrlhpgyklp plmltddeav avllglvvae rvglateqpa tasalakirr vlpaaladrl
      121 aavqehlgft lrrpdpepgp asgtllalas atrhrqrval dyrswrgers hreldpyglv
      181 fhagrwyvtg hdhrrgevrt frldrigavt pgvatftvpd gfeavawvtr slagvpyphe
      241 vevvletdlv aarrrippsv aeltattdgv llraraeslp gmaallaglg cpftvrrpda
      301 lrvavaehar rladwaarpa ggqppsprrp ld
//
LOCUS       WP_357689165             242 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357689165
VERSION     WP_357689165.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 242)
  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..242
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..242
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=26035
     Region          3..237
                     /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 matfvlvpgf wlgawawrdv taalrsqghe vhpmtltgla erdhlagpev gldthttdiv
       61 rlievedlhd vllvghsggg mpvaqaadri pdriarvvyv esgplpddta qfdtvppeeq
      121 qrlraaigtg hllpppawdp aadptnlagl deptlgllrt ratpqplrta tdpvrrtggh
      181 pvptalvast fplalvqqmi reehpfftgl adgqlhelpt ghwpmlsepk aladvldlit
      241 rt
//
LOCUS       WP_357689176             270 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora parva].
ACCESSION   WP_357689176
VERSION     WP_357689176.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 270)
  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..270
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..270
                     /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=28055
     Region          2..270
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mrvlvvggsg llgrevcrrg veagfsvigt fhsgeigvpg vdarrldvtd raavralvaq
       61 vrpdavvgtp yryedwavta dgaahvalaa aevgarlvhl ssdalhagrp vpylddeppt
      121 pvhaygaaka aaetavraid sgaavvrtsl ilgegskqiq lcrdalagra tlfsdelrcp
      181 idvtdladav lelvessyag llnvagadav srvelgllva erygldparl ktttsaatgv
      241 vrpldvrlds sraagllrtr lrgvreilar
//
LOCUS       WP_357689246             495 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Micromonospora parva].
ACCESSION   WP_357689246
VERSION     WP_357689246.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 495)
  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 495)
  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 495)
  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 495)
  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 495)
  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 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..495
                     /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=50625
     Region          12..491
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mttttghlpa laaavlqpgf vgttppqwvc rwlgdglgsv vlfarnvvdt eqvaaltatl
       61 raerpdviva ideeagdvtr lesvhgssrp gnfalgavdd palteavard lgvelaaagv
      121 tlnyapdadv nsnpanpvig vrsfgtdptl varhtaawvr glqaggvaac akhfpghgdt
      181 rvdshhdlpr itadrarldv celapfraav aagvqavmtg hllvpaldpq lpatlsqril
      241 ggllrdelgf sgvvvtdave mravadrygf agatvralaa gadaicigge radeqaarel
      301 rdaivaavis gelpeerlae aakrvgqlaa wtvaargags aaaraadvgl vaarravrvt
      361 aapgttgalp ltsaahvvef epprniaiga etpwgiggpl gellpgtstv rygepdvpad
      421 pgagagtrpl vlvvrdlhrh dwmraavhra lavrpdavvv elgvpelvtg avhlathsat
      481 rasgraaaev ltgar
//
LOCUS       WP_357689265             166 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Micromonospora parva].
ACCESSION   WP_357689265
VERSION     WP_357689265.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=18029
     Region          2..159
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrlvltadth vpkrardlpg plwaaieaad vvvhagdwvd etlldamtar srrligvygn
       61 ndgpalrarl pevarveldg lrvavvhetg prtgrekrca arfpdtdllv fghshipwds
      121 tapgglrlln pgsptdrraq pqatyltatv hrgklsevhl nplprp
//
LOCUS       WP_357689271             177 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora parva].
ACCESSION   WP_357689271
VERSION     WP_357689271.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447364
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=19456
     Region          4..176
                     /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 mehvelaage lllrpwqded apavrdalrd paiaqwnpqg ddliddeval lwvrrradws
       61 agdhaslavt savdgellgs vslhhirngd asigywtapa argrhvalra vvrltdwafa
      121 dlglhrvelc havanpascr vaeragypae gtlresyryg dgrrydehlh arlatdr
//
LOCUS       WP_357689279             277 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357689279
VERSION     WP_357689279.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 277)
  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..277
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..277
                     /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=30958
     Region          28..276
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 myrqlvaavt aalttlvvmt giasasprev dniahrgasa yapentiaac vlawaqqadm
       61 cefdvqqtkd qqlvlmhdpt larttnvekv fpgrspwrva dftlaeiqrl dagswfspty
      121 rgervptlaq avrvmrnrei gllleikhpp vnpdvdrrva aelqdlrsww sgkrlavqaf
      181 dwrsmrtfhs vmpqvpiall gkpaaarlpe laryasginl phvgltpqyv eevhdqgmrv
      241 ytwstkrraa irrlisygvd gimtnqpdhl qgvkrrs
//
LOCUS       WP_357689353             407 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora parva].
ACCESSION   WP_357689353
VERSION     WP_357689353.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..407
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..407
                     /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=44921
     Region          21..355
                     /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 mtsvaatsaa ppapalprlp sltglrwiaa llvfgfhagt mriiaepdyk avvdalftlg
       61 lsgvqfffil sgfvlvwsar pgdsrrtfwr rrvakiypnh lvlwaatlvv awwfadpvlp
      121 aaalenllll qawdprpgwf ysintvswsl scefffylcl plalpllrra rpkllwaliv
      181 vlpllilalw paqelvpevs rwwftqifpp vrslefwlga vaaelmrrgl wrgpgltaas
      241 aifvvtwvaa aqwiraelwt tllavayllv itaaadadvr grrspwrsrp liwlgevsfa
      301 fylvhvlvmt svlrwsgdwg tgfggwrgpa vvlgflvanl ilagllhrfv etpmmrrlap
      361 rrparpasvp rqraagaagd gdapasesga adevgqangr spyadlr
//
LOCUS       WP_357689401             566 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Micromonospora parva].
ACCESSION   WP_357689401
VERSION     WP_357689401.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 566)
  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..566
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..566
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=61037
     Region          218..285
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          276..343
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          335..404
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          393..460
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mrffaargnr qyttrliaga alslavigan alltispaea ssingpitra emldraqnwv
       61 drditytqtg twakdvdgsh tyrrdcsglv smawhlsqsy vtdqfqgsna mwttlgsind
      121 fqpgdamvrs ghielfafwk dkndhskgay vysfnsdgqt vqnpyannnt gsrgfngwdd
      181 lrtykpirrt gieaeptpep epeptpvadp nvvqlsgdfn gdgrddaaml ylhkdssiel
      241 ftslgnasgg fgaffgsykl panswkwdsf rtivgdfngd grsdlgamyy qadgsitmht
      301 alantsggfg aftgsltvpa saawkwdair ltsgdfngdg rddaamlyhh kdesielfts
      361 lgttsggfgt ftgsykipan awtwdsfrti agdyngdgrs dlaamyyqad gsitmhtala
      421 ntsggfgaft gsltvpasay wkwdsvrltt gdfngdgrdd agmlyrykde sielftslgn
      481 asggfgtftg syklpanswk wgsfktitgd hngdgrsdva amyyqadgsi tmhtalants
      541 ggfgaftgsl tvpasaswyw dairll
//
LOCUS       WP_357689435             257 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357689435
VERSION     WP_357689435.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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 257)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..257
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..257
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26422
     Region          101..254
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mrriiglagl vvvltacggt vtttasggpt paptptsspp atptptpsps rvitgpnvsg
       61 cfteedgeif thgddlpgvi tgkgevgvvi tyerlgnvcn wrplsdrlve agyrvllyar
      121 dssvppedma vkmgkrlagk kgvkrlffvg gsiggtvsap aaarmgdkaa givalsgaid
      181 aevaakitvp llqigtendg yggakdlqts hdaatkapan evhiikgegf hatdmfrssy
      241 gpevldriva fmdrhkg
//
LOCUS       WP_357689471             327 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Micromonospora parva].
ACCESSION   WP_357689471
VERSION     WP_357689471.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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..327
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..327
                     /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=34134
     Region          204..>324
                     /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 mttmstrakl gvvvasavll gtvaagyaat taqaprtppp vgggqavsla pgprllaitd
       61 rhvstvaatd pagprmvggl eclrvyaaag tgvclrpeta wsyqvvvlda elrqtravgv
      121 pglpnrarvs asgrmvswtt fvggdsytss gfstrtgild tvtgstvasl eefaitkdgg
      181 rhrnpdvnyw gvtftaddnr fyatmstggr rylvrgdvaa rtvetlkenv ecpslspdgt
      241 rlafkeaida dpakgwrlsv ldlssmrvta taetrsvddq aawldsgkla ytlrrddgqp
      301 dvwsvpadgs gtpvltilga espsplt
//
LOCUS       WP_357689497             162 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357689497
VERSION     WP_357689497.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 162)
  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 162)
  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..162
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..162
                     /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=17678
     Region          14..155
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtdatparrg rqlptadelr iwrdfietta algsrlesrl qsdsslstgd yavllalsea
       61 qgqamrssel aahigwersr lshhlarmer rglirrqeca tvprgaevll ttagaeafrg
      121 atvphlrair elfvdaltpd qivaageiat alrarldvlr ar
//
LOCUS       WP_357689511             140 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357689511
VERSION     WP_357689511.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 140)
  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..140
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..140
                     /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=15782
     Region          10..136
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtserggclv rvplrwrdld hqghvyhgtl ltlldearta wlrdvvriqs pdayvvarie
       61 idylaeirmd igaidvgfev srlggrsirt deivrtpdgg dlaraavviv mwdreahrsr
      121 eltpeerrrl aprrgtvsda
//
LOCUS       WP_357689514             626 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Micromonospora parva].
ACCESSION   WP_357689514
VERSION     WP_357689514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 626)
  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 626)
  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 626)
  AUTHORS   ter Beek,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 626)
  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 626)
  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..626
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..626
                     /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=66965
     Region          <190..610
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
ORIGIN      
        1 mwwetgvrar aeagvfavfa elprlvwtal giswradrlr tgvvavatvg agvmaafgll
       61 atqrvlvelf aggptpdkvr aalpalavla atvalragmg iatgyaqngl tprvsrever
      121 glfevstavr leafdadafa ddmerasrgt estiglvqas mnllaglagl lavaaaviii
      181 hpllllallv atvptawasl raghlryqty tagsvrrrrl wllhklmaer asapelrsyg
      241 lrrflldqyd rvmrvetdiq lalarrvttt ttvgaiiggl atgtvyallg lllldgqipl
      301 aaaatcviav qsaqrslaia tfqvdhvyte gqhfgdytgf mtradaylpg nadadagaal
      361 drlreltvne vslrypdrdt pavdgvtlti tagqtvafvg engsgkttla amiaglrvpt
      421 aggiewngrp lseldvdglr ariavvtqey hkwpftaatn iaigdvdsea rqdrieaaag
      481 ravahdmine lphgyetlld rtfargqdls ggqwqritaa rgflrdaell imdepssald
      541 praedalfqa irdrrgratt ilithrlanv rhadrifvlh hgrlveagsh adlvatggry
      601 aelfalqaag ydanlkdghr saptsh
//
LOCUS       WP_357689611             340 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357689611
VERSION     WP_357689611.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 340)
  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 340)
  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 340)
  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..340
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..340
                     /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=36136
     Region          35..331
                     /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 mredetetgv rlpsiplspl ravlrrmaia aaivlamfal vamdldgyrd nadggvslld
       61 alyyvtvsis ttgygditpv saearivniv avtplriafl vvlvgttlev ltkrtrdair
      121 ierwrarlrd htviigygtk graairtlle ndrtrdsivv vdpqaavvde atadgfvgvv
      181 gdgtrshvln rarigtakei iiatqrddta alvtltarsl nptativaav reaendplvr
      241 qsgadvvits seaagrmlgv atqspavstl iedflaygkg ldlferpvat eevgrppaas
      301 deivvavvrg revmtyadpr astlqagdrv vvihvpplpg
//
LOCUS       WP_357689659             239 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357689659
VERSION     WP_357689659.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 239)
  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..239
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..239
                     /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=25820
     Region          10..234
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mnttrlavfs pldstgrvda vvrrladaia lgllsdgeql pseaelagrl gvstvtlrea
       61 lmalrqqgmv etrrgrgggs fvrvpaeldl gihlrtfave elrdlgdhya aiagaaarla
      121 aqrslpsdla plwrslaema daessaerrr idgrfhiela aasqsarltr eeirlqadig
      181 pllwlshdev gghdgvaaqh raiaeavqqn dgeraralae rhvldaidll ielrlrvqe
//
LOCUS       WP_357689682              45 aa            linear   BCT 28-DEC-2024
DEFINITION  RICIN domain-containing protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357689682
VERSION     WP_357689682.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 45)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 45)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10069754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..45
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..45
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=4344
     Region          1..>34
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cd00161"
                     /db_xref="CDD:467293"
ORIGIN      
        1 mvndggglcl tvpggstsdg vrrlaqtnsc dsaatrgpdl rltpg
//
LOCUS       WP_357689688             232 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357689688
VERSION     WP_357689688.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 232)
  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..232
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..232
                     /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=25057
     Region          5..224
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mvigapqtra ealaadierm itekglgpgd pigtmdefrd rsgfgratis eaarllsdrg
       61 tvqirpgrgg glfvadpnpv vrlrhtlltv rrqpttvada iavrealell ittdaarhrt
      121 aqdiaalrkl ltrlrraaag gadrfmranw elheriaeit pnplaravyl smsrciadla
      181 tradadpdgp ddgyldlrve ihaelveaia agdverttaa terhrgsgtm rl
//
LOCUS       WP_357689660            1009 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357689660
VERSION     WP_357689660.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1009)
  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 1009)
  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 1009)
  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 1009)
  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..1009
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..1009
                     /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=110370
     Region          1..244
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          110..1007
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mrfgilgplr vgggestvta grdrtvlaml llragrlvpv delvdavwed rppataraql
       61 qtcvsrlrrr ftelglapel ivtdpagygl rtapndldae vfnrrvevar aqvvagrlae
      121 artefraala lwrgptlsgi gsrnvrrraq aldeqrlttl eecvdvelrl gqaaelieel
      181 aesvdrnplr erlrgqlmla lssvgrqada lavyregrrt yaeelgiepg aelqklhqrv
      241 lagdlalagr pappvgavrs lpraigdfig rqetvarlvk eieedgiriq vvdgmpgsgk
      301 ttlavhvata ladrypdaql fidlhghser rplttatava allrqlgvpa ervpenlddr
      361 lalwrielag rralvvldna asadqvapll pngaqslvli tsrrrligvd egrpsslpvl
      421 dadeaiellg rvagmeriaa epeaaaevar rcghlplair lagarlahrp rwrvadlaer
      481 lvagagplae ltagqrsvgq afalsyaqvs psaqrlfpll glyppgrfds rvaaalvdlp
      541 ladtqeqlde lvdahlveev qpgryrlhdl lreyarllla gperqaerha averlldhhl
      601 svtlaiartv eaagsrrnip erapgrpdll avpvaegraw feenhvalta lvrkaedegf
      661 hvqcwqlara cwrlnfeggh ldeliethti glrvaerlgd eaayatmlny lssayfrlar
      721 fpeaisamev altvrrrlgl rddtlstlwn lgvsyaangd hrlgktkfde alamirgsvd
      781 vhaltnllnn vsyaliawgr ydeslrlarl hllaarqakd drqtdnaigh lamvrhrmgd
      841 lgparrllrt alylkrrann rfgegevlne igvmervaga peraaalhre alvamvdsgd
      901 rigqcasrnl laramleqgd avsaldlhrr vladasrlaa ryekaraleg iarcvlatdp
      961 ttarahleqa lalfrevesp drheveallt dlgrriices atgaagwya
//
LOCUS       WP_357689748             250 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357689748
VERSION     WP_357689748.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 250)
  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..250
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..250
                     /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=26898
     Region          7..242
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 msgprfepvr tvrayerive qieeaiesga lcpgqrlpse rdlmgqfsvs rstvrealrv
       61 lqarglvrsr pgdphgaevq pftpaelrks mtmlarvdgl slgelvqfrm vldasaglla
      121 arlrtdehla emeaavaamr aaaeaghdef saaevafhda varagrnklv qicaevvrsi
      181 vcdlaadeia aapgraaltr rsirrheevl aavragdgpl aarlsrqsvy dhyaghvpag
      241 erpalralle
//
LOCUS       WP_357689770             261 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357689770
VERSION     WP_357689770.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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
REFERENCE   2  (residues 1 to 261)
  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..261
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..261
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=27340
     Region          1..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 mhkitvngas iaydeagtgs pvvllhagia drrmwrgqvs alatrhrviv pdlrgygdse
       61 lppapfthhd dvaglldald lpratlvgcs fggavaidta lahpdrvsal alfdtavsgn
      121 ewsdeandlw dnlvgevdpd dfvagaagev rfwvvgpgrq pedvdselia faqemdqral
      181 aaelalgave vgeltppaig rlgelaipvl vtagvadvpd isrladriaa evrlpdvpna
      241 ahllplerpe pvnaalldfl s
//
LOCUS       WP_357689783             194 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357689783
VERSION     WP_357689783.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 194)
  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..194
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..194
                     /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=20825
     Region          10..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpkiqaatva ehrasqraal ldaartllse hpeqipglae vaqhaglars svysyfksra
       61 dmfdalvtdt fprwsayvek rmeaagtpgq kiqayvdsnl qlvargdhal aralasagss
      121 ealasssrlm hdrleaplra altdhgssdp vrvaelvqsi vyalsrmieg glaldkatsl
      181 arellspyld rdsr
//
LOCUS       WP_357689797             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357689797
VERSION     WP_357689797.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=19943
     Region          1..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 mprvglnqqt vvreaarlad evgfgqltla alatrlgval pslykhvrga dalaqklaal
       61 ataelatemt naavgrsggd alramanayr dyahrhpgry patqrvpdpa dpehveager
      121 avgavvavlr gygltgddav datralrsal hgfvtleaag gfglprdvnr syqqliasmd
      181 isfrswpgtg a
//
LOCUS       WP_357689795             266 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Micromonospora parva].
ACCESSION   WP_357689795
VERSION     WP_357689795.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   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 266)
  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..266
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..266
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=28257
     Region          1..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 mttsqvrrds ghiayevrge gplvvlahgm genrasfrhl vpllvaaghr vasvdvrghg
       61 qssvgwptya paevgkdlla vvrdldagpa vlvgsssaaa avvfaatdap elvtgivqig
      121 afvgqpklnp mlrmamwsvl hsprlfgmfh ntlfpvrrsa ddaayrrsmv anlrepgrma
      181 atrgviapae phwtarapqv rqpvlvlmgs kdpdfpdpga earaarrlfg taearmiees
      241 ghyphadqpq rtaeellgfl avcaga
//
LOCUS       WP_357689835             269 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Micromonospora parva].
ACCESSION   WP_357689835
VERSION     WP_357689835.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..269
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28759
     Region          15..266
                     /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 madtllddvg dllweaadqv vlplfrkldd ddvsekapge vvtvadrrae elltaglrrl
       61 rpgsmvvgee gvaddpgllr hlrdggdvwl vdpvdgtanf aagrrpfalm vsllsngrps
      121 agwildplad tlaagwaeeg tllngrpvdg agavpplgel rgaamtkflp setrdrvrag
      181 grrlgellpg lhcagreyld iltgeqqfvl fwrtlpwdha pgtllvraag gvarrfdgvd
      241 yhpaddgrgl lvaaneqvwa evhdalltt
//
LOCUS       WP_357689836             419 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357689836
VERSION     WP_357689836.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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 419)
  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 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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..419
                     /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=44607
     Region          51..169
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msapvvdvwg pvapgprasf ppapephdew slaggtawvy ysplnrrqlv rpvilsdgfs
       61 sgssnldqlw ngleengdyr fvselhatgr dviilgyddr tasitdnadt aidcirraia
      121 ervgrakltv ggfsmgglvt rfalakmeqd pelpdhetsv ylsydtphrg awlpislqaf
      181 thfatdnwgd tdglgpvlrq fsgllnspaa kqmarwhiek vgdtpkqare rvaflqalde
      241 lggwprnlrk igvangvdtg tgngvkadat avkcngatmn dtwlktqaqg eqvvarlqkt
      301 geeptsvrtn glpdidgapg glftlasptg dtgsfglaal lmallgntvd pdvistscfi
      361 psisaaaagd indpkalyrp itpdhselda ftcagrnegh ttmteelgaw ivneivatg
//
LOCUS       WP_357689853             161 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA polymerase sigma factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357689853
VERSION     WP_357689853.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 161)
  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..161
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..161
                     /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=17632
     Region          <2..152
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 madeiandtg kivlerwdrl rgedvakpgp praylfktat hlwhrrgpre tiwasglvdp
       61 hdpgaeaasg svlasldlse vladrqaahg vvhrtlnlld ipkrqvlwlr haeefdtret
      121 aailripsgt vktrlaaavh qfkdivlasg alqetgwglt r
//
LOCUS       WP_357689879             110 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357689879
VERSION     WP_357689879.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=11410
     Region          15..104
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mccapiarqp lggdetaela vllkavadpv rlrllsmigs haggeacvcd ltgafdltap
       61 tishhlkvlr tagligserc gtwvyywiip dqvarlgalf tplavpavtg
//
LOCUS       WP_357689883             115 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357689883
VERSION     WP_357689883.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=12066
     Region          22..111
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtetttssaa tadatagatc apqlpqaaqd flkalanpsr qqiillftqg aelsvnqvae
       61 ragisqsaas qqlallrrgg ivasrrdgre vlyrgdrdgv arilgdlqny lkfcc
//
LOCUS       WP_357689992             189 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxymuconolactone decarboxylase family protein [Micromonospora
            parva].
ACCESSION   WP_357689992
VERSION     WP_357689992.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..189
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20269
     Region          37..175
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msflrqaers pdtermfdtd tkamgylpny trlfahnpav ylawqqlnga vkdgmelrry
       61 elvtlaaara lkssycglah gkflrdkffd aptvaaiasd hgsavlsaqe vavvnfagkv
      121 aadatsvtea dvaglrahgl ddtdifrvil tvgarcffst vlsaagaepd pqyqesldad
      181 lrqalsfgg
//
LOCUS       WP_357690041             175 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357690041
VERSION     WP_357690041.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 175)
  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 175)
  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 175)
  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 175)
  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..175
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..175
                     /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=19077
     Region          20..175
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 mndvrtldgs gpvevavgde gdlpgivdll ndvaansias fdtrpirvde rrawferfss
       61 agpyrllvar rdgqvvgyac sqryrdhdaf retvelsvai dagcrglgvg tslyralfes
      121 iadepihvav vgiampndas valhrkfgft evgtfheyaa kngqyisslw merll
//
LOCUS       WP_357690089              63 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Nonomuraea].
ACCESSION   WP_357690089
VERSION     WP_357690089.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..63
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..63
                     /product="helix-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=7310
     Region          5..63
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 msrrdelltv pevlaelggv srrtfyrwre lgrapvciql pnlelrvwrs dlmawldsrr
       61 eaa
//
LOCUS       WP_357690133             146 aa            linear   BCT 28-DEC-2024
DEFINITION  GbsR/MarR family transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357690133
VERSION     WP_357690133.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 146)
  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 146)
  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 146)
  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 146)
  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 146)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (residues 1 to 146)
  AUTHORS   Rosinski,J.A. 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 146)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..146
                     /product="GbsR/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=15614
     Region          1..146
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 mtetdsfvta vgdllaswnl phatgrtygl llvtdeplsl daigdelrls kgavstavrq
       61 lvswglarti prpgsrrlvv eaaggiesll eagharartl igtlrqgrel aqtpatrerl
      121 dsvvglfesy vavgedmlar hresrp
//
LOCUS       WP_357690156             242 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357690156
VERSION     WP_357690156.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24334
     Region          4..242
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mapvtvitgg grgigaatar rlaaaghhva lcyrrdeaaa tavladlhaa gvqaiavrad
       61 ttdpeqvral fdaaaelgpl tglvnnagvt sligpftelr vedlrrvvdv nlvgyvlcaq
      121 qaarrltdgg aivnvssaaa tlgspgeyvh yaavkaatdt ltvglakela pkgirvnava
      181 pgivrtdiha dsgvpdrads avgriplgra gepdeiaaai awllgpdasy atgtvlrvsg
      241 gl
//
LOCUS       WP_357690250             462 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357690250
VERSION     WP_357690250.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 462)
  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..462
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..462
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=49258
     Region          24..>82
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 maetrhtaet spqmlaavas qeygavvrla rrrlgltqeq lgartgysaa tisrfetgqq
       61 llhdigtlri lvrelrippa wlglsplepg lgvaegrsvs liaaksaamv erdqagedes
      121 vqrrqfllgv tgltgaalia gqgepadatt mvrrlerllt sdvheaevsg felaralata
      181 qrrfaacqyn evsaslpslv saakaaaves ngsraredal vrladsyllm selavkinqd
      241 dmgwvaadra leaakasgqp iavarasrai aiamrrqgrh esavnvltra alnleieaap
      301 ptaarlstys allctasyac aqgnkrhdal dlieeaqrta grvphdaqse gtpaainvsi
      361 yrigihnalg epgtalehar avnprllpts erharfcidt araweqfgdr dravqallva
      421 eraapqeirr psiaskhalc grpcagraas tggswrhhva rm
//
LOCUS       WP_357690327             338 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357690327
VERSION     WP_357690327.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11468491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..338
                     /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=37375
     Region          2..335
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mattgerile vrdlvkhfpl tqgivmkrsi gaikavdgvs fdlnrgetlg ivgesgcgks
       61 tlakvlmale rptsgsvkik grdiamargs elkrmrrniq mvmqdpytsl nprmtvgdiv
      121 gepydihtev apkgdrrrkv qellevvgln pdhinryphq fsggqrqrig iarglalqpe
      181 iivcdepvsa ldvsiqaqvi nllerlqnef nlayifiahd lsvvrhisdr vavmylgkvv
      241 elgkdaeiyd rpahpytqal lsavpvpdpe greqreriil qgdppspanp psgcrfrtrc
      301 wkaqeicate epllqirpgt qhesachfae thdvvhvg
//
LOCUS       WP_357690451             368 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357690451
VERSION     WP_357690451.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 368)
  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 368)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..368
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39627
     Region          41..357
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mrknnddpvr gpssvglivv vggygavgrv taktlgewfp gqvvvagrdl sraervarss
       61 egalkamrvd vndlqdverm vygaaivvmc vergneavar tclsqgvhyv disasapvle
      121 sierldalav sraatavlsv gvapgltnvl arrcverlps aervdinlfl gmggdhgvds
      181 vrwivehlte pgdrhrsdvk harvrlpevg lrtvypfpfs dqytvsdvlg vrattricfd
      241 salttsaifa lramgffplm rrlraapllt sllsrlhfgs drfvvhalas daegmvvsst
      301 avgretcdat givaayvarv lytgtapggv lhidqlvsad lfldelerhw itvhhkeaep
      361 aaqnrrgr
//
LOCUS       WP_357690328             284 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Micromonospora parva].
ACCESSION   WP_357690328
VERSION     WP_357690328.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 284)
  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 284)
  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 284)
  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 284)
  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 284)
  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..284
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..284
                     /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=27902
     Region          109..>283
                     /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 mavqtglgep rgpwfispel dpdgrgwwda perdpggrrp rrllaalavv vlstisgava
       61 ggvvagrdga ggpaaasaap vpaelvtaae rtvpgvvsvl aggassgsat gsgfavddqq
      121 hlitndhila kggggpvtve lpdgrrfaae vvgreprsdl avlkvpasag ltplplakpg
      181 atrvgepvla vgsplglagt vtagivsald rqvrlgnnrh savqtdasin pgnsggplvn
      241 argevvgvnt aiatidgngs igigfaipid qvqqtadtii gkgg
//
LOCUS       WP_357690419             311 aa            linear   BCT 28-DEC-2024
DEFINITION  GlxA family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357690419
VERSION     WP_357690419.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 311)
  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 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   3  (residues 1 to 311)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..311
                     /product="GlxA 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=33140
     Region          2..311
                     /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 mhtvavlald svvpfdlatp mevfqrtrlp dgragyrvlv caatptvtag afsmavpwgl
       61 dvlvdadtvv vpgvsdpaaa tpaavldslr aaaangaria sicggaftla atglldgqra
      121 tthwlatdrl atehpriqvd pnvlyvdngq fltsagaaag ldlclhlvrr dhgaavaaat
      181 arlsvmpler aggqaqfith eppaadgatl eplltwmrdn sqreltladi arhaglstrt
      241 lnrhfrdqig tsplrwlhrv rvhqaqhlle ttvhpidrva tqvgfgstta frdcfkritg
      301 tspqayrrsf r
//
LOCUS       WP_357690477              72 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357690477
VERSION     WP_357690477.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 72)
  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..72
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..72
                     /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=7204
     Region          <1..70
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mtvvaasggi fflslalktl dvgvgytiwt gigsigtvit galifkekit ipkvisfaai
       61 vagavilrla vv
//
LOCUS       WP_357690486             336 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357690486
VERSION     WP_357690486.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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 336)
  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 336)
  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..336
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..336
                     /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=36086
     Region          11..333
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mlagalllaa vwvfllryvp dgwpallyea pnrilllgaf apaaaavmaf llvfgllggw
       61 ilagrmlapl tritdatrma angslshrir lpgradefre ladafdamlv rleahvaeqq
      121 rfaanashel rtplaisral ldvarrdpdr digelverlh avntraidlt eallmlsrad
      181 qrsfarervd lslvveeave tllpltkkrg vtietsgeit pvegsqalll qlatnlvhna
      241 ivhnlsvqgt vwiktgigpe altventgek lspevvpalt epfqrgtgri rndhagvglg
      301 laivksitha hdgtltivar ptgglsiavq lpackr
//
LOCUS       WP_357690601             106 aa            linear   BCT 28-DEC-2024
DEFINITION  GroES family chaperonin [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357690601
VERSION     WP_357690601.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 106)
  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 106)
  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 106)
  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 106)
  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..106
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..106
                     /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=11796
     Region          8..93
                     /region_name="Cpn10"
                     /note="Chaperonin 10 Kd subunit; smart00883"
                     /db_xref="CDD:197951"
     Site            order(9,11,14,45..46,58,68,73,75,91..93)
                     /site_type="other"
                     /note="oligomerisation interface [polypeptide binding]"
                     /db_xref="CDD:238197"
     Site            25..38
                     /site_type="active"
                     /note="mobile loop [active]"
                     /db_xref="CDD:238197"
ORIGIN      
        1 mlepkfeiqm lhdrvmirle qaseerrsgs givipatvkl anrlawgevc gvgsnvrsvk
       61 vgdkvllnpe dqfevelhaq vylvmrerdl havatqetdh gtglyl
//
LOCUS       WP_357690650             449 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora parva].
ACCESSION   WP_357690650
VERSION     WP_357690650.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..449
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..449
                     /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=48837
     Region          7..395
                     /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 msaapphvli igagtgglcl ahglrragit vavyerhrdr aegllgyrvg igptgsralr
       61 eclppdlfat flatcarpph yfnvvtqglr qtasfalrps ddpvrtehsv armvlrqvll
      121 tgledvvhfd ktftryeqrd dgtvtahfad gstatgdllv aadgthsavr rqylphavtr
      181 dagtiniatr vpltphtrsl ipervqqgis lifgvggmmg vlhvmefkwd aeraikpgvs
      241 eadaallrsw pglahdtttd ninliiwsaa nrfpadvmqr rgqelvqval dltanwhphl
      301 relltradpa salpikvsts epvppwksst vtmlgdaiht mtpgrgvgan talrdarllc
      361 eqlsralagd ktlvqavady eavmapygfa rvaeslnrsg tngddrmyrp vvgrlallga
      421 rgyfgvtsrv prlrrrfvdd fhtyegdrd
//
LOCUS       WP_357690671             141 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357690671
VERSION     WP_357690671.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 141)
  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 141)
  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..141
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..141
                     /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=15110
     Region          2..124
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 melrqlqqsf dafdeaaaar lglnrtdlrc ldvvladgpv pagqlslalk lspaatttvi
       61 drleragmvs rspdpgnrrr vlvaatdaah saeaeiffpv gqagaqalqe ygpdelaiil
      121 dflrcarrvq eeqtarlral s
//
LOCUS       WP_357690701             531 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357690701
VERSION     WP_357690701.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 531)
  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 531)
  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
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..531
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=57334
     Region          38..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mstsvptegg pptppsaerr drslvelldd lpalddttvv hstagtlsya elraavsrva
       61 aeltragvgp ghpvgalvgs gmtgvvamfa vwtvgavfmp inrrgtgrev adlvadtpvc
      121 lllgtaedld rqsaelgdlg mveldetaws aavrrpmtap artydndial vlrtsgttgk
      181 pkavllrhrs tidaldsslr klrrrgpgpr etrrtirvnl iplslalwag ifntlfslra
      241 gfgvvlldrf tppafalair thrlkstvla pamitmlcds leidtleple ivrsitapls
      301 patarrfher fgvlvlnsyg qtelggevvg wtiedirgfg teklgavgrp yddvdlrild
      361 endqdvapge lghihvrspf rmrgyagadg ssgpqdddri vdgflrtgdi grldadgflw
      421 iegrvsdmin rgglkvfpde veevlrrhps vrdaavagvp drrlgevpya wivpqsgevd
      481 avalaawcre hlapykvpvv faevetmprs dvgkllrrel nvtvpppevt l
//
LOCUS       WP_357690782             264 aa            linear   BCT 28-DEC-2024
DEFINITION  spermidine synthase [Micromonospora parva].
ACCESSION   WP_357690782
VERSION     WP_357690782.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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..264
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..264
                     /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=28039
     Region          17..214
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mnraadrlel vadpvrrtgr tllsdgveqs yvdvedprhl hfeyvrrias avdvaapaga
       61 plsvlhlggg altlprwlaa trpgspqrvv erdaavvelv arelpplppq vrvevadard
      121 altatsagry dlviadiyra armprhvrtv efaaevaral hpdglylvnv tdlpplvgtr
      181 vqvatlravf advcvvgdrr mlrgrrygnl vlaatsrpgg lpvvrlavaa lrdpvpggll
      241 hgaaldtfva gahpvtdadg tsgr
//
LOCUS       WP_357690800             322 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-ketoacid dehydrogenase subunit beta [Micromonospora parva].
ACCESSION   WP_357690800
VERSION     WP_357690800.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Costelloe,S.J., Ward,J.M. and Dalby,P.A.
  TITLE     Evolutionary analysis of the TPP-dependent enzyme family
  JOURNAL   J Mol Evol 66 (1), 36-49 (2008)
   PUBMED   18043855
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
  TITLE     Crystal structure of 2-oxoisovalerate and dehydrogenase and the
            architecture of 2-oxo acid dehydrogenase multienzyme complexes
  JOURNAL   Nat Struct Biol 6 (8), 785-792 (1999)
   PUBMED   10426958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414334
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..322
                     /product="alpha-ketoacid dehydrogenase subunit beta"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34437
     Region          1..315
                     /region_name="AcoB"
                     /note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
                     complex, dehydrogenase (E1) component, beta subunit
                     [Energy production and conversion]; COG0022"
                     /db_xref="CDD:439793"
ORIGIN      
        1 mprlsyrral traladelar deavfllged vqvgasmvtt glakrfgadr vrdtplseqa
       61 ftsfatgaal aglrpviefq ipsllflvfe qivnhahkfp lmtggqcsvp vtylvpgsgs
      121 rtgwagqhsd hpyslfahvg vvtvvpatpa daygllvtai rhddpvvvfa paaamdvrdd
      181 vddltpvplg rgrihrfgdd vtvvaighlv hdalavaeel adqvsvevfd prtlypfdid
      241 gliesvtrtg rlvvfddgnr scgmaaeiia svlervrlla pprrvtrpdg avlpfapald
      301 ravqpgrdnl ataihltvkd ss
//
LOCUS       WP_357690879             385 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357690879
VERSION     WP_357690879.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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 385)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..385
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..385
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41071
     Region          33..366
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrqilavaag lvvlaasacs aptaprsats psatptgpav lpaptgdhpv gttilyvndt
       61 srpdpwnldv qtrelkvtlw ypteqedger apymtpkese lflrgseiag vpsdtlsktr
      121 tnaiedaepa geklplvvls pgftnpmitl tslaedlasr gyvvagidht yenyatifpg
      181 grvaeclacd sdtdpgfgtr vvqgraadvs fvldqlpskw dgaslidrsk iamagqsmgg
      241 asamaamlkd srvragidmd gttyaripks gfsrpfmflg spqhtpgsrd nswdrdwkll
      301 tgwkrwlvls gaehqsftdg plmagalgvk paygvlpaar vaeltrtyva afldqhlksk
      361 rqplldkpss rypevkfcpa tcgqs
//
LOCUS       WP_357690947             375 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora parva].
ACCESSION   WP_357690947
VERSION     WP_357690947.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Wintjens,R. and Rooman,M.
  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 375)
  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..375
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..375
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41300
     Region          13..>52
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mrgpgrsvph rgevtgylfk liresipltq eqlavdldvd rvtvqswesg rrpftavplg
       61 qaiavrrrlg rlgantllla alddaaeadl ilatvlteqv drcevaehpl gwsvlthrlt
      121 dlilwavlgq tptfarglpi arprrgpvas gptlpvdeqr affahlhvla draaagrhrn
      181 vllhrqacfl agmdptkaaa gwltqttara rrtitfrtws plwpdarsvv tslanqgdpe
      241 plrdfiarah pddacqraal nysaywvgei pyrhrddsfm petladwhgs lllrhlvhrl
      301 dpghpfvdln ihnvwallaa rrglaldnpa ttralldrsa plldsdrisa qsrqeltsiv
      361 yslradgltg tgtgk
//
LOCUS       WP_357690981             446 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Micromonospora parva].
ACCESSION   WP_357690981
VERSION     WP_357690981.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=47804
     Region          1..336
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkrrrilatv amlavgtgla acssdeggsd asnctntitk kdlpvvtmwg wypntqlvvd
       61 nfnkannevq vcwtnvgqgg deydkfqtai sagtgapdvi mveadriptf qiqgalvdik
      121 qygydavkan ysegawkdvs vgdavygvpv dggpmgmiyr kdifdkykvt ppktwaeyeq
      181 aaqkvkdagg plfgdfganv pavlmalqiq kgatpftfdp sqpkaigvkl ndqaskdvld
      241 ywgglakkgl vgtqnqftpe yisgvingny atyisaawap gyltgagvgk gqdtgkfava
      301 plpqwdlanp vqvnwggsaf svtkqakkpe laakvaygly adkesltdgw tnqiifplnl
      361 talkdpafvd lkvaffggqq ankevyvpaa dayqgvqyap fgqyyldame kqvsevikgs
      421 itgsqaadrl qedvakyake qgftvq
//
LOCUS       WP_357690983             713 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Micromonospora parva].
ACCESSION   WP_357690983
VERSION     WP_357690983.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..713
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=76941
     Region          70..361
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
     Region          413..713
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mrrrlsaaft agviataavl lapqpaaadt pwldvsedry asftvpaayv qeklgtvsqv
       61 vvegnfgpsa swaefgltrr gdvwsgvlga lepglynyql taddtltikd ptnstgvasd
      121 pllstflvag dsarwlvdap agtggkietl tyrtgnaqrs avvwtppgya akgpkgypal
      181 flqsgagvaa tdwldlgrsk qildnlsaag amspmvvvmn nadvsdakev kdlrkavtdt
      241 yrvlrdpahq aiagvsdggt qalraaltkp gqfahvgwfs gssapeidrk darainrsvk
      301 llrlytgnvt dpaynatyrl tkaldradvr fefdgvnpdg ganwttwqen lvdfvprlfr
      361 dvrdhgpspg hqplkreftp ppagttptpf vtedgfvtfe tttdftaaqh vtvwanvapg
      421 gswlrlplkr dggrwratvg plkpwfyyyr livdrvavkd tsnptkvtte pmwstffipg
      481 pgarllsdvp agqggtvesm tysstvagqd rtalvwtppg ydpgreqpyp vlylqhgggq
      541 nytdwvemgr akqildhqfl dgdltpmvvv mgngnssnfn relrenivpt arsryhissd
      601 psqqalagls mgggqafgvl kaypgefayv aafsagfgss tgvdaaainn gtkmlrvyvg
      661 dqtdfvypsf maslttmdnl giryefdgvt pgphgwdvwq knlidlaprl fkr
//
LOCUS       WP_357691119              64 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357691119
VERSION     WP_357691119.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=7283
     Region          1..56
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mttrpntllt iaevldeidv pkstfyrwlh tgrgprslkl pngkrkvrrc dldvwlttfe
       61 qtaa
//
LOCUS       WP_357691142             327 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora parva].
ACCESSION   WP_357691142
VERSION     WP_357691142.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 327)
  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..327
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..327
                     /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=33934
     Region          10..>89
                     /region_name="MDR"
                     /note="Medium chain reductase/dehydrogenase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cl16912"
                     /db_xref="CDD:450120"
     Region          65..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(66,68..69,129,133,153..158,177..178,182,192,
                     209..210,212,232..233,259..261)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mnreayacwv repgaaeirp vslaapgpde vlvrarysgv srgtetlvfs ggvpadqyaa
       61 mrapfqegdf pgpvkygyls vgvveqgpae llgrtvfclh phqsayvvpa tavvpvpegv
      121 paaravlagt vetavnalwd aaplvgdrvt vigagmvgcc vaallarfpg vqvelvdtda
      181 rragvagalg vdfanpadar gdrdlvvhas ataaglqqsl dllapegtvi elswygdrpv
      241 qvslggafhs grltvrssqv gmvaparrgr rsyadrlala ldllddpafd alitgasrfa
      301 elpdvlarls sgdlpalchl ityddge
//
LOCUS       WP_357691162             115 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357691162
VERSION     WP_357691162.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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=12068
     Region          27..111
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maetttppga ptdatagtac apqlphaaqd flkalanpgr qqimllfaqg aelsvnqvae
       61 ragisqsaas qqlallrrgg ivtsrrdgke vlywgdrdgv arilgdlqdy lkfcc
//
LOCUS       WP_357691182             107 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357691182
VERSION     WP_357691182.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 107)
  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 107)
  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 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   4  (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
REFERENCE   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..107
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..>107
                     /product="helix-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          11..>93
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mdvasgderg ttervltllg llqqrqvwtg peladrlgvt prtvrrdver lrtlgysvha
       61 sqgvgggyql gpgqdlppll lddeeaiata vsllagagga vagagda
//
LOCUS       WP_357691191             402 aa            linear   BCT 28-DEC-2024
DEFINITION  YeiH family protein [Micromonospora parva].
ACCESSION   WP_357691191
VERSION     WP_357691191.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..402
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..402
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=41650
     Region          55..397
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 mtadatrtgd epgttdvtrv gdapadvaep gtspdpagpt svvrdgafwa wtavgllivv
       61 glaaltrfle qnvpawaegt avedigaaie ypvyaillgl lgnvvvtvlg wrdriaaafr
      121 teffiktglv llgasinlav iasaagpaia qaillisgvf lftwwlagrf glddklrall
      181 asavsicgvs aaiaaagavr arreqlayta slvivfalps ifilpwladv fglsdavaga
      241 wiggnidtta avtaagalag eealqiasiv kvtqnalmgv vavaltayft lrverrpgaa
      301 rpglgelwtr fpkfvlgfia asviatwyld atgadgkati aivndlrvwf lilafvsigl
      361 evrvaslrea gwrpvavfas atvfnlalal glasvlfrnf sa
//
LOCUS       WP_357691262             430 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357691262
VERSION     WP_357691262.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 430)
  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..430
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=45263
     Region          194..423
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrplvsgaty rrgvhlllgg vlllpyllva fllvqmftlp dapygllvlv lalvvvigvv
       61 ppflrgtral eiaaarallg valpdppvta esgrearetr lraalwfalh lvaggvvall
      121 iliplvmgvt fvvqwfgiag gsldglrigp ldeydtgwls llgvamlagv lyavaglgal
      181 aavmapvllg pspaeriaal eartarlaer nrlarelhds ighaltvtml qasaalqlld
      241 sdpefargal qaieetgraa tedldqvlgm lregeradep grqraghrtd erggaradga
      301 prhglgdldr lvahsrgtgv evdteiegsv ddlpalvsre gyriiqeslt nvlrhagpvp
      361 vtlrvavdgp mltievsnpv aasrprregg hglkgmrerv tllggtvatg pdgdrwrvsv
      421 rlpalegdas
//
LOCUS       WP_357691303             102 aa            linear   BCT 28-DEC-2024
DEFINITION  putative quinol monooxygenase [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357691303
VERSION     WP_357691303.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 102)
  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..102
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..102
                     /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=11621
     Region          2..86
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mfglmvrftc kddtsatafd qlvtetieai rrhepgtlvy ashrvdgrpl qrifyelyrd
       61 raafdaheqt ehtrhflaar edllasvevd wldlqtgkgv tp
//
LOCUS       WP_357691308             280 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Micromonospora parva].
ACCESSION   WP_357691308
VERSION     WP_357691308.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 280)
  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 10167525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..280
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=28206
     Region          3..147
                     /region_name="SRPBCC_5"
                     /note="Ligand-binding SRPBCC domain of an uncharacterized
                     subfamily of proteins; cd07823"
                     /db_xref="CDD:176865"
     Site            order(3,5,7,16..18,20..21,33,41,43,45,47,62,64,74,76,
                     91..92,94,96,106,108,110,112,126..130,132..134,136..138,
                     141)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176865"
     Region          <146..>244
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mkitnefava vpierawavl tdleglapcl pgaqltgvdg dvfrgrvrvk vgpvisefag
       61 tarfvekdda ayhgvidakg rdarstgnas alvtaqlrpd gdrtlvsvdt dlkisgklaq
      121 vgsgmikevs gkllaqfvan leaklaadqs aapppatdse paappsvasp earpaastta
      181 vattpttaav apspiapspi epspiepspi epsaeastwv stpgsssves sdgstraaaa
      241 epealdllsi aggsitkrlv pvvvgvvalg aviawlvarr
//
LOCUS       WP_357691318             268 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora parva].
ACCESSION   WP_357691318
VERSION     WP_357691318.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..268
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28950
     Region          5..>68
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          95..264
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mttvarptrp lgdllrewrr trgmsqldls ieagvsarhl sfvetgrsrp spdlilrlae
       61 qldiplaern tvllaagyap aypshqltdp elaplraavr qildghgpyp avlvnrqwhl
      121 veanpavalf tagadprllv ppvnvlrltl hpggmapriv nlaqwrghll grlrqqvlat
      181 ddaalsalle elrgypdgdd apapegdtls rvviplryrh gdrelsfvst ttlfgtpldv
      241 tvsglaveaf fpadpvtrat lhalgtva
//
LOCUS       WP_357691347             105 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357691347
VERSION     WP_357691347.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 105)
  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..105
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..105
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11453
     Region          37..>87
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mtkyarwkdi raehveragg eeaveagkqe llakaqgrrl aeirrsrgmt qqdiaqrmgv
       61 tkgrvsqieq gkisgqdvla ryatalggql hqsiyfddgd iaaia
//
LOCUS       WP_357691355             294 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora parva].
ACCESSION   WP_357691355
VERSION     WP_357691355.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11449257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..294
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32178
     Region          12..292
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msdgrvavgq aavdqllevl dldptgemtf rgmsppvgpq rvyggqvagq alvaagrtvd
       61 perfvhslhg yfvrpgdpve pieyqvenir dgrsfsvrra valqhdkpif fmsasfqrae
      121 egldhqvtap ldvpmpqdvp tmsdrlaryp erlgiwgqip rpidvryvge pgwvrpgdrp
      181 adphqrvwmr idgklpddpl lhacaltyas dltlldsvls ahgevwgpgg lvgasldhal
      241 wfhrpfrade wflydclsps asgarglatg rmfttdgrqi asavqegllr rvga
//
LOCUS       WP_357691390             195 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357691390
VERSION     WP_357691390.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 195)
  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..195
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..195
                     /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=20826
     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 mdfagsspgl tstkivvagg fgvgkttfvg avseimpltt eavmtdasvg iddlgmtplk
       61 stttvamdfg rvsldrdlil ylfgtpgqhr fwfmwddlvr gaigavvlvd trrladsfpa
      121 idyfeeaqlp fvvgvngwdg qyphsdgevr daltlaphip lirldarskd svksalinlv
      181 ehaltvrmav pgwsg
//
LOCUS       WP_357691423             190 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357691423
VERSION     WP_357691423.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 190)
  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..190
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         1..190
                     /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=21007
     Region          21..187
                     /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 madaaetglk ivvvggfgvg kttlvrsvse irplnteevm tqagvgvdet dgvdaktttt
       61 vafdfgrisl nerivlylfg apgqerfwfl wdrlfsgtlg avvlvdtrrm ddswyaidrl
      121 ehhgtpfvva vnrfdddhvh sldeirkala lpehipmidc darvrrsskn vlitlvdhlr
      181 tmaiarettp
//
LOCUS       WP_357691434             598 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Micromonospora parva].
ACCESSION   WP_357691434
VERSION     WP_357691434.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 598)
  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..598
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..598
                     /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=60031
     Region          11..262
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(11,35..36,65,70,75..78,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,103,140,142,
                     144..145,147,157..158,161,178..181)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(18..19,21..24,26,39,41,73,94..97,101,142,144..145,
                     147,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(22,101,103,140,142,144,161,178..181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(157..165,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <282..488
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <393..517
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
ORIGIN      
        1 mltrgvllgd ryrlgervat ggmgavwrgt dvllerevav kvllpslvad pefttrfrae
       61 armlaalrhp gvvpvhdvgq avlddgsqvd ylvmeyvege plsarvravr rldpattmsv
      121 laqaadalht ahlagivhrd vkpgnllvka dgtvvlvdfg iarsrhmagl taanmvlgta
      181 symspeqatg qpvsaatdvy algavayfcl agqppfhgdn plavalrhaq edpaalpadt
      241 ppavaavvar alakrpedry gsaaelaaaa adardatlas ipvsarppwa laaptpgvaa
      301 saaspvplpa aapavaapap aapgappaap vsagpaalra pasvaaeptt apkptredal
      361 pggltgrrlp llvgagavvl valavavtvv alrpetkpgs adqppalage saavtdappp
      421 padatttapr psttpgasrt atadpsgspv dasasgdpar tpvqgdppta ttssrptpsr
      481 tpssrpnpyt aaqacgsgyq vidsatltgg dgqrkgrvfl lyhagtgtnc vvtlkdtavg
      541 aksaasayle vqgrtrstds gsfdyyagpv rasaagtcvr wggstggvsy gsgfehcd
//
LOCUS       WP_357691458             186 aa            linear   BCT 28-DEC-2024
DEFINITION  GntP family permease, partial [Nonomuraea sp. NPDC048916].
ACCESSION   WP_357691458
VERSION     WP_357691458.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Peekhaus,N., Tong,S., Reizer,J., Saier,M.H. Jr., Murray,E. and
            Conway,T.
  TITLE     Characterization of a novel transporter family that includes
            multiple Escherichia coli gluconate transporters and their
            homologues
  JOURNAL   FEMS Microbiol Lett 147 (2), 233-238 (1997)
   PUBMED   9119199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457667
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         <1..>186
                     /product="GntP family permease"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          7..>170
                     /region_name="GntT"
                     /note="H+/gluconate symporter GntT or related permease,
                     GntP/DsdX family [Carbohydrate transport and metabolism];
                     COG2610"
                     /db_xref="CDD:442022"
ORIGIN      
        1 gtvqksaavs viesgmggil ghvaiiiglg tmlgailevs ggaevlsarl lnafgekrap
       61 lamgmtglvf gipvffdvgi fvlapivyaa akrsgksill yampllagls mthaflpphp
      121 gpvaaaglfn vslgwvilmg ivvgipsvia awgyaawigk rifvdvpqdm veaaeeakaa
      181 vaaeqr
//
LOCUS       WP_357691572             138 aa            linear   BCT 28-DEC-2024
DEFINITION  3-dehydroquinate synthase family protein, partial [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357691572
VERSION     WP_357691572.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Carpenter,E.P., Hawkins,A.R., Frost,J.W. and Brown,K.A.
  TITLE     Structure of dehydroquinate synthase reveals an active site capable
            of multistep catalysis
  JOURNAL   Nature 394 (6690), 299-302 (1998)
   PUBMED   9685163
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         <1..>138
                     /product="3-dehydroquinate synthase family protein"
                     /EC_number="4.2.3.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003856 - 3-dehydroquinate synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          1..>137
                     /region_name="AroB"
                     /note="3-dehydroquinate synthetase [Amino acid transport
                     and metabolism]; COG0337"
                     /db_xref="CDD:440106"
ORIGIN      
        1 pnaeeaktve vaaycwkalg qtgftrtdvi vgigggattd vagfvaaswl rgvrwiaipt
       61 tvlgmvdaav ggktgintae gknlvgafhp pagvlcdlaa ldslpvndyv sglaeiikag
      121 fiadpailel ieadpqaa
//
LOCUS       WP_357691577            1075 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Micromonospora parva].
ACCESSION   WP_357691577
VERSION     WP_357691577.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1075)
  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 1075)
  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 1075)
  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 1075)
  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..1075
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..1075
                     /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=116191
     Region          6..1068
                     /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 mvrtgrasfa qerlyfldql qpgnpayvva favhlrgalr pealrtavtr vvarhdalrt
       61 tfavvdgvlt qrvssapavd vditadgwvd ratqeahlrt lvaeqarqpf dladgpvvra
      121 flrswgpdeh glavlvhhia cdgwsvglll rdlaaeydat vdgsvaayde paesylayae
      181 rqhetwrrds sgldfwraal vdaprlalpt dfprpsvlgt tgavlrrpve pelvrrlgew
      241 grargatlfa vtlaayasvl sryarqdevv vgvpvanrmd daeerlvgcl vntlpirldv
      301 sgrpsftelv drarrtsmaa fanqdvpfeq ivratvgerq lshaplfqts ltvqnfpfaf
      361 pefagvrlte vdveidvtkf dlgltldvst dvpflraeys telfteetvg rllthyltfl
      421 rsivdeeqre psmvdeaera qltegmnppl astpvthpsv lrrfadhaaa tpdavavrhr
      481 dveityaeld rwagriaagl adrgvrpgvr vglllgrspa vvaailgvwk lggvyvpldp
      541 dyprqrleli aanagmavlv vdpetaeaaa altrdsgtpl adahtldgvs vleetfpgpd
      601 dpayviytsg stgvpkgvlv ghggldalns ptpagldvta advwlaassf sfdasvwemw
      661 galttgarlv iadrvdlvdr erlarlvrre avtvlfqtpg alyrllppyl laleedetsr
      721 iryvvlggea lswsrlasli adapdlrtvf vnmygitegt ihvtifqasa advprvpega
      781 igvplpsarc yvldedlrpt glnvpgelyc ggalvahgyl dnpeltearf ppdpygggvm
      841 yrtgdvvkwg ldgsmvylgr ndtqvqlrgy rvelaevega llthpavrsc avaaeddelv
      901 afvvhgigpd aehdlrahvr etlpaymvps riltvatipl tahgkvdlpg lladsraart
      961 atapsrppaa vvgtgleeri racwvevlrr pdvglhdnff dlgghsfali alqqrmseeg
     1021 ldvsvtdlfr cgtiagcaaa lqhtapvvad pnaaqrrrgr alladrrrsv gagrg
//
LOCUS       WP_357691627             152 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora parva].
ACCESSION   WP_357691627
VERSION     WP_357691627.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora parva"
                     /db_xref="taxon:1464048"
     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=16686
     Region          1..124
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mrrdddldra aiwqdfvlaa hllevalerq sqrdgnishg hfkllvllsa aenqtvglka
       61 lagmlrfsps rvshtlnvle rqnlvtrgrv ptgrrayeat ltsqgrllva rvlraqraei
      121 rdvlldslga adaaalgris arvvrvfdev ea
//
LOCUS       WP_357691631             334 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Micromonospora parva].
ACCESSION   WP_357691631
VERSION     WP_357691631.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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..334
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..334
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34979
     Region          48..>172
                     /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 marhlvatgq lidedpaeal ahalaarrla srisavreav glaayhagew qsaiaelrty
       61 hrmsglqshl avladceral grperaidlf rgadrekldq avaielliva agargdlgqk
      121 daavamlqvp dltseatvpw tarlryayad allavgrrde arewfsraad vdtegetdaa
      181 erlleldgvv iegddedeaa eeiaagpgap gavparpdad ltgddedddd qdvddddddq
      241 dddadfddda dfdddeedaa vgrpgddegf ddededrhls gsgnadagta gdsgvtsgda
      301 anrdaanrdv akgdtanaag tlpaggdesg stqr
//
LOCUS       WP_357691668             115 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein, partial [Nonomuraea sp.
            NPDC048916].
ACCESSION   WP_357691668
VERSION     WP_357691668.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC048916
  ORGANISM  Nonomuraea sp. NPDC048916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Nonomuraea sp. NPDC048916"
                     /db_xref="taxon:3154232"
     Protein         <1..>115
                     /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]"
     Region          <7..115
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 ehvglsiaef ralvdqeypk vehplvkrdp asgrqylyga peymdsvvgf danenaeffa
       61 lldsliqdpe rvythrwttd dlvvwktett yhaatavapd avrtvhrvsi daaep
//
LOCUS       WP_357691674             217 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora parva].
ACCESSION   WP_357691674
VERSION     WP_357691674.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 217)
  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 217)
  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..217
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..217
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22047
     Region          77..217
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrisrtwtta gqlrrwtgag pvrrgataaa lvvallgvaa ctgtapggpt aagsapavaa
       61 ptatppspta sptggpqaap aqvpdvlrft gttlggaafd aaqlagkpvv lwfwapwcat
      121 casqawtvae iapkyrdtvp ivgvaglger kamkefvtef eldgtpqied skgvlwkrfk
      181 vteqsifvvi drsgavvhqg fldgealtak vaalaga
//
LOCUS       WP_357691677             393 aa            linear   BCT 28-DEC-2024
DEFINITION  saccharopine dehydrogenase family protein [Micromonospora parva].
ACCESSION   WP_357691677
VERSION     WP_357691677.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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..393
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..393
                     /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=41937
     Region          4..391
                     /region_name="COG3268"
                     /note="Uncharacterized conserved protein, related to
                     short-chain dehydrogenases [Function unknown]"
                     /db_xref="CDD:442499"
ORIGIN      
        1 mavertydvv lfgatgftgg ltaeylgrha paglrwalag rnpqrlaavr drlvaidpgl
       61 adlplltadv tdadslrava ersrvvastv gpyihhgepl vaacaragtd ylditgepef
      121 vdlmyvrhha eatrtgarlv hacgfdsvph dlgvwftvrq lpadvpitvd gyvraggrfs
      181 agtyhsalta fsrtgqasra arerravepr ptdrrvravp grlarsaelg iwtvplptid
      241 pqvvrrsaaa rpeygpdfry rhfaavkrlp tvlvgaaglg alvglvklpp srrwllgrla
      301 sgqgptaqqr asswfrvrfv gtgggrrvvt evaggdpgyd etakmlgesa lclaldelpp
      361 tagqltpvaa mgdalldrlv ragltfrvle rpa
//
LOCUS       WP_357691704             182 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Micromonospora parva].
ACCESSION   WP_357691704
VERSION     WP_357691704.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 182)
  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..182
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..182
                     /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=18865
     Region          2..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mradakrnyd livtaaseai ardgayasle eiarsagvgs atlhrhfptr wsllqavfgg
       61 cvhnlaarag dlldasdald alttwlhevt ayatttrgla dsllnepaee setcgatlva
      121 agepllrrav degsvrpdit madlmilang islaaqsmga akaeqlltla lqgigsavrp
      181 qp
//
LOCUS       WP_357691747             534 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Micromonospora parva].
ACCESSION   WP_357691747
VERSION     WP_357691747.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..534
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..534
                     /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=57723
     Region          <8..>99
                     /region_name="mnmC"
                     /note="bifunctional tRNA
                     (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase
                     MnmD/FAD-dependent
                     5-carboxymethylaminomethyl-2-thiouridine(34)
                     oxidoreductase MnmC; cl40718"
                     /db_xref="CDD:424349"
     Region          61..533
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 msdqtqsmvs rrgflrtvgi sggagamlat mgamglapsa easvtpafrp persdftltg
       61 rsgasvvvlg ggiaglttay elgkagyhct ilearhrvgg rnltirggdv etdldgrtqr
      121 agfsdgvyfn agpgriaqwm ltmdycrelg vpvevftnqn adawiynesa gmtapvryrt
      181 akadvygyvs ellakatdqg aldarlsted rerllsflqs fgaiggrssd waytgtnrrg
      241 fsaypgagnd vgtplgtppa lsdvfasnig ryfsfefgyd qamlmfqpvg gmdqiprala
      301 ravgarrirl naevtgvtdr gsrvevtyrq ngrqsqitad ycvaalpphl marvphnlgt
      361 avtaaladfp vtasgkigle yrsrwwetdq riyggitetd ldlshiwyps ygfhgkrglv
      421 vgyyntgana raysgltpeq raeravsqgv kihgekyrse lvtsyshawd rtryiegawt
      481 sprygtagyn lllqpagrvy fagdwlshev awqhgafvaa rsavsalhqr vmag
//
LOCUS       WP_357691808             297 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Micromonospora parva].
ACCESSION   WP_357691808
VERSION     WP_357691808.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 297)
  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 297)
  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..297
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..297
                     /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=31581
     Region          <164..291
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mltktpgrrr rslpalllav pvflatsvam atpasaapid npsleipvgc pgaraviqve
       61 wegtrtakvh weltdtssdg ksplikiaar ddsgngrswv frndevvfgv dggygasasg
      121 ggmswdpagi aqfnhlevkv sngtsaqgte csvtkktyny trlayqyaln qdgkpyvlga
      181 dgpdafdcsg lvkfayervv nfpgwggvrs saqqydwars easnnnadlt nlksrdairv
      241 srsqlkvgdl vfydghvgqy agggqlysam tpasgigyms vdfkpplgyy rmvgvtg
//
LOCUS       WP_357691817             523 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora parva].
ACCESSION   WP_357691817
VERSION     WP_357691817.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 523)
  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 523)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 523)
  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..523
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..523
                     /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=55758
     Region          128..383
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrilhsalpg wphrrrrlll dvllwtvvaa pvgyaeaspp ytrytlpllv gkllllaaav
       61 vasrrqplvs lvlavlgslv dgnfvfaipv fsylagrrsa tvgpaimvfv litaggtaln
      121 lgllgtgaat wfllasvllf aavfpwlvgr yrrqqqeltd agrrhvdavt reqrgaaeri
      181 rlrerariag emhdslghdl slialraaal evaadlddrh raaagelras vsaaterlhe
      241 iigvlreeag aslrpsgesv adlvdgarea gmavrldaap vvadlpamtg haahrivrea
      301 ltnaaryapg apvdvritrd gdrievtvvn dappagplpa ppsqgsglla laervrlagg
      361 rldaghradg gfavravlpa tastpeaigs aaetgptaws derpgpaerp vdaerrlhda
      421 rrrvrrsllv alvapvgfal vlsfvyypva tagtvldrat fdqlrvgapr selvglprrq
      481 lerpvaadra gceyytdgnf plaeptwrlc ftdgrlvske wia
//
LOCUS       WP_357691897             376 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Micromonospora parva].
ACCESSION   WP_357691897
VERSION     WP_357691897.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..376
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..376
                     /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=40697
     Region          3..311
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mrnryldllr slaivrvvvy hvtgwatltl vfpamsvmfa lagslmaasl trsgpaavgr
       61 rlrrllpslw vvavvfvpam lftglpvspr vllwlfpvad ppanhwgala lsviwylrdy
      121 lwfvfaspva fwlfrraplp tllapylllv mievgiypap pvlrefglyf gawllgfahh
      181 agmlrrlssw llyplalala vgggawivgh pgprgydlnd nhlgnalwsa afilivlgra
      241 pagvswlnrs rlaeravtvl nrraltvylw hmpfvvaltp lvdvvgwshq dpvglairvl
      301 lvfalvglvt lavgwvedva arrrpelipg gsaqpadeav qpdgdtsdga gttsgravvp
      361 aqrvageeps vtlnag
//
LOCUS       WP_357692004             405 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Micromonospora parva].
ACCESSION   WP_357692004
VERSION     WP_357692004.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora parva
  ORGANISM  Micromonospora parva
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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
REFERENCE   2  (residues 1 to 405)
  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 405)
  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 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 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Micromonospora parva"
                     /db_xref="taxon:1464048"
     Protein         1..405
                     /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=41581
     Region          11..391
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mfdatamttv dtqavhagrd dlralgvhvp pidlsttnpl psvddggaay eqlatggtlp
       61 adgsavyqrl wnptvarfes alaelegtaq avafasgmaa ltatllaaar ddrrhvvavr
      121 plyggtdhvl atgllgttvt wahpdevaaa irpdtaliiv etpanptldl vdiaalaaaa
      181 gdipllvdnt vatpvlqqpa rhgatlvlhs atksigghgd vlagvvacdd twavrlrqvr
      241 avtgailhpl ggyllhrglq tlplrvraqq ataeklagwl adhpaihrvh hpsvhdpaal
      301 vgrqmagpgs llafevrgga paaatvagac hlithavslg gvdtliqhpa slthrpvegd
      361 akpaaallrl svgledpedl radlaqaldt iarpvrtsgr rggpg
//
LOCUS       WP_357692166             716 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Micromonospora sp. NPDC023814].
ACCESSION   WP_357692166
VERSION     WP_357692166.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC023814
  ORGANISM  Micromonospora sp. NPDC023814
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11601498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Micromonospora sp. NPDC023814"
                     /db_xref="taxon:3154596"
     Protein         1..716
                     /product="serine/threonine protein kinase"
                     /calculated_mol_wt=74692
     Region          28..288
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(28,52..53,86,91,96..99,111)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(35..36,38..41,43,56,58,94,110..113,117,119,156,158,
                     160..161,163,173..174,177,194..197)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(35..36,38..41,43,56,58,94,110..113,117,158,160..161,
                     163,173..174)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(39,117,119,156,158,160,177,194..197)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(173..181,190..197)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          328..>587
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
ORIGIN      
        1 mtqiptwsgg pvsppngrat pgttiggrys lrsavgnggm gtvwratdtl lrrdvavkev
       61 vlppglapsd rdamyertlr earaaaaiqh pavvqvydvv tegdrpwivm elldarslad
      121 mviedgpvaq rvvakigial lgalevahai gvlhrdvkpa nvlicadgrc vltdfgvarm
      181 ptdvqlttpg mvlgsphfis peramgqefg ppsdlfslgv tlytavegrp pfdkgdpiet
      241 mhavvedppa ppqrsgpltr vlmgllekdp arrldvhtar amlrellagp ltsnaaavns
      301 mtdpysivpv qqrplpappa aqpeqpkptg qiggramlnp gesltdrlaa lrrgerpaqa
      361 alpaspaame dtsadalagp lhtptgampa pgtpapagrt yggpeatpqv agsdatqqlr
      421 tnaaglvgfg gqpdatqrmg agapafgqpd atqrmsagap vfggqpeatq qlggtygggq
      481 wsvpgtgqpw atpatapaaa ggglagrvga ignqvvgtvk gwprkvqlaa agglavvlli
      541 gavvlftggd daptvpqaap tsaapagnap emkehsgkgv rvmvpqgwer ksagnwvdyv
      601 dpqdegrkvr ilvedfrtts irwaevaedg lknrskscvk pyaqlamnem ewvgkqaaef
      661 eytcgegetk rhgvwrgvvh dgkaysfylt stdakfaesk pifdemvktf qltdag
//
LOCUS       WP_357692289             292 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [unclassified
            Nonomuraea].
ACCESSION   WP_357692289
VERSION     WP_357692289.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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..292
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..292
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33614
     Region          1..203
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mlvsigmpvr ngadhleaav rsvlaqehae ievvisdnas tddteelcrl lakedsrivy
       61 hrqerdlhvv dnfeevlrrs rgrffrwmgd ddrleptyvs ralepfqdde rlilvttevt
      121 ytwldgtvhe prylgtrlls ddpvdrleel cevwaaqhlr ldplyglmrr ervaavprpr
      181 miredevfaa rlaltapwgh vpeplahrhl rerrlsaias mlgvpawtar fattlqfrai
      241 healggmels aeqrgrarav lmraywrrqr kmlahrgrkl agmatravts kr
//
LOCUS       WP_357692352             197 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Nonomuraea].
ACCESSION   WP_357692352
VERSION     WP_357692352.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 197)
  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 197)
  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 197)
  AUTHORS   Rosinski,J.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..197
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..197
                     /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=21675
     Region          8..87
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          101..175
                     /region_name="cupin_XRE_C"
                     /note="XRE (Xenobiotic Response Element) family
                     transcriptional regulators, C-terminal cupin domain;
                     cd02209"
                     /db_xref="CDD:380339"
ORIGIN      
        1 meqqsridat laqvgarlrh lrtergvtla alaeatgisk stlsrlesgq rrpslelllp
       61 iaeahqvpld elvgapevgd prvrlkpvvr ngrtvlpltt qpgplqawks vipadqkrpq
      121 pvthegyewm yvlsgrvrli vgdhdlilgp geaaefdthl phwfgpagdq pvevlnlfgr
      181 qgermhmraq prsrqps
//
LOCUS       WP_357692359             207 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Micromonospora sp. NPDC023814].
ACCESSION   WP_357692359
VERSION     WP_357692359.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC023814
  ORGANISM  Micromonospora sp. NPDC023814
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  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 207)
  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 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 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Micromonospora sp. NPDC023814"
                     /db_xref="taxon:3154596"
     Protein         1..207
                     /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=21520
     Region          68..182
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mpesptaaap rtspptdaev yaalhadava tlerweptgp aaaeardrtv rllaagpvam
       61 srahraghvt asalvldatg srvllclhgk frkwvqlggh cepadrtlag talreagees
      121 giaglridpv pidvdihpvn cqggslhydv rfavlappaa tervsdesea lawfppdqlp
      181 eplaggtakl vapalatlrr aplrpap
//
LOCUS       WP_357692363             334 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora sp.
            NPDC023814].
ACCESSION   WP_357692363
VERSION     WP_357692363.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC023814
  ORGANISM  Micromonospora sp. NPDC023814
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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 334)
  AUTHORS   Rosinski,J.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..334
                     /organism="Micromonospora sp. NPDC023814"
                     /db_xref="taxon:3154596"
     Protein         1..334
                     /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=35537
     Region          13..237
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          261..326
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlkiyfsaed ilrtrvapaa dpvwelvlsl hllpgrgrdp llagwrrsvt ralrqgvgsp
       61 glrlllslnp prgyfpdflt phqsvsgfea gmeavrstpv sllqrdlsll atghtlpaga
      121 aalargepdt lrdltgamaq yrdlaidpyw ariqaavead rsrraralld ggvegllasl
      181 rpamhwesgv lqvrgyphsr elhldgrgll lvpsffcapt pvalldpalp pvlvypvdrl
      241 ggllptpaeg agpgtpdtgr ealaallgrt raavlavsdd gcttgevarr lnispaaasq
      301 httvlrnagl lvshrdrntv lhtltplgra mlns
//
LOCUS       WP_357692368              90 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea sp.
            NPDC047529].
ACCESSION   WP_357692368
VERSION     WP_357692368.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC047529
  ORGANISM  Nonomuraea sp. NPDC047529
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Nonomuraea sp. NPDC047529"
                     /db_xref="taxon:3155623"
     Protein         1..90
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9430
     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 mryrrlsgpg aaeaydaarl afelgravrr mpesrgwsqs dlaraadmtq savarleggg
       61 tvpmlpvler laraldaetg gaissrspat
//
LOCUS       WP_357692376             458 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Micromonospora sp.
            NPDC023814].
ACCESSION   WP_357692376
VERSION     WP_357692376.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC023814
  ORGANISM  Micromonospora sp. NPDC023814
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..458
                     /organism="Micromonospora sp. NPDC023814"
                     /db_xref="taxon:3154596"
     Protein         1..458
                     /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=48649
     Region          27..411
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mryqdlsywl stvdepltpr ppltgdaead vvivgagytg lwtayylava dptlritvle
       61 aqvagygasg rnggwcsalf ptslpalarr hgrdaaiamq ramhatvaev grvvaaegid
      121 cdwayggtvv lartgpqldr araavaeara yglgpedlal ldadeatarc aadgvrggty
      181 tphcaavhpa rlvrglarav errgvtiheg trvtrirpga avtlagtvra pvvvrategy
      241 tpglpgqrra vapvyslmva taplpaatwa riglaeretf sdhrhvivyg qrtaddrlaf
      301 ggrgapyhfg srvspghdre pavfaalrrt lgelfpvlgp dvpvthtwgg plgvardwaa
      361 svgfdradgl awaggyvgdg vgtsnlagrt ladlirgert dltalpwvnh rspkwepepl
      421 rwlavnaglr lmfsadaaen rtdrparrat lltrllgh
//
LOCUS       WP_357692451             467 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative quinol monooxygenase [unclassified
            Nonomuraea].
ACCESSION   WP_357692451
VERSION     WP_357692451.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 467)
  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..467
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     Protein         1..467
                     /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=49867
     Region          363..451
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 meilvavial agallaavat galirrlrde pegwliawtv aagalclsla vvaigsvlgf
       61 gpvtfriyqv tgsllaplwl avgliqlmad kvpprflawl fgialtvvsv ailtfdplrs
      121 tdlgkklpsg salwglipdk lligvhaidv lvllacvvva alkwrggdey dtdnlhavlv
      181 iapssialvg amrfavpplf ttallavgsa aiwytvlrpl apyedddede leaphddreh
      241 rpgrraapep vpaaepppva pprrspglgd lvaeyragdq qvdyaarmga apdtgpatgy
      301 imngsppprm dtsprmeppp qrpdysmpgt gvaypgaelf spsqpqpqpq pqqgggrpap
      361 siyglltvft imdgagaafd rlaeatveav rrsepdtlvy achavksapl qrivyelyrd
      421 evayrdhqrq phverflner qamvlatnvi elnvnaakvv plptvmf
//
LOCUS       WP_357692463             261 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [unclassified Nonomuraea].
ACCESSION   WP_357692463
VERSION     WP_357692463.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nonomuraea
  ORGANISM  unclassified Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="unclassified Nonomuraea"
                     /db_xref="taxon:2593643"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26570
     Region          5..258
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mdlqlsgrva vvtgaskgig lavartlaee gvhvvaasrt apdakvthva vdlmdpqapa
       61 qviaraveef ggvdilvnna ggpppgvtlp rigfltpgdd dwqamfefnl fsavrmiraa
      121 vphlverggg sivnissgsa rqpgamnvdy gaakaamnhv skavseeygp qgvrvntisp
      181 gpvltdwwtk dggaadviag magaskddvi aqvapgmmkl atgrlvspqe iadmvallvs
      241 prsgsttgad iavdggflke i
//
LOCUS       WP_357692613             147 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Micromonospora sp. NPDC023814].
ACCESSION   WP_357692613
VERSION     WP_357692613.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC023814
  ORGANISM  Micromonospora sp. NPDC023814
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 147)
  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 147)
  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..147
                     /organism="Micromonospora sp. NPDC023814"
                     /db_xref="taxon:3154596"
     Protein         1..147
                     /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=15881
     Region          2..127
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtdetvdqls galgdlhrvl rraasqragr valpdaqvev lrlvqrqpgv gvreaaerlg
       61 tapntvstlv geltsagllh rdrdpvdrrt vrleltdaar eriaaygrhr rdllgaalag
      121 lddadrkall aaapalrrla drmtqqr
//
LOCUS       WP_357692633             320 aa            linear   BCT 28-DEC-2024
DEFINITION  complex I subunit 1/NuoH family protein [Micromonospora sp.
            NPDC023814].
ACCESSION   WP_357692633
VERSION     WP_357692633.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC023814
  ORGANISM  Micromonospora sp. NPDC023814
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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 320)
  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..320
                     /organism="Micromonospora sp. NPDC023814"
                     /db_xref="taxon:3154596"
     Protein         1..320
                     /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=34644
     Region          4..320
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 mplwlelvir vggvlvaflt lpllvgqaeh kvmahmqgrl gpmyaggfhg waqlvadgvk
       61 fvqkedvtpr eadravfrla pavalvpyll vllviplgpd dlvgqpldig lffvlavvgv
      121 gvlavlmsaw asankysllg glrgaaqllg yelplvlaaa svamaagtls lsgivaawqp
      181 wwllwqapam vvfflaglae irrppfdmpi adselvfgym teytglrfaf fllaeyvgiv
      241 viaalttvlf lggwqgpfad aqlgwlwtll kvfavsfvii wlrvsyprlr edqlqrlcwl
      301 ilvpvslgql vltaavrval
//
LOCUS       WP_357692644             219 aa            linear   BCT 28-DEC-2024
DEFINITION  C40 family peptidase [Nonomuraea sp. NPDC047529].
ACCESSION   WP_357692644
VERSION     WP_357692644.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. NPDC047529
  ORGANISM  Nonomuraea sp. NPDC047529
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 219)
  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 219)
  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..219
                     /organism="Nonomuraea sp. NPDC047529"
                     /db_xref="taxon:3155623"
     Protein         1..219
                     /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=22502
     Region          12..207
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 miaetglasi faaaaglmga vvlltvlagg arltatttat tcddtsppep lsaepcgqfp
       61 dvmpteglae rgviavlaal hmrgvpyswg ggnangpgfg idqgahtrgf dcsglaeyaw
      121 akagarigge tstqwdagvr vprsqvrpgd liffatapar patihhvgia idttrmvhap
      181 stgstvridt wagdpyrehe figiirpatt httasrttp
//
LOCUS       WP_357692645             502 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora sp. NPDC023814].
ACCESSION   WP_357692645
VERSION     WP_357692645.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. NPDC023814
  ORGANISM  Micromonospora sp. NPDC023814
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora sp. NPDC023814"
                     /db_xref="taxon:3154596"
     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=50712
     Region          8..372
                     /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 miderpgrsa lpgsgvpaer vlaelralrg adrpthggrl fayvydpavp gldelaaaah
       61 agsahvngld ptafpsllam enalvgaaar llgggpggaa pdavgsvtsg gteslilavk
      121 aardahpeia aprivvpasa haafakaahy lrvaldpvpv saatlrpaaa dvaaaigpet
      181 vlvacsapsy ahgvvdpvte iagvaaeagv rchvdacfgg wtlpylrrlg apvppfdfav
      241 pgvtsisvdl hkyayapkgv svllhrdpal rapqyfayad wpgytmvnpv iastrsggpi
      301 aaayatlrhl gddgylrlaa atrdavagla davravdglr lmaepestvv cltatdpgld
      361 lfvlvdelta rgwhtqpqla yadlppsvhl tvtaavaprv aefgpalada vaaaraagpv
      421 alpgellala ttltpdaltp dliaglaagl glgdlaptga dapagpvpgr tavvntllna
      481 appalrerll vefvgllqrp aw
//
LOCUS       WP_409928890             279 aa            linear   BCT 28-DEC-2024
DEFINITION  protease modulator HflC [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928890
VERSION     WP_409928890.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Bandyopadhyay,K., Parua,P.K., Datta,A.B. and Parrack,P.
  TITLE     Studies on Escherichia coli HflKC suggest the presence of an
            unidentified lambda factor that influences the lysis-lysogeny
            switch
  JOURNAL   BMC Microbiol 11, 34 (2011)
   PUBMED   21324212
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Bandyopadhyay,K., Parua,P.K., Datta,A.B. and Parrack,P.
  TITLE     Escherichia coli HflK and HflC can individually inhibit the HflB
            (FtsH)-mediated proteolysis of lambdaCII in vitro
  JOURNAL   Arch Biochem Biophys 501 (2), 239-243 (2010)
   PUBMED   20599668
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Briere,L.K. and Dunn,S.D.
  TITLE     The periplasmic domains of Escherichia coli HflKC oligomerize
            through right-handed coiled-coil interactions
  JOURNAL   Biochemistry 45 (28), 8607-8616 (2006)
   PUBMED   16834335
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     gene            1..279
                     /gene="hflC"
     Protein         1..279
                     /product="protease modulator HflC"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0098797 - plasma membrane protein
                     complex [Evidence IEA]"
                     /GO_process="GO:0052547 - regulation of peptidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31299
     Region          21..256
                     /region_name="SPFH_HflC"
                     /note="High frequency of lysogenization C (HflC) family;
                     SPFH (stomatin, prohibitin, flotillin, and HflK/C)
                     superfamily; cd03405"
                     /db_xref="CDD:259803"
ORIGIN      
        1 mknpvalgvi viaalfilln tivivpetrq gvvvqlgepk rivnryqsge afgetgagli
       61 akipffeqiv widkrirdve meqqqvlstd qlrlqvdafa rfritdplrm yiaagseerv
      121 sdelrpilgs alrnelgkrp faallsperg qvmdniqagl nrvarqygae ivdvrikrad
      181 lpdgtpldsa yqrmrtardq eartiraqga kqaqiiraea dasaartyae sfgkdpqfyd
      241 fyramksyet tfqdngengp qssfvlspdn eylrqfrgr
//
LOCUS       WP_409928892             377 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA 2-thiouridine(34) synthase MnmA [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928892
VERSION     WP_409928892.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Hagervall,T.G., Edmonds,C.G., McCloskey,J.A. and Bjork,G.R.
  TITLE     Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase
            from Escherichia coli K-12 has two enzymatic activities
  JOURNAL   J Biol Chem 262 (18), 8488-8495 (1987)
   PUBMED   3298234
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF001138.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK00143
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     gene            1..377
                     /gene="mnmA"
     Protein         1..377
                     /product="tRNA 2-thiouridine(34) synthase MnmA"
                     /EC_number="2.8.1.13"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=40702
     Region          18..364
                     /region_name="MnmA"
                     /note="tRNA U34 2-thiouridine synthase MnmA/TrmU, contains
                     the PP-loop ATPase domain [Translation, ribosomal
                     structure and biogenesis]; COG0482"
                     /db_xref="CDD:440250"
ORIGIN      
        1 mmdkidgnfq lgddlagkri vvamsggvds svvaalaart gaetigitlq lydhgeavgr
       61 vgsccagqdi rdaravadrl giahyvfdha srfkdsvmdv fadeymsgrt pipcvqcnmg
      121 vkftdllqls relgadclat ghyvrrvagp dgaelhrald pardqsyflf attqdqldyl
      181 rfplgdmpkt qvreiaedmg lavafkpdsq dicfvpngdy asvvrklrpd adddgeivhm
      241 dgtvmgrhkg lihytvgqrk gleiggqaep lyvirleped krvivgpkaa lavasaslrd
      301 inwiggdyag pvevkvrsms kptlarlegn elqfhnpefg vapgqaavfy hkdrvlgggw
      361 ivstaaveqq wlagvev
//
LOCUS       WP_409928894             135 aa            linear   BCT 28-DEC-2024
DEFINITION  MerC domain-containing protein [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928894
VERSION     WP_409928894.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10505067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     Protein         1..135
                     /product="MerC domain-containing protein"
                     /calculated_mol_wt=14150
     Region          23..130
                     /region_name="MerC"
                     /note="MerC mercury resistance protein; pfam03203"
                     /db_xref="CDD:427195"
ORIGIN      
        1 mfttakfwdr dglmvrdglw driavlvsgl clahcvatia fvallssagg mflnplvhei
       61 glgiaialgf falgrgvldh gyimpvavgs lglgmmmgai tlghesghdg revlytmlgv
      121 gllalahdln yrath
//
LOCUS       WP_409928895              86 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928895
VERSION     WP_409928895.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     Protein         1..86
                     /product="hypothetical protein"
                     /calculated_mol_wt=9199
ORIGIN      
        1 mleiavhysy ntvmfnlisi figlialvls figlvpllgw tnwlilpiag igalfgliss
       61 rtsgmnfcmi vmaicalrlw igggii
//
LOCUS       WP_409928897             202 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF4136 domain-containing protein [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928897
VERSION     WP_409928897.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10612716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     Protein         1..202
                     /product="DUF4136 domain-containing protein"
                     /calculated_mol_wt=22177
     Region          29..188
                     /region_name="DUF4136"
                     /note="Domain of unknown function (DUF4136); pfam13590"
                     /db_xref="CDD:463929"
ORIGIN      
        1 mapvallsla acatpfradv qrfvalpdtt gqsfavvaad pdlsgglefg qyamlveqkm
       61 lelgyqrsdd paaaelivsm dyeidkgrek vvadvdpfyp sarfggyyrr pgyrygfhdp
      121 flyggygfsg yngvrsftvy tteldmkidr aadgerlfeg kaealsrskn ltylvpnlve
      181 amftnfpgns gervrisiap ek
//
LOCUS       WP_409928899             364 aa            linear   BCT 28-DEC-2024
DEFINITION  branched-chain amino acid aminotransferase [Sphingorhabdus sp.
            SMR4y].
ACCESSION   WP_409928899
VERSION     WP_409928899.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF009897.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK13357
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     Protein         1..364
                     /product="branched-chain amino acid aminotransferase"
                     /EC_number="2.6.1.42"
                     /GO_function="GO:0004084 - branched-chain-amino-acid
                     transaminase activity [Evidence IEA]"
                     /GO_process="GO:0009081 - branched-chain amino acid
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=39708
     Region          6..362
                     /region_name="PRK13357"
                     /note="branched-chain amino acid aminotransferase;
                     Provisional"
                     /db_xref="CDD:237363"
ORIGIN      
        1 mknlefnlep satpvhaser krllenpgfg tlftdhmami rytesegwhd aritkrepim
       61 mdpassvlhy aqeifegmka yrladgatal frpeenarrf qasarrmamp elpeklflds
      121 vealvdidre wfpsveggsm ylrpfmfase vflgvrpake ylylviaspa ggyfksgasa
      181 isiwvsedys raapggtgaa kcggnyaasl vaqaeaiekd cdqvvfldaa ehkwveelgg
      241 mnlffvmddg rlitpplggt ilpgitresi itlareeglt vveapyaidq weadaasgkl
      301 vetfacgtaa vvtavgtvks adgeftigsg gpgqlterlr rrlvdiqrgv apddhgwvkr
      361 lfea
//
LOCUS       WP_409928901             244 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxine 5'-phosphate synthase [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928901
VERSION     WP_409928901.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF003624.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05265
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     Protein         1..244
                     /product="pyridoxine 5'-phosphate synthase"
                     /EC_number="2.6.99.2"
                     /GO_function="GO:0033856 - pyridoxine 5'-phosphate
                     synthase activity [Evidence IEA]"
                     /GO_process="GO:0008615 - pyridoxine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26414
     Region          5..243
                     /region_name="PRK05265"
                     /note="pyridoxine 5'-phosphate synthase; Provisional"
                     /db_xref="CDD:235380"
     Site            order(12,14..15,23,48,50,54..55,75,105..106,109,136,156,
                     195..196,217..218)
                     /site_type="active"
                     /db_xref="CDD:237977"
     Site            order(12,46,71,73,75,93,95,134,136,154,156,192,195,
                     212..213,215)
                     /site_type="active"
                     /note="hydrophilic channel [active]"
                     /db_xref="CDD:237977"
     Site            order(23,163..164)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:237977"
     Site            order(48,75,156,195)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:237977"
     Site            99..109
                     /site_type="active"
                     /note="active site lid [active]"
                     /db_xref="CDD:237977"
ORIGIN      
        1 msdanslrlg vnidhvatir narggdhpep vraalmaaea gadgitahlr edrrhirddd
       61 lsvlmeklti plnlemaatd emlaialrhq phaacivpen reertteggl daagqhnrlt
      121 dfvgqlkean irvslfiepd prqieaairl gapvvefhtg hyaevtgaer eaelrriada
      181 aalaakngie phaghgltfd nvvpiaaipq lkelnighfl igeaifsgld gsirqmrelm
      241 dear
//
LOCUS       WP_409928903             381 aa            linear   BCT 28-DEC-2024
DEFINITION  non-hydrolyzing UDP-N-acetylglucosamine 2-epimerase [Sphingorhabdus
            sp. SMR4y].
ACCESSION   WP_409928903
VERSION     WP_409928903.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00236.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     gene            1..381
                     /gene="wecB"
     Protein         1..381
                     /product="non-hydrolyzing UDP-N-acetylglucosamine
                     2-epimerase"
                     /EC_number="5.1.3.14"
                     /GO_function="GO:0008761 - UDP-N-acetylglucosamine
                     2-epimerase activity [Evidence IEA]"
                     /calculated_mol_wt=41486
     Region          10..380
                     /region_name="WecB"
                     /note="UDP-N-acetylglucosamine 2-epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0381"
                     /db_xref="CDD:440150"
ORIGIN      
        1 mtkktmtkak iltvfgtrpe aiklfpvvqa laernsldal tcvtaqhrem ldqvmdiadi
       61 rpdfdldlmk anqslddltg rllsgigkil detkpqrivv qgdtatamcg alaayyrqip
      121 vshveaglrs yniyhpwpee vnrkiigtia dqhfaptqts adalakenip vdqiyitgnt
      181 vidalldtvd kyndpssldr nlaglyekfs drkiigvtsh rrenlgdglt niasalrtia
      241 krddvalifp vhlnpkvrai mqdalggldn vamiepldyp nfvsllnhch fmmtdsggvq
      301 eeapalgkpv lvmrdtterp egveagtakl vgtdeavlva eacrllddea hylamarahn
      361 pfgdgtassq iadiiensls a
//
LOCUS       WP_409928904             263 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928904
VERSION     WP_409928904.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     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]"
                     /calculated_mol_wt=28686
     Region          75..224
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mkyyaaplgg qparlitgla aimlmmvplg ackrlpddde lraetarayp pasrpvsela
       61 gnqwstetar dkrgeaeeim kaaglepgmt vadigagegy ytvrlaekvg argrvlaqdi
      121 degaidrlae rvnresldnv siklgapddp rlpeksfdri flvhmyhevr epyaflsrlr
      181 paligkagdh gtgevivvdv nrdfsqhgip pkqlfcefea vgyelvgfme rpelggyfar
      241 frakgpaiap gdikpcpyqr dsg
//
LOCUS       WP_409928905             281 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphate ABC transporter ATP-binding protein PstB [Sphingorhabdus
            sp. SMR4y].
ACCESSION   WP_409928905
VERSION     WP_409928905.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Vuppada,R.K., Hansen,C.R., Strickland,K.A.P., Kelly,K.M. and
            McCleary,W.R.
  TITLE     Phosphate signaling through alternate conformations of the PstSCAB
            phosphate transporter
  JOURNAL   BMC Microbiol 18 (1), 8 (2018)
   PUBMED   29351743
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00972.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     gene            1..281
                     /gene="pstB"
     Protein         1..281
                     /product="phosphate ABC transporter ATP-binding protein
                     PstB"
                     /EC_number="7.3.2.1"
                     /GO_component="GO:0009898 - cytoplasmic side of plasma
                     membrane [Evidence IEA]"
                     /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:0015415 - ATPase-coupled phosphate ion
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30900
     Region          25..281
                     /region_name="PstB"
                     /note="ABC-type phosphate transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1117"
                     /db_xref="CDD:440734"
ORIGIN      
        1 mmnddltmqe asesmnmtdp attampgdas tpkmtarnvn vfygdkqain dvsidvnmdn
       61 vtafigpsgc gkstflrcmn rmndtipiar vtgeiqldgd diyapkmdvv qlrarvgmvf
      121 qkpnpfpksi ydniaygpri hglatskdel dnivesslqr aglwgevkdr lldsgtalsg
      181 gqqqrlciar aiavdpevil mdepcsaldp iatakieeli helrgkyaiv ivthnmqqaa
      241 rvsqktaffh lgtlveyddt tdiftnpree ktrdyitgry g
//
LOCUS       WP_409928906             200 aa            linear   BCT 28-DEC-2024
DEFINITION  XrtA/PEP-CTERM system exopolysaccharide export protein
            [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928906
VERSION     WP_409928906.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Steunou,A.S., Liotenberg,S., Soler,M.N., Briandet,R., Barbe,V.,
            Astier,C. and Ouchane,S.
  TITLE     EmbRS a new two-component system that inhibits biofilm formation
            and saves Rubrivivax gelatinosus from sinking
  JOURNAL   Microbiologyopen 2 (3), 431-446 (2013)
   PUBMED   23520142
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR03027.2
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     Protein         1..200
                     /product="XrtA/PEP-CTERM system exopolysaccharide export
                     protein"
                     /calculated_mol_wt=21467
     Region          34..200
                     /region_name="pepcterm_export"
                     /note="putative polysaccharide export protein, PEP-CTERM
                     sytem-associated; TIGR03027"
                     /db_xref="CDD:132072"
ORIGIN      
        1 maslavagcs gnssgpqlpp asfvsmqegp geeyvigpld eltifvwrnp elgakvqvrp
       61 dgrittplit dmpavgktpa mlaqdltlql sqyineplvs vivnnfsgtf sqqirvvgat
      121 ekpasipyra nmtlldamia vggmsefasg nrarlirfdr gtgkqqefal riddlmkkge
      181 tranvmlrpg dviiipesmf
//
LOCUS       WP_409928908             600 aa            linear   BCT 28-DEC-2024
DEFINITION  M2 family metallopeptidase [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928908
VERSION     WP_409928908.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Isaac,R.E., Schoofs,L., Williams,T.A., Corvol,P., Veelaert,D.,
            Sajid,M. and Coates,D.
  TITLE     Toward a role for angiotensin-converting enzyme in insects
  JOURNAL   Ann N Y Acad Sci 839, 288-292 (1998)
   PUBMED   9629165
REFERENCE   2  (residues 1 to 600)
  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 11117514
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     Protein         1..600
                     /product="M2 family metallopeptidase"
                     /EC_number="3.4.17.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008241 - peptidyl-dipeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=66464
     Region          22..600
                     /region_name="Peptidase_M2"
                     /note="Angiotensin-converting enzyme; pfam01401"
                     /db_xref="CDD:460196"
ORIGIN      
        1 malstpalak hhekdameet aaptaadaeq fvaeteqklf dfsidaariy winanfitdd
       61 tdalaakaga egttmsvnaa ieaakfndvk gldavtrrkl dklrggivlp apttdgaate
      121 lneiatklns aygkgkgtln deeingsdie aamgtnrnpe elaemweswh tnvgapmkdd
      181 yarmveianq gaqelgfadv gamwrsgydm paddfakltd klwaqvkply dqlhcytrdk
      241 lneeygdavq petgpiradl lgnmwaqewg niydivapeg agdigydtte llaandydam
      301 kmvkagegff sslgfeplpe tfyerslftk padrevvcha sawdidnkdd irikmcikvn
      361 gddfitihhe lghnyyqray neqsylhldg andgfheaig dmvalsitpe ylvqvgllda
      421 ekvpsadkdv glllrqamdk vaflpfgllv dkwrwqvfsg diqpdnytqa whdlkleyqg
      481 itppvdrpad afdpgakyhi pgntpysryf larilqfqfy kaacdeagwt gplhrcsfyg
      541 neqvgaklna mlemgaskpw pdaleaftgt remdgsamis yfaplmdwlk eenkgkscgw
//
LOCUS       WP_409928909             372 aa            linear   BCT 28-DEC-2024
DEFINITION  rod shape-determining protein RodA [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928909
VERSION     WP_409928909.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02210.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     gene            1..372
                     /gene="rodA"
     Protein         1..372
                     /product="rod shape-determining protein RodA"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /calculated_mol_wt=40195
     Region          15..363
                     /region_name="rodA_shape"
                     /note="rod shape-determining protein RodA; TIGR02210"
                     /db_xref="CDD:274033"
ORIGIN      
        1 mrlsdfipap iaqlpwktil llfvlasfgf vvlysaaggs ltpwaglhmv rftifvgmai
       61 vlsrfrenfw ktmafpiyiv vvlmllgvel igavgggsqr wlnlgvirlq pselmkvaii
      121 lavarfydll ppaqirtwga iwplfgllal pcalilmqpd lgttitvvtg altiaflagl
      181 plrlfiggaa avavlaplay ffaledyqqr rvttflnpen dplgagyhis qskiaigsgg
      241 lfgkgflngt qshldylpeg htdfvfatma eewglmggil vlfcffllfr wglgvamkak
      301 trfsqltaag mtvtiffyva inlmmvmgla pvvgiplpfm shggssmmti micvgilmsi
      361 ernpgrsgna fg
//
LOCUS       WP_409928910             408 aa            linear   BCT 28-DEC-2024
DEFINITION  TIGR03087 family PEP-CTERM/XrtA system glycosyltransferase
            [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928910
VERSION     WP_409928910.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR03087.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     Protein         1..408
                     /product="TIGR03087 family PEP-CTERM/XrtA system
                     glycosyltransferase"
                     /calculated_mol_wt=44056
     Region          5..399
                     /region_name="stp1"
                     /note="sugar transferase, PEP-CTERM/EpsH1 system
                     associated; TIGR03087"
                     /db_xref="CDD:274425"
ORIGIN      
        1 mmaeilflah rvpwppnrgd kirshhflqk lmdcaavhva cfaedeaerq agwerkeela
       61 scevvlrtks qwaggveail tgkpvsltcf dsadirayva qviatrpidc ifvfsgqmaq
      121 yipadfggrv vmdfgdvdsa kfesyaaegs gpmawinrre grmlrdfeka iaeradhalf
      181 vseaeaalfr qrsgltgdrv eavgngidle fygapdvhpe slghggpmil ftgqmdyqpn
      241 vqavqsfstq vmpailarfp darfaiagra ptdkvrqldg tngtivigav ddirswivaa
      301 dvvvaplria rgiqnkvlea mamarpvvas gcaaegidav ngehflvads vneeaqllcg
      361 llqnpdearr lgeraeqlih aryswqtqla glpalcglpn iaaagvaa
//
LOCUS       WP_409928911             900 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA gyrase subunit A [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928911
VERSION     WP_409928911.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF004043.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05560
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     gene            1..900
                     /gene="gyrA"
     Protein         1..900
                     /product="DNA gyrase subunit A"
                     /EC_number="5.6.2.2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003916 - DNA topoisomerase activity
                     [Evidence IEA]"
                     /GO_function="GO:0003918 - DNA topoisomerase type II
                     (double strand cut, ATP-hydrolyzing) activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006259 - DNA metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0006265 - DNA topological change [Evidence
                     IEA]"
                     /calculated_mol_wt=99039
     Region          1..856
                     /region_name="PRK05560"
                     /note="DNA gyrase subunit A; Validated"
                     /db_xref="CDD:235502"
     Region          512..559
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          562..612
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          621..667
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          671..719
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          759..807
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
     Region          810..853
                     /region_name="GyrA_CTD repeat"
                     /note="GyrA_CTD repeat [structural motif]"
                     /db_xref="CDD:293790"
ORIGIN      
        1 mktsymdyam svivsralpd vrdglkpvhr rilfaaqegg mvagrpyrkc akivgdvmgn
       61 yhphgdsaiy malarmtqdw smrvplvdgq gnfgsmdpdm pasmrytear lnkvsnflln
      121 dldkdtvdfi pnydgslqep svlparfpnl lvngaggiav gmatnipphn lgevvnasla
      181 yidnpaitid elieivpgpd fptaplilgq sgaraaykdg rgsimmrarh eieegrgdkr
      241 sivltsipfq igksalveki aeaakdkrie gvsdirdess ragvrvviel krdatpdvvl
      301 nqiwrftpaq ssfpanmlai rggrpevltl rdiiesfvkf reevitrrtk felnkarera
      361 hillglvvav tnmdevvrii rgsstpaear esllrrewpi aeiapyirlv eatetdvegd
      421 syklspvqvk aildlrlqkl talgreeigd elkelaaaie eylailadra klyavmreel
      481 eevrdqfatp rlseitaawd glededlmer semvvtvthg gyikrtpldt fraqrrggkg
      541 ragmatkeed avtelfvtst htpvlffsth gkvyrlkvwk lpeggpqtkg rpminllpla
      601 dgetistvlp lpedeaewad lhvmfatakg svrrnsmdsf tnvpsngkfa mkfdedsddr
      661 ligvklltdg ddvllatrng kairfagnav rsfqsrtstg vrgialkgdd evislsvlrg
      721 feasteerdq ylkaapwkdn enapelsaer maefsatedf iltvcangyg krssayeyrq
      781 sgrggqgiln idnikrngtv vasfrasdde qvmlvtdqak lirmkvadmr vigrnssgvk
      841 lfnvaqgehv vgaakideee ependaedav veemvdqgvs dgdvavtddt gdetpedsse
//
LOCUS       WP_409928913             113 aa            linear   BCT 28-DEC-2024
DEFINITION  nitrite reductase small subunit NirD [Sphingorhabdus sp. SMR4y].
ACCESSION   WP_409928913
VERSION     WP_409928913.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. SMR4y
  ORGANISM  Sphingorhabdus sp. SMR4y
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02378.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Sphingorhabdus sp. SMR4y"
                     /db_xref="taxon:2584094"
     gene            1..113
                     /gene="nirD"
     Protein         1..113
                     /product="nitrite reductase small subunit NirD"
                     /GO_function="GO:0008942 - nitrite reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=11738
     Region          6..104
                     /region_name="Rieske_NirD_small_Bacillus"
                     /note="Small subunit of nitrite reductase (NirD) family,
                     Rieske domain; composed of proteins similar to the
                     Bacillus subtilis small subunit of assimilatory nitrite
                     reductase containing a Rieske domain. The Rieske domain is
                     a [2Fe-2S] cluster binding domain...; cd03530"
                     /db_xref="CDD:239606"
     Site            order(48,50..51,67,70,72)
                     /site_type="other"
                     /note="[2Fe-2S] cluster binding site [ion binding]"
                     /db_xref="CDD:239606"
ORIGIN      
        1 mvdakwidig pveqlpalga rtlpvqggqe ivifrtatgg iyalankcph kggplsqgmv
       61 hdtsvtcplh nwrislltge algedkgcvp vipvkidagr iyidrtaala gav
//
LOCUS       WP_409928918             484 aa            linear   BCT 28-DEC-2024
DEFINITION  hydrogenase 4 subunit D [Yersinia frederiksenii].
ACCESSION   WP_409928918
VERSION     WP_409928918.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            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  :: HMM
            Evidence Accession :: NF005097.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK06525
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     Protein         1..484
                     /product="hydrogenase 4 subunit D"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=51936
     Region          7..484
                     /region_name="PRK06525"
                     /note="hydrogenase 4 subunit D; Validated"
                     /db_xref="CDD:180606"
ORIGIN      
        1 mnlaimenia latilipfag ailtaclpqr makwsctffa llatlgtvll ayaylgggkv
       61 dvtfnlihyg emalfgltid ristliafav vflgllvsiy stgyltlgnr ehphegtnry
      121 yalllvfiga maglvlsstl lgqlfffeit ggcswgligy yqsqrslrsa lkallvthva
      181 aiglylaaav llvntgtfal talaqldntt kiivfggilf aawgksaqlp lhiwlpdame
      241 aptpvssylh aasmvkvgvy ifaraiysag dvpqiigtvg mvmavitliy gffmylpqkd
      301 mkrllaysti tqlsyiffal slaiygsnla feggiayifn hafakslffl vagalsyscg
      361 trmlpklkgi mgkmpllgvg fcvaalaitg vppfngffsk fpifaagfsl shehwllipl
      421 lvlaliesva sfgwflywfg qtvpgkpsde vasakplpla mqgvlvilvi msvcssfiav
      481 awlg
//
LOCUS       WP_409928919             237 aa            linear   BCT 28-DEC-2024
DEFINITION  deoxyribose-phosphate aldolase [Yersinia frederiksenii].
ACCESSION   WP_409928919
VERSION     WP_409928919.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            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  :: HMM
            Evidence Accession :: TIGR00126.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     gene            1..237
                     /gene="deoC"
     Protein         1..237
                     /product="deoxyribose-phosphate aldolase"
                     /EC_number="4.1.2.4"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004139 - deoxyribose-phosphate aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009264 - deoxyribonucleotide catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25949
     Region          6..229
                     /region_name="DeoC"
                     /note="Deoxyribose-phosphate aldolase [Nucleotide
                     transport and metabolism]; COG0274"
                     /db_xref="CDD:440043"
ORIGIN      
        1 mnettkrmar lidlsavqat nteadvrhca elashyhiis vhvlpcwtrf lstllpeqgr
       61 advmiggpvg fpggghatdi kvqevrqliv dgarevdmvv nigkvlsgdy dyvredlrrv
      121 veaaapvpak vilethylne eqirkvcdia vdvgmawvkt stgwaptgat eekvaiiadq
      181 lrgriqikga ggirdlntvr vlyrlgvrrf gmsaaatqqv leqleqdpsl fpelndn
//
LOCUS       WP_409928921             382 aa            linear   BCT 28-DEC-2024
DEFINITION  lactaldehyde reductase [Yersinia frederiksenii].
ACCESSION   WP_409928921
VERSION     WP_409928921.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            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  :: HMM
            Evidence Accession :: NF007911.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10624
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     gene            1..382
                     /gene="fucO"
     Protein         1..382
                     /product="lactaldehyde reductase"
                     /EC_number="1.1.1.77"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40677
     Region          1..381
                     /region_name="PRK10624"
                     /note="L-1,2-propanediol oxidoreductase; Provisional"
                     /db_xref="CDD:182595"
     Site            order(8..12,171,214,243)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:341455"
     Site            order(37,95..97,138..139,142,151,160,179,187,194,198,261,
                     275)
                     /site_type="active"
                     /db_xref="CDD:341455"
     Site            order(194,198,261,275)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:341455"
ORIGIN      
        1 mnrmilnems wfgrgslaal tdeverrgyq kalvvtdkml lecgvanrll drlthagldf
       61 avfdavkpnp tisivqqgva afrhsgadyl ialgggspqd tckaigiiin npefadvrsl
      121 egvadtrqpc vpilaiptta gtaaevtiny vitdeerrrk fvcvdphaip avafidadmm
      181 dsmppalkaa tgvdalthai egyltkgawe ltdalhlkai evisrslras vkgeaaated
      241 malgqyiagm gfsnvglglv hgmahplgaf ynmphgvana illpyimryn aaftgerfry
      301 iamamgvena lnsplehvre ntieavialn rdigipssls avgmvaedip alaeaafadv
      361 ctggnprdat vdeikalyhq ac
//
LOCUS       WP_409928922             271 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Yersinia frederiksenii].
ACCESSION   WP_409928922
VERSION     WP_409928922.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..271
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     Protein         1..271
                     /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=29009
     Region          1..267
                     /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 mrtliknplt aigvaiigll lvvaffapwl athnpltqdl gnalqapssq hwfgtdefgr
       61 dqysrliyga rttlyivalv svtvgpigll lgvvagyfgg kvdsvlmrit difisfpslv
      121 lalafvaalg pglehvviai tltawppiar laraetlslr nadfvsavkl qgasplrils
      181 rhivplclps viiritmnma giiltaaglg flglgsqppd pewgamissg rrymmecwwl
      241 vtipglaill nslafnflgd glrdildprt e
//
LOCUS       WP_409928923             176 aa            linear   BCT 28-DEC-2024
DEFINITION  decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase
            [Yersinia frederiksenii].
ACCESSION   WP_409928923
VERSION     WP_409928923.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            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  :: HMM
            Evidence Accession :: NF006138.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK08287
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     Protein         1..176
                     /product="decarboxylating cobalt-precorrin-6B
                     (C(15))-methyltransferase"
                     /GO_function="GO:0008276 - protein methyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009236 - cobalamin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=18901
     Region          1..173
                     /region_name="PRK08287"
                     /note="decarboxylating cobalt-precorrin-6B
                     (C(15))-methyltransferase"
                     /db_xref="CDD:181354"
     Site            order(25..31,49..50,75,91)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mtkeavrvla larlelndar hlidvgagtg svaleaalqf phlrvtaier npaalelise
       61 nrqrlachnv diiagvapll vedhadaifi ggsggqltel idwalmmlnp ngrlvltfil
      121 lnnlndalsh lqtcavsqld cvqlqlsslt plgsghyfkp nnptylisch keachv
//
LOCUS       WP_409928925             128 aa            linear   BCT 28-DEC-2024
DEFINITION  EnvZ/OmpR regulon moderator MzrA [Yersinia frederiksenii].
ACCESSION   WP_409928925
VERSION     WP_409928925.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            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  :: HMM
            Evidence Accession :: NF007915.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10629
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     gene            1..128
                     /gene="mzrA"
     Protein         1..128
                     /product="EnvZ/OmpR regulon moderator MzrA"
                     /calculated_mol_wt=14412
     Region          9..128
                     /region_name="PRK10629"
                     /note="EnvZ/OmpR regulon moderator MzrA"
                     /db_xref="CDD:236728"
ORIGIN      
        1 mklkghfsrp iwqylilpvt alllavlllt piilrtesal kirpnqqgls lpdgfslyqh
       61 ldqrgiriks ivpekdslvv nlespeqqee aievlqdllp tgyvivsses krrhrllpaf
      121 rnnlqnvg
//
LOCUS       WP_409928927             639 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent copper receptor [Yersinia frederiksenii].
ACCESSION   WP_409928927
VERSION     WP_409928927.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Bhamidimarri,S.P., Young,T.R., Shanmugam,M., Soderholm,S.,
            Basle,A., Bumann,D. and van den Berg,B.
  TITLE     Acquisition of ionic copper by the bacterial outer membrane protein
            OprC through a novel binding site
  JOURNAL   PLoS Biol 19 (11), e3001446 (2021)
   PUBMED   34762655
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Yoneyama,H. and Nakae,T.
  TITLE     Protein C (OprC) of the outer membrane of Pseudomonas aeruginosa is
            a copper-regulated channel protein
  JOURNAL   Microbiology (Reading) 142 (Pt 8), 2137-2144 (1996)
   PUBMED   8760927
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Lee,H.S., Abdelal,A.H., Clark,M.A. and Ingraham,J.L.
  TITLE     Molecular characterization of nosA, a Pseudomonas stutzeri gene
            encoding an outer membrane protein required to make
            copper-containing N2O reductase
  JOURNAL   J Bacteriol 173 (17), 5406-5413 (1991)
   PUBMED   1885521
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR01778.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     Protein         1..639
                     /product="TonB-dependent copper receptor"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:0005375 - copper ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006825 - copper ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=69982
     Region          32..639
                     /region_name="TonB-copper"
                     /note="TonB-dependent copper receptor; TIGR01778"
                     /db_xref="CDD:273801"
ORIGIN      
        1 mvnsntdnhs dkkthdaevi tvtapqhspl tivtspktpr qpvpasdgad ylktipgfsq
       61 irnggtngdv vfrgmfgsri kiltdgaetl gtcpsrmdap tsyispesfd lltvvkgpqs
      121 vlwgpgasag tilfereqpr fdqagvkgna sllvgsngrw dknldtslgn eqgylrmmgn
      181 qsqagnykdg ngtrvpskwd kwnadialgw tpdtdtllef tagkgdgeas yagrgmdgsq
      241 flreslgarf qktnigevld kieakvyyny vnhimdnntl rtppmmamss nldrrtiggr
      301 vmgtwlwedl kleagtdlqt nthrknkqnt wqkdasfany glfgeltwtm seqdklitgt
      361 rldhnqvtny tradepsrsa tlpagfirfe hnladapvmw yaglghterf pdywelfspt
      421 fgptgstsaf dgvksekttq idvgaqysgk qlnswvsayl grvndfilfk ydpnnlrisq
      481 adninaiimg gemgagyafn dhwkadasla yawgentsnh rplpqipple arlgltfeag
      541 dwsstalwrl vssqhrvain egnvvgkdfa dsagfgvlsa nvaykvtkqv kvsggidnll
      601 nktysehlnl agnsgfgysv ntplnepgrt lwaklnvtf
//
LOCUS       WP_409928929             446 aa            linear   BCT 28-DEC-2024
DEFINITION  murein hydrolase activator EnvC [Yersinia frederiksenii].
ACCESSION   WP_409928929
VERSION     WP_409928929.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Nakamura,N., Hoshino,Y., Shiga,T., Haneda,T., Okada,N. and Miki,T.
  TITLE     A Peptidoglycan Amidase Activator Impacts Salmonella enterica
            Serovar Typhimurium Gut Infection
  JOURNAL   Infect Immun 88 (6), e00187-20 (2020)
   PUBMED   32284369
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF008644.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11637
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     gene            1..446
                     /gene="envC"
     Protein         1..446
                     /product="murein hydrolase activator EnvC"
                     /calculated_mol_wt=49449
     Region          15..446
                     /region_name="PRK11637"
                     /note="AmiB activator; Provisional"
                     /db_xref="CDD:236942"
ORIGIN      
        1 masdytpagn eerntplptq wgrrpwlaly asvfcagvll lpfsvnaada plaakttdnk
       61 nqlktlqqdi aekeksvqqq kqqrsslldq lkqqentiaq asrslrdtqg tlteldkdis
      121 klttsisklq sqqsqqqdml skqldaafkq gqhsglqlil sgeesqrser ilayfsylne
      181 arqksieele qtrtdlsaek ktleqkqnqq ktlldeqknq qqkleqarta rkktltslea
      241 slekdqqgla elrlnesrlr dqiakaerea karaereake aarvreqvka keqqakktgs
      301 sykpsesers lmartgglgr pgaqavwpvr gnvthrfges lqgelrwkgm visapegsev
      361 kaiadgrvll adwlqgyglv vviehgkgdm slygynqsal vnvgaqvkag qpialvgtsg
      421 gqgepslyfe irrqgqavnp qpwlgr
//
LOCUS       WP_409928931             524 aa            linear   BCT 28-DEC-2024
DEFINITION  YrIlm family inverse autotransporter adhesin, partial [Yersinia
            frederiksenii].
ACCESSION   WP_409928931
VERSION     WP_409928931.1
KEYWORDS    RefSeq.
SOURCE      Yersinia frederiksenii
  ORGANISM  Yersinia frederiksenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Wrobel,A., Saragliadis,A., Perez-Ortega,J., Sittman,C., Gottig,S.,
            Liskiewicz,K., Spence,M.H., Schneider,K., Leo,J.C., Arenas,J. and
            Linke,D.
  TITLE     The inverse autotransporters of Yersinia ruckeri, YrInv and YrIlm,
            contribute to biofilm formation and virulence
  JOURNAL   Environ Microbiol 22 (7), 2939-2955 (2020)
   PUBMED   32372498
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Wrobel,A., Ottoni,C., Leo,J.C., Gulla,S. and Linke,D.
  TITLE     The repeat structure of two paralogous genes, Yersinia ruckeri
            invasin (yrInv) and a 'Y. ruckeri invasin-like molecule', (yrIlm)
            sheds light on the evolution of adhesive capacities of a fish
            pathogen
  JOURNAL   J Struct Biol 201 (2), 171-183 (2018)
   PUBMED   28888816
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF040981.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Yersinia frederiksenii"
                     /db_xref="taxon:29484"
     gene            1..>524
                     /gene="yrIlm"
     Protein         1..>524
                     /product="YrIlm family inverse autotransporter adhesin"
     Region          40..470
                     /region_name="Ve_YrIlm_NTERM"
                     /note="YrIlm family inverse autotransporter adhesin
                     N-terminal domain; NF040981"
                     /db_xref="CDD:468911"
ORIGIN      
        1 mgwvtlllql lfplslsfsp aiaasistaa tgniievnia tetyilktne nvdtlskkyg
       61 lsvdelkkin hhrtfskpft altagdeidv prqrspfsvd nnsvksaetk iaryvadsat
      121 llsdentaks vqqmarstan nelnrsaqqw lsqfgtakvq invnndfkld gsaadvllpl
      181 adgqksllft qlgarnknsr ntvnvgigvr tfqnnwmygm ntfldnditg knrrvglgae
      241 awtdylklsa nsyfaltdwh qsrdfsddne rpangydira eaylpshpql ggklmyekyr
      301 gddvalfgkd drqknpdait agvnytpipl vtvgvehrag kgshndssfn lqlnyrlges
      361 wqsqinpsgv astrqlassr ydlvernnni vldyqkqdvi slslpeqisg dagtrvavia
      421 qvsskhaldr iewdyaalss vggglsmtsl qsaeiklppy qltssgsnty vlsavaydkq
      481 gnvsrpvtmq vtvlagsvsi taanltvtsd napanntatn svqa
//
LOCUS       WP_409928939             356 aa            linear   BCT 28-DEC-2024
DEFINITION  2-alkyl-3-oxoalkanoate reductase [Shewanella sp. MSW].
ACCESSION   WP_409928939
VERSION     WP_409928939.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. MSW
  ORGANISM  Shewanella sp. MSW
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Sukovich,D.J., Seffernick,J.L., Richman,J.E., Hunt,K.A.,
            Gralnick,J.A. and Wackett,L.P.
  TITLE     Structure, function, and insights into the biosynthesis of a
            head-to-head hydrocarbon in Shewanella oneidensis strain MR-1
  JOURNAL   Appl Environ Microbiol 76 (12), 3842-3849 (2010)
   PUBMED   20418444
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF042423.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Shewanella sp. MSW"
                     /db_xref="taxon:2569536"
     gene            1..356
                     /gene="oleD"
     Protein         1..356
                     /product="2-alkyl-3-oxoalkanoate reductase"
                     /EC_number="1.1.1.412"
                     /GO_function="GO:0003854 - 3-beta-hydroxy-delta5-steroid
                     dehydrogenase (NAD+) activity [Evidence IEA]"
                     /GO_process="GO:0006694 - steroid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38540
     Region          27..347
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(32,34..35,37,94..96,133..135,162,166,188..191)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(111,135,162,166)
                     /site_type="active"
                     /db_xref="CDD:187535"
ORIGIN      
        1 msqekghdel hpellalare latrvkrvlv tgaggflgaa icrpllaagi qvvgvarghy
       61 paleamgatm vradicdkqa lkqaldgcel ifhvaskagv wggrasyfrp nvlgteniia
      121 carelgigyl vytstpsvtf dgkdeagide svpyarryln hygaskseae elvlagakeg
      181 lktvairphl iwgpgdphlv prvlergrkg rlklvgredk lvdtiyidna afahlsaars
      241 llaepsrcng kayfvsndqp ltmaamldsi lacdnlpave krvpatlaya igamlegiyr
      301 llaikqeplm trfvakqlsc shyydisaak rdldyrvivs meqgmsklrr slghsn
//
LOCUS       WP_409928940             430 aa            linear   BCT 28-DEC-2024
DEFINITION  TIGR03503 family protein [Shewanella sp. MSW].
ACCESSION   WP_409928940
VERSION     WP_409928940.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. MSW
  ORGANISM  Shewanella sp. MSW
            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  :: HMM
            Evidence Accession :: TIGR03503.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Shewanella sp. MSW"
                     /db_xref="taxon:2569536"
     Protein         1..430
                     /product="TIGR03503 family protein"
                     /calculated_mol_wt=47697
     Region          21..385
                     /region_name="TIGR03503"
                     /note="TIGR03503 family protein"
                     /db_xref="CDD:274613"
ORIGIN      
        1 maclllgfgg ataaeivpke qaselknrfr idhmvdrivl lvqreygsap vvvvlpdgsk
       61 wyasrhpenv kwtdgvtgdm isvenpvpgp wqligkvvpg sqitrvselg ievdelpqpl
      121 yqgerlklta hltgdslrmr lpgleyllrw tarfasshqp gdenfaagtl ivgsyqdnge
      181 alderpddgt ftaninldqp wgdytlqvnv qndvferefk qafrlepspv dikvlepddp
      241 ltqpwglmlr anpdilrlee tyfdiellgp aglqlpltvr qpkegstqlv lpqvsdfgsy
      301 rikgtvfstd kqgrelvlsl perffnfvep pkpppsaeem aaraaviaak eeaaakenal
      361 yliiggnvll llfgvgailf wrkrqslkqa lavaeaqmle qqqsrpevdt lpeidltlpd
      421 edeqksnrtl
//
LOCUS       WP_409928941             177 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Shewanella sp.
            MSW].
ACCESSION   WP_409928941
VERSION     WP_409928941.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. MSW
  ORGANISM  Shewanella sp. MSW
            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 10007160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Shewanella sp. MSW"
                     /db_xref="taxon:2569536"
     Protein         1..177
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /calculated_mol_wt=19404
     Region          12..177
                     /region_name="COG3295"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:442524"
ORIGIN      
        1 mallllmlff avtgitlnhp dwfirqgges laseealpgf llpvnsedpd wrdatahwls
       61 shwgvdghsa efsedevalv hkgpgryqsi tldlldgkay veqidygvia vlndlhkgrn
      121 sgtlwvwlld lcsiliilfs ltgaflllpq srrlkkslla magvssacal iyllfvp
//
LOCUS       WP_409928944             614 aa            linear   BCT 28-DEC-2024
DEFINITION  penicillin-binding protein 2 [Shewanella sp. MSW].
ACCESSION   WP_409928944
VERSION     WP_409928944.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. MSW
  ORGANISM  Shewanella sp. MSW
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Matsuzawa,H., Asoh,S., Kunai,K., Muraiso,K., Takasuga,A. and
            Ohta,T.
  TITLE     Nucleotide sequence of the rodA gene, responsible for the rod shape
            of Escherichia coli: rodA and the pbpA gene, encoding
            penicillin-binding protein 2, constitute the rodA operon
  JOURNAL   J Bacteriol 171 (1), 558-560 (1989)
   PUBMED   2644207
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR03423.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Shewanella sp. MSW"
                     /db_xref="taxon:2569536"
     gene            1..614
                     /gene="mrdA"
     Protein         1..614
                     /product="penicillin-binding protein 2"
                     /EC_number="3.4.16.4"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=69582
     Region          13..603
                     /region_name="pbp2_mrdA"
                     /note="penicillin-binding protein 2; TIGR03423"
                     /db_xref="CDD:274573"
ORIGIN      
        1 mhdhaaeaal fkrralftfv cvvallslll gnlyylqvvs fkdyetrsnd nrirvvplap
       61 srgliydrng kllaenlpfy tlevipekvk nmqqtldels tvidlsqder dsfteslkyh
      121 rrfkplplkt rltedevalf svnqhrfdgf yvdaglkrhy pyssllthvl gyvgkinsrd
      181 rdalersgnw knyaatkdig kqgiekfyes llhglpghle eevnnlgrsv rtlkvtqpep
      241 gqdiyltldl qlqqkatell dgrrgsivai dprdggilam vsspsydpnq fvhgisskay
      301 sellnsrsrp linratqgqy apastvkphl allgledqti sektriwdpg fwqipgvdrk
      361 yrdwkrwghg wvdvydsivh scdtfyydma ykvgidkisg fmdqfgfgqn tgvdifeesa
      421 gvipsrdwkr lkynqpwyig dtisvgigqg ywtttplqla natailanrg krftphllka
      481 ikdntariet pvderppivl knknnweiin eamrrtaqks rftdasytaa mktgtaqvfs
      541 vaedekydad tidehlrdna liiayapyed pkivlavvle nagwgganag pvaramldey
      601 llrdtwelkh epqp
//
LOCUS       WP_409928945             240 aa            linear   BCT 28-DEC-2024
DEFINITION  TorF family putative porin [Shewanella sp. MSW].
ACCESSION   WP_409928945
VERSION     WP_409928945.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. MSW
  ORGANISM  Shewanella sp. MSW
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Zhang,H., Brown,R.N., Qian,W.J., Monroe,M.E., Purvine,S.O.,
            Moore,R.J., Gritsenko,M.A., Shi,L., Romine,M.F., Fredrickson,J.K.,
            Pasa-Tolic,L., Smith,R.D. and Lipton,M.S.
  TITLE     Quantitative analysis of cell surface membrane proteins using
            membrane-impermeable chemical probe coupled with 18O labeling
  JOURNAL   J Proteome Res 9 (5), 2160-2169 (2010)
   PUBMED   20380418
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Bordi,C., Ansaldi,M., Gon,S., Jourlin-Castelli,C., Iobbi-Nivol,C.
            and Mejean,V.
  TITLE     Genes regulated by TorR, the trimethylamine oxide response
            regulator of Shewanella oneidensis
  JOURNAL   J Bacteriol 186 (14), 4502-4509 (2004)
   PUBMED   15231782
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02001.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Shewanella sp. MSW"
                     /db_xref="taxon:2569536"
     Protein         1..240
                     /product="TorF family putative porin"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=26530
     Region          25..240
                     /region_name="Gcw_chp"
                     /note="Bacterial protein of unknown function (Gcw_chp);
                     cl09901"
                     /db_xref="CDD:299108"
ORIGIN      
        1 mirrsnpllw alllggaits tsaiaevsge iavtndyrfr gvsqtagdfa vqasldwnhd
       61 sgffvgawas nvefdedgtp kedqvgadfe ldvylgyage indnlaydit llrymypgdn
      121 vsqdyneisf glefsdfraa ywytndysgs dldyhyaeln ysyefaenws ldlhlgynfg
      181 dapdddmgky ldysigvste iagfglslaw ldtdidsdae issgtfqndd tvlasvsyaf
//
LOCUS       WP_409928946             298 aa            linear   BCT 28-DEC-2024
DEFINITION  protein translocase subunit SecF [Shewanella sp. MSW].
ACCESSION   WP_409928946
VERSION     WP_409928946.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. MSW
  ORGANISM  Shewanella sp. MSW
            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  :: HMM
            Evidence Accession :: TIGR00966.2
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Shewanella sp. MSW"
                     /db_xref="taxon:2569536"
     gene            1..298
                     /gene="secF"
     Protein         1..298
                     /product="protein translocase subunit SecF"
                     /GO_component="GO:0031522 - cell envelope Sec protein
                     transport complex [Evidence IEA]"
                     /GO_function="GO:0015450 - protein-transporting ATPase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006886 - intracellular protein transport
                     [Evidence IEA]"
                     /GO_process="GO:0043952 - protein transport by the Sec
                     complex [Evidence IEA]"
                     /calculated_mol_wt=31688
     Region          2..298
                     /region_name="secF"
                     /note="preprotein translocase subunit SecF; Reviewed;
                     PRK13021"
                     /db_xref="CDD:237274"
ORIGIN      
        1 minmknatkw ryfssavsvi lmivsisvia vkglnwgldf tggvvseiri dssigakslq
       61 pvlqqaygqe vsliaagepg rwvlryaaps agqsmpelpe vlagmntqve vlntsivgpq
      121 vgqelaeqgg lallvamlci lgylsyrfew rlasgavfal vhdvifvlaf faatqmefnl
      181 tvlaavlail gyslndsiii adrirellaa kpklavkdin nqaiaatfar tmvtsgttlm
      241 tisalwimgg gplegfsiam figvltgtfs sisvgtslpe wlglssehyr vtpvtqtp
//
LOCUS       WP_409928948             712 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Shewanella sp. MSW].
ACCESSION   WP_409928948
VERSION     WP_409928948.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. MSW
  ORGANISM  Shewanella sp. MSW
            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 11448368
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Shewanella sp. MSW"
                     /db_xref="taxon:2569536"
     Protein         1..712
                     /product="S9 family peptidase"
                     /calculated_mol_wt=80938
     Region          27..711
                     /region_name="PtrB"
                     /note="Protease II [Amino acid transport and metabolism];
                     COG1770"
                     /db_xref="CDD:441376"
ORIGIN      
        1 msragslmlv lgtalwlcgc sgmnsenklv apvaekrpht mslhgvtrtd dyywlrdder
       61 qapdvidyle renaytaarl kpweplkqkl fkelisrleq dessvpyrwh nhwyyrrfea
      121 gleypviars relngeeqll ldvnlraegq efyalggvsv spdeqilafa edtlsrriys
      181 vyfkdlatge lladkltgvd grvvwsndnr yvfyiakdpq tllgyqvfrh klgspqsedl
      241 lvyeeqddtf yislgkslde slivlhhest ttsevsllda naplgefraf lprekgheys
      301 iakrgdeffi lsnwqatnfr lmkttaadag dkrkwqqvla hdpevrledl lllddylivq
      361 srsqglshik vyphtdlsrg yelafddpay vvgldinpsq hsrelrlyys spttpesiys
      421 yqldkpgerk llkqekvlgd fepgnyqaer llipardgaq vpvtlvyrkd kfrkdgsnpl
      481 yqygygaygh iiepdfdasv lslldrgvvy aiahvrggem lgrpwyddgr lfnkrnsfnd
      541 fedttralld lgyaapgkvv aaggsaggll mgavvnqapd lylavaahvp fvdivttmld
      601 esiplttney dewgnpndkp yfdymlsysp ydnirhqayp hllvttglhd sqvqyfepak
      661 wvaklrdykt ddnllllqtd meaghggksg rfrqfedtal eyafflgllg le
//
LOCUS       WP_409928955             350 aa            linear   BCT 28-DEC-2024
DEFINITION  succinylglutamate desuccinylase [Shewanella sp. KCT].
ACCESSION   WP_409928955
VERSION     WP_409928955.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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  :: HMM
            Evidence Accession :: TIGR03242.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     gene            1..350
                     /gene="astE"
     Protein         1..350
                     /product="succinylglutamate desuccinylase"
                     /EC_number="3.5.1.96"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0009017 - succinylglutamate desuccinylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006527 - arginine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38924
     Region          1..345
                     /region_name="PRK05324"
                     /note="succinylglutamate desuccinylase; Provisional"
                     /db_xref="CDD:235408"
     Site            order(71,74,114,121..122,166,179,212,216,230)
                     /site_type="active"
                     /db_xref="CDD:349428"
ORIGIN      
        1 mlskdflqlt ldnpvgleaf eftlgqhtqv svwdtgviqf eplvtqeanq egeldgkeda
       61 lksivlssav hgnetapiel cdqlitalls etliarhrll flignppail ngtrfveenl
      121 nrlfsgahak gesnaerara kkleqyvdrf fnaapeggsr yhydlhtair askhekfaiy
      181 pyphgapysg eqimflaacg intvlfhhep tttfsyfsah gyqahaftie lgkvmpmgqn
      241 dmtrfiavke mltrlvsgrd lelgefdpsq vnlyqvnrsi nkqfddfsft faddvenfta
      301 fprgyilakd ggteikveae sesivfpnan vpvgqrtvlc lvpakdyrvv
//
LOCUS       WP_409928957             962 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine
            phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase
            [Shewanella sp. KCT].
ACCESSION   WP_409928957
VERSION     WP_409928957.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Muse,W.B. and Bender,R.A.
  TITLE     Map position of the glnE gene from Escherichia coli
  JOURNAL   J Bacteriol 174 (23), 7876-7877 (1992)
   PUBMED   1360007
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF008292.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11072
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     gene            1..962
                     /gene="glnE"
     Protein         1..962
                     /product="bifunctional [glutamate--ammonia
                     ligase]-adenylyl-L-tyrosine
                     phosphorylase/[glutamate--ammonia-ligase]
                     adenylyltransferase"
                     /EC_number="2.7.7.42"
                     /EC_number="2.7.7.89"
                     /GO_function="GO:0008882 - [glutamate-ammonia-ligase]
                     adenylyltransferase activity [Evidence IEA]"
                     /calculated_mol_wt=109980
     Region          10..953
                     /region_name="PRK11072"
                     /note="bifunctional [glutamate--ammonia
                     ligase]-adenylyl-L-tyrosine
                     phosphorylase/[glutamate--ammonia-ligase]
                     adenylyltransferase"
                     /db_xref="CDD:236836"
ORIGIN      
        1 menmseqalp hevnqvaeqh wqrlaeawpd iseqltpeqt kelktifgls dfvaeqlcrh
       61 pnwivslfeg qlsmlardsf saelhsilag andeeqvkai lrryrnrqmv rlawrdflgy
      121 aelndslldl salaealiia ardwlygqmc qqygtpcdse gnpqplmilg mgklggreln
      181 fssdidlift fpehgetqgg rrsqdnqqff irmgqrlvnl lnqvtvdgfv yrvdmrlrpy
      241 gesgplvvsf sgledyyqeq grdweryamv karalgpwsa ysdelhdmlr pfvyrryidf
      301 saieslrkmk qlitqevrrr rltdniklga ggirevefvv qsfqlirggr epalrqqslf
      361 gaidtlyklg qleylavdel kqsylmlrrv enllqaigdq qtqtlpqhll dwqrlcfalg
      421 mageaelrth iesamakihr yfketvggqe sdevaeqwta qlwslveded aeallrehgv
      481 eeielwpalk swrgtvakrt igprgretld klmpwllqef iqlptptkaf lpvskvldqi
      541 ltrttylell fenpgarqql vslcmaspwi geqlakfpml ldelidpaql ydttslddyp
      601 selrqyllrv peedmeqqme alrqfklsqq lkiaaadvtg vlpvmqvsdh ltflaeaiie
      661 qvvlqawqqv skrhgtppyl apeemgfavi gygkagglel gygsdldlvf lhnytrnkyp
      721 eaqqtngdrp idighfylkl aqrilhlfst rttsgelyev dmrlrpsgas gllvseieyf
      781 gsyqreeawt wehqalvrar flfgdnrlaa rfselradvl amerdkaela kevremrqkm
      841 rthllkvdeg cfdlkqspgg iadiefiaqy lvlanthdhp elaiwsdnvr ifevlselel
      901 lphlsaqhlt qaycylrden hrltlagqvg qlvveqvevh adrvcaiyta ilggdapeas
      961 se
//
LOCUS       WP_409928959             116 aa            linear   BCT 28-DEC-2024
DEFINITION  metalloregulator ArsR/SmtB family transcription factor [Shewanella
            sp. KCT].
ACCESSION   WP_409928959
VERSION     WP_409928959.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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  :: HMM
            Evidence Accession :: NF007528.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10141
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..116
                     /product="metalloregulator ArsR/SmtB family transcription
                     factor"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12929
     Region          1..>85
                     /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 mmavaifkal sdetrllsll liqaegelcv celmvaldes qpkvsrhlaq lrkaellsdr
       61 rqgqwvfyri npelpewage viqktlagnp qllsqaqarl aemgqrperv qvcckg
//
LOCUS       WP_409928960             108 aa            linear   BCT 28-DEC-2024
DEFINITION  MSHA biogenesis protein MshK [Shewanella sp. KCT].
ACCESSION   WP_409928960
VERSION     WP_409928960.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..108
                     /product="MSHA biogenesis protein MshK"
                     /calculated_mol_wt=11428
ORIGIN      
        1 mlrikisvcl lallylgltq asaqtlrdpt rpgagaigsa qhqggsklvl nsliitdqsa
       61 taiinnktft tgdrvqgvri tritkqgvwl adgrqlklyp evtatkgq
//
LOCUS       WP_409928962             803 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA polymerase II [Shewanella sp. KCT].
ACCESSION   WP_409928962
VERSION     WP_409928962.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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  :: HMM
            Evidence Accession :: NF004421.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05762
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..803
                     /product="DNA polymerase II"
                     /EC_number="2.7.7.7"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003887 - DNA-directed DNA polymerase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=90417
     Region          9..803
                     /region_name="PRK05762"
                     /note="DNA polymerase II; Reviewed"
                     /db_xref="CDD:235595"
ORIGIN      
        1 mhdlntplvs vkgriltrhh qgselhyyls taegpvrviv pngericfcr tqdelsllgg
       61 nheswirsea lnlttfddep vsalyfannq sfrhlsriai dkgislyese lraeqrylie
      121 ryialdvefi grwqsqaldt ptliaerarr seldvnrevk lavvsldfec amdgelfsvg
      181 lygqsasgep yqqvimvgea cdsppeylel vpneaalika lldwfklndp diiigwavvt
      241 fdlallyrra kvlnipltlg rlgtqlswrv dnkyrpetli lpgrvvldgi dwlkaafyqf
      301 dsfslesvar ellgegkaih nvshraeeia ilfredkaal ahynitdcrl vweifaktdl
      361 lafvmersrl tglelgrvga svaafnnlyl phlhragyva psvpvsdgie spggyvmdsk
      421 pglyqhilvl dfkslypsii rtflidpkgl veglkegana evkgasegnd tvpgflgaqf
      481 srnspilpel iaslsakree akreanapls qaikiimnsl ygvlgsrgcv fhdarlassi
      541 tlrgheimkq tkqwieaqgl tviygdtdst fvhissperv gdidafarel vasinekwrl
      601 klkqefqldc yleleyerhf eqffmptlrg stegskkryv gaylqedqsl klvfkgmeqv
      661 rsdwsplare vqaelyyrlf akqdvlgylk qivdalqqgk lddklifskr lrrniedyta
      721 kssphvkaat lwcqrsgdds hgkrgekisy lmtqngaepv qhllgkidyq yylnkqiapi
      781 sdpilsilnt sfnnlvakqm sli
//
LOCUS       WP_409928964             517 aa            linear   BCT 28-DEC-2024
DEFINITION  M28 family metallopeptidase [Shewanella sp. KCT].
ACCESSION   WP_409928964
VERSION     WP_409928964.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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 10141072
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..517
                     /product="M28 family metallopeptidase"
                     /calculated_mol_wt=57165
     Region          89..244
                     /region_name="PA_M28_1_2"
                     /note="Protease-associated (PA) domain, peptidase family
                     M28, subfamily-1, subgroup 2. A subgroup of PA-domain
                     containing proteins belonging to the peptidase family M28.
                     Family M28 contains aminopeptidases and carboxypeptidases,
                     and has co-catalytic zinc ions; cd04821"
                     /db_xref="CDD:240125"
     Site            195..197
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:240125"
     Region          271..502
                     /region_name="M28_like_PA"
                     /note="M28 Zn-peptidase containing a protease-associated
                     (PA) domain insert; cd05660"
                     /db_xref="CDD:349910"
ORIGIN      
        1 mlllpavsas pfvfdqqsyr qdvktlasde fegrgplsqg etltveylen afkkmglapg
       61 fgdsyrqsvp makitanqnm qlkvgelvfn ngsdftarte qlqpsikldn seivfvgygi
      121 napeygwndy agidvkgktv ilmvndpgfa tqdpevfkgn amtyygrwty kyeeaarqga
      181 kavfiiheta paaygwnvvq nsntnskysl vdkdknrshi gvmgwiqhev aqkifsaagl
      241 dydklkltaa kpgfksrslh lkanlevnnd ielatsynva gllpgkarpd ewlvmhahwd
      301 hlgktvhedq thiyngavdn asgvagvlql arhfkelstt qpparsmlfs aftaeetgli
      361 gaqyfaenpp vptkqlvafl nidgmnvgkg vdyilrygeg vselenyldn aakaqgrwvk
      421 adprpqnglm frsdhfalak qgvpglmfms lgdtdpdyia hkyhqgaddy dpswtlggve
      481 qdlalssdil eklannndwp kwleasdfkt rraqdgr
//
LOCUS       WP_409928965             402 aa            linear   BCT 28-DEC-2024
DEFINITION  HD-GYP domain-containing protein [Shewanella sp. KCT].
ACCESSION   WP_409928965
VERSION     WP_409928965.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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 12112208
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..402
                     /product="HD-GYP domain-containing protein"
                     /calculated_mol_wt=44558
     Region          7..128
                     /region_name="DUF3391"
                     /note="Domain of unknown function (DUF3391); pfam11871"
                     /db_xref="CDD:432148"
     Region          <75..329
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 martepiqlp lsklqtgitv klplswknhp flfnrikiee eaqieliksl gvpyvllvsg
       61 eelleeende gdeqaekaee vvdpiieakr nvrkslrlsq krfidcvnec rstfskiasd
      121 pegayreaas lvesliehmf eyeqthlalv tagesdnsvt qhgisvavla lmiaramelp
      181 ksdmrdialg clfhdigklk vpesirrkkt pltaseanfl kmhpnfgyem lnktglfnka
      241 vlsivlhhhe fidgsgfpdg ltekkipiit qlvslandyd gqlwaeesrs pqialgylfk
      301 nhagkhsetl iavlvkllgi yppgtlvrls dgdvgkvmvt tqsvkqpqvw achpdgsepg
      361 lrflsqeevf vdsvlkleel tegamrvlqa dsgisfyfag tp
//
LOCUS       WP_409928966             434 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acetylglucosamine MFS transporter NagP [Shewanella sp. KCT].
ACCESSION   WP_409928966
VERSION     WP_409928966.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Rodionov,D.A., Yang,C., Li,X., Rodionova,I.A., Wang,Y.,
            Obraztsova,A.Y., Zagnitko,O.P., Overbeek,R., Romine,M.F., Reed,S.,
            Fredrickson,J.K., Nealson,K.H. and Osterman,A.L.
  TITLE     Genomic encyclopedia of sugar utilization pathways in the
            Shewanella genus
  JOURNAL   BMC Genomics 11, 494 (2010)
   PUBMED   20836887
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF046060.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     gene            1..434
                     /gene="nagP"
     Protein         1..434
                     /product="N-acetylglucosamine MFS transporter NagP"
                     /calculated_mol_wt=46241
     Region          17..427
                     /region_name="MFS_FucP_like"
                     /note="Fucose permease and similar proteins of the Major
                     Facilitator Superfamily of transporters; cd17394"
                     /db_xref="CDD:340952"
     Site            order(20,23..24,27,31,83,87,123..124,127..128,148,151,204,
                     208)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340952"
ORIGIN      
        1 memtlnsesk rssvipmaiv aglffilgfa twlngslmpy lkqilqltpl qaslilfsfy
       61 iavtftalps awvirkvgyk tgmamgmgim miagllfipa aktqvfvlfl faqlvmgtgq
      121 tllqtavnpy vvrigpeesa aarvsvmgil nkgagviapl vftalildsf kdrvgveltq
      181 aqidemangl vfpylgmaif igvlallvkk splpelened eqgqgtkght realshpnla
      241 lgvvalffyv aveviagdti gtfalslgve nygvmtsytm icmvigyslg iltiprfisq
      301 pkalmisail glmltlgilf gdnesyaian allvpfggam lpdtllmiaf lglanaivwp
      361 avwplalsgm gkltstgsal lvmgiaggaf gplfwgltss atslgqqggy mvmlpcylfi
      421 lfyavkgykm rswk
//
LOCUS       WP_409928967             315 aa            linear   BCT 28-DEC-2024
DEFINITION  YeiH family protein [Shewanella sp. KCT].
ACCESSION   WP_409928967
VERSION     WP_409928967.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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 10006735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..315
                     /product="YeiH family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32892
     Region          28..314
                     /region_name="YeiH"
                     /note="Uncharacterized membrane protein YadS, UPF0324
                     family [Function unknown]; COG2855"
                     /db_xref="CDD:442103"
ORIGIN      
        1 mkalfqkwpf hpaqaiffva galcltpvis spialvigft laslglvphn ldigaltkkl
       61 layaiiglgf giqldaaisa ssqniglilg sivftlllgt algrllrvda klshmiasgt
      121 aicggsaiaa vapaikadsq dtaialatvf vlnsialflf palghllqls qyhfgvwsai
      181 aihdtssvvg aasaygdeal rtattlklar alwivpvalv samafggnrr kiavpffilf
      241 yclaillahl vpqgqvlydg ifalskrvlv lclfmigagi tigkmrqagm rpmalglllw
      301 liigagslly ivnfs
//
LOCUS       WP_409928970             473 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Shewanella sp.
            KCT].
ACCESSION   WP_409928970
VERSION     WP_409928970.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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  :: HMM
            Evidence Accession :: TIGR01730.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..473
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=51955
     Region          1..23
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          41..66
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          105..132
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          164..381
                     /region_name="HlyD_D23"
                     /note="Barrel-sandwich domain of CusB or HlyD
                     membrane-fusion; pfam16576"
                     /db_xref="CDD:435440"
     Region          <356..461
                     /region_name="PRK09578"
                     /note="MexX/AxyX family multidrug efflux RND transporter
                     periplasmic adaptor subunit"
                     /db_xref="CDD:169982"
ORIGIN      
        1 mhpeetshep gsrcpkcnmf lveqetdase tsltaghevt yvcpmhpevt shepgsrcpe
       61 cnmflvaeee eeststkvep emdhsqhdpl aqakpapltg epsikyvcpm hahivsdvpg
      121 tcpicgmnle kvemsadtqq ieidvsgsmq qalalkvaka ekdtlwkfvq tvgqigydes
      181 qinhvharvn gwieklaits vgdkiskgql lyeiyspdli naqddyllal sslqsskdsr
      241 nyqdlvrkag lrlellgmnq aqikqlaksk qtqyrvpfya kadgivkals vrdgmyiqpa
      301 tevmsvvdls kvwviadvfe neqswlaigq ptevsvpamd lkgiegkidy iypeldpvtr
      361 slrvrivlan nevalrpntl akieiyggpn edvlvipqea liqtgkenrv ivkqgdgsfl
      421 arkvtvgmms qgkaeilsgi eegeqvvtsg qflldseasl kgslmrlssg hqh
//
LOCUS       WP_409928971             254 aa            linear   BCT 28-DEC-2024
DEFINITION  prolipoprotein diacylglyceryl transferase [Shewanella sp. KCT].
ACCESSION   WP_409928971
VERSION     WP_409928971.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Tschumi,A., Grau,T., Albrecht,D., Rezwan,M., Antelmann,H. and
            Sander,P.
  TITLE     Functional analyses of mycobacterial lipoprotein diacylglyceryl
            transferase and comparative secretome analysis of a mycobacterial
            lgt mutant
  JOURNAL   J Bacteriol 194 (15), 3938-3949 (2012)
   PUBMED   22609911
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Pailler,J., Aucher,W., Pires,M. and Buddelmeijer,N.
  TITLE     Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase
            (Lgt) of Escherichia coli has seven transmembrane segments, and its
            essential residues are embedded in the membrane
  JOURNAL   J Bacteriol 194 (9), 2142-2151 (2012)
   PUBMED   22287519
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00544.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     gene            1..254
                     /gene="lgt"
     Protein         1..254
                     /product="prolipoprotein diacylglyceryl transferase"
                     /EC_number="2.5.1.145"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008961 -
                     phosphatidylglycerol-prolipoprotein diacylglyceryl
                     transferase activity [Evidence IEA]"
                     /GO_process="GO:0009249 - protein lipoylation [Evidence
                     IEA]"
                     /calculated_mol_wt=28555
     Region          1..254
                     /region_name="PRK00052"
                     /note="prolipoprotein diacylglyceryl transferase;
                     Reviewed"
                     /db_xref="CDD:234599"
ORIGIN      
        1 mdpvlvsfmg ltihwygvlf asaifagfqv mkriyvregl dvesldnlli ycvigivvga
       61 rlahvlfydp syyfahpaki laiwegglas hggglgaila lyyyhrkmkl pflflldrla
      121 iataifgffv rmanfvnsei lgvpsdkpwa ivfervdmlp rhpaqlyeal aylsifialw
      181 viykttemkq kqgalfglfl vwvfsarfai efvkvkqaay aqdwtmsagq mlsipfllvg
      241 vfllvkpyla sktk
//
LOCUS       WP_409928973             243 aa            linear   BCT 28-DEC-2024
DEFINITION  spondin domain-containing protein [Shewanella sp. KCT].
ACCESSION   WP_409928973
VERSION     WP_409928973.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Tan,K. and Lawler,J.
  TITLE     The structure of the Ca(2)+-binding, glycosylated F-spondin domain
            of F-spondin - A C2-domain variant in an extracellular matrix
            protein
  JOURNAL   BMC Struct Biol 11, 22 (2011)
   PUBMED   21569239
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF038123.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..243
                     /product="spondin domain-containing protein"
                     /calculated_mol_wt=25270
     Region          46..242
                     /region_name="Spond_N"
                     /note="Spondin_N; cl05795"
                     /db_xref="CDD:471323"
ORIGIN      
        1 mmklqqlkng lpltavalsv glllsacsdn dhdtnmsepp tapversftl tvtnltanqp
       61 msplallats ngyhawqnge paslaleqla eggdqsgysa emdgidmvvs gagilppgas
      121 esltltqtea ataslslltm lvntndafsg ldaidisqma vdqsqsfytp aydagteans
      181 eikgsipgpa dggegfnaar ddvdrvhlhp gvisqddgls dsvlkashrf dnpvlkvtiq
      241 rtr
//
LOCUS       WP_409928974             349 aa            linear   BCT 28-DEC-2024
DEFINITION  anthranilate phosphoribosyltransferase [Shewanella sp. KCT].
ACCESSION   WP_409928974
VERSION     WP_409928974.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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  :: HMM
            Evidence Accession :: TIGR01245.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     gene            1..349
                     /gene="trpD"
     Protein         1..349
                     /product="anthranilate phosphoribosyltransferase"
                     /EC_number="2.4.2.18"
                     /GO_function="GO:0004048 - anthranilate
                     phosphoribosyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36517
     Region          4..343
                     /region_name="trpD"
                     /note="anthranilate phosphoribosyltransferase;
                     Provisional; PRK00188"
                     /db_xref="CDD:234682"
ORIGIN      
        1 mselqpifdr lyqgqtitre etkalfseiv egkmdpvama gmlvamkmrg etideisgaa
       61 dallqaakaf papseatrvq givdivgtgg dghntinist tsafvaaaag akvakhgnrs
      121 vssksgssdl laqfgidltm apetardcld tlglcflfap hyhggvrhav pvrqalktrt
      181 lfnvlgplin parpdymllg vydpmlvrpi cdvlkaldvk ramvvhgsgl devavhgetl
      241 vcelkqdeiv eyylspealg lsraeisdla gagpaenaei trailqghge lahteavaan
      301 agcalyvsgc cdspqqgtal alqtlasgka ytlleqlasa sqsdnlgtn
//
LOCUS       WP_409928976              41 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein [Shewanella sp. KCT].
ACCESSION   WP_409928976
VERSION     WP_409928976.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..41
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..41
                     /product="hypothetical protein"
                     /calculated_mol_wt=4709
ORIGIN      
        1 malspefkvt ewvnlaisls vgfsfrmlai ryhwgmpkfd y
//
LOCUS       WP_409928979             133 aa            linear   BCT 28-DEC-2024
DEFINITION  nitrous oxide-stimulated promoter family protein [Shewanella sp.
            KCT].
ACCESSION   WP_409928979
VERSION     WP_409928979.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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  :: HMM
            Evidence Accession :: NF007715.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10410
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..133
                     /product="nitrous oxide-stimulated promoter family
                     protein"
                     /calculated_mol_wt=14941
     Region          8..115
                     /region_name="YgbA_NO"
                     /note="Nitrous oxide-stimulated promoter; pfam11756"
                     /db_xref="CDD:432053"
ORIGIN      
        1 mnqeilsgkl lrefktiaam vhiyckdhcq akgdvancpe csefleyaht rldrcpygqd
       61 kptcnkcpvh cykpepkaka reimiysgpr mllphpimai rhlwaergpv pgkppaaasn
      121 rhlrlakehk pss
//
LOCUS       WP_409928980             173 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein [Shewanella sp. KCT].
ACCESSION   WP_409928980
VERSION     WP_409928980.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..173
                     /product="hypothetical protein"
                     /calculated_mol_wt=19198
ORIGIN      
        1 mattteqsqf fdaivahcgq afegkvmagn sadsafsgkr lvmhvhecsd selkvpfhvg
       61 edhsrtwvit ktdtglrlkh dhrhqdgsed kvtmyggdtq dggsaelqsf pvdaysidnf
      121 kqngltqsvt nvwhmgites qfiyrltren rdfkvtfdlt kpvalppapw ghe
//
LOCUS       WP_409928981             182 aa            linear   BCT 28-DEC-2024
DEFINITION  pseudouridine synthase [Shewanella sp. KCT].
ACCESSION   WP_409928981
VERSION     WP_409928981.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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  :: HMM
            Evidence Accession :: TIGR00093.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..182
                     /product="pseudouridine synthase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016866 - intramolecular transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=20125
     Region          1..170
                     /region_name="PseudoU_synth"
                     /note="Pseudouridine synthases catalyze the isomerization
                     of specific uridines in an RNA molecule to pseudouridines
                     (5-ribosyluracil, psi); cl00130"
                     /db_xref="CDD:469624"
     Site            order(37..40,144)
                     /site_type="active"
                     /db_xref="CDD:211324"
ORIGIN      
        1 mifkpygyls qfvgerrkrk pllgelanfp tgimaigrld hdsegllllt tdgktshavr
       61 sksiekeyyl qldgeiteqa ilslcegvei gikgekyrtl pcrarrldqa pdlpprgrki
      121 rdarhgptsw laititegkn rqlrkmtaav gfatlrlvrv rigdihlgal qpgevkplat
      181 lg
//
LOCUS       WP_409928984             275 aa            linear   BCT 28-DEC-2024
DEFINITION  class D beta-lactamase [Shewanella sp. KCT].
ACCESSION   WP_409928984
VERSION     WP_409928984.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            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  :: HMM
            Evidence Accession :: NF012161.0
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     gene            1..275
                     /gene="blaOXA"
     Protein         1..275
                     /product="class D beta-lactamase"
                     /EC_number="3.5.2.6"
                     /GO_function="GO:0008800 - beta-lactamase activity
                     [Evidence IEA]"
                     /GO_process="GO:0030655 - beta-lactam antibiotic catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30596
     Region          17..275
                     /region_name="YbxI"
                     /note="Beta-lactamase class D [Defense mechanisms];
                     COG2602"
                     /db_xref="CDD:442014"
ORIGIN      
        1 mgllslalls waggaaaapq tgpdkpaaeq esagplrldg eiqaafdavg akgvmvlldd
       61 kqgklltnda arsrhpyipa stfkiphsll lleagivede hsrfvwdgve raysrwnrdh
      121 nfvgamkysv vpiyqklalq lgaermargl tnldygnvni gggldsfwld gdlaisaleq
      181 vnflrrlyhn qlrvsersqr ivktmmlnea sgdwvlrakt gygvrkgqkl gwwvgwlere
      241 entyffamnm ditsdkdlvl rkrvvkhllk akgwm
//
LOCUS       WP_409928985             295 aa            linear   BCT 28-DEC-2024
DEFINITION  quinol dehydrogenase ferredoxin subunit NapH [Shewanella sp. KCT].
ACCESSION   WP_409928985
VERSION     WP_409928985.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Brondijk,T.H., Nilavongse,A., Filenko,N., Richardson,D.J. and
            Cole,J.A.
  TITLE     NapGH components of the periplasmic nitrate reductase of
            Escherichia coli K-12: location, topology and physiological roles
            in quinol oxidation and redox balancing
  JOURNAL   Biochem J 379 (Pt 1), 47-55 (2004)
   PUBMED   14674886
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Brondijk,T.H., Fiegen,D., Richardson,D.J. and Cole,J.A.
  TITLE     Roles of NapF, NapG and NapH, subunits of the Escherichia coli
            periplasmic nitrate reductase, in ubiquinol oxidation
  JOURNAL   Mol Microbiol 44 (1), 245-255 (2002)
   PUBMED   11967083
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF007013.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09477
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     gene            1..295
                     /gene="napH"
     Protein         1..295
                     /product="quinol dehydrogenase ferredoxin subunit NapH"
                     /EC_number="7.1.1.-"
                     /calculated_mol_wt=32614
     Region          25..293
                     /region_name="napH"
                     /note="quinol dehydrogenase membrane component;
                     Provisional; PRK09477"
                     /db_xref="CDD:236535"
ORIGIN      
        1 msntkmktpg adqtrfaqaa idelgwwrah kflflrrasq lcvlltfaig pwmglwvlkg
       61 nlsssellgt iplsdplvtl qvlmtgrlpe tallvgalli alfyllaggr vfcswvcpvn
      121 lvtdaaswlr rklrlprtae mprnlryyll alvlllplvt gitvwewvnp vpilyrallf
      181 sagsglwila miflldlfis erawcghlcp tgalfallgk aspvkvsavn asacdncmdc
      241 fevcperqvl kpalkgdnpm ivdsdctqcg rcidvcaqrv fqyqnrialk aennk
//
LOCUS       WP_409928987             722 aa            linear   BCT 28-DEC-2024
DEFINITION  retention module-containing protein, partial [Shewanella sp. KCT].
ACCESSION   WP_409928987
VERSION     WP_409928987.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. KCT
  ORGANISM  Shewanella sp. KCT
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Smith,T.J., Font,M.E., Kelly,C.M., Sondermann,H. and O'Toole,G.A.
  TITLE     An N-Terminal Retention Module Anchors the Giant Adhesin LapA of
            Pseudomonas fluorescens at the Cell Surface: a Novel Subfamily of
            Type I Secretion Systems
  JOURNAL   J Bacteriol 200 (8), e00734-17 (2018)
   PUBMED   29437852
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Guo,S., Stevens,C.A., Vance,T.D.R., Olijve,L.L.C., Graham,L.A.,
            Campbell,R.L., Yazdi,S.R., Escobedo,C., Bar-Dolev,M., Yashunsky,V.,
            Braslavsky,I., Langelaan,D.N., Smith,S.P., Allingham,J.S.,
            Voets,I.K. and Davies,P.L.
  TITLE     Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium
            to diatoms and ice
  JOURNAL   Sci Adv 3 (8), e1701440 (2017)
   PUBMED   28808685
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF033682.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Shewanella sp. KCT"
                     /db_xref="taxon:2569535"
     Protein         1..>722
                     /product="retention module-containing protein"
     Region          5..134
                     /region_name="retention_LapA"
                     /note="retention module-containing protein; NF033682"
                     /db_xref="CDD:468140"
     Region          61..>717
                     /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 mkslvttkng qvigvkgkvs lvteteqkev tigemipegs tiliaeqadl elafadgtsf
       61 tsqslndtta aevnalneie qlqaliasge dptaelpeta agntpasegd sgfisvnrtg
      121 aqtlagagyt tsgfsveqpt vqaftvssdd aptitandts tiaedgvatg nvldndvdfd
      181 telsvvtftv dgqtvtagtt valeggslvi nadgsytftp ndnwngsvpv vtyttntges
      241 atltinvtpv ddpsilands ntvaedtvat gnvldndsdi dselsvvsfs vggqtvtagt
      301 tveveggslv inadgsytft pnqdwngsvp vityttntge satltinvtp vddpsvland
      361 sntvaedtva tgnildndsd idselsvvsf svdgqtvtag ttvaleggsl vinadgsytf
      421 tpndnwngsv pvvtyttntg esatltinvt pvddpsvlan dsntiaedtv atgnvldnds
      481 didselsvvs fsvdgqtvta gttvaleggs lvinadgsyt ftpnqdwngs vpvityttnt
      541 gesatltinv tlvddpsila ndsntvaedt vatgnvldnd sdidseisvv sfsvdgqtvt
      601 agttvevegg slvinadgay tftpsqdwng svpvityttn tgesatltin vtpvddpsvl
      661 andsntvaed tvatgnvldn dsdidselsv vsfsvdgqtv tagttvaleg gslvinadga
      721 yt
//
LOCUS       WP_409928989             427 aa            linear   BCT 28-DEC-2024
DEFINITION  D-tagatose-bisphosphate aldolase, class II, non-catalytic subunit
            [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409928989
VERSION     WP_409928989.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Brinkkotter,A., Shakeri-Garakani,A. and Lengeler,J.W.
  TITLE     Two class II D-tagatose-bisphosphate aldolases from enteric
            bacteria
  JOURNAL   Arch Microbiol 177 (5), 410-419 (2002)
   PUBMED   11976750
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Brinkkotter,A., Kloss,H., Alpert,C. and Lengeler,J.W.
  TITLE     Pathways for the utilization of N-acetyl-galactosamine and
            galactosamine in Escherichia coli
  JOURNAL   Mol Microbiol 37 (1), 125-135 (2000)
   PUBMED   10931310
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Nobelmann,B. and Lengeler,J.W.
  TITLE     Molecular analysis of the gat genes from Escherichia coli and of
            their roles in galactitol transport and metabolism
  JOURNAL   J Bacteriol 178 (23), 6790-6795 (1996)
   PUBMED   8955298
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02810.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..427
                     /product="D-tagatose-bisphosphate aldolase, class II,
                     non-catalytic subunit"
                     /EC_number="4.1.2.40"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46162
     Region          3..425
                     /region_name="GatZ"
                     /note="Tagatose-1,6-bisphosphate aldolase non-catalytic
                     subunit AgaZ/GatZ [Carbohydrate transport and metabolism];
                     COG4573"
                     /db_xref="CDD:443630"
ORIGIN      
        1 metirnlvad hkrgrtvgit svcsahplvi eatfvhalrr darfvlieat snqvnqdggy
       61 tgmvpadfra fvegiadrig yprdrlvlgg dhlgpnawts lpadaamaka eimigdyvra
      121 gfakihldcs mscegdptpl pertvaeraa rlcrvaeday sgdpadapvy vigtevpvpg
      181 gaaedldtla vttpeaalat ldmhrslfae aglkdawerv iatvvqpgve fdhmkvvdyd
      241 paaatalsea ivpvdhivfe ahstdyqtad alaalvrdhf ailkvgpgvt falrealwal
      301 daieretvpa eqranlrata iarmqaepgn wrkyyhesgd alelqlqysl sdriryywpd
      361 aeiseaqarl fdnlrahtpp lpllsqylpv ayaavragia tldpidliva higatldayy
      421 gacnpna
//
LOCUS       WP_409928990             638 aa            linear   BCT 28-DEC-2024
DEFINITION  rhamnogalacturonan lyase [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409928990
VERSION     WP_409928990.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10179136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..638
                     /product="rhamnogalacturonan lyase"
                     /calculated_mol_wt=69772
     Region          30..626
                     /region_name="RGL11"
                     /note="Rhamnogalacturonan lyase of the polysaccharide
                     lyase family 11; cd10318"
                     /db_xref="CDD:199906"
     Site            order(140,145,147,149,153,209,211,213,217,383,389,391,393,
                     397,406..407,419,421,427,436,442,479,488,519,521,525,562,
                     566,574,619)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:199906"
     Site            order(383,421,474,557..558,618)
                     /site_type="active"
                     /db_xref="CDD:199906"
ORIGIN      
        1 mmrdaftrsv avllacaatt plfagpirqi eqldrgavvs patgggaivs wrllatdprt
       61 arfevlrdgk riatttatga tsivdqhgtp rqgyavrmig greppspala lpdgfwripl
      121 dvppggttpd glaytytand asvgdldgdg ryeivlkwdp tnshdnsqgg ytgpvlieay
      181 tlegkrlwri nlgpniraga hytqflvydf dgdgraeiam ktadatidgt gqpigdahad
      241 wrekdgevpq adrtgaayta dgkrvaklag rilngpeylt vfdgrtgral askpydppry
      301 pggnptfeql rdtwgdgygn rvdrflagva yfdgarpsmv fgrgyygrtt vaswdyrdgk
      361 lterwlfdsn apgnekyegr gnhqlsiadv dgdgrdeviy gsmaidddgk glwtdplfhg
      421 damhvgdldp arpglekfgv heemdrnggi gsalldartg eilwqkpaqh dtgrglaadi
      481 dprhvgaefw gsnsrdlfdv hgqaigtapr qtnfaiwwdg drlrelldgt tiykwdwrag
      541 ravpllettg tasnngtkan palqadlfgd wreevvlrsa dnrelriyet pfptthryvt
      601 lmqdpvyrlg vawqntaynq pphtsfylge ptatehpq
//
LOCUS       WP_409928992             933 aa            linear   BCT 28-DEC-2024
DEFINITION  outer membrane protein assembly factor BamA [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409928992
VERSION     WP_409928992.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR03303.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..933
                     /gene="bamA"
     Protein         1..933
                     /product="outer membrane protein assembly factor BamA"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0071709 - membrane assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=102014
     Region          84..933
                     /region_name="OM_YaeT"
                     /note="outer membrane protein assembly complex, YaeT
                     protein; TIGR03303"
                     /db_xref="CDD:274514"
ORIGIN      
        1 mtaikvstfg khalvtllag tvlstmpsaa daqggmrggg hrgggqrgga prgvaepipm
       61 ppapstgpav vvsdpnakki ltlrvegsqr iepetvlsyt klrvgipynn elldqaikdl
      121 lasdlfanve isgvesgniv lrvrenpiin rvilegnkrl kddkitkeik lkprqiftrt
      181 avrqdvariv elyrrqgrfa aaiepkmvtl dqnrvdvife inegpkskvr qinilgnevf
      241 sdktlrgqma tkearlttll ssntsydqdr laydqqklrq fyltngyadf rvtsavaelt
      301 pdkkdfiity vveegkrykf gdvtvdsdir dfdnkkvaag ltikkgdwyd akkvedtvds
      361 lnqsaglvgy afadtnpeft rdkealtmgi nfhiaeakrt yverinvtgn tqtqdkvirr
      421 eirlaegdaf nsfqvkrsqd rinslgffqd kfeikqsqgs apdrvvldan veekstgels
      481 lsagyssles fiiqasitqr nfrgkgqelr asvnysyysk sidlgftepy lfnkniaigg
      541 difrrdynaf nfagdtrqtt ytqvstgfql ragiplteyw slaaryglty devglastyf
      601 nadgtcnvlt agsylcsalg nrwtssvgys lifdstnsrl rptagqkfsv sqdfaglggd
      661 vryirtrvdg tkyknlgsgf ivsahveggy ifslegkkpa gvdpiritdr fylgepdfpg
      721 fdirgigprv krtpyttdaa gnqtlvtdrn sivddalggt kyynarlemq iplgsgarel
      781 glrpsiyvqa galwgvtrpl psatfpttid pvtgrvtvlp lnspgfaang qqlyvvpstd
      841 agapnatttc kvgystvagg tcvgssintl yttptspfle eflgdspkpr lsigtgvnwn
      901 spfgplridv ayallkvkgd dtklvtfnvg tqf
//
LOCUS       WP_409928997             222 aa            linear   BCT 28-DEC-2024
DEFINITION  5,6-dimethylbenzimidazole synthase [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409928997
VERSION     WP_409928997.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Taga,M.E., Larsen,N.A., Howard-Jones,A.R., Walsh,C.T. and
            Walker,G.C.
  TITLE     BluB cannibalizes flavin to form the lower ligand of vitamin B12
  JOURNAL   Nature 446 (7134), 449-453 (2007)
   PUBMED   17377583
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Gray,M.J. and Escalante-Semerena,J.C.
  TITLE     Single-enzyme conversion of FMNH2 to 5,6-dimethylbenzimidazole, the
            lower ligand of B12
  JOURNAL   Proc Natl Acad Sci U S A 104 (8), 2921-2926 (2007)
   PUBMED   17301238
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Rodionov,D.A., Vitreschak,A.G., Mironov,A.A. and Gelfand,M.S.
  TITLE     Comparative genomics of the vitamin B12 metabolism and regulation
            in prokaryotes
  JOURNAL   J Biol Chem 278 (42), 41148-41159 (2003)
   PUBMED   12869542
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Pollich,M. and Klug,G.
  TITLE     Identification and sequence analysis of genes involved in late
            steps in cobalamin (vitamin B12) synthesis in Rhodobacter
            capsulatus
  JOURNAL   J Bacteriol 177 (15), 4481-4487 (1995)
   PUBMED   7635831
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02476.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..222
                     /gene="bluB"
     Protein         1..222
                     /product="5,6-dimethylbenzimidazole synthase"
                     /EC_number="1.13.11.79"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /GO_process="GO:0009236 - cobalamin biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0032363 - FMN catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=24632
     Region          19..220
                     /region_name="Nitro_FMN_reductase"
                     /note="nitroreductase family protein; cl00514"
                     /db_xref="CDD:444950"
     Site            order(28,30,48,50..51,53,56..57,59,61,63,65..70,144,
                     146..147,150..151,154..155,167..168,178)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380311"
     Site            order(30,32,34,60,167..168)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:380311"
ORIGIN      
        1 mdiyllrrsl vqneaprrfe tgltdvlqwr rdvrhfraep vaeadmqhll hsaalapsvg
       61 naqpwrfvrv rspdlreala dhvdtcsaaa aasladedir qryrrlklhg lreapeimav
      121 fsdeapsagk rlgiatmpea lrystvmaih tmwlaaaarg iglgwvsild psvvtamldv
      181 pgdwtligll cigypaepat vpelerrgwq arepiadrvi er
//
LOCUS       WP_409928999            1129 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409928999
VERSION     WP_409928999.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR01782.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..1129
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=120407
     Region          64..1129
                     /region_name="TonB-Xanth-Caul"
                     /note="TonB-dependent receptor; TIGR01782"
                     /db_xref="CDD:273804"
ORIGIN      
        1 mcvaiagtah aqtnadpanq tsptgavagq gtagssgttl ssteasssdp qaaplssggk
       61 asdddivvtg irqslanaqn ikrnsdtvvd aitaqdigal pdrsvtealq rvpgvsisrf
      121 aasndpdhfs vegsgvvirg lnfvrsefng rdafsagigg qsinfsdvpa ellgsvevyk
      181 nvtaasiegg lagtvnlntr kpfdnkglhv gvdaegsygd lqkkwaptgs ilisdtwntg
      241 igtfgllgdv sysrvrsrad glqitnfqar dntlvtyqsq ggtticrnpl pgngdtttlp
      301 aansacgaas tagadgfadp maglysplgg qyrtqdfdrk rdgialaaqy etndgrfllt
      361 gqyirshttn lsdehtfeaa pdlseystyp igcqqnnagp ltnpadvnsg tvraqcpvgq
      421 ftnykydsng lfqsgyittp gtgyrsslsg tpmetfiptg gapislsrgq tyeqntvndy
      481 glnallhpte rlhialdady teshhqvsql nifgetyadq elnltgnlpt vmshkpatla
      541 agwagpanpt lvgendqqyf adpnvefwra amdhfedsrg kefqfkgdft ydvdgdfidk
      601 irfgaryadr dqtvkysayn wgmlsevwag tpvsinqvng gnasfynfsn ffrgatpgpa
      661 gayyyngnmi dgynktvgfi nqieavgaas qdnpstrwtp aalragvgad spylpnevtr
      721 vhqrdsaaya masfnsktlv qgldiagnig vrfvhtdmdn fggsiipsqs tlgiadsyqs
      781 rcvpaaatnl pagyapaapg gvcllgaagy arlqqfaapn ptivlgqatn kytywlpsfn
      841 lkvgltpqll vrfagskvlt rpdtnlvrnf qqisidgngn fqsqvgnpyl kpatawqfda
      901 taewyfsrvg sltadvfykd itgffyqslv slpltsngqt fdlltrgpan ysghgkvkga
      961 evayqqtfnf lpgflsgfgf tgnytfiqsn glpnsflngg spvtnvaaqt ktgslplegl
     1021 skhnvnatlf yekgpisira aynwrssyll taadviypyt sifqdasgql dasafinink
     1081 yvkigvqgvn ltnsvtktlq aysgdpnvla prsyfvndrr fsfilrgnf
//
LOCUS       WP_409929003             362 aa            linear   BCT 28-DEC-2024
DEFINITION  3-isopropylmalate dehydrogenase [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929003
VERSION     WP_409929003.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Dean,A.M. and Golding,G.B.
  TITLE     Protein engineering reveals ancient adaptive replacements in
            isocitrate dehydrogenase
  JOURNAL   Proc Natl Acad Sci U S A 94 (7), 3104-3109 (1997)
   PUBMED   9096353
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00169.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..362
                     /gene="leuB"
     Protein         1..362
                     /product="3-isopropylmalate dehydrogenase"
                     /EC_number="1.1.1.85"
                     /GO_function="GO:0003862 - 3-isopropylmalate dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009098 - L-leucine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38018
     Region          14..361
                     /region_name="PRK00772"
                     /note="3-isopropylmalate dehydrogenase; Provisional"
                     /db_xref="CDD:234832"
ORIGIN      
        1 maanssslng thvktiaila gdgigpevta qarrvlealn ldlafeeavv ggaaffaagh
       61 plppetldva rradailfga vgdprcdale ralrpeqail glraalglfa nlrpatlfpg
      121 lenasalrpe varqidmvil relngdvyfg ekgfrtaang tregfdimsy neaevrriat
      181 vgfemakrrk gtlhsidkan vletsqlwrd vvtamsadyp evtlthmyvd naamqlvrnp
      241 gqfdvmvtgn lfgdilsdqa smcagsigml psaslrawsg dnglyepihg sapdiagqgk
      301 anpcatilsa amllrhsldd eaaakrveaa vsaaliggar tpdlggtmtt semgdavlaa
      361 lm
//
LOCUS       WP_409929005             823 aa            linear   BCT 28-DEC-2024
DEFINITION  nitrite reductase large subunit NirB [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929005
VERSION     WP_409929005.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02374.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..823
                     /gene="nirB"
     Protein         1..823
                     /product="nitrite reductase large subunit NirB"
                     /GO_function="GO:0008942 - nitrite reductase [NAD(P)H]
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0042128 - nitrate assimilation [Evidence
                     IEA]"
                     /calculated_mol_wt=88585
     Region          12..799
                     /region_name="nitri_red_nirB"
                     /note="nitrite reductase [NAD(P)H], large subunit;
                     TIGR02374"
                     /db_xref="CDD:162827"
ORIGIN      
        1 meplvtdlkp hlivigngma gcraveeilv rdasryriti fgaeprvnyn rimlspllag
       61 dksfddivin dlawytdnai dlvagdpvva idrkirtvta rsgrtesydk lilatgsdpf
      121 iipvpgrdld gvvtfrdmdd vgamlraada ggdavviggg llgleaahgl alrgmkvtvl
      181 himptlmerq ldeaaawllk selerrgqti ltgadtaeih ghgkvegvrl kdgreipasi
      241 vvmavgirpn vtlardagla igrgihvddh mvtsdadila vgecvehngl vyglvaplwd
      301 mcrsladglv aspsgytgsv tstklkvsgi dvfsagefsg gegcedivlr daargvykrv
      361 ivkgdrliga vlygdtqdgn wyfdllrrqe dvaeirdali fgqafaaggg adanpnaava
      421 alpadaeicg cngvskgkvv taikggactl davractkas ascgsctglv egllavtlgd
      481 afegeraapt vckctsfthe dvrrlildkq lkaipqvmqe lhwttpdgcs scrpalnyyl
      541 lcawpgefvd dnqsrfvner lhaniqkdgt ysvvprmwgg vtnptelrai advaekyear
      601 mlkvtggqrl difgikkedl pavwadlnaa gmvsghayak alrtvktcvg sewcrfgtqd
      661 stglgirieq mtwgsfmphk fkiavsgcpr ncaeasikdi gvicvdsgye lsiggnggik
      721 lrgtdflckv ateqealdyc aafiqlyree aryldrtapw aervgldyir erivddaagr
      781 ealrarflys qsfmqddpwa kraagedykl hqhlaeirpl vta
//
LOCUS       WP_409929009             826 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent helicase HrpB [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929009
VERSION     WP_409929009.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Pietrzyk-Brzezinska,A.J., Absmeier,E., Klauck,E., Wen,Y.,
            Antelmann,H. and Wahl,M.C.
  TITLE     Crystal Structure of the Escherichia coli DExH-Box NTPase HrpB
  JOURNAL   Structure 26 (11), 1462-1473 (2018)
   PUBMED   30174149
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR01970.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..826
                     /gene="hrpB"
     Protein         1..826
                     /product="ATP-dependent helicase HrpB"
                     /EC_number="3.6.4.13"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=86764
     Region          1..821
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
ORIGIN      
        1 marivteptl pvlavlpdll aalraganav lvappgagkt tavapallge dwctgeilll
       61 sprrlaaraa aermavlagq tvgqtygyat rmdskrssat rvtvltegif vnriqsdpel
      121 tgvsavlfde vhersldsdf glalaldaqg glrpdlrlva vsatldggrf salmgaapvi
      181 esagrmfplt lhhlgragea riedavaaai rtalreedgg vlaflpgvge iertaerlag
      241 lgdgialhrl hgnldpgaqr aaiaadphgr rkivlatsia etsltldgvs vvvdcglarr
      301 prydraagmt rlvterasqa avtqragraa rqrpgtayrl weeaataglp rfnppeilea
      361 dlsaltldca lwgvsdprgl awldpppeaa vneararlrt ldaiddggrp tahgaaiakl
      421 plpprlghml vragdiglga vaaevavllg erglggsdad lemrlrrwrg ergaraeggr
      481 rlakrwaslv rhagaaredg lataialafp driarrrdas geawasvggr gfrldptssl
      541 araewlavae tqgmaagari lsaapitqtt vealfgdaiv thrtvafdpa tggvratrer
      601 rlgairlssg pdadpdrdai tqalldgvra aglallpwse aaqgllaria flrgqgrpve
      661 aidaaallar adewltpllt gkrrldaidp galaeglrgv igwdtlrlld aeapthfqsp
      721 agtshpidya aeggprvdlr pqalfglaah psvaggrvpl vlsltspagr piqttrdlpg
      781 fwsgswadva remrgryprh pwpddpaaav pttrtknada rarstr
//
LOCUS       WP_409929013              72 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929013
VERSION     WP_409929013.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..72
                     /product="hypothetical protein"
                     /calculated_mol_wt=7426
ORIGIN      
        1 msvaaryfam vgtriagaag avlgliliar attlppkvig talvlsalvm mavvpralar
       61 rwrtppeegd lr
//
LOCUS       WP_409929014             385 aa            linear   BCT 28-DEC-2024
DEFINITION  phenylalanine--tRNA ligase subunit alpha [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929014
VERSION     WP_409929014.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Abibi,A., Ferguson,A.D., Fleming,P.R., Gao,N., Hajec,L.I., Hu,J.,
            Laganas,V.A., McKinney,D.C., McLeod,S.M., Prince,D.B., Shapiro,A.B.
            and Buurman,E.T.
  TITLE     The role of a novel auxiliary pocket in bacterial phenylalanyl-tRNA
            synthetase druggability
  JOURNAL   J Biol Chem 289 (31), 21651-21662 (2014)
   PUBMED   24936059
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Mermershtain,I., Finarov,I., Klipcan,L., Kessler,N., Rozenberg,H.
            and Safro,M.G.
  TITLE     Idiosyncrasy and identity in the prokaryotic Phe-system: crystal
            structure of E. coli phenylalanyl-tRNA synthetase complexed with
            phenylalanine and AMP
  JOURNAL   Protein Sci 20 (1), 160-167 (2011)
   PUBMED   21082706
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00468.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..385
                     /gene="pheS"
     Protein         1..385
                     /product="phenylalanine--tRNA ligase subunit alpha"
                     /EC_number="6.1.1.20"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0004826 - phenylalanine-tRNA ligase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006432 - phenylalanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=42150
     Region          26..370
                     /region_name="PheS"
                     /note="Phenylalanyl-tRNA synthetase alpha subunit
                     [Translation, ribosomal structure and biogenesis];
                     COG0016"
                     /db_xref="CDD:439787"
ORIGIN      
        1 mpvelhelpp elrksldeig nlgvseeqfh ltrkrildea atsetlaald avrvaalgkt
       61 gvvsiwlkli gglppenrap asyrfnrlre evqvaiadrk aaldraelda klaretldmt
      121 lpaeaaplgs ihpvsqvmde laeifadlgf avatgpeiet qwynftalnm pethparamh
      181 dtfylnahdg eearvlrtht spvqiramqa aggskpirii apgrtyrsds dathtpmfhq
      241 veglvidkgi tlghlkwtle tflkafferd divlrlrpsy fpftepsaev dvgfsvvngk
      301 rviggsdgwm evlgsgmvhr sviaaggydp dewqgfafgc gidrlamlky gmddlraffd
      361 gdarwlkhyg fsaldvptls ggvga
//
LOCUS       WP_409929015             365 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome c oxidase subunit II [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929015
VERSION     WP_409929015.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ostermeier,C., Harrenga,A., Ermler,U. and Michel,H.
  TITLE     Structure at 2.7 A resolution of the Paracoccus denitrificans
            two-subunit cytochrome c oxidase complexed with an antibody FV
            fragment
  JOURNAL   Proc Natl Acad Sci U S A 94 (20), 10547-10553 (1997)
   PUBMED   9380672
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02866.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..365
                     /gene="coxB"
     Protein         1..365
                     /product="cytochrome c oxidase subunit II"
                     /EC_number="7.1.1.9"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004129 - cytochrome-c oxidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38273
     Region          <8..>79
                     /region_name="PRK13729"
                     /note="conjugal transfer pilus assembly protein TraB;
                     Provisional"
                     /db_xref="CDD:184281"
     Region          53..310
                     /region_name="CyoA"
                     /note="Heme/copper-type cytochrome/quinol oxidase, subunit
                     2 [Energy production and conversion]; COG1622"
                     /db_xref="CDD:441229"
ORIGIN      
        1 mrlksillaa flavagpapv saqivppaap qttpapaivp tkadpmlald gaplmlptag
       61 vgmpvdgkvt iqpqvtpngr ralwfhnvil fplitiiclf vlallvwvvi ryrraahpva
      121 sktahntvie vlwtalpvli lacialpsig llqaqfkpap dnavtlkaig nqwywsyqyp
      181 dnggfeitsn llkekdqvgk gerartdadg prllatdtrv vlpygvpirl ittsndvihs
      241 waipafwikl davpgrlnet sftiekpgvy ygvcselcga rhgympitve avspavfaqw
      301 vkakggtmpt gkpaaavaaa qplpetgaaf eagnssapve nataqaptvt qgatgnpaga
      361 gnvgq
//
LOCUS       WP_409929016             290 aa            linear   BCT 28-DEC-2024
DEFINITION  COQ9 family protein [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929016
VERSION     WP_409929016.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Lohman,D.C., Forouhar,F., Beebe,E.T., Stefely,M.S., Minogue,C.E.,
            Ulbrich,A., Stefely,J.A., Sukumar,S., Luna-Sanchez,M., Jochem,A.,
            Lew,S., Seetharaman,J., Xiao,R., Wang,H., Westphall,M.S.,
            Wrobel,R.L., Everett,J.K., Mitchell,J.C., Lopez,L.C., Coon,J.J.,
            Tong,L. and Pagliarini,D.J.
  TITLE     Mitochondrial COQ9 is a lipid-binding protein that associates with
            COQ7 to enable coenzyme Q biosynthesis
  JOURNAL   Proc Natl Acad Sci U S A 111 (44), E4697-E4705 (2014)
   PUBMED   25339443
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Korbel,J.O., Jensen,L.J., von Mering,C. and Bork,P.
  TITLE     Analysis of genomic context: prediction of functional associations
            from conserved bidirectionally transcribed gene pairs
  JOURNAL   Nat Biotechnol 22 (7), 911-917 (2004)
   PUBMED   15229555
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02396.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..290
                     /product="COQ9 family protein"
                     /calculated_mol_wt=31529
     Region          77..288
                     /region_name="COG5590"
                     /note="Ubiquinone biosynthesis protein COQ9 [Coenzyme
                     transport and metabolism]"
                     /db_xref="CDD:444329"
ORIGIN      
        1 mspraigsnn eaiwrnplct cwsecrnggy arhrlrvqei llhckqsygs tllrlhrrra
       61 gttqgaetsp mqtiapdatl deiaiqlapa iaanaafdgw gdeardtaaa gagvdpdval
      121 layprgqidm iaawfrsvda amlarvpaad lttmkireri talvearlai vapdrealrr
      181 alailalpqn vataaklgwa aadtiwraag dtatdynhyt krtilggvya atvtvflddd
      241 sedwadtrgf larridgilr fektkaglla raayrpslsr figrlrypvv
//
LOCUS       WP_409929019             169 aa            linear   BCT 28-DEC-2024
DEFINITION  translation initiation factor IF-3 [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929019
VERSION     WP_409929019.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Ayyub,S.A., Dobriyal,D. and Varshney,U.
  TITLE     Contributions of the N- and C-Terminal Domains of Initiation Factor
            3 to Its Functions in the Fidelity of Initiation and
            Antiassociation of the Ribosomal Subunits
  JOURNAL   J Bacteriol 199 (11), e00051-17 (2017)
   PUBMED   28320882
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Butler,J.S., Springer,M. and Grunberg-Manago,M.
  TITLE     AUU-to-AUG mutation in the initiator codon of the translation
            initiation factor IF3 abolishes translational autocontrol of its
            own gene (infC) in vivo
  JOURNAL   Proc Natl Acad Sci U S A 84 (12), 4022-4025 (1987)
   PUBMED   2954162
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00168.2
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..169
                     /gene="infC"
     Protein         1..169
                     /product="translation initiation factor IF-3"
                     /GO_function="GO:0003743 - translation initiation factor
                     activity [Evidence IEA]"
                     /GO_process="GO:0006413 - translational initiation
                     [Evidence IEA]"
                     /calculated_mol_wt=19136
     Region          2..169
                     /region_name="InfC"
                     /note="Translation initiation factor IF-3 [Translation,
                     ribosomal structure and biogenesis]; COG0290"
                     /db_xref="CDD:440059"
ORIGIN      
        1 mpmngprfne fiqspkvrvi dqdgenlgvm ytreafeqaq avgldlvevs pnadppvakf
       61 ldvgkfkyea qkkanlarks qktqeikeik mrpniddhdy dtkmkkiief igegdkvkvt
      121 lrfrgrelsh gqlgmqllqr vqadaaetak veayprmegr qmlmvlspk
//
LOCUS       WP_409929020             692 aa            linear   BCT 28-DEC-2024
DEFINITION  flagellar biosynthesis protein FlhA [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929020
VERSION     WP_409929020.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR01398.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..692
                     /gene="flhA"
     Protein         1..692
                     /product="flagellar biosynthesis protein FlhA"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0044780 - bacterial-type flagellum
                     assembly [Evidence IEA]"
                     /calculated_mol_wt=72721
     Region          17..685
                     /region_name="FlhA"
                     /note="Flagellar biosynthesis protein FlhA [Cell
                     motility]; COG1298"
                     /db_xref="CDD:440909"
ORIGIN      
        1 malksgaigp farqaslpva ilmlvvlmvv pipsalldvf fimnitisla vlmvalnaqk
       61 pldfsafptv llfatlfrls lnvastrvvl vhghegesaa ghvieafgtf liggdyvvgl
      121 fvftilviin mivvtkgagr vsevsarftl dalpgkqmai dadlnaglit peeakqrrid
      181 vateadfygs mdgsskfvkg davagllila aniigglilg pvshgmtian aahnyvllai
      241 gdalvaqips lmlsiaaaai vtrvkssmdl agqigsqfgs artwtpvaii lgllgvlpgm
      301 phlvilpaaa lagfsawklr qiarrpapae vvapvapadl skigwdevtd amqvnldigy
      361 glvpladerr gsplmaritg vrrqlskdlg fvvpqvrvrd dinlapytyr ivvggvvvge
      421 dsvspdemla ldtgqavgel rgkkakdptf gldavwiatg dtdaatgagy lvvdpgtvva
      481 thlnhqlash asellgpdev qslldglker aanlvaalsp splplttltq vlrgllaeni
      541 plkefrriaa aiavaaqksl dadeiielir pelggliisk lcgvreplrv mtlegqlegl
      601 lgqamradta rrhtiepdlg rrivdalqra aqpliaeakp falvvqpsir vairklvrtc
      661 lpdtpvmsff evpeekavev vavigapgal pa
//
LOCUS       WP_409929023             370 aa            linear   BCT 28-DEC-2024
DEFINITION  flagellar basal body P-ring protein FlgI [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929023
VERSION     WP_409929023.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004353
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..370
                     /product="flagellar basal body P-ring protein FlgI"
                     /GO_component="GO:0009428 - bacterial-type flagellum basal
                     body, distal rod, P ring [Evidence IEA]"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005198 - structural molecule activity
                     [Evidence IEA]"
                     /GO_process="GO:0071973 - bacterial-type
                     flagellum-dependent cell motility [Evidence IEA]"
                     /calculated_mol_wt=37826
     Region          6..370
                     /region_name="FlgI"
                     /note="Flagellar basal body P-ring protein FlgI [Cell
                     motility]; COG1706"
                     /db_xref="CDD:441312"
ORIGIN      
        1 mrvanlrtll gglaavlafs aqpawagsri kdivdfenvr pnqligyglv vglagtgdrm
       61 rnspfteesm qamlermgvn irqaqmktqn vaavsitatm pafsragsai dvtvaalgda
      121 tslqggtlia tslrgldgnt yavaqgqvav sgfkaqgaaa nisrgvstsa riaggaiver
      181 evpyalrsan tlklalrnpd fttaqrvadv inknfpgsaq mldpatvqlt ptsavpggvv
      241 dlltrvenlp vdvdqparvv vneaagtvvm nadvrvspva iaqggltisv aespvasqpa
      301 plssgttqvl prtqinvddg ggkslamleg aslkslvggl nalgvsprdl itilqalkta
      361 galqaeievq
//
LOCUS       WP_409929027             376 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA 2-thiouridine(34) synthase MnmA [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929027
VERSION     WP_409929027.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Hagervall,T.G., Edmonds,C.G., McCloskey,J.A. and Bjork,G.R.
  TITLE     Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase
            from Escherichia coli K-12 has two enzymatic activities
  JOURNAL   J Biol Chem 262 (18), 8488-8495 (1987)
   PUBMED   3298234
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF001138.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK00143
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..376
                     /gene="mnmA"
     Protein         1..376
                     /product="tRNA 2-thiouridine(34) synthase MnmA"
                     /EC_number="2.8.1.13"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
                     /calculated_mol_wt=39852
     Region          24..371
                     /region_name="MnmA"
                     /note="tRNA U34 2-thiouridine synthase MnmA/TrmU, contains
                     the PP-loop ATPase domain [Translation, ribosomal
                     structure and biogenesis]; COG0482"
                     /db_xref="CDD:440250"
ORIGIN      
        1 mkaylvtmis eadfqlgadl sgrrivvams ggvdssvvaa laartgaeti gitlqlydhg
       61 eavgragscc agrdirdarg vcdrlgiahy vfdhessfra dvidgfadey lagrtpipcv
      121 rcnmgpkftd lfkiardlga dclatghyvr rvegaqgael hraadpardq syflfattqs
      181 qldylrfplg glpkprvrel aaelglgvam kpdsqdicfv pdgdyaslvk klrpeadtsg
      241 eivdeggrvl grhkglihft vgqrrgleig gtpeplyvir ldaasrqvvv gpraalgvsa
      301 arlsginwlg gdfagpltak vrslakpvpa wldgdsvrfd apeygvapgq aavlyagerv
      361 lgggwieete ralvaa
//
LOCUS       WP_409929029             386 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929029
VERSION     WP_409929029.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF006580.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09105
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..386
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /calculated_mol_wt=41434
     Region          14..386
                     /region_name="PRK09105"
                     /note="pyridoxal phosphate-dependent aminotransferase"
                     /db_xref="CDD:181651"
ORIGIN      
        1 mlvkedvqdd llgrgfarrd lariaavfgv gaaaatlgrp afasggipdp aptakvriga
       61 necwtgpfmp gqkaaaaiia sgnryaphde rgdfikavma vegvpydhva pwpgssdplc
      121 rsvvtfcspt rglvtadptf elagrtaawl kvpvkavplt ktythdvkam laadpnagly
      181 yictpnnptg titpladiew lldnkpadam vlideaythf agvptasyla akrkdvivmr
      241 tfskifgmag mrmgfimtnp dnlgkmmryd ggmqsgalpl pslacatasl taapliaqrr
      301 aemqsarglt ldhlkkykgl evkpteanmf midwktkpar dvqaafrkqs ieigrswpiw
      361 ptvsritvgs aaemkefcma ldkima
//
LOCUS       WP_409929030              87 aa            linear   BCT 28-DEC-2024
DEFINITION  flagellar biosynthetic protein FliQ [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929030
VERSION     WP_409929030.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..87
                     /product="flagellar biosynthetic protein FliQ"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0009425 - bacterial-type flagellum basal
                     body [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /GO_process="GO:0044780 - bacterial-type flagellum
                     assembly [Evidence IEA]"
                     /calculated_mol_wt=8881
     Region          13..84
                     /region_name="FliQ"
                     /note="Flagellar biosynthesis protein FliQ [Cell
                     motility]; COG1987"
                     /db_xref="CDD:441590"
ORIGIN      
        1 mdaadamaia raglllvlti agpmliasli lgvviglfqa ltqvqeatlt fvpkllgigl
       61 vmlmclpmig ramagfmael sqriiag
//
LOCUS       WP_409929031             205 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome o ubiquinol oxidase subunit III [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929031
VERSION     WP_409929031.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02842.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..205
                     /gene="cyoC"
     Protein         1..205
                     /product="cytochrome o ubiquinol oxidase subunit III"
                     /GO_function="GO:0009486 - cytochrome bo3 ubiquinol
                     oxidase activity [Evidence IEA]"
                     /GO_process="GO:0019646 - aerobic electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=22979
     Site            order(23..24,28,31,38..39,42..43,46)
                     /site_type="other"
                     /note="Subunit I/III interface [polypeptide binding]"
                     /db_xref="CDD:239214"
     Region          25..204
                     /region_name="CyoC"
                     /note="cytochrome o ubiquinol oxidase, subunit III;
                     TIGR02842"
                     /db_xref="CDD:131889"
     Site            order(30,38,75,78,82..83,178,185)
                     /site_type="other"
                     /note="Subunit III/IV interface [polypeptide binding]"
                     /db_xref="CDD:239214"
ORIGIN      
        1 mtaggenldv fydldehehp egystmlgfw mylmsdclif amlfatygvl ghsyaggpgp
       61 rqlfelplva lntamllfss itygfamlam nqnkvgqtql wlfvtalfga afltieltef
      121 aslihegatp qrsaflssff tlvgthglhv tfglvwlftl mvqigrkgli qanrrrlmcl
      181 slfwhfldvi wigvftfvyl mgmlr
//
LOCUS       WP_409929032             402 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF445 domain-containing protein [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929032
VERSION     WP_409929032.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..402
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..402
                     /product="DUF445 domain-containing protein"
                     /calculated_mol_wt=43745
     Region          1..402
                     /region_name="YjiN"
                     /note="Uncharacterized membrane-anchored protein YjiN,
                     DUF445 family [Function unknown]; COG2733"
                     /db_xref="CDD:442039"
ORIGIN      
        1 mrliatglll amaavflvsr tydqrwpalg fvrafaeaam vggladwfav talfrhplgv
       61 piphtaiipr nkdrigdtla tflrdnflip rvvarrmlrl dvagaaglwl anplardgri
      121 argasamtis mlqaldqqrl ggivrgmlgk rladldvapl lgqaltaaia eerhlplldg
      181 ivrwaarile andhliramv hdragsimrw tgldetlsnk iiaglngllt dmadnpehpl
      241 rakadeglas lahdlmhsqe mqarveaika eiianpamqr wldgvweqar vgmmnmardp
      301 drvmrgpigd alrqlgetlg repmlratin rfvrravvgi aadygdnivr lvsetvkgwd
      361 adtitsrlen avgrdlqyir ingtlvgglv glaihtvdva lg
//
LOCUS       WP_409929033             180 aa            linear   BCT 28-DEC-2024
DEFINITION  nucleotide exchange factor GrpE [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929033
VERSION     WP_409929033.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Harrison,C.J., Hayer-Hartl,M., Di Liberto,M., Hartl,F. and
            Kuriyan,J.
  TITLE     Crystal structure of the nucleotide exchange factor GrpE bound to
            the ATPase domain of the molecular chaperone DnaK
  JOURNAL   Science 276 (5311), 431-435 (1997)
   PUBMED   9103205
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF010738.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK14140
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..180
                     /gene="grpE"
     Protein         1..180
                     /product="nucleotide exchange factor GrpE"
                     /GO_function="GO:0000774 - adenyl-nucleotide exchange
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:0051087 - protein-folding chaperone
                     binding [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=19509
     Region          46..176
                     /region_name="GrpE"
                     /note="nucleotide exchange factor GrpE; cd00446"
                     /db_xref="CDD:271355"
     Region          46..88
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
     Site            order(47..48,50..51,54..56,58,61..62,65..66,69..70,72..73,
                     76..78,80..84,86..87,107..108,110..112,115,121..122)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271355"
     Site            order(56,64,86,89,134,136..137,139..143,158,167,171,173,
                     176)
                     /site_type="other"
                     /note="Hsp70 (ATPase domain) interactions [polypeptide
                     binding]"
                     /db_xref="CDD:271355"
     Region          107..122
                     /region_name="2-helical coiled coil"
                     /note="2-helical coiled coil [structural motif]"
                     /db_xref="CDD:271355"
ORIGIN      
        1 mmieenatea adlreetaea spelaehdrt naleaelaea kkaalyahae aqnvrrraek
       61 eaadarayaa tsfardllsv adnlerglat ipaelraddk fkalvtglea tgrelesvfq
      121 rhgikkivam gekldpnfhq amlempsdke pgtvvqemqa gyvikdrllr palvavakag
//
LOCUS       WP_409929038             300 aa            linear   BCT 28-DEC-2024
DEFINITION  polyprenyl synthetase family protein [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929038
VERSION     WP_409929038.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Wallrapp,F.H., Pan,J.J., Ramamoorthy,G., Almonacid,D.E.,
            Hillerich,B.S., Seidel,R., Patskovsky,Y., Babbitt,P.C., Almo,S.C.,
            Jacobson,M.P. and Poulter,C.D.
  TITLE     Prediction of function for the polyprenyl transferase subgroup in
            the isoprenoid synthase superfamily
  JOURNAL   Proc Natl Acad Sci U S A 110 (13), E1196-E1202 (2013)
   PUBMED   23493556
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Wang,K.C. and Ohnuma,S.
  TITLE     Isoprenyl diphosphate synthases
  JOURNAL   Biochim Biophys Acta 1529 (1-3), 33-48 (2000)
   PUBMED   11111076
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Chen,A., Kroon,P.A. and Poulter,C.D.
  TITLE     Isoprenyl diphosphate synthases: protein sequence comparisons, a
            phylogenetic tree, and predictions of secondary structure
  JOURNAL   Protein Sci 3 (4), 600-607 (1994)
   PUBMED   8003978
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..300
                     /product="polyprenyl synthetase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004659 - prenyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0008299 - isoprenoid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32065
     Region          6..300
                     /region_name="IspA"
                     /note="Geranylgeranyl pyrophosphate synthase [Coenzyme
                     transport and metabolism]; COG0142"
                     /db_xref="CDD:439912"
ORIGIN      
        1 mtapatltlg dalaevgadi darfdallsl pgdpredlya amrhaaiggg krlrplltya
       61 tsrlfgvdrd cagraglaie cihvyslihd dlpsmddddm rrgkptvhkl ydeatailag
      121 dslhalafev ladpethpdp fvrselvldl arsagpagma ggqmmdieae kasfdlptit
      181 rlqamktgal iacsveagai lgrlptegrt hlrgyardig lafqiaddil dvegdeaavg
      241 kklgkdgdag ketflsllgl drareqarll vdqaiahlqs ygpeadllrd iarfilerdr
//
LOCUS       WP_409929039             318 aa            linear   BCT 28-DEC-2024
DEFINITION  4-hydroxy-3-methylbut-2-enyl diphosphate reductase [Sphingomonas
            sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929039
VERSION     WP_409929039.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF002188.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK01045
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..318
                     /gene="ispH"
                     /gene_synonym="lytB"
     Protein         1..318
                     /product="4-hydroxy-3-methylbut-2-enyl diphosphate
                     reductase"
                     /EC_number="1.17.7.4"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051745 - 4-hydroxy-3-methylbut-2-enyl
                     diphosphate reductase activity [Evidence IEA]"
                     /GO_process="GO:0019288 - isopentenyl diphosphate
                     biosynthetic process, methylerythritol 4-phosphate pathway
                     [Evidence IEA]"
                     /GO_process="GO:0050992 - dimethylallyl diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=33843
     Region          12..306
                     /region_name="ispH"
                     /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase;
                     Reviewed; PRK01045"
                     /db_xref="CDD:234893"
     Site            order(20,104,203)
                     /site_type="other"
                     /note="Fe-S cluster binding site [ion binding]"
                     /db_xref="CDD:260116"
     Site            order(23,48..49,81..82,132,134,173..174,230..233,275)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:260116"
     Site            order(132,134,231,233)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:260116"
ORIGIN      
        1 mmmsskprld lliaaprgfc agvdraiqiv elaiakhgap vyvrheivhn khvvdalkak
       61 gavfveelde vpdeapvvfs ahgvpksvpa eatvrglswl datcplvskv hrqaerhvqn
      121 grhivfigha ghpevigtlg qvppgamtll etcadvaafa pvdpdnlafl tqttlsvddt
      181 aeivaalkak fptiegprge dicyatsnrq eavkaiaqdc damlvigahn ssnsvrlvev
      241 srregtpaql ipcaaeldfa flngvktlgi sagasapevl vrdlvaklae rfdivereve
      301 ttretisfkl prgleava
//
LOCUS       WP_409929042             257 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929042
VERSION     WP_409929042.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF011648.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK15066
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..257
                     /product="ABC transporter permease"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27449
     Region          13..257
                     /region_name="ABC2_membrane"
                     /note="ABC-2 type transporter; cl21474"
                     /db_xref="CDD:473876"
ORIGIN      
        1 mssginhhgi waiyrfemar slrtvwqsia tpvittslyf vvfggaigsr mstvggvgyg
       61 sfivpgliml slltqsisna sigiyfpkft gtvfellsap vtsmemvagf vgaaasksiv
      121 lgllilatst lfvplhiahp lamiaflvlt svtfslfgfi igvwangfeq lsvvpallvt
      181 pltflggafy sidmlpqpwr tvslfnpvvy lisgfrwsff dkgdvsials lgvtaafmva
      241 clvaialifr tgwrlka
//
LOCUS       WP_409929043             309 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-N-acetylmuramate dehydrogenase [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929043
VERSION     WP_409929043.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF010480.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK13905
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..309
                     /gene="murB"
     Protein         1..309
                     /product="UDP-N-acetylmuramate dehydrogenase"
                     /EC_number="1.3.1.98"
                     /GO_function="GO:0008762 - UDP-N-acetylmuramate
                     dehydrogenase activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=32256
     Region          17..306
                     /region_name="murB"
                     /note="UDP-N-acetylmuramate dehydrogenase; PRK13905"
                     /db_xref="CDD:237553"
ORIGIN      
        1 mgaglerlav iraalalpev rgrlterapl aplvwfktgg aadwlfepad addlsvflag
       61 ldpavpvmal glgsnlivrd ggfpgvvvrl gkvfagvepi dattlrcggg asgilvsska
      121 rdagisgief lrsipgtvgg fvrmnggayg revkdilvgc eavlrsgerv tlslddlgyt
      181 yrhsnlpega ivmsatfrgr peqtaviqge mlriaaarea sqplrsktgg stfknpaghk
      241 awelvdaagc rgltrgdaqv sekhcnflln lgdatsgdie algddvierv kahsgvtlew
      301 eiqrigsak
//
LOCUS       WP_409929045             551 aa            linear   BCT 28-DEC-2024
DEFINITION  thiamine pyrophosphate-binding protein [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929045
VERSION     WP_409929045.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11483154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..551
                     /product="thiamine pyrophosphate-binding protein"
                     /calculated_mol_wt=58219
     Region          2..548
                     /region_name="PRK08199"
                     /note="thiamine pyrophosphate protein; Validated"
                     /db_xref="CDD:181285"
ORIGIN      
        1 mmispppart ggrilvdqll aqgsdriftv pgesflavld alhdtpaidv vvcrqeggva
       61 fmacadgalt grpgiafvtr gpgatnasig vhvamqdsqp milfigdvdr atrdreafqe
      121 infeamfapi akwaaridda rripeyvara yatalsgrpg pvvlalpedm lkdvveaidr
      181 pcveriiqav dpielralag lldtaerpvm ivggagwtgt aardiaawae rsgvpiacaf
      241 rrqdavpndc tvwagnlgyg pnpklvervr aadlllvvgp rlgeattdgy alvtsdhpgq
      301 tlvhvhpdpv elgstyrtdl aicadmasfg dallsidmta laagaqahdd yldwstpapr
      361 dglaldlgpc vaamrdmlpa dtiicngagn ysgwwhrywr yagpvsqlap tagamgygvp
      421 aataaalrhp qrmivalagd gcflmngqel atavthganm lvlvidnggy gtirmhqerd
      481 ypgrvsgtrl gnpdfaalar aygcwaetve ateafapalq ralaepgvkl ihlktemrai
      541 tagamlrdga a
//
LOCUS       WP_409929047             327 aa            linear   BCT 28-DEC-2024
DEFINITION  cupin-like domain-containing protein [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929047
VERSION     WP_409929047.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 10613792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..327
                     /product="cupin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35115
     Region          9..252
                     /region_name="Cupin_8"
                     /note="Cupin-like domain; pfam13621"
                     /db_xref="CDD:463936"
ORIGIN      
        1 miehvgpvas etfaaiteac apvvlrgfgr dwpvvraaaq srsallayla gfdaghpaea
       61 fvgaadiagr ydyaenldgf nfaretmpla galariaaaa ddaqagsiyv gslpverylp
      121 gfaeahtlsv lpagvnpraw igtastiach ydtfdniacv vagqrrftly ppdaigdlyv
      181 gpidltmagq ptslaagapl gdprypryaa aharavtvel epgdalylpk lwwhrvdata
      241 pfnmllnyww dsasvgpdap yttlllamta iahrperera awrayfdhyv frpdghplah
      301 lpeerhgalg rgqlgrirav vmkllrg
//
LOCUS       WP_409929048             273 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate 5-dehydrogenase [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929048
VERSION     WP_409929048.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Johansson,L. and Liden,G.
  TITLE     Transcriptome analysis of a shikimic acid producing strain of
            Escherichia coli W3110 grown under carbon- and phosphate-limited
            conditions
  JOURNAL   J Biotechnol 126 (4), 528-545 (2006)
   PUBMED   16828913
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Zhang,X., Zhang,S., Hao,F., Lai,X., Yu,H., Huang,Y. and Wang,H.
  TITLE     Expression, purification and properties of shikimate dehydrogenase
            from Mycobacterium tuberculosis
  JOURNAL   J Biochem Mol Biol 38 (5), 624-631 (2005)
   PUBMED   16202245
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Singh,S., Korolev,S., Koroleva,O., Zarembinski,T., Collart,F.,
            Joachimiak,A. and Christendat,D.
  TITLE     Crystal structure of a novel shikimate dehydrogenase from
            Haemophilus influenzae
  JOURNAL   J Biol Chem 280 (17), 17101-17108 (2005)
   PUBMED   15735308
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Lindner,H.A., Nadeau,G., Matte,A., Michel,G., Menard,R. and
            Cygler,M.
  TITLE     Site-directed mutagenesis of the active site region in the
            quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli
  JOURNAL   J Biol Chem 280 (8), 7162-7169 (2005)
   PUBMED   15596430
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Vogan,E.
  TITLE     Shikimate dehydrogenase structure reveals novel fold
  JOURNAL   Structure 11 (8), 902-903 (2003)
   PUBMED   12906820
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF009202.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK12550
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..273
                     /product="shikimate 5-dehydrogenase"
                     /GO_function="GO:0004764 - shikimate 3-dehydrogenase
                     (NADP+) activity [Evidence IEA]"
                     /calculated_mol_wt=27943
     Region          1..271
                     /region_name="PRK12550"
                     /note="shikimate 5-dehydrogenase; Reviewed"
                     /db_xref="CDD:183587"
ORIGIN      
        1 mmnkstigrd ttlcmslaar pgtfgsrfhn rlyellgldy vykaftttdl pgviggiral
       61 girgsaismp fkeaviplld gldasaaaid svntivndgg rltgfntdys avrtllgdsg
      121 lapmpfvlrg sggmakavaa alrdagfttg tivarnivag qaiartygfd wraelgdtga
      181 dllvnvtplg magadadala fpqtmiaaaq avidvvalpa etpllkaara agkpcitgda
      241 igmlqaleqf vlytgitpta eqvdtaaafa rgg
//
LOCUS       WP_409929051             144 aa            linear   BCT 28-DEC-2024
DEFINITION  YcgN family cysteine cluster protein [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929051
VERSION     WP_409929051.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF003507.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05170
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..144
                     /product="YcgN family cysteine cluster protein"
                     /calculated_mol_wt=16456
     Region          1..144
                     /region_name="YcgN"
                     /note="Uncharacterized cysteine cluster protein YcgN,
                     CxxCxxCC family [General function prediction only];
                     COG2983"
                     /db_xref="CDD:442222"
ORIGIN      
        1 msnrfwentp iekldraqwe alcdgcgkcc lhkleddetg elfptnvscr lldrrtaqcs
       61 dyrhrhayvs ecvrlnrdnv ysidwlpttc ayrlraagep lpgwhylvsg drdavhrage
      121 svkgwtised dagdfenhvi drvl
//
LOCUS       WP_409929053             496 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929053
VERSION     WP_409929053.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11494953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..496
                     /product="phytoene desaturase"
                     /calculated_mol_wt=54132
     Region          22..496
                     /region_name="crtI_fam"
                     /note="phytoene desaturase; TIGR02734"
                     /db_xref="CDD:274273"
ORIGIN      
        1 mppvtrsaiv vgagfgglal girlqsagid ttiveardka ggrayvwerd gftfdagptv
       61 itdpaclsel walsgrdmae dvslvpvtpf yrlnwadgvs fdysnddpal taeiaklnpd
      121 dvagyrkfld yaagvyeegy vklgakafld fasmikaapa laryqawrsv ysvvssfvkd
      181 ehlrqalsfh tllvggnpmt tsaiyalihk lerdggvwfa qggtnrliag mvthferlgg
      241 vlrlndaats ietvgdratg vttasgwsaq admiacngdv mhvyrdllkt srsaqrtkkr
      301 ldrkryspsl fvvhfgikgt wpgiphhmil fgprykglla diydhgvlpe dfslylhhpt
      361 vtdpsmapeg hstfyalapv phmgkfpvdw aeiapilekr ildeigrrli pdiherivtk
      421 fsytpndfaq dlnahlgsaf slepiltqsa wfrvhnrddq ipnlyfvgag thpgagipgv
      481 vgsakataal mleelr
//
LOCUS       WP_409929054             101 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-binding S4 domain-containing protein [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929054
VERSION     WP_409929054.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Novel predicted RNA-binding domains associated with the translation
            machinery
  JOURNAL   J Mol Evol 48 (3), 291-302 (1999)
   PUBMED   10093218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003114
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..101
                     /product="RNA-binding S4 domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=10651
     Region          5..>92
                     /region_name="HslR"
                     /note="Ribosomal 50S subunit-recycling heat shock protein,
                     contains S4 domain [Translation, ribosomal structure and
                     biogenesis]; COG1188"
                     /db_xref="CDD:440801"
ORIGIN      
        1 maegagetmr ldrflwfarl vktrtvaqal ataghlrlng rpvdraaaav rigaviafat
       61 psgrvrairv aalpdrrgpp aegracytdl lenasqqtpg d
//
LOCUS       WP_409929055             159 aa            linear   BCT 28-DEC-2024
DEFINITION  5-(carboxyamino)imidazole ribonucleotide mutase [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929055
VERSION     WP_409929055.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Meyer,E., Kappock,T.J., Osuji,C. and Stubbe,J.
  TITLE     Evidence for the direct transfer of the carboxylate of
            N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate
            4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia
            coli PurE, an N5-CAIR mutase
  JOURNAL   Biochemistry 38 (10), 3012-3018 (1999)
   PUBMED   10074353
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR01162.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..159
                     /gene="purE"
     Protein         1..159
                     /product="5-(carboxyamino)imidazole ribonucleotide mutase"
                     /EC_number="4.1.1.21"
                     /EC_number="5.4.99.18"
                     /GO_component="GO:0009320 - phosphoribosylaminoimidazole
                     carboxylase complex [Evidence IEA]"
                     /GO_function="GO:0004638 - phosphoribosylaminoimidazole
                     carboxylase activity [Evidence IEA]"
                     /GO_process="GO:0006189 - 'de novo' IMP biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0009152 - purine ribonucleotide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16063
     Region          3..>117
                     /region_name="PurE"
                     /note="Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase
                     [Nucleotide transport and metabolism]; COG0041"
                     /db_xref="CDD:439811"
ORIGIN      
        1 mepqvgiimg stsdwetmrh aadllselgi phesrvvsah rtpqrlydya geaagrglkv
       61 iiagaggaah lpgmaaamth lpvlgvpvqs kalsgldsly sivqmpagip vgtlaigkag
      121 aknaallaaa ilaladapls arlqswrtaq tdgvatepa
//
LOCUS       WP_409929057             411 aa            linear   BCT 28-DEC-2024
DEFINITION  multidrug effflux MFS transporter [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929057
VERSION     WP_409929057.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
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 13022939
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..411
                     /product="multidrug effflux MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43209
     Region          20..399
                     /region_name="MFS_MdfA_MDR_like"
                     /note="Multidrug transporter MdfA and similar multidrug
                     resistance (MDR) transporters of the Major Facilitator
                     Superfamily; cd17320"
                     /db_xref="CDD:340878"
     Site            order(30..31,34..35,60,63..64,121,152,155..156,239,242,
                     360)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340878"
ORIGIN      
        1 mtepiptvta rypmggfefv afiaalmavn algvdlmlpa ladigrdlai gtanerqwiv
       61 tayifgfglg qivygpltdr ygrkrvllaa laafvaaavf aagsgsfaal lgarvlqgvt
      121 sassrvlsva ivrdrfsgrp martlsiaqm iffifpilap tlgsailafg pwrlifysla
      181 gfalvvltwt tfrfaetlpv srripisfaa lrqsyrltlt drfsigyaac galtfggiva
      241 fvsasqqifv defhagdkft vlfavcafsm gcaafansrl verlgmrlis qsavlglivl
      301 slahvavias gretlytyip fqalsmtcia lcgtnfgama mepvghiagt assvqgfiss
      361 vgavavasvi gqsyngttlp laigylgigl gtlalilwie ggrlfraraa a
//
LOCUS       WP_409929062             401 aa            linear   BCT 28-DEC-2024
DEFINITION  HlyD family secretion protein [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929062
VERSION     WP_409929062.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..401
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..401
                     /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=42546
     Region          59..377
                     /region_name="EmrA"
                     /note="Multidrug resistance efflux pump EmrA [Defense
                     mechanisms]; COG1566"
                     /db_xref="CDD:441174"
ORIGIN      
        1 msqndedrie tsetpqgngd ggtdpapakd akpkkkmspv vklvlivlvl vlivvgilwf
       61 ihyqttgkyl qstndatiqa davvvapkvs gyveqvlvvd nqdvkagdpl vridprdyra
      121 kseqaqaqia qadasvqnar agiaeqyaai dqaraqlaaa rakaahdaae varytplaas
      181 gaetrqqlaq ltvtarqsad daraqaatlv aqerkiaslr aqvgqaraqg egaraqlsaa
      241 qvdvgatlir saingrigdk tvvigqyaqa gtrlmsvvpl nrlyitanfk etqlalmrpg
      301 qpatisvdal egtdvhgrve svspgtgaqf sllppqnatg nftkivqrvp vrisieatpa
      361 arrllvpgls vtvsvdtisa kndlkqiqrq ekqrdearkh g
//
LOCUS       WP_409929069              41 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929069
VERSION     WP_409929069.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..41
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..41
                     /product="hypothetical protein"
                     /calculated_mol_wt=4614
     Region          <2..35
                     /region_name="DDE_Tnp_1_2"
                     /note="Transposase DDE domain; pfam13586"
                     /db_xref="CDD:463928"
ORIGIN      
        1 mfgrlkttra iatwydqlae tsmsmihiat arywlafiha a
//
LOCUS       WP_409929072              66 aa            linear   BCT 28-DEC-2024
DEFINITION  EexN family lipoprotein [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929072
VERSION     WP_409929072.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Pohlman,R.F., Genetti,H.D. and Winans,S.C.
  TITLE     Entry exclusion of the IncN plasmid pKM101 is mediated by a single
            hydrophilic protein containing a lipid attachment motif
  JOURNAL   Plasmid 31 (2), 158-165 (1994)
   PUBMED   8029323
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF033894.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..66
                     /product="EexN family lipoprotein"
                     /calculated_mol_wt=7226
     Region          3..59
                     /region_name="Eex_IncN"
                     /note="EexN family lipoprotein; NF033894"
                     /db_xref="CDD:468229"
ORIGIN      
        1 msrliflvla vgigacspta qpvnyykshp ailekrltec vaqfeqskdc inaktaylev
       61 hhlpie
//
LOCUS       WP_409929080              57 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-hairpin-helix domain-containing protein [Sphingomonas sp.
            BAUL-RG-20F-R05-02].
ACCESSION   WP_409929080
VERSION     WP_409929080.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 57)
  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 57)
  AUTHORS   Doherty,A.J., Serpell,L.C. and Ponting,C.P.
  TITLE     The helix-hairpin-helix DNA-binding motif: a structural basis for
            non-sequence-specific recognition of DNA
  JOURNAL   Nucleic Acids Res 24 (13), 2488-2497 (1996)
   PUBMED   8692686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10628864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..57
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..57
                     /product="helix-hairpin-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=6372
     Region          1..49
                     /region_name="HHH_5"
                     /note="Helix-hairpin-helix domain; pfam14520"
                     /db_xref="CDD:434010"
ORIGIN      
        1 mllknsgldr rliqaladag itdtrqlram sdrellrlpg vadrsveair ahfqwtr
//
LOCUS       WP_409929082             922 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929082
VERSION     WP_409929082.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR01782.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     Protein         1..922
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=98871
     Region          61..922
                     /region_name="TonB-Xanth-Caul"
                     /note="TonB-dependent receptor; TIGR01782"
                     /db_xref="CDD:273804"
ORIGIN      
        1 mligasvaal vcgaaspafa qtatalpdpa vqqaatqsgt tapsgdqnva dtpaalnaaa
       61 ddvvvtgvra slqsaqnikr nadqvvdsiv aedigklpdr niaealqris giqiqrnyge
      121 gssvairglt qvrtelngrd iftasgssna lsledvpsel lagidvyknp sadliedqls
      181 gtinfrtrkp fdfdgfkisg svsntyndlv resqpaasll vsdrwhtgig eigvlvsasy
      241 qkssfrqdti stepfytldp tnatdaatla slgrtgqvtt lphgtgigev ygdrrrfgid
      301 aslqwrptdt leltgevfrn dykfrfddys yfayssgasi tpqpgatfay apngdfqsgt
      361 ftnlpigant sldtrhsvtt dyslnakwkp tanltitada qyvdskttdl rsivglngta
      421 ttltqdisga vpsfqitsap gltnaatysn afylddlnna rgkdktgrld aeyrfdggfl
      481 rsikaglrya drsnrfsdtg yryiglsgvp sdleyvdfgd ffrgdadlfg navlfnrtta
      541 lnydatraal gitggavpyl asgtntesqk tytgyaaaff kadqlavpid gnigvrvirt
      601 nvavsgyyqq yglvtnadgt qstvsnptvn pitnttdyts vlpslnlrah ltdklqlrfa
      661 asknisrpnf dqlnpslnit epgaaqltqe hdttggnpyl kpmksnnfdv slewyfthsg
      721 sltaagfykd isdyiqtgis arnvtfadnv tatynvtsys nvanakvkgv evayqqffdf
      781 lpgalkgfgv qgnftyvdsn apspatagpv hnvsleglsk ynynivglye hgllsarvay
      841 nwrsqflmtt sgngtgnlpv fekpfgqlda svsvnvnphf sltangvnll ntvtstfygi
      901 etrprdvmin drkvtivarv tf
//
LOCUS       WP_409929086             742 aa            linear   BCT 28-DEC-2024
DEFINITION  catalase/peroxidase HPI [Sphingomonas sp. BAUL-RG-20F-R05-02].
ACCESSION   WP_409929086
VERSION     WP_409929086.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. BAUL-RG-20F-R05-02
  ORGANISM  Sphingomonas sp. BAUL-RG-20F-R05-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Yang,Y., Zhou,L. and Luo,X.
  TITLE     Non-redundant expression of the two katG genes in Vibrio
            parahaemolyticus V110
  JOURNAL   J Basic Microbiol 59 (5), 535-541 (2019)
   PUBMED   30793344
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Goulart,C.L., Barbosa,L.C., Bisch,P.M. and von Kruger,W.M.A.
  TITLE     Catalases and PhoB/PhoR system independently contribute to
            oxidative stress resistance in Vibrio cholerae O1
  JOURNAL   Microbiology (Reading) 162 (11), 1955-1962 (2016)
   PUBMED   27665757
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00198.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Sphingomonas sp. BAUL-RG-20F-R05-02"
                     /db_xref="taxon:2914830"
     gene            1..742
                     /gene="katG"
     Protein         1..742
                     /product="catalase/peroxidase HPI"
                     /EC_number="1.11.1.21"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=81493
     Region          10..731
                     /region_name="KatG"
                     /note="Catalase (peroxidase I) [Inorganic ion transport
                     and metabolism]; COG0376"
                     /db_xref="CDD:440145"
ORIGIN      
        1 madedpserc pmgrksggag tvrsllgrtn kdwwpealpv eilhqhgvsp dpmgedydya
       61 eafqtldysa lkadltalmt dskawwpady ghygpfmirm awhaagtyrv tdgrggaasg
      121 qqrfeplnsw pdngnldkar rllwpikqky gkhiswadlf ilagnvaies mggptfgfag
      181 grkdvyqseg dtywgaeeqw ighaehqtri rpdeqldleg plaadsmgli yvnpegpggn
      241 pdplgsardm ratfsrmamn seetvaltag ghafgkahga kpaenfgkep aseavhmqgl
      301 gwltdseeig kghittsgie gawsnnptkw tgdyfrllfk ydyelthspa gahqwtpvnp
      361 ewedmapdar dpdkrvptim tsadmalkmd pefraiserf rddqaaldda farawfklth
      421 rdmgpkvryl gpevpeetli wqdpvpqgta psdadvatfa ekvlssglsv gqlvktawas
      481 astyrksdhr ggangarial epqktwaine paelatvlak lnelrgtisl adaivlagsv
      541 aiekaakdag fdakvpftgg rgdatqewtd vesfawmepq adgfrnylrt rqtvkteell
      601 ldkasllgls gpemtvllgg lrvlganhgd kpegvltdrk gqltndffvn llnnetfwel
      661 vdpssdeefi ghdragkhek wratrtdlvf gsnsqlrata evyaengnee kfvqdfikaw
      721 vkvmnadrfd vtakpvtsni at
//
LOCUS       WP_409929090             435 aa            linear   BCT 28-DEC-2024
DEFINITION  TolC family outer membrane protein [Vibrio chagasii].
ACCESSION   WP_409929090
VERSION     WP_409929090.1
KEYWORDS    RefSeq.
SOURCE      Vibrio chagasii
  ORGANISM  Vibrio chagasii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Sharff,A., Fanutti,C., Shi,J., Calladine,C. and Luisi,B.
  TITLE     The role of the TolC family in protein transport and multidrug
            efflux. From stereochemical certainty to mechanistic hypothesis
  JOURNAL   Eur J Biochem 268 (19), 5011-5026 (2001)
   PUBMED   11589692
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR01844.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Vibrio chagasii"
                     /db_xref="taxon:170679"
     Protein         1..435
                     /product="TolC family outer membrane protein"
                     /GO_component="GO:0019867 - outer membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48124
     Region          20..429
                     /region_name="tolC"
                     /note="outer membrane channel protein; Reviewed; cl30340"
                     /db_xref="CDD:357216"
ORIGIN      
        1 mnciqattlg laialslpvg aqtleqavaf tlesnpeiks ayneyiskry lndasggayr
       61 psidldggig yehtdlatna dttdltrkea titltqliwd gsntsndidr taadaesvry
      121 qllsnaqdia levtkvylda vkayevlsls esnlathkei ysdirkrves gigstadmsq
      181 veariakahg nllaaqnnlf dthtqfkrlv gqsplgltfp radagaipyt vdgalakafn
      241 qhpvikiaqa dvdsakfqyk qskstnyptv sfeaaqtwrd daggtegssd efsamvrlry
      301 nlynggsdqd raesaayqln kakdlresty rnveeslrls wsaldltvqq keflsdhvds
      361 asdtvisyek qyrigkrtll dllntenelf earkgyldak ydeqyakyrv mnatgnlltg
      421 lrveipeewn ekvey
//
LOCUS       WP_409929094             310 aa            linear   BCT 28-DEC-2024
DEFINITION  chromosome partitioning protein ParA [Vibrio chagasii].
ACCESSION   WP_409929094
VERSION     WP_409929094.1
KEYWORDS    RefSeq.
SOURCE      Vibrio chagasii
  ORGANISM  Vibrio chagasii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Vibrio chagasii"
                     /db_xref="taxon:170679"
     Protein         1..310
                     /product="chromosome partitioning protein ParA"
                     /calculated_mol_wt=35366
ORIGIN      
        1 mltalvgmis yswssktpet stalveqeaa aqqsddypli enheterqqd alrqpnlpvt
       61 idgkayaeql vslegkslfs efdqfwaqce qannckvqls qleselpkew fellsnypal
      121 ysewktmest ipldsvddle arvalfkqsa qqiwgelahq lfsdqfahld ftlsakavns
      181 ieaneftlhy qkllsqwqsk aealnvetka qqyelamsll pssfsptela sikaelqeiy
      241 ldesqasniv areqqvakqq qtvatyheqf aqlkssldvl rstshrdwst qewdtyyqqq
      301 vsgfretffk
//
LOCUS       WP_409929100             237 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta fold hydrolase [Vibrio chagasii].
ACCESSION   WP_409929100
VERSION     WP_409929100.1
KEYWORDS    RefSeq.
SOURCE      Vibrio chagasii
  ORGANISM  Vibrio chagasii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   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 237)
  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..237
                     /organism="Vibrio chagasii"
                     /db_xref="taxon:170679"
     Protein         1..237
                     /product="alpha/beta fold hydrolase"
                     /calculated_mol_wt=26067
     Region          <57..235
                     /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 mkpevlllwl pgllcdealf qdvnkelpdw vapftydlgt dtsmqalask vlenapesfv
       61 lgglsmggil afevfrqapq rvkglilmdt naadekpevs ekrnalvdka kagefesitp
      121 dilmpvlihp sqlanqeltq ritkmannig verfeahaqa latrpdarpl ladiqvptli
      181 itgkddllcp idnhllmakh ikqvslhvip dcghlstmeq pkivaqhirs wfeaaql
//
LOCUS       WP_409929111             260 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase [Moraxella osloensis].
ACCESSION   WP_409929111
VERSION     WP_409929111.1
KEYWORDS    RefSeq.
SOURCE      Moraxella osloensis
  ORGANISM  Moraxella osloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Moraxella osloensis"
                     /db_xref="taxon:34062"
     Protein         1..260
                     /product="glycosyltransferase"
                     /calculated_mol_wt=30454
ORIGIN      
        1 mtlpnytsap tlpdenryii cmkwgtkyga eyvnrlynmv nrhltlpfqm vcltddstgi
       61 danvkcypip elnlpsnipe rgwkklttfs pdlydlkgta lfldidiviv dnidcfftyq
      121 aqhddsvvii rdwkkpwrmv gnssvyrfkv gqhtypnlls nfeqnfdtir sqvrheqayl
      181 snylrehhhl eywdaswcvs fkyqcvqpfp lsfvkppilp kgakmvifhg evnppdaiig
      241 ksgkwyrkvl ptdwirdywr
//
LOCUS       WP_409929126              78 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF1653 domain-containing protein [Moraxella osloensis].
ACCESSION   WP_409929126
VERSION     WP_409929126.1
KEYWORDS    RefSeq.
SOURCE      Moraxella osloensis
  ORGANISM  Moraxella osloensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Moraxella osloensis"
                     /db_xref="taxon:34062"
     Protein         1..78
                     /product="DUF1653 domain-containing protein"
                     /calculated_mol_wt=8962
ORIGIN      
        1 mlklvieikl giyqhykgnl yqvlhlakhs eseeelivyr alygdygvwv rplvmfaetv
       61 evngeavqrf klikplds
//
LOCUS       WP_409929130              83 aa            linear   BCT 28-DEC-2024
DEFINITION  YdaE family protein [Salmonella enterica].
ACCESSION   WP_409929130
VERSION     WP_409929130.1
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  :: HMM
            Evidence Accession :: NF041288.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..83
                     /product="YdaE family protein"
                     /calculated_mol_wt=9515
     Region          34..83
                     /region_name="YdaE_coli"
                     /note="YdaE family protein; NF041288"
                     /db_xref="CDD:469185"
ORIGIN      
        1 mrspakqqta inrkpglirk iytlltqkgd ptlincaycq kaipeetaye yeliymhgtl
       61 isrkkrkycs krcashdqma hel
//
LOCUS       WP_409929136             253 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein, partial [Salmonella enterica].
ACCESSION   WP_409929136
VERSION     WP_409929136.1
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.
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..>253
                     /product="hypothetical protein"
     Region          <4..>240
                     /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 mflngssaga vsltagkdii lngsvggkgn gvqvtnatln ssagaitvsa stgnivlggt
       61 akltavdnis iralsgavtg gksevsstsg ainvsagtga ltlgavnyta gtnlsletts
      121 gllsvgsnas lqaagdinln gsatsgdavs isggtlsaan gslnlngtan ngagvkvqna
      181 tlnvsslavn gssqsgngfs ltnvtlgssl sdltnvtlss agsgagaini ldssvvnssn
      241 rdtllnmtie nlt
//
LOCUS       WP_409929137             134 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein, partial [Salmonella enterica].
ACCESSION   WP_409929137
VERSION     WP_409929137.1
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.
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..>134
                     /product="hypothetical protein"
ORIGIN      
        1 mflngssaga vsltagkdii lngsvggkgn gvqvtnatln ssgnltltgn sattgtgvnv
       61 tystlnassa aitgssnsgt gfsltnvtlg sslsdltnvt lssagsgaga inildssvvn
      121 ssnrdtllnm tien
//
LOCUS       WP_409929139              20 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein, partial [Klebsiella pneumoniae].
ACCESSION   WP_409929139
VERSION     WP_409929139.1
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.
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..20
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         <1..20
                     /product="hypothetical protein"
     Region          <1..20
                     /region_name="PRK11377"
                     /note="dihydroxyacetone kinase subunit M; Provisional"
                     /db_xref="CDD:183108"
ORIGIN      
        1 svqpgetivl dmrhqrlird
//
LOCUS       WP_409929141             787 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional UDP-N-acetylmuramate--L-alanine
            ligase/D-alanine--D-alanine ligase [Chlamydia trachomatis].
ACCESSION   WP_409929141
VERSION     WP_409929141.1
KEYWORDS    RefSeq.
SOURCE      Chlamydia trachomatis
  ORGANISM  Chlamydia trachomatis
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales;
            Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF011171.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK14573
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Chlamydia trachomatis"
                     /db_xref="taxon:813"
     Protein         1..787
                     /product="bifunctional UDP-N-acetylmuramate--L-alanine
                     ligase/D-alanine--D-alanine ligase"
                     /EC_number="6.3.2.4"
                     /EC_number="6.3.2.8"
                     /calculated_mol_wt=87364
     Region          1..787
                     /region_name="PRK14573"
                     /note="bifunctional UDP-N-acetylmuramate--L-alanine
                     ligase/D-alanine--D-alanine ligase"
                     /db_xref="CDD:184752"
ORIGIN      
        1 msalahvlld rgysvsgsdl segkvveklk nkgaefflgn qeehipegav vvysssiskk
       61 npeflsaksr gnrvvhrael laelaqdqis ifvtgshgkt tvsslitail qeakknpsfa
      121 igglnqegin ggsgseyfva eadesdgsir cytpefsvit niddehlsnf egdrelllas
      181 lkdfalktqq icwyngdcpr lrsclqghtf gldsscdlhi lsyyqegwrl yftakyqdvv
      241 yadievqlvg mhnvlnaaaa mgialslgid egairnafrg fsgvqrrlqr knssetflfl
      301 edyahhpsei sctlravrta vgqrrilaiy qphrfsrlre cidsfpsafk dadevlltev
      361 ysageeaedi syqklaeais qesivkcthi pfhelqrhle qsirvhdvcv slgagnivnl
      421 geklrdfepq klhlgiicgg ksceheisvl sakniakhls ksfydvsyfl itreglwesv
      481 ssletaedsg ksvfdpeiaq rlekvdvvlp ilhgpygedg amqgfletig kpytgpaiaf
      541 saiamnkvft krfmsdlgip vvpylpltla gwkqeqdkwl ahiveafsfp mfvksshlgs
      601 sigvfevhnv ielrdainea fmrdndvfve enrlgckeie vsvlgdgsga fvvaglherr
      661 gsggfidyqe kyglsgkssa qivfdtdlsk eiqeqileaa dkiyrlllgk gscridffvd
      721 eegnfwlsem npipgmtets pfltsfirkg wsyeqivhql vidglqrfnq rqrlistsfv
      781 dqafaiq
//
LOCUS       WP_409929144              23 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein, partial [Salmonella enterica].
ACCESSION   WP_409929144
VERSION     WP_409929144.1
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.
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..23
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..>23
                     /product="hypothetical protein"
ORIGIN      
        1 mnllkslaav ssmtmfsrvl gfa
//
LOCUS       WP_409929150              22 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein, partial [Salmonella enterica].
ACCESSION   WP_409929150
VERSION     WP_409929150.1
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.
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..22
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..>22
                     /product="hypothetical protein"
     Region          1..>22
                     /region_name="uvrA"
                     /note="excinuclease ABC subunit UvrA; PRK00349"
                     /db_xref="CDD:234734"
ORIGIN      
        1 mdkievrgar thnlkninlv ip
//
LOCUS       WP_409929151              60 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein, partial [Salmonella enterica].
ACCESSION   WP_409929151
VERSION     WP_409929151.1
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.
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..60
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..60
                     /product="hypothetical protein"
ORIGIN      
        1 dlsllskskk rreqsyfkkf edsdneglsd fytvdvegfm kkhgeagsin pikvlkrvvr
//
LOCUS       WP_409929152             173 aa            linear   BCT 28-DEC-2024
DEFINITION  virulence membrane protein PagC, partial [Salmonella enterica].
ACCESSION   WP_409929152
VERSION     WP_409929152.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR000732
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            <1..173
                     /gene="pagC"
     Protein         <1..173
                     /product="virulence membrane protein PagC"
     Region          2..173
                     /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 tgvlvvnvaq adtnafsvgy aqskvqdfkn irgvnvkyry eddspvsfis slsylygdrq
       61 asgsvepegi hyhdkfevky gsfmvgpayr lsdnfslyal agvgtvkatf kehstqdgds
      121 fsnkissrkt gfawgagvqm nplenivvdv gyegsnisst kingfnvgvg yrf
//
LOCUS       WP_409929157              80 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein, partial [Salmonella enterica].
ACCESSION   WP_409929157
VERSION     WP_409929157.1
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.
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..>80
                     /product="hypothetical protein"
ORIGIN      
        1 mmgfvaalss siafiilims aqllnmlnas isrdkvmasv hveiqakrlt telkkkemis
       61 yylneddvnn lnfnrniiit
//
LOCUS       WP_181491490             100 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family transcriptional regulator [Klebsiella pneumoniae].
ACCESSION   WP_181491490
VERSION     WP_181491490.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 100)
  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 100)
  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 100)
  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 100)
  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 100)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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
REFERENCE   8  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..100
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..100
                     /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=11038
     Region          9..52
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 mkknsgkqav infigqhpgc sfqdirrgtg ldssvvnssl wqmnrdgevk regecrsyry
       61 tlidttavtd sdpsvqyrqr pggvnpmtnl fnqclagvrk
//
LOCUS       WP_181493979             380 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces sp. SID8358].
ACCESSION   WP_181493979
VERSION     WP_181493979.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SID8358
  ORGANISM  Streptomyces sp. SID8358
            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..380
                     /organism="Streptomyces sp. SID8358"
                     /db_xref="taxon:2690342"
     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=39308
     Region          18..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 mtthhpiaii ggglggltaa rvlhangtea avfdleasag artqggmldi hedsgqmalh
       61 aaglhegfrg ivheggqamr llgpdgtvhv dedddgtgtr pevdrgalrd llldslpdgt
      121 vhwgrkatgv rpigggrhev afadgsavtt dllvgadgaw srvrpllspa epaytgislv
      181 etdlldadtr hpraaavvgt gsfmclgdrr gllahretdg slhiytalra dedwidtidf
      241 gdgaaakaav lahfegwhqd lralvadadg apvprrihal pvghrwdrvp gvtllgdaah
      301 lmspfagega nlamldgael glavaahpgd leaalaayee glfprgeasa aesaanleim
      361 fgghglerma efftsapeag
//
LOCUS       WP_181494238             281 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Thermosulfuriphilus
            ammonigenes].
ACCESSION   WP_181494238
VERSION     WP_181494238.1
KEYWORDS    RefSeq.
SOURCE      Thermosulfuriphilus ammonigenes
  ORGANISM  Thermosulfuriphilus ammonigenes
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Thermodesulfobacteria; Thermodesulfobacteriales;
            Thermodesulfobacteriaceae; Thermosulfuriphilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..281
                     /organism="Thermosulfuriphilus ammonigenes"
                     /db_xref="taxon:1936021"
     Protein         1..281
                     /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=30838
     Region          22..281
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mdfsgmavve vifltgihkl nrlgrlslea plwvaqsade lttlaleava ggakrlvvlg
       61 gdgsinrilp alvyqetalg iiplgrandl awslglphcl eeaikvalkg kvvsrgvfrl
      121 nrhhffvtvg glgfpalvaq waqygrslws ypfwalrlvg rarpltftln sgntiyeakt
      181 lallfgsvnr lghlfrlpvq rpfpfclwlk dhspgkafki lilsflgrlk gqvfflgsds
      241 rlrisldspr tffgdgeila rgrnftvewi shalnlvvpa n
//
LOCUS       WP_181494303             530 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Thermosynechococcus
            sichuanensis].
ACCESSION   WP_181494303
VERSION     WP_181494303.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     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=58569
     Region          1..530
                     /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 matllelrel rvaypktets saatfvvdgv sfcvaagerf glvgesgcgk stigkailql
       61 lppgsqvaga ialqgqsllg ltssqlrrlr geqiglvfqd pmtrlnplms vydhcdellr
      121 shwsawtrsq rrqrivevld rvkipanrlh qyphelsggm rqrvaialal lldppliiad
      181 epttaldvtv aaeildeltr lcqeeqrgll lishdlalma kycdrlavmy qgkivelgaa
      241 rqvlqqpqhp ytqsllaatq ltsrqpppld tapellrvhn lqrhyrvggw lqpqitirav
      301 dgvdltlrrg etlglvgesg cgkstlsrli lqlipanage vvflgrnlaq lpaaqlrtar
      361 rdlqmifqdp haclnpkmtv gqnlleplli hrlmakeaaq ervrqmlaqv eltpsevyvh
      421 ryphalsggq rqrvaiaral ithpqlvvcd epvsmldahi qrqvlalmqq lkeqlqltyl
      481 fithdlavar sfcdriavmh agkivelapt aqlfaqpqhp ytqkllaaal
//
LOCUS       WP_181494326             112 aa            linear   BCT 28-DEC-2024
DEFINITION  HesB/IscA family protein [Thermosynechococcus sichuanensis].
ACCESSION   WP_181494326
VERSION     WP_181494326.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 112)
  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..112
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..112
                     /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=12101
     Region          1..109
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mveltpaaiq elerlqahgv srgraailri qvqpsecsdw rydlalvaep eptdvltqsq
       61 gwtiaiaada aellrglrvd yiedlmggaf rfhnpnasqt cgcgmafrvs ts
//
LOCUS       WP_181494278             228 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Thermosynechococcus sichuanensis].
ACCESSION   WP_181494278
VERSION     WP_181494278.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 228)
  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 228)
  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..228
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..228
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26376
     Region          3..218
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(119,123,126..127,129..130,171,174..175,177..182,
                     185..187,191,193)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(140..147,159,162..163,166)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 msfrcwsppa rvmaillwif cisslrrles laiatllvtl lyllshipwq rfgqrlqqmw
       61 lfllglwlll avtawpiall ltwrlvlcla lgvvlleslt fsewvqvcrw wglppllvdt
      121 laltyrylfe lesqllqmqq alflrgfrls wrrlrpwaqv igifliraee raqqiylamr
      181 lrgygqvlhr rpqfpegapw swgltlgagi gagllatydv lgeiqlpf
//
LOCUS       WP_181494309             109 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Thermosynechococcus sichuanensis].
ACCESSION   WP_181494309
VERSION     WP_181494309.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 109)
  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 109)
  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..109
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..109
                     /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=11850
     Region          <3..107
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkrfywaian llsnacaytp rgaqvtlkir stdhnvqiav vdtgigipea alphvcerfy
       61 rihqgleqpp gfglglaivk qivdahrgql eirsyvgqgt tvvislpqe
//
LOCUS       WP_181494214             355 aa            linear   BCT 28-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB
            [Thermosulfuriphilus ammonigenes].
ACCESSION   WP_181494214
VERSION     WP_181494214.1
KEYWORDS    RefSeq.
SOURCE      Thermosulfuriphilus ammonigenes
  ORGANISM  Thermosulfuriphilus ammonigenes
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Thermodesulfobacteria; Thermodesulfobacteriales;
            Thermodesulfobacteriaceae; Thermosulfuriphilus.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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 355)
  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 355)
  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 355)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 355)
  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..355
                     /organism="Thermosulfuriphilus ammonigenes"
                     /db_xref="taxon:1936021"
     Protein         1..355
                     /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=39071
     Region          13..355
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mfevlpevvl vvdserrvla anraarefvg aalhqsnlkt gelltclhsk raggcgyssf
       61 csfcsikttl eeclksgepv fnreaimale keeavsvinv linclpfels eqkmavltls
      121 ditdlkamer eryeqmerls ligslaasli hdlknpltgv sgfldllrsr lsdedtrkic
      181 qkmegaldra fqvidnillv asgkedvpld iapirvdqlv gsvledfrpl hpvslfldyp
      241 deisvdvgkm rqvlwnlikn adealaetld gqitilswas qdtvticvad ngpgippevr
      301 drlflpgytr gkengrgfgl fgskkiveah ggriwfesvc gqgtkffvql plkst
//
LOCUS       WP_181494467              94 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA recognition motif domain-containing protein
            [Thermosynechococcus].
ACCESSION   WP_181494467
VERSION     WP_181494467.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus
  ORGANISM  Thermosynechococcus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae.
REFERENCE   1  (residues 1 to 94)
  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 94)
  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 94)
  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..94
                     /organism="Thermosynechococcus"
                     /db_xref="taxon:146785"
     Protein         1..94
                     /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=10383
     Region          1..81
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 msiyvgnlsy tatqedleav faeygsvkqv ylpvdretgr krgfgfvems tdaeedaaia
       61 dldgaewmgr qlkvnkarpr eamgggnnry srnr
//
LOCUS       WP_181494511             300 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Thermosynechococcus sichuanensis].
ACCESSION   WP_181494511
VERSION     WP_181494511.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 300)
  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 300)
  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..300
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..300
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=33635
     Region          <36..211
                     /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 msrrrqlwyy plfqiplilf igcvllallf sllnwgrpsv avvlsldlsg stfgnnplqf
       61 nqpqtvmaqq vlaaklylqr nqreltnpne vmihgfgrnv vfltprfetn sdllltqldq
      121 alnrsdllaq vdptetnlsg aiamatqqlq qipnrcrell litdgeapvn pdvvanarqq
      181 rvkinaivvg dhapqlaaas qitggqyrsa pvaileelvg qtffegfnsn arwpifwggm
      241 avicfmwllv lpldrwvlqg wlhlpmnlag qiallnaffw tvaipmilwr fpgwpflqtc
//
LOCUS       WP_181494547             539 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Thermosynechococcus sichuanensis].
ACCESSION   WP_181494547
VERSION     WP_181494547.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 539)
  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 539)
  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 539)
  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 539)
  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..539
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..539
                     /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=61758
     Region          3..438
                     /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 mikvssisiq nyrcidqavk inieplavlv gkndtgksti lralesffnp kqfdwddqht
       61 qgepteisvt celttshqfg erlrkinlls qentfrmrrv weqrgrgcrt slwnfcssew
      121 idvpssgnsa ireiahelve vlpsyqyfha rgtlqeaesa iqqylrriiq kecetnpavl
      181 elqkkletvi ekelesitek iraatsspet lnakrdfnws kvldikftig ekdlainsrg
      241 dgfqritmls yfeylaersi sssntqkqei ifaieepety lhpsaqetlf srlvelthlg
      301 yqvlitshsp iivaqvplss lihvqrqnnl vhyqtenlal eliirdlgia pdsqltslli
      361 qhkgfilveg kddvialsha sqvykkagei ektfeemgvi ilpvggcgni khwlnlqiih
      421 rlnkpfivff dsdresrdsl sprqkelerl dhldpsvifv trkraienyi ldsvvnrlnp
      481 slnlnytdfd nvkklpkagn liekyferlt ftdlkaafvt nneedeflel yrkissmia
//
LOCUS       WP_181495130             234 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Thermosynechococcus
            sichuanensis].
ACCESSION   WP_181495130
VERSION     WP_181495130.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 234)
  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..234
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..234
                     /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=25708
     Region          5..220
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mithwailsg iegnlralea vlkdlqrqrp pvttlyvlgd iiglkgqnda vvqrlqmpdl
       61 eplepqicig wweeqcfnlf gvgmsgevpe liaeqgeaav gqlwesisrs svqwlrslpf
      121 gfheldcllv hgspvsasev ltpatspall cdrliradan qlfcgrsgel fdcwisaegl
      181 taevrtldgt eqqafelpqr rligvgsvgr qlgiasyvly qpgsnylkqc viry
//
LOCUS       WP_181494607             588 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Thermosynechococcus sichuanensis].
ACCESSION   WP_181494607
VERSION     WP_181494607.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
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="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     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=64935
     Region          4..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 mttarpqnqs lpplrvglif gfllmvmggv varlvylqvv qgetlaaraq qqqrrytppt
       61 larypitdrr etvvaldrpv ftlfahpiqf kversaiard lapllkqspe qllakfstyp
      121 tgvpiaydid eetaakiral nydglelnqa wqriypqqel magivgyvdr ehqgqagief
      181 sqnqflqvrg nrqllsmnal gqwlpalapa dprtlsqgyh vrltidsrlq qtarqalqqq
      241 lrkfnakrgt vivlevktga lralvsepay dpnhyyradp alfrnwavsd lyepgstfkp
      301 intaialeln aitpdtvlpd egritvggwp iqnsdfsqrg grgalniaqi layssnvamv
      361 hmmnriparh yyrylhrlgl tekvgsdlpf etaaqlkppe qfinypiepa ttafgqgfsl
      421 tplhlaqllg aianggelit phvidglyde ngqlqkrleq rpprrvfsqr tsqavvkmlg
      481 evvrfgtgkp aqipgyrlgg ktgtaqkaig gtysnlrits fvavfpleqp qyvilavvde
      541 pkgddaygst vaipivravt eslitiegip pshpeelrrv aapasvsq
//
LOCUS       WP_181495156             197 aa            linear   BCT 28-DEC-2024
DEFINITION  prolyl hydroxylase family protein [Thermosynechococcus
            sichuanensis].
ACCESSION   WP_181495156
VERSION     WP_181495156.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10653727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..197
                     /product="prolyl hydroxylase family protein"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=22203
     Region          24..196
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
ORIGIN      
        1 msaaplqild lggeillfqh lipaqqcqqv iataekvgfe daqilmgtvd rsvrgggllr
       61 fdpqdpqqdm mrqillqatq tiqivlyqhy girfpeienf silryrvgeg yrrhvdnlll
      121 asrqmelaqg iptrdvslvg ylnedfqgge tyfdrqgvkv tprtgdvvvf payythphta
      181 lpvvqgtkya fatwlfy
//
LOCUS       WP_181495189             412 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Thermosynechococcus sichuanensis].
ACCESSION   WP_181495189
VERSION     WP_181495189.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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..412
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..412
                     /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=46479
     Region          192..>343
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mghshsaidr ydtrasdrfw qwqagvaale kllvvthpie gflvsfpsli lqdcplktyv
       61 lmpqgrslry lpptnanpal pamtllpavw egmnpfclll spevnlllvy rgerglhfsf
      121 apeeirafwq qlrqqlpltd lhpidqwlas vemvppsyrl vsqfgqwlld ysqppatplt
      181 vtappiaadi sllqalshev rtplttintf iqllqrqedl pqrtyqylqk igqeiqdqit
      241 rfnllsdaae iftrpsskpp lafgqthlte lfttnlsrwq kqaarrqvkl vleyppnlpl
      301 vlsdptsldq vltglveyys qtlapeselq lvvqragqhv klelrspqyk hrsdlaalgr
      361 lllwhpatgq lslnfeaakl lieavgakvi qrrdrqagei ltlylpiakd sg
//
LOCUS       WP_181495414             225 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein
            [Thermosynechococcus sichuanensis].
ACCESSION   WP_181495414
VERSION     WP_181495414.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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..225
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..225
                     /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=25443
     Region          15..214
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mrhkktaptt shispwlywg lwpihrlflp lyfsritivg reqlpkeghf llapkhcsrw
       61 dpvilplvwp yplrfmtnai efggvqgwfi rrlgafavnl nrpqpsslrh aleilnagqp
      121 lvifpeggiv rdqvvrplkp glarlvlqad rplpifpvgi aydpqpqfra rvalwigspl
      181 wtpaerqgnl kqqaqeltqq lqaalhaavl earqcanpra nrpsl
//
LOCUS       WP_181495103             237 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Thermosynechococcus sichuanensis].
ACCESSION   WP_181495103
VERSION     WP_181495103.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
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="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..237
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26063
     Region          2..219
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mplkavlfdf ngvilddeai haalideill qenlrpqrge ydlfclgrsd racldnllsr
       61 rgravtpayl dklvaqkaat yrarlaslep fpffggaial leqlhaaqlk iaivtgalrs
      121 dvdlalergn ltpivdciis aesverskpy pdpylravqq lqtleadlta adclaiedtl
      181 vgvqsareag vkvlgvahty pfhmlqrrch wvldrldqfd laeiarvfdr svaatps
//
LOCUS       WP_181495716              90 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein
            [Thermosynechococcus sichuanensis].
ACCESSION   WP_181495716
VERSION     WP_181495716.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 90)
  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 90)
  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 90)
  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..90
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..90
                     /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=9915
     Region          1..84
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mtlyignlsy eatendlrev fekygairri vlpvdretgk rrgfafvelv detqeaaaid
       61 dldgatwlgr vlkvnkakpk qpggqsnsaf
//
LOCUS       WP_181495199             302 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Thermosynechococcus sichuanensis].
ACCESSION   WP_181495199
VERSION     WP_181495199.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
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="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     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=33202
     Region          6..281
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mreplqrlvn nlrqvmvgke aaielmlvgv lagghvlled vpgvgktlla kalarslagt
       61 fqriqatpdl lptdlsgtni wnpktaefef rpgpvfcnil ladeinratp rtqsallevm
      121 eeyqvtidgv thplpqpffv iatqnpveyq gtfplpeaql drfalcfslg ypteeeelqm
      181 lqrvqggldi nqlepclsla eiqqlrqqvl qvrvesvlqk yilalvrasr esdritlgvs
      241 prgtvmlqrt aqalaflngr dyvlpddvkq laphvlahrl itaagrsgra cvaellemva
      301 vp
//
LOCUS       WP_181495325             255 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Thermosynechococcus
            sichuanensis].
ACCESSION   WP_181495325
VERSION     WP_181495325.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 255)
  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 255)
  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 255)
  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..255
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..255
                     /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=28125
     Region          <6..227
                     /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 mttpahladl kdhviicgyg slgrtlamnl aaaqipfvvi dnqrqrlrla qqsghlfyrg
       61 ddlmdenell avgvdrartl vavladdasn vfitliarrl npnlqilayg elpatesklr
      121 fagadhvvlp ssisaqrivq litrpnvldf leekdershl iellsqldlq ieeftlples
      181 slvglaiaev eakgrgrfii vavrhqngtl vthppltlsl apgdtvialg raaeiktffr
      241 qyaqrqpiry rglrn
//
LOCUS       WP_181496016             411 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Enterobacter].
ACCESSION   WP_181496016
VERSION     WP_181496016.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..411
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45486
     Region          27..383
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqnitkkfrw llltlpllsg cgtlsqmssp egtqellthd sldgdvdsvv rhymaqksvp
       61 gmtvavihnh gspqfytwgv tdavnrypir tdtlfalgsl skgitaevva clvnegqlnw
      121 ndslatllpp gtalsadaqk itllelvtht sglprqnmdv pmlgkfisyl stgdnfygel
      181 dsnnvllyla dwrapknkvp qysntgyali gyilkhktge diqslasryi fhplqmanss
      241 ftpqqlkgyp qralghagdq pkfiprgqlt pdwhfsnnmv aaaslysnae dlaayaryhv
      301 stthnrllds vfaevrdtdi qrpdgvqgia wttdfiglek ityqvgyigg yssfigydke
      361 rgnavvvlqn tfnwsnyigi allmdmakkd glitsgnrfa nnrmpervyq q
//
LOCUS       WP_181495807             135 aa            linear   BCT 28-DEC-2024
DEFINITION  (2Fe-2S) ferredoxin domain-containing protein [Thermosynechococcus
            sichuanensis].
ACCESSION   WP_181495807
VERSION     WP_181495807.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (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   2  (residues 1 to 135)
  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..135
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..135
                     /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=14890
     Region          19..120
                     /region_name="COG3411"
                     /note="2Fe-2S ferredoxin [Energy production and
                     conversion]"
                     /db_xref="CDD:442637"
ORIGIN      
        1 mtspslaqqv aalgighiqr hlflcadqtk plccdkavgl eaweylkkrl kelgldqprp
       61 egcifrtkan clrvcqqgpi lvvypdgvwy hsatpavier viqehvlrgq ivqeyllasp
      121 lperagdrpt nsphg
//
LOCUS       WP_181495324             349 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Thermosynechococcus
            sichuanensis].
ACCESSION   WP_181495324
VERSION     WP_181495324.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
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="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     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=38405
     Region          18..326
                     /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 mrrlpatpal nrfligitlf vlltlvavvg ytsfgwnwld alymyvitvf gigysevrpl
       61 vtpaqrffnm miivagsaat vytigavvql ftegeikrll diqrasrdin klnrhvivcg
      121 fgrigqvmaq elsalktpfv ildvneqrid lalqlgylay lgsaaeeetl qvvgidraia
      181 latvlpndti nvfitltars mnpsllivar anlaateskl rmagadhivl ptkigasqmt
      241 nlirrpridf leqtgdretl nellshidar leeleitady pyvgtrlsgl evrgqgafii
      301 vglrksdgql fpsranplve vgdtlillgh aqdapkfirk yasrsrhsq
//
LOCUS       WP_181496250             464 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Thermosynechococcus sichuanensis].
ACCESSION   WP_181496250
VERSION     WP_181496250.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 464)
  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 464)
  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..464
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..464
                     /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=51756
     Region          101..464
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mlkklwlkiq kwqqlpptqr giviialpvc cllstvgvli wlsasiadye gwvrhtqrvq
       61 legrellnhl idaetgvrgy hltqqvgfle pyytaaaqlp stlenleali sdnphqlahf
      121 qdlksavket fqllaqqlee glnlslaeae qrlyfyqqle qakqamdrsr aainafmsee
      181 drllvdrqqq lealrqtntv vlllavvvgl gssglaihwf rqlyqevdlr gqrlevacdr
      241 larftanash qlrapiaail shaqvgllla rqapeqslpr lekvatlaks mgqlvndllf
      301 laryegvspp dfatsfdlvp lieevvqewq etstashhfh levpsvplmi kgdremlkqv
      361 ilnlltnadr ytpkggtitl qlnqqgtsav invsdtgmgi seaalphifd yfyrdervrq
      421 qgisgsglgl aivrqivhlh rgtvtvhsqe nqgstftvkl plap
//
LOCUS       WP_181496399             350 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Thermosynechococcus
            sichuanensis].
ACCESSION   WP_181496399
VERSION     WP_181496399.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 350)
  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 350)
  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 350)
  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..350
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..350
                     /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=39233
     Region          15..338
                     /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 mqerlqpflt lgaiailvll ivaflwseea lqspvrawet lsnavitlvg eypdrprtfl
       61 gqvlqlllll fgtfafgali gkfssyfvtq alaqtlpmks fsnhiivcnw nakaplvlrq
      121 lieanrhhpr divllcaepi kldpefqera dvfvvqgdpt hhgtlerlna pkakaiilla
      181 dadmeapdek nalialavkh lekipgqeqd ihvvaelvns drqrhlkeag vdevissqdy
      241 ssgilaqsal frqmsevyrq lltysdhtne fyfiepghyp ptlyglsfpa lsawvseyss
      301 hhpdnplllv girrqnqqvl lnprptdfqg ldpsdtlivm ayrpiydlrg
//
LOCUS       WP_181496446             420 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Thermosynechococcus sichuanensis].
ACCESSION   WP_181496446
VERSION     WP_181496446.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
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="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     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=48147
     Region          <130..417
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 meliffgvgl llglmiwfwq wqqvqhalet lleqyaarpf ksspwqrlqt llsqqvqeqe
       61 rchqkmlrcq tvleyapiay levdeancvv ccnevarsll glvhpegrfl lelvrsyeld
      121 clieevrqee tmreqewpya yltptgqtkr kplrarglfl geghvgvfie dceevvrlrd
      181 erdrwaadva helktpltsl rlvtetlqqr vpeslrvwvd rlleeiirls llvqelleln
      241 rlshtpadsl erhpldlvql idtawqsltp laaakdihhe ytgpkqfpyc gnesqlfrll
      301 vnlydnaiky gpvggqvltr llsdreggyl clevidtgsg fppkdlpyvf erfyraqarr
      361 hrfviptdse grmppvgsgs glglaiarqi vechggymqa anhpdyggaw lriylpltsl
//
LOCUS       WP_181496044             692 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Enterobacter].
ACCESSION   WP_181496044
VERSION     WP_181496044.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 692)
  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 692)
  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 692)
  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 692)
  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..692
                     /organism="Enterobacter"
                     /db_xref="taxon:547"
     Protein         1..692
                     /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=76900
     Region          5..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 mlniswdpvl iaisylvafi asfvaldsag kiplssrkaa lfwriaggmt lgigiwsmhf
       61 igmlsmqmpm mmrydlwltl aslgvaiias ataldiavag kkrssfrpiv atailsagvv
      121 smhyigmaal mldgsiiwdr rivglsvvia vvasgtalwl afrlrdkgvf ierllaalvm
      181 gaaicamhyt gmsaahypem shtlpggige lglsiwvsvt tlcllgvmli islidshrrt
      241 grltdnlrql nrqlelqarf daltglanrh qmdlrmqdcl rsallsnrqf aviflnvdhf
      301 krvndtrghs vgdellitva qritsrlsre mtlarlggda fillvpecdd dklnallasl
      361 ledvrrplsi cghtlnttms agvslypqdg etlhelklka daalhhvkdd grngwaryrt
      421 emstaipakp gflqelsqal erdqfelwyq ptwyaqekti hgfeallrwr hpeqgvvlpg
      481 lfipsleqtg liipvgnwai eaacrqlhfw teqgfsqwtl slnlspvqfe qpdifhivss
      541 mlekynlsps rlilevtest alknldrsie llnafnhagi tvsiddfgtg ysnllllsvl
      601 pakelkidks fvtsmlenek tyklvetims iartmemnvv aegieteeqq avltrfgcdy
      661 lqgylfsrpl paeqvpwlll qinserqiip ln
//
LOCUS       WP_181496384             277 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA desaturase [Thermosynechococcus sichuanensis].
ACCESSION   WP_181496384
VERSION     WP_181496384.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 277)
  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 277)
  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..277
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..277
                     /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=32164
     Region          1..270
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mtqatvakpp iawptatfii fvhlgallaf lpgmfswkav llalvlhwlt agigitlgwh
       61 rlvthrsfqv pkwleyflvf cgtlsmqggp iwwvglhrhh hlysdqpndh hdsrkgfwws
      121 hiewmfrevp aeaeiprftk diaddpvyqf ldkyflliqm vlaivlylwg gwpfvvwgif
      181 vrlvtvyhtt wlvnsathaf gyrtfettdh stncwwvall tfgegwhnnh hahqysarhg
      241 lqwweldltw ltirflqllg latkvrlvea paassqd
//
LOCUS       WP_181496225             357 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha
            [Thermosynechococcus sichuanensis].
ACCESSION   WP_181496225
VERSION     WP_181496225.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 357)
  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 357)
  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 357)
  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 357)
  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 357)
  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..357
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..357
                     /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=41362
     Region          1..322
                     /region_name="PobA"
                     /note="Chlorophyllide a oxygenase/letal leaf spot protein
                     [Coenzyme transport and metabolism]; COG5749"
                     /db_xref="CDD:444459"
ORIGIN      
        1 mnssstafsl hegsnflrni wyyglpaadl kpgrcqakvl lgepilfcrt tsgkpfalrn
       61 lcphrgiplh ygrfdgeeve cpyhgwrfna hghctlipsl tsdsdvdlkh fgvfsypvre
      121 vqgnlwiffp akerdsseps ievplvpgfs adtqpqavqk fifpghldqv finfmdpsha
      181 pfvhgawwwr krgklfekak tfdpspygft mrrhpllrks wahhilgghp eveiiyrlpg
      241 irietnysdr htfcflitlt pindqetelt atyywtfpwl aplkpllapl areflnqdlr
      301 ivakqseglk ykppltlike adyqakwyyq ikreyekatq egrefinplk tqvlrwr
//
LOCUS       WP_181496532             285 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Thermosynechococcus
            sichuanensis].
ACCESSION   WP_181496532
VERSION     WP_181496532.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..285
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..285
                     /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=33056
     Region          85..190
                     /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 mkslipslvl kelhpneiaw lestfcrfnn qypsleelwk lmdevwdqln cdpeifdnri
       61 trfynhpiwl lnglfiehhe islmyrrift kwivkhspqr vadygggfgt larmigqalp
      121 stmveviepy phpaavalaa qtanvrycqd lngsydviia tdvfehvsdp lglvfqtaqh
      181 lkpagyylia ncfypvirch lpqtfhfrft wntilenmgl ipiepvaygh afqrnnelsl
      241 snarklekes irlfsfsknl pnfvnkflwt lylkmklend nsvec
//
LOCUS       WP_181496699             426 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein
            [Thermosynechococcus sichuanensis].
ACCESSION   WP_181496699
VERSION     WP_181496699.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 426)
  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 426)
  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 426)
  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..426
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..426
                     /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=48229
     Region          4..384
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mqrlqayrye lmptgeqqrk mrrfagscrf vynkalalqk aryeqgekkl gyaglckllt
       61 ewrnssdtaw ladapvhplq qalkdleray nnffakrasf prfkrkgqsd sfrypdpkqi
      121 kldqansrlf lpklgwlryr nsrevlgavk nitvsqscgk wfvsiqtere veppipqggv
      181 vgidmgiarf atlsdgtfya plnsfkrhes rlrkaqqals rkvkfsnnwk kakarvqrih
      241 arisharrdf lhkistaisk nhavvcvedl qirnmsksaa gtteqpgrnv rakaglnksi
      301 ldqgwfefcr qldyklawrg gwlvvvppqn tsrtcpccgh vsadnrqtqd rfacvecgfe
      361 anadlvgain ilsrgmqklr degrdtldaf sgtaqavspd glwieprwrs eagthrsesg
      421 aaqcra
//
LOCUS       WP_181496727             532 aa            linear   BCT 28-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein
            [Thermosynechococcus sichuanensis].
ACCESSION   WP_181496727
VERSION     WP_181496727.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
REFERENCE   1  (residues 1 to 532)
  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 532)
  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 532)
  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..532
                     /organism="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     Protein         1..532
                     /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=58950
     Region          23..463
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mnspfaaetl lfersrprpe alrviygfpn tysvgitslg yqlvwaqlas rtdvavsrlf
       61 tdvqeplprd pelvgfsfsw eldygnllal leqlgipiwq rdrhdchplv fgggsvltan
      121 pepfadffdv illgdaepll epflttmvqv rtaprsqqle alaqvpglyv pslygisyts
      181 ttgaiqaiep lkptvpatva kqvhrgntla astvvtplaa weqiymvevv rscpelcrfc
      241 lasyltlpfr tpsletlipa ierglavtdr lgllgasitq hpefpalieh lgqpqfdhvr
      301 lslasvrtnt vteslaqlls qrgsqsltia ietgserlrq vinkkletee ilaaashaqa
      361 gglkglkfyg mvglptetda dveatialfr qlkktaprlr ltlgcstfvp kahtpfqwwg
      421 vqpvaekrlk flkkelaklg iefrpesynd sliqalisrg drrlaplleq vrhygtslgs
      481 yrrafkelrg qlpdfeayvt anwpeetilp wqhlqsglpt ktlqnhlqra ia
//
LOCUS       WP_181497067             244 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein [Aeromonas].
ACCESSION   WP_181497067
VERSION     WP_181497067.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 244)
  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..244
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..244
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27930
     Region          20..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 mrvwfwlwll lsvpalgeti rlydyhqhpp fntgvdagls relvkylnek lggeprielw
       61 lvnrarlale madpdfdglv vwvnpawvgd phrerylwtf pvmrdtnelv snidnpvtyr
      121 gpdslkglvf ggvegyryqg iddaagrgel vrqdakkvkt nlellvrgri dvtlvsgssl
      181 gffidaqhyq gklfispfpq ssytrhillp ksrpelhatf ndiaeqmdrd prwhkvlesy
      241 rgtp
//
LOCUS       WP_181496917             423 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Thermosynechococcus sichuanensis].
ACCESSION   WP_181496917
VERSION     WP_181496917.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
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="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     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=47043
     Region          32..419
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mvraiqyrla lwyvgvtall llifatgfff yvrgtlieri ddtlshvvev vsrsliidtg
       61 taeaidwqts lgsrplaale edhidlegft pdqqlawstf sepldlplhl srtaetvqvg
      121 edrwlrqmtv almvgdrllg ylrvshpwfe vtqpsqallw dllvgisitl tlvsisgwfl
      181 srlaiaplqq syaylkqfta dashelrnpv aliqtnvqva latadpetqr qqllvierls
      241 rrlsrlvddl lflarqdsgm iplnaqpchl daillgviee qtpliqqkhl qleleladpq
      301 tseaaayrlw gnpdhlsrll tnllsnavqy tpaggqiqvr ldqqgkfyrv viadngpgip
      361 aselprlfdr fyrlqgtkse gtglglaiaq sivqahrgqi qvtsevgqgt cftillpaei
      421 kei
//
LOCUS       WP_181497257             245 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein [Aeromonas].
ACCESSION   WP_181497257
VERSION     WP_181497257.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
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="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..245
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27921
     Region          23..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 mrivilwgll iwqsawaapa aelklvyfdd fapyswrdeq gkmrglmidv mdrvaaqmgl
       61 rvrhegypwq raqklvrmaq adgfvtiatr errsytlive epvtttvlti ftqrahprma
      121 efqrasrlsd fksltfldyf gngwgkenla gftvhhtinv dnvfkmlaag rgdlmvtdpl
      181 varfklnqlg lsgqvvevpl qlastpfnlc igkhsrfntr itefngalqq lrqsgelari
      241 veryr
//
LOCUS       WP_181497352             253 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aeromonas veronii].
ACCESSION   WP_181497352
VERSION     WP_181497352.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
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="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..253
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28819
     Region          21..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 mrywcwflll fslsgwshpl ikvggypyap fvvklpdsry egltlelidq lnavqkevtf
       61 vfvptsaanr ykaldlgrfs lmlfedtkwg wdtdkfkmtt pflgggevyv alnkagrdqr
      121 ffddpashhl igvtgyhygv gqfnadplyl qrklnitlvk dnvsalqall kgrgevailn
      181 isylnqylqt npdtadqlli sqkwdqqyqh railhpaapi tpaqleqwla elqkkgeldr
      241 lwtkygvqqh atp
//
LOCUS       WP_181497354             499 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alanine/glycine:cation symporter family protein
            [Aeromonas].
ACCESSION   WP_181497354
VERSION     WP_181497354.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 499)
  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..499
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..499
                     /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=53276
     Region          1..454
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mneivnaing viwspaliyl clgvglyfsl rtrflqlrhi kemvrlmfdg kstdagvssf
       61 qalamtlagr vgtgniagva taitfggpga lfwmwmvafl gassafvest lgqvykekin
      121 geyrggpafy iekglgmkwy awtfaiatvf acgvllpgvq ansigsslqt afnidpnvta
      181 aglalllgfi ifggvkrias fastvvpfma lgyiivacvi ialnigqlpg villiwksaf
      241 gldagfgail glaimwgvkr gvysneagqg tgphassaaa vshpakqglv qafsvyidtl
      301 fvcsatgfml litglynvqg pdgaaiytgi asiaagpgyv qtamesmmpg fgsifvaial
      361 fffafttiva yyyiaetnia yinrkinrpw ltfllkialm aatvygtvkt adlawgmgdi
      421 gvglmawlni iailllqkta ftclkdyeaq qaqgidpvfh peklgiknad ywvgkrseen
      481 leleksghqf epdqdrkts
//
LOCUS       WP_181496724             258 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Thermosynechococcus
            sichuanensis].
ACCESSION   WP_181496724
VERSION     WP_181496724.1
KEYWORDS    RefSeq.
SOURCE      Thermosynechococcus sichuanensis
  ORGANISM  Thermosynechococcus sichuanensis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Thermosynechococcus.
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="Thermosynechococcus sichuanensis"
                     /db_xref="taxon:3161974"
     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..242
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mttalitgat gglgqafaqa ladrhhnlil tgrsldtlea lktrlsqkvs vvcipqdlse
       61 pgaayrlygq iqalglgidl linnagfgdy gafgdrdrqq ftamlqvnvt alvelthlvl
      121 qemrlrrqgt iinvssiaaf qplpylavya askafvrhfs ealwaevkpl girvlavcpg
      181 ptatnffera dmtrnpalia qqdtpaqvva etlaalqtdv atvipgqpvn rflalagrlv
      241 prqwlvqqle prfrppaq
//
LOCUS       WP_181497418             251 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aeromonas veronii].
ACCESSION   WP_181497418
VERSION     WP_181497418.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
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="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..251
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27692
     Region          28..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 mkpwigfaga llatlaqasp elgklhyite eykpynyada sgaptglave llqlvwkktn
       61 tpaqpitimp wargyylltq kpnavlfsta rtqardplfk wacpvgyiev vlvglaqrni
      121 titklddaka fnigavradv geqlllnngf detrlmtanr lsqalkmlts grvdllsthk
      181 ttmemlvaeq kidpasfkeq wvlsseqlcf afshpvsdel vkefqtgltq vlasseypll
      241 hskyfptpaa k
//
LOCUS       WP_181497511             254 aa            linear   BCT 28-DEC-2024
DEFINITION  DODA-type extradiol aromatic ring-opening family dioxygenase
            [Aeromonas veronii].
ACCESSION   WP_181497511
VERSION     WP_181497511.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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..254
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..254
                     /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=28176
     Region          5..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(11..13,44,108,164,218,245..246)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:153375"
     Site            order(11,44,218)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:153375"
ORIGIN      
        1 mslapvwfis hgapdlvlre qpatrflrtl rlgelkglvv isahwfsrel qinvelkpel
       61 mydfygfpep lyrmrwpass pewlqqgvsd qlalagltat pvrreldhgv wsplslidpn
      121 seiplvqisi pasftpaqlw qlgevlgalr sqgigilasg aithnlrala pesspvpewa
      181 sqfvdwleqk mayedrlall dyrrlapgav eshphddhlr plfvalgaad gvaptrlhes
      241 wdggslymga yrfg
//
LOCUS       WP_181497442             641 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-binding protein [Aeromonas veronii].
ACCESSION   WP_181497442
VERSION     WP_181497442.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 641)
  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 641)
  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 641)
  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..641
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..641
                     /product="NAD(P)-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70449
     Region          85..>140
                     /region_name="NAD_binding_8"
                     /note="NAD(P)-binding Rossmann-like domain; pfam13450"
                     /db_xref="CDD:433218"
ORIGIN      
        1 msitrrdfln gvaititagv apinllkaae ggstladktl ayppaftglr gnhpgsfepa
       61 hsiardgkqy dfaniplege ydlvivgagi sglaaacfyq qllgankkil lldnhddfgg
      121 hakrnefttp dglrlgyggs eslqsprsvy spvalgllka levnidelaa gfqqtfypdl
      181 glsrgvyfde khfgvnkivn gdpghnvadd iprdrlngrp laefigdfpl ddadkaalla
      241 lheskidyls gmtreqqdew vtrnsyttfl rdkvglsera ityfqqrtnd fqavgidata
      301 cadarlcalp gfdglnltpl daeeqaeldd pyifhfpdgn agltrlmvrk lipqvapght
      361 mqdvvlakfd yskldlpehk vqlrlgstal qaknvrladg klavdvtyik egklhrvrak
      421 qsimagynmm ipymvpempe pqkealrqna kaplvytkvv iknwqafvkl gvhevyspaa
      481 pysrvkldyp vsmggyehpk spdqpmclhm vyvptlpgsg lsareqsrkg ramilgmpfe
      541 qheqmireql qgmlgsagfn heqdilaitv nrwshgysyv tntlfddetq cekwielgrq
      601 pignitians dagwspyaha aideawravn elvamskgga q
//
LOCUS       WP_181497405             638 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Aeromonas veronii].
ACCESSION   WP_181497405
VERSION     WP_181497405.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 638)
  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 638)
  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 638)
  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 638)
  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..638
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..638
                     /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=72033
     Region          7..624
                     /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 mlrgkfvsli lmvtaflgva iwsvwnydra fnavtrytql sawalaqlel evhgfgeslq
       61 lyragsvsqe emnkrfdiaw nrldvflhga eakpvrsrfg aaqaagqlms lfeeyeqdvv
      121 sgtrdstrla rfsieldrdl aairdvmvkn ftgpsaiaqr ellnesrtqn failaflmsa
      181 tmvmlvmlfr evrhqqflaw ndpltrlpnr aalikhlklr aayrgggssi tvclvdlghf
      241 revndslgye igdgllkqla erihsvaapg ifvartgsde faiiisgamp tylrfpfleq
      301 lrteladlaf aadpahrvrv fmgvsqyarp vhtpeemllf adialdsakr qrlhrsvvfs
      361 ramhqhylrn rrlstelrel iqspecqqlc lyyqpivrgq savrlgaevl irwshpeygf
      421 ippldiiala eenglgealg lwifhrlqrd lsifpqdlve lleisvnlss smfnmglaan
      481 veermsvgpl glqqlivelt etialddiel skqiiaslrh igvrvalddf gtgwssfsyl
      541 relyfdklki drsfitaidn dtrqalfvea itslshqlgv rvvaegvenn delkavlsig
      601 vdeiqgyfys rplplqdfll fchryfinrs imqevaqg
//
LOCUS       WP_181497533             756 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Aeromonas veronii].
ACCESSION   WP_181497533
VERSION     WP_181497533.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 756)
  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 756)
  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 756)
  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 756)
  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 20214772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..756
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=86152
     Region          50..>505
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
     Region          <215..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"
ORIGIN      
        1 mnqlfflamm msslsapnld ldkeqlsidl qqaqsmvltd parcvqitta fltraannpq
       61 qiisnrqefg yrepilsyst aaqtigahll kgecllqlgq yqatqqaldk amtladkerq
      121 pelkahglyl kirsqalkpd nqstshalmd qldkqlavpt lkqsqlqiyg rlqrtsydie
      181 nqhfddakah ladariwaak tpnplasawv saisgdlyra lqqpqlalge yidaqqqaks
      241 lndplflgll snqivklyqq eqepqkalqy aneaanyfhs ignpsllcds lmvlarlnre
      301 qgdlnmalvy ffnaldllde gsnrpqasll kyeigktylq sgnlslasny lnaarqshel
      361 sdakeplidt llllgelylk kqeaaiaimq lenaralanq lgdtrrqyev frllslayeq
      421 kgylrqalds ykrfhrlgee vrqqeqameq aairdnyvqv ervqhikele qrlnnsqhqq
      481 erylwssitt slllalfiyl fftlwlklrt arlqlkrtne allieprsgl anwqrlmnrw
      541 premakrqlk sdrwylseqp ssefddklhy llfrvpflvn tlerhgyqas reieqafgay
      601 mdtltpqdgr iydlreghml yvvpqrhvtn lhqlagdllt aiaafpcnyp ldrrislgiv
      661 shpflpkaat aldhnglfdl cylalsgaiq lsekcqqnaw lelaaidcqq aaffngdvwq
      721 cglmaidkgl vkvnsshekq wvnwpslark paadnh
//
LOCUS       WP_181497482             318 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: UDP-glucose 4-epimerase family protein [Aeromonas].
ACCESSION   WP_181497482
VERSION     WP_181497482.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (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   2  (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   3  (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   4  (residues 1 to 318)
  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 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 10142572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..318
                     /product="UDP-glucose 4-epimerase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0016854 - racemase and epimerase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34296
     Region          7..307
                     /region_name="UDP_G4E_4_SDR_e"
                     /note="UDP-glucose 4 epimerase, subgroup 4, extended (e)
                     SDRs; cd05232"
                     /db_xref="CDD:187543"
     Site            order(12,14..17,36..37,39,70..72,91,114..116,142,146,
                     169..172)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187543"
     Site            order(92,116,142,146)
                     /site_type="active"
                     /db_xref="CDD:187543"
     Site            order(116,142,171,184,194,203)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187543"
ORIGIN      
        1 madikstvlv tgasgfvgka vcehllalga nvkgavrshp layyhvqaps ltadanwtaq
       61 lqqvdvvvhc aarvhvmldt atdplaafra vntegtlafa rqaaeagvkr fifissikvn
      121 geqtepgkpf dehvqspped pygrskyeae qglmeiakey gmavtiirpp liygegvkan
      181 fasmmtwvrk giplpfarlt narsllalpn lcdfiahama hpaavnqvfl vadpvavsts
      241 qllaaiaeae gvrcrlfylp prvirvlgrc lgidaklqri ygslemdtrk aqsrlqwsap
      301 yslsqtlslm asihsess
//
LOCUS       WP_181498103             480 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Rhodovulum viride].
ACCESSION   WP_181498103
VERSION     WP_181498103.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum viride
  ORGANISM  Rhodovulum viride
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 480)
  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 480)
  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 480)
  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..480
                     /organism="Rhodovulum viride"
                     /db_xref="taxon:1231134"
     Protein         1..480
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51667
     Region          1..>181
                     /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 mnswlrdpqk lglilisgla lfyftqlpvg qlyrfdeflt ldrtngflrf gdwttvyssn
       61 lpnfqkpplq ywmgavflga gvdetvairi pswifsvvcl vataslarsi vpahphaapa
      121 avillasste fwshamsgml etgsaafvtl allfayralk epanwwwvav avglgalqks
      181 pgalaavavf vagaalaarl rgvalpglrs rifpvaglla lclaaawpll qillhgsaai
      241 rsavdnelig rfspdatsgm rgfgdvwgiv irdepflrlg aiaglfvlpt llrdprlfgf
      301 tavvlgyvas ivlaggavyp rytlnlvplf cavvavwifq sqarlrrkwi ltgimsllll
      361 gplkpailvs gqsardqaaq stvlptvgmq lqddetlvvc gwdrktrfsp gavsfyasng
      421 rpfvyltqke dlgpklsalt grpirgvcss ssfaelsevf daaevverla pdyvvftvrp
//
LOCUS       WP_181498142             214 aa            linear   BCT 28-DEC-2024
DEFINITION  XRE family transcriptional regulator [Rhodovulum viride].
ACCESSION   WP_181498142
VERSION     WP_181498142.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum viride
  ORGANISM  Rhodovulum viride
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..214
                     /organism="Rhodovulum viride"
                     /db_xref="taxon:1231134"
     Protein         1..214
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23040
     Region          <25..78
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          80..189
                     /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 mtedpfiagl ravfeadpel rpatvsakag ldkstirrmf egaiqsprra tslkiadalg
       61 msieeivngt kaadsrtvsi agkvgagarv pvfdayekgd gpqvecpsgl sphnivavei
      121 egdsmepvys agdllfytrw saesvpsdav gkrcvcecee glgwvklire grepglfdlh
      181 sfndqtppmy gvrlkwaapi klhwpaelar rvea
//
LOCUS       WP_181497598             541 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Aeromonas veronii].
ACCESSION   WP_181497598
VERSION     WP_181497598.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
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="Aeromonas veronii"
                     /db_xref="taxon:654"
     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=58909
     Region          3..534
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mknfgwmtgs waialllglp viallfsafs aegdlfrhla dtvlldylgn tlglvvgvvl
       61 lsllfgvpta wlvamcqvpg rralqwalml pmampsyiva yvytdlldys gplqaglral
      121 fgwnspadyw fpairslgga awvlalvlfp yvylltrasf leqsvslihs srllgctpwq
      181 sfrrlslpla rpaimvavsl vametladfa tvhffaintl ttavydtwlg ygslataakl
      241 sclmllavvl lialerrsrs rqqvfqksmg heqplryplk gmsrwlaafw cwglvlagfa
      301 lpfiilldyg vryfelswtp efvrfagnsl aisaltalla mgialllgff rrldggiksl
      361 lplriaamgy ampgtvlaig vlvpltaldf aindlaewlg rqgpgllltg titaivfgyl
      421 vrfvaiaigs vessmgkisp sldmaarslg qgdggmlrrv hlplvrrglf agamlvfies
      481 mkelpaalll rpfnfdtlat hvyqfvsdem lergalgaiv ivlvgllpli wvnrsldspg
      541 h
//
LOCUS       WP_181499918             349 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Klebsiella grimontii].
ACCESSION   WP_181499918
VERSION     WP_181499918.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella grimontii
  ORGANISM  Klebsiella grimontii
            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 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Klebsiella grimontii"
                     /db_xref="taxon:2058152"
     Protein         1..349
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=40131
     Region          12..348
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mkntvkissi elinadclqy lpslpdnsid livtdppyfk vkpngwdnqw kgdedylrwl
       61 dsclaqfwrv lkpagsmylf cghrlaadie llvrerfnll nhiiwakpsg rwngcnkesl
      121 rayfpateri ifadhyqgpy rpkddgyaak cnelkqhvmt plisyfrdar eslgvtsaqi
      181 aeatgkknmv shwfglsqwq lpneadylkl qalfqkiamd khsrnelgkh hhqlvatwqs
      241 lsrkyselqq eyyrlrrpfs vsvtvpytdv wthkpvqfyp gkhpcekpad mleqiitass
      301 rpgdvvadff fgsgstlkqa allgrrglgv eleterfeqt vsemrnllv
//
LOCUS       WP_181499906             587 aa            linear   BCT 28-DEC-2024
DEFINITION  HesA/MoeB/ThiF family protein [Klebsiella grimontii].
ACCESSION   WP_181499906
VERSION     WP_181499906.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella grimontii
  ORGANISM  Klebsiella grimontii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 587)
  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 587)
  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 587)
  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..587
                     /organism="Klebsiella grimontii"
                     /db_xref="taxon:2058152"
     Protein         1..587
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64699
     Region          335..542
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mkdemiqrgi salkdclgad nasallrpae lrvgeaaafy fplpvdytgl errlrigfpn
       61 dfpsespslq vepspwlvwp hamasglclh gfrekpvtgs pekivqdsls rfasivsfsl
      121 enadparret efqneistyw lwqlkrsarn lillgepesd svlyvvsdpr ytghtglnpv
      181 wvssdksair qhfrratgrs vvirspheag ffvkltsfpg ikvpephafl ewlaphisee
      241 slaamskwse kssallsrwv vmalpggdga arftvnlctr kketdrthfy glrssrrqsg
      301 lkkegppasi lssrvniidr gaffsrdrsn taktlenshv vfvgvgslgs avsiqlakag
      361 lgrltlidpd rlespnlgrh mlgaedlgkf ksqamrhrll qdlpvldvta ldtyiewvmg
      421 qkpdifedvd lviittadwe sesalwekka sgakwgliqa wsephtlvgh aliapegrfd
      481 arylfsdrgd frhrftdwpd ggvvplpacg esfipggsag mngvatmvtq aairylttvg
      541 dvtlwhssvy rpdeagvlgg rytgpvlpeg vvqsvfernw pkpgqna
//
LOCUS       WP_181500169              61 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Citrobacter].
ACCESSION   WP_181500169
VERSION     WP_181500169.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     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=7089
     Region          4..61
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mskklpvapl lkidevceii nrhrsrlhvw vregsfpqpv rrngraigfr rgdveewlsr
       61 k
//
LOCUS       WP_181500332             354 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Citrobacter].
ACCESSION   WP_181500332
VERSION     WP_181500332.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..354
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..354
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39054
     Region          26..353
                     /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(208,231,329)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:214009"
ORIGIN      
        1 mktvlktlai camaggmvaq svyaeplviq eqgsfsaggt iitapgkfda ktpldsagqt
       61 whgdhasvfy qipenphkyp ivmlhgagqf srtwettpdg regfqniflr rgfstylvdq
      121 prrgsagrtt vegtvtpkpd eqmwfnqfrv gvwpeyfkgv qfshdkealn qyfrqmtpnt
      181 gpfdinvisd amsavvdksg pailfthsqg ggpgwytamk ndkvkaivaf epgssfvfpe
      241 kelpapmpsa fdtlkgepvp meqfmaltki piliiygdni pdkpvampaq dswrvrlama
      301 rewrdvvnkh ggdvtvthlp eegikgnthf pfsdlnnvqi admvskflee kvlq
//
LOCUS       WP_181500271             188 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Citrobacter sp.
            RHBSTW-00976].
ACCESSION   WP_181500271
VERSION     WP_181500271.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00976
  ORGANISM  Citrobacter sp. RHBSTW-00976
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 188)
  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..188
                     /organism="Citrobacter sp. RHBSTW-00976"
                     /db_xref="taxon:2742674"
     Protein         1..188
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21363
     Region          22..76
                     /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(24,27,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /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 mndvkgkdfa feddrkeklv grirqlaerh kslraaardw glsfstlnny inrgtepsff
       61 vmhdisiken vsmdwlaygs hdpfefnkvi idlqrtqsip grdtwcmifd nleseerkml
      121 infclkegap slarlvshts pldkeflals tsdkerlvrl yeqmkkgspe adsgvgqedl
      181 tstdkkag
//
LOCUS       WP_181500211            1644 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Citrobacter sp.
            RHBSTW-00976].
ACCESSION   WP_181500211
VERSION     WP_181500211.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00976
  ORGANISM  Citrobacter sp. RHBSTW-00976
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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 sp. RHBSTW-00976"
                     /db_xref="taxon:2742674"
     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=180303
     Region          26..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 iqqsqgkplt
       61 lldasevqld gaatlvltfs ipldpeqdfs rvvhvvdkks gkvdgawela pnlkelrlrh
      121 lepnrelvvt ierdllalnk atfaidyekn ittrdvqpsv gfasrgsllp gkvieglpvm
      181 alnvnsvdvn ffrvkpeslg afasqweyrn slsnwesdnl lkmaelvytg rfdlnpernt
      241 reklllplsd ikplqqagiy iavmnqaghy nysnaatlft lsdigvsahr yhnqldvftq
      301 slengaaqqg ievtllnekg qtlaqatsda qghvkletdk daalllarkd gqttlldlkl
      361 paldlaefdi agapgyskqf fmfgprdlyr pgetvilngl lrdsdgktlp dqpvklevvk
      421 pdgqvlrsvv sqpenglyrf swpldssapt gmwhirantg dnqsrmwdfh vedfmperma
      481 lnltankmpl aptdgvkfsv vgyylygapa ngnalqgqlf lrplreavqa lpgfqfgnia
      541 eenlsrslde vqltlddhgr gevttnsqwq ethsplqvil qasllesggr pvtrrveqai
      601 wpadtlpgir pqfaaravyd yrtdttvnqp gvdensnaaf divyadaqge kkavsglqvr
      661 lirerrdyyw nwsegegwqs qfdqkdlveg eqtldlkade tgkvsfpvew gayrlevkap
      721 ndavssvrfw agyswqdnsd gsgavrpdrv tlkldkpgyr pgdtmklhia apaagkgyam
      781 vessegplww qeidvptdgl disipvdktw nrhdlylsal vvrpgdksrs atpkravgll
      841 hlplgdenrr lalalespak mrpnqpltvk ikasvkngdv pkqvnvlvsa vdsgvlnitd
      901 yatpdpwqaf fgqkrygadi ydiygqvieg qgrlaalrfg gdgdelkrgg kppvnhvniv
      961 aqqalpvtln eqgegtvtlp igdfngelrv maqawtaddf gsseskviva apvitelnmp
     1021 rflaggdtsr ltldvtnltd kpqtliinla asgllelmgq dpapvnlapg vrttlfipvr
     1081 aregfgdgei qaqisglnlp getlpvqhkq wkigvrpafp aqtvnygval qpgatwqlpg
     1141 eeltnfspvt mqgqllfsgk pplnlaryir elkaypygcl eqtasglfps lytnaaqlka
     1201 lgiagdsdek rraaveigis rllqmqrdng gfalwdkngs eeywltayvm dflvraneqg
     1261 ysvpaevinr gnerllrylq dpgmmsiryt ddasasrfav qayaalvlar qqkaplgalr
     1321 eiwerraqva sglpllqlgi alknmgdanr seqaltlaln tprrdaqqwm adygsqlrdn
     1381 almlalleen klkpdvqntl lntlseqafg qrwlstqenn alflaartlq dlpgswqaqt
     1441 slseqalage ksqtrnldad alstlnvtnt gnlplwlrld vsgypqtspt pasnvlhier
     1501 qilgldgnsk aldslrsgel vlvwlevkas qnvpdalvvd llpaglelen qnlangsasl
     1561 qdsgsevanl lnqmqqadiq hvefrddrfv aavavnegqp vtlvylarav tpgtyqvpvp
     1621 qvesmyvpqw ratgategll ivrp
//
LOCUS       WP_181501908             255 aa            linear   BCT 28-DEC-2024
DEFINITION  dimethyl sulfoxide reductase anchor subunit family protein
            [Citrobacter freundii].
ACCESSION   WP_181501908
VERSION     WP_181501908.1
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 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..255
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=27130
     Region          5..247
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 mekyelplvi ftvlsqmsvg itliltlrtl qgkleskrly wlvsglvlav asvaailhla
       61 hpdraydali nlqhawlsre ilgatlygaa vgvtflakgh kapavlasvl gialvavqgm
      121 tyaapamvai angltmllff itvwvmgcaa tpllnlapav aalrqgivvc mavmiaapii
      181 wlsggtimqm tahawltspl ylaslvclav afvlsrqger rakaifvllf vgiflsrltf
      241 fgdtistivn ighly
//
LOCUS       WP_181502524              89 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Citrobacter freundii].
ACCESSION   WP_181502524
VERSION     WP_181502524.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..89
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9821
     Region          <29..88
                     /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 msnetvkkvm aekrrmtigq ltdllvsgal rrelgmdkte faglvsvmrs tirrieglea
       61 tpriglifnt aaalrfgidf pvieekakr
//
LOCUS       WP_181502757             348 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Escherichia marmotae].
ACCESSION   WP_181502757
VERSION     WP_181502757.1
KEYWORDS    RefSeq.
SOURCE      Escherichia marmotae
  ORGANISM  Escherichia marmotae
            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..348
                     /organism="Escherichia marmotae"
                     /db_xref="taxon:1499973"
     Protein         1..348
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=39936
     Region          12..335
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mantvkissy elinadclef iqtlpensvd livtdppyfk vkpegwdnqw kgdddylkwl
       61 dqclaqfwrv lkpagslylf cghrlasdte immrerfnvl nhiiwakpsg rwngcnkesl
      121 rayfpateri lfaehyqgpy qpkndgyaak grelkqhvma plisyfrdar eslgitskqi
      181 aeatgkknma shwfgasqwq lpneadykkl qalfarvaae khqrgelekp hhqlvstyse
      241 lnrqyaslqe eykslrryfs isaavpytdv wthkpvqyyp gkhpcekpad mlrqiitass
      301 rpgdlvadff mgsgstikaa lslgrraigv eleeerfnqt vmeiknnr
//
LOCUS       WP_181502137             813 aa            linear   BCT 28-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein [Klebsiella pneumoniae].
ACCESSION   WP_181502137
VERSION     WP_181502137.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 813)
  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 813)
  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 813)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..813
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..813
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=89761
     Region          67..409
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 mseitethaa wvpppfppqg rlpgralqvg qnchqqnsde rryhqelcla agrrvdppcc
       61 ktlhislffd gtgnnlnhdf fianpkhptn iarlfratig tgtaggvpsd gqselfddda
      121 egdgkyfkfy mpgvgtpfpe vndpdystmg lvgavkgedr inwallriid vlmfsatekw
      181 ltttesrrsl kemstswnrl wfggshnrye eftrllndla sdlkpliiqp epgkpkltgi
      241 klyvygfsrg aaaartfvrw lsellpppaa egekppqclq tggmqlpvsv eflglldtva
      301 svgvahvvpv adghmswadg tmelpddety gglikkcvhl vsgheqrlcf pldsvrrang
      361 kyppcatevv ypgmhsdigg gyppgdqgkg naehdghlls qivlhdmysa afncgaplkv
      421 pkqalpekfk sqswrvipld ldsqffvsev lsarfnawre ltlgqttpkt fdpeaashye
      481 ppaaggslet viaeqmawit awridryarg smlkmpfyqr atntealpaa rkaaevirdk
      541 eqekvlsarq nqianqppdr mdelvlqpgv kdfdpkmdqt qlfdaakefg kdyhdgyrip
      601 dnlaqlvldt vlqpvifiln tddeaqeyrr mkrdgearva vlfpyageas naeqpaglvr
      661 elfddqihds rawfmyaalg tremwtgyfr yrmiyfserc skplsplvla gdlvgfatvt
      721 agvvlsfrqk rltgklagla atgavrslev avldkitgea lpelpggaql rafthepgtv
      781 vaqqkarkae eqlargqaal paswledvlt ttv
//
LOCUS       WP_181502993              72 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase, partial [Paranoxybacillus vitaminiphilus].
ACCESSION   WP_181502993
VERSION     WP_181502993.1
KEYWORDS    RefSeq.
SOURCE      Paranoxybacillus vitaminiphilus
  ORGANISM  Paranoxybacillus vitaminiphilus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 72)
  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 carboxy end.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Paranoxybacillus vitaminiphilus"
                     /db_xref="taxon:581036"
     Protein         1..>72
                     /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          5..>72
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msfieyrfkv nwgdtdaagi vfypnfykwm dqathhffsk lgyptskmft enhvsipive
       61 akcqfqsplf fd
//
LOCUS       WP_181502241             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Klebsiella pneumoniae].
ACCESSION   WP_181502241
VERSION     WP_181502241.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 265)
  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..265
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..265
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29240
     Region          25..258
                     /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 msslyqlykh kdkngtgtvv nktytvplse lyvepglnir eidqdhvaef rdafiagesv
       61 ppldvqvtek gvkvidghhr yygaieatka gadiirleck dfvgseadri afmvtrnqgk
      121 pltalerata yqrlrnqgwe pdeiakkvkr slsdvdyhlh lltcgeelis mvragevspt
      181 tavalsrehg pqaasvavrq mdkarasgks kltrsaalpq fsaakarqfl qivadqadie
      241 lpadaraild nyreflketg wesea
//
LOCUS       WP_181502856             369 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Escherichia marmotae].
ACCESSION   WP_181502856
VERSION     WP_181502856.1
KEYWORDS    RefSeq.
SOURCE      Escherichia marmotae
  ORGANISM  Escherichia marmotae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 369)
  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 369)
  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 369)
  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 369)
  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 369)
  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 11471805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Escherichia marmotae"
                     /db_xref="taxon:1499973"
     Protein         1..369
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42336
     Region          150..364
                     /region_name="COG4938"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443965"
ORIGIN      
        1 mnikeyndef mfqpifgadd irhfsttyky seanpttnlt snknylsyfk ytvtqsksdk
       61 kvfgidvlgs klgsfsfenn gfddlatffn rrdrrskkle ipeyynelis akilispils
      121 ipiyspvred fniisnyfns iayeirhell kinylgplrt hprrfysser envkknkgqt
      181 nlgadlyygg ssgqekvnyw mnkfdipykl svenignnit gniislmlcd trnntsvtpa
      241 dvgfgigqvl piitcavtkk nqticveqpe ihlhprlqah ladlfietss nadgnqwiie
      301 thsealmlrl qrrirekkid knsvkvlyvd vgmsgtsvme lplddegdfl khwpegffee
      361 rmketmgid
//
LOCUS       WP_181503280             261 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Escherichia marmotae].
ACCESSION   WP_181503280
VERSION     WP_181503280.1
KEYWORDS    RefSeq.
SOURCE      Escherichia marmotae
  ORGANISM  Escherichia marmotae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 261)
  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..261
                     /organism="Escherichia marmotae"
                     /db_xref="taxon:1499973"
     Protein         1..261
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28990
     Region          22..213
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkklfillyl liflplagis qpvipvmktf ftdttgtvpd gediarkaei frqqtgiapf
       61 ivvvpdinet slrkngkaml ahasssltdv kgsvlliftt reprlivitn gqvessmddk
      121 ylgrlienyt laylnadlwy qgmnnaldil qaqilkqptp pltyyphpeq khesdppgst
      181 stlgfiswaa afvlfsrify yttrfiyalk favamtvanm gyqalclcid nsftiarisp
      241 lwavligvct ffaallwpsk s
//
LOCUS       WP_181503349             112 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Escherichia marmotae].
ACCESSION   WP_181503349
VERSION     WP_181503349.1
KEYWORDS    RefSeq.
SOURCE      Escherichia marmotae
  ORGANISM  Escherichia marmotae
            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: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Escherichia marmotae"
                     /db_xref="taxon:1499973"
     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]"
                     /calculated_mol_wt=11641
     Region          <15..104
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mknssitscv qlvgeipant favvlesdsm stsgggvsip ngstvfvapd rtaqpgnivl
       61 alpkgtttpv irkleiegpd illvptnpry psimlddlsc ilgvcfkiqq di
//
LOCUS       WP_181503480             241 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Dolosigranulum pigrum].
ACCESSION   WP_181503480
VERSION     WP_181503480.1
KEYWORDS    RefSeq.
SOURCE      Dolosigranulum pigrum
  ORGANISM  Dolosigranulum pigrum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Dolosigranulum.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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 241)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..241
                     /organism="Dolosigranulum pigrum"
                     /db_xref="taxon:29394"
     Protein         1..241
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26467
     Region          3..240
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mssiyypgna ngvlllhslt htpnvvfyla nrlkkegwtv yapclsghdq ermlsllkss
       61 vadwtadvqe avqflreegc reiavmgqsl gglltlqlll dqpdiacggi lsapafkkwk
      121 ttaiyeevae rvaandqvgl vpnlakeqqa akkkldrili dlealidtmi pnyekipqpi
      181 fvgqgmvddm vevanaetlt atveqsrlal yeeaghiltt savnrqladd liaflreqgw
      241 e
//
LOCUS       WP_181507299             306 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Klebsiella michiganensis].
ACCESSION   WP_181507299
VERSION     WP_181507299.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella michiganensis
  ORGANISM  Klebsiella michiganensis
            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 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Klebsiella michiganensis"
                     /db_xref="taxon:1134687"
     Protein         1..306
                     /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=32909
     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(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 dmlpcrsren apaftpcvgg aafntavalg rqgmavalfs glsddfmgdm
       61 lrhtldasgv dyspstrapl pttlafvrlv ggqarytfyd ensagrmlte ndlptlgddv
      121 savlfgcisl iaepcgsvye almvreaprr vmfldpnire ifipdrqehl armrrmitla
      181 divklsdedl vwfaepgeeh evigrwlalg pklivvtrga dgadawtadf hlhvpairva
      241 vadtvgagdt vnagilasls qagllqkekl vtlsreqvrq avqlgiraaa vtvsrpganp
      301 pwdhel
//
LOCUS       WP_181507213             409 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella michiganensis].
ACCESSION   WP_181507213
VERSION     WP_181507213.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella michiganensis
  ORGANISM  Klebsiella michiganensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
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="Klebsiella michiganensis"
                     /db_xref="taxon:1134687"
     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=48074
     Region          14..397
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maisdsylks clgrerekve eksdrdglwv risrkgavtf fyryrflgkq dkmtigsype
       61 fglkaareev vkwsailarg enprirqsld kakinsqhtf eelfrewhem vciqketadq
      121 ilrtfelhvf pklgkypanq ltlhnwltvl drlaegytei tkrvisngrq cyswavkrql
      181 lennplsels grdfgiqkkm gertlnrkel aivwraieds rlmernkimy klclvwacrv
      241 geirlaevqh fdfeegvwtv pwenhktgrk skkplirpii pemlpllkra ielapgryvf
      301 sryedkpmse gfhlsissnl vkfmlksyne qvphftvhdl rrtartnfse ltqphiaeim
      361 lghklpgvws vydkhtyiee mrdaygrwwa rlmsiiepdv leftprhag
//
LOCUS       WP_181507261             325 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Klebsiella michiganensis].
ACCESSION   WP_181507261
VERSION     WP_181507261.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella michiganensis
  ORGANISM  Klebsiella michiganensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
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="Klebsiella michiganensis"
                     /db_xref="taxon:1134687"
     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=35692
     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 mtktnlitgf lgsgkttsil hllahkpade kwavlvnefg evgidgalla esgallkeip
       61 ggcmccvngl pmqvglnall rqgkpdrlli eptglghpkq ildmltaaiy epwidlratl
      121 cvldprqlld ekivtndnfr dqlaaadvii snkadratee sqrafaawwq tyagdrrfvs
      181 atrgnidpal ldlprrnlap lpaspehahg hgqkqglaal clpahqrwrr slnsgqgyha
      241 cgwifdaetv fdtvallewa rlvpvgrvkg vmriaegvvr inrqqrdlhi etqnvpppds
      301 rieliadtet dwnalqasll rirls
//
LOCUS       WP_181508925             355 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Citrobacter freundii].
ACCESSION   WP_181508925
VERSION     WP_181508925.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=36576
     Region          36..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 msdprrmrra vgllavrigg havwvsalmc cvllagisig etlipwrhvl stlanhlfdt
       61 hypvdaldag ivwnyrltra lvsascgacl avsgvvlqsl lrnalaepyl lgisagastg
      121 avlialtglg agiismslga figaltafmf vallamaagg rqgggvttqi ilagiassql
      181 fnaitsliit rsanaeqarg imfwllgnls gvrwpdvvla iptalvgial cfcyarhlda
      241 fsfgaesaas lgipvkrtra vliaavtgmt aimvsivgai gfvglvipha arllvgnqhh
      301 rllpvsaltg aifliiadvi srtllpgqvl pigvitalvg apafsiilir gnqnk
//
LOCUS       WP_181508649             334 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Citrobacter freundii].
ACCESSION   WP_181508649
VERSION     WP_181508649.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=35785
     Region          25..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 mqlsnrilpq qplliaavll lgvsslclgq yplslrevfy hlthyndaeg iagqviwtvr
       61 lprilmalla ggalglcgat lqgvfhnplv dphiigvtsg aafggtlail lglspwlmmg
      121 stfffgltal ilvyaiaalq glentlvlil sgiilsgffa alvsliqyqa dteetlpniv
      181 fwllgsfata nwhkvlllav pvgiaatvly qlrwrinlls lndkdarslg vavvplrrsv
      241 lvccaflvaa qvavsgsiaw vglviphlar llvgvdhrrl lpcafwlggg fmivvddiar
      301 tlmhaeiplg iitalfgapl fafllirtsr reks
//
LOCUS       WP_181509178             205 aa            linear   BCT 28-DEC-2024
DEFINITION  IbrB-like domain-containing protein [Citrobacter freundii].
ACCESSION   WP_181509178
VERSION     WP_181509178.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 205)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..205
                     /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]"
                     /calculated_mol_wt=23569
     Region          42..141
                     /region_name="IbrB_like"
                     /note="immunoglobulin-binding regulator IbrB activates eib
                     genes; cd16397"
                     /db_xref="CDD:319255"
ORIGIN      
        1 mqqrltqell sflsglseqe rieainefrk alhsvspfre epvdcvlwvk ndhispndyn
       61 pnnvappekk lllksleadg ftqpivvvhs taeeyeivdg fhrhelgkak aslrprlkgy
      121 lpvaclerer hermaatirh nrargrhqir amseivrels llgwseekig kdlgmdndev
      181 lrlkqinglq elfadrrfsk awtvk
//
LOCUS       WP_181509254             628 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: S9 family peptidase [unclassified Streptomyces].
ACCESSION   WP_181509254
VERSION     WP_181509254.1
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 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..628
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=66824
     Region          40..199
                     /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          363..605
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mteatgsstn asvplweqrf raprvslpdw aedapdralf vsnatgtyel ytwdratgeq
       61 rqvtdrpngt tdgvltpdge avwwfddtdg defgvwmrrp fhggtgaade paaaglapsy
      121 paglaigrdg tavigrstde dgttvhvvrp gaepveiyrh resagvgdls hdgtlialeh
      181 tehgdamhsa lrvvrpdgtt vaelddtegg tkelglavlg fapvagdtrl lvghqrrgrw
      241 epmiwdpvag tqtdlaidlp gdvgaewypd gsallvehgf earselwrye patsdgrlvr
      301 vetptgtvsg atarpdgtve ylwssaaepp vvrsttgavv ldppgdkapa svpvedvwve
      361 gpggrihalv qrpaapaegp fptvfeihgg ptwhdsdafa agpaawvdhg yavvrvnyrg
      421 stgygrawtd alkhrvglie lediaavrew avksgladpa alvlaggswg gyltllgigt
      481 qpgdwalgla avpvadyvta yhdemealka mdrtllggtp eevperfeas spltyvdavr
      541 apvyisagvn dprcpirqve nyvdrlkerd avhevyryda ghgslvveer ikqvrleldf
      601 arrhlaglsp agpgdptgpd egapggga
//
LOCUS       WP_181508908             235 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Citrobacter freundii].
ACCESSION   WP_181508908
VERSION     WP_181508908.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 235)
  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 235)
  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 235)
  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 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   5  (residues 1 to 235)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..235
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..235
                     /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=25771
     Region          9..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 masvmlheee gdlesqmalt aavmadksrs rmlgalmdgr awtatelsav advsastasa
       61 hlarlceqrf vvalaqgrhr yfrlagsdia ellerlmgva waastprkit tppglrhart
      121 cydhlageva vrlfdtlvsr qwltpdgetl tplgreklaq mgivlaagss rrkltcgcld
      181 wserryhsgg vlgatllcwf seqrwikteq gsrhvtftpl girkletefg vktsr
//
LOCUS       WP_181508945             334 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Streptomyces].
ACCESSION   WP_181508945
VERSION     WP_181508945.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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 334)
  AUTHORS   Rosinski,J.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..334
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..334
                     /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=36197
     Region          <263..319
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlrihvsgwd lsrvrmaagp dalwetilsf hrlrdrrasa vfgkwrsetr prlsgevrll
       61 savvpqrgyf pdfltpsqen seplrldagm eavratpper lraeiavlee sgppgarraa
      121 rrarleplre ggpgplgrlv galrdyhraa vepywphvqs aveadrairg ralldggtde
      181 llhslppvir wrapvleady pvdrdlhldg rglllqpsyf crgtpvvlrd pllppvlvyp
      241 vahpaapafa epgpwlgrll gqtrstvlra igdgcttsel arragvslas asqhacvlre
      301 aglvhtlrhg gsvlhtltpl ggsllrggap lavs
//
LOCUS       WP_181508639             325 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Citrobacter
            freundii].
ACCESSION   WP_181508639
VERSION     WP_181508639.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (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   2  (residues 1 to 325)
  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 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
REFERENCE   5  (residues 1 to 325)
  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..325
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..325
                     /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=34200
     Region          1..325
                     /region_name="MDR7"
                     /note="Medium chain dehydrogenases/reductase
                     (MDR)/zinc-dependent alcohol dehydrogenase-like family;
                     cd08276"
                     /db_xref="CDD:176237"
     Site            order(39..41,44,137,141,162..167,185..186,190,205,
                     230..231,233,252..253,276..278)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mkcykltgls npalkletia asapgfgqva iaikavslny rdlivteyak dslpvsdgag
       61 vivevgegvt dyqvgdrvvi gfmpdwvegs yseakkassl ggpgvdgvlt erfivtstgi
      121 cripdslsfe eaatlpcaav tawsalfeyg tlapgstvll qgtggvsifa lqmaklagcr
      181 viitsssdek lararelgad etinyrktpe wadevlkltn gqgvdlavdv tgpatlnltt
      241 ratrfggris ligvlsgfng tidigilekr islqgiyvgp vstlekvvhs gikpyidqaf
      301 tfdeaelayq tlkgsqhfgk vviqi
//
LOCUS       WP_181510011             201 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter freundii complex].
ACCESSION   WP_181510011
VERSION     WP_181510011.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii complex
  ORGANISM  Citrobacter freundii complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 201)
  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 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   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
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13296807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Citrobacter freundii complex"
                     /db_xref="taxon:1344959"
     Protein         1..201
                     /product="helix-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=22316
     Region          3..188
                     /region_name="PRK09935"
                     /note="fimbriae biosynthesis transcriptional regulator
                     FimZ"
                     /db_xref="CDD:182154"
     Region          <140..196
                     /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 mqvvmfdrqs ifihgmnvsl qqripgvdvq gvsqadelwl tlenkpealv mldgdldaef
       61 ccsllqqiae rfatvkvlvt atdcrkkwlq evtklnvlai vprdsdaetf tlalnsvamg
      121 mmfiprdcit atesggqnir llsarqreil tmlaagesnk qigrllnist gtvkahlesl
      181 yqrlevknrt qaammlnnti y
//
LOCUS       WP_181509383             202 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Citrobacter freundii].
ACCESSION   WP_181509383
VERSION     WP_181509383.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=22245
     Region          4..201
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 msdsaannil siyrrhadaf asqrsrtlfe kswldkfisv mggqgsivdi gcgngqpiag
       61 yfiqqgfqlt gvdgspamla rarntfpaqr wleqdmrela lnetfdglia wdsffhlaqq
      121 dqqkmfpifd rlshpgsalm ftsgtdngia mgqfegeplf haslapdeyr allsahgfav
      181 vemvmedphc aghtiwlaqk rg
//
LOCUS       WP_181510914             424 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Citrobacter freundii].
ACCESSION   WP_181510914
VERSION     WP_181510914.1
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 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..424
                     /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=46024
     Region          11..421
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mdklsyasds stsawntylq qiervapylg elshwvdtlr hpkralivdi pvqmddgtir
       61 hfegyrvqhn lsrgpgkggv ryhpdvdlne vmalsawmti kcaalnlpyg gakggvrvdp
      121 fslsegeler ltrrytseig iiigpqkdip apdvgtngkv mawmmdtysm nhgttvtsvv
      181 tgkpihlggs lgrdkatgrg vfvsglevar ranievegar vavqgfgnvg seaarlfaaa
      241 garvvaiqdh tatlfnstgi dmavlsawql ehkqiagfpg aetiaseafw slemdilipa
      301 alegqitrhr aetltcklvl egangptypd addvlasrgi vvvpdvvcna ggvtvsyfew
      361 vqdmasffws eeeinnrmdk imtdamvhvw ekaaekscsl rtaayivace rillarkdrg
      421 iypg
//
LOCUS       WP_181510438             709 aa            linear   BCT 28-DEC-2024
DEFINITION  GumC family protein [Citrobacter freundii].
ACCESSION   WP_181510438
VERSION     WP_181510438.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            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 freundii"
                     /db_xref="taxon:546"
     Protein         1..709
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78023
     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 ivayplismm sskyvstatv
       61 likaqadnvs pfpqvdgfds trsgyyetqy almhsrivle qavrdmklde npeftgekag
      121 argadsnesr qlrmeqalkt laknlnvigi rttnlasity estspqvaad iangvaqafi
      181 nytveqkrlk vekarelnfe kmeeiqksia rqkdemdsyl knaglltfrg idgfeteqls
      241 ivtnrladat qrrvaaesvy nevngggksi esvislpsvs nhaqiqdlri aliqaqrtls
      301 eqrkvygpkn pailkaeadv qsiqsqtgrv lgelkvglrq qylaaladek nyqqqvteqk
      361 eifqkmaskr dawnsqklsl dkmedlyksl yqrtqelsls gvnadavlyd pavpalkpak
      421 pnksllllmv vmlvvvfsim yfivkaamdn sigtlsrmkk rlnvaplgei rrfsgtsgra
      481 qvrdmimknp lnadivhgir trimldnrpl qtlavasteh gdgrsllanl lansfsfdqk
      541 tllidadffn tgglsselas atsaglaell rgeteleqar iklsdnldfi phgkstissl
      601 lmlssehvel lmrelkshyq riiidvaavn qsqdvqlikr avdgvvfivk agagsagqia
      661 naldkieenn gvvigavlna veekdletqe glrslnfstd qlmatpgrv
//
LOCUS       WP_181510929             487 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Citrobacter freundii].
ACCESSION   WP_181510929
VERSION     WP_181510929.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=53109
     Region          17..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 msdvnpilsg saqsiaayqd aieqstqavv ewlkqpemyq gktveqlrer inlnftsqgl
       61 gnqaaierav eyflkdsllv hhaqcvahlh cpslvisqaa evlinatnqs mdswdqspsa
      121 tiieikliew lreqvgypag dagvftsggt qsnlmglmla rdaffarqgh siqqdgltgd
      181 lskikvfcse sahfsvqknm almglgyrsv tqvktdafsr mdladlkdkl aqakangeqv
      241 maivatagtt dagaidplad iaalaaeqqi wmhvdaawgg alllsekyrd flnglelads
      301 vtldfhkqff qtiscgafll kdarhyelmr yqaaylnsdf deeagvpnlv skslqttrrf
      361 dalklwmgle algkkqyaei idngvtlard vaefvktqph lelvmepqla svlfrfrpqs
      421 ddmafvalln qrigdvllas gsanvgvtea dgitclkltl lnptvcledv kvllasvktt
      481 aeqllna
//
LOCUS       WP_181511014             262 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Citrobacter freundii complex].
ACCESSION   WP_181511014
VERSION     WP_181511014.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii complex
  ORGANISM  Citrobacter freundii complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter freundii complex"
                     /db_xref="taxon:1344959"
     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=29800
     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 ldevkaaike tglpvttacg
       61 gydgwigdfi eerrlnglqr itrilealae vggqgiivpa awgmftfrlp pmtsprsleg
      121 drkaisdsli yldkvaqrtg tvvyleplnr yqdhmintla darryivenn lkhvqiigdf
      181 yhmnieeddm aqalhdnrdl lghvhiadnh ryqpgsgtld ftalfdqlre dnyqgyvvye
      241 grvraenlpe ayrqslawlr tc
//
LOCUS       WP_181511690             331 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Klebsiella grimontii].
ACCESSION   WP_181511690
VERSION     WP_181511690.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella grimontii
  ORGANISM  Klebsiella grimontii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
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="Klebsiella grimontii"
                     /db_xref="taxon:2058152"
     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=34893
     Region          27..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 mrshparhlw lmtlllivlt llattlgamr lpltsllpag deilrniwlt irlprvllal
       61 lvgaalalsg cvmqglfrnp ladpgllgis ggaalavacw lvlplslpal lalyapmlaa
      121 figstavmvv ifilsragda slsrlllvgi ainalcgalv gvlawisndt qlrqlslwgm
      181 gslgqaewst llvaatlmip aslvvwamas rlnllqlgde eahylgvnvr alqrllllcs
      241 allvasavai sgiigfiglv vphlmrmwlg pdhrglvpgs llcgaillll adtlartvaa
      301 paempvgllt svlgapwflw lifrqeketh g
//
LOCUS       WP_181511476             345 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Klebsiella
            grimontii].
ACCESSION   WP_181511476
VERSION     WP_181511476.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella grimontii
  ORGANISM  Klebsiella grimontii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
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="Klebsiella grimontii"
                     /db_xref="taxon:2058152"
     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=38694
     Region          8..326
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktikgpgif laqfigsqap fntleglaqw aaglgyqalq ipcnhpaifd veraaasqty
       61 cdevsgklae hglaigelst hlegqlvavh paydtafdaf dafapaalrg npqarqqwav
      121 ekvrqaavas arlglkahat fsgalawpyf ypwpphnqpl ldeafdelar rwrplldvfd
      181 eqgvdlcyei hpgedlhdgv tferflqrld nhprcnilyd pshlhlqqmd ylafidiyha
      241 rikafhvkda efrrdgrsgv yggyqnwpqr agrfrslgdg qidfktifsk lteydfdgwa
      301 vlewecclkd aevgaregse firrhiipvs grafddfaag kegre
//
LOCUS       WP_181511515             463 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Klebsiella grimontii].
ACCESSION   WP_181511515
VERSION     WP_181511515.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella grimontii
  ORGANISM  Klebsiella grimontii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 463)
  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 463)
  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 463)
  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..463
                     /organism="Klebsiella grimontii"
                     /db_xref="taxon:2058152"
     Protein         1..463
                     /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=50342
     Region          33..402
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mavvtlstvp hpplwrdvps vtlddetlrl rkakvlanml qrgldtlivy adkehggnfe
       61 yltgfiprfe eallvlhrdg eaalvlgnen lklagyarle nrvihapwfs lpnqpmdtrk
      121 tlaqllqeag vaaeksigla gwklftgaad nrsqmfdlpa fivdalrqaa gpqaklsnat
      181 gifidpaegt ritnnanela hyeyganlas tailtalnai apgktekqig allaaegqpn
      241 svvmiaatgd rfanaglypg dkviqrgdkf slttsfkggl ssraayvvad erelapevad
      301 ylevvakpyf kavvnwlenl rigmrggdmy alieqvlpka eyhwhlnpgh lvadeewlcs
      361 pigphsaacl qsgmilqidi ipsragygga siedtvalad gplrqalaqr ypqlwqriva
      421 rrlyigeqlg ivlseevlpf sstvgylrpw llsperalvc apy
//
LOCUS       WP_181510796             562 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Citrobacter freundii].
ACCESSION   WP_181510796
VERSION     WP_181510796.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            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 freundii"
                     /db_xref="taxon:546"
     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=60432
     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 pvialiwqat qsdlshwdnl
       61 ltyvlpaalk ntvlllagva vmvgvigvgs awavtawdfp grkilswall lplamptyiv
      121 afawldllhp igplqtftrf llgfdsprqf rlpdlrslsg aiillglvly pyvylttram
      181 fisqpahlle aartlgcsat gtffrvalpm arpalavgis lalletlndi gaseflgvqt
      241 ltvtvyttwi srsdlsaaaq iacmmlmfif liltlefygr rkqgfssrsl reiqptrvqg
      301 wrgwllggvi slpvvlgfla pvlflmwesa krigdenpls ssllsalqnt lslaagttlv
      361 vvcvsmlvaw sarhsaadna mpgfrrgvmr laslgyavpg tilaigfltp amavdrwlad
      421 lldvrglplm sagillvicc amrfqaiaig aldsglgrip psleqasrll gengtgtfvr
      481 vhfpllrpal vssallvfad amkelpttll lrpvnfetla tllyaeaarg tyeegaiaal
      541 mivlagtlpv illvrhqmtr rg
//
LOCUS       WP_181511799             341 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Klebsiella].
ACCESSION   WP_181511799
VERSION     WP_181511799.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Klebsiella"
                     /db_xref="taxon:570"
     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=34616
     Region          38..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 msasalllpr rqsrprlalv llsllllggs lvhlglgarw iapqtvlqal fhydprnfdh
       61 riivdlrlvr laaalltgaa lgvaglllqt virnplgeph ilglnagasl avvatsalgi
      121 slggvalarp lsaacgaall fggvmllsss grggvtplri tlcgvalsaf asavtaaili
      181 ldeqtllamr twlagdlagl nwqtlraall palagvtval aiaprlnvla lgdkvalglg
      241 vkivqtrllg laaiallcgs svavagpigf vglvvphavr rlisqdirla lplaapvgal
      301 vllladiaar tlvapqelat gamtalvgap vfifiaarff k
//
LOCUS       WP_181512275             654 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Citrobacter].
ACCESSION   WP_181512275
VERSION     WP_181512275.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 654)
  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 654)
  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 654)
  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 654)
  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..654
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..654
                     /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=73797
     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 nrsalqaylk kmhtldaplg rlssgalnkd vnsinnanqk iqtlyyiysa tsvlliilsa
      181 ilgvlifyqn rnilrahlqv kslaeelqks keklqiqnak leydvyhdsl temnnrqlfw
      241 sdlnktieia eknhdsvtvm lfdldrfkev ndtyghdagd mllrqisdrl vsmsltsdtl
      301 yrlggdefaf lssgltesha vsraqkicef isqpytiynt iinittcvgi visdterrsd
      361 ylykfadlal yeakgegsgk ikvfrqrmle klqesrtleh dmalaivnke fvvyyqpivd
      421 sfsqeiysye alirwlhplk gllspdsfip vaektgmine mgkavleiac reaacwavpa
      481 kisvnvspvq lsskafvgii lsilketglp adrlelevte sslftesttp mntlnklral
      541 gvkisiddfg tgysslsrls klafdkikid ksfvhsisth edalniikli tgmakslnmk
      601 avaegvetqe qlkslqalgc dfaqgylfgk pqpcvneeir ngqvvlinnr ktmp
//
LOCUS       WP_181511029             410 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Citrobacter freundii
            complex].
ACCESSION   WP_181511029
VERSION     WP_181511029.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii complex
  ORGANISM  Citrobacter freundii complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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 410)
  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 410)
  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 410)
  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 410)
  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..410
                     /organism="Citrobacter freundii complex"
                     /db_xref="taxon:1344959"
     Protein         1..410
                     /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=46217
     Region          145..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 msttelhsld lltlpvwivs phteelvfan tvarelmqap cfsllrkgif sthaqndltm
       61 ylsdlrnhhd iveiltvyre gedvamasrl sirtlpesgd vilfegietp tsqglkasrs
      121 anyqrkkqgf yarffqtnsa pmllidpsrd glivdanlsa lnfygyshdt mcqkhtwein
      181 tlgrhilpvm heiahlpggh kplhfvhkla dgtsrhvqty agpieiygnk lmlciihdit
      241 eqkrleqele raalrdaltg llnrrhfyqv tepeqthals ltqdysllli dtdrfksind
      301 lfghlkgdev lcalartles carkddlifr wggeefvlll prtsldtaln laeviratva
      361 kvtlpglprf tvsigvarhe tnesidelfk rvddalykak negrnrvlaa
//
LOCUS       WP_181511751             420 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella grimontii].
ACCESSION   WP_181511751
VERSION     WP_181511751.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella grimontii
  ORGANISM  Klebsiella grimontii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
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="Klebsiella grimontii"
                     /db_xref="taxon:2058152"
     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=48167
     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 mslsdakirs ikpsdkpfkl tdsqglyllv npsgsrlwyl kyrfnrkesr ialgaypqvs
       61 lsdarqqrdg irkllaqnin paqqrvtekt aaspekcfea vavawhktnk kwsadyaeri
      121 lasmnnhifp aighmpvtml ktqhftallk viedkgflev asrtrqqlcn imryavqqgl
      181 tennpalhle gvtappvknh ypalplerlp elferigdyq qgqqltrlav vltlhlfirs
      241 selrfarwse idfrhkiwti patretiekv rfsgrgakmr tphivplsrq aiailkqine
      301 isghlelvfp gdhnpykpms entinralrl mgydtktdvc ghgframacs alveselwsr
      361 daverqmshq ernsvraayi hraehldark dmmqwwsdyl dvsregyvap yiyarrhkaa
//
LOCUS       WP_181512302             328 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Citrobacter
            freundii].
ACCESSION   WP_181512302
VERSION     WP_181512302.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=36469
     Region          <3..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 mfeliaeaas sinvfsmarr iaafnvpvli hgetgtgkec iakfihsiaf aqeasspyig
       61 vncaaipenm leatlfgydk gaftgavatv pgkmelanng tllldeigdm plalqakilr
      121 vlqeqqverl gsnrliklnf rliactnknl eeevaagrfr edlyyrmsvi pltmpplrer
      181 mediiplaes fikkystvlv kniklsessr rallsyawpg nvrqlenaiq rgmilnrdgv
      241 iypdtlglps iesdswsepq wqpkptaqit tsdnlgqhgr saqyqyiadl mrkyqgnktk
      301 iadllgitpr alryrlasmr kqgieifs
//
LOCUS       WP_181512016             404 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella grimontii].
ACCESSION   WP_181512016
VERSION     WP_181512016.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella grimontii
  ORGANISM  Klebsiella grimontii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
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="Klebsiella grimontii"
                     /db_xref="taxon:2058152"
     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=46682
     Region          6..393
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 magtnklsdk klkalqggsr dapemyadge glsvraskqg qlswvfsyrl ggrgsklerl
       61 tlgrypdlsl kaarekrekc rqwlaggldp ktelelstee tlkpvtvqda leywlvnyar
      121 rkrsdeelvr aqlrkhiypr lgrypltrce trhwvscfde inqtkpmtag rmfqiskqal
      181 rfckvrryaa sdalafltiq dvgqpsgqrd rvlsdselad vwrctgsddq qpyysrllkm
      241 lvlfgartme vrlsrwsewd ftswiwtvpk ehsktrekiv rsipeairpw leelkretgk
      301 tglllgedrt rqavslkgrr lfkdfhhnep wtlhdlrrtf stglnnmgia phivelllgh
      361 alpgvmaiyn rslylpekld alnkwherlg kvrisrsflp kltr
//
LOCUS       WP_181512443             381 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Citrobacter freundii].
ACCESSION   WP_181512443
VERSION     WP_181512443.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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
REFERENCE   3  (residues 1 to 381)
  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 381)
  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..381
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..381
                     /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=40986
     Region          131..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 mteqtspaql dldsaaqppr vyirgdwvla hycvleprva qlranmpsgg vfdlnqlgal
       61 dtagatllal llgedrvanl relapklpeg rrilletvsh vlpdltpels ekptrfwlem
      121 lantgrsvdn lwqdiksllg figlaletll gtlfrpsrwr itslianiqq iglnavpiim
      181 lltflvgavi aflgatvltt fgagiftvdl vvfsflrefa vlltailmag rtasaftaei
      241 glmkaneeid aiqtlglnpv ellvlprvla llislpmltf igmvcgifgg mvvcaltldi
      301 sptmflsimq nsnglqhflv giskapifaf liaiigcleg fkvtgsaesv gvhtttsvvh
      361 sifvvillda vaalffmemg w
//
LOCUS       WP_181512766             387 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces sp.
            PsTaAH-137].
ACCESSION   WP_181512766
VERSION     WP_181512766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. PsTaAH-137
  ORGANISM  Streptomyces sp. PsTaAH-137
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. PsTaAH-137"
                     /db_xref="taxon:1305830"
     Protein         1..387
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41005
     Region          34..379
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrpragvvgl aacaimataf agpagaaqgp aatpashaat qraidaavaa gvpgitaear
       61 dasgvwksat gvgnlktgap rgqndrfrtg sitstfvatv llqmeaekkl slddsverwl
      121 pgvvqgngnd graitvrqll nhtsglfdyf sdpayvqtyv lgdgylqhry dtlahdlrvk
      181 valshppayq pgvrhwfsnt ndvlaamvve kvggkkyede vrrriitklg ltatsnpgta
      241 ttlprpssrg ysklfadqpd riedvtevng sqawgngdii ssaadlnrfy aalmggkllp
      301 pqqlkemmtt vvnpdvpvss yglgverltl scgtdvwyhd ggavgwisvs sftedgrhvf
      361 tfnynsdfag etllpvldae ycgtpag
//
LOCUS       WP_181511698             255 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Klebsiella grimontii].
ACCESSION   WP_181511698
VERSION     WP_181511698.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella grimontii
  ORGANISM  Klebsiella grimontii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 255)
  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 255)
  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 255)
  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 255)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..255
                     /organism="Klebsiella grimontii"
                     /db_xref="taxon:2058152"
     Protein         1..255
                     /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=28279
     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 msttltfnfq hrslvpfahd yahgdsepwh qhdcaqllhi lsgvvrveta hgywvvppgr
       61 gvwlpagtph tlrvtgaaaa rtlfidplar adlpsacqiv qvtpllreli vasltlaesy
      121 apgsrderiy elildeirvm avlpfglpep qsealrrlcq kvreapgdsw ssaeaakess
      181 msertlnrhf qqqttltwse wvrraklmea lvrlaqgqsv lrvaldlgyg shsafsamfr
      241 rvtgvapsdy frspe
//
LOCUS       WP_181512886             345 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Billgrantia kenyensis].
ACCESSION   WP_181512886
VERSION     WP_181512886.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..345
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..345
                     /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=36759
     Region          15..343
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mrifehpefd hhqqvvfgsd easglraiva ihdtrrgpal gglriypyts eadaltdvlr
       61 lsrgmtyksa ladlplgggk aviiadprrd ktkamlramg rlveslggry itaedsgsge
      121 edmrlirqet rhvsglghdg lsgdpspfta hgvfcalqsa vrhrlgqedl kgvrvaiqgv
      181 ghvgahlare lhaagarlvi tdvdrdslgm lvdelgadsv apdaifgaev dvfapcalga
      241 vltedvarql kakvvcgaan nqlstpgvan slhardilya pdyvanaggv ieveaqrhah
      301 ydrnavmrhv eriaatadei farakaedrs pagvadqlar erlrg
//
LOCUS       WP_181512573             554 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArnT family glycosyltransferase [unclassified
            Streptomyces].
ACCESSION   WP_181512573
VERSION     WP_181512573.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 554)
  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 554)
  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 554)
  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..554
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..554
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59628
     Region          57..>275
                     /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 msalhgsrsg srpddetfal rtvtphvpvq ptgqaepgtp gyeipetpea gwdmaasrrr
       61 swvsrgvlfc ilaiqavlsl rlsntafqde alyltaghae laqllhgtpl pkdyaayfsg
      121 spqlypvlva lvdgrfglsg aralglvlml attgllytit rrlfseraal aaagmfavtq
      181 stivmghfat ydamalflla vatwivvrtd rlpavaglla vpvavlavgv kyasalylpt
      241 ilglalltaw prrgarsail rvlllavgvg allawgahat dllagvrqtt tdrvhgadsg
      301 pylleqsakw gglmfltavg gaisyvwrsr lnesplarrl gnpgrvrrll lglllcgtal
      361 lapayqihla tvvslfkhig fglffaapma gvgvtrliga hfrhpqlgim lwtvtlclgi
      421 qqadlrfglw pdsarmirti sarvdshgry lsstpevpay ylraktshrq wqsvfgmeyk
      481 dgkggyhagd dayrsavrdg afdlivldgl tnprvddiva aaiqgnahyr llaelpfrns
      541 agtgryriwv rtrg
//
LOCUS       WP_181512860             202 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Billgrantia kenyensis].
ACCESSION   WP_181512860
VERSION     WP_181512860.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 202)
  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 202)
  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..202
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..202
                     /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=23039
     Region          10..199
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mqgwhtlqtd pplhlyrgvl gepaadmlla qldrelewqr prlklygreh piprrqvwmg
       61 dgdahyrysg rdfppepwhp avvalrdgii rllsersvsa rfnsvllnry adggermgwh
      121 sddepelgpe piiaavslga erplrfrwkq aghepfnvwl phdslllmgp gcqrelqhal
      181 lprktpglri sltfrhvqas gh
//
LOCUS       WP_181513031             401 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Billgrantia kenyensis].
ACCESSION   WP_181513031
VERSION     WP_181513031.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..401
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43488
     Region          5..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 mtkaddrrlp ldglkvlelg qliagpfatk llgefgadvi kvepphsgdp lrrwrmiedg
       61 tslwwhvqtr nkrsvsldlr shegqdlvrq lvaeadvlve nfrpgtlegw glgwealsal
      121 npglimvrvs gygqtgpyrd kpgfgvigea mgglryltgq pgepsvrvgv sigdslsaly
      181 avigtllalq erarsgqgqv vdialyesvf ammesllpey dasgeirqps gsalpgitps
      241 nayrtrsgdy vliagngdsi fkrlmqvidr qdlandpkla hndgrareak riddaieawt
      301 lqherddila qldsvrvpag ypytaadiar dphylaremi qsitrpngkp lkvpgvlpkl
      361 satpgrlgdg gpalgqhtde vldelgidae treklrqagi i
//
LOCUS       WP_181513094             448 aa            linear   BCT 28-DEC-2024
DEFINITION  PqiA/YebS family transporter subunit [Billgrantia kenyensis].
ACCESSION   WP_181513094
VERSION     WP_181513094.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Nakayama,T. and Zhang-Akiyama,Q.M.
  TITLE     pqiABC and yebST, Putative mce Operons of Escherichia coli, Encode
            Transport Pathways and Contribute to Membrane Integrity
  JOURNAL   J Bacteriol 199 (1), e00606-16 (2016)
   PUBMED   27795327
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00155.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..448
                     /product="PqiA/YebS family transporter subunit"
                     /calculated_mol_wt=48272
     Region          34..447
                     /region_name="PRK15103"
                     /note="membrane integrity-associated transporter subunit
                     PqiA"
                     /db_xref="CDD:237910"
ORIGIN      
        1 mlnrstrflp apgeprvdrt ppeartsrrr lrachecdwl salpplrpgq kadcprcght
       61 lvtrhyrpaq rsmalamaam valllaisfp fvsfsvggfg nrielsqtat tligfhqplv
      121 aiaviltiav lpgvyllgvi wlqlgllqgr plpasrsiar slahlnpwmm advfiigalv
      181 slikvaglaq ielgisfwaf cafallllft tqsidsdwmw fslagepqap egartgttaa
      241 sqgltgcstc glvnrfdaag hshcrrcger lhvrlphslq rtwallaaat vmyipanvyp
      301 imttttlghs spstiiggvv ellqmgswpv aavifvasvv vpvgklvala wlclvvarss
      361 elnansrtrl yritefigrw smvdvfvvai lvaliragsl msvtpgpaal afgavvvltm
      421 laamtfdprm iwdtplprdn rktqgipg
//
LOCUS       WP_181511786             255 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Klebsiella grimontii].
ACCESSION   WP_181511786
VERSION     WP_181511786.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella grimontii
  ORGANISM  Klebsiella grimontii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 255)
  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 255)
  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 255)
  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 255)
  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 255)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..255
                     /organism="Klebsiella grimontii"
                     /db_xref="taxon:2058152"
     Protein         1..255
                     /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=28540
     Region          23..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          <73..252
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mawldadaaf dpdtlkthli gvqsalgdhd sgshqhkmaq ilftrqgcvr ltlndgtllc
       61 llppgraawi paevrhraem knivdyrsvw fqpqrypqlp tqsailnvvp llrelleris
      121 aspwdtdwea eparhlaalc qaeirlaare pmmlalpqdk rlamvcgdal ppalgalaar
      181 cgasektisr lfrrdtgmty qqwrqqwrlm kavemlatge ritdtaqald fasdsafiyf
      241 frtmtgmtpg ryfsa
//
LOCUS       WP_181513124             401 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Billgrantia kenyensis].
ACCESSION   WP_181513124
VERSION     WP_181513124.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..401
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43094
     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 msrplegitv ldmsrvlagp wagqlladlg arvikiehpe rgddtrgwgp pwlaeddeve
       61 rvaayylcan rgkqslaidi aseggqamir rlakgadivl enfkvgglak yrldyaslkv
      121 enpgligcsi tgfgqdgpya hragydfmiq amgglmsigg epdgmpmktg vaitdvmtgl
      181 yatigvlaal hersrtgqgr yvdvalldvq vaalanqaln alvsgnsper hgnahpnivp
      241 yqafacsdgh lvltvgndsq farlaelmgh pewardpdya tnaarvgnrd vlvpliqaif
      301 rtrgrdqwla dleargipag pintvaevfd dpqvkhrgmq ctlkrdglev pqvssplrfd
      361 getalsdlap prlgqdsdai laemglsgee ierlrregiv r
//
LOCUS       WP_181513194             333 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Billgrantia kenyensis].
ACCESSION   WP_181513194
VERSION     WP_181513194.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..333
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34990
     Region          6..330
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtakqhltrf saivlplaav vgmstaaqad ewaptrnief iapanpgggw dtlvrttsrv
       61 iqeeglaers fgainvpggg gavawaqiar dsgnphklfa tsppiilvpl agasrydhtd
      121 ftpiarlitd ysivlvrdds pfedlpslie ameenpqlsv gggsapgsmd hismaglaaa
      181 agldaaavny ipfsgggeam tslmgghvea vitgageasg qlgegselra lgvsaperlg
      241 galadvptyq eqdidytfdi wrgvmgtpdm paeavayyed lfaqmletdg weqareqlgw
      301 idayqdseef gafldeqkee fstilgdlgl lge
//
LOCUS       WP_181513040             369 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Billgrantia
            kenyensis].
ACCESSION   WP_181513040
VERSION     WP_181513040.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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
REFERENCE   2  (residues 1 to 369)
  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 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 11414687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..369
                     /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=40268
     Region          32..347
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mtrfpdhltg sgpsnpfpgi kvlerrigre iphrlgsneg ldmphralrq rfgdamvehv
       61 ycygdsealg irqrlaslyg lplettlvda gadslialal rtvapygstv vsasgtyptf
      121 gyfaqgqgcr lverpyreap gvlapdleal lasahehrar lvyvanpdnp sghlhadeei
      181 rqlrarlped cwllldeayh dfrddadssf srealpgvir lrtlskahgl aglrvgyaia
      241 epetlammmk vrihyavstl tqaaaetvld hheeveahia avklrrqrla shfhelgaev
      301 lpsatnfial rlasaelagr lnqelleagr liarpahpdl ghvlritave dalvpgrfdi
      361 leralasga
//
LOCUS       WP_181513161             460 aa            linear   BCT 28-DEC-2024
DEFINITION  class II fumarate hydratase [Billgrantia kenyensis].
ACCESSION   WP_181513161
VERSION     WP_181513161.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 460)
  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..460
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..460
                     /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=48729
     Region          2..455
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 mseqyrierd smgelrvpst alygaqtqra venfpvsgqp mpaafihaia riklaaakvn
       61 qelgllddkr seaimaaare ivdgkhdeqf pvdvfqtgsg tssnmnvnev vahlasregl
      121 sigpndhvnm gqssndvipt aihlsaalev tanlrpalvr lreiiderav eldrvvktgr
      181 thlmdamplr mgqelagwss qvgqaierid gamarlsrla qggtavgtgi nahpefaarm
      241 arelseqtgl alvpndsffa slgsqdaave lsgqlkglac vimkiandlr wmnsgplagl
      301 geielealqp gssimpgkvn pvipesaaqa aaqvigldta itvagqsgnf qlnvmlplia
      361 nnlltsitlm antacllger aiatfqvred qvaeplarnp ilvtalngvi gydaaaaiak
      421 qayqagrpii dvaveqtdlg reelerlldp arltrggipe
//
LOCUS       WP_181513517             320 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Billgrantia
            kenyensis].
ACCESSION   WP_181513517
VERSION     WP_181513517.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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..320
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..320
                     /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=35231
     Region          <9..319
                     /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 manqttrfel vgespelqav vrsarlvaat datvlilges gtgkellarl vhkssrraqg
       61 pwvtlncaal pedlieself gyqrgaftga hadtpgrvqq ahggtlflde vaelplaaqa
      121 kllrfleyge cqalgagtve qvdvrilaat hqdlrtrvae gtfredlfyr lhviplelpp
      181 lrvrdgdlpl larrfceela crhgvepptf asdlmrrlla hdwpgnvrel rnliercvvl
      241 mhghtigadd lpenwlnaat prqnnatwql paggmsldal egqlirqale qaegnrsraa
      301 rllgltrdtl lyrmkkhaia
//
LOCUS       WP_181513563             159 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Billgrantia kenyensis].
ACCESSION   WP_181513563
VERSION     WP_181513563.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 159)
  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 159)
  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..159
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..159
                     /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=17300
     Region          <8..151
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mptpsmhylf rrpnlpiats wasvdandlv evpllgdvsa glpieacpsg gairapacmv
       61 rrntyalrvr gdsmvdcnif dgdviiierq esaengetav vlinqqevtl kklyiekngv
      121 rlqpanenma piylknsdiq vlgmvmgvvr qqdgpelth
//
LOCUS       WP_181514010             325 aa            linear   BCT 28-DEC-2024
DEFINITION  YbgA family protein [Billgrantia kenyensis].
ACCESSION   WP_181514010
VERSION     WP_181514010.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..325
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..325
                     /product="YbgA family protein"
                     /calculated_mol_wt=37046
     Region          77..322
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 malaestssp pripvgisac lmgeqvryng ghkrsrycle vlqecfdfep fcpeleaglg
       61 vprepirlvg apeepprvvg tvdpsldvte rlrdvgeafv arhrhlrgfv lmkgspscgl
      121 ervkvyhqng mpshsdsgif vrvlrvlype lpleeearmn davlrenfit rvfafddwkr
      181 hvegagdyha liqfhsrqky llmahhveay relgrylgse ahaqplesvk hrylqrfmaa
      241 lsrpatrkth tnalmhimgy lkdavdsevk qdllgaveey rlghvhlavp vrllnhylkr
      301 hgseyirrqt yldphpyelg lrnti
//
LOCUS       WP_181513305             711 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Billgrantia kenyensis].
ACCESSION   WP_181513305
VERSION     WP_181513305.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     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=79476
     Region          1..711
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mftiddladr lggylppdei qqvkrafyya eqahdgqqrr sgepyvthpl avanilanmh
       61 mdhqslmsam lhdviedtgv skealaeqfg kpvaelvdgv skltqitfed kavaqaenfq
      121 kmvlamsrdi rviivkladr lhnmrtlgal rpekkrriar etleiyaria srlgintirv
      181 eledlsfqal hpmraerikr avssarghrr sairqiqttl qkslddegla gtvvgrqkhl
      241 lsiykkmrdq rkpfaeimdv fgfriitedv dscyrilgvv hnlykpvpgr fkdyiaipka
      301 ngyqslhttl fgsggmpiev qirtremeam anngiaahwl ykagqtdhpi aegsharare
      361 wvkgllemqr hagdslefie hvkndlfpdd iyvftprgdi melpqgatvi dfayavhtdi
      421 gnsciacrid rhlaplstrl esgqtleiit apgarpnlaw lnfvvtakar sairhalkhq
      481 qqteavqlgr rllnkaladf etsleelpdt vlpelldels lkdeeslles iglgtrvahv
      541 varrlidllh gdmaepsere lapqgpivis ggegmvikfa rcchplpgdp vvghlsvgkg
      601 ivvhrtecrn ldelkgdpdk lfalewseei aedfpvalri eiesrrglva elaslvtdae
      661 anierigiee rdarlsivhl tlavrdrvhl ariikrirnl shvgkinrvg n
//
LOCUS       WP_181513567             159 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Billgrantia kenyensis].
ACCESSION   WP_181513567
VERSION     WP_181513567.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 159)
  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 159)
  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..159
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..159
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=16781
     Region          6..141
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mkqvfrlele eaklmveaak krseeigvle ticvvddggy plalermnga rvtgpqiawn
       61 kaftaaghkr sthlfntapn gpalpgneaf giqwsfegkf avfvggfpiv vdgeviggvg
      121 lsggngeqdt qaglaalkal qdhlreaghe vvveadikk
//
LOCUS       WP_181513720             137 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Billgrantia kenyensis].
ACCESSION   WP_181513720
VERSION     WP_181513720.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     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=15756
     Region          2..130
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mfvrtiepaf ydtdalghvn ntrlpawfel arndlfrlft pdldprkwrl imarmeidyr
       61 aelhygsdie lrtylsrlgn ssftvtqeaw qkdeltnvgh tvlvhfdhst kravpiegal
      121 realeahlqp aeetsda
//
LOCUS       WP_181514244             569 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Billgrantia
            kenyensis].
ACCESSION   WP_181514244
VERSION     WP_181514244.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     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=62000
     Region          24..563
                     /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 mrtdvrggvs prrrppiapm gglrygvvlg lvilgmllla grivtlhvld rpflqgqgda
       61 rilrtealta hrgmitdrng eplaistpvv tlwanpqevp ddriqrlmla qalgigpddl
      121 darlerfssr efmylrrqlt pdaaqrvqal rvpgvyaqhe ykryypagev vaqllgvtnv
      181 ddmgqegvel ayqpylagtp gqrrvvkdrr grlvrdletl reaqpggelt laidqrlqym
      241 ayrelkaavd ehdadggvvv mmdartgevl amanqpsynp nnragldprg lrnqaivdvf
      301 epgsvvkpla maaimesgrf dtdvvvdtsp gwmmldrfti rdirnygkld lagilekssn
      361 igmsklvlel deplipdlyr rlgfgqstet gfpgeavghl papvrwsrsq waalsygygl
      421 stsalqlasa ytalanggmr mppsllklne apqgmpaiep qvahellrim eqsvqpntgg
      481 rraavpgyrv agktgtvrkt svsgyeaday rslfagvapv sdprivtivm idhprggdff
      541 ggavaapvfs rvtgsalrll dvppdqrar
//
LOCUS       WP_181514400             794 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Billgrantia kenyensis].
ACCESSION   WP_181514400
VERSION     WP_181514400.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 794)
  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 794)
  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 794)
  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 794)
  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..794
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..794
                     /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=85311
     Region          27..688
                     /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 mtlaaqdvqs phrlveflta isrcenvaea artgaeliae efdaeigavi vndrlmstfg
       61 fgqqsvpeam lkaalpgtde aifetigsch tlaaewhaga tgrlvvarch gafgyterhl
      121 llgmagafgl aldmlavler qrreqqvlev lldiqraish raplpdilea vtqgasqvlg
      181 ghpvsllldd aqdpgrpivs gadlsgaaet vsavvhihgv pagtllveig getlsgqeel
      241 allrtfaeha slaladarsl eemqkafrdp ltglpnrrlf ldrlnqalrq qapghtpavl
      301 fidldrfkai ndtmghdagd ellcavaeri gkvmrpdatv arfggdefav lvnvddaple
      361 taarigerii evlrqpfglg gqlayigatv gvahagasdq qadvllrhad iamyrgkavg
      421 rnvvityqpa mgeallerql lqthlqsalg ggeltlhyqp ivdlrsgrpk gleallrwrh
      481 pcrgmvppcd fiplaeetga iveigrwvld qacrqlgewh rldpsltvsv nvsarqlrqp
      541 sfaddvqaal dqaglegral tleitesall edlelalgtl qalkavgial alddfgtgys
      601 alshlrvlpv delkidrsfi stmegesdsd rlaamivslg hacrlrvvae giedslqlaa
      661 lkelgcdygq gylfrrpqda qaigdylagl pfapevrnra rsrlasqgtp armvrtstrn
      721 ccqeachgtq rpscflpphh kficqgrprw qpeaepqvfh atwradgylp gpwpgaggwi
      781 rigtaagpgv ggrg
//
LOCUS       WP_181513716             222 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Billgrantia kenyensis].
ACCESSION   WP_181513716
VERSION     WP_181513716.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 222)
  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 222)
  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..222
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..222
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=24161
     Region          15..205
                     /region_name="TerY"
                     /note="Uncharacterized conserved protein YegL, contains
                     vWA domain of TerY type [Function unknown]; COG4245"
                     /db_xref="CDD:443387"
ORIGIN      
        1 matyrlnsdr dlidnpsprc acmlvldtsa smfgppirel nagvqafisa iqeddmaacs
       61 velgvitagg kvteqlpftt amnisqcrqf tasgltplge amelaldrle erteayrkag
      121 vayyqpwlvv isdgvptdqw qaasarartl aqqrklvvmp vgveeadlea lgafstrpak
      181 rldglkfref flwlsasmsr vsassfttdq vklpptdswd si
//
LOCUS       WP_181514028             414 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Billgrantia kenyensis].
ACCESSION   WP_181514028
VERSION     WP_181514028.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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..414
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..414
                     /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=46179
     Region          1..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 mrergrtrrl fglgaraggt llrsrlggea dwralgealf eglselkgpa mklaqimaqw
       61 ddllpadlae elarlqrqaq pmpwegirrs lveqygdlda rfseieqhpf asasmgqvhr
      121 avtregetlv lkvqypglae ilegdlaqlr rimrlgrwlk vpqvrldalf eelaaslrge
      181 ldyhaeacal vryreryahl hdlvipeplp dlsgprvlam ryvagtplrd mesaadavrq
      241 rvaatladwl teelfthgel hadphagnfa vdaegrlviy dlgavipvpd ahlkammqll
      301 datlardpma mddalrqlgg rqgqgaplal yresaeavvp lfepgeqdfs dvrvhrrlrd
      361 lspkvwaamd rlqppadvll lsrtlnghyw nlvrlgarld mhgrtrplla warg
//
LOCUS       WP_181514018             393 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Billgrantia kenyensis].
ACCESSION   WP_181514018
VERSION     WP_181514018.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 393)
  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 393)
  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..393
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..393
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45543
     Region          1..392
                     /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 mfiglfetlk ragvpvslre lldlhavver gvvfadmeaf yqvartvmvk derhfdrfdr
       61 afaawfdgle nldaaieali pddwlrrefe kqlseeekaq ieslgglekl ietfkkrlee
      121 qkerhaggnk wigtggtspf gaygynpegi rigqegsrhr ravkvwderr frdyddslel
      181 gtrnikmalr rlrkfarqga aeefdvdsti rdtardagll nvrmrperhn svkvllfldv
      241 ggsmddhirv ceelfsaars efkhlehyyf hnclyegvwr nnyrrtseri ptmdvlhtyg
      301 rdyqvvivgd aamspyevth pggsvehfne eagavwlkrl adkfprlawl npmpprawey
      361 thstqlirql iddrmypmtl eglenamrel arg
//
LOCUS       WP_181514510             492 aa            linear   BCT 28-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Billgrantia kenyensis].
ACCESSION   WP_181514510
VERSION     WP_181514510.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     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=54764
     Region          4..492
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mfppftlrya rlperfyerf dpvpvrdpql iafnrplaes lgfdlaafda eeaavwfsgn
       61 vvphgsepla qayaghqfgg fvprlgdgra vllgevtdre grlrdiqlkg agctpfsrgg
      121 dgrsplgpvl reylvseamh amgvpttral aavttgervi rgipepgail arvasshirv
      181 gtfqyfaarg dregvrelae hvierhypel edrqgggryl gllkavqarq asliarwmgi
      241 gfihgvmntd ntsisgetid fgpcafmeqy dpqmvfssid eggryaysnq pwiaqwnlar
      301 laetllplid ddseravela teelqrfpeq yeaewlavmr aklglgseep edktlieall
      361 atmhrgradf tltfrhlaea adnpqaeasl valferpeei agwleewrer ldrepqpqge
      421 rtrrmklasp afiprnhrvq qaltaamdeg dlgpfealld vvtqpyddqp grdeyarpaa
      481 ptervfrtfc gt
//
LOCUS       WP_181514506             324 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Billgrantia kenyensis].
ACCESSION   WP_181514506
VERSION     WP_181514506.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..324
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34393
     Region          4..321
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 msfkmtrtav avsaailtfs agsalaseas lgdgpirivm pygaggstdi tariiaanaa
       61 ehcgsridvv smpgaggmeg lqfvadaepn ghtilmadys atitqtlted tpwevedwvp
      121 ivhltdwkpt vyvkadheiq siedwiekae aepntlvfgh adplslvhlp lvmleqetgi
      181 qnvhlpttgg getrtmilgg hidlgmtlpp sivsnvnnge vtaigvfade rsdvlpdvpt
      241 fqeagydvsl eapllvytfs svpesiqqql secimtglet dtaqamgrqa saglenvqgl
      301 esaqeiyret tervrevlas ideg
//
LOCUS       WP_181514794             432 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Billgrantia kenyensis].
ACCESSION   WP_181514794
VERSION     WP_181514794.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..432
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..432
                     /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=47971
     Region          9..426
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 msgqmdhanl fddartrlve vcqaieiqgd arerlmqpsl slqvsvpvrm ddgslkvfpg
       61 wriqynttlg pakggirfhp dvsqeevttl sfwmavkcav vdlpygggkg gvkvdpkkls
      121 klelerlarg yiraiadvmg perdipapdv ntnatvmgwm adefdhlarg kvpaaitgkp
      181 pelggslgrv aatgrgalhv ldlwaarekr kpeetrvavq gfgnaayhfa rlayeqgyri
      241 vavsdskgai ysqdgldpda ikeqkernrr lhdmvycdds vcvaedveki drdelltlev
      301 dvlalaaled qiheenvdev ragalleian gpvssrader leergipvlp dvlantggvi
      361 vsyyewvqnr sgerwseedi nqrlaqrler qselvfkrae reeisyrraa yrqgieriah
      421 aielrgncqd se
//
LOCUS       WP_181514609             401 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Billgrantia kenyensis].
ACCESSION   WP_181514609
VERSION     WP_181514609.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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..401
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..401
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43524
     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 mlkldyhpsg rhflqipgps pvpdrilram slptidhrgp efgalglell gklkkvfkte
       61 gpvviypasg tgaweaalsn tlspgdrvlm fetghfatlw hkmarrlqle pefiglpgye
      121 gwrrgvqadm iearlredga heiqavcvvh netstgvtsd iaavrramda aghpalllvd
      181 tisglasady rhdewgvdvt isgsqkglml ppgisfnals ekaieasrhn rmpksfwawd
      241 eileanrngy wpytpstnll yglnealdml leegldhvfa rhqrwaagvr tavaawgldv
      301 qcldpdvysp vltgvvmpdg idadavrkii yerfdlslgm glgkakgkmf righlgdcnd
      361 ltliatlggc eagmqlsgvp lagsgvtagl eyfaqhplda r
//
LOCUS       WP_181515405            1821 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Billgrantia kenyensis].
ACCESSION   WP_181515405
VERSION     WP_181515405.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 1821)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 1821)
  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 1821)
  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 19779286
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1821
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..1821
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=199997
     Region          1272..1532
                     /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          1522..1758
                     /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 mriagtrvas alkwsgalsl allagaasls qsanayprmv fsqppndtle haqrfrgaar
       61 lvgelaegdv dkylwavdda eadqlwrmrl qmqgeaplta tlalppaaaa depaagvaaf
      121 geaqestpea easaepqalv vlesppqrpv qgrepllvsh gdylitlsgl sgeyqltlep
      181 vgevalhgra dsetspdalm aapgrdwvfq ldtdhwslpl eldeadewlw rlaawgeldt
      241 elairlvdae gaalaeeasg lalaqrwdaq alpegsqvei rhpegqaigr vmlrleqagp
      301 mpdpepevva gslaeahplv peeafeaell pgermyfrip lpaerlidra wtlqaeglgg
      361 etleaclgdl iteqeacreg egevrfvrlq pppgdyylav sladrrpdpd tlrvnlapda
      421 ppadgevvep vdhrdwampl gdgipltgsm lgerrayfql hvadssdswr iqavgegide
      481 lrvyrasegg rhylaggvta glgelegvgv dnlqlaagqy ivqidgedtd yrlvaethdt
      541 drrgwerepn hepglanelq ageslrgnlh hpsrvdwyrf ylpgengvri eitppdegsi
      601 rptlywgedq iaragsldrd dealvltgrl pageyylamn drspagtyav sydlvspwge
      661 vpghamsvtq ahaapfpsdg mlslahselg qdyqwfrlpe geaprsvtvt rlganrlara
      721 pfeivdengd alereavese rrrseverve vpaggpwylr ttsgrlgdie levddillae
      781 rhareqawqt dveatlease qtvaawngrs qavdtrltle nggaqaheip laahashagw
      841 rvegleetls lapgeqrelt ltwslppgla ddqpvalfvr vgaevaearl speetsgggt
      901 avddaareal lgradlawag lgarfvdpds gepleqeyqr lvdglgylid glssagsylm
      961 fqgepgealp plqlagegge ihalvinqrs ghapverwre veisvgdspd aletltvlpl
     1021 eatdgeqifp letpvearym gvrplrfwgq lsrrsdsgig qlrvlgepsa alaeahpdll
     1081 agsrgghwiy sepehrklhe ftlaarsqhl prerrmrrgi rhdgspaslv fgfhqqraar
     1141 lerlawqddd dwegltvdrv rvytatespv gpwerqadwr lerdddlrae ltldapvwar
     1201 ylrleilepd vedersprwr rpvrlsafea eplgrgesil gywgqdeqtg pfehalaepd
     1261 lpaevedats spddpwvlea risarvhepn dtrsyrlqva egentlavrl reglygrles
     1321 rlegpdgepv aldwtrhagg wregvaidia pgdyrldvte pkraiaflwd asgslnhhqp
     1381 silravsrfa dgldpeqeva nlmplggpml mhdwtddpvr lrrtlagyeg gfrssnsepa
     1441 lqlasraler lelepiivli tdaelmsrem svwrdlarvq prilaleish nqerpsdetr
     1501 wyqnlmkswa nvgggrytya tdrddliraf etgmrelrqg ttffieaesr yqsppepgsl
     1561 qvvsadpeqp avaggvvhli fdasgsmlrq meggrrieva rrivqqtlde ripedvpval
     1621 rayghtephs cetellvspr agnhdevrev vagiqainla rtplaasiea vrddlagfed
     1681 qprlvvmltd geetcdgdva aavdelieeg ldvrlnivgf hideiglqae ferfaaqggg
     1741 eyfdsqdgeq lvaglsqala atwrvldseg dvvaqgrvgd epvelevgdy elvvetqdge
     1801 qrrgfnlgan qdktlevgre d
//
LOCUS       WP_181515406             587 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Billgrantia kenyensis].
ACCESSION   WP_181515406
VERSION     WP_181515406.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 587)
  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 587)
  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 587)
  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 587)
  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 587)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 587)
  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..587
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     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: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=64699
     Region          83..583
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          346..582
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 msrlrrlpah fapllvivaf atflafslvr lfqveqdmre nvdenmlwvi tqaqvashrl
       61 deavnrlarg detanpglrf dnfvsrleli aqgpqqryla dlgfsdaiqe allgmqaiea
      121 mlvdmapgdl tladqvhdel aplllkfnhm anavmieewe ntglrldkhr esllqaiasi
      181 vgillsgvvm vglllrtlsq ntaakralan hrvelerqie hrtcdleaer arlaaaidta
      241 pdgfaafdae gkltltnpql vellpyaagp ahdqplaavl dtirsqagmd tareatatgt
      301 egnslqcdme ipgqgwrqlt lrttwdgghv lrvadvtryk qaalsleeal qreqgvsdfy
      361 rsfaatvshq frtplavids glqrlqrrgd nmqheerhqr yvrlrdavah mtrlvesalt
      421 varidgnqvs hrpdnfdlva ivshtcqlqe eaagsqrifv qhdapsplrv rcdralveqi
      481 lanllsnalk ysppgspvtv rlssedgmal csvsdqgmgi apndlphlfd rffrsrraat
      541 vpgiglglni arylariqrg ditvnsregv gatfcltlpl dnrgtlp
//
LOCUS       WP_181514755             194 aa            linear   BCT 28-DEC-2024
DEFINITION  anthranilate synthase component II [Billgrantia kenyensis].
ACCESSION   WP_181514755
VERSION     WP_181514755.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 194)
  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 194)
  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 194)
  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..194
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..194
                     /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=21320
     Region          3..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 msvlmidnyd sftynvvqyl gelgaevvty rndaitleqi ealapsqlvi spgpctpnea
       61 gismaaihhf agrlpilgic lghqaigqvy ggrvvrapqv mhgktsrirh rgqgvfagle
      121 dplevtryhs lvveneslpd clevtawtdd ddvtpglimg lrhreldieg vqfhpesilt
      181 rqghellanf lkrr
//
LOCUS       WP_181515473             197 aa            linear   BCT 28-DEC-2024
DEFINITION  OmpW/AlkL family protein [Billgrantia kenyensis].
ACCESSION   WP_181515473
VERSION     WP_181515473.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..197
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..197
                     /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=20789
     Region          4..197
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mkptrlipvm alaatplfas qavlaysagd tfvrggfaqt dtrsdngvld svssgetgft
       61 fgagylftdq fgielnssek iehtfsagge sntldrmpvn lmanyyplgg fdsrvqpyvg
      121 aglnytrfsg epegvdarrs ygavgqvgvd lavtdnfmln gfanyadvds risvdgerig
      181 takvdpmtig ggvtfrf
//
LOCUS       WP_181514833             243 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Billgrantia
            kenyensis].
ACCESSION   WP_181514833
VERSION     WP_181514833.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 243)
  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 243)
  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 243)
  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..243
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..243
                     /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=26476
     Region          1..227
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 maddrphlvv ftgsgisaes giqtfragdg lwaehpieev atpqawrrdp arvlqfynlr
       61 reqvrrarpn aahkalaale krgfrvsiit qniddlhera gsrnvlhlhg eilkarstvd
      121 armqyplprg gialgdicdk gsqlrpdvvw fgesvphfge acdivaeadl llvvgtslav
      181 mpaaslleha pldvpsvlid peahalappg vtricqpagk gvpalvrhwr regrlwlpqt
      241 llg
//
LOCUS       WP_181514552             742 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Billgrantia kenyensis].
ACCESSION   WP_181514552
VERSION     WP_181514552.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 742)
  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 742)
  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 742)
  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 742)
  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..742
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..742
                     /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=78889
     Region          26..722
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtehtscssc tapasqksdr pppgtqslrl hieamdcpte eallrralgd tpgierldfd
       61 lvnrvltvhh qnvmedtier riastgmsar rhdpaqrtpt asstenwwkl gaaallalaa
      121 evshwlelae pwlaaalalt aialvglptw kkgfialrhr tlninalmsv avtgalligq
      181 waeaamvlvl ftlaeriear slgrarnair ellslapesv svrqadgsfl gvaasevavd
      241 slvrvrpger laldgsvteg hpaldespit geslpvdkap ganvfagsvn qgseflyrtt
      301 raasdttlar iihtveqaqa sraptqrfid rfaavytpav faiallvglt wpwlfgvswf
      361 dgiyralvll viacpcalvi stpvtvvsgl aaaaragvlv kggnfleqgh rlvaiafdkt
      421 gtltqgrpsq rawhpldgal dmldrerlra laaglavrss hpvsaalara aeaddiapce
      481 vsdvrelpgr gvvashdgrr lwlgnrrlmq qfaaldetld ahlaehearg etlvilgeea
      541 rplalfavgd plreesreai ealhrlgvtt lmlsgdtpas vaavatqagi deahgallpe
      601 dklamieara qqgpvgmvgd gindapalar adigfamgal gsdaaietad valmdddprr
      661 ladflrlsrg thrvlmqnia ialglkavfi vlaftghatl wmavfadmga slivvanglr
      721 llghgriiqr qlqakspaqp sp
//
LOCUS       WP_181515724             313 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Billgrantia kenyensis].
ACCESSION   WP_181515724
VERSION     WP_181515724.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..313
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34684
     Region          <20..280
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mhlgrtiasl wfatlwlssp aqagevthhr faseildrdy aytlylpegy resnqaypvl
       61 yllhgsfgse rdwvesgslk rtadrlireg tlpptvivmp gseswwidgh neaartaffn
      121 elmpyieqtw qvvsqrewra vaglsaggyg alnfvlerpe lfaaaaalsp asyhplppkn
      181 ssarrhpafl dasggfdeal wqqsnytayl dgylereevv plylsagnrd vfnaehyarl
      241 vsqalaphqp dlltmevlsg ghtwrvwras lpnalawvgr flqgpvplet laegmareat
      301 qvqpalspsg ate
//
LOCUS       WP_181515715             447 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Billgrantia kenyensis].
ACCESSION   WP_181515715
VERSION     WP_181515715.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 447)
  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..447
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..447
                     /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=48906
     Region          187..430
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 miiyalagff lvlggggiyw illnpvrgiy laffssgilv tmplgplrek vgltelviai
       61 twaamvinrk wiferkfvdg rqriallaal vflliyaisc fvnnasfygf lipsvietan
      121 ivyvvllmit mlflvqtpeq wkgclfgwla gaavvslvgf wamtgsapvw aydefsgrvs
      181 stlrfenqvp sylvpimfia mvwgalstts kllrfilvsl iaamavtlvl tgsrtaflli
      241 iislfcmafi flinlknssl mtgylglvii tsvvslflyv gaviaaydgh yslgstpswq
      301 rpvvvliegs hsgvidqsrg rqaelviana ddafilghgp klsgvkyrid eihntfagvf
      361 feagalglvs liilymalfs calrfsrsgt mnllfiaagv afillclygm tmyglrqrsl
      421 wlmcglllsi psvanhinrs vhaypvr
//
LOCUS       WP_181515900             438 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Billgrantia kenyensis].
ACCESSION   WP_181515900
VERSION     WP_181515900.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 438)
  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 438)
  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 438)
  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 438)
  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..438
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..438
                     /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=47895
     Region          <15..428
                     /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 mrqfayqsrq prpgrrqptl davtglttrr daeqhlavll aeaderdsrv ailhididrl
       61 kevnhafgra agddclrqla qrfsatvgsr gsvsrldsde vmvvlpdvtd vaeviptveq
      121 llrksheple lsgqallssc ciglalfpdh gatvielmrq anlarrkaqa rgsgqycvfs
      181 pdlledcpdr iqlrgevrea lqrgemalcy rpvlcarsgq vvaisaqprw hspsfgllgp
      241 qqwvaaahea grlyeishwv layacrhars wyeagsglkv vvglpmegms gdrlvesvgq
      301 alehsglpsg llalemtend lmqapesavv lldrlkamgv qlvvdgfgsg hsmlghlaml
      361 pidtlkldaq fvkncldspr hqavirsiig mahelgmkva aggvshrqqa dflreqgcdl
      421 lqgglwsrme ysdelshe
//
LOCUS       WP_181516111             235 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Streptomyces].
ACCESSION   WP_181516111
VERSION     WP_181516111.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     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=25114
     Region          37..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 mtvemregye gtgtgaitpd gcavevytrl pigpepdiia aavpagahil elgsgvgrmt
       61 hpllergftv tavdesadml arihgartic apieeldlgg ekfdvvmlas flvhagdeev
      121 rrgllrtcar hvadggrvli qregadhhtd vprervdpag ftvrvasvtp vgdgvnsvrv
      181 eyafpdgtwt qtflarpltk eqfeaalaea glevdtyltp dgmwvravra arttr
//
LOCUS       WP_181516014             416 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FUSC family protein [unclassified Streptomyces].
ACCESSION   WP_181516014
VERSION     WP_181516014.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  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..416
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..416
                     /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=46203
     Region          15..208
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mhqvrkgfeg llrlakrrre pvvvqtlrsa taatiayvia lrlspepapl tspltallvv
       61 qvtfyatltn girrvnavva gvlvaiafsv lvgltwwsla llivaslgvg hlvrvdeyva
      121 evaisamlvl gvttvgftaw arivetliga vvgtacnlll pppvwvdkag esiedlarrv
      181 rqlmlrmgee aadripwera aerlhearrl dqyiaevdas lrqaedslrl nprvkegllh
      241 rvvlrtgldt leictvvlrv larsftdlak aresdylfpp rvgatveell seigdavvsf
      301 avlvtahlsa daesaesrlt aelhtaagtr drlaeqlreq iradwanwql lgavltettr
      361 iidemdtehr thrlleeldr vsreqraklp rmtrlrerlg vqeelwrrtg fgdrtq
//
LOCUS       WP_181515153             148 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Billgrantia kenyensis].
ACCESSION   WP_181515153
VERSION     WP_181515153.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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 10440481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     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=16374
     Region          51..135
                     /region_name="Cytochrom_C"
                     /note="Cytochrome c; pfam00034"
                     /db_xref="CDD:459641"
ORIGIN      
        1 mtegltkaaa rnifyggslf ffllfaalta hshfyivnts tqpmsdsvrl gkhvweehnc
       61 inchtilgeg syfapevgnv wtrfggrdnp egarmaleaw mnaqptgapg rrqmpafdin
      121 deemqalidf lewtdsidtk gwpphpag
//
LOCUS       WP_181516317             496 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Billgrantia kenyensis].
ACCESSION   WP_181516317
VERSION     WP_181516317.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 496)
  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 496)
  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..496
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55449
     Region          238..473
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mtkrvsrrwr prsllqlvll aflvvmlplg vlmyqagqal selsrladvs arqaveesrr
       61 arvmsnlave mersarqyav leqdslldly aerhaefqel lsqqrrflpg dsdvialeeq
      121 lmllshlpnl epealevwla lfvpfaehte amrqatsrqi dasiemisar adavqsrlwl
      181 qttalvsasl llmllfswli irpvrqlerr ilslgsgiet ndrdtiqgpa elvqlgdrld
      241 wlstrlsdle aqkqqflrhm shelktplas vregsallad gvagemtprq reiltlidas
      301 gselqrlieq lldynllqhn qriileqvdl atlvkttlak hrlalehkgm rvtafdgple
      361 wvvdrnavgr ildnlvsnai aygedggdlt irahagrehl ildvantgep iaeydrpmlf
      421 epfyqgrsrr kgplkgsgig lsvaadcari qrgglalved kdfdvcfrlt lprqsvpltk
      481 ektepagtgi carsge
//
LOCUS       WP_181516335             279 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Streptomyces].
ACCESSION   WP_181516335
VERSION     WP_181516335.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            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="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30601
     Region          5..66
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(11,15,40)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(14,39)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(21..22,33,36,40..41)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          92..271
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mrsrrlgaal rqyrqaakld qpqaaeiias sqarisries gqatprviev rllldsygvm
       61 dtdvraklee lakhsknrgw wlehaehlrp dyvdhialed datyirqwqp alvpgllqtp
      121 ayaqaviteg pdyiapdeis rlvevregrq akikeggaty aailwevvva qplvsvdihr
      181 eqltaildaa krknvtiqvl pfgagalavt tagfssfsfd septvdavai enlrgtsvle
      241 apedlaaygn mfdvlrsaal apeasvklir dilrsiked
//
LOCUS       WP_181516165             372 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Billgrantia
            kenyensis].
ACCESSION   WP_181516165
VERSION     WP_181516165.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 372)
  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 372)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 372)
  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..372
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..372
                     /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=42854
     Region          2..368
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mephwkhgnr itlipdserf ipelleaign aeasvwfeqy liesgrvtrr fidaliraan
       61 rgvevrvvld sfgavglgqr ererlsaagv alrhynpfmm rrlrhnlsrn hrkmllvdrr
      121 vaytggyclt ddylgdwfdv vvraegpvve dwislladlw essrtrgdka pinrtlpaea
      181 eafgseggmp arlvhnegps dkiirhslhq rmetaeqrlw mytpyflpsr qlrrlvchaa
      241 qrgvdvrllv agkghdhpsv ryagqrhfge lldagiriye yqprfthakf civddwvtvg
      301 scnfdhwslh wnleanveve hadfadevva lfeqhsaesr tikwedwarr pnaqryrerl
      361 aamisawlag lr
//
LOCUS       WP_181516395             483 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: purine-cytosine permease family protein [unclassified
            Streptomyces].
ACCESSION   WP_181516395
VERSION     WP_181516395.1
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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     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=52332
     Region          4..455
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msgsaqgrvs gievrsidyv plnerhgklw hlgplwfmsn aqiatlavgl isitgggnlv
       61 wsllaivagt vlgtffmafh saqgpqlglp qmiqsrpqfg yvgallvwlf ayvqyagfnv
      121 fnsilaadal httlhggvkp wvlavtvval vialvgydii hkaervltyv flvvfgiftv
      181 gilltlhypa gsfdlgafkw tpflaqfgvv agyqiswaiy vsdysrylpp dvtvrktfyw
      241 tyfgsalggi wmmvlgtlla awagahfeti tsidaagdki fdgfgaivll faalglisvt
      301 alnmyggslt lisaidsvrr vrptlsvrll tlaltaalsv igalaatahf ladfndflll
      361 vlylfipwta vnlmdyyvvr rghyavaeif nprgiygrwg whgiisylag favmvpffsv
      421 gtlyvgpaak alggadislf iglpvsally wwltrsldve aearlaraea aeleraaseh
      481 rep
//
LOCUS       WP_181516758             252 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Billgrantia
            kenyensis].
ACCESSION   WP_181516758
VERSION     WP_181516758.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     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=28027
     Region          25..236
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mnllrsllfy fgyflaifvs gvlflpvapf lalpsryrll nlynhfitaw frwtcgvtyr
       61 vrgrenlpag acvilanhqc ewetlylqvl kppvctvlkq ellripifgw glrllhpigl
      121 drskparamr qvlgqgvarl qeglsvlifp egtrvdpghr rrynksgavi acragvpvlp
      181 vahnagerwp grhwiknpgv lnvvvgqpid tvgrtpeevl aeveawiesq laeisevprp
      241 veakpavnas sg
//
LOCUS       WP_181516567             320 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Billgrantia
            kenyensis].
ACCESSION   WP_181516567
VERSION     WP_181516567.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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..320
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..320
                     /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=34960
     Region          28..302
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mtlstetrpa ggatpaaemt lrlpyrppyd wqamlgflar raiaglecid gegyhrlfhe
       61 agamgsvsvt hapadtalhv tlrlpepidp saivarlqrl fdlhadpeai rqglgrdptl
      121 aplverrpgl rvpggwdpfe iavrailgqq vsvdaatrla grlverlger laepfapgld
      181 rlfpqperft faeikalgmp garanalagl asayreqpql feqcgeldds vaqlcalpgi
      241 gawtahyiam rglresdafl psdvavqral aeqgrrptpr ellaraeawr pwrayavmhl
      301 whadaataqa karqakerwe
//
LOCUS       WP_181515144             117 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Billgrantia kenyensis].
ACCESSION   WP_181515144
VERSION     WP_181515144.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 117)
  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 117)
  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 117)
  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 117)
  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 117)
  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 117)
  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..117
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..117
                     /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=12637
     Region          <17..107
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mhlpalslll igllfpaaal aetradtlds erqaelktll yqdcgschgm tlrgglgpal
       61 prdrmeafsp ealtyiiqhg ipgsampgwk tllsdaearw iadhlrtdns letlqqd
//
LOCUS       WP_181516595             346 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase family protein
            [unclassified Streptomyces].
ACCESSION   WP_181516595
VERSION     WP_181516595.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  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 346)
  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..346
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..346
                     /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=36903
     Region          72..327
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 magrfvqrpt rtavrggqag vsadgtgpta gaggiprqaa vparvrrwvp egpldlglvl
       61 gplrrgagdp tfratadgsv wracrtpagp gtlrvraygg evlgeawgpg aqwlldglpa
      121 llgaadepea fvprhraval arhrrpglrl trtglvlesl ipsvleqkvt tdeayrawrl
      181 lvrrfgepap gpaglgerpm svmpaartwa lipswewhra gvddkrasti lravrlaarl
      241 eqtvdmppge ararlevvpg vgvwtsaevv qrshgaadev tvgdlhlpgi vgwalagdrh
      301 addsemlrll epyagqrhra arlillsglt parrvpkmpr vdigll
//
LOCUS       WP_181516761             620 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Billgrantia kenyensis].
ACCESSION   WP_181516761
VERSION     WP_181516761.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 620)
  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 620)
  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 620)
  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 620)
  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..620
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..620
                     /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=68754
     Region          30..600
                     /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 mrpssalnrp ltwaalaala aciwlpgpgl rlvavgivav glwdawrqvq rdrqhadlmq
       61 qalmlseegv qitdaenril avnpaftrit gydedevrgm naanlaaarh dsaffqrfwq
      121 tlrtkgrweg eiwnrrkqgd efpewlrvka vtdsrgrish yvgtftdisv hkareqdlrr
      181 igfedpltgl pnrrrlhdlm tsrlrhlrag esldmaiidi dgfksvndsl gveqgdrlla
      241 rfgqrlahhv aggvvgrlgg deflvirttt fddhdkwvag lrqhlgepfe lgsktlrlgl
      301 sigscraped gkgssvlfqr lesalysakr hgrnvsqrfr paldvqdspq malvyslrda
      361 langeqlelh yqtqhrimdg avvgmeallr wrhpeygmvs padfiplaer hglmgplgnw
      421 videslaqma rwremglpql pvwinisaiq mfqgeletal saglarhgie psqlglelte
      481 svllderagd ivprlealrl kghriaiddf gmgysslsyl knlpldklkl drafirslpd
      541 dpadaaivsa vlamarglsl dvvaegvetq gqleflqqag crlvqgflya rpgpaeaiea
      601 qwqasvssss glvlraepsl
//
LOCUS       WP_181516508             373 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Billgrantia
            kenyensis].
ACCESSION   WP_181516508
VERSION     WP_181516508.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 373)
  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 373)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 373)
  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..373
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..373
                     /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=43391
     Region          5..369
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mhgvwrdgnr fellaessrf lpamftaiee akrsiliely lmesgrlata lidalcraag
       61 revtvalmld aygamglsae drrrleqagv alrlfnplgi rpltrnltrd hrklmvidgr
      121 eaytggfgav defldawyev avriegpvva dwvrlfsrlw dsplskgagd ttlvrrlqle
      181 viprqdyqgm rgrvvwgqgy ryqairhsly grvssaqrri wlctpyfvpt fslrmrlira
      241 arrgvdvrll lpgrdhdhpw vryagqrfyr rllragvrif efqptfihak fslvdewssl
      301 gscnfdhwsl hwnleanqev ddtrfageva alfernyaas reityrewmq rprwqrfkew
      361 vfgsvdawlt rlr
//
LOCUS       WP_181516774             499 aa            linear   BCT 28-DEC-2024
DEFINITION  SLC13 family permease [Billgrantia kenyensis].
ACCESSION   WP_181516774
VERSION     WP_181516774.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 499)
  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 499)
  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 499)
  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..499
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..499
                     /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=52748
     Region          105..485
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mtqpfeenqt dtpssprler lrllallggp llalvliwid ppadmppaaw qvvaltawma
       61 vwwvaepvpi avtallpval lpllgtntis eaaapyanpl iflflggfll aeaiqrwglh
      121 rriamlvlrg cghrphqlva gfmmatagls mwvsntataa lmvpigvsvl rllerrggvg
      181 asrhmtltll lgialaanig gmgtligtpp nallagfmad nygieigfae wmlfalppal
      241 lllamswwll trvvyplpre pipgvaslle eqardlgrit aperrvtvif llvalawvtr
      301 pllqnllpnv eltdagiavi aaimlfvvpa rlkegrflld wnsarnlpwg vlllvgggls
      361 lgtaiessgl aamvaqglsa fgewpvwslv amtvvvvmlm shvtsntata aailpltasl
      421 tvslgaspll ltipvamaas cafmlpvatp pnavvfasgk ltvldmmrag aiislvailt
      481 illflhalam pvlgfgwag
//
LOCUS       WP_181517020             395 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Billgrantia kenyensis].
ACCESSION   WP_181517020
VERSION     WP_181517020.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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   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..395
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..395
                     /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=45555
     Region          28..338
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mkvetitqpt glqlpillde tglpvpiyne filsranlqt ntlirnsyel sifdewiksr
       61 neqflelyvk glvgeaving slvpwlrksf dknpklkklf lspdtfnerl ttvrlflnwh
      121 fnvvsgkmsy lsnefkvlke snarvesllt sayvksipvk ksvslgltln qvqdlihcvd
      181 penpnsygrn yavkyrnyvm vllmlgcgmr pgellslkvd dvqhgaypai dvvrrppdkk
      241 dtrrmkpnik rngrllpiyd pniafhldqy lveyrdefee raktpseylf lsdegrplsl
      301 ksvgeyfrii rsrhsdvlpe nitakslrht fssnllkglk esgleeeqrt kilailrgdt
      361 nlasqdrytv qvyndfasty mrryqrslvf eevpf
//
LOCUS       WP_181516994             323 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Billgrantia kenyensis].
ACCESSION   WP_181516994
VERSION     WP_181516994.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..323
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34847
     Region          5..317
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mklkligtav ltatialgma gqaqadefpt kpltlvvgfa aggstdiqar vlanvleeel
       61 gqpvsvvnqp gaggavsltr lmnnqdeght fvyagtngtl tfaphahdtd ftlddfryva
      121 sittvqhaiv tgenrpfgds wedlveyare npgtsyatqh aldrlvieyi meqegldlri
      181 vptsggggma plilsgdvdf gysggthsgy aetgempvll smdserlfaf pdaptvmeag
      241 ydldtsdfrv vvvpkntpda hverlaeale aatqderfie iteerilmpv hfrgeeeate
      301 mlyaqsdnyr ellermggvp edd
//
LOCUS       WP_181516981             146 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Billgrantia kenyensis].
ACCESSION   WP_181516981
VERSION     WP_181516981.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (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   2  (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 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     Protein         1..146
                     /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=15745
     Region          <31..144
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mtlakptpah peppslalpy plalgragis gfpspaqdye grtldlnerf vkrpsatffl
       61 svtgdsmvkl gihegdtlvv drsidpkpgh iivamvdgei tvkryelrgk vpclcsgnpr
      121 yapvplvdle cqvwgvvrav iheysv
//
LOCUS       WP_181517142             235 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Billgrantia kenyensis].
ACCESSION   WP_181517142
VERSION     WP_181517142.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia kenyensis
  ORGANISM  Billgrantia kenyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 235)
  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 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   3  (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   4  (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 10507063
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Billgrantia kenyensis"
                     /db_xref="taxon:321266"
     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=27010
     Region          14..157
                     /region_name="Autoind_bind"
                     /note="Autoinducer binding domain; pfam03472"
                     /db_xref="CDD:427319"
     Region          <102..232
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mfndienqlk eitnkaeffs tfekilqscg vskyayvytp lsldqvsdiy ifgnydhawv
       61 giykgekyyr idpvmllssr tpfpffwkdi pmnikgksdi femaqdygig kgysipmhdp
      121 gfsfgslhls vdrndtnfem risqnclllr llsimvhsyf sqdvkqynsi clssrekecl
      181 fwvsqgktyw etaiilgvte rtikfhmsnm akklnvanak qliakalamn llaev
//
LOCUS       WP_181518050             219 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LexA family protein [Enterobacteriaceae].
ACCESSION   WP_181518050
VERSION     WP_181518050.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=23904
     Region          4..215
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mktemkdrir srriqlditq lalakklgvs rvsvtkweng ttkpdgenlh qlaqalsttp
       61 ewilygsgde avddtrvvpf lkppvavpii savqaglwtd syacsrltdv iswtqttanv
      121 sdeafglvvr gesmtnpqgl psipegsivi vephygqldd lygkivvail dgtseatvkk
      181 lvwdspysyl mplnpvfkpi qidgncrivg kvvqitqni
//
LOCUS       WP_181518689             172 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase [Micromonospora].
ACCESSION   WP_181518689
VERSION     WP_181518689.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
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="Micromonospora"
                     /db_xref="taxon:1873"
     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=19026
     Region          41..169
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mvrlvfavkr gwyqlryrrl tlgrdveirg rirlrrgvrv tigdrtrlnk lvrfagpgev
       61 rvgadcllna twigtwtsvt vgdrcllsdc elldndfhnl ppeqrhappg pltrapivle
      121 dnvwvgahal vlkgvrvgrd svvgaatvvr tdvppgvvvv gnpqqtvkkf hd
//
LOCUS       WP_181518824             535 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Enterobacter
            roggenkampii].
ACCESSION   WP_181518824
VERSION     WP_181518824.1
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  :: 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="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     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=59008
     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 isyrtarqwr evvhnvsftl rrgemlafvg esgsgkttta qaiiglladn
       61 arrdagkivl ngeeisrwsa krldtlrgar islvpqdpgn slnpvktigv qvgeiiqqhq
      121 kvtahqrdeq vlalltkvgl shpeqrmkqy phqlsggmkq rvliaiaial rpdvivadep
      181 tsaldvtvqk rildlldilr resgtavlfv thdlalaaqr adrllvfrng evqehgdtad
      241 ivrtpqhayt rqllsdlqgq rltiapvagl plaspairar aiskrfslgk ghqlqaldrv
      301 tfdvrrgsth alvgesgsgk ttlarillgf eqadsgqvii ddidatdlsr earrqlrqki
      361 qfvyqnpfas ldprqtlcei ieeplknfsr lakaerkarv etvaqrvalp velltrtare
      421 lsggqrqrva ivralilept ilvldeatsa ldvtvqaqil allqqlqqql gltylfithd
      481 lstvrriahs vtvlrsgqvv ehgdvetlfp spqndytrel iaaiphfspa teefa
//
LOCUS       WP_181518906             430 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Enterobacter
            cloacae complex].
ACCESSION   WP_181518906
VERSION     WP_181518906.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae complex
  ORGANISM  Enterobacter cloacae complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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   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 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 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Enterobacter cloacae complex"
                     /db_xref="taxon:354276"
     Protein         1..430
                     /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=48910
     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 manasyptgv enhggslriw flykgkrvre nlgvpdtakn rkiagelrss vcfairmgnf
       61 nyaekfpnsp nlarfgqdrk eitvlelter wselkrmeis sntmsryesi tknmlprige
      121 nkmvsavtte dllyvrkell tgfhvmkkdh rtqvkgrkss tvnnymmlma eifqfgadng
      181 yakenpfsgi nrlrkakdep dplttdefir fiqacghqqm rnlwtvavyt gmrhgelcgl
      241 awedidltag titvkrnltq tyeftlpkte agtdrviyli qpaidalrnq aqltrlgrqh
      301 evevnlreyg qsvihpctfv fspqcvkrgs rrgyhyavns inkiwapiik ragiryrnay
      361 qsrhtyacws lsaganpnfi atqmghtdaq mvykvygkwm seksgeqvtl lnkalshiap
      421 slpqsmivaq
//
LOCUS       WP_181519317             422 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter roggenkampii].
ACCESSION   WP_181519317
VERSION     WP_181519317.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     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=48691
     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 mpkltdmqir awiragerfe gradgnglyl ryreadktpt wrfryklagk sramligsya
       61 elslakaret akelsarvsl gydvagekqe rkakalakie ddknamrvsq laaeyferqi
      121 lprwkhpdil rrridkdinp cigqmrvedv kprhiddmlk givdrgapti atdvlrwtrr
      181 ifdygikrha leinpcsafe vsdaggkeva rerwltrdel irlfqamrqa kgfsrqnelt
      241 fkllltlcvr kmelcaarwe efdlegaiwh lpeerskngd aidiplpppa vewlrelrtf
      301 scnskwvlpa rkmqnrmiph iqestlpval akvraempdv pnytihdfrr tarthlaalg
      361 vdpvvaercl nhrikgvegi ynryqyfeer kaaltlwcdl lvalesgedy nvtpiikahk
      421 ls
//
LOCUS       WP_181518370             191 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora noduli].
ACCESSION   WP_181518370
VERSION     WP_181518370.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora noduli
  ORGANISM  Micromonospora noduli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Micromonospora noduli"
                     /db_xref="taxon:709876"
     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=20419
     Region          116..>175
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mttpeitiat padrdavvrs lvaafvkdpi lrclfpdeet ypryaaaffg hlfdkrvhqs
       61 siwtlgggas vaiweppags ltgspqggla ahypadvlar vqsyddavha alptfpfwyl
      121 gvlgthpdsa grgwgravmr aglaraaadg lpailetsnp anvelyrrag wevagflaep
      181 vptwimqqpp r
//
LOCUS       WP_181519628             323 aa            linear   BCT 28-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Anoxybacillus ayderensis].
ACCESSION   WP_181519628
VERSION     WP_181519628.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..323
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..323
                     /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=36067
     Region          4..313
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(10..11,13,54..56,76,104..105,108..109,111..112,115,
                     119,121,129,131,133,135..141,143..147,165..166,169..170,
                     268..269,277,283..289,291..294,296)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(55,77..79,102,239,287,290)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(78..79,106,155..159,177..179,182,209..211,215..216,
                     237..239,263..264,287,289..290)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mgrpyvfitr klpddvvapl ydkydvnmwp hehlvvprdv llqeasraea litmlsdrid
       61 eellkqspkl rvvanvavgy dnidveaatk rgiivcntpd vltettadlt falllatarr
      121 vieaaefike gewkswspll lagtdvhhkt igivgmgkig qavahrakgf hmrvlyynrs
      181 rnmeaertlg amycsfdell eqadfvvcla pltnetyqlf nreafmkmkr samfinagrg
      241 avvdeealyd alinrhiaga gldvfaqepi rsdhpllqlp nvvalphigs atketryamm
      301 qlccrnviav legkkpytpv qsr
//
LOCUS       WP_181519668             210 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Anoxybacillus
            ayderensis].
ACCESSION   WP_181519668
VERSION     WP_181519668.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Rosinski,J.A. 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 210)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..210
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..210
                     /product="helix-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=24450
     Region          6..210
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mrkktsstke qilkmlkvqk rltvgemaeq lqitemavrr hlsalereel vestlvrqpm
       61 grptnvyqls vkghqrfprh yqqtmldfla dlermggkqi vaqlfqnrqe rmkklyerqf
      121 gdksfdekmk elvavqnehg ymselvqhdd gsfelvehnc piaevaqayp iacecerqlf
      181 etliheaeiv pktcladgdd acryhikrkk
//
LOCUS       WP_181518656             239 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            noduli].
ACCESSION   WP_181518656
VERSION     WP_181518656.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora noduli
  ORGANISM  Micromonospora noduli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 239)
  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 239)
  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 239)
  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 239)
  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 239)
  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..239
                     /organism="Micromonospora noduli"
                     /db_xref="taxon:709876"
     Protein         1..239
                     /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=24958
     Region          5..239
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtlglqaagn sdvglvrrrn edaiylgqdl faiadglggh iagdvasita inalsshdql
       61 vdpaalattl gqavrsanda lnqrikaepg lagmgttlva mlrsgvtavl anvgdsrayl
      121 lrssakgigk tiqitedhty ehlvadastv pnlperlsrf idgrpdgrsp dittwhlspg
      181 drfllcsdgl styvehhlih avlsaggtpd qavdrlinla idhgapdnvt vivldihea
//
LOCUS       WP_181519660             369 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Anoxybacillus
            ayderensis].
ACCESSION   WP_181519660
VERSION     WP_181519660.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
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="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     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=41345
     Region          12..367
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mkvpmldlte qyqqlrpeil aaleevmssa hfilgnnvkk lendiaaysn vkhgigvang
       61 sdalhislla cgvgpgdevi vpaftffata gavaragatp vfvdidprty nidplkieea
      121 itektkaiip vhlygqmadm dkikeiadrh qlyiiedaaq aigakykgkt vgelgttacy
      181 sffptknlga ygdggmivtn ddeiaekmrv lrvhgskpky yhhvlgynsr ldelqaailn
      241 vkfphlddws klriekanvy temlkelegv vttpyieehn yhifhqytir vqnrnelqkf
      301 lsdqgvstmv yypkplhlqp vfehlgykeg dlpetekaae evislpmfpe lkleqqeyvv
      361 skikefyak
//
LOCUS       WP_181519739             506 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Anoxybacillus ayderensis].
ACCESSION   WP_181519739
VERSION     WP_181519739.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..506
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..506
                     /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=57167
     Region          23..493
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mkkivvvgag pgglaaamll aakgydvsvf ekqpyvggrn grfelgeyrf digptflsmp
       61 hiieelftaa grnihdyvql veldpmyelv fndvklamtm nrkkmkeqia aqfpgnedgy
      121 drfmnenerk lqalapilqs kmdrlyhylr ptvlkalpql tlsqslydil sryfnderlr
      181 laftfqakyl gmspwecpga fsilsymeha ygiyhviggl neipkamari veeyggsvhv
      241 ntgvrklwld gttvkgvile ngekvsadev iinadfaham tnlvddgvlk kyrkeklqkk
      301 kyscstfmmy vginkpvdla hhtiifaddy krnvdeitke ktiphdpsiy vqhaaitdat
      361 vapkgksaly ilapvpnnts gidwekekgp frqklwdtls kklgwkdmeq hiecekiitp
      421 hdwehhlfvy egatfnlghq lsqmmvfrph nefeelnhcw lvgggthpgs glptifesar
      481 itangilqah rqplipvgal pkrrea
//
LOCUS       WP_181519305             724 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Enterobacter roggenkampii].
ACCESSION   WP_181519305
VERSION     WP_181519305.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 724)
  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 724)
  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 724)
  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 724)
  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 14311966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..724
                     /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=81199
     Region          30..641
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          640..716
                     /region_name="Mannosidase_ig"
                     /note="Mannosidase Ig/CBM-like domain; pfam17786"
                     /db_xref="CDD:465505"
ORIGIN      
        1 mmtrncallv alltthtvan aapvswslag ewqvqdands ahpaasgwrp lqvpanwysa
       61 gydhqgalwy khafslpvqp pdvmstlvfd gvdylaevtl ngqplgqheg yfqrfsldas
      121 qalqrhnqlv vrvdspyedp tkvwplhktv mkgilnqhdt rpggawspqg qdansggiwa
      181 pvrlhlsrga tldetilrpd wsqglmhpal kadiryralg qgpatvrlta tpanfsgrry
      241 qadfpvtles gahsvqltlp mpkaklwwpv gtgkphlyti rvalrdengl mdtavtrtgl
      301 ckiveqpdnk gwlindkrlf ikgsnyigsp wlstmtreky rrdlrlveam nanairvhgh
      361 vagralydva demgmmiwqd vplqwgynns aaftenavrq tremieqfgn spaiivwggh
      421 neppwnspwm ekrfpdwnkd lnreltqkva dtlaedtsri vhrfsaveeh ywagwyfgtv
      481 rdllapaktg iitefgaqal prlstlktii paaslwpktt aaddpgwtvw kyhnfqpfqt
      541 fkfagisrgd niqamirntq ayqsqlvata aesyrrqryq pvtalfhfmf vetwpsinwg
      601 vvdylrkpka gfyalkrayq pvlpsiepvt aqwqsgaaat vrlwaindtw kpcrecrltw
      661 ritqrdkvla kgtttmtiaa dsgtmvkavt atpvgqddvs irftiensag kivgenqrte
      721 svik
//
LOCUS       WP_181519624             462 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Anoxybacillus
            ayderensis].
ACCESSION   WP_181519624
VERSION     WP_181519624.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 462)
  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 462)
  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..462
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..462
                     /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=52954
     Region          4..459
                     /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 mretihiyht ndvhshferw pkvvhylqtv rkkhqqnreh mvlldigdfi drfhplteas
       61 agkanvilln daaydavtig nnegitlshe qldtlytnat fsvivanvfy engerphwmk
      121 pyiimtfghv rvafigvtvp fqtfyellgw rvadpfdtva qlieelsekv daivllshlg
      181 inddekmahm fpqltailgg hthhvfehgk rvnetllcga gkfahyvgcl tltidknnrk
      241 vdarayvqht dtfehecvet krklnhmieq atnalaqpiv ylpeplhmdw fspspfalll
      301 aqalnewceg diamvnagvl laslpkgvvt kgdihricph pinpckvylr gselkevilq
      361 aeteqmkqlr vrgfgfrgev mgqmvydgvt ieketmsdgq ehvrrifihh qpideqktya
      421 vatidmftfg hlypeiyrak kkyympemlr dvlawklknm yq
//
LOCUS       WP_181519954             567 aa            linear   BCT 28-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Anoxybacillus
            ayderensis].
ACCESSION   WP_181519954
VERSION     WP_181519954.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 567)
  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 567)
  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 567)
  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 567)
  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 567)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 567)
  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..567
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..567
                     /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=65196
     Region          228..567
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mkrlfaiyvt lisllgcalf lytwpfsdvn vqnewfllll fagaavllsr ytiylppngn
       61 aftlessvyl allfthglhf sliillissf vmyfwyprkt swfnhvfnfs vytmmicgsy
      121 yayivfggvv gkvsiydfga yiasfaaffv lnvllmtiyf slrsstefrl illntikeli
      181 yiymveltas lilailfvfd tifglllymf imlllsavfr qyshlyerla ddkayiekll
      241 nslpigiitm detrsdyfin ksamlllcld qrkikekire gseenrlfwn lltsqdsfqq
      301 vkisydsdeg kreflvsktd liiphkepig rivffldvte aekisrrihq seklalmgem
      361 aakaaheirn plavihgfla fmnenlherd reqyhiplll keidrinaiv edmlliakps
      421 apvmkeayie tivqdvlslf qqtleaknir vhvrldhvpl qldskqmmqv lynllhnsie
      481 ameeggtici ysdvdetynm ymydsgsgip thmqeaifep fittkssgtg lgltivkrii
      541 enhggtialh ysseqgttfv irlpirr
//
LOCUS       WP_181519776             314 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Anoxybacillus
            ayderensis].
ACCESSION   WP_181519776
VERSION     WP_181519776.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
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="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     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=35142
     Region          2..309
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mnilvtgaag figshvceal lphhhvigid sligptpkam kqktietlnt ydrftwiegd
       61 llslplddiv qqvdviyhfa gmpgvrtswg tsfdlyttnn ilatqrllea ckqhrpkqfi
      121 ytstssvyge tngrvhentp paplspygmt klagehlcri yesafhvpit ilryftvygp
      181 rqrpdmafhr firqmlfdep itifgdgtqt rdftyisdcv ngtlavlgne kaigetfnig
      241 gkerasvndv iamletfigk qakkqyvnqa igepkhtwad iskaenmlay apnvplregl
      301 rreveyirsl ygrs
//
LOCUS       WP_181519428             235 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Anoxybacillus ayderensis].
ACCESSION   WP_181519428
VERSION     WP_181519428.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 235)
  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 235)
  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 235)
  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 235)
  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..235
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..235
                     /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=26616
     Region          30..190
                     /region_name="SpoU-like_TrmH"
                     /note="SAM-dependent tRNA methylase related to TrmH;
                     cd18092"
                     /db_xref="CDD:349965"
     Site            order(122,124,144..147,150,164..165,167,173..174,176,179)
                     /site_type="other"
                     /note="SAM binding site [chemical binding]"
                     /db_xref="CDD:349965"
ORIGIN      
        1 mrmtreeelh ieeglldddn rllaemilps rlkrmydvls artryitilt eavddphnqa
       61 avlrsaeafg iqdvhvvtga apfepnkwvt rhadkwltvh khssierair hlqqkgyqvy
      121 asylgegtip leqidvskpt vllfgnehrg vseealalad gkfiipmngf vqsfnisvaa
      181 aislyeitkr akqvageryh lslaekkeiy ehwmklslsp rlrkmveski ggrnd
//
LOCUS       WP_181520188             322 aa            linear   BCT 28-DEC-2024
DEFINITION  YbgA family protein [Anoxybacillus ayderensis].
ACCESSION   WP_181520188
VERSION     WP_181520188.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..322
                     /product="YbgA family protein"
                     /calculated_mol_wt=37416
     Region          69..310
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mwhyakpivv vseclgfspc ryngdqlnde vvhklapfvq fipvcpevri glgtpretir
       61 lvqdgdhvrl vqpstgmdit eqmkefsvsf ltqlsnadgf ilksrspscg ikdvkiyrse
      121 qkgpasgkgs gmfakhvlqm fahkaveeeg rltnfvireh fltklftlal frevkesksh
      181 hhlvefhaeh kylfmayhqq klkqlgniva nrdrlpieev flyyeqtlye lfarrsrrns
      241 ninvcehmig yfkhelsgde kryvhellek yraeklplss vttvirswai ryqnkyllkq
      301 ryfqpypepl ldvtdsgkgr dy
//
LOCUS       WP_181520304             364 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Anoxybacillus ayderensis].
ACCESSION   WP_181520304
VERSION     WP_181520304.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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..364
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..364
                     /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=40857
     Region          7..364
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mmerisklqq klkekngswa fitstanvfy fsgfysnphe rllavvifpd depflicpem
       61 danqakqagw aytivsyddv hhpwhmlrde lnrrnvqter igieashmtv srleqlqsyf
      121 shasffdltd tlhelrmtkd ekelqtlrqa aeladfgvdv gvralkegkt eldiiatiey
      181 elkkrgvram afdtmvltgt nsahphgvpg mnriqpgdfv lfdlgvvldg ycsditrtvv
      241 fgkpteqqkr iydvvlqaqq eaihacqiga sigsvdkaar srieqegyga yfphrighgl
      301 gidvheypsl natntmplqa gmvftiepgi yvpsvggvri eddiymtdkg plllttypke
      361 lqii
//
LOCUS       WP_181519715             569 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Anoxybacillus ayderensis].
ACCESSION   WP_181519715
VERSION     WP_181519715.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
REFERENCE   1  (residues 1 to 569)
  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 569)
  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 569)
  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..569
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..569
                     /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=67017
     Region          12..483
                     /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(26,28,30,34)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(65,68,105,108,149,168,172,204,262,425)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(204,262,339)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          490..565
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 mesipktkqw wkeavvyqiy prsfkdsngd gigdlrgiie kldylqelgv dvvwlspvyq
       61 spnddngydi sdyqdimeef gtlsdwdell hemhargmkl vmdlvvnhts dehhwfiesr
      121 kskdnpyrdy yiwrpgkdgk epnnwqsffs gsawqydeat geyylhlfsk kqpdlnwene
      181 kvreeifnmm twwldrgidg frmdvinlls kveglpdapv tnsndryqwg gqyfvngpkl
      241 mdylremkek vlskydimtv getpmvttdd aiqftneqdg vmnmlfqfeh mdvdskpgsh
      301 lgkwdiqpwk ltdlkkimsk wqvelhgkgw nslylenhdq prsvsrfgdd ktyrvesakm
      361 latwlhmmqg tpyiyqgqei gmtnvafpsi eyyrdvetin lwndvvvnkg ydpdqilkai
      421 hyrgrdnart pmqwdateha gfttgtpwin vnpnyrdinv eqalkdensv fhyykklirl
      481 rkehpiivyg syellledde qiyayvrkfn deqllvitnf ssdqptftlp shvtftekql
      541 lisnyavder epietivlkp yearvyklk
//
LOCUS       WP_181520554             417 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidase U32 family protein [Anoxybacillus ayderensis].
ACCESSION   WP_181520554
VERSION     WP_181520554.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..417
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..417
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=47328
     Region          15..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          335..414
                     /region_name="Peptidase_U32_C"
                     /note="Peptidase family U32 C-terminal domain; pfam16325"
                     /db_xref="CDD:465094"
ORIGIN      
        1 msisqiingk rvivkkpell apagnleklk vavhygadav figgqeyglr snadnftlee
       61 maegvqfakq ygakiyvttn iyahnenipg leeylrgles vgvhgiivad pliietarrv
      121 apklevhlst qqsltnwkav qfwkeegler vvlaretsae eireikekvd ieietfihga
      181 mciaysgrcv lsnhmtards nrggccqscr wdydlykleg dqavalfdeh ddpfamspkd
      241 lnliqsipkm ielgidslki egrmksihyv atvvsvyrkv idaycadpdn fvirkewlde
      301 ldkcanrdta paffegvpgy keqmfgvhsk kttydfvglv ldydkdtriv tlqqrnffkp
      361 gdeveffgpe ienftqviet iwdeegneld aarhplqivr fkvdrevfpy nmmrkgh
//
LOCUS       WP_181520414             327 aa            linear   BCT 28-DEC-2024
DEFINITION  peroxiredoxin family protein [Anoxybacillus ayderensis].
ACCESSION   WP_181520414
VERSION     WP_181520414.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
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   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 327)
  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 327)
  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..327
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..327
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37507
     Region          195..327
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 miqgenlllv aslvmtylff yygvfvlkad rrmmdmifns slygliiwkl sygivhpnmv
       61 lanpltllyf nggvvglvla gvfivvytyw qlkkqqipfd ayirvaspiy fgywivflvw
      121 kgsgfpenrf iwlqavvaav ffivssrikt trklwqllvs fhilffifss isdmtketts
      181 qqsssnigid vgeiapdfel mtlqgekmkl sqfrgkkvvl nfwaswcppc raempemqrf
      241 yeqygqhvai vavnltnkek nrhvvemfvn kkgltfdiml dekgtvskty kvitiptsyi
      301 idekgvirsk hvgplsydam kramlse
//
LOCUS       WP_181520159             642 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Anoxybacillus ayderensis].
ACCESSION   WP_181520159
VERSION     WP_181520159.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
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="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     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=74390
     Region          95..636
                     /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 mnkmmqaiav iapngkilga dehffqhfyh revdrgllek fiqeaengrt vsyavvkqkn
       61 gqndvyvqat alynkegnlq avvatyqyep fidmrltssi aslaseftfi lsaegeityv
      121 sptaqyvlkc teevcshelf sfvhhedipl lmeklhtiya tkekettidc rwrtdeghfi
      181 wihmhahpll nekneiehvi vvakditkwk cceealtklk hfdsltdipn rfyfesyvqh
      241 miqqkrpfal cyidfdkikw indrfsyqag dfflqeavrr iqqhlqqedf fariggdefa
      301 ivlhdvnket ivtrlehllq sfvepfryke hviqsslsvg vtffpqdgmd ldtllkqadq
      361 alcyakergk gyhfyhpqqn rktmieqelp iallnnqfyl cyqpkvsldn eaimgvealm
      421 rwthptlgai splefipiae kngfifeitt wvlkeacrqv kqwqthfptl klavnlspfl
      481 lnrkefvmhv knilqdtqfp pnylileite sglmenietg rhilielkqi giqvaiddfg
      541 tgfsslayir nlpvsllkid rsfirditdn skdativdti ihlaksldlq vlaegverdd
      601 qvsllqkmdc dfaqgfyfsq sleaekllqw leqhnqskea lh
//
LOCUS       WP_181520696             348 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Anoxybacillus ayderensis].
ACCESSION   WP_181520696
VERSION     WP_181520696.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
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="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     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=37291
     Region          27..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 mpksfiqtfl nnymsallia tfalllgvsi gsqsipfssi wetllhqlfh tptnvpatvs
       61 qiivairlpr vilafligas lalagvafqg llknvladpy tigvssgaav gavlvfffql
      121 qfsilgrftl pivsiifalv tllfvllfar laernmamet ivligiimna ffgslislmv
      181 afsgeelrqv iswlmgsvam rgwsyvslfv pffiigslgl fahirelnaf sfgervaani
      241 gvhllqkkla illsaslltg aavavsgtig fvglviphmt rlicganhrk llplsflygg
      301 tflvladvva rtivsprelp igvitaliga plfaillfks lrrktgst
//
LOCUS       WP_181520132             421 aa            linear   BCT 28-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Anoxybacillus
            ayderensis].
ACCESSION   WP_181520132
VERSION     WP_181520132.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
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 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..421
                     /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=48397
     Region          80..420
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mesheqlkqk ineleeeirl ykrfvehitf pfsyvdyelg kvikkernip satietieke
       61 ekrtpilqwn idlqkdypfe qveqflapif dlvshhivfv daegkitlcn lqaandvgvn
      121 rddmigkhir ellnipdeqi mtlktlrtkq plyncevldr yygiintril ynedgsikrv
      181 ismfqslnqi keaeklaiag riaagiahei rnplttvrgy lqflkeqlpe hiitlidqll
      241 ipeldrandi itdflnvakp sevkaewigi nefirhdldl llqseallhn velsyhldek
      301 lqqcvvnidk nqllqvfinl frnaieakte kslrvdietk lhnnlvqiyv rdngpgipst
      361 iihhvfdpff stkstgtglg lslsrkiiel hkgamrvqse fghgscfiie lpayskneaa
      421 i
//
LOCUS       WP_181520635             353 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Anoxybacillus ayderensis].
ACCESSION   WP_181520635
VERSION     WP_181520635.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
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="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     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=38955
     Region          5..353
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mdkvqklraq faehgidgfl itneynrrym tnftgtagvv lisetdavfi tdfryveqat
       61 rqiegyeivq htqtlieeva kqverlgiqk lgfeqddlsy atfssyekai katlipvsga
      121 veklrlikce aeikilkeaa eiadaafrhi ldfirpgvre idvaneleff mrkqgatsss
      181 fdiivasgvr salphgvate kviekgelvt ldfgayykgy csditrtvav gevsdelkri
      241 ydvvlqaqlr gvehiragmt greadaltrd yisacgfgey fghstghglg mevhempals
      301 mrsdtvlqpg mvvtvepgiy iaglggvrie ddivitengn erltlspkel itl
//
LOCUS       WP_181520836             316 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Anoxybacillus ayderensis].
ACCESSION   WP_181520836
VERSION     WP_181520836.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..316
                     /organism="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     Protein         1..316
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=36258
     Region          6..304
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mdfknkilng dcievmkqlp dnsiagcitd ppynyefigr nwdveeikrr tervqnsntl
       61 vknipygsgl aggvrnerwy kknreniley qkwvedwgre lyrilkpgaf vftfnstrti
      121 ahvqvglenv gfyardiivw rrhsgipkgl nvakklekmg eenperwegw hsalrnewea
      181 isvvqkplvn nyietlkkyn vglfkaktee gfqsniienv krdkiedfni hvtvkpleli
      241 kklidlsipp idgnvvidpf mgsgttalaa aelgidfvgi eivdeyckia tqrldnlknr
      301 lktegeqqdi fsilnd
//
LOCUS       WP_181520942             653 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidase U32 family protein [Citrobacter sp. RHBSTW-00424].
ACCESSION   WP_181520942
VERSION     WP_181520942.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00424
  ORGANISM  Citrobacter sp. RHBSTW-00424
            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 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Citrobacter sp. RHBSTW-00424"
                     /db_xref="taxon:2742647"
     Protein         1..653
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=72858
     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 sdvgftqivl 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 tvektghnry rvwpnempad lhkvranhpl nrnldhnwqq altktsserr vavdielggw
      421 qeqliltlts eegvsithtl dgqfeeanna ekalsnlqdg laklgqtlyy arniqvnlpg
      481 alfvpngqln qlrreavdml daarlqnyqr grrkpvaqpa pvypqthlsf lanvynhkar
      541 efyhrygvql idaayeahee kgdvpvmitk hclrfafnlc pkqakgniks rkatpmqlvn
      601 gdevltlkfd crpcemhvig kmkhhilkmp lpgsvvasvs peellktlpk rks
//
LOCUS       WP_181521159             640 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Citrobacter sp. RHBSTW-00424].
ACCESSION   WP_181521159
VERSION     WP_181521159.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00424
  ORGANISM  Citrobacter sp. RHBSTW-00424
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 640)
  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 640)
  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 640)
  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 640)
  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..640
                     /organism="Citrobacter sp. RHBSTW-00424"
                     /db_xref="taxon:2742647"
     Protein         1..640
                     /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=72214
     Region          1..631
                     /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 mtlagiiffl fistgyisfl vherqqelqk lthytdswsa aqlvsqyyrf esllglytid
       61 dtmnlddvrm rldimlsqsd likegdlgry iesniahrel avtlentlsy lddnlekmnr
      121 palqaylkkm htldaqlgrl ssgalnkdvn sinnanqniq tlyyiystts vlliilsail
      181 gvlifyqnrn ilrahlqvks laeelqkske klqiqnakle ydvyhdslte mnnrqlfwsd
      241 lnktiemaek nndavtvmlf dldrfkevnd tyghdagdml lrqisdrlis tsltsdtlyr
      301 lggdefafls sgltesravs raqkicefis qpytiyntii nittcvgivi senerrsdyl
      361 ykfadlalye aknegsgkik vfrqrmlekl qesrtlehdm alaivnkefv vyyqpivdsf
      421 sqkiysyeal irwihplkgl lspdsfipva ektgminemg kavleiacre aagwavpaki
      481 svnvspvqls skafagivlt ilketglppd rlelevtess lftesatpin tlnklralgv
      541 kisiddfgtg ysslsrlsrl afdkikidks fvhsistqed altiiklitg makslnmkav
      601 aegvetqeql trlqalgcdf aqgylfgkpq pcideeirng
//
LOCUS       WP_181520727             256 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [Anoxybacillus ayderensis].
ACCESSION   WP_181520727
VERSION     WP_181520727.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacillus ayderensis
  ORGANISM  Anoxybacillus ayderensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Anoxybacillus.
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="Anoxybacillus ayderensis"
                     /db_xref="taxon:265546"
     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=29942
     Region          1..255
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 msdyqqfian vkrktgidla lykeaqmkrr ltslyekkgf knfdeffram nhdqalfhef
       61 ldrmtinvse ffrnakrwev lekkiipkll eknkrlkvws aacstgeepy tlaiilskfm
      121 plsqvsvlat diddnamara klgiymersl qevpedvkkk ffvkegshyk iiddikrtvt
      181 fkkhnlladp fdtnfdlivc rnvliyftee akhelylkfn galrpggiff vgsteqifnp
      241 aaygfevedt ffyrkm
//
LOCUS       WP_181521091             389 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Citrobacter].
ACCESSION   WP_181521091
VERSION     WP_181521091.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=44557
     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 inakpysgap evtdgdglsv ritptgtitf qhryrwngkp vrltigrypa
       61 mslkdarviv gemrelylkg lnpknyfake dgeltlkecl dqwwskyvet lkpntqtlyk
      121 svvyntmyte fpdapvvnip vsswvrffdk qekkngkkar vlllqlrsvm nwcisrqlia
      181 scevlklsvk nigkkpdvgs rvltytelak iwlalennki vtsnkvlhql lllwgarlse
      241 lrlatasefn mddliwttps ehskmgnvir rpvfdqvkpf verllnsgnd vlfpgqeldk
      301 aidrssanly mkklrdkidi pewrthdfrr slvtnlsgeg vmphvlekml ghelggvmav
      361 ynkhdwlveq kaayelyadk ifwhvkqlg
//
LOCUS       WP_181522484             489 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Enterobacter hormaechei].
ACCESSION   WP_181522484
VERSION     WP_181522484.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     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=54361
     Region          253..489
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mmrrfslsqr ltllftalll lcatvacavq lyssmqygna mvqrlsggla qqivqreail
       61 daqgrvdrsa lkplfdrlmt fnpsvelyvv spdgdilada appghikrqk idlapiqnfl
      121 ggtvmpvfgd dprsqnkkvf sasplrqdge lkgylyiilq geesnalaem awhkalwsta
      181 lwsmllvalf gllagvllwy wvtrpvkqlt ldvagleqds icaikqlaaq plepagqdev
      241 ailrntfiel arkitsqwdr ladsdrqrre fianishdlr tpltsllgyl etlslksatl
      301 spqehqqyla salrqgqkvr hlsqqlfela rlehggikpq rerfamaeli sdvaqkfela
      361 artrelnlhi dvpgplpqvf advsmiervv tnlldnairh tpaggdirla vwqendrlqv
      421 evadsgtgvd valrddlfqr psalnpqasr ehrgglglli vkrmlelhgg girlmesvsg
      481 arfrffvpl
//
LOCUS       WP_181522301             238 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter
            hormaechei].
ACCESSION   WP_181522301
VERSION     WP_181522301.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     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=27428
     Region          80..223
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mrmtvrryrr rrtgsdslgs thspftlpff drleylsqsi nqtrktdapf iilvtqdnyf
       61 rsgflsgqsp lsnccdystl daalsdlnhw pssrlvvdie srasplidll drlrrhslfa
      121 pyltpyllvr addydarlfc kaagpfhvle rqltalamqq tlleapapvg nrkewfsrde
      181 wpilqalsqg rslrqiaqlq nrpysriiyr lscilaklgl nhrhellhll nnlsdfty
//
LOCUS       WP_181522763              68 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter freundii complex].
ACCESSION   WP_181522763
VERSION     WP_181522763.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii complex
  ORGANISM  Citrobacter freundii complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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 complex"
                     /db_xref="taxon:1344959"
     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=7483
     Region          2..59
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mflnqievgr rigvgknsig yivkndptfp kpvyltpsrp qwldtaidaw alersnaaqk
       61 nsrkgraa
//
LOCUS       WP_181523236             389 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_181523236
VERSION     WP_181523236.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=44522
     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 inakpysgap evtdgdglsv ritptgtitf qhryrwngkp vrltigrypa
       61 mslkdarviv gemrelylkg lnpknyfake dgeltlkecl dqwwskyvet lkpntqtlyk
      121 svvyntmyte fpdapvvnip vsawvrffdk qekkngkkar vlllqlrsvm nwcisrqlia
      181 scevlklsvk nigkkpdvgs rvltytelak iwlalennki vssnkvlhql lllwgarlse
      241 lrlatasefn mddliwttpa ehskmgnvir rpvfdqvkpy vdrllnagnd vlfpgqeldk
      301 aidrssanly mkklrdkidi pewrthdfrr slvtnlsgeg vmphvtekml ghelggvmav
      361 ynkhdwlveq kkayelyadk ilwhvkaik
//
LOCUS       WP_181523110             214 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_181523110
VERSION     WP_181523110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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 214)
  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..214
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..214
                     /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=23663
     Region          131..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 mypteskivp lsrqflessi alidaaflrd ptlawclsaq tpgfdarrtn ylrsylqyhh
       61 daslpvlgvw vrdalvavsy ftpgsttent sslaelghqi asgcgkrslh ridllrrvve
      121 sklschdcsr iefiavsplm qghgigasll rttlaylqdi epdknvflet gevrnlplyl
      181 rhgfsvrqri gfpgldqyll rkdavcggla tsne
//
LOCUS       WP_181530352             462 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Enterobacter roggenkampii].
ACCESSION   WP_181530352
VERSION     WP_181530352.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     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=52166
     Region          150..457
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mqnvwyhlrr ptlvrriiia qmllltllwc lfltfilwed lrsppiltgs ktyetvftlv
       61 ermdgrpqdr tavleafsqa lregyggged pvlsinlivr knnavifasd gapagitntr
      121 fgelehvqse drtwtsrtlk sphsdvevtl ftpasgwnff iylnsrgyyi lpllvcfpfl
      181 lfpawlsiri amrpwnkvvn eitlrtpddl splravpkhr elrqmvdain dflarvresa
      241 ererifiada ahelrtplaa mrinvealqs wvisesqqel lagvirsnsr aarlvnqlll
      301 mmhsearidt amepvplttl iqermaelep lasarkiele ffaeddvwih gvrerlvsli
      361 dnlienavky speggriqvd vsacdrvvql rvsdagpgip pelrervfdr ffrdpnqvqs
      421 gsglglaivk avaqqhnssv nlstsseggl lvtvdfpnrt fs
//
LOCUS       WP_181531083             346 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Enterobacter roggenkampii].
ACCESSION   WP_181531083
VERSION     WP_181531083.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     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=35864
     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 mnraglrair vgslsalvrp kalaylslfa lmalgllgfg lthgslpipa saigralfsp
       61 etltaetryv vmdirlprll mavlcgamlg magaamqsit rngladpgli gvkegcsaav
      121 lllifqfpal slawrplvgm agglltallv ivlardisrp rfiligigvs wafaaamgvf
      181 ittadvrdvq tamlwlagsl haanwtlvgl aalwaapafa lllftaraad vallgnqaaa
      241 glgvrttrla llrvlapvvl taacvscvgs igfvgliaph marlllrggq talltgsavl
      301 gallvlladn vgrlaflplq lpagivisli ggpffllllw qrrdrf
//
LOCUS       WP_181531045             197 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Enterobacter roggenkampii].
ACCESSION   WP_181531045
VERSION     WP_181531045.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     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=21350
     Region          4..185
                     /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 mtslylasgs prrqelltql gvsferivtg ieeiraeges aqqyvsrlar ekaqagvacv
       61 prdlpvlgad tivilngevl ekpydaehaa rmlrkmsgqt hqvmtavala drqhvldclv
      121 vtdvtfrvlt ddeiaayias gepmdkagay giqglggcfv rkihgsyhav vglplvetye
      181 llsnfnslre grdnydg
//
LOCUS       WP_181529541             280 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Ensifer adhaerens].
ACCESSION   WP_181529541
VERSION     WP_181529541.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
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="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     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=30265
     Region          8..256
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mmsiqstkse qklawvtgas sgtgralala lvregysvvv tarnhdrlvd lqheaasegr
       61 itvldgdvtd padmervmaa ieydhghlsl vvlnagvalp vrgdelhrea feksfavnln
      121 gvvncllpav dhmktqgygh iaivssvagy gglptsaayg atkaalinma eslkfdldrl
      181 gvrlqiispg fvdtpgtari rflrpapvns eeaarrivag lksrrfeiaf prrfayavkl
      241 mdllpyslyf rllnwltrgk veamegqkra gpggrprqav
//
LOCUS       WP_181531324             602 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Enterobacter roggenkampii].
ACCESSION   WP_181531324
VERSION     WP_181531324.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter roggenkampii
  ORGANISM  Enterobacter roggenkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 602)
  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 602)
  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 602)
  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 602)
  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 10009476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Enterobacter roggenkampii"
                     /db_xref="taxon:1812935"
     Protein         1..602
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=68160
     Region          30..430
                     /region_name="COG5610"
                     /note="Predicted sugar hydrolase, contains GT1 and HAD
                     domains [General function prediction only]"
                     /db_xref="CDD:444341"
ORIGIN      
        1 msnyndfdld nssdifsyfd gltedkiaha evisfdffdt lfsrpladpe dafdilgekl
       61 nikdfrarrq daqtkafrtm kknnrkeiti adiyaefsek ehdskvlcea eyqlelslve
      121 pnpvifsffk rliasgkkvv vtsdmylpat ffkdalekyg vtgidvfssa denatkrdtg
      181 elfdilikkl kvlpdkvihl gdnhtsdyvr pkekgleafy ylshyadtls kglplsvsia
      241 qglvkhhsgc nvldsykslg fiyggtvavg flswiigkik ehsidhvlfl srdgyimkkm
      301 veqdgscnlv ksdyfygsrt sltlstinde nfveylpfll sgaeglqpre llerigvtpp
      361 desvmasfgl sankvltpel fplmsqflfa yrwqilqvcr rnrrglysyi ksvgikagdk
      421 ialvdvgwsg ttqeafytai kdiidveihg yyfclantee rkrrsrflnm yamyenancd
      481 stivdaiyen rvvvelffsa phssiigydv dpfepiqdeg rglsntmsqc vaeicegsll
      541 farkyknfce qlqfnltpye ltnsmvelat tkkwnnftsi ttvsnfdawg ssrallnksd
      601 fg
//
LOCUS       WP_181533321             219 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Citrobacter sp. RHBSTW-00903].
ACCESSION   WP_181533321
VERSION     WP_181533321.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00903
  ORGANISM  Citrobacter sp. RHBSTW-00903
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHBSTW-00903"
                     /db_xref="taxon:2742670"
     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=23853
     Region          6..213
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mtmkwydlak tlmkeqgvtq eqlaehlgit kgavshwlna rrepaleeia rileflgkkn
       61 fsvgaggliv ddtlkgdvey vgpykpgkky pvlssvkaga wgeaveaytl kdidlwlesd
      121 ahiqgeafwl evegdsmtap vglsipegtf vlfdtgrdpv ngslviakls dtneatfkkl
      181 ivdggqkylk glnpqwplvp ingncriigv gvetklrli
//
LOCUS       WP_181535055             223 aa            linear   BCT 28-DEC-2024
DEFINITION  YczE/YyaS/YitT family protein [[Anoxybacillus] calidus].
ACCESSION   WP_181535055
VERSION     WP_181535055.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..223
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..223
                     /product="YczE/YyaS/YitT family protein"
                     /calculated_mol_wt=24643
     Region          9..212
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 mtenetsyks thlvmqwgiy ftgllvmcfg ivltikanlg sapwdvlhig lyrqfgltig
       61 twsiivgfav ltataliskr fpqigafanm vfvglfidly mlipyirtpd tlwlkiimfl
      121 cgivitgygi glyisakvga dprdslmlal teltgwkvqy irigievfvl ffgwlldgpv
      181 aigtfifsva igsvvgialp qcqsfvnril mrqvhmkmng lsr
//
LOCUS       WP_181535448             690 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [[Anoxybacillus]
            calidus].
ACCESSION   WP_181535448
VERSION     WP_181535448.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 690)
  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 690)
  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..690
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..690
                     /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=76992
     Region          3..>75
                     /region_name="COG4091"
                     /note="Predicted homoserine dehydrogenase, contains
                     C-terminal SAF domain [Amino acid transport and
                     metabolism]"
                     /db_xref="CDD:443267"
     Region          111..>228
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
     Region          226..684
                     /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 mkkvlivgag kggtallkil ketkimevva ivdinekapg mllaremnik tghdwrpflt
       61 edidvvieat gnvevfkeir kmrkkntvvi pgevayitaq lveekeqlia rlkneknrhd
      121 lifnsthdgm ivvdefgyit hvndsaekmi gvkkgnaigk hileiiptsg lprvlktkit
      181 evhqeftlgn grkiittrvp midesgrlfg alavfkdite fvqlaeeitn lkeirmmlea
      241 iihsseeais vvdehgkgil inpaytritg lseeqvigkp atadiseges mhmkvlktrr
      301 pvrgvrmkvg pknrdvivnv apiivdgilk gsvgiihdvs eiqrltneln rarqiirtle
      361 akysfadivg tseemmvaie qaklaaktpv tillrgesgt gkelfahaih nasdrkynkf
      421 irvncaaise slleselfgy eegafsgakr ggkrglfeea nngsifldei gelsantqak
      481 llrvlqegei vrvggtkpip invrviaatn vnlekaiadg tfredlyyrl nrmpiyippl
      541 rarkqdipal cqhliqklnq dygrnveglt eeairyllsy dwpgnvrele nvlgramifm
      601 kfnevlidvk hipalripsn eadlairfsn ddveeqtlae mvekyearmi eralrkhngn
      661 ktatakalgi sirnlyykle kygiannnmq
//
LOCUS       WP_181535894             124 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [[Anoxybacillus] calidus].
ACCESSION   WP_181535894
VERSION     WP_181535894.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     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=14287
     Region          8..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msaaqkhdif qaiadptrrk ilklladkkl pvtaisrhfp msrtavskhl rilsesklvs
       61 vekagrekly klqpeallel kewlsffeqf wdnkismlky fveneeigkl nlimpesnee
      121 skds
//
LOCUS       WP_181535896             144 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [[Anoxybacillus] calidus].
ACCESSION   WP_181535896
VERSION     WP_181535896.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 144)
  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..144
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..144
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16197
     Region          11..144
                     /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..30,35,49,51,53,55,60,62..63,65,
                     68,74,76..77,84..85,87,89,99,101,103,105,122..130,
                     132..134,138)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mqtnnqskvp dirktavfna piqkvweava tsegiaawfm pndfepkvgh eftlqtpfgp
       61 spckvleldp phrlsfswdt sgwrvsfelk elngkteftl ihsgwgethe iipkageths
      121 virnrmdngw ealvneklrk vveg
//
LOCUS       WP_181535938             341 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [[Anoxybacillus] calidus].
ACCESSION   WP_181535938
VERSION     WP_181535938.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     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=35660
     Region          33..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 mkndtvnqys rpwiaitviv igifaivfgi alsisvgaan iqlstvweal vhynpnrteh
       61 aiiqdlrlpr sladvlvgas favagaimqg mtrnpladag llglnagatl mvavcfaflp
      121 glsynslilf sflgaavaag lvygisslar ggltpvrlvl agaavsallt alsegiaihf
      181 qlsqelafwy aggvagvkws qlkvmtpwlv valvgsllls rsitllslgd evatglgqkt
      241 glvkmlgmii vlllagvsvs avgpigfigl vvphiarffv gvdyrwiipc savlgggfmi
      301 madigarmin ppyetpigvl faligvpffl yvarkgrrel s
//
LOCUS       WP_181535755             257 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [[Anoxybacillus] calidus].
ACCESSION   WP_181535755
VERSION     WP_181535755.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 257)
  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 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   3  (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]
REFERENCE   4  (residues 1 to 257)
  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..257
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..257
                     /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=30100
     Region          1..256
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mndyqqfian vkkktgidla qykeaqmkrr ltslyekrgf knfheffkam eadeklfhef
       61 ldrmtinvse fyrnakrwev lekkilpkll aqnkrlkvws aacstgeepy tlaiilskfm
      121 plsqvsvlat didenvisra kigvypersl qevpeeikkk fftkeglhyk isedikktvt
      181 fkkhnlladp fdvnydlivc rnvliyftee akhalyhkfn kalkpggiff vgsteqifnp
      241 glygfetedt ffyrkvq
//
LOCUS       WP_181535972             425 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [[Anoxybacillus] calidus].
ACCESSION   WP_181535972
VERSION     WP_181535972.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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   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 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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..425
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..425
                     /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=48290
     Region          10..410
                     /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(20..21,24..25,28,59,114..115,117..119,122,142,
                     145..146,149,230,233..234,237..239,242,284,288,337..338,
                     342,346,362,365..366,369..370,373)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mkirdwdrnl kvrlfgeali hitfwmffpf mtiyftdafg kdkagfllif sqvfsvvasl
       61 lggycadrfg rkrmmvlsay gqglaffffa lasspwftsp fvgflcfsla gifgsfywpa
      121 sqamvadvvp eedrssvfav fytsmniavv igpmiggify eehrfellla agvscvllat
      181 ilvkmlretv pfysiesdgs mkwyqflreq irsygiiird ktfllfivag ilvgqtmmql
      241 dllipvytke vvekqtlfsi gaysvllsge kafgllisen gllvalftvw vtkwmshyre
      301 rsvfiwssii ygisimmfgq ttniwgliia mavftfaelm tagiqqtfis klapeemrgq
      361 yfaaaslrwt igrtiaplsi titvwlsyqw tflilsvlaf fsafiysimf qrfekqqakk
      421 tvpqm
//
LOCUS       WP_181536143             140 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [[Anoxybacillus] calidus].
ACCESSION   WP_181536143
VERSION     WP_181536143.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 140)
  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..140
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..140
                     /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=16248
     Region          1..135
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mkvvekqiev ryaetdqmgv vyhanylvwm eigrtqfike lgfhyadmek egvispvtdl
       61 qisykkplhy getatvktwi eyydgirvty gyeiltpdge iaatatsqhv cvkrdsfrpi
      121 sikkyfpdwh eayeqvkkqa
//
LOCUS       WP_181535096             589 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [[Anoxybacillus] calidus].
ACCESSION   WP_181535096
VERSION     WP_181535096.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     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=66450
     Region          4..583
                     /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 mltkrvwfil ftiqlgiall igriiqiqlv stesfskekv nlieasvaqr tqemvlddgr
       61 gtfidrngkp lmhdyiptlv lfpflkkmdw pieklatiin vsanviqqal qeqkqpfifm
      121 mnneplrlte tqmkkinqlr ipgvfavkkq yplekkyaeh liglirenpd llrsrypdkm
      181 hlspktkigi sglqgafdef lipdgetrll yhvdgdggpl fglqvkysep anpfypvsvq
      241 ttidrdlqei aqevvrehgl kkgglvlldv etndilamvs vpeinthdpy adndsgnqmi
      301 lpqipgsifk tviaaaaieq glvspyrtfd csktidgkpe enhnygmlnf adsfalscnn
      361 tfgtlgkelv eqdkdiieky aqklglyplv swkghvyhfe nfkqlpeekk giiwhdnkdk
      421 yvplavaqta igqkdvrisp lavanmmati arngeakqvr avnkilykng ttffsfpeqk
      481 fsnetisynt altlqkllrs vvtheegtgr rfqtlpyeva gksgtaetgk itshdeelin
      541 kwfagffpad spkyalvvve leqtsnkavt ndvfydvvkr iyefneqhs
//
LOCUS       WP_181536135             170 aa            linear   BCT 28-DEC-2024
DEFINITION  peroxiredoxin family protein [[Anoxybacillus] calidus].
ACCESSION   WP_181536135
VERSION     WP_181536135.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 170)
  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 170)
  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 170)
  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 170)
  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..170
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..170
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19122
     Region          38..164
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mkkllatlll lglvgyglwq vlaennektt glaignaapd felktldgks irlselqgqk
       61 vilnfwatwc ppcraempem qnfyekhnkd vevfavnlts qdsrdkvhsf ikengltfpv
      121 vldeegdvlk lykispipts yiidsegiir hkyvgpmtyd qmveltesmk
//
LOCUS       WP_181536460             234 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA (adenine(22)-N(1))-methyltransferase [[Anoxybacillus]
            calidus].
ACCESSION   WP_181536460
VERSION     WP_181536460.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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 234)
  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 234)
  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..234
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..234
                     /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=26246
     Region          5..233
                     /region_name="TrmK"
                     /note="tRNA A22 N1-methylase [Translation, ribosomal
                     structure and biogenesis]; COG2384"
                     /db_xref="CDD:441950"
ORIGIN      
        1 mnelklskrl etvvsfipkk skladigsdh aylpcyayln gyitmavage itdgplcsar
       61 eqvkktgleh visvrkgdgl eviqpnevdc itiagmggtl iknildkgke klvgvkrlil
      121 qpnvgahvvr qwlidhdwel iaerileede kiyevlvaek gdgkkpyvdl eaevllgpfl
      181 mkeqneafkk kwhqeiaqwr kivhelskka ttdealakrk elerkiqlve gilg
//
LOCUS       WP_181536228             393 aa            linear   BCT 28-DEC-2024
DEFINITION  alanyl-tRNA editing protein [[Anoxybacillus] calidus].
ACCESSION   WP_181536228
VERSION     WP_181536228.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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 393)
  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..393
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..393
                     /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=44440
     Region          1..226
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
     Region          244..361
                     /region_name="DHHA1"
                     /note="DHHA1 domain; pfam02272"
                     /db_xref="CDD:396724"
ORIGIN      
        1 mtkklyyvsp stvnwtttit sikkenndyl itlaetafyp egggqpsdsg tidgikvidv
       61 feedgevyhr lpalpdyssv scqidwhrrl dhtqqhsgqh llsavcielf dvhtvsfhlg
      121 ketvtidlni shlseqqlks ieeraneliy cnvpvktyfi skekaislpf rkfpdieepi
      181 rvvemegvdt saccgthvsr tgeigiikll ktekhrgltr lhfkcgiraf adyssahniv
      241 tkiaqhlgtn retlfdkiik leeenklllk elehlkgelh dfeadklirn hhslvvqvye
      301 nktlkdlqai aqritakqdk vvilattlen rlvaaksaaf tfhmgqlfke qqahfhgkgg
      361 gnerqaqmtf tnstdltafm vslqteierl ink
//
LOCUS       WP_181536362             206 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [[Anoxybacillus] calidus].
ACCESSION   WP_181536362
VERSION     WP_181536362.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 206)
  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 206)
  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..206
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..206
                     /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=24038
     Region          25..199
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 meyktiirkl snripillgh eqfsqfavll pliekddelh vlfevralhl krqpgeicfp
       61 ggkidpndkn aqeaairetv eelgiekani tnifpldyiv spfgtiiypf vatishphkm
      121 kpnkeevaei ftvplsffqq tapevyhvhf kvepesnfpf dkipngenyn wrprkmdehf
      181 yyyenkviwg ltariiyhfi elinkd
//
LOCUS       WP_181536723             365 aa            linear   BCT 28-DEC-2024
DEFINITION  chemotaxis-specific protein-glutamate methyltransferase CheB
            [[Anoxybacillus] calidus].
ACCESSION   WP_181536723
VERSION     WP_181536723.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF001965.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK00742
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     gene            1..365
                     /gene="cheB"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0008984 - protein-glutamate
                     methylesterase activity [Evidence IEA]"
                     /GO_function="GO:0050568 - protein-glutamine glutaminase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006482 - protein demethylation [Evidence
                     IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0018277 - protein deamination [Evidence
                     IEA]"
     Protein         1..365
                     /product="chemotaxis-specific protein-glutamate
                     methyltransferase CheB"
                     /EC_number="3.1.1.61"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0008984 - protein-glutamate
                     methylesterase activity [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=40049
     Region          1..364
                     /region_name="PRK00742"
                     /note="chemotaxis-specific protein-glutamate
                     methyltransferase CheB"
                     /db_xref="CDD:234828"
ORIGIN      
        1 mekikvlvvd dsafmrklit dflseapnie vvgiarngqd aiekikelkp hvvtldiemp
       61 vmnglealkr imeehpvpvv mlssttkega entvlsmqyg aidfiakpsg pisldlhkik
      121 eeiitkvlla sranlrtfgk sevkkinpvp fpnyskiete efssnvhrgq ekkkivcigt
      181 stggpralqq vlmrlpetiq apilivqhmp kgftkslatr ldslckihvk eaedgellkn
      241 gtayiapggf hlkvtkrrnv paiqidespe rnghrpsvdv mfesistlyd yekiavimtg
      301 mgsdgteglk hlrqsgyvka vaeseetavv fgmpkaaita nlvddvvpln kiaemimkyv
      361 ngqgv
//
LOCUS       WP_181536948             310 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [[Anoxybacillus] calidus].
ACCESSION   WP_181536948
VERSION     WP_181536948.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..310
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..310
                     /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=35890
     Region          41..309
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msgmnthysr plkfenredy vgprllrrlp egvedrpyll fevkplspii gaeiigvdlr
       61 epitpelqae lnrallewkv lffrnqkits eqqrafarlw gelevhpffp ieegqskeiv
      121 rfsrnnkqgg yeniwhadvt franpakaav lrlievppvg gdtlwadmga aydnlpdeik
      181 gridnltaih dftpafshlm tpeelaikqk efppvehpvv rthpetgrkt lfvnpsfttr
      241 ivglepeese kllqylfrqa hipeyqvrfh wekdsvafwd nratqhyavs dyypysrrae
      301 rvaivgdrpf
//
LOCUS       WP_181537242              71 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [[Anoxybacillus]
            calidus].
ACCESSION   WP_181537242
VERSION     WP_181537242.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..71
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7697
     Region          2..70
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mpiivnidvm lakrkmsase laekvgitlp nlsilknnka kairfstlea lckaldcqpg
       61 dileyqpddq v
//
LOCUS       WP_181537298             213 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [[Anoxybacillus]
            calidus].
ACCESSION   WP_181537298
VERSION     WP_181537298.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..213
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..213
                     /product="helix-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=24774
     Region          5..207
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 meskssstkq eivnmlkfqk rltvsemakq lgitemavrr hlntlerdql vrtilvrqam
       61 grpmnvyels ekgeelfpqs ykqialdflk diesvagrdl veklfqnrke rikqmyeeqf
      121 anksfdekvv elahiqnkqg ymtelkkdkd gtyhfiehhc pivevakdyq aacdcelqlf
      181 qqwlgtskvt sqacmakgdd vchyeikkhd yae
//
LOCUS       WP_181536647             517 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [[Anoxybacillus] calidus].
ACCESSION   WP_181536647
VERSION     WP_181536647.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 517)
  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 517)
  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 517)
  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 517)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..517
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..517
                     /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=57223
     Region          50..158
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mkkvfsllfv wflvmtavat padagkftnp gsggapgtwy igstpdnlnp sapvilfvqg
       61 lnssastwyd nndmyetayn ngyqtaflel ydssgtsedm wdngsllaak iqeiynyfgk
      121 klvlvthskg gidaqtalvh ynaypyvsnv itlgsphygs qladlayssw aswltdilgs
      181 ksdgtyslqt symnyfrsit dhhanvnknn yytlagtkwg sfgsslywgg lylsqygtnd
      241 gavtvanayl pngqmlrigd wnhstikygs stfsifkpfl ttngaasssi qtaslvsekg
      301 fesdeagshv irggifqqta venltvesnv rtltinwmsd qpvdtltmis pdhqtvnvpv
      361 dvyqeegvfq gawnhvavin qpmsgewkie aknddtsayl fvatfdselt kniklkpknn
      421 kdkwviemdg tkiktkktkv eysldfvake nnpgkkkgkk lkekvslseh eeimipkqne
      481 agvyhltidi kgetldgkpf ertfvqtiyk dekgnmy
//
LOCUS       WP_181537625             194 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [[Anoxybacillus]
            calidus].
ACCESSION   WP_181537625
VERSION     WP_181537625.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 194)
  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 194)
  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..194
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..194
                     /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=22340
     Region          1..191
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mfytsmrwll kiilcfifri evigiknfpk ngpvivaanh tsnydpvilf sifnrkihfl
       61 akkelfqrrm tnwffqklha ipvdrqsgvv irpvrrslkv iengevlgif pegkrcknge
      121 svnpkkgvaf fglktgapvl pvaiifldtk kwirkpvkvv igpmmylnel krsdyavlae
      181 avmnrsrelr emyt
//
LOCUS       WP_181537637             259 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [[Anoxybacillus] calidus].
ACCESSION   WP_181537637
VERSION     WP_181537637.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..259
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..259
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29988
     Region          29..257
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mdgtivekqr fpspnphidv ylvtymcqgl kikgflaepk afgmydgfly lrggiknvgq
       61 vrlaritqfa aegfvvmapf yrgnqggegn edfagedryd alasfkileh hekvnkdrih
      121 vfgfsrggam alhtailepk vrsvvvwggv sdmeltywer ldlrrmmkrv iggtpskype
      181 rykwrtplye aeriqapvli ihgekdrnvs vehayrlekr lkelnkhvta wyfpkfthyf
      241 ppkenretvk rltewmksk
//
LOCUS       WP_181537829             514 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [[Anoxybacillus] calidus].
ACCESSION   WP_181537829
VERSION     WP_181537829.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF004837.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK06187
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..514
                     /product="long-chain-fatty-acid--CoA ligase"
                     /EC_number="6.2.1.3"
                     /calculated_mol_wt=56186
     Region          1..508
                     /region_name="PRK07656"
                     /note="long-chain-fatty-acid--CoA ligase; Validated"
                     /db_xref="CDD:236072"
     Site            order(171,174..179,181..182)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(174,289..290,311..316,394,406,409,420,499)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(174,214..215,262,264..265,268,289..290,311..316,394,
                     406,409,417..420,480)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(214,264..265,268,289,417..419,474,480)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mnlssrltei atkhptkeay ifqgtsctya eldasiskfa sglsqmgvnk gdhvalllgn
       61 spyfviglyg alragatvip inpiytadei syilnngdvk tvitldllip llekmeerlp
      121 qvehmiicet pqgkeqgial lgkmksfatv iaegtvtyqg pdladddtav ilytsgttgk
      181 pkgamlthkn lysnaqdsan ylkisdddrv iatlpmfhvf cltvalnapl mnggtviivp
      241 kfspaeifkv akeckatvfa gvptmynfll qypegnpedl qtlrlcisgg asmpvallkn
      301 fekkfkviis egyglseasp vtcfnpldrp rkpgsigtni invenkvvne fgeevpvgev
      361 gelivrgpnv mkgyykmpee taaairdgwl ytgdlakmde egyfyivdrk kdmiivggyn
      421 vypreveevl ynhpdvveva vvgvpdpnfg eavkcfvvsk nahlteedli aycrehlaky
      481 kvpssivfle elpknttgki lrralkeqlt stka
//
LOCUS       WP_181537981             389 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl-CoA C-acyltransferase [[Anoxybacillus] calidus].
ACCESSION   WP_181537981
VERSION     WP_181537981.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR01930.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..389
                     /product="acetyl-CoA C-acyltransferase"
                     /EC_number="2.3.1.16"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41144
     Region          3..388
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mkrdavivsa vrtaigrhgg alasvpahif gaevikeair ranispemid dvilgnvlsg
       61 ggniarltal qtglsieipg ltvdrqcgsg inavilatqa iragdgdiyi aggiesmsra
      121 pylmdrpekp ysstppnfrk sqlspkeigd ppmgitaenl vkkykisree qdefalrsqq
      181 rmaiamkegr fneqivpiti pvrkgepivf ktdehprpqt tmealsklpp afleggtvta
      241 gnssglndaa salvimsrek aeelgltpla vvreyavagv dpnimgigpv patrkvleks
      301 glsledidii eineafaaqv iacdrelnmd sekvnvngga iahghplgat gailitkavy
      361 elkrsggrya litacigggq gistiiere
//
LOCUS       WP_181538032             226 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [[Anoxybacillus]
            calidus].
ACCESSION   WP_181538032
VERSION     WP_181538032.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     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=24297
     Region          1..>193
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mktiaiigag pglgfsiakk fgengfrval vsrnqeklnq laaqlkdlgi easgfaadly
       61 dknqivkafs aikekygfid vlefsptagn fpptpasqvt ednamdlfqg lvigaircvq
      121 qvlpdmlekg tgailfttgl samypipmmg nvgialaglr nyalnlhsdl kpkgiyvghl
      181 slgvfikpgt etdpkyiada wyemynkkek aedtfpvgvt petiiy
//
LOCUS       WP_181538037             286 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [[Anoxybacillus] calidus].
ACCESSION   WP_181538037
VERSION     WP_181538037.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: NF005372.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK06914
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..286
                     /product="SDR family oxidoreductase"
                     /calculated_mol_wt=31569
     Region          6..284
                     /region_name="PRK06914"
                     /note="SDR family oxidoreductase"
                     /db_xref="CDD:180744"
     Site            order(15,17..20,40,66..68,94..97,117,144..146,159,163,192,
                     194..196)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(118,146,159,163)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(146..148,153,159,190..191,197,212,215)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mnqtfdkqpv afvtgassgf glltsvalag egyrvlasmr dldnkgrlea vakeagvtdr
       61 ieivqldvtd fstvetviqd vihrygridl lvnnagyaag gfteeltvee wrqqfetnff
      121 glvavtkavl psmrerrsgk ivnissisgr igfpsmgpyv askfavegfs eslrlemlpy
      181 gvhvvliepg syktdiwskg lgavtinpns pyvkemktil kyvnqvadta papdeviqqi
      241 vqvakspspk lrypvgkgvk lgivlknvlp wkwwermmik rlwkrs
//
LOCUS       WP_181538056             639 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [[Anoxybacillus] calidus].
ACCESSION   WP_181538056
VERSION     WP_181538056.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 639)
  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 639)
  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..639
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..639
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=74016
     Region          445..617
                     /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(452,454,456,530,558)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238731"
ORIGIN      
        1 mhrfiqfndk kidsflfmql sdlaktlakn eewevefgyq syvdivhrkl fvshfwdnrp
       61 ledkvngmks dvflrsigsl yhtdfkevvr fierikttsv psfskqlfml aedvrleeic
      121 kkerpgtkka fsirrkvyrr yfksqlnfnl vkavhtdalf ntiyllltad spledvlpis
      181 ekidlampfi rnmltrffet kstkdvaeiv lemievldei lendmlntyf hlpenvyeqe
      241 ergltiddlk rkdplkncdv ldkkkdgded ihddvlptwn retsdmtksf lqfdleqgsq
      301 tdllgegvre geagdqalal vqgsaqkssr kdyskleale qkrdireghl shdygkenky
      361 afpifisptf pssadvvqye qnktivapyq kklkqmiekt lehkktlprs dlhfgrlnkk
      421 llrlltdenp rlfykkhqps tqidavfsll vdcsasmydk meqtklgitl fhealksvsv
      481 phqivgfwed tneatetkqp nyfqtvisfd rslkktsgpe imqlepeedn rdgfairvlt
      541 eqmlkrtekq kfllifsdge paafgyeqng ivdtheavie arklgievin vflangeide
      601 gqkktiqniy gkysilvpdi aelpdvlfpl lkkllyksl
//
LOCUS       WP_181537033             485 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [[Anoxybacillus]
            calidus].
ACCESSION   WP_181537033
VERSION     WP_181537033.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 485)
  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 485)
  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 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   4  (residues 1 to 485)
  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..485
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..485
                     /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=54949
     Region          1..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 manivvidde revgtfflhl legkghhvkl glngkdfsrl ikehpfdlaf idvklpdtng
       61 ldllkqlkse lpsckaiimt gystvktave aikygasdyi ekpfddinel erliegllgs
      121 gstssqndmy klaetlgfiv gknkemndli klaykiakkn vnvliegetg tgkevlahfi
      181 hhasmryeqp figincgavs etlleselfg hekgaftgav kekkgifeia nrgtlfldei
      241 geaslaiqvk llrvletgey irvggetirr tntrviaash vnlaqavaek rfredllyrl
      301 dvvkltlppl reriedlplf ieyflkklns nlsfsddail qmkqyhwpgn mrelfnvvkr
      361 avtlaegett iitpdflpek lktertslsq klfsvrknte dgidleryly ewtsyilslw
      421 kenekvdleh vlsfvkdlek qigrafvmkt lretignrke aaerlnitir klryllkekg
      481 adpkv
//
LOCUS       WP_181536933             230 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [[Anoxybacillus] calidus].
ACCESSION   WP_181536933
VERSION     WP_181536933.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..230
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26321
     Region          60..226
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mtkskkksis tsnqsskwif wvvglfsvcv lgfiflgnlp ekeaaidyeg qpylgkksap
       61 vqivefgdyk cpvcknfnks ffplikkefi dtgkakfyfm nysfinvdsi raaqfaeavy
      121 qklgndafwk fhellyskqp edakyekmdi ftesfledtl kevasdeete kvvrafqenq
      181 skdawdkdms yvkklgvtgt ptlfingkkf egetiedfke mveeaakens
//
LOCUS       WP_181538319             515 aa            linear   BCT 28-DEC-2024
DEFINITION  FumA C-terminus/TtdB family hydratase beta subunit [[Anoxybacillus]
            calidus].
ACCESSION   WP_181538319
VERSION     WP_181538319.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00723.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..515
                     /product="FumA C-terminus/TtdB family hydratase beta
                     subunit"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56492
     Region          1..297
                     /region_name="TtdA"
                     /note="Tartrate dehydratase alpha subunit/Fumarate
                     hydratase class I, N-terminal domain [Energy production
                     and conversion]; COG1951"
                     /db_xref="CDD:441554"
     Region          289..497
                     /region_name="Fumerase_C"
                     /note="Fumarase C-terminus; pfam05683"
                     /db_xref="CDD:461714"
ORIGIN      
        1 mekfqesmyk livetstklp kdvrraiara kakenagtra amalttiagn ikmadenvsp
       61 icqdtglptf kikvpvgvnq ikmkeairna iaqatkdgkl rpnsvdsltg ensgdnlgdg
      121 vpvikfeqwe ndyidvrlil kgggcenkni qyslpceleg lgragrdldg irkcilhavy
      181 qaqgqgcsag figvgiggdr ssgydlakeq lfrsvddvnp neelrqleey imenanklgi
      241 gtmgfggett llgckigvmh ripasffvsv ayncwafrrl gvkvdpttgd iiewlyqege
      301 dvdfakelek teekasvnig etrefvleap iteeqirqlk vgdvvringm iytgrdaihk
      361 hlmdhdspvd lngqiiyhcg pvmlkdedgk whvkaagptt sireepyqge imkkfgirav
      421 igkggmgakt laalkehggv ylnaiggaaq yyadciksve gvdflefgip eamwhlrven
      481 ftavvtmdsh gnslhedvek ssleklaqfk epvfk
//
LOCUS       WP_181537557             364 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [[Anoxybacillus] calidus].
ACCESSION   WP_181537557
VERSION     WP_181537557.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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..364
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..364
                     /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=40709
     Region          3..364
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mnqrlqnlsi wlkendisfa fitstpnvfy lsnfysdphe rllaliafpd kepilvcpqm
       61 evlqakqagw dyhiigysdi dnpwelvsky innqkvhvsk iavekshltm eryeqihtyf
      121 pdtsflnvee klrelrmikd ekeiailrqa aeladfgvet gvkalaegkt eleiiaaief
      181 elkkkgvrem sfatmvltge ktaaphgvpg lapikkgdfv lfdlgvvldg ycsditrtva
      241 fgeangqqke iyetvlkaqi aaihackpgi eigqidkaar tvieqagyge yfthrvghgl
      301 gidvheypsm nstntmplqq gmvftiepgi yvpaiggvri eddvfitkdg veiltkypke
      361 lqii
//
LOCUS       WP_181538513             382 aa            linear   BCT 28-DEC-2024
DEFINITION  monovalent cation:proton antiporter-2 (CPA2) family protein
            [[Anoxybacillus] calidus].
ACCESSION   WP_181538513
VERSION     WP_181538513.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00932.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..382
                     /product="monovalent cation:proton antiporter-2 (CPA2)
                     family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0051139 - metal cation:proton 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=40292
     Region          2..373
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mlilelavil faskiagdis vrlgqpsvlg klligivlgp avlgivndtd ilkeisqigv
       61 illmfiagle tdmdefkksg kaaafvgvlg iivplsmgyl aglvmelsai qavflgllls
      121 atsvsisvqa lkemnklksk egsailgaav iddilviial aflmsmaged vhlgtviikk
      181 viffavaill awkvvpimlr kfaplrvtet visaalivcf sfaylaeftg vaaiigayia
      241 gvaisftdyk hevfekieti sysifvpvff tsigvavkfs gvgqyiwviv alsilailtk
      301 lfgaalgakl agfnwrsslg vgagmvsrge valiiagigl etkllsnelf tvlvvvvlvt
      361 tivtpplmkv ifkdqqmeek va
//
LOCUS       WP_181538390             358 aa            linear   BCT 28-DEC-2024
DEFINITION  FUSC family protein [[Anoxybacillus] calidus].
ACCESSION   WP_181538390
VERSION     WP_181538390.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 358)
  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..358
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..358
                     /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=41649
     Region          1..187
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mklgarvfkt giaitlalfl aklldlpspv fagisavfam qptiyrtyls lveqlqanii
       61 gaffaviivl ifghdpffvg ltailvialf lklrlestip valvtviaim eytgdgfiqf
      121 alirfstill gilaaffvnl vfippkyekk lyykivdnte nilkwirmni rhvsehhllk
      181 eeiekfkenm ikldqlylmy keerdyfpkn kygksrklvl yrqmitttnr aletlkllhr
      241 lenelqhmpm efqqairsel dcllnyheqi llkfigkikc hpdseiatea cnsrkwlvea
      301 fnnhylkrck eadnyhlfpl vgiiieyseq lehldtlids fknyhkdeqs femseqev
//
LOCUS       WP_181538376             222 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [[Anoxybacillus]
            calidus].
ACCESSION   WP_181538376
VERSION     WP_181538376.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 222)
  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 222)
  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 222)
  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 222)
  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 222)
  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 222)
  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..222
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..222
                     /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=24524
     Region          1..221
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 metivitgag tglgkelalq yaeqgntiil tgrrldplla vqkeieqrgg tafsytldir
       61 nyenvkatve eilkrhqvtc linnagvgyf gpftslteeq ihdmietnvk gtifmtkafl
      121 pyfhtipkak ilniistagl rgkvnesvyv askfavrgfs eslvkeleqt nisvtavymg
      181 gmdtpfwegt dhikdrsrlr takevarqii aedngqpeii iq
//
LOCUS       WP_181538907             316 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [[Anoxybacillus] calidus].
ACCESSION   WP_181538907
VERSION     WP_181538907.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     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=35304
     Region          12..301
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mekheklrpi iaqvieniek viigkrdiat lsvvallaeg hvlledvpgv gktmlvrala
       61 rsvsanfkri qftpdllpsd vtgvsiynpk nmqfeykpgp imgniilade inrtspktqs
      121 alleameegn itidgttrpl prpffvmatq npieyegtyp lpeaqldrfl lkmrmgypai
      181 leeieilsra kkippiqelq pvitveelnv lqqkvkdvyv ddtikryive ivqrsrtfss
      241 vylgvsprgs ialmkaaqay afvhdrdfvi pddvqflapy vlshriilks eakfdgvtae
      301 dvvagilert svpiqr
//
LOCUS       WP_181538935             319 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [[Anoxybacillus]
            calidus].
ACCESSION   WP_181538935
VERSION     WP_181538935.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
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="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     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=35572
     Region          4..317
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkprclitgg agfigshlae elvkrghkvt ildnlykgeh syhqelfqhi pfikasilek
       61 dvieelvanh dvvfhlaail gvkstmdksv elietnidgt rnilqaakky nrkvvfasts
      121 evygkatppf sedgdrlygs tdklrwcyav cktleetlcl gyglqglpvt iiryfniygp
      181 rakdgpyagv iprfisaalq gkpiqvygdg tqtrcftyvs daveatikam degvnseiin
      241 igseneisir dlaalirtmt nskspiiyvp fekvypigfe eipnrrpdtv klkqllsfep
      301 tvsftegltq tiewfkrel
//
LOCUS       WP_181539467             155 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Micromonospora
            saelicesensis].
ACCESSION   WP_181539467
VERSION     WP_181539467.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora saelicesensis
  ORGANISM  Micromonospora saelicesensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..155
                     /organism="Micromonospora saelicesensis"
                     /db_xref="taxon:285676"
     Protein         1..155
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15767
     Region          73..134
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mratgkarvg aalfsalalg gvqligaspa lagdftiqat cyrtvsvvgg dvgvsgedip
       61 sagstaasta cgmaqgansa avkklqqtlk ycynqniaid sdfgpatkta lrnaqrsegi
      121 tadgvygtqt rntliwwtgt ttyncnsiel pvrla
//
LOCUS       WP_181539535             840 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora saelicesensis].
ACCESSION   WP_181539535
VERSION     WP_181539535.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora saelicesensis
  ORGANISM  Micromonospora saelicesensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 840)
  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 840)
  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 840)
  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 840)
  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..840
                     /organism="Micromonospora saelicesensis"
                     /db_xref="taxon:285676"
     Protein         1..840
                     /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=89521
     Region          128..800
                     /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 massqrrddg tdrrlrlivg llvvaativa laslrltfpa adaptpdgat lvtltamial
       61 gafvktrvrv rstvhlisws eaaiviaaai apvpwvvlct cigitiasar lppmklafgv
      121 gknilvaaga giafallgwt wpamqapqlv gilsvaylla afldemlaip vialasgtki
      181 stqfrsnldl rlagyavrfv vaaltlltlq mdprlllavp plvlslhlay sarirgrteq
      241 qawqrlartt dalnvvdldn vlttavtqaa elfsadevei elrdggrtvr ggtggitfdg
      301 ptgtltdvdg tivpaplegh drtvdvgmlr lrfrgpvqls ereqytlrtf asalctavrn
      361 aqayaelarv adehayaash daltglanrr hlldegteql strhadgvta lvlidlnhfk
      421 evndtlghaa gdqvlvqvad rlrgaaqpsd lvarlggdef avlmrglpap avaahraetl
      481 laalhepfel dgmrisveas ggisgapsng gmaellrrad vamyqakrag qristyaptr
      541 dtadlgrltl ggdlpravad hefvvnfqpi vdlgtgevts aealarwhhp thglidplrf
      601 leaversgll pafaeaildq aliaavswrd agfdvpvavn vsprslldar fpgsvlarlr
      661 ahdlppdrlv leltetltls qldvvdrvls rlrdegvrla lddfgtgyss lsllsripvh
      721 elkidrsfvt tmessaeaaa virstldlgr sldldvvaeg vesepqrral welgcvagqg
      781 hlfarpmpsg tllaamqrgs ggrpgtlaap lhdtgavirl sqnrrqagrs rpdrlphlpa
//
LOCUS       WP_181538580             538 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [[Anoxybacillus] calidus].
ACCESSION   WP_181538580
VERSION     WP_181538580.1
KEYWORDS    RefSeq.
SOURCE      [Anoxybacillus] calidus
  ORGANISM  [Anoxybacillus] calidus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Paranoxybacillus.
REFERENCE   1  (residues 1 to 538)
  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 538)
  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 538)
  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..538
                     /organism="[Anoxybacillus] calidus"
                     /db_xref="taxon:575178"
     Protein         1..538
                     /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=64092
     Region          7..453
                     /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(60,63,100,103,139,158,162,194,245,395)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(194,245,310)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          468..534
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mkrawwkeav vyqvywrsfy dsngdgygdl qgliekldyi kdlgvdviwl npcyespdkd
       61 ngydisdyyk imdkagtmei weklleevhk rgmklimdlv vnhtsdkhpw fiesrsskdh
      121 pkrnwyiwrd kpnnwrsyft psaweydaat gqyyfhsfav eqpdlnwenp evrdeiykmm
      181 rfwldkgidg frldaialla kpkdfpdaen pediryltnn pgvheylwem nekvlkhydi
      241 ftvgevafvs pkeglkyvge drnelhtlfh fevcdempsw eplrfkeiqk rwyeglwgkg
      301 wnsqflnnhd htrqvtrygn dkeyrvesak llgtmihtlp gtpyiyqgee igmtgvrfds
      361 iedyndiamk nkykeevakg rdpqevlksl qplsrdnsrt pmqwddseha gfttgtpwik
      421 vnpnykeinv kkaledpnsv yyyykkliql rkenpvmvyg nfhdysegdp yiyaytreld
      481 derwlivlnh cdhentyelp eqlahykrew llgnyadiqe sgavlhmrph eariyklv
//
LOCUS       WP_181541194              69 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            saelicesensis].
ACCESSION   WP_181541194
VERSION     WP_181541194.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora saelicesensis
  ORGANISM  Micromonospora saelicesensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora saelicesensis"
                     /db_xref="taxon:285676"
     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=7607
     Region          1..49
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtdrhltqke laayfgvser fvevrvqsge wpvsrlgrlv rfspadvrqi eeavrqpaln
       61 gplasrsaa
//
LOCUS       WP_181541426             346 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora
            saelicesensis].
ACCESSION   WP_181541426
VERSION     WP_181541426.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora saelicesensis
  ORGANISM  Micromonospora saelicesensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora saelicesensis"
                     /db_xref="taxon:285676"
     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=36475
     Region          238..314
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlrlqlgsad lcrvrfadrl hpvgiallag qwlrdptvaa maptlaeraa aaegtaaaqa
       61 atavlrhllp drgrlpdfvt pfdglesvea gleairatpa rrvraevtla yadtsasplr
      121 rrfaaadpev ldlfggavrt wcdavlephw aelvsayrqq vasasqrlaq hglaslfagl
      181 hpgirwrdpv leirtwwdgd lpgtghgiil lpsplagprp rvlveqgypv llvypvvmpa
      241 ggapadddal grllgvtral vlrrlatdgg ltttvlsrav gislssaseh aralrtaglv
      301 tsereggavr hhltalglgl lrgpsgdlge swptpnqaag wppvlp
//
LOCUS       WP_181541556             154 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Citrobacter sp. RHBSTW-00570].
ACCESSION   WP_181541556
VERSION     WP_181541556.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00570
  ORGANISM  Citrobacter sp. RHBSTW-00570
            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 10005179
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Citrobacter sp. RHBSTW-00570"
                     /db_xref="taxon:2742655"
     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=17671
     Region          43..154
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mrnfvtrlrv wfppplilll ffvtdvltai prftfdivni vlsvlltgvc itmilhtawq
       61 mstngttlnp lhpdrttklv tvscyawsrn piylgmsglq lsvalcfgsl vgilavplfm
      121 fvvarlhihv eevqlrkrfg lewerytqrv rrwl
//
LOCUS       WP_181541665             200 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter sp.
            RHBSTW-00570].
ACCESSION   WP_181541665
VERSION     WP_181541665.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00570
  ORGANISM  Citrobacter sp. RHBSTW-00570
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 200)
  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 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   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
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13296807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Citrobacter sp. RHBSTW-00570"
                     /db_xref="taxon:2742655"
     Protein         1..200
                     /product="helix-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=22355
     Region          3..188
                     /region_name="PRK09935"
                     /note="fimbriae biosynthesis transcriptional regulator
                     FimZ"
                     /db_xref="CDD:182154"
     Region          <140..196
                     /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 mqlimfdrqs ifihgmnvil qeripgvnvq gvsqaddlwr tlednpdalv mldgdfdaef
       61 crsllqqmae rfakvkvlvt atdcrkkwlq evtqlnvqai vprdsdaetf tlalnsvaig
      121 mmfiprdcit atecggqnir llsarqreil tmlaagesnk qigrllnist gtvkahlesl
      181 yqrlevknrt qaammlndtl
//
LOCUS       WP_181541446             129 aa            linear   BCT 28-DEC-2024
DEFINITION  cytidine deaminase family protein [Micromonospora saelicesensis].
ACCESSION   WP_181541446
VERSION     WP_181541446.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora saelicesensis
  ORGANISM  Micromonospora saelicesensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Navaratnam,N. and Sarwar,R.
  TITLE     An overview of cytidine deaminases
  JOURNAL   Int J Hematol 83 (3), 195-200 (2006)
   PUBMED   16720547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Micromonospora saelicesensis"
                     /db_xref="taxon:285676"
     Protein         1..129
                     /product="cytidine deaminase family protein"
                     /EC_number="3.5.4.5"
                     /GO_function="GO:0004126 - cytidine deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009972 - cytidine deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=13804
     Region          9..126
                     /region_name="Cdd"
                     /note="Cytidine deaminase [Nucleotide transport and
                     metabolism]; COG0295"
                     /db_xref="CDD:440064"
ORIGIN      
        1 mngepsplel asiawraren arvlgktkvg aavladngiv yagcnvehkf rshdvhaevn
       61 altsmitngg travaiaivs krehftpcgs cmdwifelgg pqcivyitns eglitsehla
      121 salmpfypy
//
LOCUS       WP_181541674             438 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase
            [Enterobacteriaceae].
ACCESSION   WP_181541674
VERSION     WP_181541674.1
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=50316
     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 rglktkstay yvwsnsaqrg tgrlgvkvqp sgskvfyfry yvekgkkekf
       61 iqlgiwpemk lvtanelakk ygawlvegke pqqeleqqrl aeqhimqihr sqgsfeelvh
      121 gyvnkmkldn krtwadvlkr lekecysvip retkakdvtp lqiktilsgi iqrdavvhan
      181 rirsylmaaf nyglkadndp mntsvgitfg levnpvsaip kqssaekvgd twltleelrv
      241 vmeqfveatn vgplmqhlir fcvyaggqrp femiasqwsa idwqqktllv iadvsknkre
      301 hlipltesal qelasvkelt kesnspyifp lstngerpvr tdslarsimy frafnpefkv
      361 ftardlrrtc ktlmgeagis keirdriqnh alndvsskhy drydylpekr raleiwedrv
      421 nnyqrqqenn vvnlfgrr
//
LOCUS       WP_181541726             227 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_181541726
VERSION     WP_181541726.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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 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   4  (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
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..227
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..227
                     /product="helix-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=25808
     Region          12..>198
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mplaerrydr lavrlsliis rlvagetlnm qklatefdvs vrtlyrdfre rliyldlech
       61 qgcyrlrtga gpqgeldvlt fahrtgiagl fpgldrrlvs lllncegapc ltgdavsvgs
      121 patqlsfyrl vqaittcqrv tlltdgnrce rlapyrliaq qshwylvaeh hdrpvvfsls
      181 dihlvqplte sfkrnerfyr ltedlsfira lphfqfiqqa itnittt
//
LOCUS       WP_181541081             346 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora
            saelicesensis].
ACCESSION   WP_181541081
VERSION     WP_181541081.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora saelicesensis
  ORGANISM  Micromonospora saelicesensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora saelicesensis"
                     /db_xref="taxon:285676"
     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=36549
     Region          238..314
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlrlqlgsad lcrvrfadrl hpvgiallag qwlrdptvaa maptlaeraa aaegtaaaqa
       61 atavlrhllp drgrlpdfvt pfdglesvea gleairatpt rrvraevtla yadtsasplr
      121 rrfaaadpev ldlfggavrt wcdavlephw aelvsayrqq vtsasqrlaq hglaslfagl
      181 hpgirwrdpv leirtwwdgd lpgtghgiil lpsplagprp rvlveqgypi llvypvvmpa
      241 ggapadddal grllgvtral vlrrlatdgg ltttvlsrav gislssaseh aralrtaglv
      301 tsereggavr hhltalglgl lrgpsgdlge swptpnqaag wppvlp
//
LOCUS       WP_181541635             739 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora noduli].
ACCESSION   WP_181541635
VERSION     WP_181541635.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora noduli
  ORGANISM  Micromonospora noduli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 739)
  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 739)
  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 739)
  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..739
                     /organism="Micromonospora noduli"
                     /db_xref="taxon:709876"
     Protein         1..739
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77286
     Region          <249..>366
                     /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 msaagsllaa vpaaavllli vaampreaga vaplrlavvr avlltgayav lvvevlgash
       61 altrgaftva wllflvaaaa atglrwrrat rlgqppaaap vpvsaapavs aasrpvpvga
      121 vvsgggpdvs tpaaelgept saptragrrf adlravavda wrtarpgerl lagtvgglvl
      181 vellvallae pnnfdsqtyh lpkvehwvaq gdldfwptai hrqvtippga eylllhlrll
      241 tggdhlhnlv qwaagvvcll vaaritaqlg ggrraqllta fvlattpmvv lqatstqtdl
      301 icaawvacaa tvvldglsrr tgwgtllglg aatgltavtk tsgliavgpl lvlwvlaqlr
      361 larsrnaast dpaaagggrr swpigglart vggsvlilvv aavvvgpfla rvtaefghpl
      421 gpprlresip merhdpasiv vnalrighta fdtplaplrr agaeliisga eaigvdpqdr
      481 aitfgrelfp epawypdedr vafplagala vigavmalar prriaperag slrayaavvl
      541 tavllhtami kwqpwgnrll lyavvlavpl aglwldallr nraggrrtva tvaavtvlat
      601 salagvlavs ygfprrlvga gsvfttsdwd trflrrpqwa defrwaatav qdsgarrigl
      661 vqqndnweyp wwlllrqpdg gspdlvalqs vlperppadp ssvdaivctg nkaacaklvp
      721 agwrlefrgy vgyalppgr
//
LOCUS       WP_181542234              68 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter
            hormaechei].
ACCESSION   WP_181542234
VERSION     WP_181542234.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae 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="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     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=7514
     Region          1..64
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mntinqslir lpevlkrtgf gkawvyrlik dgkfpapvki gtravafves eidawiqsvi
       61 etsrnnva
//
LOCUS       WP_181541210             942 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            saelicesensis].
ACCESSION   WP_181541210
VERSION     WP_181541210.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora saelicesensis
  ORGANISM  Micromonospora saelicesensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 942)
  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 942)
  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 942)
  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 942)
  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..942
                     /organism="Micromonospora saelicesensis"
                     /db_xref="taxon:285676"
     Protein         1..942
                     /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=101971
     Region          11..257
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          139..942
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          733..761
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          773..801
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          813..841
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(814,817..818,821..822,824,854,857..858,861..862,
                     864..865,894,897..898,901..902,905)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          846..882
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          893..921
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdpagappaa ryqllgpvev rsaygerlal gtpmqvrlla vlmsqpgtgw sidqlvdelw
       61 qgrppktaag nvktyvwalr ralrspgfpd pailagptgy rlaldgltvd svafddlaqr
      121 gysalrhchw saaqesfeaa lalwrgepfa glpgwgvlls vrarlqeqrs slaeevadlq
      181 lragrhheli eplrsqvndd plrerpwgql mvalartgrr adalatyrql rhllaeevgv
      241 epgpdlqhlh trilraerel ltpdprpper taprivprql papptlftgr aaelarlttl
      301 llgdsrsast vvitgtggvg kswlalrwah dnlhhfpdgq lhvdlggfgt atqeaspsav
      361 vvrsllpalg vkpleipaep aaqfalyrsl tadrrllvll dnardaeqvr pllpgstrcg
      421 vlvtsrhtlp glvatdgahp laldlpsdde arhllvrrlg tqraaaqpaa vdelirrtar
      481 lplalsivaa raaarptfpl qaiaddlaas rgglaalatd daatdvrtvl swsyrllsad
      541 aarlfrqisl hpaadvsaaa aaslagapph lirpaldelt ranllaeqsp nrfrchdllr
      601 aygeeltyal drpadrsavr rrvldhylrv ardaarlvdp gwqpldpphp ptdaspsafa
      661 dhraalawft ieqrvllaav ddavthgsda hagdlaqalt pllsrlsqwh dlaavqaiav
      721 tvaqrrgdpr aealahrdla lahiqhrrfg aahhhlrram aryeqagdrp gqasahlhla
      781 wlsdiegdag aalphareal alassaddrl geaaalnalg wsharldeha raiayceqal
      841 alyeeaedrl gaahtwdslg fayhglgkhp taadcyrral alysdvqdpc gradtlvrlg
      901 dthqavgdhd tsvdlwrqal aildrvghpq atvlserlea yr
//
LOCUS       WP_181544979              81 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Brevundimonas].
ACCESSION   WP_181544979
VERSION     WP_181544979.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brevundimonas
  ORGANISM  unclassified Brevundimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
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 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="unclassified Brevundimonas"
                     /db_xref="taxon:2622653"
     Protein         1..81
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8777
     Region          2..70
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mpiivrldvv maqrkvrsnv laraigiset nlsllksgkv rglrlatlda icryldcaps
       61 dileyrpate etarpkalkt g
//
LOCUS       WP_181545638             319 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YbgA family protein [Citrobacter].
ACCESSION   WP_181545638
VERSION     WP_181545638.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            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 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36041
     Region          77..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 vqttqgnirm cfshapgedv tdkmsdftas yinglgglsg fivcakspsc gmervrlydd
      121 kgnrgrkegt glftgtlmet ypwlpveedg rlhdpvlren fvervfalhe lnmlrasglt
      181 rhgllnfhsr yklqllahhq agyrdigpfv aslhqwddld affvvyrekl mailkkpasr
      241 knhtnvlmhi qgyfrdrlnt rqrgelrdvi lnysggllpi lapltllkhy laeypdsyll
      301 tqnyfdpypk dlalrlmin
//
LOCUS       WP_181545841             642 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Citrobacter].
ACCESSION   WP_181545841
VERSION     WP_181545841.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=72539
     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 elavtlenil sylddnlekm
      121 nrpalqaylk kmhtldaqlg rlssgalnkd vnsinnanqk iqtlyyiyst tsvlliilsa
      181 ilgvlifyqn rnilrahlqv kslaeelqks keklqiqnak leydvyhdsl temnnrqlfw
      241 sdlnktiema eknndavtvm lfdldrfkev ndtyghdagd mllrqisdrl istsltsdtl
      301 yrlggdefaf lssgltesra vsraqkicef isqpytiynt iinittcvgi visenerrsd
      361 ylykfadlal yeaknegsgk ikvfrqrmle klqesrtleh dmalaivnke fvvyyqpivd
      421 sfsqkiysye alirwvhplk gllspdsfip vaektgmine mgkavleiac reaagwavpa
      481 kisvnvspvq lsskafagiv ltilketglp pdrlelevte sslftesatp intlnklrtl
      541 gvkisiddfg tgysslsrls rlafdkikid ksfvhsistq edaltiikli tgmakslnmk
      601 avaegvetqe qltrlqalgc dfaqgylfgk pqpcideeir ng
//
LOCUS       WP_181545843             319 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YbgA family protein [Citrobacter].
ACCESSION   WP_181545843
VERSION     WP_181545843.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            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 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36067
     Region          77..315
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mntqpvigis gcltgsvvrf dgghkrmgfv mdelaqwvtf kpvcpemsig lpvprpalrl
       61 vqtaqgnirm cfshapgedv tdkmsdftas yinglgglsg fivcakspsc gmervrlyde
      121 kgnrgrkegt glftgtlmet ypwlpveedg rlhdpvlren fvervfalhe lnmlratglt
      181 rhgllnfhsr yklqllahhq agyrdigpfv aslhqwddld affvvyrekl mailkkpasr
      241 knhtnvlmhi qgyfrdrlnt rqrgelrdvi lnysggllpi lapltllkhy laeypdsyll
      301 tqnyfdpypk dlalrlmin
//
LOCUS       WP_181545884             402 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [Citrobacter].
ACCESSION   WP_181545884
VERSION     WP_181545884.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=43236
     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 mrnvtvlaac lftasvsaae sngeyiaris dcvachtteg gaamaggkkf ptpvgdiyst
       61 nitpdktqgi gnysyedfdk avrqgiakdg hplypampyp syaklsdddv qalyryfmhd
      121 vtpsaqpnne naipwllsar wplhfwnwlf tdapataver aktddnaalv krgaylvegp
      181 ghcgschtpr gmamnekayt nadaeylsga midgwyapsl rgtgmseqel ksllltgksk
      241 haavsgsmae vvtqstqylt dddataiaqy llslksekpe tvraaattvs wsnspeagkv
      301 tynrycstch glegkgtddn apslinnplv mvddptplfr viahgaetpt trgsvsfkmp
      361 ayggmlsdne mrdvinyvrk swgegngevg qedlagikka sh
//
LOCUS       WP_181545915             330 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Citrobacter].
ACCESSION   WP_181545915
VERSION     WP_181545915.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=34830
     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 msrrircslw tlalmlvvmt imatgfgalr lpvsllwrdg dealrqiwlt irlprvllal
       61 viggslalag cvmqglfrnp ladpgllgis sgaacavalw vvlpvslpal lmlyapmlaa
      121 flgalaatvv ifilsqqrda slsrlllvgi ainalcgaav gvvswvsnda qlrqlslwgm
      181 gslgaaqwst llavtsltvp tvliiwrlap alnllqlgee eahylgvdvr tvqrvlllcs
      241 allvaaavav sgvigfiglv iphlmrmwlg sdhravipgs vlagafllli adtlartava
      301 paempvgllt sllgapwflw lifrqrgphg
//
LOCUS       WP_181546186             248 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Citrobacter sp. RHBSTW-00524].
ACCESSION   WP_181546186
VERSION     WP_181546186.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00524
  ORGANISM  Citrobacter sp. RHBSTW-00524
            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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Citrobacter sp. RHBSTW-00524"
                     /db_xref="taxon:2742653"
     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=27303
     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 mdipkiftis esahrihnpf taqkyatlgq vlrmapgtri ldlgsgsgem lctwardhgi
       61 sgvgidmsrl fseqatlrak elgvnehvrf ihadatgyia eekfdiaacv gatwiaggva
      121 gtvrqleqsl kpggimlige pywrqtpate siaqacgats vtdflslpel vssfdllgyd
      181 vvemvladqe gwdryeaakw ltmrrwlean pddefapevk eqlrssparh vaftreyigw
      241 gvfaliqr
//
LOCUS       WP_181546251             555 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: O-antigen ligase family protein [Citrobacter].
ACCESSION   WP_181546251
VERSION     WP_181546251.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=62472
     Region          171..386
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mmnalnriap lpaqklllfi slffwcgvmh lywpnnggsg lslplnitsw iyavvlaasa
       61 svlvprqrwr itvpatvfsm galiltllcl ltpgvwqfea qlvagallgg vlvylvtlqi
      121 plaantltvl ltllwgacvi eclaflyqyw hlpgvdywef awrrgtrpyg ifqqvnlmas
      181 ftasgvllsa plflrlrdry rivigvalvm mgfvlhesqs qtgyvsvvvg evlllvvfpa
      241 qrrmllllll plalgmvagt larhflsvat vdhlttsqvr wtvlktslal faerpwtgwg
      301 vgsfaavfle ragplglssi shphnelvlw lvegglvgla galcfitggf wlwmhgnrwr
      361 raclvaalpv vihmlteypv rqstphwlll illlrcadsp lkgvrltlts tsliralali
      421 sfltftplll lslhtqqqlt laerqsaqwr laeslpvggw llapryrfdv qmgylqryqr
      481 trdarwleav rrwapdyvrv hpdpnvsftq illalqqrdl peahrlatrf yltypndrri
      541 pwlqdarrpf nqkme
//
LOCUS       WP_181546377             205 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: IbrB-like domain-containing protein [Citrobacter].
ACCESSION   WP_181546377
VERSION     WP_181546377.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 205)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..205
                     /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]"
                     /calculated_mol_wt=23708
     Region          42..141
                     /region_name="IbrB_like"
                     /note="immunoglobulin-binding regulator IbrB activates eib
                     genes; cd16397"
                     /db_xref="CDD:319255"
ORIGIN      
        1 mqhrltqelt gflsglseee rieainqfrm aihsvspfre epvdcvlwik nehispndyn
       61 pnnvappekk llqksleadg ftqpivvvhs teeeyeivdg fhrhelgksk pslksrlhgy
      121 lpvtclqrer hermaatirh nrargrhkih amseivrels llgwseekis kelgmdddev
      181 lrlkqinglq elfadrrfsk awtvk
//
LOCUS       WP_181546216             389 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Citrobacter].
ACCESSION   WP_181546216
VERSION     WP_181546216.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=44363
     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 mplndmqirr akpedkpytl gdgqglslli epngskswrf ryryagkpkm islgvyptit
       61 ladarsrrdd arklvaegkn psevrkeqki alqtesesaf ekiatewhqm ksakwsagya
      121 sdimeafqnd ifpyvgarpv geikplelln vlrkiekrga lekmrkvrqr csevfryaia
      181 tgraefnpaa dlssalevhh snhfpfltvd eipdflhald sytgsrlvki atkllmltgv
      241 rtielraalw sefdlgnaiw eipvermkmr rahlvplstq aldllnelki mtgnyryvfp
      301 grndpnkpms easinqlikr vgfagrvtgh gfrhtmstvl hehgfnstwi eiqlahvdkn
      361 sirgtynhav ylqkrkemls wysnyllsm
//
LOCUS       WP_181546382             271 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_181546382
VERSION     WP_181546382.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  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 271)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 271)
  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..271
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..271
                     /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=31024
     Region          5..261
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          180..261
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mthtrdipqs fwrdeqlpwl elrstwqsqq aykrhhhsql sigaileggt cclcddkeyh
       61 lkggdlivip plaphscnpv ngqfrsyhml yldarwclah lpalnsnqrl ctrtpvirdp
      121 qlfqcymhlv almpqrqttq itdaaqallr slplqsvtpe nlsvtsqylr erlqsslhsp
      181 psldeladec hmrketlirt fkqdtgltpg nylnivridy arqrlragde ivdvgyqsgf
      241 adqshfhrtf vrytaatprq yalgrsisdn n
//
LOCUS       WP_181546682             271 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_181546682
VERSION     WP_181546682.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  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 271)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 271)
  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..271
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..271
                     /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=31132
     Region          5..261
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          180..261
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mthtrdipqs fwrdeqlpwl elrstwrsqq aykrhhhsql sigaileggt cclcddkeyh
       61 lkvgdlivip plaphscnpv ngkfrsyhml yldarwclah lptlnsnqrl ctrtpvirdp
      121 qlfqcymhlv almpqrqttq itdaaqallr slplqsvtpe nlsvtsqylr erlqssllsp
      181 psldelanec hmrketlirt fkqdtgltpg nylnimridy arqrlragde ivdvgyqsgf
      241 adqshfhrtf vrytaatprq yalgrsisdn n
//
LOCUS       WP_181546779             259 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: prepilin peptidase [Citrobacter].
ACCESSION   WP_181546779
VERSION     WP_181546779.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=28762
     Region          1..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 mteliniaam alvglivgsf mnvvvyrlpi miehrhsetw niawppshcp hcqhrlsvrn
       61 tiplfswlwq rgrcqacaqp iswrypltel acscvfalsa afvssisdai aimtlfwfif
      121 alaqidlrty llpdvltqpl lwlglmyhsv ydremlsdal ygavagyltl wlvwwgckii
      181 agkegiglgd akllaamgaw cgwsalppil laasllgiaw wlilrltrrt sipliafgpw
      241 lglagwlifs aqssgvigy
//
LOCUS       WP_181547011             211 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_181547011
VERSION     WP_181547011.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 211)
  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..211
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     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=24425
     Region          <137..194
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mkiliqdpye fycdglkhff ieiffgrtan niifltsysq qnfdkadivv islapgehlm
       61 cfpelqnrtt giiigltdev vaspsdlpfc iariifihrq dslltvkekv ltawresrkk
      121 qiqpgktlcf hcphkvltrq qrrimsficq gittseiarn msisektlyv hkyiirkkfn
      181 lrtnhalfcf lqklagknsq qiylrqipln v
//
LOCUS       WP_181547121             249 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Citrobacter].
ACCESSION   WP_181547121
VERSION     WP_181547121.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=27614
     Region          25..248
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkrkimvvta aygydqvraa ggqtamlpii aeagadgvei rrelltdael ktlstmasai
       61 elfgllacys apeplfledg nlnprlpqll eeaqalqalw lkvslghfsh teqfddlrew
      121 lnnsgmelvv endqtacgrl qpmqrfneac qtqnlpislt fdmgnwlwvg dspeqaaqnl
      181 aptvgyihvk aavthrdsyr avppdeadsr wlallktlpn dvprgiefpl egqdltavtr
      241 hyvellree
//
LOCUS       WP_181546555             518 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: bifunctional metallophosphatase/5'-nucleotidase
            [Citrobacter].
ACCESSION   WP_181546555
VERSION     WP_181546555.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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   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..518
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..518
                     /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=56107
     Region          19..499
                     /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 mklkmlavgv lvslplwasa kdvtiiytnd lhahvepykv pwiangtrdi ggwanisamv
       61 kqekaknsat wfldagdyft gpyissltkg kaiidimntm sfdavtmgnh efdhgwdntl
      121 lqlsqakfpi vqgnifyqns skmfwdkpyt iiekdgvkig viglhgvfaf ddtvsaatrv
      181 gieardevkw lqryidelkg kvdltvalih egtparqssl ggtdvrrald kdiqtagqvq
      241 gldilitgha hvgtpepikv gntlilstds ggidvgklvl dyqqkphqft vknfelktif
      301 adewqpdpqt kqvidgwnkk ldkvvqqtva napveltray gessslgnla adallvaagk
      361 dtqlaltnsg girneipagv itmgavistf pfpnelatmd ltgkqlrslm ehgaglsngv
      421 lqvskglemk ydsskpvglr vsvltlngkp iedatvyhia tnsfladggd gfttftegka
      481 rntsggyyvs navvdyfkag ntltdeqlkg mrvedvkp
//
LOCUS       WP_181546651             517 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Citrobacter].
ACCESSION   WP_181546651
VERSION     WP_181546651.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=58314
     Region          11..>502
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mqmitsrqnr llkfllsrke yvtllkiaey lsvsektvqr dlrlleqwls ewkisidkra
       61 gagvilsadn itdllyldql lgsegddadg mmnnsrrvki asqllsetph etsinklser
      121 yfissasivn dlkvieswit plglslirsq sgthiegses gvrqamasli ngvinhnepg
      181 sviysrldpg sykalvhyfg eedvlfvqtl lqemendlcw slgepyyvni fthilimmyr
      241 itrgnalprk eesitscden ifsiasrmiq hiekriahpl pedevwfiyq yiissgmvie
      301 ehndvsvigh lhssdearli thrliatfae mvdcdlsqdt alydgllihi kplinrlnyq
      361 irirnplled ikgelqdvwr ltqcavnrvf sgwgeravsd devgyltvhf qaamerqiar
      421 krvllvcstg igtshllksr ilrafpdwti vgvvsagslp svltddielv vstinlpava
      481 mpvvyvtaff ndadikrvte tviteklhra tslvven
//
LOCUS       WP_181547192              68 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterobacteriaceae].
ACCESSION   WP_181547192
VERSION     WP_181547192.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=7952
     Region          7..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mitetllted klvdmlfitt ltgltdkwfy klikdgefpk piklgrssrw lqsevehwlr
       61 ervkasrs
//
LOCUS       WP_181547567             205 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Citrobacter].
ACCESSION   WP_181547567
VERSION     WP_181547567.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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..205
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..205
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=22420
     Region          <92..179
                     /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          109..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"
ORIGIN      
        1 mrilhvliia tvipfsaman ttledlqhew sicqyqtlaa kkescfsals qkthnaiqah
       61 ntdaplliws giidsswaga kgglgalslv kqarsnleka ieidpgalqg sawtslgaly
      121 yqvpgwpigf gdkekaeeml kkalainpdg idpnyfygdf llqekknqda kryldkalka
      181 parpgreiad ngrrrdiakd ltsik
//
LOCUS       WP_181547873             328 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CobW family GTP-binding protein [Citrobacter].
ACCESSION   WP_181547873
VERSION     WP_181547873.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..328
                     /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=35865
     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 mtktnlitgf lgsgkttsil yllankdpae kwavlvnefg evgidgalla dsgallkeip
       61 ggcmccvngl pmqvglntll rqgkpdrlli eptglghpkq ildlltapvy epwidlratl
      121 cildprllld eksvandnfr dqlaaadiiv ankadratae senalqtwwq hyggnrqlvh
      181 adhgqidgql ldlprlnlae lpasaehahs hadkkglaal slpsqqrwrr slnsgqghqa
      241 cgwifdadtv fdtigllews rlapvgrvkg vmrikeglvr inrqgddwhi etqnvappds
      301 rieliadtet dwntlqsall rlrldana
//
LOCUS       WP_181548118             523 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: bifunctional metallophosphatase/5'-nucleotidase
            [Citrobacter].
ACCESSION   WP_181548118
VERSION     WP_181548118.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 523)
  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 523)
  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..523
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..523
                     /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=57328
     Region          27..505
                     /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 mnmnnkfsls llslciglss aitftadard itiyytndlh ahvtpgiips vsktrevggf
       61 apiskivkda kekykdvfff dagdyftgpy istltkgeai idilntmpyd avsvgnhefd
      121 hghenlvtql sklkfpvlln nvfysnsdkp liktpytive knglkigvig mhgvsafyea
      181 iaagvregvd cqdpvpyvkk qleelkgkvd ltvllahegv pgrqssggde dvaralkadv
      241 emaktlegyg lnvlitghah kgtpepikvg dtlvvstnay tielgklvld wnpetkkvds
      301 yngklitmya dtykpdpqtq akidewnnkv kkitdrvvay speiltrsyg esattgnlit
      361 dalmykvpya dasfynaggi rselpkgnit ygdvlsmypf tndvmsveis gkdlrsimsh
      421 aadlkngtlh asktvqfkyd stkplgqriv sfnikgkpve dsqfytiald sfigkggggf
      481 sftnsknfky ikglqtaqai idymehvkni vpdhtmrvdd isk
//
LOCUS       WP_181547709             232 aa            linear   BCT 28-DEC-2024
DEFINITION  XRE family transcriptional regulator [Citrobacter sp.
            RHBSTW-00524].
ACCESSION   WP_181547709
VERSION     WP_181547709.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00524
  ORGANISM  Citrobacter sp. RHBSTW-00524
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (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   2  (residues 1 to 232)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..232
                     /organism="Citrobacter sp. RHBSTW-00524"
                     /db_xref="taxon:2742653"
     Protein         1..232
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25669
     Region          3..66
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          92..222
                     /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 mkketlaerl nqameqsgms qgalakasgv aqptiwrlts gnargstkiv eianalgvrt
       61 ewlstgigpm rsdgqqpvsi apikadpnif rvdvldltvs agpgvinsef vevlrsveys
      121 vedarqmfng rkqeqiriin vrgdsmsgti epgdllfvdi siqhfdgdgi yaflydetah
      181 vkrlqkmkdk llvisdnqty rpwepiekee mnkifvfgkv igsmpqtyrk hg
//
LOCUS       WP_181548000             229 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LolA family protein [Citrobacter].
ACCESSION   WP_181548000
VERSION     WP_181548000.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..229
                     /product="LolA family protein"
                     /calculated_mol_wt=25346
     Region          8..228
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mrvsfsprva ftallifsfa vspaenggpf spyarsadpv alsqqsfnhm tsyqvmmrss
       61 sardenkiir ysyqkpgyvr mdftqphsga vlifnpvsgk vtlwpfgvgt lpvlhlsptn
      121 sliqderghr vdrsdigvll gnvrhlqreg tttvvakerl agretthisv mgpgkqtvdg
      181 vhrydiwldn yhglpakvis yapdgqrlet vlldamvint rfpvnfftp
//
LOCUS       WP_181547607             709 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GumC family protein [Citrobacter].
ACCESSION   WP_181547607
VERSION     WP_181547607.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     Protein         1..709
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78003
     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 krestvefsr fakalkknaw kialagivag vvayplismm sskyvstatv
       61 likaqadnvs pfpqvdgfds trsgyyetqy almhsrivle qavrdmklde npaftgekad
      121 aqgadssesr qlrmelalkt lsknlnvigi rttnlasity estspqvaad iangvaqafi
      181 nytleqkrqk vekarelnye kmeeiqksia kqkeemesyl knaglltfrg idgfeteqls
      241 ivtnrladat qrrvaaesvy nevngagksa esvislpsvs nhaqiqdlri aliqaqrtls
      301 elrkvygpkn pailkaeadv qsiqsqtgrv lgelkvglrq qylaaladek nyqqqveqqk
      361 eifqkmaskr dvwngqklsl dkmedlyksl yqrtqelsls gvnadavlyd pavptlkpak
      421 pnkslllvmv vmlvvvfsim yfivkaamdn siaslsrmkk rlnvsplgei rhfsgtsgra
      481 qvrdmilknp lnadivhgir trimldnrpl qtlavasteh gdgrsllanl lansfsfdqk
      541 tllidadffn tgglsselas atsaglaell rgetqleqar itlsdnldfi ahgkstissl
      601 lmlssehvep lmrelkshyq riiidvaavn qsqdvqlikr avdgvvfivk agvesaghia
      661 saldrieenn gvvigavlna veekdletqe glrslnfstd qlmttpgrv
//
LOCUS       WP_181549272             739 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Micromonospora noduli].
ACCESSION   WP_181549272
VERSION     WP_181549272.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora noduli
  ORGANISM  Micromonospora noduli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 739)
  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 739)
  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 739)
  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..739
                     /organism="Micromonospora noduli"
                     /db_xref="taxon:709876"
     Protein         1..739
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77197
     Region          <249..>366
                     /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 msaagsllaa vpaaavllli vaampreaga vaplrlavvr avlltgayav lvvevlgash
       61 altrgaftva wllflvaaaa atglrwrrat rlgqppaaap vpvsaapavs aasrpvpvga
      121 vvsgggpdvs apaaelgept saptraarrf adlravavda wrtarpgerl lagtvgglvl
      181 vellvallae pnnfdsqtyh lpkvehwvaq gdldfwptai hrqvtippga eylllhlrll
      241 tggdhlhnlv qwaagvvcll vaaritaqlg ggrraqllta fvlattpmvv lqatstqtdl
      301 icaawvacaa tvvldglsrr tgwgallglg aatgltavtk tsgliavgpl lvlwglaqlr
      361 larsrnaast dpaaagggrr swpvgglart vggsvlilvv aavvvgpfla rvtaefghpl
      421 gpprlresip merhdpasiv vnalrighta fdtplaplrr agaeviisga eaigvdpqdr
      481 aitfgrelfp epawypdedr vafplagala vigavmalar prriaperag slrayaavvl
      541 tavllhtami kwqpwgnrll lyavvlavpl aglwldallr nraggrrtva tvaavtvlat
      601 salagvlavs ygfprrlvgv gsvfttsdwd trflrrpqwa defrwaatav qdsgarrigl
      661 vqqndnweyp wwlllrqpdg gspdlvalqs vlperppanp ssvdaivctg nkaacaklvp
      721 agwrlefrgy vgyalppgr
//
LOCUS       WP_181549400             375 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Desulfosalsimonas propionicica].
ACCESSION   WP_181549400
VERSION     WP_181549400.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=41890
     Region          154..375
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mtqnpvteya pasrsdkdai drqrkllaey qgslrqlyea vceivlivna nrqivffnsf
       61 fpsmlnvddp etlyglrpge amgcmyacsn pggcgtsrfc tqcggvnsil salnqrddlq
      121 ecrllkdesm ealellvrtt plevqgqlfs ivaitdishe krrrvlervf fhdtlntaas
      181 irvfaqmlnd spdhenaqsf rqnllsgieq ladeissqke llaaesnele vkkqavdpaa
      241 larqtaetyq lrfpdhrivv rkpghtvtln tdsrllqrvl gnmllnalea sspeqtvtls
      301 triikdqvef qvhnptplsr enqlqlfqrs fstkgpgrgi gtysmkllte rylngwisvv
      361 sspengtifs atypl
//
LOCUS       WP_181549507             460 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181549507
VERSION     WP_181549507.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 460)
  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..460
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..460
                     /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=51019
     Region          53..336
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mrtrpialia sllacicfag cgksgpdpas fryqqdpqlf dtlsqpadyp aarfivltdp
       61 hyyhpglgts gpdfaryire drkmlalsde ileaaaseiq kqpadfilic gdmtkdgeri
      121 nhlqvaekis nlhptadiyv vpgnhdvrnp eavrythegs kgvetvepeg fseiygaygy
      181 ddaiardpas lsyvaepvdg lwlfaldscl wrenepgghp vvngrfseqt lewledmliq
      241 arknnksaia mmhhglvahy pgnekyygey vvdhseaiar llatygvrlv ftghfhaqdi
      301 tvkqfedfpn pifdietgsl vtwpcpwrei tisagqtcti esrftkaids ipegfagyar
      361 nfalegtvgl ardaleqyhv sekgmdllap qiaeaylahl agdehkpdtv isakgtgimg
      421 rvvvffqkdl vegwwtdlpp adnrliielk snswqqpdds
//
LOCUS       WP_181549553             279 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181549553
VERSION     WP_181549553.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..279
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31128
     Region          3..181
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mqnplvsvii pvynrqdfia davdsvlaqk yapfelivvd dgstddtari lsaykericv
       61 ihqenagvsa arnrgvraaa aewiafldsd dywlsgkltr qmawfaanpq mricqteeyw
      121 irkkkrvnpg rrhqkqqghi fkpclwlcli spsavmlhrs lfeqhggfne alpacedydl
      181 wlkitctepv glistplivk qgghadqlsa rpgldryria aichvmasgr lspgqyraaa
      241 aalaekcriy aqgcekrgkr kqaawyrnli qdpsagvss
//
LOCUS       WP_181549046             754 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Micromonospora saelicesensis].
ACCESSION   WP_181549046
VERSION     WP_181549046.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora saelicesensis
  ORGANISM  Micromonospora saelicesensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 754)
  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 754)
  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 754)
  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..754
                     /organism="Micromonospora saelicesensis"
                     /db_xref="taxon:285676"
     Protein         1..754
                     /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=83324
     Region          1..664
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mdvlseelrr eqkyfdvawd hrermrsnlg laagaaansg aanrikqdtq arldrigtae
       61 epvafgrmdd edgerfyigh haifdddsel lvmnwqapaa aryyeashad prrlrlkrtf
      121 dcsmnrivsf sdalfaqlad aveeleayee isdallsdle snrtgtmqei vrtiqasqfd
      181 liradadqlt iiqggpgtgk taialhrvsw llfnslgnlt addilmvgps ptftrytrlv
      241 lpslgdtsva qvdvhqlhpp vkrgrqddpa avklkgdgrm aglvrralyg rvgpaegqhw
      301 vevqvgnrtl slptedlkpl vgrsrastgt yserrqlfre lltelvssrv rldrgrlrla
      361 ldpamdrlwp sytpasflre lygsrdrlit asgdeftare vsvlhrrpae rlsdetwsds
      421 dlavldeldh lingvkssyl hivvdeaqdl spmqlraiar rsrngsmtvv gdiaqstghw
      481 arddwddlld hlpaelphal eelhfgyrvp rqvfdlaarl lpiaapdvea pqvvrdgpad
      541 ptihrveded erastavrva mdhashgrsv aiicpatgre dlerqltvrd vvwraasagd
      601 lgpgvnvvsp qeskglefda vvvlepddii aederghrll yvaltrttry ldivcvrlpa
      661 eltdsphder arpgsgaakp tssgqdmagd cgvsafagqk ttsdtqqsar pvsrrfvdlg
      721 aeevvallke tvapnlwqav ldragelldq esar
//
LOCUS       WP_181549558            1149 aa            linear   BCT 28-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181549558
VERSION     WP_181549558.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 1149)
  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..1149
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..1149
                     /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=126862
     Region          1..1144
                     /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 mndiadkhqr qraldpetaf ivqapagsgk tglliqrylk llcrvnhpee ilaitftrka
       61 aaemrnrvlg aidgaqsgtr pekeheavtw elardvcqrd adlnwkired psrmrimtid
      121 alcagltrqm pvlsgfgapg riaddptdly vraarntvae leaagpeaaa metlvrhldn
      181 rldlvenlva lmlprreqwm rhvadirdad glrkmleaam advikntleq irsrfpvfci
      241 mdladlcgfa aqnlehvdpe spvcvvrels glpgtdggdl plwegiahll ltkdgqwrkt
      301 vnkstgfpap ssvrdsgqka ffegkkrqfk nlvaaldtdp elagtldgvr rlpaagytdg
      361 qwrllqalfv ilkraaghla aifeqtgqvd fseiairaka algdaqeptd lalsldyris
      421 hilmdefqdt sisqfalmqq ltagwvpgdg rsffavgdpm qsiygfreae vglfltaweq
      481 gldahlplep llletnfrsr pgivrwvnaa fsqvlpeiad adsgavpymp ataaasggre
      541 eavfvhagly akenkddvnv reardvvccv qqaleqdsrg tvavlvrsrp hlqaivpelr
      601 aaglrfsave idalgnrpvi rdlvsltrai nhpadriawl svlrapwcgl tlldlhaiag
      661 ddfktpvpel ihdpdrvaal sndgrirler irpvlaaave rrarqslrqr vegawtamgg
      721 ravadpadlp dvdvyldyve aragaeplad mdafeqgvmk lfaqpdpgad trlqvmtihk
      781 akglefdtvv lpglhkaprs qdpalllwke ragvsfeksl lmapisgage ntdptyqyiq
      841 gleqqrtnhe sgrllyvaat rakkrlhifa aafldrqgnl mrpasrslla vlwpavsekf
      901 eqaaarkksp sadvpvkdre tshpciyrla anwrppappa disvkvrgvf pdlqipdvsg
      961 desflprfdw agmtvrhvgs vvhrwlkkic eqdpenwsaa kiaalrpalq kqlefegvgq
     1021 aeiskavtha etalcnaish eigrwilsah hrgaceygis gfygrelihs iidrtfvdes
     1081 gvrwiidykt gthsgggiea fldreqlryq aqmaryaalm rkmapgglvr iglyfpmipa
     1141 wrhwadlqe
//
LOCUS       WP_181548901             237 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter cloacae].
ACCESSION   WP_181548901
VERSION     WP_181548901.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter cloacae
  ORGANISM  Enterobacter cloacae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter cloacae"
                     /db_xref="taxon:550"
     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=27467
     Region          14..>199
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtlitqeneh drlatrlsii lsrlfqgerl higtlaeefg vttrtlrrdf nvrltyldie
       61 qsngvyqlas hyfrrrterd mkilarllhl drllpamdak llslmldger pspyrimlpe
      121 prqkptlfgd fsrltlailn qtqvrirtde nvshtvhpyr llcshaewfl agctssgvfv
      181 islsrirlve vlpdttfeid ntlislieqs dfmealpymn iihqimhygs kqtnnrn
//
LOCUS       WP_181549619             161 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181549619
VERSION     WP_181549619.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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 161)
  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 161)
  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 161)
  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..161
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..161
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18383
     Region          9..145
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mtqihtlcmm aliagffala vipagaeqtg nsgseinwys yedgmkkire sekkgylhfy
       61 tdwcsycrlm dektfsdadv agyinanfia mrvnaeqeqd laesyrvkqf plnwfinsna
      121 epignqpgyi ppeqmvqmlk yvqtdgyetm nfgefmekqd n
//
LOCUS       WP_181549785             505 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181549785
VERSION     WP_181549785.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 505)
  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 505)
  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..505
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..505
                     /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=56456
     Region          66..499
                     /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 mnttkskksa eegrdkgmen gvwmandldr llemileaga rmmrarassl lllekktgrl
       61 nfqvatgakk edikqfslrm gegiaghvas tgepllipdv srdrrwyryi sdqigfktrs
      121 iacvplkvgs rvigvvefin kgekgrfqes dlelinvfae laaiaienar kfklvelenr
      181 dlkqdlhlsh eivgkshair qvvsdalqva dsmastlilg esgtgkella rlihqasprk
      241 drplvalnca ampetlleae lfgyekgaft gatgtkigkf eladegtifl deiaemspam
      301 qakllrvlqd gifyrlggnt piavdirvia atnrkigkev qsgnfredly yrlnvvelqm
      361 pplrerksdi pllaahfvew frkekgylhl eisdaamekm igydwpgnvr elqnalerav
      421 vmgrgrkiep edlpmfasrg psaegidvgm tleeamhafk kkfirmnlkk tggnqtraak
      481 imgiqrtyls rlisrygikk drkhr
//
LOCUS       WP_181549991             392 aa            linear   BCT 28-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Desulfosalsimonas propionicica].
ACCESSION   WP_181549991
VERSION     WP_181549991.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=42971
     Region          10..385
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mtkrtsatyf mkeelgrrkq enhlrflvpv tpcdgvmvkr ngkslinfcs ndylglarhp
       61 llrqrskdfm drygagatas rlvcgtlpca eavegklarl kgaesslifn sgfqanlsll
      121 paladkksli lsdrlnhrsi iegarlcrca lavfrhndla hleeilhksr yldysrifiv
      181 tesifsmdgd isdvaqlvem argygsiliv deahatgvag argmgltagt avdccmgtfg
      241 kalgsfgayg tfskqmrdyl vnccsgfiys talppsvmga vdaaldlvpe mererkqlme
      301 kardlraelh rmgwdtgpsa thiipvivgs eaqtlalagr ledagilama irpptvekgr
      361 srirlaltal htdqhlnqli daldrwkrtk qk
//
LOCUS       WP_181550006             595 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550006
VERSION     WP_181550006.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 595)
  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 595)
  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..595
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..595
                     /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=65929
     Region          <11..>130
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
     Region          124..587
                     /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 mtanrkncsm ehlyavlnst hngiiavdnh giitlfnrga ekilgfstqe aldqkvdalf
       61 nvpsllttlr sgrpdvgrnv vingksiysn rspvyrdgkq vgavaifqdt tdieklsqel
      121 aaaknsveil etilettydg ivvvdkngii trfnkayqsf lgideknalg ravedvient
      181 rmhivvktgk peigetqkiq ghemvvmrip iykkgevvga vgkvlfrdvk eirsmvekld
      241 latkelkyyk gevmrlkgsr ynfkniagrc ekmlqaknla ktaasgssnv lirgesgtgk
      301 elfahaihdl slrrygafir vncaaipagl leselfgyeg gaftdakkgg kpgkfemaqg
      361 gtlfldeigd mpsemqakll rvlqekever lggeriirld irliaatnrd leelvrkeaf
      421 rqdlyyrlnv lkieipplre iredipllce rmlqevnedl gtavetidpg vieilkahdw
      481 pgnirelknv meravavntd rqqvvrkhhl piylldmdtg qnsgalqpdk napewltggt
      541 lseilaktek aaienalraa gnnrkkaaem lgihrsglyq kinrynigag nsgpd
//
LOCUS       WP_181549405             114 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181549405
VERSION     WP_181549405.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 114)
  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 114)
  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 114)
  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 114)
  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..114
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..114
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12579
     Region          11..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 mkiqdafnnr pvevtentfe sqivnspvpv lavfwapwct acravlpavd riasnltgri
       61 kvakihmeqn palasrfqvm nvpfmiifdn gaekdsmaga vpetdilkkl tpyy
//
LOCUS       WP_181549593             285 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Desulfosalsimonas propionicica].
ACCESSION   WP_181549593
VERSION     WP_181549593.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 285)
  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 285)
  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 285)
  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 285)
  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 285)
  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..285
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..285
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32877
     Region          1..245
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtkqlqekdq fsgakryvld pelarivnis rslemplllk gepgtgktml ayaiaeslhm
       61 plivlnvksn mklidglyqy dtltrlndsr fgdstrdvsr iedyikmgki gqaftaeert
      121 vllideidka dtdfqddmld vldqmefdii eidktirarh rpviiitsna kkdlsdpflg
      181 rcnfhhiafp dpkmmrkiih vhfpeidsdl mdhaintfyq lreidmvekk patrelinwi
      241 ralsadpdfk pkqlakgelp ylgvlfkksq dyqyaanqvq rkkrf
//
LOCUS       WP_181550216             228 aa            linear   BCT 28-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550216
VERSION     WP_181550216.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 228)
  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 228)
  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..228
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..228
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=25768
     Region          <19..143
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mnprsnmeqy lqptafmnfn hpavaafaqe ksggtsdpvr qavnlyyavr dsiyydpyai
       61 vltidglcas ttlaqkrgwc vakavllaac crhlgiparl gfadvknhls tkrlrermkt
      121 dvfywhgyts iyvndqwvka tpafnielcq kfslkplefd atadsiyhpf dlagnrhmey
      181 vnergefadv pldliiktfl ekypeagpaw lnadfdrdva retgaerk
//
LOCUS       WP_181550426             132 aa            linear   BCT 28-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181550426
VERSION     WP_181550426.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..132
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..132
                     /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=14778
     Region          29..132
                     /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 mkifkrifgi cetkspenpd cwrylserae lelskvpelk ergtairleg kglpnrvlvv
       61 hgsddefyaf enkcthfgrr ldplsgqqri qccslgkstf dyagtnvsgt akepiksfpv
      121 ekrngaliie lt
//
LOCUS       WP_181550724             256 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550724
VERSION     WP_181550724.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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
REFERENCE   6  (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 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26969
     Region          1..248
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 melkdkvavv tggasgigaa lcrcfaqnga ktvvaadidl egartvaeet ggmavscdvs
       61 heqdiidlve tveekcgpid lfcsnagili agalevpnqd wqriweinvm ahvyaaravm
      121 dkmmargvgw fvvtasaagl lsqigsapys vtkhaavgla enlaityadq gigvsaicpq
      181 avetkmtrqg ggvaavdgmi dadkvaaetl nalaeerflv lphpevatym erkaadydrw
      241 lkgmrrlqar fvqntg
//
LOCUS       WP_181550243             333 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550243
VERSION     WP_181550243.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 333)
  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..333
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..333
                     /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=35364
     Region          10..321
                     /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 mgqnricsll girypiiqap mnwvsgaalt aavseaggmg tigpnagank inpdveatge
       61 lvrkqigkvr eltnkpfavn vvvgfgedtk yskkivevlv eekvpaaivs vgrpdtytqt
      121 lknagikvlh aistarhaqk ardagvdavi cegfeagghk gftelttfvl tpmvadavdi
      181 pvvtgggigd grgilaalal gadgiymgsr fmatlesesh dkvkqaiaaa kdvctvsvsk
      241 efmlardlan kfteqfqemr ksgastqeli afleehgqyq sqhlglaeda eiccgqvagl
      301 ihdippaaql mekllsdiqk rfshleqqvn nff
//
LOCUS       WP_181550725             342 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550725
VERSION     WP_181550725.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..342
                     /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=36124
     Region          1..342
                     /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 mrvvkltrpr vlepaeepdp aadgqnvvin vsacgvcgsd lhywemgtgm dgapglimgh
       61 efsgtvadag prsdlapgdr vtyiplnpcn acptcekgwf hlcpraftrp vpgnnapgaf
      121 aekvagrpdm vrhlpdtvtd eaaclvepaa vafhavkqag irlgvrvlvi gggtigllsa
      181 awariagasq vglcernpkr lsyagtwpyv dqafdaedkk lkknlkkasn ggfdaviets
      241 aadagiatai sallpkgalv laginfshqs vstlmltske irlrgsmaye indfdtalgf
      301 madkrldvsq mincragfad lqnifenlht gdseivkavv rp
//
LOCUS       WP_181550784             584 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Desulfosalsimonas propionicica].
ACCESSION   WP_181550784
VERSION     WP_181550784.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 584)
  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 584)
  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 584)
  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 584)
  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..584
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..584
                     /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=63817
     Region          10..566
                     /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 mkksrqkeek pnqtpgrnrr ilmaglvlaa cyltiagkav ylqvfedtrl ksrasgeysg
       61 saefrekrgt iydvnlrela astrvvsiga hparienpkk aaseiarhld mdaaklagrl
      121 ntdrpfvwir rdaaperare lknqfgnsla lfdnysrvyp nktlgaqilg fvgvdgngle
      181 gleyyydrql tgavrestfi rdalgrifqq seaksgqgpg nnlvltidrn iqyiaeealk
      241 ktvlkfngds gmamvmdprt gavramahyp gfnpnaftrf prqtwrnrai tdafepgstl
      301 kvflaaaale sgrcspgtrv dcedgsytvg ghtlrdlhpn enltlaevik yssnigavki
      361 aerigpenly ktlsdfgfge ktgidcpgea egrlrhyrnw rpvdhatiaf gqglsvsavq
      421 llsgvsaian hgvlmkprmv eaitdanglv vksfepevrr rvvtettark vkdmmqsvtq
      481 pdgtgsqasp rgfrvcgktg taqilnsdgt yedsdynaif vgfapagspe lavlvmvkdp
      541 kvshyggvva apafaeivre sfnymniapa relldhtrae kega
//
LOCUS       WP_181550179             159 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550179
VERSION     WP_181550179.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 159)
  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 159)
  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 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   4  (residues 1 to 159)
  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..159
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..159
                     /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=18570
     Region          26..144
                     /region_name="HTH_GnyR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     regulatory protein GnyR; cd04776"
                     /db_xref="CDD:133403"
     Site            order(27..29,43,60..62)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133403"
     Site            order(73,76,80..81,90,111,115,121,125,128..129)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133403"
ORIGIN      
        1 mtkksapsds kqvpgpqtrq erknqylise laeefgitar siryyekqgl ispgrsngny
       61 riftrkdrar lrlilrgkrf gysleqirem igywnaepee sqqirkslny gdkklaelrt
      121 rikelqqlen dllsvkqkll trleslensq hkkqkgetk
//
LOCUS       WP_181550104             465 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550104
VERSION     WP_181550104.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=52221
     Region          3..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 mtekatlliv ddelsmrefl eimlgaegyg vdtaesgrra kamvdenayd lvlcdirlgd
       61 isglevlrra kadnpdtvvi misayataen aveamnegay dylpkpfdnd elkqtvakal
      121 elktlsdekk llddelqqsm hfgllvgnsp rmmhiyevie qiaptrtnvm itgesgtgke
      181 liaraihnqs srsdrpfvvi ncgsipeslm eseffgykkg aftgasqdkk glfeaahtgt
      241 ifldevgels lpmqvrllrv vqersfkpvg snddlcvdir ivsatnkqve eeviagrfre
      301 dlyyrlnvve ikvpplrerk gdlralaqhf lekyardagk emtkissyav dllhkydfpg
      361 nirelenlie rsvalsstni llpdnlslsi hkrrwiegie nrrfdldevp kgvfldsile
      421 qierayleka lsctsgnkhk aaellgitfr sfryrcsklg iekpe
//
LOCUS       WP_181550904             159 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Desulfosalsimonas propionicica].
ACCESSION   WP_181550904
VERSION     WP_181550904.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 159)
  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..159
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..159
                     /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=18292
     Region          28..148
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrpkpfhpev yngdprfvkn rhdgciwhrc enrtlyadtd rsavvyhany lryfefgras
       61 lmrdlaypyv dieasgyvyp iielgikyhs plyyddamwv htrpgnlgkv klnfdyvith
      121 aqtggivctg ftehcalnsa grpvgident qnlwdifpk
//
LOCUS       WP_181549965             477 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181549965
VERSION     WP_181549965.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 477)
  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 477)
  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 477)
  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 477)
  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..477
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..477
                     /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=52579
     Region          1..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 maeilivddd vqlrqsfarl lgeegydvrm assgeagiqa vedhlpdlvv mdvrmpgidg
       61 ietlqriqai daklpvvimt afgttetaie atkqgafdyv lkpfdvgdml kiieqavsag
      121 rmmhqqvqmg agpetggada iigqspsmqk vykaigrvap tdatvlirge sgtgkelvar
      181 aiyqhsqrag kpflvincva ipetllesel fgyergaftg aasrrvgkfe qahggtvfld
      241 eigdmpmsiq akilrllqer sverlggqrp idvdvriiaa tnrdlerale derfredlyy
      301 rlkvvtikmp plkerkedip llidyflsrf sremqinnpg isdearqgve qhfwpgnvre
      361 lgntikkali fsrgypiqag niyqaiages rddndgggtd letagrnwir amlaseenpd
      421 mfnflmdqfg rmvvgealnl tggnrsraar llgmsrptlq ariekynlsl etsvkss
//
LOCUS       WP_181550939             468 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550939
VERSION     WP_181550939.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=52419
     Region          8..108
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cd00156"
                     /db_xref="CDD:381085"
     Region          59..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"
     Site            order(101..104,106)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381085"
ORIGIN      
        1 mlknisvlvv epgdnaasev agffneqtea nifqaknste alefinnkrs vellvtdlff
       61 pdksgleliq kgiainpamv pivvmppggr qhvveslqag ayfyihtpiy qqeilevvkn
      121 aleyqkllaq slqhkprlrk sdgfagiige srpmkklfei ieriagnseg nvllkgesgt
      181 gkelvaraih dltpernqyn fvplncaaip eelleselfg yekgaftgan rakkgrlaha
      241 dkgtlfldei gdmkanlqak llrvlqeqnf eavgsvkstq idvrviaatn rnlekavadg
      301 tfredlyyrl svvpitlppl rkrtediphl vqkfllmynr grknvplgft dqalqrlkay
      361 ewpgnvrelq nlvqrmcilh ggdtvdvgsl pqrfqdlcdp agnsetekqn nisedldfha
      421 mtqefenqli lkalhmaegn kkeaarllnm krttllekik krhlevki
//
LOCUS       WP_181550983             305 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550983
VERSION     WP_181550983.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=33985
     Region          1..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(25,242,245)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(175,212,240,243..244,247)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 milvigeilv difpqyrrig gapfnfsyhl qqmglpvcfi srigqdpigk eisdflwqnk
       61 fdaghiqsds rhptgkvmvh pqqggshnfe iitntaydhi qlpespedak nqspkliyfg
      121 tlvqrtpkma armqqfldnr gdwskcfcdv nlrpgcysse tvlasiarad ilkindeelk
      181 qvremtgrha eseddfidwl mkthdiemvs ltmgeqgsrl ytpgfchetr vpdkgpvvdt
      241 vgagdayaav valgylknws pdhileqaaa faaricqiqg aipenrdfyl pllqrttggl
      301 ndgtg
//
LOCUS       WP_181551108             668 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Desulfosalsimonas propionicica].
ACCESSION   WP_181551108
VERSION     WP_181551108.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 668)
  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 668)
  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 668)
  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 668)
  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 668)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 668)
  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..668
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..668
                     /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=75987
     Region          183..668
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          438..667
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mptnktyssv gksfislala lfsafcllas wvflgplqsn ieqnvsksve kyvhtlrlyg
       61 hnnlqslvnv iedharlphi vhsvmrthvp mwklqhqllt mklmgrdvny tlldyqgnpi
      121 asetdtsadf sgqtpwvrsi ldgrrttwid agyhdtqpfw riavpirynq yvegvlvaec
      181 pveslldiii sddvlhphvg ielvrgttvl eekgvipsdy tmfqsslshs giqwnllwdh
      241 dairkkmtmi yirwlfffcl talvivfffy lygskkivyp qealnrinqq lfaqkkeieg
      301 qyqqlkaaql dlekknrela aeknqmeaii hsvqdgiitt dahgtiqtin paarklygla
      361 eskllgktla inagfselkd alekmilekt ayrnlefflk nkktdrqhyl raslarvstg
      421 amaekeeyle fvvvlidltr ekelehmkta fintaahelr tpltsiqgfs ellvirktvp
      481 pekihfyakk ihsqtkvlsa ivsrledvst iesgrtisif ptlrdlpdli rktidlagts
      541 ygserlemqc qpcdpfyfdi nrirqviwdl ianaliysst narvrvegwm diaryfvvir
      601 degmgidtaf aarvfdgflr adtssrapgg fglsiylakh iidahhgqif mesepgrgte
      661 fticlprn
//
LOCUS       WP_181550809             314 aa            linear   BCT 28-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Desulfosalsimonas propionicica].
ACCESSION   WP_181550809
VERSION     WP_181550809.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 314)
  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 314)
  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..314
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..314
                     /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=33756
     Region          3..314
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 menngyiifs glsnpqlaes vcsylnqplg nakvkrfsdg evqieiddnv rakdvfvmqs
       61 tcspvndhlv ellmmidafk rssarritav ipyfgyarqd kkvaprvpis aklvadlltr
      121 aganrvitmd lhagqiqgff dipvdnlfaa pvlinhmrrq fsddlvivsp daggverara
      181 fakrlnagla iidkrrsapn qskamavign vegkkaiild dmadtagtlt eaanaitang
      241 akevhaccth avlsgpaidr inesslksmv vtdtiplsgk pktcdkitvl siaelfgeai
      301 yrshtgdsvt slfv
//
LOCUS       WP_181550903             421 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Desulfosalsimonas propionicica].
ACCESSION   WP_181550903
VERSION     WP_181550903.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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..421
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..421
                     /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=43653
     Region          7..419
                     /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 mkaplnrrvf vigyaaatpl grtfdrtwnn aaaglagfgq vtrcsvqsls rvvgeipdwd
       61 paacdfvdpk eahnwnadfv iltmdvcraa ladsgleind qtapktacmv gsalngtdaf
      121 rkaaetlrvk galrvspyll pnlcanlpag kagmmlgftg pvfspqgaca sgnfaiglga
      181 rmirdgdcdf vlaggvdtci mpeiihgfan mnatikvgkn dracndpsla srpfsvdrkg
      241 mvlsegcgvl vlaaeeaita hglvpraeva gvgwssdach ftlpsgptiv raisaaidda
      301 glapadigyv nahgtstrkg dfteiqclra vfgnyleslp vssnksqigh tlgasaaiea
      361 algiegmcrg vilptinhip dpelgdidvv pdsaraggye cflsnafgfg gtnccivfkg
      421 v
//
LOCUS       WP_181551117             505 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181551117
VERSION     WP_181551117.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 505)
  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..505
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..505
                     /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=54894
     Region          230..494
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 melaphntgq hyrdrglfls gagdrtdlag enggekfifr almgvlvftq lafggvhawa
       61 yclmellvft lsgvavllwl argvnwpgdt kafdirllnp allwlglfll itglqilpmp
      121 fwlvelispr afdlkiaaak atgadppgwm qlslipfetr lalirilsyf cmfalmawlt
      181 rhraqmlqai gvlagmgvfq viygaaqays hthriwwyav skhsslingt yinfnhlagf
      241 lamvcplcvg mvfaywpgrp glpkirpfkp dvikkwlvtg inrnlricfa glaallgfgl
      301 istgsrggiv afaagslfmi smfmarprfr gfgqvafill lvilacscfi gikpalekfq
      361 ktglhssrld ytlsaasmir dypvsgtgmg tfgeayhsyp vahhaggmal ihlhndwmel
      421 gvetgliglg aaaigfvtli fqyirawmgr gnhfsiglgg gaiagmlaig lhsfgefalr
      481 mpanaltlvt vaavgwnalc qdksf
//
LOCUS       WP_181551175             409 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Desulfosalsimonas propionicica].
ACCESSION   WP_181551175
VERSION     WP_181551175.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..409
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..409
                     /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=46972
     Region          118..389
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mvdflkamyv rflgktpiaf kivftdgtcy ahgtgppafv iryktktaqf nsmlffgwgl
       61 iesyinggvd iegdlkalir atadnepsla qtarqtrifh plirmrnlwh emlfgnrkss
      121 qgvknalahy nrgsdifwqy ldptmtytca ywkegtrslr qaqenkldhv crklrlkkge
      181 hlidvgggwg sllfhavkny gvigtnlspt tdqnrwlvdk arqegiadki rvqesdfrqv
      241 sgtydkyasl gvyehagkgq lkdwirsmaq clkpggigll hfiahdrpmd tdffirkhif
      301 pggylpglte tidlmavhgl eildienlrr hyaltldqwa arfdenwami nsynpklfde
      361 rfrrtwrayl hscaaffrtp nsvlrlyqit fckgnttdyp mdrgfiyns
//
LOCUS       WP_181550714             306 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181550714
VERSION     WP_181550714.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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 306)
  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 306)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 306)
  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 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   7  (residues 1 to 306)
  AUTHORS   Rosinski,J.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..306
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..306
                     /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=33973
     Site            order(7..8,10,13,16..17,20..21,24,54,74..75,77..79,81..83)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Region          7..69
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(8..9,13..15,28..30,39..42,44..45,48..49,51..52,
                     58..60,65..67)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(28,31,74)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
     Region          114..281
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mnniiyfkal sdetrirlin illhhelkvg elvsilemgq srisrhlkil adagmakclk
       61 egvwgiysit gsgpgrdfie avrylfeqdp vlradlkrae qiiearsagt lrffdhiags
      121 wdllkreilg tfdinraife ntnahgtgvd lgcgtgelle amkahagrvi gvdssprmle
      181 earkrfsdan gqkvdirlge iehlplgdne adlavislvl qyladpaaaf gevarilkpg
      241 gelilaefer hqqhslktvy gvkwlgfprk sietwlekng fvlqqvrphn lskglslnif
      301 qavmnt
//
LOCUS       WP_181550919             412 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Desulfosalsimonas propionicica].
ACCESSION   WP_181550919
VERSION     WP_181550919.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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..412
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..412
                     /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=44111
     Region          3..409
                     /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 mdrrvvitaa saitpignsk qkvvhslqng isgvqplrrd dlladylhcr vfgtvqepie
       61 ygferkyrkt mgpvsyyach vvgqlleqsg lsrefvssgr mgvafgsthg spsvqrhiyk
      121 alyhkenshs gslgavdylk smvhttavni tkmfeitgrv icsstactts sqsigygyem
      181 vkygmqdamv cggadeydtt tvavfdnlla cstayndrpg qtprpfdtdr dglvvaegag
      241 avlleeyeaa rkrgapilge vigfscnnng gdlifpnleg itrtiqlgle sagigpeamd
      301 fisahatgtk mgdviearai eqvygnspmv tglkgytght mascgvieti mtlymmekgf
      361 vaptlhleni dsrcsgighv tqltdkvidi asvqnfafgg vntslvlkap al
//
LOCUS       WP_181551376             288 aa            linear   BCT 28-DEC-2024
DEFINITION  damage-control phosphatase ARMT1 family protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181551376
VERSION     WP_181551376.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 288)
  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 288)
  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..288
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..288
                     /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=31144
     Region          2..276
                     /region_name="DUF89"
                     /note="House-cleaning carbohydrate phosphatase, DUF89
                     family [Defense mechanisms]; COG1578"
                     /db_xref="CDD:441186"
ORIGIN      
        1 mktyfacmpc flnqalracr fmglddqktr qvinavakli pqipmesspp etgravyqii
       61 reisgnadpy qqvkaentan alalypvmkq maaaaanpla aavriaaagn vidcgvnasy
      121 aiekevdqml enefavfdmd aflaqlekte rilyigdnag ecvfdrvlie qlprpvtyvv
      181 rqapiindat medalaagid rvadivssgt dapgtvlstc tsdfldllkq pwlkiskgqg
      241 nyealsagpy pvffllkakc sviardldvd egqmifasss ppdfsras
//
LOCUS       WP_181551412             201 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181551412
VERSION     WP_181551412.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 201)
  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..201
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..201
                     /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=22970
     Region          1..200
                     /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 malinpkkre vqvkivyygp grggkttnle yinrkfkkri lnemvtvkty gdrtlffdfl
       61 pfdigeikgh sikiqlytvp gqvkynatrr lvlrgvdgiv fvadsmdlrr emnirslqnl
      121 kenletfnkn ifniplvmqy nkrdladegi pilseetlqk dlnsrlnapy fqasairgdn
      181 vaatmkkiia ltvsslrkkl q
//
LOCUS       WP_181551335             161 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181551335
VERSION     WP_181551335.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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..161
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..161
                     /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=19373
     Region          <11..105
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mactpkfhqw fpdsryihit rdpraiyasm klmdirtces lprwrqcvla akrltylvhq
       61 yhwaarvham mahnekyhlf rfedtiqape dqmkklcnfl avpfdkrmll prmedssfrk
      121 reitygfdvc tlerwrnvis pytdriirkl lgremrllgy g
//
LOCUS       WP_181551021             187 aa            linear   BCT 28-DEC-2024
DEFINITION  D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
            [Desulfosalsimonas propionicica].
ACCESSION   WP_181551021
VERSION     WP_181551021.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 187)
  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 187)
  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 187)
  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 187)
  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..187
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..187
                     /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=20324
     Region          8..181
                     /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 mviennikrp avfldrdgti iedrghlsrp sqvifftetv salrrlnelf dlfivtnqsg
       61 vakglltmdd vgcvnghvvs ylaecgirit diyvcphdss dncecikpkp yflkkaekeh
      121 gidlsrsfai gdhphdvafa enagahgiyv ltghgmkhrh elskealiaa gieaaadiic
      181 rsaaagr
//
LOCUS       WP_181551384             596 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Desulfosalsimonas propionicica].
ACCESSION   WP_181551384
VERSION     WP_181551384.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 596)
  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 596)
  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..596
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..596
                     /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=66660
     Region          2..596
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtasttpavf kqtvsdrgqm vamrfkklgl whdiswdqyf daarnisaal idmglekgss
       61 aaiigdncpe wvmidmgiqc aggvsvgiyt tnawqevqyv vsnsdsvflf veneeqldkw
      121 lsfrdtvpdl kkvivwdtkg lrefsdpmvm gydelvargq alsktgvdqr sesltprdlc
      181 vliytsgttg ppkgamlthg nvtwmadaiv eqnpmdrqde vlsflplchi ferlfsvfth
      241 lrhayvvnfv ekpdtvtdnm ievsptvgya vpriwekyys aiqirmsdat rakqlayaaa
      301 lkigqkraer imhfqkvpsw ltlafglahf avfrklrerl gfdrirvays gaapisarvl
      361 ffyqsiginl vegygqtegt gvtctsregr akfgtvgtpv pgteiniaed geilvkspgv
      421 fagyykneta taetlkdgwl ysgdvgeidk dgylkitdrk kdiiitaggk nispqyienm
      481 lkasiyinda vligdrrkfl salimidedn vvkyaqenki qfstygdlaa hpeinkliqs
      541 eidqvnkgla rvenvrkfri lpkklyeedg evtptmkvkr kyvnqafagi ieemyk
//
LOCUS       WP_181551292             368 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181551292
VERSION     WP_181551292.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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 368)
  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 368)
  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 368)
  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 368)
  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..368
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..368
                     /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=41515
     Region          91..359
                     /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 midnhtkqkq tlrmrrhama fatylvpmsl vvlcwsqgll pekviyhfaa fvfvinftil
       61 flirkninlk frdpsltalh itvsclpaly vmyflehgha raifmlvlll aiiygileld
      121 trgflmaclw ilslyvllif vlwtkkpeal naslewiqii afalvlfsms viggyisslr
      181 eklrlrnqel ssaiekidkl vnidpltevs nrrrlfevlt qetnrcsrga tpfsiclldi
      241 dhfkqvndiy ghmagdeilc hiacsisrdi rnidafgryg geefllvlpr tpiagaavka
      301 ekmrsqvagl rfpdisgelg vtisigvaly rptedidttl lradralyaa kangrnrvet
      361 eknhtava
//
LOCUS       WP_181551234             462 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181551234
VERSION     WP_181551234.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 462)
  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 462)
  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 462)
  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 462)
  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..462
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..462
                     /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=49635
     Region          17..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 mksydvvvvg sgtggqtaah nlsqygvsva vvensstpgg vcalagcqak kwyyeaaetm
       61 arardlsgkg vtappemdwk tvrdqkraft gavpdstrkg ldaagidfip gtaafrdpet
      121 ltvdgqplks kfivlatgar paplpfegaq ylvsssqfle ldglppriaf vgggfisfef
      181 ahfaarlgpa qqihileagp rplgpfdgem aahlmdasra egidihidte itgieknnqg
      241 yvvktpgked lyadmvvhga grapaitnle lekgsvdfsr hgivvdekmr tanarvfaag
      301 dcadtvqlar vadyeacvaa knilaelrgg qeavmdyrav psvlftlpqy amvgateeal
      361 qsegirysra matnlswpty rrtgmkhaay kvlvdhnnri agahiisdna aglinifkqa
      421 mihhqdagql ywehvmtpyp tresdityml kpfvkhdpla gl
//
LOCUS       WP_181551666             247 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181551666
VERSION     WP_181551666.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..247
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..247
                     /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=27697
     Region          124..239
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 maksenhtia kavalispvl sagsllwfav flyagsfsvl dlglgfywal llnaglslaf
       61 flqhsimvrk wfqdrarkyi qepyhgilfs lssaaalliv ltawqksscl lfsaegvgrl
      121 afrmvfaasv agfawggral rsvdgfgnhw lllgagnpqp etdglatrgp ykfvrhplyf
      181 ftllmiwscp ditadrlifn vlwsgwivig awleekdlvr dlgrpyreyq ktvpmlipwk
      241 iwkgkyq
//
LOCUS       WP_181551651             221 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181551651
VERSION     WP_181551651.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 221)
  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 221)
  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..221
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..221
                     /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=24788
     Region          1..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 mtqlllrpni elepkalaig grrleilcvk nleplisele aegrqeiahf pfwvkiweas
       61 ivltdwlvht gldnnqeile igagmgitgl flgafghrvt ltdnhadala lmeknaahnk
      121 ietvrvsdld whkpntdetw diicgseliy rksdvdpvie ilkkklksgg kaylahdiar
      181 msmmeflmea ekefdlshkg maftgmgekk qivihtlkhk a
//
LOCUS       WP_181551497             582 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Desulfosalsimonas propionicica].
ACCESSION   WP_181551497
VERSION     WP_181551497.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..582
                     /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=64078
     Region          28..573
                     /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(212,215..220,222..223)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(215,348..349,370..375,460,472,475,486,566)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(215,268..269,321,323..324,327,348..349,370..375,460,
                     472,475,483..486,547)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(268,323..324,327,348,483..485,541,547)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mvatswptdr wpegvaadvd tseyekplfn videaardyp nqvytifndg trtyaqvkdt
       61 adrianflas agirkgdrva iflpnlpqyp aifhgilkag gvcvtcnply taselnyqln
      121 dsgarmvfcm dhpqfyptam eavkntsven vvycniksyl pkvkailgsl lkkipqaesh
      181 dpshhsfddi vaaarpeppq vsidpaedla liiytggttg kpkgaalthv nfyydlkale
      241 ewgrlvhekg gkpeklrkgg fhtylgvlpw yhsfgltvcm lsaagsgskm icvpdpragn
      301 ppfsevlkav qkykatvmpa vptifvaftn hpdidkydlt slmgcfsgga plppevckqf
      361 eaktgavife gyglsetapv vssnptdrda rkigtiglpl pgtdikivdl eigqselpqg
      421 edgelavsgp qvmqgywnrp eenqavfrql ngrryfltgd iahidengfi vitdrkkdmi
      481 lvggfnvypr diedilyqhp kvqlvavvgv pddksgeavk afiqvkpgeq vseqeirdfc
      541 kqnmagykrp kfidfrddip vspvgkvlrr vlrdeemdqk se
//
LOCUS       WP_181551623             973 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Desulfosalsimonas propionicica].
ACCESSION   WP_181551623
VERSION     WP_181551623.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 973)
  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..973
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..973
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=109451
     Region          54..490
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          547..963
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkktmkpawk illfsllaam ltaagcrglp sgpgqpenqq nhtghwaheq snlspdpeli
       61 fgkldngfsy vlmenqkpeg rvkmhlnada gsfhespeer giahflehml fagtrnfpsg
      121 elvkyfqrig mkfgpdvngr tgfynttydl dlprgdkkdi degllvmrdf aseallepge
      181 iekersvila ekrtrdtpdy rtfketfrfe lpetriagrm pigtrqtien idrqmletfy
      241 htwyrpgrlt lvavgdfdpg imenliekrf sglaakapek pepefdhfdh dglktfyhhe
      301 peagrtnvai etltrtpqpa dsreyqqkql lsemadsivg hrldrlrneq dapftradiy
      361 sghylkfvka aeisakcdpe nweeslslie qtlrralehg fteaevnrak kefandlqqa
      421 vknaptreng qiagqllhhl nakrvfqspt qrrnllqpvi esatpeklhe mfknqwapsh
      481 rlvlvtgnad laqeaetgkk kiaaayrqsr qtevqgpdak dalafpylpa psgspviedr
      541 tkmdetgvtr vrfenkvtll vketdftanq vlaavsfghg qssepqnmpa lsemtdrvin
      601 sgglgklsdd elsrvlagtt trvsfdveed kfvfsarsvp netelmfqll yhyiqdpgyr
      661 qtalrrsarq ltqkyrslsh svqgamaikg qkflaggdgr fgfpgpeais rvrindirnw
      721 itpalsqgpl eiavvgdide davidaagnf fgalpqrrdf resepvnvpd fpknreieis
      781 vptriskgll vrayptthiw dihqarrlsv ladifsdrmr irirenlgas yaqgashsps
      841 raytdygllt gyavidpdki navekamadi gaelqangat kdelkralep tftqireqvk
      901 tneywlhtvl kgagrhpeql qwsrtlledy tcitveeinq tarkwlkpah aadirilpep
      961 gdadngppep edq
//
LOCUS       WP_181552018             451 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181552018
VERSION     WP_181552018.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 451)
  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..451
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..451
                     /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..442
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mnvcivgtgy vglvtaacla etgnhvfcvd indgiiqrlk tgdvhifepg leelvqrnla
       61 eerlvfttsl kdamasatli fscvgtpsme dgscdlsavy rvagqvgdnm edhkivvnks
      121 tvpvgtaarv reiiserlaa rgvsldfdvv snpeflkegd avsdfmkpdr iiigtdnpev
      181 aqlmenlyep yarsrdklil mspksaemtk yaancmlaak isfineiani cekvgadvrd
      241 vragigsdhr igyhfiypgv gyggscfpkd vralihtaad lgyvpevlsa vdnvnnrqrq
      301 mvarkvqsff esaggvsgrv lavwglsfka ntddirhspa idivnelsra gmqirafdpg
      361 agqnakqmfa gndnvsvgdk qyeildgaha lavltdwhqf rtpdfpgiek rlkqpvifda
      421 rnlystdliv rhnftcirtg rpdiiagpai d
//
LOCUS       WP_181552093             238 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181552093
VERSION     WP_181552093.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..238
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..238
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26038
     Region          9..234
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mqetlffead glrlhgtlhl pqtpkppfii gvhgmlsngd spkqqdlarq cnrmgiayfr
       61 fdhrgcgrsd gvfaevttfe grcrdlaaam ailgrrpdlg rsaglfgssl ggavvlhaar
      121 etdfdavvtl aapirfsaih ipedyqtdpd lakirreqlt ydltenlanv hhllvchgda
      181 dpvvpyenal qihdaagkpk kllclpggdh plgqpehqqt fmentlewfg rhlgskts
//
LOCUS       WP_181552235             211 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181552235
VERSION     WP_181552235.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 211)
  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 211)
  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..211
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..211
                     /product="LolA family protein"
                     /calculated_mol_wt=23815
     Region          8..208
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 magivfarri fsrfglfaal mcavpfftgw adtmeeigdq aagiravkar fvqekhleml
       61 dnpliskgel yfrapdslrw eytdpvksil lmnrdrirqy amgedgmaar qgrdleamrv
      121 fleqvgqwlr ggfdkntafa aelkkgqrvv ltpvdknisg viekielqlt dtpgviesaf
      181 iyedetsytr ivfhdtrinp kiadsvfeqa p
//
LOCUS       WP_181552165             459 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181552165
VERSION     WP_181552165.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=50393
     Region          16..446
                     /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 mdtettrqis pesaaailds isdgvftide swrisefnra aeeitgisrq eaigkpcyev
       61 frasmcevdc amkrtlktge peinrsgfiv daegtripvs vstallrdsa gkiiggaetf
      121 rdlslvealr kelsgryqlg dmvsrspdmq qifelaaqva aststvllrg etgtgkella
      181 ravhglsprn kgpfmavncg alpdtllese lfgykagaft ganqdkpgrf araqggtlfl
      241 deigdispal qvrllrvlqe kqveplggta pidvdvrvia athrdlekmv eagefrqdlf
      301 yrinvikidi pplrkrkedi pllvdhfigr fnhiqakavk gvtgeamgll mthdypgnvr
      361 elenriehaf vlcengwiep rhlpegcggi kssgstaanf qdavnafeaq lireamreng
      421 ynrlktarnl gihkttlfrk mkslgiafpe ydgrnrmae
//
LOCUS       WP_181552080             455 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181552080
VERSION     WP_181552080.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 455)
  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 455)
  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..455
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..455
                     /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=50913
     Region          8..447
                     /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 msddtltrll sekqnliril dhlkegiiah dlkrrifffn eeaerltgys rnevlgkdch
       61 eafgqpfcgq kclfdenqpe nhqdlpeyme ypvtiltkdg qsrkaemsvs pirddtgviv
      121 gvlasvsdlt ellklrfkag elsgfgsiig rdykmlqifq qirdlaaydy pvhisgetgt
      181 gkelvaeaih hesrragasf vpincgalpe glieselfgh vkgafsgair dkkgrfelah
      241 ngtvfldeia elsnamqvkl lrflqtgkfe kvggektvsv dvriisatnk dlkkqiqaga
      301 fredlyyrln vipvhlpplr errndiplli ehflrnaare hgdeppkvvs eealgimldy
      361 dwpgnvrqlq nvlqfaivks ggsvirpsnl plelrsakss ekrrgpdkkl dvdsvraale
      421 ktggnkvkaa kqlevgratl yrfirdypea vpene
//
LOCUS       WP_181551788             612 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Desulfosalsimonas propionicica].
ACCESSION   WP_181551788
VERSION     WP_181551788.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=69246
     Region          15..577
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mgysqlrwlr sgiglllvcm lsagqavage dviqagnvvv tatktdhlie dvpvktevit
       61 rreiedrklk tlqealehlp glrvdmdsgs wgdkgkvsir gmesrhvlil vdghriyggh
      121 dasvdlqsyp temierievv kgpgsalygs eamggvinvi trkaedgkdf sasaaagsrn
      181 rrimeatgsw ksngmgsvls ytskhsdgvd pdydqykeha iqgtlrydls praeislkpy
      241 fsehrmdyed riqqrvgvnp swqwkpdnls tlrlwgswfr ydhessdeqt getateyahd
      301 myeteinysr lfsgrhlltl gsqfereerd dkikeyeaee dvlsffvsde idfnplvlvl
      361 gvrvdehdew gsevtpkfsi ayrvsdavkl rssvgrgvna ptlsklygqw rmgpyavqpn
      421 pdlepeeswg ydmgadwnpt knislsatlf qnevdnlivs rsirqgappw dlvwenveka
      481 rirgvevsta ivitddltad faytyldten ldtgmelger pmhqvsmrlg yfwrqygisa
      541 flegqyrgrr yadedneerl deyavfdivl nkdfgdhyqg fvrvdnilnk kdvtdaydvd
      601 gteflagvqm nf
//
LOCUS       WP_181551842             114 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181551842
VERSION     WP_181551842.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=12509
     Region          2..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mptaenaari fkvlsvdtrv rmidllktrt lcvnamaksl nispaavsqh lrilrdadiv
       61 igekrgyfvh yrvneetlak whktanhlld pspakpfiia gslknsnsdk ggqs
//
LOCUS       WP_181552248             251 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181552248
VERSION     WP_181552248.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=28588
     Region          45..245
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mknrliaiaw fsfvgitsvi fflaalvikv atvafdrrlv ilqqftcfwg alytwiipaw
       61 kiriegrqhi dskkarvvvs nhqslldilv lfnlfchfkf vskseifkvp ligwnmrfnr
      121 yielkrgdkr siarmmkdck kaldegssvl ifpegtrspd gnirnfkpga filatehqap
      181 iqpivisgtn kalpkhsinf hgkcdirvrv mpeiayeefa glspeetaqm vrekiiheld
      241 diekqqtadg s
//
LOCUS       WP_181552247              79 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181552247
VERSION     WP_181552247.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..79
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8667
     Region          5..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(9,13,38)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(12,37)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     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 mavfadelkr lrqakqvsta eaaravgipq sryselergv rvagegqier lekyyevdag
       61 tlaalmqkqw delmqavaa
//
LOCUS       WP_181552231             421 aa            linear   BCT 28-DEC-2024
DEFINITION  B12-binding domain-containing radical SAM protein
            [Desulfosalsimonas propionicica].
ACCESSION   WP_181552231
VERSION     WP_181552231.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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 421)
  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..421
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..421
                     /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=48666
     Region          1..364
                     /region_name="YgiQ"
                     /note="Radical SAM superfamily enzyme YgiQ, UPF0313 family
                     [General function prediction only]; COG1032"
                     /db_xref="CDD:440655"
ORIGIN      
        1 mkfkliypkw aklarqtefh lpphgpvvfa aslpddvevt fvdenlqdid fdesvdmvgi
       61 smmltiqvkr gwqiadhyrk kgicvifggi aatlhaeeta qradavflge aegkmdqvfd
      121 dfrnnrlqkf ynaleappai envgparrdi lnkslynyrg iqmvdlvhas rgcrfncypc
      181 avaylggrrf rprpvdrtig eiagidnnrl flvdnslaqd tqwekdlfae miplkknwcs
      241 hpieddpavl dlaaqagawf vyqavfdtsd yirerirryh dhgiavegti llgldrhted
      301 fikelvdfll eieldlaeft vltpfphtra wdrlhgenri fsydwddyta dkvvyhpkqm
      361 saerlqellf yawdtfyagk pqqmrmfelf qkvmrkekas gtfqprdrnl idqafgrpvk
      421 r
//
LOCUS       WP_181552253             109 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Desulfosalsimonas propionicica].
ACCESSION   WP_181552253
VERSION     WP_181552253.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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 10601782
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=12309
     Region          28..>67
                     /region_name="Cytochrome_CBB3"
                     /note="Cytochrome C oxidase, cbb3-type, subunit III;
                     pfam13442"
                     /db_xref="CDD:463879"
ORIGIN      
        1 mfrkllclfl tagfvvalag taaafeqgne rkgkymfrkn crschtegas aeplnpvskt
       61 qaqwerafqr yerfecadqw edlaesdknd iltylynhaf dspspatce
//
LOCUS       WP_181552246             141 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Desulfosalsimonas propionicica].
ACCESSION   WP_181552246
VERSION     WP_181552246.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 141)
  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..141
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..141
                     /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=16522
     Region          6..138
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mksentdric evkftvpfhd ldpmevvwhg nyfkyfditr dalfrklgvd lyrvytdtqh
       61 ifpiirtsik hvfplrfrde fvcrakltav dykigvdfii rltednrvia kgksqqaavk
      121 ipemetlfki pdpirhalgf e
//
LOCUS       WP_181552377             452 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Desulfosalsimonas propionicica].
ACCESSION   WP_181552377
VERSION     WP_181552377.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 452)
  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 452)
  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..452
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..452
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=50952
     Region          3..450
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 midrliqfaa acraadlrvs taelidchqh lqcvdlvdea rfktvlranf aksrrdqaaf
       61 drvydlffhg lgasededvq hmdakaaael lsqagmgddd ldaalfdfvt gdpasflqvl
      121 qdldqqadap sasgvksnlg qlagrmqvml rinaiqrgla rlpdgtsqap aaasasrrln
      181 qarglltrqn qpyndglrqv rshhkhyqgl geqffssltp aeieqmrdvi qqlvrklkdr
      241 mgrrfaasrr ggldvrktlr ragrfqgvpl elsyrrrplr ktrivalcdv sgsvwsaarf
      301 mlhllyslqd cfssvhsfaf vsgttdisei fahnevnral ekvlsspdig fdaltdygev
      361 fyefrqlhmh rinrkttvii vgdgrsnyqh presilaeir ekarriiwln pepeafwgtg
      421 dsemhtykah chevrtcqnl nqlidfieel vl
//
LOCUS       WP_181552449             441 aa            linear   BCT 28-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB
            [Desulfosalsimonas propionicica].
ACCESSION   WP_181552449
VERSION     WP_181552449.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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 441)
  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 441)
  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 441)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 441)
  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..441
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..441
                     /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=48520
     Region          <174..436
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 miisrtkpeq dlyrklrwli ffrglfalvm lgsafaadsr pavhlgladg slgwlmllgi
       61 gllllsagyl lvlprirslv lfaylqiaad tvavsliili tggfssifaf mylvvivyat
      121 mviyrrggmv tatlcaiqyg ilidleyygl lrpfgddaqf lidnydwpyv iykllftiaa
      181 fyavaflsgf lseqektakr dlwamedqmk rverlaavge maaglaheik nplaslsgsi
      241 qllrdqlpyd paqerlmqia lreadrlstl vtnflmfsrp gvgkaevidl eravseittl
      301 fksnpghrar idvrmdlskg lfvridpehf kqvvwnllnn aaesiegsgv ieirlypcrk
      361 nqacidisdt gsgisrdmla rvfdpfvstk srgtglglsi vqqlinaygg lvhmestpga
      421 gtavtlrlpt hqpaapgvag d
//
LOCUS       WP_181552578             378 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Desulfosalsimonas propionicica].
ACCESSION   WP_181552578
VERSION     WP_181552578.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..378
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..378
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=42623
     Region          7..285
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 metghhiwfa dsremdflad qsvelvvtsp pypmigmwde tfshlepava qsleagngwg
       61 afeqmhqvld svwqevcrvl apggfacini gdavrkisdi fslypnhsri mqafitlgmy
      121 plpavlwrkq tnapnkfmgs gmlpagayvt leheyvlifr kgakrdfnga dqrlyrqqsa
      181 yfweernqwf sdiwfdlkgt rqdlveknlr krsgafpfal pyrlismysv agdtvldpfa
      241 gtgttlfaam aaarnsagve mekdfypvme kksreipdfa rqviddrlra hmdfaaakka
      301 dgkplkymna hygfpvmtrq entlrffyph kvhvpepgrf vvgyndappa glfngghaes
      361 aqtpekpeps apvqkslf
//
LOCUS       WP_181552583             387 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181552583
VERSION     WP_181552583.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=44728
     Region          14..373
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makkklnhhl yqdsgsqvwy fqkkvkgfdk pykfsletts vtearrkrde ylkeieyhgy
       61 lptvepekpe psnttkvfge vaqewaeitk tkvaettfha ykkamnthvl pyfgnmpidg
      121 itsldiekfl snlkcspktk iniytpfkgv mgfakkhkii ssdptvdvdp irerksqkiv
      181 hpplsleeih kflenvdefw kplfifmffs gvriseaagl kwkrvdlkng vvqihrslvf
      241 vgdkqfykat ktdgshrevr ipqpvvdall eqrkrtykgn penfvflnsi gqnihrhtln
      301 knvirptlkk aglslnrsik dtrasyitnc ldngermsfi irqvghtntn mlvkhyyrwm
      361 eapndgeklv eawnstrkvp epakakk
//
LOCUS       WP_181552585             178 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181552585
VERSION     WP_181552585.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 178)
  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..178
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..178
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19823
     Region          11..>71
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          116..>167
                     /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 mekpditysw fhealkyirk kkgrgfqvtl aletgleegs issiisgrkr asfdtqvkia
       61 aaaemdypef lmfgkqlfeg kpvqipklpq qklivdvidg fekinleeha ehyrgiplye
      121 sgklapgagg ysfdekpast tvvyqseiqn rikhdlralr ikgdsmwapd tgrggsdc
//
LOCUS       WP_181552307             273 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [Desulfosalsimonas propionicica].
ACCESSION   WP_181552307
VERSION     WP_181552307.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=31334
     Region          6..273
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mngygslnek tfrqfseliy neagihlaeh kqalvsarlg krmrklrind fedyyryvqe
       61 dqsraelsql ldaistnvtf fyrepdhfev lgsmvkkwhs egqrrfrvwc aaastgeepy
      121 tialtlaeal ddlrdvkilg tdisttvlet arrgeysskk lqkiskklag ryftpmggkg
      181 ddrifrvrde iknmitfswl nlstppfpmr gpldvifcrn vmiyfdnavr qrlldemhrl
      241 lkpggylmvg haeslsgllg gfrsvrpsvy ikq
//
LOCUS       WP_181553166             337 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Citrobacter
            freundii].
ACCESSION   WP_181553166
VERSION     WP_181553166.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 337)
  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 337)
  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 337)
  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..337
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..337
                     /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=37748
     Region          2..331
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkvlvtgats glgrnavefl cskgvsvrat grneamgkll ekmgaefvha dltelvssqa
       61 kvmlagidtl whcssftspw gtqeafdlan vratrrlgew avawgvrnfi hisspslyfd
      121 yhhhrdiked frphrfanef arskaagedv iallaqanpq trftvlrpqs lfgphdkvfi
      181 prlahmmyhy gsillphggs alvdmtyyen avhamwlasq qacdklpsgr aynitngehr
      241 tlrsivqkli dqlnidcrir svpypmldmi arsmerlgnk sakepklthy gvsklnfdft
      301 ldttraqeel gyqpivtlda giertaawlr dhgklpr
//
LOCUS       WP_181553490             404 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter asburiae].
ACCESSION   WP_181553490
VERSION     WP_181553490.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     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=45831
     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 mklnarqvdt akpkdkpykl adggglylli kpnggkywrl kyrvagkekl lalgvypevt
       61 ladarakree akrgiaggid pmeakreeki aretqlnntf kdialewhss klkkwsagya
      121 sdileafnkd vfpyigkkpi adikplelln vlrriegrga tekakkvrqr cgevfryaiv
      181 tgraeynpap dltsamqghe snhypfltpk elpdffkals gytgsalvvl aarlliitgl
      241 rtgelrgafw deiniskaiw eipasrmkmr rphvvplsrq altligqlqe ltgnyplmfp
      301 grndprktms easinqvfkr igydgkvtgh gfrhtmstil heqgyntawi etqlahvdkn
      361 sirgtynhaq yidgrremlq wyadymeale nvnlwslpfl qhrf
//
LOCUS       WP_181553026             665 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: BCCT family transporter [Citrobacter].
ACCESSION   WP_181553026
VERSION     WP_181553026.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=73829
     Region          1..511
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 msenetpikk senhinkpvf ftsallifll vafaaafpdl adknfkllqn qiftnaswfy
       61 ilavalills vtflglsryg diklgpdhaq pdfsyhswfa mlfsagmgig lmffgvaepv
      121 mhylsppvgt petveaakqa mrltffhwgl hawaiyaiva lilaffsyrh glpltlrsal
      181 ypiigdriyg pighavdifa vigtvlgvat slgygvlqvn aglnhlfgvp inetvqvsli
      241 vvitglatis vvsgldkgir ilseinlsla llllvmvmll gptvlllksf ventggylse
      301 mvsktfnlya yepkssnwlg gwtllywgww lswspfvgmf iarvsrgrti refvtgvlfv
      361 pagftllwmt vfgnsaiyli mqkgatdlan tvqqdvalal fnflehfpfs silsfiamam
      421 vivffvtsad sgamvvdtla sggssntpvw qrifwaalmg lvaialllag glsalqtvti
      481 asalpfsvil lisiygllka lrrditkrds qnmttiapta arnpipwqrr lrniahlpkr
      541 slvkrfmddv iqpamtmvqd elnkqstvsh innsgedrir fevdlgneln fiyevrlrgy
      601 vaptfaisgl dneeqqaeqh kyyraeiylk eggqdydvmg wnqeqiindi ldqyekhlhf
      661 lhlvr
//
LOCUS       WP_181553499             242 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter asburiae].
ACCESSION   WP_181553499
VERSION     WP_181553499.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 242)
  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..242
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     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=27880
     Region          80..233
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mrmtvrryrr rrtgsdalgf trspfappff drleflsqsi sqprktdapf illvtedhyl
       61 rtgflnaqfp lssccdyatl ddaliaqtqw psarlvvdie srstgllekl dqlrrhslfp
      121 pfltpwllvr adnydtrlfc kaagpfhvle rqlsaaalqh slldtllplg tekdwfsrne
      181 wpilqelsrg ktlrqialmq nrpysriiyr lscillklgl shrqellhll nnlsdctfsl
      241 ts
//
LOCUS       WP_181553648             232 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MarR family transcriptional regulator
            [Enterobacteriaceae].
ACCESSION   WP_181553648
VERSION     WP_181553648.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 232)
  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 232)
  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 232)
  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 232)
  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 232)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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   8  (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 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..232
                     /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=26770
     Region          <75..110
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 maktlaeika dyqytdkktg evkdrtintp hyfrdipriy spnlqdgymd fcpkaqklyc
       61 yfqgwensgn fcyesqeelg kvidlsrert cklikklqda glitkeknpg yrskvyrtfp
      121 itdahvtppe altvqpviis dvvphqpape taktavthed tpaitpqrir tsdavkhlfe
      181 nlsqrredes fycwssrvlq rlgidhsmgi eqlfqethpy eynqieqsti pf
//
LOCUS       WP_181552652             157 aa            linear   BCT 28-DEC-2024
DEFINITION  ferritin-like domain-containing protein [Desulfosalsimonas
            propionicica].
ACCESSION   WP_181552652
VERSION     WP_181552652.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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 10099350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     Protein         1..157
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18231
     Region          11..149
                     /region_name="Ferritin_like_AB"
                     /note="Uncharacterized family of ferritin-like proteins
                     found in archaea and bacteria; cd01045"
                     /db_xref="CDD:153104"
     Site            order(20,50,53,108,138,141)
                     /site_type="other"
                     /note="diiron binding motif [ion binding]"
                     /db_xref="CDD:153104"
ORIGIN      
        1 mtevscrsmh dvvafaisre ekardfyrdc ansatnkgik effremaeee srhrqlladl
       61 dlsaekpfsd ldehgnvrdl hlsdfmidvr fspdigyqea lamamkkeek ahafyeawkg
      121 rcaseksekl fsflaeeelr hkrrleeiyd seilqeg
//
LOCUS       WP_181553238             350 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Citrobacter freundii].
ACCESSION   WP_181553238
VERSION     WP_181553238.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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 350)
  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 350)
  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 350)
  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..350
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..350
                     /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=38200
     Region          79..350
                     /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(141,145,165..170,189..190,194,212,233..234,236,
                     256..257,283..285)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mkklvatepr vaalveyedr avsanevkvr vkfgapkhgt evvdfraasp fidedfngew
       61 qmfmprpeea prgiefgkfq lgnmvvgdvi ecgsdvteya vgdsvcgygp laetvifnav
      121 nnyklrkmpe gsswknavcy dpaqfamsgv rdanvrvgdf vvvvglgaig qiavqlakka
      181 gasvvigvdp iahrcdiarr hgadfclnpi gtdvgmeikk ltgkqgadvi ietsgyadal
      241 qsalrglayg gtisyvafak pfaegfnlgr eahfnnakiv fsracsepnp dyprwsrkri
      301 eetcwellmn gylnceelid pivtfasspe symqyvdrhp eksikmgvtf
//
LOCUS       WP_181553682              66 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter freundii].
ACCESSION   WP_181553682
VERSION     WP_181553682.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=7718
     Region          1..65
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mieqpddllt peevcqklgi tqktlckwnt ehrhrstlap vkfsakvvry errnveafiq
       61 kcrsqy
//
LOCUS       WP_181552590             168 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Desulfosalsimonas propionicica].
ACCESSION   WP_181552590
VERSION     WP_181552590.1
KEYWORDS    RefSeq.
SOURCE      Desulfosalsimonas propionicica
  ORGANISM  Desulfosalsimonas propionicica
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfosalsimonadaceae; Desulfosalsimonas.
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="Desulfosalsimonas propionicica"
                     /db_xref="taxon:332175"
     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=18507
     Region          70..>141
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mskykgikne idvgcskpid fdswivlvke veplfgpmad eeafqgalkq aiicetafci
       61 rsnlnekery lkggiiiske aneilwfavs kqcrgmglgr qllkfaisel npkegifvqt
      121 fdetvpegkp arklyidlgf tdlkdgglnp agmptvimkl atseidse
//
LOCUS       WP_181553933             577 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 13 protein
            [Enterobacteriaceae].
ACCESSION   WP_181553933
VERSION     WP_181553933.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=66423
     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 plawwkkatv yqiyprsfyd tnqdgigdin giiakldyla dlgidliwic
       61 pfyaspnddn gydisdyqai hpdfgtledv delisaahkr giriimdlvi nhtsdehpwf
      121 iesrdnknsp krdwyiwrdg ceptaekptc dpnnwesifh gsaweydkkt aqyylhlfsk
      181 kqpdlnwenp 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_181554171             195 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Klebsiella].
ACCESSION   WP_181554171
VERSION     WP_181554171.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (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   2  (residues 1 to 195)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 195)
  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..195
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..195
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22058
     Region          14..74
                     /region_name="VapI"
                     /note="Plasmid maintenance system antidote protein VapI,
                     contains XRE-type HTH domain [Defense mechanisms];
                     COG3093"
                     /db_xref="CDD:442327"
     Region          <111..160
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mksiydirrd nlneiirqnf dntqlrfaer ikksqnlvnr wckgtknigg naareieafa
       61 rkerfwldid hmsdapaqlg llnpdewsve kqasftlglw mgshpslnse kkvsdaagig
      121 qatvnrilnc dgstsigvlh aiarafgrea yelimpsdar glieydhqaf eklpqeeknk
      181 itafidfifs qnres
//
LOCUS       WP_181554577             249 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Thermaerobacillus caldiproteolyticus].
ACCESSION   WP_181554577
VERSION     WP_181554577.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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..249
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..249
                     /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=27523
     Region          4..247
                     /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 mkqvfifiys lllgsffnvv glrvpmgesi vkprshcprc qrtltaweli pvvsyviqgg
       61 kcrgcgvris plypfvelst ailftisplv vgwskelivg wtlisllmii vvsdlrymvi
      121 pdrvllafaa ilipermfvp lspwwdslvg agvgfsllll iaviskggmg ggdiklfall
      181 gfvlgwkmvl lsfflstlyg tifglvgmaf gsvrrgepmp fapyivlgtl ttyffgqafi
      241 ewykqfilf
//
LOCUS       WP_181554763             394 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Thermaerobacillus caldiproteolyticus].
ACCESSION   WP_181554763
VERSION     WP_181554763.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
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   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 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 13023754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..394
                     /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=43666
     Region          16..380
                     /region_name="MFS_MFSD6"
                     /note="Major facilitator superfamily domain-containing
                     protein 6; cd17335"
                     /db_xref="CDD:340893"
     Site            order(23..24,27..28,31,64,115..116,118..120,123,141,
                     144..145,148,216,219,222..224,227,255,259,308..309,313,
                     317,338,341..342,345..346,349)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340893"
ORIGIN      
        1 mevalkrges snkttfqlfy fliffgfgsl fpllsvylqe dvglsgteig aimsispivm
       61 ifvqpvwgmi sdytrkpvav lvisllstal igflyssvhq ygwllivaal laftqsaivp
      121 isdsitlnyv qkiegsygsi rlwgsigfal avliggwlsd rfslvaifyi fafilllsam
      181 lawrlpresq amkveigrgm vqlfriprfv lflvttflvf gpiyannfyf gvfikeiggt
      241 ltgigfafll aagseapfmk itdglirryg tvailifaat isalrwmfyf fepsltlvym
      301 ttivqgfsvg lfipaalqyv relapdhvrv tavslysavg nglgswfctf aggyildyyh
      361 igyvylffsv ltfiglvilg tmmmkerrnv pdvs
//
LOCUS       WP_181553686             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Citrobacter freundii].
ACCESSION   WP_181553686
VERSION     WP_181553686.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 265)
  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..265
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..265
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29374
     Region          22..>184
                     /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 mpslgqlynd kdaglttrkt ynvpldkiya eegynvreln rahveefrda fiageyippl
       61 avevtergvk vidghhryhg alaaiemghd ivrleckdfv gseadkiafm vtssqglalt
      121 plergaayhr lqnqgwspse iaakvkrses dilqhlqlhe ctpyikklvr dgsmnyaiai
      181 gisrehgvya dreasrlmkk aeaagkkkit ksianpqfna gkarkfleli sscaedsget
      241 ltievppamq aeiisilref rheav
//
LOCUS       WP_181554805             121 aa            linear   BCT 28-DEC-2024
DEFINITION  (2Fe-2S) ferredoxin domain-containing protein [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181554805
VERSION     WP_181554805.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
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="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     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=13597
     Region          7..99
                     /region_name="COG3411"
                     /note="2Fe-2S ferredoxin [Energy production and
                     conversion]"
                     /db_xref="CDD:442637"
ORIGIN      
        1 matwdfskmk hhificngss cmrsgeeevt qairneisvq gaddlihttr tgcngrcqda
       61 cvvivypdgt wyknmdeqta kelvrgladg rvynkhvshy ykngvfqrte gtvsgkrkhv
      121 q
//
LOCUS       WP_181554881             414 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Thermaerobacillus caldiproteolyticus].
ACCESSION   WP_181554881
VERSION     WP_181554881.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 414)
  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..414
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..414
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46820
     Region          1..401
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 minkytcrng vrivleqipt vrsvaigvwi gtgsrneseq nngishfleh mffkgtktrt
       61 areiaeafds iggqvnafts keytcyyakv ldehaefale mladmffhst fvdeelqkek
      121 nvvleeikmy edtpddivhd llskacyanh plgypilgte etlrtftges lrrymadyyt
      181 pdrvvisvag nvkesfinqi ekyfgaftak qqtrqeqapi fqpqklarqk dteqahlcig
      241 fnglpvghpd iysliilnni lggsmssrlf qevreqrgla ysvfsyhssy qdggllaiyg
      301 gtgnnqldll fetiqetirk lkedgiteke lqnskeqmkg slmlslestn srmsrngkne
      361 lllgrhrsld eiieeinnvt kekvnelaqq ifsedyalal ispsgqlpse lrqs
//
LOCUS       WP_181554988             518 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181554988
VERSION     WP_181554988.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 518)
  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 518)
  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 518)
  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 518)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..518
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..518
                     /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=57344
     Region          50..158
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mkkvfsflfv wflvmavvat padagkftnp gsggapgtwy igstpdhlip dapvilfvqg
       61 lnssastwyd nndmyetayn ngyqtaflel ydsggtsedm wdngsllaak iqeiynyfgk
      121 klvlvthskg gidaqtalvh ynaypyvsnv itlgsphygs qladlayssw aswladilgs
      181 ksdgtyslqt symnyfrsit dhhanvnknn yytlagtkwg sfgsslywgg lylsqygtnd
      241 gavtvanayl pngqmlqvgd wdhstikygs stfsifkpfl ttnraisssi qttflfpekg
      301 lesdedgshv irggsfqqta venfavesnv rtltinwmsd qpvdtltmis pdhqlvnvpv
      361 avyqqeedvf qgawnhvavi nqpmpgewti qakadgtsay llvatfdsdl tksiklkpkn
      421 nknkwvietd gtkikmkqmn meysldfvak ennpgkkkgk klkekaslsa hdeivipkqt
      481 eagvyhltld ikgetldgkp fertfiqtiy kdengnmy
//
LOCUS       WP_181555294             373 aa            linear   BCT 28-DEC-2024
DEFINITION  CdaR family transcriptional regulator [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181555294
VERSION     WP_181555294.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..373
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..373
                     /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=42571
     Region          5..132
                     /region_name="Diacid_rec"
                     /note="Putative sugar diacid recognition; pfam05651"
                     /db_xref="CDD:461704"
     Region          77..373
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mqwftpklaq kivdrtmkil gkninvmdrn gviigsgdrs righthdgal lalkenrtie
       61 ideqsvnqlk gvkmgvnlpi hflgetvgvi gitgdpndir eyaelvkmaa emvlqqsffl
      121 eqvqwkqrlk edlvnqliyd dyvdessfle raktfgvnls lprlvivvei pheqiqyvnq
      181 qllrtltyel atedlaafty sseivvlksi vneerdigdi igkmerilqk vtngkagigp
      241 ccskipaikq syelakqavt vgrkmdpery vyhykevefe illsemgqlp lagsafefye
      301 qllehdetge lqetlhvyiq ekgelnktas klfvhrntlr yrfekiqkit gkdphnikdl
      361 lqlytalivh qlr
//
LOCUS       WP_181554416             708 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Thermaerobacillus caldiproteolyticus].
ACCESSION   WP_181554416
VERSION     WP_181554416.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
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="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     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=80447
     Region          28..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 mkkrkkaqvp frlnmlfffv fllfsalilr lgvvqivyge qyrkeverte deivstpvpr
       61 gkiydryhrv ivdnvplnai tytrtktttp edtlkvarql akyidkpvek vterdmkdyw
      121 iltrrdkaek kvskkerkqf akqglsekei dqkvykltle ritpedlkei tkdeleviai
      181 kreldsgyal tpqivknkgv tnkeyavvse hleelpgvst ttdwerhyvy gntfrsvlgn
      241 itkddeglpr erldhflard ysrndrvgks yieaqyedvl hgkkakikni vdksgnvist
      301 eqiyegqrgk dlvltidiel qqrvekiiee elkaakrsgg tplldrafvv mmnpktgeil
      361 amagkmftkn eqgkvelrdy algtmtsaya mgsavkgatv ltgfqtgvlh pntyirdepl
      421 yikgtpvkks yqtmgtinel talqrssnvy mfktaiaigg gkyqphapls idpdafttir
      481 kyfsqfglgv ktgidlpnei igfqgtsklp gflldlaigq ydmytplqla qyvstiangg
      541 yrmkpqivke ihepsndekq lgpvisefep vvlnridmkt eyikrvqegf rrvmqetggt
      601 aaaffadapy kpagktgtaq afydgpiksk rnaetynltl vgyapyndpe iafsvvvpwa
      661 yqhephypin nkigrkildt yfelkkermn hdseqtdsnl steqsneq
//
LOCUS       WP_181555086             152 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181555086
VERSION     WP_181555086.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 152)
  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 152)
  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..152
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..152
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17412
     Region          1..146
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mklrepmpel tgataylnge vtreqligek ptlihfwsvs chlckeampq vnefrdryke
       61 elnvvavhmp rsendldieq vkkvaeehgi tqpilvdneh kitdafenqy vpayyvfdae
      121 gklrhfqagg sgmkmlekrv nrvleenkkt ea
//
LOCUS       WP_181554221             501 aa            linear   BCT 28-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181554221
VERSION     WP_181554221.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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 501)
  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 501)
  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 501)
  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..501
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..501
                     /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=57996
     Region          2..481
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mnlemlleek fgyrsfrtgq reiiedvmrg rhvlamlptg ggkslcyqlp gyllpgsvli
       61 isplvslmed qvsqlrqrge krvialnsfl dsdlkraafs nlsyfrfiya speilqspsl
      121 mqalknvkis lfvvdeahci sqwghdfrpd flklgdirkl vgsppclalt atappevmdd
      181 ivrtlqldev qrhiysidrp niaikvekmd sveekvrqli hyaktlqspg liyfssrqwa
      241 eiiarrlqee giegvayyhg gmdaeqrmli qqqflrdqlq ivcctnafgm gvnkanirfv
      301 ihfhfpgqle aylqeigrag rdgkhsiail lytngdedmv qslmemelpt daqikqlces
      361 lltnaqdase wkqqlsaqlg ltevqwrild yffetegvfs slssltrddv qllsaklckr
      421 ieerkrwkrk klhqmlswlf hstcrrewiv rafhqqleqt pyaccdrcgf slddylykqk
      481 iekawtfhsw eeelkriffm k
//
LOCUS       WP_181555556             340 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181555556
VERSION     WP_181555556.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
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="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     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=36293
     Region          27..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 mpknsagryw tvllisfgiv lvaicvsltn gvfdmtvidv lktllridpv pdhdlvifdf
       61 rlprivvaal vgfglgvaga aiqgisrngl adpgilgina gagaaivifm fffegriags
      121 gwlsilampl fgwigglgaa vliyffawrn grldpqrlil vgiaagsglg alslylslkm
      181 npqdfematv wltgsiwnan wqyiasmlpw lailvpiiir ksyildllql gedsakslgv
      241 stekeknvll lssigivsac vsvsgnigfv gliaphiakr lvgihhhrvi pvcgtigmll
      301 vivsdfiakt vfspielpvg ivisiigipy fvyllfktkv
//
LOCUS       WP_181555861             123 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator
            [Thermaerobacillus caldiproteolyticus].
ACCESSION   WP_181555861
VERSION     WP_181555861.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
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="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..123
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14171
     Region          1..105
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkkkkynipv eatleviggk wkcvilchlt hgkkrtselk rlmpgitqkm ltqqlrelee
       61 dgiinrivyn qippkveyel seygwslkdi ldslcawgek hitkvygdkf avleesvlnd
      121 rlk
//
LOCUS       WP_181555896             257 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181555896
VERSION     WP_181555896.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 257)
  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 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   3  (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]
REFERENCE   4  (residues 1 to 257)
  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..257
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..257
                     /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=30273
     Region          1..257
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mndyqqfivn ikkktgidla qykeaqmkrr ltslyekrgf ksfqeffqam etdqnlfhef
       61 ldrmtinvse fyrnakrwev leqrilpklf ernrrlkvws aacstgeepy tlamilskfm
      121 plsqvsvlat dldenaisra kigiypersl qevpdevkkk fftkegiyyk ideqvkgavt
      181 fkkhnlladp fetnydlivc rnvliyftee akqslyhkfn qalrpggilf vgsteqifnp
      241 lsygfetedt ffyrkve
//
LOCUS       WP_181555333             538 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181555333
VERSION     WP_181555333.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 538)
  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 538)
  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 538)
  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..538
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..538
                     /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=64043
     Region          7..453
                     /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(60,63,100,103,139,158,162,194,245,395)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(194,245,310)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          460..534
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mkktwwkeav vyqvywrsfy dsdgdgygdl qgliekldyi khlgidviwl npcyespdkd
       61 ngydisnyyt imdkagtmka wetlldevhk rdmklimdlv vnhtsnkhpw flesrsskdn
      121 pkrdwyiwrd kpnnwrsyft psaweydett eqyyfhsfav eqpdlnwknp evreeiykmm
      181 rfwldkgidg frldaialla kpegfpdaan pndiryltnn pglhdylrem nervfkhydi
      241 ftvgevafas peeglkyvae drhelhtlfh fevcdempsw eplrfkqiqk rwyealwgkg
      301 wnsqflnnhd htrqvtrygn dkeyrlesak llgtmlhtlp gtpyiyqgee igmtgvrfss
      361 iddyndiamk nkyeeevakg rdpqevlesl qplsrdnsrt pmqwddsrha gfttgtpwik
      421 vnpnykdinv kqaledpnsv yhyyrkliql rkenpvmvyg tfrdytetep yiyaytreld
      481 serwlivlnh cdhandyelp aplasykrel llgnyediqe hgavlhmrph eariyklv
//
LOCUS       WP_181556085             131 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181556085
VERSION     WP_181556085.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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 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   4  (residues 1 to 131)
  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..131
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..131
                     /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=15675
     Region          4..122
                     /region_name="HTH_GnyR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     regulatory protein GnyR; cd04776"
                     /db_xref="CDD:133403"
     Site            order(5..7,21,38..40)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133403"
     Site            order(51,54,58..59,68,89,93,99,103,106..107)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133403"
ORIGIN      
        1 mnyytisqla qefdistrti ryyeergmia pmrtetgqrl ytkkdravlk lilrgkrfgf
       61 sleeihemis lfdkdrtgrk qlertieyge kklkevseri edlmqlkqem eailedfkqr
      121 lkelgesdeh f
//
LOCUS       WP_181556220             146 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181556220
VERSION     WP_181556220.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
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="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..146
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16777
     Region          1..145
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mklrdempel vgatewinge vrkedllgkp tlihfwsvsc ylckeampev nelrdeynde
       61 lnvvavhmpr seddldinvi rqmalahdii qpifvdndhk ltdtfenkyv payyvfdaeg
      121 klrhfqaggs gmamlrkrin rvlgke
//
LOCUS       WP_181553890             626 aa            linear   BCT 28-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Citrobacter
            freundii].
ACCESSION   WP_181553890
VERSION     WP_181553890.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 626)
  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 626)
  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 626)
  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 626)
  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 626)
  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 626)
  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 626)
  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 626)
  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 626)
  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..626
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..626
                     /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=67687
     Region          44..138
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          277..623
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mmtvfrqtll cllllwlpvs waaepgwlrs pdndhasvrl radtsagget rllldvkled
       61 gwktywrspg eggvapaiaw keempavdwf wptparfeva nittqgyhdk vtfpmvvrgr
      121 apatlsgvlt lstcsnvcll tdfpfsvtpt aqdptfahdy aqamgqipla sgltdalsag
      181 arageivvea hraggwtapg lyldavddad fgmpqihveg etlratvpvh dgwgegapdl
      241 rgksvtlvla dngvaqesrl aigeapvven aslplwqvvl mallggliln lmpcvlpvlg
      301 mklgsillve eksrrqvrrq flasvagilv sfmalallmt vlrltnqalg wgiqfqnpwf
      361 igvmvlvmlt fsaslfgwfe frlpsamttt lathggngls ghfwqgafat llatscsapf
      421 lgtavavalt aslptlwglf ialglgmslp wllvalrpgl alrlprpgrw mnmlrrllgv
      481 mmlgsaiwla tlllphfgfv gqstgkesvn wqplseqaie dalaqhkrvf idvtadwcit
      541 ckvnkfnvlh kddvqaalqq pdvvalrgdw tlpseaitef lkkrgqvavp ynqiygpglp
      601 egqvlptllt rdavlqtlnd akgvtp
//
LOCUS       WP_181556426             332 aa            linear   BCT 28-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Thermaerobacillus caldiproteolyticus].
ACCESSION   WP_181556426
VERSION     WP_181556426.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     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=36848
     Region          4..313
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(10..11,13,54..56,76,104..105,108..109,111..112,115,
                     119,121,129,131,133,135..141,143..147,165..166,169..170,
                     268..269,277,283..289,291..294,296)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(55,77..79,102,239,287,290)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(78..79,106,155..159,177..179,182,209..211,215..216,
                     237..239,263..264,287,289..290)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mnkpyvfitr klpdeaikpl ttlaevkmwp yedvpvtrev llseakkada lftmlsdrid
       61 revmeagesl kvianlavgf dnidvsfate rgiaicntpd vltdttadlt falllatarr
      121 vveaaefvka gewkswspfl laghdvhhkt igivgmgkig qavakratgf emnilyhnrs
      181 rneeaerklg atyctfaell eksdfvvclt pltnetrwlf nreafqmmkr saifinaarg
      241 avvdeealyd alingeiaga gldvfekepi drnhpllaln nvvalphigs asvetrvkmm
      301 elccrnivav lkgeapetlv nqqwlektrr vl
//
LOCUS       WP_181556381             390 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181556381
VERSION     WP_181556381.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..390
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..390
                     /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=42064
     Region          1..>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          47..376
                     /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(62,64,215,235,305)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mkyciynvri isgkkeqpye qgtvlfdesg iidvtetsit dkgdinidgs glsilpglid
       61 ahvhlgmdcs pdpfkkiatd readtafiay dqgqkflkag ittvrnlgtk nnvdiayrda
      121 vkngtvlgpr vyaagqpiam tgghgypmai eadgvdeirk asrkqikiga dllklmatgg
      181 vltkgndpga pqlsidelka ackeashask ttaahaigle gvknaikagv ttiehgyyld
      241 deavemmvkn gtylvptlla ptlilkhsev ipkhmikkie iieqehrqsf rralkkgvkv
      301 avgtdagtpf nypglivdem elmvtegmsp levihaatyv gaeclriekk vgtiekgkwa
      361 dlilvegnpl edvstlkkir qvfkegkpcl
//
LOCUS       WP_181556943             169 aa            linear   BCT 28-DEC-2024
DEFINITION  FUSC family protein [Thermaerobacillus caldiproteolyticus].
ACCESSION   WP_181556943
VERSION     WP_181556943.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 169)
  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..169
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..169
                     /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=18384
     Region          11..>162
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mntkvfikhl srelnrvgit lqtfkislaa giswwlatli tphfypfiap ltavlitdtt
       61 fkkavtkain rflgvaggva cslfisqwii psgiavflsi fvgmaiaktl klhqdsitqi
      121 gvtvvmvlaf lhsggyewar iietvigsvv aifvtifpph rragnydtp
//
LOCUS       WP_181556760             374 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181556760
VERSION     WP_181556760.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     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=40339
     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 ilgastvyhl akegaavtli drgdkgqatd aaagivcpwv sqrrnklwyr
       61 lakggakfyp tlieelksyg etetgyarvg aiclhtdeek lqkieeralq rresapemge
      121 itrlspeetk vlfpplaeey hsihvsgaar vngralrdsl irvaqklgat yikgnaklih
      181 qgaqvigvev egrqyvgnav iatagawske lllplgiefl vtpqraqivh lerperdtdn
      241 wpvvmppnnq yllafkdgri vvgathedev gfdyrvtagg lhevldkalt aapglancth
      301 fetrvgfrpy tpgflpvfga ipgfegiyva nglgasglta gpylgselak lvlgkpteld
      361 pldydvagai keie
//
LOCUS       WP_181557322             276 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181557322
VERSION     WP_181557322.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..276
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..276
                     /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=30928
     Region          3..276
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mvpfdftyhq pssiheaiql fqtlqqqgkk pmyyaggtei itlsrlhlvf tdavidikqi
       61 pecqvldiqq qqlvlgagvs lttieeanpf plltktasev adrtarnqit lggnicgqif
      121 yreavlplll adsevviagk dgvqqrsihq vfqqhmqlqp gefliqvkte qtylslpyah
      181 ikrrkqgevg yplvtvaalk kdgqlrvafs gvcpfpfrsq aveerlnqql pvntrideal
      241 qhlprpildd iegsaqyrlf vlkhtlfdii telege
//
LOCUS       WP_181557517             196 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181557517
VERSION     WP_181557517.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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..196
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..196
                     /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=22014
     Region          2..193
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 myhfigyflk silrifgkih vynkqhlpks ggyviactht gwvdvlylgt sllptkihym
       61 akkelfknka iawllkklna fpvdrenpgp svlkiphhll skgevvgifp sgtrtdeqva
      121 lkqgaitiaq rskvpiipaa yigpnnlkel flrkkaclif geplyitatg kegrehftil
      181 leekinalqr nlqdkk
//
LOCUS       WP_181557593             265 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Thermaerobacillus caldiproteolyticus].
ACCESSION   WP_181557593
VERSION     WP_181557593.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
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="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..265
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29935
     Region          5..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..37,75,79..80,83..84,113,117,124,
                     127,134,140,156,160..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 minsmiigky vpsdsiihrm dpraklllvf iyvfivflan nsvtyivltm ftlvllflsr
       61 ipiafilrgl kpilwivlvt fllhmfmtke gdllyqwgrl aiyeggikqg ifislrfllf
      121 imittlltlt ttpievtdgv esllaplkkl hvpvhelalm msislrfipt lleetekimk
      181 aqaargvdfs ggsfservka ivsllvplfi nsfkraeela tameargyrg gegrtkfrql
      241 twkpldtfcl iavfvlamil fvlrs
//
LOCUS       WP_181557708             400 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Actinoplanes lutulentus].
ACCESSION   WP_181557708
VERSION     WP_181557708.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            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..400
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     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]"
                     /calculated_mol_wt=42988
     Region          1..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"
     Region          <94..>176
                     /region_name="CHASE2"
                     /note="Extracytoplasmic sensor domain CHASE2 (specificity
                     unknown) [Signal transduction mechanisms]; COG4252"
                     /db_xref="CDD:443394"
ORIGIN      
        1 mrqnrlawld alrgyaavvv aafhlspvil gsathlqiyr vfdlgkyavl lfflvsgyvi
       61 pmslerhgsl rrfwvgrlcr iypaylatil laagltaagl frlpdqlrte ttasvlahat
      121 mlqdllgvrg ivrpfwtlsf emlfyllvag lfawrlhrfs gwwaggltlv avlggsrlpd
      181 alaggtgaar tivaavvavv vagvvwayqs srsglvrlag gvslglifla manghatrwv
      241 tsgssaqaml mlavmfagtv vyraehrqig rsaailalgv vlagvavhpw qgggwcaiav
      301 agtfavmfal rhrsmpgvls wlgtvsysly llhllvlavv trltsdkpli llgftvgtlv
      361 sawachrwve rpgqrlakif iathgettrt gsigkqresv
//
LOCUS       WP_181556064             247 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Thermaerobacillus caldiproteolyticus].
ACCESSION   WP_181556064
VERSION     WP_181556064.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
REFERENCE   1  (residues 1 to 247)
  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 247)
  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 247)
  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 247)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 247)
  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 247)
  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 247)
  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..247
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..247
                     /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=28432
     Region          4..239
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mdslkiiiad dnvssrtllc hfihllpqyk ivgeaasged fvqlvlkekp divlvdinmp
       61 dlngmeavkl ckqllptlqv ifitgydefa veafeisatd yivkpiertr lfnalekarr
      121 liqlsnqtnl sikaknkrlg iksqnsilfl pmedilfaek enrktvvhts heryettetl
      181 neienklddy ffkthrsyiv nlekivkiep agetylayfi dsnkfayisk lkinevqrki
      241 lnihkik
//
LOCUS       WP_181558021             193 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Actinoplanes lutulentus].
ACCESSION   WP_181558021
VERSION     WP_181558021.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     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: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=21042
     Region          38..134
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtvreaygai aglyinlfgt pdkvhaddld liarhlsgrv ldlgcgpghl tgylhergad
       61 vsgvdlvpef veharathpg idfrlgsmdd ldvtgvdgil swystihhpp teidtvftgf
      121 rralkpggtl vlgffksddl epfdhkvtta yrwpvdtmma rlesagfaei erqqrpaedg
      181 hrqhaalavr avs
//
LOCUS       WP_181558043             278 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [Actinoplanes lutulentus].
ACCESSION   WP_181558043
VERSION     WP_181558043.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
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="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     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=31341
     Region          9..271
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mtapnavart isradfdyit gvlhehtgis lapgkealvs srldkrvral glagfsdyvr
       61 llrdhrdere lrqlvdlltt netfffrepr hfeylrrevl pkraagrtfr lwsaasstge
      121 eaytaamvla dtlpggtwei vgtdistrvv egartglypi aaaekiprqm lrrfclkgrd
      181 eyeglmtvnr elrskvrfhc rnliqdfsgl grfdvimlrn vmiyfdvetk ksliprlqdm
      241 lvpgghliig sseslnaips klrmvepsiy rldgdgra
//
LOCUS       WP_181557027             401 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Thermaerobacillus
            caldiproteolyticus].
ACCESSION   WP_181557027
VERSION     WP_181557027.1
KEYWORDS    RefSeq.
SOURCE      Thermaerobacillus caldiproteolyticus
  ORGANISM  Thermaerobacillus caldiproteolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Thermaerobacillus.
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
REFERENCE   2  (residues 1 to 401)
  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 401)
  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 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 10001832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Thermaerobacillus caldiproteolyticus"
                     /db_xref="taxon:247480"
     Protein         1..401
                     /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=43934
     Region          15..401
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mskrdnheel nleglrnetl vvhaddwvtn dgavappiyy tatfrahnss efaemagtpr
       61 hpryytrygn pvhervkkim aelegtetal vtgsgmgaia ttilalvsag dhviaqtrhy
      121 mstakimdem lprfgvevti veqadinafa eairpntkli mvetpanptl vltdlaavve
      181 larphgiivv adntfaspin qrphdlgvdv vihsatkylg ghhdltagvi ctseelaeri
      241 whthisigsv lspmdawlll rglrtlpmri erinanalal aeflekqpqv ervyypglps
      301 hpqhelakrq mrgfgaviaf aikggyeetq rfvsalklpp navslggids lvvhtaamwe
      361 gvmteeqmrt agipsnfvrf svgiehiddl kadvlqalqv v
//
LOCUS       WP_181557963             308 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Actinoplanes
            lutulentus].
ACCESSION   WP_181557963
VERSION     WP_181557963.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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 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
REFERENCE   4  (residues 1 to 308)
  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 308)
  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 308)
  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..308
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     Protein         1..308
                     /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=30295
     Region          1..261
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mavvivtgas sgigratalr lagrgwtvvl aarraaelet laaeiaasaa gtsgsvpgsv
       61 pgsgsgsges gagigaahvv ptdlaepdaa anlvkrtlel tgridalvnn agvggdasvl
      121 tgdgevrtii evnllapirl mravvpvmre qgsgtivnig svageigigg aysaskfglr
      181 gindsvrrel agtgiavslv epgfiatelt ahrsglpgpe ivaeavervi krprrrvvvp
      241 gkyraaivls nafpfitdrv yagkaagkpa gkaagkpagk aaskpagkea gkaagkpagt
      301 aegkpagt
//
LOCUS       WP_181557694             960 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Actinoplanes
            lutulentus].
ACCESSION   WP_181557694
VERSION     WP_181557694.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 960)
  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 960)
  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 960)
  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 960)
  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..960
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     Protein         1..960
                     /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=104756
     Region          7..260
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          156..958
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtegelirig vlgpldirvg grpvaaggrq qqavlamlva argqvvpvdr iveqlwdgtp
       61 pprplvslqa yisrlrrvle prraprgtar vlvsegigya lrlpdeavda wafeqdlrrv
      121 qemrpmglsa gaaevalgil saamdrwrge pyepfadepw aqpaiarlae yrhsaqerit
      181 asllvlgrtg eavqaaqslt eadrwrgqaw rllavalwaa hrsaealdal rrhrrnlaed
      241 lglepepala aleqaileqr hetlaeeltf gvppastave kkpdktdktd fevrpaqlpr
      301 spatfsarqd qlaeltrlld dadgsplivv sgaggvgktt lvvrwahqva glfpdgqlya
      361 dlrgfspeda paspadvlfg fllalgvpeh rvppgesert alfrsvlagr rmllvldnar
      421 dseqvrpllp gtggcavivt srsrlgglvv tdgaatthld gfsdaeasdy lrgrlgdadp
      481 qardaivarc gglplalavv caraagmslt gvaaelaeee gldafavagl ehdlravfsw
      541 syrrlpedaa alfrrlalhp gpdvslpaav svtgagrprt rallrllrda hllderrpnr
      601 ftyhdlvggy aaemahrhdt padrdavlrr lvehhlysaa gavgllanpr pdrvgpvper
      661 iepetfadre aaltwmagey dnvlsiaeqc heswgdgylg plvwtlapyq qdlrflaeds
      721 ftlarralkv aerdgevwwv gflnyilarg ylrlgryeqa rpylertiav gratgdtlrl
      781 ahgllatavs higinqvpsr edtvaaypya learehyrri ahrnearvee ancllaiawy
      841 hfyqpggqae tlrmlersla vqrdlsdarg tadvllhlgr frqatgdpag aatdftralq
      901 lyrdmpdlqm epliclysly latgdraaaa piraeltgmv ktarypdvnr lqallagape
//
LOCUS       WP_181558092             192 aa            linear   BCT 28-DEC-2024
DEFINITION  flavodoxin family protein [Actinoplanes lutulentus].
ACCESSION   WP_181558092
VERSION     WP_181558092.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            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..192
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     Protein         1..192
                     /product="flavodoxin family protein"
                     /calculated_mol_wt=20115
     Region          3..160
                     /region_name="FldA"
                     /note="Flavodoxin [Energy production and conversion];
                     COG0716"
                     /db_xref="CDD:440480"
ORIGIN      
        1 mkalvtyesi fgntaviara iadglradfd vtvadvrtmp vigdidllvv gapthafsps
       61 rprtrahatr keateartag vgvhaylnya pwlpgvhaaa fdtsmkmpsl pgsaarmadr
      121 rlrvlgchma gapesfhvaa msgplvdgep erayrwartl aeavltarrp tllglatvgs
      181 pggpspheaa ra
//
LOCUS       WP_181558095             350 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Actinoplanes lutulentus].
ACCESSION   WP_181558095
VERSION     WP_181558095.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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 350)
  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 350)
  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 350)
  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..350
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     Protein         1..350
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37618
     Region          25..320
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mttapghrgr fmtdiapdad vrlleqtlfe vkkvivgqdr lierlltall agghcllegv
       61 pgvaktlaae tlavavggtf hriqftpdlv psdilgtriy rpsqenfdve lgpimanlvl
      121 adeinrapak vqsamlevma eghvslggrt ypvpqpflvl atqnpieseg vyqlpeaqrd
      181 rflmrvivgy psdedelgil yrmgnrrpva hpvlstdrll vlqqrardvf vhhalaeyvv
      241 rlvaatrdpa rfglpdvagq laygasprat lglvaaaral allrgrdyvl pgdlvdiapd
      301 vlahrlvlaf davadgvqpe tivhrildav tppviapaqq qpaeglgvaa
//
LOCUS       WP_181558105             278 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinoplanes
            lutulentus].
ACCESSION   WP_181558105
VERSION     WP_181558105.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     Protein         1..278
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30523
     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(6,10,35)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(9,34)
                     /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"
     Region          87..254
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgailfrwrk rqkltglqlg krvgmsqaki srletgavaa epgdvrllae algvppgeae
       61 laielaehag erliewvpag rdqaerqrei graeaaakei rilqpavvpg llqtseyara
      121 vlsahegraa tgsndaavte aviarqernr ilhsparefh fliteqvlrv gvggpavmis
      181 qidrmrevag fpnvrlsvit deaelpipiy hgffvaddrw vsvdlftall ratgrtivrd
      241 yrelfdqles aarsdiddll dhyqaryvga lqpksvar
//
LOCUS       WP_181558447             248 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Sphingobium].
ACCESSION   WP_181558447
VERSION     WP_181558447.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     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=26772
     Region          36..244
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mpplsplgtl vtalrsalfs vlfygmtvfl llaclsvmpf garkvvplaa vwsrihrfla
       61 rwvlgqkivv egafpdepvf ivskhesmfe tldavilfhr pviaakrelg dipvwgavar
      121 ayglmivdra ggasalrgir aearaafaeg rpvllypegt rvphgerarl kagfaglytm
      181 lgvpvlpval dtgrlsprns flkrsgvity rlaplippgl praeaerqvf eainslngpa
      241 aereidsv
//
LOCUS       WP_181558461             154 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Sphingobium].
ACCESSION   WP_181558461
VERSION     WP_181558461.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..154
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17405
     Region          31..>74
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mmarttnree ldcedrlfee afllmaqtqm qrllnekqlr yrdlalrlgv svarisqmfg
       61 deasnltirt variyhhlge epvimsrref eravaghdag lpssetewtm iatdvtpfav
      121 aranvvevgh aeveprssrs newfdaeshl skvg
//
LOCUS       WP_181558449             304 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: cell division protein FtsX [Sphingobium].
ACCESSION   WP_181558449
VERSION     WP_181558449.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,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 304)
  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 304)
  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..304
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..304
                     /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=31944
     Region          9..300
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 marnplegms rpyrpgpllp qgrltgpmpw viaimmfltv lataaglaln qgaralvdev
       61 sgrvtvqvae adpqargqav rrivslldqa edvgtvhvvp eselaaqlap wlgndlklad
      121 vplpalidae llapesarte rlavldkavk einpharvep hgdylsplaq lvwsiglvaf
      181 avvalmafat gavvvlaarg ahathrgtid imhmlgatda qvvrlfqrrm mldalfggvv
      241 gyaaatlvii lvgrsmaava sdlmssaslp giawiifpll pvagvgvasl sarltlrral
      301 ersl
//
LOCUS       WP_181558107             668 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Actinoplanes lutulentus].
ACCESSION   WP_181558107
VERSION     WP_181558107.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 668)
  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 668)
  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..668
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     Protein         1..668
                     /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=72902
     Region          31..>380
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mssraklvav dvvvtavagl vanaasthip apldrpwvlw pflivlvpvl iatavrigra
       61 advqvraape rqrreflaqv kyrlvqqdla aiyatsprit pavsvhssss vhsggsidsr
      121 titrvfaear tvlilgpaga gktvallela rdlirdaerd reepvpvlls lsswatkrpp
      181 fpewlagela rsyrmptama tawieearvl plldgldtvp drhrgelvra ineylvsgft
      241 rlavtsried yrrcreqllv aeqleiacpd epqvraylra agmkrpevnr flpvwrdepl
      301 latplmlqls lrvgpgaveq algasgqeaq rrvlfdayla qalnrlggrr dtlaslstia
      361 rwmtdntltv fqadrlqpai lgapalwtsl mavtwfligf vpfipvlalg vavggnwist
      421 glilaasagi wtmllgllmr hdrvirrsyh rildsaprrg lhwvilpves wrwswitara
      481 raplfgslfa lqvplvllad lpagrqvaam alpaltling vgrtpallah rprfnegiir
      541 tarrivptsv lvavlgggsm gllsgpasgl lfsitmvpll amfvgypvvq hyllrallar
      601 rqalpfrlea fleacatanl lrftgdgytf vhpllqdhlt pdsapaapgs prtdflrpsa
      661 pssdparr
//
LOCUS       WP_181558483             292 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TauD/TfdA dioxygenase family protein [Sphingobium].
ACCESSION   WP_181558483
VERSION     WP_181558483.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Sphingobium"
                     /db_xref="taxon:165695"
     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=32523
     Region          16..285
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mtvlektlia sdtdlfeikp lqpslgaqis gidlsqpltr plhaalhaal lrykvlffrd
       61 qhlthdqhia lgaafgdlet hpvfahpdhp eilplrskef agkyrsttds nwhadttfra
      121 epsaasiliq rvspglggdt vfanavaaye tldddtkari dglsaihdtr vflqfietpe
      181 kraalqvqyp pvehpvvrih pgtgekvlhv nsvftreivg laqgeseall arlfdqvkrp
      241 efqvrwswqp gsiafwdnra tqhyavpdyr gnremervti vgerprgpqs pn
//
LOCUS       WP_181558518             316 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FAD binding domain-containing protein [Sphingobium].
ACCESSION   WP_181558518
VERSION     WP_181558518.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Sphingobium"
                     /db_xref="taxon:165695"
     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=33178
     Region          1..314
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mrpftyerat spaqaatgvl sqqgarfiag gtnlldlmkl qietpthlvd vqdlkldqit
       61 qepdgglrig alvtntalaa drrvrsdyav lsrailagas gqlrnkattg gnllqrtrcp
      121 yfydtnqpcn krqpgtgcaa iegasrqlav iggsaaciat npsdmavamr lldarvetvd
      181 aqgnvrsidi adfhklpgdt phvetalapg elitavllpk pvggqhvyhk vrdrasyafa
      241 lvsvaailqp dgtgrvavgg iapkpwrtda adealtqgae avarhllaga aptrdnafki
      301 elvertlagi lhdakg
//
LOCUS       WP_181558117             942 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Actinoplanes lutulentus].
ACCESSION   WP_181558117
VERSION     WP_181558117.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
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
REFERENCE   2  (residues 1 to 942)
  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..942
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     Protein         1..942
                     /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=104567
     Region          208..872
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 maktlipslt tipdldpeaa kelaeyldsa dfadicarla leitphsarr kgqiveasvi
       61 kselkqsill hvssvgaqdc saigdiifgv vsqsiishpa vqgdlisgkp elralavass
      121 aaageasvrn tdllknlgsl knvhafeqql reqirsahss mklphagttr kvpyrqlfvd
      181 pllspvvlds kdhvnnqvav keaigsapra vilgnpgggk stlalkftwd larlsakpgs
      241 ptvpllvvlr dyseviqegq qtiasyleav cranyniepp pggveyllln gkahvifdgl
      301 delidisvrq qlvasvesfa rryptvpilv ttrevgyeqa pldemmfqaf tlaplgpaqv
      361 seyarkwfal ddsvnkmnre dlarafiads eyvadlrtnp lmlslmcgiy ssehyipanr
      421 pevyrkcael lferwdkqrg ivsplpfdah vrfalnalal wmfanpkydm glkrselvkf
      481 mtdylhekrf sdeadaenaa iqfiefctgr awvltdvgsd rqqelygfth rtfleffaan
      541 qlvrlnssad alfasllpki eneqwdmvaq lalqllgnnv edgsddfltr lldayyqfvs
      601 akdtaregrk fstdtniisf aarslafvvp rpsvvsstvs aviehdrisv mderrsvqaa
      661 wsglmscase nramvskavr eyfeakshfd eidlkcivfl geldlripts lsreetlywr
      721 alqkslfedf qpeferaatr hawvdvlrat agrmdianvi strgygglia yrvasragra
      781 pllyrwltad ydtwrdgyie eciksavpal lnskvpwlns deddarmmad acrnskatgg
      841 irawneefga ftatlilpva edilarfger eafngrlshm krgsilhqlm harlgrspar
      901 rsvldflgsr nadsqvtdlv tqwcdggisl asplaplprr rs
//
LOCUS       WP_181558509             291 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: amidohydrolase family protein [Sphingobium].
ACCESSION   WP_181558509
VERSION     WP_181558509.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 291)
  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..291
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..291
                     /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=31213
     Region          21..287
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mtsnsgmsgd grpphilpas awdfhthvfg prphfplaag gayeppsadr dlhlatldrl
       61 gfdhalliqp slygddhsal ldalrhgqgr llgvgsvsat idrdrlaalr sagvvalrfv
      121 gvpgpdggpy pgtqgfdqle dlcsdmralg lhahvwgsle qcadlalgda gsdmplvfdh
      181 laglspddrp gtyrfdrlld alitgmawvk ltyfrrsalp gdysdmqpvv salvdaaphr
      241 viwgsdwpfv rtaqvpdpsa llnqlrswvg eeafrrclsd npaallgmkm p
//
LOCUS       WP_181558596             286 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Sphingobium].
ACCESSION   WP_181558596
VERSION     WP_181558596.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     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=29811
     Region          21..278
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msafaagctp slvrpaaear plglasitva qalqrdyagt lkaakamgys hfgfplaals
       61 prqppapdpv evaamvrdag lsvgvvrlgy gvapamqmat arkigativa qsaapvffeg
      121 avpgkttraa leawlprlnd lshaardagv rlafhnhgwd hvplegeapl aliaerfapg
      181 evdfeidlaw avlggadpls lirtlgprvl amhfkdvdps rgpsdhdrlv ppgdgvlnya
      241 rliplldrmt naigyvevda pedeiaaagr gavfvqrvrr gsvsgg
//
LOCUS       WP_181558485             446 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: spinster family MFS transporter [Sphingobium].
ACCESSION   WP_181558485
VERSION     WP_181558485.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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   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..446
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..446
                     /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=47543
     Region          20..395
                     /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..152,155,233,236..237,240..242,245,274,278,329..330,
                     334,338,358,361..362,365..366,369)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
ORIGIN      
        1 mddketqaae hspypywmmf illlvalscf idrvivaalg paikadlgis daqfglltgl
       61 afallyttag ipvarladqg rrvtllavat tiwslmtmas ayaasywhll llrlgvgige
      121 aaaspctvsm vsdkfprnkr atalavvalg asfgsliggf gggwlgetvg wrhtflivga
      181 pglllallil tvkepirgrf ddpasmarem psfvamlgil rakrtflhlg macglnsfvn
      241 fgillflpmy fgrayemsmt qagllfgivt avsngtgtll ggmgadwagk rderwyawlp
      301 alcllcaapl ymiglsmpnw qtamplvvig atlaftyyap tfgaiqnmve prmrgtasai
      361 iiffqnlvgm gigplfvgfl sdtfaaraya gnyaaechga vgqaaidcaa agtvgirygm
      421 iicasfaiwa gfhywrasrt lkndvi
//
LOCUS       WP_181558891             305 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TauD/TfdA dioxygenase family protein [Sphingobium].
ACCESSION   WP_181558891
VERSION     WP_181558891.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..305
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..305
                     /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=34229
     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 mtitatpitp rfgaeisgvd iskpldadti aeliaqqdrw gvtvyrntgl ddegqiafar
       61 nfghleslpp regrpriflf nagnlnaqge inwdpgatty rkgdqiwhtd ssfmdlrtsy
      121 smlravevpp sggptwfada rsayddlpqd vkdkienlec ehslwwsrkq ggaeisredi
      181 earhrpvhkl vhvhkgsgrk miyagahcyr vvgwgweesr elidylnnfa tqdqyaisvd
      241 yavgdmviwd nlavfhkggq fdwnerrdmr ratvreapap eveddpfgel frtappispk
      301 gaaaa
//
LOCUS       WP_181558547             458 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: spinster family MFS transporter [Sphingobium].
ACCESSION   WP_181558547
VERSION     WP_181558547.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 458)
  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 458)
  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..458
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..458
                     /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=48121
     Region          23..398
                     /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(33..34,37..38,41,74,124..125,127..129,132,152,
                     155..156,159,245,248..249,252..254,257,286,290,341..342,
                     346,350,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
ORIGIN      
        1 mtddastppq qrhygpgyra mllalimlva afayidrviv qtlgqpiked lgltdfqlgl
       61 lgglgfaily stlglpiarl aerrdritii svsvglfslm salcglsanf wqlflcrigv
      121 gigeagvqap stsligdhfp phqrgfaitm mrlgsplgsf igalaavwia kdhgwrtami
      181 avcgpglvva llfrlllrdp prglsdglsn gapptskaat ppppmrevms mmarkavfrn
      241 lliglalssm alyaggafta pffmrvhdls itqagvyvai isstaatagm vlggvgidfi
      301 arrgqhwyal lpfcgiatsv plyligyslg splpalvclt vagvflffys vptlvalqnl
      361 vapnarttaa fiyffiatlv gvglgppiig lasdifagla mpgfksvctd arltgacata
      421 sawgvrhall asialyalaa fhywraacal krdaslsa
//
LOCUS       WP_181558786             236 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: anti-sigma factor family protein [Sphingobium].
ACCESSION   WP_181558786
VERSION     WP_181558786.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 236)
  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..236
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..236
                     /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=24180
     Region          4..>124
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 middetlyaw ldgelpedea krvatlvaan palgekleaq rqlqaglraa fdpvaaapvp
       61 agmaaivtse gavqglaear arrtsragfg lpqwaavaaa lvagfvgaqm lpkagttaqd
      121 glvasaelte aldtqlasag dadgaaapvr vrltfkdgkg dicrsfdtas tagvacrdqd
      181 gwavralvsh prqtegsyrm atsgdaaima yvdaqisgdp ldaaaekram akgwkk
//
LOCUS       WP_181559344             225 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: OmpW/AlkL family protein [Sphingobium].
ACCESSION   WP_181559344
VERSION     WP_181559344.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..225
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..225
                     /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=23211
     Region          4..225
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mnarlfscva glamlaapgv aqaqqgkvqv klmatgvlpn gkidtvksat vtlpagtdta
       61 asdnwvptva ieyflsdavs veticcmtah hvdgagaikg vnrllddiki vpatvtlkyh
      121 lnagpikpyi gagpsyfwvv dskvgaggta algaasaklk skvgfalqag idipvndtgl
      181 gisfdakryf vrptaefyna sgatvlatrh eldpwvvsgg vsyrf
//
LOCUS       WP_181559171             174 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TlpA family protein disulfide reductase
            [Sphingobium].
ACCESSION   WP_181559171
VERSION     WP_181559171.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 174)
  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 174)
  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..174
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..174
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18714
     Region          30..164
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrskfaavaa liaiigmsva rpahaqkikv gdlapaftlm ladgssvsla dlkgqvvvln
       61 fwatwcgpci kelptldafh dilkdkglrv favatedsvp lpklkkmlag mtipmvrrvk
      121 gpyrhlgalp tnfvigrdgr vryaatgafd ldqlnrviip lmneraptap arsr
//
LOCUS       WP_181559149             438 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Sphingobium].
ACCESSION   WP_181559149
VERSION     WP_181559149.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 438)
  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 438)
  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..438
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..438
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46547
     Region          36..416
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mraaarlaag alaclwltat plaakagaaa eavaptdala alraglqamv darelpnaqa
       61 vivkdgrerl rvsigkldle agrvlpadai frlysmtkpi tsvavmmlve egkiaidapl
      121 srympefadl rvyksgslda mvteplnrpv tigdllthss gvtynftgng pvqqyyrrhg
      181 vmraggvgqn addappartm deliarlaka pllhqpgarf sygnstgilg aliervtgqg
      241 ldaflqarif dplemtdtrf vvddaratrl vtnyaavdgg lqaiepaats eyrdparpfd
      301 gggalagtlh dylnfaqmla nrgawhgkrl lrpetvdqmf qprletggqp henvlfgygl
      361 glgdavseqr ggmpagaggw sgsansyffv hpgrnlvaiv mtnvlvgpal vdrtirlrgl
      421 vdqaaqavla eqepairr
//
LOCUS       WP_181558592             793 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 3 protein [Sphingobium].
ACCESSION   WP_181558592
VERSION     WP_181558592.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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 12807984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..793
                     /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=84196
     Region          89..639
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          <715..793
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
ORIGIN      
        1 mtgkisfsvs amalcavlsg cattdrsaaa stpsasptmt qpdvaarskp vitvaglrfk
       61 dlnasgtlep yedwrltare rardlvtrmt laekagtmli atqnpdcdgs itedgkalie
      121 keemsrfilr atvaaepadc svrltgfrlr ggyrqtplqm arftnavqem reasrlgipa
      181 lfkdnarnhv evsptfgigq gagaftefpk eaglaaaalg aaaplsaadg appanlrgdm
      241 sviagftrvm gqewraiglr gmygymadlg teprwsrfhe tfsedadlvg divtalakgl
      301 qgekgqggla lspatavsmt lkhfpgggpq qlgldahytf gkdqfytdps grygfdyhlr
      361 pfqraidagv gsimpyygvp vdahhggrpv eslgmafsrq ivtgilrdel gfrgyvnsds
      421 giieergwgl edsrinpatg kgytvadrta lavragtdil sefrskstiv dlvaqgalse
      481 agdidpaver llteqfalgl fenpyvdaea apemigtaeh ralgldiqrr slvllhnqkv
      541 dgtgvlplrp gsriytmgfa gadfaargfa atdgnydakk gqvraavpag tdyavinvrv
      601 stdaarryss ksaegggrii dpatmianra tgkrqaswge qdpcttssag kdvtcvddnl
      661 ifggafpwea gmlsftamak aqswsvypsl adiqaimrei gdprrvilni yfrqpyvlde
      721 asglrnagai iasfgasdaa qidvltgkqa pagrlpfalp asldavdrqh sdapgyaetp
      781 gstlypfgfg lty
//
LOCUS       WP_181559452             260 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CDP-alcohol phosphatidyltransferase family protein
            [Sphingobium].
ACCESSION   WP_181559452
VERSION     WP_181559452.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..260
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..260
                     /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=27816
     Region          16..251
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 marprpiarm srgitlrqva pnaitamalc fgltairygi sgewqlavaa iifagvldgv
       61 dgrvarllra dsrfgaelds lsdaiafgvs pallvylwsl qsmprfgwiv alvlalscal
      121 rlarfnasld vidqprkaag fltgvpapag agiallplya wfitgldvfr dwrlvapwiv
      181 isaflmissl ptlgwkglrv ppawrlfail lagifaaslm vapwhallll slayiallpv
      241 glvsyarvkr rlvaaslsqg
//
LOCUS       WP_181558979             791 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor [Sphingobium].
ACCESSION   WP_181558979
VERSION     WP_181558979.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 791)
  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 791)
  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 791)
  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 791)
  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..791
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..791
                     /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=84827
     Region          60..791
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 msksanltsf lalgcvsava faapavaqdg eqgrrlggmt vtetaidese ikveraespk
       61 ytrplldtpq tvtvigaktl qqqnlltlre vlstvpgitf gageggfgyg drinlrgysa
      121 nndisvdgvr sgaimnrnet ynieqvevan gansvfsgag svggsinlvt kkpladdkms
      181 vqagvgtdny yrgtvdlnkr vsdmiavrln avyhkndvpg rdvefyerwg vapavtigid
      241 gptsltlqye hlddkgmpqy glryyaaqgg ylpdfnqsay ygfanvdtqq svtdsvqaif
      301 shelsdtvkv rnltryenvs qytvtsqptg tfclanglqp dgsactvaig sstlvvpagy
      361 ylptggrgta rhirnetayn qldlsaefat ggiehtlvlg gsllwerytl nngsilraad
      421 gsnpfaapsy ypltnianpg avltgpaapa gtlarvygsn iytgpqnyiq tgynvgeqts
      481 yaaylfdtmk lsdmfeingg vryerfegst rtrnvttgvv tgpfeakdnl fswrvgavfk
      541 pmpnvsayva vgnsrtpskg svdgscavnt cnvepesakn yeigvkadlf daklqlaaav
      601 frnerdkyrv asgdptipdq vldgrsrvng vslsatgnit eawsifanym yldskliqgv
      661 sdfclanpvs cgntvanpdp tagtalsatp khsgslftty kfpfglevgy gltyqgrhsm
      721 nptatpvyyv paytlhriml aypvterlla qvnvqnvtde dyvttvrtnv nnswaqpgvg
      781 rsavfsltys y
//
LOCUS       WP_181559647             137 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Sphingobium].
ACCESSION   WP_181559647
VERSION     WP_181559647.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..137
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15654
     Region          28..125
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mttqakrpsv paspdrydqi dprvealvnd ligqvadkwt mllievlhdh geqrftrife
       61 kmpgisqkml tqtlrqmern glvhrtvhpv vpphvdyrlt elgaslgeaf cgvwtwaedh
      121 lqdidaarlr fdeartr
//
LOCUS       WP_181559662             337 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: zinc-dependent alcohol dehydrogenase family protein
            [Sphingobium].
ACCESSION   WP_181559662
VERSION     WP_181559662.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     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=34414
     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(41..43,46,145,149,171..176,194..195,199,214,
                     237..238,240,259..260,283..285)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176237"
ORIGIN      
        1 mrawqlasga tsiddlhlve rdqpapgpgq vairvhacsl nyrdqavvlg rylggpvpnp
       61 tiplsdgage viavgagvtq fkpgdrvagt ffqswddgpp npaaglalga agadgmlaev
      121 vvlpeqgvvp iakslsyaea aclpcagvta wnalfegprp vkpgervlll gtggvsilal
      181 qlakaagcev iitsssdakl erakalgadh linyreiedw gqhvsttmgg vdkvvevgga
      241 gtaqqsmaal rhngevalig vlnpiggpnp sglmfvggtl rgifvgsrgm arrlaaaidv
      301 ngikpvigar yafedakaaf ahgsgsehfs kvvidvr
//
LOCUS       WP_181559886             151 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [Sphingobium].
ACCESSION   WP_181559886
VERSION     WP_181559886.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     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=15581
     Region          <59..136
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkistlafgl aagiltgsvs valaqdaaqp rqgdpaalva qqgdadgafv mpgrfsepdg
       61 ekmyrrvcaa chmpdaagat gagkypalan npnlaasgyp mlvtlkglng mppvgemmtd
      121 qqvanvvnyv rthfgnhyed aitaedvkam r
//
LOCUS       WP_181559570             260 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Sphingobium].
ACCESSION   WP_181559570
VERSION     WP_181559570.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     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=27373
     Region          1..243
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mgekfaivtg astgigfela hliaqdgydl lvvadeplid aaaqdfrrhg gdvrsleadl
       61 stldgvdrll aaaegrridv lcanagvgtg gpfleqdvam wrrsvdtnvt gtvyllqkvl
      121 admvarndgk ilvtgsiagy ipgtfnavyn atkafidnft ealrneikea egvtlttlmp
      181 gptdteffer aglldtqvgq qdkadpakva rdgwkalldg kghivsglsn klqvaaagvv
      241 pqailaeqhr klaepgsgkd
//
LOCUS       WP_181559987             241 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Sphingobium].
ACCESSION   WP_181559987
VERSION     WP_181559987.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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..241
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..241
                     /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=25670
     Region          25..222
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msrlralarl arligvviac viphllarrr gvspwpqrfl araahatgfd vriegtpllh
       61 dvffianhvs widilalgga tgtafiskdd varapilgwl aaqnntvfit rerrgtvagq
      121 idavrtalaa hqpialfpeg ttgdgqsllp fkpalfsvll ppprsiliqp vvidygagtd
      181 lvawkegesg ianalrilga rgrrtltlrf ldpfdpgdhp drkalaasar arlaaamglp
      241 g
//
LOCUS       WP_181560000             336 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: isopenicillin N synthase family dioxygenase
            [Sphingobium].
ACCESSION   WP_181560000
VERSION     WP_181560000.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..336
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..336
                     /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=38304
     Region          18..329
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mddmiqdedr liaqavelse iplidfapfl fgdaearrev srqiaeacat igffyltghg
       61 vptetrqavf draadffhlp medkeevrvn dqlnrgwiys gdkenlnans rvfeqyriqr
      121 dfapddpllk tgnpfyqpnr wsskvdnfdk dcmtyydtms hlaeelvraf algldlpedr
      181 fnryfqksts qislmyypsl pegagneikn lsahvdegpl vilaqgeigg lelktldgrw
      241 isappvpgaf tvnignmmmw wsngryrstl hrvrntshve rfsipffwna dhdvvveple
      301 elvardgeak fapvhvgall grfykssvyi pfddkk
//
LOCUS       WP_181559554             979 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [Sphingobium].
ACCESSION   WP_181559554
VERSION     WP_181559554.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 979)
  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 979)
  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 979)
  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 979)
  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..979
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..979
                     /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=103569
     Region          21..911
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mspfitrsrv lragagasls alalgmafva tpafaqdtaq pqddeageai ivtgsriart
       61 gfdqptpvsv vggeqiarqa avnvaqvlne lpsfrpqatp stnaifanni gastadlrgl
      121 ganrtlvlin grrvvastvq gssfanagav dlniiptslv ervdvvtgga saaygsdava
      181 gvvnvildtn ltglkgsaqy gindagdgke yqfalaggms faggrghiia gveysdnkgt
      241 dgcysrdwcs layntvanpl vnpanrslgr vgaglpatli lpntrtatas ynglivsgpa
      301 anaaafnasg lrgmefrpdg tlvphdygty ygvpifqsgg gdarqafyen fpiaapverl
      361 ngfthlkfev adgvelfaeg sysrvngsti gaqrrdlgsl viradnaflp dsvaatmasv
      421 glpsfnmgrv wndlgpqrst vkrdtyravv ginaemwgdw kfdayyqfgr tdywqrgynt
      481 sitprlqfai davdqgefng gpangnivcr atlqgnpaaa gcvplnpfge nnfsaaakaw
      541 thgtveqdtr itqnvvaasm ngtlfqgwag pikaatgvel rqdiargnad aisralqfyt
      601 gpgapidgkv dvfeafgeld vpvapgvyln galrytdyst sgdvmtwkvg veaspldwlr
      661 vratrsrdir apnlfelfgp lqtsfqnvrp seggqvltsv llggdstlvp eeadtftvgv
      721 vlqpdlgsag rlrfsvdyfd ikldkavsql gaqvivdgce rdgiqeycsl itrgpvapgr
      781 rfgdiqsivn tnvnlgslit rgwdieaayt lpvnlfggsi slrgmatiid dlitnsasgt
      841 vdragmngsp vsqpsgmpry iingyvtfna epatlqvqvr hissgtynns ligpgqygyd
      901 pnldnsvndn yiapwtyvnl ngsvavwnrg dqkmeifgai nnlfdkdppv dapssfgptn
      961 nvlydvvgrs yrigarfkf
//
LOCUS       WP_181560142             429 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Sphingobium].
ACCESSION   WP_181560142
VERSION     WP_181560142.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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..429
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..429
                     /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=45809
     Region          40..405
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 marvdrsiwi llltgalatv ivyaltgsae atltsavacl fgvallfdal erratpslis
       61 apapdangas lsqidtllqa lphpsliver griercndaa lallgrhiig qdvrlalrhp
      121 aaidlltgpn qaqaparvdi iglgaagqsw aldiqpiang rllallfdqs dkqaaermrv
      181 dfvanashel rtplagilgf ietlrdpvag adaatrerfl timdgearrm qrlvddlmsl
      241 srieadkyrs pdqpvafapl veevvqvfrq gqnkrgqdiv tqvdpdlppv rgdraqlsql
      301 lhnlisnalk ygaagtavtv raephernmv llavsdqgeg ippehlprlt erfyridssr
      361 sramggtglg laivkhivqr hggilqfdsk vgvgttvrve lpvfralage eaaagtaraa
      421 sagvtesqk
//
LOCUS       WP_181560126             389 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Sphingobium xanthum].
ACCESSION   WP_181560126
VERSION     WP_181560126.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium xanthum
  ORGANISM  Sphingobium xanthum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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..389
                     /organism="Sphingobium xanthum"
                     /db_xref="taxon:1387165"
     Protein         1..389
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=43048
     Region          82..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          171..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 maeaakstii cisangktss asrsaanrml iataegvvdf rrdnldapwt rqpdmllpgh
       61 hvsalvydev tdmlfaglhy egglmvssdh gkswearnng lqsghvysll vqhdgdrtil
      121 nvgtepvmfy rsfdlgrswt afpgctqveg tehwffprsq phvkhiaahp sepdtiyicv
      181 eqgdllrted ggeswtslns merpddkfrr dqhrvtfyrd naaeiflttg iglyhtadrg
      241 etwerltdts hpcaypdplf vhprkelmfm vgagmnpnpn wgaegtaypk fmistdhgkt
      301 wqtsmvgmad piagnlevaa mhdsaeggve lfagsacgel yasrdeaqsw qriadglpam
      361 skgphfrhfl ppderaayee klralnafa
//
LOCUS       WP_181560232             252 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: prepilin peptidase [Sphingobium].
ACCESSION   WP_181560232
VERSION     WP_181560232.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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..252
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..252
                     /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=26199
     Region          15..233
                     /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 mlgadllrma lgcglgliag sflgavvtrw prsesvmrgr sacdacgrtl gaidliplls
       61 alrtrgrcrt cgaridpahm imelgaavig gvcalmlalp aaalvavalw illalavlda
      121 rhfwlpdalt lplavlgltl gdwlvpapfa drmigaaigy iglfllamsy rrlrgrdglg
      181 lgdakllgai gawlgwqllp fvlllasigg liwalilclk grtlsgdmrl pfgtclclaa
      241 plaaalawti ap
//
LOCUS       WP_181560242             208 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: prolyl hydroxylase family protein [Sphingobium].
ACCESSION   WP_181560242
VERSION     WP_181560242.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10653727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..208
                     /product="prolyl hydroxylase family protein"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=23123
     Region          34..202
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
ORIGIN      
        1 msmldaplla gqpgiqrlpr rdltlfvkkg fldsdecagl idrieanrrp stiaddlgye
       61 afrtsetcdl edsdpfvaai naklaaysgi dpaqgeqlqg qryavgqefk ahtdyfepgg
      121 mdferycgrs gnrtwtlmvy lnqpaaggat rftqvdkmiq petgklvawn nrlpdgtmnp
      181 atihhgmkvr sgvkyiitkw yreriwag
//
LOCUS       WP_181560254             445 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: bifunctional folylpolyglutamate
            synthase/dihydrofolate synthase [Sphingobium].
ACCESSION   WP_181560254
VERSION     WP_181560254.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..445
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..445
                     /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=47599
     Region          10..442
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 madhavsdhp avqaqldrlm alspgrdvlg leriselvrr lgnphlempp vfhvagtngk
       61 gstcaylraa leadgksvhv ftsphlvrfn erirlagtli dddtlarale qvldiggdln
      121 asffeittaa afmlfatvpa dacvievglg grldatnviq apvacgiasl aidhesflla
      181 pdhdvpedpl sriafekagi akagaplvtq hyrpamnati arvadkagaa hlprgrswdi
      241 aeyqgqlhyr deagrielpt prlhgahqis nmglaiamlr hqqavplpea alraaplwah
      301 wparmqrleg gplnamlpgr tlmldgghnp dagkaladal teshladegi dliigmlsnk
      361 dvagflkplr plirsirslp vpghehhgpe vfaqvarawe vphrsfttiq ealtdvaagp
      421 rrtvlmagtl ylagqvlian nqppv
//
LOCUS       WP_181560178             204 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase family protein
            [Sphingobium].
ACCESSION   WP_181560178
VERSION     WP_181560178.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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..204
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..204
                     /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=21938
     Region          1..198
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mlddaalrts ldalaadqpa iaalierlgy ppsrqrepgy etllrtivgq qvsvaaaasv
       61 wskleaalga gcapdallaq dfetlracgl srqkqgyars laemvvsggl dlhalpqdde
      121 eaiaalvrik gigrwsaeiy llfaegrrdi wpagdlavqi avgqimglda rpaeretral
      181 aeawrphrsa malmawhhyn tpvf
//
LOCUS       WP_181560210             183 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SixA phosphatase family protein [Sphingobium].
ACCESSION   WP_181560210
VERSION     WP_181560210.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 183)
  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..183
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..183
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19429
     Region          4..171
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mktvivlrha ksdwsdaalr dfdrglngrg eraaavmgqw aaghgvtfet iiaspavrvt
       61 qtlarfrday gpcpepmrdm rlylasagti aevlsetapd rasvllaahs pgledfilta
      121 sgqerlagmr asvetkfpta amavltfdva gwadlasgfa daatleafvr prdldpslgp
      181 dqr
//
LOCUS       WP_181560341             352 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: potassium channel family protein [Sphingobium].
ACCESSION   WP_181560341
VERSION     WP_181560341.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 352)
  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 352)
  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 352)
  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..352
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..352
                     /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=38427
     Region          39..336
                     /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 mfqrddprvp praflrrrss lpvwadlawr vgaililatf vlmvhwferd glrdnldgev
       61 sfgdvvyfta vtvttvgygd ivpvtdrtrl fesifvtpar ifvwliflgt ayqfvfrnvw
      121 hrwrmsqiqk sltnhiivag fgtsgseavr elvargtdpr civviersde slalaeaagc
      181 nilkgdatrd qtlmdvrvqe aqamivsagr ddtsilvtlt arhlapdipl svvvrapdne
      241 slarqagatt vinpvsfagl llagscqgah iadymadlaa sggrvqlrer rvaqaevgep
      301 lsaiqtglgv rlyragrayg fwepeaamly agdmiieiip ndgetppsss pa
//
LOCUS       WP_181560374             235 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Sphingobium].
ACCESSION   WP_181560374
VERSION     WP_181560374.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 235)
  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 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   3  (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   4  (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 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     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=26091
     Region          67..233
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <170..233
                     /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 mndilekiae asslpllwrg mtryyarngf gavsyywvki gtnmpatlpl qhgfskkeva
       61 lycsfdfqrl divpraalaa gvpirwhevw gnteltveer qfleamrqid ftdgfslpcy
      121 gpgnrngvvg lgriapdadl seermtqlhf aaqaahlric glfaeetgre rqlsarekei
      181 lhwvargksn tviadilqis pgtvdtymrr iyeklevsdr tsaavkgvgs gliaa
//
LOCUS       WP_181560417             500 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GumC family protein [Sphingobium].
ACCESSION   WP_181560417
VERSION     WP_181560417.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 500)
  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 500)
  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 500)
  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..500
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..500
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53882
     Region          26..>484
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mnnvhanydt aeesggasfl phiptilmqr kwlvivpall lllagiataf llpvqyqska
       61 vllveasllp edvagdprsa dgtsvvdqrm arirqqvlsr pqlveliqrn glyqtelrtq
      121 slsevittmr eaiaiepvta diqaanggrr stiafsmsfn ysdpvkaqav aqaltdqvlq
      181 ldastsaaqs vntiqfltdq qadlqtqiaa ldkqiadiql kngltlasst mattgggtig
      241 idsriaalqs anaqlqaqre ltqsaadrdp viaeaeaava tararyteqh pdvvlakqrl
      301 aearelaksn qsriptsais aqiaannrei srletaraae egrsasilsa qirapvvqqe
      361 laqlqqrmtg lneqyqkvsn qlmnakagkr aedeqqgerl svidppvvpd dpyspnrpki
      421 illgafaglg lgfgliflie mltrpirgad avlqatgalp lvviptimsr aeqqqrglkr
      481 lwpfggrkgr tkpddddddd
//
LOCUS       WP_181560175             250 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TrmH family RNA methyltransferase [Sphingobium].
ACCESSION   WP_181560175
VERSION     WP_181560175.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 250)
  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 250)
  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 250)
  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 250)
  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 250)
  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..250
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..250
                     /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=26636
     Region          17..246
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mkrghrtgkp kggyprlygr haitaalanp ervirkiwgt realaaldlp pvlpivysdv
       61 adlgrmvpgd aphqglvaev ealediwlgd lleqgvpdeq arrpilvldq vtdphnvgai
      121 lrsaaafnal givtqdrhap pesgviaraa agaleivpwv rvvnlarald eiaeagywri
      181 aldgdardti agaldnttrv alvlgaegeg lrlnsvnhcd mvarlpispr meslnvsnaa
      241 aialyacmtr
//
LOCUS       WP_181560344             466 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: leucyl aminopeptidase family protein [Sphingobium].
ACCESSION   WP_181560344
VERSION     WP_181560344.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     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=49597
     Region          24..462
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mtdpadlvrp dtgqtahlih lidaasheqw lagrterera alvaqnyqpk ayahailpge
       61 kpdawsvvty vanvdslssw claklpgvlp agtyrladre pgpaifgwmt aqyrferyka
      121 kpaakgpcvl ltsqpgaidg aaaqaratal vrdmvntpta emgpdeieaq aravadrhga
      181 tmtvtrgdal esgypmihav graadranap rlielvwgre ehprialvgk gitfdtggld
      241 ikpasgmrlm kkdmggaaha laladlvmga glpvrlhlll pvaenaiagn afrpgdvlrs
      301 rkgltveign tdaegrlvlg daltragedk peliidfatl tgaarvalgp dlpalftndd
      361 alaamlascg tdvddplwrl plwapyndlf ksdiadlsns getpfagast aalflqrfvp
      421 dktpwvhfdt fawrptakpg rpkggealgl ratfamlqkr ygqsgd
//
LOCUS       WP_181560424             433 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: UDP-glucose dehydrogenase family protein
            [Sphingobium].
ACCESSION   WP_181560424
VERSION     WP_181560424.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 433)
  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..433
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..433
                     /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=46834
     Region          1..433
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mritmigsgy vglvsgacfa dfghdvicfd kdeakitalq egripifepg ldhlvasnva
       61 agrlsfttqa adaladpdai fiavgtpsrr gdghadlsyv ygaaaeiapf lkrftvvvdk
      121 stvpvgtgde veriiretnp dadfavisnp eflregaaid dfkrpdrvvi ggddrraldv
      181 mrqiyrplvi grspviemsr rgaeltkyag naflatkitf ineiadlcek vgadvhevar
      241 gigldnriga kflhpgpgfg gscfpkdtla llktaqdyea pqrivetvva vndsrkramg
      301 rkviqamgge vrgktiavlg ltfkqntddm rdspaiaiie tlqdagaeih ahdpegmeqa
      361 klvlrdvtyf gnaydtmaga dalvfitewd afraldlari ksllktpvmi dlrnlyprdl
      421 veeagfsyta vgr
//
LOCUS       WP_181560501             127 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Sphingobium].
ACCESSION   WP_181560501
VERSION     WP_181560501.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..127
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14541
     Region          19..115
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdmtttrltv tshkecmrit qtlarfgdrw tlpvvaalgd gtmrfnqirr evssisqqml
       61 trtlralerd gmvnrtvhpt tppqvdyalt plghslarea irlgkwaqmh reeidahrer
      121 fdrlqeg
//
LOCUS       WP_181560291             939 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [unclassified Sphingobium].
ACCESSION   WP_181560291
VERSION     WP_181560291.1
KEYWORDS    RefSeq.
SOURCE      unclassified Sphingobium
  ORGANISM  unclassified Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 939)
  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 939)
  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 939)
  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 939)
  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..939
                     /organism="unclassified Sphingobium"
                     /db_xref="taxon:2611147"
     Protein         1..939
                     /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=98753
     Region          8..773
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mrnsaailam aaigvasaah aqnqggaapq aedqaasgsq eivvtgsrit rggftaptpv
       61 taigrdrlet taatnigdvl sqlpsfrats spsatqttpg navgsrvlel rslgsertlv
      121 lvngrrfvpt targtvdtny ipgilidrvd vvtggasaay gsdavagvvn filnnkldgl
      181 raeaqsgisq rgddrtifls aaggtsfagg rghvvfggey edndgladcy qarslcaqew
      241 tlvgrpagaa gagapalsil nnvhtatiap gglilsngpl kglqflpdgt tapyevgrla
      301 gslfqqggsg kgqnaflagl llkvpverfs tyghaeyefs dalkatleas ygevrafsvs
      361 aqlrdstgsl igpvrrdnpy lprsvtdvmd angitqfnmg ragldlgnar gatkstafri
      421 vgglsgaitd rwtwnayyqy grstyhqeat nnlirsrlll aadvtsgpgg tpicrstltn
      481 ptngcqplnl igagrfsqea layvtgtsml dlkitqqvaa ldvqgdlvdl wagplslaag
      541 aeyrrdevng stdplsptga fyvsnfaasn gkvevkeafv eavlpllkds algkslelng
      601 aarrtdysts gavttwklgg vyepvdflrl rgtlsrdira pnvnelfgsv trsfssftdp
      661 vtskqgliei vsgsnntlrp ekadtftagv vlsnlsflrg fnlsvdyyni rvndaiaqig
      721 sstiatrclv nnatefcpli trngagevtl indrlqnvng fktrgldiea syrtrigaaa
      781 sldlrllatk tfdlmiidsa gsvdragqtg frasntpgvp dyvldgmatl kagpfsvsah
      841 gryipegkfl vefvgpedag ysvglansis tnrvaarfya dltlgwnvka grsdfeyfia
      901 irnlfdkdpp iapsavgitn qvlfdqvgra frvgvrlkr
//
LOCUS       WP_181560319             292 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: arylamine N-acetyltransferase family protein
            [Sphingobium].
ACCESSION   WP_181560319
VERSION     WP_181560319.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 292)
  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 292)
  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..292
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..292
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31264
     Region          7..273
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mtaadrlday larlglesap apdadglail qaaqrrriaf enldvrldrp ilidgdsvfd
       61 klvtrrrggy cfeqnrlfad mlgalglpar pllarvllga apgdvpprth tlllleiege
      121 pwvadagfgg sfvpplplqd gaeattpdga shrlrrtgqp gdvlgewlle ragptastdg
      181 rsaetddwqp qyafhldpva pvdleqcnhw tstraasrft tlhivsivlp dgfaalters
      241 fsiaqgsnre irdiaapeey ratlaevfgl alssddvtsl plfapkshag gg
//
LOCUS       WP_181560466             336 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Sphingobium].
ACCESSION   WP_181560466
VERSION     WP_181560466.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..336
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36603
     Region          29..333
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mppkslfarc lmaaslmllp ltasraevkv ehikvhsqav egnlegnsad rdvivflped
       61 yatstkrypv vyflhgfmgs aegydkyigf adalntaeak nrqailvvpd snsrhggsmy
      121 ssspttgnfe rfiaqdlvay vdkhyrtlak qesrglsghs mggygtlria mkypgvfssi
      181 yamsacclsa rpvdaersqr legmsmddal kgdfgvradf aaasawspap dkapfyldlg
      241 tqkgvvqpqi iaqwaanapl amapqylpal kslkaiaidv gdkdtlikdn gdmaklldrm
      301 gvahsytvye gdhgnrvrer frafvlpffa ehlakd
//
LOCUS       WP_181560609             139 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Sphingobium].
ACCESSION   WP_181560609
VERSION     WP_181560609.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 139)
  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 139)
  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 139)
  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 139)
  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..139
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..139
                     /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=15251
     Region          61..139
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mplhitvpeq pseadrnavf apllayniaq agnpnirpia illtdeqger vggiwgkcsy
       61 dwmfvellai aaehrggghg kalmaeaerv arahgcvgiw ldtyafqarg fyeklgfsvf
      121 gklddhpvgq qrfflskrl
//
LOCUS       WP_181560749             387 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [Sphingobium].
ACCESSION   WP_181560749
VERSION     WP_181560749.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..387
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41497
     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 mtqplagiri adfshvmagp yashllrlmg advikiespk gdnfrsygsd prfeglspaf
       61 iaanagkksi mldlkdpadl diahaivarc dvmlenfrpg vitrlglgye aarelrpdii
      121 fcsvsgygqd spqrdwpaid nivqatsgmm mlsgeegdpp vrvgfpivdt ltgqtaalai
      181 lsalvrrlqg gggsyidvsm fdaslafmts avtpylltgq amsrmgntgy sglptaslft
      241 ardgrqislg vvqpnqfaal arftgredwl tdplfatpea rranfdamka elervfatrd
      301 aaaweaglse agipcgmvrr vdeaaelarp dalvsfdipe gpltgpvryp gagfrltpgl
      361 qvgevpprld enraeildwl lrtepgh
//
LOCUS       WP_181560606             449 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PepSY-associated TM helix domain-containing protein
            [Sphingobium].
ACCESSION   WP_181560606
VERSION     WP_181560606.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 449)
  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..449
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..449
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48741
     Region          10..414
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msarsttggg fyqavwrwhf yaglivlpil lwmamtgaly lykpeierlv yadwshvtpk
       61 dapqplsemi atveresgqq vsqiqrpaep teswrmtlqd adgtrrlafv dpyrgkllgt
      121 aqaggimqtv rdlhsliitg pvgnalveiv agwaillvlt glylwwprrg spvvglrgqa
      181 rgrlfwrdlh astgllaggv ilflaitglp wsgfsgkqlq gwvaraelgr pkapgpnpwe
      241 apaprahhgh ghdegakqsl pwsmqeatpp aasgnddigv draaeiagkr glaapwtltl
      301 pmadgapyli srslrraqda raiyidpasg avmqdarfah fgigaraiew giathqgqqy
      361 geinrilmll gclalmllcl tapvlwwkrr kngrleapar ptdprkargv aaimlaiglc
      421 lpltgltlaa alaldmligr wrnraamas
//
LOCUS       WP_181560827             966 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [Sphingobium].
ACCESSION   WP_181560827
VERSION     WP_181560827.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 966)
  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 966)
  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 966)
  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 966)
  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..966
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..966
                     /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=102608
     Region          63..890
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkaisaarsr fhlgvciaam lcplsgalaq vsddaaepat aqvtsaqpev agaassagaa
       61 adqdivvtgs riqasgftap tptsvistaq iqsvaptrvd dalrlipafs ttgngvaral
      121 ssatvvadlr nvgaqrtlvl vdgrrhvata pegtvdlgvi pailiertev vtggasaswg
      181 sdavsgvinl ilksklqgve gtvqsgisqy gdaqnvlagl aagtsfgggr ghiliggeys
      241 knegigqtpy rprpwvsrgv agnsayaqng lpatiyaddv rrtdlweggl itsgplrgtt
      301 flpgqqtgqf gygevfgnrm iggtsnytei inpggnlqqp verysamarv syevvdnltl
      361 faegsfarsi tngyfaeprq qgsvtgnptc sattipggqt gnvlvpitnp ylsddfrtra
      421 laagvtcfnf grslreqglg avrghvgsps vyrgvvgveg tlgnwsfday yqygrnhfvq
      481 eyvgqinmin yrkaidavrs gsnivcrvna danplnddpa caplnlfgfg spsqeaiayi
      541 tgtsrfdlvt kqqvaafsan galfegwagp inaafgaeyr eesidatvda isqagqwqsg
      601 arqpisgsyn vkevfgelai pllkdlpfir sfdlnlaary tdystsggvt twkvggtwel
      661 sselrlratr srdiragnfa elfapttvar qnirdprrst nytvevaslg npnldpekad
      721 tltagivyqp rwldglrlsv dyydidikgv igtisanevl ercyvdgisd fcglvttsgg
      781 apagditgvt vrfenldrlk tkgvdfeaay rsslenifgq gagslsirll gtyldtlatt
      841 avstasteer ageyvtphwr vsglvthelg rltstldlrw lqggkidndf vvgtgtlnsi
      901 nfndtkntfy tnatftvdvs rdadrsremf irlnnifnva ppfpdqaspl fdqvgrafrv
      961 glrfkm
//
LOCUS       WP_181560763             669 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [Sphingobium].
ACCESSION   WP_181560763
VERSION     WP_181560763.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 669)
  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 669)
  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 669)
  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 669)
  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..669
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..669
                     /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=73129
     Region          11..631
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 msvkasrwrl maaaalvgac vpgvrsahaq dlssysledl lttestsvak rrqrlsdsta
       61 avtiltqedi lrsgaqsipe vlrlvpgvev gqidsvstav svrgfstrfa nnllvmidgr
      121 slyvsslsgv lwdqqlvpls dierievvrg pgatlwgsna vngviniitk dsiqtqgwqa
      181 nafisadgrn gtvryggskd klsyrayvta rdidgleqpn geswnsgsra vqagfrldav
      241 pdendtitlq gdvqhgtfva dllqtppqvq qtgmypfdgs fsgmnllgrw shrwdsqref
      301 nlqayhdwvq rrefgvnisr tvddldaslr lggdrqelvl glnvrrttds lgssdrfvsf
      361 ivprethhwv sgfaqqdlwl vpdrlrlsvg tkaeyntisg falqpsvrll akptpsmtiw
      421 aaasravrtp arfeeavrvn lgipagtpmn ptpmpmvari egqadlaaen ldafelgirg
      481 slsssftydi aayynryrnl igyaargqsm vfsptpvlll dyqsanigkg qtygveaait
      541 fspapdlkvq anasmqhlsf etdsptsish alaglspkfq agmrvsydva pnlevdawlr
      601 hvsalpasdi payqdldlri nyvlmprlnl sligqnllad rrvefaqqly paprsyvgrs
      661 valrlsvdf
//
LOCUS       WP_181561141              94 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: BolA family protein [Sphingobium].
ACCESSION   WP_181561141
VERSION     WP_181561141.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..94
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..94
                     /product="BolA family protein"
                     /calculated_mol_wt=9911
     Region          8..94
                     /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 mvdaslgpvg qeiaqrlena lspqqlavin dsakhrghmg ddgsgeshft veivadsftg
       61 qsrvarqrmv naaladllre kvhalairar apge
//
LOCUS       WP_181561370             718 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: autotransporter assembly complex protein TamA
            [unclassified Sphingobium].
ACCESSION   WP_181561370
VERSION     WP_181561370.1
KEYWORDS    RefSeq.
SOURCE      unclassified Sphingobium
  ORGANISM  unclassified Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..718
                     /organism="unclassified Sphingobium"
                     /db_xref="taxon:2611147"
     Protein         1..718
                     /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=77085
     Region          126..718
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mlcllahaah aqapateqtq ptrnsdaapv eaiisdeefd asippidesa plgsvqawea
       61 dadrraastg rdasvsaept tteqsedngl pappeldkel drpltplnaf dvetfdesqy
      121 teadegpaps lrysykiegl saldgtgpvl pvdggdivsq fkslsaledg dgkadngami
      181 narleedqkl lvdilssqgf fdatvrgsle lpeqdskgpi tvilqatpgp ryhlgeirfd
      241 appvqpgdli trafrprtgd pivaerilga eaniavtlpe ngypfvnvgq rdivldpete
      301 agdytlpitp gprssfgdiv vegekpvfep dhiqkiarfr kgelydsrki ddlrqaliat
      361 gllsvgsvtp rpsgepagdg tdyatlivnq eagpartlaa qagygtgqgv kvegswthrn
      421 mfppegaliv qgtagtleqg lgvsfrrsna gkrdrsvelg idarhsnfda feaftgrlyg
      481 riayestpiw qkrltynfgf ellgsneqdy nfdagelrrr tyyvaalpgq vtfdtsnsll
      541 dptrgfrisa wlspeaslgs gaqtyarall egtgyypisd gfvlagrarv gmiggaareq
      601 iapsrrfygg gggsvrgfgy qelgpkdpda rpiggrslve aaaevryrfg dygivgfidg
      661 gqvytsqvpr fddwrfgvgi ggrfytnfgp mrldvatpin rqpgesrisv yvsigqaf
//
LOCUS       WP_181560397             698 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RelA/SpoT family protein [Sphingobium].
ACCESSION   WP_181560397
VERSION     WP_181560397.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 698)
  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 698)
  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 698)
  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 698)
  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 698)
  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..698
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..698
                     /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=78299
     Region          1..698
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mlrqyelver vkgydpdade alinrayvfs vakhgtqkra sgdpyfshpi evagiltdlf
       61 lddktivtal lhdtiedtlt ttaeierlfg qdvarlvdgv tklskieaqs esqraaenlr
      121 kfllamsddi rvllvkladr lhnmrtlhfi kneekrrria retmdiyapl aerigmyefm
      181 remqllafqq lepdaydsvt krlallkegg eskvaristq lqnmltsagm hvtvsgrekh
      241 pysiwrktqe rhisfeqltd imafrvvtds tddcyralgl ihqrfkmvpg rfkdyistpk
      301 rngyqslhtt viheenarie vqirsermhq dsefglaahw aykqsgarpd gqagwlrdlv
      361 eileqshdae ellehtrmam yqdrifaftp kgelqqlpkg stpvdfayav httlgnqtvg
      421 akingrvmpl rtqlengdqv eilksdaqep qpgwlsfait gkaraairrf irqkqrteti
      481 algeklyeei vlrlpveigd kaekaaikrl kledkaalmi aiatnrisde evmnalvpgs
      541 aedapgaarr rkkqaqavsi igltpgiaft lsecchpvpg drivglrrpg epievhtidc
      601 lvletgqdad wvdlswdsea kggtarlsvi lknqpgalat vanifavnka nilnlqlvnr
      661 egpfhtdlid levedashva rilsalravd avvqadri
//
LOCUS       WP_181561426             271 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HpcH/HpaI aldolase/citrate lyase family protein
            [Sphingobium].
ACCESSION   WP_181561426
VERSION     WP_181561426.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..271
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..271
                     /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=28938
     Region          1..269
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mplrlvrtll fvpasrprai ekarqldcdf iildledsvi aedrdaarqr aveavqagfd
       61 grpcairina egrpehgldm vaarsagvpy vivpkviear qvhdvnrvtq rpviamiesp
      121 agiinalsia repgvsalva gtndlrrgla vppdaprsai syslqsivla araagvaafd
      181 gvynnledpa glaaecdegr qmgfdgktii hpshidiand afspsgpave qaralveaft
      241 ggaqrydgrm ieamhveeak aiidraerlr s
//
LOCUS       WP_181561557             307 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [Sphingobium].
ACCESSION   WP_181561557
VERSION     WP_181561557.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     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=32201
     Region          6..301
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mstlaltgat gfvgkatvet alaaghavra ltrrpqppre gvswiagsle daaaldalva
       61 gadavmhiag vvnaptragf eagnatgtaa viaamqragv vrlvhvssla arepglsdyg
      121 wskaeaerhv qasaldwtmi rppaiygpgd aellelfqma trgfvllppg grlsaihvdd
      181 ladllvrlgt rqggetqgkv yevddgtpeg wshvdfarai gravgrasvr tismpsalvr
      241 fgaridrllr gdkarltpdr aayfchadwv skaalhppad lwrptiapea glamtaqayr
      301 dkgllpr
//
LOCUS       WP_181561579             214 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Sphingobium].
ACCESSION   WP_181561579
VERSION     WP_181561579.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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 214)
  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..214
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..214
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23651
     Region          1..214
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mdrtitvrgt yaaflthmal slapwrlifl plagivmlgy vlrlvdrgra kelnqallig
       61 rrvnrerirp aveayadkvi arniragala qiaqdrasgc rlviasasfr lyvepiakrl
      121 gfddviatdh fsqgvdyira riagencydv aklrmieawm sregiarada hvraysdhvt
      181 dapllgfade gyaanphral aslaaeegwp vlhw
//
LOCUS       WP_181561072             201 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Maf family protein [Sphingobium].
ACCESSION   WP_181561072
VERSION     WP_181561072.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
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="Sphingobium"
                     /db_xref="taxon:165695"
     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=21931
     Region          4..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 mttpplllas qsesrrrlla daavpfetvp agvdedaika slvgeglnar dladalaewk
       61 crrpsmrhpd afvlgcdqtl elddgslidk vetreaaadl larmsgrahk lhsaaviaqa
      121 gqaqwrqies vtlqmrplsa afidhyldld weqcrwcvgc yriegpgaql fsrisgslfa
      181 vqglpllpll dylrvrsilp a
//
LOCUS       WP_181561763             402 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_181561763
VERSION     WP_181561763.1
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=45538
     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 rdiassspsi stlvdewlet psvkemvkye
      121 ywkrmlklhv tdnygrliad emspveweqi flritkggsp vqagnvlvkm kqviryalrr
      181 kritsnslml leindigsrp ddgerflnde eigafwnaid ktkmswqnkm lirlvaltgc
      241 rgvelrlark gdfdlkarew vipkensktr krfvrgisql aadylqkvfd vypdqsivfp
      301 paklqvdrpm sastlisiag qveevmggeh wslhdlrrtc ktkmaelgva phvsekilgh
      361 kltgmlavyd qydyipeqqa aaelwaekiq scaansplsl qn
//
LOCUS       WP_181561914             392 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_181561914
VERSION     WP_181561914.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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 392)
  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..392
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..392
                     /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=45407
     Region          2..384
                     /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 msfgsydlvs
       61 laearekrdt arkqvangid pveerkaqkl aqqlstensf eaicrewhan kadrwtvayr
      121 eeiiktfeqd vfpfigkrpi seikplelle vlrriekrga lektrkvrqr cgevyryaii
      181 tgraeynpap dlaialavpk qkhhpflsae elphfirdle aytgsiitkn atkivmltgv
      241 rtqemrfatw eevdlekgiw eipaermkmr rphivplstq vvdlfkqlkp itghypyifi
      301 grnnhskpis kesvsqviel lgykgratgh gfrhtmstil heqgfdsawi emqlahvdkn
      361 sirgtynhaq yyekrkemmq wysdqmmyal er
//
LOCUS       WP_181561071             274 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: shikimate dehydrogenase family protein [Sphingobium].
ACCESSION   WP_181561071
VERSION     WP_181561071.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 274)
  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 274)
  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 274)
  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..274
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..274
                     /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=28993
     Region          10..268
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 msqgkpyaev igdpiahsks pvihnfwlee lgidaeyrkt rvapeelagy flrrradpdw
       61 lgcnitiphk iaaldyvddp ggvrdrigai ntvacetggp ligtntdagg flqpllargw
      121 sgtsailagt ggaaqaigfa lrsvgvtdlt ivardaakgk alldrlglag rvqgfdaalp
      181 aadllansts lgmvgqpawt pdlsplpdka mvydivyapl etpllaqark rdlmcidgle
      241 mligqaalaf diffdaqppr eldaqlrerl lvpa
//
LOCUS       WP_181562101             413 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_181562101
VERSION     WP_181562101.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=47005
     Region          3..394
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mgkltdkaik aaqpsdkqfk lhdgdglyll ihpngskywr lryfidgkek ltgigkypdm
       61 slkearerty mlkmdvrrgi dpvqakraek aeqvaelaqs feriatdymk hkqgrwsery
      121 sndvksimar dvfpaigskp ingirpadil allqvveqrg aviqarkvrs rimevfnyai
      181 alelcesnpa eklanvlqrp ehghnpflqg deipafldal eryngseiik salwlitftg
      241 crtiearlae wkefdlaagi wsrpashmks krdhvvplpr qaiamlerlk ehtgfcglvf
      301 pgrldlskpi npqslnnaly lmgykdrltp hgirstistl lydagyagnl iesqlshidq
      361 ntvrraynha eyidqrremm qnladwydti rqtgqgepmn rpdtpiqfps lae
//
LOCUS       WP_181562049             212 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Citrobacter freundii].
ACCESSION   WP_181562049
VERSION     WP_181562049.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=22729
     Region          2..>72
                     /region_name="PRK13355"
                     /note="bifunctional HTH-domain containing
                     protein/aminotransferase; Provisional"
                     /db_xref="CDD:237361"
     Region          <59..207
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 msdriarrmk alklksthlm aatgaskgtv sqwvnggtep sarylsklag vlgvserwlt
       61 egglieettg naepgpdlrr rvplissvqa gnwremiqgn wddvtqwiet takvspysfs
      121 lrvsgdsmsa psgsgislpd gsivivdpev eatngrivva ringtnettv kklaidgqni
      181 ylmplnpafq pmqidstcei vgvcvrvemd ll
//
LOCUS       WP_181560714             779 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: prolyl oligopeptidase family serine peptidase
            [Sphingobium].
ACCESSION   WP_181560714
VERSION     WP_181560714.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 779)
  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 779)
  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 779)
  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 779)
  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 779)
  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..779
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..779
                     /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=84636
     Region          66..746
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mlavsfrlpv aalllafltl paqaqpgaaa aedaavvitt daaaglavds aakpgllrtg
       61 paprlpalsy pqarrldlte thfgvpvadp yrwlegdprh dadvqawiaa enettfryle
      121 slpgrealra rmatlhgfer fgnprkager yfytrskgen fspiymregv ngaerllidp
      181 nrlstdgava laewlpsrdg ralllalqer gsdwrtvrvl dvesgalmpd qvawvrysal
      241 awnhegngfy yarfaapteg grdpsfenqq vwfhalgteq aqdrlvyarp drprllhrae
      301 vtadgrwlli sskmgteqta elvlipltvp darpvtlvrg lrnawqmigq lgdrlyfrtd
      361 akapngrivt idaghprrrp vevvaeraqt laggsmiggr lvlayivdgr ivaeitdlag
      421 krqgdvplpg lgaaagfsgr pgdpetfyaf ssftqpptiy rfnvetgets ifarsalgfd
      481 padyvteqvf ypardgtavp mfivrrrdla ragmpaptll ygyggfnvaq tpsfsptrfa
      541 wveqggvlai agvrgggefg kawydagrga nkqttfddfi aaaeylkaqg ytganqlaie
      601 grsnggllvg avvnqrpdlf aaalpgvgvm dmlrfdqfta gafwvddygr pdreadfrtl
      661 layspyhnir seadypailv ttadsddrvv pghsfkyaaa lqaaplggrp rlirvdtgtg
      721 hginrptdki vdeyadmysf aaywtgltlr qrpdrssapt esanvgsaai qpaligpvr
//
LOCUS       WP_181561677             273 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Enterobacter hormaechei].
ACCESSION   WP_181561677
VERSION     WP_181561677.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter hormaechei
  ORGANISM  Enterobacter hormaechei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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..273
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         1..273
                     /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=29336
     Region          57..273
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrksvvlllg tfslfagfsh adegddeais akevktlffg hddrtrvtdp teapwdaigq
       61 letasgnlct atlitprlal taghcllmpp egkpdkaial rfvsqigiwr yeihgiegrv
      121 dpslgkrlkp dgdgwivppg aaswdfgliv lryppsgiap lplfdgdkda ltaalkaadr
      181 kvtqsgypvd hldslythtd cvvtgwaqns vlshqcdtlp gdsgsplmlk tvngwqligv
      241 qssapaakdr wradnralav tgfrdrleal aqq
//
LOCUS       WP_181562220             368 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase
            [Enterobacteriaceae].
ACCESSION   WP_181562220
VERSION     WP_181562220.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=42154
     Region          <71..341
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkntfdkara aentsreaie ylerasglsa vstakfdgdm sfssafmlft rlsllitrrr
       61 peiavhcvli hvmphisdvk vsdisrvmvn qlvnplileg kivqgrrvfs lmkqflswca
      121 fqglidtspl ndmslnrvag gakpvprerk ltdaevwvfw nvwdyfnvce gtkwaarlcl
      181 vaarrpdevl rarkdefnlq rdvwnqgtrn ksarqhalpl splmrqcvee lfeygkgsqw
      241 lvpsnkkkgv dtpmskvaia qalrrilerp elmevesftp rdlrrtarsy fpalginqev
      301 arkimnhsle gidrvydrhd ymdemrdaln nfsayiasiv nqtdldeidh kfkgdrlate
      361 lirvnfsq
//
LOCUS       WP_181562408             470 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [Citrobacter freundii].
ACCESSION   WP_181562408
VERSION     WP_181562408.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 470)
  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 470)
  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 470)
  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 470)
  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..470
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..470
                     /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=54352
     Region          9..260
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
     Region          301..326
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          316..432
                     /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"
     Site            order(333,336..337,340..341,343,367,370..371,374..375,
                     377..378,401,404..405,408..409,412)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          333..360
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          365..395
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          400..428
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mipnlpdyar likervglhf dnamedllks alsrrmgerk iadyyeyyeq lrisqvefds
       61 fitlitinet yffresdtld licdkwvprl lqqrsgpvri lsagcssgee ayslaiklhe
      121 qyrdamtqqi eiygcdidpv ilakarnasy ssysfrgvea siqqryftrs gnlyrlhdei
      181 rekvsfhrsn ivkeqllpgv diillrnvsi yfdtptrrel hanllkmlqp qgalffgnae
      241 tlannfdilk leqeegifyf cphreaarsa pvprlavrvs ppktslryap dellapqcdd
      301 wltkaracld ekcfseakkc iacvlrddpr nqdalliqgv ialeqrefsq tagnaqkila
      361 qdewsaeakm llglatmwqh qtqqaiawfk qvvyqepgyw pahyylaemy rqselrqpaq
      421 rtyrvvmrll ndeinnpfsv crlrlpmvfp gntfrflceh qlaqfahqsg
//
LOCUS       WP_181562120             230 aa            linear   BCT 28-DEC-2024
DEFINITION  XRE family transcriptional regulator [Citrobacter freundii].
ACCESSION   WP_181562120
VERSION     WP_181562120.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii 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="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..230
                     /product="XRE family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25178
     Region          1..65
                     /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 mnignrirel rtakglkiad laeaigvdga nisrvetgkq ksfteqslsk yaqalgvsva
       61 dlftpggnkt tvceysgsnp hsgdgsvfrv eildvsasag ggfiqgsdii dvirsieynn
      121 eralamfggr tadqvkvinv rgdsmaetie pgdllfvdis ihefdgdgiy vfgfddkiyv
      181 krlqmipdkl lvisdnpkyr ewsvdetneh rfyifgkvmi sqsqsfkrha
//
LOCUS       WP_181562527             251 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Micromonospora noduli].
ACCESSION   WP_181562527
VERSION     WP_181562527.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora noduli
  ORGANISM  Micromonospora noduli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 251)
  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..251
                     /organism="Micromonospora noduli"
                     /db_xref="taxon:709876"
     Protein         1..251
                     /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=26044
     Region          64..247
                     /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 mdsvrspewp vaplggvaan saaarygmsp gtgpivgras ppatapppyr pssdagsisp
       61 tgkpaappip vkilvaggfg vgktttvgai seiaplttea emttagigvd dpgarstktt
      121 ttvamdfgcv tidrslklyl fgtpgqtrfg fmwddlarga lgalvvvdsa rlddcfpaid
      181 fferaglpfv vgvnafdgrl alelgeirwa laigdhvplv qfdardrlsv rdallvvldr
      241 aldratrdrr a
//
LOCUS       WP_181562654             326 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora noduli].
ACCESSION   WP_181562654
VERSION     WP_181562654.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora noduli
  ORGANISM  Micromonospora noduli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 326)
  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 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
REFERENCE   4  (residues 1 to 326)
  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..326
                     /organism="Micromonospora noduli"
                     /db_xref="taxon:709876"
     Protein         1..326
                     /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=35837
     Region          96..325
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          237..324
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mldgtvysgs hwqryataet deahdyirra ffdvkvrfag gsrdgaglrt ittrltdigv
       61 trlhysartq vqtapdgdlt tthlmsgrfm iarnkdeyrl rpgdvvlmlp dqpqeaefdd
      121 vdsfttrlpr alleeaahaq tgisgadlrf dssrpisaal grhwtqtlsh ltrsvlcdpa
      181 lmanplvvgn trhllaatal avfpntahgp alraagevtp ralrravtyv ddhadqpitl
      241 dqvaaaagvr pralqlafrr hhdttpmryv rqvrlerahc dlqagspttg vtvamiatrw
      301 gfthlgrfst dyraaygcsp shtlrt
//
LOCUS       WP_181562950             331 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Campylobacter hyointestinalis].
ACCESSION   WP_181562950
VERSION     WP_181562950.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter hyointestinalis
  ORGANISM  Campylobacter hyointestinalis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 331)
  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 331)
  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..331
                     /organism="Campylobacter hyointestinalis"
                     /db_xref="taxon:198"
     Protein         1..331
                     /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=37228
     Region          28..331
                     /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 melleqnetk hiqdglknli eqtyliekey ktlnesyisl qnfiqdives lgaalwvvdm
       61 sgnillknak tngfdailnl idlkranqei elenrhfaik ittkeqnkii latdisdekr
      121 sarlvsmgav aahlsheirn pigsisllts tllkradekn rpiideiqka ifrveriika
      181 tllftkgvhi nkqsfslekl eqnchiaisq yafskeiefk fsgfkgeilg didlldmvfs
      241 nlifnaidai eedenssgqv tlehvfknds hvfyisdsgv eidksvvfep fkttklkgng
      301 lglalsieii hahkgsicfq nkpkiftisl p
//
LOCUS       WP_181562797             409 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome b [Helicobacter sp. 10-6591].
ACCESSION   WP_181562797
VERSION     WP_181562797.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter sp. 10-6591
  ORGANISM  Helicobacter sp. 10-6591
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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..409
                     /organism="Helicobacter sp. 10-6591"
                     /db_xref="taxon:2004998"
     Protein         1..409
                     /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=47250
     Region          1..408
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mmevkkadnl vdwldqrlav rklievlmtk ywipkkinfl wamgvillal ftllvvsglf
       61 llmyykpdtk lafdsvndti mrevafgwlw rhihavaasm vfliiyihmm vaiyygsykr
      121 grefvwiggm llfvlfsaea fsgymlpwgq msfwaaavit nlpsalpvig pdlvewvrgn
      181 fvvadstltr ffmlhvcllp ivilmviglh fytlriphvn nqegeeidfe aeakkyeegk
      241 kkeskvisfw pdflckdifi lsvfmmlffy lvcyhfdfam dpinfdpann lktpahiype
      301 wyflwsyevl rgfffsadlg lmafgiaqva flflpwldrs ptvapahkrs gyfiwfwvli
      361 idlvvltifg klppeginnq iglvaalgfl vwifialpvi timernkgh
//
LOCUS       WP_181562810             442 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Helicobacter sp. 10-6591].
ACCESSION   WP_181562810
VERSION     WP_181562810.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter sp. 10-6591
  ORGANISM  Helicobacter sp. 10-6591
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 442)
  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..442
                     /organism="Helicobacter sp. 10-6591"
                     /db_xref="taxon:2004998"
     Protein         1..442
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49829
     Region          29..442
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mlgyrvvrii qiaiigglms vcmsagvipk hyeqvlengl qvvvvpldnk ssvievdviy
       61 kvgsrneikg ksgiahmleh lnfkstknlr agefdeivks fggvdnayts fdytkyyirt
      121 tnknldksle lfsevmqnlt lvdsefqper dvvfqerlwr tdnnpigfly fkffntafqt
      181 hpyhwtpigf kddilswkle divdfhklyy qpqnaivlvt gdiqpedvfa nvkkyfssik
      241 nttdsvpqvv pqepkqiker niviekesev dylamgykip dfahkdqval saiskilsgg
      301 ksslfasdlv dkkqlassis aynmelkddg iffimalatp gvnantlkee ivailerikk
      361 gqiesselek vkidtkaafv ygfenaasta rvfgdylakg dlaplfsfee dikaldiqei
      421 arvarkyfqt dslstaiiht kk
//
LOCUS       WP_181562500             919 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora noduli].
ACCESSION   WP_181562500
VERSION     WP_181562500.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora noduli
  ORGANISM  Micromonospora noduli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 919)
  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 919)
  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 919)
  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 919)
  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..919
                     /organism="Micromonospora noduli"
                     /db_xref="taxon:709876"
     Protein         1..919
                     /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=99130
     Region          2..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          113..917
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          711..736
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          748..776
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          788..816
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(789,792..793,796..797,799,829,832..833,836..837,
                     839..840,869,872..873,876..877,880)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          821..857
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          868..896
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mavrfgllgd vvatvddrpv algharqqcv laallvdvnr avsvdqlidr vwgqsppqra
       61 rdtlygylyr lrrsladvpd aaitrrsggy lmaademavd lhrfrhlrde araerseddr
      121 lalfdqalgl wrgdpfsgld afwldtvrtd leqekltael ervdaalslg hhdgvladls
      181 rlvsgqplne rlagqmmlal sgagrsaeal ehyrrfrnll vdelgvepsl hlqqlhrsil
      241 apdvaadppq tgspvprqlp mpsgsftgrs ddlaqldaal ltygettgta vavsgtggig
      301 ktwlalhwaa thldrypdgq lfvnlsgfhp teppmtpaga vraildaldv apnavpadld
      361 sqiglyrslv adrrmlivld dardpdqvrp llpgsascav vvtsrnqmsg lvateglrpl
      421 plgclsrdea lhllagrlgr drlsteadaa gsivgacagl plalsivaar aatnpalslq
      481 dladeladqq hgldaladrd avadvrsvia asyralsapa aalfrllaly agpdvslpav
      541 aglvglpvqq vrepldellg ahlvdltgpd ryachdllra yagellddse rasatrrlyd
      601 hwlhgahaaa ltiephrdhi dlpppaagta vasftdseqa qlwldaerlv llaaidqaae
      661 fgldghawrl awavatylsr lsrwtdlasa qraavtaarr agdlvgeahg hrdlglalhq
      721 lgelangldh lrragelfgr lgdrageayv alylgwvheg qgqhrealec deralvlfge
      781 vghlvgraka lnaigwdhar lgdhhraadh crralalhee vgnvtgaakt wdslgyvhhq
      841 rgdsdkacvc yrralelyeq sddrwgvaet ltrlgdvlhd agdveaarsn wlralrqlne
      901 dnpveiaelr hrldsagsp
//
LOCUS       WP_181565423             349 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Aerococcus].
ACCESSION   WP_181565423
VERSION     WP_181565423.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
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="Aerococcus"
                     /db_xref="taxon:1375"
     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=36650
     Region          28..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 mskqpnrpwi lvlaavlvli lgitmtisiy vgsvdlvasd vgkiiinrls qaeifpvtwq
       61 asaetivwdl rlpktlvaal tgmglslaga lmqtlthnpm adpyllgiss gastgavlsi
      121 lvgtvpvigy lplevgaflg allatglvfl isgkqgklst ihliltgval salfsaltsi
      181 iifltpdvra issalfwmsg sfsgiswkdv apvaiavlls slilflihqp ldllllgddr
      241 armnginvfa lkslifvits lltailvaks gvigfvglvi phitrllvgp thrrlllvap
      301 lagailmvva dtvsrvvfsp eelpvgivta lvgapffifl mqrskdkla
//
LOCUS       WP_181565430             258 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Aerococcus].
ACCESSION   WP_181565430
VERSION     WP_181565430.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
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"
                     /db_xref="taxon:1375"
     Protein         1..258
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29507
     Region          2..256
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mtllqttlys dslrmdvhvn iifpqncart pedkrqslkp pyrvlyllhg lssnedgwlr
       61 ftsleryard ldlvivlptt hrgwyinnai gypysnfisv elpeiiqtml pvstkredty
      121 iagasmggfg alkaaftype kygyvaslsg vtdlvnvfaq gpdpespfeh qmlfdeespa
      181 ktdndiyylv qqaidnkidl pkvyltcgte ddlieqnrhf kdrfgdvlel syhenpgehg
      241 wdywdpeikk vldwlpti
//
LOCUS       WP_181565496             365 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Paraburkholderia unamae].
ACCESSION   WP_181565496
VERSION     WP_181565496.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia unamae
  ORGANISM  Paraburkholderia unamae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 365)
  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 365)
  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..365
                     /organism="Paraburkholderia unamae"
                     /db_xref="taxon:219649"
     Protein         1..365
                     /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=41288
     Region          1..365
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mipvtiltgf lgsgkttllk rilnekhgmk iavienefge enidneilvq dsteqiiqms
       61 ngcicctirg dlarvlgdla qqkrdgkldf drvviettgl anpgpvaqtf fmdneiadef
      121 lldaiitlvd akhgnhqlde hevvqrqvgf adrifitkad lvdekeladl rhrvlhmnpk
      181 aqirqvnfge adikevfdlr gfnlnaklei dpdflaeddh ahhdhdhdhd hahdhahded
      241 hadcdhdhgk ctheghdhgh hhhahhddki ksfvyrsdrp fdpnrledfl ggilqiyger
      301 llrykgvlym kgvdrkvvfq gvhqmmgsdl aakwlpiekk nskmvfigie lpqdlitdgl
      361 dacla
//
LOCUS       WP_181565456             639 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Aerococcus].
ACCESSION   WP_181565456
VERSION     WP_181565456.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
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="Aerococcus"
                     /db_xref="taxon:1375"
     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=73898
     Region          8..638
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnsrqlkllk smlsehsyqp asyyakrmsv sartiysdld iinefikkng gevqrkpsag
       61 vkivgdisii qtnllssnll dcdiydpsnr rliiikllaf tnqdisldyl seafivskts
      121 iykdihvlne iidgtdsyie sskhglvlig neetlqkaik aivfyfsnne sdlsftqvik
      181 llfdeesiqy vdsllkdeid gfardasnyy yrslvsvlli hlsriqidhq iqsqeellld
      241 sikylevypi aeslvnklsq tfeieyqied ktyitrqlya hriqknivni ddniknsvki
      301 linevsmied inlmedrhll fslyqhfppm lmrlekgiqi enplldsiki qymelfsilw
      361 yllgdfekky nvslndhevs lilihfqial ekqsesknil iicqygmssa qliyqkvkri
      421 lpnqdnieia nanklhkvnl knvdliitti dlgdfkrnyi kvspifssqd yksilnaysl
      481 llseqnnysp sekikaptll efmnkdlinl hidstskeel ldfmitqleq kkmvkkefrq
      541 sifereklgd tnlengialp hanpntvies sisfttlnkp ikwgkgkvql ivmitfndqd
      601 tnkiklviee lfpvinnkkl vdelleikdk tqwinrfin
//
LOCUS       WP_181565590            1758 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Paraburkholderia
            unamae].
ACCESSION   WP_181565590
VERSION     WP_181565590.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia unamae
  ORGANISM  Paraburkholderia unamae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1758
                     /organism="Paraburkholderia unamae"
                     /db_xref="taxon:219649"
     Protein         <1..1758
                     /product="beta strand repeat-containing protein"
     Region          11..1685
                     /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 sniqnvvlqt agnaggtasf dtsnisgvtn ltvksagnge dnvkaaattn invthlstqd
       61 ggldagvvva ggnnvtvnta agnvdvgntt ianvnptgav nvtaantgtv nvfggttvtv
      121 ndagqnstvn vgvngtavsp septgavsvn atgsgttvnv fggtdvsvst vggnavdagg
      181 vniggvaant vyaptgnvtv nvneakayak dyltgvtsgy qsnvsvlgga nvsvttnagn
      241 vtiggiavda agkllagena tgtvtvtets nvsrvnvygg tdvtvnaagg avhvgnvagt
      301 vvatpsgavt inntasaayd givntnngfv aveggtdvnv ttnaggvrvg sssgtagaqp
      361 tgsvtvtdtt agfvgvfggs dvtvssaggl vivgndnaga stkgdvsvtq savetggqyt
      421 nnsavnvagg dnvtvnttgg nvtvgseatp ttgavsitdt yvgynvdnft vvggttvait
      481 ttatdgdidv gnvtavidsv tgalknasdy asgnvtivne skagtsaaga snvygtgdts
      541 vttngatsvs itggesatit diqtqltkgv stlsnvtldh vegnstitsd altsltvlng
      601 isgyeytidn ttkghdlslt iggdapvfgv dtiidttaga vtladngvas grvdlqldta
      661 tsvtvnttaa vnltvdagan lttvtlnnta alnlsvdgat slasidasaa tggvtvevdp
      721 tltsfkggag ndvvtidsns llhadettys tisggagnnt lvanyaaqtt dtalgsnshi
      781 sgfttlalge saksdnhtgs vyvagtptvt gvaqvstitf dqvtyntdgn vsedvyftit
      841 vganvynisp aistgetaaa lasavasail sqgiqgfsvg vsngvvtvtg pangtafsis
      901 tpvilagsgd lpptvatpta pvaavtgtpa dasydasgft alqvgqttgd vaftkvaagt
      961 tldvtasqgn gaivnyllan stgskdalsl tvgvdgaags ngvtttvatt gietlnitse
     1021 gaakslntvt igdtgatsiv lngdanialt lktdnlgasa tgvtkvdasa atgavnlsgv
     1081 elsstgstvt ggaglltvag gadsghsdvi ttgtgggvit igdggnwtga aygagsetvd
     1141 ltasasavdt lvvgentvat fngstggvkg feitssaktt drlaivssgs avnvvanaal
     1201 qnasvaglay tisngivtfs gagthninef satdliaaaq aiasgawalg satvlafvag
     1261 gntyvvsaeg nalndtsvte lvgvtgvagf gttaagntiv lantvtsetn vldvatvgak
     1321 tlsydetgfa ravlnttsvd vaatsvslsn laasavlevn adlsnvavst tqlgtsgsds
     1381 lsiqfdsaet iksltvsgdn alaihtsgad vittltdatn tvasitvdga gslsiatltd
     1441 talksfdash lvgtlaltas qdgltilgsv agdvikatga adtitvgsat aaaigavsit
     1501 asgaadaisl ttqsavstnh viqaagagdt itlngghfdn vylggtvngs nvattalghg
     1561 dtlnlfgtat dsvwlggsst vnlgsatnyf ggtanlsvqg dvtgaassgs faqtlinvnn
     1621 adatvnlafn nattyeglag nsataaqvnv asatslsqal dlaikqalvt dyqangsshv
     1681 slvngvleln antglvstfq yagntyvvea vnntnaaaah aalgandvvv eitgtstvss
     1741 vgfsghtlsa hlnagspa
//
LOCUS       WP_181565534             496 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Aerococcus].
ACCESSION   WP_181565534
VERSION     WP_181565534.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
REFERENCE   1  (residues 1 to 496)
  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 496)
  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..496
                     /organism="Aerococcus"
                     /db_xref="taxon:1375"
     Protein         1..496
                     /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=58154
     Region          11..>494
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mdkkivrirk lifylldrke ivtakelady lnvsqktiyr lvreinehnr nkplieshkg
       61 igyrlnysny ieldsqllkv dqsspklrqq nilkdllsas pnsipiykly ekyyvsdsvi
      121 stdsyeiqky isqfnlnlvr nqgllsiegs esdirkiieq vykrysvhdl skirkeyqel
      181 gfnrfdisfi akqiqqiede ldtvipvpyd inifthlyil iertkkgqft eqlseelvns
      241 egdwiqekri ylvaksvikn ienylnitvs tsevyylyqy lvssridyns smnaqyskkv
      301 idvteyyleh vtqelhipnk stqffnelan hikpminrlk ndiyiensll dqiklsypqi
      361 fsavkkvsqe vsdtfslrki ddnengficl yfarvlednk eriktiimct tgigtsellr
      421 vkvennfpei evidvvserv lkqrfkdsrt aidlllttik tdsipgvrtl lvssllnsed
      481 kfrirevise iyeskf
//
LOCUS       WP_181565871             331 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Campylobacter hyointestinalis].
ACCESSION   WP_181565871
VERSION     WP_181565871.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter hyointestinalis
  ORGANISM  Campylobacter hyointestinalis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 331)
  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 331)
  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..331
                     /organism="Campylobacter hyointestinalis"
                     /db_xref="taxon:198"
     Protein         1..331
                     /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=37311
     Region          28..331
                     /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 melleqnetk hiqdglknli eqtyliekey ktlnesyisl qnfiqdives lgaalwvvdm
       61 sgnillknak tngfdailnl idlkranqei elenrhfaik ittkeqnkii latdisdekr
      121 sarlvsmgav aahlsheirn pigsisllts tllkradekn rpiideiqka ifrveriika
      181 tllftkgvhi nkqrfslekl eqnchiaisq yafskeiefk fsgfkgeilg didlldmvfs
      241 nlifnaidai eedenssgqv tlehifknds hvfyisdsgv eidksvvfep fkttklkgng
      301 lglalsieii hahkgsicfq nkpkiftisl p
//
LOCUS       WP_181565972             403 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Aerococcus urinae].
ACCESSION   WP_181565972
VERSION     WP_181565972.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
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="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..403
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44897
     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 mniqlldgvk vidfstmvaa pttarvmadw gadvlkveap sgdqlrgtga tmnvtatede
       61 npifetdnln kkgitlnlks eegyqimmql leeadvfisn irihsleklg lgyetlkakf
      121 phliwghfsg ygtkgeeahr pgydvvgywa rggfmaslap vnhppisaps gvgdsvagls
      181 llsgilaall kqrqtgqgee vrvsllgsai fcnkmmivss qyedhypkdr mhpnnpflqs
      241 yqtkdgewim lclvryesef prfmkiigle eyiddesvnt ldafqknpkq sefvkqveaa
      301 ignmesqdli nkmlaedftf eraqtfdeip ndkqawanny lenmefgkdg krvampaspv
      361 qfsddkkkpf nhaprlgehn qeiltdlgys eediqslkek gvi
//
LOCUS       WP_181566243             349 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Aerococcus].
ACCESSION   WP_181566243
VERSION     WP_181566243.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
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="Aerococcus"
                     /db_xref="taxon:1375"
     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=36694
     Region          28..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 mskqpkrpwi lvlaaglvli lgitmtisiy vgsvdlvasd vgkiiinrls qaeifpvtwq
       61 asaetivwdl rlpktlvaal tgmglslaga lmqtlthnpm adpyllgiss gastgavlsi
      121 lvgtlpvigy lplevgaflg allatdlvfl isgkqgklst ihliltgval salfsaltsi
      181 iifltpdvra issalfwmsg sfsgiswkdv apvaiavlls slilflihqp ldllllgddr
      241 armnginvfa lkslifvits lltailvaks gvigfvglvi phitrllvgp thrrlllvap
      301 lagailmvva dtvsrvvfsp eelpvgivta lvgapffifl mqrskdkla
//
LOCUS       WP_181566439             332 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [Aerococcus].
ACCESSION   WP_181566439
VERSION     WP_181566439.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..332
                     /organism="Aerococcus"
                     /db_xref="taxon:1375"
     Protein         1..332
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36688
     Region          80..320
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtikklllll mtgllfacgq kpgsttpeqa sqedqteskp pqteqkdetq pasdqateld
       61 qltvlsqted yvqyelnvmr dgfkihgklf lpkgdqeswp ltilahginq tdltttpyat
      121 hlakrgvaay vfdfiggapl nssdgdfsdm tvlteladle aiyqkltnyk aidsnetyll
      181 gdsqgglvat mmaakhpedi qgmillypaf nmpslvhdfv pdkeeipdsi dimgvsvsry
      241 yiedmlkvdv edittsypgp vlivhgeddv lvppvyaqka aelfpkahle mipggkhefs
      301 gsdfikalsy idkfmvnqlg dehyqltide ee
//
LOCUS       WP_181566647            1427 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Escherichia coli].
ACCESSION   WP_181566647
VERSION     WP_181566647.1
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 both ends.
FEATURES             Location/Qualifiers
     source          1..1427
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>1427
                     /product="beta strand repeat-containing protein"
     Region          6..1425
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          15..34
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          36..54
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          56..72
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          74..93
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          96..113
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          115..131
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          133..151
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          154..172
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          174..192
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          194..212
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          214..230
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          232..250
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          269..288
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          290..307
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          309..328
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          330..347
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          348..366
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          368..384
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          390..408
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          410..429
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          431..448
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          972..990
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          992..1012
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          1014..1033
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          1082..1101
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          1103..1121
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
ORIGIN      
        1 gkrvlitads lansgaiqaa dsltarltge lvstagskvt sngemalsal nlsnsgqwia
       61 knltlkansl tsagditgvd tltltvnqtl nnqangklls agvltlkads vtndgqlqgn
      121 vttitagqlt ngghlqgetl tltasggvnn rsggvlmsrn alnvstatls nqstiqgggg
      181 vslnatdrlq ndgkilsgsn ltltaqvlan tgsglvqaat llldvvntvn ggrvlatgsa
      241 dvkgttlnnt gtlqgadllv nyhtfsnsgt llgtsglgvk gssllqngtg rlysagnlll
      301 daqdfsgqgq vvatgdvtlk liaaltnhgt laagktlsvt sqnaitnggv mqgdamvlga
      361 geaftnngtl tagkgnsvfs aqrlflnapg slqgggdvsl nsrsditisg ftgtagsltm
      421 nvagtllnsa liyagnnlkl ftdrlhnqhg dilagnslwv qkdasggant eiinnsgnie
      481 thqgdivvrt ghllnqregf sattttrtnp ssiqgmgnal vdiplsllpd gsygyftrev
      541 enqhgtpcng hgacnitmdt lyyyapfads atqrflssqn ittvtgadnp agriasgrnl
      601 saeaerlenr asfilangdi alsgrelsnq swqtgteney lvyrydpktf ygsyatgsld
      661 klpllspefe nntirfsldg rekdytpgkt yysviqaggd vktrftssin ngtttahags
      721 vspvvsapvl ntlsqqtggd sltqtalqqy epvvvgspqw hdelagalkn iaggspltgq
      781 tgisddwplp sgnngylvps tdpdspylit vnpkldglgq vdshlfagly ellgakpgqa
      841 pretapsytd ekqflgssyf ldrlglkpek dyrflgdavf dtryvsnavl srtgsrylng
      901 lgsdteqmry lmdnaarqqk glglefgval taeqiaqldg silwwesvti ngqtvmvpkl
      961 ylspeditlh ngsvisgnnv qlaggnitns ggsinaqndl sldssgyidn lnaglisagg
     1021 sldlsaigdi snissvisgk tvqlesvsgn isnitrrqqw nagsdsqygg vhlsgtdtgp
     1081 vatikgtdsl sldagknidi tgatvssggd lgmsagndin iaanlisgsk sqsgfwhtdd
     1141 nssssttsqg ssisaggnla maaghnldvt assvsaghsa llsagndlsl navresknsr
     1201 ngrseshesh aavstvtagd nfllvagrdi asqaagmaae nnvvirggrd vnlvaesaga
     1261 gdsytskkkk einetvrqqg teiasggdtt vnagrditav assvtatgni svnagrdval
     1321 ttatesdyhy letkkksggf lskkttrtis edsatreags llsgnrvtvn agdnltvegs
     1381 dvvadrdvsl aagnhvdvla atstdtswrf ketkksgltg tggigft
//
LOCUS       WP_181566568             328 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein, partial [Helicobacter sp.
            11-8110].
ACCESSION   WP_181566568
VERSION     WP_181566568.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter sp. 11-8110
  ORGANISM  Helicobacter sp. 11-8110
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..328
                     /organism="Helicobacter sp. 11-8110"
                     /db_xref="taxon:2004997"
     Protein         1..>328
                     /product="coiled-coil domain-containing protein"
     Region          274..>328
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mrvalhfvgh lrtfretypk lmenvinpnv lrgceisvfm htwdvwsttn yvtsryrfyc
       61 nldlnekkid dedvkwlnqi yglkaikiek qnknihsdvr kikdelmdvr gyslaevcrl
      121 reeyskenni kydffmfmrp dilcvqplil snyidkvlkd gfftlaasnv frrqtafgns
      181 visdprfyde cdliwisnyg dadfwgrfas sshrfnrndl smnvpimidy rlgrdffilr
      241 ststkedyip freiddkeyk klcdnlerne lvtkeltskt qqliqtknql dtikvqldst
      301 knqlnsaqke ldstkqqlds kvkelssl
//
LOCUS       WP_181566858             342 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Bacillus].
ACCESSION   WP_181566858
VERSION     WP_181566858.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
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="Bacillus"
                     /db_xref="taxon:1386"
     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=36008
     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 mqdkrkpqqk rsshilffli fflaviglaa amffavsyga ktlslqtvwt avfdyqsnvt
       61 eqqiihelrl prvlgaalvg aafavagalm qgitrnplad agilgingga mfvvalcfaf
      121 fpgmpysalm ffsfigavls tllifaigaa ggvltplrlt vagavvaall halssgiaiy
      181 fdlsqdlafw yaggvagvkw pqltiltpvi livivwamll grslsllslg edtaanlgvk
      241 trqvrilgma aavllagvsv savgsigfvg lviphiarkl vgvdyrfvip msailgamll
      301 vfadlasrtv npprelaigv mvalvgvpff lyiarkegrn ls
//
LOCUS       WP_181566013             226 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Aerococcus].
ACCESSION   WP_181566013
VERSION     WP_181566013.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
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="Aerococcus"
                     /db_xref="taxon:1375"
     Protein         1..226
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25384
     Region          7..220
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mktelkqikl vifdldgtlv dtekiyqagw rtvlkdynts isqdqlekmr ggtrqhnnrl
       61 iqeilggdet lakearekrn ayfqavikqg kidlkagavd lldhlkvagl slavatsspl
      121 drgkdileis glmpyfdfvi ygnqiehgkp qpdiylkvle hfqvrsqeav viedslngll
      181 assraklatf yvpeiplrdg efdqvdeqyv igvynsliev kdvfdk
//
LOCUS       WP_181566504             496 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Aerococcus].
ACCESSION   WP_181566504
VERSION     WP_181566504.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
REFERENCE   1  (residues 1 to 496)
  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 496)
  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..496
                     /organism="Aerococcus"
                     /db_xref="taxon:1375"
     Protein         1..496
                     /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=58155
     Region          11..>494
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mdkkivrirk lifylldrke ivtakelady lnvsqktiyr lvreinehnr nkplieshkg
       61 igyrlnysny ieldsqllkv dqsspklrqq nilkdllsas pnsipiykly ekyyvsdsvi
      121 stdsyeiqky isqfnlnlvr nqgllsiegs esdirkiieq vykrysvhdl skirkeyqel
      181 gfnrfdisfi akqiqqiede ldtvipvpyd inifthlyil iertkkgqft eqlseelvns
      241 egdwiqekri ylvaksvikn iedylnitvs tsevyylyqy lvssridyns smnaqyskkv
      301 idvteyyleh vtqelhipnk stqffnelan hikpminrlk ndiyiensll dqiklsypqi
      361 fsavkkvsqe vsdtfslrki ddnengficl yfarvlednk eriktiimct tgigtsellr
      421 vkvennfpei evidvvserv lkqrfkdsrt aidlllttik tdsipgvrtl lvssllnsed
      481 kfrirevise iyeskf
//
LOCUS       WP_181566600             241 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LysM peptidoglycan-binding domain-containing protein
            [Aerococcus].
ACCESSION   WP_181566600
VERSION     WP_181566600.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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..241
                     /organism="Aerococcus"
                     /db_xref="taxon:1375"
     Protein         1..241
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27039
     Region          196..239
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mafkdnwnqf nnkwkkedpa vkeensdvee feekaeassa deyenlknrq ysrssrnkke
       61 kgvsptvkvl ialgllfili pyaayiiygn qqkqpesmnv dqvmvsksen dsqkqaeees
      121 kkaeeskqae eskkqeesqq aaqasqqaaq earqaaeqsq avqqsqqqva aqeqsrqqas
      181 rnqnqqntnq nqnvgsyqvs agdnlyriav nhgmtlnqll elnglhansp iapgtvlrvy
      241 q
//
LOCUS       WP_181567487             124 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora robiginosa].
ACCESSION   WP_181567487
VERSION     WP_181567487.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=13070
     Region          24..112
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 megvgtakta ampsisplag epikradaer lagvlkafad parlrllsli qsapqgeasv
       61 sdltaplgls qptvshhlri lteagllere krgvwayyrv vpsaiaaiad lltpprkrat
      121 krar
//
LOCUS       WP_181567499             107 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor
            [Micromonospora].
ACCESSION   WP_181567499
VERSION     WP_181567499.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
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="Micromonospora"
                     /db_xref="taxon:1873"
     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=11982
     Region          2..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpdldlafaa lgdpvrralv trlargeatv gelaepfdlt pqaishhvgv lrrcglveqr
       61 regtrrpcrl radqlallgt wideqrrawh drldaldehl tdedpar
//
LOCUS       WP_181566949             463 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Faecalibacterium
            prausnitzii].
ACCESSION   WP_181566949
VERSION     WP_181566949.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacterium prausnitzii
  ORGANISM  Faecalibacterium prausnitzii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Faecalibacterium.
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="Faecalibacterium prausnitzii"
                     /db_xref="taxon:853"
     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=49247
     Region          1..463
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mlvtliesvy nflwgdlltl plggvtlnls lmvillftag iyftlrtrll pmrlfrdmld
       61 avcekkqgkq gglsslqtlv vstatrvgmg nlvgvvaavs vggagavfwm wvtallgast
      121 sfvestlaqk ykepdplygg wrggpafylh klaerkrgkl lkksvvaslf avsglicwcg
      181 isqvisnsvs eafsnafsip plmttlalta laavivlrkd atvksldviv pimagcyflm
      241 tlyvvftnlp qlpgvlarif seafglrqaa aggfgavvmn gvkrglfsne agsgsapcaa
      301 aaaecddpvk mglvqalgvl idtivicsct afvmllvpes vtaglqgmnl lqaamqyhlg
      361 gfgvvfiavt lalfsfstfi gilfyarcnv aylfgdhwgw qtaykllala mmlvggvaay
      421 tvvwdlgdvg iglmtifnmi alyplsgeal talqeyekkk hlk
//
LOCUS       WP_181567150             463 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Faecalibacterium
            prausnitzii].
ACCESSION   WP_181567150
VERSION     WP_181567150.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacterium prausnitzii
  ORGANISM  Faecalibacterium prausnitzii
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Faecalibacterium.
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="Faecalibacterium prausnitzii"
                     /db_xref="taxon:853"
     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=49187
     Region          1..463
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mlvtliesvy nflwgdlltl plggvtlnls lmvillftag iyftlrtrll pmrlfrdmld
       61 avcekkqgkq gglsslqtlv vstatrvgmg nlvgvvaavs vggagavfwm wvtallgast
      121 sfvestlaqk ykepdplygg wrggpafylh klaerkrgkl lkksvvaslf avsglicwcg
      181 isqvisnsvs eafsnafsip plvttlalta laavivlrkd atvksldviv pimagcyflm
      241 tlyvvftnlp qlpgvlarif seafglrqaa aggfgavvmn gvkrglfsne agsgsapcaa
      301 aaaecddpvk mglvqalgvl idtivicsct afvmllapes vtaglqgmnl lqaamqyhlg
      361 gfgvvfiavt lalfsfstfi gilfyarcnv aylfgdhwgw qtaykllala mmlvggvaay
      421 tvvwdlgdvg iglmtifnmi alyplsgeal talqeyekkk hlk
//
LOCUS       WP_181567590             478 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora robiginosa].
ACCESSION   WP_181567590
VERSION     WP_181567590.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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   4  (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   5  (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   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 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..478
                     /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=50751
     Region          153..452
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrrlvisyl llmvlvlval etplavtlas retdrvradr ladatrfasl agpalrggsp
       61 gplggelaay ddlyrigaav vdrdrrtvaa sarwdpgggt gtavdtalsg qqfsgpesvw
      121 pwedgplvta vpindggevl gavvtttptg pvrrtvtvww lllaglgllt vlacvstafg
      181 lagwvlrpvt eldtatheia egrrtarvrp rlgppelrrl atsfndmvda vsdvmdrqra
      241 fvahashqlr npltalrlrv eelgpsltdp dgraehrlal eetdrlatvl dalltlarae
      301 reenqrvtvd aaaaaesrva awlplarhrs vtlrldadea pahartvpta idqaldalid
      361 navkfsgagg evtvtvrrvd ggteltvrdt gpgmtasqid qaterfwrap dvqnvdgagl
      421 gltiaavlvd asdgrltmrq geprglvael wfpappaepa dpddraaape rhgepvgg
//
LOCUS       WP_181566931             108 aa            linear   BCT 28-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Klebsiella
            pneumoniae].
ACCESSION   WP_181566931
VERSION     WP_181566931.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 108)
  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 108)
  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 108)
  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..108
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..108
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=12043
     Region          1..>105
                     /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 mvpvqggefl mgdfgplvge klpfsiqqdd ktlhkvilsd fsiskykvtn ddfnvylkvt
       61 dkknppvdil akrhpsllkg dypagviwqq akdycqwlga llnksnfc
//
LOCUS       WP_181567603             443 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Micromonospora robiginosa].
ACCESSION   WP_181567603
VERSION     WP_181567603.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=46157
     Region          165..368
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mvmiggrvpt aaggpigler tppqataasa vvravavval lnfdlfprlv grgllitavv
       61 lavplllhdi lsgqsrarmv vcavlttfgi lalppilepp qteygqqkff llvtltmfaa
      121 lavavlrgrr dveafaavfv vsglvlavaa lvgdpengra tgfganpiwv araiggaiva
      181 liwlslkkrl svwwtagaaa llllglfatg srgpllaavv alfvlvlagl rlkirrtrre
      241 wvglglmgal vvtvialpsl lpprvyafvv dpseelhgsa raamrdvtlp miaehpggvg
      301 vgnwsyyadm pmhnyphnlw lelpaesgww vagafalavv vvavglwrss rrdpaagfal
      361 alvtfyavav stsgdingdr plfaalalgv lvlagatrat srrpgvpstr hpavggadas
      421 wrlvplagea garrqtgpsk vvg
//
LOCUS       WP_181566520             169 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NuoB/complex I 20 kDa subunit family protein
            [Helicobacter].
ACCESSION   WP_181566520
VERSION     WP_181566520.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter
  ORGANISM  Helicobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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 169)
  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 169)
  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 169)
  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..169
                     /organism="Helicobacter"
                     /db_xref="taxon:209"
     Protein         1..169
                     /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=19013
     Region          1..160
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 maehevdylr hkglpialss vdklvnwgrs nslwamtygl accaiemmat gasrydfdrf
       61 gtifrasprq sdvmiiagtv tkkhaqfvrr lydqmpepkw vismgscant ggmfntyatv
      121 qgvdriipvd iylpgcsprp etlqyalmvl qqkirkqkan hkkmpkrli
//
LOCUS       WP_181567613             352 aa            linear   BCT 28-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Micromonospora
            robiginosa].
ACCESSION   WP_181567613
VERSION     WP_181567613.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 352)
  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 352)
  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..352
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..352
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=38129
     Region          1..333
                     /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 mtvtvdvtda gpidpatdsr rpdvyftsgy geavaadgsg swrlahhddd lvllpyllrp
       61 lgddaadavs pygycgihva pecrpsdlva fwsalgdrwr aegvvslflr fspldpasvd
      121 avrgldgmsl trradtvtvp vratpteiwd dmegrsrtai rkarrggmhg tvrpaeaedv
      181 aaaspfrqly estmtrvgsa agyffpeayy rrlltglgps lllaevrdgt savvaaalvl
      241 rhggrvhyhl agsrpeaare gannmlvwti lewaaetgad vvhlggglqa ddnlfrfkra
      301 fgglrtpfwt gtvildhery drlteeraar lglpaahlrq sgyfpayrfg ga
//
LOCUS       WP_181567638             834 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Micromonospora robiginosa].
ACCESSION   WP_181567638
VERSION     WP_181567638.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 834)
  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 834)
  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..834
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..834
                     /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=92078
     Region          1..821
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtltaalpkt adpdtlydaf aswasergld lyphqeeavi eivsganvim ntptgsgksl
       61 vaiaahfaal addrtsfyta pikalvsekf falcevfgae nvgmltgdas vnadapiicc
      121 taeilanlal regrradvgq vvmdefhfya epdrgwawqv plielpqaqf vlmsatlgdt
      181 trfvddlsrr tgrptavvrs aerpvplifs yattplhetl eelletkqap vyvvhftqaa
      241 aleraqalms vnvctraekd miaqaignfr ftsgfgrtls rlvrhgigvh hagmlpkyrr
      301 lvetlaqagl lkvicgtdtl gvginvpirt vlftglskyd gvrtrllkar efhqiagrag
      361 ragfdtigrv vvqapehvie nekalakagd dpkkrrkvvk kkppegsigw geptfqrlve
      421 aepepltssf qvshsmllnv igrpgdafas mrhlltdnhe dpaaqrrhir raiaiyralr
      481 aggvveelpe pdetgrrvrl tvdlqldfal nqplsplala tielldresp syaldvlsvi
      541 eaildnprqi lsaqqfkarg eavaamkaeg ieyearlell devtwpkpla ellegayemy
      601 rqghpwvadh elapksvvrd myeramtfpe yvqfyglsrs eglvlrylad ayktlrqtvp
      661 edakteelvd liewlgelvr qvdsslidew erlrnpsdva evaaslddrp pavtrnaraf
      721 rvlvrnalfr rvelaalrrw dllgeldage gwhadawada lepyfdayds igvgpdargp
      781 allmieqgre rwtvrqildd pdgdhdwgis aevdlaasde vgaavvrvtd vgql
//
LOCUS       WP_181567766             269 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Micromonospora robiginosa].
ACCESSION   WP_181567766
VERSION     WP_181567766.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 269)
  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..269
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..269
                     /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=27616
     Region          3..262
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mdllvvgasg flggevcrra vaaghrvvgt yhstavavpg aasrrldvtd raavralltg
       61 vrpdavvstp yrfddwavta dgaghvasaa aevgarlvhl ssdavhagrp epypdaavpt
      121 pvypygaaka aaetavravd pgallvrtsl ilgegskqiq rcrdalvgra tlfsdeircp
      181 vdvgdlaaav lellptdlag plnvagpdev sradvgrlla rrlgvdpagl rttttvaagl
      241 frpievrlds araagllrtr lrgvaelfg
//
LOCUS       WP_181567952             409 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Micromonospora robiginosa].
ACCESSION   WP_181567952
VERSION     WP_181567952.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..409
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..409
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43897
     Region          169..400
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtqgtgtgpr aahldldaev aamlrgrlpm vaertvtait aevpdysgal tgtmrekien
       61 avrialgtfl qliegtqafd pstplapale aayalgsgea ragrsmdall aayrvgarva
      121 wrevstttvr sglaaetvae faelmfayid elsaasvagh adelvsagrv rrrdlerltr
      181 qllagepees lrrsaeradw pppqtltvvl lprrhlravl allgpqtles gedlpgmrpa
      241 eemvvllvpd ahggrrrqlv rllhghravl gparpwhrva tsyqraaral alglgeadag
      301 pvdterhlaa lllsmdpeal adlrtqalap laalppatah rlaetlrswl lhqgrrddva
      361 adlfvhpqtv ryrmgklrel fgdrlhdpat vldltialav ppeqggapa
//
LOCUS       WP_181567949             437 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Micromonospora
            robiginosa].
ACCESSION   WP_181567949
VERSION     WP_181567949.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 437)
  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..437
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..437
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47324
     Region          51..426
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mngnndapap srprpashga elerqlalhg grpvrrtpwp tydkgavfvh aededaaira
       61 irshlyfryd hrpqnetecg rfedelcryf gtrhalavss gtaalalalm gagvpagslv
      121 acpgftfvat psaivlagcr pflvevdddl rmdlddlrrr wrpdiravmv vhmrgfaadv
      181 ealaafaaem gvpliedavp algaelngrk lgtfgaagaf stqsdkalnc geggflvtdd
      241 stlfaraval sgayegrlrr hfpageptlt gldlpllslr mdeiraallr aeltrlpqrl
      301 alfhrnyahv sraladvpgi varrpvapga ylgeaflfrv pggdagwftr alraegidar
      361 nigadddlnv rafwnwrfly dsadpgevra mlprtarllt etvdvplssn ltpddcddlv
      421 ravrkvadar daalarp
//
LOCUS       WP_181567984             202 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora
            robiginosa].
ACCESSION   WP_181567984
VERSION     WP_181567984.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..202
                     /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=20795
     Region          33..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 mdssawddry anasglvwsa epnrfvvesv aglspgsald iaagegrnav wlagqgwrvn
       61 avdfstvaie rgrelaaarg vtvdwrvadv tayrpvpgsy dlvlisylhl paadfagvla
      121 atrsalrpgg tlvvvghdla nlsggtggpq dptvlltpea vvdglaglri rraetarrpv
      181 ptsdggtvda ldtvvvatrp ad
//
LOCUS       WP_181567990             200 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora
            robiginosa].
ACCESSION   WP_181567990
VERSION     WP_181567990.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=20878
     Region          37..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 mgkptrwatd tepghsqwyv drfrrlaaeg adlagearlv dalvppgari ldagcgtgrv
       61 aaalaargha vvgvdadpsl veaaradhpg prflvadlae ldlpahgepa pfdaavvagn
      121 vmtfvapgte rgvlahiaah vrpdgvvvvg fgtdrgypla dldadavaag lrpehrfatw
      181 dlrpwheead favtvlrrpa
//
LOCUS       WP_181568007             369 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora robiginosa].
ACCESSION   WP_181568007
VERSION     WP_181568007.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..369
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..369
                     /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=39427
     Region          1..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 mrvaivgggl ggltlarilh rhglgaavye reshraertq ggsldlhpes gqralaaagl
       61 earfrsearp qgeehrildp agrvlvhhrp rpgsfagrpe idrrvlrdll ldslpedtva
      121 wdhrlvaaep rpdggfrlaf hggrhadcdv lvgadgarsv vrplltdatp savstlvslt
      181 vddadrrhpa ladlvgpgnl wcvgerrils gqrlgdgsir vgislpaddr dldtyrskra
      241 lldlfagwdp rltalieagd gppvphraev lpvgtrwphr pgvtllgdaa hlmppvgega
      301 nqamldaadl aaalaadpad pdaairayee amfarvqpia emcvrvqamm lsptaaddlv
      361 rfftprpad
//
LOCUS       WP_181567655             177 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Micromonospora robiginosa].
ACCESSION   WP_181567655
VERSION     WP_181567655.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=18985
     Region          85..177
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtergditir pggpadapiv lrlfdsaiaw ltergrpeqw gtdaastdpr ridqaegyah
       61 gdglwfaeid gtaagalvvg aateyvpaat epelyvnllv tdrayagrgv garllahaad
      121 larerglgll rvdcfrspdr alvrfyegcg ftatdpftvv rpgrppwpgq vlarrld
//
LOCUS       WP_181568011             245 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Micromonospora
            robiginosa].
ACCESSION   WP_181568011
VERSION     WP_181568011.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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..245
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..245
                     /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=26161
     Region          <61..129
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 msqlfgetag tyhearpgyp adfadairay hggppetlve vgagtglata allalgaatt
       61 cvepdtrmar vlaerfpgvd vvtssferws pppggvaala camawhwldp atrnqrarda
      121 lrpggtlavl shryayveda qgeairaafs tadpadrgdr pdgwfrddiv dsgcftdvrl
      181 srfrravpld taaylrlvdt fspqlrrppe lrervraavg aavdgfggtv vldlrtslal
      241 arrpa
//
LOCUS       WP_181567661             241 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Micromonospora
            robiginosa].
ACCESSION   WP_181567661
VERSION     WP_181567661.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=25332
     Region          5..241
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtlklrsvga sdrglirsgn qdaqhagpwl vavadgmggm aagdlasria idaiapldve
       61 tpedalvaal qgaieqatvg irraveedpe rqgmgttlta llfartgscl alahvgdsra
      121 ylfrdgvlkq vtrddtfvqm lvdqglitpd qasshprrav vtqalqgdqv spayatmvpr
      181 pgdrwllcsd glsnvvradt ltevlgerle rdacaarlid lalraggpdn itvviadvve
      241 e
//
LOCUS       WP_181567956             490 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora robiginosa].
ACCESSION   WP_181567956
VERSION     WP_181567956.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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 490)
  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..490
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..490
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52061
     Region          156..489
                     /region_name="RPT1"
                     /note="ATP-dependent 26S proteasome regulatory subunit
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1222"
                     /db_xref="CDD:440835"
ORIGIN      
        1 mtgyevrpde etvsllgaev hvtdpvglla aavdgpvell aganfpapvr evrctvradt
       61 ddgrpvhrfe aylrveaapa gllalglagp vglllaerla aragdgpaaa avgraaaeas
      121 rrlglrpagt alatpprdpa gravlaaaea agvrprveqe ngtvrirvdv psaevgpehl
      181 ravlgllfqa vreltgdsve ptvlrgrtyl vgrrpvavaa prsetvtldq vggladvvar
      241 frevavsfrh pqamarwgar rpqgilmygp pgtgktmlar alanevgadf veirtpeild
      301 kylggserni krifrdarry rrptvmlfde fdsiisyaga ggdaasqavn avagifkqem
      361 ntlfeenpdv ivvattnfpq rvdaslirsg rfdlkiaipa pddtgraeil gkmirelier
      421 herpgfrmfa ddvdpaalta dtagltgadl reslrrvqla kalreaaega ppapisqddl
      481 reavaglrrg
//
LOCUS       WP_181568164             926 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Micromonospora robiginosa].
ACCESSION   WP_181568164
VERSION     WP_181568164.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 926)
  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 926)
  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..926
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..926
                     /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=101157
     Region          21..923
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 msspaeryaa arrraaqasa fpaldefsrd lgfdlddfqr eacealergs gvlvcaptga
       61 gktvvgefav hlalreapgg dgpavrrkcf yttpikalsn qkyhdlvdrh gaeqvglltg
      121 dnaingdapv vvmttevlrn mlyagsatle glayvvmdev hyladrfrgg vweeviihlp
      181 esvtlvslsa tvsnaeefad wlvtvrgett vvvsehrpvp lwqhmlvgkr mfdlfhdada
      241 arkhdvhpel lrytrdtvrr lelgegrsag pgggrrgprw rgpmrpdivd rldregllpa
      301 ilfifsragc qaavqqclaa glrltspeer aeiravvesr itaipgedlt vlgywewldg
      361 lerglaahha gmlpafkevv eelfvrglvk avfatetlal ginmparcvv lerlvkfnge
      421 ahvdltpgey tqltgragrr gidveghavv vwspetdprh vaglastrty plrssfrpsy
      481 nmavnlvgsv gaeparalle ssfaqfqadr svvglarqvq rntetieayg aeaachqgdf
      541 deyfalrvai adreraiarq gqtqrkaaav eslerlrvgd virvpsgrra glavvldpat
      601 ggfgeprplv ltqdrwagrv tpgdftspae vltrirvpkh fnhrspaarr dlaaavsgtg
      661 ldrhggrrgg rsrqavgedh rlsqlrvelr ahpchacpdr eeharwaers rrlerdteel
      721 rqrvsgrtgs lartfdriva lltargylap dgevtdagrm lariwteadl lvaeclrrrv
      781 wdglspaela aavsvvvfea rrdlderasl prgavgdavd etlklwgdie adeaargltv
      841 trepdlgfaw piyrwargea lakvlasghq idgempagdf vrwarqvvdl lgqiadsgga
      901 stelratarq aisavnrgvl ayhasa
//
LOCUS       WP_181568257             292 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Micromonospora robiginosa].
ACCESSION   WP_181568257
VERSION     WP_181568257.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..292
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31256
     Region          8..289
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 meatvgaldl patldlpggp vrgglvvlhg shadqrsfyl yqhlarllpp agvavlrydr
       61 rrrvgghdvp ladqaedaaa avtalrrhvg aapvglwgfs qgawaaavta aahpvdflvl
      121 vgcsgvspaa qmrhgtaeql rrhghgpadv aelarlreva egflrgdvpr pvaqaeldaa
      181 rrrpwfplaf lpdelpatpg twadmdfdpa pvfarltgpv llcygetdgw ipieeslavw
      241 rrtareaelt varlagcdha ptldgredla gvsphyeavl ldwldrrlpp ar
//
LOCUS       WP_181568304             981 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            robiginosa].
ACCESSION   WP_181568304
VERSION     WP_181568304.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 981)
  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 981)
  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 981)
  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 981)
  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..981
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..981
                     /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=104928
     Region          16..262
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          137..981
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          728..756
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(729,732..733,736..737,739,769,772..773,776..777,
                     779..780,809,812..813,816..817,820)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          767..797
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          808..836
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(851..852,855..856,858,888,891..892,895..896,
                     898..899,927,930..931,934..935,938)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          851..875
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          886..916
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          926..954
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpapsddpst gpaddelyfr vlgpltverh gepvavggpq havalalllc hadqpvpvdg
       61 fvaelwrdrp prsyrvqvqg iiselrrrla pggraaapiv trpsayllht apdgldlrqf
      121 adevaaaaaa ratgdnaaal rlldvalgrw rgpafsgltg rsieataatl hearldaate
      181 lvdariadgr lnglvaelga ligerplder lhrhlmtvhd rlgrpadala ayrdlrarlv
      241 relgiepavp tqelhrrila gepgpagpah vaaapasahr qlppdiadfv grerelrtlr
      301 rwlardasag avpivvvegm agvgktrfav haahrlaaay pdgqfyldlh gfsaesapaa
      361 pgavlesllr rlgvpapaip esvddravll rdrladrrvv lvlddaades qvspllpata
      421 gclvivtsrr alaldgacvv tldvfsptea relltgmlgr drvtaepasv eelagrcghl
      481 plavavagrr lrgrpawrvg hllarlsdad rglaefavga rgvedvfals yralppgrqr
      541 lfrllgvhlg ddvtaastaa lvggdpvdte rdlealldeh lvqqvrpgry elhdllrrya
      601 arqaaatpde taaarrrlvd wyvatadrat rlirrfplpp vgrppepaap apgfgdeeaa
      661 lrwldaefvn lravihgaad lpswrnavvl ahllqpylvr rgqvddalvt lraaaaaarh
      721 lddpvaeaht lttlgqayet agrtdqalec lhdaldrhvr ldqpggeaat rhhlamvfrr
      781 lgrhedaige yrravtlfra lrdgqweasa lsglsvdlhl agrdeealaq alralslqrv
      841 vggpglgsve nnvgllharl grhaeaipya lralafqrrt gsrpgqanal anlafsyart
      901 grpadavraa teaveladgl gpdlranaln tlgeayrfag dhrsalrchr ealdiatrig
      961 daeeqarara gidpatmpas a
//
LOCUS       WP_181568179             449 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora robiginosa].
ACCESSION   WP_181568179
VERSION     WP_181568179.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=48142
     Region          116..420
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msrpglrarv taafavgall laalmalfsy dltrrsllde reraavraay ydaavvrsgl
       61 dtgtpdvvav lrsldtgsar rpllhlrtgw yartadvgas svpvelqrvv aegqpavqri
      121 rldgqptllv gvplpgelgy yeltslreve dtfqvvglal tavaimvaga gaalgwyatr
      181 nslrpltava daaeriaagd fatrldpttd pdltrlstsf nemvdklvqr idrdrrfaad
      241 vshelrsplq tlaaaasvln rrkehqdert ataaglvade varfqrlvdd liqlarteqp
      301 ahretvdvae laraacrers lpeslvrvgd gvphewwvdr rrlaqillnl lenaeryggg
      361 pvavrldvvd gagvlavdde gpgvpaadre aifdrfvrgr aaharagtdg tglglalvaq
      421 haaahggtaa vrdrnpgarf rvelpgalr
//
LOCUS       WP_181568434             339 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            robiginosa].
ACCESSION   WP_181568434
VERSION     WP_181568434.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=36991
     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 mrasrlvsll lllqtrgrmt agelaealev svrtvyrdve slgaagvpvy adrgpaggyr
       61 llegwrtrlt gltgpeadal flaglpgpaa elglasavaa aelkvraalp deladrtgri
      121 rqrfhldapg wfrhpepvph letlagavwt drlvrlryrr wrapreitrl vaplgvvlka
      181 grwylvarcd ddvrtyrvga vldasvtdeh aerpdgfdla tywrewtary erdvyreqar
      241 irltaaalef mpyvfppems raaraaagep gpdgwlettv piesvrhahg ellklgaeve
      301 vlapaelrar ftatahaltr lypdadagaa gvpaspasa
//
LOCUS       WP_181568444             256 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Micromonospora
            robiginosa].
ACCESSION   WP_181568444
VERSION     WP_181568444.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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..256
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..256
                     /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=27409
     Region          6..232
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mdtspwrapl lwrgaqmlah avvaligrle vtgdvpadlr rgplilaanh ispfdpvvla
       61 aacrarrvap rimatgglfr apvlgalmrr aghirvdrgt tavhrsleia aeavaggsvv
      121 lvypegrigl dpgmwpergk tgaarlafas gaavvpvaqw gshevlpyra pkgmlrglar
      181 alrrrpvirv hfgapvalrd lrpgvpgaar hatdriidai tdtlaplrph epdrprhvdp
      241 grpvdpsrah rrhrtg
//
LOCUS       WP_181568085             150 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine dioxygenase [Micromonospora robiginosa].
ACCESSION   WP_181568085
VERSION     WP_181568085.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 150)
  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 150)
  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 150)
  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 150)
  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..150
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..150
                     /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=16279
     Region          35..125
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
     Site            order(35,37,49,60,62,105,119,121)
                     /site_type="active"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mtstdptdlr tvaacwadpt gwpvplrfdr serwyarlha daahevwals wlpgqgtdlh
       61 dhggssgafl vvagvlteet vsggrlrphr laagagrrfg arhvhqvtnr gdqpavsvhv
      121 yrpalrrmtr yrldagglrv aevaeagvaw
//
LOCUS       WP_181568219             263 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Micromonospora robiginosa].
ACCESSION   WP_181568219
VERSION     WP_181568219.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 263)
  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..263
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..263
                     /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=26885
     Region          6..253
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mtaiggatrl yallgdpiaq vrapgllnpv larrgtdavl vpvhvpaaal pdvvaglrqv
       61 tnlhgmlvtv phkaavlpla drvtdrarra gsvnalrret dgtwtadtfd gdgfvrglva
      121 aghdprgrrv cvvgaggags aiavalldag vaalhladtd parlaalggr lsaaypgrvh
      181 aasrprladv dlavnatpvg lrpgdpppfp vaelparavv adiimspaet tllraardrg
      241 lpahpgepml ahqidgyldf fgl
//
LOCUS       WP_181568503             499 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Micromonospora robiginosa].
ACCESSION   WP_181568503
VERSION     WP_181568503.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 499)
  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 499)
  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..499
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..499
                     /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=54205
     Region          1..430
                     /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 masdhvdvli vgaglsgvga avhlgrecpg ktyavlearg aiggtwdlfr ypgvrsdsdm
       61 ytlgysfkpw tdpkaiadge sirryvreta reygvqehir fhhrvtraew dsatarwtvh
      121 ahrddtgedt tltcaflftn sgyyrydegy tprlpgvery agtlvhpqhw pegldvtgrr
      181 vvvigsgata vtlvpamaht aahvtmlqrs ptyvislpsr dafadaarrw lppkaayava
      241 rwknvalgva nfqlsrrapg lvkrflrraa kgrlpigydv drhfsprydp wdqrlcvvpd
      301 gdlftalaeg rasvvtdtid tftahgirla sgdelpadvv vtatglnlla lggmtlsvdg
      361 advdlaatia ykgmmlsgvp nfamtigytn aswtlkadlv atyvcrllrh lddtgqqivt
      421 pvaphtddlv piidlksgyv lravdqlpkq gphapwrlhq nyprdvrlmr hgpltdgvrf
      481 aragapataa aatsggsda
//
LOCUS       WP_181568500             426 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Micromonospora robiginosa].
ACCESSION   WP_181568500
VERSION     WP_181568500.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 426)
  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 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   3  (residues 1 to 426)
  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 426)
  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 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   6  (residues 1 to 426)
  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 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 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..426
                     /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=44281
     Region          24..415
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 msagrrpaal vyavavtayv aavfhrsslg vtgvdaadrf gidatalatf svaqlavyaa
       61 mqipvgvlld rygsrrllla ggalmvagql vfavavdvrl avaarvlvgl gdamtfisvl
      121 rivaywfpgr rnpllvqltg tvgqlgavlg avplvallhr agwtpaflta aalgatvlll
      181 vlaavrdtpr aaqagaptpt latvrrqlad awgqpgtrlg lwthfvtqfs gavfallwgy
      241 pflvqgqgfa ptaaaglltl mtvvtlvcgp vvahlcarhp fhrsvvvfai taataavwav
      301 vlawpgraph wllvalvvvl avngpgsvig fdyartfnpv hrigsatgiv nvggfvasiv
      361 lvlavgvvld latpagrdap plsafrwafa vqyllwalga vqvlryrnaa rrrwaddraa
      421 avpvpa
//
LOCUS       WP_181568555             309 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora
            robiginosa].
ACCESSION   WP_181568555
VERSION     WP_181568555.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..309
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..309
                     /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=32947
     Region          19..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 mrtkqelsaa irerrraalv vnahsrrgrr lydtvharlr aagftllgay padrpgdldr
       61 alaeavglgp dllvvgggdg tigaaarlla hrdvalgllp lgttnnfart vdvpldldaa
      121 vavltdgkvi dvdlgligdt rftnhvgigl sadimlaapp rlkravgrla ypltalglla
      181 rhrplrvtvr aegrehaftt hqvyvanggf hagrpitada naddrllvay pvggasrrgl
      241 lretarnaaa grrrtlgdep flavrqlwle tdrparievd gepygqtpvr vgldpnalrl
      301 mapahspdh
//
LOCUS       WP_181568487             596 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Micromonospora
            robiginosa].
ACCESSION   WP_181568487
VERSION     WP_181568487.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 596)
  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 596)
  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..596
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..596
                     /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=63851
     Region          38..572
                     /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 mtsssgasrr qvlavaaaaa tapllagapa eakpkqpktw dltvlgtsdt hgnvynwdyy
       61 kdaefddskh ndvgvaklat lvnqiraert gkatlvldag dtiqgtplat yyakqepits
      121 tgethpmana mnvlrydavt lgnhefnygl pllatwikql gfpalaanai nektgkpafl
      181 pyvikevrlg ghgapklrvg ilgltnpgva iwdkanvegr lvfadmvata akwvpvmrrr
      241 gadvviisah ggdsgtssyg pelpnenpta liaeqvpgid ailfghahne vpekfvtnlk
      301 tgkavltsep skwgqrltrm dftlarekgc wkvvdssatt lntntvvedp avlaavrgqh
      361 aktvdyvnkv vaqssvelsa aesrykdtpi ldfinhvqte vvtaalagga yaglpvlsia
      421 apfsrtavfp qgdvrirdva glyvydntle avvltgaevk ayleysakyf vtvpvgapvn
      481 petisdpavp dynydvfsgv dyeidiskpv gqritrlvla gtdtplpada qfvvavnnyr
      541 rsgggnfpgi vktqvynaqq eirqllidwa qakgvidpad ffvpnwklvr egvpvf
//
LOCUS       WP_181568565             140 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora robiginosa].
ACCESSION   WP_181568565
VERSION     WP_181568565.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 140)
  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..140
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..140
                     /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=15289
     Region          1..134
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 madpfrvrvt vrgyeldtqg hlnqavylqy aeharweclr aagiaqdrll aagvgpvale
       61 vtvrylrelr ggdevdvtce frwgegktfg ivqdftrpdg tpvaavtgvg glldlaarrl
      121 vpeprerfra laadpvpmsl
//
LOCUS       WP_181568588             191 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora robiginosa].
ACCESSION   WP_181568588
VERSION     WP_181568588.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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 191)
  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 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 191)
  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 191)
  AUTHORS   Rosinski,J.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..191
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..191
                     /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=21489
     Region          16..84
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 madesnhvhl tdpramrala hptrlrllge lrlrgpqtvg mlsertgeav gsvswhigkl
       61 aehgfvaeap dlardrrerw wraahattdw dpvellddpe rrlagdllrr aameryvary
      121 qayleseasl dlawvrgtts sdtvlhltpd elgelrdels elgrrwqarg apgrpgaemv
      181 tliwqayrgp q
//
LOCUS       WP_181568652             246 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora robiginosa].
ACCESSION   WP_181568652
VERSION     WP_181568652.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 246)
  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 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   5  (residues 1 to 246)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..246
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..246
                     /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=25730
     Region          1..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtiradgrgl agfaalladp tragfclall dgrawtagel arsagvaast asdhltrlvr
       61 ggllveerqg rhryvrladp tvahlvedla arapapatpp rtlraasaga alayartcyd
      121 hlagrlgvll ydallargvl drsagltltp tgtswlddlg vpveplratr rplvrdcldw
      181 terrphlaga lgaalcvrlh hlgwtvpgtg rsvrlsptgr helaealald patlappsrd
      241 ggpara
//
LOCUS       WP_181568927             922 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            robiginosa].
ACCESSION   WP_181568927
VERSION     WP_181568927.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 922)
  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 922)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 922)
  AUTHORS   Rosinski,J.A. 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 922)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..922
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..922
                     /product="helix-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=97579
     Region          <6..871
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          857..913
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mggsvapaaa vgtatdggad dllgradech rltgmladav dgrggalvlr gaagvgktal
       61 ldhcaahagg mrvlratgvp feaelpfsal helvrplldr ldelparqad alrtalavdg
      121 gsgtvnrlaa ylatltlltt aaertpvlcl vddahwidpa saeallftar rlladrvaiv
      181 faardvpgfd grgvpelpva glapdaavrl amragldrra aedlaaatag nplalielpa
      241 alaeehrdgw lpleeplvla drirtsvlah arglpeatwr alvvcavagt tgpallqqvl
      301 tmqglhldal dpavdaglvr vggrevtfrh pltraavhsv agagqrrsah laiasvltga
      361 daadrrawhl aaatsvpder vaallagsae raqrrggvva earayersar ltpdadlrae
      421 rligatrawa nagagrhava lgeealtltr rvdllcrvkp llthlalqhs daavreqafl
      481 aeaesyagvd plgaaklmsa gvnqfwarfd iagmlplctr vvalartadg ppwpkglirl
      541 aaaqvlaglp egaalarecv avcaghadgs aaelaevfcw ladhdtaral lapeidrara
      601 nddvfllaya lprlaelewr ggrlhaayra ateavrlaeq valpvlraea laglalveal
      661 sgaepaarar vddarrllpv efgevevrlr yatamtsvva arwdeavtel ewiraaqrhg
      721 glaepgwlpv agelaeayah lgraeraaqa saelgdgraa aarvhgllap erdldeafta
      781 alarcdpaag slerartllg ygqrlrrakr rrdarerlha alrlfesaga qgwarrcrae
      841 idatgrrapa pddrgvdrlt sqerqialhv aegltnreia triflspktv eyhlgnvyrk
      901 lqlrsrpeli rhlsrrpvsd sd
//
LOCUS       WP_181568937             151 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Micromonospora robiginosa].
ACCESSION   WP_181568937
VERSION     WP_181568937.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 151)
  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..151
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..151
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16931
     Region          4..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(5,7,9,18..20,22..23,28,44,52,54,56,58,67,69..70,72,
                     75,81,83,85,98..99,101,103,113,115,117,119,128,129..133,
                     135..137,140)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mtidmrmtrq lpaspeevfd aytdaekqki wfsildeepg iveidvdlrv ggkqtavwgp
       61 spdmlfretq tfleierprr lvtesvgssp dgetmtthie itfeerdggt lmtvvqsgfp
      121 tpevrdffag eawsgaldrv eaylarersr g
//
LOCUS       WP_181568973             422 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora robiginosa].
ACCESSION   WP_181568973
VERSION     WP_181568973.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..422
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..422
                     /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=44316
     Region          19..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 msadvvvvga gagglasara lgalglrvlv ldrqrtpasi akgeilqpet vrildtwgtl
       61 dalratgarp vgrlairdps gepllcldya glpgayreil cadygdlrav ladglpdpvd
      121 lrwgrrvtgl lrddggrvtg vrvtgdggeq dvpaalvvaa dgmssplrra agvaverrey
      181 phglvafdva gaevtdevta yrtgrglclv yplpggrcrl yvqvtpdefr gradlgpwcd
      241 rlladvpair plepairasl hrrqllavyr lraarltvpg lallgeaaha vhpmaaqgvn
      301 sslgdaetla atlaaeggtp epdavdralr ayqaarrsrl dhvatvshna srmitsvtgl
      361 pkllggrmmr rtaanprllg ltagnlsgtd vrplslvdrl hqlglladrh ahapsapaps
      421 er
//
LOCUS       WP_181568978             287 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Micromonospora robiginosa].
ACCESSION   WP_181568978
VERSION     WP_181568978.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..287
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..287
                     /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=31999
     Region          8..258
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mttstaadvr lvagalgaev hgidlntltd dgfalihdll lkhqvvfvag qagltpqahv
       61 afgrrfgeve lhpylprleg hpeivvidst dggkvdvwht dmtfhqsppi asilhltelp
      121 avggdtmwtn qcrvyealsa plrdlvdglt aihvirigte ftsraehpvv rvhpetgrrs
      181 lyvnrlftsh ipqltrgesd allehlfrfs egpqftcryr wrvgdvavwd nrvtqhyain
      241 dydgvrrgqr itvlgdhptg daprwehyap apgerywpdr vnavesy
//
LOCUS       WP_181569011             247 aa            linear   BCT 28-DEC-2024
DEFINITION  aminoglycoside phosphotransferase family protein [Micromonospora
            robiginosa].
ACCESSION   WP_181569011
VERSION     WP_181569011.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 247)
  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 10007009
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..247
                     /product="aminoglycoside phosphotransferase 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=26509
     Region          14..218
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
     Region          <137..204
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
ORIGIN      
        1 mdgngvevvi ahseratlrv gdvfvkvdad qarldvevqa maaapvptpq vrwheppala
       61 laalpgvalg rlgepstasp aawaaagaav rtlhdaplpp wpgrsrdela sglaeecewl
      121 lahdvlpadv vtrnrrlaet alrpwtpvfi hgdlqvdhvf vaddqvtgil dwseasrgda
      181 hfdlatltlg hpehlgdvia gygadvdrdl vrawwslrcl tnvrwlaehg ygspddfpev
      241 avlraqp
//
LOCUS       WP_181568607             324 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Micromonospora robiginosa].
ACCESSION   WP_181568607
VERSION     WP_181568607.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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..324
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..324
                     /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=34231
     Region          86..246
                     /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 mtalnrrtll raaaltgaaa atglagglaa apasaaeagn gpwlvsvgwg vlqidpgrtt
       61 prsllpdgdh akaspdgryv awvntawsgd gtllpyvavh drvtgrkrtl ladppgvlyg
      121 aptwspdgre ialvtgsqqd rliavdvatg gtrvlvqgha msspdwsrdg smivmhwrsr
      181 segpqlrvle latgtvrrly apqagervsg pvftpdserv vfcttrwypd latlnqslas
      241 vriggaglkk ltdeprfyls pvfspdgryc aalsippene ypdggniivs tsgfgaqwwv
      301 pgdeyddstr ldwarpvatt gasa
//
LOCUS       WP_181569257             331 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [Micromonospora].
ACCESSION   WP_181569257
VERSION     WP_181569257.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
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="Micromonospora"
                     /db_xref="taxon:1873"
     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=35379
     Region          19..308
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mntheplsqp evqgfaalaa rladnvnavv lgkpqvvrla ltalfaqghv lledvpgvgk
       61 ttlaravaat vkgewrriqf tpdllpsdvs gvtifnqasr gfefhpgpvf aniviadein
      121 raspktqsal levmeertvt vdgvrhpvpq pflvvatqnp vemdgtyrlp eaqldrflvk
      181 lsvgypdeav evevlrgatv rspdsltavt dtatvgemvk marrvhiaep lyayavrlaa
      241 atrthpqvrv gvsprgvial traacayali dgrgwimped lkalvepvfa hrllltpdaq
      301 vrgvtpaevl rqavasvpvp lpsgqpapvh g
//
LOCUS       WP_181569309             270 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Micromonospora robiginosa].
ACCESSION   WP_181569309
VERSION     WP_181569309.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=28809
     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 mpvheitdpd ddriadyral tdvelrtrwe pphglfiaeg elvlrralra gyparsylve
       61 akradqladl dtgdapvyaa saevlqratg fhvhrgvlas fhrralpsaa evlaaarrvv
      121 iledvnnhtn lgaifravaa lgvdavllsp tcadplyrrs vrvsmgevfa vpyakleswp
      181 aglaevraag ftvlaltpae davpiqrltg eqraraalll gaegagltra amaasdvrvv
      241 ipmrrgvdsl nvaaatavac welgrddpla
//
LOCUS       WP_181569324             368 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora robiginosa].
ACCESSION   WP_181569324
VERSION     WP_181569324.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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 368)
  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 368)
  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 368)
  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..368
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..368
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39923
     Region          35..331
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 maqpttpdvp npteappdap ppatttpaqd atlleralfe ikrvivgqdr mvermfvall
       61 arghcllegv pgvaktlave tlaqvvggsf arvqftpdlv padimgtriy rqssekfdve
      121 lgpvfvnfll adeinrapak vqsallevms erqvsigget hrvpdpflvm atqnpieqeg
      181 vyplpeaqrd rflmkivvgy ptdaeereiv yrmgvappep apvfdtpdli alqrkadqvf
      241 vhnalvdyav rlvlatrapa ehgmpdvaql iqygaspras lglvratral allrgrdyal
      301 pqdvqdiapd ilrhrlvlsy daladdvpad hivhrvmsti plpavaprqq atppppavgg
      361 hgwpgqrp
//
LOCUS       WP_181568812             408 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Micromonospora robiginosa].
ACCESSION   WP_181568812
VERSION     WP_181568812.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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 408)
  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..408
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..408
                     /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=44993
     Region          20..406
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(56,63,87..88,95,99,106,239..240,243,247..248,251,
                     284,289..290,293..294,296,319,346..348,351..352,354..356,
                     360)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(63,81,83,86,88..89,171..172,184,238..239,242..243,
                     247,290,293..295,396)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtedvvpaae lytdafaadp yptfarlraq rpvcpvgspr fdswlitrfd dartaltdpr
       61 lskdlygpdq hylrifgpns eglnrnmlns dppehtrlrr vvsqafaprr iealrprvaa
      121 ivdqlidkmv prgeadlmre faiplpmtvi cellgvppad hdrvldwtqv irtsgstsrp
      181 paeeraavqe aqlrlhdyla dlvrakradp addiigalvd avdrdrtlse aelvtttfll
      241 lfaghqttad flgnavlall thpeqmellr stprllptai eellrfdgpl pvaspriate
      301 dvdyqgvrip rgaivgvain aanhdpahft dpdrldlrrv rgphlgfghg vhyclgvsla
      361 rmeallalsa llrrlpglrl avplaevrrl paaspfrgll elpvaftv
//
LOCUS       WP_181569381             245 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            robiginosa].
ACCESSION   WP_181569381
VERSION     WP_181569381.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=25044
     Region          15..234
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mknaaalseg svtstvagat apadlstrdr vtqlllerga ttaaqlgsal glspaairrh
       61 ldamladgdv vareqtvrgs rgrgrpakvf vlteaarvrc gthhydnmat aalrwiartg
      121 gaeavaafaa dqvaalehrc raamedagda plaraealag altaegyaan astiasggql
      181 cqhhcpvahv aaefpqlcea etavisrlvg thvqrlatia hgdgvctthi paqsgstvtt
      241 vrtdr
//
LOCUS       WP_181569408             191 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Micromonospora robiginosa].
ACCESSION   WP_181569408
VERSION     WP_181569408.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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 191)
  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 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 191)
  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 191)
  AUTHORS   Rosinski,J.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..191
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..191
                     /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=21428
     Region          12..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdqptvrqvt dsrvlaalah plrrrlmdvl kvygpctvgm laertdqapa nvshhlkvla
       61 aadllveape lardrrerww kprnrgvrws htdfdddpsa rvvadaassl nlerhaelvr
      121 awhaapeeah vawgdgpfst dhwlhltpde ltelsrevia llmrwadrat pddgqtrepv
      181 fvfahgvpgr p
//
LOCUS       WP_181569478             395 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Micromonospora robiginosa].
ACCESSION   WP_181569478
VERSION     WP_181569478.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=41515
     Region          1..373
                     /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 mrsavvvgag lggmavagal arsgwqvtll ekadrvrpea tavvlwpngv ralralglga
       61 gldaiatplp dggirrpdgq wlvqprptpa drmpvvvhre dlhdaliagl gervelrtgv
      121 svrsvrasag erpavgdgrh lfeadlvvaa dgidseirrq lapetavvss gcaawravip
      181 wyrapqlpdd qqpngetlga gyrfvaaslg ergtagasrr ggiywvataa gaprpeppei
      241 qlallkrwfa gwpapiatll datdpadvvq qevrelrplp raygfgagpg gvvllgdaah
      301 ampphlgqga clafedaatl agllresrlp davaaydrlr rpraatmvrq trrmsavlqt
      361 rgrlalrard aalgtisprl rntaaaaaad wqpps
//
LOCUS       WP_181569422              97 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Micromonospora robiginosa].
ACCESSION   WP_181569422
VERSION     WP_181569422.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=10640
     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 mvlevalidv tpgheddfaa ayaqarpila gsegcrsvrm trgvesptrf vllvewdsve
       61 ahdvnfrqte rfgrwrglig phfagpplve hfvdvpa
//
LOCUS       WP_181568808             325 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Micromonospora robiginosa].
ACCESSION   WP_181568808
VERSION     WP_181568808.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (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   2  (residues 1 to 325)
  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 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
REFERENCE   5  (residues 1 to 325)
  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..325
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..325
                     /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=34172
     Region          70..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(70,129,133,153..158,177..178,182,192,209..210,212,
                     232..233,259..261)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mtvdahafwl rapgegeirp vrldppgpge vlvrtrfsgv srgtetlvft grvpadqyat
       61 mraphqegdf papvkygyln vgtveagpae lrgrtvfcly phqsayvvpa eavvvvpdgv
      121 paeravlagt vetavnalwd aaplvgdrvt vigggmvgcg vaallarfpg vrvelvdadp
      181 aragvadalg vdfalptdat gdrdlvvhas asadglqrgl dllrpegtvl elswygdrpv
      241 tlalggafhs rrlgirssqv gtvsprradr gyadrlalal dlladpafda lltgrsrftd
      301 lpdvldrlas grlpalchli tygee
//
LOCUS       WP_181569174            1033 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Micromonospora
            robiginosa].
ACCESSION   WP_181569174
VERSION     WP_181569174.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 1033)
  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 1033)
  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 1033)
  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 1033)
  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..1033
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..1033
                     /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=112219
     Region          1..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          123..1033
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          709..737
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          751..777
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(753..754,757..758,760,790,793..794,797..798,
                     800..801,823,826..827,837..838,841)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          782..818
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          823..857
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mefrvlgpve ihsddvvtvv ggrqprlila vlildanrpv pverlidliw aqapppsara
       61 alqamvsrlr atlrrigapa hlvgerdayr lqvepmltdv hrfsalvqqv sdspdddtvv
      121 gvldqalalw rdeplldvvd devrhrlcat llearstave draeallrlg qtrrvvrdla
      181 gevarhpyrq rltgqlmlal yregrpdral evyrhhqtrl adelgldpat dltrlhqlil
      241 qgdpalraer apspgpptps ppaelppdvs gftgrvvelt qldratsgst aptiwilrgi
      301 pgvgktalav hwahrarhtf pdgqlfidlr gfdierspvt psaalgqllg glgvdlrnvp
      361 ddedaratlf rsrmaglril lvldnardar qvlpllpsgg tvlitsrhhl gelvvrtgar
      421 slllntldpt esaqllavml gddavhaeaa aaarlaqlcg hlplalriaa anlqvsgesg
      481 iagltreltd gdpltgltln gaddvavtrt falsylampt aarrlfrrlg lvpgvsftdd
      541 vaaaldpaas gtagrtlral aaahlveqra sgryrfhdll rryavdrlla eeddrarhda
      601 rerllshyls tadaagrrvi phfvrlprpv pedpfadvda algwldaeat nlmaaiqhaa
      661 eqgqpryawq ladalrswfh qrgrrtewla aatagltaae aehdvraeai mhlsialaqv
      721 tsghyedare hllaglrvss addwpegrig llnnlsavhq rlgdpraaid carnsltlnr
      781 qhgseggetm planlgfahw qlgalaeadr niraalsrar qnkahyneav llvdlagicr
      841 drgdheqaer lydralsanr dlnyrygeat alsgrallws ttgraaaaga daehavtltr
      901 eigdlgteaw arealgrvll aagllaesaq efdqalhlar rtrfvwcean alvglaaacl
      961 aagdpdaart daeaalriav eagyrvieth avrllarlre saddrvgare lhrradrlag
     1021 emdlreghpy lar
//
LOCUS       WP_181569494             608 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Micromonospora robiginosa].
ACCESSION   WP_181569494
VERSION     WP_181569494.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=64644
     Region          5..603
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 maldvpyrsv pdmflkrvad spdrhafahp aqddsgpvwl tweqvgqrak aiaaglhglg
       61 vgledpvail antrlewvla dfgvmcagga tttvypttep edavyilads gsrvlfaenp
      121 aqaakiagae lpalthvvll dgaadpaagv pqltlaelee rgaatlaaep dlvdrlvagi
      181 gpdhlatliy tsgttgrpkg vellhggwcw egvaqaelgl lrvddlqylw lplshsfgkt
      241 llcgathvgl ptyvdgrvdk lvellgvvrp tlmcgaprvf ekvynkavtt aqsaggakak
      301 ifawgvavgk ekvaleqagk pvpaglrlky glaeklvfsk lqarlggrmr vlvsgaapls
      361 qeiatffaaa nlpisegygl tetsagafvn ppdglkigsv gramgdlecr idtdgeilvr
      421 grpvmrgyhn lpgetaeaft ddgffrtgdi gtldddgylr itdrkkdlvk tsggkyvaps
      481 hiegvfkavc pytsqavvig qarnyctmlv tldpdaiqaw aagtrlegsd yttivtspea
      541 qemvegyvae lnaklnrwet ikkvtilprd ltiadgevtp slkikrrsve tnfageidkm
      601 yegtlael
//
LOCUS       WP_181569555             495 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Micromonospora robiginosa].
ACCESSION   WP_181569555
VERSION     WP_181569555.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=52205
     Region          1..491
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 marivvigag vgglavaarl avtghevtvl eragtvggkl grwahhtpeg twrfdtgpsl
       61 vtlpqvfadl featgaklde yldlvpldpi vrhvfpgggp aldscadpde faarigaafg
      121 drsaadwrkl wrraervwta shrdilrrtv dsprdlaala wrlgdlaaig pgrtlrglgr
      181 thlsddrlrm lldryatytg adprrapaal vavpyaelay ggwylrgglg tladallsrc
      241 ldlgvvvrtd aavtridaag grvhgvrvag savpvpadvv vantdaltvy rdllphprrl
      301 aaltdrslag fvmllgvrgd tgvahhtvff prdydaefda vfgdpgrgvr arpapdptvf
      361 vtaaddpavr pdgheawfvl vnaprhgtaa davdwrrpgl aetyagrild vlaergvdvr
      421 drlvfseirt padldaatga pggaiygtag gllrpanrgp vaglwlvggs thpggglpmv
      481 tlsaeivaha igpaw
//
LOCUS       WP_181569558             472 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            robiginosa].
ACCESSION   WP_181569558
VERSION     WP_181569558.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 472)
  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..472
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..472
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48036
     Region          9..77
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
     Region          <51..466
                     /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 mipsspsgpr llgpllaelr aargwsqqrl aaelcaasgv ptltrhevsr werqlrlpgd
       61 fwsawlatvl gvpgellaea garsrrlgat parvdaagsr arlalltlah rwaadptgga
      121 lagpladglp ppaarsgrag qpapagpadp pgegglavlr rwddllgggd ltgygarrlr
      181 rvvrghrlag pagrrrllpe laesaqlagw laadagdltg glvayrlalr aalaagdrpl
      241 aghvlgsash llagagdpag altlarigya agragasagl ralllhrval aaalagrrra
      301 agqalagadr agtpdpgrep pwlywldeae laamtgrtlv avgrpaaava llapvvagsr
      361 grprraavyg awlarahlrl davpeactva gaalldavrs gspravgqlt gfrrgladrp
      421 dgrrfpella aarpylpvpa rdgpdptgrg asgrragaat grvrrgptsv ga
//
LOCUS       WP_181569594             595 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Micromonospora robiginosa].
ACCESSION   WP_181569594
VERSION     WP_181569594.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 595)
  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 595)
  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 595)
  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 595)
  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 595)
  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..595
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..595
                     /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=65850
     Region          43..>592
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mdvdaghgaa lggslptqge lpltrrlrsl lawptadgdp vtalvrahrg ihpsadasvl
       61 rraytiaenm hrgqfrksge pyithpfava qicadlgmdt itlvaallhd tvedtrytlq
      121 alqedfgrev ahlvdgvtkf dkafygkaae aetvrkmiva agkdvrvlvi kladrlhnmr
      181 tlgvrsaasr eriarktlev lvplcdrlgi qtlkrelddv vllhlqpdeh ariarfvhdr
      241 pgwdayltdv vartraalrr srvdaevspr prhlysiwkd tvagdhaapl dlpriaivvd
      301 gpptdcyaal gavhglwrpm pgrfkdfias pknnlyrslh tsvcgpqdrt vevlirttem
      361 hraaeygvaa hyrfpraagr aadraeelaw lrrvldweqe tvdpgqfmas lrcdlaeaqi
      421 qvvadgrqvv lpagatpvdl ayelgsergd hclatringr laplsselee gdvveiftes
      481 daesgfevdv aprgprrewl gfvksphaqm qinrwfaeht epgisiadkv rlgrasigla
      541 lrkhdrglas dlpllrlsee lgypdletml vavfdrsvep dtvvrqlidl vdhrq
//
LOCUS       WP_181569803             335 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            robiginosa].
ACCESSION   WP_181569803
VERSION     WP_181569803.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=37863
     Region          4..318
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 marpitlftg qwadlpfdev crlaaewgyd gleiacwgdh fevdkaladd syvdrkretl
       61 akhnlqvfti snhlvgqavc dhpiderhqd ilpariwgdg epegvrrraa eeikdtaraa
      121 aklgvrtvvg ftgssiwhtl amfppvppam iergyqdfad rwnpildvfd aegvrfahev
      181 hpseiaydyw ttkrtleaig hreafglnwd pshfvwqeld pvnfifdfad riyhvdckda
      241 kvrtgdgrrg rlsshlpwad lrrgwdfvst ghgdvpwedc fralnaigyd gpisieweda
      301 gmdrlvgape alqfvrrlaf daptaafdaa fstrp
//
LOCUS       WP_181569810             296 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            robiginosa].
ACCESSION   WP_181569810
VERSION     WP_181569810.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 296)
  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 296)
  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..296
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..296
                     /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=31586
     Region          20..286
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mttvtpaaap rrpapapgrl rfgygtngfa nhrlddalav ladlgyagva ltldhdhldp
       61 fapglarrvd avrrrlsasg lavvvetgar ylldpwhkha ptllhddpsr rieflrravr
      121 igadlgaeav sfwagvrppe vpprvawerl vdgcaavcae aggvplgfep epgmlvedia
      181 gwrrlraalg eppgfgitld ighcrclepl pvpdcvaava dhlvnvqidd mrrgvhehle
      241 fgageidfpp vlaaladagy pglvavelpr hshaaptvaa rsldflraaa rrgerr
//
LOCUS       WP_181569870             446 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Micromonospora robiginosa].
ACCESSION   WP_181569870
VERSION     WP_181569870.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..446
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..446
                     /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=47002
     Region          7..446
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 msdrtdpafa eveaalnarg ftrirfelek ieslldllgs pqraypsihl tgtngktsta
       61 rmidsllraf glhtgrytsp hletvreris ldgepvseer fvatyreiap laelvdqrsa
      121 epltyfdltt alafatfada pvdvavvevg lggaedatnv iqagvavitp igldhtewlg
      181 dtiedialhk agiihpgatv iaaaqeedaa rpilercaev natvaregae fgvmrravav
      241 ggqvltiqgl ggvyeeifip lhgahqaqna avalaaveaf lgagarrqld ieavregfaa
      301 tsspgrlerv rtaptvlldg ahnphgmaat vtalqeefaf sklvgvlavl gdkdaaglld
      361 llepvldtiv vaensspram pvdelaelar evfgaervqv arempdaiea avaeaesdvp
      421 gelagvgvli tgsvvtvada rrllkr
//
LOCUS       WP_181569912             147 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Micromonospora robiginosa].
ACCESSION   WP_181569912
VERSION     WP_181569912.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=16391
     Region          1..142
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msdrfvyhca lrwsdldayg hvnnarfltl yeearvammf aggrawgvds fadgvvirrh
       61 evdylrpvdy algrssaeaa ptvrielwvd qiraasfsva yelydgdvla gtarsvlvpf
      121 dlsvqrprri saderafllr yapgltg
//
LOCUS       WP_181570059             136 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Micromonospora
            robiginosa].
ACCESSION   WP_181570059
VERSION     WP_181570059.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..136
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14918
     Region          16..116
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtsqddrcgs gpadgaract vrealdrvgg kwsigiliaa stgpvrftel errvegisrr
       61 mltltlrnle rdgllvrhvh atvppkveyt atpmarelye slvaltrwae rhrdaisgar
      121 aaydrehpva kptqsv
//
LOCUS       WP_181570395              93 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            robiginosa].
ACCESSION   WP_181570395
VERSION     WP_181570395.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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 10601889
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..93
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9909
     Region          20..77
                     /region_name="HTH_26"
                     /note="Cro/C1-type HTH DNA-binding domain; pfam13443"
                     /db_xref="CDD:433211"
     Site            order(21,25,52)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(24,51)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(31..32,43,46,52..53)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mttnagegta tlsadvaaei rawmgrlgvn qaelarrigq naqwlsvris akatvainld
       61 emqriadalg ilvkdllpey asqrvsrsea ttr
//
LOCUS       WP_181570513             936 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora robiginosa].
ACCESSION   WP_181570513
VERSION     WP_181570513.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 936)
  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..936
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..936
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=100393
     Region          44..915
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msqrihlpsg wvtfvftdie gstrlarmlg pvyrpvlteh rrllrdtltg tdgaellteg
       61 dsfflafpda gaavhaclta qralvahdwp npdatprvrm glhtgyaepr dgeyaspevh
      121 raarvaaaah ggqvlcsaat arhadplpdg aslldlglhr lrgfddrerl fqlvapgler
      181 rfprprtada aahnlptqvt sfvgrhfera elgrlveayr lvtvlgagga gktrlavela
      241 sgivenypdg vwfvdiaavt dpglvafeia avlglrpepg rpmvdtlvey agprrmlvvl
      301 dtcdaqpaas aevisrllag grgvrvlats resfgvpgev vwripplsvd egpgvggsda
      361 vallldrtaa arggrapevt eqedlrrvvr rldglplaie laaarlrvls agqlaerldd
      421 mlgtldagrd saepppveag wsgnqqdtvd lvaaatgsap ptpasravqr saserhltiq
      481 atvtwsyrtl garssrllrw mavfagpvdl ptvqwllded pldplsvlvd ksmvlaepha
      541 sgstyrmldp irayaarrli stgeeqtard rhvawsrhal drahlgpdgr pvtlslyald
      601 plagelraal rwcatggsar sglhlaggld qwwrerglar egrlwlfrly griaetgeei
      661 peaelaaayh mhslhagadg efaeelrysq raeaaarqag dlgllarvla graaplvdmg
      721 qfaeaervcr evldwayaqd vvgdallavy nlaellwrrg aldeaaevlg aarpveatrp
      781 vergrrsvdm llgmvalgrg dlvaahehll valrsrmshg ylgracdtin aiavrcalag
      841 davaaarlfg aaqatraslr atpgiyepyw larqaelrrs lgdeafdaay gagaglrlde
      901 aaamalhveh pdlsadsfwf gpsssrpaae prstag
//
LOCUS       WP_181569574             231 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Micromonospora
            robiginosa].
ACCESSION   WP_181569574
VERSION     WP_181569574.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 231)
  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 231)
  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..231
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..231
                     /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=25105
     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 mlywllkyii lgpllrlvfr pqveglahvp atgpvilasn hlsfsdsift plivkrkvtf
       61 iakaeyftgr glkgwltklf fvgsgtipvd rsggraaraa ldtqlqvlra ggiagiypeg
      121 trspdgrlyr gktgvarlal esgapvvpma mlnsdaiqpt gqiipnlgrv rirfgppldf
      181 sryaglagdr fveravtdei myelmdlsgr eyvdtyaqka knppprqpvp a
//
LOCUS       WP_181570165             145 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora robiginosa].
ACCESSION   WP_181570165
VERSION     WP_181570165.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=14799
     Region          3..144
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 myisaradya lramlavada gatgdglsgg elvkaaslad sqdiplsflq gilldlrrae
       61 llhshrgteg gyaltrppae isvgdvlrav ggaltsvrgl padragyhgv atglrdvwla
      121 vdgaialvvd rttladllad rtpap
//
LOCUS       WP_181570540             268 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Micromonospora
            robiginosa].
ACCESSION   WP_181570540
VERSION     WP_181570540.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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..268
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..268
                     /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=28626
     Region          9..260
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtsrvpvlls tssvfperta aafqlasalg ydgvevmvwt dpvsqdagal rglsehygvp
       61 vlsvhapcll vtqrvwspdp werlrraael aetleaptvv vhppftwqrd yartftdgld
      121 aiagqfgglr favenmfpvr magrqfvpyv pgwdptdtgy asytldlshc aashtdalam
      181 adrmgaglah vhlgdgtgeg rdehlvpgrg gqpcaellrs lagrgftgsv avevttrgak
      241 sravreadlr eslefaranl tapspvda
//
LOCUS       WP_181570514              74 aa            linear   BCT 28-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Micromonospora robiginosa].
ACCESSION   WP_181570514
VERSION     WP_181570514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 74)
  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..74
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..74
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7137
     Region          1..46
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mpryefrcra cgdtfevnrp maeagrpatc phghadtvkl lstvaftgrg gagpvggapa
       61 paggggccgg acgc
//
LOCUS       WP_181570548             441 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Micromonospora robiginosa].
ACCESSION   WP_181570548
VERSION     WP_181570548.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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 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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..441
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..441
                     /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=45943
     Region          20..389
                     /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(29..30,33,36,69,119..120,122..124,127,147,150..151,
                     154,229,232..233,236..238,241,268,272,321..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 mrtvrgwfrd tagglprsfw ylwtgtlinr lgsfvlifla iyltrergfs aaqaglvigl
       61 wgvggavgtt vggiltdrwg rrptlltahl gaatmmvalg larplwavav galllgtfae
      121 aarpafgamm vdvvpekdrl rafslnywai nlgfacaavl agfaaeagyl llflvdaatt
      181 vvtaliiftr vretltrpaa pvakgaaapa galrtilrdr vflgfvalnl faalvflqhi
      241 smlpiamvds glspatygsv ialngvlivi gqlfvprlir grsrshvlal aalimgvgfg
      301 ltafadtiwl ygltvliwtl gemlnspsna tliaelspaa lrgryqgvfs lswqlagasa
      361 pilggllreq agntalwlac agigavtava hlvsgparer ravqlraagv paapvtlart
      421 papeaaeaaa tapaepartg s
//
LOCUS       WP_181570140             312 aa            linear   BCT 28-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Micromonospora robiginosa].
ACCESSION   WP_181570140
VERSION     WP_181570140.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=33537
     Region          1..311
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mrdiavfsgt ahpelaaeic ahlavplhpv rvsrfandcl evqlqancre rdvfliqplv
       61 ppvqehlvel llmidaarga saaritvvlp hyayarsdkk daprisiggr lvadlltsag
      121 ahrvlamtlh spqvhgffsv pvdhlhalre laahfrghdl snavvvspdl gnakeaaafa
      181 rmlgtpvaag akqrfsddrv qistvigdva drdvivldde iakgstvvel ishlrerrvr
      241 sirlacthgl fssgalerls aqdgvleivc tntvpipvek rvpklevlsv apalaeamrr
      301 ihngesvsal fg
//
LOCUS       WP_181570385             492 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Micromonospora robiginosa].
ACCESSION   WP_181570385
VERSION     WP_181570385.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 492)
  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 492)
  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..492
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..492
                     /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=50342
     Region          9..371
                     /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 mtdpagagal paeglpatrv ldeiralraa drpthggrlf ayvydpdvag ldelaqaaya
       61 qsahvngldp tafpsllame nalvgaaarl lgggpgtdap dvvgsvtggg teslllavka
      121 ardarpdlae privvpasah aafakaahyl rvaldrvpvd pvtlrpavda vaaairpetv
      181 lvvasapsya hgvvdpvagi aavaadagvr chvdacfggw alpwlrrlgl pvppfdfavp
      241 gvtsisvdlh kyaytpkgvs vllhrdaarr apqffayadw pgytmvnpvi astrsggpia
      301 aayatlrhlg edgylrlaas trdavaglag avratdglrl maepestvvc ftaddpkldl
      361 fvlvdeltar gwhtqpqlry adlpasvhlt vtaavaprva efapaladav aaaraagpva
      421 lppeltalag gltpealtpe lvaglaeglg lgggagapek mavvntllda apapvrerll
      481 aefvgllqrp tw
//
LOCUS       WP_181571050             293 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Micromonospora].
ACCESSION   WP_181571050
VERSION     WP_181571050.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
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   Wintjens,R. and Rooman,M.
  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 293)
  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..293
                     /organism="Micromonospora"
                     /db_xref="taxon:1873"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32623
     Region          14..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..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mserrsptir rrrlgaelrr qreaagitie vvaeqlecsa skvsrietgh ttatprdvrd
       61 mlriygvvga esdelvqiar earqkgwwhp ystvlvgayv gleaaasqir ayeqqvvpgl
      121 leteeyagam iraarpdfta eqieqrvrvr lgrqslltqd dpvdlwvvld eavlsrpvgg
      181 davmrgqlkr lvevaelpnv tvqvlpfevg ahagmdgtft ilsfpepsdp dvvyaenatg
      241 glfleksdel qkysfifdhi raaairpees vahiaklaee plwkwrprss pwt
//
LOCUS       WP_181571160             360 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Micromonospora robiginosa].
ACCESSION   WP_181571160
VERSION     WP_181571160.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..360
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..360
                     /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=38134
     Region          15..357
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mgvfastddp gatgheqvvf cqdkqsglka iigiystalg palggtrfyp yaseadalad
       61 vldlsrgmay knalanldlg ggkaviwgdp dqlkseallr aygrfvesln gryytacdvg
      121 tyvadmdvia retryvtgrs vehggagdss iltawgvfqg mraaaehvwg sptlagrrvg
      181 vaglgkvgky ltthlisdga evvatdvnpr aqewvrathp qvtlvhdtaa lvasdidvya
      241 pcalggalnd dtvpvlrakv vtgaannqla hagiekvlad rgilytpdyv vnaggviqva
      301 deiegfnfer aklratrifd ttreilrlad degvppavaa drlaerrmad vgrlraihlr
//
LOCUS       WP_181571343             454 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Micromonospora robiginosa].
ACCESSION   WP_181571343
VERSION     WP_181571343.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..454
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..454
                     /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=48815
     Region          205..307
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
     Region          309..>400
                     /region_name="DCC1-like"
                     /note="DCC1-like thiol-disulfide oxidoreductase; cl01136"
                     /db_xref="CDD:470091"
ORIGIN      
        1 mtaarylala vplaavivtg rherdrnvra aallaflaam vgiaalneva rstawygfap
       61 vrgtyrgmpi dlwigwaalw gplpvllrra lplplalgll lwldavampa lhplvrlgph
      121 wlvgellglv avalpaqmlg rfcadrrhlp arallqvalf aavllwflps vafevgdgsw
      181 trltalppsa avlvaqvall vatpaliavr efvvrgggtp ypwdppgrlv ttgpyaylan
      241 pmqlggvalt lflgvltgsg tllltagaav afstavagph erhdlhtrhg dswhdyrrqv
      301 rtwwprwrpy aperpavlwl dddcgpcgat wrflarrdpv glivrpareh pgvlwragya
      361 ggdgheergv aavaralehl hlgwalvgwt lrlpgvtwla qlttdamiap phpvkprgep
      421 cptpssasst grsrqsvsta spasrrgpsr prpe
//
LOCUS       WP_181571261             192 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Micromonospora
            robiginosa].
ACCESSION   WP_181571261
VERSION     WP_181571261.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..192
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20085
     Region          50..184
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mltrrlaaal lvavtagtal vgctsgsdes rcaadgltvt capdqrsktp kvsgellggg
       61 nydiardrgq vvvvnfwgsw capcraeadd ledtyqatkg dgvtflginv qdskdkaaaf
      121 easygvtyps lfdpasrqal nfdippnstp atvvldrdgr vavvirravt qdelrpivak
      181 iaaekpapng sr
//
LOCUS       WP_181571454             113 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            robiginosa].
ACCESSION   WP_181571454
VERSION     WP_181571454.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Rosinski,J.A. 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 113)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..113
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..113
                     /product="helix-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=12209
     Region          17..83
                     /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 mttmattpse dgsrrnwtfl tnhghvllai arnptarlrd vadevgvter aaqaivadle
       61 sggylhrtrv grrneytinp sgrfrhpaea dqqvgalldl favesvadpg tep
//
LOCUS       WP_181571547             207 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Micromonospora robiginosa].
ACCESSION   WP_181571547
VERSION     WP_181571547.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 207)
  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 207)
  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 207)
  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 207)
  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 207)
  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..207
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..207
                     /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=22938
     Region          59..197
                     /region_name="SpoU-like"
                     /note="SAM-dependent rRNA or tRNA methylase related to
                     SpoU; cd18096"
                     /db_xref="CDD:349969"
     Site            order(132,134,154..157,160,174..175,177,183..184,186,189)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349969"
ORIGIN      
        1 mtddqldvgv gpwpgdppad prldpellaa gdrrnvvdry rywrreavva dldrrrhdfh
       61 vaienwqhdf nigtvvrnan aflaaevhiv grrrwnrrga mvtdryqhvr hhptieefva
      121 waagerlpvv gidnlpgcrp letgvlprrc vllfgqegpg lspvartacd alfsiaqygs
      181 trsinagvas giamhawirs yagpppg
//
LOCUS       WP_181571805             329 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Micromonospora robiginosa].
ACCESSION   WP_181571805
VERSION     WP_181571805.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=34847
     Region          22..316
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtgpviaaas ptagsdaraa lhrlrtevgk avvgqdavvt glviallcrg hvllegvpgv
       61 aktllvrtla taldldskrv qftpdlmpgd vtgslifdpr taaftfregp vftnlllade
      121 inrtppktqs allevmeerq vsvegerrpl pepfivaatq npveyegtyp lpeaqldrfl
      181 lkltvplpgr deelgvlrah hagfdprdlr aagvravaga adlaaaraea havhvaepvl
      241 gyivdlcrat rsapalelga sprgatalla takawswlag rdhvtpddvk avarptlrhr
      301 lrprpevele gvtadavlds vlatvptpr
//
LOCUS       WP_181571092             204 aa            linear   BCT 28-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Micromonospora
            robiginosa].
ACCESSION   WP_181571092
VERSION     WP_181571092.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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 204)
  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..204
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..204
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=21398
     Region          1..204
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mrirpvgaha llldcddaeq veawraelwr rraagdlaav divpaaltvl ldgvpdpett
       61 aariagwhpr ataagadaae vrvptvydga dlpavaehwg vdvptvvdrl rrtrfrvafc
      121 gfapgfayla glppelavpr latprtrvpa gsvalagpya giypaaspgg wllvgrtemv
      181 lfdvhadppa rltpgtpvrl vpas
//
LOCUS       WP_181572019             135 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Micromonospora
            robiginosa].
ACCESSION   WP_181572019
VERSION     WP_181572019.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   Rosinski,J.A. 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 135)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..135
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..135
                     /product="helix-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=14145
     Region          42..>79
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mnsptnhadq ttrtttdstt tapdvgevwt iericalgvt ttlattasvl gisrsqayrl
       61 aaadqfpvpl iragsriivp vaallhllqp dpaatggggr ldadakvsvd amppppadst
      121 rhrwrhhpeh pgdde
//
LOCUS       WP_181572036             340 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Micromonospora robiginosa].
ACCESSION   WP_181572036
VERSION     WP_181572036.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 340)
  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 340)
  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..340
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..340
                     /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=35476
     Region          103..337
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrdlalifgv alaaalavgl vgavalrslr grsitvhisv llamtvaava agvvgvaqam
       61 flsphdlqvv litvsaaavv slavgwlfar rlaaaavwad qararerrie kgrrdlvawv
      121 shdlrtplag lramaealed gvvddpatva eyhrrirvet drmtrlvddl felsrinaga
      181 lrlslstval gdvvsdalag aaplaaarri rlvaaeagwp tvtaserela rvvgnlllna
      241 irytpadgtv wvdagrdvdt awlavadtcg gipeddlprv fdvafrgepa rtpaaaepgg
      301 sgglglaivr glveahggrv evqnvsdgcr fvvrlpavgi
//
LOCUS       WP_181571491             567 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Micromonospora robiginosa].
ACCESSION   WP_181571491
VERSION     WP_181571491.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 567)
  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 567)
  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..567
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..567
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=61406
     Region          267..305
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          311..339
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(312,315..316,319..320,322,346,349..350,353..354,
                     356..357,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          317..566
                     /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          344..374
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          379..407
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          413..441
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          447..475
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(448,451..452,455..456,458,482,485..486,489..490,
                     492..493,515,518..519,522..523,526)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          480..510
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          514..542
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtggperydc hrdhgpyagv saflgrvaad rprlaarhtv elraiapqld paarpaaeee
       61 pirfhparrt aylaygaael vaawagtlrr pvtvrfdhva sadettaell dalarrlgst
      121 pvrldlrdda asdpapdert pqalrralgd glaggfyhha arvarrgrat vtpdgdlrhw
      181 wafttglata laaldraaea ldlydearav tddpkitmsa ayatamlhar hlpaadqdpe
      241 qarlwleral hlaagladpr qrllstvfye qglalldsra grpdralrlv ddglarltaa
      301 lgpgerpqdl arlrhnraqv hlalgdptra ladldtviah dpdnceyyvd raalyraagr
      361 trdairdyda airlgphlpe ayynravlqq ergrpgrara dlervlaidp ghldarialv
      421 nlhvergald aaeadaragl agapqdpall ctlglvraer ggpaeadell tralsedpdl
      481 veawtnraav rfergdvaaa ladldraval saapvprynr gtalarlgrw deaahdfaqa
      541 laqpglnral rrdlraelar crralag
//
LOCUS       WP_181572070             887 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Micromonospora robiginosa].
ACCESSION   WP_181572070
VERSION     WP_181572070.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 887)
  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 887)
  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 887)
  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 887)
  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..887
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..887
                     /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=93770
     Region          13..864
                     /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"
     Region          <520..>625
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 matgdprnsv ppgrarpffg fvgavgavav lvsagplaal parltelpva fwtmaalava
       61 cdarpfvppg rrqtsalfps tcftfaillg wglgpavavq avavavsgwr lgyaawrtgf
      121 naaqyacala aayavshlgl gelfdggrlh wtdvaalgga tvawfvvnyg lvnsairlrf
      181 gdrwwpsvrl glayellstg sllllapvlv atarasaali plvlvplfav yrmarlsaer
      241 eqladvdplt glpnrkallt evaeqvhvha eraargepda hlalllldld rfkhvndalg
      301 havgdrllve vsarlidvad egelvarlgg defaivvprl agvdearera drvvaalaep
      361 vpldglpldv ggsigvalfp dhgedfatlm rhadvamyda khrndtvavy apesdhnsae
      421 rlslladlrr vlespvsapp eepvgvrggd gaalapslpa arparderrs rderpahder
      481 rshddgpgga rpgagparwr lrrrrepvea rsddelieri ltgadpirrr avastapgah
      541 aastasagpt asagptasav saeatpvtsa vdvgtadtqv aevtevaeva eavgrpdgep
      601 agpgdvaava ggradpddpa gdpgeitmyy qpqiaiatge vvgveallrw rhprrgmvdp
      661 geliqvaeqs avmrlltrrv vddvveqlak wsaagltlra alnvsvrdlh tgeiadqiad
      721 rltrygvppe rlqveitega lmadprrvla sitqlhrigv gialddfgtg ysslqhlrrl
      781 plsevkvdrs fvlgmaddpd daaivrsmie lagalglrvv aegvedertw rllhaagcdv
      841 aqgwfharpm paeelitwls ryrpvrpapv eadgrggpae geskass
//
LOCUS       WP_181572446             335 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Micromonospora
            robiginosa].
ACCESSION   WP_181572446
VERSION     WP_181572446.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=35950
     Region          15..308
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mdgaddkrpv taenrtprsa vvvnpvkvad ldefrrivdg aldaagwpap twhkttvedp
       61 grgqaeeavk agaevvfacg gdgtvmacvt alagtdvala vlpqgtgnll aanlglsndl
      121 aaglevaver gmrrldvgvv ddqcfavmag mgfdaqmlds tsettkkrig wpaylvgaar
      181 hlrdrpmrvs vridgrpplr rrarsvlvan vgrlqggvrl ltdaepddgw ldvavltprt
      241 lghwlamgwa lvrrtgsvpr mevfrartve iasnraqprq ldgdliepgr sltatirpes
      301 lwlcvpqped hpdlaedaka aaergerlve darre
//
LOCUS       WP_181572376             745 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Micromonospora robiginosa].
ACCESSION   WP_181572376
VERSION     WP_181572376.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 745)
  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..745
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..745
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=79277
     Region          4..745
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          536..564
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          576..604
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(577,580..581,584..585,587,617,620..621,624..625,
                     627..628,657,660..661,664..665,668)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          615..645
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          656..684
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          696..722
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mfgeavrelr rrcaltqeal aekaglsvrh vrdleagria rprpatmmll adalalhgpe
       61 rerflagssa sadggavpaq lpadgfgfvg ragalarlde iltraadqpt amglavvsgt
      121 agvgktalav hwahrvaahf pdgqlhvdlr gfdpagtpvs pgtalagfvn alagagerpp
      181 aglaeqvary rsllsgrrvl vvldnagdad qvrpllpgap gcfvlvtsra qflglvsvng
      241 aqpvtldvms gaearellsr rlgaqrvtae pdavdaivla saglplalsv vaaraavhpg
      301 frlaelaael hpvagrldaf dggepvtdlr rvmswsyrtl dagtarlfrl lsvhpgpdft
      361 lpaaaslagt apaqtrrdla altrahllte hrpgrftchd llrayaaelt aaedgeadrh
      421 aararlldhy ltvayaadel vypqrdrlpv dppgpgvtpv pladrdqalw wfteerpvll
      481 salrlagghg fdrhtchlaw aittylnqrg ywedwtgslr aalsaaerlg ddrleayahg
      541 vlgfagisrd rladarhhle sayeryrrlg dlagqarvel nlgwihdrtg qpeqalahar
      601 ealrlhrrag hvtgqafaln avgwshaqlg dhraaiesce qalalftsag nvlgqaitwa
      661 slghahlqld afpdavgcyr havrlrreig hrqleadalv slgdahlaag dagsarqvwq
      721 qardilasla eagtdtvdak laalr
//
LOCUS       WP_181571652             584 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Micromonospora robiginosa].
ACCESSION   WP_181571652
VERSION     WP_181571652.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     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=61029
     Region          1..450
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          516..582
                     /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(539,548..550,557)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            549
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mrkvlianrg eiavrvirac rdaglasvav yadsdrdalh atladeayal ggdtaadsyl
       61 ridklidvaa ragadavhpg ygflsenadf aqavidaglt wigptpqair dlgdkvtarh
      121 iaqragaplv pgtpdpvaga devtafateh glpvaikaaf ggggrglkva rtmeeiphlf
      181 esatreavaa fgrgecfver yldqprhvea qvladqhgnv ivvgtrdcsl qrrhqklvee
      241 apapfltdaq raqihdsaka icreagyhga gtveylvgad gtisflevnt rlqvehpvte
      301 etagidlvre qfriadgdkl ritedptprg haiefringe dpgrnflpap gtvtalrlps
      361 gpgvrvdtgi sagdviggnf dsllakviiv getrtealer arraldemvv dgmatalpfh
      421 rlvvrdeaft sepftvhtrw ietefdntvp aftaaagaae apaeretvvv evagkrievv
      481 lpaglgagta aaapaarkpa rrggtgkaga avsgdtlasp mqgtivkiav adgdtvaegd
      541 lvvvleamkm eqplhahkag tvkglaaevg avitagapic tieg
//
LOCUS       WP_181572667             256 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Micromonospora
            robiginosa].
ACCESSION   WP_181572667
VERSION     WP_181572667.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 256)
  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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..256
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28079
     Region          4..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(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"
     Region          73..249
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manevlrvam aekgetsesl aakvrvdpkt aarwlaagri phpqtrvava evlgravael
       61 wpepfrrrdl pwfrpwvele qdatsfrwye pllvpgllqt egyahavlst galfapavvd
      121 eivagriarq rvldrddppq lvavidevvl rrpvgdrsvm vgqlghlaav agrehvqvrv
      181 ipadgpwhtg lagpfvlgrl pdgtelayld nqlrgqvvtd pvdvaslgrr wesvtgealt
      241 qrrsielirg vaetwt
//
LOCUS       WP_181572477             151 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Micromonospora robiginosa].
ACCESSION   WP_181572477
VERSION     WP_181572477.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
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   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..151
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..151
                     /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=16398
     Region          2..140
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mqisargdya vraalslata yptllstqai aaeqdmprkf leavladlrr sgivraqrga
       61 eggytlsrpp revtigqvlr avdgplagvr gmrpeetkye gaaenlprlw vavrasvrrv
      121 vdevsldelv sgrlpahvrk lttqpdawep r
//
LOCUS       WP_181572703             345 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase [Micromonospora robiginosa].
ACCESSION   WP_181572703
VERSION     WP_181572703.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 345)
  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..345
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..345
                     /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=35843
     Region          21..337
                     /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 mgrdgepvgg ptdadwaaav eavrvlrada rvllvchvnp dgdalgsmlg falglrrlgv
       61 rhlqatfpgp agapepfrwl pgvellvpqd daypapdlmi cfdaasesrl gdlagrlata
      121 gtslvldhha sntgfgrvnl vdphaaatsv valglldrlg vtldapmatg lyvalttdtg
      181 sfrfeattpa vhemaarlla tgirpgdisr rvfdtrpfga vrlfgevlgr atlepeaaag
      241 hglvwayatr ddlarhgqpa yvlealidpv rctaeadvsc vvkqsgeaew avslrskgav
      301 dvsrvavglg ggghrfaagf tghgpldevi atiraalppp syphp
//
LOCUS       WP_181573614             561 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Aerococcus].
ACCESSION   WP_181573614
VERSION     WP_181573614.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus
  ORGANISM  Aerococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 561)
  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 561)
  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 561)
  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 561)
  AUTHORS   ter Beek,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 561)
  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 561)
  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..561
                     /organism="Aerococcus"
                     /db_xref="taxon:1375"
     Protein         1..561
                     /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=62002
     Region          2..527
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mlkqhsqlfw rlifsfialt vficplltii ikgietpagl gfenfalifd ssrtfqaikn
       61 tlilglgstc isfifgllva iivaytnirf kkafelltil pfvipgyimt lswtsvfafn
      121 spmnslltql klpmvnlysm ggmifilgls naalvylnvi dilkkvpieq ewasrisgyn
      181 ivstlkninl psakygiang iilaflsaid nfaivstlgt psgipvlsty iyekaigfgp
      241 hsfneaavls iilsliaftg vafraymlrk svaidterar sndriqltpk yrrtvegmmf
      301 iilltlnilp lvtmffsslq vgysrsifdv snmaldnyaf ilqtpsmyng fwnsfilttl
      361 ailvclmlsi fatyyksrid skatsllelg asitystpgi vlalsmilyw snvpnvygsl
      421 lilfiayitr yflvifngss taitsipvdl eqsaqisgsk qpqiwrkiil plmkgqllss
      481 sflmfssalt eltlssllaa antktiglti ynlqtsgdtn taqaysvllt lfillllfcr
      541 nyflakeeks idgsndnysv k
//
LOCUS       WP_181571987             238 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Micromonospora robiginosa].
ACCESSION   WP_181571987
VERSION     WP_181571987.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora robiginosa
  ORGANISM  Micromonospora robiginosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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 238)
  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 238)
  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..238
                     /organism="Micromonospora robiginosa"
                     /db_xref="taxon:2749844"
     Protein         1..238
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25025
     Region          76..236
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mssrkgrrda arvvreqiar ekrrkrtlwt tiaavlvlvi aggigwavys sqksdgftap
       61 pgandagtgi vsgsgpvtvd lyedylcpic kqfqqtngat lnqlvsegka klvfhpvafl
      121 nrfsttqyst rssaasgcaa kggkfreftd qlfarqpaeg saglsddeli digagvglnr
      181 ddfascvndg tytswtehvt eeasksgvtg tptikvngte vqdkspdgik aavaaagr
//
LOCUS       WP_181573811             493 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Klebsiella pneumoniae].
ACCESSION   WP_181573811
VERSION     WP_181573811.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=53915
     Region          20..489
                     /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 mtamstlnpi lagsaqsvea yqqvieqtsq avvqwlkqpe myqgksvdel rerislefne
       61 qglgnqaaid raieyfltds lsvhhpqcva hlhcpslvis qaaevlinat nqsmdswdqs
      121 psatiiemkl iewlrarvgf pagdagvfts ggtqsnlmgl mlardaffar qghsiqqdgl
      181 pgdirkykvl csenahfsvq knmalmglgy rsvtlvktde farmdvsdlq akiaqaqang
      241 eqimaivata gttdagaidp lrdiagiaae hqiwlhvdaa wggalllseq yrdyldglel
      301 vdsvtldfhk qffqtiscga fllkdarhye lmryqaayln sefdeehgvp nlvskslqtt
      361 rrfdalklwm glealgqkqy aaiidhgvtm aknvaeyvks qptlelvmqp qlasvlfrsr
      421 paqmagsdaa viallnqrvg dallasgran vgvtehngvt clkltllnpv vtlddvkvll
      481 nlvertaqel laq
//
LOCUS       WP_181573846             337 aa            linear   BCT 28-DEC-2024
DEFINITION  phage tail protein, partial [Escherichia coli].
ACCESSION   WP_181573846
VERSION     WP_181573846.1
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 10506211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>337
                     /product="phage tail protein"
     Region          31..68
                     /region_name="Phage_fiber_2"
                     /note="Phage tail fibre repeat; pfam03406"
                     /db_xref="CDD:427282"
ORIGIN      
        1 aeaaakseqs akqhrdeaqr ivddlkgtna sttqkglvql csdtdndsee laatpkavkt
       61 vmdetktkap ldspaftgtp ttptppddav gletanaafv rkllaalvds spealdtlne
      121 laaalgndpe fattimnala gkqplsdvlt aisnleerad nllcfnqdgn aslsplseka
      181 rsllaqatve amrnelelks aavkdiqtyl ydssegrial pgafgygmtn pgstaiiasd
      241 mfdvartahn vhpgryytfs tqteettgit eiiwldngwg dktsqtatkl vlffgkdgri
      301 lmtvrgdnis apvtwtnltp qlgnaaqkda qeniydr
//
LOCUS       WP_181573777             330 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Escherichia coli].
ACCESSION   WP_181573777
VERSION     WP_181573777.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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..330
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..330
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38202
     Region          7..>177
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mspnyipkvs vivpvynter yveraiislm eqtlddvqfi iiddgskdns lniikqviar
       61 yparqgqvtl isrenrgvaa traqgmelat gdyvihldsd dwaelnwlea lytkaiedna
      121 dvvicdyykv yknkkievsq nvlpspyncv kqlfnrklsn sncdklvrkk ifddneisfi
      181 dgldmgedfl vtllvllnsk kisyinkply yynknndssl tksysnkaly dlvkvvdlad
      241 nymkekgile fflhemnmfk ldvksliiln snnnidlvny afnlypntnk liigsnmktl
      301 kfvyilrslr llsfykyivr frilikkifn
//
LOCUS       WP_181574121             185 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HIT family protein [unclassified Microbacterium].
ACCESSION   WP_181574121
VERSION     WP_181574121.1
KEYWORDS    RefSeq.
SOURCE      unclassified Microbacterium
  ORGANISM  unclassified Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 185)
  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..185
                     /organism="unclassified Microbacterium"
                     /db_xref="taxon:2609290"
     Protein         1..185
                     /product="HIT family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19901
     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 mtgssdtprp vedaarlagv pdefqrlwtp hrmayiqagp eplrdecpfc aapgksdadg
       61 livargrtay vllnlfpyns ghllvcpyrh iptydlatae evaeigaltq tamrvlrevs
      121 rcdgfnlgmn qgavagagvd ghlhqhvvpr watdanffpi iaktkalpql lgevreavag
      181 awptd
//
LOCUS       WP_181574206             300 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Microbacterium sp.
            SMR1].
ACCESSION   WP_181574206
VERSION     WP_181574206.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. SMR1
  ORGANISM  Microbacterium sp. SMR1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (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   2  (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   3  (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   4  (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   5  (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
REFERENCE   6  (residues 1 to 300)
  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..300
                     /organism="Microbacterium sp. SMR1"
                     /db_xref="taxon:1497340"
     Protein         1..300
                     /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=31206
     Region          10..264
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 maassrladl sgltvvvvga stgigrgval raasfgaavv vfsrrpdalt slverirdsg
       61 grahavagdv sragdlerla deaetvfgri dvwahnagvg tiglfgdvpi eehvrvvetn
      121 ligamrgahv alrrfiaqgs gvlvntasve svvplayqas yaatkaglls ltqtlqqelr
      181 ltgvsgvava avlpwavrtp fwrhagnhag ralrmplmde pepvvdailr aglrprvaqp
      241 agwkarasli garlaprvta rlsadiadar vrrgaktpps dgalfeplad patvaetprr
//
LOCUS       WP_181573828            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181573828
VERSION     WP_181573828.1
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=166391
     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 eqfryplwqa kpfepqqgvk
      181 legassnfis pqpgniyipl gqqepglylv eamvggyrat tvvfvsdtva lskvsgkell
      241 vwtagkkqge akpgseilwt dglgvmtrgv tddsgtlqlq hispersyil gkdaeggvfv
      301 sekffyesei yntrlyiftd rplyragdrv dvkvmgrefh dplhsspivs apaklsvlda
      361 ngsllqtvdv tldarnggqg sfrlpenava ggdelrlayr 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 arikvavpql 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 pqkifrnnld 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_181574278             324 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Microbacterium].
ACCESSION   WP_181574278
VERSION     WP_181574278.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium
  ORGANISM  Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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..324
                     /organism="Microbacterium"
                     /db_xref="taxon:33882"
     Protein         1..324
                     /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=34438
     Region          88..304
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnpsrsearr arilgivlai vcagfvvaai gsllvflllg velpwaavlv favagagtlv
       61 tvwlvgwpll atppreaaaq dafdaaveaq rrllddvrhe lktpiaivrg hlelvdaddp
      121 advdavreis igeldrmtrl igdidllasv egerfaldev diesltqrvv dlvtvipghd
      181 wavestqrgi ihgdadrllq awlqladnaa khtpvgtaie lgsgiyagaf hlwvrdhgpg
      241 ippaarhrif rrfdrggrrr svggsglgla ivdaiakghg gsctvtetag ggatftitip
      301 lrsarrlpap vradevvlqr keig
//
LOCUS       WP_181574450             443 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Odoribacter splanchnicus].
ACCESSION   WP_181574450
VERSION     WP_181574450.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 443)
  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 443)
  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..443
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..443
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51629
     Region          305..441
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkivfvlscw flweaqafsq vkvrfdatfg qeeirigfre qaykvkldes gvgritipds
       61 lapgyaalyg prnvysfylv pgqqqeitkl ngqeikftga akainiylns pflnnrdpgy
      121 ekgeeeflke walmpgrlqa hldslplpad fkkserkrly yvachslldy pllharllrl
      181 ksyspgeryy rkvsellqed psahefweyr qffrngiqll gekkktetgk pldklkceld
      241 yicnhikdee lasylvdesm sgyiryfgte gmeaflplyr ekvkdekqka affrsyeqyt
      301 rlekgrkaph fslldkdgnr knlsdwlgny vyidvwatwc gpccrelpaf hklkeefkdk
      361 picfvsisid adeaawrtki ekdsldgiql rvneedtfkk dykiswiprf llidregkvl
      421 danmtrpsdt ktiekltall sdr
//
LOCUS       WP_181574726             426 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Lysinibacillus capsici].
ACCESSION   WP_181574726
VERSION     WP_181574726.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus capsici
  ORGANISM  Lysinibacillus capsici
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..426
                     /organism="Lysinibacillus capsici"
                     /db_xref="taxon:2115968"
     Protein         1..426
                     /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=47393
     Region          24..423
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mnectkfift lkavdhkrap lvlmrevlgh ldephnklrv ihvagsngkg stvnalreml
       61 qhagytvgaf tsphlervne rmtinghqis deqflyyfnk lakiieehyn gefpsffevv
      121 tlimfqyfah egvdialiet glggrldatn vvtpllaiit tislehtafl gdtfakvaae
      181 kagiikegip vvvgvhneea lavikataee rhascfvlgq dftvtnswqc tdyqhftyek
      241 ahvlmkdvpl kmagqhqinn aslaitailt lreqgaivit ddsicqglqc aqwagrfeqw
      301 pnqivldgah nsegtaaliq tlknvyprnn yhfiyaalad kdhansielm davatsitft
      361 qidlpnampa eslamlstha nkmvhtewlk slqtllqerq kedivvitgs lyfiaqarqw
      421 lqeegr
//
LOCUS       WP_181574832             572 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: dipeptide ABC transporter ATP-binding protein
            [unclassified Actinomyces].
ACCESSION   WP_181574832
VERSION     WP_181574832.1
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  :: 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="unclassified Actinomyces"
                     /db_xref="taxon:2609248"
     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=61852
     Region          16..560
                     /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 mtdtsiadkr pdpdrpllei rdlqvafrss tglvpavrka nltvypgqsv aivgesgsgk
       61 sttahavigl lpgtgrvtgg kilfegqdla sasakemtal rgariglvpq dpmsnlnpvw
      121 signqvkeal rannvvpgge ldrrvtellt eaglpdaarr akqyphefsg gmrqraliai
      181 gmaadpslli adeptsaldv tvqrvildhl qtltrergta mllithdlgl aaeraehlvv
      241 mhrgrvvesg psleilkdpq hpytkrlvqa apslashrie qahargvett deellgagmg
      301 qvstedvlrv ehltkvfpvr gakgkantlk avddvsfglr kgttlalvge sgsgkstvan
      361 iilnlidpts gkvfhhgtdl stlnkrelfg lrrvmqpvfq npygsldpmy svfssveepl
      421 rvhrvgtrke rerrvaelld mvalprsamr rypgelsggq rqrvaiaral alrpeivvld
      481 eavsaldvlv qaqilkllsd lqaelklsyl fithdlavvr lladdvvvme qgrlveagps
      541 delfahpree ytkrlieavp gagidlyraa td
//
LOCUS       WP_181574874             816 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 3 protein [unclassified
            Actinomyces].
ACCESSION   WP_181574874
VERSION     WP_181574874.1
KEYWORDS    RefSeq.
SOURCE      unclassified Actinomyces
  ORGANISM  unclassified Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 816)
  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 816)
  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 816)
  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 816)
  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 816)
  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 12028645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="unclassified Actinomyces"
                     /db_xref="taxon:2609248"
     Protein         1..816
                     /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=86164
     Region          20..258
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          312..382
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
     Region          568..>808
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mnqyevdhla tvragapesm vllkadgsfp laapgrialy gagarrtikg gtgsgdvnsr
       61 hvvtleegle nagftittkp wldaydgvae enhktfvadl kaqakaagqp aiyfgmgave
      121 papafdlpld gdgeaavyvv ardsgegndr hpdagdvklt dseirdital aakfekfllv
      181 lnvggvvdls pvkdvknill lsqlgaaigd afadvllgks ypsgklsttw aawedysteg
      241 dfgdpddthy regvyvgyry fdsvgtapif pfgfglgytt ftigapvvsa vgseitvktt
      301 vtntgtrpgk evvqvyvsvp agdldqpyqa laafaktgel aagaaeevav tfdltdvasf
      361 daaksatvle agnyvvrvga ssrntvpaav velpetaivr qlhnalgdpg ftdfkpaapv
      421 avevpadlpr ltvaaadlrr edihapvdlt daldfvkdls dddlsyivlg dysddaekqs
      481 iigqasqalv gaagqtttrf eglpslimpd gpaglrlspq vgvdadgpfa lgealgglfa
      541 elmddestaa lggaaaaprt pertyeqyat aipigtaiaq swnpelaaay gdlvgaemdh
      601 fgahlwlapa fnlhrtilcg rnfeymsedp llagrmaagi trgvqahpgr avtvkhfafn
      661 nqetnrlnsn shvsqraard lylrsfeivv reaqphalmt synlingvht sesadlleti
      721 lreewgfegl vmtdwvvdsm artdlknpra tasatikagn elfmpgcead rqdilaalrg
      781 egtaavtltr aelekqaarv vrmahllgdv apapev
//
LOCUS       WP_181574207             659 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Microbacterium sp. SMR1].
ACCESSION   WP_181574207
VERSION     WP_181574207.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. SMR1
  ORGANISM  Microbacterium sp. SMR1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 659)
  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 659)
  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..659
                     /organism="Microbacterium sp. SMR1"
                     /db_xref="taxon:1497340"
     Protein         1..659
                     /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=71284
     Region          127..564
                     /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 mpewllftia avvfsiaatw lakralearv gwvrgpvvsl ivfvvfgplg iwvlrgagvl
       61 qeqgglltdq pvafgfvllv lawlfaivli alitlelmwp arppvgpvty vrealhrrrr
      121 avryarivai asrhglggmr sesaraelpr alaatlddag vtfvklgqil strndllpae
      181 itsalaslqm dttpipwpea kaaiekqlgr pielvfagid etplaaasvg qvhsarlkdg
      241 ravvvkiqrp karaqvatdl diieraaadl errttwakdv gasalaaqfs aalreeldyr
      301 vevanmemlr dsmtaadara vripdvypdl cteqlivmeh vqgipfsrlp epgsdapgav
      361 apaeatriad avldvivgqi alrgvfhadl hpgnlilqpd givalidfgs vgiiersmrr
      421 lllpmlvalh neddsgatda vlmlvkprgd aeldvgalqh digviltrlh nstsdqhlft
      481 alievlrrhr lalppglllg frtlgaiegt lrrldpdydm ikralsrapq yalhmgdprs
      541 apmtaqvqlq lglerarelp rrvdgilsdl esgrltvrlr alespddrsw vesltgrltt
      601 tlvgatlviv gvmmgvvqhg plltdsvsvf pflgsvvglg glllllrslr salvrrdgr
//
LOCUS       WP_181575086             303 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium
            jejuense].
ACCESSION   WP_181575086
VERSION     WP_181575086.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium jejuense
  ORGANISM  Chryseobacterium jejuense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..303
                     /organism="Chryseobacterium jejuense"
                     /db_xref="taxon:445960"
     Protein         1..303
                     /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=34573
     Region          70..302
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mktpekvssi nalhqflglk kpsnplisvf nfddvnlepe tilsaittdf yvialkkeca
       61 ggkcrygqqy ydfdegimyf iaphqvlqfe dvllngvkgf vlvvhpdffq gyplasqvkd
      121 ygyfsyatne alhlsekeet svmdiihnvg neiegnmdsf tqdllvsnie lllkycdrfy
      181 nrqfltrkka nndlltklen lldgyfkndn lvingipsvh liaselnlsa nylsdmlrvq
      241 tgkttqqhiq nrliekakel lsttelsvse iayhlgfehp qsfhrlfknr ttfsplefra
      301 sfn
//
LOCUS       WP_181575123             228 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chryseobacterium
            jejuense].
ACCESSION   WP_181575123
VERSION     WP_181575123.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium jejuense
  ORGANISM  Chryseobacterium jejuense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
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="Chryseobacterium jejuense"
                     /db_xref="taxon:445960"
     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=26929
     Region          <132..224
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkkarniyle nqsystnlvy kwlfqmtllf mvvhyfatfk nilrytdnhq llifinsfle
       61 iialivtswf vlkalkypef frgvdtqlql ihdfnnetlp ktksenqqnp denitiqlel
      121 lkkymteekp yldpaltvqn laaqmnmpsr elsilinsnm nqhffdfvnk yrienamell
      181 tnhskkdctv leilyqvgfn skssfntafk khtaltptey rntfyktn
//
LOCUS       WP_181575223             134 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Actinomyces sp. Z5].
ACCESSION   WP_181575223
VERSION     WP_181575223.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. Z5
  ORGANISM  Actinomyces sp. Z5
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
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="Actinomyces sp. Z5"
                     /db_xref="taxon:2250216"
     Protein         1..134
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14608
     Region          85..134
                     /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(89,93,118)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(92,117)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(99..100,111,114,118..119)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mlsfrnvdad pvddpatwpf dakitaverg dlddyrrika acdrdpetra afldacdvlg
       61 ddpgaalvrl wleglpreer amlaarrmra aversglsra qaasrlgtst srlstylsgk
      121 vvpradlyes ilal
//
LOCUS       WP_181575712             407 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella pneumoniae].
ACCESSION   WP_181575712
VERSION     WP_181575712.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=45423
     Region          15..404
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mpkkakeltg lavsklkkeg sfavggvdgl ylrnrgqsra wvlcvtmgvr vnalgrtvpr
       61 rlymglgpyp evslaeardk arelrkqirn gidplaekha hkvqqeqray knksfascae
      121 dviaiktkel knqkhiaqwr stletyaypv igqkpiaeit kvdllailep iwltknetas
      181 rlrgrieaii dyakakeyfe gdnpaawkgm lkpllpmpsk vqtqkhhaal pyseigsfis
      241 dlqeragtsa ralefsiltv arsgevrgae wseidlkgkt wtipgnrmka gkehrvplsd
      301 aavallkalp rfkdnnlvfp aprggqlsdm sllavlkrmg hsgltqhgfr stfrdwaget
      361 tdhqrevieh alahqladka eaayqrgtlw pkrvalmddw trycfav
//
LOCUS       WP_181574876             214 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Actinomyces].
ACCESSION   WP_181574876
VERSION     WP_181574876.1
KEYWORDS    RefSeq.
SOURCE      unclassified Actinomyces
  ORGANISM  unclassified Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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..214
                     /organism="unclassified Actinomyces"
                     /db_xref="taxon:2609248"
     Protein         1..214
                     /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=22134
     Region          68..205
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 mpalprpagp ddaapfalvp aayvlllrpr kdattamate tlgaghpvgv draprspagw
       61 phgaaatevl lqlrrntgfm dghwaagiag hvepgesvta aavregaeem gvvvdpgdlv
      121 pltamhrsna vggpaleqra dffftltrwr gtptiqephk sgalrwfald alpepvpphe
      181 lkvlrllaaa ldggravpai ttfgfagapg apqp
//
LOCUS       WP_181575893             310 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Enterobacter
            hormaechei].
ACCESSION   WP_181575893
VERSION     WP_181575893.1
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   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 310)
  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 310)
  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..310
                     /organism="Enterobacter hormaechei"
                     /db_xref="taxon:158836"
     Protein         <1..310
                     /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          <7..304
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 lfvgkiteht fqavakkwld ekvktsgisq dhandiwrsl ernifptlgd tpikeirpkm
       61 lkqhlepiek rgvletlrri isrlneifry aateeliefn padnlgqrfs kpkkqnmpal
      121 ppselprflv alnnasirle trlliewqll twvrpgeavr trwsdidiet gmwnipaefm
      181 kmkkphkvpl skealrvldl mkaisghrew vfpsikapln hmheqtanaa iirmgfggel
      241 vahgmrsiar taaeesgkfr tdvleaalah skkdeiiaay nraeylterv vlmqwwsdfv
      301 ssqkykiiaa
//
LOCUS       WP_181575961             419 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Escherichia fergusonii].
ACCESSION   WP_181575961
VERSION     WP_181575961.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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..419
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..419
                     /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=46485
     Region          2..414
                     /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 mteqitvtdt lvvgagqagv amsehltnlg iphlvlekqr iaeawrsgrl dslvangpaw
       61 hdrfpnmsfp dcdgdsfvak dqiadyfesw aktfnapirt gvevlhaqal dgrpgfrvet
      121 skgvietqri vaatgpfqkp vipaiaqqns dlhqihsahy frpqqlpagg vlvigagssg
      181 vqiadelqra gkkvwlsvga hdrpprryrq rdfcwwlgvl glweasvkqp gkehvtiavs
      241 gargghtvdf rqlahrgitl vgqtlelnhg kalfgddlqe nirrgdesyl elldaadayi
      301 trnglnlpee pearyflpdp qclthplhel dlanagitsv iwatgyatdy rwlkvnafde
      361 hnqpchqrgi ssepgiyflg lpwlsrrgss fiwgvwhdak yiadhiaiqr qyqayhpsh
//
LOCUS       WP_181576028             276 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181576028
VERSION     WP_181576028.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=30485
     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 lpmgtkdlye
      121 areqvkqgir qllphskdvg vpialeplhp mtaadrsclc tlrqaldwcd eldpdgefgl
      181 gvavdvyhvw wdpdlasqir ragkrilafh vsdwlvpttd lvndrgmpgd gvinipsirr
      241 lvenagfnga ieleifspyw wqkdinstle vmlpty
//
LOCUS       WP_181576218             419 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Escherichia fergusonii].
ACCESSION   WP_181576218
VERSION     WP_181576218.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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..419
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..419
                     /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=46572
     Region          2..414
                     /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 mteqitvtdt lvvgagqagv amsehltnlg iphlvlekqr iaeawrsgrw dslvangpaw
       61 hdrfpnmsfp dcdgdsfvak dqiadyfesw aktfnapirt gvevlhaqal dgrpgfrvet
      121 skgvietqri vaatgpfqkp vipaiaqqns dlhqihsahy frpqqlpagg vlvigagssg
      181 vqiadelqra gkkvwlsvga hdrpprryrq rdfcwwlgvl glweasvkqp gkehvtiavs
      241 gargghtvdf rqlahrgitl lgqtlelnhg kalfgddlqe nirrgdesyl elldaadayi
      301 trnglnlpee pearyflpdp qclthplhel dlanagitsv iwatgyatdy rwlkvnafde
      361 hnqpchqrgi ssepgiyflg lpwlsrrgss fiwgvwhdak yiadhiaiqr qyqayhpsh
//
LOCUS       WP_181576274             282 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181576274
VERSION     WP_181576274.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=31587
     Region          1..218
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktglstway fwqlsekapk plslfdaidd shrlgatvfq icdypqiaqw ssgertrlae
       61 haaragitle lgtkgikpdh lqrylaiaae lecsllrtmi nspdhrptls earrsvetvl
      121 pafeqqgvai cletyeqvlt ddnialvqai nsarfgicld panciaslel padvvaktas
      181 yvlnwhvkdf afsrrdgwvg ftlagrplge gllryddiyq qiqpqtrgin qiiehwlpwq
      241 gdsettcrle aawtehnmry lldkqnlina sstqskesdh vc
//
LOCUS       WP_181576292             385 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Escherichia fergusonii].
ACCESSION   WP_181576292
VERSION     WP_181576292.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=44085
     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 mntysikekk evysiqyarg faalfvffsh ykdtinnslt ingrglgdfl fmnggfgvdl
       61 ffvisgfvil msteksssrg mncmdflikr ffriyplliv tvltigflrg ydmhrilisi
      121 iplhlnyasm apyfnynvly vawtityeli fyavfllama inhkyrglic illlsimfsa
      181 irvytgdgit fdtknnidis qlvfftpias vlssplilnf ilgmlsytfy kllvndfnks
      241 sylkipmill isicilflfs dsvlkghgpl kwggvsfili ttitlyedff giqkrkgwlf
      301 lgdisyslym vhpivlwima typmsyfglt qipkfifgti ivisvssisy fviersfskl
      361 arhllrkhvn kkqdnenfan tsfsv
//
LOCUS       WP_181576366             150 aa            linear   BCT 28-DEC-2024
DEFINITION  flavodoxin family protein [Lactobacillus crispatus].
ACCESSION   WP_181576366
VERSION     WP_181576366.1
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 10002233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..150
                     /product="flavodoxin family protein"
                     /calculated_mol_wt=16920
     Region          5..150
                     /region_name="FldA"
                     /note="Flavodoxin [Energy production and conversion];
                     COG0716"
                     /db_xref="CDD:440480"
ORIGIN      
        1 makktliiyy swegntknma ekinseiens elkevtvatd afdsdmyktn dialdqiqgk
       61 ipypeiqmdd idfnnydlil vgspvwsgyp atpikpllek mknyrgevas fftsagtnhk
      121 ayvshfkewa nglnvvgvar ddsevrdwvk
//
LOCUS       WP_181575082             233 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Chryseobacterium jejuense].
ACCESSION   WP_181575082
VERSION     WP_181575082.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium jejuense
  ORGANISM  Chryseobacterium jejuense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
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="Chryseobacterium jejuense"
                     /db_xref="taxon:445960"
     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=26866
     Region          8..229
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mihltskkyn ciivedepia aeiletfisr dpelnligkc sdavyasnll sihevdlmfl
       61 dlhlpvvkgf dflkklknpp fvivttayhq yaiegyeldi adyllkpipy erfvtavekf
      121 kylieaedal leiaerdhif issgkkqiki ilqdifyies lreyihihtk tetftfkmpi
      181 skieeslnpn mftrihksyi iskpkievks atvvqikgkn lpigrtykpf idl
//
LOCUS       WP_181576978             265 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Lactobacillus crispatus].
ACCESSION   WP_181576978
VERSION     WP_181576978.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            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 crispatus"
                     /db_xref="taxon:47770"
     Protein         1..265
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30039
     Region          5..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 mskiivgryi pgdsliykmd prskllvtil filaiflann sityaivtif cflavvatgl
       61 nakvfwdgvk pligliffts llqlffmtgg hiywywwifs lssyglinai yifirftlii
      121 listvmtvtt mpleiadame wllkplklfk vpvdkialvi sialrfvptl fdetfkimna
      181 qrsrgadfnd ggliqrakai tpilvplfiq sletaidlst amesrgyrss egrtkyrvls
      241 wskydlialf yfvllvglll ifrth
//
LOCUS       WP_181577021             391 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Lactobacillus crispatus].
ACCESSION   WP_181577021
VERSION     WP_181577021.1
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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     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=44846
     Region          106..371
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mlektfykmm lsksfpfpvk vtywdgksev ygngtpeiei vfngkipmgd itrnaslalg
       61 egymdkkiei ygdiqklifg ayesadsfmr sskfrkflpk qkhtekqsee dvqshydign
      121 dfyklwldpt mtyscayfed gnendleqaq iakvhhilnk lnpqkgktll digcgwgtlm
      181 ltaakeyglk vtgvtlseeq yklvqkriyd egledvaevr ledyrelgdq kwdyvtsvgm
      241 fehvgsenlp kyfqdvykyl nkdgialihg itrqqggatn awinkyifpg gyipglpeiv
      301 sdivdsglqi tdmealrrhy qrtleiwdkn fnavrnqved kmgerftrmw dmylnacaas
      361 fesgnidviq ylltkgpsgk nlpmtrdyml k
//
LOCUS       WP_181577029             308 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Lactobacillus crispatus].
ACCESSION   WP_181577029
VERSION     WP_181577029.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..308
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..308
                     /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=33174
     Region          37..305
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mkkkviwinl ilavllisti ffalthgasn fsmqkmtnsq lnilfnirvp riisalvaga
       61 slsvsgaffq atlrnpiaep gimgissaas lcqllaviil peiffgkiif aiiggllafg
      121 llllfqkkmt pyqliiigva lnavftgmqe vftnnqnsgs slatsswgst myllvigiig
      181 lifaicfmnw anylkindee ltslgvsakt lrlvlmliav vlaatttaci gvlafigiiv
      241 pqvarllfgy dyqkiipfsi fagawfllfv dtigrvitap neiaaniila ivggpvmili
      301 lwkrqkna
//
LOCUS       WP_181576865             443 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Lactobacillus
            crispatus].
ACCESSION   WP_181576865
VERSION     WP_181576865.1
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=51395
     Region          14..432
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrmsslayh fglkvrfyps skqkkiikln ydaqrfvyns yvgrnrnnyr akgylavrqy
       61 qvmpfafsvl snyetklaee vvadnellak pknirdaysf lrvkeidsla ianaiqnyqk
      121 awnnyrklgh giptfhkkrs dwsyqtncqy pkqteafldn gtakfidskh iklpklgvvr
      181 iasfrklike rllnhiptri gtvtikktad dqfylsmqlg sdiafvkelp kmqsqigidl
      241 nldnfltasn gamvanprfy rktkkklaha qrvlsrrqrr akkegrnlrl aknyqkqrla
      301 vaklhdkirr qrndflqvls taliknhdlv vaeelrsrnl lknhalsqai sdvgwrsfln
      361 mlaykadlyg kefktidpky ttqrchqcgs imgqngykkl tlkdrewtcp icrthhirdw
      421 naavnilekg lgnwqnskik kaa
//
LOCUS       WP_181576959             408 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Lactobacillus crispatus].
ACCESSION   WP_181576959
VERSION     WP_181576959.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     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]"
     Region          1..397
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 fvynsyvgrn rnnyrakgyl avrqyqvmpf afsvlsnyet klaeevvadn ellakpknir
       61 daysflrvke idslaianai qnyqkawnny rklghgiptf hkkrsdwsyq tncqypkqte
      121 afldngtakf idskhiklpk lgvvriasfr klikerllnh iptrigtvti kktaddqfyl
      181 smqlgsdiaf vkelpkmqsq igidlnldnf ltasngamva nprfyrktkk klahaqrvls
      241 rrqrrakkeg rnlrlaknyq kqrlavaklh dkirrqrndf lqvlstalik nhdlvvaeel
      301 rsrnllknha lsqaisdvgw rsflnmlayk adlygkefkt idpkyttqrc hqcgsimgqn
      361 gykkltlkdr ewtcpicrth hirdwnaavn ilekglgnwq nskikkaa
//
LOCUS       WP_181577111             425 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Lactobacillus crispatus].
ACCESSION   WP_181577111
VERSION     WP_181577111.1
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=47620
     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 egrlspknak
       61 pafgdqrdpi nrnflggqyn peavyqyryf avmideshrv hvlndnnvyk 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_181577158             405 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Lactobacillus crispatus].
ACCESSION   WP_181577158
VERSION     WP_181577158.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
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="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     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=45013
     Region          29..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(29..30,33,66,116..117,119..121,124,143,146..147,150,
                     227,230..231,234..236,239,266,270,319..320,324,328,344,
                     347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mrtahgkqpa deiklhwlll gqlltwlgss fiwpltsvyl hdhlgvslal vgvvllfncv
       61 anmigsfisg wcydhmdpyv llivgaalda avlfgmalnh swplywlwmt ltgflggwng
      121 alinsiatsi kskpgryvfn miyfaqnvgv vcgtlavgyl ydysvtllfv iagllfvgvc
      181 vnaiinyrpm iqfhkerlan kgeskkqafe pmpkynlims igffvtiavi wlmymnwesn
      241 lsvymvylgi pfhlysllwt inagiivivq ailsrftifk slfrqilfgt lmfaisfvtl
      301 ifakdfahfa lsmviltlge atampsipty vndlspdssk gkyqgltlsa ssigralgpl
      361 fggliiedfg yiqffavaai giflllvmli pmhaklqkkl klfvk
//
LOCUS       WP_181577205             318 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase [Lactobacillus crispatus].
ACCESSION   WP_181577205
VERSION     WP_181577205.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 318)
  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..318
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     Protein         1..318
                     /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=35015
     Region          5..307
                     /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 mssfddiyek ilqyptiilh rhtspdpdai gsqaglarai mekfpdkrvl cagendegdl
       61 awinhmdqvk atdyegalvi ttdtantpri snklyekgdf likidhhpdv dpyadmsyvd
      121 pdapaacqii vdflnkedfk itkeiayply agivgdtgrf mypetsehtf kvaaqlaatg
      181 initeiarni advtfneakl qalamdkmei dpvgaaytil mqddlkklgl tddqanvavs
      241 tpgrikdvla wnvfvekpdg tfrvhyrskg pvinelaakh dggghalasg anakdmdevk
      301 qvfaevvevt kkfkedhe
//
LOCUS       WP_181577652             526 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Mycobacteroides abscessus].
ACCESSION   WP_181577652
VERSION     WP_181577652.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 526)
  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 526)
  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..526
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..526
                     /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=58165
     Region          13..458
                     /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 mgvqlalgrl sgnrpnrris vaivgcgfgg laaaielkra gfeditiler asavggvwrd
       61 ntypgaacdv psaiysysya lkpdwsalfg tqaeiqryla dvavefgiep mirynsevas
      121 aafdeasgkw tvvtvggaei ivdvlilatg qlsrpkmpdv pglatfrges fhsaewnhda
      181 dltgkkvvvv gsgasaiqvv paiadrvkdl tvvqrspnwv mwksrrvpgp fqtalmrrfg
      241 wlrtlhhiml flayesrypl vtrsaepirr vsqwyliwrl krhvkdpaev kaatpdyrll
      301 cnrlllsndw yptigrdnvh ligsavdrvd ecgvhtvdgr hieadvivwc tgfkaseflt
      361 pivvtgrggt dlhqqwkpsg aaaylgmtvp nfpnmfmlfg pntnsitnti vfllerqssy
      421 irqaveykar hgvaslevse aayqkfqgwl qekldrtvft dncpgwytnd qgkvtamwpa
      481 shvayakatw rfkrsefngh tavvsnrvgt aecldsasei pevnhs
//
LOCUS       WP_181577965             487 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Limosilactobacillus frumenti].
ACCESSION   WP_181577965
VERSION     WP_181577965.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus frumenti
  ORGANISM  Limosilactobacillus frumenti
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 487)
  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 487)
  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 487)
  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 487)
  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 487)
  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 487)
  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..487
                     /organism="Limosilactobacillus frumenti"
                     /db_xref="taxon:104955"
     Protein         1..487
                     /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=55625
ORIGIN      
        1 mkliyrlmls ftiaitalmi vlasafihat nrtlyqntwq qlqnysdslv edairydvnd
       61 hsfegfanes laanaallsd qkihfaifdm skkqifinsg ytpsiskgew qrlkkgktiy
      121 lktanprikv nskngtgmte vlrpyfyhhk liavvsigtf lsviqenlhq tkinlllsli
      181 igcvvtiils yflahaitsr ierlrkatkq vtkgnydvhv pvrsndeidd lsrsfnqmtv
      241 slresekeir rqeerrrqfm adaahemrtp lttingileg lqydaipeed kqhsielmrn
      301 dtqrlirlvn dnldyekirt nqismerkvf dasaalhnli dqlqkkaheq ndqlkltvpq
      361 alrvyadydr fvqimfnliq naiqftshgt ihisgrhlek gsqfvvtddg lgmtkdqvan
      421 iwdrfykadp srsttkgesg lglaivhqlv qlhggsikvk stlhegttft vyfpdreyap
      481 hlkaqnk
//
LOCUS       WP_181578075             375 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Limosilactobacillus frumenti].
ACCESSION   WP_181578075
VERSION     WP_181578075.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus frumenti
  ORGANISM  Limosilactobacillus frumenti
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
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="Limosilactobacillus frumenti"
                     /db_xref="taxon:104955"
     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=42437
     Region          54..374
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkltgrekss lifegivtvv llillnlaii tiaqdivesn pgitsgifmi kqslrigpmq
       61 aqiwsyqrii iafliiidiw vvwwrlrrry hlyqmnhiig elhyiaqghl dhripfklkg
      121 neqhvitsvn alvdsavqsm ddkrkieksk delitnvshd lrtpltsiig ylgliedkqy
      181 rseddilkyt htayekakqm knlvedlfey tkvqqhgapv nimkidlnql leqltasfel
      241 eaqhrgieit shvepdplml eadpeklgrv fsnlvsnafk ygngasyiki darqrgtkvv
      301 vkvsndgtpi paesidhlfe rfyraeasrs ratggtglgl aivksivdlh hgtvkaesne
      361 qqtsfivtlp lkqhk
//
LOCUS       WP_181578088             947 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Limosilactobacillus
            frumenti].
ACCESSION   WP_181578088
VERSION     WP_181578088.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus frumenti
  ORGANISM  Limosilactobacillus frumenti
            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 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Limosilactobacillus frumenti"
                     /db_xref="taxon:104955"
     Protein         1..947
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=108021
     Region          105..943
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 matrqqsare fvktwsspnk gredadrqtf wndllqrvyg indyynyity ekdvqvkagg
       61 kvttrridgy ipstkvmiem kgkkvkdltk plkqsggggd ltpfeqakry anflpnseqp
      121 rwilvsnfne idihdmekpl atptviklsd lpqkvkllef ivnasqqkii dekklsvdag
      181 nlvakiyhel tnayaqgrgv dvnspeiqrs lnmlivrlvf llyaddsnlf gkdnifqafi
      241 erreprdirr dlsalfkvld qseserdpyl ddefnqfsyv nggmfsdenv iipqftdelk
      301 rliveeagag fdwsgispti fgavfegtln petrrsggmh ytsienihkv idplflndlh
      361 defdkiqnmg nnnqrvikar efrvklgklk ffdpacgsgn fltetylslr kmeneclrii
      421 tgnqgtlait ddsdpkvkiq nfygieindf avsvartamw iaesqmweqt kditfankdf
      481 lpldsnnsiy egnairiews divkpyeldy imgnppfvan agrvsaaqsh skamlskeqk
      541 edkrklfgqh ggvldyvccw ykkaaiymkn ttikaafvst dsivqgqqvy plwnnlftdg
      601 ihinfayrsf kwgneasnea ivfvviigfs yidnsdklif thdgikqvdn inaylldtdn
      661 vliksrtkpi sdmpkmisgg kpveggnlif tdkqkeeflk kepqaakffk hftsgdgfik
      721 nkmrwclwlv datpseinhm plvkkqiekv kkfrlnstkn atrkaaqrpt tfveikqpst
      781 dyllipltts knryyipigy vskniianng asfipsasky ifgvitskvh mawmrvvsgy
      841 fgpsyrysnt itynnfpwpn idekqkekis etaqaildar klypdsslad lydpltmpae
      901 lrkaheandk avlqayglkp saseseivqh lfkmyeeltr kdkrnhe
//
LOCUS       WP_181578100             194 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Limosilactobacillus
            frumenti].
ACCESSION   WP_181578100
VERSION     WP_181578100.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus frumenti
  ORGANISM  Limosilactobacillus frumenti
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
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="Limosilactobacillus frumenti"
                     /db_xref="taxon:104955"
     Protein         1..194
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21818
     Region          3..63
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(5,9,39)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(8,38)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(15..16,32,35,39..40)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mnrirecrqn kkltlkqlse elakqdfris adalgkyerg drepkletwl klasffgvsv
       61 sylqgisens eplftsdssa telkqiinff dsqskgeksv spndlindik hlpmeqravv
      121 sgsfstflyc idfliandey qtiaslgnll gvilavqcme grdydiqdli nnyideaisr
      181 inniskktsn dsnn
//
LOCUS       WP_181578083             143 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl-CoA carboxylase biotin carboxyl carrier protein
            [Limosilactobacillus frumenti].
ACCESSION   WP_181578083
VERSION     WP_181578083.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus frumenti
  ORGANISM  Limosilactobacillus frumenti
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 143)
  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..143
                     /organism="Limosilactobacillus frumenti"
                     /db_xref="taxon:104955"
     Protein         1..143
                     /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=15670
     Region          9..140
                     /region_name="AccB"
                     /note="Biotin carboxyl carrier protein [Lipid transport
                     and metabolism]; COG0511"
                     /db_xref="CDD:440277"
ORIGIN      
        1 mdlknlkdim adfenssvre lkiedgdfhl ylsknnqptt naqlpttkpa iqqdngsqqq
       61 vvsdaqikap lvgtvylqsk pqqppyvkvg shvhkgdvvc vieamkmmte vksdvdgvis
      121 avkvdngelv eyqqplftvk egd
//
LOCUS       WP_181578251             206 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Arthrobacter sp. AQ5-05].
ACCESSION   WP_181578251
VERSION     WP_181578251.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. AQ5-05
  ORGANISM  Arthrobacter sp. AQ5-05
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 206)
  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 206)
  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..206
                     /organism="Arthrobacter sp. AQ5-05"
                     /db_xref="taxon:2184581"
     Protein         1..206
                     /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=21725
     Region          39..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 mdqetkwqqq arrdpaqarn yigrfaelre sgadldaear fadamlsrgs rvldagcgtg
       61 rvggelaarg hqvtgvdlda ellaaaradf pgsrwlegnl atldvrdeag tresfdlvis
      121 pgnvlafvap gtagsvlgal aahlapegrl vvgfsplkgy alesftedaa aaglridtlf
      181 stwdmrpmrp gadfvvalle pvqtvn
//
LOCUS       WP_181578260             359 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Arthrobacter sp.
            AQ5-05].
ACCESSION   WP_181578260
VERSION     WP_181578260.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. AQ5-05
  ORGANISM  Arthrobacter sp. AQ5-05
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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..359
                     /organism="Arthrobacter sp. AQ5-05"
                     /db_xref="taxon:2184581"
     Protein         1..359
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37437
     Region          <11..203
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 miernehfkc snigygllgl lveaagglpf adfvdarila plqlrdtgad lderagelat
       61 gygtlalagd hgaltgrtri ehihtrspga atgfhsttsd mpryfsshlv gpgtgvpddd
      121 skrlmqreae dsgapgrgyg lgliiqdvag hgsfgrsggy pghitrtwav pktkvvlsvp
      181 tnaidgpate ygerlfalaa lagkptpdsc agvdeevllr ftgrfaslwg vvdiaalggk
      241 lyrinpaapv avettvplef vdeatlrsld pngfsgygev irfevdvaga ltmrgpggml
      301 ferptgfhap avlrvpagce pgmepgavsr sgnnaganrh ssrvdgavgd hqhlgydpc
//
LOCUS       WP_181578379             304 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Arthrobacter sp.
            AQ5-05].
ACCESSION   WP_181578379
VERSION     WP_181578379.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. AQ5-05
  ORGANISM  Arthrobacter sp. AQ5-05
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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..304
                     /organism="Arthrobacter sp. AQ5-05"
                     /db_xref="taxon:2184581"
     Protein         1..304
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31066
     Region          41..271
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mdgktipasl grmlppgaaa acrgpgsega vqvfgssepl pvfsvtkmfi aagvlravda
       61 grftladpla srlpgapagr tisqvlthta gmgnyasspg ylaavrqrpa dpwslediaa
      121 agafsvpgpf aysntgywyl galleevagm slgqylhrev fepadmastr ypdpetaltd
      181 sgystlwagp agaafstpad llrfgdlvte rnplfpssls pamraafmds vpvaatapwr
      241 aprygagvmi dtdlqlwghg gagpgyraav ftsgatgiaa aaiapetsgf speealvsll
      301 gpkg
//
LOCUS       WP_181578395             235 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Arthrobacter sp.
            AQ5-05].
ACCESSION   WP_181578395
VERSION     WP_181578395.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. AQ5-05
  ORGANISM  Arthrobacter sp. AQ5-05
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
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   Rosinski,J.A. 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 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 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Arthrobacter sp. AQ5-05"
                     /db_xref="taxon:2184581"
     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=25092
     Region          12..229
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mtgpsdrspa ptrrtsfgrp lsptrlrile lleaqsapat laavthicgl hentvrahle
       61 dllrdgylsr eraaskgrgr pawlweakkp iehspyasla salatvlhet sahpvqdavd
      121 agkawgrelt lkqqgehhgq rpaeagrshv vdmleevgfa pdpdafnehv vltrcpliea
      181 askhpdivcg vhlgiiqgaf aemgldgsas tllpfsapgq ctlqlraaag ethte
//
LOCUS       WP_181578630             419 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella pneumoniae].
ACCESSION   WP_181578630
VERSION     WP_181578630.1
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=48067
     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 mpkltdmqir awikagerfe gradgnglyl ryraadkipt wryryklagk sramligsya
       61 elslskaret akelsarval gydvagekqe rktealakme aeknamrvse laaeyferqi
      121 lprwkhpdil rrridkdinp cigsmkvedv kprhiddmlk givdrgapti atdvlrwtrr
      181 ifdygikrha leinpcsafe vadaggkevs rdrwltrdel iqlfkamrta kgfsrqneit
      241 fklllalcvr kmelcaarwe efdldqavwr lpeerskngd aidiplappa vewlrelktf
      301 scnsawvlpa rkmqnrmiph iqestlpval akvraempdv pnftihdfrr tarthlaalg
      361 vdpvvaercl nhkikgvegi ynrhqyfder raaltqwagl lvalekgedy nvtplrksk
//
LOCUS       WP_181578780             321 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-nucleoside phosphorylase [Nocardia huaxiensis].
ACCESSION   WP_181578780
VERSION     WP_181578780.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..321
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..321
                     /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=34336
     Region          41..313
                     /region_name="NUP"
                     /note="Purine nucleoside permease (NUP); pfam06516"
                     /db_xref="CDD:428985"
     Site            order(80,83,109..114,207,210..211,219,230..231,245..246,
                     267,270..272)
                     /site_type="active"
                     /db_xref="CDD:350166"
ORIGIN      
        1 mtsrcqklav algvavlaat gcsdstgdsg kfevgvlvvt mfdpehevwl knedlsvkvd
       61 vpgafapvqc nrdrlcvaet gqgkanaatt mmailgsdel dlskawflta giagtppdqg
      121 tlggaawarw ivdfdlgnhl dpaeapgvpf gfrpvedynt aayhldeglv drayalsrdl
      181 kladspeaaa eramypgqqg rtpavtkcdt mtgddffsgk qlsdtaryim evrtkgqgvy
      241 cstqmednat atalnahgyl nrylslrtls nfdqpypgqs vidhldhsta gfqlaldnqy
      301 tlgkevamdl lknppengsg r
//
LOCUS       WP_181578356             249 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Arthrobacter sp.
            AQ5-05].
ACCESSION   WP_181578356
VERSION     WP_181578356.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. AQ5-05
  ORGANISM  Arthrobacter sp. AQ5-05
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 249)
  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..249
                     /organism="Arthrobacter sp. AQ5-05"
                     /db_xref="taxon:2184581"
     Protein         1..249
                     /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=25659
     Region          34..191
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mdvqaapgag igpgapwwai aplsaaaahp gvkllpeela rargyaagrp redfvagril
       61 arvlaaellg lagvqgrdvl pgdlqlaqwc pqcastahga prlclphrgd ryalsyarta
      121 gwlllglapg rgrlgvdlad sadaafgpgd gnlledyaya pgertrlral pgparqqlra
      181 rwwalkeava kaageglage ggipvvageh rhpllraagt rvleplpgtp dslgrtlpgt
      241 lvagivwvp
//
LOCUS       WP_181578218             358 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Arthrobacter sp.
            AQ5-05].
ACCESSION   WP_181578218
VERSION     WP_181578218.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. AQ5-05
  ORGANISM  Arthrobacter sp. AQ5-05
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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..358
                     /organism="Arthrobacter sp. AQ5-05"
                     /db_xref="taxon:2184581"
     Protein         1..358
                     /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=37659
     Region          13..343
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mtiaarpwld eiqayrpgtr sasadgsmas nesplgaspk lgdsiakala gvhrypdpla
       61 delrsqlagl hgvhpeqili gngsdelifl lsttflaqgg havcadpayq idrigalsvn
      121 atitqvplrd wkhdlaamaa lradiayivn phnptgttrs raeidtftae spahlvvvde
      181 ayidfttdpe altaiplvag grvavlrtfs kihglaglrv gylvadsaii aairkvrapf
      241 svgslaqaaa laaladtghr eavrehtlrl rgqlvdllac hglhavesea nfvllpvpde
      301 nafvaglrth gvsvrpgsal gapgtvrisv pteaglellr salhhthpan hretanhr
//
LOCUS       WP_181578765             380 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Nocardia huaxiensis].
ACCESSION   WP_181578765
VERSION     WP_181578765.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   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 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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..380
                     /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=38829
     Region          116..239
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrpkiralgg aacagatala lvfsggvaga epenpatadt laslidagll paadgrtpks
       61 ivdtgsgsgs agisstasda vgegpemsay laafayglvn pdaappgsnd wncrpsaehp
      121 hpvvlvhgtw lnaydtysym spriaragfc vfsfnfgklg vlqggglgpi lpgrngvgpm
      181 eesarqlgaf vdrvlaatga pavdvvghsq ggpvtsyfmk feggagkvgk litfgatnhg
      241 tslmgiatlg riinnlgvni lgfyepligt aniqqavgss fyaelnadgd tvpgvdytlv
      301 gsrhdeisnp yewtfmtagp gatvnnialq qdceqdlsdh ltvmysprav sivlraldpv
      361 anptlectfn pwmiggggkl
//
LOCUS       WP_181578911             376 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181578911
VERSION     WP_181578911.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..376
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39598
     Region          34..374
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 maaktfgiml vaataafata gtpaadadel tgllqadlda ivtgmdvpga qlvlrdgern
       61 rlvasgvgdi atgagfpdna qfriasntkt fvavvvlqlv gegrveldap ierylpgvvr
      121 gpggdgnait vrqllqhtsg ipdylpmlel esvaalrqwk taddlialgl geqaqyrpge
      181 ravysntnyl lagklveqvt gapvgvevtr rilmplqlvd tywpvfpaen tirgphaqay
      241 hefggnrvdv tdidpgwgls dgamvstsad lsrfyaalvs gavlgpdqla emrktvpsgd
      301 frrseefglg lfhwvtscga dawghggtmh gsfvyggatt grsvtvsmnq ipdifggtqq
      361 rvdmhqvvdd alcang
//
LOCUS       WP_181578788             281 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Nocardia huaxiensis].
ACCESSION   WP_181578788
VERSION     WP_181578788.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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 10002380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..281
                     /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=29199
     Region          25..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 mqpalptprd dtalhivrkn fsdtaisslr tfgrtvelaw dsvrgvvtdv pagkfpwrem
       61 lhqawyfitv talpailmav pfgvvvsvqv gnlihqlgad sligaagglg viqqgapiat
      121 glllggagas aiasdlgart vrdeidalrv mgispvhrlv iprvvamvlv apllnvliif
      181 vgivagyvva igaqnvtpgs ywatfgaftv ladvwislak svlfgfivvi vacqrglear
      241 ggprgvadgv naavvlsvaa iivvnlvitq vvtmflpmrv a
//
LOCUS       WP_181578628             501 aa            linear   BCT 28-DEC-2024
DEFINITION  xylulokinase [Klebsiella pneumoniae].
ACCESSION   WP_181578628
VERSION     WP_181578628.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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 501)
  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..501
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..501
                     /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=54886
     Region          5..492
                     /region_name="XylB"
                     /note="Sugar (pentulose or hexulose) kinase [Carbohydrate
                     transport and metabolism]; COG1070"
                     /db_xref="CDD:440688"
ORIGIN      
        1 mkdkiltidv gtgstraaiv ridgamigfa qreyeqttpr agwseqapsl wwqaacdcir
       61 evlyrypeta aqiavigacg qmhgtvlldd rgelvedral lwndkrsqpq vdafnaregw
      121 ekwlahlnnp paaawpafkl awwrenhpdr wsqlakvlmp kdyinfmltg amatdyseas
      181 cyflmdsetr swssqacetf glrvdqlpel klssdiigqv tqraadltgl pagipvvagt
      241 sdmaasllgs gvyepgmasd stgtstlmtv vsprplhhpl vnnlhlanaa wggftildag
      301 gdavrwarla ladnhithpq llqeaaavpa gaegllflpy ltgerlaeht nsraqffglq
      361 rkhrrghlfr avlegvafas wrnlrqlqkc gqypqqmias gggahsslwl eikaaaynlp
      421 ilstrnqeng vtgcgiiagv gvglyadfas gvrqtvqfdk lispdprlrd yyhaccelfd
      481 tlyrqsaaly drldalsvgp d
//
LOCUS       WP_181578795             347 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nocardia
            huaxiensis].
ACCESSION   WP_181578795
VERSION     WP_181578795.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 347)
  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 347)
  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 347)
  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 347)
  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 347)
  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..347
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..347
                     /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=37442
     Region          5..338
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtnrralvtg asgflggalt rrlvrdgdfd vsilvrgssn lrdlievide vrvvtgdltd
       61 aasleraaeg vdvvfhsaar vdergsreqf wrenvtatar llaaakagga srfvfissps
      121 almdrdggdq ldidesvpyp rrylnhycet kaaaerlvlq anapgfstta lrpraiwgag
      181 drsgpivrll draaagtlpd lsagrdvyas lchvenivaa cvkaaasekv ggrpyfiada
      241 ertnvwpfls rvasdlgyap prrridprlv nllvevietl rrapyiaarw spplsrysva
      301 vmtrsgtydt gaaardfgyv pvidrdtgma elqdwlksga vntgiah
//
LOCUS       WP_181578915             342 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nocardia
            huaxiensis].
ACCESSION   WP_181578915
VERSION     WP_181578915.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=36280
     Region          2..304
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrvlvtghqg ylgtvmvpvl qaaghdvtgl dsgyfaecvl geapaapptl svdlrdvtad
       61 qlsgfdavvh laalsndplg alapqitydi nhhasvrlar lakqagvrrf lyastcsvyg
      121 aagaglvted aplrpltpya eskvkveddv aaiadsgfsp vflrnatafg fsprlradiv
      181 lnnlvgyavl tgevrvlsdg tpwrplvhar diaaafatcl eapieaihcr aynvgteann
      241 ltvaeiaqsv veavpgstlv itgesgadpr syrvdfsyar kelgfeaqws ipegaaelhr
      301 eyvargltad affarftrla hlkslkqagi ldddlrrvri ga
//
LOCUS       WP_181579002             476 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nocardia huaxiensis].
ACCESSION   WP_181579002
VERSION     WP_181579002.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=50437
     Region          2..463
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mthdgpadvv ltperhtidv vpdaerhgsp rsqftlwfga nmqitaivdg alavifgada
       61 lwaiigllig nvaggavmal hsaqgpklgl pqmissraqf gvrgavvpll lailmylgfa
      121 atgtvlagqa iakilhidsp qlgmvifgll tafiavtgyk lihvvgrvat vvgivgftyl
      181 airlfseydv pahlgvqgfe matillaigl sagwqltfgp yvadysrylp rstsdratfw
      241 stfcgtvigs qwsmtfgali aavagkafmk dqvgfigdla gpaavavliy lvivigkltv
      301 nvlnayggfm svlttvtafg gvqristlar tayilgftta atlvavaasa dflnnfknfv
      361 lcllmvftpw sainlidyyl iskerfdipa lydisgryga wnapalgcya igvlaqipfl
      421 atkfytgpit eklggadisw ivgivltaal yyplakrlnn ppphmiypad teiara
//
LOCUS       WP_181579078             401 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nocardia huaxiensis].
ACCESSION   WP_181579078
VERSION     WP_181579078.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..401
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43864
     Region          134..394
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mqartrdrai eelyrravvv reeftstalp pyrnlphnlv asgfergakl nldlifdylr
       61 tgalpteeat revveialgr vrdgepleev ldryrigady iwsrlraaad daerelltds
      121 ampllnyisl ittrvatacv qrahdprwel lerrraiada lltgrdpiew adepaiavpe
      181 sfvvavfrlg asrgadtgel rhriesipgv flrldsggwt alvplqpgdd gtatvaalta
      241 rlpqhaaeaa kpvtrstppa pfwvgvavap shadipalfa earilselgr clarsqpvcr
      301 radlmfeytv aaggaartgl aavlapldpq pllaetlevf vdsgfnqlat arllnihrnt
      361 vtyrltrvhe ltgldphrpt damtlsaari arrlesacfa p
//
LOCUS       WP_181579105             381 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181579105
VERSION     WP_181579105.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..381
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40747
     Region          4..373
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpglqeflda yvrkgvlpga vavlargdrl evavagsaha dgsapmrrds ifrlasltkp
       61 vtaaallmlv ddgrvaldqp vdgwlpelad rrvlrtpasp ldevvaavrp itvfdlltsq
      121 aglgwaadse lpfvralfpi qrdgreplsy psadewmael gqlpllgqpg eywlydtcst
      181 vqgilvtrvc gqslpeflaq rifeplgmdd sgftvaqgkr erftsyyrnt pegfeladgp
      241 dgqwageppl plghgglvgt addvlkfhrm lladgvgadg krllstesvr lmhtdhttpa
      301 sralagffld gqgwgcggsv diavrgpwna pgrygwvggt gtsayhvpat gaidvvltqv
      361 avdspvpaew leefwrfaaq s
//
LOCUS       WP_181579072             172 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nocardia huaxiensis].
ACCESSION   WP_181579072
VERSION     WP_181579072.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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 172)
  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 11444526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..172
                     /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=19035
     Region          3..164
                     /region_name="Idi"
                     /note="Isopentenyldiphosphate isomerase [Lipid transport
                     and metabolism]; COG1443"
                     /db_xref="CDD:441052"
ORIGIN      
        1 mpeqiavyda agrqtgaedr atvyaeglwh asagvlvrsr dterlyvhrr tdtkmvfagm
       61 hdclaggvla pgedpaeaai relaeelgit lsptddkplp lataswdgew qgrpmrchlf
      121 ayelrhdgpv thqpeeiadg wwwtdaelrs hladpawpfv pdtrvliadl lr
//
LOCUS       WP_181579197             206 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardia
            huaxiensis].
ACCESSION   WP_181579197
VERSION     WP_181579197.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   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 206)
  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..206
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..206
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22129
     Region          4..97
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrsygqycgl arslevvgdr wnlliirqll laparyrell dglpgiatnl ladrlrelea
       61 tgvierrltg rgsvveyalt pwgaelrepi eslirwstpl mvrgpegdaf rpewlalavp
      121 allnarvtpr paatigleig gslfqlrsar sgfevaphdg rdldatvrad paqvlglaag
      181 alslddalgl veidgdesvv ravfaa
//
LOCUS       WP_181579000             487 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia huaxiensis].
ACCESSION   WP_181579000
VERSION     WP_181579000.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=54447
     Region          2..424
                     /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 msstpehvdv livgaglsgv gaayhlqqaf pwrtytilem rdaiggtwdl frypgirsds
       61 dmftlgyrfr pwlgdkaiad gdsilayvre taadngidkh iryrhkvvra ewssadnrwt
      121 vtadhdgepv titasflfsc sgyyrydagy tpdfpgterf sgpivhpqhw peqlevagkq
      181 vvivgsgata vtlgpalaeq gaqvtmlqrs psyiismpar davadrlrki lparaaytla
      241 raknvalsta myqisqrypk rmrawirglq qrwlppgydi dthfnptynp wdqrlclvpn
      301 ndlfrairhg tleivtdrid tftesglhla sgrdldadii itatglnlav fgnveivvdg
      361 skidmpkama ykammlsdvp nfafiigytn aswtlkadlv ceyvvrllrh mdshgyvkat
      421 pvrdesvgta pflnfepgyv lraldilpkq gdrapwklhm nylrdlpklr ygkvtdpamr
      481 feravng
//
LOCUS       WP_181579090             299 aa            linear   BCT 28-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Nocardia huaxiensis].
ACCESSION   WP_181579090
VERSION     WP_181579090.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 299)
  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 299)
  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..299
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..299
                     /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=34007
     Region          10..283
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 mgdeatllpr esfaqrlltg svkksydpvv dldwdapldp eklflppevv slygtdlwea
       61 mtaeqrrels rqelanvlsv giwfenllnr lllrelmagd ptsrhshytl temgdecrhm
      121 mmfgrlieri earpywpnry erlvisslqq flrgpmvwvg alvgeeifda iqrrtlddpe
      181 lqpivaramr ihvteearhi gfardalarr vpemsksela ytklcvaiaa plfvhlmtnw
      241 hmyvragled graarraara nphsrralgl gaanlgafld kqgligpmgk riwrrqgll
//
LOCUS       WP_181579128            2392 aa            linear   BCT 28-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Nocardia
            huaxiensis].
ACCESSION   WP_181579128
VERSION     WP_181579128.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 2392)
  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..2392
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..2392
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=256831
     Region          6..>2115
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2119..2371
                     /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 msismryplt ayqrdiwtiv elfpglpsyl ssvvgrfsld idvdamvtai ertwarndgl
       61 rlrfrvvdgv pfqelstepm pavqvidvsd aadphaealr rvheltgnai elvdavpfra
      121 hivragadrs yvlvtthhia adatglfnig aqiltdyagi tttgdpfdlp gssflgcldf
      181 erdyraseqy gidrdalvdr lrattpalfe rpratgglap vtshtftler alvdriraag
      241 vslypyfcam lglylsrvlr theiaigipf gnrhnpteqs tighfantlp lpidtgghat
      301 vrdlvaavka dvrqmkpher yplgdlmgel rragnparql fdvtvayprl pdtagliagl
      361 eevqqpsqgy splamawtis eidddgplli rldyatdifd adypiesaaa hltallyagi
      421 daldsdpall pmlsaaeyda lvdreratty pydaqasvig riteqaartp gavavhaadg
      481 atisygdlla rvaqlsgllr esgvsagdlv avvlergpdm lvamlaamha gaayvpvdpg
      541 ypadriayvl adsaakvvlt daaraetied avtltperws agahaaapvp dgsdlayviy
      601 tsgstghpkg vavehhsvin rlawmqrryp lragdvilqk tpssfdvsvw elfwwalega
      661 qvallrpgge kdpreilsai adsgvtvmhf vpsmltpfld lleadpaavs qasglrtvfc
      721 sgeallphqv trwnrafagl gsaaprlvnl ygpteatvdv syhdtpqdpa rpvtrvpigr
      781 pidntrlyil gpadqpqplg vagelciagv glargylhrp elnaekfvad pfhpgermyr
      841 tgdlvrrlad geieylgrid rqvkirgnri elgevenala alpgitaaav idhhspsrga
      901 ylaaycvate glepanlrag lartlpeymi paqfvridai pltpsgkadr talaairpea
      961 daaeqtaprt pveqqlaqvw cevldresvs vfdnfydlgg dsilllrvra raeargllis
     1021 ardiaespti aelaerartg avvaapiepf alvpgidrar lghvedaypl trlqlgmlfh
     1081 sreraessly hdvfryslrm pwdeaefraa lrrsiarhpm lrtsfdlaay seplqlvhgh
     1141 ldapltitdl rgaepdtaet avrehvaerr lrpyvfdqpg lfhlavfrla dridivlsfh
     1201 haildgwsva tllsellady rgigdlsage lpsfaeyvra eresiadpad refwareldg
     1261 aetaripgvr phgpvtpdsa agpvdarvsr tipvpaells radavaaath vpvksvllaa
     1321 hvatvgllsg rtdvttgvvt hgrperldae rmaglflntm plridfagrs rrdlltgifd
     1381 rdrnsaphkr fplteiqral gvvldtafny vhfhaagaal ealdvtllgi diredtnfal
     1441 lvnavrnpld gtlalridgd paaytreqld sigetylavl elltgdpaap vdfgalapap
     1501 aaapgpiapg tvldlfdata artpdaiale fgsrtvtyaq llalsnriat alvargarpg
     1561 driamavdrs pelvatvlgi akagaacvpl dvtypqsrlh amleqarpfa vvtgpghesl
     1621 vpqqhsrigl ddlvtaagta alpavaqdgt ayvlftsgst gtpkgvamph ralvnlirwq
     1681 lstasgwlsd verapattqf aplsfdvsfq eiystlcggg rlillgeeqr rdlpalarll
     1741 gstaaerifl pyvalqqlae aairldiapa slrviissge qlrvtdeira lcaagtgvvl
     1801 enqygpteth vatrytmtgd parfpvlppi gravdnveil vldeqlrpvp dgvpgeihlg
     1861 gaaladgyeh rpdltdaafg phpfapgrrl yrtgdigrrl pggdvisdgr rggqvkirgh
     1921 rvepmevela lqrvtasvpg vsevavvaha tagassaqtl lvgflvgtre dvdepdilaa
     1981 lrewlpdymi psrlvwldal pltpsgkrad avlagmalpa pqaadrvapr tpveaglaal
     2041 maealglpev gihddffalg gtsltamrli vsieqrfgls lpvsalvtgp tvaalarhld
     2101 eragagfdpl vplregsgtp lflvhpiggn vlcyvelskr lpanqplygl qaaglepgst
     2161 aaqsipemas nyiaalrrvq pegpyhlggw slggmvafem aqqlresghe vgmlalvdtm
     2221 tvrhgdgtpv pqhslyeffl wellwlarga dtavieiple lesedevfdf ildsaveagv
     2281 lppagsralv rrlfevftgg wraidsyrph ayegditllr aaeplpevlr pahdsagtlh
     2341 rdptngwday aaghleviev pgdhltliqa phvaavaaql trllehasat as
//
LOCUS       WP_181579248             311 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardia huaxiensis].
ACCESSION   WP_181579248
VERSION     WP_181579248.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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
REFERENCE   6  (residues 1 to 311)
  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..311
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..311
                     /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=33601
     Region          8..255
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 malpppspnt rvvvtggasg igkeiarnla qhgydlvlvd iqqsvketge elrakgvese
       61 eflldltdrd arqefidqvl erpydivglc nvaglisagr fedlplqrer vlvdvsvsal
      121 hhltgaflpg mrarragail nvsspvgilp lpynasysaa ksfsmffsya lhqelkksgv
      181 svttlmpgpt ktnllygise trfmpdwawr lpvffdaapt arrgvngmlr gsrmvaagay
      241 pwaavalgrf vplwlvlgpi rlagqlgfpa reettgrrir avadkvgtri ggkryavvpe
      301 papvqveaat r
//
LOCUS       WP_181579249             298 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardia huaxiensis].
ACCESSION   WP_181579249
VERSION     WP_181579249.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  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 298)
  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 298)
  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 298)
  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..298
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..298
                     /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=31530
     Region          1..265
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mrtavvtgaa sgigmgyata lveqgyfvlv tdiddakaeq vatrltalgp gwaeaayldv
       61 ssadavaaav ygvkdrfgrl dlmfnnaglf iggpveeltv ghwqkaidvm iagvaygvda
      121 aykimveqgf ggivntasma gftpfsylgp yntakfavvg mtmslrgeaa ahgihvtavc
      181 piaihtdivl ganagldnkt teidyvaaly rrfghlghll pnfilqdpvv hgrkvlravq
      241 rnrafviqpa ygrllwwlcr aaptltpavg haatrganiv rgpvnhawgr lpgwirda
//
LOCUS       WP_181579250             298 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardia huaxiensis].
ACCESSION   WP_181579250
VERSION     WP_181579250.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  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 298)
  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 298)
  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 298)
  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..298
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..298
                     /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=31404
     Region          1..266
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtvktaivtg aasgigmgya aalvekgyfv lvtdvnevga kqvaahltsk gpgtaeaafl
       61 dvrdgdaira tvqgvkdrfg rldlmfnnag mfvggpvedl tpehwdraid vmirgvaygv
      121 daaykimveq gfggivntas maglatigym gpynmakhav vgmsnalhge akkhgvhvtc
      181 vcpiaintni llgindglge wrggdglgaf yrrfgrfgkf vpnfilmdpv vhgrkvllav
      241 qrnkaiiikp aygkavwvla rigprlpyla gdvgtrvlak vepvfvraae sldpapka
//
LOCUS       WP_181579254             476 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Nocardia huaxiensis].
ACCESSION   WP_181579254
VERSION     WP_181579254.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 476)
  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 476)
  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..476
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..476
                     /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=51791
     Region          31..454
                     /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 mtdwlggtrr srkfgsrpad psghppahpa artvrlaalp iayagrhaag lgkllhgapa
       61 etvyaeirer tarhifevlg nlrgcaaklg qilalypggl pyeiagpyre alanlqfaap
      121 pmlpgavhaa mtqylgpdwr daflefddrr pmaasigqvh raiwrdgtpv avkiqypgva
      181 eaiesdlrqv rhlafvagvm lpsmdldglv gelcegirie ldyrreaenq riaaekytdd
      241 pefaiprvve qragvlvtew ldgellttal lhgmpsetrd rvgasifrfc mlspartgli
      301 ycdphpgnfv ilpdgrlgvi dfgactpqpp gfddmiapal eaalngsade fdallrdygf
      361 ippgqdvdia eftrvldpfv rmaleptaef stewlrarig eglsprldnv hrhlamppal
      421 wsysrtllsm vavlaqlgat ipagdiaier lpefeairar arartaagng vslrrv
//
LOCUS       WP_181579265             253 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Nocardia
            huaxiensis].
ACCESSION   WP_181579265
VERSION     WP_181579265.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=27392
     Region          25..247
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mkppavtlen ygavydyyrd hrqnllkaka aywllgrrfa prvgfaagar kglrdfiseg
       61 rplviainhl seqdpytvsg aawrsplrpv ightrvlakh evfadpalrn tldmmggmpv
      121 frskdhesls vkaaserlid tcavvlargd svalfpegtc nyvdhtrvld lgggighivc
      181 rarelganpv lvslglsygp rpdpaaelsk advhsasfyf rtpvgelpsq padimdvvrd
      241 elqaaldgav asy
//
LOCUS       WP_181579381             341 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD-IIIC family phosphatase [Nocardia huaxiensis].
ACCESSION   WP_181579381
VERSION     WP_181579381.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..341
                     /product="HAD-IIIC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36587
     Region          4..331
                     /region_name="FkbH"
                     /note="Predicted enzyme involved in methoxymalonyl-ACP
                     biosynthesis [Lipid transport and metabolism]; COG3882"
                     /db_xref="CDD:443090"
ORIGIN      
        1 mattvkclvw dlddtvwpgv vlesdggapk pealhairtl dergilhava srgepaaata
       61 hlrahdiedm fsaieiswgp kseavrriae alnighdtia fvdndpvela evaaalpevr
      121 cypadriael pglpeftpat atseargrrs lyraererqa sqaefagsda dflasldlvm
      181 tvreageadl lraheltert hqlnttgvtf dlgelralca spdhevlvas ltdrfggygt
      241 iglavterrg pdavlllllm scrvmsrgvg taliaevvrr ahdaglrpaa efvatplnrv
      301 mlvtlrfagf evvdtdgeri llacsvppeh isgtghvevv r
//
LOCUS       WP_181579429             196 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nocardia huaxiensis].
ACCESSION   WP_181579429
VERSION     WP_181579429.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 196)
  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..196
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..196
                     /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=21167
     Region          1..194
                     /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 masenfdssr plaasvkili aggfgvgktt mvsaiseitp lrteelitel stgvddlsgv
       61 egkttttval dfgritidqn lvlylfgtpg qdrfwflwde largalgavv ladtrrlegs
      121 faaidfferr gvaftvavnc fegaplytpv evrdaldlde hipvllcdar drgscknvlm
      181 tlveylidra atrvts
//
LOCUS       WP_181579458             585 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Nocardia huaxiensis].
ACCESSION   WP_181579458
VERSION     WP_181579458.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..585
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..585
                     /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=62772
     Region          14..>131
                     /region_name="PLN02487"
                     /note="zeta-carotene desaturase"
                     /db_xref="CDD:215268"
     Region          74..585
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 msiggvsrrq llrtalagma asgvaacara sgegavdglp rgtshtlare llgvgerged
       61 ltlaylkvlv dtglpatntr kkiivvgagp aglsaanlla daghqvtvle angnrtggrv
      121 ktlrgvfadk dlyaeagamr lssahpmvla ladklgvrrr pfynsdvlpe tvtpattpvy
      181 yrsftgeewt ngprteyaap asagrslirv ngltrtraey aanpgavhas fgcglaepsr
      241 vvlgsalrqt salgdqpier qlerwtelld thenhslrdy lkdqgwpkdr letvgtlenl
      301 tarlghsvvf plvdhtlipv gafywelagg tasltdaltr rlgpavllgk rmtrleqteh
      361 gvrvwttget gtetsdgaps gpaesfdady aivaiplsaa rfctfepals ydkrraiiem
      421 hhdaatkvll efktrfweqg pagfrggrca tdlpnrslff pshvensegg vvlasytfad
      481 damrwdslte gerihfalag mrelfgarvd seftgvgitq swvraryalg eaaipapgql
      541 hehhlatrsa egrvhfagdh tslntawieg alesgvraal evhrr
//
LOCUS       WP_181579559             109 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardia huaxiensis].
ACCESSION   WP_181579559
VERSION     WP_181579559.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=11913
     Region          13..87
                     /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..30,33,63,82..83,85..87,
                     89..91)
                     /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(37,40,82)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mpglqrplyq mkaeffkilg hpvrirvlel lsereravse miteigveaa nlsqqlsilr
       61 raglvtarre glsvtyelts pqvaqllata railtgvaag qvemleqlt
//
LOCUS       WP_181579571             303 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181579571
VERSION     WP_181579571.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..303
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33810
     Region          21..78
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(27,31,56)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(30,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(37..38,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          110..293
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtsaheddte fnpsstlprr qlgrflrewr eangftlgva aklvdlsqsa lqrieagqtq
       61 kvrkqdvral cevygvgead taaamdlaal arahgwyhay gglysdafnm yvgleaaarr
      121 lvtyhehipg llqtadyara visafpgfts psdvnrriel rmkrqalitr rtnpvvlevl
      181 lhesalhrlv gdrrimaaql rhlaevsklp nvsvrlhpya agltwgiprg sftildfgve
      241 agpieppivy ieggptqdvy lekpddvriy seyasairsa aledkqtrel vrrvtkefey
      301 dqh
//
LOCUS       WP_181579603             359 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardia huaxiensis].
ACCESSION   WP_181579603
VERSION     WP_181579603.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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: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=37794
     Region          179..283
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtstvesapv dpdklmsfvl tavgevgaal naalvvlgdk lglyrtlagl gpmtavelae
       61 atgtdahyvr ewlnaqaagq yltyqpgpgt ytlpperava ltdpsspafl pglfqlavgt
      121 ivdwprvlea ardgsgigwh ehgpdvhsgc erffrpayra hlvndwlpal dgvvdtlrrg
      181 arvadigcgh gastilmaqa fphsrfqgsd ahpesvrtas rraadagvas qarfevaaah
      241 efsgdgydlv ttfdalhdmg dpvgaarrvr qalapegtwm ivepaagdrv ednlhpigra
      301 fygfstllct psslsqpvga algtqagpar lrdvvtaagf ghcriaaatp fhmvlevrr
//
LOCUS       WP_181579614             464 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardia huaxiensis].
ACCESSION   WP_181579614
VERSION     WP_181579614.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=48167
     Region          143..461
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrrllaalt afatlavlaf alplcltaat srtqqlisgr tgdadrfaal aatatalddr
       61 ralireidry helygeavlv vdargepvvn agvdltdpai taavsaarrn qrpatperlt
      121 pwgqstvlia rpigsdvhvd gavliaastt aartditrlw tvvavgalaa maactalall
      181 larwvlrpla glstavselt aslpsphtpa tmtrrhggpp elravaesvd tmaaavrdsa
      241 aaqrrliddt ahamrnplaa ltirldslep aipanaagtf hgatreverl tglldglltl
      301 avaegrdltt pdtcdatqia ddridawrsa yddagmtlqh qpapedpadt avsaavlaqi
      361 ldvalsnscr yagpgattrl avtttpgwvs ltvtdngtgv padeldrltt rfyrgssadg
      421 iggsglglpi aaaltsarhg hltltaveph gltvtirlpa avpr
//
LOCUS       WP_181579693             147 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nocardia huaxiensis].
ACCESSION   WP_181579693
VERSION     WP_181579693.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..147
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..147
                     /product="YybH family protein"
                     /calculated_mol_wt=15960
     Region          3..130
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtsnfpsdea airaridtvi dalhakdlda lkqvyaadvv sfdidpplqh vgiaaklenw
       61 vrvfeffdtv ryelrdltft vggdvafghg fgrlsgtlsn gtatsgmwvr vsyglrkieg
      121 twmiahdqvs vpldiasgkg vvdleph
//
LOCUS       WP_181579958             484 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia huaxiensis].
ACCESSION   WP_181579958
VERSION     WP_181579958.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 484)
  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 484)
  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..484
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..484
                     /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=53828
     Region          1..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 msehthiavv gagfggigla vklraagfed fvileraddl ggtwrantyp gcacdvpsql
       61 ysysfapnpe wsrtygkqae ileyiravav ehglerflry rtevldarwd esatlwrlet
      121 trgprtanfl vsatgifaea kypdlpglnt fagtsfhslh wdhahdltge rvavigtgas
      181 avqfvpeiqp rvaelllfqr sapwivprld rptlaaeryl lrtvplaqka vrglwysaie
      241 tfglislvdq rfrhpyealg rlqllrqvrd pllrktltpd yvigckraif sdaylpaldq
      301 pnvqvvtepi aevrphsivl rdgaehavdt iifgtgftsi ptayerfhgt dgrslaelyr
      361 qrpqsylgaa vagfpnffct lgpfgaagnq saiymiesqi ayivdalksv rhsgarrvev
      421 rpeaqrefls emsrrssstv wltggctgyy ttsdglnagl ypnwsfeyrr rtstfdsday
      481 evta
//
LOCUS       WP_181579993             380 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nocardia huaxiensis].
ACCESSION   WP_181579993
VERSION     WP_181579993.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=41290
     Region          14..368
                     /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 mtavvvvgag pvgltaaltl arrgievtvl eqgdalaaes rastfhpptl emladlgvlr
       61 sllaqgiiat tfqyrerggg eiatldlgvl addtaypfrv qceqskltpi lhaalpdhar
      121 vlfghrvhgl yagqdgvilh tahgplhadw vigadgahsv vrravgasfe gstyperflv
      181 asvdedltav lpgiapinyv fdphewlvll rtpehwrvll ptpahtrdev emsrlperla
      241 avadlgrpwr llhaslyrvh qrvtesfrmn rvllmgdaah vnnplggmgm nsgihdavrm
      301 ssalaetlcg avgsdldava arrrtvaieh vqrashdnwr rlrghderyr aelrelaadp
      361 vaarahlrra clldsleatr
//
LOCUS       WP_181579974             128 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nocardia huaxiensis].
ACCESSION   WP_181579974
VERSION     WP_181579974.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=14289
     Region          2..127
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mhsydiqlrr tdmdalehln nvvfaqylde aradllarhd sggepwrvvv agqrlgyrtp
       61 ltfraepvtv tsaverigtt sftlrhevrd adnvylsais tlvavhdgap rpltdaerky
      121 ladltvre
//
LOCUS       WP_181580000             314 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nocardia huaxiensis].
ACCESSION   WP_181580000
VERSION     WP_181580000.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..314
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32716
     Region          23..298
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mrsirslwws vrtdgsapfd tahlkvyypa lasgsdaerl tgvfapdpaa apypvvlfls
       61 gvnvgqesyr rfattiaesg fvvvtldrva elfggqhglt pgvdlaaarp daygtrptcp
      121 tiglvleala elntvaplrg tldldrvalg ghsaggtvvl qsarffpsva avfawgahtm
      181 vatmlgwdpg tvlpaqvrcp vllgvgtndg viqgsadryg edgadrpdpv rrtffealpa
      241 gdhllavvpg anhfgiadad ptaarafldg pgdadaftpf trlasaflrt hlrgeaaakt
      301 elaepgtgvr virs
//
LOCUS       WP_181580014             144 aa            linear   BCT 28-DEC-2024
DEFINITION  tautomerase family protein [Nocardia huaxiensis].
ACCESSION   WP_181580014
VERSION     WP_181580014.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..144
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..144
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=14751
     Region          67..127
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpftviaprg vltetgerql ipqliealie asgltgnpff tpvvgghlhl ldpehvhtgg
       61 vnrpvlliel klpgiglptp qdraafitta taiatnhvvs ghapddiwin isyaadggwg
      121 iggvaysnda liaaitdaap tpag
//
LOCUS       WP_181579826             597 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Nocardia huaxiensis].
ACCESSION   WP_181579826
VERSION     WP_181579826.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 597)
  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 597)
  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..597
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..597
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=63843
     Region          402..501
                     /region_name="PilF"
                     /note="Type IV pilus assembly protein PilF/PilW [Cell
                     motility, Extracellular structures]; COG3063"
                     /db_xref="CDD:442297"
ORIGIN      
        1 mtrpappsgq spliatpkss lgrgllatas avatalsyql vrtlvadtfd dnpavrrtlq
       61 alqwlpvlvv aaaagyvvhr svrslrerrr yardaellad lmgpghtave glspttatia
      121 pgvnavvppv aigavirvlr alpvwryrri gfmvmlgaml eaparvpaqe tddwnlppga
      181 paavlaelvs rrevapdgpd ayecmynvlt avprapdtvv aamraaalpa liayhagras
      241 rwavaldtla lgaaargwfa regpylrtli vdcaapspta rtplpsaavr dltriadald
      301 awyarlglee ngpdsaavpt lpdavlgldg ienepvaqel aqirsrglha pprrrgsrrl
      361 rsslaarreh rralnflqry rppilftgvs atrlraavvq prlaaaertl esawwllprt
      421 diagevcalv nlavvhihqg rydaagdrpe laealtrngi dpagcahvre tmgvvmwakq
      481 epegavrywq galrgyrtlr depgiarclq hlgsaavvtp grigglllpd vaplttvevh
      541 rqatgwlaea lhlgantgla sdyraqavgl lpstvaplnr vdrwplppee tarstat
//
LOCUS       WP_181579552             333 aa            linear   BCT 28-DEC-2024
DEFINITION  fascin domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181579552
VERSION     WP_181579552.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Jansen,S., Collins,A., Yang,C., Rebowski,G., Svitkina,T. and
            Dominguez,R.
  TITLE     Mechanism of actin filament bundling by fascin
  JOURNAL   J Biol Chem 286 (34), 30087-30096 (2011)
   PUBMED   21685497
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kureishy,N., Sapountzi,V., Prag,S., Anilkumar,N. and Adams,J.C.
  TITLE     Fascins, and their roles in cell structure and function
  JOURNAL   Bioessays 24 (4), 350-361 (2002)
   PUBMED   11948621
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Yamashiro,S., Yamakita,Y., Ono,S. and Matsumura,F.
  TITLE     Fascin, an actin-bundling protein, induces membrane protrusions and
            increases cell motility of epithelial cells
  JOURNAL   Mol Biol Cell 9 (5), 993-1006 (1998)
   PUBMED   9571235
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Edwards,R.A. and Bryan,J.
  TITLE     Fascins, a family of actin bundling proteins
  JOURNAL   Cell Motil Cytoskeleton 32 (1), 1-9 (1995)
   PUBMED   8674129
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Bryan,J., Edwards,R., Matsudaira,P., Otto,J. and Wulfkuhle,J.
  TITLE     Fascin, an echinoid actin-bundling protein, is a homolog of the
            Drosophila singed gene product
  JOURNAL   Proc Natl Acad Sci U S A 90 (19), 9115-9119 (1993)
   PUBMED   8415664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10083566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..333
                     /product="fascin domain-containing protein"
                     /GO_function="GO:0030674 - protein-macromolecule adaptor
                     activity [Evidence IEA]"
                     /GO_function="GO:0051015 - actin filament binding
                     [Evidence IEA]"
                     /GO_process="GO:0007015 - actin filament organization
                     [Evidence IEA]"
                     /calculated_mol_wt=35555
     Region          14..167
                     /region_name="beta-trefoil_FSCN-like"
                     /note="fascin-like domain, beta-trefoil fold, found in the
                     fascin-like family; cd00257"
                     /db_xref="CDD:467441"
ORIGIN      
        1 mplsaadlas lgetpitlrs tafanvylrl dgsgvsspad yggglvncqy tagsyeqfrv
       61 rpqsdgshaf esvafpkvyl rmdgsgvttq ttsgggtvnc qygsggpgpy ekfhagpqpd
      121 gsfslesiaf pkvylrlngt gvtafsgsgg gtvncqfaad ggvhekflle padqrldfrm
      181 qhqqqtqwcw aataasvelf ynpasqwtqc avvdaevgrs dccggagsvy pcnqpwwldr
      241 alqrvghynq imgpmttlql atelthalpv gtrvgwaggg ghfmvlrarf vadgveyvsv
      301 adpwygdsdv tdasyrnayq gsgtwthsyk tkr
//
LOCUS       WP_181580022             432 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nocardia huaxiensis].
ACCESSION   WP_181580022
VERSION     WP_181580022.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=45993
     Region          38..401
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkllhetgwa atpahseasl dkeitcdvvv igggvggmsa alraaengad vvlleshtlg
       61 wgassrnagy itnsiaadpe llrlllkper lrnlyryaen svhfaeeaia rheidcgfqr
      121 egivmaavsk gqlrharrna kamaeagssa efvegraagl pegflggvre gvggtlnpge
      181 fvlglraati asgvrvcehs pardvadtgd qvivttpdgr vrarkalltt naysaglsia
      241 pkrlatpvwt slvetepvaa erldeigwts rapmvtlhmi lesyrvtprg tivfgtrrlq
      301 tgrnplpdrt pdpkvaddlv rgfhdrfpgl rdvkaqsawg gwigmsstwl pvageasdnv
      361 lyslacnghg faqaqyvghl ladsaagkam hddlaaiwhg rkrfapsfvs gpalyagwla
      421 drvsdrlaal tk
//
LOCUS       WP_181580020             451 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Nocardia huaxiensis].
ACCESSION   WP_181580020
VERSION     WP_181580020.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..451
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..451
                     /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=48304
     Region          7..450
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mntheipdet ttvvvigagi agltaattls aetdvvvles tdraggrvet vrqgdywinv
       61 gtqftegtgt liealdrhgi ergslagksv alhlngrtid tsnplalmfr trmsmldrig
      121 maivgarila vmpflesqsr iaqrirarld akpasyllkg vrselaaaiv rswsaqwmgc
      181 evgetaatql vtsvglalad pakipnfslp vggnqtltdv laedlgdrir lnatvqsvrq
      241 dgedvivdyl dgnrparlra rraivtvpad iaeriipdla pryegafgdi aygryvitgf
      301 ftdeigvqrw ddyfavstpq lsfqamfnha aakrtgddrk pggalacfag gaqadamfdl
      361 sdaeivarft edllsvfpel egklgegivr rhhrvvpfwa pgrrtslptl raplgllhfa
      421 gdyqldlpsl adaaasgeqa aqavlaglsr p
//
LOCUS       WP_181579795             901 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Nocardia huaxiensis].
ACCESSION   WP_181579795
VERSION     WP_181579795.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 901)
  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 901)
  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 901)
  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 901)
  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..901
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..901
                     /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=93477
     Region          7..881
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mnpatvladn evglsaaeaa lrlrrdgpnt lpvpprprpi llmagqlthf falmlwaaag
       61 laliagmpal avaiavvvvl ngafafaqey radraaerlr dllplrarar rdgrvtsvda
      121 aelvsgdlit leagdrvcad aevtaagrlq idesmltges rpidiaagsv ihagtyvvag
      181 qceavvtatg rgtrlaglaa itqrasrprs pltkqlhrvv rvvavlallv gvlsfaafaa
      241 lgrdttesll faigvtvalv pegllptvtl slaraaqrma kanalvrrle avetlgattf
      301 ictdktgtlt rnemqvvrvw tplgevtvhg agydpdggle gppaavnaaa aladsaarcs
      361 pdahvmqrag rwtpvgdpme valhvlaara gcppappira rdpfdphlrr aqvtdadgih
      421 itgapeavlp lcdserdtgc sagsdtgret gpgtdrapnp ttgcasapdt gdarataear
      481 vaelsarglr viavarrtdq ggtrllglvg ledpprpdva eaiaacrrag vrvamvtgdh
      541 pgtaaavaae vglfgdrriv vegkdlpgdd helgallnsd gvvvarvape eklriarvlq
      601 qcghivamtg dgvndgpalr tadigiamga sgtdvareaa dlvllddhfg tivsairlgr
      661 atfanirrfl tyhltdnvae ltpfavwaas ggavplgftv lqvlaldigt dmlpalalga
      721 eppnprtmdg parvrslvdg rllrrvfltl gpaeagagml aflavlyagg wrwgapadpa
      781 lvalasgslf tavvfgqltn afacrsesrp arfggwrdnp llpaaiavel vllgvflwlp
      841 plpellggsv pnalgwltaa lavpavlvld liykginarf gagssaadry asprrlrrpr
      901 a
//
LOCUS       WP_181580346             497 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia huaxiensis].
ACCESSION   WP_181580346
VERSION     WP_181580346.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 497)
  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 497)
  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..497
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..497
                     /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=55750
     Region          21..447
                     /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 mapqydaivv gagfggmgag ieldrlglsn flilereddl ggtwhvnhyp glavdiasvt
       61 ysysfepnph wsrlfapgae lkkyaehvad kydlrrrmrf ntvvggarwd eehqqwsvai
      121 engesltary iftatgflsq pytppfpgie tfqgkiihst awddsydltg rkaaligtga
      181 tgvqlapela akvseltvfq rtpiwvvpki dfeiperlqg lfqrvpltqk aarmvnttll
      241 eglmvigvlh fkeakplnka agvlakahmf sqlrdkktrk amtpdydfgc krptfsnkyf
      301 kifnephvrl etnsidhiep dgivtadghk teidtlvlat gfnlwdvnfp aieiigrdgv
      361 nlgkfwrdnr fqayegitvp kfpnflslns pysysglsyf ttieaqmkhi grlftemfrr
      421 geqvfevtee ankkfldtvt eklgssvfyd gqcstarsyy ynqhgeaall rpnstltthr
      481 havsfplddy sygpvpa
//
LOCUS       WP_181580423             464 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181580423
VERSION     WP_181580423.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..464
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49282
     Region          41..378
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mmqtrraawl aalatlltaa plvvpaasae tagvscaepv pgqplpranp edvqldsaal
       61 ndaldfgart ggvalqvyrh gclvgdrtpt gnlpmplasa tkgvaatvvg raitlgyfgl
      121 ddplgkffpq adaahaeltv rqvltqttgl hfswpadiag lytdsvlqtl aepadyapgt
      181 tyqyaqnvia vlskiielst gsdfqdfaqr elfaplgidr dnwiwlrdrs gntavnggla
      241 mrpddlaklg rlmlqqgqwg dswlldpdyi rqattgttan pgygfltwln sgdtylgtef
      301 ptaithphpq fpgsprdmya fqgalgqfmt vvpsrdmvii rmgiplridp tnpaailsga
      361 gnpdnkelyh ritaavtdlp aepyvdpytl psspapvrsl ddlaklvdpv ntatillgvg
      421 pyastacnil wcngkpvpvd vfrlildiga qaanallalg ntpr
//
LOCUS       WP_181580602             267 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Nocardia huaxiensis].
ACCESSION   WP_181580602
VERSION     WP_181580602.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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 14398449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=28411
     Region          38..125
                     /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          183..264
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mspnghrrtp appsgdaesm visapagpta mvfgagalpa glwfdehahp qhqiawatrg
       61 vitveigdgr wvlpptralw ipggmrhrtg tsegammsgi ylepdrtpva fpaptmlrvs
      121 tllhelfghl taatttagqr qraeavifdl lqpvdvipvg armpedarar rvadalladp
      181 adprtleqfa pyaaasprtl araflaetgi tfghwrtqir laaslpllad glpvariaar
      241 vgyatpsayv aafhrevgva pgryfar
//
LOCUS       WP_181580568             221 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Nocardia huaxiensis].
ACCESSION   WP_181580568
VERSION     WP_181580568.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=23414
     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 myvvimgcgr vgsslaralv righevavid qnssaflrlg rdfpglcvtg vgfdrdvltr
       61 agieragafa avssgdnsni isarvaretf gvdrvvariy dakraavyer lgiptiatvp
      121 wttdrflrtl vsdqsttswr dptgtvavte lvlhedwygr tvhsleeatg srvsflirfg
      181 qgvlpngktv lqaddtvyva atsgsvgeav alagnppase d
//
LOCUS       WP_181580639             116 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardia huaxiensis].
ACCESSION   WP_181580639
VERSION     WP_181580639.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=12597
     Region          1..99
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 msiavdddlw savgdptrrr mldlllsegg gtatslsarl pvtrqaiakh lgvldrvglv
       61 haspagrekr yrvdeaqlar avaqltsvga twdarlrrik siaeaiqrkq dqnrte
//
LOCUS       WP_181580760             516 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia huaxiensis].
ACCESSION   WP_181580760
VERSION     WP_181580760.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=58140
     Region          1..450
                     /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 mstpdhefvi igagpcgiga gitlkrhgie dfviverfde pggtwsvnty pgigcdvptp
       61 gyefffarnp gwsrffpkga eineyhlgia rshgiephyr frtdvtrqaw deqqhlwrlt
      121 iangreitar yiiaaigqfs dprlpdipgv dsfagkvqqp arwdhtydmr gkrvivvgtg
      181 asavqiipei aplaqrlevf qrtpiycvfk pdfvppraia rafsapalnt lqyvlwtvgf
      241 dllmealtea pgviahpalr gfdrlartym rarlrwtvrd pdtrrrlmpg hggaakrpal
      301 sntylptfnr pnvelvttpi ervtetgivt adgvthdcdv lvlatgyhff adpefykvgw
      361 vtgrdgrdlg efflehdvqa yesasvpgfp nrwmlsgpws wshivhtmse fltaniarsa
      421 naaraqgita levsehahew yhaktvrknr nfqwyfeeln rdartyytns hgtvaglrhv
      481 twiemwlrnl lsplggydcr rlgapvrtdq pleqvg
//
LOCUS       WP_181580908             403 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181580908
VERSION     WP_181580908.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 403)
  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 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   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
REFERENCE   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..403
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..403
                     /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=42582
     Region          19..398
                     /region_name="BagY_FevT"
                     /note="LuxR family transcriptional regulator BagY/FevT;
                     NF041232"
                     /db_xref="CDD:469135"
ORIGIN      
        1 mttasrhava allddieaap dahalfatts erlrrvapfd aavwvatdpv nglttapvrv
       61 enlheggcgt ywesellaeh vnlfrdlara rvpvaglrav tgdrpeasal yrnfmrprgf
      121 tdelravfri ggrpwgqlsl frergraeft raevalldtl stplaqrlra faqpgpvasa
      181 vagaawtepg spaskggdav ngvgaspgal tpvdisdgpg mllfdadggl vsinaeardl
      241 laqmppgpat atplgidlpl pvwilstagr arltggstri rirsvtgrwl vchasclrda
      301 egrpgatamv iepakpseia alvvaayelt rremevveli arglgtadia arlvvsphtv
      361 rdhvkavfdk vgvtsrgelv aklftefqep llprgtvrve tag
//
LOCUS       WP_181580914             336 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181580914
VERSION     WP_181580914.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..336
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..336
                     /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=35767
     Region          1..326
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkpiayarpt tveqavstvt srpgtvflag gttlvdmlri gamepdnvvd itwlplggle
       61 htpdgglrig alakmsevaa eagvrerypf lsvalwkgas aqlrnmatmg gnlmqkvrca
      121 yfrepgracn krdpgagcaa mdgihrghai lgtspmcfat hpsdvaiplv aldatvtvwg
      181 prgertiafd dffllpgstp hvehplagde litridvpal pfarnshylk vrdresyefa
      241 ltsaavamnv adgtvvdvri glggvatkpw rartaesvli gksatranfe kaaaaeleaa
      301 dtshpmnvfk velaqrtlvr aleavrpqvh plggtr
//
LOCUS       WP_181580967             471 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nocardia huaxiensis].
ACCESSION   WP_181580967
VERSION     WP_181580967.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=51710
     Region          39..408
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqakgsklwa saltdavpap ywtdrpdrpv pteplttata adlavigggy sglwtallak
       61 ernpgtdvvl vesamcghaa sgrnggfcaa slthglangl erfpdeiddl erlgranlda
      121 ienaiarygi dcdfertgem evataphele wlreshvaat algyrsdlld aaevqrlvhs
      181 ptylggwwdr dgvamldpar lawglrracl klgvrifegt pvqriskstg gtltlhtphg
      241 evraprvalc tsafagplpk vsrhvvpvyd yalmteplta sqldtigwrg rmgmgdasyr
      301 fhyyrltrdn rilfggydai yhfggriapa lesneatfet lsrhffqtfp qldglrfthr
      361 wggiidtcgr fcaffgsayr grlayaagyt glgvgatrfg aevmldrlwg ldtertrlrl
      421 vrsrplplpp eplrsagiql trwslarada hqgrrnlwlk tldytglgfd s
//
LOCUS       WP_181580216             548 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Nocardia huaxiensis].
ACCESSION   WP_181580216
VERSION     WP_181580216.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=59441
     Region          3..508
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mgmsrrqllr fgaagsaavl vgtsaasssr lrtarlaggd pfalgvasgd ptpdgvvlwt
       61 rlapdplapd ghggmtnapv tveyevahde gfrqvaargs avatrelahs vhpevnglep
      121 drwyfyrfra gsaispvgrt rtapaagqam rrlrfafasc qswssgyfta yehmsredld
      181 lvvhlgdyiy eqswiharvg tapdpdvage amdlrgyrlr yaqakaeapl qaahaafpwl
      241 ttmddhevdn nwagdtpglg fdiyaipalf rrrraaafqa myehqplrva qmpsgpnill
      301 hrrfrfgdla eitmidtrsy rsplacndgk avadcearya tgrtilgsrq rdwlvdgfrs
      361 sparwqvign qvpmarsdyd pgaavelgtd swdgyvadrn tvlgaaadhg vrnlvvitgd
      421 rhenvvadlr rdhsdlesai vasefigtsi tsrgdgvdlt paarqvlatn pdlkfsnsqr
      481 gyvrveldhg lwrsdfrvvp yvrrpgapih trasfvvrdg vrgvvaastp dpasdtaalp
      541 apdspgpr
//
LOCUS       WP_181580996             121 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardia huaxiensis].
ACCESSION   WP_181580996
VERSION     WP_181580996.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=12628
     Region          6..111
                     /region_name="ArsR_Rv2640c_fam"
                     /note="Rv2640c family ArsR-like transcriptional regulator;
                     NF041413"
                     /db_xref="CDD:469304"
ORIGIN      
        1 mskqelplia tadccatlss pldpdtaagl asafkaladp arlrllsmia aaggeevcvc
       61 eltpafdlsq ptishhlkvl reaglltser rgtwvyyrvi pqalqrlsdv lvpaaattap
      121 a
//
LOCUS       WP_181581027             441 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Nocardia huaxiensis].
ACCESSION   WP_181581027
VERSION     WP_181581027.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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..441
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..441
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=46401
     Region          72..107
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(73,76..77,80..81,83,115,118..119,122..123,125..126,
                     149,152..153,156..157,160)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          84..314
                     /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          113..143
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          148..176
                     /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"
     Site            order(219,222..223,226..227,229,253,256..257,260..261,
                     263..264,286,289..290,293..294)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          221..438
                     /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          251..280
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          389..419
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mshcptrlra rthrtpalvv ltliavaaai igvaavpdrh staapavsgp gaalaaqiet
       61 mrgqldrmpg navrwadlga ayvelarmtg dpshygaaqr aldrslevqp dgnadafigl
      121 galknalhdf gpaktyaena itlrptsada ygvlvdaltq lgaaddatva vqrmldlrpg
      181 vtsftraayd lelhgrtdea rtalgmalda antadqiafc ryhlgelafd sgqldeaenq
      241 yraglltvpt saalrqgqak vfaargdtdr alalyaelts dsalpqylie ygellesagr
      301 aaeaaaryqd vvaqfralea qgatdavdaa llaaehgdpt eavrlaqley grrqsvltad
      361 vlawalhrag rdaeaigyad qanslgwqna slayhrgmil aalgrtdqaa taltdalrin
      421 phfsplhapr aaqaldalta r
//
LOCUS       WP_181581090             378 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nocardia huaxiensis].
ACCESSION   WP_181581090
VERSION     WP_181581090.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..378
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..378
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42011
     Region          145..372
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtaeattsre rliagllarr arltdrivlr arteipgyhh lssaelrprt glmievvlqa
       61 fgaqrtpset elrsfhewgv ararqgisla dmltawriav reildeitsi grshniadrl
      121 qlelvremld lvdiaileft sghreielen arldhqarae fvrsvltgtv graelavraq
      181 ryglgidhpy ipfrvrptaa hslealerll prpsftttvd gdlagftdrl peslpvplgf
      241 adpapidals pgftqatral naatafqrtg ahslaelgll pavladsevg dlligryldp
      301 lrhtgtpevy ldtlrcyles gqhidstakt lvvhpntvry ridrfqaltg hdlrkpsval
      361 elwwalqrqr lrtdrpgp
//
LOCUS       WP_181581134             294 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181581134
VERSION     WP_181581134.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..294
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32797
     Region          12..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          103..285
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maapstlpri llglelknlr egttvkreda aelsgiskpt lwriesgldv rlnpvliqkl
       61 cevydatpeq tnailalvqe aaedkdgwwh afsdaipkef nlfvslenra nhlvsyqttf
      121 lpgqlqtley rralswiefp dkssrdterm lqvamkrqer ltssdnplql avlidesvlr
      181 rdtggpevma tqlkhlsamg elpnvsvrvv pasagtyqgl fagtfvlfef pdhpnneltr
      241 ppivyvqgya ggrydkqpdv itkyrgvlad terlaldegn srqlilsiak eyst
//
LOCUS       WP_181580731             260 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Nocardia huaxiensis].
ACCESSION   WP_181580731
VERSION     WP_181580731.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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..260
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..260
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26702
     Region          99..260
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msdrvrvadp dcggyavgvg hacadydgtv igmrerlsar glgvfafivv vvlavvgwsv
       61 wdakrdrgsd teagetvaag papfeagrlr fgdpnapgtl vviedyqcpl ckslnvvsgd
      121 ainaavtegk aaveydivav ldgestteys sraanasacv avadkekwra frglvlqrqq
      181 ptgsaglgda elvelarqag vadpgldacv tsgryrdfva ahtkvvvagg lsrvpvvlan
      241 gaevisptpq gisdalagkr
//
LOCUS       WP_181581141             215 aa            linear   BCT 28-DEC-2024
DEFINITION  YceD family protein [Nocardia huaxiensis].
ACCESSION   WP_181581141
VERSION     WP_181581141.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 215)
  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..215
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..215
                     /product="YceD family protein"
                     /calculated_mol_wt=22864
     Region          20..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 mpadsghgsr rrlkqtdagf vldtrslgra pgsmrelhrt httdgklgle mvgipagaqv
       61 emdlvlqsvs egvlvtgtvs apiegecsrc lesfsdeidl qitelfaypd sateqtteed
      121 eihrlvddmi dlepviidav glelplqplc epdcaglcpe cgvrmaiags dhtheildpr
      181 waklagfavq ngehsavpng asgtdqsaes dseek
//
LOCUS       WP_181581163             273 aa            linear   BCT 28-DEC-2024
DEFINITION  EamA family transporter [Nocardia huaxiensis].
ACCESSION   WP_181581163
VERSION     WP_181581163.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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..273
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..273
                     /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=27379
     Region          1..273
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mpptalvlgg ivsvqlgaaf akqlfgatgp agavslrlgf agiilliiwr salridrrai
       61 pvvlaygavl gsmnlcfyea idriplgmav tieflgplav alagsrkwid pvwallaggg
      121 vllltqadgp vsmagvllal aaggfwagyi lltarlgert sgggglalam afggllmapa
      181 gifeagtall dpavlavgfa vallssvvpy slelealrri pprvfgilms lepavaamag
      241 llvlgqvlgv gqwagvvcvv aasagatrtg tpd
//
LOCUS       WP_181581325             361 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Nocardia huaxiensis].
ACCESSION   WP_181581325
VERSION     WP_181581325.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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..361
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..361
                     /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=39306
     Region          3..334
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mgrripvlvv agflgagktt llnhllrnnr girigvvvnd fgavnidaml vagqvdamvs
       61 lgngcvccav dvgeldalfd qlaqpkakid vivveasgla eprnlirmiv nsenprityg
      121 glievvdaeh feesraqhpe lathlrmadl vmvnkadrvt pealdtlrde igalafpaav
      181 yatahgridp gllfdaprra askprvgeql sldellfaet eahddhehda hcdhhhlhde
      241 yqslsftsdt dlnpraliav fedpppglfr akgtlafatp ddqrkfvlhm vgrhivvepv
      301 pwprheprts slvligagld tdialerlra tvhtgpeplg eqellpvwry vtahdhadtp
      361 a
//
LOCUS       WP_181581377             767 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nocardia huaxiensis].
ACCESSION   WP_181581377
VERSION     WP_181581377.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 767)
  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..767
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..767
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83872
     Region          2..767
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 marrvtgnlp aevtsfvgrr delatakrll pttrvltllg pggmgktrls rqigqlvara
       61 fpdgvwlvel advldpnlvt lsvaetlslh destaplprl tefladkrll lildncehli
      121 eacaalvgri iattpdvrvl atsrevlgip geqvmpvppl tvpdphadae sdalqllter
      181 ataanpafrp tpanhaalee icrrlegmpl alelaalrlr mftpeqildr lddtmgllsa
      241 gprtaphrqq tiegairwsy dlctpaeqql weqlsvfagg fdidaaetvc elggaslida
      301 ltglvdksvv mlrfedeqar ysmlepirqf aadrlaergd eqrvrtrhri yyrqlamrgq
      361 taywtaddva wfrdlgreha nlraalrsgm vdeplatmet vtvlrpfweh hrflsegyrw
      421 lveslqhnpe ptlararals saaslaallg drdsaarqvt hcltlidalg dtdilpeval
      481 drallafaeg drehslelar sgielarthg qraiemdsha fafmcahlle apdrseiakd
      541 fvaittasgs hllgglalwt mgldhwrlgd ldaatgyhtr aiqqlalfer cvwlssafeg
      601 lawtvsaqge hdraarllga aeslqrstir lahtitiavg dkerekvrea lgedtfraaf
      661 gaganlplee aidyalrrtp apavvtpapa apkpaarkss avgeanvltr rerdvarlva
      721 aghsnkriaa dlvisvrtae thvehiltkl gftsrtqvaa wahetgl
//
LOCUS       WP_181581411             271 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardia huaxiensis].
ACCESSION   WP_181581411
VERSION     WP_181581411.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=28995
     Region          4..255
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mkdfhgkvav itgagagigr alaiefarng aqlalsgrnl dnvaetaalc ekegakaray
       61 qldvtdraav yahadevvad fgkanilinn agvsltanie dvtwedlewi fginfwgtah
      121 gtkaflphvi asgdghianv ssmfglvacp sqggyssskf amhgftdalr qemiiaghnv
      181 gvssvhpgmi kteiawkara sanrdrddla rnfdrlaqts pefcaqtilk girknkplil
      241 igkdakamnv mrrllgsgym kpltaqmrke i
//
LOCUS       WP_181581442             310 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Nocardia huaxiensis].
ACCESSION   WP_181581442
VERSION     WP_181581442.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=31494
     Region          7..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 mtnrtirsia lvtnplsgag kgalvavdaa ngfaargiev telcgdsaad terlvraala
       61 dpvtrpdavv aaggdglvgv vlqalvgtgv plglvpggtg ndlarevgvp dgtdaaidvv
      121 lggrtrtidl gaveteagas ptwfatvtgt gldarvtlra nhmrwpkgpl rytaaaliel
      181 agklavpyri elhgspdhrd gtvfelpavm vavgntrtyg ggmlicpdav iddglldltv
      241 vgamsrldml rllpalssgk ridhpatvqy raarikltap dapatadgdp agmlpatfra
      301 lpgalevlvp
//
LOCUS       WP_181581440             340 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Nocardia huaxiensis].
ACCESSION   WP_181581440
VERSION     WP_181581440.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   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 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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..340
                     /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=34952
     Region          78..204
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrriirrlph taailaaaaf vtlgmntgva hadsgshssd tvgygpefrd eaaavaygla
       61 npdvapqgsn dwnckpdaah prpvvlvhgt wasafsaysy mspqlaragy cvftfnygra
      121 napgaglvqp tigatgyied sarqladfvd rvraatgaaq vdlighsqgg vvareylkfd
      181 ggadpadpsd nkvanlitfg atnhgttlag lgnllgplsg llgvnltqpt edlighagiq
      241 qlvgspvlta lndggdtvpg vhytivadql devstpapqt fltagpgatv dnvtlqdgcg
      301 adtsdhnsml fspravsial haldpvahpd lvcstnpwll
//
LOCUS       WP_181581474             506 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia huaxiensis].
ACCESSION   WP_181581474
VERSION     WP_181581474.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=56226
     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 msaatqpldv aiigagfagi gtairlrqkg ignfailerd shvggtwrdn typgaacdip
       61 srlysysfap npewsqtysg sgeilgyies mvdefgirpf irfghnvtgv efdevsglws
      121 itlagkrtrl rarsvvlasg plsnagfpqi pgiddyeghk ihsarwdhdy dftgkkvavv
      181 gtgasavqii pelvrkaaav kvfqrtpgwv lprvnrnthg ltkklyrqfp isqtlardaw
      241 fwghesvalg vvwntpltrv veriallhlr tqvedpwlrr qltpdfragc krllmssdyy
      301 palqrdnctl vtwpiarisp hgirtaegie hrfdcivfat gfevskqgtp ipvtgrdgrr
      361 lseewqrgay afksvavagy pnlfltfgpn sgpghnsalv ymeaqieylt eaidlllrkd
      421 lrmlevrrdr qdrynaglqr rltattwnsg crswyltedg fnatmypgfg tqyvrqlaal
      481 dpadytltpr daapvsagdr ttarlg
//
LOCUS       WP_181581525             488 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia huaxiensis].
ACCESSION   WP_181581525
VERSION     WP_181581525.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 488)
  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 488)
  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..488
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..488
                     /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=54433
     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 mttasdhydv aiigsgfsgl gvainlrrlg idnfvilera dtvggtwrdn vypgcavdvp
       61 svlysysfap npdwtrlyat qpelreyten vvdsfdlrrh vrlrsevgsa dfdesaklwt
      121 iqltdgreir araavmgyfs lheatvpdip grmeftgpqm hssrwdpafe pegkriavig
      181 sgasavqivp alartsarvl sfqrtaawvl prgdrpippa vrtvlrripp lrlaarafvf
      241 tflealhfae fhprlvslya rvclaalkrq vpdpetrrkl tpdysfgckr pmvsdeyyaa
      301 farptvdlvt ekiieitptg lrtadgahhe vdaivwatgf hvqdsiarfp dfrtpttstr
      361 rkfaedgfta yrgiafaglp nlfavtgpnt alphtsqfla ieptarliar tiahmrahhi
      421 prytpsagae rewvtrardl lssrvwstgg ctnyfttadg tntltypggt wtlrrdrrql
      481 rledwqlg
//
LOCUS       WP_181581668             371 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181581668
VERSION     WP_181581668.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..371
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40514
     Region          42..322
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mefaesparg vefpratpea vgldpvavrd avafserrst rsiriyrygq lvatgerdav
       61 rahavrpvws asksilamvt gravtlglle lddpigryvp eadarhrdit vrnllnqssg
      121 lafrtmrela ipaydqvrla ltaepkhapg tyfeyaqapl sllghvvara agtdsvtfaq
      181 relftplgig adrwrvvkdr aghpywaglv fatahdlarf ghtllrdgkw adedllspdf
      241 vrqartpapt npgygflvwl nasidtitcr apgrsildrp viasapadty lfsgmfdqiv
      301 aiipsldmvi vrtgqvpnrt aditgmmsvi taewaheffr rlfaghadpa vpadpgpfra
      361 dglrpllrgr g
//
LOCUS       WP_181581479             374 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181581479
VERSION     WP_181581479.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..374
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39206
     Region          28..370
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlaavgcees taadstanrs advsmstrvt daltglvrsg mpgaqaiisg pdgqhaftag
       61 agdlatgapy adgahirigs vtktfaatvv mqlvgegavd leapierylp gvvqdngndg
      121 nritvhqllq htsgladfap eggseklpqq ldqttdgray rdftsadlvr iatsmppqfe
      181 pgaqfrytnt nyallamlie hvtgrpfaae issrifdpla mrdsyipsrg dtglrdphpl
      241 gyrkvddkwv dvteaevawa gaagaivstg advnrffial vtgkllpaaq laqmedtmpm
      301 ppftemtygl glvrfqvpcg nevkeawghs ggipgfstma iatstgtaat isvnteqtne
      361 qyssaftaiv cava
//
LOCUS       WP_181581711             442 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181581711
VERSION     WP_181581711.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..442
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46751
     Region          90..322
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msvlavllaa aapqafadpv dppwgekrca pssgrapeta tpeevglnpq lvadavafaa
       61 arqrldiqiy rnnclvavgp therdggiaw nlwsatkgvv sliagaaytd glldidapid
      121 lylphglgdi ehraitvrdl ltetsglrns viaegltlpv dpdvvaqala vpfafppgtg
      181 ptysqravdl lvyviqqavg adfqdyaqrr vfgplgirsg dyhwardrsg htygyahllm
      241 ppddfaklgl ltlnegrwnd ttvisadyla martperqnc ygfllaigsn gcsgdfdgfp
      301 geisamtgwl lqtnymipdl nllvswtglg ggtpgqgvqg vleddgelqq tffrmladaf
      361 dltptaprvp spdanalpdl gklidpeial galglgraay pgctvltcld hplaapfagw
      421 pagcfilacl pavptapair dr
//
LOCUS       WP_181581673             448 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Nocardia huaxiensis].
ACCESSION   WP_181581673
VERSION     WP_181581673.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 448)
  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..448
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..448
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=44745
     Region          57..133
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          122..190
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          179..246
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          235..298
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          287..362
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          351..422
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mrshvlvcaa lvagttfaag qavaapstgs gggagtqfsg phyfdtgtap wvtragdvng
       61 dgrpdiitan agsttingtt ygglkgvsvl lnttadgaaa psftapkqfv agvgtlsvel
      121 adldgdgape iitsnffdtg tngvsilrnl tpagstaaaf aepinlatga fpslvrtldi
      181 nadgkldlvt gdagipfglg isvllntsqp ggpltftppt qflggsvaeg lavgdinndg
      241 ledvivantt tsnvavlvnt tapgsftptf nvtqewvvts tdaqladldg dgrldmivsr
      301 taggftvrln rtapgaptae fgedivgdlv gevtraqgtm gvvtegvaia dfdgdgiadi
      361 avnndfpipg ygisvftnht qpgartinls gpdgyngssw iigtnsiaaa dfngdgkldl
      421 atgnvpslav ednvlvhggi svllnthp
//
LOCUS       WP_181581769             523 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia huaxiensis].
ACCESSION   WP_181581769
VERSION     WP_181581769.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 523)
  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 523)
  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..523
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..523
                     /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=58290
     Region          36..459
                     /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 mstvsngrga paetrpdhev ivvgagfggi gtgialqrkg ihdfvivdkw drvggtwhan
       61 typgvavdip sfiysfsyeq rgdwsrifap gtelreyaes mvdkyglrnk lrlnttvvga
      121 efdernslwr latdgghelt aryvvlaigg lerpkmpdip glqdfggtlv htalwdhdva
      181 lrgkrvavig tgatalqlip aiveetahlt vfqrtpiwvf pkqdaeigwl grqilgrsri
      241 rsalrvagnl gtelamsgmv vgppwltgag rrlaeipirr wmraqvhdpe lrekltpryg
      301 lgckrpsmsn dylktfnrtd vslvtesidr itehgvvtad ghehridvlv catgfklwdk
      361 gaippfpvrg rggldletfw dehryqsyqg vsvpgfpnaf titgpygfvl gsyiwmieat
      421 aahlsraiae skrrganeie irqevheeyf rkclarqqkn flftpvcegs ntyyidnhgd
      481 spfrpsthge mywqnrhfdl dvyrytvgap vpsdelalse eas
//
LOCUS       WP_181581610             112 aa            linear   BCT 28-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Nocardia
            huaxiensis].
ACCESSION   WP_181581610
VERSION     WP_181581610.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..112
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12420
     Region          1..110
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 markvivemv ddydgkstae etvqfaidgv ayeidlskln aakmrgefeq wtqharkvgr
       61 aprgkasgra raavdreqtq airewarkng fevssrgrvs aeimeaynka ns
//
LOCUS       WP_181581951             365 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nocardia huaxiensis].
ACCESSION   WP_181581951
VERSION     WP_181581951.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..365
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39351
     Region          6..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 mstpstakqg plagirvvel agigpgphaa llladlgadv vrvqragqfp gfmerpqwrg
       61 rtiveanlkd padiekvlgl vekadvlleg frpgvtermg lgpdvalern pklvygrmtg
      121 wgqygpladr aghdinyisl tgvlnaigrk gerpvpplnm vgdfgggsmf lvfgilaalv
      181 erqtsgkgqv idaamidgal alshmiwgmk gmglwsderg tnlldtgmaf ydtyetadgk
      241 ymavgciepq fyaeflkgle idpeglphql dpagqdqlrk lfadkfktkt rdewwaifep
      301 tdacttpvlt fteaeqnphi qartglidid gvvqhapapr fsrtpggipt pppnegtpie
      361 qvwad
//
LOCUS       WP_181581599             155 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nocardia huaxiensis].
ACCESSION   WP_181581599
VERSION     WP_181581599.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 155)
  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 155)
  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 155)
  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..155
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..155
                     /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=17001
     Region          22..155
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 msapiagttp spkpqrhkvt gdvhlllrrg nqvlfgqrqn tgfedgawhl psghleades
       61 vidavireae eeigvaikqe svqfshvmhn ssssgrmaff ftvrswegep tnrepdkcsa
      121 lawfapdalp dhmidycraa mghiangtpf svygw
//
LOCUS       WP_181581962             871 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia huaxiensis].
ACCESSION   WP_181581962
VERSION     WP_181581962.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 871)
  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 871)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 871)
  AUTHORS   Rosinski,J.A. 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 871)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..871
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..871
                     /product="helix-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=92834
     Region          <6..859
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          803..857
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 marnwpmver enelesirsa ltgddfvgav ltgdagvgkt tlarqataav ggnirwvagt
       61 esarsiplgv fahmvgvyta hdpvtfmaaa realladght iigvddahll dqlsatlllq
      121 laidkaahiv atvrsgvpvp davtslwkdg hllridlspf tqrqsvelve smlggqlegf
      181 tanlmwessg gnalflrhlv egaleagtlr qvngvwqlrg raavtselaa lledrveqlp
      241 esvlrvlell tfcepidldv lcelageeav emaesrgvir ivenshqllv rynhplfgev
      301 irrrlgiasa rrlrgrlyss lkerrinsas drirlaelal dsdksadlel feaaaadaig
      361 lanlplgerf araaverrgg veaadllara llwqghriea ertlaafdpd rmnevqlarw
      421 ggtrvanlfw smgdsdrade vldsvrsrvk hpkisiildg lasacavhen rldeafalae
      481 pvmetegapp wavwwaafgg glalalmgrg daarqyaerg raveshidgl nrfmsqhaev
      541 laltftgdfd aarhcasgpy aysspgqyva wgmnkilhgt vdvaqgrfpq gidnleqaia
      601 altaegaasw miparlrlae aysalgrtad aaesiaaaie rggrhsavyd pqleiakawq
      661 aaaegmvspa irialgaada aarsrqhaie aialhaaarf gdqtvagrla dlaarvdgrl
      721 vqaqarhava vaahdgpgld saaaefeqig allsaadaaa qaasaherag drrrllesaa
      781 tanrlaaacg gastpalrqs aqplpltsre reiaslvaag lsnrqiadrl tvsvrtvegh
      841 lyracikldv tdrealaelm rggssfgkpe s
//
LOCUS       WP_181582173             527 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Nocardia huaxiensis].
ACCESSION   WP_181582173
VERSION     WP_181582173.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..527
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..527
                     /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=55905
     Region          13..502
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msdserhprp rrdrydvviv ggghnglvaa aylaragrsv lllerephtg gaavservfp
       61 gvlarlsrfs ylvsllpeli vrdlglrfet rkrrissytp vgehgllvdn asvagtrdsf
      121 arvtgserdf lawqrfyamt gelarrvfpt ltqplpsrae lrrrvgdpaa weavferplg
      181 evveatfadd tvrgvvltda ligtfaqahd psllqnrcfl yhvigggtgd wdvpvggmga
      241 ftdalaaaar aagaeivtdc tvtgletdgg taevrftlgd avagavaarh vlvnaapyvl
      301 agllgeeaak pegaqlkinm llrrlprlrd asvdprtafa gtfhiaesat qldkayreaa
      361 agripsapps eiychtltdp silapelieq gmhtltlfgl htparlfate pestkarlvd
      421 atlaqldsvl sepirdclal dadgnpclea mspvdletev hmpgghifha dlafpfhted
      481 gdpatpaarw gvatahanvf lcgagavrgg gvsgvgghna amavles
//
LOCUS       WP_181582279             491 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Nocardia
            huaxiensis].
ACCESSION   WP_181582279
VERSION     WP_181582279.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 491)
  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 491)
  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 491)
  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 491)
  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..491
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..491
                     /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=51800
     Region          2..490
                     /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 mntplrrvsl avmvmivall anatyvqwwk addlrtdtrn rrvlldeyar qrgqisaqgv
       61 vlassvated rykylriypt dprayahvtg yytmqngrdg lenaedsils gsdndlfgrr
      121 lvdmisgrdp rggnvittln pamqkvaydq ltskgytgsv vaiepstgri ltmvstpsyd
      181 pneltvhdga qvtekktelq qddgqplinr avsmiyppgs tfkvvvtaaa langlatpsd
      241 qltaasritl pdtnttleny ngshcgpgdg ataslteafk yscntafvdl gikvgaaklk
      301 deaaafgigd hsgiplewgt stvgdipdka algqssigqr dvsitpldna viaatiangg
      361 vrmqphlvdq lqapdlttlk ninamsvgqa vsaqvasqit ammieseknt qggtqprsyt
      421 iasktgtaeh gddprntpph awyiafapaq npkiaiaviv enggdralaa tggsvaapva
      481 ravldaglqg g
//
LOCUS       WP_181581778             513 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA synthetase [Nocardia huaxiensis].
ACCESSION   WP_181581778
VERSION     WP_181581778.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 513)
  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 513)
  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 513)
  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..513
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..513
                     /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=54963
     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(166,281..282,304..309,394,406,409,420,500)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(166,207..208,254,256..257,260,281..282,304..309,394,
                     406,409,417..420,481)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(207,256..257,260,281,417..419,475,481)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 myltqglhra vqqspdrvav ihgtrsrtft elhdrvarfa galrelgvre gdrvaiasln
       61 sdryheyffa vpwadavlnp inirwspaei aysledsgtg vllvddafaq avpaieqhys
      121 glrhvvfigd garpegmldy eeliaastpv edahrggyal aglfytggtt gfpkgvmlth
      181 nnlltsalga mstgvlhtpg grvlhaapmf hladyalwna aslagnthvt vpmfepkavl
      241 aaieqhgvtd tllvptmiqm lvdspalaeh dtsglrkmly ggspiaaavl eramkafpnv
      301 rftqaygmte vapvatlllp edhilegpgs erltsggraa phaevrivde sgrevprgtv
      361 geiivrgahv tpgywnkpae teaavrdgwm htgdggrmda dgyvyvvdri kdmivtggen
      421 vystevenai akhpgvaava viglpdeqwg ervhavvvpm pgssptaeei rahtkeliag
      481 ykaprtvdfa eslpisgagk ilkrdlraly tsk
//
LOCUS       WP_181582363             344 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nocardia huaxiensis].
ACCESSION   WP_181582363
VERSION     WP_181582363.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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 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 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..344
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36702
     Region          62..343
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mrfgrsavag gapsgrsahr rwsarllaag aaalaiptaa avaapsiala apahgpvhrs
       61 paggfeelmv pssmgpvkvq vqwaknggsk alylldglra rddrnawsfe tnamqqfend
      121 ditlvmpvgg qsswyadwts asntngqkyt ykwetfltke lpdflagygv sktnnaivgl
      181 smsgpaalrl aaynrgmfkh assfsgplnw napgmreair vmmldagrfn vdsmaapwsp
      241 awlrmdpavf apqlkglpmy isaasglpgs hdapnsavgv fntanamgie aismvttrlf
      301 qqrlnslgin savydfpasg thswkywede lwkarphilg alng
//
LOCUS       WP_181582341             247 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Nocardia
            huaxiensis].
ACCESSION   WP_181582341
VERSION     WP_181582341.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 247)
  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 247)
  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..247
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..247
                     /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=26882
     Region          4..206
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mepvyfpiig lartvfalqg lkftvtgden ipaqggavia inhtgymdft yaglpartsk
       61 ryirfmakke vfdnsisgpi mralkhipvd raagadsyhe avnrlkagel vgvypeatis
      121 rsfelkefks gaarmaiean vpiipiviwg aqrvwtkghp krlgrtntpi sievgapiap
      181 fepaseltek lhstmeamll nvqrdyvhep gaywvparlg gsaptleean eldraeaaek
      241 aarrsgq
//
LOCUS       WP_181582738             394 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardia huaxiensis].
ACCESSION   WP_181582738
VERSION     WP_181582738.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   ter Beek,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 394)
  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 394)
  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..394
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..394
                     /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=40036
     Region          62..386
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrdnrralae tsrstagtdr agspaeqgks ldpavetfdv rfcslepvaa rrysgrsvns
       61 ivrqrrrvlv ygigcvavla vlatvalvsg eiampvptal saalgmgdag dvyvvqqfra
      121 prlvagviag aglavagail qrlfrnplas pdvmgvtgga slgvvlilaf gasqaaipfg
      181 alaggvlagv llillgskag lpvarlvlvg lavqaglqaa vnlfvvrfpr elassatqwt
      241 vgslygrtwt evqgaalala vvlvlafvqy rtlatldlgd esagalgisv psarlrllmt
      301 avvlaslaaa iagpitfval avpqlvrmlv gppsalslfv tglagavllv gcdlvaqhvs
      361 pvtvpvgivt atigapwlli lmlresspah rrta
//
LOCUS       WP_181582560             238 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nocardia huaxiensis].
ACCESSION   WP_181582560
VERSION     WP_181582560.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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..238
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..238
                     /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=24872
     Region          44..206
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mrseisgngs vpewlravae hepadptgin pvlrrvasai skpreasvlv lfggspdadp
       61 nalgglpdda dvlltqraat lrthsgqvaf pgggvepgdd gpigtalrea eeetgldpag
      121 vepisvlpki fvppsrfevt pvvaywrtpg evgvvsetea arvvrvplse lidpanrfvv
      181 rhplgymgpa faadgmlvwg ftagvlagll avsgwelewd hhdvrdlqas laavgmtl
//
LOCUS       WP_181583157             550 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nocardia huaxiensis].
ACCESSION   WP_181583157
VERSION     WP_181583157.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..550
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..550
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59576
     Region          9..484
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mvevdtrstd sdgiaaaket ledytlrfap rsyrkwspav vgvsalggia yladfaigan
       61 igiahgtgna llgigifaiv vmltgfplay yaarynidld litrgsgfgy ygsivtnvvf
      121 asftfiffal egsimaqgle lglgiplwlg ylastliifp lviygmntla klqvwttplw
      181 lllmvlpfgf lvvrhpdsvd affayggeng agvslsgtll aagvclslia qiaeqidylr
      241 fmppktpenk rrwwgwmlma gpgwvlfgaa kqvvglflav ylianlpaaq gianqpvhqf
      301 leiykdmvpg wlamtlavvl vvisqikinv tnaysgslaw tnsytrvtkt ypgrliflav
      361 nlvialvlme anmfdflnni lgfyancgia wivtvatdia vnkyllkisp kvpefrrgml
      421 ydfnpvglvg fglsavlsim tffglfgell kpyspivavv vsfvatplta vltkgkyylr
      481 rtddgielpl fdehgnpsge tlpcvvtgme ferpdmiasa vpgpegeiqy isslalstdk
      541 agihllpqqk
//
LOCUS       WP_181582932             374 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Nocardia huaxiensis].
ACCESSION   WP_181582932
VERSION     WP_181582932.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 374)
  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..374
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..374
                     /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=42479
     Region          12..358
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mstltapesg pmvlspqeve eigrrldalr aritadlgrr dreyiysiik aqrslevagr
       61 glmylgllpp fwlagvtals lskildnmei ghnvmhgqwd wmheptlnsq vfewdlvcpa
      121 dqwkhshnyi hhtytnirgr drdlgygflr idesqrwypy ylgnpvyaaa lmllvewgvm
      181 lhdleveniv rgkrnwsdlr rlisaqwrka grqvlkdyvt fplltgplfv ptlagnatan
      241 ivrniwayti ifcghfpagv qtfteeqtad etpgewyvrq mlgssnitgs klfhilsgnl
      301 shqiehhlfp dlpanryqei apevrdlcen yglpyntgpl saqigsvwkk ifrlalppii
      361 tgnasrpagv imtr
//
LOCUS       WP_181583236             437 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardia huaxiensis].
ACCESSION   WP_181583236
VERSION     WP_181583236.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 437)
  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 437)
  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 437)
  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 437)
  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 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   6  (residues 1 to 437)
  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..437
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..437
                     /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=46677
     Region          140..411
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrrillsmv aaltlttlvl gvplaftawq wvedisrnel rnrldriave vvaqergdgl
       61 vhgdldlrsv rplvpsggrl tivyptpqdn asridvgaea vtdplvesla mgtsgslrle
      121 tpaapmhsmq rqalgavvgl vlislgagia vavvtarrva dplrdvaara arlamgdfra
      181 dprrhgitel drvsdvldsa tveiagrlqr ehalvadvsh qlrsrltavr lrldelstht
      241 dpevvheaee amaqvdrltg aidelvrasr degaddrdpv pvvaelrgvv aewrhpfaea
      301 grklvllgdp tlkapvtgsr lreavavlvd nalmhgggtc tvsvrtvtgg rdireplvcv
      361 evadegdgvr delaphifdr gfsaagstgv glalaralie adggrlelqr rrpalfsvfl
      421 gapgsariqn diaaepr
//
LOCUS       WP_181583129             186 aa            linear   BCT 28-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Nocardia huaxiensis].
ACCESSION   WP_181583129
VERSION     WP_181583129.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 186)
  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..186
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..186
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=20944
     Region          5..186
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 msgverptlf fpdeqsfrdw laanhaavdg iwvkfakkgt gylsldydga lrqalcfgwi
       61 dgqsrrlnee fylqgftprr rrspwsqrnv glvaeliaqg lmhpagqaei drakedgrwd
      121 naygrdlpqd fldalarnpe aaaffetlpa qsriavgyhl gsaarpetre rrlqqliqkl
      181 idgqpl
//
LOCUS       WP_181582281             501 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nocardia
            huaxiensis].
ACCESSION   WP_181582281
VERSION     WP_181582281.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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 501)
  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 501)
  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 501)
  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..501
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..501
                     /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=52255
     Region          5..239
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
     Region          <238..>323
                     /region_name="PknB_PASTA_kin"
                     /note="Stk1 family PASTA domain-containing Ser/Thr kinase;
                     NF033483"
                     /db_xref="CDD:468045"
ORIGIN      
        1 mtlvlryaar sdrglvrann edsvyagarl laladgmggh aagevasqlm iaalahlddd
       61 epgpdllgkl dravregnas iadqveeepe ldgmgttlta ilfagsklgl ahigdsraym
      121 lrggeltqit rddtfvqslv degritpeqa hthpqrslim raltgneiep tlvvrearag
      181 dryllcsdgl sdvvsdetia ntlregstde sadrlielal rsggpdnvtv vvadvidldy
      241 gqshpivaga asgededtpp pntaagraaa mrppratprr avampepepp kkghkwrwia
      301 lsaallvavg agltigynmv rsnyyvgaeg gkvvilrglp gsvlgftird vdqiacatrn
      361 geiqladpgs afppgcrelt lpdlkstvqd svqkglpgvs rdeavkqmqn lsgdkgllpp
      421 cekpaappvt tpppgdpnqp gasttaaapt ttgapatstp pntgeqtlep rtpgseqptt
      481 tppvttttap kaseqncrva d
//
LOCUS       WP_181583335             147 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardia
            huaxiensis].
ACCESSION   WP_181583335
VERSION     WP_181583335.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..147
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16122
     Region          34..132
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mstrhsslev pgpdpaddpe alaadsadpt leadvfarnc lsrpvlgnva srwgvlalva
       61 lregpyrfsa lrrrvdgise rmlsqtlqal erdgmihrev qtsipphvey tltdlgaqva
      121 yhlhdlidvl esnigkiraa qesyhrd
//
LOCUS       WP_181582517             384 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Nocardia huaxiensis].
ACCESSION   WP_181582517
VERSION     WP_181582517.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 384)
  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 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   3  (residues 1 to 384)
  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 384)
  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 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   6  (residues 1 to 384)
  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 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 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..384
                     /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=39929
     Region          4..355
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mnarnltlat lafaltfwaw nligplsgsy tddlnlspgq tsllvatpvl vgslgripag
       61 vltdkfggrl mfavicflsi iptlfvgwsn sfgalifwgf flgiagtsfa vgipfvngwy
      121 epakrgfatg vfgagmggta lsalltprlv dhlgraqthi lmavalaimg vvmymfsrna
      181 pgwtpatepa lprikdalkl katwqgslly avafggfvaf stylptvlrn vyefaqsdag
      241 lrtagfsiag vlarpiggil sdkigpvrvl tiafagtavm avvlgfepap efpagislvl
      301 mafflglgtg gvfaliaklv eparvgtvtg lvgaagglgg yfpplvmglv yssrgdytlg
      361 ylllaltaaa alaytlkvgr eird
//
LOCUS       WP_181582688             244 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Nocardia huaxiensis].
ACCESSION   WP_181582688
VERSION     WP_181582688.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 244)
  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..244
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..244
                     /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=25936
     Region          2..239
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mdwressgpi gvltgagist dsgipdfrgp rgvwtrdpia ellstyqnyv adpelrvraw
       61 larrdnpawq arpnaaheal vrladagrav giitqnidrl hqragsktvv eihgnmfevv
      121 cidcdfgttm raaldrvaag epdpacpacg gilkaatimf gqqmdaasir aaveiaesse
      181 ifmavgsslq vepaasmcav avdagahlvi vnaeptpyde yadeivrdpi gealprlvde
      241 mlal
//
LOCUS       WP_181583355             114 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nocardia huaxiensis].
ACCESSION   WP_181583355
VERSION     WP_181583355.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 114)
  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..114
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..114
                     /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=11472
     Region          2..105
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mpwvfllias vfevvfalat nathgftvlg pslltaaaaa ggifflslal ksldvgvgyt
       61 iwtgigsvgt vvfgsvvfhe eftpakavaf vliiggvlgl kladklsapa avha
//
LOCUS       WP_181583356             106 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nocardia huaxiensis].
ACCESSION   WP_181583356
VERSION     WP_181583356.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=10943
     Region          2..105
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mswvylliav vfevafalgt natkgftrlw psvftllaaa ggiftlslal rtldvgvgyt
       61 iwtglgsigt vvlgaliyke kitvpkllsf asiiagaivl rvaagv
//
LOCUS       WP_181583580             277 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Nocardia
            huaxiensis].
ACCESSION   WP_181583580
VERSION     WP_181583580.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..277
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..277
                     /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=29915
     Region          5..274
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mnwempgpaw lfcpadrper ygkalaaadv viidledgva esdkaaarea lvahpqdper
       61 tvirvnaagt ldhmldldal vrteyrriml pkcesaeqit rlgdyevipl iesplgamav
      121 gravmarnai gvmwgaedlv aalggnssrh adgsyrdvar hvrsqsllaa kaygkfalds
      181 vyldipdldg laeesldava vgfdakvaih psqvpvirra yapvaaevdw arrllaevpn
      241 hrgvftfegr mvdmpvirha erivqraqga dsagfas
//
LOCUS       WP_181583639             901 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nocardia huaxiensis].
ACCESSION   WP_181583639
VERSION     WP_181583639.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..901
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..901
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=96198
     Region          <1..900
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mlygrereer rigtllteaa rgrsgavavv agpgegksal leraaemtga tlpagaspww
       61 rvlrctgmet aaelpfcglr allepalahl palpqpqaga lsgalglasa erdperflvg
      121 latlsllael shegpvlcli ddaqwldqps ldallftarr lgdegiavlf agrpdftaag
      181 leilhpapld aqaarallae hspelpvevr drvlaesagn plallelpgm nldalpvgpl
      241 alsdrlqsgy qehigdlpep irlallvsaa desgalglvl nvlcalgsga epladaertg
      301 lvtvtgqsvt frhplvraaa yriaseaqrv avhsamaral addpdrqtwh raaaatgpde
      361 svaaaleasa lragertgfg taatawersa qltpdpaerg rrllaaveta tnagqfarat
      421 rlghaaaaas csaesrarla gvlahiefeh galasahgrl ragaaavahs dpdraavlll
      481 dagritwaag dlaafracrd llaelppstd rnrflqayda flalyeddpt qgilllrkvv
      541 edpdrhrdra pairfalath aivlgdvdta revlsevaes crlrgqlgwl aaielwlstv
      601 eliggrfrea tvlavegrri gesidqpiri vhaatnlalv aavagdeqrc lelvdtvran
      661 prtasmhhal ldwavaqldm tcgrylsale rlealdhvpl yrqgqwvlay adrveaavra
      721 nqperaapal aalriwsdal eapwaqalll rctallngda daftralelh arqgrwfdra
      781 rtsllfgewl rrerrtaear selrdaleaf erlglpawad rardelraag egavpqanpg
      841 laelltpqel qvtrlaagga tnkeigarlf lspktvghhl srafrklgvs srvelarlel
      901 d
//
LOCUS       WP_181583735             220 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Nocardia
            huaxiensis].
ACCESSION   WP_181583735
VERSION     WP_181583735.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=24066
     Region          2..211
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mwywvlkhil vgpvlrllgr pkmeglhhvp kdgpviiaan hlavvdslyl clvldrpvtf
       61 iakqeyftgg gvrgrinrwv mkatnqvpvd rtggtagsds laaasriler ggiwgihpeg
      121 trspdgriyr grtgvirvam qtgapvipvv lsgtdkvnpr nrrtlrpakv risfghprff
      181 vpadkagvra atddlmfdlv rrsgrpyvdc yaatfkshaa
//
LOCUS       WP_181583811             491 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia huaxiensis].
ACCESSION   WP_181583811
VERSION     WP_181583811.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=54547
     Region          7..447
                     /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 mssaesrrpp gqpriavvga gisgicmaia lqragftdft vyekaadfgg twrdntypgl
       61 vcdvpsryyq ftfamnpews qlystgpeik dylvgvarsh glhgktrfga evkgaefeag
      121 awrvttadgd verfdfvlca tgflhhpnrp diaglrdfag pvvhsarwdh sielsgkrig
      181 vigtgstgtq lvsalagqvp kvvmfqrtaq wilptvnrpy srlakaayrr apalgriayg
      241 fnrtvfeifs qglvhpgrvr rliqwvvarn lrqvrdpqlr rkltpdyqam ckrlvvsdrf
      301 ytavqrpdvq lvtegidrvr aegvvttdgv lheldmlvla tgfdshafmr pmgitgtagr
      361 tldeawaegp rafegvmmpd fpnffmligp hspfanhplt avaeaqaari vgwlqrwqag
      421 efdtvaptra atdrynarmr aaapstvwtt gcqswylgkd glpelwpwtp sryeklirst
      481 pdpvdyeler r
//
LOCUS       WP_181583992             506 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia huaxiensis].
ACCESSION   WP_181583992
VERSION     WP_181583992.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=55767
     Region          12..455
                     /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 msrkvtdkav gnrparhshi vivgsgfsgl gmairltqqg qrdfvvlerg ndvggtwrdn
       61 typgaacdvp shlysysfal npnwsrsfsk qpeiqsyiqg vadkygvrdk hifgcdmtga
      121 rwnaersvwe idtnqgpfta dylisavgal cepnlpdikg intfegeifh sarwdhdsdl
      181 sgkrvavigt gasaiqivpa iakqvahldv yqrtapwllp radrpylgve kfafknipgf
      241 qalsraaiya aretqvvgla kfppamlale avaraklfae irdpelrrkv tpnfrigckr
      301 mlisneyypa ldrenvdvvt dgikeitans vitkdgverp vdaivvatgf hvtdspafet
      361 iagrdgrtla evfdesgqqg ykgsaihnyp nmffllgpnv glghtsmvym iesqinyiad
      421 aidqieakgl ktvevrkdvq defntelqkk lqgtvwstgg caswyldkhg nnttlwpdft
      481 frfrsllekf dvaaydttta vaakas
//
LOCUS       WP_181583358             274 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Nocardia huaxiensis].
ACCESSION   WP_181583358
VERSION     WP_181583358.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 274)
  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 274)
  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 274)
  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 274)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..274
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..274
                     /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=27839
     Region          39..149
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mirlltvaaa vvalslpala paaadpvpal gepaactpap nhpypvvllh gtmddasawn
       61 alaprltaag ycvfapsyga ypsvipvggg vapieqsaat iadyvdrvla vtgaarvdiv
      121 ghsqggtiae yyaknlggas kvrsaillav athgtdllgt velanqvpal gglvnstmlp
      181 sfcpacvdlq rgsafmrtlg agpiaqpgvr ysvlatydds vvtpagaasf idepgvtnlf
      241 vqdlrpgvva hkdmpsnqav mdwvtmrlnt diad
//
LOCUS       WP_181584282             286 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia huaxiensis].
ACCESSION   WP_181584282
VERSION     WP_181584282.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 286)
  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 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   3  (residues 1 to 286)
  AUTHORS   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..286
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..286
                     /product="helix-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=30407
     Region          116..285
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <225..286
                     /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 mvsasdalmr prdtdalrae lrrisamskm pvvfggevqa gtlvlsefvg trtngmrgla
       61 vapssglgga avatgrprsv adyrsastit hhydapvlge glravvavpv vvrgearavl
      121 yvanrdsgpi gdrvademvq agqrlsmeft irdevdrrlr lnsaweaaag akavvteqlr
      181 dlhaelrgit qgvsdaqars rlrdvsdrla rlvsgvaepe dqvalsprel dvlaqvslgc
      241 tnaeaaqrls vraetvksyl rsamtklgah trheavvrar ragllp
//
LOCUS       WP_181584047             612 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nocardia huaxiensis].
ACCESSION   WP_181584047
VERSION     WP_181584047.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 612)
  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..612
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..612
                     /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=64553
     Region          4..>367
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mlsngdvfag yviertlgrg gmgsvylakh prlprmtalk llnremvfdk eirarferea
       61 dlvsgldhhn ivtvydrgle dgqlwismqy idgvdassvn pqalpperav qivaetadal
      121 dyahrnevlh rdvkpanill arstggkger vyltdfgiar lrdetsnltq tgtftatlay
      181 aspeqltgsa ldgrsdqysl actlfwlltg sgpfqatnpa aviqghlqnp pppaanlrpg
      241 lppaldmvia kamakrpedr fascsefaaa arralaapsa pamplvnprt appmpfantg
      301 ganptvgpmt ggptptaapm tggpmqtagp rtagpnptaa pvpyptmvnt atpppqpvag
      361 ftpnrptnqy ttpgynysnp gnatvpppgv ppgmgqagpr ppmpprksnt gliigailgv
      421 lvlaivvvvv vaaagddsgn gsaggttttt vstngsspsn adltwstvsq efprmvpstk
      481 sgedgyngat cwladasspp eadegepdfg nwtvqwrcfg ggnnedpfyr iygydssadv
      541 qsvvsgltsa kkstdtnggn tytnyqftdq srprmvtnft gdsdraqmlm ytdgvvgsid
      601 evlrwwrsap ln
//
LOCUS       WP_181584138             581 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nocardia huaxiensis].
ACCESSION   WP_181584138
VERSION     WP_181584138.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 581)
  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..581
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..581
                     /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=64096
     Region          1..581
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mydtiikngr wfdgtgapsa lrhlgiragr vatvsaqpld etgcarvida agqwvmpgml
       61 dihthydvev lldptlsesl rhgvttvmlg scslstvhvd gadagdlfgr veaiprkhvv
      121 eavdalktwn sahgyvrale slplgpniaa fighsdiraa qmgleratrp devpteselk
      181 amehklseal dagfigmssq qlmfdkldge vcrsrtlpst yatarerrrl nrilrdrkra
      241 lqggpdvarp qsllamaass lglfrpnlkv sllsaadika ipgvvhmfpl iakvlnklgg
      301 dfrwqhlpvp fevysdgidl pvfeefgsga aalhlsnqle erhalladen yrrwfrkdyd
      361 kkwgprvwhr dffdaeitec pdasvigktf gqvgverggv hpvdafldlv veygskvrwr
      421 ttisnhrpev ldrlaadpsv qlgfsdagah lrnmafynfg lrllkrvhna qqagrpfmtv
      481 ehavhrvtge ladwydldag hlrvgdradv vivdparlde sledyaenpi pefdglsrmv
      541 nrnddtvtav lvngeyvfgl geraaalgkt rvgdflragr r
//
LOCUS       WP_181584055              73 aa            linear   BCT 28-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Nocardia huaxiensis].
ACCESSION   WP_181584055
VERSION     WP_181584055.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 73)
  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..73
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..73
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7042
     Region          1..52
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mpsyayrcrs cgdtfeltrp maeasdpaac pqghgdtvkl lttfgtvtrg ggsapvsapa
       61 psgggccggg cca
//
LOCUS       WP_181584627             305 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nocardia huaxiensis].
ACCESSION   WP_181584627
VERSION     WP_181584627.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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 305)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..305
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..305
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32230
     Region          65..304
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mgennrtger afsrrslfas agllgvaaag aaavsasvna apdadtpqrt lhagavdgkt
       61 vlgidatirt erlfsaargr evdvvtilpp tvpldglpms lllhglhgna heaavgglad
      121 vlsvavatrl vpafgfiaid ggdnywhehh sgddpmrmll devpqwlaar rlggpagepf
      181 actgvsmggf galvysrrrn ergraanaia aispglltsw pemskrnafs tpdewaaldp
      241 lrntdklgps pigvwcgdrd kfidgnrrfm ssarleiarv tpgghteeyw rtitpdvvgf
      301 lgrhv
//
LOCUS       WP_181584643             852 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia huaxiensis].
ACCESSION   WP_181584643
VERSION     WP_181584643.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 852)
  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 852)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 852)
  AUTHORS   Rosinski,J.A. 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 852)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..852
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..852
                     /product="helix-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=90233
     Region          6..124
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
     Region          <93..851
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          786..839
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msltwpfagr geelsrirrv lgsggsvvla ggagvgksrl aaeaapgaar vrgseaakal
       61 plgafgallp geavtdnllg wagqlvrkav rgvlvvddah qldavsgalv rqladsgqql
      121 lvtvrsgeac petirslwre gpaerielep lsdadaaevl rrvlggsven aerlislsrg
      181 nmlylrelvn eavtrgeltq qdgvwrwsga aplsgqlrel ittrigaltt aeaevlelva
      241 lgepielnil lagedpqala saeerglvti adeagtevrl thplygevvr aglprlrtmn
      301 ryrrlvelhd tdgrgdqlri alwrleagms sepgpllaal rlawagydyp laerfgwaav
      361 esgagpeaav llapvlgygg kldqaeavla qaweqpcder trtlmistrl nilatlgrae
      421 eaialvetae mllteaenrq elmfwqssih falghfdkal tvvdailadp vsvpmraqav
      481 gqrgwiltfi grtvdaladv eaaldcreqw qdavpvyvra lqgikqiaas fageletaat
      541 avelgetttg egtdwavsea enahargale rqrgrvrtaa rllaiptpgv alsdmqahrw
      601 aelataaala gdvetaeaal aqgaetalev vlgfgvdlar pwiavargef arageialdn
      661 vermrhagai tqavvaghda vrlgcaagva eqlaelamsc qgefsraaad haramvandg
      721 seltavsqrf etlgylllaa daaaqaadvf dragrsasar satararlla dacegvitpa
      781 larldaprlt preleiarla adglpnrdia erlvlsvrtv ennlhiayqk lgvanrselc
      841 allragtadw rg
//
LOCUS       WP_181584318             205 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Nocardia huaxiensis].
ACCESSION   WP_181584318
VERSION     WP_181584318.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 205)
  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..205
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..205
                     /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=22387
     Region          17..194
                     /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 mgfepsrfes apagvdylpp tvtksvkllv agnfgvgktt fvgsvseikp lrteetitha
       61 svgvddmagl rekttttval dfgritlnpq lalylfgtpg qqrfvplwee lalgalgalv
      121 lvdtrrieqs devlavleqr gvpyavavne fegahrypls eirdaldltd etpltaldar
      181 drrtcvqsli tlveflfhsr qesrl
//
LOCUS       WP_181583359             509 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase [Nocardia huaxiensis].
ACCESSION   WP_181583359
VERSION     WP_181583359.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 509)
  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 509)
  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 509)
  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 509)
  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 509)
  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 509)
  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 10261875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..509
                     /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=54730
     Region          28..486
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mtralrtlal pllmpallla pllvpgpavh adpapalpvs vpgvrgwepa agrfdlpggv
       61 rivdggggav vaarfagdlr ragraadvas gaahtgdvvv riddsgpaep esyridigdt
      121 vtatarthag avhatqtllq wfsqtttlpa gtvtdhpdya erglmldvgr efmsvgfikq
      181 riremayyrm nllhlhlsdt ggfrlaslsh peitapqhys raeiaeivsy ageygievvp
      241 eigfpahmna ilaphqdlkl rpastgpadv vsdtllagsa egkidislre srqliedllr
      301 efvplfpgey fhiggdeyvr dfsrypqlsv dmvasffnwa ngivrsygkt armwndgiph
      361 dsavpvdasi lveywtsgdg llpwignqng pqsivdaghp imnsgftpty wasggyaapl
      421 nappealyaw dpglfvngvr lraeqrsalt gsklhvwcdd ptamteeqmv gpirtrlpim
      481 aqqlwsgtgg lltypefteh vrilgvpsa
//
LOCUS       WP_181584781             646 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Nocardia
            huaxiensis].
ACCESSION   WP_181584781
VERSION     WP_181584781.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 646)
  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 646)
  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 646)
  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 646)
  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..646
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..646
                     /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=68162
     Region          73..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 mgfgrerqga grgrsgggra tagrsgagrp gpapvtrarp raaglngamr frfgvgrvvm
       61 lvalllaaaq llwiqtinap rlsadaakqr tmteqdpavr gaitdrfgkl lafttpaqkl
      121 nfqpvqvrka lteahektpn tapepddrlq aiakfmhekl gdavgpekdl laklrsdepf
      181 vylafkvdpr ianeirkkfp evgaeaqdlr dnpggslaan vigtvgwdgh gavgleaamd
      241 svlagtdgsy tydrgsdgav ipgserdrqt aangnsvelt idsdlqyyvq qqvqqakems
      301 garsasavvl dahtgqvlam andntfnpkl gpehwseanl gnpsvsevfe pgsvnkivta
      361 aaaieygltt pdevlqvpgn tfmggvtvnd awphgtvpft ttgvfgkssn vgtlmlaqri
      421 gedryfdmlk kfglgqrtgv glpgesagvv pardqwsgst fanlpigqgl smttlqmtam
      481 yqaiandgvr ipprvvkaei gadgsrkeqq qpdgirvvsa qtaqslrqmf qavvqkdpng
      541 gdqfgtgpqa aisgyqvagk tgtaqkidps crcystdsyw itfagiapad npryvigmml
      601 dnpvrssdgs gggsaaplfh siaswalqrd rvppsppakp lvlqas
//
LOCUS       WP_181584864             314 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nocardia
            huaxiensis].
ACCESSION   WP_181584864
VERSION     WP_181584864.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=33509
     Region          2..314
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mriivagatg aigrplvaal rrnghevlal trggrsaelv ralggtpiia nvleredllr
       61 aadglaadav iheltayrhs ppthyrspgl lrtnalrgtg srnlvefavn vgaaryltqs
      121 livgygirdh gpelvteqeg fgraqgdand pflsalyeae ewawraagid gialrygvfy
      181 gpgasdmfvr alklrmlplp rigtgsigvv hiedaaaatv aalengragq aynivddepv
      241 twealfdama etvgarrplr vparvlrhgs plaaaqmldm slrvsnvkar aelgwkpryp
      301 syreglatla sapr
//
LOCUS       WP_181584705             523 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Nocardia huaxiensis].
ACCESSION   WP_181584705
VERSION     WP_181584705.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=56439
     Region          9..512
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mavesssgls rrtllrasat gllvapalaa cakgdgpglv lnrpalthgv avgdprsdga
       61 liwarsdrpa klivetaate sftgakrfeg pmltpdsdgt grvrlsglpa gqqvhyrvtl
      121 egeggatsea ltgvfrtvpa assditllws gdvvgqgygi npdlggmqif samaardphl
      181 fihsgdsiya dnpvkesvtl adgrvwknit aeaknavaqt ldqfrgnyay nlidehyrkf
      241 naavaqivqw ddhetvnnwy pggqvpaakq gytersmdtl atrswrafhe wmpvepreav
      301 dgrlyrkvsy gpmldvfvld mrtykdande nrspagtilg eaqtrwlmdg lrgsqatwki
      361 vandlplgli vkdgeqkdrt afegvangdp gapsgreaei arvlssirsn rvsgvvwlta
      421 dvhytaahhy speratyqdf defwefvsgp lnagafgpnd ldptfgpeav fvhappvqna
      481 spldaayqhf gevkidgksr eltvnlcdst gnvlftkrla pgr
//
LOCUS       WP_181585015             107 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Nocardia huaxiensis].
ACCESSION   WP_181585015
VERSION     WP_181585015.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=10812
     Region          4..107
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mtllllglai acevtatvsl klsegfskll psvvvvfgyg faffflsqal krgmpvgvay
       61 giwsaigvva vaiigalfld ehvtpvqigg iglviagvla lelggah
//
LOCUS       WP_181585032             345 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardia huaxiensis].
ACCESSION   WP_181585032
VERSION     WP_181585032.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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..345
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..345
                     /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=36376
     Region          99..340
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mptdttglvg yalagsvpvv lvgalllryt rgramttsma vlvliptlat lagvvavsgl
       61 mfgdeferta vvlavvtavt vpaaillgre qaratvwerq mrdkeraaeq srrelvawvs
      121 hdlrtplagi ramaealadg vvdqprdvkr yadgivrdth rlsamvddlf emskinsgal
      181 rlelepldlr elvdevlaan qptalrarit ltaqqpenri mvagndralg rvltnlvvna
      241 iahtppggri dissgitdgh awarvddtgp gvaakdlpri fevayrgssa rspgaaelgs
      301 ssgmglaiaa gliaahsgdi rvenhtagar feitlplppa qqvsa
//
LOCUS       WP_181585140             423 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Nocardia huaxiensis].
ACCESSION   WP_181585140
VERSION     WP_181585140.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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..423
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..423
                     /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=46902
     Region          91..399
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgnqvslmpl giqirgniee rkrskpflar vrwtnpatkr rdsksqafed raeaeawier
       61 iqqaasrgvd pamatatlkd ygdtnwdiam rgveaktldp yragwrrrvv ptlghlpitm
      121 itagiadrav gmwiaeghsk stikntlaal grvmdqavrd evidrnrvdv sgwqrqyarh
      181 edeltnpral alpdwqtlte ladalvsasa nrfrgwgdvv lftactaari gevagcrvgd
      241 idtnswlwtl rrqttpgpgg lkdkgtkgkr artvpiihel rplvvsriam ararvasvpg
      301 yerldeaarr tahanarlfv gprngriqit vlrratnwda vvaelgyehl rrhslrhtgl
      361 twfadagvse hllqdiaghs dprvtklylh pgaaafqqag nllslhlaap krppnghhlr
      421 lvk
//
LOCUS       WP_181585782             363 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardia huaxiensis].
ACCESSION   WP_181585782
VERSION     WP_181585782.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     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=37094
     Region          42..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 mpheisadav dpepardarr asrtalifgg alitlvllam lsagigqvpt sfaevagsif
       61 hkigldwgpm pqhpagyvtl wevrfprvvl amlvgaalat agallqgvfa nplaepgvig
      121 vsagaavgag tvivfggafa aawsvaagaf iaglgttllv yvlarsngrt evvtlvltgv
      181 ainaftagll sfllftaspa ardqivfwql gslngatwqs vyvvaplali gvaaavlmsa
      241 kldllalges aarhlgvdve rlrrnvivvv avlatagvaf tgvilfvgli vphlvrmlvg
      301 pahrvlipls ailgaivlla adigarslvd nadlplgmlt slvggpfffw llrrtrassg
      361 gwa
//
LOCUS       WP_181585774             579 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nocardia huaxiensis].
ACCESSION   WP_181585774
VERSION     WP_181585774.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 579)
  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..579
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..579
                     /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=63670
     Region          2..578
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 msydtiikgg rwfdgtgaas avrhlglrgd rvvtvtaqpl desgcsnvvd aegkwvmpgm
       61 idihthydve vlkapaltes vrhgittvll gscslstvhv dataagdlfg rveaiprrhv
      121 meavaqktwr caheyvaale dlplgpnvaa llghsdirta lmgldratrk rvrptaaeqa
      181 ameaalheal dagfvgmsaq qllfdkldge varsrtlpst yararerrrl nailrqrdrv
      241 lqagpdvtsp rsiaamtlss aavfrrrlkt tllsaadlka npflvhlmgp iarlvnalgg
      301 dfrwqhlpvp fevyadgidl vifeelgaga aalhlsdqve rnalmqdeaf rrrfrkeyda
      361 rfgmrvwhrd ffdaeivacp ddtvigktfg qvgvdrgglh pvdafldlvv ehgtklrwrt
      421 tisnhrprfl dklsaspavq lgfsdagahl rnmafynfgl rflqrvhrae qsgrpflsle
      481 qavhrmtgel adwygldagh lregdradli vvdpahldds ldayaeepip vydnlsrmvn
      541 rndaavsavf iggdrvfgdg epadilgtrr tgrflratn
//
LOCUS       WP_181585897             312 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nocardia huaxiensis].
ACCESSION   WP_181585897
VERSION     WP_181585897.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..312
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32889
     Region          20..308
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mlvvclvgaa gllcvpaqad drrftlsvys aamgreipvd iqraagtsrp rpvlyllnga
       61 dggvgeanwn rrapqaldfl adkdvnvvqp iggftsyyad wrapdpvlgv nkwqtfltee
      121 lppvidevlg angfnaiagl sssgasvlql aiakpglyrs vaaysgcaqi sdplgyafvn
      181 vvvaqgrgnt vnmygpqgdp mwaandpylh adrlrglhly isngsglpgp hdtldgpfal
      241 pgldglanql tvggvleaat dhcgrnlqar lttlgipaty dfhpvgthsw gywldaliss
      301 wptlarglal pe
//
LOCUS       WP_181586457             347 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Paenibacillus taichungensis].
ACCESSION   WP_181586457
VERSION     WP_181586457.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus taichungensis
  ORGANISM  Paenibacillus taichungensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus taichungensis"
                     /db_xref="taxon:484184"
     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=38819
     Region          18..344
                     /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 mydvlvigag qaglaagyyl qrsgltfliv dnvssvgesw rkrydslrlf tprmydglpg
       61 mslignensl pskdeiadyl esyakqmhlp irlnclitrl skqdevyyae tndgiiearn
      121 iivatgpfqt knvphfaksl senviqlhss eyknisqllp gttvvvgggn sgaqiavela
      181 sddkqtvyis iarnitfrpl himkrsifwy feklgvlrsg adrmvgkwlr nqpeyvygye
      241 lkelitkgkv nkrprainak dnrilyedgs eapihniiwa tgfkrndgwi diatafdsrg
      301 eilheagvsp vvglyfvglp wqtsrgsall gwvkydaqki vnhviqr
//
LOCUS       WP_181586719             601 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus taichungensis].
ACCESSION   WP_181586719
VERSION     WP_181586719.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus taichungensis
  ORGANISM  Paenibacillus taichungensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 601)
  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 601)
  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..601
                     /organism="Paenibacillus taichungensis"
                     /db_xref="taxon:484184"
     Protein         1..601
                     /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=68033
     Region          219..601
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mypnryryrl sirgrgmrrn gvtmklflvm agfllllygt tviaqlvwfp dfyqhqkiss
       61 ikkkltkfeq qystghwndv qlaketgkfm rqnqshlvil tntgklvndp fhivllqedg
      121 kqvnislslf insenagwla thlkygqqlt vtgsasgmnd pmvyplkikd qssvvsgted
      181 fqeltepvee wsgtlkevvl pnlgtwsqrq gllvqaldsr fplstedqls langkminee
      241 wtdswsgvrn vltiapvhss gpqqqlifsl tslqemreas eatqlfyayf giaafvlivf
      301 lslllsrivt kpllalnhva kkmstldftv kspirrndei gslsnslnal sttlgqtlee
      361 lrqansqmrt dmemkqrieq rqreffadas helktpisii kgyseglkdg vseskreryi
      421 eiiadeavkm etmveemldl vrlesqaikl ntdavalgdm iediagrlgp qlkekelevv
      481 lvstteqtie gdrskleqvi ynmmmnairh avpktdimie isrpegqvri sienqgeqis
      541 eaerqyiwer fyrversrnr kmggtglgla iakqildlhg csygventpd gvrfyiifpn
      601 a
//
LOCUS       WP_181586780             297 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Paenibacillus
            taichungensis].
ACCESSION   WP_181586780
VERSION     WP_181586780.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus taichungensis
  ORGANISM  Paenibacillus taichungensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus taichungensis"
                     /db_xref="taxon:484184"
     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=32984
     Region          20..287
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 metavvtggt gflgfgllse lvrkgifvyv vvrenskrlk rlhgiegiqi iemdmknisn
       61 lgsyvknidv fyhlaweger ndfsgqmkni gqtveamqva sqlgakqfiv tgsqaeygii
      121 cnekinentp tnpntaygac klacyqilsc lakqigislt wvrvfsvyge gdnpntlisy
      181 lfkcfsdgkt peltsgeqfw dflylndaan alyllgeqkk eglynlasgd nrplkefile
      241 vrevispdsn lifnanlgke vvqlradvgk vqrelnwkpq tcfnegisni ktssfil
//
LOCUS       WP_181586807             136 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: nucleoside 2-deoxyribosyltransferase [Paenibacillus].
ACCESSION   WP_181586807
VERSION     WP_181586807.1
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 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..136
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=15570
     Region          7..126
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 mhknvylsgs iltsgerrkl erlntimeah fltthlphrd ietqsvdsks rdemfkfavk
       61 aieecdmfva vinndlnlsn tcweigyaya hkkpifclhe gefninqwgq lmlmnssvvc
      121 hnveeltgql nltlqk
//
LOCUS       WP_181586075             124 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nocardia huaxiensis].
ACCESSION   WP_181586075
VERSION     WP_181586075.1
KEYWORDS    RefSeq.
SOURCE      Nocardia huaxiensis
  ORGANISM  Nocardia huaxiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 124)
  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..124
                     /organism="Nocardia huaxiensis"
                     /db_xref="taxon:2755382"
     Protein         1..124
                     /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=13953
     Region          1..124
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mdafqhinha rmvtlleear ipwlflddrp tvglksgcvl adlrvqykgq lrhedspldi
       61 smwverlrav dftvgyevra agaapdspaa viastqlaaf didtqrlrrl tteerdylsl
      121 wqda
//
LOCUS       WP_181587178             442 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Streptomyces sp.
            KM273126].
ACCESSION   WP_181587178
VERSION     WP_181587178.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. KM273126
  ORGANISM  Streptomyces sp. KM273126
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. KM273126"
                     /db_xref="taxon:2545247"
     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=45641
     Region          6..431
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mhrhtiavig tgyvgltaga claslghrvv cadldpvkva elgrgdvril eeglpelvqa
       61 gldagrlrfv vgaadavrga rtvficvgtp tgpdgradlt avdavveeir tllepdsvlv
      121 tkstvpvgta arvtaalgrp dvgvvsnpef lregtsvsdf lqpdrvvigs dspwaaaqva
      181 elyagvdapv viadaasaev vkyaancfla vklsyvntla elceevgadi grvttalgqd
      241 hrigsaflrp gpgwggsclp kdtrallgta dalgvdfplv raaigtndhq rtriadriar
      301 lcgdtdgsla gvrigllglt ftagtddlrd spalalaael arrgaeltah dpavpatrht
      361 elpadinvvd dphqaakgas alvlctewph yrgldwaria adlhhpvvvd trnhldpaal
      421 saaglswhgt gtspvepapt av
//
LOCUS       WP_181587196             839 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces sp.
            KM273126].
ACCESSION   WP_181587196
VERSION     WP_181587196.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. KM273126
  ORGANISM  Streptomyces sp. KM273126
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 839)
  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 839)
  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 839)
  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 839)
  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..839
                     /organism="Streptomyces sp. KM273126"
                     /db_xref="taxon:2545247"
     Protein         1..839
                     /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=86794
     Region          34..716
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtkvnefaas tsgnmtvppe sevgarryrv isgcvecasd ltalrrvpgv rdvrvlsatg
       61 tlvveasktl dddvllrtan asglvlepeh aigtdksaaq atkrsrwwlr pemilleiaa
      121 vllifvesfg cyaqyesvae ifayacvavg iiypartavm mlkakrvsin vllvvaviga
      181 laldrateaa cvvvifslgv vlesyvadra rksiqklmdl spamaerfas dgtveqveve
      241 qlkvgdvvlv rpssrlptdg tvvqgaswid asaitgesmp vevepgaevy ggtlnghaal
      301 riqvakpfed tvlarvikev eeaqqnrgqa qrfadkfati ytpimialav lmaafgpqvf
      361 disytdalyr alvvlivscs cslvlsvpvs vvsavaraar dgvlikggay leqlskleav
      421 afdktgtltl grptllqvha ldsldenell tlsaaveaga thpiaeaivr aardrgitvt
      481 pasdvevipg vgaqsvvdga mvvvgrvgdl ssnpaaqaal davedaggtp vavtvdghlv
      541 gllgvadelr pesvtalksl rqvgithttm ltgdrervar aianrvgies vraqlmpdek
      601 stavasikqs gitamvgdgv ndapalatad vaivmgaagt dvalemadva lmaddlnklp
      661 yavalarras rviaqnials lavilflvis avsgrftltq gvlineawal viianglrll
      721 rlhsslraag sitssaskvs svatakpaaa tggsaaaedd cgcgtqssvl plsqieslkv
      781 qsvsgsdggc gcgpgcgtqe petvlpaqvt veadscsadg gcgcssvsvn statsdrrv
//
LOCUS       WP_181587422             435 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Streptomyces sp. KM273126].
ACCESSION   WP_181587422
VERSION     WP_181587422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. KM273126
  ORGANISM  Streptomyces sp. KM273126
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  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 435)
  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 435)
  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 435)
  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 435)
  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..435
                     /organism="Streptomyces sp. KM273126"
                     /db_xref="taxon:2545247"
     Protein         1..435
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45843
     Region          51..>243
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtpstllpap vpaagrlapt pvdtagtgsq lalaedlltl lrtttteprp deqleavtla
       61 vaadlpvllw gepgigktav ltqlatsldl plttviasvh epsdfsglpi vgddpavqgv
      121 pmappqwave lvragrgllf ldelstatpa vqaallrvvl errvgalhlp pgvrivaaan
      181 prasaadgwe lspplanrfv hlywvhdrev vvrglggvwp raelprlepe rlpeavafar
      241 ravcgflqar ptlihrlpst etrrggawps prsweaaltl lafataacvs revlallvrg
      301 avgdgpglel lahldrmdlp dpeslladpv saelpvrgdl rqaaleavva avgarperer
      361 weagwavlvr aletgapdll vapakalaal rrddwevpea verlgavvgl arradqsver
      421 aaasadagra tgtrr
//
LOCUS       WP_181587857             318 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181587857
VERSION     WP_181587857.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=34009
     Region          1..314
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkaftferan tpaeaaasaq rtpeakfiag gtnlldlmkl eietpthlid vnhlgmnhie
       61 pttagglrig alvrnadlaa derirrdyav lsrallagas aqlrnqasta gnllqrtrcp
      121 yfydtnqpcn krqpgsgcaa lhgksrqlav vgtsdaciat hpsdmavamq lldavvetvt
      181 pdgserhipl sdfycspgds pqretvltag elivavtlpp pivgthvyrk irdrasyafa
      241 lvsvaaiiqp dgngrvalgg vahkpwrmne adkriplgtk avyeqlfata hptaeneykl
      301 ilakrtlasv ltqagvtr
//
LOCUS       WP_181587590             262 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181587590
VERSION     WP_181587590.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 fergusonii"
                     /db_xref="taxon:564"
     Protein         1..262
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28714
     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 mkkiiillsl lillpltaas tplipimktl ftdvtgtvpd aeeiahkael frqqtgvapf
       61 ivvlpdinne aslrqngkam lehvsssmsh vkgsvlllft treprlimit ngqvesgldd
      121 khlgllvenh tlaylhadlw yqginnalav lqaqilkqpt ppltyyphpe qlhenappgs
      181 tttlglfawa vafivftaff nyttrlnyal kfavamtian mgyqalclyi ddsfaitris
      241 plwagligvc tfiaalllts kr
//
LOCUS       WP_181587917             327 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Escherichia fergusonii].
ACCESSION   WP_181587917
VERSION     WP_181587917.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=33690
     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 mmrtglvtvi flalllvgcv vypgigarfi apqtvlqafl hfepqnfdhn vivrlrlprl
       61 aaalltgasl gvagallqav irnplgephi lglnagaala vvaasalgla fpigrpllas
      121 tggallflli lllssagrsg ltpmkvtlcg valsafvssi taailildeq tllamrtwla
      181 gdlagqdwat lgtsawfslg gvvlaiylap slnmlalgdr maqglgvsvl rtrtftllai
      241 allcgaavsi agpigfvgll vpqivrrlvs adlrvllpls acvgalllll adiiartlft
      301 phelatgvmt alvgapvfvi matrmfk
//
LOCUS       WP_181588061             249 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181588061
VERSION     WP_181588061.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=27559
     Region          25..248
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqrkifvvta aygyehiqaa ggqkallpvi aksgadgvei rrelftstdl lalaelglai
       61 ehaglqacys apeplfieng dlnpqlpqll qeakdlkslw lkvslghfgr pdqlntlrdw
      121 lassdmalvv endqtpcgrl qpmlrfkeic qqfelpvklt fdmgnwlwvg nspeeaayql
      181 ansvgyihvk aalphkesfr aippdnadsr wlklltmlpa dvargiefpl egadlaavtr
      241 ryvdllrke
//
LOCUS       WP_181588558             384 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Escherichia fergusonii].
ACCESSION   WP_181588558
VERSION     WP_181588558.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=44293
     Region          33..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 mtpqfiisiw mliitfviic vfntnyfkfl dvksknlnye vnglrfflai gvafhhfiys
       61 ymyhsghgwv lrgfdinffl grfgvaiffi isgylfynkv ssktnwkvff ikrylriapm
      121 ailssaicia iaiylddgtf dlskqiwniv ywfdagiynl rmnvssvpna slinagvtwt
      181 lfwewafyfs lpflslfmkk nnrlpviiti iavsyyfipl vnykaacyia lfaagflake
      241 iefksdnyfl iniaplilia imvyagsssl slpmiplcfl ffllcnnnns lfgifrnkgv
      301 trlgeisysi yilhgiawyv lnismestni idpwylfmsg ltlilivimc aftyitierp
      361 cmtlldrkrk tiisktdnqe vkal
//
LOCUS       WP_181588609             217 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Escherichia fergusonii].
ACCESSION   WP_181588609
VERSION     WP_181588609.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23579
     Region          3..187
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mfnckavifd mdgviidseg lwrqaqkgal arwgacvsde ecirltkgkr ldeiaqtwce
       61 ychlhiepal leseirrlit tliagtgeam pgvqdvlsfl rrsgyqlala tsssyqvida
      121 vltklniqhy fsvicsadde nhgkphpavy lsalrelqls aadclvieds lsgfqaaqaa
      181 gintimvsed aqqccfnaas arylsmyell aalavaa
//
LOCUS       WP_181588730             343 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181588730
VERSION     WP_181588730.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=37616
     Region          2..331
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkilvtgats glgrnavqsl lqsgvsvvat grnrevgksl isagaqfval dltevteddc
       61 arlmdgcdav whcaaksspw gdktafwlan vkathtlsqa agrlniprfi histpavyfd
      121 fqhhydlpet wlarsfsshy asskyaaeqa iagavaqypa trfillrprg lfgphdnviv
      181 prlmqqlqqd ggclrlprgg ealldltfvq nvvyamqlat qveglrsgsi ynisnhqpqk
      241 lsvmldallr qqlglsyria tvpwpllslv arglelygkc vnqepvitry sagtlcfdmt
      301 lsaqkaitel gyhprfsmeq giaitgqwlr ehglrehgkn nri
//
LOCUS       WP_181588427             382 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181588427
VERSION     WP_181588427.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 382)
  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..382
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..382
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42124
     Region          1..>192
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrifllllml cgfqafaeql psvtdltgtl tteeqtaltq qlqtleqqnh fqvavlvtpt
       61 tggkdiklaa sqsyglyhwk pvgekrygeg ililvvwper lasmkighgl eemlppeqaa
      121 qivhyhmqpe fkknnlfsgl tqgiegiaqf tyikanlspl dalanhlfan pqrslpclaw
      181 tllmivaivv lwrftthpgp giwmismitp mvwffcfqnd viirrvsvvc fslffaaicw
      241 qrlavvfnic rafpmmlapq nknakvkkqk kapqvresgr nslfvvllii vvgwclvfas
      301 nkdiafisti iglidhfigp itiagivlli ivakftgnlk lgsghksnrk tgnrnahsrs
      361 ssknsfrggg gssggggssg rw
//
LOCUS       WP_181588827             337 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181588827
VERSION     WP_181588827.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 337)
  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 337)
  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 337)
  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..337
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..337
                     /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=38003
     Region          2..331
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkvlvtgats glgrnavefl cqkgisvrat grneamgkll ekmgaefvpa dltelvssqa
       61 kvmlagidtl whcssftspw gtqqafdlan vratrrlgew avawgvrnfi hisspslyfd
      121 yhhhrdiked frphrfanef arskaaseev inmlsqanpq trftilrpqs lfgphdkvfi
      181 prlahmmhhy dsillphggs alvdmtyyen avhamwlasq eacdklpsgr aynitngehr
      241 tlrsivqkli delnidcrir svpypmldmi arsmerlgrk sakepplthy gvsklnfdft
      301 ldmtraqeel gyqpvitlde giektaawlr dhgklpr
//
LOCUS       WP_181588193             517 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Escherichia
            fergusonii].
ACCESSION   WP_181588193
VERSION     WP_181588193.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=56405
     Region          20..499
                     /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 mkikmlaagi altlpfwaca kdvtiiytnd lhahvepykv pwiadgkrdi ggwtnittlv
       61 kqekaknkat wffdagdyft gpyissltkg kaiidimntm pfdavtignh efdhgwdntl
      121 lqlsqakfpi vqgnvfyqns sksfwdkpyt iiekdgvkig viglhgvfaf ndtvsaatrv
      181 gieardeikw lqryidelkg kvdltvalih egvparqssm ggtdvrrald kdiqtasqvk
      241 gldilitgha hvgtpepikv gntlilstds ggidvgklvl dykekphtft vknfelktly
      301 adewkpdpqt kqvidswnkk ldevvqqtva qspvelkray gesaslgnla adallaaagk
      361 ntqlaltnsg girneipaga itmggvistf pfpnelmtme ltgkqlrslm ehgaslsngv
      421 lqvskglemk ydsskpvgqr visltlngkp iedatvyhia tqsfladggd gftaftegka
      481 rnttggyyvy havvdyfkag ntitdeqing mrvkdik
//
LOCUS       WP_181588830             530 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181588830
VERSION     WP_181588830.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 530)
  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 530)
  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..530
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..530
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=57921
     Region          61..387
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          345..528
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mrvnkiyiis icgvllsgcs ssvrspqaee rwhyvtmsay apspvqqgql qqntarythh
       61 eanpikqtaq eplatfsldv dtgsyanvrr flktgslpga dvvrveelvn yfplteatkk
      121 nipgckgcee nspfsinyel tpapwnekht llrldisand iarsklppan lvflidtsgs
      181 mnsderlpli ksslkllvne lrdqdrisiv tyagsarlll sstsgseknt ilnaianlqa
      241 gggtnggagv amayeqaqag yikggvnril latdgdfnig ddpssvedlv kkqresgitl
      301 stlgvgdnny neammvkiad tgngnysyld slseaqkvls nemnqtlvtv akdvkaqief
      361 npqqvieyrq igyekrqlra eefnndavda gdigagkhvt vlfeltlagq qasvdklryg
      421 kspastqtsn snelmwvklr ykvpqgessr lvempimssa vtrdfsrasp dmhflsavaa
      481 ygqklrgsey lnktswqqiq swaqegkgad qygyraefiq lvglaeslsr
//
LOCUS       WP_181588837             345 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Escherichia fergusonii].
ACCESSION   WP_181588837
VERSION     WP_181588837.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=36355
     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 mnvglrplrv gkfstlvrpk nlvllgglfl favgilifgl mqgsfsvpas evgralfape
       61 nvstdaryiv qdirlprvim allcgamlgm agaamqsiar ngladpglig vkegcsvavl
      121 wlifqfpklg mfwrpvagla ggllvalivi fcardisrpr fvligigvsw ffaagigvfm
      181 ttadvrdvqt almwlsgslh aanwmlvgis acwmlpaall llftartadi allghqvatg
      241 lgvnssrlal lrvaapiilt avcvscvgni gfvgliaphi srfilrggqt tlllgsavsg
      301 allviladsi grlaflplql pagiiislig gpffllllwq rrnsf
//
LOCUS       WP_181589572             373 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactiplantibacillus
            plantarum].
ACCESSION   WP_181589572
VERSION     WP_181589572.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
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="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     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=43219
     Region          59..357
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msvtklnngk wqarvsykdd dgnyksvthl ekrktdavew etktknalle gadlsrstes
       61 lkhyfldwir iyktdgvsrh thelymgnwr hisayfkdqp msaikrpdyq kflnefgrsh
      121 giatshklhq qvhtaikdav adgilkrdfa ykahvtgrpp kpveekyltl sdykklrkyl
      181 iktadydhmt mlmmlfqlet gtrfeeaagl twdnldlnng ivhikqqwda rrqtfrptkg
      241 ngqadgditi gpaycrfmrg yrsaqkdyle lhemknpknl vfwsklgkiv gngnaneelg
      301 ricnrlkink vtthamrhth asililnhes lpyvqhrlrh qklettvnty vhlieeengv
      361 sdkkatelmd egf
//
LOCUS       WP_181589599             602 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Lactiplantibacillus
            plantarum].
ACCESSION   WP_181589599
VERSION     WP_181589599.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..602
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..602
                     /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=66047
     Region          269..556
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mistitldty kqqissgdaf nlsdsfngrv gdeqvplvvq fkerglaqqf qdrlvpfltg
       61 fvgsldendq vtaetgeavs yvgtsddivg lgrvkmnlpg tifpqegyfy gflglqnadg
      121 krvttfnvwf hvyngnpdmf vnkapfrtel qklldesdql isktdgniqa kliewqnain
      181 klitdgntnl daykqrvsla edqitalaak ikadglltqa dfdaaiqple dllvgkvnid
      241 esldiggkls rswetqvddf iaklpadgfk laivsdshye dlydesspys yqytadafkh
      301 lnafnrlgna vnvmiadgdn vngldgdvqh siadgtvyat kllqtsmtad kyvmlgnhdd
      361 nspqlrlgnl lptdvitddq fkkmyqtddl ingenrsdgs lyfykdyadk kvrviglnsf
      421 dvpegvtnad gtvkypryli snysqnqvnw lanvalnnip anyqivvvth aplpygyslt
      481 devkmynqtv vkglldavat gtsysgksdd gtpaecqvsi aadfssqgar pivgffgghv
      541 hkeiikpldh ftscvvlada nidqanvgti nelgvtvvti dtvnrkvmln glgratdrqf
      601 ty
//
LOCUS       WP_181589884             828 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF2345 domain-containing protein [Klebsiella pneumoniae].
ACCESSION   WP_181589884
VERSION     WP_181589884.1
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 10008437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..828
                     /product="DUF2345 domain-containing protein"
                     /calculated_mol_wt=91105
     Region          1..828
                     /region_name="COG4253"
                     /note="Uncharacterized conserved protein, DUF2345 family
                     [Function unknown]"
                     /db_xref="CDD:443395"
ORIGIN      
        1 mdtssiitgt tlnryqldip sctasldvee fsgaeklsel yyytitftsa eknidaaqll
       61 skpamltmgg galqqladck rvhgvvtafr risssedqsk yqitlepfls lldkqfrshr
      121 ffvnksvpev veqvlqehhl hdweyefnlk qhyprreqin qyqesdlafi qrmlaevgif
      181 yfftlqeeaq sevvhfsdaq ralmfdktlp vnspsgmsds gtesiwglni thnvveanvt
      241 trdynprdaq svlqsatadm trgngegity gevyhyklrh rergdkidpq tetanfyarl
      301 dherflahqt litaistaaw lapaqvltvt dslpstlpap vqdplliigt gftasrreal
      361 rvsllavpys etlcwrppll prpnvtgtmt arvtsakand iyawqdasgl yrvkfdpdre
      421 ekgqgqesmp vrlakpyggd vygfhfpliq gtevaiafhe gdpdrpyiah alhdsrhvdp
      481 vteknstrnv irtptnnklr medkrgeehi klsteyggkt qlnlrhnvna qrelrgegae
      541 lrtdkwvsir ggagvfisad kqpsagdrml ameeaiaqle nalgiaksla saaesaqalp
      601 sdtgnqqtln dalkelaqpg ivlnapqgvs isspqavrls sgsasvgivs qqntdisalk
      661 rftvaageav sllarkagmk lfaakgkiei qaqddaleat akkditvtsv egrveitaae
      721 elvvncagay irlsggniel gcpgnillks anvqkmgkad frvpplelpk gfeerftvkd
      781 qktgeivpfa ryrittekgq vfegradadg ktasvytalp esikiell
//
LOCUS       WP_181589993             255 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Klebsiella pneumoniae].
ACCESSION   WP_181589993
VERSION     WP_181589993.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 255)
  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 255)
  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 255)
  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 255)
  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 255)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..255
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..255
                     /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=28560
     Region          1..252
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          16..111
                     /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 mrnvkidevd rldrdvvalg ndyaqgfilp phqhrraqll ygatglmyvt tqdgewvvpp
       61 qhavwippet vhavrfagvt trslyiepdc vaafikhrrc evisvspllr qllleavdlp
      121 plydsprdrt liqlmllela ampvrefdip lpqhpallal cqafllnpsi hdpaarwara
      181 lfmspstfrr hflkqlglsf sawrqracvv salawliagk pvnevalslg ydnassfatm
      241 frrvtgqpps lyhpa
//
LOCUS       WP_181590058             400 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Lactiplantibacillus
            plantarum].
ACCESSION   WP_181590058
VERSION     WP_181590058.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
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="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     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=45810
     Region          76..383
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mprqwkplkr hpgiyeyetk rgkkygirrs ytdinhkyrt wsksgfmtwr dadielkkfe
       61 vtlgtgqita sisdtitlqa yfdkvlkrni dlklwrpati tqkknywnnq lkpvfgnqki
      121 neitrqsyqn fidqmikdgy akntiittns vmqilmndaa rndvivknkl sgisidggks
      181 pssktitekq ynqlmavaps vlskyqycml alltlgerre elmglqfssf kfsqwndeev
      241 caiqfkkgrt naepdggdlk nnssyrtiyv rgemlnichy aitysqniys kthrnindes
      301 flfvnektgm pmgvqqankv lnkvgeaavi hitphifrhy fatmaltngq vatdvmhwlg
      361 hsslqmtqsy trenvrgaln vfngmaptll gdsddehqsl
//
LOCUS       WP_181590063             248 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Lactiplantibacillus plantarum].
ACCESSION   WP_181590063
VERSION     WP_181590063.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
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="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     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=28479
     Region          1..232
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mikvyicedd tkqlqtlqql vskviidrql dmgfgltsad pheilahvks qqptqavfll
       61 dialnsding iqlasqirdl girskiifvt thtelsltvf qyqvealdfi lkdfpdrlye
      121 rlntvlrvaq erfkaedndq nsyiqikige tirsldvqhv lffessmsph kiivhlddge
      181 leyygllkdv pdlnsdfyrc hksyvvnltr irsldkryrq ltmangetvl csvaasrylv
      241 rqigknnr
//
LOCUS       WP_181590282             193 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Klebsiella pneumoniae].
ACCESSION   WP_181590282
VERSION     WP_181590282.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=20865
     Region          2..185
                     /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 mttlylasgs prrqelltql glaferlvpg ieeqrqpqes aqhyvvrlar kkaqagvama
       61 trdlpvlgad tivilngevl ekprdaehaa amlrllsght hqvmtavala dkqqtldclv
      121 vtevtfrrls eqdiadyvas gepldkagay giqglggcfv rkingsyhav vglplvetye
      181 llsnfnslrk gkg
//
LOCUS       WP_181590385             551 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Klebsiella pneumoniae].
ACCESSION   WP_181590385
VERSION     WP_181590385.1
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=58205
     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 givlvmtfsi fpvvyfavsr sllasgtrla vvarvhgasa
      181 wrafwhvtlp mlspalaagm llaftlaiee fgvpaalgsr agvvmltvgi ekkladwpvd
      241 lpgaallsll lmavalfaww lqrrlvgeke vtsvtgkpge nhgaslgwmm lpavlamaav
      301 gglavgvpav smmltsvmgt lsggvsvenv tlrhfaalfd qqgdalsalg tslslalgsa
      361 livgalglla awlvmvqkik grgmvdalsl mpaalpgvvv gvglillwnq pfwprspynt
      421 lwmlllsycc lllpwpvryv gsalrqlgpn leptarvhga splqalrliv lplvfpalla
      481 amlmvfavas relvtsllls pagtqtvavf iwrqfeqgsv gqgmamaslt lltglvlmlt
      541 alalmqrrtr g
//
LOCUS       WP_181590047             224 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Lactiplantibacillus plantarum].
ACCESSION   WP_181590047
VERSION     WP_181590047.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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..224
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..224
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25268
     Region          <23..199
                     /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          32..62
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(69,72..73,76..77,79,102,105..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          69..95
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          100..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 maktsrpska kqqalvhqli gkidaqpedy hayyelvvll tagqdfeqae alamkalgkf
       61 dhqqpaadyl ryalgnvyyq aqtydkalpy yqqitddqlk qdaylmsaqa lmaqhdyqhg
      121 lvwaitaqea rpqqldanll vadillalgn nqqasdyyqr aykidsqsgr aafnlgltam
      181 vlgkpyatwf eraqkldsqy fkshqqqltd iekmlaaqad nqnh
//
LOCUS       WP_181588787             790 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Escherichia
            fergusonii].
ACCESSION   WP_181588787
VERSION     WP_181588787.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 fergusonii"
                     /db_xref="taxon:564"
     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=89451
     Region          39..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 lcgadlavaa ednekytpff eqmtvyapvp vpvngnthyt sesierlptg
       61 ngnisdllrt npavrmdttq stslnqgdir pekisihgas pyqnaylidg vsatnnlnpa
      121 nesdssnatn isgmsqgyyl dislldnvtv ydsfvpvefg hfnggvidak ikrfnaddns
      181 iklgyrttrs dwmtshidek nknawnqgss gstyyspefk knfyslsfnq eltdnfgvta
      241 gfsrrqsdit radyvsnngi vegraqyknl idtalskfsw fasgtithdl tfkytesrrd
      301 yntstfpesd remgnksygv awdmdyqlak aklhttlgwd hisdytrhdh diwytedvct
      361 ygdirgrctr gglghisqai dnytfktrld wqkieignft hqpyfgaeyi ysdawtqrhn
      421 qsesyqikss giktnhtiyh kgkgslgidn ytlyladrms wknislmpgl rydydtylkn
      481 tnisprfmte wdifadrssl itagynryyg gnildmglrd irnswtesls gnktltryed
      541 lktpyndela lglqqkitdn viaranyvyr sahdqiskts htdsatktti teynndgttk
      601 thsfnlsfel aeplqvsqfa inpqivfsyi kskgnlrlns gyeetntgdn kvvyngnlvs
      661 ydsvpvadfn nplkislnmd fthqpsglvw antltwqdar kariqlgktn sqyqsqyady
      721 kqyvdeklds slnwdtrisw tpqflkaqnl tfsadilnvl dsktavdlst agvstyasgr
      781 qfwldvsmkf
//
LOCUS       WP_181590771             228 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia
            fergusonii].
ACCESSION   WP_181590771
VERSION     WP_181590771.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 228)
  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..228
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=26088
     Region          <136..195
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mgldiklknl mcsscslhca mmpeksprqe ycanacfctw pedslyfnrg iidgivnknh
       61 narlngyifv dfsvsffrlf ldnewinyla sssmgivlvt drnmqplany wrknhpavsa
      121 viyhnesmnv anekirqlfi grflsfakgs tltkmefkim gsmirgsdpq diaqdldldi
      181 rsvyaykqri ekrmgrklns lfidshpvtr eqpsplptek rkaelvla
//
LOCUS       WP_181590356             297 aa            linear   BCT 28-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Klebsiella
            pneumoniae].
ACCESSION   WP_181590356
VERSION     WP_181590356.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 297)
  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 297)
  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 297)
  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..297
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..297
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=33266
     Region          40..296
                     /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 mrklivvasv aaslllgcdq kstgkretls ealvakslsn mvpvqggefl mgdfgplvge
       61 klpfsinqdd kvlhkvvlsd fsiskfkvtn ddynkylqit gikkppinil vkeypslqkd
      121 dysvgvtwqq akdycqwlgk esdknidlpt eaqweyaars rgqylpfstn ngnfelgsni
      181 peqkkldeyt dgygfpiypi gkyppnplgl ydmglsgaew sndwystnyy shspvydpqg
      241 pvkgnekvlr gyvggdrqya ltifrqssqp vpkfagrddy qkfgvsplfv frcvink
//
LOCUS       WP_181589971             261 aa            linear   BCT 28-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Klebsiella pneumoniae].
ACCESSION   WP_181589971
VERSION     WP_181589971.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..261
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28444
     Region          46..244
                     /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 makdsklvyg asgktnvlaf epeklhlvtd kthplyderi hlpiseamvl nimdqgvlep
       61 iivwkdpetg lscvvdgrqr vrhtleankr lskagkepll vpgvpkrgsa irmaqamvsa
      121 neirqadtpl grakkmadal erghdeddla lmfgvsvqtv ratlslldat qavrdavesg
      181 tvtvtqarql galppeeqri kvaeielata gtkghekarr qrqilgeakp riksrkeiak
      241 aledasgeya ealrwvlgea q
//
LOCUS       WP_181591488             790 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Escherichia
            fergusonii].
ACCESSION   WP_181591488
VERSION     WP_181591488.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 fergusonii"
                     /db_xref="taxon:564"
     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=89527
     Region          39..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 lcgadlavaa ednekytpff eqmtvyapvp vpvngnthyt sesierlptg
       61 ngnisdllrt npavrmdttq stslnqgdir pekisihgas pyqnaylidg vsatnnlnpa
      121 nesdssnatn isgmsqgyyl dislldnvtv ydsfvpvefg hfnggvidak ikrfnaddns
      181 iklgyrttrs dwmtshidek nknawnqgss gstyyspefk knfyslsfnq eltdnfgvta
      241 gfsrrqsdit radyvsnngi vegraqyknl idtalskfsw fasdtithdl tfkytesrrd
      301 yntstfpesd remgnksygv awdmdyqlak aklhttlgwd hisdytrhdh diwytedvct
      361 ygdirgrctr gglghisqai dnytfktrld wqkieignft hqpyfgaeyi ysdawtqrhn
      421 qsesyqikss giktnhtiyh kgkgslgidn ytlyladrms wknislmpgl rydydtylkn
      481 tnisprfmte wdifadrssl itagynryyg gnildmglrd irnswtesls gnktltryed
      541 lktpyndela mglqqkitdn viaranyvyr sahdqiskts htdsatktti teynndgttk
      601 thsfnlsfel aeplqvsqfa inpqivfsyi kskgnlrlns gyeetntgdn kvvyngnlvs
      661 ydsvpvadfn nplkislnmd fthqpsglvw antltwqdar kariqlgktn sqyqsqyady
      721 kqyvdeklds slnwdtrisw tpqflkaqnl tfsadilnvl dsktavdlst agvstyasgr
      781 qfwldvsmkf
//
LOCUS       WP_181591225             282 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181591225
VERSION     WP_181591225.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=31507
     Region          1..218
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktglstway fwqlsekapk plslfdaidd sqrlgatvfq icdypqiaqw ssgertrlae
       61 haaragitle lgtkgikpdh lqrylaiate lecsllrtmi nspdhrptls earcsvetvl
      121 pafeqqgvai cletyeqvpt ddnialvqai nsarfgicld panciaslel paevvaktas
      181 yvlnwhvkdf afsrrdgwvg ftlagcplge gllryddiyq qiqpqtrgin qiiehwlpwq
      241 gdsettcrle atwtennmry lldkqnlina sstqskesdh vc
//
LOCUS       WP_181591489             928 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia fergusonii].
ACCESSION   WP_181591489
VERSION     WP_181591489.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 928)
  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..928
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..928
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=104633
     Region          23..444
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          517..928
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrklcylltf vatllliper liaaplpqde klitgqlqng lkymiyphaq pkdqvnlwlq
       61 ihtgslqeed nergvahfve hmmfngtktw pgnkvietfe smglrfgrdv naytsydetv
      121 yqvslpttqk enlqkvmsif sewsaeatfd ekevaaergv iteewrahqd akwrtsqarr
      181 pfllantrnl drepiglmdt vatvtpqqlr afyqrwyqpd nmtfiivgdi dskealalin
      241 nhlgklpatk saqnrvwptt aennlrfnii ndkenrvngi alyyrlpltq vtdeqsfieq
      301 aelsmliqlf nqrlleriqs gklkhisggt arsvkiapdy qslffrinar ddnmqdaana
      361 lmtelatidk ygfsteeled lkatrltwlk naadqqderd lrmltsrias sslnntpfls
      421 pqqtyqlser lwaqitvesl aqkwqqlrkn qdafweqmvn sdaaatkals pqaikqlekt
      481 yadkklppyv fpginltltv adnaqakith qekladdlts ltlsngarvv vaktasneek
      541 lqiiavsdkg dlsfpaeqka iialankavs gsgvgqlsas slkrwsaena vtmstnvsgq
      601 ntllsvnarv nnpepgfqll nqrisnskin dniwdsmkna qiqslktldq rpaekfaqqm
      661 yearyaddra qrltekqlaq fsaeqalavd rqlfsspadl tfvivgnide etllplvtry
      721 igslkqsehv lsagqplkra ttnanitlke qnepvaqvaq wkrfdtrspv tlpvrmalda
      781 fnavlakdlr vnireqasgv ysvssrlsvd kqandlthvi gftcqperhq elltlankvm
      841 adrlvkgina qelneyrknm qrnleiqqqn tqqlantivs slvqyndpaa wteqekllqq
      901 ltpeqvnnta rkylssavni ysgvllpk
//
LOCUS       WP_181591645             459 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Klebsiella pneumoniae].
ACCESSION   WP_181591645
VERSION     WP_181591645.1
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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..459
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49885
     Region          3..452
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mserrsidyi peserhghpf sqftlwfggn lqitaivtga lavvlggdvv wslvgllvgq
       61 mlgaavmslh alqgprlglp qmilsraqfg vfgavvplvl vcvmyigfsa sgtvlagqam
      121 akllnishva gmlifsaiii viavlgykvi hklgklasiv gilafvymfi tlllsadlsa
      181 lahnnhfslp tfllavslss swqiafcpyv sdysrylprd vsatktwcsv ffgtvlgtqt
      241 smtlgvltaa iagsafpghe vsylvglgks qamamviyfa icfgkitftt lnaygsfmsl
      301 ttivsafrrq tvlsqkcria fvvlmvtasc iiallsepaf lkhfthfllf llaffvpwsa
      361 icltdyylis kgaidipals dpqqrygvwn lyaitlyivg vliqlpfien plfhgsltwi
      421 fagndvswii gwfgtgvlyy alrrfdrrsl paqslfpst
//
LOCUS       WP_181591786             408 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA-guided endonuclease InsQ/TnpB family protein
            [Enterobacteriaceae].
ACCESSION   WP_181591786
VERSION     WP_181591786.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=45742
     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 krcfdkklaa kapvfkrksh gndsvrfvnf
      121 dkycqleyrr vklpsglgwv tfrqsrdivg kiknatvsqh agswyisfqv emevdqpahp
      181 stsavgldag vsklatlsdg tvfepvnsfk qnqsrlarlq rqlarkvkfs anwkkqkari
      241 srlhshiani rrdylhkvtt tvsknhamiv iedlkvsnms ksaagtvdep grnvasksgl
      301 nraildqgwy emrrqleykq rwrggevlav npaytsqkca ccghtakenr qsqakfvctv
      361 cgyeanadan garnilaagh avlacggkvq sdhptkqepd tersavth
//
LOCUS       WP_181591722             325 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Klebsiella pneumoniae].
ACCESSION   WP_181591722
VERSION     WP_181591722.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=35514
     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 mtrtnlitgf lgsgkttsil hllaqkpade kwavlvnefg evgidgalla dsgallkeip
       61 ggcmccvngl pmqvglntll rqgkpdrlli eptglghpkq ildiltaavy epwidlratl
      121 cildprqlld eravsndnfr dqlaaadiiv anksdretae saraladwwq rwggerrkvs
      181 aiqgnidlal ldeprrntap lpagaehahr hpptsglaal slaehqrwrr hlnngqgyqg
      241 cgwifdaetv fdtigllewa rlapvgrvkg vmriaegavr inrqgedlhi etlsvappds
      301 rielisanea dwnalqtsll rlrls
//
LOCUS       WP_181591177             382 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181591177
VERSION     WP_181591177.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 382)
  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..382
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..382
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42008
     Region          1..>192
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrifllllml cgfqvfaeql psvtdltgtl tteeqtalnq qlqaleqqnh fqvavlvtpt
       61 tggkdiklaa sqsyglyhwk pvgekrygeg ililvvwpeg lasmkighgl kemlppeqaa
      121 qivhyhmqpe fkknnlfsgl tqgiegiaqf tyikanlspl dalanhlfan pqrslpclaw
      181 tllmivaivv lwrftthpgp giwmismitp mvwffcfqdd viirrvsvvc fslffaaicw
      241 qrlavvfnic rafpmmlapq nknakvkkqk kapqvresgr nslfvvllii vvgwclvfas
      301 nkdiafisti iglidhfigp itiagivlli ivakftgnlk lgsghksnkk tgnrnahsrs
      361 ssknsfrggg gssggggssg rw
//
LOCUS       WP_181592250             259 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Mesorhizobium atlanticum].
ACCESSION   WP_181592250
VERSION     WP_181592250.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium atlanticum
  ORGANISM  Mesorhizobium atlanticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 259)
  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 259)
  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..259
                     /organism="Mesorhizobium atlanticum"
                     /db_xref="taxon:2233532"
     Protein         1..259
                     /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=28048
     Region          178..257
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mapvsrhpas vlavvrryea agfrawpaaa vhydgtwvvr ltaghpakrl nsvnpldpgd
       61 thaieerigr aarrfdaygr pltfrmspls gqvlsthldk agwnrfgesi vmrlplkdle
      121 lgaamdqipl kdisrfigas lrtggsdasl rpglseviga iqpeaglfal edgneplatl
      181 icvhdgdlag lfevateksa rkqghgrnli lsalkwarlr gareawlqve agnapalsly
      241 gslgfeevyr yhyrrppga
//
LOCUS       WP_181590413            1037 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_181590413
VERSION     WP_181590413.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1037)
  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 1037)
  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 1037)
  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 1037)
  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..1037
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..1037
                     /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=114835
     Region          25..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkkllcsv cflfafmsal wgqnitvkgn vtsktdgqpi igasvvetta ttngtitdfd
       61 gnftlsvpan stlkityigy kpvtvkaaai vnvlleedtq mvdevvvtgy ttqrkadltg
      121 avsvvkvdei qkqgennpvk alqgrvpgmn itadgnpsgs atvrirgigt lnnndplyii
      181 dgvptkagmh elngndiesi qvlkdaasas iygsraangv iivttkqgkk gqikinfdas
      241 vsasmyqskm nvlnteqygr amwqayvndg enpngnalgy aynwgynadg npvlygmtls
      301 kyldskntmp vadtdwfdei trtgviqqyn lsvsngsekg ssffslgyyk nlgvikdtdf
      361 drfsarmnsd ykliddilti gqhftlnrts evqapggiie taldipsaip vyasdgswgg
      421 pvggwpdrrn pravleynkd nrytywrmfg dayvnltpfk gfnlrstfgl dyankqaryf
      481 typyqegtqt nngksaveak qehwtkwmwn aiatyqlevg khrgdvmlgm elnreddshf
      541 sgykedfsil tpdymwpdag sgtaqaygag egyslvsffg kmnysyadry llsltlrrdg
      601 ssrfgknhry atfpsvslgw ritqenfmke ltwlddlklr aswgqtgnqe isnlarytiy
      661 apnygttdsf ggqsygtayd itgsngggvl psgfkrnqig ndnikwettt qtnvgidfsl
      721 fkqslygsle yyykkttdil temagvgvlg eggsrwinsg amknqgfefn lgyrnktafg
      781 ltydlngnis tyrneilelp etvaangkfg gngvksvvgh tygaqvgyia dgifksqdev
      841 dnhatqegaa vgriryrdid hngviderdq nwiydptpsf syglniyley knfdltmfwq
      901 gvqgvdiisd vkkksdfwsa snvgflnkgt rllnawsptn pnsdipaltr sdtnneqrvs
      961 tyfvengsfl klrniqlgyt vpaviskkmr mdrlrfycsa qnlltikskn ftgedpenpn
     1021 fsypipvnit fglnigf
//
LOCUS       WP_181591980             295 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Mesorhizobium atlanticum].
ACCESSION   WP_181591980
VERSION     WP_181591980.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium atlanticum
  ORGANISM  Mesorhizobium atlanticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
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="Mesorhizobium atlanticum"
                     /db_xref="taxon:2233532"
     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=33591
     Region          3..293
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mqkaidahfh iwrqkdqpwl vgpmvprifg pyepirrdyp itefledqkg sgvekavyvq
       61 tnwakedfek evaflqktad eigwphaivg yadmtvddvr pqidrlmkyk llrgvrmqlh
      121 whetpafrfa asadqvidpk vrknvarlkd yglsfdlqlf paqmkdgltl vgenpetnfi
      181 lthagmltgm epetteawkt glrtlaaapn fyaklsglgt fvhrndpeli ayivdntiei
      241 lgsdrlmfgs nfpieklwts haelikahra avarhgakae adifwntaer vyrpv
//
LOCUS       WP_181592039             406 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Mesorhizobium atlanticum].
ACCESSION   WP_181592039
VERSION     WP_181592039.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium atlanticum
  ORGANISM  Mesorhizobium atlanticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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..406
                     /organism="Mesorhizobium atlanticum"
                     /db_xref="taxon:2233532"
     Protein         1..406
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45999
     Region          6..202
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 maarqkptvt vivptfnrek flpeaidsll rqtvapdqil ivddgstdgt gtvassfpap
       61 veyyrkengg kstalnfalk hckgdfvwif ddddvahpta lerflaafer epeadfafge
      121 yarfqrsaqi eeqnyeivaf ghvsqdnffp shleychvhq pgllvrrecy eevggfnetl
      181 vrsqdyemml rlarrfkgvr vdglmffqrq hdmvrgstkv visyanrika wgsydraime
      241 eiyrsvdlhe yldrseqalp rtadlemqal lqrssimark glwhhaaedi rryallaera
      301 gktslsdker aivrrtfeay dtglssapad efvsavkawk sgplkadivr eymhsfphyl
      361 ardlkagkvi paskllreys tlsfsalvsr lcqamtsklp sarsas
//
LOCUS       WP_181592465             232 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Rhizobium tropici].
ACCESSION   WP_181592465
VERSION     WP_181592465.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium tropici
  ORGANISM  Rhizobium tropici
            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 tropici"
                     /db_xref="taxon:398"
     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=25497
     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 mtvtepppms rtaaisyaig lsiallalif lpvgrldwtp gwifilffft vygvavlvlk
       61 rvnpaifrar nrfqagtkrw dvilvslicl glvaeipvat ldsgrmswsa mpisvvilgy
      121 illgagialg twaqavnrff epgvrlqrer gqrvistgpy afvrhpgyvs aimvfaglal
      181 alaswwalip aawatallil rtswedallh aelegyadya rrvrfrlapg lw
//
LOCUS       WP_181592906             368 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Paenibacillus sp. YN15].
ACCESSION   WP_181592906
VERSION     WP_181592906.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. YN15
  ORGANISM  Paenibacillus sp. YN15
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 368)
  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 368)
  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 368)
  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 368)
  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..368
                     /organism="Paenibacillus sp. YN15"
                     /db_xref="taxon:1742774"
     Protein         1..368
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40684
     Region          247..367
                     /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 mklaksllal lllgalaagc ggkgengesr ganteletiq ngvvlyydds aqsqsllgal
       61 telsktekfd lvtidttkdk skldkyekdn qklvdsykev rsleaglskl klvgnanskd
      121 qqnnvmlnyr kalnlvkngk lnaeqekeld glvkdiagkq elseadlkkl ldlqkdprlk
      181 vpvyssvdgd aapeklpvmk viyegnhrts yyfgqkpipa etlanaenlr fylkekawis
      241 nfqdssdgpt iekklenkdt fvllvwgnsc phchkvmpvl dkltsqtgik veridtfies
      301 nnkayakmaa sgkyglteik wvptlvyikd gkqqatigvy dwavenaasd lgydideski
      361 kafmekak
//
LOCUS       WP_181591661             732 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Klebsiella pneumoniae].
ACCESSION   WP_181591661
VERSION     WP_181591661.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae 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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=79149
     Region          78..732
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mhtthyssfp lrktllalai gaasqtvmaa daaaakqpge etliveanet sdfksggdlv
       61 vpafldgqia hggrlgmlge qkamdvpfnv igytskliqd qqaktiadvv sndagvqavq
      121 gygnfaetyr irgfkldgdd mtmgglagvv prqvmdtqml erveifkgan sllngaassg
      181 vggminlepk raedlptarv gvdytsdsqv ggtldlgrrf gdnnqfgarv nlvhregega
      241 idndkrrttl aslgldyrgd rfrssldfgy qkktfhggtm gvnisgvdfv palpdnskny
      301 sqkwgysdie sefgmakaey dltdswtvys alggqhshei gtysapklln kngdatvgrl
      361 dtnriidais gmggvrgdfn tgaishkvnl gyaaqvhtda tawrmsarnp ttniydnhdv
      421 ampdnayfgg nyhdplvtsr srtqgwllsd tlgffndkvl ftaaarhqkv vvrnysnatg
      481 ledtssrytq srwmptfglv ykpweqlsly anhtealqpg svapttaana gqstgiahsk
      541 qdevgvkidy gtiggslalf eikkpnaisd tagnygldge qrnrgvemnv fgepmlglrl
      601 nastvwldak qtktaegatd gkdaigvanf yavlgaeydi kpvegltata rvnhsgsqya
      661 daantkklds yttldlglry rmrlnadqne miwrvgvtnv tnekywsgie dtgtylfegd
      721 prtvrvsmsy df
//
LOCUS       WP_181592985             345 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            YN15].
ACCESSION   WP_181592985
VERSION     WP_181592985.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. YN15
  ORGANISM  Paenibacillus sp. YN15
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (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
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 345)
  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..345
                     /organism="Paenibacillus sp. YN15"
                     /db_xref="taxon:1742774"
     Protein         1..345
                     /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=39063
     Region          75..324
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          238..321
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 meigleaehf davyeglkgy csssgeqlhp edavfllpdq vgkgylkqtk lrhgmalsws
       61 rmqliepvvm dvgvryphme lsftlegdgs wsrhgttrey glsggtgnlm ymhnegfhae
      121 qyagkpidhm evridfalwr hllsplpwqa eesfycrpcp ltprvrdiie emrgcsysga
      181 irqlylegks meliaiclne sgaghgdllq daaksfrksd aealvqardi lartwqepps
      241 lmqlarmvgl ndfklksgfk elfgttvfgy vrrmrmqear lllekgqanv seaayrvgyt
      301 nvshfasqfh kafgsspgef msrrntawke pelpvrkrge eenrr
//
LOCUS       WP_181593056             245 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Paenibacillus sp. YN15].
ACCESSION   WP_181593056
VERSION     WP_181593056.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. YN15
  ORGANISM  Paenibacillus sp. YN15
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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 245)
  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 245)
  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..245
                     /organism="Paenibacillus sp. YN15"
                     /db_xref="taxon:1742774"
     Protein         1..245
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27167
     Region          2..209
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mmikavifdf ggtvldtetp ryqsfleayr qqgaeldwsl yaqcigtgfq dfnpyedllg
       61 rmklpvqlna frdairsrca elteqeqlrp gvmdalvrak amglkiglvs slprreidpy
      121 lqkwgiapyf dcirtaddat rlapdpelyq qavrmlgvnp rqaaaiedsp agaeaamlag
      181 mytvvvpnat tagmkfghch arldsldqle lpelldrvqg akamvyepav fwnrvlpieh
      241 eaevg
//
LOCUS       WP_181593061             318 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus sp. YN15].
ACCESSION   WP_181593061
VERSION     WP_181593061.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. YN15
  ORGANISM  Paenibacillus sp. YN15
            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 sp. YN15"
                     /db_xref="taxon:1742774"
     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=35830
     Region          18..318
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mepkpsnrpi mpgwlpawqr laarlsrdrf fylllipfig wylifaykpm yglqiafkdf
       61 svfkgiaasp wigfehfitf fqspyfvrtl tntllislys liwgfpapii lalllnevkh
      121 vffkkavqtl tylphfisvv viagivtnfl apsnglvnim laklglekiy flivpeyfrt
      181 ilvsmniwke tgfgailyia alsginpely eaavidgank wkqiwhvtlp gilptvmiml
      241 ilrighildv gyeaiillyq patyetadvi stymyragik egnydlttav glfnsavglv
      301 lviaanklsk kftesglw
//
LOCUS       WP_181593082             781 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. YN15].
ACCESSION   WP_181593082
VERSION     WP_181593082.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. YN15
  ORGANISM  Paenibacillus sp. YN15
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 781)
  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 781)
  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..781
                     /organism="Paenibacillus sp. YN15"
                     /db_xref="taxon:1742774"
     Protein         1..781
                     /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=87117
     Region          260..610
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mhllhgckra sfllpaflpv lgiaflrmmp dsaalfihkp aygmmvtiav llsgglglaa
       61 srsyqmeldv slryftlafa gfaflfafqa lllpvaaeep mlflamgsla rlaiclysya
      121 glrsllakrs pefrkkpliw whrhfaawav iilltaavae agflhayvlk iveslalgaa
      181 laasiqpllm rnpapplrlq llaqlilaqa slafilaapw nalwwfahav stagfltlgy
      241 allhsyeetr stgrvfnenl lypalrsimr tthegfvmtd tlgkinyanp rmealfqekp
      301 apgqlmsayl arlnlktash epltaivgnl lsgaaasidl hlealrdgte pvyyecyasp
      361 vldelsqtpm gylfvfrnrs eeerlnrmkd dfvsivshel rtpmsaiqgf teillerevp
      421 pekrirylet vhdeivrlsg lvddfldiqr metgrlayhf epldvgplva evarqwqetd
      481 khtlrldlpa hglfirgdre riiqllhnli snavkyspga eavdisltca egraairvkd
      541 yglgipeesl prlfqkfyrv etarhrkirg tglglsivre iadthggeir vesapgsgse
      601 fsvflpayep pelkgriall qepdeknpll laaaaerage plrfvsreel rfvlqharsl
      661 pklwiadirl eeqrdgwsll rmlledkqyr tnplfiavpg aapacapdqp spdrqglmdr
      721 marellrrpl egqllaaayd eetllqllhr qgleiaaier mggistfmil srprdseepa
      781 s
//
LOCUS       WP_181593207             410 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Enterobacter asburiae].
ACCESSION   WP_181593207
VERSION     WP_181593207.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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..410
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..410
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45244
     Region          27..383
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqnitknirw llltlpllsg cgtlsqmssp egtqellthd sldgdvdsvv rhymaqksvp
       61 gmtvavihnh gspqfytwgi tdavnrypvr pdtlfalgsl skgitaevva clvnegqlnw
      121 ndnlatllpp gtplsadaqk itllelvtht sglprqnmdv pmlgkfigyl stgenfysel
      181 dsdnvlryla dwqapknkvp qysntgyali gyilkhktge diqslasryi frplqmanss
      241 fipqqlkgyp qralghagdq pkfiprgqlt pdwhfsnnmv aaaslysnae dlatyaryhv
      301 stthspllds vfaevrntdi qrpdgvqgia wttdfiglek ityqvgyigg yssfigydke
      361 kgnavvvlqn tfnwsnyigi allmdmakkd sqspgsrfai ngipkrvyqq
//
LOCUS       WP_181593719              99 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Enterobacter asburiae].
ACCESSION   WP_181593719
VERSION     WP_181593719.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 99)
  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 99)
  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 99)
  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 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   5  (residues 1 to 99)
  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 99)
  AUTHORS   Rosinski,J.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..99
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..99
                     /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=10510
     Region          1..97
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mteleqlqas agqaaallka msnprrllil ctlcgapgts agelaratgl spsatsqhla
       61 rmreeglids trdaqrilyf ikndavhqli stlktlycp
//
LOCUS       WP_181593800             589 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Enterobacter asburiae].
ACCESSION   WP_181593800
VERSION     WP_181593800.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     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=64914
     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 mntlrrkwqs lprgivvlit alviytplsf iviqsflsap ffspskewsf esfefiftdp
       61 dfykalksgf ilafglvfis iplggvlafl mvrtdlpgrr lieplilvpi fvspmvlgfg
      121 yvvaagpvgf lsqwaqalig fvpwniydms sivviaglth vphaylyiss alrsvgsdve
      181 eaartagasp wqvmtsvslp mvrpsilyat vllfflglev fglmlvlgdp egnmvlatyl
      241 ykltnkmgtp synlmaavav vlicitiplv mlqrrlmrta nrfvtmkgka sqaralplgk
      301 wrwvaggmia fwltvtigvp llgvvlrafi snwgvgvslw delslntfrt iwaqpnllra
      361 ivnsmaigvi ggalavvcyl fvgiamhrkp dnttrfldys vlvpravpgl laglaflwvf
      421 lflpmwldns lksgwlsgfa wtdwmrenvi vwlrslrsti fsvwlaytvv wmayglrlis
      481 stllqvgpel eeaarstgat rgqitrhvti plsrygligs wllmflifer eystgvylls
      541 pgtetigsml vslwaagaid ivaalsfini llvvvglgia lrfgvkihd
//
LOCUS       WP_181594042             254 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter asburiae].
ACCESSION   WP_181594042
VERSION     WP_181594042.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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   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 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
REFERENCE   4  (residues 1 to 254)
  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..254
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..254
                     /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=28884
     Region          <49..249
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          161..243
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhsditrlla dlvnrtlpls qihfsalseq ytrtspclvi tldtsceaif ssfghitqps
       61 pdalsihfgk qlltielqhd ntlvqqlqva rrgprtgafl lqtltelqmq pdeqetailv
      121 vlsllshcrd llgsdihtas rsralfeair rfieehhasa ltresvaqaf yvspnylshl
      181 fqkignvgfn eyltqtrleh arqllkgydl kikdiavscg ftdsnyfcrl frkhtersps
      241 eyrrqyhsel iakk
//
LOCUS       WP_181594788             119 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Enterobacter
            asburiae].
ACCESSION   WP_181594788
VERSION     WP_181594788.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..119
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13506
     Region          11..118
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maetlevcce kkseaytcpm tqfvnlisgk waipilyrli vfntpvrfgd llraaapitq
       61 keltkqlrlf eqrglvtrtv ypeipprvey qitelgltlq dalsplaawm seygdqler
//
LOCUS       WP_181593307             472 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Enterobacter asburiae].
ACCESSION   WP_181593307
VERSION     WP_181593307.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 472)
  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..472
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..472
                     /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=51826
     Region          19..>296
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mtdndnnrtv pnalpvgyrf nefeikevig gggfgivyra wdhqlertia ikefmpssla
       61 vrgddmtlvl rserfgkafs aglnsfiqea rllarfnhpn llhvlrfwvq ndtaymgtlf
      121 ysgttlsrlr eekpelinea wirrtlpmlf gaiktihneg ylhrdisldn iqiqdnglpv
      181 lldfgsarrt ignlsdetet mlrpgfapie qytddneseq gpwtdiyalg avlrtlivgs
      241 pppvsvvrsi qdtckplvei mpqgysipll qaidralalh medrpqside faaliempva
      301 gindvlmakk pgtmlvpved ekpaslldwr rykipgmvaa gvlvgvvaga mlfsggndap
      361 eqaaqapaet rptetaanap evkpetakvn eqatpqqtpp pvespvalvy iriqdgetlr
      421 vngetkalrp atngyaslkl pagevkielq gngrtrgqtl ditkpgtwlv np
//
LOCUS       WP_181594789             264 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Enterobacter asburiae].
ACCESSION   WP_181594789
VERSION     WP_181594789.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            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 asburiae"
                     /db_xref="taxon:61645"
     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=28040
     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 rlktlaadlr arygvavdil
       61 vadltdeagi raveeelrsn taidtlinna gtaqmapfla gdvaqhqain tlnttalmrl
      121 tyailprlaq nnrgtlinia svlalhvrag salysatkaw vlsftrglqe efadssvriq
      181 avlpaatate iwshsgvtvn dlpegsvmtt ddmvdaslag ldqgetitip pmhdaglwdr
      241 yeaarlelfn sartgipapr yakr
//
LOCUS       WP_181592719             321 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus sp. YN15].
ACCESSION   WP_181592719
VERSION     WP_181592719.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. YN15
  ORGANISM  Paenibacillus sp. YN15
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. YN15"
                     /db_xref="taxon:1742774"
     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=36206
     Region          42..321
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mesltgkevy sqpdaidrqk gkgikklkpy lplyllflpv liyyllfsya pmaglviafk
       61 nynfldgifh sewvglshfr rflqngdfwl vfkntvllag frlavvfpap iifavllnem
      121 rfsrvkriiq tisylphfls wvvvyaicyn flsdsglvns ilayfgmeki aflgepslfr
      181 pifvgssvwk elgwnaiiyl aaltridtdl yeaasidgan rlrriwhvtl pgirtivsim
      241 llmalgdils vsfeqvtimm npmvssvaev idyyvyrvgl lgannfsyat avgffrsiia
      301 ltvviianvl akkidedggi w
//
LOCUS       WP_181594989             398 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Enterobacter asburiae].
ACCESSION   WP_181594989
VERSION     WP_181594989.1
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=44112
     Region          9..387
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 miknqhsslw rwicarilal aigsviviat cmwlryavqn ywimgkmpaa vrqefltlsq
       61 npqanparfh sivdtwwgls ystpsiasad watvallvlv mipfivvmgl kharplalqf
      121 srlrdaakdv adgqfgrqae liedapaemv sfandfnsmt gqlaryekel rashvamahe
      181 lhspltaaig rlqgmldrvf daspaqlgmv mkqlqhlnrl tdelhllsla dagnlvledq
      241 pfcldeliqe raawimpead ahhfritlrn prtspfrgda frlgqvvtil menalrygre
      301 gghlevalhy asghyileft ddgpgvspqf lpemfkrfsr eeqsrarhsg gsglglsiar
      361 aiceahggei saslpetggl avrillpwhp sgnenihs
//
LOCUS       WP_181594322             247 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter asburiae].
ACCESSION   WP_181594322
VERSION     WP_181594322.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            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 asburiae"
                     /db_xref="taxon:61645"
     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=27257
     Region          5..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 mtdtrhirqt fhrasglelr stwqstqayk rhshpqlsig aivegqtccv chdreyilnp
       61 gdlivipaca phscnpvagq prsyhmlyid tglplalqvi rsptlfahyl dvvetlspas
      121 letllsalpr aadnadalra tsqqvkqafl sdltcppsld elaqrfslrk etlirtfrqd
      181 tgltpgsfln isrveyakar lragddiadv gyqsgfadqs hfhktfvsyt aatprqyatg
      241 rsisdnk
//
LOCUS       WP_181595301             319 aa            linear   BCT 28-DEC-2024
DEFINITION  YbgA family protein [Citrobacter freundii].
ACCESSION   WP_181595301
VERSION     WP_181595301.1
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 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36403
     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 mdelaqwvsf rpvcpemaig lptprpairl
       61 tltdsgetql rfskpphddi tqkmadftad ylpkigdlsg fivcakspsc gmervrlyde
      121 ngnrgrkegv glftaallet ypwlpveedg rlhdpvlren fiervfalhe lntlrakglt
      181 rralldfhsr yklqllahhq agyreigpfv aslnewedld affvayrekl mtilkkpasr
      241 knhtnvlmhi qgyfrnqlns rqrvelrdvi lhyrdgllpi lapltllkhy maeypdrylm
      301 tqnyfdpypd dlglrlavt
//
LOCUS       WP_181594699             517 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Enterobacter
            asburiae].
ACCESSION   WP_181594699
VERSION     WP_181594699.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            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 asburiae"
                     /db_xref="taxon:61645"
     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=56629
     Region          22..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 mkktviavll lsgyaslspa qdvtiiytnd lhahvepykl pyvaegkrav ggfanistyv
       61 kqekqknkat fyfdagdyft gpyissltkg raiidimntm sfdaasvgnh efdhgwdntl
      121 iqlsqakfpi llgnvfykns nvlfwnkpyt ilekdgvkig viglhgvfaf ddtvsssmrq
      181 gieardevky lqryldelrg kvditvalmh egfparqssi gntdvkrald kdiqtakqvk
      241 gldilitgha hvgtpeplkv gntlvlstds ggidigklvl dvdlkkhhnk iksfelktly
      301 adewkpdpat qsvidswnkk lsetvrqkvg etpvtltray gessslgnlf tdamlaaapd
      361 aqlaltnsgg lradlnagti tlgdvisafp fpneltvmdl ngkslrnlme hsasltngvl
      421 qmskglemry dqhkpvgqrv vlftlngkpi vdsetyrvat nsflapggdg ftafidgqnk
      481 qvkggynlsd avidylvkgn kiipqqvnem rvkeftq
//
LOCUS       WP_181597133             696 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Salmonella bongori].
ACCESSION   WP_181597133
VERSION     WP_181597133.1
KEYWORDS    RefSeq.
SOURCE      Salmonella bongori
  ORGANISM  Salmonella bongori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
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="Salmonella bongori"
                     /db_xref="taxon:54736"
     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=76136
     Region          10..680
                     /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 mpvseynhil vavsfavaif asytalnmag rvagsarssa rvwltgggfa mgvgiwamhf
       61 vgmlamdham ymrfdpvltg lsmliaigss lfalwlvsae qlrlrrllpg alvmglgisa
      121 mhytgmaalq fasiivwdsv wvalsilial lascaalwlt fhlrhegtdv alrragaavl
      181 mgiaiagmhy agmkaaqfpq swpiehrgvd gnwlamlvsm valtilgitl lvslfdarlq
      241 artallassl aqanqelaql alhdtltrlp nrvlledrle qaiskanreg tpfallfmdl
      301 dgfktvnday ghdigdkllv avthrlnqll sgqftlarig gdefvlltev sapdeaasla
      361 salvhsidap ftidpyeltv tlsvgialyp ldgknerelm fnadaamyht khtgrngyhf
      421 fqpsmnmlaq tqlqlmndlw lalerrelrl vyqpkvqald gtivgfeall rwhhpkqgvl
      481 npdqflslae ktglivsign wvideacrql hewhlqghts wsvavnlsal qfeqpglidt
      541 itqslarhci rphlltleit ettamnkpeq svailtrlte mgvkasiddf gtgyssllyl
      601 krlpacelki drafvhelsd agdgativaa ivalakalnl hivaegvene tqqqfltqlg
      661 chtlqgflpg kprtaeeisr dptnsfirpi hhdtqk
//
LOCUS       WP_181597298             319 aa            linear   BCT 28-DEC-2024
DEFINITION  YbgA family protein [Salmonella bongori].
ACCESSION   WP_181597298
VERSION     WP_181597298.1
KEYWORDS    RefSeq.
SOURCE      Salmonella bongori
  ORGANISM  Salmonella bongori
            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 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Salmonella bongori"
                     /db_xref="taxon:54736"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36318
     Region          69..315
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mknkpvvgis acltgaavrf dgghkrmdfv mnslaswvty kpicpevaig lpvprpalrl
       61 iqttrgdirm ryshaphddv teqmnafadr flptagelag fivcakspsc gmervrlyde
      121 kgnrghkagt glftaammnk ypwlpveedg rlhdpvlren fvervfalne lnalraqgls
      181 rhsllafhsr yklqllahhq ggyreigpfv arlhewddle affiryrekl mtilshpasr
      241 knhtnvlmhi qgyfhrtlns rqraelrevi lryragqlpi lapltllkhy laehpdaylr
      301 tqnyfepypd tlglriaia
//
LOCUS       WP_181597507            1644 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Salmonella bongori].
ACCESSION   WP_181597507
VERSION     WP_181597507.1
KEYWORDS    RefSeq.
SOURCE      Salmonella bongori
  ORGANISM  Salmonella bongori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
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="Salmonella bongori"
                     /db_xref="taxon:54736"
     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=179671
     Region          23..1642
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkhlrvvacm imlalagcdn ndktapttkn eapaaaqtsq aqdpeqlqkl aqqsqgkalt
       61 lldaseaqld gaatlvltfs ipldpeqdfs rvvhvvdkks gsvdgawela pnlkelrlrh
      121 lepervlmvt vdpgikalnn atfgkpyekt ittrdvqpgv gfasrgsllp gkmveglpim
      181 alnvnhvdvn ffrvkpesla afvsqweyrs slsnwesdnl lkmadlvytg rfdlnparnt
      241 reklllplse ikplqqagvy vavmnqaghy nysnaatlft lsdigvsvhr yhnrldvftq
      301 slengaaqsg ieivllndkg qtlaqatsda qghvqletdk aaalllarke gqttlldlkl
      361 paldlsefnv agapgyskqf fmfgprdlyr pgetvilngl lrdsdgktlp dqpvklevik
      421 pdgqvmrtiv sqpenglyrl nypldssapt glwhvrantg dnvlrtwdfh vedfmperma
      481 lnltaqktpl tpadavkfsv vgyylygapa ngntlqgqlf lrplrdavat lpgfqfgnia
      541 eenlsrslde vqltldksgr gevsaasqws ethsplqvil qasllesggr pvtrrveqai
      601 wpadtlpgir pqfaakavyd yrtdttvnqp ivdedsnaaf diiyvnaqge kkavsglqvr
      661 lirerrdyyw nwsesegwqs qfdqkdlveg eqtldlnade igkisfpvew gayrlevkap
      721 netvssvrfw agyrwqdnsd gsgavrpdrv tlkldkpnyr pgdtmklhia apvagkgyam
      781 vessdgplww qeidvpaqgl dltipvgktw nrhdlylsal vvrpgdksrs atpkravgll
      841 hlplgdenrr ldlalespak mrpnqpltvr vkaranhgdm pkqinvlvsa vdsgvlnitd
      901 yatpdpwqaf fgqkrygadi ydiygqvieg qgrlaalrfg gdgdalkrgg kppvnhinii
      961 aqqaqpvtln dqgegvvtlp igdfngelrv maqawtaedf gsgeskvvva apviaelnmp
     1021 rflaggdvsr lvldvtnltd rpqtlnitla asgllellsq qpqpvklapg vrttlfvpvr
     1081 aldgfgegel qatitglnlp getfaaqhkq wkigvrpawp aqtvnsgval apgeswrapa
     1141 qhlanlspat lqgqlllsgk pplnlaryir elkaypygcl eqtvsglfpa lytnaaqlqt
     1201 lgivgdsdek rraavdigis rilqmqrddg gfalwdkngp eeywltayam dflirageqg
     1261 ysvppeaine gnarllrylq dpgmmlirys dntqagkfaa qtyaalvlar qqkaplgalr
     1321 eiwerhrqaa sglplmqlgi alkmtgdarr geeaitqaln tprqderqwt adygsalrdn
     1381 almlslleen nlrpdaqnal lsslseqafg qrwlstqenn alflaahslq asagawqaqt
     1441 sfaaqplsgd kaltrnldad qlaaltvtns gsqplwlrld ssgypssape pasnvlqier
     1501 qilgtdgqrk slsslhsgdl vlvwltvlad rnvpdalvvd llpaglelen qnladssasl
     1561 sesgsevqnl lnqmqqadiq hiefrddrfv aavavnegqp vtlvylarav tpgtyqlpqp
     1621 qvesmyvpqw ratgasegll ivtp
//
LOCUS       WP_181597580             278 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Salmonella bongori].
ACCESSION   WP_181597580
VERSION     WP_181597580.1
KEYWORDS    RefSeq.
SOURCE      Salmonella bongori
  ORGANISM  Salmonella bongori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
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="Salmonella bongori"
                     /db_xref="taxon:54736"
     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=31700
     Region          18..274
                     /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 myhdvshlls rlingplplr qiyfasasgp apelayqvdf prleivlege ltdmsitapl
       61 ipcdvlyvpa ggwniprwqt pvttlsilfg kqqlgfsvvh wdgqqhqnlt kqhvarrgpr
      121 igsfllqtln emqmqpqeqq tarlivasll shcrdllgsq iqtasrsqal fdaireyide
      181 ryaapltres vaqafyispn ylshlfqktg aigfneylnh trlehakall kgydlkvkev
      241 ahrcgfvdsn yfcrlfrknt erspseyrrq yhsqltek
//
LOCUS       WP_181597748             255 aa            linear   BCT 28-DEC-2024
DEFINITION  dimethyl sulfoxide reductase anchor subunit family protein
            [Salmonella bongori].
ACCESSION   WP_181597748
VERSION     WP_181597748.1
KEYWORDS    RefSeq.
SOURCE      Salmonella bongori
  ORGANISM  Salmonella bongori
            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 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Salmonella bongori"
                     /db_xref="taxon:54736"
     Protein         1..255
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=27485
     Region          5..247
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 mekyelplvf ftvlsqmsvg maliltwrtl rgeieakrvy wlvtglvlal asvaailhla
       61 hpdraydalr nlqhawlsre ilgatlfgva vgvtflakgh kapaivasvc gvvlvavqgm
      121 tyaapamvai angftmllff itvwvmgcaa iplltlkpah salrqgivvc iavllsapll
      181 wlsggtimqm tarswlvspf ylaslaclai afivsrrnds rpallfillf vgvflsrlvf
      241 fgdtvstivn ighly
//
LOCUS       WP_181597930             128 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Salmonella
            bongori].
ACCESSION   WP_181597930
VERSION     WP_181597930.1
KEYWORDS    RefSeq.
SOURCE      Salmonella bongori
  ORGANISM  Salmonella bongori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
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="Salmonella bongori"
                     /db_xref="taxon:54736"
     Protein         1..128
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14208
     Region          14..117
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtahslsrql regnlfaeqc psrgvlkhvt srwgvlilva lrdgthrfsd lrrkmggvse
       61 kmlaqslqal ehdgflhrms ypvvpphvey sltplgeqvs dkvaaladwi elnlpqvlaq
      121 rdrqtdag
//
LOCUS       WP_181597981             273 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Salmonella bongori].
ACCESSION   WP_181597981
VERSION     WP_181597981.1
KEYWORDS    RefSeq.
SOURCE      Salmonella bongori
  ORGANISM  Salmonella bongori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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..273
                     /organism="Salmonella bongori"
                     /db_xref="taxon:54736"
     Protein         1..273
                     /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=30684
     Region          10..268
                     /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 mtdvivhfyf wfdlilvsvi glcvgsflnv viyriplsyt chgggmsvaf ppshcpvckh
       61 sipardnipl asyillkgrc rfcherinvl ypvtegatfi aficfymlff ntdivlflls
      121 vflfcllyvi siidfryyii pdrlllvlfg gggvysylyg niiydalglv iyflifaiiv
      181 facesfsdkq ilgmgdikly lsvvpwvggl nfpfvmliss iaglclagiw klyvkkiyvs
      241 neltkdiden rfipfgpaia vallivylav llr
//
LOCUS       WP_181597944             387 aa            linear   BCT 28-DEC-2024
DEFINITION  integrase [Salmonella bongori].
ACCESSION   WP_181597944
VERSION     WP_181597944.1
KEYWORDS    RefSeq.
SOURCE      Salmonella bongori
  ORGANISM  Salmonella bongori
            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 11426456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Salmonella bongori"
                     /db_xref="taxon:54736"
     Protein         1..387
                     /product="integrase"
                     /calculated_mol_wt=44607
     Region          10..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 mslfrrgeiw yasystpggk rikeslgtsd krlatelhdk rkaelwrvdk lgdfpdvtfd
       61 dacmrwleek aekkslkddr srmafwlahf egirlkdvte qkiysavnrm snrkqleiwk
      121 ikaaaakkng epapvysakp vttstkakhl almkailraa erdwkwleka pvikipsvrn
      181 krvrwleade akrlidecpe plksvvkfal atglrrsnii nmewqqidmq rrvawvnped
      241 sksnraigva lndtackvlr dqigkhhkwv fvhtkegirp dgsktptvrk mrvddqrawn
      301 aacrragied frfhdlrhtw aswliqsgvp lsvlqemggw esiemvrrya hlapnhlteh
      361 akqidsifsd dvpnmshlen kelaeng
//
LOCUS       WP_181598622             271 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter sp.
            RHB36-C18].
ACCESSION   WP_181598622
VERSION     WP_181598622.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB36-C18
  ORGANISM  Citrobacter sp. RHB36-C18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  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 271)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 271)
  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..271
                     /organism="Citrobacter sp. RHB36-C18"
                     /db_xref="taxon:2742627"
     Protein         1..271
                     /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=31069
     Region          5..261
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          180..261
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mthtrdipqs fwrdeqlpwl elrstwqsqq aykrhhhsql sigaileggt cclcddkeyh
       61 lkvgdlivip plaphscnpv ngkfrsyhml yfdarwclth lpalnsnqrl stctpvirdp
      121 qlfqcymhlv almpqrqttq itdaaqallr slplqsvtpe nlsvtsqylr erlqssllsp
      181 psldeladec hmrketlirt fkqdtgltpg nylnimridy arqrlragde ivdvgyqsgf
      241 adqshfhrtf vrytaatprq yalgrsisdn n
//
LOCUS       WP_181598741             517 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Citrobacter].
ACCESSION   WP_181598741
VERSION     WP_181598741.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=58346
     Region          11..>502
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mqmitsrqnr llkfllsrke yvtllkiaey lsvsektvqr dlrlleqwls ewkisidkra
       61 gagvilsadn itdllyldql lgsegddadg mmnnsrrvki asqllsetph etsinklser
      121 yfissasivn dlkvieswit plglslirsq sgthiegses gvrqamasli ngvinhnepg
      181 sviysrldpg sykalvhyfg eedvlfvqtl lqemendlcw slgepyyvni fthilimmyr
      241 itrgnalprk eesitscden ifsiasrmiq hiekriahpl pedevwfiyq yiissgmvie
      301 ehndlsvigh mhssdearli thrliatfae mvdcdlsqdt alydgllihi kplinrlnyq
      361 irirnplled ikgelqdvwr ltqcavnrvf sgwgeravsd devgyltvhf qaamerqiar
      421 krvllvcstg igtshllksr ilrafpdwti vgvvsagslp svltddielv vstinlpava
      481 mpvvyvtaff ndadikrvte tviteklhra tslvven
//
LOCUS       WP_181598635             637 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Citrobacter].
ACCESSION   WP_181598635
VERSION     WP_181598635.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=72784
     Region          14..609
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mrfpnqrlaq lfgmlqneal pqdelaqrls vstrtvradi talnalltqy gaqfvlsrgn
       61 gyqlkiddpa ryhalqtqrp dallriprts qervhwlvvr fltsafslkl edladewfis
      121 ratlqndmae vrehlqryhl tletrprhgm klfgsemair acltdllwtl aqqdpqhplv
      181 tqealnagip eqlqpvlqdi farfhirltd egelflrlyc avavrriseg yplpefaaee
      241 aeqsvclatr eiaavlhrla dkpltvseen wlqvhiaarq vqeiapsain adddealvny
      301 ilrfinsqyn ynllndkqlh adllthiktm itrvryqimi pnpllenikq hypmawdmtl
      361 aavsgwgkyt pytiseneig flvlhigvgl ersynigyqr qpkvllvcda gnamarmiea
      421 vlarkypqie ivdtvtlrdy eqresisedf vistarvgek dkpvvmiapf ptdyqleqig
      481 klvlvdrtrp wmlnkffdaa hfrvidepmd qqtlfnvlcr qlqdegfvda efldsvvere
      541 aivstmlgds ialphalgll akktvvytil aprgiawgde tahvifllai skseyeeama
      601 iydifvtflr eramtrlcac rnfsefktva mecvsrf
//
LOCUS       WP_181599102             412 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter sp. RHB36-C18].
ACCESSION   WP_181599102
VERSION     WP_181599102.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB36-C18
  ORGANISM  Citrobacter sp. RHB36-C18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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 412)
  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..412
                     /organism="Citrobacter sp. RHB36-C18"
                     /db_xref="taxon:2742627"
     Protein         1..412
                     /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=45722
     Region          32..377
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkapkkitkq sqvdaltlpa dknvmriavm nggltglslv lrrtssggvt asyitrrdgk
       61 disigsrtsw tlaaaqerhr eimtnmargi darteaisvp hdlnalfray innpafapad
      121 stvktyvctw qkycnrlsay gettienftr asahslirtv aekhsvnsak klrdillalr
      181 hylesqfdie afetlmtlqk llgknntele rsrqprtnyl ekdqlralwk ylcedetrpa
      241 hlaarmlica plrkgevvgg qweevdedag lwripgsrtk tgfplnvpis pameeifeaa
      301 rrcvdggfif gisssainhr lpemrvacgn aemtvhdlrr tasqlsasde lnepgsgltf
      361 ieadlilnhv kgaksqasai attyqpetlq kmvtdaiaky qnwlekeits ip
//
LOCUS       WP_181599192             487 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Citrobacter sp. RHB36-C18].
ACCESSION   WP_181599192
VERSION     WP_181599192.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB36-C18
  ORGANISM  Citrobacter sp. RHB36-C18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB36-C18"
                     /db_xref="taxon:2742627"
     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=53034
     Region          17..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 msdvnpilsg saqsiaayqd aieqstqavv ewlkqpemyq gktveqlrer inlnftsqgl
       61 gnqaaierav eyflkdsllv hhaqcvahlh cpslvisqaa evlinatnqs mdswdqspsa
      121 tiieikliew lreqvgyaag dagvftsggt qsnlmglmla rdaffarqgh siqqngltgd
      181 lskikvfcse sahfsvqknm almglgyrsv tqvktdafsr meladlkdkl aqakangeqv
      241 maivatagtt dagaidplad iaalaaehqi wmhvdaawgg alllseqyrh flnglelads
      301 vtldfhkqff qtiscgafll kdarhyelmr yqaaylnsdf deeagvpnlv skslqttrrf
      361 dalklwmgle algkkqyaei idngvtlard vaafvktqph lelvmepqla svlfrfrphs
      421 ddmafvalln qrigdvllas gsanvgvtea dgvtclkltl lnptvcledv kvllasvkat
      481 aeqllna
//
LOCUS       WP_181599311             286 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter sp.
            RHB36-C18].
ACCESSION   WP_181599311
VERSION     WP_181599311.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB36-C18
  ORGANISM  Citrobacter sp. RHB36-C18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB36-C18"
                     /db_xref="taxon:2742627"
     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=32560
     Region          <97..277
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          188..271
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 myhdvshlls rlingptplr qvyfasssss tpelayqvdf prleivlege fidngvtgas
       61 atllpcdvlf vpagswnfpq wltpvttlsi lfgkqqlgfs ivqwdgkqyh nltrqhvarr
      121 gprigsfllq tlnemqmqpq eqqtarliva sllshcrdll gsqiqtasrs qalfeairdy
      181 ideryasplt resvaqafyi spnylshlfq ktgaigfney lnhtrlehak tllkgyelki
      241 kevahtcgfv dsnyfcrlfr knterspsey rrqyhsqlte ikanpk
//
LOCUS       WP_181599392             369 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Enterobacter asburiae].
ACCESSION   WP_181599392
VERSION     WP_181599392.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            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..369
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     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=41859
     Region          1..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 mkdinmvksi hylrgiaalf vvlfhlrgyv nntyvqsnlg dllfvngafg vdlffvisgf
       61 iicfatqkke yfyplkffir rffriyplli lsvsiyfifl tikkgstgld swfiwsiipl
      121 qidyhagapf fgynvlaiaw tltyeisfyi iflasmiish kyrailcssi iltmvlstql
      181 msvtptlngi ntnyikndfi tlisspiyid fvygiisyvi yihilpalsi ykgtvlnvll
      241 istitvttvl ifttknidhg plgwgvmafi ivvattlmda sfttaknkpl imlgnisfsl
      301 ymwhyifiei tntyfpsism ngfytlvimt tcsiaiasis fnlieipsin lskkiiswid
      361 rnnpervvs
//
LOCUS       WP_181599319             535 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Enterobacter
            asburiae].
ACCESSION   WP_181599319
VERSION     WP_181599319.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            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  :: 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="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     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=58787
     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 isyrtarqwr evvhnvsftl grgemlafvg esgsgkttta qaiiglladn
       61 arrdagkisl ngeeisrwsa krldtlrgar islvpqdpgn slnpvktiga qvgeiiqlhq
      121 kvtraerdeq vlalltkvgl shpeqrmtqy phqlsggmkq rvliaiaial rpdvivadep
      181 tsaldvtvqk rildlldilr resgtavlfv thdlalaaqr adrllvfrdg evqeqgntad
      241 ivrtpqhayt rqllsdlqgq rltiapvagr plaspairar aiskqfslgk ghqlqaldrv
      301 tfdvrrgsth alvgesgsgk ttlarillgf eqadsgqvii ddidatalsr earrqlrhki
      361 qfvyqnpfas ldprqtlfdi ieeplknfsr lgkaqrklrv etvaqrvalp velltrtare
      421 lsggqrqrva iaralilept ilvldeatsa ldvtvqaqil allqqlqqql gltyffithd
      481 lstvrriahs vtvlrggqvv eqgdvgtlfa spqndytrel idaiphfspa teefa
//
LOCUS       WP_181599422             265 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Enterobacter asburiae].
ACCESSION   WP_181599422
VERSION     WP_181599422.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            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 14398439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     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=29538
     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          <144..230
                     /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 mptvidktpi hddaigwsrg aisytrgevd pphqhpqgql lfaikgvmlv etgnkrwvip
       61 pqralwippf qehtysvlst telravwfsp alisqcepfk rkeevhvita talfkeliag
      121 lfsaqyrpas qrsmavllle ilseaqqisa elpmpvderl hrvacdiias nlwdvsmerl
      181 aeqvamsert fsrafikdtg fsfrawrqra ricasldlla ngypakqvaw mlgfsgsaaf
      241 aaafravvga tpadffpeqk rfpai
//
LOCUS       WP_181599468            1650 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Enterobacter asburiae].
ACCESSION   WP_181599468
VERSION     WP_181599468.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
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 asburiae"
                     /db_xref="taxon:61645"
     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=179816
     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 mkpfrlaals lallttftlv gcdnsddksq aaapaastas tpkaaekpna etlaklaaqs
       61 qgkaltlldt sevqldgaat lvltfsvpln pdqdfaktvh vvdkksgkvd gawelapnlk
      121 elrlrhlepn rnlvvtverd lqalnkatfg idyekalttr dieptvgfas rgsllpgkvv
      181 eglpvmalnv nnvdvnfyrv kpeslaslvs qweyrnsltn wesdnllkma elvytgrfdl
      241 nparntrekl llplkdikpl qqsgvyiavm nqaghynysn aatlftlsdi glsahryhnr
      301 ldiftqslen gaaqsgvtvt llndkgqtla eansdadgha kletdkeaal ilaskdgqtt
      361 lldlklpald laefdiagsp gyskqffmfg prdlyrpget vilngllrds dgkplpdqpv
      421 kldvlrpdgq vartivvkpe nglyrfnypl dsgaqtgmwh iranagdnlq rmwdfhvedf
      481 mpermalnls gqktpvspqd nvdfnvvgyy lygapangns lqgqlflrpl rdavaalpgf
      541 qfgdiaeenl srsldevqlt ldeqgrgqvs tesqwkevhs plqlilqasl lesggrpvtr
      601 raeqaiwpaa elpgirpqfa skavydyrtd ttvnqpivde ngnasfdivy adasgakkav
      661 sglqvrlire rrdyfwnwse segwqsqfdq kdlvegeqel tlkadetgkv tfpvewgsyr
      721 mevkapdemv ssvrfwagys wqdnsdgtga arpdrvtlkl dkpayqpgdt inlhiaapsa
      781 gkgyamiess egplwwkeid vpangldlai pvdkawkrhd lylstlvvrp gdksksatpk
      841 ravgllhlpm gdenrrlnia ldnpqkmrpn qtlsvkvkas vkegavpqkv nvlvsavdsg
      901 vlnitdyvtp dpwqaffgqk rygadiydiy gqviegqgrl aalrfggdgd elkrggkppv
      961 nhvtiiaqqa qpvtldange gtitlpigdf ngelrlmaqa wteddfgsse skvvvaapvi
     1021 telntprfla sgdtsrltld ltnltdkpqt lnvaltatgk lsleggqpqp vqlspgarst
     1081 lfipvraleg ygdgevtaqv tglqlpgetf apqqkswkig vrpafpaqtv ntgamlnpge
     1141 swtapaqhsn gfspatlqgq lllsgkppln laryirelqa ypygcleqtt sglfpslytn
     1201 aaqltalgik gdtddkrraa idigisrllq mqredggfal wdkngpeeyw ltayvtdflv
     1261 rageqgysvp adavnnannr llrylqdpgm msirysddtq askfavqaya alvlarqqka
     1321 plgalreiwd rheqaasglp lmqlgmalkl mgdaprsqqa ldlalktsrn dsktwmadyg
     1381 sqlrdnalml slleeykllp daqntllnal seqafsqrwl stqesnalfl agrslqtlsg
     1441 awqaktslse tasggdkslv qnvsgdelga lqvtntgttp lwvrldstgy peyapqpsan
     1501 vlqverhila tdgsskslss lksgelvlvw levkanqnvp dalvvdllpa glelenqnla
     1561 sssaslqdsg sevqnllsqm qqadiqhmef rddrfvaavp vnegqpvtlv ylaravtpgt
     1621 ylvpvpmves myvpqwratg aasgplivvp
//
LOCUS       WP_181599636             199 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter asburiae].
ACCESSION   WP_181599636
VERSION     WP_181599636.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 199)
  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 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   3  (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   4  (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 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..199
                     /product="helix-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=22513
     Region          30..188
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          137..187
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mfkillidrc hftrtgfeaw lnhsglfpgh yvvtglnnlf larehilqwk ptlviadlyg
       61 frqdihhfqq lssllsaser lpfillqsge dsgmtdwlgq fpvwssllkn asleevatii
      121 ndalisrasa drptaaapll trqeekvltl wmdgasnqki aahlsingkt vytykrnirm
      181 klhmdtrfsp flslqeses
//
LOCUS       WP_181599659             408 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter asburiae].
ACCESSION   WP_181599659
VERSION     WP_181599659.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae 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="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     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=47109
     Region          9..393
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 magtnklsdk klkalqgasr dapemyadge glsvraskqg qlswvfsyrl ggrgsklerl
       61 tlgrypdlsl kaarekrekc rqwlaggldp ktelelstee tlkpvtvqda leywlvnyar
      121 rkrsdeelvr aqlrkhiypr lgrypltrce trhwvacfde inltkpmtag rmfqiskqal
      181 rfckvrryaa sdalafltiq dvgqpsgqrd rvlsdselad vwrstdsddq qpyysrllkm
      241 lvlfgartme vrlsrwsewd fsswiwtvpk ehsktrekiv rsipeairpw leelkretgk
      301 tglllgedrt rqavslkgrr lykdfhhnep wtlhdlrrtf stglnnmgia phivelllgh
      361 alpgvmaiyn rslylpekld alnkwyerle llagnhqnvv llpvmnrd
//
LOCUS       WP_181599804             654 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidase U32 family protein [Enterobacter asburiae].
ACCESSION   WP_181599804
VERSION     WP_181599804.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            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 asburiae"
                     /db_xref="taxon:61645"
     Protein         1..654
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=72536
     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          447..505
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mrlqshhlel lspardaaia reailhgada vyiggpgfga rhnasnslsd iaelvpfahr
       61 fgakvfvtln tilhddelep aqrlitdlyq agidalivqd mgvleldipp ielhastqcd
      121 irtvekakfl sdvgfsqivl arelnlnqir dihqatdati effihgalcv aysgqcnish
      181 aqtgrsanrg dcsqacrlpy tlkddqgrvv afekhllsmk dndqtanlga lidagvrsfk
      241 iegrykdmsy vknitahyrq mldaiiedrg dlarasagrt ehffipstdk tfhrgstdyf
      301 vnarkgdiga fdspkfiglp vgevlkvakd hldvevtepl angdglnvmi krevvgfran
      361 tvektgenry rvwpnempad lykarpnaal nrnldhnwqq allktsserr iavdielggw
      421 eeqliltmtc edgisvthtl dglfkvanna ekalnslkdg vaklgqtiyy araidvnlpd
      481 alfvpnslln afrretaeml daarlaqypr gsrkaeavpa pvypdthlsf lanvynhkar
      541 efyhrhgvql idaayeahee kgdvpvmitk hclrfafnlc pkqakgniks wkatpmqlvn
      601 gdevltlkfd crpcemhvig kmknhifkmp qpgsivasvs pddlmktlpk rkgs
//
LOCUS       WP_181599506             222 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Enterobacter asburiae].
ACCESSION   WP_181599506
VERSION     WP_181599506.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter
            cloacae complex.
REFERENCE   1  (residues 1 to 222)
  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 222)
  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..222
                     /organism="Enterobacter asburiae"
                     /db_xref="taxon:61645"
     Protein         1..222
                     /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=24519
     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 msmkqrwqdl aksrmkevgm tqeqlaealg mtqgglghwl ngrrepnlev iakifkilqm
       61 pgfvvdadga vsdaradhnv sfhamneskg sypviswvsa gdwmeavepy hrraierwyd
      121 ttvecsedsf wldvrgdsmt spaglsipeg mvilvdpqve pingklvvak ldgdneatfk
      181 klvidagqrf lkplnpqypi ipingncrii gvvvdakitn lp
//
LOCUS       WP_181599905             469 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Sphingomonas].
ACCESSION   WP_181599905
VERSION     WP_181599905.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 469)
  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 469)
  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..469
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..469
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50608
     Region          187..468
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mgkraeacsg esrslgrwap afagallsla tpahaaeptt yqralaagyk aaflcsgifn
       61 agrtqaqvea leltgiyaey aaivptlsag idyrtrqvtv afdpalpprr sewrhgrgce
      121 tqpigqlems eaaeypavnv agpdsrrwpa gdgginpstg paasvaagaf gpaygeeart
      181 vgvvvvqdgq iiaeryatgf spytsnrtws vaksisgtll gvasrknllq vhspapvrew
      241 rvhpyddprr sitldnllrm asglhsdtag nrtdalymga ttvtqetthw pleakpgtrf
      301 ryanndilla irslraalnd darylafprt elfdkigmth tvaetdwqgn filssqvwst
      361 ardlarlgll wlndgvwqge rilpegwvky mttpsgpqpe egpgygatmw lfgpkqglpe
      421 gsyaaqgnrg qyimvipser lvivrrgedp vgarfdiakf sadvaaalr
//
LOCUS       WP_181599911             141 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ExbD/TolR family protein [Sphingomonas].
ACCESSION   WP_181599911
VERSION     WP_181599911.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Sphingomonas"
                     /db_xref="taxon:13687"
     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=15412
     Region          1..137
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mamsggqddg mpfiemnmtp lidvllvlli mfiitipiqt havkidlpvn sdvnnpppid
       61 pikntvsvdp agtvtwngsp idmvtlrlyl ertramspep elhvqpdpqa ryavvdnvla
      121 vikrsgvtkm gfvgneqyra f
//
LOCUS       WP_181598998            1644 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Citrobacter sp. RHB36-C18].
ACCESSION   WP_181598998
VERSION     WP_181598998.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB36-C18
  ORGANISM  Citrobacter sp. RHB36-C18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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 sp. RHB36-C18"
                     /db_xref="taxon:2742627"
     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=180292
     Region          26..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 iqqsqgkslt
       61 lldasevqld gaatlvltfs ipldpeqdfs rvvhvvdkks gkvdgawela pnlkelrlrh
      121 lepnrelvvt ierdllalnk atfaidyekn ittrdvqpsv gfasrgsllp gkvieglpvm
      181 alnvdsvdvn ffrvkpeslg afvsqweyrn slsnwesdnl lkmaelvytg rfdlkpernt
      241 reklllplsd ikplqqagvy iavmnqaghy nysnaatlft lsdigvsahr yhnqldvftq
      301 slengaaqqg ievtllnekg qtlaqatsda qghvkletdk daalllarkd gqttlldlkl
      361 paldlaefdi agapgyskqf fmfgprdlyr pgetvilngl lrdsdgktlp dqpvklevvk
      421 pdgqvlrsvv sqpenglyrf swpldssapt gmwhirantg dnqsrmwdfh vedfmperma
      481 lnltankmpl aptdgvkfsv vgyylygapa ngnalqgqlf lrplreavqa lpgfqfgnia
      541 eenlsrslde vqltlddhgr gevttnsqwq ethsplqvil qasllesggr pvtrrveqai
      601 wpadtlpgir pqfaaravyd yrtdttvnqp gvdensnaaf divyadaqge kkavsglqvr
      661 lirerrdyyw nwsegegwqs qfdqkdlveg eqtldlkade tgkvsfpvew gayrlevkap
      721 ndavssvrfw agyswqdnsd gsgavrpdrv tlkldkpgyr pgdtmklhia apaagkgyam
      781 vessegplww qeidvptdgl disipvdktw nrhdlylsal vvrpgdksrs atpkravgll
      841 hlplgdenrr lalalespak mrpnqpltvk ikasvkngdv pkqvnvlvsa vdsgvlnitd
      901 yatpdpwqaf fgqkrygadi ydiygqvieg qgrlaalrfg gdgdelkrgg kppvnhvniv
      961 aqqalpvtln eqgegtvtlp igdfngelrv maqawtaddf gsseskviva apvitelnmp
     1021 rflaggdtsr ltldvtnltd kpqtliinla asgllelmgq dpapvnlapg vrttlfipvr
     1081 aregfgdgei qaqisglnlp getlpvqhkq wkigvrpafp aqtvnygval qpgatwqlpg
     1141 eeltnfspvt mqgqllfsgk pplnlaryir elkaypygcl eqtasglfps lytnaaqlka
     1201 lgiagdsdek rraaveigis rllqmqrdng gfalwdkngs eeywltayvm dflvraneqg
     1261 ysvpaevinr gnerllrylq dpgmmsiryt ddasasrfav qayaalvlar qqkaplgalr
     1321 eiwerraqaa sglpllqlgi alknmgdanr seqaltlaln tprrdaqqwm adygsqlrdn
     1381 almlalleen klkpdvqntl lntlseqafg qrwlstqenn alflaartlq dlpgswqaqt
     1441 slseqplage ksqtrnldad alstlnatnt gnlplwlrld vsgypqtspt pasnvlhier
     1501 qilgldgnsk aldslrsgel vlvwlevkas qnvpdalvvd llpaglelen qnlangsasl
     1561 qdsgsevanl lnqmqqadiq hvefrddrfv aavavnegqp vtlvylarav tpgtyqvpvp
     1621 qvesmyvpqw ratgategll ivrp
//
LOCUS       WP_181600001             201 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Sphingomonas].
ACCESSION   WP_181600001
VERSION     WP_181600001.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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 201)
  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 201)
  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..201
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..201
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22376
     Region          3..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(9..13,109..110,142,166..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 mtvrgvvfdv gnvlftwdpr flyerliedd raldaflrdv vtrdwhfqhd agrpfaetsa
       61 eliaeypqha eliaawsprf nesvgppvdg miplveelda agvplfaitn fsgefwgpfr
      121 dtqpvfdrfr dvivsgterl vkpdaaiyql alkrfgmpad alifiddsar nvagaeaigi
      181 rghlfrdaat lrteltalsl l
//
LOCUS       WP_181600150             396 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Sphingomonas].
ACCESSION   WP_181600150
VERSION     WP_181600150.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
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="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..396
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43691
     Region          14..363
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msqvaaasfl aaapieagqp afkaaveefr qlhreevrra givgssfyfi rdgrtvvadh
       61 lgeqdadahi pvdaqtiyhw asitktmtgi aimqlrdrgl ltlddpivry vpelaavhnr
      121 fgdtdritlr qlmshsagfg gatwpwrehd wqpfepkswa qlaamlpyte vrfkpgtrfs
      181 ysnpgivylg qvierlsged yevyvdkhil kplgmhasyf dttpphllph rshsyyvrgg
      241 artaapfdvd tgvtvsnggl naplpdmary vafligdper qaeydlvlkr asleemwrpq
      301 iaagddftqg rmaettqagl sffiddspgl rfighngdqn gfraylslcp drragsllaf
      361 ntetrpvand psnrdtaesr ialaagklce aiapdg
//
LOCUS       WP_181600220             188 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Maf family protein [Sphingomonas].
ACCESSION   WP_181600220
VERSION     WP_181600220.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 188)
  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..188
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..188
                     /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=19750
     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 mplilasasp rrldllvrig vvpdavmpad idesvlkgel pahhaarlaa ekaaavakpg
       61 alvlaadtvv aagrrilpkv edestarrcl ellsgrrhrv hsavtlvdae gkarhrlsts
      121 ivtfkrltrd eidaylasge whgkaggyai qghaeafvrf lsgshsgvvg lplfetrall
      181 vaaghslg
//
LOCUS       WP_181599693             727 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Enterobacter asburiae].
ACCESSION   WP_181599693
VERSION     WP_181599693.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter asburiae
  ORGANISM  Enterobacter asburiae
            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 asburiae"
                     /db_xref="taxon:61645"
     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=78333
     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 mnntimhktl lalavgaath safaaddqke dtlvvqaapa sdfkpggdql vpafldgqva
       61 nggrmgmlgq qnamdvpfni isytsklved qqaktiadvv andagvqfvq gygnsaetyr
      121 irglkfdgdd mtfgglsgvl prqvvdtqmv drieifkgan slmngaassg vggminlepk
      181 hagelpqakv gvdytsdsqi gttldagrry gdsdqfgarv nlvhregetg iandrrrttl
      241 lstgldyagd rfrtsldlgy qkktfhgspt svnisavdfv peppkndrnf sqkwaysnie
      301 nefgmwrsey ditdgwtayt glgaqhahee giysapklvd ksgkatvsrl dtnrisdsvs
      361 gmagvrgnft tgfvshkvnv gysamtknek iawkmsatkd npttniyhnt gvdmpdstnl
      421 ngsggkysdp ltsgrtrtqg wllsdtlgvl ddkllftaga rhqkvvvrgy nkvtgaenaa
      481 dgfdgsrwmp tygvvykpwe aislyanhte alqpgktapn tatnygqstg ivhskqnevg
      541 vkadfgrvgg slalfeikmp sailddsghy gldaeqrnrg velnvfgepa lgmrlnasat
      601 wlqaeltktk ngvnqgndai gipnfyavvg aeydikpvdg ltatarvnhs gaqyadlant
      661 kkldsyttld lgmryrfavn hnenqmtvra gidnvtneny wasvddsgty itqgeprtfk
      721 vsvgyaf
//
LOCUS       WP_181599979             391 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: phospholipase D-like domain-containing protein
            [Sphingomonas].
ACCESSION   WP_181599979
VERSION     WP_181599979.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 391)
  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 391)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 391)
  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..391
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..391
                     /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=44169
     Region          20..374
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 msrivvdewv mpeqsdsfdv egnrltllve prdrltgllt liegaeqslr llyytfaddh
       61 iggrvrnali aacergvhvs liidgfgsdp ddaflqplrd acvdicrflp rygrrfllrn
      121 hqklciadet rlviggfnie dayfagpeed gwrdlglive gpaagrlvgy fdalsawtkr
      181 pqarmrdlrr alrrwsepeg kvrwllggpa rrlspwaram rsdmlkarsa sliaayfaps
      241 pamlqrldka girgdvrvit aaksdnttti aaarftypgl lrkgvrifey qraklhtkly
      301 iiddavhigs anfdmrslfl nmelmlried rvfadrlral fnhelndsve itldamigwg
      361 htlararnai ayflvstldy gvtrrlnida e
//
LOCUS       WP_181600258             911 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Sphingomonas horti].
ACCESSION   WP_181600258
VERSION     WP_181600258.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas horti
  ORGANISM  Sphingomonas horti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 911)
  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..911
                     /organism="Sphingomonas horti"
                     /db_xref="taxon:2682842"
     Protein         1..911
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=98729
     Region          23..907
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 madldqqige ricfgpfclt pdarlltrhg epveiggrsf dllvvltdqp grvlskrell
       61 krvwsdvvve dgslrfhmag lrkllgdgvd garyiatqvg vgyafvapve rhggtaprrl
      121 eesvrapttn lpgrlphlig rerdvallve rvadtplfsi vgaagvgktt lavetghrla
      181 ptfadqvafv dfsmlenmav vpsmiagamg iavqsedpla vilghirdrp fllildnceh
      241 vieavagive rivegapkar vlttsreplr vrgehvlrld alsypedlag ltrdqllayp
      301 avqlfreraa aadsalmldd aaarllaemc qrldgmalpi elaavrvath gieatarqlg
      361 erfslgwsgr rtaqprqqtl qatldwsydl lsdservvle rlsifvgpfs idaalgvvag
      421 adigsdevav aidelssksl ivpdrsrrtg tyrllemtra yareklrahg dnapiaiarr
      481 haayflaele magqeegvlq darplrpqlg nirsaldwcf gregdrriav rlaaasapvf
      541 lnlshliech twstralaei tddqrgtale lelqaalgit lmftrgnsea agtalarale
      601 iatalddkwn qlrllgrlhi fhervgeyal amrhakrava vaeaigapea isvahslagi
      661 shhlagdqkn arralelslq msppssrgrt ihygfdhrnr sgialartlw lsgdaeqagr
      721 larqfvgeaa rldhplthci amiwsfsvfl wmedftaaea dlaafaecae vnalgpyiaa
      781 aagfrgeldi qrgrtedslg aleeslfrlr aaryellttp fsiaiargla aesrtgeala
      841 lidatlahce angeryaape llrlkarivr aageedagia llgqalalsr eqgarawelr
      901 aatdladppp d
//
LOCUS       WP_181600356             232 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Clostridium intestinale].
ACCESSION   WP_181600356
VERSION     WP_181600356.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 232)
  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..232
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..232
                     /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=27229
     Region          3..218
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 meriavvadi hanihalqvf mdhinkecev skilnvgdfl qigpnpvevf divmndkrfl
       61 nimgnnehvl fnrelmkfpk eevehqdwvi hklgeermdk leklpfkrii niknkkilml
      121 hsrinsiief pllyekksle efiddydenv dyvlighthl plyatnwssk nilnpgafgc
      181 gkdgivkfii meidnelvni tykqlrydkq kviddfkmnn vpygekfcei fy
//
LOCUS       WP_181600403             113 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Clostridium
            intestinale].
ACCESSION   WP_181600403
VERSION     WP_181600403.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..113
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12594
     Region          10..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvvnkelpqc pvattvgvig nkwkllilrn llsssqrftd llkgidgisk kvltenlrsl
       61 eedgiinrkt ypdevpvkve yslseigetl kpifdvltdw gngykeflnn tsk
//
LOCUS       WP_181600458             473 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Clostridium intestinale].
ACCESSION   WP_181600458
VERSION     WP_181600458.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     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=54392
     Region          230..464
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mkikltakil ismilvfqit fliygllnll iyktdisfge kiysvsfsts dfiepfieel
       61 edrndfslnd enikrlkenn vwiqvldkgn nevfkenkpd niptsyttse linfiqnpwe
      121 siapttvstk elikgnekyt llvgfpinkv fkysltftee sfryhlsmiv fgfvlvgiva
      181 yifsrnlvkp mvsviqdied lkdgiykakk nkkgvyeevs kninnlsvil kenemhrkev
      241 deakeewian ishdlktpls sikgyaellq geeydinled akryshiila ntnhiqelvn
      301 dlsliyklkn kvipisfsye nlvtilqeci idllnnsnys erevnfnfdd eniiincdkk
      361 yikraitnll vnamdhnted tvidvsvfkk dsfiniiied ngqgigeedl knifnryyrg
      421 vnssskskgs glgmaiskei itwhkgdikv qseigkgtki eiffeeiken hvk
//
LOCUS       WP_181600498             348 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Clostridium intestinale].
ACCESSION   WP_181600498
VERSION     WP_181600498.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     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=41159
     Region          1..322
                     /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 mkkerlfyld firalsmiii vifhfnctin qerllgnril pvlyangdfg qigvslffii
       61 sgaslmyaye nkfslieyfk krfiklypmf yiayfgafly lfyiskslpy vipmipkwtf
      121 iytilgidgy mintlpdyyl lgewflgcil fiyllfpilr riiikypkll fmfglvfyim
      181 vverynsvir idwnfttrif dvligmyfik yikkisvyqf ifgllisgim lyrplnitgm
      241 ykitiigial fvtlvyiaqw isnertknif ekmskysypv flvhhialgq vvlhfrgatl
      301 ryievffvli icciviglta fclnnindkl lqiffakren elsivqkk
//
LOCUS       WP_181600542             562 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Clostridium intestinale].
ACCESSION   WP_181600542
VERSION     WP_181600542.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 562)
  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 562)
  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 562)
  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 562)
  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..562
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..562
                     /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=65318
     Region          1..460
                     /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 mklskliikn frglkgdkni infdnsdiif lighndvgks tflkayefft nstqvakksd
       61 fynydennei eiigefikes dddsnkdfnk epnwinnwvd kdskkviikk vwnkaderfs
      121 kytynpndge krfvqngfgg ldtlfkkyap taifinavet pesfekkvnd ivekeylkel
      181 rekygleyde aiekinvlqk kitssdgilk ynekisksfn nvfpdlslki sqkgedgidl
      241 akafkanhsv dvvkegndrk enitqhghgi irqalfnfit flktdtrstk keylilfeep
      301 elymhpkasr alrkelyevi kdspfqilca thspimidis kphsslvriv kepdestktf
      361 qvghdifqse enkdfvqmin rfnpyvceaf yasevilveg dteaivfryl ldkyydkket
      421 diyvlntgsk nnivfyqkil thfnikhhvv hdidqpknnk ndddnsawtl nyrieeqmnk
      481 sneecgylic kryvhftnfe vahpqyklnk kkgkplcaye faknlslesd arcvnvirai
      541 vencdiddei ekiealllat le
//
LOCUS       WP_181600161             434 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SLC13 family permease [Sphingomonas].
ACCESSION   WP_181600161
VERSION     WP_181600161.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  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..434
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     Protein         1..434
                     /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=44837
     Region          61..434
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mtpdqlvtvl vlaavvaali wdkvradvva lsgaavllmt gvvrpsevqg afaspalial
       61 aslfvivyai elsglldrli elavvlcrki gvlglwitig lcgaasgfln ntpivvlsap
      121 ivrdaarklg ldpkrflipv symavlggct tligtstnll vadmarvagq ptfglfeitp
      181 vglaiagvga lylllvsgrl irlgpseegs srdveiepdm agaqvgapev fvpratlqpr
      241 raavavgvfv gviavatlni apiaaaalag avllillrvi sadeayhglr peillliagm
      301 vvlgialees glaatatnal vgfiqplgpl malalfygat lfltellsna tvavlcapva
      361 valaeslgvs prpflvavmm aasaafatpf gyqtnvlvyq mgrysymdfv rvglplnfit
      421 watgvfaith vfpf
//
LOCUS       WP_181600743             363 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Clostridium intestinale].
ACCESSION   WP_181600743
VERSION     WP_181600743.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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..363
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..363
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42311
     Region          157..279
                     /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          225..349
                     /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          249..277
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(250,253..254,257..258,260,284,287..288,291..292,
                     294..295,317,320..321,324..325,328)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..311
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          316..342
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdyrnlfkek lskllfleln kegflktini snlelknkel fvpikttyla snieneikik
       61 nlpiydfieg msfalgaddk lkfnedyiil lknikdsipc iksavakkik enlfdeayil
      121 lrgltnvtne eevweklfli getireqdkg fteifkedie ryknlnpnsh kasiyealiy
      181 ndegnnekay vyineylnsg gepeeyilsl kaeledtldy engkkliegn pnealkklip
      241 lldrfgdnps lfyyvalcyr klenyekaiy ylnesiaids sivetinemg inyasledfe
      301 naikyfrkaf eatrdieict nlimcylnsg dlkqarlhle iaekinkdde ilkeikeymk
      361 rfn
//
LOCUS       WP_181600754             245 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Clostridium
            intestinale].
ACCESSION   WP_181600754
VERSION     WP_181600754.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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 245)
  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..245
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..245
                     /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=29152
     Region          4..145
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mecykdlsyl ydkliyddin ykeisdyiin kykqyssnnl lyldlacgtg nisvhlakyf
       61 kdtflvdlse dmlieasdkm rkekvkfkil cqdmtelnln rkfnlitcvl dstnyilekn
      121 elisyfrgvy nhldnggvfi fdinscykik tilgdniysy nteeifytwe nsleddivdm
      181 yltffvkege lyrrfeehht eraydekele silrdsgfei mekhdgysde pvsekseriv
      241 yivrk
//
LOCUS       WP_181600762             434 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Clostridium intestinale].
ACCESSION   WP_181600762
VERSION     WP_181600762.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            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 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     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=49481
     Region          1..432
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mdykecmkyi hdlgkfgmnf glerterile llgnphkhlk lihvagtngk gsttsmitsv
       61 lieagykvgm ytspfleefe eriqinreni skedlvkvvm evkeiipkvi eegfhsptef
      121 eiitcvmfky fsdkkidfgv ievglggrld stnvinplvs vitsisydhm nilgndirdi
      181 akekagiike ktplvlypqv dqvteviedi aktknsniiy tqkeqvkvld fvhgehesyq
      241 iferveggkk riyelpllge hqifncntai ttieilrdnf ninisdehil sgikkvkwig
      301 rmeilkrnpf viidgahnid gikalkqnih kyfeyekmil ilgiladkqv ddmieeicle
      361 atevvavtph sdraelavdl knkienhgik tialenyeea ykyahnklgk kdilvvsgsl
      421 ymigdmrkii rkeq
//
LOCUS       WP_181600770             493 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Clostridium intestinale].
ACCESSION   WP_181600770
VERSION     WP_181600770.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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="Clostridium intestinale"
                     /db_xref="taxon:36845"
     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=56029
     Region          118..489
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrskigkkif fitfialiil vslilifqkh ffekfyinek nkalikavne yrntysftkd
       61 skeiisasmf qfekenntni siaypngsli ytapnnknyp edlfkqiynk lylpnsqfis
      121 sgkifittsd nayadatisi vicamdggsi lmavssvepi reatsvlnrf lpyfivgtlm
      181 valfysmils kyigdplikl nkiakkmsnm dfserytple ddeinnlgtt lnflsenles
      241 altelksknd ilqeeveher kieemrkgfi advshelktp igiiegyaeg irdgivqgea
      301 kndylniiid eahkmnklvm dmlelsklqs gnvkpnietf niirmiqgsl rkynvlirek
      361 slevvfnpef eylyvegdtf qieqvlsnfm tnaikytpss ekivisiekl eskvlisien
      421 lgaqiskdel dniwnkfyki dksrvrdkns sglglsitkg ildlhnssyg iqntsngvls
      481 yftlnlsadd ile
//
LOCUS       WP_181600810             355 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Clostridium
            intestinale].
ACCESSION   WP_181600810
VERSION     WP_181600810.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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..355
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..355
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40440
     Region          3..354
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrdldklnki idekeekqef sgvvlisekg ekifrkacgy anrgwsiknt ldtrfriasv
       61 skmftsvail qliekgeldf etkvveyldl rdtkisnevt venllthtsg igdyfdeslg
      121 deewekmwrd fpiykmrrnl dylplfinkd qinkpgekyh yngagyillg liiekasgis
      181 yfdyirknif kkadmkdsdf lsldkvcdrv aegyevirds nkniiglekn iytstpdgaa
      241 dggatstayd lvkfilslrn ntllgekmsk eifkpkviye eangargytw mygygnsfvl
      301 diegkniirc ghtgeeygvs crlyyypekd itvvilanqg wcagtlgwdi hnalg
//
LOCUS       WP_181600876             145 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Clostridium intestinale].
ACCESSION   WP_181600876
VERSION     WP_181600876.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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 10140351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     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=17111
     Region          19..136
                     /region_name="NUDIX_RppH"
                     /note="RNA pyrophosphohydrolase; cd04665"
                     /db_xref="CDD:467550"
ORIGIN      
        1 mmevkfheln sikdekimfa vimakykdkw ifvkhkdret weipgghree dedimftarr
       61 elfeetgaet ysmvpvciys vkkddgesfg qlfyaeveti gdlpdyeisq veffetmpke
      121 ltyqliqpkl fnyikklkln megvn
//
LOCUS       WP_181601236             494 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Clostridium
            intestinale].
ACCESSION   WP_181601236
VERSION     WP_181601236.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 494)
  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 494)
  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..494
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..494
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=55852
     Region          355..>492
                     /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 mgeyreitrg qlfirmminp ifivvywfsf ynlytlckfg rmnnnltmll lclaffviyl
       61 iifiarsikk pitikpgrfi knrnirltyg vialififsl fifyggkiyk tsinfngkls
      121 wilkdlkdkk tvelkhnniy edgiegilqd inkkvpmaqk lyiannvdlk fdkegtitsf
      181 dtflygenkk gkletylisy nktksskimi yihgnansdf sedkllepfi ntmkvipike
      241 tiskwdenqy gilysgkrsf gyngsgvlyi dsegktrsvr nrdpeiigya vsvyvpgken
      301 tltpyryilv ddlnnikset lnkgskdlpk eesngvdkfy lsektgyrle vtdaaagsra
      361 yalektldgg tkwslvngdp flgnigtagg ivflddrlgf lclahsggar gelyrtedgg
      421 ttftkisfpe vkvplngaep ynpfdlpgmp tkegenlnil vgqgsdgdyn ggikalyksk
      481 dqgkiweyvk edkn
//
LOCUS       WP_181601075             288 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA 2-thiocytidine biosynthesis TtcA family protein [Clostridium
            intestinale].
ACCESSION   WP_181601075
VERSION     WP_181601075.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 288)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..288
                     /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]"
                     /calculated_mol_wt=32972
     Region          46..231
                     /region_name="TtcA-like"
                     /note="tRNA-cytidine(32) 2-sulfurtransferase and similar
                     proteins; cd24138"
                     /db_xref="CDD:467514"
ORIGIN      
        1 msktagegce ilvpfnerkp ldeierslik kyrkkiwtkf vkavkdyklv eegdkiavai
       61 sggkdsmlma klfqelkkhg qvnfelefia mdpgyhenik ellidnckhl nipvqiyesg
      121 ifdvvdriaq eypcymcarm rrgslyskaq elgcnklalg hhfndviett mlnvlyagnf
      181 ktmlpklkak nfegielirp myyieeqsiq nftqssgiwp lncacmvaak ktgnkryeik
      241 elietlkknf envdksifka aenvamdsil gwekdgvkhs fldafeee
//
LOCUS       WP_181601048             357 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Clostridium
            intestinale].
ACCESSION   WP_181601048
VERSION     WP_181601048.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 357)
  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..357
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..357
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40802
     Region          1..357
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 minvtktylp nldkyknyve kifesgwltn ngqfvkllqe rleaylgveh vilvsngtla
       61 lqvaykalel tgdvittpfs fvattstliw enlnpifvdi dketfnidsn kiessitert
      121 saivpvhvfg npcdvekise vatknnlkvi ydashafnik ykndsilnyg distlsfhst
      181 kifhtiegga iivknhklye kiklminfgi sgpdrveclg inckmnefqa amglcilddm
      241 dsilksreev ssyyrnnlsk klkmqkhedy vtqnysyfpv vfesekilvk ikeqlnnndi
      301 fprryfypsl dtlsyinndk slpisfdlan rilclpiyes myhdeldkiv kiinssl
//
LOCUS       WP_181601166             150 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Clostridium intestinale].
ACCESSION   WP_181601166
VERSION     WP_181601166.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 150)
  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 150)
  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..150
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..150
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=15676
     Region          22..150
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 minedmvkki tsdlvsslkp nkltldiakk lldkaenkak einvpvvial vdeggnliaq
       61 hkmddallis vslslnkayt svatkmsten lselilpgkp lytlenikni savgggipii
      121 isgsivgaig vsggsveedi liaktaleei
//
LOCUS       WP_181601521             428 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Clostridium intestinale].
ACCESSION   WP_181601521
VERSION     WP_181601521.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 428)
  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..428
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..428
                     /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=48645
     Region          161..414
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mfkkeitlil tiiagvmpli mhpftddsyy lpktvflyvm yfllifillr drknirldkn
       61 drvliiylgi allstifsik pmvsifgtei ryegvimllf ygltyycgkn yldidkkvil
      121 avllpavvis iysifqfyni dpipkdsyha rmlfnsigtq ghrnflsayi slflpctivl
      181 yilkgkkvyi giaavlftsl lctltrsgwi afiaysllga iyiiinfnkk yliralilmi
      241 afigifgild ytsgekissr sdqliydtks asgdllrngk itnealgsar vyiwkvalkt
      301 ieknpligsg tdtfrysiek yfpedgqdyi dvygaiidka hneflqiaat mgipalivyl
      361 vfiflslknn iknmwkskin fiisitfigy liqsffnisv invaplfwmg lglaqnskvl
      421 ekaeklir
//
LOCUS       WP_181601525             299 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Clostridium
            intestinale].
ACCESSION   WP_181601525
VERSION     WP_181601525.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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..299
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..299
                     /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=34989
     Region          21..291
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mdfknvefld dkvilkecrn fnikqtfecg qcfrwektkd ntyigvvygk vieleqkedt
       61 iiihntnked feniwidyfd lerdygsike elskdellnk aveygygirl lnqdpfelvv
      121 sfiisarnsi pvimktikki serwgkeley kgntyyafpt pselrkasld eirdtgasfr
      181 skyivdtvek vneaieagnd sefsldrikn lsddechvel qkfqgvgakv adcimlfsmr
      241 kyssfpvdvw vkramqhfyl apdvslpkir ifardkfkel sgfaqqylfy yarennikl
//
LOCUS       WP_181601188             320 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Clostridium intestinale].
ACCESSION   WP_181601188
VERSION     WP_181601188.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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..320
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..320
                     /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=37235
     Region          2..275
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mkfylapmeg itgyiyrnsy erifgnidky fapfitpnks rslktkelrd ilpennkgin
       61 mvpqiltnds egfietsmkf kqlgynevnl nlgcpagtvv sknrgsgfla kreeldrfld
      121 difkiddmki siktrigkds peefyeliki ynkypmeeli ihprtredfy gnkpnlevfk
      181 dalslstnti cyngdiftke dynkftkefq tvdkvmigrg vlanpclinl ikdnstldka
      241 dlkdfhdeif nnyieifnee knaifrmkel wgymiyifsd nkkygkkikk aqklaeynea
      301 vlslfeeqei iqgaglfynq
//
LOCUS       WP_181600450             400 aa            linear   BCT 28-DEC-2024
DEFINITION  cation:proton antiporter [Clostridium intestinale].
ACCESSION   WP_181600450
VERSION     WP_181600450.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 400)
  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 400)
  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 400)
  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 400)
  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 400)
  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..400
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..400
                     /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=42126
     Region          16..>382
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 matslaiiil lgilantlft klkmpgllgm lilgvilgpy gfnllqpdil nasadfrkia
       61 liiillragf gvsvedlkkv gktaikmsci pgliegffia fastkflgfs fiqggllgfi
      121 iaavspavvv pqminfienk igtkkgiptl ilagasiddv faitifttfl glysgshvni
      181 gvkllgipvs ivlgiaagai igfimvwafr kyhirdtkkl llivgtaiml talenllknk
      241 veiagllgvm tigfiilekm pkvgkrlsak lnkvwvfaei llfvlvgaqv ninvavnaga
      301 mgivvifigl vgrsigviis vlgtdfnwke rifcvisyip katvqaamga iplsmgvqsg
      361 dvilaiavls iiitaplgai aistssrsll dveddkikaa
//
LOCUS       WP_181601616             269 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Clostridium intestinale].
ACCESSION   WP_181601616
VERSION     WP_181601616.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 269)
  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 269)
  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..269
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..269
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29984
     Region          6..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..37,75,79..80,83..84,115,119,126,
                     129..130,135,158,162..163,165..167,169..170,173..174,
                     177..178,203..204,206..208,210..212,214..215,217..218,222,
                     225..226,232,234)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(161,165,168..169,171..172,217,220..221,223..228,
                     231..233,237,239)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(182..189,205,208..209,212)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mikditigqy vpgdsfihkl dprtkiisal lfivslfiin efigyifvva fiasaiissk
       61 vsprfyfkgi kpvmtliiit ailnifmikg tndtllfswk fikvyeegin iaifmtlrll
      121 fliigtsilt lttspieltd alerllkplg vigissheva mmmtialrfi ptlidetdki
      181 mkaqkargad fdggnifqka kslipllvpl fissfkrade lamamearcy rggdgrtrmk
      241 qlkytsidtl ayfivamliv isigvrill
//
LOCUS       WP_181601655             232 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Clostridium intestinale].
ACCESSION   WP_181601655
VERSION     WP_181601655.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 232)
  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..232
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..232
                     /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=26220
     Region          2..216
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mriavisdih gniyalmkvl eeidsenidf imclgdlvgy gphpnevial mkrkripclk
       61 gnydasvvdn eysyirntsi nsfslpwtvd elrasnshyl nnlplsmsme fegkkitfvh
      121 gsprkineyl lqdgentkei metfdgdilv cahthipsyk efvdklfing gsvgkpkign
      181 pnatyailel engskptvkf kevpyeykri ikdmeilkfp sqlictfetg ne
//
LOCUS       WP_181601984             404 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Clostridium intestinale].
ACCESSION   WP_181601984
VERSION     WP_181601984.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..404
                     /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=45478
     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 mktigdnpiw tsvnpisyhy pslnenidcd vvivgggisg alccyyfaka giktvllesn
       61 ilgysssscs tsilqyeids nisglssqlg kekafeafae tlqafndlkd iinelnidcd
      121 fkavpsllyt nkpthsqair neynlrksag fdvqyidfnn srdyfpfpiy sgilshegsg
      181 ivdpyklina lirnafdnga kvfehtpvdn ikslytgvli ntpkakinak kviiatgyea
      241 iedyhipnqn ltrsftistt kflneneevw yknsivrdms dpytylrptv dgriligged
      301 idnleyndel nskkylilek rlrellcspk dfkiefqfng vfddtndslp iigenqdypn
      361 hyfclgygsn gilystfgak mlldlylnqn ashldlfefs rnti
//
LOCUS       WP_181601888             318 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Clostridium intestinale].
ACCESSION   WP_181601888
VERSION     WP_181601888.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..318
                     /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=36257
     Region          45..308
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mkrfrvliii avilvigiia tlfiknqnsp vnkdiktaei pdvdlsfgvf gdvhenvdsf
       61 qkaindmyti npginalvln gdsvdqgiek qyesmkkiid knkdllpnki iknignheff
      121 nynievnske qvqlfinryl dfagedkvyh dtwvnnyhfi slgsedgnse tlnsvkayis
      181 peqqmwlkek ladkyekgkp ifvflhqhls sgknggwvgs dqadevrqil dkypevilft
      241 shthrdltes svvlyqpftt ihtgaihyti ipdenseggr rnepyikgly vevngnkvtv
      301 kgrdfkekqw ifskdisk
//
LOCUS       WP_181601515             254 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Clostridium intestinale].
ACCESSION   WP_181601515
VERSION     WP_181601515.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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..254
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..254
                     /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=28175
     Region          4..253
                     /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 mntvisifvf lygiiigsfl nvciyripkg esiayppshc sncnnklgwk dlfpvfsflf
       61 lkgkcrycwe kisiqyplve lvngllylsl lfkfgfgvkf iliclfisli lvigiidykt
      121 qdiydntiyv gvvlgvlyig vekylggvsp fnyilgavia agilaliait tkamgwgdve
      181 lvfiiglflg wpnallmlfi sivlggivgg llllikyksi gghymafgpy ialagyitlm
      241 ygneilnwyl kmfi
//
LOCUS       WP_181602462             322 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Clostridium
            intestinale].
ACCESSION   WP_181602462
VERSION     WP_181602462.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..322
                     /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=37384
     Region          <239..320
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdeykdsswd aladkynllk kpygegqiyd fpphwsngwi aelnpakgly vssawltpse
       61 qivhtinssk pfmiifcvdc gdiiyshqgk krqtlspith viinpqkqft ltflkdvhyc
      121 ftsvlifddf ikpflkdrtt apkisvqdak lwktqhynsp dimlileqir wavrnadmpl
      181 lafegmtlhl lssitrnfpd ipkrrssrrh yvtweneqki yqvknkided ilnppdtiel
      241 criagmsesk lretfknhys vplykyirie tmkramqlls ddhlsirnis elcgyknpak
      301 faaafkdvhg itpsdfrksf nl
//
LOCUS       WP_181602541             360 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Clostridium intestinale].
ACCESSION   WP_181602541
VERSION     WP_181602541.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..360
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..360
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42535
     Region          58..342
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mmlvdifkef invvqenkky tigllneegi vvscsrekfv gecfnvdssd lnnvfyairi
       61 krenygyiwv rgedenlkmi ssllldsltt rlmyeinnss lkqkvtkdde likfllneeq
      121 fdlnnildli nrlgidenkt raaiyiinqk ghnleeimrl klradskqmi ysllnkrsll
      181 lfkdmpsgld nteakrffkk yirslqdwgl qgcyyivgsv qdklkqysvs yknclwlekn
      241 inyevdepif ftdylfeyfv skihlddvrn ifdfyndrgk gidideftni ankllindyn
      301 itqtaddlfl hkntliyklk kyeqifnidi rgdfkgkflm vliantlrey qrqkqvgeki
//
LOCUS       WP_181602560             455 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Clostridium
            intestinale].
ACCESSION   WP_181602560
VERSION     WP_181602560.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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="Clostridium intestinale"
                     /db_xref="taxon:36845"
     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=48345
     Region          1..451
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 menltqlfsk iddlvwgppl lilligtgvy ltiklgllqi fklplafkyl fskdedydgd
       61 gdissfaalc talaatigtg nivgvatala aggpgalfwm wvaalfgmat kyaegllaik
      121 yrvvdkngqm sggpmyyiek glgikwlaka faffgicval lgmgtftqvn sissainitf
      181 kvpqfatial ltiivgliti ggikkiskaa elivpfmaif yvlgaliili tnisklpeai
      241 slivrsafsp saafggalgv tiltsmqkgi argvfsnesg lgsapiaaaa aktkscvrqg
      301 lismtgtfid tiivctmtgl tlvitgmwns teysgaqvtt eafkagfgnf pmigqfivti
      361 gliffaftti igwnyygerc teylfgvkgi lpykiiflva iassifmkle liwiiadivn
      421 glmalpnlvg liglrkviig ettsyfnqik lnkaa
//
LOCUS       WP_181602959             285 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Clostridium intestinale].
ACCESSION   WP_181602959
VERSION     WP_181602959.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 285)
  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..285
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..285
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30724
     Region          48..270
                     /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 mkrgykkllv ilalissvsv magcggksta tsggkkdtla tikekgvltv assndapfaf
       61 idaktnefsg idaeiikeia krlginkvem kqipfenllv elnnnsvdmv tdgmyvkeer
      121 kklalftniw ykegeaivip kdskvsskad lknlvlggqk gtafletaqk wqqagqvkev
      181 kvfgsqselm lavntgkida citdgmvagy tlsqdsslsl kilspyepea sgmvaaavrk
      241 ddtsladavn ekldemkkdg tvlkllekyg mnkdyfvsve dgqsk
//
LOCUS       WP_181602100             169 aa            linear   BCT 28-DEC-2024
DEFINITION  deoxycytidylate deaminase [Clostridium intestinale].
ACCESSION   WP_181602100
VERSION     WP_181602100.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 169)
  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..169
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..169
                     /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=18842
     Region          5..156
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
ORIGIN      
        1 mgdtkrenyi swdeyfmgia lisslrskdp ntqvgscivn sdnkiigigy nglpkgcsdd
       61 dfpwgnsgdf lqtkypytch aelnailnsi gtslenckiy ttlfpcnect kaliqvgikd
      121 iiylsdkysd tdivkaskrm lntanvtftk feasrkdlli sfenmedkk
//
LOCUS       WP_181603136             114 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Clostridium
            intestinale].
ACCESSION   WP_181603136
VERSION     WP_181603136.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..114
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13110
     Region          7..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mifkgieync smeltldiig gkwkpiiiwh lgketmrfne lkrklpnith kmlsqqlkal
       61 eennlivrkv yaeippkvey sltdqgesll pilitlcewa tnhvdsiqve esec
//
LOCUS       WP_181603185             289 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Clostridium intestinale].
ACCESSION   WP_181603185
VERSION     WP_181603185.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 289)
  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..289
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..289
                     /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=32688
     Region          1..280
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mrfivfgdsk gkenginkkv lhslmkessk lypspefilv cgdsvaggsk eetlaiqlmd
       61 frdiiskyhp nkslfpvign hevniepedd rfeqvldqfy rnltptyaln gynntvycvd
      121 fddtrlmiln sfhpsalhki dkvqlnwfks masvpsknkl vfihspafpt gahlghsldl
      181 ypedrnefwd ivdkcnidiv fsghehnysr rvidssfseg gftyqnkvpq iisggggekl
      241 rnkykskkgi vvapvavyhf lvvdideysi kvsaitskgk kidefeikk
//
LOCUS       WP_181603195             354 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Clostridium intestinale].
ACCESSION   WP_181603195
VERSION     WP_181603195.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 354)
  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 354)
  AUTHORS   Rosinski,J.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..354
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..354
                     /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=41952
     Region          263..351
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkydirkdin iykeildliy icineeyeik nrldnyeksg vdykvfekky cdninkyiks
       61 fkklikinke dadfyftsei dlvygigqil ltdfeleelg niienidfls ieflrdklik
      121 aleetfelen reglkiesls hyinfinkln isenikwrfv kiyddpkfyy ekllkiisnn
      181 yvaftkayee vkddvrdfik ylldnaetnf kllddkygik iqentiiyps vvrnrfieat
      241 ylakrnviyy gilfnksmef ldsnkldnen llqflkaisd kskfeiikll kskemygqel
      301 aakldlstat vshhmnallv tnivkvkren gksyfylnge sikkflkelg dnii
//
LOCUS       WP_181603235             592 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Clostridium intestinale].
ACCESSION   WP_181603235
VERSION     WP_181603235.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 592)
  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 592)
  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..592
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..592
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=68608
     Region          <137..411
                     /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          316..547
                     /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          348..374
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(350..351,354..355,357,381,385..386,389..390,
                     392..393,416,419..420,423..424)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          379..410
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          449..479
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          518..547
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdnfkenlym ikdkckklik tlyskynkaa ekwsflkskt fvgivvavlc ivifstvanl
       61 kkgrltiann kaetlfyerd fenslveykk iqeddkwpiw tvkmaevhsv krdyeqsnnl
      121 lkeamekrde lmvsktekli ekdkefinhv vftyfmnkdy ddalkigeef ldtyegykpl
      181 iktmytvymv ngeknkaeel vkeypvdees aydiavlakm qmilndwdkg ldtlkeawnk
      241 dkdeqkvfdi iaqeaaynkn fileklverv skepeelayk mwiakvysms svsadmadky
      301 lqeldgkdvg kvnikiikak nyenlgesek aaallgeitk enknsyiayh teawnyyekg
      361 eydkalemad ksilankdyp dnygflipdv mmkkgnteea epyfrtallk epfnfnimvk
      421 iadfywytak dsnaayeyfn laslvkpmds evnynmamik ltnnemesav dllkksisln
      481 eaipkyhrtl gtvymnkeky teaitevrya ysadkadplt lnnagcfyis ingdldrgmi
      541 nlkaaldgkd sindeeikka iednynkakn lydefqketg asipvpeftl fy
//
LOCUS       WP_181603367             126 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Clostridium intestinale].
ACCESSION   WP_181603367
VERSION     WP_181603367.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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   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..126
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..126
                     /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=14040
     Region          2..126
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mkytkatnya lhimaylikq egkenlslip lanhmnipst ylskiltqlv kadlvqstpg
       61 vnggyslrks kseisfydvi qaiegsgalf tcemgennac rienvmreae dkmvkhlkek
      121 lifdii
//
LOCUS       WP_181603404             153 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Clostridium
            intestinale].
ACCESSION   WP_181603404
VERSION     WP_181603404.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..153
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16956
     Region          17..67
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     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 mtrgikgmne tcvnyyktcr enagltqaka sellgvsers isdyennktk vpdeivdrma
       61 mayntpllaw whiknssvlg kylpeiitpq tnvdmafqti laqdeldpav tslkkimsdg
      121 iisederlef hssiniinnv agklisvvtf akd
//
LOCUS       WP_181603407             331 aa            linear   BCT 28-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Clostridium intestinale].
ACCESSION   WP_181603407
VERSION     WP_181603407.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 331)
  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 331)
  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 331)
  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..331
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..331
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38250
     Region          16..>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 mflqglsekv nsfdakdkfs lleinielle pssnnfygir eidelsesik eqgllhnlvv
       61 rekegkyeil sgerryhalk klgvkkvpck vqrnlsdids evllieanar treltpsefm
      121 rgisrleeiy kdkksngeqi egktreaigk vlgksgtqvg ryqkinkkls edlkedldkd
      181 kltvtqaeii snlkpqeqke iakqiknldp keskeeisil iegikqpvek krdkellkei
      241 ypepkpkdkk hkttkfafen keqlqtiqel cedmvrtlks mlpkkgqkwt efdhevkgqy
      301 dafdlmritl rdygysdglv femplidsee d
//
LOCUS       WP_181603382             407 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidase U32 family protein [Clostridium intestinale].
ACCESSION   WP_181603382
VERSION     WP_181603382.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            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 10787090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..407
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=46364
     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          323..401
                     /region_name="Peptidase_U32_C"
                     /note="Peptidase family U32 C-terminal domain; pfam16325"
                     /db_xref="CDD:465094"
ORIGIN      
        1 mripellapa gsleklktai dygadavylg gnklnlrafa dnftneqike gveyahkrgk
       61 kvymtlnvip hngdlygled ylkeiyslev daiivadpgi iatarevvpe leihlstqan
      121 ntnwrsakfw ydqgvkrivl areltmkein dvrekipegc eieafihgsm cmsysgrcvm
      181 snymtgrdsn rgacaqpcry kyylveekrp geyfpiiedd kgsyimnskd lcmiehipel
      241 mesgiysfki egrmkssyyv aaivksyrqa idaylenpeg yelkqswvdn llkvshrsyh
      301 tgfyfnepnk qvydtssyvr dydivgvvke ydevnkiati eqrnrvfegd kvevlgpvge
      361 nyeivlsdmh dgkgekieva praqmifsik vdaplkvkdm likgkdn
//
LOCUS       WP_181601702             240 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Clostridium intestinale].
ACCESSION   WP_181601702
VERSION     WP_181601702.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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="Clostridium intestinale"
                     /db_xref="taxon:36845"
     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=28158
     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 mgnkkieisi cddesiiqna vkklcekyld ehnmdyriel fdngtrliny egdinilfld
       61 vempgingfq vakelnnkhn nifiifitsh snmikeafkv kafrylykpl dheeffeaie
      121 eaikeftesh siivkqrees iliekkdily ieslgegsai htrennyvtt sslkkwreel
      181 gdrhffqchk sfivnfqnvi kiesghfllk nnkeapvsir nrkvakdrfi eyisqnaryv
//
LOCUS       WP_181603761             150 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Clostridium intestinale].
ACCESSION   WP_181603761
VERSION     WP_181603761.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 150)
  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 150)
  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 150)
  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 150)
  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..150
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..150
                     /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=17520
     Region          73..148
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mreedsrysk enitvadfnd evlgaivmip yedldkltir tdfrvinwve glrdklyflm
       61 krvnyirfre ckkgdlyvsn iatssrargl gigkalmkya eqtakkeeyn gvsllakneq
      121 vskfyekldy kkiydkitfg eriikmakfv
//
LOCUS       WP_181603770             637 aa            linear   BCT 28-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Clostridium intestinale].
ACCESSION   WP_181603770
VERSION     WP_181603770.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 637)
  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 637)
  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 637)
  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 637)
  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 637)
  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..637
                     /organism="Clostridium intestinale"
                     /db_xref="taxon:36845"
     Protein         1..637
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=71580
     Region          116..239
                     /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          283..567
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(287,289..292,312..313,339..341,362..364,366,381,404,
                     420,443..446,449..450)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(313,315,319,323,337..340,343,346,364..367,370,374,
                     377,380,450..451,456)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(366,406..408,416,444..445,451..453,456..457,
                     468..470,474,476,511,538,541)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(382,406,416,420)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mkryknlilm iidialinla ylsafffrfi dgqnieyfpn ythnivfitl iyigvffifk
       61 fykslwiyas idefmllicg cvianilsit lgkifdfelp yglsivsgmi atiyilafri
      121 sfrvyrrivt nlaninkigf krvmiigags agnmivneik rrpemklepv aliddskykq
      181 gtfiagvkvf ggskdierta klkaveeiii aipslkgedk kelidivkrt gckmkiipgv
      241 yeliqgkvis sqirevqved llgrdpvvld negisdyitg ktvlvtgggg sigselcrqi
      301 skyepkrlli ldiyennayd lqnelkvkfp kldlkiiias vrdrkrveki feefkpevvf
      361 haaahkhvpl mednpseaik nnvfgtlnva ecadrggvkr fvlistdkav nptnvmgask
      421 rmcemiiqai nkqsktefva vrfgnvlgsn gsviplfkkq iesggpvtlt nknitryfmt
      481 ipeasqlvlq agayakggei fvldmgkavr iydlacdlir lsgfepykdi kievtglrpg
      541 eklyeellma eeglgstkhe kifvgsptft dmnmlkkgfd efrfiiengd kedlirkvee
      601 lvptykrtpn dvvsneeqee taadeidvfr nnvitvv
//
LOCUS       WP_181603773             355 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Clostridium intestinale].
ACCESSION   WP_181603773
VERSION     WP_181603773.1
KEYWORDS    RefSeq.
SOURCE      Clostridium intestinale
  ORGANISM  Clostridium intestinale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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="Clostridium intestinale"
                     /db_xref="taxon:36845"
     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=37746
     Region          14..355
                     /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 mnikplqign lvsklpiiqg gmgvgvsssk laaavanagg igiisgaqig ydqedfytnn
       61 leanlralkk hiktakenal ngvigvnlmv amkqydehvk aaieagvdli isgaglptal
      121 pklakgfnvk lapivsslka cnvilklwdk hhgvapdaiv vegpkagghl gfskeelidd
      181 nidfdkiivd iveavkvyed kynksipvia aggiftgydi akylqlgasg vqmatrfvtt
      241 eecdahinfk naylsssred igivkspagm pgraiknpfm kkvelegskv tkcyacltpc
      301 npattpycit ealinsvkgd vdnglifcge nayrldkivk vqelmdslet eilea
//
LOCUS       WP_181603812             363 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Citrobacter sp. RHBSTW-00599].
ACCESSION   WP_181603812
VERSION     WP_181603812.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00599
  ORGANISM  Citrobacter sp. RHBSTW-00599
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Citrobacter sp. RHBSTW-00599"
                     /db_xref="taxon:2742657"
     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=41086
     Region          4..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 mtvaerksld yiqalrgiaa mlvvlchard flrhsplenl aydlfwpgaf gvdlffiisg
       61 fiiiytsidy dkkdtfkfir krflrvwply fictiayial vngfdfsgmk gfyynqngsp
      121 fdilniiksl lfiplnldsp iylgpptlfv gwtlnyevyf yvicaigiac grfrytfyii
      181 wfsvtllaip aiiggvnfdr pkiigagyln ltmqsiiwef ifgavvaily krgalsisks
      241 siaipviilg isvpvyayvt kidaghgiah sgkffcfmfl cltscadyiq knikipslii
      301 sigdasysly lihplvfmlc ykiasyfidw smmssfwfig vvfiasilas nisykyieck
      361 ipk
//
LOCUS       WP_181603881              72 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter sp.
            RHBSTW-00599].
ACCESSION   WP_181603881
VERSION     WP_181603881.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00599
  ORGANISM  Citrobacter sp. RHBSTW-00599
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..72
                     /organism="Citrobacter sp. RHBSTW-00599"
                     /db_xref="taxon:2742657"
     Protein         1..72
                     /product="helix-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=8594
     Region          10..71
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mnnlptpdtd lmndklvdmv fittftgltd kwfyklikdg mfprpikfgr ssrwresdvr
       61 rwvmehiees rk
//
LOCUS       WP_181603918             427 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Citrobacter sp. RHBSTW-00599].
ACCESSION   WP_181603918
VERSION     WP_181603918.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00599
  ORGANISM  Citrobacter sp. RHBSTW-00599
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHBSTW-00599"
                     /db_xref="taxon:2742657"
     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=47392
     Region          178..415
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mlrqhmfsrf icsiknnpfd fiyflfyagi latlamvlvn pdealkvfif stalslpllg
       61 knikhvcsnk qnlvlpfmll lfgllqiiwv eifkqpgsaf tgayrsyqng gkvmifaalv
      121 mtiltsqaps ankirltsiw viltaiglyl fagyqlsgaq nplryrvalg fehqtgtays
      181 ltliallasq aiinlrlrht vslyllhfli slaviittqt raailvypll siglffihyr
      241 hnhnillral lgfvilvgia aiplkpvies ryqnflidlh synqnnsnts igarlamqra
      301 gieagkghhw gqsleqrgae iqrlavqdts lqgtlkfinv hlhneiidtf slkgisgviv
      361 llllytamfl raywqrspll fvisgaiaiy glsdlllyak gealssmlal ciaavlssnp
      421 trescye
//
LOCUS       WP_181604093             107 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Citrobacter].
ACCESSION   WP_181604093
VERSION     WP_181604093.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=11596
     Region          2..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mqleevakal kelghptrlf ifkhlvkage qglpvgdlqk qlgipastls hhisalvsvg
       61 lvkqnresrt lmcvsqyeil eaiieflree ccvnsktdaa esagrng
//
LOCUS       WP_181604122             275 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604122
VERSION     WP_181604122.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 275)
  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..275
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..275
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31395
     Region          31..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 mlsllisfal sfpvhaqvkl repsscekry vlafldaapg fyknekgike gssydilmev
       61 grrlgckvse epgsysaile gfvrhrvdit glttkspkme nfgefvemyr vprslvvrkd
      121 sfgvndsies ilknpkiifa giigglffik esekeqlfke rrlrevpgpq evfnalsegr
      181 vqatfsspaf tayylkrqnk ldqfkiipde kgewqslgfy lsikrlskee reriraiisn
      241 vrqdgtllni ekkyvtpady lyyepitlkd ishie
//
LOCUS       WP_181604138             353 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604138
VERSION     WP_181604138.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..353
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40033
     Region          14..342
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkfsvleknl ilqledrird ttpgvmvray qggriicdva vgntyayydf asvtkviftq
       61 qammyayelg kwnfetkvsq flpwfpstet kitellthss glpwwlpfyq einmnlsmek
      121 rrdqlrdiik glklekseta vysdvgflvl gyilevifek plldvwtdtk nkfyagttle
      181 fhannttstk islfapteec pvrkklvqge vhdlnawsfg gvsthaglfg siddlgwysl
      241 hlrsqllgia rysirqktaq lfakralpeg kgdwamgymm ptpgsascgs yfsldsight
      301 gftgtsiwyd pkmdmsvnil snrvlygsen kafaklrsei hnwivenyrr sgv
//
LOCUS       WP_181604252             341 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604252
VERSION     WP_181604252.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     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=38063
     Region          1..341
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mnrgfgsdnh agvhpriles lakanvehap sygtdewteq avgafrshfg eqsqvffvfn
       61 gtaanvtalr aitrpwqsvl cadvshinmd ecgapeqmgg fklqtvptvn gklsvealen
      121 qfirrgdqhf sqaavlsitq ptelgtvytl eelrsliswa rerklfvhid garlsnaavs
      181 lclgfkeftt dlgvdvvsfg gtknglmmge aviflnkala hdfkyvrkqs sqlpsksrfi
      241 acqfieyfkn dlwkdiagns leraqelyea irdvpgvgvr tkptsnavfa tipaawvkpl
      301 rekfffyvwd ektfecrwmt swdtqssdvq nfanaikels r
//
LOCUS       WP_181604265             428 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604265
VERSION     WP_181604265.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 428)
  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..428
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..428
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=49411
     Region          13..68
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 msnelieids kalrnllkhh qmsqydlavr ldistktiqr wmnqsirrvk petieklmev
       61 lgptageikr dspalslrpt dkavaelcse rsfqsirltd dwnryleilk sihtealpse
      121 qcfvisrnig issfylgkfq aakiylskam kyaellqnen hmgdvrnwfa rldeavgnlf
      181 kaddylnqnl qnlekitrps vlaeysyvrg rvhlhrwqna eaevqlrrgl lttlktrskp
      241 ypllaawmyl hlvhlylrtk nlpkaqacgr rflktaersg wgrgillgny ylgiiakfkn
      301 gpttlsaqyf gkarlmhkct lvdrycplls qaeflyfilk gryaeartil ahrlyktrra
      361 efylasttid glllsklnpg shgirksmit kakeyyqaqg iqyplaliek legrnevapq
      421 eiaefyyy
//
LOCUS       WP_181604398             202 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Bdellovibrio sp. KM01].
ACCESSION   WP_181604398
VERSION     WP_181604398.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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 11428160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..202
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22586
     Region          11..199
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mlnsffpnhd fkallfdfdg tvadtmpahl gawnkalaky slslsreqhq awagrpthri
       61 vemmnelhka tidpqqflae kevhylsslh evktitsvmd vithyhgkvp maivtgsrrk
      121 ivdltmkqln lhsyfdllvc aedytqgkpa pdcfliaask lniapaeclv fedavlgmqa
      181 ahsagmkclm vdeqysltht rk
//
LOCUS       WP_181604121             273 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604121
VERSION     WP_181604121.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..273
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31147
     Region          40..262
                     /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 msrlfalllv vltplisqaq dgftpvggsc ekryvlsfqd dapgffvdkn nkkngtayel
       61 lleivrrlgc ksteqitpyl kikenflrnk sdiyalstqd kemdkvadfv emysfprslv
      121 vnkkdfsekd nvasllknpk ivfgnvtggf lfiqpqerae levrhrlref pgptsvfnal
      181 legriqatfs spaftyyfit rekkmeqfra ipdpkgglyh agfylarrrl tdaerakire
      241 iirqiradgt llkiaskyvn pedliyykpi gsf
//
LOCUS       WP_181604621             485 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Bdellovibrio sp. KM01].
ACCESSION   WP_181604621
VERSION     WP_181604621.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 sp. KM01"
                     /db_xref="taxon:2748865"
     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=54090
     Region          8..475
                     /region_name="PRK10337"
                     /note="sensor protein QseC; Provisional"
                     /db_xref="CDD:182388"
     Region          248..482
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mflkslrkff anlslrvrls lifvvffgat tilfnmfifk msidnlqqdf ddalfnysvd
       61 vsegveigvk gdlnfpplrl dhgkilpfpl gtaliqvrhs sgavlarvgn fgefnppykk
      121 dferiwagee atyrtiehih nipsaeadsy rlisfpldnv akpqlllqia vpmtlletqi
      181 skrltllevg ipivllfatl gglflsaral apvnhmidia kkikaselss rvpipaande
      241 ikklaltlne mldrieqafq sqerfvadas hqlltpltim rqeiellkse kqidvdqytr
      301 salqevdnla nivqemllla radaglgals lqeisleelv fealtrcekl anskgiklkf
      361 ninneskadr ksvrgdkdll enlvfniien aikyspnnev vtitlvwkdd vsqlfvqdng
      421 pgipddklpf iferfsrgaa venrvkgfgl glaiaqkian lheaklsagn nerngaifsf
      481 eikni
//
LOCUS       WP_181604517             440 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Bdellovibrio
            sp. KM01].
ACCESSION   WP_181604517
VERSION     WP_181604517.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 440)
  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..440
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..440
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49295
     Region          9..370
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtlktkafrf fykahiylgl fvavhfifls isgsillfke evegsvhdav avtadqtsms
       61 ystllsdvlk kfpgerplav fkddeheniv nvrlgmndsk mfrgarklmf dshtgaelna
      121 eagkssfmdw mlklhreffl gsygkiyvgf igllyffvml sgffiygnfa kkvafgevri
      181 ksprhwfsdm hryigigvfa wgliigatgf flgisstlik vyqyqelkei nqqykdihge
      241 ndhahnasvl dqviktseqa lpdakvdyia mpdtqfsppn hflvvmvgnt pqtermtqlv
      301 vvdaatgtqg evrelpwymk itlaseplhf gnygglflki vwlgfslfsl llpifglviw
      361 ykrkkatqvk gvsmetrkls esalfknrft tplalfvvta vmiigafilg gtfavvsgyv
      421 llipliltgv vvlrgkrgks
//
LOCUS       WP_181604601             512 aa            linear   BCT 28-DEC-2024
DEFINITION  M17 family metallopeptidase [Bdellovibrio sp. KM01].
ACCESSION   WP_181604601
VERSION     WP_181604601.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 512)
  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 512)
  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 512)
  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..512
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..512
                     /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=55531
     Region          95..508
                     /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(104,201,203..205,250,252,282,288,293,296,299..300,
                     332,334..337,339,341..345,351,353,357,397..401,404,
                     430..431,433,438,440..441,446,448,457..458,460,494)
                     /site_type="other"
                     /note="interface (dimer of trimers) [polypeptide binding]"
                     /db_xref="CDD:238247"
     Site            order(278,283,290,301,360,362,364,392)
                     /site_type="active"
                     /note="Substrate-binding/catalytic site [active]"
                     /db_xref="CDD:238247"
     Site            order(278,283,301,360,362)
                     /site_type="other"
                     /note="Zn-binding sites [ion binding]"
                     /db_xref="CDD:238247"
ORIGIN      
        1 makkkvaask asaklqirsw ietfdigkel kaknemtgfv yflaaddsnk lqglveehal
       61 awqmesikkn dkelnhfvgl qgpvwivrpk gknsvghdgl ldeatytwar dqfgslvphf
      121 kshqlkalri effgtekaqe lgalvgldma pynyrqfvdg khladmpkvs likssedfdk
      181 alikeasvra ravtlarhlv nmppndlnpk tfaematkkl pfgknlkvtv wddkklasek
      241 mglhlsvgmg athgprmvhm kyrptkksgl kpvafvgkgi tfdtggldik pssamrlmkk
      301 dmggaasvia lalwasesqy pgpldfylal aenavdanaf rpgdivtarn gmkveidntd
      361 aegrlvladv ldvackqkgs ddpefvidva tltgaikvgl gaeiaglfan dddlaneltk
      421 agqragdlnw rmplfdkywg dlsspfadck nsgggfggai taalflqkfv ggkkwahldv
      481 yawadranga igssggsgqp vqclieflqs rv
//
LOCUS       WP_181604714             208 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604714
VERSION     WP_181604714.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 208)
  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 208)
  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..208
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..208
                     /product="LolA family protein"
                     /calculated_mol_wt=23173
     Region          7..203
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mrvcpqilff lvsfvvaqis laatqdaeal kdlklaeftk lsgqfrqsks lkeldveikt
       61 egtfqvsrpt vdtsvfhwni ekpkpsnici drvgivvdsg tplkrknlkf sevgreagdq
      121 iasllkiitm nqsriveefn iqkqgglfll tpkkpaqaff esstleidka glvkkvlile
      181 kskdeirief lgmktqnsav akdekctr
//
LOCUS       WP_181604729             246 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604729
VERSION     WP_181604729.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 246)
  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..246
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..246
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25858
     Region          18..237
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrilswlllp illvasfqar aefkvpalqg pvmdevgvip rsmrqdltql lfdfnkrgka
       61 qiqvlivgtl egepieqasi kitdqwklgd akkdngvlfl iavqdrkmri evgqglegai
      121 pdvyakriia dvvtpyfrkq ryadgiyagv aqiialadke fadekgmttd drsddkgggi
      181 pigviillli iisvlgrfgg grgrylggrg gygggtfggg gwgggsgggw sgggggfsgg
      241 gssgsw
//
LOCUS       WP_181604628             220 aa            linear   BCT 28-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Bdellovibrio sp. KM01].
ACCESSION   WP_181604628
VERSION     WP_181604628.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 220)
  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 220)
  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 220)
  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..220
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..220
                     /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=24676
     Region          17..205
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 meqyqdlllk kslplseqvv eayyryprhl fvpeytlqea yedaplllyk kgafvstisq
       61 psfvmrildm lqlapghkvf elgagsgwnt almsyivgpq gkvvsseiip evadrargil
      121 dqmritnaki ftgdgfegye peapydriif tagssemphk ifaqlkedgl mvfvkkqdkk
      181 adllqlikks hgeqqilnsi pcsfvtvnre sesrlqdgtp
//
LOCUS       WP_181604416             399 aa            linear   BCT 28-DEC-2024
DEFINITION  J domain-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604416
VERSION     WP_181604416.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 399)
  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   2  (residues 1 to 399)
  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   3  (residues 1 to 399)
  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   4  (residues 1 to 399)
  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   5  (residues 1 to 399)
  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 11437593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..399
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=46649
     Region          251..298
                     /region_name="DjlA"
                     /note="DnaJ domain-containing protein [Posttranslational
                     modification, protein turnover, chaperones]; COG1076"
                     /db_xref="CDD:440694"
ORIGIN      
        1 mqhdlqkadd qkirtelfst ssqlikkirk lekdhadfll cdqmmyhdwr kltfreelqe
       61 iealerrqki lntfqvhlny vattsnvspa qayamlkeee gqyqcgddmw kyvidnlrkt
      121 ryesatqslp raqnpavesa ervdfaeiff rddsalsglk rtarsvyhyl sdidnqkieq
      181 hladptagyr lfkeslqiti kcgdwhllgr vwksadpsyr qrylhnmpmh lkkfwqkvis
      241 dnerdealee srtdadtvlr ttyhklvrll hpdklvgqsl eyqqwasvkw qrtqaayqdg
      301 dvaalkrlel lclaelgqln dltteeisqc sdlfeteles lkksiaqctq hpawkfssrr
      361 sydslkqsey delrkhlipl radvsamevl legyaskch
//
LOCUS       WP_181604763            1944 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604763
VERSION     WP_181604763.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1944
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..1944
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=193376
     Region          444..1932
                     /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 mgsfnykktm lrigilcsll aistealasa tsltyqgril tasgqpfeya hasflfkits
       61 pdgqcviyqe qfngvdmtns ngifdvpigt gsvqyisspa ltvidifnns gsyqcgtctp
      121 sagntytcsp smaapyvaap adgrllrvaf ydgsgwnavt pdnkiravpy agysftsykl
      181 gshtandfml kadvpsacgt agnfltwdag qskfacstla sagagtitgv tagsgltggg
      241 ssgnvtvsla ntgvtastyg satqvpvlti daqgrvtgvt ntsitgiapt gaasgdltgn
      301 ypsptiagna vtsakildgt inaadmnftg tntatsgivi kdslgnfsef acstvghiam
      361 wtsvgwgcqa psttdstklp ltggtmagai dmnsnnitni gfmtmsanks lhvsnnssdp
      421 slvaadkgki wfnsttnelk ywngtaavav gstgaaitdl tgdvsatgpg saaatiansa
      481 vtnakmanma ahtlkgnitg saaaptditi aslqgtsgtt faagndsrit galqsgtaag
      541 gdlagtypnp tlatgavtst kiasativga nldftgansa ttgmvlkdat gkflsfvcst
      601 agdvptwtts gfscqtpspl lpaladgkiw vgvagtatav tmsgdanlsn agaltlasvv
      661 sagtytkvtv dvkgrvttga nlaagdiita ltytpvnkag dvmtgslglg nftnateatl
      721 itgwtaadkg ktwfntstnq vkywdgsaaq algvsgaglt slngesgsaq tfatpgtagt
      781 apawssasnt htlnipmasa agvtagllnk tdydtfaakq aagnyvtalt gdvtasgpgs
      841 aaatiasnav tsakiadgtv vaadmdftgv nagtanlvik dssgkfanfg cstaghvatw
      901 svagwscaap tplmpsladg kmwvgdnant atavtmsgda tlsnsgaltl anvvsagtyt
      961 kvtvdtkgrv ttganlaagd ittaltytpv nkagdvmtgs lglgnftnat eatlitgwga
     1021 sdkgktwfnt stnqmkywdg svaqalgvsg agltslngqs gstqtfatpg tsgtapawss
     1081 ssnahtlnip masaasvtag llsktdydaf aakqaagnyv tsltgdvtat gpgaaaatia
     1141 anavtsskia dgtivgadid ftganaattg ivlkdstgkf mnftcatagh iptwtasgfa
     1201 cqaptallpt ladgkiwvgv agtataatms gdatisntga ltlatvatag tytkvtvdtk
     1261 grvttganlv aaditsalty tpvnkagdvm tgslglgnft dateatlitg wntadkgktw
     1321 fnttsnvvky wdgsaikvig svgaaissmn glsgttqtfa tpgttgtaps wssvgsshtl
     1381 nipmasassv tagllsktdy dafaakqaag nyvtaltgdv tasgpgsaaa tiansavtna
     1441 kmanmaantl kgnntgsaaa ptditiaslq gttsttfaag ndsritgamq sgataggdlt
     1501 gtypnptvas gavttgkias gtilgtnmnf tgtnagttsm vlkdstgkff dfacstaghv
     1561 atwtvsgwac qvvsltpsgf gsqtqntfla apngsagnpt frtiasadlp itgatgvyin
     1621 ggnsfgsaat lgtndansls letnnttqlf isatgsvgig tvsptaklhi sssltgnsgq
     1681 lytnffyata dptaassaty ygsqgtvsny nsntrlngat ltgvaglveq ggtgivgnan
     1741 aiealvskfa sgnmtsvngv yshlnsstsg ttdtfrglyv stnisgtstl tngygvyids
     1801 msgttnsygi yqngasdrny fagrvginta spsanaklev tgtivstpts vagasvnlat
     1861 sntitltavg gtaitlsnmv nggnytllvs dttsrtytft gcntskfrpa naatvagtat
     1921 mysiitiyng stydcwitwg sgyq
//
LOCUS       WP_181604911             256 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604911
VERSION     WP_181604911.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 256)
  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..256
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..256
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28658
     Region          32..>190
                     /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 mflsimvfag fmataspevg rskiqiytve tpptvvkkad gldglagdfg kliaatlkks
       61 gkekefeivw vpwkrallev ernpqalffp ftrtfereyk fnwivhladv dcwlyavdsn
      121 iqitdlkdlr kyrigvlsgs areqellryt gksskvegmt edlanyrklq sgridiwath
      181 pvvmaeaqkn fmaqgksara vrslkklfsq slwlagnrdm pdtsrnlvqt vfgwgakrsl
      241 ksppltsgdf lggall
//
LOCUS       WP_181604700             293 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Bdellovibrio sp. KM01].
ACCESSION   WP_181604700
VERSION     WP_181604700.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 293)
  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 293)
  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..293
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..293
                     /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=31711
     Region          1..268
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrslsliial iltaacsrqa phlyssaqih sqdsiiggea vkssdfarsa tvaiyttsrr
       61 gleflctgtl isnnlvvtaa hcmqsvytiv yvsfgeelpk stlsmirvee fishpdygnv
      121 qkpgedtely wttehdlall klntnapmgf spiaihgdtd kiplksklll agfgttndek
      181 gtaalsmnqv evtldslvdd ylvidqtqyk gacfgdsggp aylqtaqgwv vvgathaarp
      241 gyfdchhksd ytslskysaf iqsmadelra eapvfvtpve tlkrpvrppi aiq
//
LOCUS       WP_181604629             175 aa            linear   BCT 28-DEC-2024
DEFINITION  Dps family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604629
VERSION     WP_181604629.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 175)
  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 175)
  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 175)
  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 175)
  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 175)
  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 175)
  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..175
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..175
                     /product="Dps family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19779
     Region          36..174
                     /region_name="DPS"
                     /note="DPS protein, ferritin-like diiron-binding domain;
                     cd01043"
                     /db_xref="CDD:153102"
     Site            order(49..50,54,56..57,68,79,83,86..87)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:153102"
     Site            order(56,68,72,83,87)
                     /site_type="other"
                     /note="DPS ferroxidase diiron center [ion binding]"
                     /db_xref="CDD:153102"
     Site            order(150,157..158)
                     /site_type="active"
                     /note="ion pore [active]"
                     /db_xref="CDD:153102"
ORIGIN      
        1 mkyaaqkest anstvhtfnk asakstqtaa qsgtieemkk tladeyflql ktqnfhwnve
       61 gplffslhkl feeqyedise fvdrsaeilr alkspapgsf qafkkladve ectdeklsst
      121 kmidiltadh ttlaelykar letaeqeeet savtlyedli tfhekaawmi rshls
//
LOCUS       WP_181604844             263 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181604844
VERSION     WP_181604844.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 263)
  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..263
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..263
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29225
     Region          43..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 mklliaamml tigfrtsvam adtilvrsda wcpyvcdssk dpgymvevvs kifeknghkv
       61 nfsmvnwara vsetrrnkat aivganynda pdfvfptktl ghgqdfffvk kdstwtykgs
      121 aslvgkkigv ingyayggdm drivsenkdi fisisgehpl dqiikmiesk rldafienqt
      181 vlrtnlanmg lsqdeykpvs aqvandaklf iafspankks eiyakiftkg itemrqtgel
      241 nrilakyglt dweqqealet atk
//
LOCUS       WP_181605043             199 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181605043
VERSION     WP_181605043.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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..199
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..199
                     /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=21900
     Region          18..193
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 maifrpgerh ryhnilskkk gkrgvtavls ltamvdmftv lvifllqnyn ttgdilympk
       61 evtlpkassv kelkpahvvt isnkeivldk dtvatfeeiq aagpddwnip klkeqltlal
      121 aksksdyeak lqnriknavd qtkgqttdda nawskvtiqa dkgidfltvk kvmftvteag
      181 ageinfavtk nsnqststq
//
LOCUS       WP_181604976             410 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Bdellovibrio sp.
            KM01].
ACCESSION   WP_181604976
VERSION     WP_181604976.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 410)
  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 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   3  (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   4  (residues 1 to 410)
  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..410
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..410
                     /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=46191
     Region          16..409
                     /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 mstisgnvtg esrelilivd delrirdsls lalhsfgyrt ivasnvaqai davrrsnvdl
       61 iltdlnmpgd tgldllhqvk kedptvsvvm mtafgsieta vsamkegaed yllkpvelgt
      121 leilvnkile krhlrkenqr lsaenralke nldvryhlas mlgtspqvqe lqksiklylk
      181 vrtpvlilge pgsqlseiaq ilhynspwss nsliqfncsm vpgefhepql fgieervqdg
      241 vrlrgapglv ekahfgsmil sdidhiekrc qgmlsrvfnq kktqrsggth fyeadvriig
      301 tahekeiemr vrknkfrwdl wefmsdnviv vpplrtrked lpilvlaeak rlghfygkqi
      361 qsvhpqviee lskrsfpgny relealieta vlssqqsvla wsdfksvten
//
LOCUS       WP_181605049             167 aa            linear   BCT 28-DEC-2024
DEFINITION  KdsC family phosphatase [Bdellovibrio sp. KM01].
ACCESSION   WP_181605049
VERSION     WP_181605049.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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 167)
  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 167)
  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..167
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..167
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=18472
     Region          7..157
                     /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 maveisklkn ikmlvldvdg vmtdtriwfe ngewrrfysi rdgvgikrlt eagykiavit
       61 gtkaedvrar akslgihyfy egaldkepsf lqlqkesgis pnemayvgdd ifdipllqav
      121 sfgatvpeav devieiadyv tkrpggcgav revcdyiyky gafssgr
//
LOCUS       WP_181605065             453 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181605065
VERSION     WP_181605065.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 453)
  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 453)
  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..453
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..453
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=51217
     Region          <55..233
                     /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 mmikalcltl llgfsvtsaf gaedldkfdy dpskipvseq gtadlgelqg vptplveyii
       61 dssgsmgqil tgkktkifvm kkllsrylvs qwtektssgm rvigsrrkkd ckdnylaipp
      121 gnaklglieg mvksmdpvgm tplydsmkea ykdlekydgp krvviftdge etcgkdpckl
      181 seefknknvd lkffvvafgl qgqqetlqkl kcigdlhqad deeqldkmfe dldkdlnpnk
      241 nlfvdspepq atvmlfraet pneiyrrfqa sygiqvppgr yyavvnlkpk yrfkefivpp
      301 nkkvtlkvkg eakfkanfid glmkvellnk nrkvvkrfns davvslppgk wnfrfyrdpf
      361 yekvvnnylv vpnaeyeyti eeagvayved pqvkgiyvfg nrgimmgnhv tnfplvlgkg
      421 vyeirvddkc ifkdiimgsn kevvklqcsk vkk
//
LOCUS       WP_181605217            1813 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181605217
VERSION     WP_181605217.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1813
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..1813
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=183911
     Region          29..1655
                     /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 mkwlliiiti fvfsactkkg ssiqdgflag vsvsagasti tvssasilag nsttvtlttr
       61 dsegniyhvp gsnpvitfkt sggtstgifg pvtnnndgty talfsgstag tataimanvd
      121 svelttqaat itvlpanfsa tnsyvtlsas tiasgsnita tfyaydvnns pithgglnvt
      181 fviqsgtstg tfgtvtdnnd gtysatftgk ivgtaasika tvagisitsa mptvtvtpga
      241 aagiavsagn sqsgvvnsal ttvlkvlvsd aegnavpsvq vdwsttgnss lgsatsntns
      301 tglasntltl gtvtgtytvt akihgtttta titatahpga innfllsgvl atatagnsft
      361 ttvtardsyn niktdytgav qftssdsntp slpasytfda sdagtkqftf tlktsgdqti
      421 tatqvsggtp tvtssaisvs aatatqlami sgptntvags sistllvral dayantatsf
      481 ngsvtisigt npgsanlngt vtgtassgsv slaglsinta gtgytlvats sgltsatsgs
      541 fnittaapas itvqsgnnqs atvgtalasn lvavvkdtyn nvisgttvnw ttdagtlgsa
      601 ssstntsgla ansltmattt gshnvtatia stalstsfva tatnaiasql vystepvggv
      661 tpgtllatqp vvqiqdsygn lvttgadata dvtlsltsgt gslggtvtat asggvatfss
      721 itvsaygsgk vitatkantv ssggtssvtr qsnsftiipp apaaftisda vagssqvvls
      781 wgssadatsy tvkygtssgs ytttvstnat spltinsltp gttyyfqvda vnstattsat
      841 aeasatplsa faissvsvns gnklrvqwgn stgatnytvk fgtstgtyst tdstsatspy
      901 diasltggtt yyvmvtatns sgsvnasaea igvpisafsl ssitpsvgss aiafasangt
      961 stydllydts shtadqtyas sktnvtspas ntglsagtty yyrvrannsy gsvvstnels
     1021 gavyqtfsls ipftagteas ytmsnstsfe lasgvarlaa asltdststn faagttagtq
     1081 wdstlnvlrl nstenktafd sswtpkwsnl iaywkmdnnl ndsvgsynlt atgtptftap
     1141 gkvgshygtf ssgnygsmaa gpalanssfs isawvyvtns sgtnkhilgy gttttdnglh
     1201 fgytstgtlr lgfysddlss ttnynildvn rwvhlaatyd sttktrviyr dgiavatgta
     1261 aadfagsgsf yigqglgtnf fpgnidefgl wnatltaaqv saifnnqsak ysgrfssrii
     1321 daggtgstny twsnlalktt lpfykevpls seasgnyssi vgnmntnlia fwrfneaswn
     1381 gtagevldit gnnngvrsgt attfaggrfg naglfsaand avvtsagstf iasadhalti
     1441 sawiypysig ttgsgaidnr iisihkgata gstlafglgn tnklmhytns tgvftsstin
     1501 vststwthva ltydgtcfqm yingvsggtc ytaglvaggs fgtrigsyss sgnsfnglid
     1561 emgiwarsms qaeiqqlyrr gvnrvkyqvr tcttndcsdq aaatnlgwkg pdnsastyfs
     1621 elynttnnil ggtlaagtpt mtfsnfgsls lgttnryfqy raflesddnn slctyasasa
     1681 ncspelqyag tgptrydsss psitatgaav tsafevldsa aftevlggns cssgvkysls
     1741 adgsnfyywn psnsaweast gvstasdatt iaahistfss vagtgtlrvk tylqssgssq
     1801 ceidsltitg kky
//
LOCUS       WP_181605196             330 aa            linear   BCT 28-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Bdellovibrio sp. KM01].
ACCESSION   WP_181605196
VERSION     WP_181605196.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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 330)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..330
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..330
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36857
     Region          65..167
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          66..297
                     /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 mktlsvplsv llsslslfqt spghaqeivp ftpkderkll gpryegrlvp lapmnqisea
       61 gleaeplvfi hgrqgsiknf tqlllntpkf tdyqlyyfay ddlhrslkrs agdlalsllk
      121 lkvsritiia hsmggliare tlntlsragh tellpeirvi svdspwqggs sinckhkgan
      181 ldemveyfmp aaltdmrscs dffqnlysvs wpeqfsmely faqhgtqald hseapinrlp
      241 akiaslftdn tpmkgslyem nfwnaistss qypgfvnels alhehqkita advsrllekh
      301 yprfpgdhas vlkahpqael dlpkylqtil
//
LOCUS       WP_181605316             470 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Bdellovibrio sp.
            KM01].
ACCESSION   WP_181605316
VERSION     WP_181605316.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     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=52095
     Region          2..458
                     /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 mrsqrvlild desslrtalf rvldrkglnv itankieeak alsqgdtpid laivdlnlpd
       61 gdgiefmtyl kalnpacevi iltghaties airatqkgaf hfvtkpfnle elmsliekal
      121 thkklqqenq qlrselnkky kfdqivgsse piqnvlrlie rvadsdstvl vtgesgtgke
      181 liaraihyns praqgpfipi ncgaipsell eselfghmkg aftgaianri grfemadggt
      241 ifldeigdle pslqvkllra lqersfepvg stktvsvnvr viaatnihle eavehgrfre
      301 dlyyrlnvip ihvpalrerk sdiplllnhf meifnknkgr gltgiaadal dalgnypwpg
      361 nirelenlve rmtilkgqgt vemndlpvky ksmkpvasld asqmeipdsg mdfntavdnf
      421 ennlilkale ktgwnrnqaa allrlnrttl vekikkkglt ppndinpsnf
//
LOCUS       WP_181604833             273 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Bdellovibrio sp. KM01].
ACCESSION   WP_181604833
VERSION     WP_181604833.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 273)
  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 273)
  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..273
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..273
                     /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=29119
     Region          1..272
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mkktiissvs lfvglailsg ctisneardk legqclpgvv ggsvtaksdp lskqvvmlig
       61 srynekgeee ssvctgtpit edviltaahc vkgnvrmaai fandmncssg frasrdsiva
      121 ssfeydhsfv esysgfyndv glvrlkskip sdyeiselya gaelssddvt lvgfgktset
      181 ksdsmilrsk tksfknditv ssdrvtieqs egglcqgdsg gpifvevnge kqvigvtsyv
      241 snryesnich gkavgmlsks vlpwiektlp tlk
//
LOCUS       WP_181605469             108 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Bdellovibrio sp.
            KM01].
ACCESSION   WP_181605469
VERSION     WP_181605469.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..108
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12140
     Region          5..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtksdkktk qspcpvtktm qviggkwkpm ilfnllsgrk rfnelqrlag npsarvltlq
       61 lreleddkii krdvfdqipp rveyslttkg kslssvlemm akwgqahg
//
LOCUS       WP_181604965             307 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Bdellovibrio sp. KM01].
ACCESSION   WP_181604965
VERSION     WP_181604965.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 307)
  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 307)
  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 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   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 18916493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..307
                     /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_function="GO:0031419 - cobalamin binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /note="Presence of a B(12) (cobalamin)-binding domain
                     implies dependence on cobalamin itself, in one of its
                     several forms, or in some unusual lineages, dependence on
                     a cobalamin-like analog."
                     /calculated_mol_wt=34433
     Region          8..75
                     /region_name="HTH_MlrA-CarA"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators MlrA and CarA; cd01104"
                     /db_xref="CDD:133379"
     Site            order(9..11,25,42..44)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133379"
     Region          101..272
                     /region_name="MtbC1"
                     /note="Methanogenic corrinoid protein MtbC1 [Energy
                     production and conversion]; COG5012"
                     /db_xref="CDD:444036"
ORIGIN      
        1 mvtpdalldi dqvnqltgls qatlrnwerr ygfprpqrsq gghrlydvge vkrirevasl
       61 ykngikivda ieqvlngiat vrgnsepasf ptssvlletl neglaqvlka lyrydmdfae
      121 qqlsrlgmrl setdllemvy pkllmqvgdd wensriniaq ehfswnflrt rllnyfktnr
      181 sgtgqpkvll atpsgelheg glivlaaylm lkgwsvyylg vnlpiedllh ayvniepdiv
      241 clsaidstni qknwtdleki kavavggpcl aqlrsqelph skniffvdgs lhsavsqmdl
      301 liqqfkt
//
LOCUS       WP_181605503             278 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Bdellovibrio sp. KM01].
ACCESSION   WP_181605503
VERSION     WP_181605503.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 278)
  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 278)
  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 278)
  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 278)
  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..278
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..278
                     /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=31537
     Region          196..274
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mknfeirtid ltslseleel lsvslgypts madeisyfee espkgwfyav dknekklgfi
       61 rcfkqgddws lgelfveags qdrkliaeel vktfltsnsf sskhrlrfdv gcddndvndi
      121 fkqsafniks qtfhhfelti prclgvknve eahrmapade vaktmsnlha vsaneaqewi
      181 esgslriema sgqvaavakv diypqsakid rlathekflr qgharklmak ismelsacni
      241 ptlflkvedv rgpaiafyrn fgfeeilekk qtwhsihf
//
LOCUS       WP_181605505             915 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Bdellovibrio sp.
            KM01].
ACCESSION   WP_181605505
VERSION     WP_181605505.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 11436754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..915
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..915
                     /product="class I SAM-dependent DNA methyltransferase"
                     /calculated_mol_wt=104811
     Region          59..890
                     /region_name="YeeA"
                     /note="Type II restriction/modification system,
                     endonuclease and methylase domains [Defense mechanisms];
                     COG1002"
                     /db_xref="CDD:440626"
ORIGIN      
        1 mkssyatiqm nlskfyskwq nfsgnerqgs qifladffsc fgltfddpna ipfevntgkg
       61 fadaflkdsv vfemkskklv kdksslekql pqalkywdgk grhapfivlc nfvdfiifdt
      121 rdrskhyiki geleskaesf nflmklnpaf apeqeavtrq aakimgklyq dlknrlkgrk
      181 eevdifvlqc lfclfsedig ylpvemfsns vrrirdgedn sanilstlfk mmderdsdrk
      241 rgkfehvryf ngplfrikpe ivltdtevec lweacqydwk tvrpeifgal fessqskksr
      301 hadgmhftse idikkviypc vvepwneile nckspkdlqe ahqklksyrv ldpacgsgnf
      361 livayrelkk ieegifikyk aatgmtynev qaelgwfplt nlygievnaf pslltrvslw
      421 itkkmvksdl kltepdlple elkhiicada levkwddvdv vvgnppylgc kqirkargdr
      481 yfkwlgerfp dhskmsdyct ywfekvledv kpgvriglvc tksisqtnsr laslekivss
      541 ggtifnaisn kkwsgeakvh vsivnfvhks gfvgkkyldn kevmeissrl knfaiqsesr
      601 klkanggtay vgpvpngkgf iidshtrsel lkespknrav ikefltgedl vhnadqsasr
      661 wiidfqdwpl ekamefkgpm kiitekvkpv rkkirgstnd aknyrmnwwr fgrpqmglrq
      721 qishlkkfvt vsrvgkypif vfvnnknilp adstvaiafd sfgqmgvlqs kfhtqwfnyq
      781 csslkgdary tnttvfetfp fpekissevg timkkieayr skfckkmdig lttlynqmnd
      841 gahiplkqlh kqldqavaec ygypkakies yndiinfltd lnllrasqed eialrekaae
      901 lakkasrkat kkraa
//
LOCUS       WP_181605520             392 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Bdellovibrio sp.
            KM01].
ACCESSION   WP_181605520
VERSION     WP_181605520.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     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=43885
     Region          5..390
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mndfrwpliq nniteadkta lvkhimtsdr ftqgdkvkkf eqewskwlgv khsifvssgs
       61 aanfltlsal rdvasvgevi vppltwvsdi vsviengftp vfvdinpetl aldyeatkka
      121 itkntkavfl thilglngls tplqqllkkh kipliedace shgakmgthk vgsigfasnf
      181 sfyyghhmtt ieggmvctnd pefaqlvrik rghgllrest dpaqlqkhln nskqvykefd
      241 fpvvgfnfrn nelgavlgln qlkrldknnt qrslrlhrfl kgldkntyft ryntkgsssy
      301 alllqilpdk ahlkskvekv lsdlgveyrr gmsgggnqlr qgflktrgid idptafvnte
      361 qihhngfyig nfpslplkwi dqlckalnev ak
//
LOCUS       WP_181605594             211 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181605594
VERSION     WP_181605594.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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   Wintjens,R. and Rooman,M.
  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 211)
  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 10599636
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..211
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23772
     Region          5..>76
                     /region_name="PRK14291"
                     /note="chaperone protein DnaJ; Provisional"
                     /db_xref="CDD:237661"
     Region          137..193
                     /region_name="HTH_25"
                     /note="Helix-turn-helix domain; pfam13413"
                     /db_xref="CDD:433187"
ORIGIN      
        1 meattrsnyy eilelpansp qhevtaayer arntysgenp aiytifsehe areflvliee
       61 ayqvlgnkil rniydqrlls gmaslndlty asiveaskkv tpvevkatek kpaaaytkde
      121 afeaeikaqe nwtgdflkkv reykgitver mseitkinaw yvkaiektep dnlpavvfvr
      181 gyvvqiaral gvddkkaads ymktfkqalg k
//
LOCUS       WP_181605619             438 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Bdellovibrio sp. KM01].
ACCESSION   WP_181605619
VERSION     WP_181605619.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 438)
  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 438)
  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 438)
  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..438
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..438
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51087
     Region          7..332
                     /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 mkdlkrlwli slfvklilaa liplsadeay ywvwshrlql syfdhppmva wlfslghfle
       61 pflhsvrwpa vilghasiwv gikllskhmd lekirtwiyl vlfspllgfg slivtpdlpv
      121 iffwivslyy ldlvlekkdl ksyaafgval glgfcakyhi vlfvpcllly limekkwnav
      181 hwklvpatli tgllfclpvi lwnyqndfas frfqlehgfe rphynpewti syvlaqivii
      241 fpwvlwaavr ikpakpvryl myfawlpllf flgtsfkalv eanwpiiayp avfmlaamhp
      301 rmsqwkkyyi gffgsiiaaa vvilfvprfr tidpkinepf alqnlaqeta eyqplygdsy
      361 qmssslwyfs kspvfklkdi srfdffdtlp eakpagnkfy lvkhqgnglp qwlseqqwty
      421 qeikkiapdf vvleftrp
//
LOCUS       WP_181605770             335 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181605770
VERSION     WP_181605770.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     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=37002
     Region          1..335
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mrvsilinpk agssnqgqve aivrealfrc dlhfatpktl eeldlflahe mlnktnalii
       61 cggdgtinvt fqtmiriher lgfdmppvtl vrsgtandla ermgistkih qavrnilegt
      121 tknidvievt gdgkksymlt ngglglpamt aemsndfrsy lqkrsdcpka tlafkflakq
      181 sysmvkkmgp qiysmmalea irtwdptdwk levnipnkan fettapiilv nnqpnvastf
      241 tpapftsntd gtmnllises ssqaehvrta lnirrgtaar lpysksyelk efslktkntk
      301 rtltffgdge vlhkgvselt vkclhrflpi vvaak
//
LOCUS       WP_181606027             328 aa            linear   BCT 28-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Bdellovibrio sp.
            KM01].
ACCESSION   WP_181606027
VERSION     WP_181606027.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..328
                     /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=36698
     Region          12..327
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mrtietssha enstlrkvpt lslasytkgs gsekarfidq lftglkeygf iilkdhdvka
       61 adlhkaydll ekfyalpedv kksyisptag fqrgytpfgk ehakdspvmd lkefwhvgre
      121 lvvaselksi ypdniwptdv ipefkdhflk lfsaleeagd vmlealtmpl evdkdffarm
      181 tkdgnsilrl lhyppipegv dprcvraaah edinfitilp aatasglqlq drdgtwldie
      241 sepdtlivdv gdmlarltnd vlpstthrvi npqdgtnshr ysmpffmhph ptamlsclps
      301 ckgtgakyad itgqdflmqr lreiglik
//
LOCUS       WP_181605708             361 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Bdellovibrio sp. KM01].
ACCESSION   WP_181605708
VERSION     WP_181605708.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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 361)
  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 361)
  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..361
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..361
                     /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=38390
     Region          3..322
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mntikslkla lslgalatia actpnksasl ksgnnsgiig geavaqndii rkstvsivvn
       61 vltqdnqqgq flctgsiiad nmiltaahci pgteykkaam fvvfatdlnk mtkdqikpvt
      121 gvvvhnqyge gdarlratie klkkagnpng dgvelsdrdq gadnydlavi kiqgkipady
      181 qianilkdet ilknganvtl agygltnvkk eqvdlkkypd ldaaiasgqi actydkktcy
      241 iltqenenil kktdvgviqp ygdtevaldq sqgkgachgd sggpafinvg gveylwgvts
      301 rgtgkegidd csnyaiytki naewnfvsaa mkqlntsake dvqtqeapad tqeeaaldye
      361 i
//
LOCUS       WP_181606164             259 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181606164
VERSION     WP_181606164.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..259
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29431
     Region          40..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 mktlvwtfll sstvvifafl svvyasdeai tlqlryhprp pflkleggnl tgfcgapavr
       61 aleragisys lvetppfrql aliqssegyd cavgwlkipe rekiykysdp vcddgtwfvv
      121 ghkgsfdksi dkiddllknr rlklinrrhy sfgpqvdtla kryntnityi enaeitpqmf
      181 emiragrvdy tfisgleldy ilkrfkwaas dfivfqpvdv ahssprhfic skkvpdevir
      241 rineaiqktt ahaaktesk
//
LOCUS       WP_181606182             110 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein [Bdellovibrio sp.
            KM01].
ACCESSION   WP_181606182
VERSION     WP_181606182.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 110)
  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 110)
  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 110)
  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..110
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..110
                     /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=11296
     Region          2..84
                     /region_name="RRM"
                     /note="RNA recognition motif (RRM) domain [Translation,
                     ribosomal structure and biogenesis]; COG0724"
                     /db_xref="CDD:440488"
ORIGIN      
        1 mgkkiyvgnl sfnvdsdqlt stfsefgtve saniitdrdt grskgfafve mssdseataa
       61 idklngmdlg gramniseak pqaprtgggg gggfrgnsrg gfgsgsrrsy
//
LOCUS       WP_181606252             582 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181606252
VERSION     WP_181606252.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 582)
  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 582)
  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..582
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..582
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=65293
     Region          <195..372
                     /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          243..564
                     /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          258..286
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(259,262..263,266..267,269,293,296..297,300..301,
                     303..304,327,330..331,334..335,338)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          291..321
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          435..465
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          470..494
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mavevsntdk vwliksstri lgpfsvdeva tllksrqvsi ideirlpsgr wsyirenqrf
       61 mdivrsiree qdnapentmt qsiphnttft kteptvdpde qtltpvpnhs pqmkdvsfas
      121 eravnksaip asgvsygtsn darvqnkirq qsnvlrwavm gvaaiavlai yvtlghrdst
      181 hnvnydelis rairyksvgl ydkslqayka assikepdld tqiqmapvli sedrqtlqgr
      241 rilekaivqe nrqrselvda ylgiavsymm dgdlkeaent lqkaighepf nisarlnlai
      301 vemkkgnyke amhkfehvls kdptnvmaly grsmaameva ktssdlsflk plvsdlqtvl
      361 kktnllrqel slfliysynl lgdvdamnqa ivkflnetpg vsnlythsls vdwrftqwdy
      421 lekycsevyn ksvpsaelka vralclmevn rdtdadkllr eavsegpkdp yvlaaqaayl
      481 kktgrapeal avlkmpevms lpvrdrlvgd icmsthdvnc aqaaftkmye rnntsaaaly
      541 glawvvikrk drnsaynyvr aglqseptfi pllemrdqle ad
//
LOCUS       WP_181606267             134 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Bdellovibrio sp. KM01].
ACCESSION   WP_181606267
VERSION     WP_181606267.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     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=15249
     Region          1..130
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msefgnykil irethidsyg hvnnatylsl yeearweait prgfgfsdih rlqqgpvile
       61 vsikflkeik lresitivss imdyegkigh mkqqmikhdg tvaseavftf glfdlkarkm
      121 ilptpewkka cgle
//
LOCUS       WP_181606367             280 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Bdellovibrio sp. KM01].
ACCESSION   WP_181606367
VERSION     WP_181606367.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     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=30885
     Region          50..226
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mkliisllav mtvaatahal plpgahqlvs lpenftaqyn fegivgldnc sgslirlens
       61 rdtdnalvlt nghcletgfp kpgtyvygkp srrtfrlfna gmevvgrlna ttivyssmtk
      121 tdmtiyklae tyaeikskys vnplllasqr pvektqievi sgywkrgysc eieafipyle
      181 eagftwqdsi rysrpgcqvi ggtsgspivq kdtrtvigvn ntgsdsgemc tmnnpceidq
      241 nghkkayrgy sygeqtfwvy sclnqyneld vnvagcqlhh
//
LOCUS       WP_181606240            1032 aa            linear   BCT 28-DEC-2024
DEFINITION  UvrD-helicase domain-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181606240
VERSION     WP_181606240.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 1032)
  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..1032
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..1032
                     /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=118513
     Region          6..1003
                     /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 msstapqlkn tilragagag kttrltelfl dyaayfktvh gklprivvtt ftrkatqelk
       61 erlsaealkr ksdelfhyan srsqvqisti hgvlslflsr ygsaigltpd ykimsdseir
      121 rgarkimrkh ilenpnlqel leeyefsvie sallqyfser ivfpqsrfis aeeqeietrk
      181 vikdiggrlk rvcleidqet dnekwkeyca nlwsfnwdaq dlgqffgmlq gmwdgitkpq
      241 yrkasppfsg slndeleelr dridklleas ryrpdywmkh qknceqfetl aqlfcqdlmq
      301 qklesgllsm sdletlsyki ikespesaen fsqewdfwmv deyqdtspiq veilrgligs
      361 klhfvvgdpq qsiylfrgar sevfqekvne islqegdvqe klvnyrstpe vleffnhyft
      421 rldrkqfasm tphpekekkg padpvvqvlv tettaedevs keylgtvsri qellnegvsp
      481 eqicvlsrth kvlsdiakva qdygvplqlh sgsgfyerre vldalsilkf lvnphdnanf
      541 vallrspwla mtdteimdlc hsfkhsfwre alktlesrsa qhpisilktl letseekgls
      601 ftlksalidl glfdysarid stgrreanlw kvvsllseee rrpgfnfldf ldssldslst
      661 deggedsdat pviepkrvnf mtvhaskglq fehvilpgmg kdprasfapv isfhektgqw
      721 tlkvrdeetq mlagsiladq imeelrrreg defhrvlyva ltraksgvtl qwdekkigkk
      781 swaalcplni eegfheeadf syvvrrenph pvkmadqele hkelrapwsv nhkeekrkyi
      841 svtelvapea vsgseyvqtv aqlapglara qqgtmahrlf eslkftsyee llkisdedlk
      901 apltflaete qlpllkiien gfvewgfalm eqnalmqgqi dlwgivddtv wlvdyktgsq
      961 rysetafkql eayawalyrm kyldrvrtvk lavvypmdei vkikeipqlt elntrmksqi
     1021 adyikqpdnk rp
//
LOCUS       WP_181606507             390 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Bdellovibrio sp. KM01].
ACCESSION   WP_181606507
VERSION     WP_181606507.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..390
                     /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=44775
     Region          121..386
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mnnmtfkskl lmkllqnskg atiqvtfpdg aqdsfgagep iisvrarnwr vfdelidkgd
       61 lgmaeaiirg dlevddiaal vqwacvneda vnrllhgtwy gtlfarlrhf mnpntkngak
      121 knimahydlg nqfyslwldp smtysaglfd saaedlqqaq mkkydriida ldisaddhvl
      181 eigcgwggff sravertgcr vtavmnspsq aqynreliar sgfanqvelr qqdyreiegr
      241 ydkivsiemi eavgekywpe ffnkvssslk dkgsaliqsi tiqdqyfeqy rrktdfiqry
      301 vfpggmllsn qvfdkyasry dlkndrpfef gvsyadtllk wkenfhsvea dirqmgfddk
      361 fmrlwdlyls ycegafraer invghyllqk
//
LOCUS       WP_181606535             336 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181606535
VERSION     WP_181606535.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 336)
  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 336)
  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 10541058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..336
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=37063
     Region          1..74
                     /region_name="BatA"
                     /note="Aerotolerance regulator N-terminal; pfam07584"
                     /db_xref="CDD:429551"
     Region          86..283
                     /region_name="vWFA"
                     /note="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 para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Site            order(95,175,199)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
ORIGIN      
        1 mtihsplafw lllpliavvv wvlwrkktkt ptlqfgsvqv lksvtpsirt rllniplilk
       61 algiafaifa larpqemntk ikknvegidi vialdisdsm liedmkplnr leaaketikq
      121 fisgrssdri glvifagesf tlvpptldyq lilsrvdeit taasarikdg talgvalana
      181 agrlkdsqak srvvifmtdg ennsgtidpe tgleiakgyg ikiysigigk dgptripiyt
      241 rdifgqkikt yqpfdstvne dllgrmasqt ggkyyraske dslkgvfkdi dslektkidv
      301 nkftnyteky ppylvagiil ylvglllgrt wlrrvp
//
LOCUS       WP_181606605             581 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Bdellovibrio sp.
            KM01].
ACCESSION   WP_181606605
VERSION     WP_181606605.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 581)
  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 581)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 581)
  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..581
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..581
                     /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=63229
     Region          203..577
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mgmskvnkfl tvsglllssa lapsvvmaae qcsaiftaqt qapapavnpa ilmgllkqql
       61 qaqvgqyafq ivkgdptevl ktksisplnv rdlaelgtvk qeaillnqla vlsnsgklts
      121 slvsllaqlk alpelggkpn pliglskeke aylietavsn iegvlalrgl tnttvkyvew
      181 salsktmter ldnspagldn ilhfaksefh ktskvqilid geqsfalrds lmskakksid
      241 vmtwavysdk tgfeaadlli skhksgvkvr livdgqvakk pgyteavqkm eqagievirw
      301 tnpshvfegq hrkmliidge hvisgglnfg dvyshknpdm niprwrdtdv yvqgesvnes
      361 rrlfadvwnq qvkekklayk tiqvraskqv apetgdvvav lnhdpvknqn gstimmtllk
      421 gireakstvd ienayvvmfp alkneiqaav argvrvrvlt nshtsvdepi vslpilrsah
      481 dlaavgaqvy lkkgatlhsk lavidgeysm vmsynlhprs ekvegemavv vkgkrfadtv
      541 tqaftndiss drataipsad liqlpsspev vpvlriffdm l
//
LOCUS       WP_181606746             227 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Bdellovibrio sp. KM01].
ACCESSION   WP_181606746
VERSION     WP_181606746.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 227)
  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 227)
  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..227
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..227
                     /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=25745
     Region          45..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 msenrknahn vqdgydiwaa hydhypnptv atdemgfpnf wchhsgkkvl eigcgtgrht
       61 kkwleagnsv taidispkml avargkipss qvnfvegdfl lqkdlphdfd ilveslmleh
      121 iqdlsaffkq cvsvlktggd lylseihper tqagigahfk vqdsemeihl vsfahtenei
      181 vswgdktgfk lvnskdllgd kklselnpkw erhmnrpmvr iwhfvkr
//
LOCUS       WP_181606962             737 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181606962
VERSION     WP_181606962.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 737)
  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 737)
  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 737)
  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 737)
  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 737)
  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..737
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..737
                     /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=84116
     Region          16..737
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 maepqketgl shkpvktvdd llnrirsywp nadlkfieka yyfsekhheg qirrsgepyi
       61 shplsvaail adlrldldti atgllhdtve dtdatledir refgdavahl vdgvtkigqm
      121 kfknshekqg enirkmivam gkdvrvvlvk ladrlhnmrt lnfmpfdkqe kialetleiy
      181 cplagrmgis alkieledlc fryyrpdmyy eliqqvkkte aeqnryiedv khliskelsk
      241 vgfkfevygr skhlwsvyrk mqsrnldydq vydvlafrvi vesvaecyaa lglvhslwkp
      301 vpgrfkdfia mpktnnyqsl httvvgpgge rieiqirtse mhliaemgia ahwkykergk
      361 mesdemqqan wlrdlvswhq qvrspdefld tvktdlfete iyvftptgev refpegatpv
      421 dfayavhtel gnkcvgarvn gkmvplkhql sngdtveiit gkgqepskdw lkfvvtnkak
      481 akirafvkee qrrrsillgk elvekefrkf gmaavkylkg pafeqylkdf glkdveelyv
      541 tvgygkletr vlverlspen iakeaakted stfmervmra athktrktns lvsvdgmddm
      601 lvhyakcchp ipgdpivgfi srgrgitihr sdcskafefd qlrkvdvawn vkvagegqer
      661 ivrlkiisqd npgllksmse afaqqginiq saqirttkdk kavcnfevsv kdalqlnqai
      721 yeiqkikgii gvtrviq
//
LOCUS       WP_181606947             359 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Nonomuraea soli].
ACCESSION   WP_181606947
VERSION     WP_181606947.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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..359
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..359
                     /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=37572
     Region          147..348
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mtlstpllaa apliaglmgp aivgaapsep hvesrpivrs aaqertppva divervatrs
       61 aadqrrvlay wtpermaaal piklldelak tvdgdgllsg lsnrtglgaa peiangvtkv
      121 tprrqsarpq tttvgsrwvt ggavakttgr vfltldgvdf vcsagtvksa nkdvvvtagh
      181 cvkdgrggwa enwtfvpgyv eggerpygtf tarrmfvagp wsrsaddsyd iamvalnkhg
      241 gkhvadavgt qdiafnagrg gqifgfgypa dppydgerli ycagrvrddp hgatrdqglg
      301 cdmtagssgg pwmsgfnpst grgtvmsvss fkysddretm ygpyfgdaak alfgtaera
//
LOCUS       WP_181606849             388 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Bdellovibrio sp. KM01].
ACCESSION   WP_181606849
VERSION     WP_181606849.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 388)
  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 388)
  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..388
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..388
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42837
     Region          10..363
                     /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 mttfndeysl lapgpvnlhp evrkalalpm ihhrtpefdv ilkrvlegir qifqtkedvy
       61 llsctgsggm eallvnvisp gdkvlaivsg kfgerwaema ktfgaevsii nvpwgeavkp
      121 esvadhlkrf petravlcqa cetstavahp ikeiseivsq hsqtlflvda italgayplp
      181 mdawkidglv agsqkafmlp tgmafisfsk kaqgyfdsak cprfyydvrk ekkanaaget
      241 ffssnvaitr aldvvlnlin kqgleslfht ihrraeftri faqklgftly akspsdsvta
      301 lvvpqsmdgq kirleleqsh nitimggqdq akgkiirvgh mgyiqdhell klidnlgqvl
      361 rkfdpgsltl eqisvvvdeg kqwleqnp
//
LOCUS       WP_181607042             320 aa            linear   BCT 28-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Bdellovibrio sp. KM01].
ACCESSION   WP_181607042
VERSION     WP_181607042.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 10143103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     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=35455
     Region          12..311
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(12,52..54,75,103..104,107..108,110..111,114,118,120,
                     128,130,131,134..140,142..146,164..165,168..169,267..268,
                     275,281..287,289..292,294)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(53,76..78,101,238,285,288)
                     /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..263,285,287..288)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mkntillpyi apknvaalak ekfdafvsdr eltteeivql anekkpqgmi ivpkqkftkd
       61 iiaklpdslr iiatssvgfd hldiaaaker giqltntpdv ltectadiam llllnacrrg
      121 reyleimeag wrkpfsqsem lgvkvsgktl giygmgrigq avadrargfg mkivycnrrr
      181 lspelekgat yfakledmlp hcqilslnap gnadtrhiin dqtlallpdd avlvnvargs
      241 lvqedalmra lqsgklfaag ldvfenepay dlrlkefhnv fltphmgsat retrdamgfr
      301 alenieqslk gqrpqdslwe
//
LOCUS       WP_181606493             824 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Bdellovibrio sp. KM01].
ACCESSION   WP_181606493
VERSION     WP_181606493.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 824)
  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 824)
  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 824)
  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 824)
  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..824
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..824
                     /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=90659
     Region          18..816
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mrtvisvsal kgmpltnegl rsdqvivqqn rfgrneftns skarwwqilw gslkdpmill
       61 lfvtgtifls vgnrhealtl yvailplllm dlylhrrtei stedlknkis kiasvirdnk
      121 aseincdelv pgdlillktg dvlpadgyle ssesillnes iltgeslpvs kvslgalpti
      181 lnddqlsids aclvyagtrv mrgkgilrly rtgshteygm iiqslssvpk ertalqksis
      241 dlvklltiag lcgcvvlgli rlfqgdslan allsaaifav aampeefpiv fsfflgvgvy
      301 rlakkkalvk ravtvesigr vqcictdktg tmtsgeltls evlpsqsfsr qqlleaaasa
      361 seehpvdpvd vvisiafgkd hlkkikvfpf temrkketai cktpedqvmg fskgapevif
      421 kqcelteadl lywrslvsky snmgmkviac arqakvsdre ietepvngfs llgilgfsdp
      481 lrpgvknaie fcqknrikvl mltgdhpgta laiasqagmg nehpkvltfe drpelwseqg
      541 ildkaselle ydviarcnpl hklwivrslr thfsvvavtg dgvndvpaiq qadigiamgk
      601 rgvqsardva sivladdnfv tiinaiqegk qllknlnssf eylllmqvpl vlgaliipmm
      661 gqpllflpvh lvwlelilhp tsllgfqmdv skskkfqend ffnkerilai slkgllvcaf
      721 mssnfflalw enkgvahara nallvlilag isyhlfktrl strasfsifl lnsvvtvaif
      781 qvsyfatfls vdvlslsdwv raslmvvlsi slselviktw nyks
//
LOCUS       WP_181607168             476 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181607168
VERSION     WP_181607168.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 476)
  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..476
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..476
                     /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=54188
     Region          113..366
                     /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(164..166,168..169,171,181,183,242,261..264,306,
                     310..311,313,327..328)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:270872"
ORIGIN      
        1 mdekksakkq nndaqaskke dlglhkikss vfsrglsiak ltlqtgasva qhgvttvlks
       61 kefkeanwkk lletqasnis telgqlkgsl mkagqmlsmy gehflppean eflkslqsds
      121 pslnwaaiek rlkellppek laqleiekea lasasmgqvh rakikatgel ivlkiqypnv
      181 dkaidsdlra iktllstlkl ipkdfntdsl faeiremllq etdylqeada tedyhrrleg
      241 dkrfvvpkvf refsgpkila tsferglrad dpviqslpqe rrnrlatnfl dlyfkeifew
      301 gvvqtdphsg nyriridpqg hdqlilldfg atrvydasfl ipyrqmvkgs lfnhrdmfte
      361 aalklgfike gdsaelksvf eafcfetvep fiefndprnt lgvidqqgny dwkntdlpqr
      421 lskkvfqiar qfsfrtppre iifldrktgg vfiflsilka kmrgrdlllk ylnkmd
//
LOCUS       WP_181606311             303 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Bdellovibrio sp. KM01].
ACCESSION   WP_181606311
VERSION     WP_181606311.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     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=33266
     Region          57..293
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mkknnfrsgs knnsqrssqg ssrppgsrpq qsggrsqggr pqqgsrsens iprewrivvg
       61 nhaikealym rpkkvkgmwl kngwessadl rdleemarkh hitpeirqea vidkfgsshq
      121 gaalfvegap gmdldhlgnl etsivlmldg iedphnlgai lrtswltnvk gvlipedrav
      181 gltptvhkva cggvehvave sttnfskyae tlkekgywiy glsprgkksi feldlpekvi
      241 waigaedkgl rvtterlcde lvfipqtsas asynasvata maltetlrqh aqrgkskksq
      301 sdr
//
LOCUS       WP_181607201             385 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181607201
VERSION     WP_181607201.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     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=43028
     Region          13..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 mktieffkks ffsaakypal tglralaayl vftrhypvle dvsptlssml tqgylgvaif
       61 fvlsgflihq tygltrrlse eglfvyfgrr fariyplyfv vciatfvyan nyepfdlfin
      121 ltmlkgffnd viftgvaqaw sltteetfyf capiifffak gwrrlalalg atycvggllt
      181 vigsqlnwlg ffediyftle wsffgrafef fagiglsmfl sarksvrsck lplatyigva
      241 gvmltlylla lvgqersdgl gifspqgifl nnwfsvvfiv lliyglates slfskllstr
      301 lfsllgkssy afyllqqgpl qnicdgndlt vaetfgvtil vsivvfalie epinhvirsq
      361 llkfkkrpvr liptpvpasa pspat
//
LOCUS       WP_181605652             123 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Bdellovibrio sp. KM01].
ACCESSION   WP_181605652
VERSION     WP_181605652.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 123)
  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 123)
  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 123)
  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 123)
  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 123)
  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 123)
  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 123)
  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..123
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..123
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13851
     Region          12..115
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mktqitetiv tecrrklilt kqdilnrira aqsafvhaek sgdegdvsaa hieehtflvs
       61 qermrnqlle iemalgriet gtfgvceete epieaerlla ipwtrlsieg aemreavgrk
      121 far
//
LOCUS       WP_181607251             360 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181607251
VERSION     WP_181607251.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..360
                     /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=41785
     Region          29..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 mahspqldgi rffafflvfl ahtprgmgid alqnigwigv dlffilsayl ltsimllein
       61 rtgsinlkhf fvrrclriwp lyfialffgf fvfpyfavrl gpiapsneys qlfqhfkyfl
      121 tfsqnistsi sqvktgnmla plwsiateeq fyvifpfiii wfsrkgfnkt filqfavtsi
      181 alsilfkyim lqnrkdmlaa ylnlptriep fmlgillaif sksvmnnpif rffnrniwil
      241 vpilifwsir hwphptagds niyiylingv afgiliisan idkslsnvff sskilttlgk
      301 ytyglyvwha viiygctqle ilnkniyllf itsltltvlv aklsydiiek rflrlkqkfr
//
LOCUS       WP_181607252             293 aa            linear   BCT 28-DEC-2024
DEFINITION  dTDP-4-dehydrorhamnose reductase family protein [Bdellovibrio sp.
            KM01].
ACCESSION   WP_181607252
VERSION     WP_181607252.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 293)
  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 293)
  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 293)
  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..293
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..293
                     /product="dTDP-4-dehydrorhamnose reductase family protein"
                     /calculated_mol_wt=32509
     Region          2..281
                     /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..12,33..34,55..58,78..80,82,97,119..121,144,148,
                     163..166)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187564"
     Site            order(98,121,144,148)
                     /site_type="active"
                     /db_xref="CDD:187564"
     Site            order(121,144,165,180,190,196)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187564"
ORIGIN      
        1 mkilvlgaag mlghqvwlkc lksfgvgnva atlrkskshy ekfeifkdge vfdgvdasdf
       61 dslskvlski kptvvvncig ltlrkeelgn iekcievnsm lphkltlwgn enacrvihfs
      121 tdcvfdgtkg nysetdvpta nelygkskfl gevggpnalt lrlsivgrel egkteliewf
      181 lsqsgrking ysrfmysglt tnfvadevvr lirdfpqlsg vyqvsseyis kydllgkane
      241 iyhcgvevmp ydgyvgnktl nceryakatg fikpswdqml ramnqdssvn ygv
//
LOCUS       WP_181607457             268 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181607457
VERSION     WP_181607457.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
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 11448200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..268
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29154
     Region          139..169
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(141..142,145..146,148,176,179..180,183..184,
                     186..187,215,216..217,220..221,224)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          145..262
                     /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          174..209
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          214..238
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mstkfskedl knpdqvtktl rqgfvwttth skivitavia fvvigagasl mgylsnkkev
       61 atqekyfsle ksytekkrgf eeaaraemma atakdkkgap afdpskkasg dmqkdfgtli
      121 tgfealinea pktvagqmaa lnlsdiylsy kkydeaaatl skveaglnks dltsglvwmq
      181 mgnvmadkgd ckaaiekwsv vtaskafsfa hdeaklrqgl cyetlndsak aeqlytevsn
      241 tadsqntdsi ssreaakylr llkakknl
//
LOCUS       WP_181607485             161 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181607485
VERSION     WP_181607485.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            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 10494393
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..161
                     /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=17386
     Region          38..159
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD/TolR; pfam02472"
                     /db_xref="CDD:426791"
ORIGIN      
        1 mrtsfvnank qrsplmeaqt lkpggkkkss garglalalp ltslidafsi iviylligtq
       61 sngievksgq mnlpiaehsq gvdkemailr iekgnyfind ervvgsqlgs kleslkkdsk
      121 edvelmiqad temkyadldp iikagslagi eklkfavvpk q
//
LOCUS       WP_181607293             338 aa            linear   BCT 28-DEC-2024
DEFINITION  TRM11 family SAM-dependent methyltransferase [Nonomuraea soli].
ACCESSION   WP_181607293
VERSION     WP_181607293.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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 338)
  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..338
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..338
                     /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=37125
     Region          104..333
                     /region_name="Trm11"
                     /note="tRNA G10 N-methylase Trm11 [Translation, ribosomal
                     structure and biogenesis]; COG1041"
                     /db_xref="CDD:440663"
ORIGIN      
        1 mpryallilp afnrvygesa vrltrselav fgtatrspis aieesviggv pyvtfeaels
       61 eddvallsnl ssvyavfgve gpllrplemr pldrlssdll tiqkyagktn ehftklllnv
      121 tllasglpfd grlsvfdpmc grgttlnqal mygydaygmd vdakdfeayt vflrrwlkdk
      181 rlkhtaevvp vrreralvgk rlnasfalsk eaqkagdvqq vavvnadtlr areffkprsf
      241 dlvvtdapyg vqhgsrsggg glsrspldli aravpgwael lrpggaigis wntygggrde
      301 lgeilvkhgl rvreypdfeh rvdqaivrdi mvavkpar
//
LOCUS       WP_181606965             289 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Bdellovibrio sp. KM01].
ACCESSION   WP_181606965
VERSION     WP_181606965.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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 289)
  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 289)
  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..289
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..289
                     /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=31090
     Region          1..283
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mkkpsvlltw vtsiaitlsa capgsgdstv slnddssgvi ngtkvtarrd dgsrgvvlfl
       61 pvnslgmtvg ictatllsnh sfltaahcfd kkksptlsrf kivfanekgl fnprehtrsg
      121 sqivihpefr yskvgilndm aigffaggip agfepieier dqnrnyqnqf lniygygktk
      181 dsaeifaigy gsagelhkav vkvnggyglm qdryailsng ntqficsgds gsgqfinvng
      241 vprligvtsf vtgekkfagh vtctkgrsta mkvsyfakwi devheearl
//
LOCUS       WP_181607758             259 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Bdellovibrio sp. KM01].
ACCESSION   WP_181607758
VERSION     WP_181607758.1
KEYWORDS    RefSeq.
SOURCE      Bdellovibrio sp. KM01
  ORGANISM  Bdellovibrio sp. KM01
            Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
            Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Bdellovibrio sp. KM01"
                     /db_xref="taxon:2748865"
     Protein         1..259
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29390
     Region          16..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 mvcvllasvp alakpikilv edswppfafk kenravgmsi divraafknv genielvqvp
       61 ytrckaqtat gryvacfnsa hskemdadfl fpkeplfksk gliiankitv rskpakvkdl
      121 egksvalpae fpfgkefden tqinkiftss dqtslmmlks nrvsyvaide fvyyyylktn
      181 pdfknqfhvv lelseepifv hfskkhqdta dlikkydigl amlkvsnryn eiledwvgvk
      241 gqkrvqifsv lpkthaydy
//
LOCUS       WP_181607939             540 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181607939
VERSION     WP_181607939.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..540
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..540
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=56580
     Region          8..116
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          255..517
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtvvtardll ndpafhgyrl lggasgldhv vrnaaqiqtg adlsriapgs vgvtdlgdra
       61 gvsaqhlvev fcrrlhgrgg rmlvivgnve aatqstirla drfglplvav aptsipasaa
      121 altarllglv qqpellyara magvvsklvt adtlervvai aaealrgtaa vvaaegrivs
      181 gglrwatpeq vtrhatitte rlpdhawasc pvpgsghrlw lvaetadggp awqeaaravt
      241 qtaavaagaw vahdrlrqer drarlagllt ellqlegapv ipehvarraa ragivldgwh
      301 vgvhltwgyg geqtsadltp qltsaleeeg falpvferad gwsswvtspe rpseqevgll
      361 aarlrkvlaw fnaayaenrs fvplaagvgr patgpaavaa tlgqahqaal taasdgpgvv
      421 ehiddvgpeq lmwrwfttea freqaarlla pvlaapdsgm llrtldaylt cgsspgetak
      481 aiglhrntvt qritvlerll ggpvasldrl alhlacrslt agasrtpggg hpapartphl
//
LOCUS       WP_181607954             373 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea soli].
ACCESSION   WP_181607954
VERSION     WP_181607954.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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 373)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..373
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..373
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39370
     Region          32..359
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mtkktlttal aaaliaagtv aaapaqaavq leipavtgqs pvgrevlhlv drdrvdpwtg
       61 kgprelmvsm yypalpggga tapymtieea rlllkgqkrd qpgaaemvsa tkvnakagaa
      121 pargrhplvv lspgftlprg lltglaedla srgyvvaavd hanesygtaf pggrittcva
      181 cdkvkeggla evaegrakdv sflldrltgp rsawpyakmi drsrigmagh siggntaarv
      241 maedrrvrag vnldgtfftp vdglkrpfmm vgtrsghspg gvdaswdrsw qrlggwkrwl
      301 tvkdtghlsf vdlpvlgaql gmvdpaapls gkrsgeipra yvgaffdrhl kgenepllda
      361 ptkdnpevaf hqp
//
LOCUS       WP_181607995             752 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181607995
VERSION     WP_181607995.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 752)
  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..752
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..752
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80767
     Region          2..749
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          512..538
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(514..515,518..519,521,551,554..555,558..559,
                     561..562,591,594..595,598..599,602)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          549..579
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 maeesfahll rrlrvsvglt qeelahrstv sarsisdler aiyrtarket trlladalel
       61 sgparaqfea targraadpa lsavlslpap ltslvgreae iaaicelver qdvrlltltg
      121 lggvgktrlc laaaqrlspa fpegvffadl taagtpelal aavaqaagvr ddgagplart
      181 lvehlrgrqc llvadnfehl adraaeilgg llaecpgltc lvtsrrtlrl rgghevavrp
      241 lrtpdpssst aelaanpava lfsqcvrahw pdwrledssp avvaricarl eglplalela
      301 aarmkvltse ellrrltgrl allspgsdrq gglratldws hglldegara llarlsvfag
      361 gwtlesveei cgcelddlat lvdnslvhrs gtrfvlletv reyaaellga aesaemglrh
      421 ldwfadlaer gdreligagq rhwlallvde qdnlrraiah alelgdatra qritgalwrf
      481 wemhgrlaeg rrwlelaldl pgdsppvvrg lafkaagnla rdqgdrasar eshgralemf
      541 eaagfapgva tafnnlanil ldegdheaaa ehferglerf lalgdrwnta llrvnlalal
      601 rkttatlgra aslaresiee frglgderge aravealari ldhggdhrgg aelhvraval
      661 rhavgdrggl arsmeglaha lsglgeaelp awllghaaai rtatgdcrna ddefewqdtv
      721 rglrerlgdv ydaqwaagra atteealgrc ta
//
LOCUS       WP_181608055             133 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181608055
VERSION     WP_181608055.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Wintjens,R. and Rooman,M.
  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 133)
  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..133
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..133
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14335
     Region          24..79
                     /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(27,31,56)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(30,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(37..38,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mddddlpllp gfremamarr dmierlaeer rssglsqtev aarmgtsqsa varlesgead
       61 vrastlerya aaighriswr lsldavtgtp septetdhgs glvreprpll dprtppstgg
      121 glgsrrlrrp grs
//
LOCUS       WP_181608080             410 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181608080
VERSION     WP_181608080.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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..410
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..410
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44820
     Region          11..410
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 manheshgfs stglrrlhet larhvdsgkv pgvvalvsrg rqthvealgt mavggsapmr
       61 rdtifrmast skpvtvaatm vlvdecrvrl ddpiqqwlpe ladrqvlkri dgplddlvpa
      121 rrpitvrdvl tstfglgldf tavgtpifna ifeqgltpnl pvpmpepdew lrrlgtlplm
      181 sqpgerwqyh igndllgvlv arvsgrpfee flrerifdpl gmkdtgfhvp adqlyrlpdl
      241 yapdpetgef hvwdpadggr hsrppafpsg ggglnatvdd ydayfrmlln ggvhngrril
      301 sraavrlmtt nrltaeqnaa rdelardnvh isfgqgqhgg wgfgmavrty qsdyapigqf
      361 gwdggsgasa yadpvngltg ilvtqvglsv pnsahvfhdf wttvyqaldd
//
LOCUS       WP_181608132             466 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Nonomuraea soli].
ACCESSION   WP_181608132
VERSION     WP_181608132.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..466
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..466
                     /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=49233
     Region          1..459
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mahdvtvvgs gpnglvaail larsgrrvll veaagtfggg lrsaeltlpg vvhdvcatvv
       61 pmalaspamr alrpdvefah ppvaaahpld dgpavllhrd lertvaelgp dgrawratvg
      121 tsahqdlidt llsplglpra plraarfgly gappatalar lfrtgraraa fagmaahsmi
      181 dlrlpitagy glvlaslvhl agwpvvrggs grladalvaa frelggetva ghrvrslrel
      241 dsptvvldae pvqfaadfpe pygrrlrsfr hgpgvfkldw aldgpvpwrd pevaragtvh
      301 lggsleeivt seaetfrgrh sprpfvllvq pyaadptrgg hplyaychvp ngstrdmtae
      361 ieaqierfap gfrdrilarh amntadlaah nanyvggdig gglatlgqfv krpvwsltpw
      421 rtplpgvylc sastppggsv hgmggwqaar liahdarrpa rlrgqa
//
LOCUS       WP_181608227             264 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181608227
VERSION     WP_181608227.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438138
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..264
                     /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=28817
     Region          3..256
                     /region_name="ModF"
                     /note="ABC-type molybdenum transport system, ATPase
                     component ModF/photorepair protein PhrA [Inorganic ion
                     transport and metabolism]; COG1119"
                     /db_xref="CDD:440736"
ORIGIN      
        1 myaleltgvt vnvvgrtlla gvdwqvgyge hwvvlgpnga gkttmlslaa avrhpsegtv
       61 tvlghrlgrv dmrelrrhlg lvsasqhlid eelleeegat ahtvvltght gtsaplwdry
      121 gpaereratr mladlgckel gerpfrvcsq gerarirvar almpepsvif ldepfagldl
      181 paredlieav eelagnrpml ttvtvthhle eipattthal lmkdgrvlaq geveqvltge
      241 llsecfgrpl rverdggrwy grrg
//
LOCUS       WP_181608203             603 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Nonomuraea soli].
ACCESSION   WP_181608203
VERSION     WP_181608203.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 603)
  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 603)
  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..603
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..603
                     /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=64678
     Region          37..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 mkqfpeisrr qalgglsata alalagwpga ahaspggpvt itvmgtsdlh gncrnwnyfn
       61 ddvykdsagn higvakvssl vkqirkdrge kytllfdsgd tiqgtpltty yakikpitet
      121 gelhpmaram nplrydavtl gnhefnygip llnawaeqmn apvlganalv hgtgkpafrp
      181 yivkrmrvpg qgrpilvgvl gltnpgsavw dkdnvdgkld fedivvsark wvkvlkdqer
      241 cdvvvvtaha gddgfssyld vnnggtipve nasklvaqqv pgidviifgh ahkeekgyla
      301 sgpngeqvlv cspskwgmrl avvdltlawk rgrwtvtakt sttvnantva edpeivaavd
      361 aqhevtkkyv ntvvatstea msaaeatykd apiidyiqyv qtkvvkeaia gteyaslpiv
      421 siaapfsrta afpagevsik niaglyifdn tlmakvitga qikdyledsa dyfntvpvga
      481 pvdvatltna vvngqatpdy nydhmagvsy didiskpags rivnltfega pvdpaqrfvi
      541 avnnyratga gqfrhiagap tiynkqveir qamidtavae gvidpstfav snwklvregv
      601 pvf
//
LOCUS       WP_181608308             252 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea soli].
ACCESSION   WP_181608308
VERSION     WP_181608308.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..252
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..252
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27658
     Region          4..246
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mplmagaepy rheagqvgvl lchgftgtpq slrpwaeyla ahglsvslpr qpghgttwqe
       61 mnrtrwedwy selekafqdl rgrcpevfva glslggcmal rlaqvhgeai rgvvavnpsi
      121 andvpllria pvlrwfvrsv pgvandvkke gvtelaytrt pvaaastlpr lwslvqaele
      181 kvtqpllvyh stddhvvkpt svaiirrilp ntqieelsds yhvatldnda dtifagsldf
      241 irthasvplq rd
//
LOCUS       WP_181608246             539 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Nonomuraea soli].
ACCESSION   WP_181608246
VERSION     WP_181608246.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 539)
  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..539
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..539
                     /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=55656
     Region          15..483
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mpslrpllpe dppsvgpyqv harlgsggqg tvfaargsdg asvavklldp pldgardrfl
       61 devetakrva pfctaqvlds gfhgsrpyiv sefvdgpslq esvrdsgprg agalqrlain
      121 tvtalagiha advihldfkp gnvvlspdgp vvidfgiara vdltrssiss qivgtpayma
      181 peqfaggpvg aaadlfawaa tmvyaatgrh afpgeripal mhsivygepd lgtledplrg
      241 illeclakda slrpsaasva erlralpapa wqatvesarp pastarppag pahppaltdr
      301 ppavqahppa vparptqpsp avqasapghh prrlrrrlaw agavvlvata gtgyalwpsd
      361 pitvppasaa tttpsptlnp vspsptttpa hrdrqrqepg krktaaptsp arspkgdtnp
      421 gptaqttkaa vqpeptpdrt tarpsskpss kpstkptatq spvptsepka aesgtlvwad
      481 aeafcaakgg taagswynls citsgmdfys phqvcqwkyp gttagvptgt qgsvdcrks
//
LOCUS       WP_181608457             220 aa            linear   BCT 28-DEC-2024
DEFINITION  cell division protein FtsQ/DivIB [Nonomuraea soli].
ACCESSION   WP_181608457
VERSION     WP_181608457.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..220
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..220
                     /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=23212
     Region          2..220
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mrartllivl ltacvvgsaa wlvfgspvlg vrsvaivgnl tvatdeirrr aavpelqpla
       61 tvdlagvegr vmeirklaav evsrswpstl tievverepv avvpvngkaa lidregvvte
      121 irdvapprlp vlkldrpgpa dpatraallv vnslppdlar qvdqiratsa dgvsllladg
      181 rqvvwgapdq aeakirvlgt llakkariyd vsspdvvtvk
//
LOCUS       WP_181608476             123 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea soli].
ACCESSION   WP_181608476
VERSION     WP_181608476.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=13523
     Region          1..94
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtppdieaia eqvfqaladp trrailarla ahgpatatdl adhlpitrqa iakhlalltd
       61 aglvsperge wrrvryrlhs apvrlaqqfl aalahdwddr lqalgehlds stplprhndq
      121 rpd
//
LOCUS       WP_181608582             168 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Nonomuraea soli].
ACCESSION   WP_181608582
VERSION     WP_181608582.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..168
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..168
                     /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=18382
     Region          50..163
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mrrahavtgs tvffllapgt vaalvpwwit gwrmlsplps wamlplrvvg vllilaglpv
       61 lagafvrfvv eglgtpapva apeklvvggf yryvrnpmyv avfaiilgqa allgqgslvv
      121 yaavvavpvy lfvrfyeept lrarfggdyd ayraqvpsww prwrparr
//
LOCUS       WP_181608651             194 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea soli].
ACCESSION   WP_181608651
VERSION     WP_181608651.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=21605
     Region          7..78
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnrkldartl ksfthplrlr iyelledqgp qtattlavel gentgatsyh lrelakhgmi
       61 eiaegvgkgk ekywrvtpgg fmtgppweek dpaaaagaev mldstlrrrg eelarwreeg
      121 attpqewiea svlahrvfrl tapemgemtr evlavleryr lmseahverr tedaarvvvh
      181 fdtfpvgvsa appa
//
LOCUS       WP_181608596             272 aa            linear   BCT 28-DEC-2024
DEFINITION  segregation and condensation protein A [Nonomuraea soli].
ACCESSION   WP_181608596
VERSION     WP_181608596.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=30215
     Region          11..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 mtsgeveqqq gfqvhldvfe gpfdlllgli skhklditev slskvtdefi syirsrgpew
       61 dldqtshfll vaatlldlka arllpsgeve deedlallea rdllfarllq ykaykevasv
      121 fsglmareal rhprivpmep afadllpelv lgigpdqlar iaaraftpkl pptvnlghvy
      181 qplasvreqa ailvahlrrl rvatfrqlta dcegtievia rflavlelfr esavtfeqle
      241 plgdlhvtwt gtddgdvavg ddyeeenrsd de
//
LOCUS       WP_181608309             237 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Nonomuraea soli].
ACCESSION   WP_181608309
VERSION     WP_181608309.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=26240
     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 mfywvakail apilhllfrp wfegidnvpk qgpvilagnh lsfadhffgp lqlkrkvisl
       61 gksdyftgrg ikgfftrlff sgvgtvpidr sggkaseaal rtglrilreg qilgiypegt
      121 rspdgrlykg ktgvarlale srapvipwam vntfemmppg hplpkmgirp gvrfgkpldf
      181 sryygmeddr lvlravtdei myalmelsgq eyvdkyaasa rvemeraara assaesr
//
LOCUS       WP_181608588             368 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nonomuraea soli].
ACCESSION   WP_181608588
VERSION     WP_181608588.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 368)
  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..368
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..368
                     /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=38225
     Region          23..364
                     /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 mrlterlgid vpifafshcr dvvaavtnag gfgvlgavay saeqldtels wldretggrp
       61 ygvdvlvpgk ldargvrvad lipeehrafl dtlfskygma ppsratgsqa gsaaddvarr
      121 vtasgatgli evalkhrigl iasalgpppp emvalaread vpvaalvgtv ehalrqreag
      181 adiivaqgte agghtgeist mvlvpqvvda vapipvlaag giasgrqmaa aialgaqgvw
      241 cgsvwlttee aetpqavkrk flaassldtv rsrsrtgkpa rqlssawtre wdgenspgpl
      301 gmplqmllae gamatigpaa ergepgavel anyfvgqvvg qldqvkpakq vvyemiseya
      361 eaverlap
//
LOCUS       WP_181608670             421 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea soli].
ACCESSION   WP_181608670
VERSION     WP_181608670.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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 421)
  AUTHORS   ter Beek,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..421
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..421
                     /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=45182
     Region          42..414
                     /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(147,149,273,275,306..308,347)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrkwtrvgag vfgaivalsa cssgtgsgag tqapkeasgp vtlsyavwda nqkpvmeela
       61 aefskanptv kvqvqltpwa dywtklkaaa tggaapdvfw mngpnfqlya sngvirpiee
      121 qvdasvypkp lvdlytyqgk lyglpkdmdt igvwynktlf daagvpypkd gwtwtdfqqa
      181 aakltdagkg vygtaaqlgs fqeyqyntit qaggyvispd grksgyddpk tiaglkfwtd
      241 litakhspdl ktmtdttplq lfeagkiamy wggswnvtef sgndytkdkv dvaplpkgek
      301 qatiihgvan vmsaktahpa eawsfvkflg skqaadllgk kgpipaytgt qgdwvgahpe
      361 fklqtfldav syaapfpvsk ntaawneael tqltkawtge vpveqaaatl aatmndllak
      421 e
//
LOCUS       WP_181607786             107 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181607786
VERSION     WP_181607786.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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..107
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..107
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11991
     Region          <62..106
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mpklgsvqiq tlrealeeql rwriaqlael kvtvagisae eptwqdamss iaaadqaiaq
       61 teesldrlaa gtygtchdce adiaferlkv rplarfcmdc qrrrerw
//
LOCUS       WP_181609194             297 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea soli].
ACCESSION   WP_181609194
VERSION     WP_181609194.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..297
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31632
     Region          21..287
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mirslwwaad tggeppfgta hlkvyypare pgrltgtaap dggpypvvlf vsginvgqds
       61 yrwlatevar agfvcvtfdr vaelfggeyg ltpgvdleaa tpewygtrpt cpaigsilss
      121 leripllkga ldldrvalgg hsaggsvvlq sarhfpqvka vfaygahtmv atmlgwpagt
      181 vlpaqvdcpv llvggtrdgv imgsadryge rrhasdpvtr tfeealtdrd gqhvlalfeg
      241 anhfavadpv dptaarafld lepeteprse iaqlitaflr thlygeahsl pgasrrr
//
LOCUS       WP_181609044             461 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Nonomuraea
            soli].
ACCESSION   WP_181609044
VERSION     WP_181609044.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..461
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49245
     Region          23..417
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtstdvrppa daertpprts twsalkplvl rlhfyagvlv apfllvaaat gllyaasfql
       61 erivhahelt vpagqqrvpl aqqiaaaqaa rptgtitavr ipaeadastr vlmnvpglpe
      121 stqlavfvdp ytaqvrgtle syggsgalpv rawisqlhrh lhlgepgrly selaaswlwv
      181 valgglvlwv trrrskrrvr allapdrslp asprrlswhg siglwavlgl lflsatgltw
      241 skyagenvgd vrvalgwttp kisaasgdha ahagagghrh ggtvsadelv raaagkglsg
      301 pleivwpake gapfvvkeid ktvpqrldqv avdgtsgqvt aelrfadfnl aakltqwgid
      361 ghmgllfgla nqlvlmllaa gvitlvilgy rmwwkrrptr gfgrpyargg wrgvrwavla
      421 plalvvagig wflpvmgfsl aaflvvdvll glrararppv g
//
LOCUS       WP_181609379             425 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea soli].
ACCESSION   WP_181609379
VERSION     WP_181609379.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..425
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..425
                     /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=45716
     Region          1..368
                     /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"
     Region          <191..>255
                     /region_name="ALDH-SF"
                     /note="NAD(P)+-dependent aldehyde dehydrogenase
                     superfamily; cl11961"
                     /db_xref="CDD:448367"
ORIGIN      
        1 mkalivgggl sgpllsifls arghevelve rrpdprtspp aggrsinlgv sargiralra
       61 aglwaevrkl avpmrgrmvh lpgrapafhp ygrsrdqilh svrrdglasl lveraekqsg
      121 vrltfdtpcl avdpdtatlt lpgrqvtgdf vvgadgassv vrtalhrrla gnfrrdhlew
      181 gyleltipas aglpiealhl wpgsgglava hpnldgsltc tlflprqgsd paaliagqlp
      241 gltalipdlp dqlaaaemst lttvrtspwq hdgrvvlvgd achavypfyg qgmnssfedc
      301 vvldrclgeh ppaeafaaye rarrphtdvl aelsernffd lrdgvrspla varkrldlel
      361 hrlfphawvp lytlvshttv pygdalrrar tqeriaaaaa gltgaalvaa tgiaarrfrr
      421 ertst
//
LOCUS       WP_181608521             526 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase [Nonomuraea soli].
ACCESSION   WP_181608521
VERSION     WP_181608521.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 526)
  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 526)
  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 526)
  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 526)
  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 526)
  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 526)
  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 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..526
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=56512
     Region          15..519
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 msprlalvgl llavslpaca aaperpsvap glalvpqpvs vgrpegsavr ldggsailig
       61 pgqpeeiqaf agqlrevtgl plpvresgea aitldalgps elgregyllk adgritlrah
      121 taeglfrglq tlrqllparp ggqvsvpavd isdrprfayr avmldvarrf vpveqvkrli
      181 dqaaqykvnv fhwhltddqg wrvpvegypa ltgvgastqa gwsggpwfyt aqeirdvvay
      241 aaarymtvvp eidgpghtaa amasvpelnc sgrarqpyqg fdvkvsvlcl knteavgrfv
      301 stvfrevsal fpgpylhigg devpsttaad yaayirtaga avtangkrvi gwhqigegpl
      361 ppgsvvqywa pdgedsdlva kalaqgakvv lspadrayld mkydagtpyg lrwagfvpve
      421 kayawepaem lglreeqilg vgaplwsdra yrdstslpts heqypepsvy ldhmafprlp
      481 alaevgwssa dsrdwegfrs rlsphaarwe aqgigfhrsr eiewtg
//
LOCUS       WP_181608740             209 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Nonomuraea soli].
ACCESSION   WP_181608740
VERSION     WP_181608740.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 209)
  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 209)
  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..209
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..209
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21399
     Region          26..>157
                     /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 mldvhdpllg allllialaa egslllgllv pgdlailavg galngpaela lagvaglagc
       61 ylgasggyll grsfgpgiry gragrwvgdr rwrraealvg egvvlslayf lpvvhaltpv
      121 lagalgvpyr rfvrramaga mawvglyllv gnlagsaare hhqlivpvaa avavivagva
      181 wlverivkak spsrsepcds apadrhvar
//
LOCUS       WP_181609404             250 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea soli].
ACCESSION   WP_181609404
VERSION     WP_181609404.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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: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=27444
     Region          35..129
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 miernvifge aveqyesara gypdqlisdv layagpgpvl evgagsgkas vgfaargvdl
       61 tcvepdprma evlrghcpra rivvgvfedf epdrafqlly caqawhwvdp errsdlahaa
      121 lapggglalf wniysvadpa vhralaeida rngvdgsslh rysasdlddd ffardhglaq
      181 drrftdleer ryrrsewypa eryldlirsi sayrilpagq reallgdmag vigdgldlti
      241 ltdlalarra
//
LOCUS       WP_181609432             286 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181609432
VERSION     WP_181609432.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=30126
     Region          4..285
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mqvpaqfeya raqsvshals lldrygpear vvagghslip mmklrlaqpe alidindlse
       61 lsrievegge lvigalvrha ellasapatg lfpifqdaer viadpivrnr gtvggslcqg
      121 dpsedlsavf aalrataiie ggdgrrsvpi rdfhegpyet avqagellie lrvpatpgtg
      181 sayvkverrv gdwavaaaga vlsvaggvie ragigltavg aehfcapeae eyltgrepge
      241 eafaeagria aehcspqpdq rgpadykrhl aaeltaralr tameri
//
LOCUS       WP_181609441             295 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nonomuraea
            soli].
ACCESSION   WP_181609441
VERSION     WP_181609441.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=32024
     Region          2..287
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkvtvtgarg kvgraavqal qraghqvtat dlgpavhere lpeearylqa dltdaaaaaf
       61 vvrdadavvh aaaipdplan pphvvfgnnl matfnvlega vrqgvtrfvn issetvpgff
      121 fperpclpvy apvdedhptf pqdpyalskl fgeqlmdaav rrsdircisl rpswvqhegn
      181 yernlgpqvr dhsvigaglw syidvydlad aivlacesrl pghevfyias pdnagghdfa
      241 avlrahygqa ielrpltrtd ssgidcskah rllgwtpkrs wrdyldadgr tlpgg
//
LOCUS       WP_181609266             246 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Nonomuraea soli].
ACCESSION   WP_181609266
VERSION     WP_181609266.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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..246
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..246
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=27149
     Region          3..204
                     /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 mteirvmivg dsishgssgd wtwryrlwkh lcahdvavdl vgsrdhldni rteecgdgdr
       61 tyadpafdtd hdaqwgrpyl lekaaieakv aahrpeymlv llgindlfwy gvdpqafean
      121 lrefvtnarr aapalrfvvg amlptqrahd dlafatrvav cnlriravag elstpespiv
      181 vantdaefva aehtwdgthp nprgefriaa afadalaawy tvgapyprpy pdaddiapda
      241 krplia
//
LOCUS       WP_181609566             262 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181609566
VERSION     WP_181609566.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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   3  (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 12820769
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=28528
     Region          1..252
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          169..250
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mihsvpalgq aepyemivrr spphlrpyvl gavgfrtrta edarmlplna atlivdftgm
       61 spivtgprat atfavrtpwr hgmavgltpa gmsaltgapv revagatvpl adllgvraee
      121 lagrlgests wderfallwe rltawlrpgp grdhlimsaw wrlqapdcpr tiaglaaelg
      181 vsrryvelgf rrvvglspkt variarfqrt mdswrrpsat ldaalscgfa dqphlsreir
      241 amsqltpgql fafvqdtgrl ae
//
LOCUS       WP_181609698             323 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea soli].
ACCESSION   WP_181609698
VERSION     WP_181609698.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=35632
     Region          31..323
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mtlstaappa gpaekaparg rpgrrpirra flrdwqlytl aivplaffvi fryapmigni
       61 iafrrfqpgg smfggtwvgl ryfemfladp tfwrvftntv iigllstvvc fplpivlalm
      121 lnevrnhafk rfvqsvsylp hflstvvvaa ivmqlltvdg pvnqllsftg gppvaflqea
      181 dlfrtiyvss evwqtvgwgt iiylaaltti deqlyesaki dgagrlrqiw hvtlpgirpt
      241 iitllvlnig tfmavgfeki lllynpatyp tadvistyly rlgvvsgnfs yataiglfea
      301 viglvmvfga nllsrrtvga slw
//
LOCUS       WP_181609478             261 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea soli].
ACCESSION   WP_181609478
VERSION     WP_181609478.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   5  (residues 1 to 261)
  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..261
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..261
                     /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=28062
     Region          1..261
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mtaiylyptl ilygfrkhat yvwaalagaf tnsvfgilra yvlialwqar phlggydvvd
       61 avtfcfvtqa migpmqlfgg glgiperirs gdialdlvrp aslqawtlae dlgraayllv
      121 vrglpptllg allfglthpd gpdrwalfgl sfllgvvvsf awrylvalsv cwlidergva
      181 tvsmilmtff sglalpltif pgwlgelars lpfaamvqvp idvylgkgdg lafqvlwaav
      241 llalgaagtr lvrhkvviqg g
//
LOCUS       WP_181609615             327 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nonomuraea soli].
ACCESSION   WP_181609615
VERSION     WP_181609615.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 327)
  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..327
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..327
                     /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=33365
     Region          9..314
                     /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 mrptvaavlg tevsllqsgm ggvsgtelac avsnaggagc aggyklagap ltamldrlae
       61 gtdrpvglnl vpevvgpdel drqvtqilae tpghvylslf gmpddsvler vaaagrklvv
      121 qvgtvadgvh aagygavvva qgieagghll ghagrdelva glrerlpgac lvaaggigsp
      181 hearralaag adgimlgtaf vvtyesrahp yfkravcaae addtvitdvy eigwpgrrhr
      241 vlatdvtrnp hqpknfigrt vvegqtflvp rfsaavptdt ttgkieemal ycglscgail
      301 gelaaadvva qfarilpgae ivesgkg
//
LOCUS       WP_181609859             152 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            soli].
ACCESSION   WP_181609859
VERSION     WP_181609859.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..152
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16676
     Region          15..114
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msrttmgapn lgwtdpecpv artldlvgdr wsllvvrdam dgarsftefq rrtgiarnil
       61 adrlrkltah gllaqraapt grrqeyvltd agrdlfpvil tlrqwgerha fapgethstl
      121 vdqhgipvpe iaptsadgtl ldadtthvqk tr
//
LOCUS       WP_181610095             291 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nonomuraea soli].
ACCESSION   WP_181610095
VERSION     WP_181610095.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 291)
  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 291)
  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 291)
  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 291)
  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..291
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..291
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30923
     Region          36..257
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mrrllrrrqq veaeiageva aaaavatlpv apdtqaaaff dvdntmmrga siyhfargla
       61 trgmfstsdl vkfavgqaaf rlrgsenpeh iavaretala fvagskvedv vrlgeeiyde
      121 amadriwagt ralaqahlda gqrvwlvtat pvelarviaq rlgltgalgt vaetadgvyt
      181 grlvgdllhg pakaeavral arregldltr ctaysdsand lpmlslvgha vainpdsels
      241 eharkhdwpi kdyrtgrkat miaipvaaga gvvaggiaaa lalrrhyrrk a
//
LOCUS       WP_181609468             953 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181609468
VERSION     WP_181609468.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 953)
  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 953)
  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 953)
  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 953)
  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..953
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..953
                     /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=102785
     Region          1..241
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          119..933
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          746..774
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(747,750..751,754..755,757,787,790..791,794..795,
                     797..798,827,830..831,834..835,838)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          785..815
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          826..852
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfkvlgplv aeregqelhl ggalpriila tllleagrpv pieriieaaw gadapgtarn
       61 qvqirisqlr rglgdtaspy rrlvtrppgy llrvepgeld laefeeltar aeaeepktaa
      121 mtlrralalw rgpvlaglds pmlapvaqdl eerrllahea cvaieldagr hdelvaelrg
      181 lardhplrer vhgflmtaly rsgrqaeale afrayretlq etlglepgde lrtlevsiln
      241 qhpgldlpgg ggsrsprapr qlpplidplv grtaergrlr allapapgeg sgdgeppvav
      301 vvgrpgigkt alalqvahdl iarhpdgqly adlgesrpra sdvlsrflra lgaaavpqte
      361 qeraaafral tagrrvlvll dnaqsaeqih altpggdssa vlvtarrrpa dlpdhrvlal
      421 qplgtaeava lltrdigpar agtapgalre laaqcgglpl alriagarla arpqwsietm
      481 vtmlgdthsi ldtlsygdse vraglrvayd slspqarrll relglldcsq sgewlasllt
      541 gdpgdarael veasllevsg grlrlhdlvr afareraaaq eshdrrtava erfcsvvlhl
      601 agrahvhhyg ghftllrgqs lppgpperea ddllgddpig rldeerevlm aavrlsaahg
      661 lhelcwnlam tcvvlfetrg yfddwrtace taleacrtag dtrgeaamly slssmllfrq
      721 lyaeaqepls qaltvfdaig dlhgralalr nvallertrg lqetalasyg ralpllriag
      781 drageahvlv nmaaihvdad rldeaetllg ralaifraeg vgrgqaqalt riallavrrg
      841 dqdralelye eagtlvraeh dtigeayvlq gtaealiafg rvpearatlg rvlelaeavg
      901 erliegrahl glgslpaenh etarrhldra helfsvmgaq qwraraaeal arl
//
LOCUS       WP_181609899             508 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181609899
VERSION     WP_181609899.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   2  (residues 1 to 508)
  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 508)
  AUTHORS   Rosinski,J.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..508
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..508
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=55531
     Region          3..>69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          74..503
                     /region_name="MurA"
                     /note="UDP-N-acetylglucosamine enolpyruvyl transferase
                     [Cell wall/membrane/envelope biogenesis]; COG0766"
                     /db_xref="CDD:440529"
ORIGIN      
        1 maddylgrig rlirdarqhr gwtqlqlada lgtsqsavnr iergnqnisl emiarigeal
       61 dseivslgya gpmhlrvvgg rrlsgaidvr tsknacvall caallndgrt ilrsvariee
      121 vyrilevlss igvrarwvng gdleivppsr leleamdtea arrtrsvimf lgplmhrfeq
      181 ftlpyaggcd lgtrtvqphm talrqfglev aatqgfyhaq vdssvsptra ivltergdtv
      241 tenalmaaar hdgvtvirna ssnymvqdlc ffleelgvkv egigtttltv hgvpvidrdv
      301 dyspsedpve amsllaaavv tgseltirrv pvefleiela vleemgldce rgleyaaang
      361 rtrlvdltvr psklvspidk ihpmpfpgln idnvpffaai aasaqgstli hdwvydnrai
      421 ylteltrlga svklldphrv lvegptrwrs aemmcppalr pavvvllaml aaegtsvlrn
      481 vyvinrgyed laerlnavga rietfrdi
//
LOCUS       WP_181609905             308 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181609905
VERSION     WP_181609905.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..308
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33774
     Region          6..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 maepliqarg lvkrfgdfta vdgidlevap geafgflgpn gagksstmrm iscvsmpsag
       61 elrilgrdpr vegpairarl gvcpqldnld pdlnvrenlt tyaryfglsr aqarakaeel
      121 lefaqlteka sslveplsgg mkrrltiara mvndpdlvll depttgldpq arhllwerlf
      181 rlkqrgvtlv ltthymdeae qlcdrlvvmd rgrivaegsp rqlieayssp evvelrfgld
      241 elaglvpllq gvgervdplp drlllyakdg daavnevhrr gltpssvlvr rssledvflh
      301 ltgrtlvd
//
LOCUS       WP_181609762             366 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181609762
VERSION     WP_181609762.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 366)
  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 366)
  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 366)
  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 366)
  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 366)
  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 366)
  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 366)
  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..366
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..366
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40291
     Region          76..217
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mlrapaetky adeldylesi dtgpkpftwr lsprmvrifv lgsersdgld reiaqkwfgd
       61 rsfversivt lasdrgllli gdpgtgkswl aellaaaicr nstlvvqgta gttedhikys
      121 wnvsmviakg qsrqsmipsp imtameqgmi grfeeltrst sdvqdalisi lsekyvsipe
      181 ldddnivfaq pgfsiiatan srdrgvndls salkrrfnfv ripvvtnkks eaeivrfrta
      241 ellrrhqiel elpptlldil lqsfadlraa sdaaagdddr lesalstaeq igvledailh
      301 shffgdrtlr aqtlagslvg slarrspedl ailnkywhgv veprgreggd wgdfldggrq
      361 aistls
//
LOCUS       WP_181610056             319 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nonomuraea soli].
ACCESSION   WP_181610056
VERSION     WP_181610056.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=32574
     Region          11..314
                     /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 malstsftql lgvrhpiala pmggsaggal aaavcrgggl gllggaygda awlareapiv
       61 aatglpwgig fltwsidata veraleydpr avmlsfgdps pytrsvhdag allilqvggl
      121 eearravdlg adlivaqgte agghgalhgr stlpfvpavv dlvapvpvla aggiadgrgv
      181 aaalalgaag alvgtrfqat aealvdpsvt kaivegrgqd tersrvldia rgsawpqeyp
      241 artlghpyld rwrgredela adprarqdyq ddvargaipp lpvwageavd liadvpsard
      301 lvvamaaqae eslaralgr
//
LOCUS       WP_181610289             412 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Nonomuraea soli].
ACCESSION   WP_181610289
VERSION     WP_181610289.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 412)
  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 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   3  (residues 1 to 412)
  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 412)
  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 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   6  (residues 1 to 412)
  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 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 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..412
                     /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=43161
     Region          6..389
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mallfwavgv laylvavfhr qslsvaglda aermgvseag matlamlqll vyalmqvpvg
       61 vlldrfgskr llltgaltma agqlvfalsd nllygiaarm liglgdamtf isvvrlvnla
      121 fpphrnplll qltgligqlg aiastvpmia slhtygwapt fygaagvgvv mavlliavlr
      181 dkpsgqaaep glkaawthpg trlgmwthva tqcsaaafll lwgypflveg qglapqtagv
      241 llatltavgm vcgpvlgyla gryplrrswl vlgvigstaa awtavlawpg haplwllvvl
      301 vvvlaangpg smigfdyart fnpagrigaa tgivngggfl asmsvialia iglevfddyr
      361 lafllqypvw llgvvqvlry rakarrllaq ldeglgevrg aqepalgtka ld
//
LOCUS       WP_181610355             166 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            soli].
ACCESSION   WP_181610355
VERSION     WP_181610355.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (residues 1 to 166)
  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 166)
  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..166
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..166
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17975
     Region          3..102
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 meprsgcpin aavevlgdrw sllvlrdvif gdrryfrall tgslegiasn iladrlvrlv
       61 eagiltrgta vrgqrarysl teagiqtlpi iyalgnwgld wrqgsaelrv rqevmraega
      121 gfveelmdel rvrhlgatsk ahdgpgafer lnaayaaaaa eqgdak
//
LOCUS       WP_181610371             190 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GTP-binding protein [Nonomuraea].
ACCESSION   WP_181610371
VERSION     WP_181610371.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea
  ORGANISM  Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae.
REFERENCE   1  (residues 1 to 190)
  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..190
                     /organism="Nonomuraea"
                     /db_xref="taxon:83681"
     Protein         1..190
                     /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=20596
     Region          9..190
                     /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 mdsglsedpv alkiliaggf gvgkttlvgs iseikplkte evlsdrgigv ddldgvegkt
       61 tttvamdfgr itirdglvvy lfgtpgqerf wfmwdelsyg algavviadt rrltdcfpsi
      121 dyfeqrgtpf vvavncfdgv pshsiedvki aldledhvpv lmcdvrrras akevmitlve
      181 hslrtlttal
//
LOCUS       WP_181610260             243 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Nonomuraea soli].
ACCESSION   WP_181610260
VERSION     WP_181610260.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=27050
     Region          4..>132
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mqdfdhwael yitwtamgga dprevayyrr laamaegpva dlgigvgrla aelrprfgvd
       61 vsaamldear erlgdgieli radlagctlp epaalqycgq ntlnhltrea vrdalarafh
      121 nslpggrlaf evvqprperq kardgvprlr vwderravwe itrmldkegm evemigllet
      181 lddhrtvgrr yfppirmcll tmaevekwag eagwdvedah agfggepltp esstavwclr
      241 rpa
//
LOCUS       WP_181610450             440 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nonomuraea soli].
ACCESSION   WP_181610450
VERSION     WP_181610450.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..440
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..440
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46298
     Region          25..440
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtrvvdqhha evpltlegap pkvlgvldqg alwanlavsl lgfsgalalv naaqdaplsl
       61 aaaltatvvg sligtvmval saipgtqtgq psmvllrglf gakvsyvptv lnvvqmlgwg
      121 afelwviaig cqaifgdavp yavwviaagv lttvltiwpl gairvlrryv tiaviismay
      181 fawrflgeap pqsggswtgf gpavdyvial svswvplaad farhsrssga afagvvggyt
      241 laqvaclglg iyavaltgsg dvfptfvavp lgalffgili lretdqsfan vysttvslqn
      301 flprvdrrvl svivgvittl iavwvsadty asflsvigav fvpmfavlav dyfvlggrar
      361 wntgedapsr wsmlipwalg fvaywlttsa vtvagwdsfw tgvrdsigfe rqpwmngalg
      421 afvvaalvtl ligllrgsrr
//
LOCUS       WP_181610514             468 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181610514
VERSION     WP_181610514.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..468
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49291
     Region          3..342
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnadalntta tkirdhiaaa cesdaipgfv agihqggeqv vvahglanva tgapmlehtg
       61 fllgsvtkvl tttlvlqqvd rgvldldapv vkylpefgsv sgkilvrhli ghtngidadl
      121 yfpgdkgrda lkayvegmps stlfepgeql sysnggmiva grllevvtgl pypellardv
      181 ygpvgmtdss tsaeqailrs tavghfldle tmaprpttmf tlpetwgpag gtpigtiadl
      241 lafgrthlag gvspsgtrvl sagstalmrq vsfdmespnt ppiglgwvly pfggttvlam
      301 sgaspggvsl lcvipehdlv faaygnspga imlqdrilql iltehlgiel prlvtgdeqd
      361 adlapyagty rsnqlrievs vvdgqleevi tyepadpsqe riftefaggt tsappqryvp
      421 vgpglfapag ypleafdgyl rlllvsyhdv rdgqarfrng ggrlarra
//
LOCUS       WP_181610315             455 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea soli].
ACCESSION   WP_181610315
VERSION     WP_181610315.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 455)
  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 455)
  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 455)
  AUTHORS   ter Beek,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..455
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..455
                     /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=49156
     Region          41..450
                     /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(151,153,302,304,336..338,379)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mntrkrvgta llsgllassa ltacsssetp apaaggseqv tlnywlwddn qlasyqacad
       61 afaaanpgit vkitqtawaq ywqnlttqla ageapdvwtn qvsyypqfvs sqqildiqpy
      121 vdsekvdltq yqdgladlwt kdgkryglpk dwdteavvyn sdmlakagvk peelaeltwn
      181 pqdggsfeqv iakltvddkg rngldpafdk dnvkvygyqp ewndgsqgqn gwgelaaang
      241 wtyldknpwg tqykyddpkl ietiawykal tdkgfaprfd kqstlgidav mnsgkaalti
      301 agswtintyl gegaeqkfal aplpvgpvgs rksainglsd aiwagtknkd aawkwvkylg
      361 ssacqdvvgg navvfpaikt atekalaahk akgrdvqvyv dytktpggtf llpitehgte
      421 isqivqdslq avilgqiepa ealqkanqqv nglfg
//
LOCUS       WP_181610547             131 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            soli].
ACCESSION   WP_181610547
VERSION     WP_181610547.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..131
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14329
     Region          3..108
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdrdefvadc rvravtdlfa htwdpvvlft lsagphrrre lrdaiggisd kvltqalhrl
       61 lssglidrra haeapprvvy altglgqslv dgpisalgrw aeehgdelld aqerkdpfdp
      121 rgeavdplti s
//
LOCUS       WP_181610441             236 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Nonomuraea soli].
ACCESSION   WP_181610441
VERSION     WP_181610441.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 236)
  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 236)
  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..236
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..236
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24798
     Region          2..213
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mtpdtavvip akdeaarigp tvvaalalpg vdlvvvvddg srddtgrvar aagarvvrhs
       61 rnrgkstame tgaeavrlld taaprhllfl dadlgssaat aaaliepvra gtadmttavf
      121 vnrvklgglg mvvglsregv kratgfeaaq plngqrcltr dafeaarpla hgwgvetaml
      181 idllrkgfrv vevevemahr atgtdwkaql hrarqlrdva ralvareslm rgaask
//
LOCUS       WP_181610617              68 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181610617
VERSION     WP_181610617.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..68
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7305
     Region          3..68
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mgivvdidvm lakrkmsvge laervgitpa nlavlkngra kavrfttlda lcealdcqpg
       61 dllrwehd
//
LOCUS       WP_181610665             155 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            soli].
ACCESSION   WP_181610665
VERSION     WP_181610665.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 155)
  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..155
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..155
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17457
     Region          8..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnvafrvdnc siertleivg ekwtflvlre afsgvrrfad mqtmtgaprq vlsarlarlv
       61 degllrkvpy repgqrqrye yrltekgrel ypllvalmhw gdkymadpeg ppvvlthrdc
      121 gapihqhfrc sqghdlsgpr evtpvpgsga klqsa
//
LOCUS       WP_181610763             511 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Nonomuraea soli].
ACCESSION   WP_181610763
VERSION     WP_181610763.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 511)
  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 511)
  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..511
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..511
                     /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=55451
     Region          4..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(173,176..181,183..184)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(176,293..294,315..320,398,410,413,424,504)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(176,217..218,265,267..268,271,293..294,315..320,398,
                     410,413,421..424,485)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(217,267..268,271,293,421..423,479,485)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mlnlsivled sarhvpdrta lvfgdlrlpy smvdtvanqv anllvargvg kgdkvalmcp
       61 nvpyfpfvyf gilkagatvv plnvllqpre iayhlddsda kalfcfegta elpmgargre
      121 afdatggcel flvlpatpla tesehgesfw aaidgmsgdf etvqtapddt aailytsgtt
      181 gqpkgaelsh vnllintmvs dqmfpadpag dvslavlplf hsfgqisvms vtmrrrgtlv
      241 lmprfdpgea lalmrkekvt mfagvptmyw gmlskihadg devpttlkva vsgaaacpve
      301 vikdfettfg vailegygls etspaasfnq lsrptkpgti gfpiwgvemk lvdddwntil
      361 gegpgeiavr ghnimkgyyg rpketeevlr dgwfrtgdia trdedgyyai fdrskdmiir
      421 ggfniyprel eevlithpav slvavvgvpn dshgeevkay vipapgatvs edelvawcke
      481 nmaaykypri vefrdtlpmt atgkilkrel r
//
LOCUS       WP_181610843             350 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181610843
VERSION     WP_181610843.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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..350
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..350
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38111
     Region          6..348
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mminvmvatv laasgqvvdl rpdldkiveg qgataalarv sddkrsrtas vgkrdlqrgg
       61 rpaangyfri gsvtktfvat vvlqlvdegr lrlddpidrh lpgtvpgger itvrqllnht
      121 shlydymsep gystnrwrge arfrsyqprd llkvafakql pddgrwhysn tnyvvlglli
      181 ekltgmpyge qitrrilrpl glrhtiipgd ragvpsphak gyepmpelvd atrmnpsldw
      241 aagemistta dlerfmgall ggrltseesl qamrttvqtg agfgyglgvq ayplpcgtvw
      301 ghsgeligyl tfafrsdsgk sltlsinpst rnpsteevmg mavktfcgta
//
LOCUS       WP_181610454             215 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Nonomuraea soli].
ACCESSION   WP_181610454
VERSION     WP_181610454.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=22548
     Region          5..194
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 msvtiaeell llahseeagk qlvdstslnl alggallael algeridleg rhvvvkdptp
       61 lgdgeldral ariveetkpr kpdwwvnklh agklrdrllt rladagvlte qqgkvlgifp
      121 skrwpeadgt veagvreria salggsdpdp rtavlvavmh avklerkafp gadkkrikei
      181 aegewagaav artiasiqaa imagavaavv aagas
//
LOCUS       WP_181610851             361 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea soli].
ACCESSION   WP_181610851
VERSION     WP_181610851.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..361
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38132
     Region          124..360
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mkkvlvwtas vlavlvvval gaggwyysgm vidpargpas ypievtavsg gqvtlkgggd
       61 tdspgmyglt waggsalvgp vssvsgesvt rllikvrkge lkpgvrayld rwmygdedpt
      121 salglpyekv sikgypawrl dgqaktwvva vhgrnanpse tlrvmpffhr lgmpvlsigy
      181 rndrgapasd dgkfhlgase wqevaaavay aqsqgasdvi lygwsmggai vstaarkmpd
      241 apikgiimds pvldwtppie agareqgvpv wfagvakfiv errtgisfdd ldqvkhasaf
      301 ktpmlvfads adtgvpmgaa aafakarpdl vtfvqtdggg hvgswnvdqa ryeraladfv
      361 s
//
LOCUS       WP_181610986             341 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea soli].
ACCESSION   WP_181610986
VERSION     WP_181610986.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Rosinski,J.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..341
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..341
                     /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=36580
     Region          1..240
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          250..316
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maltidlgia elaatrfais plsetvsglq qlggldrnpl nlrwlrwatn elarhpldlt
       61 htwplivner pswpgflvpa ppgsggsidd dlaalqrtsp aqvrislrrv fgdelpaaaa
      121 elaegpvagl raiaaelraa hdrliaphwp riravletdv vyrakqmaag gveklftnlh
      181 pdlrwnggrm klsetrrrae svvelgpggl vlmpvvlgsp yvlikkrtst qttvryparg
      241 vgtlwtagtq eranstarll graraellea lrspatttdl aralgitpsa isqhlrvlre
      301 sglvtrersg rsvlytttal gaslsgmaav sardsasaah w
//
LOCUS       WP_181611301             317 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea soli].
ACCESSION   WP_181611301
VERSION     WP_181611301.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=35135
     Region          14..223
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          232..304
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 melifttqdv antrfaispl wevvasvrvv knpaahsllr pwaeqvsrrl rdvdwrllsd
       61 lvpvptpyip gfvcpppats vpdlevelaa mraltddltd lpdtrhtral ladpergler
      121 lseeirnywa aaiepywari gallegdvly rartlaghgl rqmladldpg vswegerlrl
      181 psvhctgerp lrgmglllvp svftwprvfs vtappyqptv rypprglatl wehaeveppq
      241 alaavlgrtr arllaeldqp astrelaqrt gltepganqh ltalrkaglc sahrtgrfvl
      301 yartavaetl lrqdara
//
LOCUS       WP_181611040             342 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Nonomuraea soli].
ACCESSION   WP_181611040
VERSION     WP_181611040.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 342)
  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..342
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..342
                     /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=38010
     Region          12..339
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 maqataaata asdfsrlskr irqaglldrr pryylirisa vaaayvagaa afpwlgdswl
       61 qlllavyfai vfaqvalvlh dlahrqvftd rrpseilgrl ggnlaiglgy gwwmnkhtrh
      121 hanpnhedld pdvapdilvw spkqarnarg larliggrqa fllyplllle glnlhvggvr
      181 alrqpwmkqr vlegtllfah fafylgvlvw tlspgkalvf favhqglfgv ymgcvfapgh
      241 kgmptltgea kldflrkqvl ttrnvrggrf tdlamgglny qiehhlfpsm ptpnlrlaqp
      301 ivqahcrqlr lpyhevsfva shrealrhlh qagaplrekg rs
//
LOCUS       WP_181610479             733 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Nonomuraea soli].
ACCESSION   WP_181610479
VERSION     WP_181610479.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=76532
     Region          7..732
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msvthdtiel siggmtcasc anrierklnk ldgvtatvny atekaqvsfp egiapeelva
       61 evekagysae lprppqaega peeprdelkp lrdrlilsvv lsvpviamam ipalqftywq
      121 wlsltlaapv vlyagwpfhk aawtnlrhga atmdtlvsig tlaafgwslw alffgtagvp
      181 gmthpfefti artdgsgniy leaaagvtaf ilagryfear skrragaalr allelgakdv
      241 eltdgrrvpv dqlkvgdlfv vrpgekiatd gvvhegtsav dasmvtgesv pvevgagdrv
      301 vgatvnaggr livkaerigq dtqlaqmakl veqaqtgkaq vqrladrisg vfvpivigla
      361 vatlgfwlgt gegasaafta avavliiacp calglatpta llvgtgrgaq mgilikgpev
      421 lestraidti vldktgtvte gkmtltdvhv aegenrdevl rlagalehas ehpiaqaiak
      481 aaqsdatved fanveglgvq givdghavlv grprllaews qhlpedlagk ladeqaagrt
      541 avavgwdgka ravlvvadvv kptskeaiqr lralgltpvl ltgdneavak tvaaevgidq
      601 viaevlpadk vdvvkrlqge gktvamvgdg vndaaalaqa dlglamgtgt dvaieaadlt
      661 lvrgdlrvaa dairlsrrtl stiksnlfwa faynvaalpl aalgllnpmi agaamafssv
      721 fvvtnslrlr rfs
//
LOCUS       WP_181611309            1093 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181611309
VERSION     WP_181611309.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1093)
  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 1093)
  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 1093)
  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 1093)
  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..1093
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..1093
                     /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=117057
     Region          1..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          118..1085
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          775..803
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(776,779..780,783..784,786,816,819..820,823..824,
                     826..827,856,859..860,863..864,867)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          814..844
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          855..883
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          894..924
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          929..962
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfvilgpvm aygkdgqvpl gppkrrllla llltsgerav pletavqavw ggnppasavq
       61 nlyqhishlr qvlghdtiag qgrpgytvag lpgnldahtf edlaergsra laggdaptaa
      121 rslrqalamw rgpafgdlag epalhqeaer leelrlaale nrieadltlg lhepaiaell
      181 vltrshpyre rfvtqlmhgl rvaqraseal evyrrtralf veelgiepgp vlrrlhqail
      241 tgepyttgps agsvrpsaig paapddepal agvavphelp agvarfvgrr aqlreldrll
      301 prttdrtppt vivaavvgta gvgktalavh wahrvahrfp dgrlylnmhg ysaesprqpl
      361 havsallrsl gmpaeqipvd laeaaaryrs liagrrmliv ldnvrsaaqi rpllpgegas
      421 fvlvtsrdrl tglvaqdgac rltlgvmtek esvallartl gagrvhhepq aaaalaarca
      481 hlplslciaa allsdhpkqd ithfvgqlag gealagltvd gqedgeiavr aafdlsyqal
      541 dpslrsvfrg lglvgcpdft aeavgaqtga epaaadralr rlaaahlvee sqpgrytlhd
      601 llreyasrla tttddeetla aarrrlcdwy lttvttaqrl lhagqrqspp edfvghappa
      661 ltdydsalaw ldaerhnive vvkcasrhgl daicvhladr lrgyfdlrrh tadwetvarl
      721 aretaarggd etlhpialhg aahlgfvlar yaqaitcvke lmaltpadap akaradlmcn
      781 lgylltrvgr taeaestlde arvlartags tasqaailln lanlhldcgs laegrtaalt
      841 alrlsrnsde prwvamslgt lgelaqlqgs yaeaisyfdd clemhrrqgd rpgelaslsw
      901 lartcldlgr weechhnasa ardlareigd rhqlvhsvtv laahsratgd leaalstsrt
      961 algmaaelgd pylecdaale aahaaagtgs qaeqlarral tiarrcrfrl legraltlla
     1021 tlaheradhh aaveqafhal avhrstghrl geahthallg qalraagdpr aeehgraaer
     1081 tladlgltgr lks
//
LOCUS       WP_181611558             267 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nonomuraea soli].
ACCESSION   WP_181611558
VERSION     WP_181611558.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..267
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28795
     Region          13..267
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mkvikeeksq rgvsltvasp slttqtlaev llptgwkpgt twpvlylleg cchentidwt
       61 argqadeltk dlpviviale gghagfysdw adgpqwesfh ikelipylet tyggngrrai
      121 agfsmgglga fayaarhpgm fraaasfsgl ldagradady lardrsrdlw rdedipkhsp
      181 tslvaeltgi plyvacgnge pgpldspstp kdngeatiee qnrrfvaaae kagaqvtvsl
      241 ygpgthawpy wtreleralp llagalr
//
LOCUS       WP_181611608             360 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181611608
VERSION     WP_181611608.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..360
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38239
     Region          29..358
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrrtlpvvpa llpvlllvvg cagyqrgdld davrrvrnag avgaqammav dgrfiaatsg
       61 pavpenghfr igsttktfva tvvlqlraeg rlrledpvat hlpgvipeqi tvtdllrhts
      121 glpdysqdpa wdpfasaedf aerrfqhyta rdlvevamrr pprsepglah qysntnyvvl
      181 gmlieavtgr gwqrevrgri ieplgltgts tgegtrvpep hargftrfet ggplvdttrl
      241 dpsagdagga iistprdllr ffaallggel lapaelaamk stvpaeggry glglawselt
      301 cgggywrhgg svpgyltyeg faddgsrgvv lsvssmsmdg fsdleqdaaa qelidaalca
//
LOCUS       WP_181611398             390 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181611398
VERSION     WP_181611398.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 390)
  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..390
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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]"
                     /calculated_mol_wt=40934
     Region          <193..384
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mitapargrr psrldvflsl svtaaglves ygrrggspge igsphlfaag tlaagalllv
       61 rnrfpitall vliavgeavv qlspgtayya awhlysmlil ahtiaaaydl rsrhgiaglg
      121 cvigayiflq tleitdvpem litaiflgva ygsgillrrq taqttrlaal tarleaeree
      181 rarravaeer ariardlhdv ishnvsvmtl haggvrmmlg eeatrerell qvveqagrea
      241 vgelalmlgm lrevedsegs rpgldrlgdl vaqmeesgvd vtltiagsrr avpsdvdlaa
      301 yrvvqesltn vlkhagasrv eltvtyapgq vtveltddga gpataghagg fgqigmrerv
      361 tlhggtlttg aapgggyrvl acfpsataag
//
LOCUS       WP_181611347             263 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Nonomuraea soli].
ACCESSION   WP_181611347
VERSION     WP_181611347.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 263)
  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..263
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..263
                     /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=28679
     Region          30..262
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mrhslcalli ttmllaaspa aaatvtvvah rgssadapen tlaavklalr hgadlvefdv
       61 qqtrdrklvl mhdtslartt daervfpgrs pwrvrdltla eirrldagsw ygarfrgerv
      121 ptlravlgel rgsgagalve lkaprlyqgi eqrvatelss sgvralvqsf dwasmrrfhr
      181 wapdvpvgll gtpavsrlde larfathinp pyrdvtasyv rqvhrhgmki fpwtvdsraa
      241 arrliaagvd giitntpgvl tqp
//
LOCUS       WP_181611609             195 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea soli].
ACCESSION   WP_181611609
VERSION     WP_181611609.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=20654
     Region          18..>89
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mfdvaviedp gaaeasldpm rarllaelae pgsasslaak vglprqkvny hlrtlekhgl
       61 velveerrkg nftervlras aasyvispsa lgavqpdpgk apdrlsarwl lalaarlike
      121 vgllvtgatk agkkvatfal daevrfasga draafaeela havatlvsky hdenaeggrp
      181 hrvliavhpa vkeqq
//
LOCUS       WP_181611637             346 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Nonomuraea soli].
ACCESSION   WP_181611637
VERSION     WP_181611637.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..346
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..346
                     /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=36474
     Region          <157..271
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mplhltpdda apyldgrapg ahldvigamt vhavaaalrl gvfaalgapa daptlartld
       61 adpaaltvll dvlvatgyla regpryrltp lagtldwygd sllfwhevtg elwsgltesi
      121 rgggrgadfy twlgdrpear srfetilygq adwlsteivt lappppgatr lldlggghar
      181 yslaycaahp rlhatvadlp aaldagmsaa kqagldervt fdgrdltaal pyrdqdcvll
      241 fnllhgfpaa raralvaaaa gtlrpggrli ilerdpdraa dpvtgafsrl falnlhhtqg
      301 gtlhtladla awarecglte pgvadltrsp ahrlliadlp pgtprp
//
LOCUS       WP_181611679             365 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Nonomuraea soli].
ACCESSION   WP_181611679
VERSION     WP_181611679.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 365)
  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 365)
  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 365)
  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 365)
  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 365)
  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..365
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..365
                     /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=39521
     Region          79..356
                     /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(135,140,173..178,197..198,202,221,241..242,244,
                     264..265,291..293)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 mnkvlsidgp geiswveekp adipdggfrv etlfsgvsag teltfvkgvn pylksvwdps
       61 lglftegtpg aaypvrgigy mqvgevvesr tsmlkpgarv amayghrtgy vadpmtdrfv
      121 elppgfdplm giyvahmgpi cangllhaah dlhgqsvrsl gdgvrgrrva vtgagvvgll
      181 vaqfarayga aevavldetp drlaiadrlg fltlsgdpal elkrrwrhgp ndrgadvvfq
      241 crgqaralal alkllrpqga vidlafytdg ahevrlgeef hhnglalrca qigrvprgla
      301 hswdrerlsh etiqllrehg delgehvitd vvafdeapdl lydlatrrrh tvqavlrrdv
      361 qhesg
//
LOCUS       WP_181611889             391 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181611889
VERSION     WP_181611889.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 391)
  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..391
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=42598
     Region          136..390
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mfgrvrawsk rhsrvidaik lspllfvclm ylesytamqg fapqpgtyvg algylaltav
       61 litplvwrrd ryrlvftiis llcfaqwlah vpilpanfav ivalysmalr dtfrwalaam
      121 lvaelgvflg lsqwdtvtls qffsfsilvv tvwlaglyss trrryvegle eraeraerer
      181 dqqariaata ertriarelh dvvahnvsvi vvqadgaaya ldrdpelarr avqtisktgr
      241 dalaemrrlv gvlrqdetat dylpqpglaq ltdlvkgagl pvelrvagtp rglpegeqlt
      301 iyrivqealt nalkhggpgv kalveldyqg pevivkvtdd grgagapagg gghglvgmre
      361 rasmyggavt arprpgggfe vcarlpmtea a
//
LOCUS       WP_181611715             355 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181611715
VERSION     WP_181611715.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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
REFERENCE   3  (residues 1 to 355)
  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..355
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=36809
     Region          130..354
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtiwtlagpp lvlwpllvmp lagegargvv aivlvtllvv ttirlmlrav divrgrgawl
       61 eavsgglaat aafplirqig drpaalfwsm aagllamaia lrlprgrrvp ailaaavail
      121 aaqwisgypp ataalmgasa lgtaagvgmq wwtyevaqrl edarvvaael avaeerlrfa
      181 aelhdiqghh lqvialksel aarvadrdka velmrevqel arealtdtra vvggyrqvsl
      241 svelanavkv lraagvaatv taddevggta grllglvare attnilrhsh asrasvvlav
      301 qeghgtltvt ndgaeeasaa gsglaalaer veaaggrlsw gneqgsftvr avvpa
//
LOCUS       WP_181611937             402 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Nonomuraea soli].
ACCESSION   WP_181611937
VERSION     WP_181611937.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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..402
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..402
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42951
     Region          52..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          124..154
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          194..224
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          229..253
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrvliaaggv vlagaliftv atvaappqqs aatrttetlq srlqrlpgdy rgwarlateh
       61 leqaritgnp afypkaeqal ikanglapqd davltagaal aaarhdfsqa vrlaeravaa
      121 npysttalgv ladartqlgd hdragqaier mialrpgvas fsrasyaael rgdlagarrh
      181 leyaladayq padvaycrfy lgelalrsge laqaqqwygq alqampsftp aiagqaraha
      241 lsgdlkaalp lyesvvgrlp lpqylveyge vrikaglapd wtllraqqrl atesgvlddl
      301 tlaefeadhg dpalavrhar aefgrnpnpv aadalawalh ragrsrealp yakqatatgw
      361 rnallhhhra eieqalglrg tslartynpt fdpalpalar fs
//
LOCUS       WP_181611761             372 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181611761
VERSION     WP_181611761.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 372)
  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 372)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 372)
  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..372
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..372
                     /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=39342
     Region          162..353
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 milrgnvprm atvwaltmgv alawtgavrg liehpvgpwq aagaiaamvl fsvlyirisr
       61 aavaggrrwa dlaaagaval alvawmdvgg eprlwallgp iwasaavlvm spwpamlvca
      121 avaggylvlt peadsgsaft yvtlcfgipw anrlqlwfwk iiqqaeagkk aqaalavaee
      181 rlrfsrdlhd lvghslsvia vkselavkla rrdqeraete maevrtlakq algeirsavq
      241 gyrsvdlaae lramrltlea agiacsieep prdlpaevat llawvaregt tnvlrhsgat
      301 tvsiafdvre gelellmrnd gagepgsgng tgltglaerv ttlrgefrag peagghfvvg
      361 vvvpwsrsat ig
//
LOCUS       WP_181612060             367 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181612060
VERSION     WP_181612060.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 367)
  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 367)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 367)
  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..367
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..367
                     /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=38243
     Region          122..363
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mrrtrrqlls dvllwavlsv lvaaagpdpv tdlpaflgvt garvalvgva vavgrpwppa
       61 avlllsaalp psmteslats dvtwlnpalv dikvfpvaai tpgviwysyl tgrrmtrqwp
      121 alavfavvta gglligqwit vlsglllayv lpyglgllrr glsqqrerat qsaeaqarlr
      181 ertriahdmh dslghdlali avraaalemm dgahakaage lreaasaate rlreiigllr
      241 edgaaplvpv gedvaalvar ardsgmtitl tadgaepala hrvvqegltn aakhapgarv
      301 avsvtaslit vrngppagrh varsgglgla glrervrlag gtleagpdgd gylltvklph
      361 egeappr
//
LOCUS       WP_181612071             264 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea soli].
ACCESSION   WP_181612071
VERSION     WP_181612071.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 264)
  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 264)
  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 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   6  (residues 1 to 264)
  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 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 10001941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..264
                     /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=29416
     Region          1..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          108..256
                     /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(109,111,113,122..124,126..127,132,140,147,149,151,
                     153,161,163..164,166,169,175,177..178,207..208,210,212,
                     223,225,227,229,235..243,245..247,250)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mdevfkalad psrralldsl narngqtlre lcagldmarq svskhltvle eaglvttvrr
       61 greklhylna apvheiahrw isrydqarvq aladlksale etpmdaptfv yttyirttpq
      121 klwqaltepa ftrrywatef atdwaagspm twdnhgvtis dpeqvvlead pfkrlsytwh
      181 avtpelaarf gwdddllarl saesrskvtf tieeatsqvv kltvvhdgfe pgsslaemvs
      241 hgwpnvvasl kslletgepl peda
//
LOCUS       WP_181612220             408 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nonomuraea soli].
ACCESSION   WP_181612220
VERSION     WP_181612220.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=44107
     Region          15..403
                     /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 mrthiavigg gigglclaqg lhgkgvdvav ferdrtpsdr lqgyrvhidp qgaralrqcl
       61 peplwrtfla ttghggqdfg flteqlgqll lvetppdaeh ysvsritlrq vllsgleevv
      121 rfgkkyerye rnadgtttlh fadgstcvad ivvgadggts rvrrqylpha ervdtgittv
      181 agkfpltprt rgliaprlad gpnmilpppg fgmfcaphdv aeavgeigrt eqegalmdnn
      241 ssyilwavga saerfpggla rmpgeelrat vsglvatwhp dlrrlvelsd pdtvsllpir
      301 tsvpveawep stitllgdai hsmtpmrgig anialrdaal lcaalddgtv eaigryeqem
      361 rqygfaavrd slkaaqsfvs drrlarmgfk aflrtaarfp glrekafa
//
LOCUS       WP_181612228             438 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Nonomuraea soli].
ACCESSION   WP_181612228
VERSION     WP_181612228.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 438)
  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 438)
  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 438)
  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 438)
  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..438
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..438
                     /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=47577
     Region          4..432
                     /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 mdwliflagi liilvglmvs iglheighlv paklfgvkvt qymvgfgptm wskrkgetey
       61 gvkwlpfggy irmigmlppr pgddpnkvrq tstgpfqgli eqardlaqee vrpgdenrvf
      121 yrkkwwqkvi imsggpfmni llafvlfgvv ymvmgvqtlk pvlaqvqqcv vsaevqqkep
      181 nractaadpk tpsaqaglkp gdkvvsfngt pitrweqvrd giraagasqv tlgieregkl
      241 qdlkvaliaq dmpnvedpkk idkgvgylgv vpqvvieqkd fpylvtefge tvahvgesli
      301 nlpqrmvgvw naafsgderd angpigvvgi griggeiatm diavenkllv fvnllagfnl
      361 avglfnlipl lpldgghiag glweglkrgf ariarrpepa pvdvakvlpl tyalafvfmf
      421 magllvyadl vnpvkltg
//
LOCUS       WP_181612257             261 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181612257
VERSION     WP_181612257.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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]"
                     /calculated_mol_wt=27899
     Region          1..248
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mselrmvart pgpalrpyvt dlvayreeyp eprarteypf pgavliigla apmhvggvpy
       61 tsftgglsdr asgtlvsgaa egvearlspl garrlfgvpm geltnvilpa edllgpwfrt
      121 aaarlaetgs werrlelaer mltahiherp elgpqvpwaw aqllgsaggv siaslaeslg
      181 wshrhlvarf hdevgltpkt aarmirfsra mrllraglpp alvaaeagfy dqahlnrdfr
      241 afagappgvv aagftavpqp v
//
LOCUS       WP_181612272             210 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DUF47 domain-containing protein [Nonomuraea].
ACCESSION   WP_181612272
VERSION     WP_181612272.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea
  ORGANISM  Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Nonomuraea"
                     /db_xref="taxon:83681"
     Protein         1..210
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=23561
     Region          21..210
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mkrlrrirdl lrgrmdsalt eallgqleat kegawlamam iggevgrtga heqmrsiehl
       61 gdeerrrlvd elrdalvtpi dredlfrlsr siddvldslr dfvreshlyr vpdqirfspl
      121 ldqvivgida lenavrdlas rpsavvhdal eakkaggvir rmyqyeisri fsgeltadam
      181 kerelvrrle ivgmaigeaa daiadgamkr
//
LOCUS       WP_181611906             212 aa            linear   BCT 28-DEC-2024
DEFINITION  adenylate kinase family protein [Nonomuraea soli].
ACCESSION   WP_181611906
VERSION     WP_181611906.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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 212)
  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..212
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..212
                     /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=24413
     Region          1..208
                     /region_name="Adk"
                     /note="Adenylate kinase or related kinase [Nucleotide
                     transport and metabolism]; COG0563"
                     /db_xref="CDD:440329"
ORIGIN      
        1 mrkyliigvq gsgkgtqagl lakaydlvhi nvgdifrwhv qqhtklgalv rrtmaageli
       61 gdehvekivr drleqhdwny gfiidgfprn rrqteffles ydidgvihld lpddevrrrv
      121 larrlcpncg mdynliydrp aeegicevcg helvrraddt eealserlrt ynektnpild
      181 llrrkeyvft vnaaqsvdev qtsireklgl df
//
LOCUS       WP_181612252              71 aa            linear   BCT 28-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Nonomuraea soli].
ACCESSION   WP_181612252
VERSION     WP_181612252.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 71)
  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..71
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..71
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6601
     Region          1..45
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mprydfrcrs cgstfevsrp msasgdpatc pgghddtvkl lstvamtgna gapagggggg
       61 gggccgggcc g
//
LOCUS       WP_181612411              63 aa            linear   BCT 28-DEC-2024
DEFINITION  YegP family protein [Nonomuraea soli].
ACCESSION   WP_181612411
VERSION     WP_181612411.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..63
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..63
                     /product="YegP family protein"
                     /calculated_mol_wt=6540
     Region          2..59
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 magkfiiskd krgefrfklv aangqtiavs eayttkaacv ngvesvrkha aeatvvdetl
       61 aav
//
LOCUS       WP_181611656             256 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Nonomuraea soli].
ACCESSION   WP_181611656
VERSION     WP_181611656.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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 256)
  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 256)
  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 256)
  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..256
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..256
                     /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=26937
     Region          5..231
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mkhniryaag sdvgrrreqn edagyasarl lavadgmggh aagelassaa iavmreldtk
       61 lpetgadlea alegavaeag rrlvelaeid parrgmgttv tamlwdgyaf slahlgdsrg
      121 yllrdgalyq mtkdhtlvqs mvdegrited qaavhprrsm vlrvlgsegr adpdmalrea
      181 qlgdryllcs dgltnvlgpe tlhevlttla dpaaavqrli dlaneggspd nvtvvvadvv
      241 spgegdemvy rvgaga
//
LOCUS       WP_181612437              76 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Nonomuraea].
ACCESSION   WP_181612437
VERSION     WP_181612437.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea
  ORGANISM  Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae.
REFERENCE   1  (residues 1 to 76)
  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 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   3  (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   4  (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 18824274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Nonomuraea"
                     /db_xref="taxon:83681"
     Protein         1..76
                     /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=8568
     Region          14..74
                     /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 mrvddaayeh vtlslskrea evmelialgq sngqiaerlf lsektvknhv nriysklgvd
       61 sritaidlwk rrvgdr
//
LOCUS       WP_181612498             139 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            soli].
ACCESSION   WP_181612498
VERSION     WP_181612498.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..139
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15035
     Region          5..102
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtvprpcsia dtlavvgeky sllvlrevfl gvrrfdamvr gigaprdvla arlkhlveag
       61 vlekvayser pprheyvpta aglelqgvlh llrqwgdrhl aerpplvlgh dcgaaldplv
      121 vcahcrqpvt pqsvslpps
//
LOCUS       WP_181612541             965 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181612541
VERSION     WP_181612541.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 965)
  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 965)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 965)
  AUTHORS   Rosinski,J.A. 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 965)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..965
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..965
                     /product="helix-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=102963
     Region          <2..880
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          897..953
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 magsdagrvt cpiligreqe ldrlvaavsr ppavvvlege agigksrlla elaerpemdg
       61 rlllrggarr irepfplgpl vealrgtgdy lvraelspva galrallpel apvlppaldp
      121 qndraaerhq lfrglaevlr aleplvlvve dlhwadqqtm eflsyalalp lprtsvvlay
      181 rgeeagpavr evtgrhadav fhdhilltal nsaqtgdmaa ailgeegvta dfgahlyels
      241 sglplavqel mallrargal irlrsgrwar kavaeldvpp gvrdsvrerv arlpeparvv
      301 aeaaavlhvq arleelqrvs glpradtvag vdellvsgll veqdgsvafr hvltaqavyg
      361 aiplgrrqel haraaaavra rkpvplgqea hhlrqagrla dwvetaeqaa eqasqlgdda
      421 eavriledvl rhaplepehr srlavrlgwa apqmlrppev idllsqales eqpgllrgql
      481 hfligllqer rgedpgaqrr afaaavgdla grpdlvawvm aalgrpidpr vplsehavwl
      541 eralravpai gnpveevfvl gkiatslggy gdsrwrelte evrgrtggrp rhrqevgayr
      601 siaenacltg syeiaaalla aamreaagee wsreplarcr lvalvlsccq grwdgleeet
      661 allleeydgr pfdrlgaetv aaclalarge ldtarrelpd vagkavamga yellplsvag
      721 llrlstasge argalaatee avavwdtkgl wplavraapa laeamvaagr qddaaaltdr
      781 latrldglda plaaaalaha rghlasedma aaahfraaaa gydllgapye aaqarelaag
      841 rlfaggrsga gelllaamat frdlgarwdl draaqlarrh gvtvkgrypg gpqgygadls
      901 prereiaela aegltnreig qrlfvsprtv ekhlgaalrk lglrsraalg ahlgterprs
      961 dppgp
//
LOCUS       WP_181612599             324 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea soli].
ACCESSION   WP_181612599
VERSION     WP_181612599.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=36237
     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 matdlapppt easrkakkqk aprvplgaai lryrwlylml lpglayfvif kylpmyglti
       61 afqdfvpflg ysgsewvglk hfetlfaggd fgmlfsntmi lamlifliaf pmpiivalml
      121 nelrinvvkr svqsliyiph flswtivagl tyilfsvdfg vianwihsvv gggkvdyvaq
      181 adwfrpiiil qtvwkgtgwg tiiylaalas vntelyeaar mdgagrwrqf whvtlpairp
      241 tivlmailhs ghlldqsfeq lwlltnslnr evanvfdtyt yyvgitqggy syatavglfk
      301 gtvgvllifg cnwlakrlgq rglf
//
LOCUS       WP_181612607             361 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nonomuraea soli].
ACCESSION   WP_181612607
VERSION     WP_181612607.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=39901
     Region          1..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 merdrlyemd alrliaalcv vlfhytfsgw akgetavvfa aesvvskygy lgvdlfflis
       61 gfvvlmsawg rsprdfvvsr fvrlypaywv glvvtavvva tlgagvfevt pvqflanltm
      121 fqsvadvpnv dvvywtlwte mrfyavifal tlvgmtknrm mavlwgwlal tfavqaglap
      181 rlldllvqse yshyfiagma mfmlyrfgms rqialivpic lgnavfravg faeavgrryq
      241 vgyseaviva vvvlifviml lvamrvtkpl grpgmataga ltyplyllha higfilfnlf
      301 dayvnayvll agittlmlvs aygmhrfvek plasrlkral srpapsrpav gvipaqisks
      361 f
//
LOCUS       WP_181610637             225 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FadR/GntR family transcriptional regulator
            [Nonomuraea].
ACCESSION   WP_181610637
VERSION     WP_181610637.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea
  ORGANISM  Nonomuraea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae.
REFERENCE   1  (residues 1 to 225)
  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..225
                     /organism="Nonomuraea"
                     /db_xref="taxon:83681"
     Protein         1..225
                     /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=24453
     Region          4..>180
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mslrtaqras lvdqvidqlk eqitsgswam nrkiptetvl aeqlgvgrnt vreavralth
       61 agllecrqgd gtyvratsel sgamlrrlrq aeqleilevr ralevesarl aatrrndddi
      121 vrieaalsar drawesgtae efveadlafh mavvhathnl vlidlyedfs aalrasitaa
      181 gtslnksyip hdaiaraiaa gdataaerag hacmehilia ltdqe
//
LOCUS       WP_181613125             252 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea soli].
ACCESSION   WP_181613125
VERSION     WP_181613125.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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: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=27733
     Region          33..129
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mehlfggaap yyaryrlshg daaiahlart fgpaatvldl gsgpgtiavp lachvarvla
       61 adpdeemlqe gakagvanir wikadstmlr qlppfdhvvm grsfhwmdrl avladlddll
      121 ppggvialvg ptreahhqew hpvaqrvcee fgltrhqarg syqdtglhhd dvletspfar
      181 lervtsertv vwdvdsvigy qlslsistpa rlgerreefl talrraveqa hpegtwsvpy
      241 ttevlvarrt qe
//
LOCUS       WP_181612488             107 aa            linear   BCT 28-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Nonomuraea soli].
ACCESSION   WP_181612488
VERSION     WP_181612488.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 107)
  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 107)
  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..107
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..107
                     /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=10977
     Region          3..106
                     /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 mgkrlavisa ggvigalgry glgslvpgiw ttfainvvgc fligvvmarl prelprlfla
       61 tgvlggfttf saytvdvlrg gqwlylaatl vcallavqgg lvlgarr
//
LOCUS       WP_181613157             483 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nonomuraea soli].
ACCESSION   WP_181613157
VERSION     WP_181613157.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 483)
  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 483)
  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..483
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..483
                     /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=53562
     Region          2..441
                     /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 mtpriaiiga gfgglcmair lekagitsya vfekaeavgg twrdnsypga gcdipshlys
       61 ysfekyaswt rrypgqpeil gylehcadky dvrrkirfat evtdaafdga gwrvtsretg
      121 tagasrteqy dvvvaavgql nrphmpeieg mgdfegvafh sarwdhghdl sgrrvavigt
      181 gssaaqfipk vaeraghltv fqrtpnwvip kpdaeftpfv qsalhfvpgl qrayrewiyr
      241 yaegtlypal aggwstqllk kralahlhtq vadpglrakl tpdyppgckr vvidsrfypa
      301 ltrpnvdvvt dritritpkg vetgsglhev dtivygtgfl steflapidl tgrdgrklhe
      361 qwkdgaeayl giavpgfpnl fllygpntnl ghnsivfmle cqvdhimrcl pylvsrgpme
      421 vrpqvmaawt eqleramerm vwgngcrswy ktaggrvtnn wpgptplykr ltsrspgpmy
      481 kyg
//
LOCUS       WP_181613270            1049 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181613270
VERSION     WP_181613270.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1049
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..1049
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=110296
     Region          3..1047
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mddrievrlv gplavrrgdr ilpagavgsr qartllalla vrhgqvvpad tladavwgga
       61 qpprparnla tlvsrlrtal gaavieggsg gyrlgasvev dltvaagria eaeerltgre
      121 lalalaaara asglldgpgv ladrpdvwwa eparaaheal lrrarhlaae aalragnsaa
      181 avsaageamr adpldesacr llmrahdgag eagralavye rlrstlaqel gadpspatrd
      241 lhaailaers psahdtrrah eaefvgreae lerlagawqq amrgearlvl ltgeagigkt
      301 slalrfartv aasgahcvsa rcfeaerslf lqpfaelltq laaglspael reaasgraap
      361 lallvpdlaa vldagdgerg saeierrray eaitlflrrl carqplllvi ddlqhasrat
      421 vellhylaah fgsgrllala taraeegqav rdllgeaaep ievgpldags verlataagh
      481 aglagqiger trghtlfvve slralaages gvpeslrtsv larvrragap aeellraasv
      541 lgpsfapatv aglldigvqe aarrcerale arlsvitgre yefandliqe ilyssipvpt
      601 rtayhraaad llagnpeava rhsaaagdwq raasgwlaag qraiaryavd dahslldlal
      661 gaatraadpe lrgqahlhrg ranemafrfe aaladheaav elgratgdrr lemsalrqlg
      721 gaawagcgrp vaeglehvrd glrqatllgd rgaeahllgw lavvssnqlr lgdalghghr
      781 alaaarqahd dhalaaaldg lktahahlgr mpelsrlige lepllrelgd lwllqwcvfe
      841 salpmvavga wddaaarihd alavnrrsgy tgydrwylah lgwiarlrgd ydeavrygrq
      901 sldgdshaww taatpamhat tlielghdae atallerame acsahgtlay tlrclaplae
      961 vtgsatllke adtlvsgiet ppgaawlqgt dayvsvarah largdargal rvlepvltaa
     1021 pgagwtapva aarelagrcr aalspargg
//
LOCUS       WP_181613368             227 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Nonomuraea soli].
ACCESSION   WP_181613368
VERSION     WP_181613368.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 227)
  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..227
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..227
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=22397
     Region          1..143
                     /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..65,68,74,76,78,89..91,93,95,104,106,108,110,124..128,
                     130..132,134..136,139)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176853"
ORIGIN      
        1 mkvagsavig adrervwaal qdpavlvrti pgcerleeig pdtyrmtvsa gvatikgvyd
       61 gevalssplp pdsfvlkarg agapgtveat vavrlsdadg gtrvdydaea vvggviggvg
      121 qrmlgavakr tagdffaave avllapeggp lsaaapadad ttaltptgap svastgaasp
      181 ptvfhrpaat ptaspspnal laafglgalt alagvavgwl lgrrrph
//
LOCUS       WP_181613399             365 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Nonomuraea soli].
ACCESSION   WP_181613399
VERSION     WP_181613399.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 365)
  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..365
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..365
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38201
     Region          7..339
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mnwpawpppl ddaqrklvnd vlesglwgat qggdvvarlt aafaarsgvp ygvavgnatl
       61 glfaalkglg vrpgdevvvp aytfvasats vllagavpvi advdpvhlhl speavsaals
      121 prtaaimpvh lagspapmde lnalaarhgl avvedaaqah gatyrdrpvg glgdagvysf
      181 qaskamtage gglitcrees vheavwsvcn vgrglcgawy ghpnvgwnlr lteiqaalll
      241 pwldrlddei drrnafcdal dldglpverv prpegttrds rhllmlrldp svdkarvlgs
      301 pvfdggypal gsmpalveag arvtdcpaae eaarsvvwir qnilmadpgr aceisenlnt
      361 vlaet
//
LOCUS       WP_181613490             496 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea soli].
ACCESSION   WP_181613490
VERSION     WP_181613490.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..496
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..496
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52699
     Region          67..311
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mgagrgtlgv aaglvllala tlgyalppaf dppplqvdaa fqalpeqpen errpvvaadp
       61 yrtekitipa vgqqlqatvr apatpgrhpa mvfisgsgng sqeefvpqae flaaagvvtl
      121 afdkrtvgyn frdrdfslla ddalrmikyl rsrpdvdpnl agiwavsegg wvapiaaadp
      181 avgfvvliss pnvsplrqva walneqllrl rapagvrdll tramgnfgfd flrhdampal
      241 rqmrqpvlal ygttdpsipf vestqaltka ltetgndkft irfldqadha mriaggpfap
      301 gyletlanwi kalpgaakpa lpiagatptq rfqasdvpaa pwyaggtmlg lticlaavgy
      361 vagpfaelvv rlrgrpltpa ahnaelwapi rrrlrrmawt glgllasvia fitllvmfsv
      421 nqagawpavl sgwlivrvla vlmllqevta vatvvsalrd gmrptrgqhv aiagvlggtg
      481 lllvaaayyg lfsfpw
//
LOCUS       WP_181613433            1133 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181613433
VERSION     WP_181613433.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 1133)
  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..1133
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..1133
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=121052
     Region          98..1019
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mgdplrilll gpphlllgdr plpirsakar allyylaatr tprsraelag llwgerpdar
       61 argslrlavl elrrdagawl disrdqvalr lgagcfvdha alagdpgveq alrwwrgdfl
      121 dgvglddapa ftawlegerq rtrlllrqvv lrhagrpdaa lvrlarvlaa ldpldeeagr
      181 llmsalagtg nraaalttye alrrrlreel gvapapqtva lreelarvpg rppgaaalts
      241 raalpvprts lvgrqaeieq vlallgterl vtlhgpggvg ktrlaiavaq rwggageraf
      301 vsfvgvhaea vvttlarrlg vdlspprsae dllvaaladr pvllvldnld hlpgfdvvia
      361 rvlqaapgvr mlatsrrrpa vpeqvcvavr glagppaeal faerarallp qieapggpgg
      421 qarggpggqv pggpggqvpg gpggqvpggp ggqvpgpggs salvaavcaa tgglplaiel
      481 aasllralpl eevarrlatd ldllaahesa prrrhgslrt vfeaswrlld ppaqqalaal
      541 svfrggftld aalevartsw rvlmrlvdhc mihldpagry hlhpiiqqya gshlsyrarp
      601 evvgrhtacf srllhghave ngldtaaarv lgaeldnlrl vlergdgdaa fldrywtlcl
      661 rlrlyeegla vlsrrlerta dpprlrarwl rlsgamlyql grdpdavgha eaalravglg
      721 wpasapalvt alvrdvlghl wqraragghd pvaaeaaqal aliallayrr hdllamlaas
      781 agqantawrs gdaalraeac ahlaialrva gsrrladrig hradtdlvrh sapppgvlgh
      841 gdaadwarla rglshlnagr lrearlvlte crertvdprl aetcagllae taiwqgdfat
      901 ardlfdetae laasrvgdev grhwcltgaa etllrldgtd pgeiravldr araaeerrrt
      961 hgallgvrdd paarlvqeir lltatarlha rqdprspaep rlqaslaavd hilelaarlp
     1021 rtqpgmiecw sglaelawih wihtsapatp draarrrlrv ldrhlaryin rypgaaarlg
     1081 wgrallhqar ghhrgadaha gralaaatrm nvaydarraa avssrdpaqa awp
//
LOCUS       WP_181613265             256 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Nonomuraea soli].
ACCESSION   WP_181613265
VERSION     WP_181613265.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=25515
     Region          17..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 mqpelvllll avalaagwvd avvgggglvq lpalllafpv appatllatd klssisgtta
       61 saigfargar idlrlavpaa vcamalsglg aataglipaq vfrpfvlgal vvvaavvvlr
      121 prlgtgtper rpargrsvaa ltvagvvlpf ynglvgpgtg amillaltgl lgldfidgsa
      181 takvvnlgan lgallvfalh gqamwmlglc maacnvmgar lgtrtalrkg agfiratllc
      241 vvaalivklg ldylna
//
LOCUS       WP_181612674             164 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine dioxygenase [Nonomuraea soli].
ACCESSION   WP_181612674
VERSION     WP_181612674.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 164)
  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 164)
  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 164)
  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 164)
  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..164
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..164
                     /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=18325
     Region          45..132
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mntlpernld rrelrdlvde laadpaqwqd qvefpegggr hyaslyrday vdvwllcwrp
       61 eddtgwhdhd issgavtvvq gallecnpri ggehletvvs egqsfsfgpd hihrltgaid
      121 ksvsihaysp plwrlgqysi ddtglmrrvs vsyadelrpi dava
//
LOCUS       WP_181613480             355 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181613480
VERSION     WP_181613480.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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 355)
  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 355)
  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 355)
  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 355)
  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 355)
  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..355
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..355
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38456
     Region          74..212
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
     Site            78..85
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(79..86,151,195)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            147..152
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            211
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mstvlrphae dlyseelall akdddrvrpp gwrlspwavt tyllgdgeri tpkyvgarri
       61 vevavatlat drallllgvp gtaktwlseh laaaisgdst llvqgtagts eetirygwny
      121 arllaegpsr eamtpspvmr amaegriarv eeltrmpsdv qdalitvlse ktlpvpelgl
      181 evqaqrgfnl iatandrdrg vnelssalrr rfntvvlpvp asaeeevaiv arrvgelgaa
      241 lhlpetstgq aeirrvvtvf relrnglted grtklkspsa tlstaeaisv vtsgialaah
      301 fgdgvlrasd vaagivgavv qepvsdrvaw reyletvvre radwrdfyra creis
//
LOCUS       WP_181613551             616 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Nonomuraea soli].
ACCESSION   WP_181613551
VERSION     WP_181613551.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 616)
  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 616)
  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..616
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..616
                     /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=65279
     Region          1..430
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          541..606
                     /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(563,572..574,581)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            573
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mitrllvanr geiarrvfrt crslgvetva vfsdadadap hvaeaghavr lggpspylsi
       61 eeilracsas gcdavhpgyg flsenaafaq avldagltwv gpspeaiaam gdkvaakrlm
      121 reagvpvlta dgqsfpllvk aakggggrgm rivrepreld eamaaasrea qaafgdgtvf
      181 aepllerarh ievqvladgh gtvwtlgere csiqrrhqkv ieeapspgit davrgrlfea
      241 aeraarkigy vgagtveflv kdetiaflem ntrlqvehpv telvhgvdlv alqleiaega
      301 rlpqaapsps ghavevrlya edrdflpqsg plhlfeipgd vrvdagvesg svvttfydpm
      361 lakviafgss rtaavrklvr alkdarlhgi ttnrdllvdv leseaflagd thtgfldrgl
      421 ppkdpptdvs alaaalagaa anreratvlr svpagwrnvr sqrrtarfae aevvydplpe
      481 gvtvisatpt rvtmergslr htfhvstygd tvhvdsslgs vrltalprlp rpvvevapgs
      541 llapmpgsvl rvevepgdhv dagrvvvvle amkmehqiva pasgvvseva vekgrqveag
      601 avlavisqgi segera
//
LOCUS       WP_181613572             309 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Nonomuraea soli].
ACCESSION   WP_181613572
VERSION     WP_181613572.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..309
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..309
                     /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=33547
     Region          15..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 mrtkaehtea ihrdrrvavv intrsrrgrk hyfevldqih glgfeplaey svvnpkrlra
       61 hldkaldlqp dllivgggdg tlssavrhva hrdvalgvlp lgttnnfars lglpldlaga
      121 ikvfaegkva didlgmagdr pfanlasfgv svevagkvkp wlkriigrpa ypltaltilp
      181 ghtpfrayit vdgkrhellt hqlniangrf hggwqvakdi sidngklvay qlgsgkklrl
      241 lgetlaratt grwrslaggp fvtgremlle tdppmaadvd gevrlrtplt lrvvpngvrv
      301 mvpssfedn
//
LOCUS       WP_181613692             447 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Nonomuraea soli].
ACCESSION   WP_181613692
VERSION     WP_181613692.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 447)
  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 447)
  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..447
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..447
                     /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=47981
     Region          2..441
                     /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 mdlrhwlera vsaieeweag hgpferhpsl avkdvepafd alvarlhdny pffhpryagq
       61 mlkpphpaav vgyltamlin pnnhaldggp ataameretv allaamfgfg thlghltssg
      121 tianlealfv arelhpglgi aygaeahyth armcrvlgve ghavpaddrg rmdlgaledl
      181 lrtgrigtvv lttgttglga idpvhealpl arrygarvhv daayggffal lagtdldaap
      241 wraiagcdsv vvdphkhglq pygcgavlfr dpavgrfyvh dspytyftsd elhlgeisle
      301 csragasaaa fwftlrllpl treglgevla agrraavrwa sllsgsqvle lyqppeldiv
      361 tyfpkaatlg ridrlsarml ddgmaeglhl stftvgrqam aarhpaiald tthgrvmrsv
      421 lmkpeselvv dslhaavesl agqrpta
//
LOCUS       WP_181613778             226 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea soli].
ACCESSION   WP_181613778
VERSION     WP_181613778.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=24181
     Region          3..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 meadiapvaa lmadptratm ltallsgral aagelarlag vsaptasahl aklldgglve
       61 avkqgrhryy rlkghevaev letlarisar pavrslrqss qarqleeart cydhlagrag
      121 valfdgmrer gylaggevta egervlgrlg vdvegarrar rrfapecldw terrahlgga
      181 lgaaltgvll eeewlvrgra prsivvtekg rrgleatfac keltsh
//
LOCUS       WP_181613997             395 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Nonomuraea soli].
ACCESSION   WP_181613997
VERSION     WP_181613997.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=40523
     Region          12..377
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mnrvairftr dratwlvylq igvfatylyg lssalqilra eqgvsqtvag lhgismavcg
       61 vaaglalpyl trrfgrratt waglvginag valvfassav pvtilgygla sgfgtftlyt
      121 gmaalsdhhg pagpaalnea nafgvifgiv apylvsaaaq safgwraall ltpvstvlla
      181 lalgrhwfpd knvetaehhe gpppgfgwrf yvaggvlfcc valeftfnlw ssalvttrtg
      241 lspavaastl taltaglavg rfvgtplalr mrttnllvga lavtlagwll fwlstspvls
      301 yagvfvcglg ialqfplala giiansgnrp drasaigsiw astavgvgpl vlgaladasg
      361 tvnaflmvpv lialavaglv ssrprpsess pvpas
//
LOCUS       WP_181614119             211 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            soli].
ACCESSION   WP_181614119
VERSION     WP_181614119.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   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 211)
  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..211
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..211
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22949
     Region          2..103
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
     Region          122..>179
                     /region_name="SCP2"
                     /note="Putative sterol carrier protein, contains SCP2
                     domain [Lipid transport and metabolism]; COG3255"
                     /db_xref="CDD:442486"
ORIGIN      
        1 mtgrrkyddg cavahgldll gerwallivr elllgpkrft dlraglrgas admltqrlre
       61 lgdsgvvrrr rlappaaswv yeltawgrel epiviqlgrw ssrspalrrd apigadslvl
      121 slkalfdpea argytatial hlgehrfrvr vddgglavar despeadavl etdpdtlaaa
      181 lwddgprpsd dptgvvarfl tlfplpqaar a
//
LOCUS       WP_181613754             436 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Nonomuraea soli].
ACCESSION   WP_181613754
VERSION     WP_181613754.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=46596
     Region          42..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(154,156,284,286,319..320,362)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mritsalaaa avlalsaacg sggstgatgg gtaseapaep vklnflslaw qkesieanka
       61 lvdewnknnp tiqvtyvqgs wdnvndqlvt qfegggapdv ihndspalsg fatrgylldl
      121 kdklpaelks dipqpawdtv tfgaeggvyg vpflqesqvi iankklldaa kvrvptadnp
      181 wtwdefaevs kkltkdgafg vawpmkspvn ktlnlalnfn gtffqtgadg kstvkvgpee
      241 kevlqriynq ihvdksadpk tlgmgtadpl pgfykgeyam lpvgvylrqq vaeqapegfe
      301 wvtlpplkgt ssnqgavsqt lsvsadsknp dealkfisff lngpnqarla kgdwllptsq
      361 kaatdpsitg aengwdvata svknlvvapf lkvngydewk skvatpvlqe yyagkisldd
      421 aakrlveegn kvlery
//
LOCUS       WP_181614366             408 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181614366
VERSION     WP_181614366.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..408
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..408
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43332
     Region          128..399
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msaeelaaai aarcesrvns ltreivaehe avlpgfaelh ggmlevetas ttrhgvrlfl
       61 rvaqgrgssd qdmrlfrera aqrmsdgvrl ttllsgyavg yraiwrmlce eagpgeeagl
      121 hrlgelmvta lertmtavce aylleaelar rgeamravar lllqspptre dptpdpgvpg
      181 vpgvqalaaq hgitlepsyr vlaftlrhpg appavsrrrh avqgaldrla aqpvltlfdq
      241 haghallpar lavptaklgr rlveaagplh aglasadslt dipatsrqaa riaqvaaacd
      301 rppgvyelgd vlvefhlstp gpaaqalssr lallepslva tleaffaadf drrataaalt
      361 vhpntvdnrl arvaealqad prtaggillv gaalavrrle gfhfrqtv
//
LOCUS       WP_181614373             335 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181614373
VERSION     WP_181614373.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 335)
  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 335)
  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 335)
  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 335)
  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 335)
  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 335)
  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..335
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..335
                     /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=35956
     Region          71..333
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrtvrlrlt vlysglflas avalivvvff vfrflpsppa pvapgqldvp spfpesdrvv
       61 rssliglgam alvsawlgwv msgrvlaplg rmtatvrrit adrldrrlsa sgpddelkel
      121 adtfdelldr leaaftaqrr fvanashelr tpltlqrama evaladpgad lravlermva
      181 agqeqerlie allvlargqq gltrrepldl avlaggtrpa pflgdralme rlvanlldna
      241 rryngpdgwv rvstgvrqgr aelvvansgp fipqervgal lepfqrlegg rragadglgl
      301 glsivaaiva ahhgtldlrp rpegglevtv tlpgs
//
LOCUS       WP_181614126             273 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181614126
VERSION     WP_181614126.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 273)
  AUTHORS   ter Beek,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 273)
  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 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..273
                     /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:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29348
     Region          7..252
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtdalgltgl ryrfgkveav agvdltvaeg eifgllgpng agkttairci ttllpvpsgm
       61 vrvfghdasr ermavrrllg yvpqqlsadg nltgrenvam farvfdvprr eraarveqal
      121 tavglaeasg rmaatysggm vrrlelaqal vsaprllild eptigldpia rtgvwehina
      181 vraatgmtvl vtthymdead qycdriglmh rgvlracatp yrlkedlrar qggdgvptle
      241 evfrdlagsg legeleggfr dvrstrrtat rlg
//
LOCUS       WP_181614329             392 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181614329
VERSION     WP_181614329.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=41576
     Region          135..391
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mgdtqrivyw vqrlseiamv gwlsmlllvd vvasasvrga qflvplcgva givaimlrrr
       61 hlvmgfcvtv glslvtslvi gvtntpglpg maesgailll tisllrhvtp mrravlvslv
      121 glvalmaegv grdylgsagl afsfvlfvgw siaeglglyl riqqdrrrdt lssvrraerl
      181 elarelhdlv ahhitgivvq aqaaktvaem kpeavgpald aianagteal tsmrrlvgvl
      241 raddeaarrp gttladlrll tesftasgpq vafevgagld eralapevlt tmhrvlqeal
      301 tnvrrhapgt gwvevdlrpv ggpyspaall gsglgvrlrv rnyssaadpr ikrlgggfgl
      361 vgmaerveal ggrlwagpte egawevvaev pt
//
LOCUS       WP_181614448             493 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181614448
VERSION     WP_181614448.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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 493)
  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 493)
  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 493)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 493)
  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..493
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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: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=54431
     Region          1..487
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mtdrlrtlpv grwflyasiv galvlvagta atlnslhqld darsdiidvi dpatmrtldl
       61 tlalstqegs arsfgltkdp qfaanyqrav iaeelalrel nrlvpgdrae lqeiartaqa
      121 wrtayaekml agtppntdla rvgsglmtta rdamsrernt leqrhaaaki tieerarevy
      181 laigvvlavi iallvvlgli vrnfvvrpis elarqvdgva kgdfdrtihv drpaeletls
      241 ghidgmrrei vqqlqlsedq atelrrsnsd leqfayvash dlqeplrkva sftqlleqry
      301 geqlderakq yitftvdgak rmqllindll dfsrvgrmgg eiatldsavp lraalhnlea
      361 qidhtdavis hdpmpkvrgn rthltqlfqn lignalkfrt datpavhiga rhnddgtwef
      421 scadngigid akyaerifii fqrlhpreay pgtgiglalc rkivenhggt iwvdtsaspg
      481 ttvrwtlrga dda
//
LOCUS       WP_181614522             310 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Nonomuraea soli].
ACCESSION   WP_181614522
VERSION     WP_181614522.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..310
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..310
                     /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=34154
     Region          1..302
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mrsrrsvlav pgsnprflek aqsldvdevf ldledsvapl akaqargnvv kallegdwtg
       61 ktrvvrvnal etqwtyrdvi evvegagerl dcvmlpkvqd atevvwldtl ltqiektmgf
      121 evgrigieaq ienarglvnv daiagsskrl etlvfgpadf masinmrtlv vgeqppgype
      181 gdayhyilmr llmaarmhdl qvidgpylqi kdvegftkva rraaalgydg kwvlhpsqvq
      241 acnevfspsq edydhaelil eayehyttve qrgavmlgde mideasrkma lvvaakgraa
      301 glsrttsfrs
//
LOCUS       WP_181614293             297 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea soli].
ACCESSION   WP_181614293
VERSION     WP_181614293.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 297)
  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 297)
  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..297
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..297
                     /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=32643
     Region          7..228
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 msspqviflg glgrsgttll erllgqlpgv aplgevvhlw argvlagepc gcgapfaecr
       61 fwhevgelaf egwtpqvart vlalrqrvdr trripfvdhr dlgryvhayr avyeaaaeva
      121 gadvvidssk haslafclma ggvdvrvvhv vrdpravahs wrrtverped grpmtrwgal
      181 rtsmhwtaqn laldlfagag ritrvryedl ladprttltr lageldlepd fgflrgstam
      241 lqprhtvsgn pmrfavgpve lsrddawhdg lprrhqtlva gltwplmsky gyrgaaa
//
LOCUS       WP_181613722             529 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 64 protein [Nonomuraea soli].
ACCESSION   WP_181613722
VERSION     WP_181613722.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Wu,H.M., Liu,S.W., Hsu,M.T., Hung,C.L., Lai,C.C., Cheng,W.C.,
            Wang,H.J., Li,Y.K. and Wang,W.C.
  TITLE     Structure, mechanistic action, and essential residues of a GH-64
            enzyme, laminaripentaose-producing beta-1,3-glucanase
  JOURNAL   J Biol Chem 284 (39), 26708-26715 (2009)
   PUBMED   19640850
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Rutenber,E., Ready,M. and Robertus,J.D.
  TITLE     Structure and evolution of ricin B chain
  JOURNAL   Nature 326 (6113), 624-626 (1987)
   PUBMED   3561502
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19012039
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..529
                     /product="glycoside hydrolase family 64 protein"
                     /EC_number="3.2.1.39"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54923
     Region          36..393
                     /region_name="GH64-LPHase-like"
                     /note="glycoside hydrolase family 64:
                     laminaripentaose-producing, beta-1,3-glucanase
                     (LPHase)-like; cd09216"
                     /db_xref="CDD:185755"
     Site            order(150..152,154,159..161,163,165..166,300..301,366,
                     369..370,379)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:185755"
     Site            order(150,166)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:185755"
     Region          407..527
                     /region_name="beta-trefoil_Ricin_laminarinase"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in glucan endo-1,3-beta-glucosidase and similar
                     proteins; cd23451"
                     /db_xref="CDD:467329"
     Site            order(415..418,429,431,434,439..440)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467329"
     Site            order(458..461,471,473,476,480..481)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467329"
     Site            order(501..504,514,516,519,523..524)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467329"
ORIGIN      
        1 mrippriari lattllaapl alanaspaqa igpailpvtv tnnsgradav hlyvlgtnla
       61 tgrlghvnaa gtftpwsggq ippspapdvs iggpgnggss tirfprgfsg rvyfslgqkl
      121 qffltpdglv qpapwaggdp nrsilfdwse ftyndaglwi nssqvdmfav phavsvtgas
      181 gatkrtgdlv angrdaiiga iraqagwant vitrsdgtvl rvlspgkaad agllsptyld
      241 syiasawnay taktltvvpf tdqpntrffg rtsgtvmtft ntsgaqvasf nrpssadvwg
      301 cagnlhapnd lvvgpiartl caalnrgtlg tvdtqpslna aefyrnnptn hyariihanm
      361 tdgkayafpf ddvgafeslv hdgdprsagi iltpftggsa npartivgpg gkcvdvsgdd
      421 tggngaavql wdcqswavdq rwtrngdgtl rtlgrcldvv sggtangtkv qvwdcngtga
      481 qvwapqadgs lrnpqsgrcl dspggatang trlqiwdcng tgaqrfpls
//
LOCUS       WP_181614621             280 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea soli].
ACCESSION   WP_181614621
VERSION     WP_181614621.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 280)
  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 280)
  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..280
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..280
                     /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=32304
     Region          27..231
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mkrsvlsvsr aagrltsagr vlpsflivga qrcgttslyr alaqhpllak pvmhkgvhyf
       61 daaydrgldw yrghfpltvg sallkrrygt rpqafesspy ylfhplager ivrdlpgvkl
      121 ivlvrdpver afsahahela rgfetesnfe yaieledkrl agaeerlrae pyslhhshrh
      181 haylargrya eqldrleplf grdrihvids hrffsqperv yerlleflgv prmddpvfer
      241 hngrprphpm petlrqslld hfevydtqlv pwldgdpswr
//
LOCUS       WP_181614391             463 aa            linear   BCT 28-DEC-2024
DEFINITION  class II fumarate hydratase [Nonomuraea soli].
ACCESSION   WP_181614391
VERSION     WP_181614391.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=48991
     Region          1..460
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 msefrtehds mgevlvpada lwraqtqrav enfpisgrrl epahiaalgl ikavaaevng
       61 elgvidkela qaiaqaaadv aenehdaqfp idvfqtgsgt ssnmnanevi aslaeqrlgr
      121 pvhpndhvna sqssndvfpt sihvaaatev vyhlvpslrh latvlrvksa efatavksgr
      181 thlmdatpvt lgqefsgyaa qiehgvnrvn aalprlvelp lggtavgtgi ntppgfaara
      241 vdklseatgi rfaeaedhfe aqsaqdsive lsgalkvvav smtkiandlr wmgsgpragl
      301 geinlpdlqp gssimpgkvn pvipeavlmv asqvvgndaa itfagasgsf elnvqlplla
      361 rnilesvrll anvsrlladr cvsgitanhe rlreyaegsp sivtplnrhv gyeeaariak
      421 qalaerktir qvvierghva ngtlteeqld saldvlsmth pae
//
LOCUS       WP_181614689             269 aa            linear   BCT 28-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Nonomuraea
            soli].
ACCESSION   WP_181614689
VERSION     WP_181614689.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..269
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..269
                     /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=28535
     Region          22..267
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 mtaadagrwe etadepqgpv gkafrlsaad slslgnalcg flsvcvmata aiqslqaghg
       61 lkveprffat avvllligat cdlfdglvar rfrasamgae ldnladvisf gfapafmvvi
      121 wgsssgdlql wsvllvagai llagvvrlar facvktksgd fmglpipmga mtvisiimlf
      181 ttpnylvlaa llgvawlmvs rieypkpkgq llavvlawil vnvafltfwv afpengdlpi
      241 kvggamqial vaaiplrmlf ykrekrkvs
//
LOCUS       WP_181614669             242 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Nonomuraea soli].
ACCESSION   WP_181614669
VERSION     WP_181614669.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..242
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..242
                     /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=26807
     Region          10..141
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mslrfheiae aghrilnpft edklrllgei criapgtrql dlacgkgell stwslqyglq
       61 gvgvdisrvf leaagkrave lgvedqvsfv ygdagayeae edsfdivsci gatwigggla
      121 gtlelirkpl kqsglvlvge pywispppkg kgeefsefts lagtaerfea aglelvemvl
      181 adqdswdryv asqwmtlsdw irdnpddeei eevkeflans rrpylewqrd hlgwgvfvar
      241 pl
//
LOCUS       WP_181614765             201 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nonomuraea soli].
ACCESSION   WP_181614765
VERSION     WP_181614765.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=21717
     Region          33..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 mfdqafweer yssapaiwsk npnpqlvtev seltpgtald vgcgegadar wlaargwrvt
       61 gvdisptalk raaeaepsve wvhadlfgaw pfagrafdlv saqfmhppad eravlfgala
      121 savapggtll ivghhpldle mgvprppmpe lfytaedlaa alapgewsev vtdtrprqtt
      181 ydgqeytihd avltarrtha r
//
LOCUS       WP_181614006             660 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nonomuraea soli].
ACCESSION   WP_181614006
VERSION     WP_181614006.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 660)
  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 660)
  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 660)
  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..660
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..660
                     /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=71727
     Region          9..659
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpvdqlapdi laseqahlae srkalqamre haqslssdaa gdwvsqqilq slldqrvaal
       61 adhpdtplff grldrnaddd lprtiyvgrr hvhdghskpl vidwrapvsr afyqaspgdp
      121 mgvhlrrrfg yhggkltafe depldtgadv gpsrilteei erprtgpmrd ivatiqpdqd
      181 eivrsdlgtt vcvqgapgtg ktavglhraa yllfthrekl aragvmivgp nkaflsyiss
      241 vlpalgevkv dqttvadmlg tpgateepev aalkgsarmv dvleralwah ivkptegvvy
      301 tqgvyrfrva dhevreivas lrgttrynpg rdaltqriah lvlvrmeqrg espddrvhdk
      361 varskevkav vesvwpkltp qqvlfkllsd peflakaars dltaeeqqll lwrkpyrgak
      421 sakwtaadaa lldelndlme rtpslghlvv deaqdlsemq lralgrrcrt gsatvlgdla
      481 qgttpwsvss wetvlkhlgq asgevteltl gfrvprevld yaarllpsia phlaaprslr
      541 pgagslsvrp ggslteavtq aldkegsigv ivpdarvdei aqelgapvlg pdstedhrll
      601 vvpaslvkgl eydhvivvep adivaaetrg larlyvvltr avtsltvlhd rplpeqlaag
//
LOCUS       WP_181614892             947 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181614892
VERSION     WP_181614892.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 947)
  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..947
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..947
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=100824
     Region          72..947
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          725..753
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(726,729..730,733..734,736,766,769..770,773..774,
                     776..777,806,809..810,813..814,817)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          764..794
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          805..833
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfrilgtte vagepvpgrg lqmllsellm aggaavpeqr lrhdgatana lqsqisrlrk
       61 lvpvertpag yrlpadpeev dahlftrlaa egeralragr padaagllre aldlwrgeaa
      121 ldglnearqr amehrveadl rlgapvveel relvrehplr erprvllira lardgreaea
      181 lsafeegrrl lgerlgadps aelqrlhvqi lrgehgrrps lrapltsfvg rdaelatlgd
      241 llarrrlvtl tgpggagktr laveaarrle agggrsggrv vlvelapate vapavlaaag
      301 ggsdpvdala gesgvllldn cehvlaeaag lvarlldgcp dlrvlatsre plgldgesvl
      361 pvqplparva esllvdrara vrpdfepsea varicrsldg lplaielaaa rlralsaedl
      421 adrldldlla srtapprhrt lravvswswe llcprerrla arlsifpsga tlaaaeqvcg
      481 atpgllaalv dkslvqadgg ryrmletvra fcaeqlgddp vrqahaeffa rlteeaepyl
      541 rnhrqlaala elaaehdnln aalhwaigag hagialrmtg slwfywwlrg lrhhgarlsl
      601 raldlpgadq cgehyvmsvl qvvsagppep virplmevae rlaagldhpl vrmvhpmtai
      661 idgdyaalip allrsstepq pwlrgfaelm lgllrsggge laradrhlds altafrlagd
      721 rwgaaqamlq qaliaglrgd hrtelaitdq alaltapfga tedtsgalss rglalarcgd
      781 ldgarrdllq aaevartret eemlaialfg lgevarlgge peqalelygq alagcetlwv
      841 gaeevraril iglgqvtgda glhreafavl mrtldlpaaa eaveglaale pageraallq
      901 gaaaalrgvp gtrtddayvr gaamsraqiv rlvsapragc asaaahr
//
LOCUS       WP_181615015             213 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181615015
VERSION     WP_181615015.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..213
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..213
                     /product="helix-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=22588
     Region          5..210
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 msstddleal agladparrr lydlvaasph pvgraeaaea agisrtlaaf hldklaesgl
       61 ldshfqppak kgpgsgrpak vytrarqert vslpprdyvt laavlaetve lldaqdkaeq
      121 aarkagekla agggdlietl rergyepyae geqirlrncp fhtlaedqpv lvcslnlalc
      181 qgllqglgqd parvsldprp geccvavskt nen
//
LOCUS       WP_181614635             604 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181614635
VERSION     WP_181614635.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..604
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=64331
     Region          62..250
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          360..602
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mrvylellar easavefegp iiearargaa peevaeleqa kvealkvrel lrrrarreae
       61 lsalydtasd laglrdldav leaivhrarq llgtdttylt lhdpdkgdtf mrvtdgsisa
      121 afqnlrlapg aglgglvaqt arpyatadyf adprfqhknh idtavheegl vailgvplkl
      181 gqrvigvlfa anrsarpflq eevalltsla ahaavaidna rllqetrnal eelssthrsl
      241 rehgdavera arahdrmmel vlqgrgiedi aavvaesgel tvldglgnvi vgqatddpgi
      301 feaaqasral grtvrrhdll iasvdvggep lctlivrsad aderiveraa lvcallllfr
      361 rsvaeaegrv rgellddlis rpddeglidr anrlgvnlar phvvivakhq gqreraafwa
      421 ssqaalshgl aaarpeevvl llpgprdakr iakdlsaalq spatagaagp vtgiadvhga
      481 yreaqrcada lialgrrggg asaselgfvg lligeagsip gfvhatigpv vdydakrgts
      541 lvgtlaayfg aggspsrtae amhihvntvs qrlerigrll gegwqdpera lelqlalrlh
      601 rlsg
//
LOCUS       WP_181615024             913 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Nonomuraea soli].
ACCESSION   WP_181615024
VERSION     WP_181615024.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 913)
  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 913)
  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..913
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..913
                     /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=101006
     Region          1..910
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mttpaspaer yaafreklsg dgpamtsfrr lydfeldefq ldacraleag dgvlvaaptg
       61 sgktvvgefa vhlaleqgrk cfyttpikal snqkyndlvk rygtakvgll tgdnsvngea
      121 pivvmttevl rnmlyagsgt lsglafvvmd evhyladrfr gavweeviih lpesvrival
      181 satvsnaeef gewlgtvrgd ttvivdehrp vplwqhmmvg nriydmftae ageggpkhin
      241 ptlmriarde erlagrggrr gygrpprnrp pdraqtiekl dsegllpait fifsragcda
      301 avmqclyagi rltderekhe irqivderta hlpdedlavl gflewrdcle rglaahhagm
      361 lpafkevvee lfvrglvkav fatetlalgi nmpartvvie kldkwngemh adltpgeytq
      421 ltgragrrgi dveghavvlw qpgmdplsva glagtrtypl rssfqpsynm avnlvgqfgr
      481 erartlleas faqfqadrav vglarqlrkh eealagykda mtchrgdfpe yaalrrrlsd
      541 reaelakqrg harraaalrs lealkpgdvi rvpggrragl aivldpgitp rgegprplvl
      601 tigkqvkkld padfpvpvep ietlripknf nsrspkeran lvstllakig drdlgkpdra
      661 rdhavedael lelrrlirqh pchgcdered harwaeryyk llreteglrr rvegrshvia
      721 rtfdrvcgvl eqlgyleget vteagrrlgr lyteldllta eclrsglwdk lepaelaacv
      781 salvfesrqs ddarrpkipa graqdaltam irlwgelegi erdngvsiir epdmgfawaa
      841 frwtkghsld avlmdgingn elaagdfvrw vkqlmdllsq lgdacppgsp vrqtaskaid
      901 amrrgvvays slv
//
LOCUS       WP_181615060             646 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181615060
VERSION     WP_181615060.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 646)
  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 646)
  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 646)
  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 646)
  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..646
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..646
                     /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=68760
     Region          1..236
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          123..>603
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mdfrvlgpve agspatrlsp kpllllatll ceantrvghh rlvealwgar ppesaassmr
       61 iyvsqvrqal rddsrivaer ggyriridpg eldshefeel vrqaasadpa tagrllgeal
      121 rlwrgpafad lehhgslsat avrleelrvm ateqwvaael gqgrhreilt elqtlvrahp
      181 lrerlcgllm lalyrsgrqa ealeayartg allaeelgvd pgpelrrvye gllrgdegva
      241 adlgipgsaa apaaqspvpv apavprelpa pvpgftgrqa alaaldrllp gdgasppmai
      301 saiagavgvg ktalavhwah rvagrfpdgq lyvnlrgydr alpmrpldal agfllalgvp
      361 resipgeves aaarfrsvva grrilvlldn agsaeqvrpl lpgtpgclvl vtsrdrltgl
      421 laregasrvt lgvlsqdgar alltealgps rveaepgatg elaelcgrlp lalriatayl
      481 fdhpgqtiad yvhtlrtgdp mtalaisgep daavraafdl sygtldpaar rvfrllglvp
      541 cddfdlrsaa vlaamaeqea agavdrlada hliewhgaeg rggrfglhdl lrryagglar
      601 qedsdaeraa arrrlftwtr ettsteappy pgytgcprst acrqwt
//
LOCUS       WP_181615066             227 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF47 domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181615066
VERSION     WP_181615066.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..227
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=24197
     Region          <63..188
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 msrarrsgrl rrawddlrga sgprivalva aqiatarsga vlaletahgr vappaararm
       61 ariehegdaa raelvkalrg slatpidred lyrlsrsvdd vldhlrdyvr egdlfgptgp
      121 tdgtgaggar faveplraii dgldgleval grvladpasv tscalaarka ggrvrqhyqa
      181 elarlfagpl emevlrrrel larldtvgrr lgeaadalad amlkrsm
//
LOCUS       WP_181614982             495 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nonomuraea soli].
ACCESSION   WP_181614982
VERSION     WP_181614982.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 495)
  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..495
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..495
                     /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=51302
     Region          1..493
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mdlllrggtv ydglgspgvv advaisggrv aavgsgltas rvidvsglav apgfidahch
       61 sdlvplmdda qpfklfqgvt teingncgfs yapsapalee ltghavpgws fagyldaiea
      121 agptnhvatl vghstlraav sgfsettsve amaelareaf eagacglssg liyppgsygd
      181 teelvalarv ahaygrpytt hmrnessela aaldeaieva trarvrlqvs hckvgglpnh
      241 gqasmllerl rsarargvdv lgdqypylag stvlaallpp valsggnvaa rlsspgerar
      301 llelssgsgl wrdaapgkvl vtshtrpgva grtladlggt wdtlcdlvae dpaaqmviem
      361 mdeadvveim adpligigsd ngapvglehp rtwgcfprfl gayvrerrvv pmaeavrkmt
      421 slvadqfgla grgwlgagay aditvfdpet vghagtylep sarptgivhv llegrpvveh
      481 gefggaragr vlrma
//
LOCUS       WP_181615124             147 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            soli].
ACCESSION   WP_181615124
VERSION     WP_181615124.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..147
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16082
     Region          18..135
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 matltaaqqr aqakveydaf vaacpsrrll drisdkwvtl ilaalgsdsa hqpgagcdge
       61 prvmryselq rllagvsqkm ltqtlrsler dglvsrtvvp tvpvtvsyel tdlglslhem
      121 mrglkawaet hmddvlahre tydtrga
//
LOCUS       WP_181615067             599 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nonomuraea soli].
ACCESSION   WP_181615067
VERSION     WP_181615067.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 599)
  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 599)
  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 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   5  (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
REFERENCE   6  (residues 1 to 599)
  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 599)
  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..599
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..599
                     /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=64408
     Region          38..592
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mfksrpriry rlqvlrhdpt aamglvlavl lvylvvaplg avlsdafrvq fgdqvhagqq
       61 pgewtgyylw rvfrsriael ifwepllntv vvslgtvafa llvgggmall vartdvpgrr
      121 flagalvvpy mlpswtfsla wltlfknera ggqpgvlqaa gvrtpdwlay gavpiivtlg
      181 lhyfpfvfll vgnalrrids qledsarilg asratvlrri tgplllpals savllvvgrv
      241 lgtfgtpyil glpadyrvls tglyqsirdr stgvasvlag viviigvlvv lvdmrlmreq
      301 rrfvtvggkg amdrvghlrr grwplwsvaa gvlilsvvvp imtlllstvm rtpgvwrldn
      361 ftldfwlaes lpgavgfphg vlrggelwea aynslvivgl asvicgvlgl lvgyvvvrgt
      421 aprvaaflrq vsflpylipg iafaaaslsl favqrgpvpa lygttallvl vmavthlpys
      481 srsgiaamtq lgrepeeaaq icgaswparm rrivfpiqkg alvtgvvlpf vsglkelsiv
      541 imltttgtql lttlsitlvd ygytqlanav vlmialvsft mtylaqrltr sslasglgg
//
LOCUS       WP_181615157             428 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181615157
VERSION     WP_181615157.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..428
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..428
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46341
     Region          162..423
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mndsacrwll glrpqgggpg savpaatqal areilghgpa gwavetaewm thevirqvpa
       61 ygggrtqfet lrrsveatvl aalggllrda rptpeqvpme avegnaelvr rgvpldlvlr
      121 gvrighaclh qrlmdaidae pepvrlpesh rvsellfsya dahasrmaee yiaerdrwqa
      181 steaarrriv ddilggrrid qgsatrtlgy ditrhhlafi vaadeldtpa evlrrfasev
      241 gravggqgvl tvqagpsdvw awtattaeap avpsaearqa qartvevpag lrlalgppaa
      301 gvagfrrshl gareaqgflg gdvrlrrhad irvrsllaad aersrwfvee tlgalledgg
      361 rtaelretlr tylaagrspq raaellhvsr ntvtyrikra eellgrplsg dlldvrlale
      421 itrsepkp
//
LOCUS       WP_181615159             383 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181615159
VERSION     WP_181615159.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..383
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41575
     Region          35..375
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mktktirrvt vpflaaglla galtapaaag drpelrqnlq ewidagftgi qlrvrdekge
       61 wagsagmrel gasakpptng sfwtgsvtkt vvatvvlqlv aenrvtldsp vadhlpeygl
      121 drritvrmll qhtsglfnyt gdlgpdgtwm pgitasgdaw vterfrsytp qelvrvalsk
      181 pprfepgagq eysntnftla qlliekitgr pyadelrdri lrplgmrdtm vpgdrtrlpg
      241 phahgyyrvq gkvvdvsrqn lslltgagdl itttkdqatf msalnggrll paplldemrk
      301 pygklgyglg lfvqdlgpgc gtvyqhngsp phgygalmys spdgrktlta svtwvdespa
      361 rgaaqhfdrl lkslltqvyc ear
//
LOCUS       WP_181614772             288 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Nonomuraea soli].
ACCESSION   WP_181614772
VERSION     WP_181614772.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 288)
  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 288)
  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..288
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..288
                     /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=31071
     Region          <113..244
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mrhilvvngi kvrrpvflmg aphsgadllg ralkrspgfh vtmgrtcvah vvyafarrps
       61 isrssgaarv irdalaeawq vvpgacaqcp dacreaggvt gtgpcvsaas lsrfcdaspd
      121 llysatalln afpdarfvql irdgrdvaad mladpaclaw fkpvmlsdet efpnpflgls
      181 kgehrdnwks mpvagkaalr wrsairlsag lrqdlpadql ltvryedlvr apaqslatls
      241 afletqiskv alygrrlqps agrlrpadre lvekvakeel srlgylap
//
LOCUS       WP_181615180             222 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181615180
VERSION     WP_181615180.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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   Rosinski,J.A. 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 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 11457150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=23609
     Region          4..211
                     /region_name="COG2345"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441914"
ORIGIN      
        1 mqgmdsgtra rvarlilehg pitaaalger lgltpaavrr hldaleaegm ieprtmrprg
       61 qrgrgrpakl faitdagrsa fehayddlag salrflaerl geeavsdfar sqvkglverl
      121 epvmsavpad rrvqmlaeal saegyaasas kaksggdqlc qhhcpvahaa aefpqlceae
      181 teafaqllgt pvqrlatiah gdgvctthvs pvriresket gr
//
LOCUS       WP_181615422             164 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-class carbonic anhydrase [Nonomuraea soli].
ACCESSION   WP_181615422
VERSION     WP_181615422.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=17550
     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 mtafddllaa nadyardfld sglpgkaarg lavvtcmdsr idplgllglk pgdakilrna
       61 garvtddvlr tlvlavyllg vervlvmpht dcgmakvsds dvyeltqshg vdtrslefht
      121 vpdqhaallh dltrirtspf lpkdmpvgga iydvrtgkll pvdv
//
LOCUS       WP_181615427             281 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Nonomuraea soli].
ACCESSION   WP_181615427
VERSION     WP_181615427.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..281
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..281
                     /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=29599
     Region          1..281
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mkllvicnra aggvdeeare evlrelraha evvvaeevgg fpdhipvvmg gdgslhhvvr
       61 tlhergelga raiglipmgt gndlartagi tpdnavkavl egrerpmdll vddhdgvvvn
      121 avhvgvgaea sqraqalkpv larlayrvga vvagvrargw rlrvtvdgec vadgtrrvlm
      181 vglgngrtig ggtplaprae pgdglvdvvv sfavgplqrl afgvrlrrge htrlgevkvt
      241 rgrkvsiagq pvpvnadgel egkinrrtwt vlpgawrlls p
//
LOCUS       WP_181615505             317 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181615505
VERSION     WP_181615505.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 317)
  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 317)
  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..317
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..317
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33654
     Region          4..310
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtpidqaass lakrspgavv tvvtdsgadh ratgqaadet alfeigsltk vftslalata
       61 vtrgeltvdt plndllpgar ldgvtlgqla thtsglprlp kglmpraflp mddpyarftr
      121 dvlladlprp kesrgwkysn lgtgllglal aehagtdfeg lirkrvtgpl gmgdtvvtpt
      181 peqarrtvpg hnrwgrrrpy wnlaalagag glrstaadla tfvrhqldgg aavelthreh
      241 vtvnprlsmg lawlrmtaps gkqtllwhng gtggfrsfma ivperrvgvi vlanstrsad
      301 pigmkllral tldnida
//
LOCUS       WP_181615687             362 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181615687
VERSION     WP_181615687.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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..362
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..362
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38658
     Region          9..351
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 maeihgtydp rfskvaeala dsldgddvga saavhvgdep vvdiwgghld earslpwqrd
       61 titsvwsttk tmtalcalil adrgdldlda pvarywpefa aagkhdvrvr hllghtaglp
      121 dwdepttlad myawspatsr laaqtprwqp gtaagyhslt ygfligevvr rltgrslgtf
      181 faeevagplg adfhigvpae hdhrvaplla apdgdrpegf algvsdanta dwrragnptv
      241 ggfgnarsvg avqsvlasgg tyrgvrllsa agcervleeq fngedrllgt pirwglgyrl
      301 egrtcswggw ggslvlvdld lrmtvsyvmn qilwedgysr alaivlaayd gvaagsqhrq
      361 ng
//
LOCUS       WP_181615528             383 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181615528
VERSION     WP_181615528.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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 383)
  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 383)
  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 383)
  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 383)
  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..383
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..383
                     /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=42225
     Region          63..379
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtlrvrfavv sgaiffvlag llliglyllv raqlepvpgw rnpdvirvag yefypgqagw
       61 evanqrgiqi rrlyqagtld svrnvgllvl plgtalaafl gwrlarvvhr pleqatltar
      121 rvaqshdlre rldyraddei keladtfdtm ldrlsrafdg qrrfvanash elrtplainr
      181 tlvdvavrrp dasddlrrlg esllvvnerh erliagllal aegeqivldr rafdlsdvve
      241 haldlaaeea asrkiaihrl ldsapvagdp vlierlvqnl vengmrhnep gggvwvttrq
      301 rsdrvelvva ntgllvhphe vesifqpfrr lhgdrlnsdr gtglgmsivk tvveahgghv
      361 svrprdeggl tvtvelpaal pag
//
LOCUS       WP_181615913             836 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181615913
VERSION     WP_181615913.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 836)
  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 836)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 836)
  AUTHORS   Rosinski,J.A. 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 836)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..836
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..836
                     /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=87429
     Region          <78..818
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          781..>827
                     /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 mptpwpftgr saelagladl laagasvvls gtagvgksrl aaeavgcada lrvsatvpdl
       61 plgalspllp avppegnvla waadaiagsg rvlllvddah rldatsatlv hqlvaagraq
      121 lvatvrtgep cpdaivslwk delaervdvg pltyvhalle rvlggpverd aadrlaeltr
      181 gnalylrelv aagalrlddg rwrwagrltl prrlseliel rigtlaeper aalelaalge
      241 plgldmlvrl agagavenle erglitvigd rrrqavrlsh plygeavrag tprlrtmrrl
      301 relagavest garrrddvlr lavwrldsgs atdpepllaa lrlawavady plaerlgraa
      361 veagggpeag lllgtvlgya grpeeaaeil rstweqecee rtrallattl grtlgqlgrl
      421 aeaerlleda avmvddlenl qeitlmrtmf tmaagrytat aelaatilar pgnpglavqa
      481 hvttawallf tgrpldales vdraiglgta wreeipvlvm smnfirihaa tligdldlcr
      541 saaaeigaig tetweaarfg hqwaegvaal magrvreave llrpappvlp drvdsinrad
      601 lalaaglagd valagralae aeaippatpi hqtmidlarp wltgsaaeal raaalagerg
      661 lpglevlalh tavrlgdrsp atahrlaela glcqgrlael aalhaaavhh grdlmavaee
      721 fagaglllha aeaaaqaaga faeagrqasa raasarawal srecrgaatp alarlaapal
      781 tkreleiarl aaaghsskei adrlvlsprt vdnhlqaafg klgvsgrgdl gpllgq
//
LOCUS       WP_181615829             705 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nonomuraea soli].
ACCESSION   WP_181615829
VERSION     WP_181615829.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 705)
  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..705
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..705
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=77208
     Region          2..705
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          391..421
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(392,395..396,399..400,402,428,431..432,435..436,
                     438..439,469,472..473,476..477,480)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          426..463
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          468..496
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkrllgrarl vtltgpggvg ktrlalkaah avrrafedga ffvdlsdvra pemldralvt
       61 clrlvdqtar pacevlhahl adkrvllvld gvehlveece allgpllkaa aglsvlvtsr
      121 qvleadgehv vvvppmsagd avslfadrag daslgrgqte lvrqlclrld llplaielaa
      181 vrlrvmclee vviqllpldl gnrnttlrtv igwshelctp herllwarls vfcgsfalea
      241 aeavcsdscl paveiadvvg glvdksilsa eetagglrfr mldsikdyga ewlarldsqs
      301 erlerrhkdf ylaqartsaa awfgpdqqri fvrtraqldn lrgafercev dealelastl
      361 wfywvgcgql gegwtwlgra larggstgpr aralwvagyv avligefsra remleecral
      421 edpatkayav hrlgclalvs ddhdravelf neavehyaan rtlecnvlma cvelalvmaf
      481 qqqveachel cdqvresces vgelwvrsyv dyveaytawl tgdgdlaltl slrslqvshh
      541 fhdlfctvlv iefvallrae sgdveraavl qgaaariwes vgprlldssy fnaahvacae
      601 lsrkalgrha yagahtrgtr ldldaavava mgaaetrqel pltpreweva elvslglsnr
      661 eaagrltisk rtvdthvehi laklgfstra qiatwvteqq desar
//
LOCUS       WP_181615951             458 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Nonomuraea soli].
ACCESSION   WP_181615951
VERSION     WP_181615951.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 458)
  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 458)
  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..458
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..458
                     /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=49267
     Region          6..450
                     /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 mwnieefvga agiaveelaa yvdesqrgav pvlarrppge larllglrew iaeggmtpda
       61 freflrcflr egtrlhhpay lahqtaspdf paaladlvhg atnnpmaiye mgaaaataef
      121 evlrwmlgkv gfpegggvlt hggslanltv mlaararavp dawdegvpgd lvvlappsah
      181 ysvsravsil glgqraivpl atdelgrida grlpdvsgkr vmalvagaca tgtglhddlr
      241 tigqwcrerd iwfhvdaahg asallspehs glldgielad sviwdahkml rtsalaaavl
      301 vrregdldaa fqqeasylfy gdqgfdlinr tvectkaelg lkiflnlawr gerglgdyva
      361 aqygtahrfw elgrdrpgfv fpyepesniv cfrygtgdqa llrerlmdsg rfhltsaelg
      421 gvrhlritvm apatddktle alldavaehg spggsmea
//
LOCUS       WP_181615983             280 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181615983
VERSION     WP_181615983.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..280
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..280
                     /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=29577
     Region          3..278
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mipaqfdyvr ptsvqeasqa lagdddakvi aggqsllpll rlrltyptll vdvgrlselq
       61 gvhdrgdhvf igaavthdev vrsgvirdac plvalaaatv adpavrhrgt fggslahadp
      121 agdlpavala ldailvtser eipaseffvd ylesamhpge ilvgikvpkl gpgwgfhyek
      181 fhrtaqawai vgvaaavrrs ngsiaearig ltnmgsvpvr aretearlrd ldlgeavrqa
      241 cahaaedtsp psdlhaqady rrhlaqvlth ravraaagsp
//
LOCUS       WP_181615996             400 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Nonomuraea soli].
ACCESSION   WP_181615996
VERSION     WP_181615996.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..400
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..400
                     /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=42201
     Region          5..>66
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          45..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(63,65,226,246,318)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 msrllivnah plepvagqlg drswievagg rivdtgtgap psgehrvida agrtvlpgli
       61 dahvhlvant ldtreaatwt pgyaavrslr aaeqmlrrgf ttvrdvggad ygmaqalaeg
      121 lvpgprlihg gkalsqtggh gdlrprseeg rpcchtpgfa riadgveevr laardelrkg
      181 aahlkltvsg gvasphdevs avqytleeir aaveeagnag ryvtvhayha rainraleag
      241 vrcvehgnll ddttlkllve rdaflvptlv tyeqlalrgr elglgeesyr kiaevrdagl
      301 aalerahrag vnvvfgsdll gpmreaqlqe fdlrarvqpa aavvlsatat aarllgmegq
      361 igtlavgaha dllvvdgdpl sdlsvltrpk ayvikagqvv
//
LOCUS       WP_181616125             524 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nonomuraea soli].
ACCESSION   WP_181616125
VERSION     WP_181616125.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..524
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..524
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=55530
     Region          263..506
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 matttlgnll aalrpelvql gigdahlava gvelldtgal epaaprclll apgldlsssa
       61 avdqalrhaa etggalavkc adglpaavme rareagttvv rvnpdiawsr lyglvstlla
      121 tqptttgepa atlgggdlfs lansvaaicg gavaimdtdq tivaysnlad qpidetrrlg
      181 ilsrqvpsha lphhlteelw rsdsvrlirr dgyhprlavv iragdtalgs lwavfpdeda
      241 itdceavlaa aaklaalhll tirrrldadq esrnavlqta lqhpghadha lplpgsllcl
      301 aeaadaghra drrasllrti glleldarsl ghepalsmik drlyvlvpta prgavtvatl
      361 aahfhqraar llhtdlllvr sepvedpdgl rqarddldra ishlreaaap pggyaardlh
      421 aeivqqrlfh avrtdpalqa gfgrviaahd lahgtayrat llsylrnfgd vrtasaeltl
      481 hentvrkrir raqelfgivl dnpthrllle lelgagasst aada
//
LOCUS       WP_181616209             205 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF47 domain-containing protein [Nonomuraea soli].
ACCESSION   WP_181616209
VERSION     WP_181616209.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..205
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=23437
     Region          5..205
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mrlrltpred syydlfadsa nnlvtasrll veiisdgsdr eglaekmrac ehtgdertha
       61 imnrlnesfi tpfdrediyr lasnlddvmd ameaasdliv lyqidhlpkd vvrqvevler
      121 aaeltaeamp rlrsmknlne ywievnrlen qadqvyrrll aklfsgeyda ltvmkmkevi
      181 dqleaaadhf ehvantiesi avkes
//
LOCUS       WP_181615440             213 aa            linear   BCT 28-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Nonomuraea soli].
ACCESSION   WP_181615440
VERSION     WP_181615440.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 213)
  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 213)
  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 213)
  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..213
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..213
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=22249
     Region          8..213
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mtvpagairf agehgllvet gslaqshrid allrserppg vveivpgpet vlvvapgadm
       61 prlrghlgal laattapitg ehdvsppaep ivipviydge dlesvaeaag ltpdevvtrh
      121 tssdlvvgwl gfapgfaylt gldpalhlpr lttprtsvpa gsvavagpys avypsaspgg
      181 wrllgrtger iwdvradpps rfrpgmrvrf era
//
LOCUS       WP_181616323             119 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nonomuraea soli].
ACCESSION   WP_181616323
VERSION     WP_181616323.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=12433
     Region          5..105
                     /region_name="ArsR_Rv2640c_fam"
                     /note="Rv2640c family ArsR-like transcriptional regulator;
                     NF041413"
                     /db_xref="CDD:469304"
ORIGIN      
        1 msleccapia replsesdaa elaallkava dpvrlrllsi igshaggeac vcdltgsfdl
       61 taptishhlk ilrtaglidg errgtwvyyr iipetvnklg alfapmaepa radlglapa
//
LOCUS       WP_181616403             394 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nonomuraea soli].
ACCESSION   WP_181616403
VERSION     WP_181616403.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..394
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..394
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43074
     Region          138..387
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mfeyfpgnyv wnlsvnlals tgaaigevde acrplrtgep sdvtperffe twtalaarls
       61 alarsdaaag rrlsaaaryr rasvyfltae rmqhhgygpr adayasgldc frqaitlgee
      121 ncefvevpys dehgdrslpg llvrartsge drnpyvvlfn gldstkemvy gtglaqelar
      181 rgvssliidq pgsgealrlr gmtgyaeser ygsacvdyle srtdcdpari gvaawslggy
      241 yapraaafep rfslcvawga iydweelscr rlaaadsras epsvphfveh ilwvfgstsv
      301 eefaafaptm slaevsdrir vpflvvhgag drqipvemar lqydavvnsp rrelkvmteq
      361 dggvehvgad nmspttnyia dwiadvfavn aasc
//
LOCUS       WP_181616200             312 aa            linear   BCT 28-DEC-2024
DEFINITION  ribose-phosphate diphosphokinase [Nonomuraea soli].
ACCESSION   WP_181616200
VERSION     WP_181616200.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     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=33194
     Region          1..310
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mrditvfsgs ahpelaeeic aqlgtplhpv rvsrfandcl evqlqancre rdvfliqplv
       61 ppvqehlvel llmldaakga saarttvvmp hyayarsdkk daprisiggr lvadllvtag
      121 asrvltmtlh spqvhgffsv pvdnlhalne laahfqkadl antvvvspdl gnakeaaafa
      181 rmlgvevavg akqrfsddrv vissvigdva gkdvivldde iakgstviel larlrergar
      241 nvriacthgv fasgaverls aepnvveivc tntvpvpkps dnltvlsiap alaeamrrih
      301 dgqsvsalfs ts
//
LOCUS       WP_181616512             350 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nonomuraea soli].
ACCESSION   WP_181616512
VERSION     WP_181616512.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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 350)
  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 350)
  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 350)
  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 350)
  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..350
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..350
                     /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=36307
     Region          52..346
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mtprrslrar lalayaagiy aagvlvvvlv dvplvsidat apdgspapgs eagialpqll
       61 lgsavallvl ipvalalgwy vagrflrplr aitataqvis agdlhrrldl gepadeltel
      121 grtlddlfar lqasfdaqrh fvanashelr tplagmrtll evtladpdad aatlraacee
      181 alslgehqer lvqslltlat sergvarwes vdlalvagev lasgraagrd ltadlepalt
      241 agdprlvesl ianlvdnavr hnhdgghvrv ltrtsgtrav ltvvnsgpli agdqiqrlfq
      301 pfqklapgph gsglglaivh avaqahhagl sacprpeggl sitvtftasg
//
LOCUS       WP_181616551             131 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            soli].
ACCESSION   WP_181616551
VERSION     WP_181616551.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..131
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14453
     Region          22..121
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mptmsaadrr evlrreynan laecpgheil atlsdkwvtl vlsaladgpl rhseiariva
       61 gatqkmltqt lrklerdglv qravtasvpp rvdyeltelg fgllpiqrai kawaeshiae
      121 vhaararydk e
//
LOCUS       WP_181616027             354 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Nonomuraea soli].
ACCESSION   WP_181616027
VERSION     WP_181616027.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 354)
  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..354
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..354
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37509
     Region          1..353
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mippaapvig eaeieaavrv lrsgnvvqgp evaafeaefs qwvdgrhcva vnsgtsalql
       61 slmalgigpp devivpafsf aatanvvrlv gatpvfadid pltyclspda vaaaitprtv
      121 aivpvhlygh paamhelrti aaghglavve dacqahgatl hgrpvgafgv ascfsfyptk
      181 nmhaleggmi ctpdpdlart lrllrnqgme qryaneivga nlrmtdveaa vgrvqlgrlg
      241 egnarrqana ktldalisrv atpyvadgag hvyhqytvri dgdreaarah laarrvgsav
      301 yyptpihrlr pfagprrwdl peteraaaev lslpvhpslt eselarisea vnel
//
LOCUS       WP_181616587             108 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nonomuraea
            soli].
ACCESSION   WP_181616587
VERSION     WP_181616587.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
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="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..108
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11863
     Region          5..100
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrpgayhcgi daamdviggk wkvlilwale drphrfgelr revgatekvl aaqlrelevd
       61 givhrrvfde vpphveyslt elgvslneal aplgewgrrn vlavkaag
//
LOCUS       WP_181616092             593 aa            linear   BCT 28-DEC-2024
DEFINITION  terminase large subunit [Nonomuraea soli].
ACCESSION   WP_181616092
VERSION     WP_181616092.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 593)
  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 593)
  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 593)
  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..593
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..593
                     /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=64638
     Region          63..561
                     /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 maggkpastk trgrgylpsp aelkrlklsp evawylidrg iplpdcpprw ktpeagellk
       61 tarfdpervd rvlkafsllr htkgkwagkp ltpdpwqiay viapvfgwik knragtwvrv
      121 vrdlyvdvpr kngkstlcgg lgiymtaadg eggaeviaaa ttkdqagyvf gpikqlcehs
      181 palkpyvkal agkiihkask stfsvvssva eslhggniha giidelhvhk tgdlveaiet
      241 gtgsreqpli viittaddgr pntiyarkra rieelarrvi rhpstygvvw aadpkddpfa
      301 patwkkanpg fgvsptyeyl ekvaaeakqd pavlgsflrl hlglrtkqat ryitledwdr
      361 sagivderal rgrpchggld lsnvedital awlfpgdegs yqavwrfwlp edrlrvlskr
      421 tagaaelwvr egwlkltpgn vidndailrq idkdarafrv qtigydrwga tdvvrrlddg
      481 gmtcvaigqg vaslndplkn tlrliksell rhggnpimrw midnlatvan pdglvkpdka
      541 nsgdkidgvs allnamkecm daeaaaappa tapaaqaagg erdlwrptsr lgi
//
LOCUS       WP_181616640             483 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Nonomuraea soli].
ACCESSION   WP_181616640
VERSION     WP_181616640.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 483)
  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..483
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..483
                     /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=52389
     Region          239..456
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mssivrgrvs tllhkrwglp tvylvvcgls ltlptflpnf tlgilvvtlf aafamvmrwn
       61 eqtvlgllla agfliptsls iealgqvgip smliglllll lwlygrctpe lgldsgpqpv
      121 rymalyimia lfasyiagql rgmssleasg adatmifvas slgmllftad tikdmtgvrr
      181 llgwlvglgv vlsvtgmlqn fqvidiyrdl ripgmkyfdp igleslareg ylrvqglagh
      241 piefsvvlgm llpialhfal hspreqrlrw waavavigag lpmalsrsgi laagvslviy
      301 llatrvrvla tlvpvglvgv lgmslvfpgl lgsirnlflf gyiandtsis srtddyaial
      361 klwadypvfg tgpgtyipkl yrildngyly ylitqgvfgl lglvglfacg yflvrriewt
      421 tkdphmrdla qalagsiaga alvtatfdsf gfnimfvtth flvgiagvmw rvairdrdkv
      481 pvq
//
LOCUS       WP_181616726             367 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Enterobacter sp.
            RHBSTW-00593].
ACCESSION   WP_181616726
VERSION     WP_181616726.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00593
  ORGANISM  Enterobacter sp. RHBSTW-00593
            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 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Enterobacter sp. RHBSTW-00593"
                     /db_xref="taxon:2742656"
     Protein         1..367
                     /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=40006
     Region          5..303
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mkgnviiiga gvsglyagtl lekagvdyli learkrtggr vlsgqvlant pdgvhvdmga
       61 twfwpeiqpd fahlvhqlgl tplpqgrpgd mlyerqttsp aqrypayvts pesfrlqggm
      121 qaltsaltrq ipaqkiksdh qvvsisrlge gmqvatqsea gegslftgeh vflalppala
      181 akmtfepalp ervlshwrkt ptwmaphaky valyqtdflq aqhlsgdvss rvgpmveihd
      241 vsepdtgkta ifgfigvpak srwtvseael krlcreqlvr lfgedaaepe aewikdwaad
      301 pftttefdlq qdvghaqpqq vpaqeewadk ltgiasewsp qfsgylagai daaaegvghw
      361 lrhvarp
//
LOCUS       WP_181616880             428 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter sp.
            RHBSTW-00593].
ACCESSION   WP_181616880
VERSION     WP_181616880.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00593
  ORGANISM  Enterobacter sp. RHBSTW-00593
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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 428)
  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..428
                     /organism="Enterobacter sp. RHBSTW-00593"
                     /db_xref="taxon:2742656"
     Protein         1..428
                     /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=48356
     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 tdgegmvllv hpngskywrl ryrfggkekm lalgkypevs
       61 ladararrde arkllangvd psenkkavkv eqeqeaitfe vvardwhasn qkwsashsar
      121 vlkslednlf aiigkrniae lktrdllvpi kavessgrle vaarlqqrtt aimrfavqsg
      181 lidynpaqei agavatakrq hraalelnri pellhridhy sgrpltrlav eltllvfirs
      241 selrfarwse vdfetamwti pgereplegv khsqrgskmk tphlvplsqq alailekiks
      301 mngnrdlifv gdhdprkpms entvnkalrv mgydtkteic ghgfrtmacs sliesglwsr
      361 daverqmshq erssvraayi hkaehlgerr lmlqwwadyl danrergvsp fdfskiesvn
      421 rqgdssal
//
LOCUS       WP_181616281             353 aa            linear   BCT 28-DEC-2024
DEFINITION  Leu/Phe/Val dehydrogenase [Nonomuraea soli].
ACCESSION   WP_181616281
VERSION     WP_181616281.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea soli
  ORGANISM  Nonomuraea soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 353)
  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 353)
  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 353)
  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 353)
  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..353
                     /organism="Nonomuraea soli"
                     /db_xref="taxon:1032476"
     Protein         1..353
                     /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=37444
     Region          7..124
                     /region_name="ELFV_dehydrog_N"
                     /note="Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
                     pfam02812"
                     /db_xref="CDD:460706"
     Region          141..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(175,177..179,198..199,203,234..235,256,258)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133444"
     Site            288
                     /site_type="active"
                     /note="Phe binding site [active]"
                     /db_xref="CDD:133444"
ORIGIN      
        1 mtevfgheqv vfcadrqsgl raiiaihnta lgpglggtrf ypyeseqaal advlnlsrgm
       61 ayknalagld lgggkaviig dpatdkseal lraygrfves lngryftacd vgtysedmdi
      121 varesrfvtg rtianggagd ssiltsfgvf qgmrasaqhi hgrstlhglr vgvegvgkvg
      181 hrlvdllied gasvvvcdvs eravdqvrqr hpqvevvasl aelvaeeidv fapcalggsl
      241 ddttvatlra rivcgaannq lahpgvekql eergilyapd yvvnsggviq vadeirgfnm
      301 erarakagqi ydttlkifai aaeegvppav aadrlaerrm sevgrlkgiw lgh
//
LOCUS       WP_181619996             336 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter sp.
            RHBSTW-00994].
ACCESSION   WP_181619996
VERSION     WP_181619996.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (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   2  (residues 1 to 336)
  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 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
REFERENCE   4  (residues 1 to 336)
  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..336
                     /organism="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..336
                     /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=38081
     Region          81..326
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          250..326
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 marnrtfsln igwqallkda glqpglvlrr aglpddvfsr pergltteey crfwlaleke
       61 andasfplrl vervsadifd pplfaalcss nmmqavqrla rykqliapme ldvlvdeagv
      121 lcvsprwlsa plvlplslqi aelafllrll rlatrepvna lsvvlpqhln eaqgrhcarf
      181 fgteiqlges ptirfsatdt lrpfltlneg mwrvfepelr rrlselneta tmaervravl
      241 felipgnaat iettaarlgm skrtlqrrle degenfralv nrcredlarh ylgntrlsgy
      301 eiafllgfed ptsfyrafqt wtgqtpetvr eilrft
//
LOCUS       WP_181620014             420 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter sp.
            RHBSTW-00994].
ACCESSION   WP_181620014
VERSION     WP_181620014.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     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=47964
     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 mslndskirn lkpsskpikl sdshglyllv npggsriwyl kyrfggkesr vslgayplis
       61 laearqqrda irkllaqnin paqqrmdeka aaspekcfkt valgwhktnk kwspdyaeri
      121 lasmnnhifp aighlpvttl ktqhftallr viedkgflev asrtrqqlcn imryavqqgl
      181 tennpaqhle gvtappvknh ypalplerlp elferigdyr qgrqltrlav vltlhlfirs
      241 selrfarwge idfrnkiwti patreaiekv rfsgrgakmr tphivplsrq aiailkqiqe
      301 isghlelvfp gdhnpykpms entvnralrl mgydtktdvc ghgframacs alveselwsr
      361 daverqmshq ernsvraayi hraehldart ammqwwsdyl dvsregyvap yiyarrhkaa
//
LOCUS       WP_181620158             328 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CobW family GTP-binding protein [Enterobacteriaceae].
ACCESSION   WP_181620158
VERSION     WP_181620158.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..328
                     /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=35849
     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 mtktnlitgf lgsgkttsil hllankdpae kwavlvnefg evgidgalls nsgamikeip
       61 ggcmccvngl pmqvglntll rqgkpdrlli eptglghpkq ildlltapvy epwidlratl
      121 clldprqlld ekalsnenfr dqlasadiiv ankadratte sreafdawwq hfgggrqriq
      181 ttqghienal ldlprlnqae lpasaahths hsvkqglaal slpehqrwrr slnngqgyea
      241 cgwifdadtc fdtigilewa rlapvdrvkg imrtpdglvr inrqgadffi etqniappds
      301 rielisavna dwnalqssll klrltsgg
//
LOCUS       WP_181620177              68 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Enterobacter sp.
            RHBSTW-00994].
ACCESSION   WP_181620177
VERSION     WP_181620177.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     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=7689
     Region          1..64
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mnqhnsrlir lpevlnrtgy gkawiyhlis kgcfpspvki gsravafies eveewiqlti
       61 ensrkhva
//
LOCUS       WP_181620375            1651 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Enterobacter sp.
            RHBSTW-00994].
ACCESSION   WP_181620375
VERSION     WP_181620375.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 1651)
  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 1651)
  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 1651)
  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 1651)
  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..1651
                     /organism="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..1651
                     /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=180257
     Region          46..1651
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkpfrlaais lallttftla gcdnsdekpq aassaastat teaktpakpn geqlaklaaq
       61 sqgksltlld asevqldgaa tlvltfsipl npdqdfaktv hvvdkksgkv dgawelapnl
      121 kelrlrhlep nrnlvvtver dlqalnkatf gidyekaltt rdveptvgfa srgsllpgkv
      181 veglpvmaln vnnvdvnfyr vkpeslaafv sqweyrnslt nwesdnllkm adlvytgrfd
      241 lnparntrek lllplndikp lqqsgvyiav mnqaghynys naatlftlsd iglsahryhn
      301 rldiftqgle ngaaqsgidv tllndkgqtl aqgvsdadgh vrletdkeaa lilarkegqt
      361 tlldlklpal dlaefdiaga pgyskqffmf gprdlyrpge tvilngllrd sdgkplpaqp
      421 vkldvlrpdg qvartvvvqs englyrftyp ldsgaqtgmw hvrantgdnq qrmwdfhved
      481 fmpermalnl sgqkmpvspe devkfdvvgy ylygapangn slqgqlflrp lreavsalpg
      541 fqfgdiaeen ltrsldevql tlndmgrgqi stesqwkeah splqvilqas llesggrpvt
      601 rraeqaiwpa qtlpgirpqf askavydyrt dttvnqpivd ensnasfdiv yadasgakka
      661 vsglqvrlir errdyfwnws esdgwqsqfd qkdlvegeqa ldltddetgk vsfpvewgsy
      721 rlevkapdet vssvrfwagy swqdnsdgag aarpdrvtlk mdkpayqpgd tinlhiaapa
      781 agkgyamies sdgplwwkei dvpangldla ipvdkawkrh dlylstlvvr pgdksksatp
      841 kravgllhlp mgdenrrlni aldnpqkmrp nqtlsvkvka svkdgavpqk vnvlvsavds
      901 gvlnitdyvt pdpwqaffgq krygadiydi ygqviegqgr kaalrfggdg delkrggkpp
      961 vnhvtiiaqq aqpveldang egtitlpigd fngelrlmaq awteadfgss eskvivaapv
     1021 itelntprfl asgdtsrltl dltnltdqpq tlsvaltasg klalagaqpq pvqlapgsrs
     1081 tmfipvrald gygdgeinaq vseltlpget fvpqqkswki gvrpaytaqt vnsgamlnpg
     1141 eswrapsqhl sgfspatlqg qlllsgkppl nlaryirelq aypygcleqt tsglfpslyt
     1201 naaqltalgi kgdtdekrra aidigisrll qmqredggfa lwdkngpeey wltayvtdfl
     1261 vrageqgysv pvdavnnann rllrylqdpg mmsirysddt qaskfavqay aalvlarqqk
     1321 aplgalreiw erhaqaasgl plmqmgmalk lmgdaprsqq aldlaiktpr ndsknwmady
     1381 gsqlrdnalm lslleeykll pdaqnmllnt lseqafsqrw lstqesnalf lagrslqtis
     1441 gawqattsis dtalgsdkaq vqnvngdqls alqitntgtt plwvrldstg ypeyapqpss
     1501 nvlqverhil atdgstksls slksgelvlv wlevrasqnv pdalvvdllp aglelenqnl
     1561 asssaslqds gsevqnllsq mqqadiqhme frddrfvaav pvnegqpvtl vylaravtpg
     1621 tyhvplpmve smyvpqwrat gaasgplivv p
//
LOCUS       WP_181620438             456 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Enterobacter
            sp. RHBSTW-00994].
ACCESSION   WP_181620438
VERSION     WP_181620438.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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 sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..456
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50706
     Region          9..394
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mttctsrvaw vnllrrlhfy vglfvgpfif faaltgtlyv atpqlegyvy rtalhtdtsg
       61 dalplseqia vaektvgtgl rlhavrpgla egettrvmfa dpmlgpsetr aifvdpvtlq
      121 vrgdmtvygt sgilplrqki dylhsslmlg dtgrlysela aswmwiaavg givlwfytrp
      181 krrlnnrfqn rrrvhitlgw lllggmllfs atgltwsqwa ggnvdklrae mnwltpqvnt
      241 tlhgtsentd ehsehrghhg gmmmpdmamd ltqfdnvlla arkagidaek leirpakman
      301 qawtvteier swptqvdava idphsmqild rtqfehfplm akltrwgvdf hmgilfglan
      361 qlvliafgia lcvliiwgyr mwwmrrpaqs vaspvqtlcq swlalplagr smtvvvcall
      421 glalpvmgas lallmlidwl rwraastvsl tessak
//
LOCUS       WP_181620102             488 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Enterobacter sp. RHBSTW-00994].
ACCESSION   WP_181620102
VERSION     WP_181620102.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     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=53789
     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 msdsnpilfs saqsieayqq aieqstqavm qwlkqpemyq gktvaqlrdr ikldfnpkgl
       61 gneaaierav efflkdslsv hhpqcvahlh cpslvvsqaa evlinatnqs mdswdqspsa
      121 tiieikliew lrtrvgyqag dagvftsggt qsnlmglmla rdaffarqgh svqqnglvgd
      181 lrkirvlcse nahfsvqknm almglgyqsv tlvktdefsr mdlndlaaki dqcnangeqi
      241 laivatagtt dagaidplre iaelaakqni wvhvdaawgg allmseqyrh yldgielvds
      301 itldfhkqff qtiscgafll kearhyelmr yqaaylnsef deeagvpnlv skslqttrrf
      361 dalklwmsle algqeqyaai idhgvtlaqq vaayvndqaa lelvmkpqla svlfrfrpqv
      421 rmddaniall nqkigdalle sgranvgvte hngitclklt llnptvtldd vktllslver
      481 tatevmak
//
LOCUS       WP_181620734             317 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter sp.
            RHBSTW-00994].
ACCESSION   WP_181620734
VERSION     WP_181620734.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 317)
  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 317)
  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..317
                     /organism="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..317
                     /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=37388
     Region          1..315
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnnafeqvld dyffskslrp atewsyrkvv rsfisfsgeg ispeqvdktl vltwrrkiih
       61 eeglsrttwn nkvthmraif nhaivnglvt mrenpfngvi trpdvkrkkt ltdvqmnkiy
      121 lhmqareede rvgmmelrks alrpawfwlt vldalrrtgm rqnqllhirl edvnfehrwi
      181 nlrpegsknh kehrvpiten lrprlerlyn lslergakmq dqlfnlsrfd grkneissnm
      241 dypplraffr rlsrecgftv sphrfrhtia tnlmrlpdrn lkmaqdllgh stpavtleyv
      301 esdldkvrdm leeldaa
//
LOCUS       WP_181621033             696 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Enterobacteriaceae].
ACCESSION   WP_181621033
VERSION     WP_181621033.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=75869
     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 vvlsfvvail aaytalnmaa rvagsqgvsa riwlagggva mgigvwamhf
       61 igmlamelsm smsyspgltl lsmaiaigss lfalwlvsce klrlrrllpg alvmgmgiva
      121 mhytgmaale ttpgivwdkt wvaisvlial aaslaalwlt frlrheaaqv almrlgaait
      181 mgiaiagmhy agmkaaqfpt atmmhhdgin gswlavlvsv valsilgitl lvsmldarlq
      241 artsllassl aeanrelaql alhdtltrlp nrilledrld qaiskadreg thfalmfmdl
      301 dgfktinday ghdvgdkllv avtqrllqpl kgqytlarig gdefvmlaei ggpddaasla
      361 nslvraidsp fnldpyelvv tlsigialyp hdgqndrelm fnadaamyht khmgrngyhf
      421 fqpsmntlaq thlqlmndlw laidrnelrl lyqpkfhapa gpilgfeall rwqhpkqgll
      481 tpdmflplae ktgliipign wvineacrql rewhiqghhd wsmavnlstl qfeqpslvks
      541 vldclarhnv ppemlilevt ettamsnpde svrvlteltd agvkasiddf gtgyssllyl
      601 krlpacelki drafvkelsg esddativsa ivalaktlnl kvvaegvete aqqefltelg
      661 cntlqgyllg kpvtaqtvee lclrgeipay khdmpl
//
LOCUS       WP_181621238             140 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Enterobacteriaceae].
ACCESSION   WP_181621238
VERSION     WP_181621238.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 140)
  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..140
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..140
                     /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=16434
     Region          3..132
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mltdprftte veltvpfhdv dmmgvvwhgn yfryfeiare allnqfdygy rqmkasgyvw
       61 pvvdtrvkyr davtfeqrir vrahieefen rlriayqifd aktgkrtttg ytiqvaveet
      121 sremcfvspa ilfermgvtp
//
LOCUS       WP_181621458             282 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterobacteriaceae].
ACCESSION   WP_181621458
VERSION     WP_181621458.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=31704
     Region          <93..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 mqqdisqilt dlingalplh qvyfanaatp apelalqvdf prleivlegv vedsassalq
       61 kndvlyvpag gwnhpqwknp attlsilfgk qqlgfsllhw dgvafrnlak qhvarrgpri
      121 gsfllqtlhe mqmqpheqqt arlivaslis hcidllgsqi qtasrsqalf eairvyideh
      181 yaapltresv aqafyispny lshlfqktga vgfneyltht rleharqllk gydlkvkeva
      241 hacgfvdsny fcrlfrknte rspseyrrqy hsqltgkpat pq
//
LOCUS       WP_181621915             158 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Enterobacter sp. RHBSTW-00994].
ACCESSION   WP_181621915
VERSION     WP_181621915.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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 158)
  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 158)
  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..158
                     /organism="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..158
                     /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=17883
     Region          76..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 miifrsmhed eypgyleyfi pdyaheiasn yrlsdkdsla rarqeiaedl pegvntpgqi
       61 llclisrsnn adrhvgylwy kpdtakrivf iydfhifnsc qgkglgkqal lafeqelrvk
      121 gfeqirlrva gdntcaqhvy eatgfgvtgv nmsktitd
//
LOCUS       WP_181621924             419 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Enterobacter sp.
            RHBSTW-00994].
ACCESSION   WP_181621924
VERSION     WP_181621924.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     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=47420
     Region          2..405
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mpltdtairn akpldkpwkl sdaqglylli kpngsklwql kyrfggkekk lafgpyptvt
       61 lanarklree aravlsagdd pgvkkqqekq akksgnsfee varqwlagni rwtehhaaki
      121 lrslelhvfp ligkipvadl ktadlliplr vaekkgnlet aariqqrtta imryavqesl
      181 iasnpandlt gaiapppknh ypalplekmp ellehlesys grlltrlavq lnllifirss
      241 elrfarwtei dldgamwtip aqrepipgvr ysergakmkt phlvplskqa vtvlkqlkll
      301 sgssellfpg dhdprkpmse ntinkalrvm dydtkvdicg hgfrtmacsa liesgrwskd
      361 averqmshqe rnnvraayih kaehldertq mmqwwsdyld acrqkfvapy rydrqvqva
//
LOCUS       WP_181621936             199 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterobacteriaceae].
ACCESSION   WP_181621936
VERSION     WP_181621936.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 199)
  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 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   3  (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   4  (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 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..199
                     /product="helix-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=22520
     Region          14..188
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          137..187
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mfkillidrc hftragfeaw lnhsglfpgh fvvtglnnlf larehilqwk ptlviadlhs
       61 fkqdihhfqq lsslliaset lpfillqsge eqemggylaq fpvwssllkn vdleklatvi
      121 ndaltscssv eipqiaapll trqeekvltl wmdgasnqki ashlsingkt vytykrnirm
      181 klhmdtrfsp flslqeses
//
LOCUS       WP_181622187             357 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease
            [Enterobacteriaceae].
ACCESSION   WP_181622187
VERSION     WP_181622187.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=37669
     Region          47..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 mnsslaaseq sgettiashy rkilirrfil agilllcivc slildftlgp sgisvstlwh
       61 tlvnaagada gtrvivwdlr lpfalmavav gmalglagae mqtilnnpla spftlgvssa
      121 asfgaalaiv lglgipgiad kwfipanafv fallacfild gisrwtrvat sgvvlfgial
      181 vftfnalisi lqfvasedtl qglvfwtmgs laraswdkla ilavalviiv plslknawkl
      241 talrlgedra vsfginvkkl rlttllrisi isaltvafvg pvgfiglvap hisrmmfged
      301 hrfylpgsml igalvlslas vfsknivpgv iipvgivtsl vgvpfflsii irnrgni
//
LOCUS       WP_181622389             235 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Enterobacter sp. RHBSTW-00994].
ACCESSION   WP_181622389
VERSION     WP_181622389.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            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..235
                     /organism="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..235
                     /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=26603
     Region          16..144
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mktpytdnyd haflrdtmmg pnamrlteel vaslpitpgm rildlgcgkg issvllaeky
       61 datvfaadlw isptenaerf aalgldrqif plrvdatkpi pfahnyfdli isvdayqyfg
      121 snntmlatll pflktggyva vavpgfigey dehnlpdvvk pfwtpewyfy plrwwkacwe
      181 kepgitlntv remdtcqqaw ddfmecdmaq eimvsmmeag vgdyfnmiql tgikn
//
LOCUS       WP_181621602             248 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 4'-phosphopantetheinyl transferase family protein
            [Enterobacteriaceae].
ACCESSION   WP_181621602
VERSION     WP_181621602.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=27236
     Region          1..157
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mathfargil teghlepvrv spachdeark lpeyrrtrfl asrallaell fmlygtselp
       61 dmitqpegrp vfadpelphf siaytgnivg valttegdcg ldmelqratr gfhgstahda
      121 yplssneklw vrnqndpnea raqlitlrqs irklsgcaad dasllqllpg sgrlrasqaa
      181 lvealsdaed vliwsiavtp aierlkiwef dshrgwhslp dvparanepa arlmrltslp
      241 aekaltln
//
LOCUS       WP_181622551             524 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Enterobacter sp. RHBSTW-00994].
ACCESSION   WP_181622551
VERSION     WP_181622551.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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 sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     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=56222
     Region          14..520
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 msglsltlgk nslrqparrr palpmvalav lfsllallpl gfiiatgiet gwetikalvf
       61 rprvaellsn tlwlaalavp gciilgvaia wlterttlag rrvwsalava plaipafvqs
      121 yawvsavpsm hglssgifls vlayypfism pvaavlrrld ptledvaasl gtppwhvffr
      181 vvlpqlklai cggallvalh llaeyglfvm irfdtfttai ydqfqstfsg paanmlagvl
      241 alcclailll egatrgkary arigagaare qkrwplsrtm avlgqllfiv livlalgvpl
      301 gvlcrwiwlg giqnwmsadl wfslrqtlml glggaglttv cvipiawlgi ryphrlfrml
      361 egciyitssl pgivtalalv tvtihyarpi yqtevtlfla yllmfmpral inlragiaqa
      421 pvelenvars lgsspakalw svtmrlaapg aaagaalvfl gvsneltatl llsplgtrtl
      481 stgfwaltse idyvaaapya mlmilislpl tgilymqskk iagl
//
LOCUS       WP_181622835             490 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Enterobacter sp. RHBSTW-00994].
ACCESSION   WP_181622835
VERSION     WP_181622835.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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..490
                     /organism="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..490
                     /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=54515
     Region          258..490
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mmrrfslsqr ltllfilllm lcatvacvvq mytsmqygna mvqrlsggla qqivqrepil
       61 daqgqvdrsa lkplldrlmt fnpsvelyvi spdgellada appghiqrqk iditplqtfl
      121 sgaampvygd dprsagkqkv fsvtplrqdg elkgylyiil qgeesnalad mawhkalwst
      181 alwslllval fgllagllvw ywvtrpvkrl tadvtgleqd sisaikhlaa qttdltsgde
      241 vtllrntfie larkiavqwd qladsdrqrr efiatishdl rtpltsllgy letlslksat
      301 ltpqehqqyl atalrqgqkv rhlsqqlfel arleyggikp qrerfamgel isdvaqkfel
      361 tartrevnlh idlpgplplv nadvsmierv vtnlldnamr htptggeirl avwqeneqlq
      421 vevadngsgv daslrdelfq rpsalnsqas renrgglgll ivkrmlelhg ggirlmdsvs
      481 garfrffvpl
//
LOCUS       WP_181622181             476 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Enterobacter sp.
            RHBSTW-00994].
ACCESSION   WP_181622181
VERSION     WP_181622181.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     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=51087
     Region          1..448
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mpdflsfine ilwgsimiyl llgagiwftl rsgfiqfryi rqfskslkns vspqpgglts
       61 fqalctslaa rvgsgnlagv alaisaggpg avfwmwvtai igmatsfaec slaqlykeqd
      121 kngqfrggpa wymsrglgmr wmgilfslfl llayglifnt vqansvahal ryafscpewl
      181 tgavlaaftl ltmttgikgv arlmqwmvpa mallwvaagl fvtvihidql pdviatifqs
      241 afgwreaasg algytisqal tagfqrgmfs neagmgstpn aaaaaaswpp hpaaqgivqm
      301 igvftdtivi csasamivll agplphasgt agiqlvqqal vnlaggwgag fvslivilfa
      361 fssivanyiy aennliflrl dsrrtqwvlr lgvilmvmag sllslplvwq ladvimalma
      421 itnltailll spvvtliard ylrqrklgvq pvfdasrype iesqiapgaw ddlprq
//
LOCUS       WP_181623234             330 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease
            [Enterobacteriaceae].
ACCESSION   WP_181623234
VERSION     WP_181623234.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=35022
     Region          25..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 mtrritlslw gltatlllmt llatgfgalr lpvsllwnns dealrqiwfi irlprvllal
       61 viggslalag cvmqglfrnp ladpgllgis sgaalavalw vvipftlpal mmlyapmlaa
      121 ffgalaatvv ifflsqqqds slsrlllvgi ainalcgaav gvlswvsnda qlrqlslwgm
      181 gslgqaqwst llavtslmvp tvwiiwrlaa tlnllqlgee eahylgvdvr vvqrilllcs
      241 allvaaavav sgvigfvglv vphlmrmwlg adhravipgs vlagaflllv adtvartlva
      301 paempvgllt sllgapwflw lifrrggqhg
//
LOCUS       WP_181623065             194 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Maf family protein [Enterobacteriaceae].
ACCESSION   WP_181623065
VERSION     WP_181623065.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=21422
     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 pyrrmllekl gipfecaapt vdetpqpges prhlvtrlaq ekaqslaary
       61 pahliigsdq vcvlegeitg kphteenacr qlmsargniv tfytglalyn sasghlqtec
      121 epfdvhfrhl seqeiidyvr rerplncags fkseglgial fekldgrdpn tlvglplial
      181 cqmlrrehfn plta
//
LOCUS       WP_181623530             498 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Enterobacter sp. RHBSTW-00994].
ACCESSION   WP_181623530
VERSION     WP_181623530.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 498)
  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 498)
  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 498)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..498
                     /organism="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..498
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55035
     Region          114..348
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 manlpwrvsv rlvlltkkiv lvlgivlvvl lavriylsqq gpelhlwhtw tademsvrei
       61 dkasfaqyla reskifadlq trvtnktagd drtplnryyr gslvwpgrft pdtnrsfvlm
      121 pegtprgavv llhgltdspy smkhlavdyq rrgfvtvvpr lpghgtapga ltrvdwemwl
      181 avtrlavrea trlagndvpl hlvgysngga lamkytldtl etpalrkpqq lvllspmigv
      241 ttfarfagla glpamlpafa kaawlnitpe ynpykynsfp vnaarqswll tqvlqqqlsr
      301 darnntltgl ppvlafqsvm dstvstravv eslfnqlpen gselvmfdin qaasfrplfk
      361 psswtavsel lptavrrytv tiitnasant fntvakttla gskqetvssl dtrypqeiys
      421 lshvavpfpp eddlygshpa vknrygvslg tvslrgetsv livskdalmr vtsnpfyddm
      481 lsmihqhngt islnrkap
//
LOCUS       WP_181623550             169 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RrF2 family transcriptional regulator
            [Enterobacteriaceae].
ACCESSION   WP_181623550
VERSION     WP_181623550.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=18853
     Region          5..151
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mafyssgvey gihslmcmvd akgneremsv remaalqgvp ydylgkiftr lsraglvtst
       61 egkgggfkla rpaelisvld vahaidgekn mfecrevrqr lavfdetppg wvcdgpcgvr
      121 svmdsaqqrm eeelarhtil dlarkmyrka pdtfqievqe wisdrrnas
//
LOCUS       WP_181622970             413 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Enterobacter sp. RHBSTW-00994].
ACCESSION   WP_181622970
VERSION     WP_181622970.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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..413
                     /organism="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..413
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45564
     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 mdiaqfpqln ppprllmgpg pinadpralr amssqligqy dpamthymne vmalyrgvfr
       61 tdnrwtmlvd gtsragieai lisairpgdk vlvpvfgrfg hllceiarrc raevhtievp
      121 wgevftpdqv edaikrvrpr mlltvqgdts ttmlqplael gaicrrydvl fytdataslg
      181 gnaletdawa ldavsagmqk clggpsgtsp itlsarmeea irrrkcveeg irtdahhdgv
      241 demvysnyfd lgmvmdywgp erlnhhteat talfgareca rlilqegldn giarhklhgd
      301 allkgiqsmg letfgdlkhk mnnvlgvvip qgvngdqvrk lmledfgiei gtsfgplhgk
      361 vwrigtmgyn arkdcvmttl salesvlnyl rftttqgaam qaawdhyrse tal
//
LOCUS       WP_181623586             551 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Enterobacteriaceae].
ACCESSION   WP_181623586
VERSION     WP_181623586.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=57517
     Region          38..527
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mnqrilsmmt lallvilval plsfivfqav fpqfsagslq gafsgvtvll aepqlpamlg
       61 gtlqialgva lvsaligfpl gvarglfalp lprmwdllfl ipfltppyis alswmlvlqt
      121 ngylqqltgl nlndllfskt givlvmalni fpviyfavsr sllasgqrla lvarvhgasa
      181 grafwhitlp mlspslaagm llaftlaiee fgvpaalgtr agvvmlttdi ekkladwpvd
      241 lsgasmlsvv lvvialcawg vqkkltgqhd vtsitgkpte ntgahagvya lpmviimgsv
      301 giiavilpgl smalsgvlgt lsggvtlsnv tmshyvalfs qqgdalaalg tslslalgaa
      361 cltgglglla swlvvvqkik grgaldalsl mpaalpgivv gvglillwnr pglpvspynt
      421 wvilllsycc lllpwpvryv ssalrqlggn lepaarvhga safqalrfiv mplvspalla
      481 amlmvfaias relvtsllla pagtqtvsvf iwrqfeqgsv gqgmamatlt lltglvlmls
      541 algimqrsar g
//
LOCUS       WP_181622559             729 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Enterobacter sp. RHBSTW-00994].
ACCESSION   WP_181622559
VERSION     WP_181622559.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     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=79036
     Region          69..729
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkytgkmnkt llalaigtvm hsafaadakk edtivvqsas tgdfkaggdq lvpafldgqv
       61 anggrmgmlg qqnamdvpfn iisytsklve dqqaktiadv vandagvqyv qgygnsaesf
      121 rirglkfdgd dmtfgglsgv lprqvvdaqm vdrieifkga nslmngaass gvggminlep
      181 khagetpqak vgvdytsdsq igttldagrr fgdsdqfgar vnlvhreget piandrrrtt
      241 llstgldykv dnfrtsldvg yqkktfhgsp tsvnvsavdf iptppkndrn fsqkwaysni
      301 enefgmwrse yditdnwtay tglgaqhahe eglysapkll dksgkattsr ldtnrlsdtv
      361 sgmagirgnf ntgfvshkvn vgysaqtkne kiawkmskaa dnpytniyhn tgvdapdstn
      421 sngkggkysd pltsgrtrtq gwllsdtlgv fddkllftag arhqkvvvrg ydkitgaend
      481 adgfdgsrwm ptygvvykpw etlslyanht ealqpgktap ntatnygqst givhsrqnev
      541 gvkadfgrvg gslalfeikm psaildsetr hygldaeqrn rgvelnifge pmlgmrlnas
      601 atwlqaeltk tnnglnqgnd aigvpnfyav lgaeydikpi dgltatarvn hsgsqyadla
      661 ntkkldsytt ldlgmryhfa vnqsqnqmtv ragidnvtne nywasvddsg tyltqgeprt
      721 fkvsvgyef
//
LOCUS       WP_181623630             191 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Enterobacteriaceae].
ACCESSION   WP_181623630
VERSION     WP_181623630.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 191)
  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 191)
  AUTHORS   Rosinski,J.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..191
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..191
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21286
     Region          6..75
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          91..184
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mntitdnmnq risaririer esrgwslsel adragvsram ihkiergdss ptatllarls
       61 gafgismsml iaraemqegk llrqanqpvw rdpqthylrr hvsprtdlpi dlvqvelpag
      121 sdvpmpassy alarqliwlq sgelvfqege trhemkagdc lelgppndcr finetdetcv
      181 ylvvrlnqsg s
//
LOCUS       WP_181624027             249 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Citrobacter
            freundii].
ACCESSION   WP_181624027
VERSION     WP_181624027.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            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 freundii"
                     /db_xref="taxon:546"
     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=27383
     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 htlstvasai
       61 eifgllacys apeplfledg slnprlptll eeaqalqalw lkvslghfsh teqfnvlrew
      121 ldnsgmelvv endqtacgrl kpmqrfneac qtqnlpislt fdmgnwlwvg dspeqaaqkl
      181 astvgyihvk aavahrdsyr avppdaadpr wltllktlpg dvprgiefpl egqdlaavtr
      241 ryvellree
//
LOCUS       WP_181623999             415 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_181623999
VERSION     WP_181623999.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii 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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=48091
     Region          36..342
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 meknyrvttf vmdsgerycm vvdratglpm yyptlflttq irnrgnafst tlaaannlvl
       61 llrfldsrgi nleqrlltkd ffkphelddl rdfaqrkhgr mpskalsnpw lddeltnivd
      121 ngtqhsrltt sanylrwyam hilkmpeldv veqiktmaaq ikvrrpskks rnstlqdrsl
      181 ndvqldvlfe tikldsewnp fsidvqrrnr lmilllyhlg irsgellnir iqdidfssnr
      241 irivrrader adsrtnepna ktrerlipla eslaqelhsy itkdrrkiqn akkndylfvt
      301 ykrgptvgnp iskagyhkif slvkdvspql yvvtghslrh twnrkfserm damdepvsee
      361 rqeqiraylq gwkpgsgtaa tynkrfiqqk gfeaalalqk angtrlpedl kndne
//
LOCUS       WP_181624070             582 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Citrobacter
            freundii].
ACCESSION   WP_181624070
VERSION     WP_181624070.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 582)
  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 582)
  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..582
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..582
                     /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=64874
     Region          148..582
                     /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 misvlsniqd dicnyadais gitgtdveii deslmriagt gkyrhmlnen vakngyiyrh
       61 vlqvretvli knpgehplcq lcekhhycse mldlnapifl nnrvigvigi icstqaqrdt
      121 llsqidkfvt fieqiavmis skvfeclerl raqetlgafr rlidamdrgv vaidgkgliw
      181 hanhsadril nrevqglplt iettgdslyg deeawltleg qkhhvlckqi slssqdndrl
      241 tmvifrdahd ylsnltpspy esdiqvrlig hspsmeqlrs tigkiansya svlitgesgs
      301 gkevvafaih qssprkaapf vtincaaipe qlleselfgy vrgafsgadp kgrmgkfela
      361 nggslfldei gdmqlhlqak llrvlqekai trvgsnntin idvriiaatn kninamvenn
      421 qfredlfyrl nvvplvlpsl rerradiavl aqyfadefsv syqrppqklp ddvinrlyaw
      481 hwpgnirelr nvieyifvmr geaaginash lppylltaad grkttmtaqp rqlankgkqa
      541 ereaienviq rfgssvegkk qaatelgisi atlyrkikly gl
//
LOCUS       WP_181624251             389 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter sp. RHBSTW-00017].
ACCESSION   WP_181624251
VERSION     WP_181624251.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00017
  ORGANISM  Citrobacter sp. RHBSTW-00017
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHBSTW-00017"
                     /db_xref="taxon:2742629"
     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=44640
     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 inakpyngap evtdgdglsv ritptgtitf qhryrwngkp vrltigrypa
       61 mslkdarviv gemrelylkg lnpknyfake dgeltlkecl dqwwskyvet lkpntqtlyk
      121 svvyntmyte fpdapvvnip vsawvrffdk qekkngkkar vlllqlrsvm nwcisrqlia
      181 scevlklsvk nigkkpdvgs rvltytelak iwlalennki vtsnkvlhql lllwgarlse
      241 lrlatasefn mddliwttps ehskmgnvir rpvfdqvkpf verllnsgnd vlipgqeldk
      301 aidrssanly mkklrdkidi pewrthdfrr slvtnlsgeg vmphvtekml ghelggvmav
      361 ynkhdwlveq keayelyadk ifwhikqic
//
LOCUS       WP_181620781             411 aa            linear   BCT 28-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Enterobacter sp.
            RHBSTW-00994].
ACCESSION   WP_181620781
VERSION     WP_181620781.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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 411)
  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 411)
  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 411)
  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 411)
  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 411)
  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 411)
  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 411)
  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..411
                     /organism="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     Protein         1..411
                     /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=42816
     Region          3..408
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mltailaafv ggiilnfmpc vfpvislkal gilrhqgnst sartegggfl lgviftmmal
       61 aavllalrag gtavgwgfql qsplviaila liilgaalnl lgvfevgltl qrageidvgg
      121 rgaffrsalt galaivvatp csapfmagav gyalvqppia slgiflalal gfaapftlis
      181 lfpviaqrlp rpgawmdilk rglafpmfga fawlvwvlaq qagttalaam lacavvvsft
      241 awlygiaqrr rlighsykal lavtvvlfla aitplpgvmh tqsstqdspg vesitevkws
      301 pqtvaemrgh gkaifvnfta swcitcqvnd rtslstqavk qaisrtgtvy miadstkfna
      361 diddamnafg qgglplyvvy padgsapkvl pqvltpsivv nalnqasgkk a
//
LOCUS       WP_181625024             387 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Citrobacter].
ACCESSION   WP_181625024
VERSION     WP_181625024.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=44184
     Region          2..385
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mplndmqirr akpeakaytl gdglglslli epngskswrf ryrfagkpkm islgvyptit
       61 ladarsrrdd arklvaegkn psevrkeqki alqtesesaf ekiatewhqm ksakwsegya
      121 sdimeafqnd ifpyvgtrpv geikplelln vlrkiekrga lekmrkvrqr csevfryaia
      181 tgraefnpaa dlssalevhq snhfpflkad eipdflhald sytgsrlvqi atkllmitgv
      241 rtielraalw lefdldnaiw eipaermkmr rahlvplsiq aldllnelkt itgnyryvfp
      301 grndpnkpms easinqvikr igfagkvtgh gfrhtlstil heqgfesawi emqlahvdkn
      361 nirgtynhaq yldgrrvmmq wyselff
//
LOCUS       WP_181623733             342 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Enterobacter sp. RHBSTW-00994].
ACCESSION   WP_181623733
VERSION     WP_181623733.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter sp. RHBSTW-00994
  ORGANISM  Enterobacter sp. RHBSTW-00994
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
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="Enterobacter sp. RHBSTW-00994"
                     /db_xref="taxon:2742676"
     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=37778
     Region          80..338
                     /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 msdiilarvs etlateqsle slvrqlleml eivtdmesty ltkvdinarl qhilyarnsk
       61 qmqipeglsv pwgdtlckra idsssffsne vaerwadcda akalgittym sipihladgs
      121 lygtlcatst qkqelserge qvlrlfagli aqyiqkeslv aqlreanaal vahsytdalt
      181 glpnrraife hlatlfslak hlkrnaiiaf idlddfklin dlhgheagdq flievgkrlt
      241 qeqteddiig rlggdeflva clshnendge ksqisllktr isariageyc lgnvhifypg
      301 aslgvievdp tqtdadsalr aadvamyqdk kgknktrflt md
//
LOCUS       WP_181625369             108 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RrF2 family transcriptional regulator [Citrobacter
            freundii complex].
ACCESSION   WP_181625369
VERSION     WP_181625369.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii complex
  ORGANISM  Citrobacter freundii complex
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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   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..108
                     /organism="Citrobacter freundii complex"
                     /db_xref="taxon:1344959"
     Protein         1..108
                     /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=11415
     Region          7..>78
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mkrvvasvqv vailnriyng spvsiasisk esklsvsyle qifsklrsse ivtsqrgagg
       61 gyhlskanps vadvvravth tpdsfepvln alewvpvaql vqgksptp
//
LOCUS       WP_181625962             402 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Citrobacter].
ACCESSION   WP_181625962
VERSION     WP_181625962.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     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=43260
     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 mrnvtvlaac lftasvsaae sngeyiaris dcvachtteg gaamaggkkf ptpvgdiyst
       61 nitpdktqgi gnysyedfdk avrqgiakdg hplypampyp syaklsdddv qalyryfmhd
      121 vtpsaqpnke naipwllsar wplhiwnwlf tdapattver aktddnaalv krgaylvegp
      181 ghcgschtpr gmamnekayt nvdaeylsga midgwyapsl rgtgmseqel ksllltgksk
      241 haavsgsmae vvtqstqylt dddataiaqy llslksvkpe tvraaattvs wsnspeagkv
      301 tynrycstch glegkgtddn apslinnplv mvddptplfr viahgaetpt trgsvsfkmp
      361 ayggmlsdne mrdvinyvrk swgegngdvs qedlagikka sh
//
LOCUS       WP_181626133             530 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Citrobacter
            freundii].
ACCESSION   WP_181626133
VERSION     WP_181626133.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            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 freundii"
                     /db_xref="taxon:546"
     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=57942
     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 vaigqievgv neqvidatgk iifpgfidth
       61 thsdlsaiin palsakirqg ittellgqdg valaplpeey ipawrkniag ldgdtdkidw
      121 kykntdgyln llasrhpatn laylvphgnv rmeamgldgr pstredvakm cevlerelka
      181 gafglstgli ympcafgdta emielckvta kydgifvvhq rseaddiins tqelidiata
      241 tgvwlhishm kvcgkknwgl idqmlgmleq aqkegirisf 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 csgtvirkqy
//
LOCUS       WP_181626061             377 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Citrobacter freundii].
ACCESSION   WP_181626061
VERSION     WP_181626061.1
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 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..377
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=40373
     Region          4..363
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mtyqlhvgrc evvlksipdn svdsivtdpp yglsfqnhkw dydvpsveqw qeclrvlkpg
       61 ghllafggsr tyhrlvvnae dagfeirdqi lwiygsgfpk shnldgqwdg wgtalkpahe
      121 pilmarkpfk stvaenmvah gtgalninac riptgeqlsg gsgcllshqr dgtnptadfe
      181 qsvggrwpan iihdgsddvi acfpanagaa apvtgnepsa dstgqvlgmr qrvatvhhgd
      241 kgsaarffyc akvkpserde glerfivtsa sdmtggrkeg sagindprag agrtkgaknn
      301 hptvkpialm kylcklitqp ggtvldpwmg sgstgraaie egfnfvgidl dpdyvtiasa
      361 rlafslkkya nekaeal
//
LOCUS       WP_181626200             337 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Citrobacter
            freundii].
ACCESSION   WP_181626200
VERSION     WP_181626200.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 337)
  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 337)
  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 337)
  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 337)
  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 337)
  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..337
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..337
                     /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=37721
     Region          2..331
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkvlvtgats glgrnavefl cskgvsvrat grneamgkll ekmgaefvha dltelvssqa
       61 kamlagidtl whcssftspw gtqeafdlan vratrrlgew avawgvrnfi hisspslyfd
      121 yhhhrdiked frphrfanef arskaagedv iallaqanpq trftvlrpqs lfgphdkvfi
      181 prlahmmyhy gsillphggs alvdmtyyen avhamwlasq qacdklpsgr aynitngehr
      241 tlrsivqkli delnidcrir svpypmldmi arsmerlgnk sakepklthy gvsklnfdft
      301 ldttraqeel gyqpivtlda giertaawlr dhgklpr
//
LOCUS       WP_181626238             194 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Maf family protein [unclassified Citrobacter].
ACCESSION   WP_181626238
VERSION     WP_181626238.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     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=21611
     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 mpqlilasts pwrrallekl aipfecaape vdetplpgea prhlvlrlaq kkaqslahry
       61 pshliigsdq icvldgeitg kplteenarq qllkargniv tfytglalyn satghlqtev
      121 eqfdvhfrhl seteiedyvr kerplhcags fkseglgial ferlegrdpn tliglplial
      181 cqmlrredmn plka
//
LOCUS       WP_181626371             342 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Citrobacter].
ACCESSION   WP_181626371
VERSION     WP_181626371.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=38551
     Region          8..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktikgpgif laqfigdrpp fntlegvakw aaelgykalq ipcnhkslfd veqaaisqay
       61 cddirgmlag hglviselst hlegqlvavh payddafdgf aplsvranpq arqawaietl
      121 hqaaaasqrl gltahatfsg slawpffypw pphnrqrfee aflelarrwr pildrfdhhg
      181 vdvcfeihpg edlhdgvtfe rflalvnhhp rcnilydpsh lllqqmdylg fidvyhsrik
      241 afhvkdaeyh assrsgvygg yqpwldragr frslgdgqvd fktifskltq ydfpgwavle
      301 wecclkdaqt garegsdfir rhiipvssra fddfaagdev rk
//
LOCUS       WP_181626483             356 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [unclassified
            Citrobacter].
ACCESSION   WP_181626483
VERSION     WP_181626483.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..356
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41591
     Region          3..219
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mptplvsiiv tsynhsafle ealdsvfnqt wknteviivd dastdrsvdi ikkyqqkyhc
       61 ktilretnyy sqkdktgdkp iieamnmaag kyiavvdsdd livptkishq vnvleknphc
      121 vmcystiqvi mpdgsrfpys dlfldgdvfh hllvsgnlsl yigslirrea ylkiersdph
      181 lvqedwdmfl klsrqghfis trrlvayyrr hdnntwyrrd nsklmyrnrm milnqwkhed
      241 awveamnsrw kqyahpdhtl akqdiddlli esptdpllhf qgfiaaiynk evnkaqyhim
      301 qaiiycdvrl eilpqlyfaa lksiadskik stlltslktr lpehyqqise qftqdf
//
LOCUS       WP_181626485             331 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DegT/DnrJ/EryC1/StrS family aminotransferase
            [unclassified Citrobacter].
ACCESSION   WP_181626485
VERSION     WP_181626485.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 331)
  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..331
                     /organism="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..331
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36788
     Region          3..329
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mhqlleekla sylnvpyisl fcnatialia amqtlrikge vittpysfva tthsilwnql
       61 tpvfvdidph sfninphlie saitaktgli mpvhvygqtc ntaeienisn nygipviyda
      121 ahafavedcs gsilrhgdls vlsfhatkvf ntfeggaivs ydkktkqrid ylknfgiade
      181 ltvvapging kmnevqsafg llqlkyvdea iakrqkidkc yreqlantqg ifipagnanh
      241 ksnysyfpil vgpdykmsrd alydhlkshn iltrryfypl lsnlnmyknm sganketlpv
      301 anqiaeqvlc lpiypdmtsa elstiielit a
//
LOCUS       WP_181626538             523 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: bifunctional metallophosphatase/5'-nucleotidase
            [Citrobacter].
ACCESSION   WP_181626538
VERSION     WP_181626538.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 523)
  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 523)
  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..523
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..523
                     /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=57200
     Region          27..505
                     /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 mnvknkfsls llslciglss aitftadard itiyytndlh ahvtpgiips vsktrevggf
       61 apiskivkda kekdkdvfff dagdyftgpy istltkgeai idilntmpyd avsvgnhefd
      121 hghenlvtql sklkfpvlln nvfysnsdkp liktpytive knglkigvig mhgvsafyea
      181 iaagvregvd cqdpvpyvkk qleelkgkvd ltvllahegv pgrqssggde dvaralkadv
      241 emaktlegyg lnvlitghah kgtpepikvg dtlvvstnay tielgklvld wnpetkkvds
      301 yngklitmya dtykpdpqtq akidewnnkv kkitdrivay speiltrsyg esattgnlit
      361 dalmykvpya dasfynaggi rselpkgnit ygdvlsmypf tndvmsveis gkdlrsimsh
      421 aadlkngtlh asktvqfkyd stkplgqriv sfsikgkpve dsqfytiald sfigkggggf
      481 sftnsknvky ikglqtaqai idymehvkni vpdhtmrvdd isk
//
LOCUS       WP_181626556             419 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [unclassified
            Citrobacter].
ACCESSION   WP_181626556
VERSION     WP_181626556.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     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=48061
     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 akpkdktykm adggglylev sakgskywrm kyrrpsdkke drlafgvwpt
       61 vtlaqarakr deakkllvqg idpkaeqkea qaensgaytf etiarewhas nkrwsedhrs
      121 rvlrylelyi fphigssdir qlktshllap ikkvdasgkh dvaqrlqqrv taimryavqn
      181 dyidsnpasd magalsttka rhypalpssr fpeflarlaa yrgrvmtria velslltfvr
      241 sselrfarwd efdfdkslwr vpakreeikg vrysyrgmkm keehivplsr qavilleqlk
      301 qisgdkellf pgdhdatkvm sentvnsalr tmgydtktev cghgfrtmar galgesglws
      361 ddaierqlsh ternnvraay ihtsehlder rlmvqwwady ldinknktit pydyalvgk
//
LOCUS       WP_181626716             318 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [unclassified Citrobacter].
ACCESSION   WP_181626716
VERSION     WP_181626716.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     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=36046
     Region          36..244
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mgkcnqella erarniplyl hayafhlnmr yervlpgdll diahqqqlkg vkihvedges
       61 qslqklndrq lhdfkekakk ynldvhiets asdnatltda iriavatgat svrfypryeg
      121 hlndvmakia ndiawlsqyd dcglsftieq hedlqghelv tlvnnsgmkn lsilfdfgnm
      181 inaneqplsa levmsplitq vhikdakiik edkgwgheac rsgygdlpme emlkallllg
      241 edkpqvnafg leeeveyyap afrfddegdn pwipwrdasy tplpdsnmid arlaqekeha
      301 laqikyirdl cdkftsnk
//
LOCUS       WP_181626792             446 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MFS transporter [Citrobacter].
ACCESSION   WP_181626792
VERSION     WP_181626792.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=48323
     Region          26..437
                     /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 maysgkvniq qaiddsafsr fhwviivlgf lvlaidgfdt aamgyiaptl sadwgikkqd
       61 lgpvlsaall glsfgallag pisdrmgrkr vlvfsclffg laslgtayaq tlnmltfwrf
      121 ltglglgaam pnaitlvsef apkrcrsmai ntmycgfplg aagggvissw lipnygwhsv
      181 llagaisplv ltallvlflp esvkylvhrg kgvaqikria qrfmsgsleq vtqfyldedr
      241 itvkkssvaq lfsmpwlpgt lmiwmtyfmg lviyyvllsw mptlmlgmgy plaesawlts
      301 lftfggtagi llagwlmdrw eahkvvslgf iltmlfalal gfehnhiilf galiflmgit
      361 mngaqsglqt laatfypthc ratgiawmqg vgrfggvagt mmsaqllslq wqadsilmfl
      421 slpalvaaaa tiyklqrykp haltva
//
LOCUS       WP_181627052             582 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sigma-54 interaction domain-containing protein
            [unclassified Citrobacter].
ACCESSION   WP_181627052
VERSION     WP_181627052.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 582)
  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 582)
  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..582
                     /organism="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..582
                     /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=64701
     Region          148..582
                     /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 misvlsniqd dicnyadais gitgtdveii deslmriagt gkyrhmlnen vakngyiyhh
       61 vlqvretvli knpgehplcq lcekhhycse mldlnapifl nnrvigvigi icstqaqrda
      121 llsqidkfvt fieqiavmis skvfeclerl raqetlgafr rlidamdrgv vaidgngliw
      181 hanhsadril nrevqglplt iettgdslyg deeawltleg qkhhvlckqi slssldndrl
      241 tmvifrdahd ylsnltpspy esdtqvrlig hsssmeqlrs tiskiansya svlitgesgs
      301 gkevvafaih qnsprkaapf vtincaaipe qlleselfgy vrgafsgadp kgrmgkfela
      361 nggslfldei gdmplhlqak llrvlqekai trvgsnniin idvriiaatn knisamvenn
      421 qfredlfyrl nvvplvlpsl rerkadiavl aqyfadefsv syqrapqklp ddvinrlyaw
      481 hwpgnirelr nvieyifvmr geaaginash lppyllspad srkttmtaqp rqlaiqgkqa
      541 erdaienaiq rfgssvegkk qaaselgvsi atlyrkikly gl
//
LOCUS       WP_181627387             653 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: peptidase U32 family protein [unclassified
            Citrobacter].
ACCESSION   WP_181627387
VERSION     WP_181627387.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            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 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..653
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=72857
     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 sdvgftqivl arelsleqin aihqatdati effihgalcv aysgqcyish
      181 aqtgrsanrg dcsqacrlpy tlkddqgrvv syekhllsmk dndqtanlga lidagvrsfk
      241 iegrykdmsy vknitahyrq mldaiieerg dlarssagrt ehfftpstek tfhrgstdyf
      301 vnarkgdiga fdspkfiglp vgevlkvakd hldvevaepl angdglnvli krevvgfran
      361 tvektghnry rvwpnempad lhkvranhpl nrnldhnwqq altktsserr vavdielggw
      421 qeqliltlts eegvsithtl dgqfeeanna ekalsnlqdg laklgqtlyy arniqvnlpg
      481 alfvpngqln qlrreavdml daarlqnyqr grrkpvaqpa pvypqthlsf lanvynhkar
      541 efyhrygvql idaayeahqe kgdvpvmitk hclrfafnlc pkqakgniks wkatpmqlvn
      601 gdevltlkfd crpcemhvig kmkhhilkmp lpgsvvasvs peellktlpk rks
//
LOCUS       WP_181627391             259 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Citrobacter].
ACCESSION   WP_181627391
VERSION     WP_181627391.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 259)
  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 259)
  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 259)
  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 259)
  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 259)
  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 259)
  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..259
                     /organism="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..259
                     /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=29342
     Region          17..250
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          18..107
                     /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 meiapdddfd adsfdkpvig iasemgvhds grhshlrhql lfsaagsiti elehalcllp
       61 prravwipag tvhraimrgv mayrslyfst tlplstlplq ivdvnplffe viermafwpw
      121 empaaqqasl itvfceemra arsenwtlrf psdprlnvwl egvrmgelpp rlnqlsqrvg
      181 acertisrif trdtgmnyqs wrqqfrllka memladggqi sqvaqylefv sdsafiaffh
      241 qhtgttpsry agnimpqkd
//
LOCUS       WP_181627604             143 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Citrobacter].
ACCESSION   WP_181627604
VERSION     WP_181627604.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 143)
  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 143)
  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 143)
  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 143)
  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..143
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..143
                     /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=16236
     Region          54..141
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mvndtirflc eviegdlnlk csilnnyhki ddyinklveh atiisirend qivgaicfyc
       61 nnqkdliayv smiavhtdyr gkgigdells famancrrkg fahcklevnk knvkalalyn
      121 kngfsilses eniylmqkni nri
//
LOCUS       WP_181627734            1647 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha-2-macroglobulin family protein [Citrobacter].
ACCESSION   WP_181627734
VERSION     WP_181627734.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 1647)
  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 1647)
  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 1647)
  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 1647)
  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..1647
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..1647
                     /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=180652
     Region          30..1646
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkhirvvacm lmlalagcdn ndkapiaakn dapaaqpaae kkaekdtaql qklaresegk
       61 altlldvsev qldgastlvl tfsipldpeq dfarlvhvvd kksgkvdgaw elspnlkelr
      121 lrhlepnrdl lvtierdlra lnnatfeiny ekslttrdiq psvgfasrgs llpgkvvegl
      181 pvmalnvnnv dvnffrvkpe slaafvsqwe yrnsmsnwes dnllkmadlv ytgrfdlnpa
      241 rntreklllp lseikplqqa gvyvavmtka gqyeysnaat lftlsdvgvs ahryqnrldv
      301 ftqslengaa qqgvdvalld ekgqtlakat sdakghvqle nhqnaallla rkegqttlld
      361 lklpaldlae fdiagdpgys kqffmfgprd lyrpgetvil ngllrdsdgk tlpdqpvkle
      421 vvkpdgqvir tvvsqpdngl yhftypldsg aptgmwhira ntgdnqsqmw dfhvedfmpe
      481 rmalnltsqe tplspsdkvt fsvvgyylyg apangnalqg qlylrplrda vpslpgfqfg
      541 niaeenlsrs ldevqltlde tgrgdistns ewrethsplq vilqaslles ggrpvtrrae
      601 qaiwpadtlp girpqfavka vydyrtdttv nqpivdedsn aafdivyvda qgekkavsgl
      661 qvrlirerrd yywdwleseg wqsrfdqkdl vegeqtldlk adetgkvtfp vewgayrlev
      721 kapndaissv rfwagyswqd nsdgsgaarp drvtlkldkp ayrpgdtikl hiaapaagkg
      781 yamvessegp lwwqeidvpa qgldlsipvd kswnrhdlyl stlvvrpgdk srsatpkrav
      841 gllhlplgde nrrlelales pakmrpnqpl tvkikasskn getpkqvnvl vsavdsgvln
      901 itdyvtpdpw qaffgqkryg adiydiygqv iegqgrlaal rfggdgdelk rggkppvnhv
      961 nivaqqaqpv tlneqgegsv tlpigdfnge lrvmaqawta ddfgsneskt ivaapviael
     1021 nmprfmaggd tsrlvldvtn ltdrpqslnv tlaasgliel vsdqpaqvnl epgvrttlfv
     1081 pvrakegfgd gelqatlsgl nvpgedigpq qkqwkigvrp afpaqtvnng vmlqpgeswt
     1141 lpeegvmnfs pvtvqgqllf sgkpplnlar yirelkaypy gcleqttsgl fpslytnaaq
     1201 lqalgitgdt dekrraaiet giarllqmqr dnggfalwdk ngpeeywlta yamdflvrag
     1261 eqgyrvpaag inqgnarllr ylqdpgmmsi ryssdtqask favqayaalv larqqkaplg
     1321 alreiwerrs qaasglpllq lgialktmgd akrsddaval alstprhder qwladygspl
     1381 rdnalmlall eennlkpdvq nsllntlseq afsqrwlstq ennalflaar slqdlpgtwq
     1441 aqtslaeqpl tgdkaqtrnl dadqlaalqv tnngaqpmwl rldvsgypqs apapasnvlq
     1501 ierhilgsdg qsksldslrs gelvlvwlev kasqdvpdal vvdllpagle lenqnlangs
     1561 aslqdsgsev qnllnqmqqa diqhvefrdd rfvaavavns gqpvtlvyla ravtpgtyqv
     1621 pmpmvesmyv pqwratgvag dilivkp
//
LOCUS       WP_181627794             499 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Citrobacter].
ACCESSION   WP_181627794
VERSION     WP_181627794.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..499
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..499
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54837
     Region          119..353
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mllknlfrrv kwvssgllal ikhvvltllv vliiflgvrv yqtesgpdlh swhtwhgnem
       61 saaaldnatf aqyqvreaal fadlqkqvgd tlspdeqtpi nrfwsgsrva paqftpnwnr
      121 sfvlmpqgkp rgvavmlhgl tdspyslkdi ariyqqqgfi avvprlpghg tapgaltavd
      181 weawlaatrl avreatrlvg nevplhlvgy snggalalky tldslddatl rrprqvvlls
      241 pmigvtsfar faglaglpal fpafakaawl nvtpefnpfk ynsfpvnaar qsylltkalq
      301 qqivqdaqtm rlhdlppvlt fqsvmdstvs tqavveslyr ylgpngselv lfdinqaanl
      361 rpllrtssyt aaatllpsvp rayrttvvtn ataetlavva rdtlagtrdv qvqplqeawp
      421 qemyslshva vpfpmtdsly glkpdvlnry glsigtialr getstllvgl dtlmrvtsnp
      481 ffpymkerie avigrnvkn
//
LOCUS       WP_181628074             160 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: prepilin peptidase [Citrobacter].
ACCESSION   WP_181628074
VERSION     WP_181628074.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 160)
  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 160)
  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..160
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..160
                     /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=17459
     Region          <2..146
                     /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 msaalpflll ytalsltlsf cdmrsrrlpd rftcpllwgg fifhlciipt qladavwgav
       61 agyasfafiy wsywllrkre glgygdvkfl aalgawhgwi flpslvfwaa llgcfgivvv
      121 givhgksalk nplpfgpfla aagfitgycr ltsgaiswsl
//
LOCUS       WP_181628187             262 aa            linear   BCT 28-DEC-2024
DEFINITION  dimethyl sulfoxide reductase anchor subunit family protein
            [Citrobacter sp. RHB35-C17].
ACCESSION   WP_181628187
VERSION     WP_181628187.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB35-C17
  ORGANISM  Citrobacter sp. RHB35-C17
            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 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Citrobacter sp. RHB35-C17"
                     /db_xref="taxon:2742625"
     Protein         1..262
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=28203
     Region          5..262
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 meqyelplvf ftvfaqwgag gvlaltlcqv fsaqkfsamq crtlalrfwi itvlgscasl
       61 ahlgapegay rsltglgssw lsrevavfiv lngvmfcwll lcwfrpaprg mtllggvtal
      121 vglgtilvts qvyyqmplhp lwhnaatpaa flgtalltgf msvaiarayw hlspstvcna
      181 givagivlsa galglryqvp gadasspllw wqlfasvcva vwgvsrlnsg mrswlwvali
      241 itgelagrml fysnvmssap wf
//
LOCUS       WP_181628339             304 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [Citrobacter].
ACCESSION   WP_181628339
VERSION     WP_181628339.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  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 304)
  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 304)
  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..304
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..304
                     /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=33626
     Region          4..301
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msitvavtgg tgfigkhiid dllsrgfavr altrtirhdv rdnlvwirga ledsevlaql
       61 vagaehvihc agqvrghtea iftrcnvegs qrlmqaakes gscrrflfis slaarhpels
      121 wyanskyvae qrlttmaaei tlgifrptav ygpgdkeltp lframlrgyl prfgaaearl
      181 sflhvsdlaq avsqwlmadr msvypyelcd gvaggynwqr iqeiaaavrn gpvrtvtipl
      241 plltlfadas tlisrfagke pmltrskvce lihsdwsann kslcekinwf prvsleyalr
      301 qglf
//
LOCUS       WP_181627626             481 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Citrobacter sp. RHB35-C17].
ACCESSION   WP_181627626
VERSION     WP_181627626.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB35-C17
  ORGANISM  Citrobacter sp. RHB35-C17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 481)
  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 481)
  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 481)
  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 481)
  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..481
                     /organism="Citrobacter sp. RHB35-C17"
                     /db_xref="taxon:2742625"
     Protein         1..481
                     /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=54366
     Region          1..>365
                     /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 mfikklkien fkgyhgenne lefnipdget egsglnifvg ennagkstvf eiidfikdgt
       61 kkniedlick svpdniaekl saeltftgnl seviaahvqa nkvaaftshv fedegvnffr
      121 vkrcseagek kilfwngnef vnpsgidapf kkfydnnfiw adtnpsneak fgstticgsl
      181 lkeialghia tdeyrafseq yhrvfnhpes elrqkislve nqvrevfssq fgmadisfif
      241 eelqvenffk tisimiddgv nvpmgekghg mqralalsll qvyaeitcna hgagiskpfy
      301 lfidepeicl hpsgqqklle almiisksrq vfvtthspfl lsspylknig lfvfkkennk
      361 nvveradtsp wfpwspswge infkaynlat velhnelygy lqeknscpse ktmeqwlnsk
      421 giafdkvwvk efkgaaqppa dttlqtfirn hihhpenvtm qshrytqqel ltsiqqmvgl
      481 l
//
LOCUS       WP_181629134             522 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: formylglycine-generating enzyme family protein
            [Citrobacter].
ACCESSION   WP_181629134
VERSION     WP_181629134.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 522)
  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 522)
  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 522)
  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..522
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..522
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=58547
     Region          105..306
                     /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 mtltpstlsr wlaltllvkm spvlaepwae kiynpkpdse diilpmpceg smvfrqveip
       61 vsgplddmpi tlgedggewg fvehsyptfi agsfteskkn kgryylmaky eltalqyqal
      121 tsgtcptpsr klsiaetnis wfdavnfadk ynqwlrtnal dklpkedgnp gflrlpteve
      181 wefaargglk vnsaefrdsh ypmddmknye wysgsqssng kvqligllnp nplglhdmlg
      241 nvsemmltpf ylnkinrlhg qaggfvvrgg svisneseir satrkeinyy deahpftskt
      301 tglrlvlvsp titstdrvkq leknwaalga dkpgidkske vptdtakalg slasgiedte
      361 lkkklkdlen qlrasnqqqq eeraqsiras lnlgsflctk lqddgrfldf lnhnyellck
      421 dkddsdknca irktklgeqt drlqqltsyy asslvdsatl ygqeglkhev mvfdqmltln
      481 krlaglkpfl aahwqnqqqy langkidatr wldtckqiks dh
//
LOCUS       WP_181628926             403 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: trans-sulfuration enzyme family protein
            [Citrobacter].
ACCESSION   WP_181628926
VERSION     WP_181628926.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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
REFERENCE   2  (residues 1 to 403)
  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 403)
  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 403)
  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..403
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..403
                     /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=44528
     Region          25..400
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mkeiicnyae ndyavqdami csgvgeqhqk nfgavspplv ktslfvqqsy qqycddmqhe
       61 aeryiysrgl npttellehk laalergaac kvfgsgmgai satlfgllks gdhiilvnnv
      121 ygptvvlvkq mqqrfgidyd ivlsgdvedi rqkikpntrm iytespgtmt mrvvdlqmia
      181 glakenniit aidntwatpl fqkpltlgfd lvlhsctkyi gghsdltaga vvgakvyldi
      241 irdfshqllg avlapdsawl virglrtlpl rmrqhqnnty ailtflnsra evenichplm
      301 adakqreivs qqmfgtsgli sfelkdgsfe kvkaiidscr ifkpgcswgg yesliispnr
      361 gynqdvickd gmapgliris igqespemli adlenafdsi kty
//
LOCUS       WP_181629640             200 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_181629640
VERSION     WP_181629640.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 200)
  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 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   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
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13296807
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..200
                     /product="helix-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=22348
     Region          3..188
                     /region_name="PRK09935"
                     /note="fimbriae biosynthesis transcriptional regulator
                     FimZ"
                     /db_xref="CDD:182154"
     Region          <140..196
                     /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 mqlimfdrqs ifihgmnvil qeripgvnvq gvsqaddlwr tlednpdalv mldgdfdaef
       61 crsllqqiae rfakvkvlvi atdcrkkwlq evtqlnvlai iprdsdaetf tlalnsvaig
      121 mmfiprdcit atecggqnir llsarqreil tmlaagesnk qigrllnist gtvkahlesl
      181 yqrlevknrt qaammlndtl
//
LOCUS       WP_181629181             555 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: O-antigen ligase family protein [Citrobacter].
ACCESSION   WP_181629181
VERSION     WP_181629181.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=62453
     Region          171..386
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mmnalnriap lpaqklllvi slffwcgvmh lywpnnggsg lslplnitsw iyavvlaasa
       61 svlvprqrwr itvpatvfsm galiltqlcl ltpgvwqfea qlvagallgg vlvylvtlqi
      121 plaantltvl ltllwgacvi eclaflyqyw hlpgvdywef awrrgtrpyg ifqqvnlmas
      181 ftasgvllsa plfvrlrdry rivigialvm mgfvlhesqs qtgyvsvvvg evlllvvfpa
      241 qrrmllllll plalgmvagt larhflsvat vdhlttsqvr wtvlktslal faerpwtgwg
      301 vgsfaavfle ragplglssi shphnelvlw lvegglvgla galcfitggf wlwmhgnrwr
      361 raclvaalpv vihmlteypv rqstphwlll illlrcadsp lkvarltlts tsliralali
      421 sfltftplll lslhtqqqlt laerqsaqwr laeslpvggw llapryrfdv qmgylqryqr
      481 trdarwleav rrwapdyvrv hpdpnvsftq illalqqrdl peahrlatrf yltypndrri
      541 pwlqdarrpf nqkme
//
LOCUS       WP_181629731             197 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Maf family protein [Citrobacter].
ACCESSION   WP_181629731
VERSION     WP_181629731.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=21341
     Region          4..185
                     /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 mntlylasgs prrqellaql gvtferlvpg ieeqrhpqes aqqyvsrlar ekaqagvala
       61 qrdlpvlgad tivilngevl ekphddahaa amlrklsgkt hqvmtavala drrhsldclv
      121 vtdvtfralt dediagyvas gepmdkagay giqglggcfv rkingsyhav vglplvetye
      181 lltnfnalre krdkhdg
//
LOCUS       WP_181630413             420 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Citrobacter].
ACCESSION   WP_181630413
VERSION     WP_181630413.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=48229
     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 mslndskirs lkpssrpvkl sdshglyllv npggsriwyl kyrfngkesr vslgayplvs
       61 lvearqqrdv frrqlaqnin paqqrvaeka aaspdkcfqa valdwlktnk kwskdyaert
      121 lasmhnhifp aighlpvtll ktqhftvllk vieekgllev asrtrqrlcn imryavqqgl
      181 tennpaqhle gvtappvknh hpalplerlp ellerigdyq qgrqltrmav lltlhlfirs
      241 selrfarwse idfrnkiwti patreeiekv rfsgrgakmr tphivplsrq aiailkqiqe
      301 lsghqelvfp gdhdpckpms enttnralrl mgydtktevc ghgframacs alveselwsr
      361 daverqmshq ernsvraayi hraehldark ammqwwsdyl dmcresyvap yiyarqhkvs
//
LOCUS       WP_181630558             704 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Citrobacter].
ACCESSION   WP_181630558
VERSION     WP_181630558.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 704)
  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 704)
  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 704)
  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 704)
  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..704
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..704
                     /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=77844
     Region          75..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 mlhvswdpvl igisfvvafi asfialdsag kvaisskres tfwrlsggat lgmgiwsmhf
       61 igmlamkmtm pinyhlslta fsffialisa tlainiaisg ntlstkrlvi atsilsagvv
      121 tmhyvgmyai iehvaiswdr slillsviia vvasgvglwl afhlrqntrr vlinrliaal
      181 imalaiasmh ytgmgaatft hfghtahdgl stlelsvwvc avtliilgim lvvsmvdsql
      241 rtsrladnlh qlncqlehqv hfdaltglan rtqidtrlqa clrhsklhqq hfalvfidld
      301 rfkvvndtwg hhigdqllia stqriyscld dsmtlarlgg defillvpdc nqqaisalla
      361 risdaigdpf tlfghtirvs lsagssiype hgstlhelkv kadmamyhvk qagrngwaiy
      421 spqmeaiadt pptflqelsq alernqfelw yqpkytagdh sltgfeallr whhpergmll
      481 paeflpalee tgliipvgrw viqqaclqlh qwtlqgntew tlavnlspaq feqhdiidvv
      541 cnalaqyqls pacltlelte stalknlkrs ieilnafsal gitvsiddfg tgysnilmlk
      601 slparelkid rifvkdisen skntkivsti idiahsmnmr vvaegietqe qellltqmgc
      661 smlqgflfak plpahkihel iqsensikqk pvvqplshrq sitl
//
LOCUS       WP_181629781             527 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 13 protein [Citrobacter].
ACCESSION   WP_181629781
VERSION     WP_181629781.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 527)
  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 527)
  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 527)
  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..527
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..527
                     /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=59915
     Region          8..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(22,24,26,30)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(61,64,101,104,140,159,163,195,249,393)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(195,249,309)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          442..512
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mkkqpwwqac tcyqiylpsf cdgnndglgd fpglisrldy lqalgigavw itpfypsplv
       61 dngydisdyy avdarfgtld dfrrvvdgch argirviidl vvnhvssehp wfrdawnnpg
      121 sryrdyflfr rqpnnwrsff sgsawtaepd tgefyyhkfa pgqvdlnwan paveqeiyrv
      181 vdfwvtqgvd gfrfdvinfl ttdgigpdnp eengeqrhef dinqprlpet lqrlcahvra
      241 qgdyfligei gsedpdvlsr yqspqlmdvv fnfnigsqkn fdvsrlfsql kttlaaqpgl
      301 ptlffsshdm srmisrfgen erdtgralav lalqltvsgv pfifqgeelg mtdyrpqtae
      361 qlfdiqgkth yrtalaagss pqqalalaie hsrdgsrapl pwrdapfggf ssvapwmpvg
      421 gdialinaer qqqdetsfwh qyrrlialrr rvaalhqgqq dsldltdecv wftrsttaeq
      481 vwvainfgap vrnpwqeiea evlygedaqw igknqclikr rvhgqaq
//
LOCUS       WP_181631117             450 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Acinetobacter baumannii].
ACCESSION   WP_181631117
VERSION     WP_181631117.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 450)
  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 450)
  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 450)
  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..450
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..450
                     /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=51739
     Region          25..378
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maqhikftks vidsiplsee kqifyrdtat igfglcvgkt ksyfaekkmp ngkskrkvig
       61 khgvytleqa rteakrllim mdegvdpvkq krdlrasaiq ndalqklvpt lseayqyykl
      121 rkklaetsli aydgcienyf sdwkdvkldq itssmiidrh lklseaspsr anlaskflha
      181 lfnhtisryk desgnkilni knpvvivkee kafnkikrrk ghvradqrea walavattyw
      241 mgeqnndfra ytnqdflfll altgfrrsea eavewknvdl qfgtikivnt knhedlllpm
      301 gdtlwhlmre rkkragnnky vftdrngvsh isdrraarek vtensgieft fhdlrrtfgt
      361 ianslaigsy tikrlinhtt ddddndvtdg yiqvsfddlk kamnmiedvi isdpvkelik
      421 srlyfeknes rnqaqalldh htrilgnynk
//
LOCUS       WP_181631149             949 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Acinetobacter baumannii].
ACCESSION   WP_181631149
VERSION     WP_181631149.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 949)
  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 949)
  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 949)
  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 949)
  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..949
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..949
                     /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=110520
     Region          <29..79
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          51..73
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320175"
     Region          347..946
                     /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 msglqeeylq hqtkieqhrl siqyirwylv slillclisa iiffcyftsy itnfiwsigf
       61 tiltltcllf vpkllthyrd ihfikktdlv lqgiclasgi lmginiivlh fslpdtlisv
      121 sdvhilialf itsahiiglt fltqqpryfy llfipstvpl iigqfthsqi tqlpfyfayn
      181 lafvatllca yatqrnyqki sqllfknkql vqvaeqhtqw aeelcvqlqq evnkskdiea
      241 qlqfnnhlle qkvrertydl tkmnerlesh hhnlafahet agirpwdwdi ekqkleitff
      301 dqqkqtqntp lhlksileri hpndrklfde rlkehlegks dhfnitfril rrngswrwih
      361 dvgrvisrdp ktnkalrmvg mtrdihqekk dqehlrlsai vleqaaegif ildeklnyie
      421 vnpyyekltg fsksellsqq lfnitinqkl qqqqfhdsit qqllktgeym gqfdekftsg
      481 ksvylwlhin avkdeynqii nyigfardlt dqkrqeqhls ylknydslth lpnrfyyynq
      541 lhqylvnpsy sfknlaliri nidrfrafne flnndsgdel lkqfaqrlrl tninailvay
      601 lngddfaiiy eispihpnie qycqnilqal napfyideqe yfitasigva cfpehgrqid
      661 hlnnhaeqal seakrlggnt isyycnkttn pyktadleqe lrkaiqndef vvyyqpkinl
      721 ndksikgfea lirwqhpekg lvmpnmfipf aersslisdi gkvvldkvgk qlqewkkagy
      781 advrvsvniv aqqihrglll sdldevldty hldgsnlele itesalldnt dnvkkllhsi
      841 kernisiald dfgtgyssla ylteypidvl kidrafvski gdqkqeaivn amiamgksmg
      901 lklvaegvet eeqviylqkq qcdflqgfff srplhpnqil qylqtnthi
//
LOCUS       WP_181631175             473 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Acinetobacter
            baumannii].
ACCESSION   WP_181631175
VERSION     WP_181631175.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 473)
  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 473)
  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 473)
  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 473)
  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..473
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..473
                     /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=52797
     Region          4..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 maeqqplvll vddeedlcll mqmtlarmgi kthlayrveq akqlftqfhy dacltdlnlp
       61 dgsgidlvkh vsqnytntpi avltaygnmd iaiaalkaga fdfvskpvnq vhldqllqka
      121 lnrqkvehda tenalenkll igrslpiqql riaikkiars qapvfvtges gtgkevvanl
      181 vhrlsnrseg pfiaincgai ptelmeself ghkkgsftga tqdkqglils ahggslflde
      241 iaelplsmqv kllravqekk irpvgsdqei dvdfrvisas hqdldllvrq gkfrqdlffr
      301 ihvmdlilpp lrergedvll lanhfiqkvc mdwetppkql teaaktyllq qhfpgnvrel
      361 rnmieraitl sedatidvsh lhpaplrani snpfasaaqs iqttvaapqv vkklpsegle
      421 ryleniekdi llnalnmthw nrtlaakklg mtfcslryrl kkfgldtete qev
//
LOCUS       WP_181632400             343 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter sp. RHBSTW-00229].
ACCESSION   WP_181632400
VERSION     WP_181632400.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00229
  ORGANISM  Citrobacter sp. RHBSTW-00229
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHBSTW-00229"
                     /db_xref="taxon:2742641"
     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=40208
     Region          8..315
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msdknhyttw eelleeyffa rnlraatews yakvvkgflk ftgaditpsm vthhevlrwr
       61 rhvlrekqqs aqtwnnkiah lralynyame sgllpagknp fnnctvqrdr kkkrtlnrsq
      121 ltrlylimqq aeiesnrkif arggrsalyp awfwitvldt lrytgmrqnq llhiqlrdvn
      181 ltegyidlrl egskthrewr vpvvkqlrlr lqllltrame agagpkdnlf dvsfyiagkk
      241 akfdrndvtv mhqkirsffr rlskecgfav sphrfrhtla telmkapern lqlvkdllgh
      301 rsvsttmeyv elnmdivgkt leeelslhtd lcverelqll tqn
//
LOCUS       WP_181632496             653 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidase U32 family protein [Citrobacter sp. RHB35-C21].
ACCESSION   WP_181632496
VERSION     WP_181632496.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB35-C21
  ORGANISM  Citrobacter sp. RHB35-C21
            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 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Citrobacter sp. RHB35-C21"
                     /db_xref="taxon:2742626"
     Protein         1..653
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=72918
     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 sdvgftqivl 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 tvektghnry rvwpnempad lhkvranhpl nrnldhnwqq altktsserr vavdielggw
      421 qeqliltlts eegvsithtl dgqfeeanna ekalsnlkdg laklgqtlyy arniqvnlpg
      481 alfvpngqln qlrreavdml datrlqnyqr grrkpvaqpa pvypqthlsf lanvynhkar
      541 efyhrygvql idaayeahee kgdvpvmitk hclrfafnlc pkqakgniks wkatpmqlvn
      601 gdevltlkfd crpcemhvig kmkhhilkmp lpgsvvasvs peellktlpk rks
//
LOCUS       WP_181632666             386 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome b [Citrobacter sp. RHB35-C21].
ACCESSION   WP_181632666
VERSION     WP_181632666.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB35-C21
  ORGANISM  Citrobacter sp. RHB35-C21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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 sp. RHB35-C21"
                     /db_xref="taxon:2742626"
     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=44443
     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 mrservyslr wripfprsia glwvfaigai llvilgvqil tgivlamfyv ptaelafdsi
       61 ihimravrhg ellrnmhaig aslfffacyl hifrgmyysv yrkpwttmwm isvtlyvllm
      121 mtaflgysli wgqksywaat vitrfaqaip lvgdtlyayl vgshtpgtpm lgrffvlhfi
      181 lpfvivgatv fhirtvqsaf aqamkkrfse kesrsllfdy kitdldaiki ilflmifawf
      241 lffaphylss adnfipadpt vtpaivapew yflpffsilr cfpnefvgla amcssvlify
      301 flpwldtsra rfrhysklvk cgfwlwvina cflgwlgska lvgpdlidgf rneegwiraa
      361 sqlstliwfa wflivlpcrr flekqd
//
LOCUS       WP_181632691             377 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-methyltransferase [Citrobacter].
ACCESSION   WP_181632691
VERSION     WP_181632691.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            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 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..377
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=40301
     Region          4..363
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mtyqlhvgrc evvlksipdn svdsivtdpp yglsfqnhkw dydvpsveqw qeclrvlkpg
       61 ghllafggsr tyhrlvvnae dagfeirdqi lwiygsgfpk shnldgqwdg wgtalkpahe
      121 pilmarkpfk ttvaenmvah gtgalninac riptgeqlsg gsgcllshqr dgtdpaadye
      181 qsaggrwpan iihdgsddvi acfpanagaa apvtgnepsa astgqvlgmr qrvatvhhgd
      241 kgsaarffyc akvkpserde glerfiatsa sdmtggrkeg sagindprag agrtkgaknn
      301 hptvkpialm kylcrlitqp ggtvldpwmg sgstgraaie egfnfvgidl dpdyvtiasa
      361 rlafslkkya nekaeal
//
LOCUS       WP_181632805             342 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Citrobacter sp.
            RHB35-C21].
ACCESSION   WP_181632805
VERSION     WP_181632805.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB35-C21
  ORGANISM  Citrobacter sp. RHB35-C21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB35-C21"
                     /db_xref="taxon:2742626"
     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=38535
     Region          8..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktikgpgif laqfigerpp fntlegvakw aaelgykalq ipcnhkslfd veqaaisqay
       61 cddirgmlag hglviselst hlegqlvavh payddafdgf appsvranpq arqawavetl
      121 hqaaaasqrl gltahatfsg slawpffypw pphnrqrfee aflelarrwr pildrfdhhg
      181 vdvcfeihpg edlhdgvtfe rflalvnhhp rcnilydpsh lllqqmdylg fidvyhsrik
      241 afhvkdaeyh assrsgvygg yqpwldragr frslgdgqvd fktifskltq ydfpgwavle
      301 wecclkdaqt garegsdfir rhiipvssra fddfaagdev rk
//
LOCUS       WP_181632806             192 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Citrobacter sp.
            RHB35-C21].
ACCESSION   WP_181632806
VERSION     WP_181632806.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB35-C21
  ORGANISM  Citrobacter sp. RHB35-C21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 192)
  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 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   3  (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   4  (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 18629715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Citrobacter sp. RHB35-C21"
                     /db_xref="taxon:2742626"
     Protein         1..192
                     /product="helix-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=21614
     Region          <64..179
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          134..>176
                     /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 mskaiflges iypwlgmrei lrgsslyidi ayyssqtlsa vniipyemdc iiinpdnsdf
       61 lkyariirnm alrpatkiiv ladeatfsif qtvcgrnmqf ldqdasldrl lravtcisqn
      121 kkpinikein nkitanefnv mmmlargwsl tqiagasqks ektigayksn iarklgknns
      181 rlkytishys qp
//
LOCUS       WP_181632937             241 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_181632937
VERSION     WP_181632937.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=26894
     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 mlpgrcknai iisklpivqt glkgvmqgqf adyeltycrs veeltllqlr cadlviadls
       61 gdcnhprsvc eqyysllsqy rdihwvflvs rvfyplaiel lmcpvsslls daetieslvn
      121 vihagnsrae risqsllspp vmpeladhsa rsivltlser kvlrllgkgw ginqiatllk
      181 ksnktisaqk nsamrrlsih snaemyawin ssqgsrelnl psvygettew kaeasketlr
      241 w
//
LOCUS       WP_181633163             259 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Citrobacter sp. RHB35-C21].
ACCESSION   WP_181633163
VERSION     WP_181633163.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB35-C21
  ORGANISM  Citrobacter sp. RHB35-C21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB35-C21"
                     /db_xref="taxon:2742626"
     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=28857
     Region          1..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 mteliniaam alvglivgsf mnvvvyrlpi miehrhsetw niawppshcp hcqhrlsvrn
       61 tiplfswlwq rgrcqvcaqp iswrypltel acscvfalsa afvpsmsdai aimtlfwfif
      121 alaqidlrty llpdvltqpl lwlglmyhsv ydremlsdal ygavagyltl wlvwwgckil
      181 agkegiglgd akllaamgaw cgwpalppil laasllgivw wlilrltrrt sipliafgpw
      241 lglagwlifs aqssgvigy
//
LOCUS       WP_181633518             270 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Citrobacter sp.
            RHB35-C21].
ACCESSION   WP_181633518
VERSION     WP_181633518.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB35-C21
  ORGANISM  Citrobacter sp. RHB35-C21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB35-C21"
                     /db_xref="taxon:2742626"
     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=29206
     Region          1..268
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrisisnlaw dvkedlevan llnlfnvdai diapgkyfpe pasasiadih avkdwwqerg
       61 idiigmqall fgtiglnvfg sesiqkklld hlaavcriga glgasrlvfg spknrdcsgl
      121 svsqvqeisr lffrqlgdia adygvivcle pnpsvyganf mttsletcnv vndidhpaik
      181 mqldtgavii nqedisavvt qakdvighvh iseaqlappg dtyshhedia alitsqfpah
      241 patiemlatq nephlvsirr alqlvtslyr
//
LOCUS       WP_181633625             354 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Citrobacter sp. RHB35-C21].
ACCESSION   WP_181633625
VERSION     WP_181633625.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB35-C21
  ORGANISM  Citrobacter sp. RHB35-C21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..354
                     /organism="Citrobacter sp. RHB35-C21"
                     /db_xref="taxon:2742626"
     Protein         1..354
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39084
     Region          26..353
                     /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(208,231,329)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:214009"
ORIGIN      
        1 mktvlktlai camaggmvaq svyaeplviq eqgsfsaggt iitapgkfda ktpldsagqt
       61 whgdhasvfy qipenphkyp ivmlhgagqf srtwettpdg regfqniflr rgfstylvdq
      121 prrgsagrtt vegtvtpkpd eqmwfnqfrv gvwpeyfkgv qfshdkealn qyfrqmtpnt
      181 gpfdinvisd amsavvdksg pailfthsqg ggpgwytamk ndkikaivaf epgssfvfpe
      241 kelpapmpsa fdtlkgepvp meqfmaltki piliiygdni pdkpvampaq dswrvrlama
      301 rewrdvvnkh ggdvtvthlp eegikgnthf pfsdlnnvqi admvsqflee kdlq
//
LOCUS       WP_181633721             286 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_181633721
VERSION     WP_181633721.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=32502
     Region          <97..277
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          188..271
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 myhdvshlls rlingptplr qvyfastsss tpelayqvdf prleivlege ftdngvagas
       61 atllpcdvlf vpaggwnfpq wltpvttlsi lfgkqqlgfs ivqwdgkqyh nltrqhvarr
      121 gprigsfllq tlnemqmqpq eqqtarliva sllshcrdll gsqiqtasrs qalfeairdy
      181 ideryasplt resvaqafyi spnylshlfq ktgaigfney lnhtrlehak tllkgyelki
      241 kevahtcgfv dsnyfcrlfr knterspsey rrqyhsqlte ikanpk
//
LOCUS       WP_181634483             389 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter sp. RHBSTW-01044].
ACCESSION   WP_181634483
VERSION     WP_181634483.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-01044
  ORGANISM  Citrobacter sp. RHBSTW-01044
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHBSTW-01044"
                     /db_xref="taxon:2742678"
     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=44689
     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 inakpyrgap evtdgdglsv ritptgtitf qhryrwngkp vrltigrypa
       61 mslkdarviv gemrelylkg lnpknyfake dgeltlkecl dqwwskyvet lkpntqtlyk
      121 svvyntmyte fpdapvvnip vsawvrffdk qekkngkkar vlllqlrsvm nwcisrqlia
      181 scevlklsvk tigkkpdvgs rvltytelak iwlalennki vssnkvlhql lllwgarlse
      241 lrlatasefn mddliwttps ehskmgnvir rpvfdqvkpf verllnsgnd vlfpgqeldk
      301 aidrssanly mkklrdkidi pewrthdfrr slvtnlsgeg vmphvtekml ghelggvmav
      361 ynkhdwlveq keayelyadk ifwhikqic
//
LOCUS       WP_181634671             625 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Citrobacter europaeus].
ACCESSION   WP_181634671
VERSION     WP_181634671.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter europaeus
  ORGANISM  Citrobacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 625)
  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 625)
  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 625)
  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 625)
  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..625
                     /organism="Citrobacter europaeus"
                     /db_xref="taxon:1914243"
     Protein         1..625
                     /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=69232
     Region          26..349
                     /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 mnnesdeftw pisvkyplvd nlgtiatikv gpgitvlvgp ngsgktralr aiksqlmsen
       61 llntnnrkvh flsagrsspl esyrsssnsp hgvdtnnaav gnigymdnww nfesitgdlm
      121 vldrrpdlkl kiearlqqlf drsvelkwsq ngmiirmtsv tsgdgypanh easgilqvia
      181 llsaihndei gtliidepei slhpqhqafl leemelvagd psdptkklii iathspsmlp
      241 lrrieelski iffnsaqrvp aqieskseil ksrkltalia rlsathrtam faehvllveg
      301 psdeiivtql arkfglrmla rnaqilpvtg kgefieaakl frlmnkqvsl ladldalade
      361 ndlvnyfsgl peamafadqi grtnladfdr dlrgeitsfi adfkaeidma addypdwssk
      421 esgadtkrrv tlariltnpr sfgtetsssa erlfikynll lsslekvgcy flrrgaieny
      481 yretadigag kpdraalesa gfdarekhel easykdiyaa lqyaapnkiv dedtllrmkl
      541 gaillpvmlg mkfnssdkei ealasstign datvfklsnk sdeqqiklev dlrsplfkre
      601 nfpfeistse npiavlqkvl pginr
//
LOCUS       WP_181634946             230 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_181634946
VERSION     WP_181634946.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=26503
     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 ivqilrgrrv ttaallaerl evsertiyrd irdlslsgvp iegevgsgyr
       61 lmagfdlppl mlthreseal mvairllktw ggdslsqale saqekvlail ppecrrraeq
      121 trvfapdfgn qphsrsafdl ihravsaqqv lalhyrdesg nlswrdvqpl glffwgehwl
      181 lvawcekrdd yrcfrvdrcl kitpldrhfr esadrslsdf lrkvrcedql
//
LOCUS       WP_181635013             476 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alanine/glycine:cation symporter family protein
            [Citrobacter].
ACCESSION   WP_181635013
VERSION     WP_181635013.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=51264
     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 rtgfiqfryi rqfgkslkns ispqpgglts
       61 fqalctslaa rigsgnlagv alaiaaggag avfwmwvsai igmatsfaes slaqlykerd
      121 skgqfrggpa wymerglgmr wmgvlfaifl liayglifns vqansvshal tfafdipplf
      181 tgialaivsl laiiggikgv arlmqwfvpm mallwvgcsi viclwhfgql pgiimtiiks
      241 afgwqeaaag aagytlsqai asgfqrgmfs neagmgstpn aaasaaswpp hpaaqgivqm
      301 igvlvdtlil ctasamivll agndasyvpm egiqllqkam vsvtgewgag fvalivilfa
      361 fssivanyiy aennlvflkl dnirvvwllr iatvstvigg tlvsvpliwq ladiimacma
      421 itnltailll spvvqtiacd ylrqrklgvr pefdprrypd irqqlapesw detprg
//
LOCUS       WP_181635401             354 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Citrobacter].
ACCESSION   WP_181635401
VERSION     WP_181635401.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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 354)
  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 354)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..354
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..354
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39051
     Region          26..353
                     /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(208,231,329)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:214009"
ORIGIN      
        1 mktvlktlai camaggmvaq svyaeplviq eqgsfsaggt iitapgkfda ktpldsagqt
       61 whgdhasvfy qipenphkyp ivmlhgagqf srtwettpdg regfqniflr rgfstylvdq
      121 prrgsagrtt vegtvtpkpd eqmwfnqfrv gvwpeyfqgv qfshdkealn qyfrqmtpnt
      181 gpfdinvisd amsavveksg pailfthsqg ggpgwytamk ndkvkaivaf epgssfvfle
      241 kelpapmpsa fdtlkgepvp meqfmaltki piliiygdni pdkpvampaq dswrvrlama
      301 rewrdvvnkh ggdvtvthlp evgikgnthf pfsdlnnvqi adlvsqflke kdlq
//
LOCUS       WP_181635501             205 aa            linear   BCT 28-DEC-2024
DEFINITION  IbrB-like domain-containing protein [Citrobacter freundii].
ACCESSION   WP_181635501
VERSION     WP_181635501.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 205)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..205
                     /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]"
                     /calculated_mol_wt=23541
     Region          42..141
                     /region_name="IbrB_like"
                     /note="immunoglobulin-binding regulator IbrB activates eib
                     genes; cd16397"
                     /db_xref="CDD:319255"
ORIGIN      
        1 mqhrlthell gflsglseee rieainefrr aihsvspfse epvdcvlwvk ndhispndyn
       61 pnnvappekk lllksleadg ftqpivvvhs taeeyeivdg fhrhelgkak aslrprlkgy
      121 lpvaclerer hermaatirh nrargrhqih amseivrels qlgwseerig kdlgmdndev
      181 lrlkqinglq elfadrrfsk awtvk
//
LOCUS       WP_181634223             400 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sigma-54 interaction domain-containing protein
            [Citrobacter].
ACCESSION   WP_181634223
VERSION     WP_181634223.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=45427
     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 sqradiinva ylceeisels mseperpryf sdiicssqsm rlliekaiki adskytvlir
      121 gdtgtgkell araihnsgqr rfypfipvnc salpeslmes effgyekgaf sgadgkgkkg
      181 lfemadkgtl fldefgempl slqakllrvl qdggirrvgg aqiipvnvri ivatnanlee
      241 rveqrllrad lyyrinvlsl tipplrerpq disllirhfv qkyakefqrr iildkacfda
      301 lhhhnwpgnv relentiirl mlmaesdvit reelgmvnlp aveqapterp fkeqvlcaer
      361 qlieqmveen vssrhiakal gvshttvlnk irsyqlegvd
//
LOCUS       WP_181634365             257 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Citrobacter europaeus].
ACCESSION   WP_181634365
VERSION     WP_181634365.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter europaeus
  ORGANISM  Citrobacter europaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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..257
                     /organism="Citrobacter europaeus"
                     /db_xref="taxon:1914243"
     Protein         1..257
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=28138
     Region          31..219
                     /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 mkkitllaaa talalssica hadtllapsa hakmdgenki valygnsftf ynnnintrlr
       61 dltqsllpdh akgykyrgit issghlgwqi enmryqntlq kwdvvvlqgn stetiskkes
      121 trqnfvdsat qmanmahqag akvvyfmtwp kkdkpedsqk ladayisiaq ktggyvapvg
      181 lafekarkth peinlyyhdg vhpsisgtyl aacvffatly nqspvggalp vdtdmtpata
      241 kalqqiawdt vtefqks
//
LOCUS       WP_181635717             239 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Citrobacter].
ACCESSION   WP_181635717
VERSION     WP_181635717.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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 Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..239
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25576
     Region          10..207
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mcnailkaaa vlfdmdgvli dsnevieraw reaaamygkt iseheiikhi hgqpgphtir
       61 alfsdlplvd qqkvqahiih ventasynpi pgvaelitvl dasgiqvgiv tsgwrekidr
      121 vtamlqiqsc isviverddv argkpfpdpy llaaerfaip aektivfeds ksgvtsavaa
      181 gafcvgigsa eliscgarlt isdftgvevi srldgniais fcpghvlmid kkdasqetk
//
LOCUS       WP_181636120             694 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein [Citrobacter].
ACCESSION   WP_181636120
VERSION     WP_181636120.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..694
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..694
                     /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=77921
     Region          81..>165
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mrvisiagit ayllcshaaa tenyqyrvaf mpdihfhdvy gefqdgafsg lknrksgqra
       61 mirtmyaqlt strlfnenyf alraalddag kkgiklialp gdfsddgqsv hirglvtllk
      121 eyeqkyamrf fatpgnhdpn rpfdlpdgee dflgqggktq rifsfgakec tgyqgktali
      181 stgaelptic seemvsrgye yimkmmspfg idpqpediyw etpyssygqq dytfakakqa
      241 sdfrqrqyei caqgtggsyr qpdygpcftv adssylvepi pglwllavda nvyvpredad
      301 ltnpqsaknf agsgdagynk mlthkqqvva wmtsvamrak eqkktlitfs hfpmvefdng
      361 aasdlesifg kgkfqlkrap kedtshalak tgigvhvggh mhfndtgvrk ypdgsllfni
      421 qapsmaayvp aykilnfanr seidvqtvtl dsvprfnelf ehyqqewehl katgsahlwn
      481 kavlsakdyy dftnwhitel trlrfipeew pceirqmlfs lngaemltls qlsshnswqd
      541 vltvpmssdr avcakgdvpp vrsigqiylq knagawqlaq qkaltlarda gmtleqfasw
      601 ngfdlavdfy rlrnadelal rdisaqrlre yhlltrtlah slpdeasavm adsdfetifr
      661 lrfgsifsvi dkylrggpsr nfhlnsetge isar
//
LOCUS       WP_181635066             637 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: BglG family transcription antiterminator
            [Citrobacter].
ACCESSION   WP_181635066
VERSION     WP_181635066.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     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=72826
     Region          14..609
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mrfpnqrlaq lfgmlqneal pqdelaqrls vstrtvradi talnalltqy gaqfvlsrgn
       61 gyqlkiddpa ryhalqtqrp dallriprts qervhwlvvr fltsafslkl edladewfis
      121 ratlqndmae vrehlqryhl tletrprhgm klfgsemair acltdllwtl aqqdpqhplv
      181 tqealnagip eqlqpvlqdi farfhirltd egelflrlyc avavrriseg yplpefaaee
      241 aeqsvclatr eiaavlhrla dkpltvseen wlqvhiaarq vqeiapsain adddealvny
      301 ilrfinsqyn ynllndkqlh adllthiktm itrvryqimi pnpllenikq hypmawdmtl
      361 aavsgwgkyt pytiseneig flvlhigvgl ersynigyqr qpkvllvcda gnamlrmiea
      421 vlarkypqie ivdtvtlrdy eqresisedf vistarvgek dkpvvmiapf ptdyqleqig
      481 klvlvdrtrp wmlnkffdaa hfrvidepmd qqtlfnvlcr qlqdegfvda efldsvvere
      541 aivstmlgds ialphalgll akktvvytil aprgiawgde tahvifllai skseyeeama
      601 iydifvtflr eramtrlcac rnfsefktva mecvsrf
//
LOCUS       WP_181637535             394 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Citrobacter freundii].
ACCESSION   WP_181637535
VERSION     WP_181637535.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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 11469162
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..394
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=46073
     Region          58..85
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          59..193
                     /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 msrlkgilnr awreskgfnk itniplailf vyfiesgksr alirlfslin psylpklsyy
       61 yiahayflsa nyekarnyle kltakfpsha daiyllcdid vlenrkkdaw eritllsetn
      121 lrlktwlvms nlvqdehefn hlydtwqrsi kktnlkpyhf dvngyiatga lraglyhkae
      181 eiwdeiieql lnnkpvaqnk fvsnkfssky gekallslkk vfdenninff lvsgtllgci
      241 resrllrhdk dadvgiwddq nhgvtenvlr ksglfyiqts rtphtirakh vngtaidifi
      301 hyrepenywh ggvklkwsnt pfkltkyqfl gqhfyipeny dlylkenygn wrvpkiefds
      361 sidtnnatii nqyemkvhek kklalsllaq skki
//
LOCUS       WP_181637677             579 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Pseudomonas aeruginosa].
ACCESSION   WP_181637677
VERSION     WP_181637677.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 579)
  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 579)
  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 579)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..579
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..579
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=63058
     Region          225..525
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 msavstslll flnlltpaqa aqpvpladgr ieiaagesrq ryldlapgel qlldlevdrg
       61 rvrlrattpd gkalratela grqslglqag erqglrltfs adedtaltli ptqrltpqtp
      121 aldspapqsp tlqrlqaela ekrpgalkaf wkqvakqgtp lvepldaerv lvtflwrqqr
      181 pgdvrllwpt pevntrrfea lagsdvryls lplrrdarvs yqlsadlpdl qqadrgtlrl
      241 alqaaarpdp lsrtpwlnsr alpraeqasl vqlggapaet wdqprkdvpr gkverlgyss
      301 qalanqrqlt lytppgydpe gqrypllvlf dedhyardvp tptildnlia agrirptlav
      361 ivgnvdassr grelpcneaf admlahellp wlqqryalse epadrvlsgs sygglasgci
      421 ayryperfgk vlslsgsfww gpdeqqpqwl vrqfaagerl plafflssgl leepeadgil
      481 gsnrslraal qgkgyplhyr efpgghdyaa wsvelaeglq allpgalsrl agvgriaacr
      541 yppcrglevg egcpgacpqc pprcgigknr pgpfasvgg
//
LOCUS       WP_181638486             274 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Kluyvera ascorbata].
ACCESSION   WP_181638486
VERSION     WP_181638486.1
KEYWORDS    RefSeq.
SOURCE      Kluyvera ascorbata
  ORGANISM  Kluyvera ascorbata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Kluyvera.
REFERENCE   1  (residues 1 to 274)
  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 274)
  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..274
                     /organism="Kluyvera ascorbata"
                     /db_xref="taxon:51288"
     Protein         1..274
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31871
     Region          1..205
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mpkvlivtrt knrtcfipra vgsilsqiys dwhhvivndg gnaceleqai spfrslykdr
       61 ltiinnvtsm gmetasnigi nssdskyiai hddddsweny fllemvnale fnnvdgvvch
      121 vsqcfeqite geikilskry ynpdlvscnq rklkyknqfm pisfvfsrea ylaiegfden
      181 flvcgdwdfh yrfikqyrik viskrlanyh irsgdvsdps saavnsvhkk elharyrqef
      241 fikhgiders llrdrlyevi iqrtiriimr lvhk
//
LOCUS       WP_181638786             414 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Sphingomonas
            chungangi].
ACCESSION   WP_181638786
VERSION     WP_181638786.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas chungangi
  ORGANISM  Sphingomonas chungangi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 414)
  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..414
                     /organism="Sphingomonas chungangi"
                     /db_xref="taxon:2683589"
     Protein         1..414
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=45910
     Region          4..400
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 msltrrfwvv ahrwagltla ifltiagitg allpfeesln yatrpslsra vpphpgaqpl
       61 davtiaerve ratggriayl plevprnham rmfiaaaphg palpydvvwa dpysgvarlt
      121 ytwggvrdgp enimpflyql hygyvagpwg mitfgiaali wtldcfvgfg ltlpvpqrta
      181 lrsplagwwr rwklawtvrr hvrghklnfd lhratglwlw plllvfawsg valtlpqver
      241 pvmqifgasd ryvppqrpqp ladppidrre aiaiglrelr tigmrrsftv sqpamlgyda
      301 gsgayalytr tsldavhagg rtilwldaas ghplhwddpi grtgadrlet wfemlhmadv
      361 fglpyrifvs tlglavttls vtgvliwlkk rsarlaasar grrltpqarp kvaa
//
LOCUS       WP_181635624             273 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Citrobacter sp. RHBSTW-00986].
ACCESSION   WP_181635624
VERSION     WP_181635624.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHBSTW-00986
  ORGANISM  Citrobacter sp. RHBSTW-00986
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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..273
                     /organism="Citrobacter sp. RHBSTW-00986"
                     /db_xref="taxon:2742675"
     Protein         1..273
                     /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=29248
     Region          57..273
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mhktiavllg sicllpvvah adqpatasae aenvktlffg hddrikvtdp tqspwdaigq
       61 letasgnlct atlisprlal taghclltpp kgkpdkaval rfvskkgvwr yeihgiegrv
      121 dpslgkrlka dgdgwivpss aapwdfglvv lryppsgitp lplfegdkaa ltaalktadr
      181 kvtqsgyped hlddlythqd cvvtgwaqnt vlshqcdtlp gdsgsplmlk tdtgwqligv
      241 qssapaakdr wradnraisv tgfrdkldel ane
//
LOCUS       WP_181639001             420 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_181639001
VERSION     WP_181639001.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=48875
     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 mgkltdiqir twirnnehfa grsdgnglyi cfpetysapf wrfrykmagk arvmligyys
       61 sislakarei akelsarval ghdvagekqe rkaealkkme eekhalrvse laaeyferqi
      121 lnrwkhpdil rrriekdinp nighlrieev kawhiddmlq kivqrgapti andvlrwtrr
      181 ifdfgikrhm lesnptssfe isdaggqeqs rerwlsreel mkffqampmt kgfsrqnelt
      241 mklllvfccr kmelcgarwe efdldeavwh lpaervkngd aidipiplpa lewlkelhqm
      301 scnsqwvlpa rkmqhrmiph iqestlpval skvksnlpdm pnftihdfrr tarshlaalg
      361 vdpvvaercl nhrikgvegi ynryqyfder kqalelwadl lvslergevy nvtpliksia
//
LOCUS       WP_181639165             324 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Pseudomonas sivasensis].
ACCESSION   WP_181639165
VERSION     WP_181639165.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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..324
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..324
                     /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=35188
     Region          1..316
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 msialnvitg flgsgkttll krllqgeslg dtallinefg dvgidhllve evapdtvllp
       61 sgciccsirg elkdallgll qrrergevpa fkrvilettg ladpapilat lnndvqlrgr
      121 fhiglvitlv dashaalqer lhpewlaqva aadrlllskt dlageceplr ahlralntgt
      181 pilnthdihs gdqlllgegl rsaepamevs rwqlhqttta thgaaqvcsl tfdqpldwvg
      241 fgvwlsmllr chgerilrvk gllnvnasna pivihgvqhc lhapvhlpaw pgtdrqsrlv
      301 filrgldpal lrrsfdvfsr rfag
//
LOCUS       WP_181639379             338 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas sivasensis].
ACCESSION   WP_181639379
VERSION     WP_181639379.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     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=36233
     Region          106..336
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mskrageder eaanaahelf llgqktvear avlaalqqql sdansrleds qhveqliean
       61 qqlvlailla qsvpvatpgm eeqlfqelre anaqlviaal gaqdlqatae raldqqkgil
      121 amvahelrnp ltpikliaer mvrlpsdqlp rmreliegqv qhisqlvddl ldvsrastgk
      181 lrincsevdm lrilnaavda cspvmiarkq qfdvelpdaa livngdpgrl aqilhnllan
      241 aakytpvggt ismtatvtak vlrisiadng igvtakalpf ifdpyvqdth aigfnvtglg
      301 igltvvrelv eahggkvtgm sdghgkgsef vvtlplvr
//
LOCUS       WP_181639463             240 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Pseudomonas].
ACCESSION   WP_181639463
VERSION     WP_181639463.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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="Pseudomonas"
                     /db_xref="taxon:286"
     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=26327
     Region          28..237
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mlfllrmllm glhfmlagvl gvllgicrpf npdnsrlcar lyalpamril rlnvkadvds
       61 lrnkpgtcvv ianhqsnydl fvvgtvvphr tvciakkslk wvplfgqlfw lagnvlidrg
      121 nahkarraml ttthtlqhkd tsiwvfpegt rnlgkgllpf kkgafhmaia agvpivqvcv
      181 snyvvhmkln rwnsgdvlir slppvptagl tandvpalmq acqaqmdaci aeldrevqsa
//
LOCUS       WP_181639480             452 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas sivasensis].
ACCESSION   WP_181639480
VERSION     WP_181639480.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 452)
  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 452)
  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 452)
  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 452)
  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 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   6  (residues 1 to 452)
  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..452
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..452
                     /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=49341
     Region          86..439
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mdkssthhps epqsraekiv efkrqktllk tgalqdaifn sayfssiatd ekgviqifnv
       61 gaermlgyaa vdvvnritpa disdpaelit raaalseeld tpitpgfeal vfkasrgied
      121 iyeltyirkd gsrlsamvsv talrnrndti igylligtdn tarkqeeaer kgferaleek
      181 nlelehanhm kseflatmsh elrtplnavi gfsealkdgl vgdmteiqre yigdiftsgq
      241 hllslindil dlskveagmm dlelepvela gllanslliv rekaalqriq lkldsqddlg
      301 tlildlrktk qivynllana vkfsahgsdv tlavrevsrd evglvagdwp vhgfalqpsa
      361 hrrflelsvs dsgigiapdd mgklfkafsq idsslarkfe gtglglamvk qltdlqggsv
      421 avasreglga rfvvwlplhr aaatveatwp ts
//
LOCUS       WP_181639735             231 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudomonas sivasensis].
ACCESSION   WP_181639735
VERSION     WP_181639735.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     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=24854
     Region          1..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mngqdddaal sqvagaiaep artkmlcalm dghartstem aviaevstst asahlarlkd
       61 dglitlhtqg rhryyslagp svaqaieglm visrnsakaf vpstptrlqf artcydhmag
      121 tlavtlhdhf ieagwltgnd syqlsahgek amvelgidva alrtqrrrfa cacldwsmrr
      181 phlagalgaa llqnavrrew vtqdldsral svtpkgrkal karfgttice p
//
LOCUS       WP_181639131             387 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Pseudomonas sivasensis].
ACCESSION   WP_181639131
VERSION     WP_181639131.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            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 sivasensis"
                     /db_xref="taxon:1880678"
     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=43784
     Region          1..387
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 miysygarny ysfregmdvs fklsnkvpsn fsqgrkaatv lgikganasg ktnilkclef
       61 laqfitesfg fdegeyigfd syfdnespsd fyidfelsgv ryfyelcatp nevvsevlyr
      121 klqrktlvfe rkglsivdrp selsaidlve lksnasvist vvkykikelh diflpiyeyf
      181 dnitgnvart svvpdermfk qgsassfyyk tpdafafake iikksdlgit divihknela
      241 agkteyfplf lhkvgntglt hylsayqqss gtmalfrrla mywvvltdgg vlvmdefdqn
      301 chpmllplll elftdkkinr qnaqfiftah nsdiiddlgk yrtilvskkd gesycyrldd
      361 ipgdlirndr siaalyregk iggvpil
//
LOCUS       WP_181639455             711 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Pseudomonas sivasensis].
ACCESSION   WP_181639455
VERSION     WP_181639455.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 711)
  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 711)
  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..711
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..711
                     /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=81630
     Region          158..>461
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mikvgkhrdk estidifkry gfeyreefse teiliftkks gffdnasivk lstsanseta
       61 vknlvkvgys vkehifsssi elefelfdgf fsidrskref kndyfkhiek iikaytmeld
      121 dykyrsapys knlvkqdsid sddiiaaisk dlssdgprli lieaaagfgk tctayeiakn
      181 isetqkqklv lfaelskdrq akifshvlnk evmrsfpslp selviqeikn griavildgf
      241 dellknhdee kqfeksqaml etigeilssn akvvlttrkt ailqgddfnn wieshsedfe
      301 fvryslhepe ikqwldasrl qqleergiri knisnpvllt ylqfipdelf qktvqqpdli
      361 ieryfnsmle reidrqalnm siedqkqlla glavdmvdrn ytkdareniv khflineaei
      421 idgirdsypv terptkdela nkfanhalld rsanddkigf indfvlgnfv snnisnsesn
      481 ewvgddifie sailassprs tifreglwek lnfvrasind qdrikfqsll ldrvdekykn
      541 sninnmrfes idlfytgtad scifyectfk dclinfenik ncffvccvfy dcssvknlps
      601 etnsfiscqq hgntnfqitk seqllpavag gdqvkkfile kfwpigkhsi afahrplsmf
      661 fgknthpsde veaaieelkr dgiiqdahrk swigidtshi aeitrilgrq g
//
LOCUS       WP_181639895             698 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas sivasensis].
ACCESSION   WP_181639895
VERSION     WP_181639895.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 698)
  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 698)
  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 698)
  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 698)
  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..698
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..698
                     /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=75022
     Region          17..682
                     /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 mligsystsl vvislcvail asytaldltg riatakgrav ylwmaggala mgvgvwsmhf
       61 igmlalrlpf algfdigita lslliavmss gfalwlvsqp rlpawqlvfg alvmgtgiat
      121 mhytgmaamr mtpgidydpt lfgaslliav vasgaalqia fnlrrntpyv rlarggaavv
      181 mgfaivgmhy tgmaaarfad esycaaaldg ltgkgldnlv lvttlavlai alltslldar
      241 leartavlad slslanqelt hlalhdmltg lpnrtlladr iqqaiqavne qggcfalmfi
      301 dldgfkpvnd afghhmgdql lrevglrlre dlrghdtlar iggdefvllv qlsqpddalr
      361 laerqvglin rsfqvaehel kisasigiav fpgnggnpqe llmnadaamy hakgmgkngy
      421 sffdvsmntn arkqlqllqd lrnaldqeqf rlyyqpkfda vsgiavgaea lvrwehpqqg
      481 lllpatfiel aektgliipi gewvlneacr qmsvwyalgy ehwriavnls alqfchaglv
      541 ksvadaldrh qlpansltle itettamsda dasmtvlqql sdmgvdlsid dfgtgysslm
      601 ylkrlpadel kidrgfvrdl ehdsddaaiv saivalgqal glrivaegve tdvqqsfltr
      661 lgcnslqgyl lghplpadgf madilraeda qapdknsa
//
LOCUS       WP_181639974             391 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudomonas sivasensis].
ACCESSION   WP_181639974
VERSION     WP_181639974.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..391
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41784
     Region          1..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 msgplaslkv ldfstllpgp faslmladmg aevlriespt rldmlrvlpp hdqgtsasha
       61 ylnrnkrslg ldlkqveale ivrtlvkdyd ivleqfrpgv merlglgyea lkainprliy
      121 vsitgygqtg pykdraghdi nylalagvas ytgrqdsgpl plgvqladvg ggslhavvgl
      181 laaviarqqs gvgqyldvsm tdcsfslnam agagylacga epeweghvln ggsfydyyrs
      241 rdgrwmsvgs lepafmqqlc ealgrpelaa qslkperqaa lkqalqvefe krsfaelcel
      301 fagvdacvep vltlseavah pqlkaralvs qvprgdgssq aqiacplkfs eglpaprhig
      361 vavgahsdev laelglsppr iselrsskvi m
//
LOCUS       WP_181638798             688 aa            linear   BCT 28-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Sphingomonas
            chungangi].
ACCESSION   WP_181638798
VERSION     WP_181638798.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas chungangi
  ORGANISM  Sphingomonas chungangi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 688)
  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 688)
  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 688)
  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 688)
  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 688)
  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..688
                     /organism="Sphingomonas chungangi"
                     /db_xref="taxon:2683589"
     Protein         1..688
                     /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=75527
     Region          9..683
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mhdispdgpi aypetardda ieelggrrfa dpwrwlegdv rtdervqawv aaevaltdsy
       61 ldtlpgriai rerltklwny ervslprrrg gryfflrnsg leaqavlcar eahdaparvl
      121 idpndwsedg atalgeweps ddgrrlaftv qdggsdwrvv rvldaiggdt lsdevrwvkf
      181 sglawasngs gffysrfpep ragmehqaqn ldhavyfhrl gtdqaadfqv yatpdrprli
      241 htaevsedgh wllissaegt earteltvid ltapklapki lvrglendwr lagskgdify
      301 fvtdleaprr rivsidvase mrrrreivph gedlvadall vgdrllvsvl rnvaselriy
      361 nldgrlmdtv vlpgigavtg megrgdssea ffaftsydrp teihrldags avalpyaqpq
      421 lqfdrdeyvv eqtsctskdg tviplfllrr kdvthaaptl lygyggfeis ltpgfssaal
      481 cwaamggvya vanirgggey gkawhdagrr askqnvfddf iaaaehlkte gvasgvvvhg
      541 hsnggllvaa vtnqrpdlft aalpavgvhd mtrfhrftag rywiddygdp gkeedlavlm
      601 ayspihnird gadypailia tadtddrvvp ahsfkyaaal qaanigpkph lirietragh
      661 gagkptakqi deiadlwafa akwsglaa
//
LOCUS       WP_181640151             342 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-nucleoside phosphorylase [Pseudomonas sivasensis].
ACCESSION   WP_181640151
VERSION     WP_181640151.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            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 10534769
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..342
                     /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=37712
     Region          37..340
                     /region_name="NUP"
                     /note="Purine nucleoside permease (NUP); pfam06516"
                     /db_xref="CDD:428985"
ORIGIN      
        1 mntftrlsma igiallphlv ladtpapikp kvmlitmfap eaqtwidrlq lkqevrvpgl
       61 saeypvircn tqdvcllvtg mgqtnaaast lalalspkfd lrqsyfliag iagispkhgt
      121 igtaawahyl vefgtqweld srdapkdwpt gyigintkgp nekppldykt evfelnpklq
      181 akafalsqkv elteskesta wrkhypaapa nqppqvtrcd tlagntwfsg trlseraevw
      241 tklltdnkge ycttqqedns tyeallrasr eglvdiqrla vvragsdfdr pypgysevdn
      301 llnyadqggf vpalenlyrt gnplvqailn nwsawekgvp da
//
LOCUS       WP_181640153             254 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Pseudomonas sivasensis].
ACCESSION   WP_181640153
VERSION     WP_181640153.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     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=27837
     Region          16..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          179..252
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 malaappdls dhavpvqpla rtyprgwyve phrhewgqll yamsgvmwve tprealvvpp
       61 qravwlppgv ehgirvvsdl qmrniylrpa laatldsqvq vievggllre livtlveegd
      121 scdgayydav vglallelqr arrsririam pveadrrlis acqavmaaps lvipfeqhae
      181 vagasvrtla rlfqnhlgmg faewrrqvql atavaeliqg qsvsgiarsl gyspssfsdm
      241 frrelgvaps hytg
//
LOCUS       WP_181640230             297 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Pseudomonas sivasensis].
ACCESSION   WP_181640230
VERSION     WP_181640230.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            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..297
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..297
                     /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=33368
     Region          17..296
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msatstvpta ipsaqdfevr plpgsvgaei igldlsrpvn dqdfarihra hldhhvvvfr
       61 dqritpeqqi afsrrfgvlq ihvlkqflla nhpeilivsn iiengqsigl gdagkfwhsd
      121 lsykelpslg smlhaqelps eggdtlfadm hkawdqlpeh lrkavegrsa ahsytaryse
      181 tkfegnwrpt ltpeqlaqva evvhpivrth pengrkalfv segfttrivg lpedesrdll
      241 aqlyahsvlp hniyrhqwqp hdlvfwdnrs lihlaagcps hlrrklfrtt iqgdapf
//
LOCUS       WP_181640243             141 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Pseudomonas sivasensis].
ACCESSION   WP_181640243
VERSION     WP_181640243.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 141)
  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..141
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..141
                     /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=15832
     Region          11..141
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrspgvmhcd teilvpffdv dtmnvvwhgh yvkylevarc alldkighny tamleagyaw
       61 pvidmqlryv rgavfgqtin vraslvewen rlkvnylitd lasgerltra ttvqvavema
      121 sremqlaspk vftdaveral a
//
LOCUS       WP_181640275             220 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudomonas sivasensis].
ACCESSION   WP_181640275
VERSION     WP_181640275.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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 10008106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     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: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=24208
     Region          29..>176
                     /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 mtpplnlqra lsaligdaql vpcplpgtel slwlldadnm drafspeetr rilheppyws
       61 fcwasglala rylaanpewv agkrvldfga gsgvaaiaav kagavevvac dldplalasc
      121 ranaelnnva ltyspdffae adrfdlilva dvlydranlp lldhflsrgr ealvadsrvr
      181 dfqhpayqrl eildaltlpd laepwefrkv slyhsrrqpl
//
LOCUS       WP_181640278             242 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas sivasensis].
ACCESSION   WP_181640278
VERSION     WP_181640278.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 242)
  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..242
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..242
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27517
     Region          39..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 mdvrhwlltl lcvipawvla qdesvvpgki mlaseawdgy tnadgsglaw dvlrqvfepv
       61 gitlhtriep ytrsvglaqr gevdgwvgsy rdevtgvlyp hwkldsdaiy alglatsptp
      121 svatlgeyrl awvrgyryea ylpnvrrfnq iqrrdgilpm lqhgradfyi dalsetqyvl
      181 kqardpstfr lthiidlply vgfadtergr slrtvydqrm avlvksgvlk pifqrwnlpy
      241 pf
//
LOCUS       WP_181640303             329 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Pseudomonas sivasensis].
ACCESSION   WP_181640303
VERSION     WP_181640303.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            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..329
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..329
                     /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=35310
     Region          1..323
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mnpfhyskpv dvqeavhlts gasrfiaggt nlldlmkeni srpehlidit glplhgieet
       61 adgglrigal vsnadlawhp lieeryplls qailagaspq lrnmastggn llqrtrcyyf
      121 ydatvpcnkr epgsgcpars glnrihailg asaqcvathp sdmcvalaal earvhvegrg
      181 garviefadf hrlpgdtpqr dnlladdeli taielpadhl arhshylkir drasyafalv
      241 svaaaleldg dtivdarlal ggvahkpwrd raaeaaligq tvsretfsna advllqdaep
      301 lehngfkikl arraiirals daavageqp
//
LOCUS       WP_181640545             308 aa            linear   BCT 28-DEC-2024
DEFINITION  FecR family protein [Pseudomonas sivasensis].
ACCESSION   WP_181640545
VERSION     WP_181640545.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            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 sivasensis"
                     /db_xref="taxon:1880678"
     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=32838
     Region          19..57
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          102..306
                     /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 mnifslsiar ksaasplhde ardwllllts gratvadaka lkawcaqsae haqafeqtkg
       61 lwqqlapale qpsaprqfgr raflgaaiaa saavvmvrvg vpggfsglta dyrtevgeqr
      121 qvllsdgvsl elntqtrisr vgqgielleg evevvahiaq plkiqagegw vsaaqarfnv
      181 rhtdhrvcvt ciegslsvdv ggnsvslgrg rqmsygaagv sdvitvdtqs vvawreqvlv
      241 fdnatlatvv deinryrpgm lvllnkelgq rrvqarfslq qlagvallir daygakctel
      301 pggvvlls
//
LOCUS       WP_181639465             268 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Pseudomonas sivasensis].
ACCESSION   WP_181639465
VERSION     WP_181639465.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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 268)
  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 268)
  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 268)
  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 268)
  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..268
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..268
                     /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=29265
     Region          88..264
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkpifallal llalpaaaaq ltieldhtrk twqtadllkh pdaqtvqivd dvsykrnmty
       61 ravplavllp gltpqshvqa valdgfaael taaplleqhg arawlavedp akpwpaladg
      121 khsagpfylv wtdpqaghis peqwpfqvst ikqlktvaer fpallpnpel aanapinqgf
      181 alfqknclac hrlngagdaq vgpdlnipys pteyfggdfl kryirdpqsl rhwpqakmpa
      241 faasvlpdse ldllvgylkh magrkqqp
//
LOCUS       WP_181640627             917 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-glucosidase [Pseudomonas sivasensis].
ACCESSION   WP_181640627
VERSION     WP_181640627.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 917)
  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 917)
  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 917)
  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 917)
  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 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 13307224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..917
                     /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=98702
     Region          13..846
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
     Region          50..394
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mnkrkmigaq safallalav sqvhaatspa ldegrvnrae ktadktlakm tmeeklayig
       61 gtggwdvkpl tqygipqihg adggvgvryt segnaqgvvy psgpnlaasw nprraidlgr
      121 algydtasgg yqfvtgpgvn lyrmpysgra feylsgedpf lgaslgpavi ngiqsrgvwa
      181 nakhfaandq esnrfhldei iservlremt lppfesaskn skvammmcaf qkvngefacq
      241 nkhlmrdilk tewgypgfvq sdynavvngl paaqagtdld mmgyqmnstv lkpfldsgel
      301 ssatiddkvr rilkqiylyk fdskapltsh nmnsatsnrv alnaaregiv llknqnnllp
      361 ldakkvktia vvgnlakyap ptgfgsanvm aanyiselsg lqqlapgakv efidglsldp
      421 tasnwthtds dgnsvkgvkt effnntnwsg dpaasrtdrh vdldwstdsl pvngdtaats
      481 irysgqitpt vsgeqvfkir adgavrlyvn gkkvldngdg kplpnnsipp tipvfakvnl
      541 eagkavdikl eysrrngyls tmgglvgvqm swaslvapqd lakydavlva agnsneyege
      601 gfdhsfdlpe fqgqliqsia kvnpntvvtl hggtglkmsd widqvpaalh afypgqnggq
      661 alaeillgkv npsaklpisi erniednpiy atfpkfdnqe tlaemsykdd lflgyrgyek
      721 kgikplypfg yglsyttfgy snisvtpgva vagapikvsf dlantgkvag aevaelyvgq
      781 nnpkveralk elkgykkvfl kpgeskrvti elndrslayy dvkskqwvvd adsfnlsvga
      841 ssqdirlnak lvnpfrqels tttsnplprs alnstlrelp qvktggvlhq negdsgtseg
      901 dgydmsddss qgsaagn
//
LOCUS       WP_181640635             228 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudomonas sivasensis].
ACCESSION   WP_181640635
VERSION     WP_181640635.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 228)
  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 228)
  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 228)
  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 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   5  (residues 1 to 228)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..228
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..228
                     /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=24256
     Region          7..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 meeapcisqi asllaepkrt amlwtlmdgs aksskelaal tglpsasana hlarltssgl
       61 lrtearygkr lfrladgdvs aaihalastt lasatrsapg vstqvlvapp slrrarlchg
      121 hlggelaaql yermmaarwi erheqrlavt fkgaqqmagl giftqalamp llcdcfdwsr
      181 qqphlggalg aglfqlflqs nwislvnesq avvvndvgle eiarlaal
//
LOCUS       WP_181640674             477 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Pseudomonas sivasensis].
ACCESSION   WP_181640674
VERSION     WP_181640674.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 477)
  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 477)
  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 477)
  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..477
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..477
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53031
     Region          22..>248
                     /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 mtrpapllll lagllfflal gnhelqgste arvsgiamam hldndwvvpq lfrepflekp
       61 plslwldaga irlfggtpga vrlasafagl fsvmllygml rrfgrpktla fcaalilatm
      121 asywgnvrgv gedsllslgv ttallafyqa mrpgregssa wawmlftagm viatlskgvl
      181 glalpgivif vyltsislmd krlrigewlk pgvftvlalv plmiwlgflf qrggmqavge
      241 vlwtnsvgrf sgsfveaghy epfyyyfakl pqaflpwnil vylglwhfrk slvrdryrlf
      301 fsvwlvaqft lltlasskrt vylmaltpaa avlaaeyagv llewlkvrkp alyryhrgvi
      361 igvfslamas yltaafwfap kadkresfvp visqarafqt egknvvmfqp neriagasvf
      421 ylqaylpilq teaelhsflt akpgnialld ntrqlsgkit vikemkigrq pyyfieq
//
LOCUS       WP_181640949             656 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Citrobacter
            freundii].
ACCESSION   WP_181640949
VERSION     WP_181640949.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
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="Citrobacter freundii"
                     /db_xref="taxon:546"
     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=73099
     Region          24..624
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mnfnksclyt alsfafahsa fagqesetmt vwsspasaat ttvlgletiq qldkqnvaqa
       61 lsvvpgvvlq ksgnrneqqv kvrgfdsrqv pvffdgvpvy ipydgnldlg rfltsdiasv
      121 evskgyssll qgpnqmggai nittkkptkp iegsigyrqg wsrskdnahd mhasfgasnd
      181 lgyiqlsgsq lkqdflglph gvdnpvagsh gkianssadd krgivklgft prgddeyvlt
      241 yinqdgekdn ppyagtssqk srywqwpqyd kesyyyqgtt hlgdrftlks rlyrdtfent
      301 lmmynsladl knkkgnyshy sdysdgaglq laadmrendl lsfavnwkdd vhrekgapna
      361 aydryedrtw svaseyqwaa adnvdvvagi sydwrdsleg mkhekngsvt hyddnnqstf
      421 nwqmmtkyhf enadtlalsy sdrtrfptlk eryttskpay nqvalvnpql kperarsvdl
      481 twngslsqnw gfeasvyynr isdailshni dadtiqnqns grvdytglda gvkgkvfdml
      541 dvglsyglih advkrsdigk itdlptqtlt awmtlkpwdp lsitlseear sssysnsdgs
      601 qkaagfaith lradyaighg fsvnasvnnl fdtqyvyseg fieegrnywa gieyqf
//
LOCUS       WP_181641423             128 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein, partial
            [Nocardioides massiliensis].
ACCESSION   WP_181641423
VERSION     WP_181641423.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 128)
  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 128)
  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 128)
  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 128)
  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 128)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..>128
                     /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]"
     Region          2..>124
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkvavtgatg vlgraavrdl vsaghdvfgl artagkaqll esydvtpvha dlfdrdslva
       61 mftgcdvvln lathvpvgsl rekawrehdr ilrwgaatva eaaeaagvrr lvqestssvy
      121 adhgdgwi
//
LOCUS       WP_181641341             654 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Citrobacter freundii].
ACCESSION   WP_181641341
VERSION     WP_181641341.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 654)
  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 654)
  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 654)
  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 654)
  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..654
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..654
                     /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=73832
     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 nrsalqaylk kmhtldaplg rlssgalnkd vnsinnanqk iqtlyyiysa tsvlliilsa
      181 ilgvlifyqn rnilrahlqv kslaeelqks keklqiqnak leydvyhdsl temnnrqlfw
      241 sdlnktieia eknhdsvtvm lfdldrfkev ndtyghdagd mllrqisdrl vsmsltsdtl
      301 yrlggdefaf lpsgltesha vsraqkicef isqpytiynt iinittcvgi visdterrsd
      361 ylykfadlal yeakgegsgk ikvfrqrmle klqesrtleh dmalaivnke fvvyyqpivd
      421 sfsqeiysye alirwlhplk gilspdnfip vaektgmine mgkvvleiac reaacwavpa
      481 kisvnvspvq lsskafvgiv lsilketglp adrlelevte sslftesttp mntlnklral
      541 gvkisiddfg tgysslsrls klafdkikid ksfvhsisth edalniikli tgmakslnmk
      601 avaegvetke qlkslqalgc dfaqgylfgk pqpcvneeir ngqvvpinnr ktmp
//
LOCUS       WP_181641461             436 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Nocardioides massiliensis].
ACCESSION   WP_181641461
VERSION     WP_181641461.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 436)
  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 436)
  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 436)
  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 436)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..436
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..436
                     /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=45910
     Region          65..171
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mpsrvsvgtr ahrllvatta lttllatllt algaapppag aapgpaytvp aaerraalac
       61 agdpatsqat pvvlvhgtgv taqenwgaty vpdlrragha vctvdlpqqs lgdvqrsaei
      121 vahavravsr rakgrkislv gqsqgafhaf fvvrvwpdla arlddvigls gvydagsaai
      181 rddcrdgcsp afhqiaagsr llrllarrpl pagpdyttvg tladatitpq paanhqpgat
      241 qvqiqdvcpg rrspvpdtdh vlmagdavah alvrdalrhp gparrtrvpa stcllpvfag
      301 vdllgfalsl ptmltrerpe taseprvrcf lrpgctdlre rgrvvrsvdv rrgpraavlr
      361 lvvqapgavr vsvggrhrvh rvargtttvr vpvppggaar vrlqgrpdgf arwvtervlr
      421 vpratanvsm sristr
//
LOCUS       WP_181641655             244 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nocardioides massiliensis].
ACCESSION   WP_181641655
VERSION     WP_181641655.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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..244
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..244
                     /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=26862
     Region          41..198
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mraatphhel pdwlipvrea ldtitghdlt rflpppdadp rrsavlmlfg ecdsgpdlll
       61 terahhmrsh pgqvsfpgga mdptdldllh talreaeeev gvdpagvevv gllpelwipp
      121 snhavtpvig wwreecpvav vdpdevhavl rvpvaelldp ahrirvrhps gwlgpgflig
      181 ddkdlilwgf tagliarlfd yvgmtrpwed saavhdlpph mlavpegaae rirraeallr
      241 eerp
//
LOCUS       WP_181640702             219 aa            linear   BCT 28-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Pseudomonas
            sivasensis].
ACCESSION   WP_181640702
VERSION     WP_181640702.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 219)
  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 219)
  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..219
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..219
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=24596
     Region          <12..137
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 metylspsrf idsdhpavve faekhrgtra dltdqavsly yavreavryn pytfsrdpdt
       61 lnasyalatr esycvpkatl laacarhygi parigladvr nhlstprlla llksdvfamh
      121 gytelhlngg wvkatpafnq qlcavfdvpp lefdglndsv fhafnrqgqr smeyvvdhgq
      181 fadvpehlff thiqkcyphl fvedmpnllg dmqsdlsrg
//
LOCUS       WP_181641799             145 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardioides massiliensis].
ACCESSION   WP_181641799
VERSION     WP_181641799.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 145)
  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 145)
  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 145)
  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 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   5  (residues 1 to 145)
  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 145)
  AUTHORS   Rosinski,J.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..145
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..145
                     /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=15983
     Region          50..127
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(55..56,60..62,76..78,87..90,92..93,96..97,99..100,
                     106..108,113..115)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mdkdkdsvrt qddnpepvts agdrhqhpvd ptrvamarer lpsaeegdrl tsvlslmadp
       61 trarllyald vveelcvgdl alalsvseda vsyglrvlrt aglvarrkeg rivyyrlaeg
      121 fpeplrqhcl rqliemsraa vdddg
//
LOCUS       WP_181641847             511 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardioides massiliensis].
ACCESSION   WP_181641847
VERSION     WP_181641847.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
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="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     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=55710
     Region          142..495
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mttdpsages spaggwrarl trwgafsvrt ritvafvava alalfsagff vytievraie
       61 rdvrdqirqe laefrtlses dpppadvdtg apistadqlv rvfltrnvpd ddelllgyag
      121 gsprvisptr yaaeyrdtst glqaqlrqta epllqsggte rihhadlgei vltvqpvdyq
      181 gspgalvian flgdeyseld sfirtyiils llmlgaiavl ssfqagrllr pvrtlretaq
      241 slgatdlsrr ipeqgnddit dltrtvnqml drlerafrtq reflddaghe lktpltimsg
      301 hlelldphdp edvaatrdll ldetdrmsrl vrelmllakl drpdfldpre vdvaplttrv
      361 wekcrglger gwvldaaaev talldeqrit qamvqlaqna tkhtedgavi gigsayadgd
      421 vtfwvrdtgp gvrpedreti ferfgrgria agddgfglgl sivhgiatah ggtlavgdeh
      481 phgarftltl pvadatasps prkedpswpa s
//
LOCUS       WP_181640116            1059 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Pseudomonas sivasensis].
ACCESSION   WP_181640116
VERSION     WP_181640116.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 1059)
  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 1059)
  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 1059)
  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 1059)
  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..1059
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..1059
                     /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=115153
     Region          2..1033
                     /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 mstaqqgtvd aglallveqq qhldarqqga swgdlthclk ldirgeldpv rlqhaldsla
       61 vrhealsaqf apvsgyhglr qrvapaeavs ltqwldvasp qqviarqqqw lqqqqpliga
      121 llqrletdhw qlligvsrya adagtlaliq qellaaygqq gfeedepgqf sqylewrsev
      181 ifdedadtak aywqqylqgh egllsgpdlp yrltcaevlp aerlsvpldq sllarlrttg
      241 lpldvlmhaa wwvllarisg resflagwrh darldyeffs hslglfektl plairidpas
      301 tfrelvttla aqldqhrtwq eywtplsfpq qaapavgfgn rwvsepreva gmvwvgsdlp
      361 arlpefelal qleiaasgep qglsldfnpa rytapavetl lgqlrellhs iadkpdetla
      421 rlnllgadek srllalnppa qimqtpqllp qriaawadqt pdavalvaag qalsyaelda
      481 rtarlsaell rqgvgagsiv glalprsael vvailatwra gaaylpldpq wpvarqaeia
      541 rhaaaslilv thapgqddpl safkllnpga stqdastapa vsvqardvay vlftsgstgq
      601 pkgvviehga llnytasssq qlglsacrhv afsstvaadl gntalfgaly ngatlhiadd
      661 atlqdpqgfa gflrensidc lkivpshlaa lleadtavlp dtlvlggeai gaslvqrirq
      721 lrpdcrvfnh ygpteatvgv mvhpllpaed vshgvplthv lpgnqvfvlg adaqllatge
      781 lgelfigghq lcrgylqgea dadafihspl vdgerlyrtg dlaryrvegg vqlygrrdhq
      841 vkvrgfriel aeieaqllrl pevseavvvl vqeepqafvv mraataedvg pqlknqlaqh
      901 lpaamvprqi vslermprlp ngkvdrkalq haqpvvslav yvaprdalet llstrmaqlv
      961 glerlsieed ffaagghsll viklvagirk llqceihpgv vfdhprvaal arelreretv
     1021 agqleriaqa rlrmdamtpd ekaalmekar qlqaskeqg
//
LOCUS       WP_181642035             440 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Nocardioides massiliensis].
ACCESSION   WP_181642035
VERSION     WP_181642035.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
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="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     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=45965
     Region          196..423
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mpslravspa rrragvavia tsvlavviga atalepvlvl glvvacttvv vmtlrietav
       61 lvyiavepfs gyltqvssia vklvglivfv awvlrlatdd rpptarhpvt yaagglvlvv
      121 laalvihpng mtglvvatry vsyvavlivl vdtlrnrldp wllgrtlvls stvaavvgii
      181 vfvnenggra agpiedandf alhllcalpf alalgrrsga hralwataav ilvvaiaatf
      241 srggllglgv mlilalalqv lrwrtamigl avvavavlva lvvapdlmqr sldekqhvas
      301 anvtsrfvgw tlaaemtada pvlgkgpggy svhydeylgs rvsdpphldv ahqmfldvas
      361 elglvglgvf aamilaglta awrarstpgp epdrrllatt vcvafagvlt gamflssqyy
      421 lpvwlllala aaltparrsr
//
LOCUS       WP_181642047             424 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nocardioides
            massiliensis].
ACCESSION   WP_181642047
VERSION     WP_181642047.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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..424
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..424
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45401
     Region          8..306
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtrpavgera qalvdrlqag grlpslvlgv lrdgelawsg gagdlvgpve qtryrigsit
       61 ktlvavailr lrdaglldld dplrrhldaa aygevtvrql lahtgglqse pvgpwwersp
      121 gvdrdrllaa ndgsgavtap gswfhysnlg hallgavlee vrgrgwwevv aaevlaplgm
      181 dttsydacap haqgysvdhf lgttleephh atgamapagq awstiadlar warflslghp
      241 dvlaettlae marrqppapa yglgvrlldv dgrtwvghtg smpgflascf vdrtngdgvv
      301 alanatiglp tadlprllce dpaagscepw rpttvvpplv aelaglwfwg ttavelrwsn
      361 drlelrtlan gvhsdtfvla edgavrgveg yhrgevlqah rdptgrvehl ecatfrytrt
      421 pygr
//
LOCUS       WP_181642106             169 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase, partial [Nocardioides
            massiliensis].
ACCESSION   WP_181642106
VERSION     WP_181642106.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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 169)
  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 169)
  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 169)
  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 169)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..>169
                     /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]"
     Region          1..>160
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msgtalvtga srgigrqval alaragydva ftartlregd gtvpprtare aaagagplgv
       61 pgslesvaae irahgvqalp vpmdltdlas vraaatqvte awghvdvlvn nailhvphar
      121 vleldldalr asleanhvhq lalvqallpr mvergsglvv glwsgsvvn
//
LOCUS       WP_181641967             215 aa            linear   BCT 28-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Nocardioides
            massiliensis].
ACCESSION   WP_181641967
VERSION     WP_181641967.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 215)
  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 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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..215
                     /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=21663
     Region          <10..162
                     /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 mtsalrtscr aslmavlval illvasspaa gfgepastdg vwpldprpev vkgfdppavt
       61 wgaghrgvdl rgyvgqpvra alggtisyag mlagrgvvvv dhggrrttye pvdvevsvgd
      121 vvarggrlgt laptpghcap lyclhwglih ttftgdeyvd pltlvgggpv rlvpwdglps
      181 trgfgpsgpa pssalaaaal pvesgarvgl tvgla
//
LOCUS       WP_181642195             213 aa            linear   BCT 28-DEC-2024
DEFINITION  Na(+)/H(+) antiporter subunit B, partial [Nocardioides
            massiliensis].
ACCESSION   WP_181642195
VERSION     WP_181642195.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            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 10003971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..>213
                     /product="Na(+)/H(+) antiporter subunit B"
     Region          <31..>59
                     /region_name="COG1563"
                     /note="Uncharacterized MnhB-related membrane protein
                     [General function prediction only]"
                     /db_xref="CDD:441171"
ORIGIN      
        1 mtgtagvidv alagavlvva vaavalprrp aavtaflvfg illavlwarl gapdvalaea
       61 algggvagal lvdalssppa pgvrrrsgwl vgaaalagav vvgtlvaivr tlpdsagpvp
      121 alvdqeiges gathpttavl lnfrsydtll eiavlvvvvv aasgvahgta pvlgppppvl
      181 htlavlllpv lvllagwllv agttrpggaf qag
//
LOCUS       WP_181641151             709 aa            linear   BCT 28-DEC-2024
DEFINITION  GumC family protein [Citrobacter freundii].
ACCESSION   WP_181641151
VERSION     WP_181641151.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            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 freundii"
                     /db_xref="taxon:546"
     Protein         1..709
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78086
     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 ivayplismm sskyvstatv
       61 likaqadnvs pfpqvdgfds trsgyyetqy almhsrivle kairdmklde npeftgekag
      121 argadsnesr qlrmeqalkt laknlnvigi rttnlasity estspqvaad iangvaqafi
      181 nytveqkrlk vekarelnfe kmeeiqksia kqkdemdnyl knaglltfrg idgfeteqls
      241 ivtnrladat qrrvaaesvy nevngggksi esvislpsvs nhaqiqdlri aliqaqrtls
      301 eqrkvygpkn pailkaeadv qsiqnqtgrv lgelkvglrq qylaalaaek nyqqqvteqk
      361 eifqkmaskr dawnsqklsl dkmedlyksl yqrtqelsls gvnadavlyd pavpalkpak
      421 pnksllllmv vmlvvvfsim yfivkaamdn sigtlsrmkk rlnvaplgei rrfsgtsgra
      481 qvrdmimknp lnadivhgir trimldnrpl qtlavasteh gdgrsllanl lansfsfdqk
      541 tllidadffn tdglsselss atsaglaell rgevqlekar itlsdhldfi phgkttissl
      601 lmlssghvep lmrelkshyq riiidvaavn qsqdvqlikr avdgvifivk agtgsagqia
      661 naldkleenn gvvigavlna veekdletqe glrslnfstd qlmttpgrv
//
LOCUS       WP_181642339             437 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter freundii].
ACCESSION   WP_181642339
VERSION     WP_181642339.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 437)
  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 437)
  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 437)
  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..437
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..437
                     /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=49256
     Region          14..417
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mdkvtyptgv enhggtlriw fnfkgkrvre slgvpdtskn rkiagelrts vcfairtgtf
       61 dyatqfpdsp nlkafgvskk ditvkeleek wldlkrmeic anafnryesv arnmvprlgg
      121 nrlvsavtke ellylrkdll tgyqnptknk fpakgrsvvt vnyymttmag mfqfaadhgy
      181 levnpfegik plkkaraepd plsrdefirl idacrhqqtk nlwslavytg mrhgelvsla
      241 wedidlkagt itvrrnytkl geftlpktea stdrvvhliq paisilknqa emtrlgrqhh
      301 ievqlreygr svnhectfvf nphvvrrskq vgfiyrvdsv gdsweaalkr agirhrkayq
      361 srhtyacwsl saganpsfia sqmghasaqm vfnvygawma dssaeqiaml nqkladfapl
      421 mphshesstg gllksvs
//
LOCUS       WP_181641797             162 aa            linear   BCT 28-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Nocardioides massiliensis].
ACCESSION   WP_181641797
VERSION     WP_181641797.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 162)
  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 162)
  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..162
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..162
                     /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=16949
     Region          34..155
                     /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 mpsppaspcs dgdaapsrts rrhrartare qapvfaavav gggigavary aagvtwptya
       61 gafpwttlai ngvgcavigv fmvlitdvwt phrlvrpffg tgvlggfttf styaikvqrs
      121 vdeghallgl tymmttplva laavwssaav trrllmtrrs sp
//
LOCUS       WP_181642439             125 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nocardioides massiliensis].
ACCESSION   WP_181642439
VERSION     WP_181642439.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 125)
  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..125
                     /organism="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     Protein         1..125
                     /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=13426
     Region          1..115
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mdivqihfas yfrwmdmays rllddlghpl railaggrgt pvvdaqcsyl spvglgdvvd
       61 vdsrvvrhgr ssyvvrhdfe hagrpvatge vthvwavqdg sgamsepvpd wiraashstg
      121 agart
//
LOCUS       WP_181642537             381 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardioides massiliensis].
ACCESSION   WP_181642537
VERSION     WP_181642537.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides massiliensis
  ORGANISM  Nocardioides massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
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="Nocardioides massiliensis"
                     /db_xref="taxon:1325935"
     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=38095
     Region          60..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 mgptgttprg svvpavdpaa apatdadetg dllgiaarrr rfvgwaggll vvligsvllg
       61 vawgsvslap gvvagvladr sgfpvevtwa psvdaivwqv rlprvllgva vgaglavcgv
      121 alqamvrnvl adpyllgins gassgaaaai lfgfaaglgq halsvsaflg amaasalvyg
      181 iarsggqvta vrlllagvvv gyalyattsf lifasgsaeg arsvlfwllg slglaqwgsp
      241 lvvvlvvval tvvllmlssr qldllmigda taralgtsaa aartrllllv slcigvvvaa
      301 agsigfvglv vphlarravg akhayvvpva almgaillvw adivartlla pqeipigiit
      361 slvgapflli lvrrlhasat g
//
LOCUS       WP_181642822             160 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas].
ACCESSION   WP_181642822
VERSION     WP_181642822.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 160)
  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 160)
  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 160)
  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 160)
  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..160
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..160
                     /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=17672
     Region          83..>152
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtayyqllrr dltaglpapq wtagtvldhy rdalapaiha vlrmtqdqgg grvanldewr
       61 qqfvtdaefd ptlclvasna dgilgvaqcw tsafiknlsi hpcaqgqglg ralllhtfqv
      121 fkqrgepyvd lkvlesnlra rqlyesagmv fvlrdvveed
//
LOCUS       WP_181642837             174 aa            linear   BCT 28-DEC-2024
DEFINITION  KdsC family phosphatase [Pseudomonas sivasensis].
ACCESSION   WP_181642837
VERSION     WP_181642837.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     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=18810
     Region          5..174
                     /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 mtsdllqrgk nirlaifdvd gvltdgrlyf ledgsefktf ntldgqgikm lmaagvqtai
       61 isgrktpvve rraqnlgiph lyqgredklv vldellgqln lsyeqvaylg ddlpdlpvir
      121 rvglgmavan aaafvrehah gitcarggeg aarefcelil raqssleaah aayl
//
LOCUS       WP_181642874             423 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SAM-dependent methyltransferase [Pseudomonas].
ACCESSION   WP_181642874
VERSION     WP_181642874.1
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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..423
                     /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=47585
     Region          139..405
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mkspslsvkt srlnvngvts allrkgvlrq lsqlrhgqlv viedgerqvf gareahllge
       61 iqildpavwg lvaangsiga geafihgyws spdltavvrv mvsnldvlda megglarlar
      121 pftqglhwln rntrkgsqkn iaahydlgnd lfeefldptm mysaaqflsd ddtleqaqln
      181 klericqkla lkptdhllei gtgwgsmaly aaqhygckvt tttlskeqfa ytekrietlg
      241 lqgkvtllls dyrdltgqyd klvsiemiea vghrflptyf kqcahllksd glmllqaiti
      301 reqrfeqakn svdfiqryif pggalpsvqn mlqivsrdtd mnllhmedfg lhyartlrlw
      361 henfrrahgr ltelgydeyf lrlwefylcy ceggfmerti gtaqlllakp aainppllgr
      421 fna
//
LOCUS       WP_181642918             632 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PhoX family protein [Pseudomonas].
ACCESSION   WP_181642918
VERSION     WP_181642918.1
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 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..632
                     /product="PhoX family protein"
                     /calculated_mol_wt=68027
     Region          18..626
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mslleenqat dleqmvgltr rrfigagalc gaamflggnl lsrsalavna asaspllgfa
       61 siaaatsdti tlppgysasv liswgqplhk sapafdpsgn gtakaqeqqf gdnndgmslf
      121 afpgddnral mainneytny rylyahggap qsaedvhkaq asegvsviev rrkgdtwqfv
      181 qdsrynrrih gnspirlsgp aaghdwlkts adksgkkalg tfqncangkt pwgtyltcee
      241 nftdcfgssn pqqtfdtaqk rygvvaaskd inwhqhdprf dlaknpneln rhgwvveidp
      301 fdpqstpakr talgrfkhen aalaetrdgr avvymgdder gefiykfvsr dkinhknpka
      361 nkdlldhgtl yvaifdagng dadhpkgkgq wvelthgkng idassgfanq aevliharla
      421 asvvkatrmd rpewivvspt dgqvyctltn nakrgedgqp vggpnprekn vygqilrwka
      481 naddhgaadf swdlfvvagn pgvhagkpkg gssninpqnm fnspdglgfd kagrlwiltd
      541 gdysnagdfa gmgnnqmlca dpvtgeirrf mvgpvacevt gisfspdqkt lfvgiqhpge
      601 tggstwpehl pngkprssvi airrddggiv ga
//
LOCUS       WP_181642948             701 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Pseudomonas].
ACCESSION   WP_181642948
VERSION     WP_181642948.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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="Pseudomonas"
                     /db_xref="taxon:286"
     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=78200
     Region          28..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 mecapphgdg ssvllvvddy penlismral lqrddwqvvt aesglealev llqhevdlvl
       61 ldvmmpgmdg fevarlmrgn qrtrmtpiif lsanaqspaa vlegyasgai dylfkpfdph
      121 ilkpkvqall ehqrirralq rlshdlesar afnasvldna aegilvvsee gvieyanpai
      181 srllnapiqe lqgqeflsfm qkphvptwld sqmyagyrkg etwrlhdall rtgrgqqvpa
      241 alscaplpae qkamvvtvld msevrhlhqq lefqavtdpl tgllnrrgfh qaventllrs
      301 erteqslvll yldldgfkrv ndslghdagd rvlrwvseql qgglrsydii grmggdefta
      361 llelefpeqa akiseklier vsvcqqvdgl dvmlgvsigi atfpdcgsdl ngllraadia
      421 myeakragrq qyryydqemn grarsrlmle dsvrtaiqnk dftlvyqpqv sladgrlrgv
      481 eallrwqhps vgdvppglfl plleearlis qlsawiyqqv aaqrqvwqst fddelvlsvs
      541 lsssqfnmpn lanqlqqvme rhglqagqle veigedclms sleeatkqlk llrrigvria
      601 lddfgsgqcs lahlrdlefd tlkldpqlva rlpgsvrdaa marsiielcg hfdvlvvaeg
      661 vetqeqaqwl kahgcpfiqg pwaahplmad evvdwsrarl r
//
LOCUS       WP_181643187             292 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_181643187
VERSION     WP_181643187.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..292
                     /product="helix-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=32929
     Region          13..255
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 midlseysqa qrerlvyidf rlyftgavsr adlmdrfgvg aaaatrdfaq ykdvapqnte
       61 ldtvtkqyvm retfspliah aservltals qgfgygldsy ekpliphesv sllskpkvev
      121 lapitraihl krvvkisyts gsgqsertiv pfaigcdglr whvrafdrkr kkfadfvltr
      181 vghaelqmge kagdeetpkh ddqwnrmlel pivphpdkds teivkrdydm ldgvlklrvr
      241 aamagyvlqq yhvdcspdhs iadkayrlwl qdplalygve ssmfapgyks pk
//
LOCUS       WP_181643188            1447 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NACHT domain-containing protein [Pseudomonas].
ACCESSION   WP_181643188
VERSION     WP_181643188.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 1447)
  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 1447)
  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..1447
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..1447
                     /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=163336
     Region          46..748
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mtmhsddfid ldrtfskipl nadlsddvdl sgrhqsrgel hwtdllnhhr villseagsg
       61 ktaeiqnvtr qlrsagknaf flrienvypd ledaieegtf defkswldsg tegwlfmdsv
      121 dearlkdprd ferairklgr ltkssgaqah ilitgrstaw rpstdlaick tafefeakar
      181 ravpiqtdal esavqtttte aepdtsflvv tlddihdaqi drflkatgvq dvkafltave
      241 rkeawslttr pldfmelvgf whkhqrigtr lelmkssidr rleerdqnra efspiapekl
      301 regarliaaa atfgqisvis vpdgdaskkg ipiravlrdw ddadagalla rpifepgiyg
      361 tvrfhhrtvr eyltaewlhe lirgagsrvr ienlffrtqy glevinpsmr pvlpwlalld
      421 erickrlekv apevffeggd pgqlplstrr rvlrkacehl aqpahswtmt dysavqrfah
      481 hdltedikel ltlyrtnddi awfllrmvwq gevvgalaet kqfalnaqhk htrlaairav
      541 tdlgtaqdva dvrlallagk lkvnrewlae lldgftldtq wlpwllqaie ksakkerysg
      601 rdalalklsa latvcslenl palicglrvl ldkppmedhg fsviskkysw laeiagtavl
      661 rllqvrdpfv leepalails klaqahiyge ldtrelgeel reivptwpel dyklfwydvv
      721 larnglvhrg epvvnvwqll gfrpfwslnr qnfslacdhi esltnmddrl malsmafniy
      781 tqyeeptcwe sqlkqaaeah vvlrekleil lnpperdvdk weikqaqwke eaakrkaeet
      841 errrswregl aaevtlinsp kpgvmtrsqs ylierlldgs tssntwssgn wqslitefgl
      901 piaqmfrsga vnfwrgycpt lpsegapans tpyqvilglt glaiearees lsftqmsadn
      961 aeyaaryall elngfpewfp nlfrlypsvi reivmrevnh eldplrlgsg gnrilqrlrw
     1021 sgdwmygelv apllilleqq isdleslqlv lsivqnssvh dgvlaelsrk raleeanldi
     1081 aptwyavwig tepalaipal asridslsld eekakfamlc liaivgnrts srcrqnyktv
     1141 ghakslyllm htyiriaddi dragtgvysp glrddaqgar dgllaliret pgkeaflalq
     1201 eiaqahpaep lrpwgafyah qkatadsqts pwepakvvef heslestpst hrelwnlaid
     1261 rlldlkhdle dgdssyaeil lltnqetsir kfigkwlrdr avgryvvpqe eqladdkrpd
     1321 yrfqnsqtya pvpvelklsq nwsgpehfer ienqlcgdyl rdvssscgif llvnnggqva
     1381 wdspnngrig fedlvialqe hwlaiaskfp nvedikvigi dltkrggvta tkaikanqae
     1441 asqrgeg
//
LOCUS       WP_181643207             298 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein, partial [Pseudomonas
            sivasensis].
ACCESSION   WP_181643207
VERSION     WP_181643207.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         <1..298
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          18..298
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 ttttqpklia dsavfigala vpdappasge hplivlshgy ggnwgkqtwl asalahqgyi
       61 vaavnhpgtt tkdrspqaaa qlwqrpadls raidavldqp tqfgavankq iaavghslgg
      121 wtvleiagar fdpdlfakec stypklggci gyhemnpaat pegkaklaad lsdkrvtaiv
      181 sldlglsrgf tdaslaalpv palviaggvp tedmapeles admvrrmaka stqyveiada
      241 thfsfmsick pgaialiees spgdgmicrd gegarargvi qqqvvglitg flsrsfrn
//
LOCUS       WP_181643575             231 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Pseudomonas].
ACCESSION   WP_181643575
VERSION     WP_181643575.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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="Pseudomonas"
                     /db_xref="taxon:286"
     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=24895
     Region          1..90
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mngqdddval sqvagaiaep artkmlcalm dghartstem aviaevstst asahlarlkd
       61 dglitlhtqg rhryyslagp svaqaieglm visrnsakaf vpstptrlqf artcydhmag
      121 tlavtlhdhf ieagwltgnd syqlsahgek amvelgidva alrtqrrrfa cacldwsmrr
      181 phlagalgaa llqnavrrew viqdldsral svtpkgrkal karfgttice p
//
LOCUS       WP_181643688             260 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Pseudomonas].
ACCESSION   WP_181643688
VERSION     WP_181643688.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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="Pseudomonas"
                     /db_xref="taxon:286"
     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=28710
     Region          5..219
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mhkypvsisl ssygadlvrq qgqlsfvqll aaagaqriew reelltgena aelaqaaaek
       61 gleavfsspl elwvagraqp naelnatldr aqafgahwlk vslgyftdtn dleslhalln
      121 rhpvhllven dqtlhggrie pmqrffteve rlglpvkmtf dignwqwqdq saltaarllg
      181 rhvdylhcka varrpdgklv alppgatdlh lweqllkhmt qgitravefp lqgddlidvt
      241 aqqvatlall gqprqenahv
//
LOCUS       WP_181643752             251 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [Pseudomonas].
ACCESSION   WP_181643752
VERSION     WP_181643752.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..251
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27502
     Region          13..238
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtarsetisi diddeqmsgt flspkskvpg vlfvhgwggs qerdlerakg iaglgcvclt
       61 fdlrghagng iplnrvtred nlrdllaayd rllahpaidt savavvgtsy ggylaailts
      121 lrpvrwlalr vpalyrdqew lkpkrdldkv dlmdyrstlv haetnralha caaftgdvli
      181 vesetddhvp hatimsyraa cqqthslthr iidgadhsls dpvsqqayts ilvdwitemv
      241 vgerlsilqs q
//
LOCUS       WP_181643888             468 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Pseudomonas].
ACCESSION   WP_181643888
VERSION     WP_181643888.1
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..468
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     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=51820
     Region          29..406
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpawrnislw mdqlddplva rptlehdldv dvaiigagyt glwtayylkr qapelkiaii
       61 eaqtagfgas grnggwlmgn llgedrllag lapeqrrasf dllhsipdev ahvlasegid
      121 cdyrkggaly caarypeqes slrayldkly aqglteadyr wltpqqlaeq iriakpyggi
      181 yaphvatihp aklvrglara vermgvtiye kspvtqwqsg slctdkasvr aawvvpaveg
      241 yantlpplgr yqlpvqsliv ateplpastw deiglrhgqa fgessrqvty gqrtadnrlv
      301 fgarggyqfa gklrhnfdlt dsevelrryl fgelfpqlkn vrithswggn lgmsrhfrph
      361 mlcdhttgia lsggyggegv gatnlggrtl adlilrrdtp ltyqpwvire rgldalkawe
      421 pepcrwlgyn aiirsfvhed qvlanpntap wrrklatgla gfmegfmh
//
LOCUS       WP_181643941             270 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudomonas sivasensis].
ACCESSION   WP_181643941
VERSION     WP_181643941.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     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=29508
     Region          46..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 mdmpsaqqai asnkdawdqs aglhkttdtw salltgvgna dfscldptit gvlqdlgvag
       61 kdvvqlgcnn sreslslfal garsvvgvdq saaflrqare ladvsphape fiesdihqlp
      121 qrlherfdia lvtigvlgwm pdvalfmrhv astlkpggsl vmyethpfle vfdpraqkpl
      181 lpassyfqre pfvlqesivy egqgevvgpt sywyvhtlgd vvsaaicadl qishlqeyah
      241 snreelydqy ehqaaqlplc ftltatkrpa
//
LOCUS       WP_181644018             405 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Pseudomonas].
ACCESSION   WP_181644018
VERSION     WP_181644018.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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..405
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..405
                     /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=45182
     Region          167..303
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
     Site            order(199..205,228..229,254..256,270)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 msvtaqpvrp apdhhaqfie llstslaqna fiklvlakyv gdeaelqrli ikvvtvkeqp
       61 clsfvyrykt rditknlpla dgvaaiaell pasfknahll sltdeaqley skknksslfk
      121 skpqqlreap saehnreknr fldlsrpfla dlgvtdakqa lipsmsrkwk qinkfievfs
      181 haltssplkl dqpvrvadfg sgkgyltfai hdylrntlka egevtgvelr edmvtlcnta
      241 aarlehpglv fkcgdvrsva pseldvmial hacdiatdya ihtgirsgas iimcspcchk
      301 qirlqiqspv llkpmlqygl hlgqqaemvt dslralflea cgyetkvfef islehtnknk
      361 milavkrnep vdntqlleki qelkafyhit ehcletllra dgyla
//
LOCUS       WP_181643115             259 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SIR2 family NAD-dependent protein deacylase
            [Pseudomonas].
ACCESSION   WP_181643115
VERSION     WP_181643115.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 259)
  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..259
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..259
                     /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=28400
     Region          1..248
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mtdyeqavka lieakkivis tgagisqesg iptyrdgltg lwaghnpqyl etanafrenp
       61 qlvwgwylwr rqqvarakpn aghialhqma tlgrkvsiit qniddlheka gskevlhlhg
      121 slatpkcfac hrpaalspdn vhvtdfgali epprckkcng klrpgvvwyg eelpkgawkt
      181 amslikdcdv lvsvgtsgiv tpasdlpdia fglyktvihv ntidqgveeh elneislvgk
      241 stevltrlys mmlkevqtr
//
LOCUS       WP_181644094             521 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudomonas].
ACCESSION   WP_181644094
VERSION     WP_181644094.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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="Pseudomonas"
                     /db_xref="taxon:286"
     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=55880
     Region          15..513
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mnpslpatal rrglsprrkr psiwlllpvl flvglsllpl ayvglkawqa gwaeavhllw
       61 rpyvfgllrn tlalmvgvtv tcgviglsla wllersnlpg rriwgvilcl pfavpafvss
      121 ftwvslsanf eglggailvm slskyplvfl pvaatlrnld psleesartl glnrravflr
      181 itlpllwpsl lagallialh mlvefgalsi iglqtfttai yqqfelefsn anaamlsavl
      241 lvmcltllwl elrvrgkgrh vrigqgaarh aeqvrlgkwa plgqvyclal avigsgiplg
      301 mlgywlavgs saafpvaeig eallsslals lggaalclvl avpvgllvvr ykgklaiwae
      361 rlpyllhalp glvialtlvy falhyvpaly qtsallliay allflplaqa pirtalnkaa
      421 pqleeaartl gassfsafcr vtlpiifpal gaafalvfld amkeltatll lsptglntla
      481 tavwshtsnv efaaaapyaa llilvsglpv yllttrmyls r
//
LOCUS       WP_181643712             200 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [Pseudomonas].
ACCESSION   WP_181643712
VERSION     WP_181643712.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 200)
  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 200)
  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..200
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..200
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=21750
     Region          2..200
                     /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 mdrgrqgkar saqqgsinwp gtllggrphs redllfhlrs rsaqqlwlvi vdasastrrh
       61 haltdakgll aqlfddayrq rarmalltas gqspkwqvqg lkaakglagw ldqlgagggt
      121 pllaalteag qwltarrrry paeqqrllvi tdgrlkdiaa lpslecsgll vdiergpirl
      181 graealaagl qldyrhidnl
//
LOCUS       WP_181644195             920 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-binding protein [Pseudomonas].
ACCESSION   WP_181644195
VERSION     WP_181644195.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 920)
  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..920
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..920
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=101650
     Region          3..920
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msdqrdqavh fgpyrihphq rlvleagrpl rlgrravdil lilleqagnv vskqeliarv
       61 wpksvvedgn lrvhmaalrk algdgqagqr yivtvaqrgy sfvaplsiep mslptegtpq
      121 rpchnlplrr trmlgrqali dslvqhlpeq rfitltgagg igkttvalrv aellighyrd
      181 girlldlapl sapsmilpnl aalldlthte heplatfarr lqerqvllvi dncehllddi
      241 alisetllrh apklhilats realraeges vqrleplacp patgnraqal gypalqllie
      301 ramshqdsfe lseaelplai dicqrldgip laielvaaqi erfglpgllv qmednfrllt
      361 rgrrsalprh qtlratldws fdllttceqi clrrlavfrg gfslasaaav iageqiapte
      421 vlgsitqlva ksllnvepgd demvyrlldi trtyalekls vadeldatre rhanrclalm
      481 dqaqedweqi atqpwidrya plrediraal dwglgdqgvh vlgirltvsa mplwqelsll
      541 rehglyvska larlgqssap sqrlhmalql afgsfsyhaq gstpqtidaf acarrlaead
      601 knlpgqlrav sgqmavslcs gnyrealkqs lhfdqlgpha esllalsaqr lrvlaqhfag
      661 nqvlaqhnae qviqrmaqsg hlnrfthgfg vqydqsvasl tilarilwlr gfperawrta
      721 sqalalalqi nhgtsicytl alagvviaqy ngdtlaardq ldlllqqaqk hsvqlfhtwa
      781 qcyegtaqia evqglglved ilvtfnaiav ddalferars gaagwctpei lrvraeampd
      841 aqsaesllle alglahqqga lawelrcads larlwhkqgr vqaardllgs vyerftegfa
      901 tqdlirvrrl ldelqdkrpa
//
LOCUS       WP_181643284             403 aa            linear   BCT 28-DEC-2024
DEFINITION  nitrate/nitrite transporter [Pseudomonas sivasensis].
ACCESSION   WP_181643284
VERSION     WP_181643284.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            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 sivasensis"
                     /db_xref="taxon:1880678"
     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=42470
     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 mkssfwksgh tptlfaafly fdlsfmvwyl lgplavqisa dlhlttqqrg lmvatpilag
       61 avlrflmgml adklspktag ligqviviva lfgawklgvh syeqalllgl flgmagasfa
      121 valplasqwy paehqgkamg iagagnsgtv faallapvla aafgwsnvfg falipliltl
      181 ivfawlakna perpkaksva dyfkalgdrd swwfmffysv tfggfiglas alpgyfndqy
      241 glspmtagyy taacvfggsl mrplggalad rfggirtllg mysvaaicia avgfnlpssy
      301 aalalfvctm lglgagngav fqlvpqrfrr eigvmtglig maggiggfal aagmgaikqs
      361 tgsyqlalwl faslgvlawf glhgvkrrwr ttwgsaavta arv
//
LOCUS       WP_181644497             222 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Pseudomonas sivasensis].
ACCESSION   WP_181644497
VERSION     WP_181644497.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 222)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..>222
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          1..210
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrllriglal wllacvgvaq aaltfpeltg rvvdnaqmid pavraqlsqq lqaleqtagd
       61 qivvvtvpdl qgvpiedfgy qlgrhwgigq kgkdngalli varderklri evgyglegvl
      121 tdaqswviin qvitpkfktg nfsqgisdgv aamiqvvgge plavpahvad anfakdnpgf
      181 siglvillig vlwlcnrmgl pvgaillail sssgrggggg gv
//
LOCUS       WP_181644474             475 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: O-antigen ligase family protein [Pseudomonas].
ACCESSION   WP_181644474
VERSION     WP_181644474.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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="Pseudomonas"
                     /db_xref="taxon:286"
     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=51532
     Region          218..444
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mnlaslvail fgllfgalal llspakafla vvglaaavti lrfpfwglll faavatfmpy
       61 stvnlgirtt vseailaltw gailwhsfls slpqapsltr rptdqmllwl mlfsafpfmv
      121 gqvithadss glanwlrwll nlsgvflaak llvdqkhres lvialllgtl amlvlsigvf
      181 vrtrsgagia pilglfnyan fdmlkfglea mssrmgspwt hpnaiggima lllplafcfg
      241 mteqgwkral glgvaclgaa alllassrga mvslalvliw masrrvpytg rllmigaalt
      301 ialvmayppl qdrlatifst nnastevrfd eyrmfpqava ayplgigfkv dppvpgtgll
      361 gisnlwlnyi ykiglvgmll fvavtvrwwr earpekgpir ltkdnalwlg ttagilsalv
      421 sglfdhyfsf avvmvalfwl mvginvlear rlfparlpqv ktvtyrkplf sgarp
//
LOCUS       WP_181643921             810 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Pseudomonas
            sivasensis].
ACCESSION   WP_181643921
VERSION     WP_181643921.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sivasensis
  ORGANISM  Pseudomonas sivasensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 810)
  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 810)
  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 810)
  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 810)
  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..810
                     /organism="Pseudomonas sivasensis"
                     /db_xref="taxon:1880678"
     Protein         1..810
                     /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=87602
     Region          31..765
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mpdltsplpl knfhlsllts slllatapsf aeaatedaql gtvtvistgl rgqertvads
       61 papidvinse qllktgrael seaiakllps fnfgtniagy nsvtrplsnr slgpaytlvl
      121 vngkrrhnga tgqrgsidns ganavdidli pvssvdhiev lkdsaaaqyg sdavagvini
      181 ilktgnsggh letsygqlfs gqgetikvag dqgfklgdgg ffhlsadark rgeaswndka
      241 dgsvrafndp akeaawdrva ikngdpdlka fnlaynaelp ledltlysfs tygerdaeaa
      301 nyfrlptgra avpevfpdgy yplnnikdrd yqllfggkgq aaewnwdlst tygrnnvhhs
      361 sdlninpslg tasptkfdnl atfrfeqwvn nldftrryds lfnltspvqv saglehrweh
      421 fstfagdpea yitgtypaas gaqaavtirp edevslirnn yagyldlgfd lterwfldva
      481 grvehyddds gntfglkvns ryeltdsvav rgtvgtgfra psltqigytv adnrvavdvn
      541 gnvvpavtrl tpsgsnlaka lggddlkpek srnlglgltw qpaprtsita daylididdr
      601 ialtsniydq gngvingilt aqgvpsgtwv nyytnafdtr trgldvvadh ttpldawgdv
      661 rwslgfnwnk ttiegnrdtp svlansgvtl vgrdregdlt easpktkwil ganwkvedla
      721 vnlqtsryga vktlavnptg drsfgakwit dldvsytfvd qitvsiggtn ifdvrpdrha
      781 vysnlglapy gnppfypggg ywytklaydf
//
LOCUS       WP_181645785             456 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein [Pseudomonas aeruginosa].
ACCESSION   WP_181645785
VERSION     WP_181645785.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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..456
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..456
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=41602
     Region          <44..>455
                     /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 mrksrsgvvf fgdaaritlp gpdlgtggel gvatgntlpr ielgavdelg gatgttspgs
       61 slgaveelgd stgitppgtd psaggelgva tgntlpridl gavdelgdst gitppgtdps
      121 aggelgvatg ntlpridlga vdelggatgt tspgtdfgag gelggstgtt plgtdfgagg
      181 elggstgitp pgtdpsagge lgvatgntlp ridlgavdel ggatgttspg tdfgaggelg
      241 gstgttplgt dfgaggelgg stgttppgtd fgaggelggs tgttplgtdf gaggelggst
      301 gttppgtdfg aggelgvatg ntlpridlga vdelgvatgn tppgpglgav delggatgtt
      361 spgtdlragg elggstgttp pgtdfgagge lggstgitpp gtdpsaggel gvatgntppg
      421 pglgavdelg gatgttspgt dlraggelgg stgttp
//
LOCUS       WP_181645804             203 aa            linear   BCT 28-DEC-2024
DEFINITION  pyocin knob domain-containing protein [Pseudomonas aeruginosa].
ACCESSION   WP_181645804
VERSION     WP_181645804.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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 15331322
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..203
                     /product="pyocin knob domain-containing protein"
                     /calculated_mol_wt=21660
     Region          <1..41
                     /region_name="pyocin_knob"
                     /note="knob domain of R1 and R2 pyocins and similar
                     domains; cd19958"
                     /db_xref="CDD:410997"
     Site            order(1,3,5..8,13..15,17..19,23..24,26..28,30,35,38..41)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:410997"
ORIGIN      
        1 mltvhaptst miyqtyrgya agglywrcry ngtwsawyra wdsgnfnpan yvakseyswa
       61 slpgkpatfp psghnhdatq itsgilplar gglgannavt arsnigagti ataslgssgw
      121 wrdndtglir qwgrvtvggd ttagitfpip fpnvclggfa gqtanfhpgt dastsfynlt
      181 ttgatvengy qlqmvlfwea fgr
//
LOCUS       WP_181645918             436 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium heidelbergense].
ACCESSION   WP_181645918
VERSION     WP_181645918.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium heidelbergense
  ORGANISM  Corynebacterium heidelbergense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 436)
  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 436)
  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 436)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..436
                     /organism="Corynebacterium heidelbergense"
                     /db_xref="taxon:2055947"
     Protein         1..436
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46304
     Region          157..431
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mpshislidg wfptsvqiav lltavlafwr rgrrwwrvcl plaagvgglv alglrfysis
       61 qgmsaaplpw ilwvwcglga aavvvgavgw tygrhwqqvs avacvllsll aaahvlnqwt
      121 gyvstarqay etavdaplpg evplsaledm hrdpprsgvl vrvnapsvas gmkhrpevvy
      181 lppawfagph ppqlpvlvli ggafntpadw vrsghadvva dryaaahdgf apvlvladvs
      241 gsmgtdtecv dgprgnsaty atqdlpqyiq atfgtypgss gwgiagwsmg gtcaitltta
      301 hpevystfld iagdlapnag neretlarlf agdvaardry dpatamrths pldyagvtgr
      361 fvegkpvggt eglaeltqeq aqrsqapgev lcpqaraagi dcdvvttdlp hqwglaeaqf
      421 eeqfgwlsnr lfanls
//
LOCUS       WP_181646021             639 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator [Aerococcus mictus].
ACCESSION   WP_181646021
VERSION     WP_181646021.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus mictus
  ORGANISM  Aerococcus mictus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
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="Aerococcus mictus"
                     /db_xref="taxon:2976810"
     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=73976
     Region          8..638
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mnsrqlkllk smlsehsyqp asyyakrmsv sartiysdld iinefikkng gevqrkpsag
       61 vkivgdisii qtnllssnll dcdiydpsnr rliiikllaf tnqdisldyl seafivskts
      121 iykdihvlne iidgtdsyie sskhelalig neetlqkaik aivfyfsnne sdlsftqvik
      181 llfdeesiqy vdsllkdeid gfardasnyy yrslvsvlli hlsriqidhq iqsqeellld
      241 sikylevypi aeslvnklsq tfeieyqied ktyitrqlya hriqknivni ddniknsvki
      301 linevsmied inlmedrhll fslyqhfppm lmrlekgiqi enplldsiki qymelfsilw
      361 yllgdfekky nvsfndhevs lilihfqial ekqsesknil iicqygmssa qliyqkvkri
      421 lpnqdnieia nanklhkvnl knvdliitti dlgdfkrnyi kvspifssqd yksilnaysl
      481 llseqnnysp sekikaptll efmnkdlinl hidstskeel ldfmitqleq kkmvkkefrq
      541 sifereklgd tnlengialp hanpntvies sisfttlnkp ikwgkgkvql ivmitfndqd
      601 tnkiklviee lfpvinnkkl vdelleikdk tqwinrfin
//
LOCUS       WP_181647008             426 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Streptomyces sp. WAC00263].
ACCESSION   WP_181647008
VERSION     WP_181647008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..426
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..426
                     /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=44594
     Region          15..407
                     /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..147,150,221,224..225,228..230,233,262,266,330..331,
                     335,339,355,358..359,362..363,366)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mnslamqfrs fngcirllmv qqftintafy mlmpylavhl adglgmaawa vglvlgvrnf
       61 tqqgmflvgg tladrfgykp mimagcvlrt vgfgllgfvd slpalvvasa atgfagalfn
      121 pavraylaqe agerrveafa tfnvfyqagm fvgplvglal ltadfglvcs vaavlflalt
      181 viqfrmlpdr egfpsaepgg vladwrtvvh nrpfllfsaa migsyvlsfq vylalplqah
      241 rvardsgdav ttalfavsaa vavvgqlkit awararwtsq raivygialm gvafvpllvg
      301 pgtvtggfgv mgwgmalapl faavallglg tavvypfemd tivslaggrl vathyglynt
      361 vsglgitlgn latgavwdaa ermghpeltw walaatgalc agcvgllars gllaarsepe
      421 lavvts
//
LOCUS       WP_181647176             420 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181647176
VERSION     WP_181647176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..420
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44348
     Region          69..407
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtharrrlrr gavtatavgm ltvpaagpaa faapgsvrta atapqppppp ssasptgevr
       61 tltpavtgql drtvqqvmre anvpgvtvgl wtphqgtytr sfgvadkssg rpmspdlytr
      121 igsetktftv tallklvdeg kaglddpigr yvagvpngdr itlrelagmr sglfnytedp
      181 gffkaftsdp rrpftphell ayafghpvlf ppgqkfsycn tnlillglvv ekaggkpvqd
      241 yihdnvlapa glrhtlfptd aafpsphaqg ytdqtatgrv edtagwnpsw awaagamist
      301 lddlrvwart vatgvltdgt tlispatqkq rlttppttip gagyglgifd vqgwighngs
      361 lpgyesltvy lpaaqttlvv llntdinhng aepstlfgqa itkivspghv fnlpaqpaar
//
LOCUS       WP_181647195             317 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181647195
VERSION     WP_181647195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  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 317)
  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 317)
  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..317
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..317
                     /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=34605
     Region          <42..315
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mtaplevgaa gharctyrlr vsstaltall gewdrcrcla gpslnynrng frlkdgrlhl
       61 aggigvtvvw srdlpadpss vrvhrdslgh wyasfvvate vqplpetgnv lgvdwgvkqt
      121 atttsdthdf phvehgrkaa akltgyqrmm arrrpkagqa askgyrtakk ltaklykkva
      181 rqrqdtgrkw akqvvrdhdt iavedfrpkf lakstmarka adaaisatka elinmarkhd
      241 rdlrlvrpah ttmdcahcga rakhalplse rtytctacgi ssprdknsar vmlvraglnp
      301 asadrgrpdt ppgrqaa
//
LOCUS       WP_181647128             476 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181647128
VERSION     WP_181647128.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=51070
     Region          1..439
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkltvvgcgy lgathaacma elghevlgmd cdmdkvailn tgkapfherd lddllakhta
       61 sgrlrftasy aeaaafadlh figvgtpqqp genaydlshl faavrqlapr lhdaavivvk
      121 stvpvgtapr vrdllheyap agdaievawn peflresfav edtlrpdrlv lgfhaehswa
      181 eavlrrcfek iieagtptiv tdwataelak ssanaflatk isfinamaev ceasgadvgq
      241 ladilghdar igrrgmrpgl gfgggclpkd irgfmarage lgvdqaltil revdainnrr
      301 rermidlare qvggnfagqr itvwgaafkp etddirdspa lavahklhel gatvtvtdpq
      361 aldnarklhp eldyaddpia avqdadlllh ltewaqyshi dparlasrta sprvidgrgt
      421 lnadswreag wtvralgrpw vahsncgpvp gkapghgpaa stntrseght gtdsrt
//
LOCUS       WP_181647153             372 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Streptomyces sp. WAC00263].
ACCESSION   WP_181647153
VERSION     WP_181647153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  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..372
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..372
                     /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=42842
     Region          11..357
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtaidptahl taeqieelgr eldairdevi asrgekdaay irkvisaqrk lelvsrgvll
       61 fsffppawvl gtaglsvaki mdnmeighni lhgqwdwmrd pkihsttwew dhvspseqwk
      121 hshnelhhty tnvigkdndl gygimrvded qkwhpfhlgq plwnflnacf feygiaaydl
      181 elgknlhkrr rknpefrera kavgrkirkq vlkdyvihpl lsgpsflttl aatftanlvr
      241 niwshsvimc ghfpegvqvf errsikgetr gqwylrqmmg sanisgsram hfmtgnlshq
      301 iehhlfpdlp snryaevavk vralfekyel eyvtgplpkq vfsawhkvfr lslpnkkhqv
      361 ktpdreqelv aa
//
LOCUS       WP_181646982             223 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181646982
VERSION     WP_181646982.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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..223
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..223
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23109
     Region          79..215
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 maapppcagr rsapttrntr qparcprawr saalaaagla laacgsgsas kasgssvass
       61 nrgqsafaqy pvgkrpagpr isgklvgggr ldldawrgdv vvinvwgswc apcraeaptl
      121 akvadatrkl gvrfvgfdtr dndaaarafe rnskitypsf rdpdgrlvlr fngrvpisav
      181 pstvlidrsg riaariigpt syetlntvvr elaaekpgag aia
//
LOCUS       WP_181647216             397 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181647216
VERSION     WP_181647216.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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 397)
  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..397
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..397
                     /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=44509
     Region          5..379
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 msthvkrayr yrfcptdaqa aelsrtfgcv rkvynlalaa rteawarqer vschqtsaml
       61 tawkktgepa ylnevssvpl qqalrhlqta fthffgkrar yprfksrkts rrsaeytssa
      121 frfrdgkltl akmteplavv wsrplpegas pstvtvsqda agrwfvsllc edpsvkplpa
      181 rgnavgvdvg ldhlltlstg ekianprher rdraalakaq rnlarkargd ganrrkarlk
      241 vakiyariag rrrdtlhklt trlvrenqtv viedltvrnm vknhrlarai sdaawsefrs
      301 mleykarwyg reviavdrwf pssrlcsacn tlrdtmplni rtwtcdcgvt hdrdvnaahs
      361 llaaglavav cgagvrpqrs tpdgqsatkq kpsrrep
//
LOCUS       WP_181647309             147 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tautomerase family protein [Streptomyces].
ACCESSION   WP_181647309
VERSION     WP_181647309.1
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 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..147
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=15355
     Region          67..123
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpmidvyata gtftdghqla kdlaatlmai eevpdipmfr qntaafihel ptgalsnvdg
       61 asdnvrvqvl tnagaldrdk qiavvsrftg mvaeaagdpt ladrtwvllt eavpggwglg
      121 ghantndelv aaarkqiael ramageq
//
LOCUS       WP_181647408             249 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181647408
VERSION     WP_181647408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=27467
     Region          29..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 mlqseiwddq aaqsydspgt gmfaptvlrp tvdrlveltd ggralefaig tgrvavplae
       61 rgvpvsgiel skpmidqlrt kaddaaipvv vgdmatarvp gefqlvyliy ntisnlltqa
      121 eqvacfrnaa rhlapggrfv velwvpelrk lppgqqavvw esatgyigld tydvlrqqvv
      181 shhfrfdtea grearlfrsp hryiwpaeld lmaelagmtr esrhadwtge eftaescshv
      241 svyrmaspl
//
LOCUS       WP_181647416             359 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. WAC00263].
ACCESSION   WP_181647416
VERSION     WP_181647416.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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..359
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..359
                     /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=38824
     Region          54..358
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mhrrpglsar lkltlsyagf lavagallla vvwgfllryv pdnpkgllgi spnryllvht
       61 fapaaavamv fllvfglvgg wllagrmlap ltqitdaarm agngslshri rmkgrqdefr
      121 elsdafdsml eqleshvaeq qrfaanashe lrtplaisrt lldvarkdpa rdrdelierl
      181 hvvnsraidl teallllsrg drgnfsresv dlsliaeeaa etllplaeqr ritldvtgga
      241 aqtsgsaell lrmvtnlvqn aivhnlpadg tvtvhtevhg dtsvlrvent grqlppelvp
      301 tltepfqrgt ervrtdehag vglglaivhs ivrahdgtld llprpaggll vtvrlpcap
//
LOCUS       WP_181647603             268 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181647603
VERSION     WP_181647603.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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
REFERENCE   4  (residues 1 to 268)
  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..268
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..268
                     /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=28914
     Region          25..250
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          165..242
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mteirhdpva ptrtqwlasg aaidahrhdd hqivyagrgv lavttgagtw iapgtraiwv
       61 pagtvhahqa hgelelhlvg lpasdnplgl deptvlsvgp llpelilayt htphddsper
      121 grlravlldq lraspqqplh lptpttpqlr avceilrtnp addrtlaalg rqvgasdrtl
      181 srlfksdlgm tfpqwrtqlr lyhalvllae nvpvtavahr cgwssasafi dvfrrtfght
      241 pgthqsrrqs gsctidaapl taaqargr
//
LOCUS       WP_181646944             877 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181646944
VERSION     WP_181646944.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 877)
  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 877)
  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 877)
  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 877)
  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..877
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..877
                     /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=91012
     Region          24..850
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mrqdsnhhdh qhrdhrpggg kdrstavldv rglawasqqn tvaaalgrrp gvldvevnpv
       61 aqsatvvfdp grtslaelrr wvqecgyhca gqsvpahlcd pmaepdpppp ppehpehpeh
      121 pghlahgggt alaappehag haehaehpgh avsaappahd rhappeapag haghaepegm
      181 psphevmghg ghggmsmaam vadmrnrflv avlfsipivi wspigkdvfg ldvpvpfglr
      241 qdvwalllsl pvifysctif fdgavralra rtldmmvlva vavgsgwtys livtltgggd
      301 vfyeaatvla sfvllghwfe mrargganda vrtlldlapp kalvlrdgep vevptaevav
      361 gdlllirpga kiavdgivee gesdvdesmv tgeslpvhks pgeavtgati nangtlrvra
      421 tkvgadtala qivklvqqaq nskapgqrla draafwlvfv allggaatla vwllatdrpl
      481 gtamlfaitv vvvtcpdalg latptaimvg tglgaqrgvl fknapaleas ariqtvvmdk
      541 tgtltkgepe vtdvitadgl aeaellrlva averesehpl aeavvrhaea ngvaqmraag
      601 fenvpghgav advdghrvvv gnrrlaereg ialgdlaeqr etlaatgrtv viaavdgraa
      661 gligiadapr atsaqavadl halgvevvml tgdnqatadr iaqqlgidtv iaevlpgdka
      721 akiaelqtgg rrvamvgdgv ndapalaqad lgiaigagtd vaietadlvl mrsdpldvpt
      781 alrigrgtlr kmrqnlgwai gyntialpia agvfepalgl ilrpeiaals msgssiivav
      841 nalalkrlhl paaappapep grtgqrdagh htepraa
//
LOCUS       WP_181647612             397 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA-guided endonuclease InsQ/TnpB family protein
            [Streptomyces].
ACCESSION   WP_181647612
VERSION     WP_181647612.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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 397)
  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..397
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..397
                     /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=44713
     Region          5..379
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mtthvkrafk yrfcptdaqa aelsrtfgcv rkvynlalaa rteawvtrqe rvnynatsam
       61 ltawkkteel aylndvssvp lqqalrhlqm afthffgkrv kyprfksrkt srrsaeytss
      121 afrfrdgklt lakmteplav vwsrplpega spstvtvsqd sagrwfvsll cedpsvkplp
      181 atgqavgvdv gldhlltlst gekianprhe rrdraalakq qrrlakkekg sanrararlk
      241 vakihariad rrrdslhklt trlvrenqti viedltvrnm vknhrlarai sdaawsefrs
      301 mleykaqwyg reviavdrwf pssrlcsacg tlrdrmplkv rtwtcdcgvt hdrdvnaahn
      361 llaaglavtv cgagvrpqrs tpdgqsatkq kpsrrep
//
LOCUS       WP_181647683             964 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181647683
VERSION     WP_181647683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 964)
  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 964)
  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 964)
  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 964)
  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..964
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..964
                     /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=102741
     Region          5..254
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          152..959
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          752..777
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          789..817
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          829..857
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(830,833..834,837..838,840,870,873..874,877..878,
                     880..881,910,913..914,917..918,921)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          868..898
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          909..936
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mapdpvrfav lgpvrvwrag telhlgrpqe rallalllvr agqpvsvsei vdvlwggrpp
       61 dtavnvvhrh vgalrrllep glptratgqw llrdtggyrl vadsdsldll rfralrvear
      121 raasdgaper avdllteals lwqgptahgi pvearthaaf vslegerlat vkeaadvalr
      181 advpgvvlpr lreaaadspl deplmarlml alsatgrrpe alstyvtvsn rladelgidp
      241 gpelrdahqa vlrdtastaa gpaagvsear taqgpaasdl agpraaslpv paqlpldlpt
      301 ftgrraelae vlaprssegr saetvvisai ggmagigktt lavhwahrva drypdgqlyv
      361 nlrgfdpsga vmrpdeavrg lldtlgvppe rvphgldaqa alyrsmlagr rflvlldnar
      421 dsdhvrpllp gtpgcltivt srnqlsglva ahgahsltlr plgtdegrel lirrlgaerv
      481 saereaaaei talcaglpla lacvaaraat hphfslsava aelreahgsl dafieadtsa
      541 dvgavfswss ralspaaarl frllglhpgp dftapaagal aglavrearl lltelsrvhl
      601 inehapgrya fhdllrayaa elahtqhgea ecraavnqlf ehylytahaa grliapyvdt
      661 mplpplpegi lpepladdes alawlaaeya vllavidvat dsgadrlvcl lvsslerffd
      721 rqghwhdwaa vqrtaleaal rlsdpvveah gllglarvag rlglrdeaga hldrvlglft
      781 elgddvgray vhlslgweae qhgdlpdalr hdqlaldlfr atgrqaaqat alnavgwdha
      841 tlgdhqqald hclealtiqr dlgdhigqaa twdsiayahh nlgdhpqalt syrnaltifr
      901 dlgvpaeeag tlvrigdthr atgdhdaara awrsaltlft elahpdaerv rvrleelgep
      961 pgda
//
LOCUS       WP_181647605             483 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Streptomyces sp. WAC00263].
ACCESSION   WP_181647605
VERSION     WP_181647605.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 483)
  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..483
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..483
                     /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=51400
     Region          10..117
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          231..476
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 masnkltvgd llsfpalqls vkagsgglnr svswahasel adptpwllga evimtaglav
       61 prtaagqray lerlddagvs alalsaqlhm pplhdaffqa aeergfpvlv vplavpfiav
      121 aqeiaaaaqe darhrlgaql qvfgalrwlv aedldtptll rrleglsgyd vylctpqgrp
      181 llpgvpvpdp avlpasvdap ptipggfvlp vpapggpagf lvayerqgaq paglavvqhi
      241 atvaalrlam vrneretlrr egaetlaell qevldpeaar rrlarhaieg dtvllvvrht
      301 tdeallrcle drphllltrg edryvlgape lgaavgelpa vaagisrpfl pgaalrvaqr
      361 ealwavskav esgrpvvryg ddstgrwlpd dpavltalve hvlgevlryd ethdsqllvs
      421 artwmerdrr tetaaaalhi hpntlayrlr rfgaladrdl tstgalaevw laiqaagalg
      481 ltd
//
LOCUS       WP_181647721             332 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Streptomyces].
ACCESSION   WP_181647721
VERSION     WP_181647721.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=35852
     Region          3..328
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 malklgayta clhdrpltea ldilkenglt svevntggfi psphcpvdll lasatareey
       61 latfadrgme ltglncngnp lnplpgvgpk haddlrrtir lagllgvrhv vtmsgtpgsd
      121 pdatypswvv npwdgvymdv ldyqwgvave fwkeidalar endvrvaiem hphnlvfspv
      181 tlkrlvdetg atnvgaemdp shlmwqgmdv vacikwlgpl vfhaaakdat lcpgadirgv
      241 ldtsftrvpa dapdkvptgy gfwcnawpen pawkfvavgv ghdvpywtef lralaeidpd
      301 mavnieheda aysqteglal aaktlqsaat al
//
LOCUS       WP_181647779             443 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Streptomyces sp. WAC00263].
ACCESSION   WP_181647779
VERSION     WP_181647779.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=46388
     Region          19..425
                     /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(29..30,33..34,37,71,121..122,124..126,129,149,
                     152..153,156,257,260..261,264..266,269,296,300,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mspspdlrar gtglatlvvg lcwlvvlfdg ldmfvygsvl pnmlaehalg lqpsqagdlg
       61 syatfgmlig alsagtvtdw igrkkviitc tavfslasal cavapslgvf glgrfvaglg
      121 lggllpttit mvaeyaprgr ralivgtlmt ahqaggilag fvglwttgag qwrvaywicv
      181 vplligvpli akylpeslnf lvakgrtrea celaerydve lpapaaerpa agdrwsavva
      241 lfrgglwrtt llfwlasfcg lllvygvsnw lptmmrgagy elgsslsfvi vinlggiagm
      301 liagrfsdhf ggarvatvwf aatalgvyll gihmalplty vvvfltglfl fsaqamiyat
      361 vagrssddnr atavgwvsgi grfgavfgpw lggqlvaaks eswgftafai aavlatvfva
      421 ltglrgpqrt prrdaaqqlt ttg
//
LOCUS       WP_181647800             554 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: dipeptide ABC transporter ATP-binding protein
            [Streptomyces].
ACCESSION   WP_181647800
VERSION     WP_181647800.1
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  :: 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..554
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..554
                     /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=58235
     Region          1..535
                     /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 mtadilrien lgvtfstetg evaavrevsl rvrpgetlal vgesgsgkst valaamgllp
       61 gtaratghav vggtdvvgat eadlaglrgr tasmvfqepa taldpltrig aqiaevirnh
      121 rpvtakeaag eavellrrvg ipdpgtrasa fpfqlsggqr qrvviamaia napslliade
      181 pttaldvtvq aeildllrsl aadfdtgvll vthnmgvvad fadrvavmlq geivetgpve
      241 evllrpthey tkrllgavpr ltvaepgads rrtegdrpaa dpvvelrdvs vrfgrgrrav
      301 raldgvsltv gagetvglvg esgsgkstaa rvalglvpps sgsvslfgad lgrtrgrarr
      361 allagvgvvl qdpvasldar msvaecvaep lrvhrrgmpa aerrtrvgda lelvrlprel
      421 arrgprelsg gqrqrvslar alvleprllv adeptsaldv svqqsvlevi aglqgelgfa
      481 clfvshdlav vqqfaqhvvv lragrieeeg stattllhpr tdytrrliaa vpvpdpvlqr
      541 rrreerraat gvta
//
LOCUS       WP_181647833             270 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces sp. WAC00263].
ACCESSION   WP_181647833
VERSION     WP_181647833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  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..270
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..270
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29550
     Region          38..269
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtdlwndllt clelrpdpsa peavtgfegs nqhlsyhrlf ggqllaqfvr aaaltcpdka
       61 vkslhaqfpr eglpgepvry evtrhreggt fatltivarq tpgviatasa slhaeedgld
      121 qqsdfevpsv pgaehdtdlg lipwttrsvt dlespkaepp eydlwmrtpe vapelapali
      181 ayatdltlig tavrrldgis qrdsrtafts avtshslwfh rpprtedwll lhqhspilah
      241 grcfgrgdvl tedgalvasy aqeallrfrs
//
LOCUS       WP_181647845             298 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Streptomyces sp. WAC00263].
ACCESSION   WP_181647845
VERSION     WP_181647845.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 298)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..298
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31544
     Region          22..>129
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
     Region          28..264
                     /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 mtgvsrvvdv dgipvsallq earrpravvl alhggaahsg yfdypgrphl sllrtgsalg
       61 ftvlaldrpg ygssaphgge lapverrvdl ayaavdrlla srprgagvfv lahsigcela
      121 lrmaadergs dllgveiagi grhhhddaad ilgvrhnesw prpaagsvrd llwnpsrlye
      181 ddvvggarfa spspsyegvv arswplvlpe laplvrvpvh yslgehervw rsgpaaladi
      241 aslftasprv vvdeqadggh nlsigltama yhlkilsfve ecvlarasaa qerpgras
//
LOCUS       WP_181647850             268 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Streptomyces sp. WAC00263].
ACCESSION   WP_181647850
VERSION     WP_181647850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            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 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..268
                     /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=29883
     Region          1..265
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 miatkalsps lgvevtgvgn llddrlisrc aealqwrgvl lirglhldde gqlafsrrlg
       61 kvfavrgkei ftvsldparn ptaeylkgtf hwhidgttdp vptrtttlta rhvamtgggt
      121 efastyaaye nlpeadrkqy ddlrvvhsfq aaqrlvtpdp gpemlagwrk vpthetplvw
      181 krrdgrrslv igatadhivg mdaaesrall drllewttle rfrythdwrv gdlvvwdntg
      241 mlhralpysa dsertlqrtt ivgdeels
//
LOCUS       WP_181647853             406 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: metal-dependent hydrolase family protein
            [Streptomyces].
ACCESSION   WP_181647853
VERSION     WP_181647853.1
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 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..406
                     /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=42320
     Region          42..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(58,60,232,252,320)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mvtlkaarvl hvetgrieep glvtvdgdri aggggeggdg dvldlgdvtl lpglmdmevn
       61 llmggrgevp glspvqddpp lrmlrgvana rrtlrsgftt vrnlglfvkt ggylldvala
      121 kaidagwidg privpaghai tptgghldpt mfaayapgim plsleegian gvdevrkavr
      181 hqikygaqli kvcasggvms htgtagaqhy sdeelraivd eahrrglkva ahthgaaavr
      241 saveagidci ehgfllddat idlmaergtf lvattalidg mdiskappel kakageifph
      301 artvvaralk agvkiavgtd apaiphgrga qelialverg mtplevlraa tvnaaelida
      361 edrgriaegl ladliavpgn pledisvmad vrfvmkggkv frherg
//
LOCUS       WP_181647852             420 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Streptomyces
            sp. WAC00263].
ACCESSION   WP_181647852
VERSION     WP_181647852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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 420)
  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 420)
  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 420)
  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 420)
  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..420
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..420
                     /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=48252
     Region          21..411
                     /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..>339
                     /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 mphfskpdag swteqypelg tspvnyedsi dpayyeaere aifkrtwlnv grveqvpkpg
       61 hyftkelaaa gtsliivrgr dqqirafhnv crhrgnklvw ndfpgeevkg tcrqftckyh
      121 awrydltgkl tfvqqegeff dldkddyglk evacdiwegf vfvnldprqs lreylggigk
      181 glegypfhem tdvftykaei gsnwklfida faefyhapvl hqkqatkeea ekllgygfea
      241 lhyelhsphs misswggmap pkdpsmvkpi erelrsglfg pwdrpdiagl dplpagvnpa
      301 rhrswgtdsf vlfpnfmlll wapgwyltyh ywptavdkhl feanlyfvpa ktardrlaqe
      361 ltavtfkeya lqdgntleat qtmlkgryvt dfplndqeil lrhlhkvvrd yvkehadaae
//
LOCUS       WP_181647893             230 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181647893
VERSION     WP_181647893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  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 230)
  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 230)
  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 230)
  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 230)
  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..230
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..230
                     /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=24187
     Region          1..230
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mthasaqlig drshqcdata tythngaray vlcdgigssd avrawtltaa rhadaeaglr
       61 avydsyaaep ersdqyadvp nasaavavtd pgkplaiawc gdvrayvftl sgtlqcltad
      121 hnmrrvfrgs rnlvtsylga tesddqrkar yghpaietat gpakacrlll asdgayeple
      181 dsartlanyl grspkqaatd vvtaavehag gyadnatilv adlpvadsre
//
LOCUS       WP_181648047             575 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: dipeptide ABC transporter ATP-binding protein
            [Streptomyces].
ACCESSION   WP_181648047
VERSION     WP_181648047.1
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  :: 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..575
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..575
                     /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=61206
     Region          1..528
                     /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 masivsvnsl svayrsggrd vpvvhevswe vaegrtlalv gesgsgkstv aatllghlrh
       61 gsritagsvh vdgsdvfsls arelrrlrgn tvamvaqnag haltpsmrig rqiaeaggdv
      121 pvvdlleqvr lprpaelarr yphelsggqq qrvaiamava arpkvlvlde pttgldvvtq
      181 rgvldligal rdelglaavl vshdlgvvah madevtvlrs gsvvesaptr qlfampqdpy
      241 trrllasvpr lddaglalvg aagerevrpk apvpdtapva vsardltidy gssravhgvs
      301 fdvrrgevla lvgesgsgks tlawtlaglr tpsggtmthe sgdlarsaqk rplalrrrvq
      361 lvfqnadtsl nprrsvgdav rrplrffgta atrtqaadra rrlisdvrld paladrlpaq
      421 lsggqrqrig iaralagepd vliadeitta ldvsvqadvl rllddlrrer elaclfishd
      481 lavvrgiadr vvvlrhgvvv eegptdavfa spghpytrrl maaalepdpd aapfvdgavd
      541 wsdaaepddl wtdhgpghrv rrwrpadrli tegvs
//
LOCUS       WP_181648063             555 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. WAC00263].
ACCESSION   WP_181648063
VERSION     WP_181648063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  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 555)
  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 555)
  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 555)
  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 555)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 555)
  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..555
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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: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=60906
     Region          27..537
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mtrtpntpgp ddatahrpee gkstrvarlt vqgwihvvla anvllvivfa vsggvlqara
       61 ddrtdlltdr iqparatayq letslvdqet gvrgyalsrd agfldpyasg ardektfear
      121 latqladhsg ivadlktagr lsdawrrdya eplieaarap ggakapslea skarfdelrg
      181 qlatlekdie qlrdrirasa ddsrrsrnll fggmlaafla sglaltlllh rivgrplrvl
      241 eaasvdvsgg aferrirldg prdlervaqa veemrrrive elsaskarev llerqaeeld
      301 aqtlelkrsn aeleqfayva shdlqeplrk iasfcqllek rygdqlddra kqyidfavdg
      361 akrmqilind lltfsrvgrv geelipvald dvldralgnl svvleetgar vvregplptv
      421 tgdvttltml wqnlignavk frhpdrppei avrceaeped gqwrltvqdn gigiepefre
      481 kvfiifqrlh grdeyegtgi glavcrkive hhggaitldg tagggtrvtf tlpmarpepd
      541 lgaeeaarpp egaht
//
LOCUS       WP_181648165             297 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HpcH/HpaI aldolase/citrate lyase family protein
            [Streptomyces].
ACCESSION   WP_181648165
VERSION     WP_181648165.1
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 10006304
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..297
                     /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=31384
     Region          10..297
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtstaepfsa rswlfapgds erkmekaaag padivlldle davaeegkpk sramissfla
       61 drspeergrl wvrinpldga haladlaavi pagpggimlp kargradvel ldhylsalev
      121 sagrergstk vivlvtetae gmfttgtyqg aprmvamtwg aedladsvga senrnpdgsy
      181 gftyelarsl cllgaaaagv apvetiqgdf rdveglrrra ervrrdgyrg mlaihpaqvd
      241 vinaaftpte qelaaaqeiv dlfaarpgvg aighrgvmld rphlaraqal lasggra
//
LOCUS       WP_181648168             388 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [Streptomyces].
ACCESSION   WP_181648168
VERSION     WP_181648168.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..388
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40381
     Region          7..371
                     /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 mqssdgsagp lvglrvlela glgpaphaam vladlgadvv rverpsgral rlgpqdatdi
       61 vrrgrrsvfa dlkesegral vralaaradv lieglrpgva erlgvgpedc grdnpglvya
      121 rvtgwgqdgp laqdpghdln yigltgllha mgragdpppp plnlvgdfgg gsmllvigvl
      181 aalwertrsg agqvvdsamv dgtallgqmt yalrgmgews dersanlldg aapfydtyec
      241 gdgkyvavaa lepqffaall eglgitgahp saqgdrggwp alrarfarrf asrtrdewaa
      301 hfagtdacvt pvltfaeaga hphvvarstl ievdgilqaa paprfsrtpn rrpsapgapg
      361 adtesvlrdw gvgspavtpa vrarprar
//
LOCUS       WP_181648188             862 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. WAC00263].
ACCESSION   WP_181648188
VERSION     WP_181648188.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 862)
  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 862)
  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..862
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..862
                     /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=92249
     Region          3..830
                     /region_name="PRK10490"
                     /note="sensor protein KdpD; Provisional"
                     /db_xref="CDD:236701"
ORIGIN      
        1 margklriyl gaapgvgkty amlseahrrv ergtdcvvaf vehhnrprte vmlhgleeip
       61 rkeleyrgtv ftemdvdavl arrpqvalvd elphtnipgs rnakrwqdve ellaagidvi
      121 stvniqhles lgdivesitg irqqetvpde vvrradqiel vdmsppalrr rmahgniykp
      181 dkvdaalsny frpgnltalr elallwvadr vdeylteyrs ehrvskiwgs rerivvgltg
      241 gpegrtlirr aarlaekgag gevmavyiar sdgltsaspk elavqrtlve dlggtfhhvv
      301 gddvptalld fargvnatqi vlgvsrrkaw qyvfgpgvga tvardsgpdl dvhlithgea
      361 gkgrglpvar sarlgrlrvv wgwltgvagp alltllltgv apevglandm llflamtvaa
      421 allgglypal asavvgslll nwfftppvht ltiadpkniv aiaifvgvav svasvvdlaa
      481 rrthqaarlr aeseilsfla gsvlrgetsl eallervret fgmesvalle resdvtpwtc
      541 agrvgtgrtl erpedadvdm pvgdrmalal sgrvlpaedr rvlaafaaqa avvldrqrlq
      601 sqadqsrala egnrirtall aavshdlrtp lagikaavss lrsddvawse edraellegi
      661 eegadrldhl vgnlldmsrl qtgtvtplir eidldevvpm alggvpedsv eldipetlpm
      721 vvvdpgller svanlvenav kyspadelvl vaasamadrv evrvvdrgpg vpdeakdrif
      781 epfqrygdap rgagvglgla vargfaeamg gtlnaedtpg ggltmvlglp aaagngatav
      841 payahervsp traadarsgp ph
//
LOCUS       WP_181648414             622 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. WAC00263].
ACCESSION   WP_181648414
VERSION     WP_181648414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 622)
  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 622)
  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..622
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..622
                     /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=65840
     Region          273..614
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnsriplrkr llvrlmitsv lialcsvaat awlavqtttr aiqeeqgqvl addtdilrql
       61 sgyaathpsw agvqdtvrrl saatgrrial ttadrtpiad sarsrtalpp gaaatvdplh
      121 tdtysepgaq lsgvdpravg pyrltplera rlgklatlrq kcaarngvdt titwtpsgrp
      181 vladengilp nstvpdvcad gqlntlthte etavarlasl aeaclrrenv alpgkgfisl
      241 efssrapqpq falgrkdlgg hptaigakgn eclaearreq ldpdvapvae lflgtgdsal
      301 phfdmsnank akivgvtglv laltvavtal vatrlvrplr altqaaqqpl erhvrvpvtt
      361 rdetgilava fnelterrer meaqrkamvs diahelrtpl tnirgwlevt rdgivdpepe
      421 llaslheeav llqrviddlq dlsaadagtl alhreavrad ellaqvaaah rvgaeaagig
      481 lrtgtdgtsa ptgsgtawid adpvrmrqal gnlvsnairh tpdggtitls areeedqvvl
      541 avadtgsgia aedlpsvfdr fwraeksrsr rtggsglgls ivrqlvaahg gtvavaselg
      601 agsvftlrlp atdppvdgde vr
//
LOCUS       WP_181648221             277 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Streptomyces sp. WAC00263].
ACCESSION   WP_181648221
VERSION     WP_181648221.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 277)
  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 277)
  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 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 10787854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..277
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29862
     Region          16..277
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mttndaqrie rvnatgrvpv vfvhglwllp sswdrwtahf eqagyapvsl swpddpdtve
       61 eanahpevla gktvgqvadh lealigglek kpavighsfg glltqilagr grsavsvaid
      121 papfrgvlpl pisslrsaap vlgnpanrhr avpltfdqfr ygfanavgee eakelydtfa
      181 vpapgaplfq aatanfnpwt evkvdtenpd raplliisge kdhtvpwaia nasykkqqhn
      241 pgvteiteip grghaltidh gwqevadtal efvrrfa
//
LOCUS       WP_181648455             497 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181648455
VERSION     WP_181648455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..497
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54034
     Region          7..324
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msarplpast paaqgvdaag ihafldavea apdiephslm ilrhghlvas gwwapytpdr
       61 rhllyslsks ftstaagfaa tegllrlddp visyfpefea ditdprsram lvrhvaamas
      121 ghleetyats irrdrdeivr gfllfppdrd pgtvfaynqp ctytlaaiiq rvsgqsltey
      181 lrprlfdplg igetawlqrp pgrdlgfsgl hattdaiarl gqfylqdgvw dgrrllpssw
      241 iaeatrahvs tadgtregaq sdwqqgygyq fwrsrhgyrg dgaygqfclv lpehdaviat
      301 taatddmqgl lnlvwrhllp afgaetlsae slaaerlpae rlpgtadegl rrrlaelalp
      361 pveaspeppa rgddwrgavf apedgecpqq rtltgvtvta dadgkgwgvs laeddeliel
      421 rlgatgwtvd aggpptavsg gwtdqdtlrl dvlfletphr ltvtcslpdg tftvrwhttp
      481 ihggrlhslr apvgdrv
//
LOCUS       WP_181648478             392 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces sp. WAC00263].
ACCESSION   WP_181648478
VERSION     WP_181648478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            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..392
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=41106
     Region          2..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 msthhpiavv gaglggltla rvlhlngies avfdldaspa artqggmldi heesgqaalr
       61 aaglheefra vihaggeamr ildreatvrt addgeggirp evdrgvlrdl llgslpdgti
      121 rwgakvtgvq tledgrhevt fadgrtitad lligadgaws kvrplvsdat payldlsfve
      181 ahlldadtrh pesaavvgng mmfalaeghg flahrtpggs lhvyaalrap adwvtsgpid
      241 ftdveaakas llehfegwde rlraliadad galvarqvha lpvghrwdrv pgvtllgdaa
      301 hlmspfageg anlamldgae latalaahpd dtekaltvye qalfprseaa aaasaenldl
      361 cfaphapqpl vdrmafyrae aeaetatana td
//
LOCUS       WP_181648570             388 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Streptomyces].
ACCESSION   WP_181648570
VERSION     WP_181648570.1
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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..388
                     /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=42151
     Region          16..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 mgtplavspp lerpetrgrg qvlgldglrg laalyvllfh cwlltmpgfp enrgpawlgw
       61 lmygrlavvf flvlsgfsla isparngwhl ggvsrflrrr awrilppywa alalslavar
      121 fmvpashfgp ptgttilvyg fvvqdvftap tpngafwsig veaelylvfp llllvrrrlg
      181 avvlvasvtl lvvargllap haspvegvnw ltpnlapvfv aglvgagivv apekvrrlpw
      241 hwlaalaalp vvalvvgkgs awtvdhyfwi dlavapamtm miaavatgrp avlmrllatr
      301 pmrglgdfsy slylvhlpiv mivcrkmaph fvspglpafw ftltlalpas vlaawlfakl
      361 felpfkrnrs wksmfpagra lpgphssr
//
LOCUS       WP_181648568             283 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Streptomyces sp. WAC00263].
ACCESSION   WP_181648568
VERSION     WP_181648568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            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..283
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=29638
     Region          3..283
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mippafdytr pasvdeavrt ladagedakv laggqsllpl lrlrlafpel vvdvgripel
       61 rgiredagtl vigamtshhd virdplvrrh agllaaatat vadpavrhrg tlggslahad
      121 pagdlpavvl aldatliavg pqgrraipar effldylqta lrpdellvgv eipstegwgf
      181 hyekfqrvaq awavvgvaal vrrddghlae srigltnmgs tplratstea altgidaepg
      241 avaraaeaaa egthpssdps gspeyrahla rvltrravla ale
//
LOCUS       WP_181648651             374 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181648651
VERSION     WP_181648651.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..374
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39448
     Region          35..338
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrgsrfgala lltvcalvpt aggavaappa vgpdatalqa aldrvtatga vaevrqgsav
       61 wrdssgksrl ngrqaapvdg rfragsvtkt ftatvvlqlv gegrlrlsdt aerwlpglvp
      121 apggdkitvr ellqhasglp eytdglldgd aphdrfrtwt paelvrravk dgdrnrpllf
      181 ppgtdhhysn tdyialgmii ekvtgrsyrt eidqriirpl alrdtrlpss spfltgphsh
      241 gyepvekedg tlvpvdyttv nmsiagaage iisttadldh ffrtllsggl lhpaelremt
      301 adtsgdgwgl glemaalpcg tivghgggtp gyrtisfhtl dgtrqvtvdw tdwgtdadas
      361 paalalmtaa lcps
//
LOCUS       WP_181648658             438 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Streptomyces].
ACCESSION   WP_181648658
VERSION     WP_181648658.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=45567
     Region          39..435
                     /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(154,156,280,282,319..321,362)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrriraaaag avtvslltav tacgggsstg ggsndspktl tywasnqgas ievdkkvlqp
       61 eldkfekqsg ikvkvevvpw sdllnrilta ttsgqgpdvl nigntwsasl qatgallpwd
      121 asnfakiggk drfvdsalgs tgaqgkdpaa vplysmayal yynkkmfada giatppatwd
      181 eliadgkkls kggkwglgae gsnpsenihh tfvfakqhga dfftadgkpd ftsdgtvaav
      241 kqyidlmakd kiiapgnaey aqnqsvsdfa kgknamllwq sasanlksqg msddaygiap
      301 vpvqsgtpgt gtnvnsmvag inlavfknsh nldgatkfvk fmtsdaeqki lntayssipp
      361 vktaqtdatf ntpanavlkd tlaksaaalp qvadesqfet tvgtavkalf adaaagravt
      421 tesvkaelek aqqqmpak
//
LOCUS       WP_181648566             661 aa            linear   BCT 28-DEC-2024
DEFINITION  elongation factor G [Streptomyces sp. WAC00263].
ACCESSION   WP_181648566
VERSION     WP_181648566.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 661)
  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 661)
  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..661
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..661
                     /product="elongation factor G"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=71041
     Region          5..244
                     /region_name="TetM_like"
                     /note="Tet(M)-like family includes Tet(M), Tet(O), Tet(W),
                     and OtrA, containing tetracycline resistant proteins;
                     cd04168"
                     /db_xref="CDD:206731"
     Region          9..630
                     /region_name="PRK12740"
                     /note="elongation factor G-like protein EF-G2"
                     /db_xref="CDD:237186"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206731"
     Site            order(11,13,17..18,21,24..25,59..60,78..79,102..103,139,
                     143)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206731"
     Site            order(13..18,128..129,131,225..227)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206731"
     Site            48..59
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206731"
     Site            55
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206731"
     Site            74..77
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206731"
     Site            76..94
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206731"
     Site            128..131
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206731"
     Site            225..227
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206731"
ORIGIN      
        1 mhmlnlgila hvdagktslt erllhsvgvi deigsvddgn tqtdslaler qrgitiksav
       61 vsfavddvtv nlidtpghpd fiaevervls mldgavlvis avegvqaqtr vlmrtlrrlr
      121 iptlvfvnki drggaccerv ldavaarltp aivplgevra qgtrdarfgl fdeqrlgapl
      181 ldllsehdda llaayvegrv sydliraalv rqtgqalvhp vffgsavtga gvdeliagir
      241 ellpraeadv dgpvsgsvfk vergpageki ayarmfsgtl rtrdrlplgd geegrvtais
      301 vfdrgaavre qsvaagrigk lwgladirig dtigvprkss agehhfsppt letvvepcrp
      361 adkgalhgal tqlaeqdpli dlrqdetrke isvslygevq keviqatlad efgidvlfre
      421 ttplcierpl gsgaavefik kglnpflatv glrvdpapvg sgmefrleve lgampfaffk
      481 avedtvketl aqgihgwqva dctvtmthsg ywprqshahq gfdksmsstg adfrgltplv
      541 vmdalraagt qvyepmhrfr leapadtlga vlpvlakqga vagttelrga scvlegripv
      601 arvhglerql pgltrgegel ecafdhyapv lrgavpdrpr tdlnpldrke yllnvtrrvg
      661 a
//
LOCUS       WP_181648760             951 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181648760
VERSION     WP_181648760.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 951)
  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 951)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 951)
  AUTHORS   Rosinski,J.A. 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 951)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..951
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..951
                     /product="helix-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=101444
     Region          <6..891
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          883..940
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msstdpaddq aggrgnqamt glrlrgrdre itavrealdt vrggrgacvv vegtpgvgks
       61 rllaeldema rrsgfdvvsv radeldqyaa gaalqsalhs sdgsnraaaa tddqrlwlld
      121 sitdaledra qhapvavlvd daqwadpatl fvlrtlpgrl aasrilwvla vrsdterptv
      181 arvredlerl garwltlgpl pqqelqdiaa dvlgarpspg larllravag npflaielvr
      241 afadtdaakm eageagllhd gipvsfrrsi aarldrlpdd avrllqigsv lgrefdlgta
      301 armlgrqvgs llsgveaaln agllsadgpr lafrhdlirq avhenlplav rtalhreaad
      361 slrgigarsa evawhvvmsg gpvdddavat lttavrelss sapdaaadla qrvagllpph
      421 dgrritlltd aaeylgrtrr vhealdlvdt tlpegleplq eahlrlvaae ihqaagddaa
      481 amthlqqald lpalppdlrv rllktkatgh vylgditaae qtgpwlveas yrshdpavvv
      541 samvfqsqts fyrgrlaral elaeeatrra gtqsaalylr ppripalwla tvltatdrla
      601 dtervlregq reaealglgw slphwhaara calleqgald daaveaeasl mvageleitl
      661 pnpqarsvla lveirrgdla kakdhlraae tgsgtnttqr ygpwvslara gladaegedg
      721 eaaaaltasf qsreptrlla vppshwpgiv rialrdkdps laqavsgalr sltaqdesrq
      781 iigavrthvd gllhrdpral asaitgyrst grplalaaac edlgelmaas adttpaipyf
      841 eeagrlasas gagrdqerir rrlrrlgvrt gpvrnhtagp qglgsltese rkliplvveg
      901 ltnraiadrl yvsvhtvnth mkhiftklgi nsrveltrla iereisadga g
//
LOCUS       WP_181648766             512 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Streptomyces sp. WAC00263].
ACCESSION   WP_181648766
VERSION     WP_181648766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 512)
  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 512)
  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..512
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..512
                     /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=55170
     Region          7..448
                     /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 mipaqrtrtd rdlravvvga gfsgigaavr lreagfndvl vlekgtqlgg twrentypgc
       61 acdvpstlys ysftpdaaws rvfagqreil aylratakry rlddmlrcgv qvlgarwdga
      121 agrwlletsd gpysaavlvl atgpwhvprr levpgiedfn gpvfhtarwd hsidltgrrv
      181 tvvgsgasav qvvpaieaqa asvglfqrta qwvlpkpdll lpaafnrlld hvpgargalr
      241 agqyalqegf gyafrhpqga rlleagarah lrlavrdrql rrqltpdyrl gckrlltsst
      301 fyqalsqphv rlhptavtav rgnevvgadg ttvptdvlie atgfrvgelp lakslygtng
      361 rtldeawsge pqaymgttvs gfpnlflllg pnllggstsa itvleaqlty liaalahldq
      421 gghraldvrs aaqaahntav qdalattvyn tggctsyyft stgrntfawp wstgrlvrrl
      481 srfdadayts dvparplplp aqtrgaanae qp
//
LOCUS       WP_181648890             549 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces sp. WAC00263].
ACCESSION   WP_181648890
VERSION     WP_181648890.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 549)
  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 549)
  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 549)
  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..549
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..549
                     /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=58650
     Region          14..370
                     /region_name="FAD_binding_3"
                     /note="FAD binding domain; pfam01494"
                     /db_xref="CDD:396193"
ORIGIN      
        1 mnrleeagev gqhtpvlivg gslvglstsl flgrlgvphl lverhsgtsi hprgrgnnvr
       61 tmelfrvagv qrrieeaasv laenhgimqt ptlvgdagew lfkeidpggg larfspgawc
      121 lcsqndlepv llksarelgg dlrfstemls feqdahgita qlksretgeh staradylva
      181 adgprspire rlaigqsgpg dlfhnvsvtf tsrgladvvg drrfivcylt npeadgallp
      241 vdneehwvfh apwhpehget leeftderca dhirravgvp dldvritgra awhaaervae
      301 rysdgrvfla gdsahemspt gafgsntgiq dghnlawkla avlggwagpg llksydaerr
      361 pvaeatsara ssrsvehshp gyipapgaag pggkkggiln valayryprg avlgadqsap
      421 ivpdglrltg epgsraphmw ldragtrvst ldlyersmvl ltssdkwhsa akdvaqrlsv
      481 pldayrigsg adaelspasd tdwaevhgvt edgavlvrpd gfvawrsegp saspetalre
      541 altaildrg
//
LOCUS       WP_181648913             350 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: fatty acid desaturase family protein [Streptomyces].
ACCESSION   WP_181648913
VERSION     WP_181648913.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 350)
  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..350
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..350
                     /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=39372
     Region          8..344
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtdspavnss pyepaaqded freltrrvqa aglmrprtgq yvtgiavvwl mnalgwaala
       61 fsggtwwkvv laavwlavwh eqlaflvhda ghrqitrsrk fiqalglvhg nlmlgvcfgw
      121 wvqhhnrhhn hpnhleldpd ilrrvaifap eqaqdrkgfa rflaanqryl ffpllgleal
      181 vlriagvial rrralrkpll egglmvlhav lffgalfvll pwpsvllfla vhqvllgyll
      241 glafavnhkg lptrvgkews wlerqvltsr tlptgyigdf fygglnyqie hhlfpgmprs
      301 alrrayplvk qfcvereipy vetgvlesyr dlaehlgsas evlrgttata
//
LOCUS       WP_181648918             394 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. WAC00263].
ACCESSION   WP_181648918
VERSION     WP_181648918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=42064
     Region          56..280
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mtqymqdpal waliagtpla ataiirgkrs arslrqgnqe lkdhyaelen qysasvkkaq
       61 eqaeeatrta lksamrtlqg laaeqqlais klqskygesv ilqdlleidh mnsqfgrraq
      121 siavlcegwl grqrdvasvy dvvrsaqgri rhfqrveils qvdfavtnra vepvalalae
      181 lldnatsysa petsveinvr avpkgicivv ddagvgmnee ekaraaklls serasgvsgl
      241 gnppqfgfav igvlcerygf tvsvdstspy ggvravvllp delltsmpqp keraqtvstv
      301 pslnpsgpep aaavsttadg lpkrrrrram aivpptettg apmttgtpir seeetasimg
      361 afqrgtqsgr aalpepagrt snahdasseg hevs
//
LOCUS       WP_181648977             149 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Campylobacter hyointestinalis].
ACCESSION   WP_181648977
VERSION     WP_181648977.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter hyointestinalis
  ORGANISM  Campylobacter hyointestinalis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
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 hyointestinalis"
                     /db_xref="taxon:198"
     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=15948
     Region          79..149
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 msigkiiasi lgvlvvalmc ymllsgdgss vakdstpkie kqevkvvqke ennfqtsdel
       61 nkikelkqsi apandgvskl ylkscapcha kdgkgviaps ivgktkdell vslhdykagk
      121 mpnslmkgll dnisdenlti ladeiskfk
//
LOCUS       WP_181649086             408 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181649086
VERSION     WP_181649086.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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..408
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..408
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44545
     Region          12..408
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mghlrqeiep reagldpkal arldqhfshl vddlrlpgyl vsvsrhgrva hlrtyghrdv
       61 earlpvetdt lwriysmtkp vtsvaalmll eegrlrlndp varflpafad prvyvsgsga
      121 dtktrpagqp llirhlltht sgltfgfyhs hpvdalyrda glessvapga dlagtcdvya
      181 glplqfepgt ewnysvstnv lgrlievvsg qdldvflaer ifgplgmtda gfcvtdeqag
      241 rlaelygeda egritpiagl plhgrprfls gsggmvasay dyhrfmemlr rrgeldgvrl
      301 lkpetvdtma anhlpggvdr rtfgsalhre pgnaglgfgl gvsvvvdpei trspssegaf
      361 gwsgvasttf wvdprhdltv qfytqvrpts shsiypefkr lvheavlg
//
LOCUS       WP_181649065             112 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Campylobacter hyointestinalis].
ACCESSION   WP_181649065
VERSION     WP_181649065.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter hyointestinalis
  ORGANISM  Campylobacter hyointestinalis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 112)
  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 112)
  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 112)
  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 112)
  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..112
                     /organism="Campylobacter hyointestinalis"
                     /db_xref="taxon:198"
     Protein         1..112
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12773
     Region          2..>93
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 miylydldkt likedsaklw adfiyekglv gaefveeayd ddyangvldi deyqkhflap
       61 ikgktkqdie pllsefvdkk ikgivyddai klvnlnggsy lgykrfysts rv
//
LOCUS       WP_181649177             390 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Streptomyces].
ACCESSION   WP_181649177
VERSION     WP_181649177.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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..390
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..390
                     /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=42748
     Region          72..385
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtafndepat gealrralgl drrrflstct avataaiaap vlgaspalaq drdrghdqeh
       61 ghggdvlvpa nrrgiilytv rdatgrdpla tdlpsgfrev fkqlsrfgyr qvefagygqh
      121 anapggasle svqgakllrs wldeyglraq gnhgfippsw plttadldtf kkhleianil
      181 gmahmgtggd ptgsayradw dvaadkwnal geiarreglk lythnhdaay gflldggpld
      241 aqgnptrssg irkleyflki tdpkvvwlem difwahvaqy kfhtytahdg siqekvfdpa
      301 glvvrnnkry plfhakdgvv nttngmgydm vpfgtgvidy ttffsrvgdr nyhnpmveqd
      361 napsstdpgq slthakigyd nlaalrkrrh
//
LOCUS       WP_181649458             132 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181649458
VERSION     WP_181649458.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..132
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14190
     Region          24..119
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mpvpqhpqsa rqtahpqstd aspaitraft llsrrwngli lmalakgpad faqirerlpg
       61 istrmlaqrl qeltvidlva qdvqpglssr tryalsphgn afliplavlf lwaedhlpas
      121 sspsdqpaas gh
//
LOCUS       WP_181649468             950 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181649468
VERSION     WP_181649468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 950)
  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 950)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 950)
  AUTHORS   Rosinski,J.A. 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 950)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..950
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..950
                     /product="helix-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=101924
     Region          <6..910
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          884..939
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrstdptgdl dpgrgnqagt glrlrgrdre iaavrealvt vragrgacvv vegapgvgks
       61 rllaeldera qrcgfdvvsv radefdqyaa gaalqsvlqa sdgsaraaaa vndqrlwlld
      121 siadaleera qrapvlvlvd daqwadpatl falrtlpgrl aasrilwvla vrseaerptv
      181 arvredlerl garwltlgpl pqreleniaa dilearpsph larmlrgvag npflaielvr
      241 yfpdadavke kasaagrlyr dipvgfrqsv aarleqlped avrllqigsv lgrefdfgtv
      301 arllgrqags llsgveaaln agllaaegpr lafhhdllrq avhenlppav rtalhreaae
      361 slratgarsa evawhvvmag gpvdddavas lhtavrelss tapdaaadfa qriagllppr
      421 drrrvslltd aaeylgrtrr vhealdlvda alsdgleplq eanlrlvaae ihqaagddaa
      481 amthlqeald lpalpsdlra lllktqatgh vylgnitaae qtdtglvaas yrshdpavvv
      541 svmvfqsqtf fyrgrlaral elaeaatara yteptvpylr ppripalwla ivltttdrla
      601 dtervlregq heaealglgw slphwharra calleqgald daaveaeagl avadeleitq
      661 pnplarsvla lveirrgdla rardhlraae agsgtnaqry glwvalarac ladaegrnka
      721 aaaaltgsfe dneptrllal ppshwpgivr ialrgeepsv aqavsgalrt ltarddsqei
      781 iaavrahvdg llhsdrralt saitsyrstg rrlalaaace dlgelmstsv dtaqaircle
      841 eagqlalasg alrdherirr rlrqlgvrag aarhdtvssp gwgsltqser kliplvvdgl
      901 tnraiadrlh vsvhtvnthm rhiftklgin trveltrlav ergdiadgae
//
LOCUS       WP_181649343             385 aa            linear   BCT 28-DEC-2024
DEFINITION  FUSC family protein [Streptomyces sp. WAC00263].
ACCESSION   WP_181649343
VERSION     WP_181649343.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 385)
  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..385
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..385
                     /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=40416
     Region          55..211
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mewtgwatra vrrhggaavr avrrawrepg rerdltvqag kaalaacvaw avagwwlqap
       61 mafvapwvav vlvestvygs lahglqqvaa iaagtvvatg valvlnntmv tmvvvlpavl
      121 llvqwqrlgs qgiyaatgal fvltsgqvsl atsgariaea vfgavvgitv nalvrppvyl
      181 rdtraalqda aceaqeilda vaegldvgew dshaagerhe ralglgrlve qarsaigwsr
      241 esmrgnhrgr gtgavsppgk ayddaltvld hvavhtagvt rtvletashn gkaarpgpqi
      301 tgpyadflrh taraiglygr trfagtgtsq padgalheav eelnrsldel hrtlpgavqd
      361 dpdalathga llaqarrlad qlvqd
//
LOCUS       WP_181649196             608 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces sp. WAC00263].
ACCESSION   WP_181649196
VERSION     WP_181649196.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            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. WAC00263"
                     /db_xref="taxon:1917422"
     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=66299
     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 sappvgglad vvfdhaqedp lraafgrkde neqwrdvtaa efrdevlala
       61 kgllaqgirf gdrvaimsrt ryewtlfdya lwtigahvvp mystssaeqv fwmlhdaqvs
      121 aavvehedha mtiatvidrl pqlhklwqld sgavqelyea gtgiddevvh rhrravtpes
      181 iatiiytsgt tgrpkgcvis hanfmaeast viglmepift skrdngastl lflplahvfg
      241 rmvqvagvlg kvklghqpqm hasvllpdla afqptfilav pyifekvfna arrkaekdgk
      301 sgafekavev avryadaiea kawgigagps aslrmqhqff dkvvytkmra amggrvrhav
      361 sggsamdrrl glffagagiq iyegygltet taaavvtppe rtrygtvgqa ipgttvhiad
      421 dgeiwlhgdn ifqgylndpk atdaalhdgw latgdlgald edgfltitgr kkeilvtsgg
      481 ksvspgvlee rvrdhplvaq civvgndrpy iaalvtldse avehwlqmrg karlspsdlv
      541 rdpdletevr ravvaantlv sqaesirtfr ilanqfteeh glltpslklk rkaienayat
      601 evealyra
//
LOCUS       WP_181649550             218 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces sp. WAC00263].
ACCESSION   WP_181649550
VERSION     WP_181649550.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 218)
  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 218)
  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 218)
  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 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   5  (residues 1 to 218)
  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 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 10001925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..218
                     /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=23713
     Region          11..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mvsdehkrvl dperdagalk althplriql lgmlrqdgpa taselavrtg essastsyhl
       61 rvlakyafva eaahrdgrer rwqavhsvts wsnkamedsp asrdfvslsr rrqiehleas
      121 lvryeadvae grlgqewvep sgitdlmprl taeslselwe vigrkleela ardaedprae
      181 rvvfvaaglp laprepdaep greepgtags gteggsgs
//
LOCUS       WP_181649143             524 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA synthetase [Streptomyces sp. WAC00263].
ACCESSION   WP_181649143
VERSION     WP_181649143.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  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 524)
  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 524)
  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..524
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..524
                     /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=57564
     Region          8..512
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(178,181..186,188..189)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(181,296..297,319..324,403,415,418,429,509)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(181,221..222,269,271..272,275,296..297,319..324,403,
                     415,418,426..429,490)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(221,271..272,275,296,426..428,484,490)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mhnfasildy hlaqrpdavv vaqderrltv rqfhervnrl aaglaelgig rgdvvgllly
       61 nrpeflelvy atnrlgavfl plnyrlseee wqyilghaqa kaivtepefa paversagcl
      121 tdlehrilve ddsstepwts adartatdaw tgyedllarh pgarvepvdv glddlqrlmy
      181 tsgttsrpkg vcvtygnlqa knlahivhfg ltaadttlvc gplyhvggld mpalatlyag
      241 ggvvlqrrfd apgvlraiqe hrvtnvwlap amvnavlevp dresydttsv rfvlgggekt
      301 pepvlrrimt afpnawfada ygltetvsgd tfldrehala klgsvgrpvp htrvrivddt
      361 gkevpagelg eitlrgpkvf vgywrdekat aaalrdgwfh tgdighvded gflfiddrkk
      421 dmivsggeni atpevervly ehpavleaav vglshprwge vprafvvfrp gasagteelr
      481 efcrarlakf kvparfdivd elprtpsgkv lkrtlrdlaa gger
//
LOCUS       WP_181649748             488 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Streptomyces sp. WAC00263].
ACCESSION   WP_181649748
VERSION     WP_181649748.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 488)
  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 488)
  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 488)
  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..488
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..488
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51946
     Region          17..356
                     /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 mlagllespr saaasrmsgp gywrrllpvl gvlvcltrap sfvrplwnpd egylavqari
       61 lagggelyet vvdrkpplvp wlyeaafavf gsgsltsvrv laivaqlsta vllaslarrr
      121 wgdragrtag vlyalvsigl npedaqaatf evfilpctta amwcadrsrw gaagvavacs
      181 fltkqtggvv mvpvlwmlwr qekasrkgll wlgvgvvvpv lgaallttpa gflfwtvtgs
      241 gayvsfrgse lhvlsrgltn tgilaaacag lippilralr varagaaelw lwlgssavav
      301 lvgfhffghy ylqlipsval lataalqilp rdrlvtavfa svgccalfla wgllaprpel
      361 ghaqrlaaal hhrtdpgdrv lvwgihpety wlanrtpasr yltaglltny sggrdgpqvg
      421 ekyavegawp vfraeltahp palvvddsrg kpyapdrvss lrrllaagye eagtvdgavl
      481 yartgppd
//
LOCUS       WP_181649655             988 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181649655
VERSION     WP_181649655.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 988)
  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..988
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..988
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=102652
     Region          942..>984
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mglavvataa vvgmmsppas aepvptadea vmgpygksvl yeylysagrt gflhhtygqg
       61 wrwtdyatge sttpdipadg sagrifntha dtvayqtgts gvvlidpagg gkrtlqlpeg
      121 ftlrsvqgdt vlgvangech lfrltsdgsl ddrpvtdvps gatcglsflp dvgdgngvvv
      181 hyrsatgdgv glvdlstarm svlpvpqsyl gsvqvtpqav awydssagve rivsrddpqa
      241 tpwsvpkpyt pysvvlrlvg srvlrmtmdp grtvtvvssd gvvtkpldhg weafdnllpg
      301 pdgdllvsge lngeygvhrl sespdgglqr savldipwvp srtsslalfq grldtadtyv
      361 dnvtayherk lvvsgtpsvi trenlgdads cgasgcplyp tgdgrvlyqt vyegkavlrl
      421 vdktqptpgt tidtgltglt vesvsgryva yrtatatvvr dldsgavvrt tsaapgalwg
      481 atlwqsagag kvtatdvrtg tvsrtlsvgt scspssvqat vryvyvecga gkdtaflvnl
      541 adgtvrglpt gsapgllgdg fvvrvgadrq vtltdvtsat patrvlgtar gttagtdwtv
      601 dayggqvayv dadenvhvvp tgiavgalsv tdssvpasah vvvegpawkp rwwiskpvgf
      661 wqltiknrts gktvrtltgg eargqitpsw dgwtgvtgvg vpdatyawtv tawpadgqgp
      721 evvksgsvki tggqaayhdf vgrdrsgdll tlnssgaftf qqgtgtgtfs gktsasgwpt
      781 savavpfgtg ddqcnsvlvr lgsgelrdyr agcgtlkpst pytslgtgwn aygsltapgd
      841 ltgdsrpdll arnkstgdiy lfaaqsdgsl aagkkirtaw tgytrivgag dldgdgygdv
      901 lardkagtly rysgtgtgll kdrvkvfsnw ggsynavvgv gdinsdgksd lverdtagnl
      961 yrnngdgkgs fgarvkiatg wqgykgif
//
LOCUS       WP_181649782             352 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Streptomyces].
ACCESSION   WP_181649782
VERSION     WP_181649782.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..352
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..352
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37962
     Region          76..345
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtghdipedy lsgyalllae asatgrrltr deiesrralg eraantghgl ralvsahlsa
       61 araawpttpg sadstlaaiq qvidafaegy eraqflavrk eeaarrefid dllygrsdlg
      121 rlaeraerfg lrlshahava vaqgttayde gavvprqveq aliarfgdrn illttkhgrm
      181 lcvapgdqdd vltyfakray aatdggriai grpqpgpggv vqsyeealnt lelaerleld
      241 dpvlraadll vypvltrdrq amadlvldal gplttargga qvlldtltay fdcgcvaaea
      301 arrlslsvra ltyrlerihk ltganpadpa hrymlqtavi garllnwpaq sl
//
LOCUS       WP_181649804             272 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family serine peptidase [Streptomyces sp. WAC00263].
ACCESSION   WP_181649804
VERSION     WP_181649804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 272)
  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 272)
  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 272)
  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 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 12184331
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..272
                     /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=27538
     Region          32..265
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; smart00020"
                     /db_xref="CDD:214473"
     Site            32
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(79,132,229)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(223,244,246)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
ORIGIN      
        1 mrrpfapvla laaaaalipl aspapaatdd ivigghpvdi aqspwtvals srdrfggtra
       61 gqfcggvvig psqvltaahc lsplvlgvpp qqmhdlkiia drtdllsdkg keipvrdtwv
      121 npqydavtna gdfavitlas plpqssvirm apsgdptyap gtaatvygwg dttgtgnyal
      181 glrsagvnvl sdsvcerayp gsengtyqat smvcagaaag grdacqgdsg gplvaqgrli
      241 glvswgsgcg qagspgvytr vsdvvkalgk rr
//
LOCUS       WP_181649806             252 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Streptomyces sp. WAC00263].
ACCESSION   WP_181649806
VERSION     WP_181649806.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=27004
     Region          44..236
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mpydpsafpp favtvdlvvl tvrrhalcal avrrgeqpfq grwalpggfv rpdedlaqaa
       61 arelveetgl cahdpsapaq dngahleqla tygdpkrdpr mrvvsvahla lapdlpapra
      121 ggdansarwa pveellqqsg ygrdgeqaap lafdhaqils dgverarski eysslatafc
      181 pseftvgelr rvyeavwgva ldprnfhrkv tgtpgflvpt ggtttrqggr paqlfragga
      241 tllnppmlrp ev
//
LOCUS       WP_181649875             390 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Streptomyces].
ACCESSION   WP_181649875
VERSION     WP_181649875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..390
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41026
     Region          67..389
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpartrtvta vaaalvlgla agplavpava asstaprtat agtvttgpda aalraalagl
       61 pdadataalv rvggtdgrwl gsggvhdlts graadpdalf ragsttkvvt aavvlqlaae
      121 grvdlgapvq rylpgllspa fkpvsvrrll nhtsgiqagd gfgdsfeday ahrfdtltpr
      181 qvvasavakg pefrpggrqh ylninytilg mliekvtghs yaseatrrvl rpagmphtyf
      241 pgtdprirgp hnlgyqavkr adgttefvdv tewnqadrwa agdmisttad lerltlhlfr
      301 gelvpepqlk emftvpsgid gatmsagler feyggrvywl ksggrygytt vmaatrdlsr
      361 tlvysvnatd akgeemnpva lriamaalkq
//
LOCUS       WP_181650018             328 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Streptomyces].
ACCESSION   WP_181650018
VERSION     WP_181650018.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 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   5  (residues 1 to 328)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..328
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..328
                     /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=36220
     Region          16..238
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          <262..321
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpsllhfged dllncrfavs plwetqeavr tlnrparhgy hahwlrrira aadgldlapl
       61 wllmpqrgyc pdwlcpppig paatfeeeia avraadpeaa reeaarslad tpgalesprg
      121 rsllkdptrm vqeladlmet awhalvepdw prlrallead iafhsrrlae vglggllpei
      181 drrfgwrsht ltiewkgrhe rdlagqglil vpsvfiwpev vssfdppwqp tlaypargig
      241 glwaeptdht pdalvrllgr gratvltald epttttalah rlrlapssvs ahltvlragg
      301 lltsrryghq vlyertplgm alasgpeq
//
LOCUS       WP_181650091             607 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Streptomyces].
ACCESSION   WP_181650091
VERSION     WP_181650091.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 607)
  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 607)
  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 17317557
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..607
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=64743
     Region          6..178
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          58..87
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          122..412
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          126..151
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          157..182
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          196..232
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          236..264
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          267..296
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          299..328
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          319..568
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          363..391
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          507..536
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          539..566
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 mdvmgdkatl ldtgrfvqps drdetgeaae earqrlaaea gdveamsvlg amllrrgdld
       61 gaepqlraat aagdraaann lgvllhqrgy tdeaagwwri aavagsaaaa halgryhrer
      121 gdepaaeywl rqsaeqghal gayaladlle hrsdvgaeqw mraaaerghr eaayrlartl
      181 drkaadageg rgdngvigvi gaageeaeqw yrqaaarghr raalhlgail ekrghlkeag
      241 rwyltsakdg earaacalgf llrdagdtes aavwwlraaq dgdgnaanal galhaerget
      301 qtaerwyraa mdagdvngay nlgllcaeqg rtaqaeqwyr raayaghrea analailllq
      361 vgdsagaepw fskaaeagsv daafnlgilh agrgseddee aalrwyeraa saghteaalq
      421 vgiarlrdgd epeaerhlrc aagggsaeaa yrlaavldar rppapahelg eptqeksece
      481 ewyeraaslg hrraqvrvgm laaargdvve aarwyrsaae agsrngafnl glllaregse
      541 peaalwwtra adaghgraal rlalvyarrg elaegqrwad ravalgpaev aeraarlrda
      601 lrqelsa
//
LOCUS       WP_181650061             445 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Streptomyces].
ACCESSION   WP_181650061
VERSION     WP_181650061.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 445)
  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 445)
  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 445)
  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 445)
  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 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   6  (residues 1 to 445)
  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..445
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..445
                     /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=46973
     Region          <145..426
                     /region_name="MtrAB_MtrB"
                     /note="MtrAB system histidine kinase MtrB; NF040691"
                     /db_xref="CDD:468655"
ORIGIN      
        1 mrlpsrrfrp prrlppwaat ltwkaaafit vmccglaall gvlvhvsvtn qtvgeargra
       61 ldrlaevtad yeagdrlppg agldlpglpa plrelatdgr rgtmvgdndp hptmwaagpa
      121 sggralavqf dysqgahaid aldrsivwss alaigatllv gvfavtrvtr rlhataqvar
      181 risagdldar vndprtavdp rtrypagpqd evaavagald tmasslqskl tseqrftadv
      241 ahelrtpltg lhaaaellpp grptelvrdr vatlrtlted lleisrldag relleldsep
      301 laplaervvr asgtetevrv vddvrvetdr rrlervlgnl vanahkhgeg pvvltvdgpv
      361 vtvrdhgggy peyllehgpq rfrteggskg hglgltialg qaevlgarlv fanapeggai
      421 atltlpqder gapgptggeg ptgar
//
LOCUS       WP_181650108             526 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: dipeptide ABC transporter ATP-binding protein
            [Streptomyces].
ACCESSION   WP_181650108
VERSION     WP_181650108.1
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  :: 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..526
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..526
                     /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=55944
     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 mslvevtdlt vgfgslravd glsfrlakga alglvgesgs gkstvasall glhrgtgaev
       61 ggsvrvagid vqeasdaelr rlrggkaamv fqdplssldp yyavgdqiae vyrvhvkasr
      121 raararavev ldrvgipdaa rrarsrphef sggmrqrali amalacepdl liadepttal
      181 dvtvqaqild llhtlreetg mglllvthdv gvaaesvdei lvmrhgrave hglvgavlga
      241 paqaytqell gavprvdapr tasavteevv leasglrref grgkkafaav ddvsltihrg
      301 etlgivgesg sgkttlgrml vglleptage ikpgggvrpd vqmvfqdpvs slnprrsvge
      361 siadplraqg erdegrirgr vrellervgl eaahydryph efsggqrqrv giaralaadp
      421 rvivcdepvs aldvttqaqv iallaelqre lglalvfvah dlavvrqvsd rvavmrrgri
      481 veygpadevy esprdpytkq llaavpaldp evaarrrtar rqltav
//
LOCUS       WP_181650280             206 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181650280
VERSION     WP_181650280.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 206)
  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..206
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..206
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=21803
     Region          17..79
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
ORIGIN      
        1 msawqplpee lpaevrhfve qlrllkdrtg mslvalgtrt aysksswqry ldasqppprq
       61 avvalcrvag vageeterfg vrwelavraw prepvppvss vppvppvrvp aggpvpgpvs
      121 vpggepapga easvpavqgv pvaradsaar grdgyeedpt lpwwdlldee ssrrpagprt
      181 prlllyaall avvillaavv gavtlg
//
LOCUS       WP_181650312             201 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Streptomyces].
ACCESSION   WP_181650312
VERSION     WP_181650312.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=21744
     Region          6..114
                     /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 mpfdhndhyh rmllrklpkh grvaldvgcg tggfarrmaa rgyevdavdp saeviavarr
       61 igggprfrrt dvasaglpkg hydvitclas lhhmpfgtvt rfrealapgg vllvlgcyag
      121 itwwdlaavp snavaragva vgerlrggga vpprapvrep rmsladvrse adrllpgsrv
      181 rqllywryll tyrvggvdrv t
//
LOCUS       WP_181650057             586 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: beta-ketoacyl-[acyl-carrier-protein] synthase family
            protein [Streptomyces].
ACCESSION   WP_181650057
VERSION     WP_181650057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 586)
  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 586)
  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..586
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..586
                     /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=61729
     Region          174..584
                     /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 mhrssdvpvq phavtvaevi pgdlvalseq dvaentwyvv mhtlpetpht irltlrpplg
       61 gidhdevfer ghqvttacrr mdvgaipeit stdlgpvefr dgdritslra vdpraveesy
      121 trrwghwhrd ldrraedpvp deelrnlaeq vtqkghvvrh yprprraaea yaprrvvvtg
      181 lgavtplgvg veelwrglve grcgiseleg eefaelpvri agsvpvdpvg llprpqarrm
      241 nrsaqfavla areawqdagl dpagttesgl apervgvsvg ailgdasvlv gadrklrdkg
      301 pravsplttp mtvpsqaasq vslalritge artvtsacas gteaigqaid rirygrvdva
      361 laggaeavvt paimasfaam ralsthelgs tspsrpfasd rdgfvngega gfllleaeeh
      421 arargariyc eaagwglsad ahhmaapdps gsgvalalrr avhdagahvv dvvhvnahat
      481 atvdgdlaea salravlggs vpvtalkghl ghlqgaaggv eavatvltlh hglipptigc
      541 ddqddaidld vvtkrprrlp algdlalsns fgfgghnavl alrrtg
//
LOCUS       WP_181650391             416 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LolA family protein [Streptomyces].
ACCESSION   WP_181650391
VERSION     WP_181650391.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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..416
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..416
                     /product="LolA family protein"
                     /calculated_mol_wt=41979
     Region          <116..296
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mapyesdrta gaeglpdead dvragrrkaa ryvvpvavvg vaaatiglvp aladsgdpsl
       61 pkitaeqlie kiaksdvqql sgtvkvstdl glpslggles gmlsgvtkgs ggssadpqsk
      121 lmelasgtht vrvaadgpdk akvsvlenaa eysiihngnd vwaydsksne vyhstapaae
      181 kgqekapkdv pttpkqlade alksvddtts vtvdgtaqva grdaykllik pkqsgstvga
      241 itvavdaktg vplkftlvpt sggaavvdag ftqvafakpa astfdftppk gakvtegkds
      301 kgskdlkgsk dskapesaps rgdlgkgldg lktvgkgwst iaefdtggqg mpsgsssqgg
      361 nvsgflnslg dhvkgkfgsg tvfstrlvna litddgkvya gavtkdalvk aanaah
//
LOCUS       WP_181650411             634 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AMP-dependent synthetase/ligase [Streptomyces].
ACCESSION   WP_181650411
VERSION     WP_181650411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 634)
  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 634)
  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..634
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..634
                     /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=68371
     Region          38..632
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mstqpspyds ppslvepeir rldgvvrevs vprlvgqvth gsladipfdn aavapnaavl
       61 srknadgawe dvtatefaaq vlavakglia eglapgdria imarttyewt lldfaawaag
      121 lvtvpvypts svfqvrwilq dsgavalate tvaqasslgp erdripdlrh mwvfekghle
      181 rlaelgqdip dqevavrrgv lgpdtlatli ytsgttgrpk gcalthgnff aeidnaiell
      241 ypifkaktsd aasmllflpl shvfgrmvav aclrarvrlg hapslstedl ladlasfrpt
      301 fllaipyvle kvfntgrata ekmgrgssfd raariacsyg eaieakqhgt gpgpsrslra
      361 aralydplvy rrirnalggk vryaicggsp lgrrlaafya gagieifegy glteataaat
      421 vtpplkprlg tvgwplpgtr vriagdgeil lggeqifrgy wdpnaggvvd aapdgwfatg
      481 digelddggy ltitgrkkei litaggksva paplenwlrs hpliaqcivl gdrrpyvtal
      541 itldqdgvth wrqmigkhpv ppellmddpe lnvilqraid eanklvsrpe sirrfavlpg
      601 dftelaghvt ptmklrraai erdfskeiee lyvr
//
LOCUS       WP_181649808             732 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RecQ family ATP-dependent DNA helicase
            [Streptomyces].
ACCESSION   WP_181649808
VERSION     WP_181649808.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 732)
  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 732)
  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 732)
  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 732)
  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 732)
  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..732
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..732
                     /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=78185
     Region          36..576
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 msnddprppt htdlpntdlr aaadvvlarl vgapagearl redqwraiea lvadkrralv
       61 vqrtgwgksa vyfvatallr ergagptviv spllalmrnq veaaaragih arsinssnte
      121 ewetiqaeva asevdvllvs perlnnpdfr dqvlpklaaa tgllvvdeah cisdwghdfr
      181 pdyrrlrtml adlppgvpvl attatanarv tadvaeqlgt gastdalvlr gpldreslsl
      241 gvlrlpdaah rmawlaehls dlpgsgiiyt ltvaaaeevt aflrqsghtv tsytgktena
      301 drqqaeedll anrvkalvat salgmgfdkp dlgfvvhlgs psspiayyqq vgragrgvkh
      361 aevlllpgke dqaiweyfas iafppeeqvr rtldvlarae rplslpalep lvelrrsrle
      421 tmlkvldvdg avrrvqggwi stgvpwtydt eryawvakqr aaeqqamrdy vsttgcrmef
      481 lrrqlddela kpcgrcdica garfeasvsp taldaangel gragvdvdpr kmwptglpav
      541 gvdlkgripa geqaasgral grlsdigwgn rlrpmltpqa pdgpvpddva kavvgvltdw
      601 akgpggwasg qpdaqprpvg vvtmasrrrp qliqslgari aevgrlpllg sveyvgeava
      661 qvsrsnsaqr lkaldgalav ppalaaalke aggpvllvdd atetgwtlav aarmlrrsga
      721 qgvlplvlav qa
//
LOCUS       WP_181650416             463 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181650416
VERSION     WP_181650416.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..463
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48307
     Region          13..423
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mttapagtta pitpeygdrv iavetagsep ipdaerhgsp lqllwtwasp niefatvyig
       61 visvlffgln fwqaaaalll gtalgaltqg vlsldgprfg vpqmvigrls fgyrgnllpa
      121 gvnalvagvg wfavnsvsaa falntltglr plpslllvva veivigfigh nfvhafekya
      181 fpalavvflv agvwtfdhad lgasgggggi ggfllafsta wgyaagwnpy atdysrylpr
      241 tanrfrtaly pavglflsva vvslvgaasa tiaapagatp taaftghlps wlgdlvllsi
      301 ilggisanal nvyssamsit slglrlpawl grgalvvisg vagtaaawas lsdaghayea
      361 fllviaywig pwlgvvlver wlrtrtpddq parrlgdraf tnwpgitall vgvavsvplf
      421 snqekyvgwv pkhwasfgdi tclvgfalsa alyallrrap rtg
//
LOCUS       WP_181650478             412 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: threonine aldolase family protein [Streptomyces].
ACCESSION   WP_181650478
VERSION     WP_181650478.1
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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..412
                     /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=45238
     Region          65..347
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 msdtaetaag qdpmtvgqdp etagqdpesg gqdpeeaaer lrarrsaalr aarrvlwqps
       61 hqhtvrerla wlndgaegvy dldrpvdmyg gqivetleer vagllgkeaa affptgtmaq
      121 qvalrcwagr tgnptvalha lghpevherq afsqvsglrp vrvtdeprlp taqevrdfee
      181 pfgalllelp lrdagfvlps weelsevvea ardrdavvhf dgarlwects hfgrpldeia
      241 gladsvyvsf ykslggfgga viagpktlid eaktwrhryg gmilqqfptv laaligldre
      301 lprlpeyvah arvvaaalre gfteakvpwa rvhpeephth qfqvwlpydp dvltdaalrq
      361 teetktslfs qswmrggpgl altevtvaap alewtaqdvr aavrefverl pg
//
LOCUS       WP_181650545             411 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181650545
VERSION     WP_181650545.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 411)
  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 411)
  AUTHORS   Rosinski,J.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..411
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..411
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45186
     Region          9..73
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          122..>268
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
ORIGIN      
        1 mrglgdhlsi geriafyrkr rgytqevlag lvgystdwla kietgrrkpp ridmlaelsr
       61 ilrvplgdll gqavlveder qqddvpavrd almsprrlsr llfgreaevq lptpapvavr
      121 veqawndyqg grlgsviaal pallqtaqel eeraarrged rsdcwavsar thhlaattla
      181 kigesdiswl aaeramraad esddplvlas aarsgthall angryddale lgntaaawls
      241 sraaendpaa lsllgmihlr aavaaarhqd rptatglldr aeeladdlgs denywqtgfg
      301 ptnvllhrls veldldnvsy vvehgrinvd hmpqersvsh ridfaralsl agqgdeafte
      361 lrtaertspq lvrnnprvre tlrdlikqsp vtrgsrssev fvmaqrcrav q
//
LOCUS       WP_181650564             626 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Streptomyces sp. WAC00263].
ACCESSION   WP_181650564
VERSION     WP_181650564.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            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 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..626
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67447
     Region          <42..>99
                     /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          159..317
                     /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          383..625
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mtesngsieq qqaampdwek rfraprvslp dwaedaphra lfvsnatgty elyawdrgtg
       61 eqrqvtnran gttdgvlspd gewiwwfddk dgdefgiwrr qrftapkstd sgdgdggldd
      121 gdgdgvaead apaapgleps ypgglaigrd grtavvgrst dedgstihvv rlgeepveiy
      181 rhresagvgd lshdgsliav ehtehgdamh salrvlrpdg stvtelddtk ggtvelglea
      241 lgfapvdgds rllighqrrg rweplvwdvs tgeetdlald lpgdvaaewy pdgsalliah
      301 sfearsdlwr ydlasrelvq vptpqgtvsg atarpdgtve ylwssaaeps vvrsttgeiv
      361 ldppglkspg svpvedvwvd gpggrvhali qkpagttgpl ptvfdihggp twhdsdsfaa
      421 gpaawvdhgy avvrinyrgs tgygrewtda lkhrvgliel ediaavrewa vtsgladpar
      481 liltggswgg yltllglgtq pdawtlgiaa vpvadyvtay hdemealkam drtllggtpe
      541 evperfeass pltyvdavka pvyisagvnd prcpirqidn yvarltarsa ihevyrydag
      601 hgslvvderi kqvkleldfa trhlph
//
LOCUS       WP_181650561             137 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: cytidine deaminase family protein [Streptomyces].
ACCESSION   WP_181650561
VERSION     WP_181650561.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Navaratnam,N. and Sarwar,R.
  TITLE     An overview of cytidine deaminases
  JOURNAL   Int J Hematol 83 (3), 195-200 (2006)
   PUBMED   16720547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..137
                     /product="cytidine deaminase family protein"
                     /EC_number="3.5.4.5"
                     /GO_function="GO:0004126 - cytidine deaminase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009972 - cytidine deamination [Evidence
                     IEA]"
                     /calculated_mol_wt=14744
     Region          <39..131
                     /region_name="Cdd"
                     /note="Cytidine deaminase [Nucleotide transport and
                     metabolism]; COG0295"
                     /db_xref="CDD:440064"
ORIGIN      
        1 mttqihpvdh eliqaaahva rtrcqgdnht maaaarardg rivtavnayh ftggpcaemv
       61 vigaaaaqga yeldtivavg drdrgvvppc grcrqvlldy fpalkvivge ddrirtvlit
      121 dllpesyiwa dhrldae
//
LOCUS       WP_181650384             262 aa            linear   BCT 28-DEC-2024
DEFINITION  NuoI/complex I 23 kDa subunit family protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181650384
VERSION     WP_181650384.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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 262)
  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..262
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..262
                     /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=27674
     Region          11..166
                     /region_name="PRK05888"
                     /note="NADH-quinone oxidoreductase subunit NuoI"
                     /db_xref="CDD:235637"
ORIGIN      
        1 maeplpptrs ripgsglakg lavtlrtmtk ktvtaqypda qpelpprsrg viglfeenct
       61 vcmlcarecp dwciyidshk etvppaapgg rersrnvldr faidfslcmy cgicievcpf
      121 dalfwspefe yaetdihelt herdklrewm wtvpappald pgaeepkela aarktadkla
      181 aeaataaeaa elaartaeqa aqpeppadgt ttttgpttae ttgttsgttt datsgttsgt
      241 tsgttsgtpe pskpsdpqdg as
//
LOCUS       WP_181650568             431 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Streptomyces].
ACCESSION   WP_181650568
VERSION     WP_181650568.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=45490
     Region          104..423
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mirqlivsyv llvavaltaf tvpvaftlts qlrgdteasv rreantmalm laqgdpasra
       61 alnrlataya drtpghvdvl pasgtdgtdt arwgdgalrv tvpairdnhi vgavrvtypt
      121 sdltarlwri wgfrailavg vlavaaglga lvarrltrpl rqlnemaskf gdgdltarsp
      181 vtgppetqrl artlnsgaer ldtlidsqri fvadashqlr tpltalrlsl dniadgveda
      241 fvredvdqat aevvrmsrlv ngllvlarae akvsaaealp lrelvenrla vwrpaaeerg
      301 vtiaqegelg grslvlaspg hldqvldnil snalevspdg svitvkvavr pdevvlsvld
      361 qgpgmsdaek arafdrfwrg qgltgrsgsg lglaivkqlv addggtvalr dapggglwva
      421 vslrasprsg g
//
LOCUS       WP_181650599             128 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181650599
VERSION     WP_181650599.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..128
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14131
     Region          26..122
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnrpthrard saarhdaetr tqvdegitrv fqllgkrwng pimsvlitgp tyfadlrrai
       61 pgisermlsn rltelaatel vvrevdkgpp lrvsyrltea gaalgpalke laqwaktrlp
      121 epsrptcc
//
LOCUS       WP_181650709             591 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Streptomyces sp. WAC00263].
ACCESSION   WP_181650709
VERSION     WP_181650709.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 591)
  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 591)
  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..591
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..591
                     /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=62062
     Region          1..466
                     /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 mrkvlianrg eiavrvarac rdagiasvav yaepdrdalh vraadeafal ggdtpatsyl
       61 diakvlqaak dsgadaihpg ygflsenaef aqavldaglt wigpppqair dlgdkvaarh
      121 iaqragaplv agtpdpvsga devvafareh glpiaikaaf ggggrglkva rtleevpely
      181 dsavreavaa fgrgecfver yldkprhvet qcladthgnv vvvstrdcsl qrrhqklvee
      241 apapflsddq vaelyssska ilkeagyvga gtveflvgtd gtisflevnt rlqvehpvte
      301 evagidlvre mfriadgeel gygdpalrgh sfefringed pgrgflpapg tvtlfappsg
      361 pgvrldagvq cgsvigpawd sllaklivtg atreqalqra araleefeig gmatalpfhr
      421 avvkdpafap eltgsvdpft vhtrwietef andipaftdp aevaeaedep gresvvvevg
      481 gkrlevslps slgmslartg laagakpkrr aarrsgpvas gdtlaspmqg tivkvaveeg
      541 qevkegdlvv vleamkmeqp lnahrsgivk sltaevgasv asgaamceit s
//
LOCUS       WP_181650770             147 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycine-rich domain-containing protein
            [Streptomyces].
ACCESSION   WP_181650770
VERSION     WP_181650770.1
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 10008452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..147
                     /product="glycine-rich domain-containing protein"
                     /calculated_mol_wt=15498
     Region          19..140
                     /region_name="COG4278"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443419"
ORIGIN      
        1 mtatandqkt gravageelf eslahfvvih ngqsseraer iadqavaflv taatatvpmv
       61 psddvdfglh alilhtkeya elceqyagrf lhhspmpggg ardpekvaas ahamkaagfa
      121 vfddlwtvng anlaqcdsdc grpygra
//
LOCUS       WP_181650918             608 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. WAC00263].
ACCESSION   WP_181650918
VERSION     WP_181650918.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 608)
  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 608)
  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..608
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..608
                     /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=64040
     Region          <71..>207
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          192..388
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mtapipsger ptlrasapap lltalaaava vvvavslapd sarvplawgt gaaavllcva
       61 vavaaralqt aklarrrldt vaqdagrllq erarmaeefn qersrlaees ardrarlada
      121 dareralltq gfeeerqrlt teiaeerrrf aelaeentrl termrragsd raaaisatan
      181 aagrmqalst gmladlrame ekhsdeevla dllhldhrta qagrladsva vlagarsgrr
      241 warpivmesi lrgamgrigg yqrvrvhsas daavaghaae gvmhalaell dnaanfsppt
      301 aevhvyveev pagvivsved sglvmgdvql rraeravsad aenaadlggl tgtrlglavv
      361 grlarkhglk vsfrpsargg tgvlvlipqd ilslpsapvp aapaatepqa kpaaatpsde
      421 drplaeprpq asyaaarape dldpdpvpth esprhatttd tppngtpttg tpatgglpkr
      481 rrgrtlahae rsrahltnqa dpeprttdsk ataarfssfr qavrgtapdq aavqgtvpee
      541 davrptayta edavrdelaq eepvrvestq desgnavrge eavrepapah pshatshtss
      601 hpegdtts
//
LOCUS       WP_181650980             243 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Streptomyces sp. WAC00263].
ACCESSION   WP_181650980
VERSION     WP_181650980.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..243
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25136
     Region          78..242
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mtstqttdat vremvhrrqr rrrtvvvslv aalvvvaaal vgaglvrann tapgkapsrv
       61 paglaadksg vaastgavrv dvyldylcpe crrteraltt aldslrahgg vsvvyhpvaf
      121 lddrsapagy stqaasaaac aadagrfeqy stvlfskqpa eqgpglseaq liaagrdagi
      181 taasfarcve dapylpwvry vsdlaasrkv altptvmvag rrvdvtgsdp ggaltravta
      241 arr
//
LOCUS       WP_181651057             460 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Streptomyces sp. WAC00263].
ACCESSION   WP_181651057
VERSION     WP_181651057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..460
                     /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=48576
     Region          17..350
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 massahalae atpasrdkyv dllrvaslgt vvlghwlmaa vsvrgdgrae vgnllavepr
       61 lqlltwalqv mpvfffvggf shalsyrslr rkagengeng eagenggaal ysvflrarlq
      121 rllrptvvfi gvwgalalal qlagreggll dvslrlvaqp lwfigiylam vaftppllrl
      181 herygwgafg glaaaaglvd vlrfgfgvpy veflnfafvw lavhqlgflr adgklrrpyl
      241 lagaglagav llvaygpypl smvgmpgeki snmapptfal lchglwlvgg veslrgparr
      301 wlrrprvwra vvaangvsmt aflwhltaml gvygallalg vrlpepatgv wwaqvpvrvv
      361 vaggvtallv tvfrrfeqps avvlgetgvs pagarpaaal gvtlclfgvl glsmvgfggl
      421 legrtavlva vrvtapvava mtlagwllve ragrgrpaaa
//
LOCUS       WP_181651166             205 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces sp. WAC00263].
ACCESSION   WP_181651166
VERSION     WP_181651166.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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 205)
  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 205)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 205)
  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 205)
  AUTHORS   Rosinski,J.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..205
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..205
                     /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=23394
     Region          18..108
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 meepeeplpe erqvrtldar tlrgiahplr mqllyalrqr gpatasmlae rlgessgats
       61 yhlrqlathg fvedapergk grerwwqavd qgvifnanll kdadptvrga adtflhevat
      121 thtrelstwl gtradwsedw yrasdmsdwt lrltaaqsre liekmhdlle syrplaraed
      181 dpdaeqvrfh thafpltqdr tethp
//
LOCUS       WP_181651101             447 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: UDP-glucose dehydrogenase family protein
            [Streptomyces].
ACCESSION   WP_181651101
VERSION     WP_181651101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=47976
     Region          4..445
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 malkitvigt gylgathaaa maelgfevlg ldvvpekiem lqrgevpmye pgleellrkh
       61 vagiegstgr lrftmdwaev gefgdvhfvc vntpqkhgey acdmsyvdaa fetlaphlsg
      121 palvvgkstv pvgsaerlar tlaelspage daelawnpef lregfavqdt lhpdrlvvgv
      181 rsdraekilr evyatpvseg spfvvtdfpt aelvktsans flatkisfin amaevceaag
      241 gdvallaeai ghderigkkf lragigfggg clpkdirafm aragelgadq altflreids
      301 inmrrrgqmv emarealggg sflgkrvavl gatfkpdsdd vrdspalnva gqihlqggqv
      361 tvydpkgman akrlfptlgy adsaveavrg advvlhltew refreldpav lgeaasarll
      421 ldgrnaldpe vwrragwtyr amgrpna
//
LOCUS       WP_181651256             761 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Streptomyces sp. WAC00263].
ACCESSION   WP_181651256
VERSION     WP_181651256.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 761)
  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 761)
  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 761)
  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..761
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..761
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=76316
     Region          37..>257
                     /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 mtsatdplpp apgpsvapga paaeppqeps ptpaaprwsl paliaimala talyswnlsg
       61 sglnsfyssa iysgtqswka wffgsldagn fltvdkppla lmvmglscri fgfgtwqmml
      121 pmivaalgti wilhssvkrv fghaaaalaa lvlaltpitv ainrdnnpdt lllllmvsga
      181 alglratrdg rllpllgsav cfglafntkm lqgyialpav favylyashl gwakrirnll
      241 latvalavss fwwatavslv paddrpyigg stdgtawnli fgynglgrvl ggegnggggg
      301 ggggfsgsag lgrlfndilg gqiswlipfa gialagglvl cgrapridpt raalvlwggw
      361 lllhyltfat aegtmhpyyt tavapgiaal cggggvmlfr afrggdvrws wvlpaglavt
      421 giwavvllrr atdwntwlwp aiavvmalav vglfvfrsgn rirllaasla aavvaalagp
      481 aaysfavpas aggagggmgg tnptagpstg qggfgggrgg pggnvggpgg gempggtqqg
      541 gqaagqeggq vtpggggtge lpggapqgge nggfpgggtg gqngefpggq aggengtapg
      601 gtggqrggfg ggggmggets selisylekh qdgakwllav snsqsagqli lsthkpvism
      661 ygftgadkgm tvaklkelvk kgelhyiqvg gsgmgggmgg dnstssavta wvqknatavk
      721 esaysktsss esssatgses engqstqsas tlyrldpsdl n
//
LOCUS       WP_181651272             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181651272
VERSION     WP_181651272.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..332
                     /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=35618
     Region          34..290
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mvtrivsrag hgpggaweta larphprlrp gvisyrgfrl aldrprrrle apigaatlll
       61 gfeqplrisr vgrppvtlrs vfsgptttaa vgehdgrlag ievllapwaa ftlfgtpqye
      121 ladrtldpde lphglgsrda gpggrrlrsv gelsaalaal pgwperfell ddvlvrwhsa
      181 gtpgsarvvr awaqlqrtwg avpvarlaed vgwsvrqlen rfreqiglgp kaaarvlrle
      241 rarrllaagr sqaetaaacg fydqahlsge framtgctpr eftaargaqp vprpgppgad
      301 rmageatslv lspdrsdrsd rgaifsktgg lr
//
LOCUS       WP_181651293             315 aa            linear   BCT 28-DEC-2024
DEFINITION  GDP-L-fucose synthase family protein [Streptomyces sp. WAC00263].
ACCESSION   WP_181651293
VERSION     WP_181651293.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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 315)
  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 315)
  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 315)
  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..315
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..315
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35408
     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 mdhrariyva ghtgmvgaav vrrlrsagye dlalrtrael dltdqvavre fmakerpayv
       61 vdcaarvggi kanmsfpaef lyenlqiqnn liwsakeagv rtflflgssc iyprgcpqpm
      121 reeffmtgrp eptneayaya kiagmklcey ihaefgrnfv scmptniyge gdnfdpgtsh
      181 vipalvrrmh earaagasev liwgtgdsrr eflhvddlad avlwllrhhr grrflnvgtg
      241 qdisvrelae rirrlvgfeg slvfdaskpd gmprklldvs alhesgwhhr ievdeglrrt
      301 ydwylthiar vpata
//
LOCUS       WP_181651330             379 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181651330
VERSION     WP_181651330.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..379
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39938
     Region          37..370
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msvrtglvaa tavalaaala gpavaapaga ghhgatraam daavkagvpg vtatardtgg
       61 twsatagvgd vrtlaprgta dhyrvgsitk tfvstvllql eaerrlsldd kvekwlpgvv
      121 rghghdgrri tvrqllnhts gifnytaddd fartyflkdg flehrydtkt peqlvaiama
      181 haplfapgts wsysntnyvl agmviekvtg hsyateirrr vveplglrat svpgtrttlp
      241 rpsshayskl srattgptyd vtrlnpslas sagemisdsa dlnrfyaalm ggrllppkql
      301 kemrttvkad gipgaryglg lidrelscgv hvwghdggih gstssavtta dgrhslafnf
      361 ngdwsgdsda viegefcgk
//
LOCUS       WP_181651437             256 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181651437
VERSION     WP_181651437.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=26913
     Region          48..160
                     /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 mtpttstptt asatatapar rglrdfyedp svpvasgtpr slrqarilaa algpatagar
       61 tvldigcgdg taaataapll aghrlvgvdw sqdalrraha rlpyairgel tdgglpfada
      121 aadavlfsev iehlvdpdsa ldeirrvlrp gghlmlstpn laawynrall lagvqpvfse
      181 vslraihgrp grevvghlrl ytaralrefv taagfevvrl sgapfhgvpr plrpldrlac
      241 atpalssill lharrt
//
LOCUS       WP_181651604             269 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Streptomyces sp. WAC00263].
ACCESSION   WP_181651604
VERSION     WP_181651604.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  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 269)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..269
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..269
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29114
     Region          5..248
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mpvlpgaepf rheggevgvl lchgftgspq slrpwaeyla ergltvalpl lpghgtrwed
       61 mqltgwqdwy aevdrelral rercaqvfvf glsmgaaltl rlaakhgdev sgivvvnpan
      121 kvhgaaahal pvlrhlvrtv sgitsdiake gvaevgydrv plhaahsmrn fyrmadgelp
      181 qvtqpmlllh spqdhvvppv dsarilsrvs stdvteille qsyhvatldh dadrifeesy
      241 afiarlapsv gkrsdtgqvg qqegtatgg
//
LOCUS       WP_181651663             286 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Streptomyces mirabilis].
ACCESSION   WP_181651663
VERSION     WP_181651663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces mirabilis
  ORGANISM  Streptomyces mirabilis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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 286)
  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 286)
  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..286
                     /organism="Streptomyces mirabilis"
                     /db_xref="taxon:68239"
     Protein         1..286
                     /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=29085
     Region          37..286
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mratavvscg lgvpprgfqp ptrgstlkss kkftgikrvl algavalatv slqpvsaqaa
       61 ptpvvggtra aqgefpfmvr lsmgcggaly tqqivltaah cvsgsgnnts itattgvvdl
      121 qsssaikvks tkvlqapgyn gkgkdwalik laspvnqptl kiatttaynn gnftiagwga
      181 areggaqqry llkatvpfvs datcqqaygs dlvpgdeica gfvqqggvdt cqgdsggpmf
      241 rkddsgafiq vgivswgqgc aepgypgvys evstfaadia raastl
//
LOCUS       WP_181651664             589 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 35 protein [Streptomyces].
ACCESSION   WP_181651664
VERSION     WP_181651664.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 589)
  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 589)
  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 589)
  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 589)
  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 589)
  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..589
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..589
                     /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=64249
     Region          10..323
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mseftvgdtd flldgrpvrl lsgalhyfrv hegqwghrlg mlramglncv etyvpwnlhe
       61 prpgeyrdvq algrfldavr eaglwaivrp gpyicaewen gglphwltgr lrtrdeeyvg
      121 hverwfhqvl heivprqidr ggpvlmvqve neygsygsdq vylrrladvl raegvsvplv
      181 tsdgpedhml tggsipgvla tvnfgsrara afevlrrhrp egplmcmefw cgwfdhwgge
      241 hvvrdagdaa ralreilecg asvnlymahg gtnfagwaga nrgggalheg plepdvtsyd
      301 ydapidelgr ptekfwrfre ilgayadgpl pelppapapl gagaavdlge waaldavlet
      361 lggrdaeyav pptfeeldvd rglvkyevtv pgprgpyplv lrglrdlavv yvdgvaagvl
      421 teddpglkep vagharveaw veslgrvnyg prsgepkgit ggmlherqfl hgvrarglrl
      481 dafdaggvgr vpfgglpaeg grglyrgtvq vrgagdafle lpgwtrgfvw vngfclgryw
      541 svgpqrslyv pgpvlregan evwllelqep sptapvlrrp daaasapgr
//
LOCUS       WP_181651707             303 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate kinase family protein [Streptomyces].
ACCESSION   WP_181651707
VERSION     WP_181651707.1
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 10100215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..303
                     /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=30826
     Region          1..292
                     /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(33,240,243)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(185,210,238,241..242,245)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mivvageali dlvpqgagal vglrparggg pyntalalgr lgsptafcsr vsydafgdal
       61 lgglreagvd vssvqrgtep ttlavasida dgsaaysfyv egtadrlfaa perlpdatra
      121 vsfgtcslvl epgasayeel mraaaargvf ttldpnirav lipdadayra rfkswlpsvs
      181 llklseedal wlggtphewl asgpaavvit qggdgltvft qdgsvhsvpg epvevvdtig
      241 agdtvnaall hglaardals paalaelgpd gwsellrfaa raaaitcsra gaeppfaael
      301 dap
//
LOCUS       WP_181651735             274 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [Streptomyces].
ACCESSION   WP_181651735
VERSION     WP_181651735.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 274)
  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 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   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..274
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..274
                     /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=29911
     Region          6..234
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mpaprtvllt gaagglgtlm rgllpdygye lrlldlmpve gepdaltadl adkaalreav
       61 rgvdaiihla gisleasfdk ilkaniegty nlyeaareeg vrrivfassn havgftprpr
      121 geapfddsal ipidtphrpd tfyglsksfg edlaqfywdk hgletvsvri gscfaeptsv
      181 rmlsvwmspe dgarlfhaal taedvrhtvv ygssantrlw wdlstaralg yeprddsepy
      241 aekliaeqge ldpanpdhah lgghftthpp iwpy
//
LOCUS       WP_181651975             241 aa            linear   BCT 28-DEC-2024
DEFINITION  5-oxoprolinase subunit B family protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181651975
VERSION     WP_181651975.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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 241)
  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..241
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..241
                     /product="5-oxoprolinase subunit B family protein"
                     /EC_number="3.5.-.-"
                     /calculated_mol_wt=24749
     Region          38..238
                     /region_name="PxpB"
                     /note="5-oxoprolinase subunit B/Allophanate hydrolase
                     subunit 1 [Amino acid transport and metabolism]; COG2049"
                     /db_xref="CDD:441652"
ORIGIN      
        1 mkavpaaggt qsspavdgtq aspaagstqa spaadgtral pvgdhallve vssvaaaqal
       61 haellrrrae gslsateivp aartvlldgl edprrlaeql pgweipphta raeeaieipv
      121 rydgpdladv aalwgvpehe vpaihaaaef rvafcgfapg fgyltglpar ydvprrttpr
      181 tavpagsval agpytgvypr sspggwqlig ttdavlwdha rvpaallapg trvrfvpvgc
      241 s
//
LOCUS       WP_181651960             153 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces sp. WAC00263].
ACCESSION   WP_181651960
VERSION     WP_181651960.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=16993
     Region          17..151
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtaeapaapa lsygrllpvt vhfddldalg llhnarypvm verawtalwn degflafegd
       61 weaagdfcna vkelrisyea pinrpgeyav hlwlerlgnt gltygfrfcs adgaltyahg
      121 trvlvrldaa tlrptpwsdr fravgrellr ard
//
LOCUS       WP_181652061             458 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181652061
VERSION     WP_181652061.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 458)
  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 458)
  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..458
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..458
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48779
     Region          2..343
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msqeklsdfv vaqatefgvp gvavgvlldg qeiyashgvt slshplpvde ktlfplasvs
       61 ktftatalmr lvaegkvdld apvrryvpel kladeqaaaq itvlnllnht agldwnlidd
      121 gkgdrslagl vaklpelpli appgarasys qagynlagri iekvtglpfe qamaslvlep
      181 vglwdtvygl aevmvrkfav gynrgddgel hparpwgafk egargdnpgg glassvsdll
      241 rwarfqlgdg egvlpaealh rmreqtvelr astlgegfgi cwflhdldgv hgighggsgn
      301 gqfaellivp ernfavvsla nagpdgypfn qsvakwaleh ylgvveqaae plpydegqar
      361 qvvgrydida mnldiaadga rltlaveikp eireasdeem ppdypaaaig flpgdgdeyi
      421 itegglkgqr gyfsrddnga vigvdlagrl fnrvmeas
//
LOCUS       WP_181652029             819 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: beta-glucosidase family protein [Streptomyces].
ACCESSION   WP_181652029
VERSION     WP_181652029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 819)
  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..819
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..819
                     /product="beta-glucosidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0015926 - glucosidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=86521
     Region          53..451
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          353..686
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          736..806
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mshtfsrrst lrllggaiav aaaattatgp lplaraesrs gagprvegli gkltldekis
       61 llhgatdpas lgqagyvpgv prlgipplrl adgpagvrvt rhatalpapv llasafdpgl
      121 arrygqvigr egralgqdvl lspmvnlirt pyagrnfetf sedpllagdl vaaeirgiqg
      181 egliatvkhf alnnqeqdrm sidvrvdeqt mhevelrgfe aavaartgav mgaynkvngt
      241 facenktllt dilrerwgfd gwvmtdwfaa hstvtaltag ldmempdgty fgaalktavq
      301 sgavaesyvd ravrrvlavm drfglldgsv pprpardpka gatvalevak agatllrner
      361 halpltgaaa rsiavvgptg slpfvsgggs ahvvpdhads pldairsrag ggarvsytlg
      421 edlfgkaipd galtagidte gqrvaaggaw tytgtltvad adewtfvihy sgirptvlvd
      481 gvelfpplpg ygeyfsgglv saapdglavr rkalnlsrga hqvsitaqga dtgqlfrlrr
      541 itgatraqdv aeavdaaraa hsvvlfayed ategldrgtl alpgnqerli ravaaanprt
      601 avvlntssst smpwldgtaa vlqmyypgqe gaaataavlf gdcdpggrlt qsfavddahh
      661 pvagdphryp gvngaeeyse gihvgyrwyd aqgvrplfpf ghglsytsfa yedlrvrgre
      721 vgftvrntgr rhgvevaqvy lgrspdlrld qavrvlagyr rltlragerr rvtvrldaht
      781 lsswdagrhd wvlgtgrrav wvgsssrdlr lrgsvevgg
//
LOCUS       WP_181652644             415 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181652644
VERSION     WP_181652644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  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..415
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..415
                     /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=46112
     Region          1..382
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mqlrynyray pdaaqrrala qafgcarvvw ndclrdrkea haaglpyvks adlsrlritq
       61 akrtekrawl advsavvlqq slrdldtayk nffdsingkr qgrkvgppry kskkdtrqsi
      121 rlntnafclq gngtvyvakv gnlkvkwsrr lpavptsltv tkdscgryfl sfvvntepdi
      181 lpgletesgi dlglsafavl sdsrkidspr flrraekklk rlqrelsrka kgsknrakar
      241 ikvarqharv adrrrdfhhk astqiirdsq avyvedlavs algrtrlaks vhdagwsafv
      301 gmleykavrh grtfarvdra fpssqvcsac gfrdgpkplh vrewtcgacg vvhdrddnaa
      361 rnvlfegrri vaagraetln asqsagktra kvpaqrveag sprkgqttqa gipgl
//
LOCUS       WP_181652337             360 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Streptomyces sp. WAC00263].
ACCESSION   WP_181652337
VERSION     WP_181652337.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     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=39771
     Region          22..350
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 msqtatavve drpgagvgqn pgsdfapllr tvrarglldr rhgwyarait vnalalaavv
       61 tgvaligtsw walalaplla vfsartafig hdaghaqitg nkwvgraigl vhgnlllgms
      121 yswwnhkhnr hhanpnhidk dpdvvadvlv ftgeqaevrv gfrrwltrnq awlffpltll
      181 egvalkvhgf qdlrrqppre rvvealllvt hvvayatlll tsmslgkala faalhqalfg
      241 lhlgmafapn hkgmempdpd gerwghlrrq vltsrnvrga altdwflggl nyqiehhlfp
      301 smprphlrla qplvrahcre lgipyaetgl vdsyrqalrh mhevgeplrt eeprkvsgge
//
LOCUS       WP_181652841             120 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181652841
VERSION     WP_181652841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..120
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13716
     Region          2..100
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mcpyrlvleh vtsrwgvlvl ielldrpyrf selrraigrv sekmltqtlq tlerdglvhr
       61 dakpvipprv dysltelgre aaeqvralav wtkdrmddve ksrhaydear vsatrtpgts
//
LOCUS       WP_181652996             508 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Streptomyces sp.
            WAC00263].
ACCESSION   WP_181652996
VERSION     WP_181652996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC00263
  ORGANISM  Streptomyces sp. WAC00263
            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..508
                     /organism="Streptomyces sp. WAC00263"
                     /db_xref="taxon:1917422"
     Protein         1..508
                     /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=54862
     Region          47..505
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mlatmgalgl aptaeaaqre qpfrapqpgd ftltgrgaak vvvvgggiag latayelgka
       61 gydctvlear grtggrnftv rggdtttdlh gntqtarlsd gqymncgpar ipqwmvtldy
      121 crelgvpiev ftnvnadayl fnestgmkkp vryrtakadv ygyvsellak atdkgaldke
      181 ltatdqeklv eflkdwgelg dkltyegger rgyttvpaaa gtsgvllgdv psasdvlasg
      241 vgryfsfefg fdqamlmfqp vggmdqipra ltraigehri rtgavvskit dkgsgvsvty
      301 tqggrtkvid adycvgalpp nilariphnl gsgvqsalea itpssaakig leyrsrwwel
      361 dhhiyggite tdqdvthiwh psygfhgarg vmigyynygg dadsyaqltp kerekravaa
      421 gvkiygekyr telassfshh wrqtphleaa whntpggpdd irykplnept grvyfagdwl
      481 sytdawqhga ftsarkavta lharvlsa
//
LOCUS       WP_181653169             295 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Streptomyces].
ACCESSION   WP_181653169
VERSION     WP_181653169.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (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   2  (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   3  (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   4  (residues 1 to 295)
  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 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
REFERENCE   6  (residues 1 to 295)
  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..295
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..295
                     /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=31804
     Region          3..>148
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mnasrialvt ganqglgral aeglaarmdp ddvvlltgrs hqrvsdaare vaqlpgtrsh
       61 vrgqvldvtd tddiarlade lrarhggvdv vlsnavarll peesqaerad efidvsntat
      121 hailrsfgpv lrpggrlivv asslgtlghl dprlhhlfeg asldqveyav eswrsaihnr
      181 taeeagwprw lnvpskvaqv aavravaaer rerdladgtl iasvcpgmvd tatsrpwfsd
      241 fsqaqspsea aravldlvft ehvdpalyge lirfgkalpw hdgtppveqd rllrp
//
LOCUS       WP_181653320             267 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Aerococcus urinae].
ACCESSION   WP_181653320
VERSION     WP_181653320.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus urinae
  ORGANISM  Aerococcus urinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 267)
  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..267
                     /organism="Aerococcus urinae"
                     /db_xref="taxon:1376"
     Protein         1..267
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30716
     Region          19..>167
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mavlvltgmy yflmrtyrqp dypavsqeyy vsdysqrlnd fttqhimteg ykldqltqak
       61 vavallptte sfnrskysqt lvdkwgmtde pqnewallli rtdasypret svdnpylhle
      121 iggglkdelt dpaieevieh ydtdiynnhn nfdqatfdsf navarqiyqa hqlkvpdslt
      181 qtyeeaardp anqskinsql mqtdlkqaes qtlrnpaply lllgraffmt ictflalvvv
      241 cvvcfflatg ylylvkfisk ifhwdkk
//
LOCUS       WP_181653366             429 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Aerococcus mictus].
ACCESSION   WP_181653366
VERSION     WP_181653366.1
KEYWORDS    RefSeq.
SOURCE      Aerococcus mictus
  ORGANISM  Aerococcus mictus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Aerococcus.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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..429
                     /organism="Aerococcus mictus"
                     /db_xref="taxon:2976810"
     Protein         1..429
                     /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=46616
     Region          126..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 msgaikreis ggkpislfig nwldedfmsa aravssieig lyyredgvfr qvfsshnmnt
       61 nrvlptgilr rleathapvl qqangfgygn vlyrgittnn getvavlsts mvkptiiegv
      121 igrkslffgi fisglllsal vgvlvsrrls apmhnlakat qrialgdyaq vpvngddeva
      181 dlarafnrma edlgkmhale gelrrreria algeisvgia hevrnplgti ktsaelvrrr
      241 gglceedlml ighvidevgr idalitdfld fakprspvmr nvrlsdivtr iaqffapefa
      301 rrnidieiqd eipgletqad sdqvfqasin lvlnaldamp mggklfirts regnnarisf
      361 tdtgggvepd iqdkifnpff ttkatgtglg lakvfaimrs hdgsvechse agngatfvlv
      421 fpivdgers
//
LOCUS       WP_181653481              91 aa            linear   BCT 28-DEC-2024
DEFINITION  recombinase family protein, partial [Staphylococcus aureus].
ACCESSION   WP_181653481
VERSION     WP_181653481.1
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 10252564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         <1..91
                     /product="recombinase family protein"
     Region          <1..30
                     /region_name="Ser_Recombinase"
                     /note="Serine Recombinase family, catalytic domain; a DNA
                     binding domain may be present either N- or C-terminal to
                     the catalytic domain. These enzymes perform site-specific
                     recombination of DNA molecules by a concerted, four-strand
                     cleavage and rejoining...; cl02788"
                     /db_xref="CDD:445923"
     Region          32..74
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(33..35,68..69,71..73)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 ifatlaefer dlirertmag lpsarargrk ggrkfaltka qvrlaqaama qrdtsvsdlc
       61 kelgiervtl yryvgpkgel rdhgkhvlgl t
//
LOCUS       WP_181653525             368 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Campylobacter
            hyointestinalis].
ACCESSION   WP_181653525
VERSION     WP_181653525.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter hyointestinalis
  ORGANISM  Campylobacter hyointestinalis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 368)
  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..368
                     /organism="Campylobacter hyointestinalis"
                     /db_xref="taxon:198"
     Protein         1..368
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42850
     Region          6..363
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mffkkkkyif nlhlilgfmi ciplilvals gslisydkqi anlinkfmlk dtkseilnpd
       61 fenllsnfrd knpnleiisv kfdeknkkfy tiqalkeken ltlfvsdkge ilgqdygnkf
      121 nrfvrqlhrw llfsefdlqk lgknivaltt igfmvlvisg fyiyfphlky saikafsinf
      181 hakkqmifyk fhavfgvifg liflficltg lywsyewinn linrafgvpn setrmahkke
      241 iniiensfak ddftivlskf kehfrdynks lsitqtkegi ytfayedrgi kklaqittds
      301 gfkevnsamq mserkkvsmt ilalhsgrff gnigefifcv vsffgaliam sgifmtyfrl
      361 kpkfrhkd
//
LOCUS       WP_181654224             179 aa            linear   BCT 28-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein, partial [Escherichia
            coli].
ACCESSION   WP_181654224
VERSION     WP_181654224.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 179)
  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 179)
  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 179)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>179
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          36..>179
                     /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 msvteskvkt erkssrkpak tqetvlsall aetaevsvpl asliksplnv rtvpysaesv
       61 selaesikgv gllqnlvvha lpgdrygvaa ggrrlaalnm laernilpad wpvrvkvipq
      121 elataasmte nghrrdmhpa eqiagframa qegktpaqig dllgysprhv qrmlkladl
//
LOCUS       WP_181654240            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181654240
VERSION     WP_181654240.1
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=166351
     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 lgetakmlit 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 slawrslvdh 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_181654443            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181654443
VERSION     WP_181654443.1
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=166362
     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 pelhlgnaii kpsryvqnnq fsplkkyplv eqfryplwqa kpvepqqgvk
      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 glaldkkefk 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 saqlmvgvvd 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 enalmlpeqa snirlqsset
     1021 pqeifrnnld alvdepwggv intgsrlipl slawrsladh qsaaandirq miqdnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqalgvt qqpeywqhml dsyaeqadnm
     1141 pllhralvla waqemnlpck tllkgldeai arrgtkdedf seedirdind slildtpesp
     1201 ladavanvlt mtllkkaqlk stvmpqvqqy awdkaansnq plahtvvlln sggdatqaaa
     1261 ilsgltaeqs tieralamnw lakymatmpp vvlpapagaw akhkltggge dwrwvgqgvp
     1321 dilsfgdels pqnvqvrwre paktaqqsni pvtverqlyr lipseeemsf tlqpvtsnei
     1381 dsdalyldei tltseqdavl rygqvevplp pgadverttw gisvnkpnsa kqqgqlleka
     1441 rnemgelaym vpvkeltgtv tfrhllrfsq kgqfvlppar yvrsyapaqq svaagsewtg
     1501 mqvk
//
LOCUS       WP_181655092            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181655092
VERSION     WP_181655092.1
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=166249
     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 miqdnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqaigvt qqpeywqhml dsyaeqadnm
     1141 pllhralvla waqemnlpck tllkgldeai arrgtktegf 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_181655110             163 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181655110
VERSION     WP_181655110.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 163)
  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 163)
  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 163)
  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..163
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>163
                     /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..>159
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mlilkaykfr leptpeqlqr lrqlcgcarf vwnsglaetk risgsgeklp safelnrmlt
       61 vwkkmpeyif lqdaytdnlq qklkdlhtaw krcfdkklaa kapvwkrkne grdsirfvnf
      121 ekycrpenrr vklpsglgwv kfrqsrrvng kiknatisql agq
//
LOCUS       WP_181654807             364 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Escherichia
            coli].
ACCESSION   WP_181654807
VERSION     WP_181654807.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 10169520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..364
                     /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=39253
     Region          15..362
                     /region_name="THR_DH_like"
                     /note="L-threonine dehydrogenase (TDH)-like; cd08239"
                     /db_xref="CDD:176201"
     Site            order(51..53,56,169,173,193..198,217..218,222,238,
                     261..262,264,284..285,308..310)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176201"
     Site            order(51,53,81,169)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176201"
ORIGIN      
        1 mkinrivneg fmktmlaayl pgnstvdlre vavptpginq vlikmkssgi cgsdvhyiyh
       61 qhrataaapd kplyqgfing hepcgqivam gqgcrhfkeg drvlvyhisg cgfcpncrrg
      121 fpisctgkgk aaygwqrdgg haeyllaeek dlillpdals yedgafiscg vgtayegilr
      181 gevsgsdnvl vvglgpvgmm ammlakgrga kriigvdmlp erlamakqlg vmdhgylatt
      241 eglpqiiael thggadvald csgnaagrll alqstadwgr vvyigetgkv efevsadmmh
      301 hqrriigswv tslfhmekca hdltdwklwp rnaithrftl eqagdayalm asgkcgkvvi
      361 nfpd
//
LOCUS       WP_181655113             163 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181655113
VERSION     WP_181655113.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 163)
  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 163)
  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 163)
  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..163
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>163
                     /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..>159
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mlilkaykfr veptpeqlqr lrqlcgcarf vwnsgltetk risgsgeklp safelnrmlt
       61 vwkkmpeyif lqdaytdnlq qklkdlhtaw krcfnkklaa kapvwkrkne grdsirfvnf
      121 ekycrpenrr vklpsglgwv kfrqsrrvng kiknatisql agq
//
LOCUS       WP_181655168             927 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_181655168
VERSION     WP_181655168.1
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=104029
     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 ankklaayvf pgrnlsltvd adpqaeissk etlaenltsl tlsngarvil aksageeqkl
      541 qiiavsnkgd lsfpaqqksl ialankavsg sgvgelssss lkcwsaensv 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_181655177             927 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_181655177
VERSION     WP_181655177.1
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=104109
     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 ankklaayvf pgrnlsltvd adpqaeissk etlaenltsl tlsngarvil aksageeqkl
      541 qiiavsnkgd lsfpaqqksl ialankavsg sgvgelsssn 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_181655208             410 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_181655208
VERSION     WP_181655208.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia coli"
                     /db_xref="taxon:562"
     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=45911
     Region          48..388
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mskkaeptka eidlfvsqpv epnkskqslt ignglciqkr knresavwiy rysvagkgrq
       61 eytlgsfdrl tlkkakeaae tlrakvvige dpmqskreak keqaakkltv gklvsvwfdt
      121 pavlnltkrd elrqtvekhv mptigkipae ilqtaqvsrl lgdiskqykt tpkfvlwvlk
      181 nsyayhhrng lvkndpvsrl kasdfgvtts irervlapde itqivdkade vnkrrglvlr
      241 lllslavrkm ellaaewaef dldagvwrlp aertktkkgi diplspivig wlkelktyae
      301 ggayvcpaeg ksqkahlsdh alnkllgkit ppdsepitph dlrrtartml adlgvdyrta
      361 emclnhqlag verhynhakl fdqrreallm lsekvatltg sniiplkktv
//
LOCUS       WP_181655371             466 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Streptomyces himalayensis].
ACCESSION   WP_181655371
VERSION     WP_181655371.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  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 466)
  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..466
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..466
                     /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=51096
     Region          1..443
                     /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 msdlprkavt rtaklaalpl gfagratwgl gkriggksae ivgrelqqrt aeqlfkvlge
       61 lkggamkfgq alsvfesalp eeiagpyraa ltklqeaapp mptrtvhsvl eerlgeawre
      121 hflqfedkpa aaasigqvhr avwhdgreva vkvqypgage allsdlnqls rfarllgpli
      181 pgmdikplia elrdrvseel dygleaqaqq vhaevfaddp dvlvpavvhq cdqvlvtewi
      241 dgvplsevia dglpeqrdra gqllarflfs gpartgllha dphpgnfrll pgdnddwrlg
      301 vldfgtvdrl pgglpstigd slrmalvgqa esvyaklree gfvneeaeld peavldyllp
      361 iiepaqveef eftrswmrsq aariadprsp ayqlgkrlnl ppsyllihrv tlstigvlcq
      421 lgarvrlree leawlpgfve seprtgdfdt ldefddltee epaaea
//
LOCUS       WP_181655634             969 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces himalayensis].
ACCESSION   WP_181655634
VERSION     WP_181655634.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 969)
  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 969)
  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 969)
  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 969)
  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..969
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..969
                     /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=104174
     Region          260..939
                     /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 mssrptpvav lggalrallp aegrlplpad agsrmrmrkp qlvlvlvcaa ytagsafgwg
       61 sdllamimgd fglsaaaaaa avscfrfars rhsrfrpawl lfalssamsa lgngvwgwye
      121 vvlnspmptp syadlfflcf appaivgllv lakrpvtrsg wfclvldawl iggslltlsw
      181 slalaqtaqs egrgvaqaaf tlayplldia lvsmvlalhf rrtsanraav ntaigalalt
      241 vmcdalftsp llhdsyrsgq ildagwfags lllayapwag rrpgqpeeed harvehghah
      301 ghpygdgqgw ypatrplmss laaltpylaa tvctlgilyn vlngrsvdrv mlftactvvl
      361 alvvrqgiml ldnlrlthel aqkenhfrsl vqgssdvimi aapngvlryv spaaagvygr
      421 eahelvgsel aalihpedlg rvvhevrrfl aasqieeptt riecrfksgt gdwlnvestv
      481 nrhhggliln srdvtervrl qaqlqhnaeh dpltdlpnra lftkrvshal ggrrssdrgt
      541 avlfidldgf kavndrlghq agdellvqaa rrlqeavrkg dtaarlggde faalivgdgt
      601 rdraareqhi leladrlrmi lsqpyavdgg dvrvaasigv afaepglsag ellrnadlam
      661 yrakaagkdr velyapqmqt dvvrrtelag rlrsalhdge fvllhqpvvs latgrisavt
      721 agprwrsaqg ilftpdeflr gaedsertae lgrwtleeav kqaadrgsag lavpvtirms
      781 arrlldrtmp lssvealltr hglasgalvv eladsdprvs ldeverrltv lrrlgvrial
      841 dpfgsgyaai talrrlpvdv lkldrglveg vvesarlhki tsgllriaad lglhsvadgv
      901 dlpeqvvalr amgcthgqgk afsgpldeyr lrraltagrf pvphgpvepv faggappprs
      961 hdetpvppt
//
LOCUS       WP_181655688             140 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181655688
VERSION     WP_181655688.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..140
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15521
     Region          19..122
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkpiaqaega vdcqdlafdv fsrhcpsrgt lehvtgrwga ltlgalhegs frfnelrrrv
       61 dgvsekmlsq tlhalerdgl vhreaqptnp prvdyeltpl gravaerlma lihfvegrmd
      121 evlearasyd akrstldgra
//
LOCUS       WP_181655750             350 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Streptomyces himalayensis].
ACCESSION   WP_181655750
VERSION     WP_181655750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 350)
  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 350)
  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 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   5  (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   6  (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   7  (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 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..350
                     /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=38861
     Region          57..348
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 malqaerppr pagtrggrep qqprrfqgfr lsrrtrtaar lgsltwrtrl rrdrtlilmt
       61 lpavvlllvf nyvpllgnvv afqdynpyis tngvtaifns pwvafeqfek mfndsnfwga
      121 fentlvlffi qlvlffpvpi vlalvinsvi rprvralsqa ilylphffsw vlvvtvfqqm
      181 fggagliaqi ledhgisgfd lmtnagifky lvtsemiwkd agwgiivfla alasvspdly
      241 easamdganr wrrmwhvtlp alrpvialll vlrvgdaltv gfeqlllqrd avgagasevl
      301 dtyvwnvgiq ngdfsyaaav glvkgvigvc lvlaankfah llgeqgvykk
//
LOCUS       WP_181655843             459 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Streptomyces himalayensis].
ACCESSION   WP_181655843
VERSION     WP_181655843.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=49374
     Region          34..450
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtsrsskata rtssearava rtqtllkgkd gigtvrrttl pgglrvvtet lpsvrsatfg
       61 iwahvgsrde tptlngathy lehllfkgth rrsaldisaa idavggemna ftakeytcyy
      121 arvldtdlpl aidvvcdmlt gslieqedvd aergvileei amteddpgdc vhdlfahtml
      181 gdsplgrpvl gtvdtvnalt adrirrfykr hydpthlvvt aagnvdhakv vrqvrnafek
      241 agalsgtaae plgpregrra iraagrvdll drkteqahvv lgmpglartd errwamgvln
      301 talgggmssr lfqevrekrg laysvysyts gfadcglfgv yagcrpgqvh dvlkicrdel
      361 ehvaahglsd deigravgql sgstvlgled tgalmnrigk selcwgeqms vddmlaniaa
      421 vtpddvreva rdilgqrpsl svigplkdkq aarlqeavs
//
LOCUS       WP_181655956             384 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Streptomyces himalayensis].
ACCESSION   WP_181655956
VERSION     WP_181655956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..384
                     /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=41929
     Region          45..376
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mtdpteqerk rrlaalrsae rtlsrtames tlreqlaqls dgapavydle easdvygdgv
       61 veelerrvas llgkdagaff ptgtmaqqva lrcwagrtgn ptvalhplah peqhergale
      121 tlsglrtvhp tteprlptad evrdfgepfg tlmlelplre agfvlpswee leavveaare
      181 rdavvhidga rlwecpthfg rpleeiagla dtvyvsfyks lgglggsvla gprslideak
      241 awrhryggqv fqqfptalsv liglerelpr lpeyvahagv vaaalregfa eagvpwarvh
      301 peephthqfq vwlpyaaevl ndalirqaee tktalfrvfw egggppgvsv tevtvtaagl
      361 ewtpddvraa vadfverlpg evsr
//
LOCUS       WP_181656018             277 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces himalayensis].
ACCESSION   WP_181656018
VERSION     WP_181656018.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..277
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30460
     Region          11..233
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mlwhvenhss praaaffdld ktviaksstl tfsksfyqgg linrravlrt ayaqfvflag
       61 gadhdqmerm reylsalcrg wnvqqvkeiv aetlhdlidp iiydeaasli eehhtagrdv
      121 vivstsgaev vepigellga drvvatrmvv gedgcftgev eyyaygptka eaikelaase
      181 gydlarcyay sdsmtdvpml esvghpyavn pdralrreav srqwpildfh rpvrlkqrip
      241 afkvpprpal vamaavgaaa ataglvwyas rrrttta
//
LOCUS       WP_181656030             291 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Streptomyces himalayensis].
ACCESSION   WP_181656030
VERSION     WP_181656030.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=31394
     Region          30..236
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
ORIGIN      
        1 mangqwyppe wpgliralas geltpatprr aatvmllrdg dggpavhmlr rrasmafagg
       61 ayaypgggvd prdddrlvrw agptraewaa rlgvdeasaq aivcaavret yeeagvllag
      121 ptadtvvgdi tgedweadrv aligrdlsfa efldrrglal rsdllgawgr wvtpefeprr
      181 ydtwffvaal pegqrtlhas leadrtvwir paeaaaryda gellmmppti amlrrlaayd
      241 saaealaaap scdmtpvlaq arledgnvvl twpghdeftk sipiptrgpa t
//
LOCUS       WP_181655132            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181655132
VERSION     WP_181655132.1
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=166393
     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 eqfryplwqa kpvepqqgvk
      181 legassnfis pqpgniyipl gkqepglylv eamvggyrat tvvfvsdtva lskvsgnell
      241 vwtagkkqge akpgseilwt dglgvmtrgv tddsgtlqlq hispersyil gkdaeggvfv
      301 senffyesei yntrlyiftd rplyragdrv dvkvmgrefh dplhsspivs apaklsvlda
      361 ngsllqtinv tldtrnggqg sfrlpenava ggyelrlayr kqvysssfrv anyikphfei
      421 glaldkkefk tgeavsgklq llypdgepvk darvqlslra qqlsmvgndl ryagrfpvsl
      481 egsetvsdds ghvalnlpaa dkpsrylltv sasdgaayrv tttkeilier glahyslsta
      541 aqysnsgesv vfryaaless kqvpvkyewl rledrtsysg dlpsggksft vnfdkpgnyn
      601 ltlrdkdgli laglshavsg kgsmahagtv 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 itargmsgdg lvgqgsaylr seknlymkws
      901 mptvyrmgdk paaglfifsq qdnepvalvt kfagaemrqt ltlhkganyi sltqniqqsg
      961 llsaelqqng qvkdsistkl sfvdnswpve qqknvmlagg dnalmlpeqa snirlqsset
     1021 pqeifrnnld alvdepwggv intgsrlipl slawrsladh qsaaandirq miqdnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqalgvt qqpeywqhml dsyaeqadnm
     1141 pllhralvla waqemnlpck tllkgldeai arrgtktedf seedtsdind slildtpesp
     1201 ladavanvlt mtllkkaqlk stvmpqvqqy awdkaansnq plahtvvlln sggdatqaaa
     1261 ilsgltaeqs tieralamnw lakymatmpp ivlpapvgaw akhkltggge ywrwvgqgvp
     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_181656068             459 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces himalayensis].
ACCESSION   WP_181656068
VERSION     WP_181656068.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=48859
     Region          141..451
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mirqlivsyv llvavavaaf tvpvaftltd qlrgdtelsv rreattmall lgaendpsrd
       61 altemaeaye lqtpstvqai tadgsgvgti srlslddpav araledgrpt vdwgssfvwg
      121 pylvitvpav srtdedetvg avriryktse lterlwtiwg frailavavl afaaglgava
      181 arrltrplrq lndmasrfsd gdltarspvt gpqetqtlar tlnqgaerld tlmaaqrifv
      241 adashqlrtp ltalrlsldn iadgvddefv redveqatae vvrmsrlvng llvlaraeak
      301 vsaaeplplr divqerlhvw rpaaeergvt ialggvadgr plvltspghl dqvldnvlsn
      361 alevspdggt itvrveprgd evelavldeg pgmsdaekcr afdrfwrgqg ltgrsgsglg
      421 lavvkqlvtd dagtvalrda pggglcvais lrasqrsgg
//
LOCUS       WP_181656111             293 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181656111
VERSION     WP_181656111.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 293)
  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..293
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..293
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32497
     Region          13..70
                     /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          113..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mglrttiser qrrlgfelkq lreqagltag eaaerigmgr aqlsqietak ttilterlrd
       61 lcrlygctde tyvdalvtms eatgkgwwsa ykgpmetgal slaeleaaav alrvhqtlfi
      121 pglfqtadya kaifnspklg fenvdealrf rmerqriltr hnppsvhavi heaalhmrfg
      181 gtqvvreqll rlielarlph vtiqvypfsa eahaalsgnf vhiipslpql stvvlerptg
      241 ssylsepahl hryeelfdrl aenalapvdv slapeahsvk dslaliqhll ytl
//
LOCUS       WP_181656082             161 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces himalayensis].
ACCESSION   WP_181656082
VERSION     WP_181656082.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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..161
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..161
                     /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=17110
     Region          30..154
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msakptarrh eeettrhhqd llsstalttf rlngqllava delarpaglt aawwqvlgav
       61 lreplpvagi aramgitrqs vqriadllvd kglaayapnp ahrrakllap tdegraavar
      121 igphhaqlad rladelgeea faetvrvlgl lsaaldavte p
//
LOCUS       WP_181655888             766 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Streptomyces himalayensis].
ACCESSION   WP_181655888
VERSION     WP_181655888.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 766)
  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 766)
  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 766)
  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..766
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..766
                     /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=83512
     Region          14..756
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mragaelsna rftdeelqre qefidglyar vdalrggtea elagalapvg nglqarlerd
       61 vlvaersgll aalnavdgsl cfgridlteg tshhigrvgi rednaertpv lidwrapvar
      121 pfylatghtp mglrrrrhit tkgrtvtelh deildlddqe rtghedptgd avllaalnsa
      181 rtgrmgdivq tiqaeqdrii raphrgvlvv eggpgtgkta valhraayll yehrellakr
      241 avlivgpnpa flgyigevlp slgetgvlla tmgelypgvr atgtdtpkaa avkgraemvd
      301 vlaavvrdrq alpdpvraie hdrdvllldd glvrvahdrt retglphnva rehfeghiln
      361 tltdmvaeri gtdpydgsnl ldasditqir delaenpevw aaidelwprl tpqqlvadfl
      421 adpthlsded aavirrrstr awtpadvpll deaaellged drvakaaadr erreqiafaq
      481 gvldvsyasr tyefedkeds dpdasevlsa hdiidaerma erheeadhrs aaeraaadrt
      541 wafghiivde aqelspmawr llmrrcptrs mtlvgdpaqt aeeagvgswe kilepyvedr
      601 wehnrlgvny rtpseimdma aavlraehpg feppssvrst gnrpwaraat radlagtvak
      661 avaettpaeg rlaviaprdl hrelaahlpg itagaepdlt rsvvlldprq skglefdtvl
      721 vvepsrygts dlyvaltrat qalgvihstp lpeglelsps ggtsqr
//
LOCUS       WP_181656147             466 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181656147
VERSION     WP_181656147.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 466)
  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..466
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..466
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=46902
     Region          157..232
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          221..283
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          367..427
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mvpipsagsr sqrhrhtglr ataavlgcal llsgcgelah dggsatkhqq atrtagasra
       61 pgkdggtprl pvprgkgsrv addfngdghr dlvlndlvkg pdelhgddag igvvygggqg
      121 rgqglvpgar qllspaeyaa ptkgqlpaaf daeascdldd dgftdlvvst dppydgqgqp
      181 pvplqllfgs pkglagkavt vripararfg ndwpdqsvcg dfdgdgamdl vvhasdsris
      241 ylrgpfsrkg spraagtpla apgnvpvgps vdvnrdgydd vlvrataspe sasslvlggp
      301 agptrtgsvf pagsavafgr fgkgrgtdaa igtsdgvalr ydvpgtlrgs lsrsgtagag
      361 avlaagdldg dglselvvgg drlqifkgrs kglsaagavt vapaaqgstq llavadfdgd
      421 kradlvvrty rgetkdtval fpgrksglva vepevtfsta eflggs
//
LOCUS       WP_181656268             482 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181656268
VERSION     WP_181656268.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=51447
     Region          1..482
                     /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 mnkplrriai fcgllvlall irdnwlqyvq adalqsdknn rrvtieryas prgdiivdgk
       61 sitdsvettg tdlnykrtyk ngemwapvtg fasqivgtsq legvedgilt gnddrlffrn
      121 tldmitgkkk eggnvvttls aaaqkaafeg lgskkgavaa idpstgaila lastpsydps
      181 vfaglndgdk fdkldkdadk pmlnralret yppgstfkvv taaaalenge vtdidaktds
      241 pdpwplplst dkltnehgec lnatlrvalr dscntvfgkl sddvgnkkmi eqaekfgfne
      301 eqfvpvrave svypednrpq namggigqas nratplqmam vaaavandgt lmepymvdkl
      361 qapsldtieq htpkklsepi skenaqklqs mmetvvsegt gtnaqipgvt vggktgtaqh
      421 glnnsekpya wfisyaktse gspvavavvv edgsanrddi sggglaapia kavmqavidr
      481 kk
//
LOCUS       WP_181656455             427 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces himalayensis].
ACCESSION   WP_181656455
VERSION     WP_181656455.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..427
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..427
                     /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=46356
     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 mkqipywmdt apalpdrsgk dlpdeadvvv igggltglst ayhaarkgar vvlvekdqvg
       61 sgasgrngsh cnpgitispa qarkrygqer arelydafrd avdvveeiav rekidcdfhr
      121 agrlgaickp qhfeglqakq rdlaenfghe tvvlskselr aelgtdyyhg alldplgaai
      181 hvgkfvvgla gaaeragaei hernaatglt rlpgggfsve tlrgtirakq vmaatdaytd
      241 qsmpwfrkrl invgsfiivt eplgearake lipngrllva qknvgnyvrl tpdnrlafgg
      301 rarfapsnpa sdvksgdilk remteifpql agtridyvwg gmvgfswdri phagdvngly
      361 ysmgycghgv qmatymgrav aemmdgkpea npmrgfgfpk vpvpfyngtp wflpfggayy
      421 kakdrll
//
LOCUS       WP_181656498             271 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Streptomyces himalayensis].
ACCESSION   WP_181656498
VERSION     WP_181656498.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..271
                     /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=30058
     Region          9..256
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mtttvasyei rragprfgae vtgidltagv ddrtaeelrr afrehkvlvf rdqhltpdqh
       61 vaavrifaep fdhptavkdp vnplvypynv qqtgkastwh igglwrkpvf aiesltyevv
      121 pelgghtlwa dlqaayddls epfkellesv savydanaen yaqgskrvav eetvehpvvl
      181 khpetgrkgl fistsaiglt gvtaqegkvl lehllrhass pdytirfgwn pgdfvlwdnr
      241 atwhyavddy gdgarvyrkv igvepvqqpa a
//
LOCUS       WP_181656470             557 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase [Streptomyces himalayensis].
ACCESSION   WP_181656470
VERSION     WP_181656470.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=60001
     Region          42..190
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mdrdqsvrrf dhcpwlfaeg ateeqraaql grqqaidgds digeqcyvae saavfpdrlr
       61 lgdnsyiaah ayvtgtlttg sdcslnpftt vrgnvtlgng vrigahtsll gfnhsmapdr
      121 pvfqqpltsk gitvgddvwi gshvvvmdgv tigdhcviga gavvtkdlpa wtvaagnpar
      181 plrnrlepka vaaarpghgg drltrfadda raqaadlltl cwdgdvyvdr pgaaptvrah
      241 cdaveiadll lgtapeqlta dehvkrlaal qdprtglvpe fgdplpaada dgffgegsel
      301 yhvlsvgyal dllgesfphp vrgvremtar qlvarlehlp wqdgawgaga widswataah
      361 wnlrqgdngv ipgtvealfg wllthadpwt gmwgtpspea grlqvvngyy rltrgsfaqf
      421 glpvphperv vdavldhard aryfgagqen acnvldvahp lwlctqqlgt stngdsyrsa
      481 eirtwaerql aatllrwqdg qgfgfgpgat gpgpepglqg temwltivwl ladllgrcdt
      541 lgyrprgvhr peparrp
//
LOCUS       WP_181656607             417 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181656607
VERSION     WP_181656607.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..417
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44971
     Region          20..417
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 maqlrregtt arlrqevepa eagldaeale rldrhfarlv degrmpgclv alarhgkvah
       61 vtaygcrnre aalpvetdtl wrmysmtkpv tsvaalmlce egliglddpl arylpafadp
      121 qvydggegnd iktrpaegpi rirhllthta gltfgfyysh pvdglyraag lessvpsgad
      181 laetcdvyas lplqfepgtq wnysvatnvl grvievasgr pldeffaeri fgplgmpdag
      241 fcvtedqaer lgelygenad gsisaiaglp lhgrprflsg sggmvasald yhrfmeflrr
      301 rgeldgtrll spstfdamvs nqlpggadlr tfgspahaep gnsgigfgfg vsvvvdpdit
      361 qapshlgtyg wsgvatttfw vdpqkdltvq fltqvrptts htlyadlkrl vdeaivg
//
LOCUS       WP_181656552             341 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family NADP-dependent oxidoreductase [Streptomyces
            himalayensis].
ACCESSION   WP_181656552
VERSION     WP_181656552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 341)
  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..341
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..341
                     /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=35178
     Region          8..339
                     /region_name="PGDH"
                     /note="Prostaglandin dehydrogenases; cd05288"
                     /db_xref="CDD:176190"
     Site            order(53,132,136,160..162,182..183,187,203,226..227,
                     248..252,254,283..285,328..329,331,333)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(54,254,286)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(57,61,242,247..250,253,268,274,277..284,287)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176190"
ORIGIN      
        1 mpaalprtar evriaalpeg lpspehfavv etplpepgpg rllvrnryfl vfpglrtlmg
       61 tetddvplpp lrtgdtlfgp avgevvtapd gsplrpgdav lhmlgwreya evaiadcall
      121 dgslpdpvay laqgsaayga mtrlaevrpg dvvfvtgaag avgslagqia rllgaarvig
      181 stgspqkaer lvselgydav vlrgagpiap qlddaapegi dvlldtvgge qlaaalgaar
      241 qgarfaliga lagqlsagra ggsapveids yrlvvkgisl rgysggdhpd veqewterfg
      301 awlrsgrirf pytpiagidr asqalpdlig grhfgaaive l
//
LOCUS       WP_181656756             213 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces himalayensis].
ACCESSION   WP_181656756
VERSION     WP_181656756.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  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 213)
  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..213
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..213
                     /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=22621
     Region          <51..139
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msavdnarlv ltapktrssk nwvaisprva aalerraaar ntaddptdqy tglvfcrpng
       61 rplrpqtvld rfrrlaaeag vprvtlhdlr hlaaaltita gipltvvskt lrhstlstta
      121 niyshltqqa arsavdaidt psptptetvt apalaqlaat tprplnlarq paeprllpvp
      181 aasspaasqp qgidattprp prpqtrkrpp phl
//
LOCUS       WP_181656710             315 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181656710
VERSION     WP_181656710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=34670
     Region          8..307
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msysadswpi gaallqfpnt tkdgrsvqda parhwarvfr evaaagfdhv dltdtwlrpg
       61 dlsperltel artlkeaelg ltavttarrs vidpdphtaa anleyllrtv eaaaelgvgt
      121 vcaglhrplt saqreavwfw heqggrdpdg deriralave rfravgeraa glgvqislem
      181 yedtylgspe savrmvrdig lpnvglnpdv anlvrlhrpv phweelltpv lpyanywhik
      241 nyyrdhdpat gayftvpapa esgvinyrqa velaldagfe gpicvehygg dglsvsarnr
      301 dylrkilsvk laers
//
LOCUS       WP_181656846             361 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181656846
VERSION     WP_181656846.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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..361
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..361
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=38937
     Region          50..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          163..342
                     /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 mtdvlltvgt rkglfigrrr ggawqfddsp yfnaqavysv aidtrgrvpr llvggdsahw
       61 gpsvfhsddl gatwteptrp aikfppdtda slervwqlhp aaaepdvvya gtepaalyrs
      121 edrgetfeli rplwehptrs kwapggggeg lhtvvtdprd ardvtvavsa agvfrtqdgg
      181 eswapsnsgv savfmpdpnp efgqcvhkia qdsadpdrly lqnhwgvyrs ddagahwsdi
      241 geglpstfgf aavahphrad tayvfpinad sdrvpagrrc rvyrtadagk tweplsaglp
      301 egdhygtvlr damctdgakp ggiyfgnrng evyasaddgd swrqlashlp dvlcvraavi
      361 g
//
LOCUS       WP_181656830             235 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces himalayensis].
ACCESSION   WP_181656830
VERSION     WP_181656830.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..235
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24911
     Region          12..>174
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mskagraatt svifdldgtl vdsepnyfea grhvlaqhgi tgftwedhqq yvgigtqetl
       61 alwkerfglg aplhellaek nrrylelarv stpvypemrk fverlhdtgv qmavasgssr
      121 eaieailssa glatllpvvv sadevahgkp apdvfleaar rigaepadcv vvedaapgaa
      181 aahaagmrci aipyvaaqad dprfatagll frggqgefta qaafewlala rttps
//
LOCUS       WP_181656691             155 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Streptomyces himalayensis].
ACCESSION   WP_181656691
VERSION     WP_181656691.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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..155
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..155
                     /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=15899
     Region          2..132
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mqisaradya vralvelaad sarpltcegi asaqdipfrf lksvfrdlrs aglvrsqrgc
       61 eggywlgrda atitvaevmt avdgefftvr gvrpealgyp gaasglpdlw rgvesaaqal
      121 larttigdla ergagagaed ggagrardas aavta
//
LOCUS       WP_181656952             306 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181656952
VERSION     WP_181656952.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=33704
     Region          14..304
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maavnsapap ldrirvgsap dswgvwfpdd pqqvpwerfl devsgagyew ielgpygylp
       61 tdparltyev tkrnlkvsag tvftalhrgp gvwestwehv sdvarltqam gakhlvvips
      121 fwrddktaei ieppeltgeq wahltkgmer lghevrerfg ldivvhphad thidtethve
      181 rfldstdsdl vnlcldtghy aycggdsvkl ietfgerigy lhlkqvdpei ladvvknevp
      241 fgpavqrgvm ceppagvpal epvlaaaqgl gvdlfaiveq dmypcppdqp lpiavrtrkf
      301 lrscga
//
LOCUS       WP_181657002             413 aa            linear   BCT 28-DEC-2024
DEFINITION  FUSC family protein [Streptomyces himalayensis].
ACCESSION   WP_181657002
VERSION     WP_181657002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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..413
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..413
                     /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=45125
     Region          18..213
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mpevrgaava apvaefvkrs repvvvqtlr staaatiayv valqlssepa pltapltall
       61 vvqvtlyatl ttgirrvnsv vvgvliaigf salvgltwws lgliilaslt vghfvrvsef
      121 vpevaisaml vvgvtrvadt awdrvletli gaavglafnf llappvwvge agasiedlar
      181 rmrrlmlrsc eqltsptppd qaadqlhear rldhdiadvd aalrqaedsl rlnprvkegl
      241 lhrvvlrtgl dtleictvvl rvlartltdl akirrtdepl lrrdigvalq ellghvadav
      301 vsfavlvttq vsenaeaaea rlagelaaan asrdklalvl legvqqdprn whlhgallte
      361 vnrildeldm ehrskrlfee ldrnareqre rhpwlarirh rlgsdrpsre dtp
//
LOCUS       WP_181657021             288 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Streptomyces himalayensis].
ACCESSION   WP_181657021
VERSION     WP_181657021.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..288
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..288
                     /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=30541
     Region          3..286
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mipaafdyar petvdeavrt ladargetkv laggqsllpi lrlrlafpdl vvdigripel
       61 rgvredgdkl vigamtthha vihdplvrqy agllaeatae vgdpavrhrg tlggslahad
      121 pasdlpavvl aldgelvaag pqgrrtipar dfftdylqta lepdellvev rlpktaaadg
      181 wgfhyekfhr vaqswaivgv aamvrrddgr itesrigltn mgttpvraea teaalvgaaa
      241 epdpvaraae aaadgthpss dvsaspeyre hlarvltrra vlaaarme
//
LOCUS       WP_181657030             211 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces
            himalayensis].
ACCESSION   WP_181657030
VERSION     WP_181657030.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=22963
     Region          1..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 mtddsfsaee ywdgryaesd rmwsgkpnpv lvreaaglqp graldlgcge gadaiwlagq
       61 gwqvtavdis rlaleraaah aaaegvadri dwqqhdlaas fpdgafdlvs aqflhspvem
      121 prekilrnaa tavapggvll ieghggfpaw ehnhhpdlhf ptpdeviddl glqdgqwevl
      181 lseeheriqn dpdgrpttri dntvkarrlp a
//
LOCUS       WP_181656858             227 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Streptomyces
            himalayensis].
ACCESSION   WP_181656858
VERSION     WP_181656858.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  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..227
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..227
                     /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=24706
     Region          3..218
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mnfltighrg imgvepentl rsfiaaehag ldlieldlhl skdgalvvmh dadvdrttdg
       61 kgpiaektld elraldaggg eripvfeevl davksplqae ikdvaaaral aevmhrrdlv
      121 srvevlsfhd eaiaeisrlv pgvrtalvas rygtdvvera tavgaaalvl nirrltleiv
      181 erarkadlri igwvvntqeh lrlvraleld gattdypeik rtgrfta
//
LOCUS       WP_181657071             405 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181657071
VERSION     WP_181657071.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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..405
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..405
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42789
     Region          54..371
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mqshgriaaa vlaaaallts aacsgtptsa ppaaavaaps pgatvraltp dvaeqldkav
       61 tqtqrqagvp gvivglwipg kgsyvrafgv adkssgapms dglhmrigse tktftvtail
      121 rlvdegkvgl ddpvstyveg vpngdritlr qlaemrsgly pysedpdfgk aflsdpnrrf
      181 tpqqlldyaf khpvgfepgq kfqysntnai llglvvekas grrfgdylkq qvlepsnldn
      241 tffptgaefp ephahgyttq tpngevadat nwdpswawsa gamisdlsdl rewarivatg
      301 tllkpatqae rlrtlptgdp gtgyglgifn shgwighngs lpgyqsvtvy lpsaeatlvi
      361 ltntdtsyeg nenstlfaka vttivtpanv ydlpptpvts aspsr
//
LOCUS       WP_181657167             475 aa            linear   BCT 28-DEC-2024
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Streptomyces himalayensis].
ACCESSION   WP_181657167
VERSION     WP_181657167.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 475)
  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 475)
  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..475
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..475
                     /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=50798
     Region          30..475
                     /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 msesprrprp gakpyrrpqk dpvrilafea lravderday anlvlppllr karekdgfdg
       61 rdaalatelv ygtlrrqgty daiiaacidr plrevdppvl dvlslgvhql lgtripshaa
      121 vsatvelarv vlgdgrakfv navlrkvaqh dldgwleqva ppydedpedh lavvhshprw
      181 ivsalwdalg ggragiedll eadnerpevt lvarpgrsta eellgglgee aalrgrwspy
      241 avrlteggdp gsldavregr agvqdegsql valalanapl egpdrawldg cagpggkaam
      301 laglaaqrga vllasekqph raglvakala gnpgpyqvia adgtrppwrp gtfdrvlmdv
      361 pctglgalrr rpearwrrrp ddlesfaplq rgllrtalas vrvggvvgya tcsphlaetr
      421 avvddvlkhd ggaelidarp llpgvpalge gpdvqlwphl hgtdamylal lrrtg
//
LOCUS       WP_181657283             468 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Streptomyces himalayensis].
ACCESSION   WP_181657283
VERSION     WP_181657283.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..468
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49680
     Region          193..465
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mthassdras gtsrrtalag lvggagavla agcspsgasp vnaptpsasa paptagatpg
       61 vmtlfkdpaf nfngllalgg sghgaaevge vltavnaink aglsaqtyte tfrklgnqlm
      121 eapegakpgt ettrfralra sqyyaqalff vlgsedpgse eqlyksgrga wdrfcelshp
      181 aavtadvpyg rsplpvwffr pdesgerrpt viltngsdgq nvdmwtygva aalgrgwnal
      241 vydgpgqghl lfvdrvvftp rwetvvtpiv dwlaarsdvd tgkialtgls mggclapraa
      301 afesriaalv ampgvlapwl gfppeirkil tpdkeetnti wnkevvpelp psaaatlkkr
      361 iepfsvpaml daregkmftd fstparlies lditsvvgri kaptlvldyd deqfypgqpr
      421 qmfdkltgpk dyvkltaatg aqlhcspmap qqhcevvfdw lqeklsgs
//
LOCUS       WP_181656659             496 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces himalayensis].
ACCESSION   WP_181656659
VERSION     WP_181656659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 496)
  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 496)
  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 496)
  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 496)
  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..496
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..496
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52148
     Region          18..495
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mvtvdvklhq draehdlprp rlviggkdvt dasgglyehr npatglvqah vplagaaevd
       61 ravaaarqaf evwapmrpae rrrlltrfag llrdhipdfa aicplengvc iggwaenvgp
      121 hvaewteyya gwadkiegmv gaaysphenv eytiaepygv ighiitwnsp alslamkvpp
      181 slaagntvvi kpaestpfsa llfadlarea gipegvinvv tglgdagaal vthpgvdkis
      241 ftggpvtarr imadaalslk pvvfelggks anllfadtdl dtvvpycaaf amsntgqgca
      301 lptrllverp iydevvarva gvvahlpvgd pldtatyigp lineaardrv qgvidkaveg
      361 gagrlvfggd ridsdgyfvs ptvfadvdnr sdlaqqeifg pvlaitpfdt edeavaland
      421 teyglsayiq srdiarvnrl vprlkagtvy vnpgpnpits patpfggvgi sgfgreggka
      481 gldefinvkg vgisrv
//
LOCUS       WP_181657119             201 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces himalayensis].
ACCESSION   WP_181657119
VERSION     WP_181657119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 201)
  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..201
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..201
                     /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=21887
     Region          15..198
                     /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 milghsargk tpvepvtlki lvaggfgvgk ttlvgavsei rplrteemlt eagrplddtn
       61 gvegkhtttv amdfgritlr edlvlylfgt pgqdrfwflw delatgalga vvladtrrle
      121 dcfaavdyfe rrsipfivav ncfegaerhp adqvqqaldl dpgvpvvlcd ardrqsvkev
      181 liqvvehamt vavdrrqavt t
//
LOCUS       WP_181657084             126 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Streptomyces
            himalayensis].
ACCESSION   WP_181657084
VERSION     WP_181657084.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 126)
  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 126)
  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..126
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..126
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13563
     Region          36..126
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mhrpsarglt nerkrrtavr grdggrrlgt aelggelger atlvqfssaf cqpcratrrv
       61 lsdvaglvpg vrhveidaed hldlvreldi vrtptvlvld aeghivrrat gqprkadvia
      121 algkav
//
LOCUS       WP_181657332             317 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181657332
VERSION     WP_181657332.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=34959
     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 maiskaerlm nlalcllgtr rplskrelrg sieayleags ddsfnrmfer dkddlrelgl
       61 vietvenldg evgylarrds nrlppvtlda eeaaalglaa kvwqqarlag aasgalqklr
      121 aaglpedvdp ygahgaleph ipvheaafep lmlacrdrrp vafeyrkata arpelrqvep
      181 walecwrghw ylagwdrerg aervfrlsri tgkvrnrpgk ftaavpdvvt vretvaswag
      241 etadrsalir lragagyplr akavsvrelg dgweeleipy ghgldawlve fgpdvvvlep
      301 aelradvvdr lravakg
//
LOCUS       WP_181657661             395 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181657661
VERSION     WP_181657661.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..395
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42518
     Region          8..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 madglrlldg irvvsleqfi aapystqmla dagaeiikve rpvtgdprrw ydpkvgpddd
       61 yisggfasyn rgkksveldl tdaddrqafe ellatadvlv snlrpgsldr qglapkelre
      121 rfprlvicei sgfgttggpy akwpafdsvi qgmsglssli gdkdgppsla pmgtmdlmag
      181 iyatigilta lvgrattgqg shvdaamydi gaaflerplt lheytgevpt rgidrfspvg
      241 afragdgawv siviptdemw rrccaalgqp dlehdpeldt tlkraenmag rivplleewa
      301 kdmdrheava alraagqpag avqtiadvra ceqlahrglf apidderahr tdgttlslpr
      361 lpllfdghga rpgpiprlga dndefrtphs tevpq
//
LOCUS       WP_181657663             274 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181657663
VERSION     WP_181657663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..274
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=28683
     Region          1..270
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mttsftrtvl avpasserfl akaqkatasa lmvdfedgva epskeaarnl faraapqlad
       61 qrrglwlrvn aadtahldad laaakdaaqh ldalvlpkat pkavdwladr tnlpivalie
      121 taegvehawt vaahpsvrav mfgeldyrse lagsgglhah dtswaqariv naaagaaiaa
      181 iagpttaigd peqlradcar qialgftgkl cihptqldgv eaafgpssdm vawarrvvha
      241 vqeapdsgai tvdgamvdrp vldraqhila etdq
//
LOCUS       WP_181657841             332 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181657841
VERSION     WP_181657841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=35585
     Region          3..328
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 malklgayta clhdrpltda ldilkenglt svevnaggfi psphcpvdll lssatardey
       61 latfadrgme ltglncngnp lnplpgvgpk haddlrrtir lagllgvkhv vtmsgtpgsd
      121 pdatypswvv npwdgvymdv ldyqwgvava fwkeidalar endirvaiem hphnvvfspv
      181 tlkrlvdevg atnigaemdp shlmwqgmdv vasikwlgpl vfhaaakdat lcpgadirgv
      241 ldtsftrvpa dapgkvptgy gfwcnawpen pawkfvavgl gndvpfwtdf lralaeidpd
      301 mavnieheda aysqaeglal aaknlhsaaa al
//
LOCUS       WP_181657797             204 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            himalayensis].
ACCESSION   WP_181657797
VERSION     WP_181657797.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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 204)
  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 204)
  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..204
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..204
                     /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=21106
     Region          1..197
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mrrldgkval vsgtagdhgr avalrfaaeg alvvggdllh eeavetqrli areggialta
       61 gplgvtdegs lhrwvedavd afggidivya ntgavrfgsv dgrpdcgfal raeqksvwlt
      121 ahaawshlvr srgciltdsw rrgvieltwh iavegaphgi ransvgpgvl daavylasde
      181 ashisgthlv vdggrsavtp gaah
//
LOCUS       WP_181657933             326 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Streptomyces himalayensis].
ACCESSION   WP_181657933
VERSION     WP_181657933.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..326
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..326
                     /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=35112
     Region          1..320
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mhpfsftkaa ntrealdagr hggryiaggt tlvdlmretv erpetlvdis dlpmrdvkvt
       61 ergglrigal vtmseaaahp kvrslypvis qalelsasaq lrnmatiggn imqrtrctyf
      121 rdvtadcnkr epgsgcaale gfnrthailg tsdacvathp sdaavafaal earvhllgsd
      181 gerqvsfadf llrpgrtpnr eqalrrgeli tgveipalpr plksgylkvr drqsyefalt
      241 saavalhvrg gvireakvaa ggvgtvpwkl paverhlvge rpseslwtaa aakaaegarp
      301 lqhnrfkvel lkrtverqlr vvggsk
//
LOCUS       WP_181657850             449 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            himalayensis].
ACCESSION   WP_181657850
VERSION     WP_181657850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=48013
     Region          37..439
                     /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(149,151,277,279,313..315,359)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mpstrqtlia giavvgvlat gcagaggggg sgtgesinvl mvgnpqmedi akltkdtftk
       61 dtgikvnfti lpenelrdkv tqdiatqagq ydvatigaye vpiwnkngwl helgsyadkd
      121 ssfdkndllk pmvqslsged gklyalpfyg essflmynkd vmkekgitvp erptwqqvad
      181 iaakvdgarp gmkgiclrgl pgwgelgapl tsvvntfggt wftkdwkaqv nspefkkatn
      241 fyvdlvkkhg eagapqagft eclnamsqgk vamwydatsa agsledakss kvagkvgyay
      301 apvaetkssg wlwawawamp kttkkadaas kfmlwasskk yeklvgeelg warvpagkra
      361 styeipeykk aasafgditl ksieqadptn pgvqprptvg iqfvaipefq dlgtkvtqei
      421 saaiagktsv dkalndgqkl aeevakkhk
//
LOCUS       WP_181657972             250 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Streptomyces himalayensis].
ACCESSION   WP_181657972
VERSION     WP_181657972.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=27282
     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 mlrvlavdde epalaellyl lradprvrsa egatdatdal rrigraldag pdggdaidvl
       61 fldiqmaglt gldvarliag farpplivfv tahedfavqa fdlkavdyvl kpvrrerlae
      121 avrrvaeqaa varppaidrs adripvelgg vtrlvniadi tyaeaqgdya rlhtgdgshl
      181 vriplstlee rwqphgfvri hrrhlvalhr idelrldggg msvrvgeavl avsrrhasrv
      241 rellmrqags
//
LOCUS       WP_181657323             937 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Streptomyces himalayensis].
ACCESSION   WP_181657323
VERSION     WP_181657323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=104309
     Region          23..934
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtedlspaer yaaarkraae qatalasfre mydfgldpyq ieacqaleag kgvlvaaptg
       61 sgktvvgefa vhlalqqgkk cfyttpikal snqkytdltr rygpgkvgll tgdnsinsda
      121 pivvmttevl rnmlysgsqt lsglgyvvmd evhylsdrfr gavweeviih lpesvtlvsl
      181 satvsnaeef gdwldtvrgd tevivsehrp vplfqhvlag rrmydlfeeg eghkkavnpd
      241 ltrmarmeds rqtfgrdrrr grnnmreadr ererrqrsri wtpgrpevie rldaegllpa
      301 itfifsraac eaavqqclya glrlndeear akvreiveer tasipgedlh vlgyyewleg
      361 lergiaahha gmlptfkevv eelfvrglvk avfatetlal ginmparsvv leklikwnge
      421 qhaditpgey tqltgragrr gidveghavv lwqrgmnpeq vaglagtrty plrssfkpsy
      481 nmavnlveqf grhtsrelle tsfaqfqadk svvgisrqvq rneeglegyk asmtchlgdf
      541 eeyarlrrel kdretelakq gaaqrraeaa valeklkpgd vihvptgkfa glalvldpgl
      601 pagrtnghrg fdhydgprpl vltaerqvkr latmdfpvpv ealermripk sfnprspqsr
      661 rdlasalrtk aghivpdrhh kkrsaaaddr eiarlrtelr ahpchgcder edharwaery
      721 hrlmrdtkql erriegrtnt iartfdriva llteldylrs devtehgkrl arlygeldll
      781 aseclregvw eglnpaelaa cvsalvyear vgddalapkl psgkakaalg emvriwgrld
      841 aleedfrinq aegvgqrepd lgfawaaymw asgkgldevl neaempagdf vrwckqvidv
      901 lgqisaaapg dgstvpknar kavdallrgv vayssvg
//
LOCUS       WP_181657296             287 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Streptomyces himalayensis].
ACCESSION   WP_181657296
VERSION     WP_181657296.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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 287)
  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 287)
  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 287)
  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..287
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..287
                     /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=29905
     Region          8..275
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mpapelispr sprvaaakrl arrnfrgkdr rflaegpqav regaryrdgg eptlvelfat
       61 veaaeryadi vadaraagar vhlaadevig eisttvtpqg lvgvcrfldt dfddilaarp
      121 rlvavlahvr dpgnagtvlr cadaagadav vltdasvdly npkavrasvg slfhlpvavg
      181 vpvewavqgl kvagvrilaa dgagehdldt eldhgtmggp tawvfgneaw glpketrdla
      241 davvrvpihg kaeslnlata aavclyasar aqraaggcra tasgqnr
//
LOCUS       WP_181658285             282 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181658285
VERSION     WP_181658285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31593
     Region          13..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(17,21,47)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(20,46)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(27..28,39,43,47..48)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          98..277
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mrtnptgrql rlgtelrklr eragltstqa sqllgvkqqn qisnmesgrl gvspervhtl
       61 achydcsdka lvaalaemaa nrkrgwweey reilpaalld laevehhstl lrsavtvhip
      121 glfqttdyar eifrqdvpel sppdiehrvs frikrqavlf getptphqai vheaalrmqf
      181 ggptitraql khlldmserd hitihvipfs agtfpgsgqs iyyskgpvpq ldtvnldqsh
      241 gpvfldaeaq ldkyrvlldr meatalspee srdfihkviq dl
//
LOCUS       WP_181658327             710 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Streptomyces himalayensis].
ACCESSION   WP_181658327
VERSION     WP_181658327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 710)
  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..710
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..710
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=77765
     Region          2..699
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 maaehaptrq rgnlpgepdl vgrqqelsea grlltsarll tltgvagvgk trlarrvadq
       61 vrasfpdgvw lvelaplede sllpqtvagt lglgdqaarh pvqllvdhlr dkrallvldn
      121 cehlltgcal ltdrllreap rlrilatsrq plrlegesvm vvaplpvpas dvpyrperla
      181 dyaavrlfal raqqavpgfv lgpenldtvv rlcrrldglp laielaaggl rtlpadqily
      241 rvgrrlepar gtgtavaltr hetltaaidw shdlcspger alwarvsvfa gafdleaaee
      301 vcsgdgiard dvldlvaglv dksilirqeq aervryrlle tirqygmdrl aglglvpalq
      361 rrhrdwchrl aclaetewlt wrqeewlarl rsehsnlraa lefccsdpad aragleiaaa
      421 lwphwicggy lsegrhwlgq llwlvpeetv argralwvda wlatlqgdts saqprleecr
      481 alalrldhpp trtrctqhlg glalfegdfp gaarllqeal aghrtagdrn gvmtclyqlt
      541 macalygdyr aalfgeecla lcesagaqws rsyalwalgl ytwrqgatrr gtelvrdalr
      601 trwavrdgwg maqclevlaw iaassgqpea aarmlgsasa mwrsigtsqs gfrhlaaghe
      661 qtaarlrgdl gerayedafr qgtelapdea agralhdpap snpmtpladl
//
LOCUS       WP_181658362             340 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Streptomyces himalayensis].
ACCESSION   WP_181658362
VERSION     WP_181658362.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..340
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..340
                     /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=35526
     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 mkafryerpt epgaavaahg gapdarylgg gtnlvdlmkl gvespgllvd vsglphgsie
       61 sttggglrig aavrnsdlaa dprvlarypv lsqallagas gqlrnaatvg gnllqrtrcl
      121 yfqdvgkpcn krdpgsgcpa rdgvhrdlai lgasphcvat hpsdmavala algadvlvhg
      181 rhgprtvpvt elhrlpgdhp erdtvlepgd lithielgpv peaarsvyrk ardrasfsfa
      241 lasvaaalda hdgtvrrvrl afgavaakpw rawtaeerlr gapataesfa qavdaelaaa
      301 eplrdngfki plvrnlaira ltdlasrrda agdrdpeasr
//
LOCUS       WP_181658141             532 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Streptomyces himalayensis].
ACCESSION   WP_181658141
VERSION     WP_181658141.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  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..532
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..532
                     /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=56646
     Region          21..530
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtvlasaldt tapdhaahre amlgklaeld aeharalagg gekyvarhra rgkllareri
       61 ellldpdtpf lelsplaawg sdyavgaslv tgigvvegve clitandptv rggasnpwsl
      121 kkalraneia yanrlpcisl vesggadlps qkeifipgga ifrdltrlsa agiptvavvf
      181 gnstaggayi pgmsdhvimv kerakvflgg pplvkmatge esddeslgga emharvsgla
      241 dyfaldeqda lrqarrvvar lnhrkahpdp gpaeppkyde dellgivpgd lkipfdprev
      301 iarivdasdf defkplygts lctgwatlhg ypigilanaq gvlfseesqk aaqfiqlanq
      361 rdipllflhn ttgymvgkey eqggiikhga mminavsnsr vphlsvlmga sygaghygmc
      421 graydprflf awpsaksavm gpqqlagvls ivarqsaaak gqpydedada alramveqqi
      481 eseslpmfls grlyddgvid prdtrtvlgl clsaihtapv egarggfgvf rm
//
LOCUS       WP_181658217             428 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Streptomyces himalayensis].
ACCESSION   WP_181658217
VERSION     WP_181658217.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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 428)
  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 428)
  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..428
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..428
                     /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=44579
     Region          29..402
                     /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(38..39,42..43,45,78,128..129,131..133,136,156,
                     159..160,163,236,239..240,243..245,248,275,279,328..329,
                     333,337,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mpaagaatgl aalrraards vsglprafww lwtstlvnrl gafvatfmal yltldrgysa
       61 syaglvaslh glggvisslg agvmtdrlgr rptlliaqts talsvallgf mhhpvaiaav
      121 aflvgmasna srpavqamma divrpedrvr afslnywain lgfavssmga gfiaefsyla
      181 gflveaamtl vcavvvfvkl peskpertaa qraeepeagl gtvlrdsrfm gvvglsflia
      241 lifqqgsvgl pvamgeagft padygmaiav ngvlivvlqi pvtrfiehrd pqqllvvssl
      301 vagygfglta fagsvgvfal tvcvwtlaei vnaptqtglv vrlspvhgrg ryqgmytmsw
      361 svaglaaplm sgfvidrfga ewlwgscavi gtvaavgywg lmrglpagde daaeapspta
      421 gkpevsaa
//
LOCUS       WP_181658377            1035 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-mannosidase [Streptomyces himalayensis].
ACCESSION   WP_181658377
VERSION     WP_181658377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..1035
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..1035
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=114544
     Region          247..1034
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mhderrriee rverildqri qpavhaasvp feveawevpd epvpfaeaqs atyepfamgt
       61 pwgppwgttw fkvrgevpae wagkrveavf dlgfvgdwpg nqaealvhtp dgaplkavnp
      121 qnqyvpiahp aaggeqvdfl ieaasnpdil angfrptplg dkttagrapl ytfaradlav
      181 ldenvwhlsl dlqvlrelml elgehdprrh eimhaidral daldlddvsg tatdvrellk
      241 gvlerpahas ahtlsavgha hidsawlwpi retkrktsrt fsnvtalaee ypefifacsq
      301 aqqyewvrdn ypkvweriqe avkngqwapv ggmwveadgn lpggealarq lvhgkrffmd
      361 efgietkgvw lpdsfgynac ypqlaklagn ewfltqklsw nqtnklphht fwwegidgtr
      421 ifthfppvdt ynaefsgkem ahavrnyqdk grgtrslapf ghgdggggpt remmerarrl
      481 adlegsakvv vehpddffaa araeypdapv wsgelylelh ratytsqart kqgnrrsehl
      541 lreaelwata aalhapgyay pyekldhlwk tvllhqfhdi lpgssiawvh reaeaeyarv
      601 arelevitse araalgtgap yafnasprar aevvtvpaev aealdpglpr ltdgssaifv
      661 qvpasgsapi tasvprptpv tvtdrvldng lvrvefaedg tlasvrdlva drevlapdsa
      721 gnllrlhtdl pnywdawdid khykhrftdl ldaesvtvte kgpllgavrv erafgkgsri
      781 vqtvtvrags rridveteid wheaekilka afpidihadr staeiqfghv hrpthtntsw
      841 esarfevygh rwvhveepgy gvavindsty ghdvsrttre dggttttvrl slvraprvpd
      901 peadqgkhrf tyallpgatv edaiaegyal nlplrvaesg tavdplvttd gpaavveavk
      961 laddrsgdvi vrlyeslggr trttvrpgfp htgatvtdll erpladaqpl tiaedgtvtv
     1021 dlrpfqvltl rfrra
//
LOCUS       WP_181658010             252 aa            linear   BCT 28-DEC-2024
DEFINITION  IclR family transcriptional regulator [Streptomyces himalayensis].
ACCESSION   WP_181658010
VERSION     WP_181658010.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..252
                     /product="IclR 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=26339
     Region          14..248
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msgdtvalsg rqprairsal avlrhvaaaa pgvtakeisa alglapatty rllnllveee
       61 ylvrmpdlrg falgrrvael tgprpvpavp aaahaavsrl rdqlrfgvhl agyadgridf
      121 tdpdpdhppt daafltrhph asalgkllla dahtmpshla altghtittp ealaaelvrv
      181 rtdgvamqqc eldplhacla vpvhsettgr laaglavcgt pdrigavarp geqsalvdql
      241 recarrlapl vv
//
LOCUS       WP_181658449             135 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces himalayensis].
ACCESSION   WP_181658449
VERSION     WP_181658449.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 135)
  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 135)
  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 135)
  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 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   5  (residues 1 to 135)
  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 135)
  AUTHORS   Rosinski,J.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..135
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..135
                     /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=15262
     Region          3..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhafevlgdp vrrrilella egeqpsgavs aviraefgis qpavsqhlrv lretgfasvr
       61 aegtrrlyav daqplrevdl wlerfrgfwe qrldalgtep argrrqsrrq nqelrrtkqa
      121 gheqtggeqg grher
//
LOCUS       WP_181658546             185 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Streptomyces himalayensis].
ACCESSION   WP_181658546
VERSION     WP_181658546.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  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..185
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..185
                     /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=20667
     Region          2..173
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrlllmsdth lprrarelpp elleevplad vvihagdwvd tdtldllesr arrvigvygn
       61 ndgpelrarl pevaraelag lrfgvvhetg saqgrerrcs erfpdldvlv fghshipwdt
      121 tapgglrlln pgsptdrrrq phctymtavv eegrltdvrl hrlppraeea trrppvtrrp
      181 appaq
//
LOCUS       WP_181658785             296 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces himalayensis].
ACCESSION   WP_181658785
VERSION     WP_181658785.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..296
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31753
     Region          42..285
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msdlwsdlld clglralpsp ppqpgtggag vqlpspqsar lvfegpnqql syhrlfggql
       61 laqfvraasl acpgkavksl hvlfpragrt detvryeaec lheggtfatw tvvarqrsgv
      121 vatasvsmha deggpdhqtv apvaaplspe hrveldllpw etrasadlds paaqppeldl
      181 wmrtpeadph lapallayat dltligtalr plegvsqqda gkaftsavts htvwfhrpfr
      241 tdewlllrqh splvahgrch grgdvlttdg slvasyaqea llrfrpadrp adqpss
//
LOCUS       WP_181658819             292 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces himalayensis].
ACCESSION   WP_181658819
VERSION     WP_181658819.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..292
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..292
                     /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=30563
     Region          1..>162
                     /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 msrtalvigg giagpatama lqmagidatv yeahteaadg agvfltlgsn gidalkaiga
       61 dqaiddtgia tpqvtlcssk gkrlgvskis saagtpsrti rradlyraly qeavrrgitv
      121 yhgkrlvaae dtggavratf adgttaaadl ligcdgvhsa vrmavdpkap apsyaglisl
      181 ggytrdvavd aepgsytmif grraffgyav aldgevwwfa nlpranepar gevervggde
      241 wrrtlveafk ddagpgrahh rshrqrqrhe gqpgppaqap phlasrpddr pr
//
LOCUS       WP_181658861             307 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181658861
VERSION     WP_181658861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..307
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..307
                     /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=33186
     Region          2..297
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mreprarrse latpasserm cekaassgad fvfldledac apsakdaarg iavaaltdld
       61 wgrtvravrv naidtpwchg diievvtgar daldvlivpk arsardvwwv dvlltqletk
      121 lrltrpigle vlieeaegla naaeiarass rleavifgag dlsaslrarv ngnfdpvgey
      181 pgdfwhfara tvlaaaraag vdaidapypd yrdaegyrrs avhaslmgyd gkwaihpdqv
      241 pianevftpt aqeieearea meiyreseae gvgaigrdgr lvdaahmrla tnvlykasla
      301 resafqk
//
LOCUS       WP_181658875             332 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Streptomyces himalayensis].
ACCESSION   WP_181658875
VERSION     WP_181658875.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 11450649
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..332
                     /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=36681
     Region          24..313
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mttdsgkgse alpavavetv rvpgvevkpv aghigaeitg vdlgdpleda vvaviraavl
       61 rwkvvffrgq rldhtghvaf arrfgepvvl rrrgsaspqd vpeiettadr lelggrygme
      121 haewlqrrrh splrgwhcdh garidppaat ilraetvppy ggdttwsnla aayaglskpv
      181 rdfvdglrae hrlgvgyqar pgddayvrhl lehqvasvhp lvrvhpetge rvlfvngyyl
      241 eqiqdvsrae srllldmlle qatrpeytvr frwepgsvaf wdnrstihla padtahldhp
      301 rimhrvmlag dvpvgvdgkp sepivgsepr rw
//
LOCUS       WP_181658884             104 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181658884
VERSION     WP_181658884.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 104)
  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..104
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..104
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10951
     Region          11..67
                     /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(14,18,43)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(17,42)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(24..25,36,39,43..44)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mrmtldervr savaallhat gesqtdlaaa lgvsqaqvsr rqsgsaawsl adceavaahy
       61 ridvldllsg ptraseslpv esrrtsvrrg aerpvavqeq gapr
//
LOCUS       WP_181658990             451 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces himalayensis].
ACCESSION   WP_181658990
VERSION     WP_181658990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..451
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..451
                     /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=48482
     Region          2..>190
                     /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 mggslaglla ahvlaehadq vtvverdrfp eepgprpgvp qsrhlhvlle ggqqaldsll
       61 pgfmdelraa daprvgmpsd mvqwqdgrwf rrlpatthls tgsraqleql vrrrvlanpv
      121 itvveatnvv glsgdasrvr gvllrergeg tgqegrslea dlvvdasgrg tkaaqwlsav
      181 gaeavyeesi dtglayasrv yrdtsgtlgt eslgyyvvpn psqvyggvvl pledgrylat
      241 fsglrgdepp tdeeefvaya krlphpfvhr wlrtaepqsp vfgfrqtanv rrrydlpgrr
      301 pagflaigda lctfnpvygq gmavaamsav alrdalsdpr rtpttrrvqq allaasrqaw
      361 disagadkam pgaignavtt raverpggwy lrrvqeryag dpvvgqafrs vlaltapvta
      421 lfapkvarav lfgpvpatpa eppmtreetg i
//
LOCUS       WP_181658558             367 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Streptomyces himalayensis].
ACCESSION   WP_181658558
VERSION     WP_181658558.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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   5  (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 11431245
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..367
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39790
     Region          87..>318
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtaqeerdph awrvfqatgv ppkgkapslp kppawrrfag gpalpeppad epaelrrlgr
       61 vditphldes evdtvnaall lrrpllvtgp pgvgkstlay liarelglgr vlswnivsrt
      121 slrdglyayd aigraqaiaa wraesraagp ddsprppasp esspehtgdp adaqhrpptl
      181 gdfitlgplg tallpydrpr vllvdeldks didlpndllh alengsyeia elardaadta
      241 svhtddlggr adilrgrvec rqfpivvits ngerefpaaf rrrclplemr mpgkeqllai
      301 vrshleadee qaeplvdqfl qrvqgggths ldqllnavql ttmggfqadg ngrklvesll
      361 rdlakgr
//
LOCUS       WP_181659028             417 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Streptomyces himalayensis].
ACCESSION   WP_181659028
VERSION     WP_181659028.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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..417
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..417
                     /product="LolA family protein"
                     /calculated_mol_wt=41938
     Region          <119..302
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mapyesgnts aegpgaaaev edlragrrra aryvvpvavv gvaaatiglv paladsgdpd
       61 lpkisaqeli ekiaasdvqq lsgtvkistd lglpslggva gsfapgggps gddsgssadp
      121 qaklmelasg thtlrvaadg pdkqklsvld daaeyslirn gdevwaydsa sneayhatga
      181 ehaekgdkav pedvpatpke laeealkaad dttsvtvdgt aqvagrdayk llikpkqsgs
      241 tvgaisvavd aktgtplkft ltpasggaav vdagftkvdf akpaastfdf sppkgakvte
      301 sdeltaqesq efqdkapksg eeleeglsgl kvigegwnai atfempggqg lpsagsgdaa
      361 peaqqlldal gdkvsgkfgs gtvfstrlvn alvtddgkvy agavtkdalv kaadaak
//
LOCUS       WP_181658878             203 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces himalayensis].
ACCESSION   WP_181658878
VERSION     WP_181658878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 203)
  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 203)
  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..203
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..203
                     /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=21860
     Region          4..>133
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mttprdlllv amgmeasrpv eqgdlslala gaeaidlldh rairlvddri vpshpsatgd
       61 rlldeavssl vrqepyesvd dwlwrrgrgl ssvyrdalva egqltgqrar rmlfrsrkpv
      121 padssahdqa anrwsshepv laalaaavgi qdsrtadsps mtevddavat ilaavngavi
      181 elgatrqqra ieasafdniw rge
//
LOCUS       WP_181659295             274 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181659295
VERSION     WP_181659295.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  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 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   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..274
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..274
                     /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=29843
     Region          6..246
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mpaprtvllt gaagglgtlm rgllpaygye lrlfdmvpie gepdaitadl gdkdalreav
       61 rgvdaiihla gislessfdk ilkaniegty nlyeaareeg vrrivfassn havgftprpg
      121 gdapldsrvl ipidtprrpd tfyglsksfg edlaqfywdk hgletvsvri gscfmeptnv
      181 rmlslwmspg dgarlfhaal taenvghtvv ygssantrlw wdlstaralg yepqddseqy
      241 aekliaeqge ldpdnpdhah lgghfctnpp iwpy
//
LOCUS       WP_181659373             518 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Streptomyces himalayensis].
ACCESSION   WP_181659373
VERSION     WP_181659373.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  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 518)
  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..518
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..518
                     /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=53545
     Region          106..517
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mahlpsrrtg rpgrrkaala vpigialtas lslmpgvata aapdtptaaa aesstypyvv
       61 ntstdhktie svkkaitkag gsiviayeki gvivvhssnp dfgkqiravr gvqsagatrt
      121 apltaagtte agapqyisaa daakakaqaa dadadaeple aeqwdlraig adkaakinpg
      181 skdvtvavid tgvddthpdl apnfsasqsa dcvsgkpdtt ygswrpvdad hyhgthvage
      241 iaaarngvgv agvapgvkva gitvaqpden qlffaesvvc afvfaadhgv eitnnsyymd
      301 pwlyncmddp dqralvdavn raqmyaqkkg tlhlasagns nhdlasdaiv desspddstp
      361 vtrtidpsec fdvptqlpgv vtvsatgvqn lksyystygk gvidiaapgg dryqipdtps
      421 kngrilstmp ngeyaylqgt smasphaagv aallksthpn atpsqlqwll kaqadnpgcp
      481 tepydpdgng vvdstceggd rvngfygfgi vnalkavk
//
LOCUS       WP_181659283             106 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Streptomyces himalayensis].
ACCESSION   WP_181659283
VERSION     WP_181659283.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=10413
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mgygllaaai aaevagttam kysegfsrlw pslatvagyl vafallaqtl ktlevgtaya
       61 iwagagtavi aaigmvflge tmtaakvagi alviagvvll nlggah
//
LOCUS       WP_181659433             460 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-amylase [Streptomyces himalayensis].
ACCESSION   WP_181659433
VERSION     WP_181659433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  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 460)
  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 460)
  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 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..460
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49335
     Region          35..376
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(79..80,83..84,119,122,171..174,204,206..207,
                     209..210,233,235,240,296..297,302)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(121,176)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(206,233,297)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          382..456
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 masrtlsgal alvaaatvav avpgataqas ppgtkdvtav lfewdfdsva kectnrlgpa
       61 gyglvqvspp aehiqgsqww tsyqpvsyki agrlgdttdf rdmvatchna gvkvvvdtvi
      121 nhmsagsgtg tggssytkyn ypglysapdf ddctaqisny qdrynvqhce lvgladldtg
      181 eeyvrsaiag ymntllgygv dgfridaakh mpaadlanik srlsnpsvyw kqevihgsge
      241 avqpteytgn gdvqefryay dlkrvfnsen laylknygeg wgymssgvsg vfvdnhdter
      301 ngstlsykdn anytlanvfm lawpygapdv nsgyewsstd agppndgtvn acwqdgwkcq
      361 hawpeiesmv afrnatrges vtnwwdngad aiafgrgskg fvainhesss ltrtyqtslp
      421 agtycdvqsr stvtvngsgq ftatlgsnta lalysgkstc
//
LOCUS       WP_181659454              78 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181659454
VERSION     WP_181659454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=8656
     Region          21..71
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mprtshpaaa sgraerapla tpeevaaylg vpvktlyqwr hrrigpnalk vgrhlryrwp
       61 evdewlaaqs aheyglta
//
LOCUS       WP_181659514             493 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces himalayensis].
ACCESSION   WP_181659514
VERSION     WP_181659514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=54243
     Region          179..487
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtttaarete tttgpattae aargrisarv rillwlllvm avalaavaat trsillrdvd
       61 hrvnrllaqe tgefahfedr gvdpgtgrpf tdparllrvf lerqyadpde eliglvgrpg
      121 atpaqltqpr eidvkrplhe dsdarrrife sprstgtlhr asgeirwakv tvarhdgeae
      181 aafvvafhpg reqagadevf rillaisgva llmttgigwv vagrilkpvr lvrtaaaqlt
      241 eqdltrripv rgrddiaalt etfnamldrl erafaaqref vddaghelrt pitivrghle
      301 lmgddpaerd etlrlvtdel drmsrivedl lllakaerpd fvrpepvqla eltadvfvka
      361 rtlgdrrwel vetadrevrl dpqritqamv qlaqnavqht tpgqpirigs rstgrgvely
      421 vadsgpgvdp edaeviferf rrgtarrgar ttgaglglai vraiaeghrg rvrlhgtegg
      481 gatfvlvmee erp
//
LOCUS       WP_181659547             420 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces himalayensis].
ACCESSION   WP_181659547
VERSION     WP_181659547.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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..420
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..420
                     /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=44223
     Region          25..417
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mneqtpagsr taqdapggss gqaerrvviv gagmagvhta valreqgfag eitligaeph
       61 qpydrpplsk avllgkaegs afdvdfealg lalhlgrevt glrpaeheld teqgpvpydv
      121 lvvatgaepi qlpgavgvpg vhllrtldda erlrpvlaeq hdivvvgagw igaefataar
      181 eagcavtvve aadrplagal paevaapmev wyadagvdlr tharvdrvep gtvvladgtr
      241 lpadavvvgi garpatrwle gsgielgshr evvtddrlrt sapdvyavgd cssfpsgryg
      301 erlmvhhwdn alqgprtvaa niigetpety dpvpyfwseq fgrfvqyagh haaadamvwr
      361 gdpsgaawav cwlrderlva llavgrprdl aqgrrlieag npmdatllad psrplkaata
//
LOCUS       WP_181659585             555 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Streptomyces himalayensis].
ACCESSION   WP_181659585
VERSION     WP_181659585.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  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 555)
  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..555
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..555
                     /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=59986
     Region          47..523
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtrrlsslns pnspnsaapr rrtvvkaaaa tavlaplaaa ttaeaadgpa flhgvasgdp
       61 lpdgvllwtr vtpvaeavpg sgkgpdtevs weiaedkgft tvvgrgtata kagsdhtvka
      121 dvrslrpasv yyfrfragna vspvgrtrtt paydasasgv rfgvvscsnw eagwfsayrh
      181 lagrtdldav lhlgdyiyey gtgeypaaqy gvrkhepqhe ivtladyrtr hgnyktdpdl
      241 qalhaahpvi aiwddhefan dawsggaenh tpgtegdwaq rqaaakrayf ewmpvrpste
      301 gtvyrrlrfg kladlhlldl rsfrsqqstv gngdvddper titgraqldw lksglagsda
      361 awklvgtsvm ispvafgsls adllgplael lglpkeglai nvdqwdgytd drkelithlr
      421 dngitntvfl tgdihmawan dvpvkastyp lsasaatefv vtsvtsdnld dilhvapntv
      481 slvaeaaikg anrhvkwldm dshgygvldv taersqmdyy vlsdrtdpra taswersyrt
      541 lsgtqkverv yapvr
//
LOCUS       WP_181659638             285 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181659638
VERSION     WP_181659638.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..285
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..285
                     /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=29380
     Region          18..285
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mrgtaawppa pppltwlyap gdrpdvaaka lasgadvvvi dledavalhr keyaraatae
       61 llsvrppvpv hvrintldsp faeadirava alpglsalrl pkitspddvv riaelaapae
      121 ggalplyall esalgveraf avasahpalr gialgeadlr adlgvlddag ldwargrivl
      181 aaraaglapp aqsvypdvrd idglaascah gralgflgrm aihprqlavi krsylpspae
      241 iasaeeilks atsdsgalal pdgrfvdpai vacahrtlal aqhad
//
LOCUS       WP_181659658            1133 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181659658
VERSION     WP_181659658.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1133)
  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 1133)
  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 1133)
  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 1133)
  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..1133
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..1133
                     /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=122039
     Region          3..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          137..1072
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          416..445
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
ORIGIN      
        1 mdpvryrflg ptqalrpdgt lvpvggarlr alltvlalra grsvpaavlv devwgdeppa
       61 datgalqalv arlrralgad avasvgggyr lcataedidl yrferlageg aralsdgdpa
      121 kaavvlddal alwhgpalad lpdgaaesar wearrldarr trltaavalg qaeqvlpela
      181 alcgshplde plhllhlral raagrtaeal aayeslrhel adrlgsdpgp elralhtell
      241 rgaapeergr aaapspspsy agsavprdrt tppapdgttp ppvdratppp pdratppppg
      301 nlrarltsfv greadidair gdlaatrlvt llgpggagkt rlsqeaaetv rdaardgvwl
      361 aelapvddpe avpeavltav garetvlrga gaeemravad rhddplvrla ehcarrrmll
      421 ildncehvvd aaahlvehll ercpelrila tsreplgvpg ellrpveplp lpvalrllad
      481 rgaaarpgfr idsdeeaaaa aaeicrrldg lplaielaaa rlrmltlrqi adrlddrfrl
      541 lssgsrtvlp rqqtlravvd wswdlldede ravlrrlsvf aggcdlaaae avcgaaalqa
      601 igslvdkslv vaapsaggdm ryrlletvae yagerldeag ereavarahl tyyrelarla
      661 dpllrgpgqs aaierfetey enlrtalrha vaahdeqeal clvhslfwyw qmrdlriear
      721 nwsrevmalg pdpftspaqp vppvherctd apppmspell eearrgvhlv hlacmdteld
      781 awntpqaqak lraisetyrp gmpqtcrspg nlwffavllt gdmkrthavi desirtcrel
      841 gyawelgmal qlranilanr sdwagdatrd adealevftr lgdawgtaea lsargeaqer
      901 kgeyaaaaqt yeaaityaqr lgaraqaavl rarlgavlie sgepergeem lrdvveqsrg
      961 tandampaar lflamwlgrt rrteeareql ealrsdfgaa afvvfagfml gveawlevvd
     1021 gryeqglvka rqamersrep lahmmapqmp svhlttgava lagldgggra rdaarllgaa
     1081 rallpprhfs tpleremheq gesaaravlg deaydaayae gggltldeaa all
//
LOCUS       WP_181659046             322 aa            linear   BCT 28-DEC-2024
DEFINITION  complex I subunit 1/NuoH family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181659046
VERSION     WP_181659046.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  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 322)
  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 322)
  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..322
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..322
                     /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=34583
     Region          3..322
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 mndaldvalr llvvfvvflt lpliigqteh kvmahmqgrl gpmyaggfhg waqlvadgvk
       61 faqkedvvpa gadrrifqla pavallpyll vlvaipigps esavgqivda giffvlavmg
      121 vgvlgslmag wasankfsll gglrtaaqll ayelpmllta asvamaagtv slpgivnafe
      181 wwwlpwqivg aivffvagla elqrppfdmp vadseiifga yteytglrfa lfllaeyagi
      241 vvlcglttvl flggwhgpwg adglgwvwtf lktavlafiv iwlrvtyprl redqlqklsw
      301 tllvplslaq ialtgvvkvv iq
//
LOCUS       WP_181659771             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces himalayensis].
ACCESSION   WP_181659771
VERSION     WP_181659771.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 265)
  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 265)
  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 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   6  (residues 1 to 265)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..265
                     /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=29803
     Region          1..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          108..255
                     /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(109,111,113,122..124,126..127,132,140,147,149,151,
                     153,161,163..164,166,169,175,177..178,207..208,210,212,
                     222,224,226,228,234..242,244..246,249)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176902"
ORIGIN      
        1 mdevfkalad psrrrlldsl narngqslre lcaglsmarq svskhlavle tanlvttvrr
       61 greklhylna apinaiaerw ihqydrervr aladlkrale qepmtsdefv yttyinttpe
      121 rlwqaltdpa ftrrywgvaf etdwntgsam vweeggnrta dpaqvvlese pfrrlsytwh
      181 tftpewaksa gvsddvlari saerrskvtf eieplgqmvk ltvvhdgfdp gstvldmirg
      241 gwpallsslk tlletgealp epase
//
LOCUS       WP_181659891             601 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Streptomyces
            himalayensis].
ACCESSION   WP_181659891
VERSION     WP_181659891.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 601)
  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 601)
  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 601)
  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..601
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..601
                     /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=65761
     Region          7..155
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          237..567
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mgrdlqlrta tpedlewiye lrhrvyaqel gqhvpdpagr lrdgldgdnv ylvaargatr
       61 igfvsvtppw lgryaldkyl trdelpllte gdlfevrilt veprwrataa apllmyaalr
      121 wiaarggrrv vamgrtelld mylaaglrpv grtvhsgalt fevltgnvte ltkvtmdryg
      181 ttlerlrsev dwrldmpfap rpdgcehgga sftaigtdfr slhrrhqvva advldawfps
      241 apgvraalte dpawaartsp ptgaegllae iagaralpve tlvvgagssd lifrafgqwl
      301 tpesrvllmd pgygeyahvt ervigcrvdr frlrreegwr idparlsaav gsgrydlvvv
      361 vnpnnptgrh apaaelrsvi aaapartrww ideaylgyvd laeslvglaa mdsrvvvcts
      421 lskmyalsgm raaylvaepn taaqlrrwtp pwpislpaql aavaalrdpa yysdcwrrth
      481 alrrelaadl aaldeavvve esvanfltvt lplggpsaaq lvhecrrhdv ylrdlsplss
      541 eyqgrtaria vkdtaenari vaacqaaldv lrprsaslfs mpeipetpei segvpvagsa
      601 r
//
LOCUS       WP_181659552             720 aa            linear   BCT 28-DEC-2024
DEFINITION  YhgE/Pip family protein [Streptomyces himalayensis].
ACCESSION   WP_181659552
VERSION     WP_181659552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Geller,B.L., Ivey,R.G., Trempy,J.E. and Hettinger-Smith,B.
  TITLE     Cloning of a chromosomal gene required for phage infection of
            Lactococcus lactis subsp. lactis C2
  JOURNAL   J Bacteriol 175 (17), 5510-5519 (1993)
   PUBMED   8366036
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR03062.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..720
                     /product="YhgE/Pip family protein"
                     /calculated_mol_wt=75239
     Region          40..198
                     /region_name="pip_yhgE_Nterm"
                     /note="YhgE/Pip N-terminal domain; cl19580"
                     /db_xref="CDD:354443"
     Region          503..707
                     /region_name="pip_yhgE_Cterm"
                     /note="YhgE/Pip C-terminal domain; TIGR03062"
                     /db_xref="CDD:274414"
ORIGIN      
        1 mrspklaale lrrfgrgrlp raalasllll pllygalylw sfwdpygrld ripvalvned
       61 kgataagkkv aagdeiaeql rdsqvfqwhe vsaadaragv edgtyylslt mpsdfsrria
      121 ssaatgthsa dsatdtepad satgsrsgsg sgpqtgalqv rtndannyiv gqisrtvfse
      181 vrsaastsas rsfldgifis fsdihdatek aaegadelkg gigkakkgae dladglkdak
      241 dgssglaegv srldrgagdl elgsqqvaeg tqkladkvnr aadqvrpfle dngktiadaa
      301 rivadstgvv rghldtfvrt aplaekgtre asatldavya rrcekplvad pacgdlrkak
      361 daaaeaaqla kdvntvvqgy dgdvaaldkd latlqrqana laktaphlde dlatavaein
      421 elndgaarva kgaatlhsgl ttaksgsael dagvgelkag asdldgglfk ladgsgelag
      481 glhdgadqip dydkhdrdrr tevmadpvql asqslhkapn ygtgfapyfi plslwvgamv
      541 aymliqplnr ralaagasaw rialagwlpv aalgvlqtaa lmavlhwglg lemaraagtv
      601 gflclvtgcf aaivqwlnar fgaagrilvl aflmlqltsa ggtypvqtsp qffgavhpfl
      661 pmtyvvealr rlitggglgp vweacavlaa ftagalalta vsarrrqvwt ldrlhpelsl
//
LOCUS       WP_181660300             528 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA synthetase [Streptomyces himalayensis].
ACCESSION   WP_181660300
VERSION     WP_181660300.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 528)
  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 528)
  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 528)
  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..528
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..528
                     /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=55995
     Region          10..507
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(175,178..183,185..186)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(178,293..294,314..319,398,410,413,424,504)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(178,218..219,266,268..269,272,293..294,314..319,398,
                     410,413,421..424,485)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(218,268..269,272,293,421..423,479,485)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mrnegigswp grrarktphr talihqqqtf syaelhqrtn rlahalraag vrrgdrvayf
       61 gpnhpsflet lfatgllgav fvplntrlaa peigyqlads gartlihdps lydptdnggg
      121 skgdggaspa easpaeaspa vkhrielgdp yeqvlaaapd nlidepvgpd dicmimytsg
      181 ttgrakgaml thgnltwnai nvlidqdiaa devalvsapl fhtaglnmit lpvllkggtc
      241 vlvgafdpag tldlierhri tfmfgvpamf dqiarqarwa eadlssvrql tcggapvptp
      301 liatyqsrgl nfqqgygmte aapgtlflaa ehavskagsa gvphfftdvr vtgpdlspva
      361 vgepgeivvr gpnvmpgywg lpeetaaafa dgwfrsgdla rvdedgfvti vdrlkdmiis
      421 ggenvypaev edvllghpai vecavigvpd ekwgevprav vvaqegarld pdeviaflsg
      481 rlakykipks vvvaetlprt asgkllksrv rarfgagpqs gtternps
//
LOCUS       WP_181660409             217 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181660409
VERSION     WP_181660409.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  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..217
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..217
                     /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=23243
     Region          28..201
                     /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 masgatsaaa atrtspavth tspaqaaaps pheprfdagr icldllatah peerlgsier
       61 lrawcaaagl vppdtplsaa epswlaafre lrlrvdelvr geldgryagg alervnalar
      121 wappapravr aedgtlvral hddpgctall aavardavel ltdpvararl rrcegdncpl
      181 iyldtsrgrr rrwcsseacg nrervarhrr raalara
//
LOCUS       WP_181659961             590 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Streptomyces himalayensis].
ACCESSION   WP_181659961
VERSION     WP_181659961.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 himalayensis"
                     /db_xref="taxon:2820085"
     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=62097
     Region          1..456
                     /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 yadpdrdavh vraadeafal ggdtpassyl
       61 diakvlqaak dsgadaihpg ygflsenaef aqavldagli wigpppgair dlgdkvaarh
      121 iaqragaplv agtpdpvsga devvafaeeh glpiaikaaf ggggrglkva rtleevpely
      181 dsavreavaa fgrgecfver yldkprhvet qcladqhgnv vvvstrdcsl qrrhqklvee
      241 apapflsedq nrqlysaska ilkeagyvga gtveflvgnd gtisflevnt rlqvehpvte
      301 evtgidlvre qfriadgekl gyddpavrgh sfefringed pgrnflpapg tvttftpptg
      361 pgvrldagve sgsvigpawd sllaklivtg atrqqalqra aralaefqve gmataipfhr
      421 avvtdpafap eltgstdpft ihtrwietef vneikpfaap adadaedesg retvvvevgg
      481 krlevslpas lgmslartgl aagakpkrra akksgpvasg dtlaspmqgt ivkvaveegq
      541 evkegdlvvv leamkmeqpl nahrtgtikg laaevgasit sgaviceikd
//
LOCUS       WP_181660518             437 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181660518
VERSION     WP_181660518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 437)
  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..437
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..437
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47960
     Region          28..88
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
ORIGIN      
        1 msgpqphral ppellaspew reacrvrdfg rifrlvkvka giypsriaal cgmtpsrvge
       61 imagrrslah idviervadg lripgamlgl ahrpweipqp vrtrgsvpep epqaahepvt
      121 eavpsdgfdd lmaladgqvn rstlaalrss vedywrrddq hggaplrpav vghlryvtql
      181 mtgadsalrn dlqslaaela rlagwayfda rqystartyf aqalslsrgq gdrlfianvl
      241 scmslqatyd gnpmdavala ckaqdmarsa ggqplvmsml hmreafahat lrdaaschqa
      301 ldrsrdtyeh grgredeaps wvryfdetkl vvdtgialar lgeaaraepl iaeglrreka
      361 gqqrgrafha fwlastqlqq gkldeacrsa glaleltasi dsprvaghvq efqrrlgpya
      421 reapvlafeq rmrerlg
//
LOCUS       WP_181660113             371 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Streptomyces himalayensis].
ACCESSION   WP_181660113
VERSION     WP_181660113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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..371
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..371
                     /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=39328
     Region          32..321
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 msaydgepqg ayhgahvdpl aglrttddpp wdvyltgtvf ldivftglds apergteswa
       61 rgmgsspggv anmatalarl glrtslaaaf gddhygeycw daldqgegid lsasrrvagw
      121 hspvtvsmay egeramvshg hepppeepap ecppraraai asltpgrrap wiadvasegt
      181 lifadvgwdd tgrwdlagla dlehceaflp naeeamrytr tdcpraaaha lteyvplavv
      241 tlgaegayav drrtgetaev paievealdp tgagdvfvag fvtgtlagwp ladriafagl
      301 taalsvqefg gslsapgwae iaawwrrvga yddqdpaalr ryafleallp dvarpwplrr
      361 avptigfrag r
//
LOCUS       WP_181660694             505 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces himalayensis].
ACCESSION   WP_181660694
VERSION     WP_181660694.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 505)
  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 505)
  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..505
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..505
                     /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=53981
     Region          137..352
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 maalavvsia vvvivllmqe gaadaatwgv lsaaavlgcs cvagavvaan aeargasrry
       61 aalqrlaagg qadvqemlhr margerieqp pfarpgplea gpldrlahei allrshataa
      121 liqvaqpavp tsegegrera evfanlarrl qslvhraige iddleheved pellkrlfqv
      181 dhlltrnrry aenlavlgga vsrrqwsnpv slmevlrssi aeveqysrvk lvpeiegtlh
      241 ghavadvihl laelvenatv fskphtnvll ssqrvaagla vevedrglgm ppedqgrina
      301 llanpndvdv sklladgrig ifvvaelarr hgiavqlrrn iyggvqavvv iphrllgded
      361 epvaprpatv dmprhttavp tqrsavqaap aaqplaappa vaqplpevrr vtmsphvpqh
      421 qprtaeaapp rdygsahhvd aqdgrpelpr rnaqqhlvpq lmdtpgtrtp ggeddvepsm
      481 rnwtaftggf nraegadesp sdgsr
//
LOCUS       WP_181660696             252 aa            linear   BCT 28-DEC-2024
DEFINITION  IclR family transcriptional regulator [Streptomyces himalayensis].
ACCESSION   WP_181660696
VERSION     WP_181660696.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..252
                     /product="IclR 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=27457
     Region          13..244
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 malkheptvp hhsvqhtlrl leiisrrgag vthaelardt glpaerlapl lrilcregyi
       61 ermtdgayia gdaltrlssa qgrdqalrdk lqdtldrlrd svgaavyfsr yvdgeirvtq
      121 cadsprtpkv newvdfrsaa hasaigksll gqldlngrrd hlsrhkmarl tsrtitnerv
      181 llnrldsqpp tvpvldlqey avgtvcaavp vtagsavgcl alslpiehay rlrqaadtln
      241 reaapvvlsl ai
//
LOCUS       WP_181660940             239 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces himalayensis].
ACCESSION   WP_181660940
VERSION     WP_181660940.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 239)
  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 239)
  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 239)
  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 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   5  (residues 1 to 239)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..239
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..239
                     /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=25237
     Region          7..98
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrptkpsrds aapqlaalag lfadetraac llalldgraw tagelaryag vaastasehl
       61 gklvagglla eerqgrhryv rladdrvaql vedlaahaap hverprtlra ssagsamarg
      121 rtcydhlagr lgiaitdalt ergllrqdtg faltsaglsw fdglaipler tgrrplargc
      181 ldwterrphl agvagaalcr haldadwcvr igseravkvt dvgtralael lgieaaalr
//
LOCUS       WP_181661083             121 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181661083
VERSION     WP_181661083.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..121
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..121
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12967
     Region          42..109
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mrqrrlvtls aalctaaslg aavpqvaaai psecsyvsst yrptltqghi stavkqaqcl
       61 snmwggqppk ltldgvfdsv mlkkvkwiqg chglpesgvi dpntwrvlyh paldcylpyp
      121 p
//
LOCUS       WP_181660412             460 aa            linear   BCT 28-DEC-2024
DEFINITION  nitrate/nitrite transporter [Streptomyces himalayensis].
ACCESSION   WP_181660412
VERSION     WP_181660412.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 himalayensis"
                     /db_xref="taxon:2820085"
     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=48466
     Region          40..431
                     /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(50..51,54..55,58,90,144..145,147..149,152,171,
                     174..175,178,246,249..250,253..255,258,286,290,342..343,
                     347,351,384,387..388,391..392,395)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mtapstttas rkggrwieqw dpeneefwke tgervarrnl ifsvlsehig fsiwtlwsvm
       61 vlfmgpeygi dpagkfflva matlvgafvr vpytfavarf ggrnwtiiaa smlllptiaa
      121 fvvmepgtsy ttfmlcavlt gvgggnfass mtninsffpl rkkgwalgln agggnigvpv
      181 vqlvalgvig asggprvllg iyipfilvsa vcaalfmdni asvkndtgaa keavrdahtw
      241 imsflyigtf gsfigysfaf glvlqtqfgr tplqaasvtf igpllgslir pfggwladky
      301 ggaritlwnf aamavatsvi vmasmekslp lfttafialf vltglgngst ykmipgifaa
      361 kavqkgltge eaaaygrrls gasmgligav galgglginl afrqsfmtag tgtgafvafl
      421 afyavciavt wavylrrpaa aassaeatse akpqlsyaev
//
LOCUS       WP_181661160             498 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces himalayensis].
ACCESSION   WP_181661160
VERSION     WP_181661160.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=52102
     Region          24..498
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mtthlapvvr dfllpsarsw lerpplepfi ggsfraarsd dripvidpgt glalteyaaa
       61 seqdvndava aartafddgr wseldpeqre selrlladll egatetvaql ealdtgktla
      121 earldvdeav avlryyagwa tkaegavypa prsflatgtr eplgvcaait pwnyplpilt
      181 yklapalalg ntfvakpseq tvlstayfan lcaqagipdg vvnvvpgaga tgaaltaaeg
      241 vdkiaftgst rtgqavmraa attmtqvsle lggkspqvvf adadmdaaie gvmagiwtna
      301 gqvcvagsrl lvdrrvhdef vsellrrtaa atslghglap gttlgplisa kqrdqvttlv
      361 ekaaaegaev qtacslpaed gffaaptvvt garpgqtieq eevfgpvltv lpfndeaeai
      421 rlangttygl assvwskdis rvhrvarglr agtvwantyg ifhptlpfgg vkasgfgrel
      481 gsaaidhyte lkttvigl
//
LOCUS       WP_181660728             590 aa            linear   BCT 28-DEC-2024
DEFINITION  IucA/IucC family protein [Streptomyces himalayensis].
ACCESSION   WP_181660728
VERSION     WP_181660728.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 590)
  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..590
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..590
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=66231
     Region          10..588
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtlsdavahl sperwaqanr llirkalaef aherlfspes igddryvvrs ddgtveyrft
       61 arrlrldhwq vfpesitrhr dgtelplhal effielkesl glsdsilpvy leeisstlsg
      121 tcykltkpav paaelaradf qaietgmteg hpcfvanngr lgfgvheyls yapetaspvr
      181 lvwlaahrsr aaftagvgld yesllrselg eetlkrfsgt ltdqgldpdd yllipvhpwq
      241 wwnklsvtfa aevaqrhlvc lgegddeyla qqsirtffnt sdpakhyvkt alsvinmgfm
      301 rglsaaymka tpaindwlag lvendevlks tglsiirera avgyrhleye aatdryspyr
      361 kmlaalwres pvpslqeger latmasllht dregasfaga lieqsgltpa ewlrpylray
      421 ltpllhsfya ydlvfmphge nvilvlkdgv vqravfkdia eeiavmdpda vlppvverir
      481 vevpedmkll siftdvfdcf frflaanlvt egvldedtfw ravadcvrey qgsrpeladr
      541 frqydmfape fglsclnrlq lrnneqmvdl adpsgalqlv gdlknpiagl
//
LOCUS       WP_181660363             413 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Streptomyces himalayensis].
ACCESSION   WP_181660363
VERSION     WP_181660363.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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 413)
  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 413)
  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..413
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..413
                     /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=42372
     Region          1..413
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mrdvyivdav rtpfgkyngg lasvrpddla ahairellar tpeldpsrig dvffgnanga
       61 geenrnvgrm agllaglpts vpgvtvnrlc asgleaviqa araialgdas ialaggvesm
      121 trapyvlpkn dkpfpaghte lysttlgwrm vnpkmdpqwt vplgesaeli aekhkisreq
      181 qdafalashq kaaaaqaagl fdgeiapvsi pqrkgepvvf gadecvrpda slaamaklkp
      241 sfrqasearw gsprpeaggg tvtagnaspl ndgaaalllv deeglkatgr qplarvsasg
      301 vsaidphyfg lapveavnra lakagktfgd lttlelneaf aaqvlgcvae wpefdpavln
      361 prggaiaigh plgasgarla gtvahqlaaa gsgtgvatlc igvgqglalv ler
//
LOCUS       WP_181661341             299 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces himalayensis].
ACCESSION   WP_181661341
VERSION     WP_181661341.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  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..299
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..299
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32878
     Region          15..296
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msqalqslld lldlerieen ifrgqsrsav vprvfggqva aqalvaagrt vpedrlphsl
       61 hayflrigdp gapivytvdr mndgrsftar rvvavqhgqp ifalsasfqk yeegldhqap
      121 mppapdpatl ptaeerlpvy gnldpevver llearaavdl ryvddppygr ygepraprsq
      181 vwfrtngkld ddpppnsvwg dpllhiclat yvsdmtllds vllahgrggw avgdvvgasl
      241 dhamwfhrpf radewllydq esptssggrg lgqariytqd grlaisviqe gvmrvprps
//
LOCUS       WP_181661394             209 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces
            himalayensis].
ACCESSION   WP_181661394
VERSION     WP_181661394.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 19424215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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: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=23176
     Region          7..>98
                     /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"
     Region          <59..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 madgtreywd trhreqdela sgghigldrp gnelfyalrl gqlltligdl sspaaplfvl
       61 dagcgkghfa ralarcghrv dgfdasqeai aharaedggl ryavaaldew rspwpydvvl
      121 cvdvlfhvld daewtaglrn laslvrvtgr liltdedape rsprgdyivh rpaaayrami
      181 eplglrhtlf rpygfrenlv gfhvftrtr
//
LOCUS       WP_181661405             142 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181661405
VERSION     WP_181661405.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..142
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16064
     Region          21..123
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maegidvtes taqgsrievs penacpiapv vdivfsrwtt pilwalneyg rqrfvelerr
       61 iatitpkvlt qrlrqlerdg lvvrtyhpev pprveyeise lgrslaplfa tlaewsanld
      121 qveqarrayd trertgnrsv tt
//
LOCUS       WP_181661432             333 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181661432
VERSION     WP_181661432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 333)
  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 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   3  (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   4  (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 11972964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=35600
     Region          1..245
                     /region_name="YrhO"
                     /note="Sugar-specific transcriptional regulator TrmB
                     [Transcription]; COG1378"
                     /db_xref="CDD:440988"
     Region          269..318
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mlaaigldet hesayralvs vgaaevpdla rrltlgeydt eralrrlerh glaaqssarp
       61 grwvaappgv algalltqqr helekaelaa allaeeyrsq aaepavhdlv evvtgaaavs
      121 qrflqlqlga tdevcalvtg kpvavsgmdn daeeqaanrg vayrvviere vlslptglte
      181 lsaalgrneq vrvvdrvptk lvvadratam vpltsraaep aavvvhasgl lesltglfea
      241 vwrealplrl gedgeateee peapdgtdle ilslllaglt dasvakqldl glrtvqrrvk
      301 rlmelagvtt rlqlgwhaye rgwvarharv pqd
//
LOCUS       WP_181661477             389 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Streptomyces himalayensis].
ACCESSION   WP_181661477
VERSION     WP_181661477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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..389
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..389
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39482
     Region          16..387
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mtstvtqsaa grlfsrpaaa ascvgfvlig mlqalygpav pglreeyals pseaglglsl
       61 hftggvagvl afnaihsris nrsllaasya lmaaggagfa lapnwplala aaflgglgfg
      121 gidyglnqlf avgfgdrsta mlnvlnahfg igavlgpali awtgadgyay afgacavlsa
      181 vlilctggvr tepqvsgesp vtpksslgls rilvgflvly vlnvgveagv ggwepthlet
      241 vgfssavaas atsvywlmmt vgrfvvvpit lrysperilt vcaagmtacl llalipgaap
      301 wayagvglfi apvfptglpw lnralpeakr agawviaasm iggvaappll gvgieasgir
      361 avpwlltvls atsllatvwl irltrrsaa
//
LOCUS       WP_181661592             333 aa            linear   BCT 28-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Streptomyces
            himalayensis].
ACCESSION   WP_181661592
VERSION     WP_181661592.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=36356
     Region          16..331
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mtealteqsa grqpkpript idlrpwltgd pearaeiart vdealqtagf llvtghgvdp
       61 slrariraaa reffalpasv kepysakvgg rgwlgpgaea ngysegtetp pdlkesltfa
      121 thepfedpei naewyapnvw paevpelqml ceeylarmge lenqllsllg ealglesgff
      181 trhmdhptyg fninwypgte vvgapqegqf rigphtdfgt vtildrqagk gglqvftdeg
      241 gwedapydpe aftinigdlm arwtgdrwrs grhrvlpppa dapaeelmsl vyfgectpgt
      301 lvesvpapvg rvayepvdsh vylraqldai tvg
//
LOCUS       WP_181661656             276 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Streptomyces himalayensis].
ACCESSION   WP_181661656
VERSION     WP_181661656.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 276)
  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 276)
  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 276)
  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 276)
  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..276
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..276
                     /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=27945
     Region          36..267
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrcslakavt gglamvaaaa vlplaaptpa aadrivvggt pvdvadnpwv valssrarfg
       61 gtrggqfcgg vvvgrstvlt aahcmsaevl ggppsrrddl kvvvgrndll akdgkeipvr
      121 rvainpghns vtnagdaavl tlatplpqrn vipmarqgds aytpetratv ygwgdttgag
      181 hyartlraaq vrvlpdslck qaypgtsegt ylaasmlcag eraggrdacq gdsggplvar
      241 grlvglvswg sgcgwagspg vytrisavlr plglgh
//
LOCUS       WP_181661431            1255 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Streptomyces himalayensis].
ACCESSION   WP_181661431
VERSION     WP_181661431.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1255)
  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 1255)
  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 17582184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1255
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..1255
                     /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=131844
     Region          131..581
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
     Region          <777..>913
                     /region_name="myxo_dep_M36"
                     /note="myxosortase-dependent M36 family metallopeptidase;
                     NF038112"
                     /db_xref="CDD:468355"
     Region          799..>862
                     /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"
ORIGIN      
        1 mratprtavt aaitavlavt avapsgaqpr dgaadgtrpl vgspaaaqgd gtrqatvtlv
       61 tgdrvvvrtd kdgrstatvl phedgtqplv qtrqsgkdly vypesaipai asgkadeqlf
      121 nvtglvrqgy ddahtdqlpl iatydtsvdv aesapaaprg serkrvldav dgvalkadkk
      181 kaadfwadvt nsrsraagdl kklwldakve atldrstkqv gapeawaagy dgtgttvavl
      241 dtgadadhpd lkdriaesrn ftdsdtaddr dghgthtist vggsgaasdg kkkgvapgtr
      301 llagkvlndy gygetswiia gmqwavdqka dvvsmslgsp eptdctdpms iaaeelagts
      361 dtlfvvaagn sgpalnrvss pgctpgvltv gavdrddsta sfsspgpaph thtlkpeiaa
      421 pgvgisaaaa ggrgvyayqs msgtsmatph vagaaailkq rhpdwspqel kaalvssahs
      481 gipgdvretg ggrldvkaai gqtvlgspav qggtfdwpgt ssdrttvevp ytntsdnpvt
      541 ldlsvtgvtg ndgtkvhatv aklgqrsvtv pagetvkvpl tldpsahler sqygdvtgrv
      601 iaeadgvtvs tpfslyvqpe tvtlrvklvd rlgepasgls sldvigtdda sgerrfnega
      661 adqtyelrpg syflsafvat tdnggdlvns laylarpefe ltkdttvvld arvahrltve
      721 tdrptedrnt tlafarswdd twlhggsmsg nrqvkgyyas vegrahdgdf efgsywrrya
      781 pqiesfgieg gpqlhpvtas tgsdnldgsg saevvdagsg taaelaaanv kgkialikva
      841 ddetylyqqa qdaknagava vvahhasadr wypsvgwtng plpvlalpad eagelldrla
      901 sgpvtvkwqa taaspyvynl afpedaplas draykvgdtk lgrnettyha mgvaadylda
      961 vtayrpnadv yltglfdlva apgkrteyyt agdtsfsqwv sssfpygesm lnaqhayeag
     1021 errteswygg vlaptapldd ageqelaaer qgdligiapa fwgdsehagl qgsfgdigsi
     1081 qlridgeeqe sspvpwgvwk vpaedaayel tlttmkfgip grvwkrstmt qttwefrskl
     1141 desvysqglp ilfpqyrlpe dgmktlaaed dqkltlgvtg hagytpeale saqlsysydd
     1201 gqtwteakta vedgtwtatv hhagasgkpv tlkseltdan gnsvtqtvtr aydvr
//
LOCUS       WP_181661490             253 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Streptomyces himalayensis].
ACCESSION   WP_181661490
VERSION     WP_181661490.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  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..253
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..253
                     /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=26415
     Region          6..>87
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mandvtcetl rengaelalg vlpgreraea vahldrcadc reyieqltlv gdgligllpg
       61 seppvgfetr varaltqasa gregrrathg fgrlrrgfrg rrpgrvrlrv aaaaaalala
      121 fgfggwavgt aienwtsspp gpadstsrll saeltgvgpd rpeageiyah agapgwiyms
      181 vdlddagipy tgeiscller tdgttvrvgt fplhdgygyw galvdvdpst lsgarltsad
      241 gtvlavahfe tas
//
LOCUS       WP_181661748             485 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Streptomyces himalayensis].
ACCESSION   WP_181661748
VERSION     WP_181661748.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 485)
  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 485)
  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 485)
  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 485)
  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 485)
  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 485)
  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 485)
  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..485
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..485
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53679
     Region          1..331
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 mfdrdfewse lvrfvtypgp eatlgvvsgr rrqgktflld giaratdgff faaseateae
       61 slrqygvama rfegrtvpyr fthwdeavea tmhlatartg pltvvidefp flakaspelp
      121 sllqralgpq grreggpvrl llcgsalsfm gnllsgtapl rgrasleliv ptldfrlaad
      181 fwgitdprla mlvnsvvggt paygreftlg dvpadlddfg pwilrnilnp grplfrearf
      241 llaeepdlrd talyhgvlaa iaqgnhtrgg iasflerkst dlghaltvle dtgmisrepd
      301 afhgkrsayr inepiltfyy almrpewsdl erpgqaesvw qrshptfrsk vigphfeqlc
      361 rtwtrwyasp dtlggqrtrv esgtvadtaa rashevdlaa fgrdedgret llaigeakwn
      421 etmgfghvqr lehirdlira rgtvnapatr llcfsgagft ddlhtraahd pniqlvdler
      481 lykga
//
LOCUS       WP_181661864             331 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Streptomyces himalayensis].
ACCESSION   WP_181661864
VERSION     WP_181661864.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..331
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..331
                     /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=34586
     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 mrsfayvrpd dvaaavrtva aqpdakflgg gtnlvdlmre gierpatvvd vtglpleeie
       61 elpdgglrig agvrnsrlag hrlvrsrypm laqailsgas aqlrnmatvg gnllqrtrcl
      121 yfyddaaacn krepgagcaa rdgfhrsgai lgasptciaa hpsdmcvala aldavveves
      181 vrgvrripla gfhrlpgdtp hietelaade litavelpav pvaansryrk vrdrasyafa
      241 lvsvaaaldv rdgavtgarl alggvaakpw raskaeqall gapateesfr haaevelasa
      301 eglpgnafki dlarrtivat lrqvltegga a
//
LOCUS       WP_181661899             263 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Streptomyces himalayensis].
ACCESSION   WP_181661899
VERSION     WP_181661899.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 263)
  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 263)
  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 263)
  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 263)
  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..263
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..263
                     /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=28633
     Region          184..>256
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mntrpftsgl senavmitrv adrqwhaldd dlvvgrghae hrpdgrlfvs idawhdatfd
       61 rlaeamlaql paplytvvde adveltagwr ragfairrre weyavptdpr itgleavlpp
      121 sgvtivpagq adesllravd rairdeveat vgwqsmpaev itrpegdtiv dpskyavaaa
      181 pdrylglirv vtvnrprigl vavrageqrr giarallaha lgtlhrsgfa aawtevhesn
      241 qaasalfegi garpmssnre lvr
//
LOCUS       WP_181661986             403 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181661986
VERSION     WP_181661986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..403
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43685
     Region          1..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 mgndafdgvr vvelaqwvfv pvagalladw gadvirverp egdpyrglst qgigsdstgt
       61 nlsvalanrg krsvaldlrs degprlldrl ldtadvflts frpaalrrlg ldaeelarrf
      121 prlvyarghg fgvrgpgadr agydssafwa qggmahvltp perdhpisqr gamgdrngam
      181 alafgissal lrrertglgs vvdvsllata mwtlssdvla alaggkprgv sgrggavnpv
      241 vgayrtkdgr hiqlvflesd rywpefcrli grddligdpr fadlrargen reacvaelea
      301 efalrtfdew kdllsridap wapvqaveel lsdpqvlang yvgeveledg ssyrlptvpv
      361 qfderppalr rapehgehte avlvelgftw eriaelkdag vip
//
LOCUS       WP_181662185             231 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF899 domain-containing protein [Streptomyces himalayensis].
ACCESSION   WP_181662185
VERSION     WP_181662185.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 231)
  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 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   3  (residues 1 to 231)
  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 231)
  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 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   6  (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 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..231
                     /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=25735
     Region          5..205
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mttralppvv daatwerrlq alrarekaat reldaiaaer rrlpmvempd ytlegedgpv
       61 rladvfegkr qlivynhmwf agkewqcpgc tgftsqytrl efldnydarf vivtqgpike
      121 alaykqrvgn qmtwystans sfgadvgapp gggfavnvfl rdgdtvyrtw htngrgteql
      181 shtfalidvl pygrqeewqd spegwpqspt ysrwatskdi aalygsgsgg g
//
LOCUS       WP_181662135             198 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181662135
VERSION     WP_181662135.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 198)
  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..198
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..198
                     /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=21684
     Region          3..138
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgtrrailaa agaefgahgf dgarvvriae aagvshqlit yyfggkrgly ealseqwlee
       61 smrvsqthtf aeavrryvhw agedaawvht ltreepgkrp paederaael fkhveelrer
      121 qgrgefrsdl dvgavalvff aasiapaaip wiareltqqd paspefidhy aeqvgriisa
      181 laeatqdegs pvngeped
//
LOCUS       WP_181662274             493 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces himalayensis].
ACCESSION   WP_181662274
VERSION     WP_181662274.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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 493)
  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 493)
  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..493
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..493
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52006
     Region          13..492
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mtssttvshd lgttgplvdg twldrtsagq mdhinpatar angtvllsgp qevdaavaaa
       61 kaafpswram spderrrilq rveelmrerv pelgrlntle lgvpfttsaa laylcagwfg
      121 yyagwadkie gatippsprm vpgldytvpe pygvigiilt wngpimsvgm kiapalaagn
      181 cvvvkspdla pftvarfaei aleaglppgv lhivpggpea gdrlvrhpdv akisftggip
      241 takkildaar htlkpvllel ggktanvvfp dadldaavae tvrscytlsg qgcnlttrml
      301 vhrdvydrvv rstaeaaaal rvgdpfdqgt algpvigkta herilgmier aakdsrvvvg
      361 grpadpsala peirdgyfie ptvladvdph sevgqqevfg pvlsvipfds edeavelans
      421 tpyglgtavq trdvsrvqri vpllqsgtvl vngasgqppg apfggykhsg ygreggkegl
      481 yeflqtknvf ira
//
LOCUS       WP_181662204             162 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces himalayensis].
ACCESSION   WP_181662204
VERSION     WP_181662204.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 162)
  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 162)
  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..162
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..162
                     /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=18199
     Region          1..146
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtssdptalp dpwhslhell aamdaeieqv yvergiegvr prfayplirl ahtgpltire
       61 lakslgrshs aisqtiaamr kedlvtsepg pdartrridl tergrslvpf leaewrathe
      121 avaeldsevp camttvveev rralerrsmr qrilhhlvep pr
//
LOCUS       WP_181662130             140 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Streptomyces himalayensis].
ACCESSION   WP_181662130
VERSION     WP_181662130.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..140
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13903
     Region          27..111
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mrepltyaia ygaaeaalea araegaricv vvvnrsgvtk vllsddgvgp igvetarrka
       61 ytaavtgipt stfaafaasp amavapvhlv dahllpvpgg vpitvddgev igavgvggad
      121 getddrlasr aleglkdlla
//
LOCUS       WP_181662460             435 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Streptomyces himalayensis].
ACCESSION   WP_181662460
VERSION     WP_181662460.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  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..435
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..435
                     /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=44833
     Region          158..423
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 msslsrwwpl apaiapvlll avpveygngs stsahvsvad aasaflvlfc avrlvrhrar
       61 pltpvaafvl gipavgfava titaadpvaa lpgfvrylqv fvvvpaavvl llrdardfrv
      121 vagsfvvlal iqgtlgvhqy vtrtgasymg sdiravgtfg ptdvmgmatv vayglviatg
      181 lalrpaqgap pwlrpaaaat avaltlplal sfsrgawiat llgsvavmll tglrqaaral
      241 aavvavavvl vggfgvgsqa vsarfssitr vtdtpdqsvt drytmwaaav smwreepasg
      301 vglkgfpahr dghsslglss gsdtagagra fqrqpllsph smyllvlseq gligatalfg
      361 swaallvggv rrltgarrsr ksavdcglma mglmiwqtvd flyadiggps taltgivfgl
      421 vawwalaepe tsssv
//
LOCUS       WP_181662029             441 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Streptomyces himalayensis].
ACCESSION   WP_181662029
VERSION     WP_181662029.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..441
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..441
                     /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=46158
     Region          54..409
                     /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(54..55,58..59,62,95,145..146,148..150,153,179,
                     182..183,186,256,259..260,263..265,268,295,299,357..358,
                     362,366,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mteqparala rlrpgrgapa attrtadrak phrertwrtl spllrllilt qlafnigfya
       61 vlpflaehlg taigmagwlv glvlglrtfs qqglfvvgga ltdrygvrpv vltgcvlria
      121 gfawlgyaeq twsvigavll igfaaalfsp avesevarqa lrreeagggs rthvlalftv
      181 agqagafvgp flgamllsad flavclagag vfvlvlsghl wllprhtpgr aerpkvsggt
      241 atllrnrrfm rlcgaygayl laynqlylll pdeveraags qaplawlfal ssllvvtaql
      301 pvtrwtadrl glrrsmaagm lliaagfavv alarpaawtg tagllplagf vvlltlgqml
      361 vapaarawvp dlaedgrlgl ytgamssvsg livlagsaga gslldtglpp aapwlvlaav
      421 aaasiallph rsergqrsta r
//
LOCUS       WP_181662622             429 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181662622
VERSION     WP_181662622.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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 429)
  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..429
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..429
                     /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=48182
     Region          3..390
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 msrfrmyprr eqeqqmllrc aharyvwnla veqhshwrrg rkpapsfaeq crqltearae
       61 newlrqgnad vqqqalkdft kaksarftsg fgkptwrkky vhegfrvigt drlpefdddg
      121 spklnaktge qvmgrsvvvq klnrkraqvk vpgcgwvrfr ltravlpvak tfrvnyrngq
      181 whiafavipe pipapgtsea igidrgvtit aalsdgrkln cpqltvkera qirkyqrraa
      241 ratkgspekt aeyakvarlk areanrrkdw cektstmlaq sydvirfekl nvknmtrsak
      301 gtveqpgknv rakaglnrgi laqgwgllrq rtehkapgrv qdvpapytsl rcsacgwidk
      361 nsrksqaefi csscgftcna denaatnvaa gqggilrprr qacaggttpp tqrssvrepq
      421 ptwvgiplf
//
LOCUS       WP_181662793             232 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces
            himalayensis].
ACCESSION   WP_181662793
VERSION     WP_181662793.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=24757
     Region          44..142
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mdddallaeq mayykagaae ydrpyaeced lqelldvvde lpiagdvlel acgtgqwtpr
       61 laarahsvta vdvaaevlal arartasptv rfleadllew qpprrydtvf fafwlshvpp
      121 arlpafwdtv aaalapggka ifiddgpaaa ageevlanqp apaalrrldd gsqyrivkvf
      181 hdaraltddl talgwsvrir pvaesfigia eppptagkea atatpasnvp sh
//
LOCUS       WP_181662816             321 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Streptomyces himalayensis].
ACCESSION   WP_181662816
VERSION     WP_181662816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..321
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=33133
     Region          5..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(39,253,256)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(192,224,251,254..255,258)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 msprqitvlg ecvadafaep astsnelalr vlpgggpant avalarlgtp arflarlsgd
       61 vfgrlfrahl easgvdlssa vqaaepstla vaeldaqgqa afsfhaqgta dwqwtaeela
      121 rvdlseaacv htgslalvre pgaaavedfl aaaapqatis idpnvrpllv hpdvyrarla
      181 hwcaladvlr lseddlelll pgtppeqacd iwhaaggarl vvvtrgaggv lasfdgeriq
      241 vpavatrvvd tvgagdsfta gllhhlgarg llggrltelr lddvaeacrf avrvaaltcs
      301 vagpnppwqs qlaqlatadg m
//
LOCUS       WP_181662878             136 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181662878
VERSION     WP_181662878.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 136)
  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..136
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..136
                     /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=14706
     Region          39..129
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mtdssatpss atpssatpss atpdvahgpv pqpafevpyy avvftsvrte gdggygetag
       61 rleelvkdvp gflgmdlart pgglgitvgy frdedaikew rsdmehraaq krgreewyes
      121 ytlhiakver shgfrk
//
LOCUS       WP_181662822             299 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Streptomyces himalayensis].
ACCESSION   WP_181662822
VERSION     WP_181662822.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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 299)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..299
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..299
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32088
     Region          25..298
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mtisgrerpq lqphirvlhd asrrdlrepd rprpvrlylw epcrpvavpa plvvvshgtg
       61 gsgsdmewlv gplakagfrv avvdhhgnnf vdgydpdgfc fvwerpkdis faldalareq
      121 plgpvgaagf slggytvmal agarldpqvl qavvagrval pvvpefpgls ealrkkvsea
      181 sedelrtvms vaaadlsdpr vravfqvaps lgasvtpesl tavrvpveir wggadtivpf
      241 ddhtkpyleh ipaaqgcsvg ldirhedfig rsdpagpade tvrvrvgqea safflrhlg
//
LOCUS       WP_181662989            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181662989
VERSION     WP_181662989.1
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=166438
     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 gknaeggvfv
      301 senffyesei yntrlyiftd rplyragdrv dvkvmgrefh dplhsspivs apaklsvlda
      361 ngsllqtvdv 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 miqdnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqtsqaigvt 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_181663451             377 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Actinomadura madurae].
ACCESSION   WP_181663451
VERSION     WP_181663451.1
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 11429741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     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=39497
     Region          10..369
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mippeqmpav vigggvigsa aayylaqagi kpivlerdpm paqasvrnag gvraqcrsrv
       61 erllamrsid lwakftadtg ddleyhrggn lrlalkesgl ktfaaeavee aadglhteiw
      121 dradlrrrap ylsprfagak ycasdghanp ilatwamtra aaragavmww garaegietr
      181 grrvvgvrgs adgapfriat plvihaagpw tsklaadlgp qlpltparna ilvtqaaapl
      241 fgtfvsshel gvymrqarag qvhiggvsnv lgtfdqevtt geitslarac evipelggmn
      301 vlrvwsgtld mtpdhlpiig rpagidgyiv aagfsghgfc lspavgrtlc dlacesapgl
      361 distlspdrf stgggta
//
LOCUS       WP_181663475             927 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_181663475
VERSION     WP_181663475.1
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=103974
     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 ewgnaatfdk levdaergvi teewrahqda kwrtsqarrp
      181 fllantrnle repiglmdtv atvtpaqlrq fyqrwyqpnn mtfivvgdid skealalikd
      241 nlsklpanka aenrvwptka enhlrfniin dkenrvngia lyyrlpmaqv 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 qitavsnkgd lsfpaqqksl ialankavsg sgvgelssss lkrwsaensv tmsskvsgmn
      601 tllsvsaran npepgfqlin qrithstinn niwaslqnaq iqalktldqr paekfaqqmy
      661 etryaddrtk llqenqiaqf taadalaadr qlfsspadit fvivgnvaed klvalitryl
      721 gsikhsdspl aagkpltrat dnasvtvkeq nepvaqvsqw krydsrtpvn latrmaldaf
      781 nvalakdlri nireqasgay svssrlsvdp qakdishlla ftcqperhde lltlanevmv
      841 krlakgiseq elneyqqnvq rsldiqqrsv qqlantivns liqyddpaaw teqeqllkqm
      901 tvenvntavk qylshpvnty tgvllpk
//
LOCUS       WP_181663401             524 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Actinomadura
            madurae].
ACCESSION   WP_181663401
VERSION     WP_181663401.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 524)
  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..524
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..524
                     /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=55155
     Region          1..523
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 myelvvrggt vldgtgaaar radvavaggr iaavdvldgv raateidatg rhvmpgfida
       61 hvhgeaavfd pdvqlaalrq gvttfvlgqd gisyapagta tlryvsryfa pvngthpgld
      121 ggpvsvaell agydravpln tvylmphgti rhgvlgtarr apepgelaam wdqverglad
      181 gaaglstgle yvpgsyadaa eigalcapvg aaglpyvthm rgyesaavta maevleiart
      241 grvaphvshy hgprdelial vdgaraegid ltfdsypylr gcstltfvtl pdrlpiadld
      301 atldaladps vrewlhrdwf ahraevwpri vlshvpsgey rwaegmslpd aaeragsspg
      361 efccdllvat rleagcvfgq pptnsdesmr allrhpvhma gsdavyqggh phprgwgafa
      421 rllarhvrdl gdwtweeaav hlagraadrf rladrgrvea graadlvvvd paavtdraty
      481 eaprtlaegi dhvlvngvpv laggaltana vppgralkpd gras
//
LOCUS       WP_181663601            1296 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Escherichia coli].
ACCESSION   WP_181663601
VERSION     WP_181663601.1
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 both ends.
FEATURES             Location/Qualifiers
     source          1..1296
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>1296
                     /product="beta strand repeat-containing protein"
     Region          <1..1296
                     /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 nanitagnft lnatangsnl nnvtlmathd iiltgsnttg iglqlngtnt lnatngsisl
       61 tgnstngtgl qlsngtntln atngsisltg nstngtglfl ggnktlsasn gsinltgsst
      121 sgvglylger nstnaftatn gsinlngvsv aksaieirgn ntltadninl tgnstksfgi
      181 daqdgantln atngsinltg nstngtglql nngtntlnat ngsinltgns tngigidleg
      241 tniltatgga isfngtsgrn rginicgtsn mtatainltg sstgaegidi sgsstltats
      301 gnislngtaq sqwygvriqg snitatngsi sltgnstngi gidlegtnil tatggaisfn
      361 gtsgrnrgin icgtsnmtat ainltgsstg aegidisgss tltatsgnis lngtaqskwy
      421 gvriqgsnit atngsisltg nstngtglql ngtnvhaing niningtvnk lshhdvgqag
      481 vhlnnvilna ssgsvnings vnstvgdaya ntfkggvilg pgvnisalds yingtifgay
      541 gfgvalgseg ysnteinisg nasingfssg deeyepsasw gvafgfsett lnvqngtlni
      601 ngtsggygyg vatkpaygqw astqvainle nanvtisgcg svagvffarh dnsapyspsg
      661 llinggtgni sghsdtgvgv vlgnstning vtvngtsntg tgviinegan vinasvngns
      721 ngtgvsitga vnitgstvtg nasgngngvn isgnitdgvi sgsatgngsg vdisgdstlt
      781 nttvsgngtd gagvsisgnl snsgnstvtg nasgngngvn isgnitdgvi sgsatgngag
      841 vdisgdstlt nttvngngtd gagvsisgnl snsgnstvtg nasgngngvn isgnitdgvi
      901 sgsatgngag vdisgdstlt nttvngngvn gsgvdisgnl tnsgnstvtg nasgngngvn
      961 isgnitdgvi sgsatgngsg vdisgdstlt nttvngngtd gsgvnisgnl tnsgnstvtg
     1021 nasgngtgvd ingtvtggdi tgnasgngng vnisgnitdg visgsatgng agvdisgdst
     1081 ltnttvngng vngsgvdisg nltnsgnstv tgnasgngng vnisgnitdg visgsatgng
     1141 sgvdisgdst ltnttvngng tdgsgvnisg nltnsgnstv tgnasgngng vnisgnitdg
     1201 visgsatgng agvdisgdst ltnttvngng vngsgvnisg nlsnsgnstv tgnasgngng
     1261 vnisgnitdg visgsatgng agvvisgnst ltnttv
//
LOCUS       WP_181662956             415 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181662956
VERSION     WP_181662956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  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..415
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..415
                     /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=45966
     Region          1..385
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mklvvqvkml ptpvqaalea tlracneaag wasevafdkd vkrnfalreh tyaeikarwr
       61 lgaqaaqhvi kkvcdayatl kanlkagnlg kpgskryrra vdkpiafraq gaqpyddrml
      121 swqigerrvs iwtvhgrvkd vaftaspeql atlalyrkge sdlvcrdgmw llfatcevpe
      181 aplnadpvdf lgvdlgvvni avtsdgeita grelnrirmr ertlrrklqr kntpsakrrl
      241 kkrrrkearr akdinhkiak hvvaeaertg rgialeeltg irervrlqkp qrathsswsf
      301 aqlgafiayk arragvpvvy vdpaytsrtc aecghvdkan rvsqawfacr scgvvahadr
      361 ngsrnirara welwrsgaes tapapppshr dgagrkrsit asdarcaspg pvpgs
//
LOCUS       WP_181663683             524 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Enterobacter].
ACCESSION   WP_181663683
VERSION     WP_181663683.1
KEYWORDS    RefSeq.
SOURCE      Enterobacter
  ORGANISM  Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:547"
     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=56472
     Region          16..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 nsvqeparrr palpmvalav lfslmallpl gfiiaigiet gwetiktlvf
       61 rprvaellsn tlwltalavp lcimtgvaia wltertqlag rgiwsalava plaipafvqs
      121 yawvsvvpsm hglsagvfls vlayypfiym pvaavlrrld ptledvaasl gtppwrvffr
      181 vvlpqlklai cggallvalh llaeyglyvm irfdtfttai ydqfqstfsg paanmlagvl
      241 alcclailvl egvtrgkary arigagaare qrrwplkpaa aalgqlffiv livlalgvpl
      301 ivlcrwiwlg gvqnwmnadl whslrqtlml gvggalltta cvipiawlgi ryprrifrml
      361 egciyitssl pgivtalalv tvtihyarpi yqteitlfla yllmfmpral inlragiaqa
      421 pvelenvars lgstpakalw svtmrlaapg aaagaalvfl gvsneltatl llsplgtrtl
      481 stgfwaltse idyvaaapya mlmilislpl tailymqskk iagl
//
LOCUS       WP_181663740            1043 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Escherichia coli].
ACCESSION   WP_181663740
VERSION     WP_181663740.1
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..1043
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..1043
                     /product="beta strand repeat-containing protein"
     Region          <158..946
                     /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 vldggdsgvv hlsgtlqadn asgqggkvvv qgqnillgkg ssitatgskg ggevyigggw
       61 qgkdssirna dkvvmqdgar idvsatqqgn ggtavlwses ftnfrgqisa kggenggngg
      121 qvetsshgnl qafgsvsasa kkgkagnwll dplditivng adnavtetnd tlsqpphtqf
      181 tptatgsqvs ntsindelnn gtsvtvltss ttaggnqngn itvdadinkt ngtdatltll
      241 adgnitvnkn itstagklnv nlaaantsrt gtitlgnnvs ittnggdita gtanasnsvt
      301 invtgttlnt sngsqagnin lngsrvnvtn anitagnftl natangsnln nvtlmathdi
      361 iltgnnttgv glqlngtntl natngsislt gnstngtglq lngtntlnat ngsisltgns
      421 tngtglflgg nktlsasngn inltgnsqkg vglylgernn tntltatngs inlngvsetk
      481 saieirgsnt ltadninltg nstngmgidv qgasntltat ngsisltghs ddnigvslsg
      541 ssswdatnit itgssswngs tfsedvyvrr giqldgnltf tgnvaingtg eggsgvalrt
      601 lvnltfnngt aiingtstgh svndiytagi glhsyigetd itniilnnsn ltmnghsqna
      661 agiggwsdsd tktkwnisgn gnvtingssv emdgfrtisi natglngsva lfgkstngsg
      721 vkitktemsn vtisgsatgn gsgvdisgdn tltnttvsgn gtdgagvsis gnlsnsgnst
      781 vtgnasgngn gvnisgnitd gvisgsatgn gsgvgisgds tlinttvngn gtdgsgvnis
      841 gnlsnsgnst vtgnasgngn gvnisgnltg dagstvtgna sgngtgvdin gtvtggditg
      901 nasgngngvn isgnitdgvi sghavngngv eytgpstltn atvsgtsvhg ydvkeylqda
      961 iqqharstqa alaelraegs qvtetsgyrp etrtltisvc deenncsrnt vlssaeadvq
     1021 ppyshprvva tpmtsgsekn vnp
//
LOCUS       WP_181663165             608 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Actinomadura madurae].
ACCESSION   WP_181663165
VERSION     WP_181663165.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura madurae
  ORGANISM  Actinomadura madurae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 608)
  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 608)
  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 608)
  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 608)
  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..608
                     /organism="Actinomadura madurae"
                     /db_xref="taxon:1993"
     Protein         1..608
                     /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=66550
     Region          6..493
                     /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 mrlhvylarl glagfrsfdq veiplredit vlagennggk ssvmdsirlv ttpldgkrdl
       61 yfdaddvhrg aavnhvtlta tyggeglalh gdaydfttre atysltyvpp ppgrqrgsts
      121 wqagrtqtnd pdptpearkg irhlylpplr daqrelasrq gsrvqgvver llrepaerdv
      181 fvdamrahft aiskvsplpa avaavqgpls dltsgareqn aalgfgdpsl asitrglrll
      241 mneagldpqe laesglgyan llfiatvlaq lvdaaeadlt illveepeah lhpqlqtvli
      301 ehlkeeaiks rervsdtewl griqvvvtth sphiavgctv edlvilqrrq vlstsspeqk
      361 aepdepdkkn apryistsva vsdldlsakd lrklqqylna trntlvfgpr vmlvegisea
      421 illpvfaqql lddprnlrrf tgaalipidg vdfepylrll ltvgpggtri aqrvavitdg
      481 dfgkcarpkd ltdliaslga gsdarvfanh tslepelllt ssknedlirq awremrpraw
      541 qedwqkidga daeqraqtfk eqgdaarirk gdfaqellav avdakqpldv pgyladalrw
      601 iaaeaddr
//
LOCUS       WP_181663868            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha-2-macroglobulin family protein
            [Enterobacteriaceae].
ACCESSION   WP_181663868
VERSION     WP_181663868.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=166196
     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 pelhlgnaii kpsryvqnnq fsplkkyplv eqfryplwqa kpvepqqgvk
      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 glaldkkefk tgeavsgklq llypdgepvk narvqlslra qqlsmvgndl ryagrfpvsl
      481 egsetvsdas ghvalnlpaa dkpsrylltv sasdgaayrv ttakeilier 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 slaqniqqsg
      961 llsaelqqng qvqdsistkl sfvdnswpve qqknvmlggg enalmlpeqa snirlqsset
     1021 pqeifrnnld alvdgpwggv intgsrlipl slawrsladh qsaaandirq miqdnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqalgvt qqpeywqhml dsyaeqadnm
     1141 pllhralvla waqemnlpck tllkgldeai arrgtkdedf seedirdind slildtpesp
     1201 lgdavanvlt mtllkkaqlk stvmpqvqqy awdkaansnq plahtvvlln sggdatqtaa
     1261 ilsgltaeqs tieralamnw lakymatmpp vvlpappgaw 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_181664342             699 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Latilactobacillus sakei].
ACCESSION   WP_181664342
VERSION     WP_181664342.1
KEYWORDS    RefSeq.
SOURCE      Latilactobacillus sakei
  ORGANISM  Latilactobacillus sakei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Latilactobacillus.
REFERENCE   1  (residues 1 to 699)
  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 699)
  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 699)
  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 699)
  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..699
                     /organism="Latilactobacillus sakei"
                     /db_xref="taxon:1599"
     Protein         1..699
                     /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=75944
     Region          6..696
                     /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 mkkknkrnre rshipfrlnf lffivfalfa aliiqlgrlq vlngasyqam vnstdkkivt
       61 gnvprgmvld akgrvlvgns aksaitytkn mnvladkmya eanqltkylt idkldtlter
      121 dqidyylsnp knlkkwnarl pkskkvaadg skipdktvyq stidlveksf tglsdkqkqa
      181 aaifkimsga yqlstvyikn dnvtdkeiae isehltslpg invgtdwers ypngdsmrsi
      241 ighvsteeqg lpedginsll aqgysrndrv gtsylekqye silhgsksqt qvevgnnnqi
      301 lsskvlfkgq kgsnlnltid qayqtkveaa lkkiyakavt agattysdga yavamnpktg
      361 ailamageqn drttkqasdd algvinrtfv mgsavkgatv mggmmdgvis psnntlpdtp
      421 iylpstpvkk svypvgtfgs lsaqsalevs sniymmqlal regkaeyipn ksikispdif
      481 tkmrgyfnqf glgqktgidl pgeakgiegp tltdaglpav gsaldlsygn ydaytliqla
      541 qyistiangg nrmkpylvds iqqtgtdgnl gklesktspt vlntinapks yfnvvkegmy
      601 nvvngtnawg tahtlkdikp tfgaktgtaq sfaredpnds tskqvetvts slvgfapynd
      661 pqvaiaivfp nltsdeghyn tllaremitd yyklnnisk
//
LOCUS       WP_181664511             927 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_181664511
VERSION     WP_181664511.1
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=104108
     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 rymiyphphp 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 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_181664594            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181664594
VERSION     WP_181664594.1
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=166374
     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 slpscnyapp aggtffllad ssfssseeak vrleapgrdy rryqmeeygg
       61 vdvrlyripd pmaflrqqkn lhrivvqpqy lgdglnntlt wlwdnwygks rrvmqrtfss
      121 qsrqnvtqal pelqlgnaii kpsryvqnnq fsplkkyplv eqfryplwqa 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 glaldkkefk tgeavsgklq llypdgepvk narvqlslra qqlsmvgndl ryagrfpvsl
      481 egsetvsdas ghvtlnlpaa dkpsrylltv sasdgaayrv tttkeilier glahyslsta
      541 aqysnsgesv vfryaaless kqvpvtyewl rledrtshsg elpsggksft vnfakpgnyn
      601 ltlrdkdgli laglshavsg kgstahtgtv divadktlyq pgetakmlit fpepideall
      661 tlerdrveqq sllshpanwl tlqrlndtqy earvpvsnsf atnitfsvly 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 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 paktaqqsni pvtverqlyr lipgeeemsf tlqpvtsnei
     1381 dsdalyldei tltseqdavl rygqvevplp pgadverttw gisvnkpnaa kqqgqlleka
     1441 rnemgelaym lpvkeltgtv tfrhllrfsq kgqfvlppar yvrsyapaqq svaagsewtg
     1501 mqvk
//
LOCUS       WP_181664704             135 aa            linear   BCT 28-DEC-2024
DEFINITION  phage tail protein, partial [Escherichia coli].
ACCESSION   WP_181664704
VERSION     WP_181664704.1
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 10506211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>135
                     /product="phage tail protein"
     Region          28..65
                     /region_name="Phage_fiber_2"
                     /note="Phage tail fibre repeat; pfam03406"
                     /db_xref="CDD:427282"
     Region          84..121
                     /region_name="Phage_fiber_2"
                     /note="Phage tail fibre repeat; pfam03406"
                     /db_xref="CDD:427282"
ORIGIN      
        1 sevlaatpka vkaaydlang kytaqdattt qkgivqlssd tnstsetlaa tpkavkaayd
       61 laagkapssh thpwnqitgv ptasltakgi tqlssatnst sevlaatpka vkaaydlang
      121 kytaqdattt qkgiv
//
LOCUS       WP_181664903             488 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Escherichia coli].
ACCESSION   WP_181664903
VERSION     WP_181664903.1
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 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..488
                     /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=52775
     Region          69..>131
                     /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          111..463
                     /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(129,131,298,318,386)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mlyntlsykn spahteaclc qspafihint iltrkaskas sitmetvsaa lpgtnsnphl
       61 esintknikv finvrlfdgi sdklregvqv ivegnkikti eaqdsdlpdn aeiidgkggf
      121 lmpgmidahw haimarpsim tamtadfnyi qalaiaeaqa tllrgfttvr dmggpvfglk
      181 raidehvtsg priypsgafi sqtgghgdfr mlsdiprapv dhlsyiervg itaiadgpdq
      241 vmlrareqlm rgasqvkfma gggvassydg idvtegslpe iraavtaaen wgtyvtvhay
      301 ttravtmaie ggvkciehgq lidettaqlm aqkhiwwclq pflddedavp matsasrakq
      361 qlmsagtdta yglakkykik tawgtdtlfd ahlatrqgaq laklirwytp leilkmatsv
      421 naelcsmsgp rnpypgklgv veagaladmi lidgdplsdi qlladpdraf qvimkdgiiy
      481 kntleckv
//
LOCUS       WP_181665303             341 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Staphylococcus aureus].
ACCESSION   WP_181665303
VERSION     WP_181665303.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 341)
  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 341)
  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 341)
  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 341)
  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 341)
  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..341
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..341
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37705
     Region          4..285
                     /region_name="AR_SDR_e"
                     /note="aldehyde reductase, extended (e) SDRs; cd05227"
                     /db_xref="CDD:187538"
     Site            order(9,11..14,34,82..86,123..125,156,160,185..188,
                     199..200)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187538"
     Site            order(86,88,125..127,130,156,185..187,203,215,221)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187538"
     Site            order(125,156,160)
                     /site_type="active"
                     /db_xref="CDD:187538"
ORIGIN      
        1 mnnkvlatgg tgfvgmriis rlleqgydvq ttirdlskad kviktmqdng isterlmfve
       61 adlsqdehwd eamkdckyvl svaspvffgk tddaevmakp aiegiqrilr aaehagvkrv
      121 vmtanfgavg fsnkdknsit neshwtnede pglsvyeksk llaekaawdf venenttvef
      181 atinpvaifg psldahvsgs fhllenllng smkrvpqipl nvvdvrdvae lhilemtneq
      241 angkrfiama dgqinlleia klikekrpei aqkvstkklp dfilslgakf nhqakegkll
      301 ldmnrnvsne raktllgwep iatqeeaila avdsmakyhl i
//
LOCUS       WP_181665215             295 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181665215
VERSION     WP_181665215.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 295)
  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 295)
  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 295)
  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..295
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>295
                     /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..>278
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpggqqece mrrfagacrf vfnralarqn enheagnkyi pygkmaswlv
       61 ewknatetqw lkdspsqplq qslkdleray knffrkraaf prfkkrgqnd afrypqgvkl
      121 dqensriflp klgwmryrns rqvtgvvknv tvsqscgkwy isiqtesevs tpvhpsasmv
      181 gldagvakla tlsdgtvfep vnsfqknqkk larlqrqlsr kvkfsnnwqk qkrkiqrlhs
      241 cianirrdyl hkvttavskn hamiviedlk vsnmsksaag tvsqpgrnvr aksgl
//
LOCUS       WP_181665655             419 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Escherichia fergusonii].
ACCESSION   WP_181665655
VERSION     WP_181665655.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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..419
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..419
                     /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=46657
     Region          2..414
                     /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 mteqitvtdt lvvgagqagv amsehltnlr iphlvlekqr iaeawrsgrw dslvangpaw
       61 hdrfpnmsfp dcdgdsfvak dqvadyfesw aktfnapirt gvevlhaqal dgrpgfrvet
      121 skgvietqri iaatgpfqkp vipaiaqqns dlhqihsahy frpqqlpagg vlvigagssg
      181 vqiadelqra gkkvwlsvga hdrpprryrq rdfcwwlgvl glweasvkqp gkehvtiavs
      241 gargghtvdf rqlahrgitl vgqtlelnhg kalfgddlqe nirrgdesyl elldaadayi
      301 trnglnlpee pearyflpdp qclthplhel dlanagitsv iwatgyatdy rwlkvnafde
      361 hnqpchqrgi ssepgiyflg lpwlsrrgss fiwgvwhdak yiadhiaiqr qyqayhpsh
//
LOCUS       WP_181665848             297 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia
            fergusonii].
ACCESSION   WP_181665848
VERSION     WP_181665848.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=33874
     Region          <97..285
                     /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 mngklqssdv kndtpynipl linenvissg islislwhty adehyrviwp rdkkkplian
       61 swvavytvqg ckkillknse qitlhgncii flkpmdihsy hceglvweqy wmeftptsmm
      121 dipvgqqsvi yngevynqel tevaelitsa eaiknnlava fltkiiyqwi clmyadgkkd
      181 pqrrqiekli atlhaslqqr wsvadmaati pcseawlrrl flrytgktpk eyyldarldl
      241 alsllkqqgn svgevadtln ffdsfhfska fkhkfgyaps avlkntdqhp tdasphn
//
LOCUS       WP_181666030             382 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181666030
VERSION     WP_181666030.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 382)
  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..382
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..382
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42228
     Region          1..>192
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrifllllml ygfqafaeql psvtdltgtl tteeqtalnq qlqtleqqnh fqvavlvtpt
       61 tggkniklaa sqsyeiyhwk pvgekrygeg ililvvwpeg lasmkighgl kemlppeqaa
      121 qivhyhmqpe fkknnlfsgl tqgiegiaqf tyikanlspl dalanhlfan pqrslpclaw
      181 tllmivaivv lwrftthpgp siwmismitp mvwffcfqnd viirrvsvvc fslffaaicw
      241 qrlavvfnic rafpmmlapq nknakvkkqk kapqvresgr nslfvvllii vvgwclvfas
      301 nkdiafisti iglidhfigp itiagivlli ivakftgnlk lgsghksnkk tgnrnahsrs
      361 ssknsfrggg gssggggssd rw
//
LOCUS       WP_181666041             310 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181666041
VERSION     WP_181666041.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=34570
     Region          1..296
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 malslslntn plvnriatpe dllntiarqi rirdiqlthe finpgwpast iaqmlrrmkk
       61 aqlstgvrvt sgmtgpygrl nhfghpdasv rryyidwfkt faditaelgg daigsqfaif
      121 tqqdhndpqq realiniatd cwgevaehak saglkylfwe pmsigrefge tipaclalqn
      181 rlsaapfaip mwmmadidhg dvtspdprdy dpyawaqavp ryspiihikq smqdkgghrp
      241 ftaqynkhgr iqpeallnal arggakdnei clelsfkere ptdsltcaei aesvaywapy
      301 idtgvedlni
//
LOCUS       WP_181666077             282 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181666077
VERSION     WP_181666077.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=31456
     Region          1..218
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktglstway fwqlsekapk plslfdaidd sqrlgatvfq icdypqiaqw ssgertrlae
       61 haaragitle lgtkgikpdh lqrylaiaae lecsllrtmi nspdhrptls earcsvetvl
      121 pafeqqgvai cletyeqvpt ddnialvqai nsarfgicld panciaslel padvvaktas
      181 yvlnwhvkdf afsrrdgwvg ftlagcplge gllryddiyq qiqpqtrgin qiiehwlpwq
      241 gdsettcrle aawtehnmry lldkqnlina sstqskesdh vc
//
LOCUS       WP_181666105            1659 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia fergusonii].
ACCESSION   WP_181666105
VERSION     WP_181666105.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 1659)
  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 1659)
  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 1659)
  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 1659)
  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..1659
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..1659
                     /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=182637
     Region          32..1658
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mrklnvvacm lllalsgcdn ndktsatgkt nppaeqaase knntsteats pakpssqsle
       61 krqklaqqsa gkslalldls evqlegaatl lltfsipldp eqdfsrlvtv vdtrsgtvdg
      121 awelsdnlke lrlrhlepqr elvvavrrel kglnnaafgi dyqktittrn iqpsvgfasr
      181 gsllpgkvae glpvlalnvn svdvnffrik petlpsfvsq wnyrnsmenw qsdkllkmad
      241 lvytgrfdln ptrntreklq lplsdikplq qagvylavmn qagrydysyp atlftlsdig
      301 vsvhsyqnrl dvftqsleng aaqqgievtl lndkgqtlsq aasdaeghvq lendknaall
      361 larkdgqttl ldlklpaldl aefdiagepg fskqffmfgp rdlyrpgetv ilngllrdad
      421 gkvlpdqpik levikpdgqv lrsvvskpen glyhftypld sgaatgmwhi rantgdnqyr
      481 mwdfhvedfm permalnltg kkkplspkes vkfsvvgyyl ygapasgnal qgqlylrplr
      541 eavaalpgfe fgdiaaenls rtldetqlsl dnsgraevyv ssewqethsp lqvifqgsll
      601 esggrpvtrr veqaiwpadt lpgirpqfat qpaydyssnt tvkkpmvden siasfdivya
      661 daqgvkkpvs glqvrlirer rdyywnwses egwqsqfdqk elveneqsld lqadetgkvs
      721 fpvewgayrl evkapneavs svrfwagysw qdnsaggstv rpdrvtlkld kanyrpgdii
      781 klhiaapaag kgyamvesse gplwwkeidv paqgldlsip vdknwnrhdl ylstlvvrpg
      841 dksrsatpkr avgvlhlplg denrrldlal etpakmrpnk pltvkikasn kngetpkqvn
      901 vlvsavdsgv lnitdyvtpd pwqaffgqkr ygvdiydiyg qviesqgrla alrfggdgde
      961 lkrggkppvn hvnivaqqaq pvtlneqgeg tvtlpigdfn gelrvmaqaw taddfgsses
     1021 kvvvaapvia elntprfmas gdtsrltldi tnltdkpqkl nvtvsasgll elvgespapv
     1081 elapgvrttl fipvraltgf gdgeiqanis gldlpgetfg dqhkhwkigv rpafpaqtvn
     1141 ygfalqpget walpaeslsn fspatlegql vlsgkppfnl aryikelkay pygcleqtts
     1201 glfpslytns sqlwalgikg dsdekrraav digisrllqm qrnnggfalw dkdsqeeywl
     1261 tayvmdflir ageqgysvpa tainhgnerl lrylqdpgmm sipyadnlka skfavqayaa
     1321 lvlarqqkap lgvlreiwgr hedaasglpl lqlgialknm gdatrgeeai alalktprrd
     1381 qrswwgdygs plrdnalmla lleenkllpa eqnsllftls eqafgkrwls tqetnalyla
     1441 artfenlpgk wqaqtslsae sltgeksqtr nldsdqlstl qvtnngdqpl wlrldtsgyp
     1501 qsapepfsnv mqierhildt ngnskslesl rsgelvlvwl evkanksvpd alvvdllpag
     1561 lelenqnlan gsasleqsss kvqnlliqmq qaninhvefr ddryvaavav dkyqpvtliy
     1621 laravtpgty qvpqpmvesm yapqwrasga segfmvvrp
//
LOCUS       WP_181666329             326 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181666329
VERSION     WP_181666329.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 fergusonii"
                     /db_xref="taxon:564"
     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=36842
     Region          37..262
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mvtinnarki lqrvdtlply lhayafhlnm rlervlpadl ldiasennlr gvkihvldge
       61 rfslgnmadk elsafgdkar rlnldihiet sasdkaside avaialktga ssvrfyprye
      121 gnlrdvlsii andiayvret yrdsgltfti eqhedlkshe lvslvkdsem kslsllfdfa
      181 nminanehpi dalktmaphi tqvhikdali vkeqgglghk acisgqgdmp fkellthlic
      241 lgddepqvta ygleeevdyy apafrfeded dnpwipyrqm setplpenhl ldarlrkeke
      301 dainqinhvr nvlqqikqea shllnh
//
LOCUS       WP_181666437             597 aa            linear   BCT 28-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Herminiimonas fonticola].
ACCESSION   WP_181666437
VERSION     WP_181666437.1
KEYWORDS    RefSeq.
SOURCE      Herminiimonas fonticola
  ORGANISM  Herminiimonas fonticola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herminiimonas.
REFERENCE   1  (residues 1 to 597)
  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 597)
  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 597)
  AUTHORS   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 597)
  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..597
                     /organism="Herminiimonas fonticola"
                     /db_xref="taxon:303380"
     Protein         1..597
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67894
     Region          53..577
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mleknpydnl afermasawl tpltynypes anesayldlm snawlgrttc nispaamfna
       61 yadwlthlfl spskrvvllq kawqncwqwh lynrncvvte dqplycvtpl sqdqrfsdpa
      121 wqkwpfnais qgfllqqqww hrattgvrgl skhhedvvtf tvrqlldtla psnfpltnpv
      181 iqqaaiqswg cnfvqgwlna vgdwrrsmpn dviesdnafk vgrdiaispg kvvfqnhlie
      241 liqytpttkt vhalpllfvp awimkyyild lspqnslvry lvnqgytvfm iswknplaed
      301 rdlsmedyrk lgvmaaidav melthapqln aagyclggtl lsiaaasmar dgderiasms
      361 lfasqvdfee pgelslfide sqisfleaim weqgyldtkq magafqllrs ndliwsrrln
      421 qyllglsekk sdlmawnada trmpyrmhse ylrqlflqnd laegryfteg ksthltdisi
      481 pifavgtltd hvapwrsvfk ihrlsdtevt fvltsgghna gvvsppgypd rsyqiatrae
      541 kehgidtdtw qatiehkegs wwpaweswlr vksgkrippp pmpahkpaap gkyvmqp
//
LOCUS       WP_181666469             790 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Escherichia
            fergusonii].
ACCESSION   WP_181666469
VERSION     WP_181666469.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 fergusonii"
                     /db_xref="taxon:564"
     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=89492
     Region          39..718
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkrvlipgvi lcgadlavaa ednekytpff eqmtvyapvp vpvngnthyt sesierlptg
       61 ngnisdllrt npavrmdttq ssslnqgdir pekisihgas pyqnaylidg vsatnnlnpa
      121 nesdsssatn isgmsqgyyl dislldnvtv ydsfvpvefg hfnggvidak ikrfnaddns
      181 iklgyrttrs dwmtshidek nknawnqgss gstyyspefk knfyslsfnq eltdnfgvta
      241 gfsrrqsdit radyvsnngi vegraqyknl idtalskfsw fasdtithdl tfkytesrrd
      301 yntssfpesd remgnksygv awdmdyqlak aklhttigwd hisdytrhdh diwytedvct
      361 ygdirsrctr gglghisqai dnytfktrld wqkieigdfv hqpyfgaeyi ysdawtqrhn
      421 qsesyqikss giktnhtiyh kgkgslgidn ytlyladrms wknislmpgl rydydtylkn
      481 tnisprfmte wdifadrssl itagynryyg gnildmglrd irnswtesls gnktltryed
      541 lktpyndela lglqqkitdn viaranyvyr sahdqiskts htdsatktti teynndgktk
      601 thsfnlsfel aeplqvsqfa inpqivfsyi kskgnlrlns gyeetntgdn kvvyngnlvs
      661 ydsvpvadfn nplkislnmd fthqpsglvw antltwqdar kariqlgktn sqyqsqytdy
      721 kqyvdeklds slnwdtrisw tpqflkaqnl tvsadilnvl dsktavdlst agvstyasgr
      781 qfwldvsmkf
//
LOCUS       WP_181666500             363 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Escherichia fergusonii].
ACCESSION   WP_181666500
VERSION     WP_181666500.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=41920
     Region          38..358
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mnlfkpdrli tfptddpqlv kqlqngtksy lakagdhrya ngwafakmav liiaclscys
       61 lalsqsqwgl yllwylammf camllavnvv hdashdaflr gkkanawlnr lvaipmgldp
      121 dcwrvrhvrf hhgftniefy dpdtaengil rqtpwqrwrp fmrqqhrywp lvaaltfpwy
      181 iwvvdwldra gvtpvtrhla lrgfagwgyf lagklahcal clilpwllse fnfmtillty
      241 llsqllasli fvmliigthw akghtqlppe egkmavgrla htfattfdwt pqpawlgywl
      301 gginlhlthh lfphwhhrhy palsriiaqi asqqgldyql ltladllrlq qqflrrmgek
      361 pid
//
LOCUS       WP_181666747             419 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Escherichia fergusonii].
ACCESSION   WP_181666747
VERSION     WP_181666747.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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..419
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..419
                     /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=46544
     Region          2..414
                     /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 mteqitvtdt lvvgagqagv amsehltnlg iphlvlekqr vaeawrsgrw dslvangpaw
       61 hdrfpnmsfp dcdgdsfvak dqvadyfesw aktfnapirt gvevlhaqal dgrpgfrvet
      121 skgvietqri iaatgpfqkp vipaiaqqns dlhqihsahy frpqqlpagg vlvigagssg
      181 vqiadelqra gkkvwlsvga hdrpprryrq rdfcwwlgvl glweasvkqp gkehvtiavs
      241 gargghtvdf rqlahrgitl vgqtlelnhg kalfgddlqe nirrgdesyl elldaadayi
      301 trnglnlpee pearyflpdp qclthplhel dlanagitsv iwatgyatdy rwlkvnafde
      361 hnqpchqrgi ssepgiyflg lpwlsrrgss fiwgvwhdak yiadhiaiqr qyqayhpsh
//
LOCUS       WP_181666764             352 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia fergusonii].
ACCESSION   WP_181666764
VERSION     WP_181666764.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 352)
  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 352)
  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..352
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..352
                     /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=40591
     Region          9..326
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mgskkagklt wdelldeyff srnlrpdtew syrkvvrgfv dfmgegvfpa dvtqrdiqhw
       61 rrqvlktqsl stytwnnkva hlraifgfgi kkgllpqten plceasvake akkkktlnkd
      121 qmiqvylvvq kfaeyetqqr vpcdrrrnal yparywltvl dvlrytgmrf nqlqhirlkd
      181 vrpgegviel qlegskthre wcvpivaplk aplelllsra rrlgagsddf lfdvcrftdr
      241 iepddyeycp arahqavkgf frrlsrecgf lvsahrfrht latilmespe rnmhlvksml
      301 ghqsiattme yvdvsaasaa gtletalgly tdtrtvsevc keeedreedt en
//
LOCUS       WP_181666731             228 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia
            fergusonii].
ACCESSION   WP_181666731
VERSION     WP_181666731.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 228)
  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..228
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=26142
     Region          62..195
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mgldiklknl mcsscslyca mmpeksprqe ycanacfctw pedslyfnrg iidgivnknh
       61 narlngyifv dfsvsffrlf lddewinyla sssmgivlvt drnmqplany wrknhpavsa
      121 viyhnenmnv anekirqlfi grflsfakgs tltkmefkim gsmirgsdpq diaqdldldi
      181 rsvyaykqri ekrmgrklns lfidshpvtr eqpsplptek rkaelvla
//
LOCUS       WP_181667104              87 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Escherichia
            fergusonii].
ACCESSION   WP_181667104
VERSION     WP_181667104.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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   Wintjens,R. and Rooman,M.
  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 87)
  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..87
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..87
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9829
     Region          <29..>77
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 midlknqere iinlmfsqgi swltavlirh klslaevskm lgisinslkq iekterlssn
       61 iknkmagiyg cppellicpy wmtaehk
//
LOCUS       WP_181667159             382 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181667159
VERSION     WP_181667159.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 382)
  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..382
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..382
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42134
     Region          1..>192
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrifllllml ygfqafaeql psvtdltgtl tteeqtalnq qlqtleqqnh fqvavlvtpt
       61 tggkniklaa sqsyglyhwk pvgekrygeg ililvvwpeg lasmkighgl eemlppeqaa
      121 qivryhmqpe feknnlfagl tggiesiaqf tyikanlspl dalanhlfan pqrslpclaw
      181 tllmivaivv lwrftthpgp giwmismitp mvwffcfqnd viirrvsvvc fslffaaicw
      241 qrlavvfnic rafpmmlapq nknakvkkqk kalqvresgr nslfvvllii vvgwclvfas
      301 nkdiafisti iglidhfigp itiagivlli ivakftgnlk lgsghksnrk tgnrnahsrs
      361 ssknsfrggg gssggggssd rw
//
LOCUS       WP_181666926             664 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Escherichia fergusonii].
ACCESSION   WP_181666926
VERSION     WP_181666926.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 664)
  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 664)
  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..664
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..664
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=74953
     Region          152..>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"
ORIGIN      
        1 mlspkisrls vvvflslina nvnacgpfip nhlltdrnsa llempngsfv fevqqlvkrd
       61 pglpvwqent peeatqtdnd aeppvqnral elyysgakdf hqgkydspyf qqllalpkte
      121 qgewrlaaly slarggfdas ddeldliink ggfnqqlaeq aiqryqqiie evrngaadpe
      181 llslaslgqi ghyylkkgdv aaavkmyarq aaqgspsgka slrmislyit reknlplles
      241 vindplvqql viaelfirhd wgyvseacte dlvdytcpth rdrlikllsq hrvkgfsysd
      301 rlaalayrag nyslaqtlle dapesglsew lkakmalrag diplatrhya raaplfptde
      361 vwgsmdpesp syhgdkaiip scriaseqai lalkrddylq aaalfyqakd lywadlawva
      421 envltlpelq afveknvpvp qhplkpvdln nssygyyisp diiptdvklr allgrrlirh
      481 gqyqqainwf dipnyrqaaq kladlmaiak nknipdkqra qaqyeaarll rfsgielvay
      541 emypdyaits gqysspfeys nndqwisrke kqrthhaipt adehflhyrw qavawaenaa
      601 dllhpktqaw aailcnansw ikfrdpvlnh alwqryvqkg kafpwaasfg qdcpepffta
      661 likr
//
LOCUS       WP_181667201              92 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Escherichia].
ACCESSION   WP_181667201
VERSION     WP_181667201.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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 10007659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     Protein         1..92
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10596
     Region          1..68
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mirchlnrlm gerrlkvadv vrdtglprst vtalwkdnat rielpvlsil chyfncdvse
       61 lleftsdesh velsrpgkgl nnfshrvwfm rk
//
LOCUS       WP_181667419             273 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Escherichia fergusonii].
ACCESSION   WP_181667419
VERSION     WP_181667419.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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..273
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..273
                     /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=28937
     Region          57..273
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrktvavllg svcltamnyv aneaaatttn adevktlffg qddrvpvnap skspwdaigq
       61 letasgnlct atliapnlal taghclltpp ggkldkpval rfisskgvwr yeihgiegrv
      121 dpglgkrlka dgdgwivppa aapwdfgliv lryppsgitp lplfsgdkaa ltaalkaadr
      181 kvtqsgyped hldslyahqd cvitgwaqts vmshqcdtlp gdsgsplmlh tddgwqvigv
      241 qssapaakdr wradnraisv tgfreklqal aqq
//
LOCUS       WP_181667698             362 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Escherichia fergusonii].
ACCESSION   WP_181667698
VERSION     WP_181667698.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..362
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39581
     Region          78..220
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mspqnnhlqr ppaavlyade laklkqndna pcppgwqlsl paarafilgd saqnisrkvv
       61 ispsaverml vtlatgrglm lvgepgtaks llsellttai sgdagltiqg gasttedqik
      121 ygwnyallin hgpstealvp aplyqgmrdg kivrfeeitr tplevqdcll gmlsdrvmtv
      181 peltgeasql yaregfniia tantrdrgvn emsaalkrrf dfetvfpimd faqelelias
      241 asarllahsg iphkvpdavl ellvrtfrdl rangekktsm dtltaimsta eavnvahavg
      301 vrawflanra gepadlvdci agtivkdnee drarlrryfe qrvathkeah wqayyqarhr
      361 lp
//
LOCUS       WP_181667968             403 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Escherichia
            fergusonii].
ACCESSION   WP_181667968
VERSION     WP_181667968.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 403)
  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 403)
  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..403
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..403
                     /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=45567
     Region          <65..395
                     /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 lkefsccdln ivsmkvtpgr ilikswcrqv qdipvlqtrl
       61 eqnadivnva ylsetensls spdstrpryf sdiicnspam kividkaiki adskytvlir
      121 getgtgkdll araihntgsr rfypfipvnc salpeslmes effgyekgaf sgadsqgkkg
      181 lfemadkgtl fldelgelpl nlqskllrvl qeggirrvgg tqiipintri ivatnanlee
      241 miahrtlrad lwyrinvlsl tipplrerph dlnlliryfv qkyakefkrn iildktayet
      301 lrqhtwpgni relentiirl mlmcendiir sndlgldksl ssvsinspns fkdqvlhter
      361 qliekmladn vssreiaktl gvshttvlnk ihryqqgisa asd
//
LOCUS       WP_181667971             249 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181667971
VERSION     WP_181667971.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=27585
     Region          25..248
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqrkifvvta aygyehiqaa ggqkallpvi aksgadgvei rrelftstdl lalaelglai
       61 ehaglqacys apeplfieng dlnpqlpqll qeakdlkslw lkvslghfgr pdqlntlrdw
      121 lassdmalvv endqtpcgrl qpmlrfkeic qqfelpvklt fdmgnwlwvg nspeeaayql
      181 ansvgyihik aalphkesfr avppdnadsr wlklltmlpa dvprgiefpl egadlaavtr
      241 ryvdllrke
//
LOCUS       WP_181668283            1659 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia fergusonii].
ACCESSION   WP_181668283
VERSION     WP_181668283.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 1659)
  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 1659)
  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 1659)
  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 1659)
  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..1659
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..1659
                     /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=182773
     Region          32..1658
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mrklnvvacm lllalsgcdn ndktsatgkt nppaeqaase knntsteats pakpssqsle
       61 krqklaqqsa gkslalldls evqlegaatl lltfsipldp eqdfsrlvtv vdtrsgtvdg
      121 awelsdnlke lrlrhlepqr elvvavrrel kglnnatfgi dyqktittrn iqpsvgfasr
      181 gsllpgkvae glpvlalnvn svdvnffrik petlpsfvsq wnyrnsmenw qsdkllkmad
      241 lvytgrfdln ptrntreklq lplsdikplq qagvylavmn qagrydysyp atlftlsdig
      301 vsvhsyqnrl dvftqsleng aaqqgievtl lndkgqtlsq aasdaeghvq lendknaall
      361 larkdgqttl ldlklpaldl aefdiagepg fskqffmfgp rdlyrpgetv ilngllrdad
      421 gkvlpdqpik levikpdgqv lrsvvskpen glyhftypld sgaatgmwhi rantgdnqyr
      481 mwdfhvedfm permalnltg kkkplspkes vkfsvvgyyl ygapasgnal qgqlylrplr
      541 eavaalpgfe fgdiaaenls rtldetqlsl dnsgraevyv ssewqethsp lqvifqgsll
      601 esggrpvtrr veqaiwpadt lpgirpqfat qpvydyssnt tvkkpmvden siasfdivya
      661 daqgvkkpvs glqvrlirer rdyywnwses egwqsqfdqk elveneqsld lqadetgkvs
      721 fpvewgayrl evkapneavs svrfwagysw qdnsaggstv rpdrvtlkld kanyrpgdii
      781 klhiaapaag kgyamvesre gplwwkeidv paqgldlsip vdknwnrhdl ylstlvvrpg
      841 dksrsatpkr avgvlhlplg denrrldlal etpakmrpnk pltvkikasn kngetpkqvn
      901 vlvsavdsgv lnitdyvtpd pwqaffgqkr ygvdiydiyg qviesqgrla alrfggdgde
      961 lkrggkppvn hvnivaqqaq pvtlneqgeg tvtlpigdfn gelrvmaqaw taddfgsses
     1021 kvvvaapvia elntprfmas gdtsrltldi tnltdkpqkl nvtvsasgll elvgespapv
     1081 elapgvrttl fipvraltgf gdgeiqanis gldlpgetfg dqhkhwkigv rpafpaqtvn
     1141 ygfalqpget walpaeslsn fspatlegql vlsgkppfnl aryikelkay pygcleqtts
     1201 glfpslytns sqlwalgikg dsdekrraav digisrllqm qrnnggfalw dkdsqeeywl
     1261 tayvmdflir ageqgysvpa tvinhgnerl lrylqdpgmm sipyadnlka skfavqayaa
     1321 lvlarqqkap lgvlreiwgr hedaasglpl lqlgialknm gdatrgeeai alalktprrd
     1381 qrswwgdygs plrdnalmla lleenkllpa eqnsllftls eqafgkrwls tqetnalyla
     1441 artfenlpgk wqaqtslsae sltgeksqtr nlnsdqlstl qvtnngdqpl wlrldtsgyp
     1501 qsapepfsnv lqierhildt ngnskslesl rsgelvlvwl evkanksvpd alvvdllpag
     1561 lelenqnlan gsasleqsss kvqnlliqmq qaninhvefr ddryvaavav dkyqpvtliy
     1621 laravtpgty qvpqpmvesm yapqwrasga segfmvvrp
//
LOCUS       WP_181668049             517 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Escherichia
            fergusonii].
ACCESSION   WP_181668049
VERSION     WP_181668049.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=56417
     Region          20..499
                     /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 mkikmlaagi altlpfwaca kdvtiiytnd lhahvepykv pwiadgkrdi ggwanittlv
       61 kqekaknkat wffdagdyft gpyissltkg kaiidimntm pfdtvtignh efdhgwdntl
      121 lqlsqakfpi vqgnvfyqns sksfwdkpyt iiekdgvkig viglhgvfaf ndtvsaatrv
      181 gieardeikw lqryidelkg kvdltvalih egvparqssm ggtdvrrald kdiqtasqvk
      241 gldilitgha hvgtpepikv gntlilstds ggidvgklvl dykekphtft vknfelktly
      301 adewkpdpqt kqvidswnkk ldevvqqtva qspvelkray gesaslgnla adallaaagk
      361 ntqlaltnsg girneipaga itmggvintf pfpnelvtmd ltgkqlrslm ehgaslsngv
      421 lqvskglemk ydsskpvgqr visltlngep iedamvyhia tqsfladggd gftaftegka
      481 rnttggyyvy havvdyfkag ntitdeqing mrvkdik
//
LOCUS       WP_181668838            1523 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Yersinia enterocolitica].
ACCESSION   WP_181668838
VERSION     WP_181668838.1
KEYWORDS    RefSeq.
SOURCE      Yersinia enterocolitica
  ORGANISM  Yersinia enterocolitica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 1523)
  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 1523)
  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 1523)
  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 1523)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1523
                     /organism="Yersinia enterocolitica"
                     /db_xref="taxon:630"
     Protein         1..1523
                     /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=175357
     Region          12..141
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mdlklirspl getkyhaifv hgldgdliet wqspiskefw pnwlfddipg laiwtigypa
       61 akslwhrgqa mhvtdrgrci yellvieeql ktgdlifigh smggliikqi lrvasdrsse
      121 nqiahdfitr vrkvvflatp hsgsslsswg qkagvvfkps patyslgkdd pnlrdlnlfy
      181 rrlvrenntq nltlvemqts lligpikgqi vdpssadagv etdpipvdad hysickpesr
      241 ekavykyivn fikeeaplen srlrienkld qsidinerie hkisilanks lsntllydke
      301 ikqiifrirk lrffgnfsth eeatqflgrv sdgdlcqgsn eirsqaiswc irllsysked
      361 idlnsyvkra ralhecvevd iadafirsrq vedadklivd liksnnkskr sagllilsnk
      421 kkpidainwy knsgeninyf dedgianilk ycihledwel ldnilyeikl edyhesliit
      481 hllaisyftk aiadtelkhr itekmlfsnf plssdkeale nrriavklfq aavkiskklg
      541 qddikained yslwlrlqdp dfrseallel nesmhgdgsl mlrrfpmavg flnvedlnll
      601 lieeqinket atslglsysa alarycylfh ilrtnhpkdi ynylkkhedq lkhcalaedi
      661 lglecellik ldqiplalek iqilkntatd tslyiqyeni ikqksgedsv llslqqysnt
      721 ksiydlshlv nllrdkneye qlefyekelf nrtrsidnll hftkclqeng kfldihnlls
      781 mhknivdqsf tlqvqwgwsl frqghlelcg dlikkikghv dvtlleihry iangdwpsla
      841 mlieeiwhck deqdiqtllq vanlskaiip sraaelinyi adrddnnpnt laslyglats
      901 lgieeqagiw lnkaislsds ngpmkqislk eivdmapewq kkeknlseif dnikapifli
      961 akylnrtiss fyiipflvnk pvldirsfqs ipayashrpk mllenesitl dltslmtlgc
     1021 lkqldkvfdy fkiifiphsl matlfhekek isfhqpsrfv nakninqyil nkkiraydet
     1081 iidninlale vgeelaslie qadktsgenf vvstlpihkv gsymtqtadl gehkkiiisc
     1141 ttvvinlkrh gfissqesel aleylnkkds stnindadit innesnlyis dlalnyfqit
     1201 nildplvnss fnilihnssv nddislltyr diitsadhii eyirsalkna iegkkvklts
     1261 tnynhtkeid pdfhmleeim kseeskyivs ddrflnqyhi fptekihspt ytsldilntl
     1321 hansllsene friqeiklra ahyhfipish deidywldkt sispdgvlle tqelatirry
     1381 liklkmsrsl qlprdaewli tmireisacl knqwikpivn eekvarsnwl lrlldyrgws
     1441 qfhheslqsg lalngqvmlv ssllfwekdr vsndywfwld nyvlekmeqd dpysyqqvik
     1501 vykdetikai dketnhsevn deq
//
LOCUS       WP_181668894             310 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181668894
VERSION     WP_181668894.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=34605
     Region          1..296
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 malslslntn plvnriatpe dllntiarqi rirdiqlthe finpgwpast iaqmlrrmkk
       61 aqlstgvhvt sgmtgpygrl nhfghpdasv rryyidwfkt faditaelgg daigsqfaif
      121 tqqdhndpqr realiniaid cwgevaehak saglkylfwe pmsigrefge tipaclalqn
      181 rlsaapfaip mwmmadidhg dvtspdprdy dpyawaqavp ryspiihikq smqdkgghrp
      241 ftaqynkhgr iqpeallnal arggakdnei clelsfkere ptdsltcaei aesiaywapy
      301 idtgvedlni
//
LOCUS       WP_181669037              75 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia
            fergusonii].
ACCESSION   WP_181669037
VERSION     WP_181669037.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=8689
     Region          19..70
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mkkiaivdkk gleyipnidr mirekecrel ttlanstrwk lekegkfpkr ikigstavay
       61 rlsevqawir gewvv
//
LOCUS       WP_181669222             234 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Brevundimonas vesicularis].
ACCESSION   WP_181669222
VERSION     WP_181669222.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas vesicularis
  ORGANISM  Brevundimonas vesicularis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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..234
                     /organism="Brevundimonas vesicularis"
                     /db_xref="taxon:41276"
     Protein         1..234
                     /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=25476
     Region          1..234
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mprmieidrd klrqliadrg tspravsrgv ggndhlvrdi lsgrsrnara dtiakiadyl
       61 evpssafmsg sdaaeraati aaatlpirgv vqagawleid edqsepetyp aaadlrfpia
      121 aqwlsvvrgd smnalerngq paaiydgdmv hcvdvtaiey sprdgdivev eriraqggvr
      181 evtlkqveii ggvvqlwprs tnprwtspip yadgdvsdte vrirgwvigs lrrf
//
LOCUS       WP_181669304             249 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Escherichia
            fergusonii].
ACCESSION   WP_181669304
VERSION     WP_181669304.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=27599
     Region          25..248
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqrkifvvta aygyehiqaa ggqkallpvi aksgadgvei rrelftstdl lalaelglai
       61 ehaglqacys apeplfieng dlnpqlpqll qeakdlkslw lkvslghfgr pdqlntlrdw
      121 lassdmalvv endqtpcgrl qpmlrfkeic qqfelpvklt fdmgnwlwvg nspeeaayql
      181 ansvdyihvk aalphkesfr avppdnadsr wlkllamlpa dvprgiefpl egadlaavtr
      241 ryvdllrke
//
LOCUS       WP_181667578             410 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181667578
VERSION     WP_181667578.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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 410)
  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 410)
  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 410)
  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 410)
  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..410
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..410
                     /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=46268
     Region          145..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 mithnftpld llsipvwivs pateellfan avarklsqnq sfnqmrnniy svgaqqtltq
       61 yltdlyhrhd ivelltvwrd gkkiplscrl slnhladige vivfegmelp atqglkasrs
      121 anyqrkkqgf yarffqtnsa pmllidpard glivdanlaa lnfygydhen mcqrhtwein
      181 mlgrdvlpvm qeiarlpggh kplnfvhkla dgstrhvqty agpieiygdk lmlciihdit
      241 eqkrleqele qaamrdaltg llnrrqffll tehnssqpgl msqdysllli dtdrfksvnd
      301 lyghqkgddv lcvlartles carkgdlvfr wggeefvlll phttlddala laetiraqva
      361 kitltglprf tvsigvarhe idetidalfk rvddalyrak ndgrnrvlaa
//
LOCUS       WP_181670073             419 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Escherichia fergusonii].
ACCESSION   WP_181670073
VERSION     WP_181670073.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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..419
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..419
                     /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=46616
     Region          2..414
                     /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 mteqitvtdt lvvgagqagv amsehltnld iphlvlekqr iaeawrsgrw dslvangpaw
       61 hdrfpnmsfp dcdgdsfvak dqvadyfesw aktfnapirt gvevlhaqal dgrpgfrvet
      121 skgvietqri iaatgpfqkp vipaiaqqns dlhqihsahy frpqqlpagg vlvigagssg
      181 vqiadelqra gkkvwlsvga hdrpprryrq rdfcwwlgvl glweasvkqp gkehvtiavs
      241 gargghtvdf rqlahrgitl vgqtlelnhg kalfgddlqe nirrgdesyl elldaadayi
      301 trnglnlpee pearyflpdp qclthplhel dlanagitsv iwatgyatdy rwlkvnafde
      361 hnqpchqrgi ssepgiyflg lpwlsrrgss fiwgvwhdak yiadhiaiqr qyqayhpsh
//
LOCUS       WP_181670075             318 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181670075
VERSION     WP_181670075.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=33994
     Region          1..314
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkaftferan tpaeaaasaq rtpgakfiag gtnlldlmkl eietpthlid vnhlgmnhie
       61 pttagglrig alvrnadlaa derirrdyav lsrallagas aqlrnqasta gnllqrtrcp
      121 yfydtnqpcn krqpgsgcta lhgknrqlav vgtsdaciat hpsdmavamq lldavvetvt
      181 pdgserhipl sdfycspgds pqretvltag elivavtlpp pivgthvyrk irdrasyafa
      241 lvsvaaiiqp dgngrvalgg vahkpwrmne adkriplgtk avyeqlfata hptaeneykl
      301 ilakrtlasv ltqagvtr
//
LOCUS       WP_181670188             530 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181670188
VERSION     WP_181670188.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 530)
  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 530)
  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..530
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..530
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=57919
     Region          61..387
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          345..528
                     /region_name="DUF3520"
                     /note="Domain of unknown function (DUF3520); pfam12034"
                     /db_xref="CDD:432277"
ORIGIN      
        1 mrvnkiyiis icgvllsgcs ssvssplaee rwhyvtmsay apspvqqgql qqntarythh
       61 eanpikqtaq eplatfsldv dtgsyanvrr flktgslpda dvvrveelvn yfplteatkk
      121 nmpgckgcer nspfsinyel tpapwnekht llrldiaand iarsklppan lvflidtsgs
      181 mtsderlpli ksslkllvne lrdqdrisiv tyagsarlll pstsgteknt ilnaianlqa
      241 gggtnggagv amayeqaqag yikggvnril latdgdfnig ddpasvedlv kkqresgitl
      301 stlgvgdnny neammvkiad tgngnysyld slseaqkvls nemnqtlvtv akdvkaqief
      361 npqqvieyrq igyekrqlra eefnndavda gdigagkhvt vlfeltlagq qasvdklryg
      421 kspasaqtsn snelmwvklr ykvpqgessr lvempimssa vtrdfsrtsp dmhflsavaa
      481 ygqklrgsey lnktswqqiq swaqegkgad qygyraefiq lvglaeslsr
//
LOCUS       WP_181670277             375 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Escherichia fergusonii].
ACCESSION   WP_181670277
VERSION     WP_181670277.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..375
                     /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=42046
     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 mpasqrlnsi qamrgvaall vvlyharhyl ngqmphekvg dflfgygyig vdlffiisgf
       61 iityvtysqk rdgglsyitk rlfkiyppfi valfsacilr glnfdnlqlt ggftldniik
      121 salfipinfn nppytatnll pvawtityel ifytiffaam qtnhqlrgll tafiiillfl
      181 isslgrgvid fspgakpmss nfislitnpi mltfvlgiis nwlffkiinv einivnayst
      241 ltllaaivli lsgkftghgl lgygfisfli fisimlliei nnvkiprpil flgeisysly
      301 lshmviilti dkykerfplf gdthgfskfa svvivsiffa yilymliekp cvnlsrlllk
      361 krglikasqv stnse
//
LOCUS       WP_181670731             137 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptococcus salivarius].
ACCESSION   WP_181670731
VERSION     WP_181670731.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus salivarius
  ORGANISM  Streptococcus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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="Streptococcus salivarius"
                     /db_xref="taxon:1304"
     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=15809
     Region          2..115
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mfickhevhy yetdrmgith hsnyvrwmee artfflreig wpyekieeeg iispvtsisc
       61 dykatstfad eisieiivks vksarlsfvy hmvnqngvlv ctaasehsfl skdggfvnlk
      121 rdypsffnll kehsvmq
//
LOCUS       WP_181670820             285 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptococcus
            salivarius].
ACCESSION   WP_181670820
VERSION     WP_181670820.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus salivarius
  ORGANISM  Streptococcus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 285)
  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 10599636
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptococcus salivarius"
                     /db_xref="taxon:1304"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31854
     Region          9..69
                     /region_name="HTH_25"
                     /note="Helix-turn-helix domain; pfam13413"
                     /db_xref="CDD:433187"
ORIGIN      
        1 mklhslgeql raarikkels lydvekisgv eaqfllamem dqlkalpedi qqealekyat
       61 svgldgkrlf eeqkqneqkl kkekkpverk edtlaakapm srflkhkree krksnylpll
      121 mlsavsllii csvgyiiirh lsnqpqvikp ntistvnhls tasrakssrs isevtvsgan
      181 vttttqgnql mvdfsnvnss vvldvelskd sddtwfsvdn sdtsesylls ktknskysld
      241 fsdktkptqi iiaqsskvtl kvngesldls qldkntpsyl tlriq
//
LOCUS       WP_181669814             928 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia fergusonii].
ACCESSION   WP_181669814
VERSION     WP_181669814.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 928)
  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..928
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..928
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=104725
     Region          23..444
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          517..928
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrklcylltf vatllliper liaaplpqde klitgqlqng lkymiyphaq pkdqvnlwlq
       61 ihtgslqeed nergvahfve hmmfngtktw pgnkvietfe smglrfgrdv naytsydetv
      121 yqvslpttqk enlqkvmsif sewsaeatfd ekevaaergv iteewrahqd akwrtsqarr
      181 pfllantrnl drepiglmdt vatvtpqqlr afyqrwyqpd nmtfiivgdi dskealalin
      241 nhlgklpatk saqnrvwptt aennlrfnii ndkenrvngi alyyrlpltq vtdeqsfieq
      301 aeqsmliqlf nqrlleriqs gklkhisggt arsvkiapdy qslffrinar ddnmqdaana
      361 lmtelatidk ygfsseeled lkatrltwlk naadqqaerd lrmltsrias sslnntpfls
      421 pqqtyqlser lwaqitdesl aqkwqqlrkn qdafweqmvn sdaaakkals pqaikqlekt
      481 yadkklppyv fpginltltv adnaqakith qekladdlts ltlsngarvv vaktasneek
      541 lqiiavsdkg dlsfpaeqka iialankavs gsgvgqlsas slkrwsaena vtmstkvsgq
      601 ntllsvnarv nnpepgfqll nqrisnskin dniwesmkna qiqslktldq rpaekfaqqm
      661 yearyaddra qrltekqlaq fsaeqalavd rqlfsspadl tfvivgnide etllplvtry
      721 igslkqsehv lsagqplkra ttnanitlke qnepvaqvaq wkrfdtrspv tlpvrmalda
      781 fnavltkdlr vnireqasgv ysvssrfsvd kqandlthvi gftcqperhq elltlankvm
      841 adrlvkgina qelneyrknm qrnleiqqqn tqqlantivs slvqyndpaa wteqekllqq
      901 ltpeqvnnta rkylssavni ysgvllpk
//
LOCUS       WP_181670961             407 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptococcus salivarius].
ACCESSION   WP_181670961
VERSION     WP_181670961.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus salivarius
  ORGANISM  Streptococcus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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="Streptococcus salivarius"
                     /db_xref="taxon:1304"
     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=46046
     Region          95..407
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mfrrlrlqfi tiaslailfi lvftvgiint vrsfqteqei skvlntlten ngsfgktkki
       61 etnqgreips dsfrffsvtl sgdevvsqdt shtslindee aatyaraasr mtstigtire
      121 kninlsyqvs kvsknkilvv fldttsyyns sqallslsil lsmfgfiffv iivsalsgiv
      181 irpfirnyek qrrfitnagh elktplaiis antelqelmt genewtkstn dqvarlttli
      241 nslvalsrle eqpdivlqdv dfsyitedaa edfkgpvvrd gksfvmditp dihvkaeeks
      301 lfelvtllvd nankycdpeg tvtvrlrqig rtrkrarlev sntykdgkdv dyskfferfy
      361 rieeshnnre hkgfgiglsm aqsmvklfkg rifasykndt itftvil
//
LOCUS       WP_181671101             347 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Streptococcus salivarius].
ACCESSION   WP_181671101
VERSION     WP_181671101.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus salivarius
  ORGANISM  Streptococcus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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="Streptococcus salivarius"
                     /db_xref="taxon:1304"
     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=36667
     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 mpfkktkhlv fsrylsllcl llvllvasvf vavslgavti digdtygvif sklglpiash
       61 tiakpleaii wnmrvprvll glivgaglsm sgsvmqstvn npiaepyilg isagatfgat
      121 laiilglkav vglgafvgai latvlvliia smqgrvttsg lilsgtvvna lfiafanfii
      181 sigatadsvm tikfwtmgsl tgtswsdlll pavvvglafl ffstqyrvfn ammmgdeaal
      241 tlgiplklyw ylyialvavi tavlvascgi igfvglitph iarslvgtny rklfpvatll
      301 gslfviwadv larilvknae lpigiftalv gapffiyivt rnrrkvv
//
LOCUS       WP_181671064             360 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Streptococcus salivarius].
ACCESSION   WP_181671064
VERSION     WP_181671064.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus salivarius
  ORGANISM  Streptococcus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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="Streptococcus salivarius"
                     /db_xref="taxon:1304"
     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=39978
     Region          5..356
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mskldrirhf lnenkaglai vsdpvtvnyl tgfdcdpher qmflfvyenr epalfvpale
       61 varasavldf pvfgyvdsen pwqkikagla stdspiiyae fdnlnvtkfq glqtvfdgrf
      121 enltpfiqkm rviksadeiq kmlvagdyad kavnigfdni sldvtetdii aqiefgikrl
      181 gyemsfetmv ltgnnaanph gipgsnkiek dalllfdlgc mvngyasdmt rtvavgqpdq
      241 fkkdiynicl eaqltaldfi kpgvtasevd aaarnvieka gygeyfnhrl ghglgmdvhe
      301 fpsimegndl vieegmcfsv epgiyipekv gvriedcgyv tkdgfevfth tpkellyfdv
//
LOCUS       WP_181671352             264 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptococcus
            salivarius].
ACCESSION   WP_181671352
VERSION     WP_181671352.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus salivarius
  ORGANISM  Streptococcus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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 11443800
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Streptococcus salivarius"
                     /db_xref="taxon:1304"
     Protein         1..264
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29900
     Region          9..81
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          163..262
                     /region_name="Peptidase_S24"
                     /note="Peptidase S24-like; pfam00717"
                     /db_xref="CDD:425835"
     Site            order(188,224)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119397"
ORIGIN      
        1 mkeckdsnnt kgmmfterlt klrlargwtk kefsvqigkt qqtvgkweng tnaptfkdlv
       61 klvelfgvts dyllglsdsp skyayppfnd nkeeyvgemf kqldegnqdv tvdfienrld
      121 nqhlskeire kdhrkqilgq gerptkrvsi yarvssqgfe lsevpvdcld ypvpipvhdi
      181 afkvagdsle psffddevif vikdsilrtg disivqinsr ffvmkvgqnr engdillnsl
      241 nsdeapitls ekddfsifgk ivlm
//
LOCUS       WP_181671281             256 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptococcus
            salivarius].
ACCESSION   WP_181671281
VERSION     WP_181671281.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus salivarius
  ORGANISM  Streptococcus salivarius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 256)
  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..256
                     /organism="Streptococcus salivarius"
                     /db_xref="taxon:1304"
     Protein         1..256
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29763
     Region          6..66
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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 migkwlkekr enlsltaqdi kqetktsstl islvetgkrl psekflesyl lvlakasgfd
       61 etlrdryttt ecfeewkskl tiehkgkdti yyscgrkicv dskglylkni epydlhvyfi
      121 gyswsdfady qnsylkqeln idvlestpnr lnkkidliet ldidaevtqy wlekyrdelk
      181 kliedsfdel pksyekiyys ltkfgleeei kkensngiei sqlsqlnlvl dgelltdgel
      241 eaiatviegi rarrrk
//
LOCUS       WP_181671564             313 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: O-antigen ligase family protein [Clostridium].
ACCESSION   WP_181671564
VERSION     WP_181671564.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 313)
  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..313
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     Protein         1..313
                     /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=35766
     Region          58..>237
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mfmliiitlf dqndiknlly svifsvnlsc lygfiqifkd gislhninkn ralltfgyhn
       61 vnifagilvt vmpfvleyil ynknskaekr ffysslfiqi iallitftrg awlsalialf
      121 liliskkykk lviimviiga ilikpamsfi ltrgnnvssf lenessiari qsiytdarii
      181 kdypfgvgms sfpeyykefa trgylmmpqe lrwkvkaahy mlehahnlil qigvefglis
      241 lliyillmln rvkvvfkdys knrglfvsli tyiifstltg nefnhkgvit gtiiiflvlg
      301 lieinnckgr inn
//
LOCUS       WP_181671636             419 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia fergusonii].
ACCESSION   WP_181671636
VERSION     WP_181671636.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=48199
     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 kyrrssdkke drlafgvwpt
       61 vtlaqarakr deakkllvqg idpkaeqkea kaensgaytf etiarewhas nkrwsedhrs
      121 rvlrylelyi fphiglsdir qlktshllap ikkvdasgkh dvaqrlqqrv taimryavqn
      181 dyidsnpasd magalsttka rhypalpssr fpeflarlaa yrgrvmtria velslltfvr
      241 sselrfarwd efdfdkslwr ipakreeikg vrysyrgmkm keehivplsr qamilldqlk
      301 qisgdkellf pgdhdatkvm sentvnsalr amgydtktev cghgfrtmar galgesglws
      361 ddaierqlsh sernnvraay ihtsehlder rlmvqwwady lekntvdyit pydfakrqv
//
LOCUS       WP_181671740             928 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia fergusonii].
ACCESSION   WP_181671740
VERSION     WP_181671740.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 928)
  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..928
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..928
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=104695
     Region          23..444
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          517..928
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrklcylltf vatllliper liaaplpqde klitgqlqng lkymiyphaq pkdqvnlwlq
       61 ihtgslqeed nergvahfve hmmfngtktw pgnkvietfe smglrfgrdv naytsydetv
      121 yqvslpttqk enlqkvmsif sewsaeatfd ekevaaergv iteewrahqd akwrtsqarr
      181 pfllantrnl drepiglmdt vatvtpqqlr afyqrwyqpd nmtfiivgdi dskealalin
      241 nhlgklpatk saqnrvwptt aennlrfnii ndkenrvngi alyyrlpltq vtdeqsfieq
      301 aeqsmliqlf nqrlleriqs gklkhisggt arsvkiapdy qslffrinar ddnmqdaana
      361 lmtelatidk ygfsseeled lkatrltwlk naadqqaerd lrmltsrias sslnntpfls
      421 pqqtyqlser lwaqitdesl aqkwqqlrkn qdafweqmvn sdaaakkals pqaikqlekt
      481 yadkklppyv fpginltltv adnaqakith qekladdlts ltlsngarvv vaktasneek
      541 lqiiavsdkg dlsfpaeqka iialankavs gsgvgqlsas slkrwsaena vtmstkvsgq
      601 ntllsvnarv nnpepgfqll nqrisnskin dniwesmkna qiqslktldq rpaekfaqqm
      661 yearyaddra qrltekqlaq fsaeqalavd rqlfsspadl tfvivgnide etllplvtry
      721 igslkqsehv lsagqplkra ttnanitlke qnepvaqvaq wkrfdtrspv tlpvrmalda
      781 fnavlakdlr vnireqasgv ysvssrfsvd kqandlthvi gftcqperhq elltlankvm
      841 adrlvkgina qelneyrknm qrnleiqqqn tqqlantivs slvqyndpaa wteqekllqq
      901 ltpeqvnnta rkylssavni ysgvllpk
//
LOCUS       WP_181672208             393 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella pneumoniae].
ACCESSION   WP_181672208
VERSION     WP_181672208.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae 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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=44483
     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 mklnarqvda akpkekaykl adgaglylev vpsgsrywrm kyrfngkekr mafgvypavs
       61 laqaralrde akkklaegid psfakkeekl vrdvrlhntf qavalewhgt kvsrwsegya
      121 sdiieafnkd ifpyigqqpv neikplvlln vlrrmesrga tekakkvrqr cseviryaiv
      181 tgraeynpaa dltsamsghe skhypfltve elpdffkals gytgsplivl aarlliltgv
      241 rtgelrgafw sefdlekavw eipaermkmk rphlvplstq aleivqqlkv msgqyplvfp
      301 grndprktms easinqvfkr igytgkvtgh gfrhtmstil heegfntawi etqlahvdkn
      361 aisgtynhal ylegrkemmq wygdyvdsce snn
//
LOCUS       WP_181672241             828 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF2345 domain-containing protein [Klebsiella pneumoniae].
ACCESSION   WP_181672241
VERSION     WP_181672241.1
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 10008437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..828
                     /product="DUF2345 domain-containing protein"
                     /calculated_mol_wt=91020
     Region          1..828
                     /region_name="COG4253"
                     /note="Uncharacterized conserved protein, DUF2345 family
                     [Function unknown]"
                     /db_xref="CDD:443395"
ORIGIN      
        1 mdtssiitgt tlnryqldip sctasldvee fsgaeklsel yyytitftsa eknidaaqll
       61 skpamltmgg galqqladck rvhgvittfr rvnrsedqst yqitlqpfls lldkqfrshr
      121 ffvnksvpev veqvlqehhl hdweyefnlk qhyprreqin qyqesdlafi qrllaevgif
      181 yfftlqeeaq sevvhfadaq ralmfdktlp vnspsgmsds gaesiwglni tynvveanvt
      241 trdynprdaq svlqsatadm trgngegity gevyhyklrh rergdkidpq aetanfyarl
      301 dherflahqt litasstaaw lapaqvmtvt dslpstlpap vqdpllitgt gftasrreal
      361 rvsllavpys etlcwrppll prpkvtgtmt arvtsakand iyawqdasgl yrvkfdadre
      421 ekgqgqesmp vrlakpyggd vygfhfpliq gtevaiafhe gdpdrpyiah alhdsrhvdp
      481 vteknstrnv irtpannklr medkrgeehi klsteyggkt qlnlghnvna qrelrgegae
      541 lrtdkwvsir ggagmfisad kqpsagdrml ameeaiaqle nalgiaksla saaesaqalp
      601 sdtgnqqtln dalkelaqpg ivlnapqgvs isspqavrls sgsasvgivs qqntdisalk
      661 rftvaageav sllarkagmk lfaakgkiei qaqddaleat akkditvtsv egrveitaae
      721 elvvncagay irlsggniel gcpgnillks anvqkmgkad frvpplelpk gfeerftvkd
      781 qktgeivpfa ryrittekgq vfegradaeg ktasvytalp esikiell
//
LOCUS       WP_181672468             319 aa            linear   BCT 28-DEC-2024
DEFINITION  YbgA family protein [Escherichia fergusonii].
ACCESSION   WP_181672468
VERSION     WP_181672468.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 10007153
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36769
     Region          69..315
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mikkpvigis gclagsavrf dgghkradfl mdklvewvtf rpvcpemaig lpvprpalrl
       61 vrstqgnirm cfshdqnedv termtefsrs ymnklkdvsg fvvcakspsc gmervrvyde
      121 ngnrgrkdgv glftstlmek fswlpveedg rlhdpvlren fvervfalhe lnhlykekls
      181 rrellafhsr yklqllahsq agykdmgpfv aaihewadle syfevyrdkl mailrkpasr
      241 knhtnvlmhi qgyfsnylst rqrkelsevi lnyrsgtlpl lapltllkhy lgeypndyll
      301 tqnyfdpypd elalrlmvn
//
LOCUS       WP_181671786             336 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Elizabethkingia
            anophelis].
ACCESSION   WP_181671786
VERSION     WP_181671786.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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..336
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..336
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=37540
     Region          <251..328
                     /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 mrkilslgll svsflgfsqq vefttllkdk isiralevsn gkvwysgtes kfgfvnvndt
       61 ldkkqirlsd knlqfrtlaq dkkyfyaini espanffrve kkslkvenvf qdkgptafyd
      121 alhftgggaa yafsdtdesl klklaqmdkk gmwsipnhnv qlnkgeaafa asntniassk
      181 nylwiatggm ssrilrqnlk tqkweifntp fvqgkssqgm ysvdfygdrf giavggdyta
      241 qkenqnniat ttdggktwei qasgknggym tcvrikpgse gkeiiavgdq hisysvdygk
      301 twkviseekn lyvcqwldrn tvvlagnnki lkmkfq
//
LOCUS       WP_181672498             328 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Escherichia
            fergusonii].
ACCESSION   WP_181672498
VERSION     WP_181672498.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 fergusonii"
                     /db_xref="taxon:564"
     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=36233
     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 vakyihtiaf gendnapyig
       61 vncaaipenm leatlfgydk gaftgaiasv pgkmelanng tllldeigdm plalqakilr
      121 vlqeqqverl gsnrqiklnf rliactnknl eqevaagrfr edlyyrlavi pitmpplrer
      181 lndiiplaes fikkystvlv knitlsestr rallnyrwpg nvrqlenaiq rgmilnrdgv
      241 iypdalglpd tdiadhsdlq wpvqpavhia etgdlgqhgr saqyqyiadl mrkyqgnrsk
      301 ianllgitpr alryrlasmr khgievfs
//
LOCUS       WP_181672556              83 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Shigella sonnei].
ACCESSION   WP_181672556
VERSION     WP_181672556.1
KEYWORDS    RefSeq.
SOURCE      Shigella sonnei
  ORGANISM  Shigella sonnei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 83)
  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..83
                     /organism="Shigella sonnei"
                     /db_xref="taxon:624"
     Protein         1..83
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9304
     Region          6..69
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mlnentpeni krlrqkiglt qkecaeifsm sprtwrrkee pvgtasgtal tpvefkflll
       61 lagehpdyvl ckrnkknsds gsk
//
LOCUS       WP_181671821             381 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease, partial [Escherichia coli].
ACCESSION   WP_181671821
VERSION     WP_181671821.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 381)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..381
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..381
                     /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          <75..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 yeyysvrfst fsgghfasfr rylrhlllds aridnehaaq eytrtvysvn vpvadryrle
       61 nsyrqqkmhf carhlsaind tlktyqfgvr sgaksglean lditedgisi rhrgkgrqcf
      121 iktefalqrh qqqggeihal lleepenhls hvsmkrlvnq laterqtqvf iathsshiss
      181 rldlrkaill gatrpvlmne lsaetaaffm kapdnnvlef alarrvllve gdaefiliea
      241 fyhrlygrap eddgvhiiai ggtsfrryle larllenrva alrdndgnyq qncderyadv
      301 lcsrsrvfad hdnsrstfei clyqdnadlc dalfrgtrrt ltvqdymlan kaeaafqllq
      361 lhaekltvpd yiqealawir e
//
LOCUS       WP_181672816             274 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181672816
VERSION     WP_181672816.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 274)
  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 274)
  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 274)
  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..274
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..274
                     /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..264
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 lpklgwmryr nsrqvtgvvk nvtvsqscgk wyisiqtese vstpahpsas mvgldagvak
       61 latlsdgtvf epvnsfqknq ktlarlqrql srkvkfsnnw qkqkrkiqrl hscianirrd
      121 ylhkvtttvs knhamivied lkvsnmsksa agtvsqpgrn vraksglnrs ildqgwyemr
      181 rqleykqlwr ggqvlavppa ytsqrcaccg htakenrlsq skfrcqvcgy tanadvngar
      241 nilaaghavl acgemvqsgr plkqeptemi qata
//
LOCUS       WP_181673170             237 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia
            fergusonii].
ACCESSION   WP_181673170
VERSION     WP_181673170.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     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=27436
     Region          14..>199
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtlitqeneh drlatrlsii lsrlfqgekl higtlaeefg vttrtlrrdf nvrltyldie
       61 qsngvyqlas hyfrrrterd mkilarllhl drllpamdak llsllldgeh pspyrimlpe
      121 prqkptlfgd fsrltlailn qtqvrirtde nvshtvhpyr llcshaewfl agytssgvfv
      181 islsrirlve vlpdttfeid ntlislieqs dfmealphmn iihqimhygs kqtnnrn
//
LOCUS       WP_181673770             498 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia fergusonii].
ACCESSION   WP_181673770
VERSION     WP_181673770.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 fergusonii"
                     /db_xref="taxon:564"
     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=55753
     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 ggllvmatag yvqadalqpd pawqqgtlsn glqwqvlatp qrpsdrievr
       61 llvntgslae stqqsgysha iprialtqng gletaqarsl wqqgvdpkrp mppvivsyds
      121 tlfnlslpnn rndllkeals ylanisgnlk vtpetvahal qsqdmvatwp ldtkegwwry
      181 rlkgstllgh dpadplkqpv daekihefyq kwytpdamtl ivvgnvdars vaeqinktfg
      241 elkgkrqtpa pvptlsplra eavsimtnav rddrlsimwd npwqpiress alqrywradl
      301 arealfwhvq qmlsknnskd iglgfdcrvl ylraqcaini espndklnan lntvarelak
      361 vrdnglpeee fnalvaqkkl elqklfatya radtdilmsq rmrslqnqvv diapeqyqkl
      421 rqdflnsltv emlnqdlrqq lsremalill qpkgepeynm kelqatwdqi mapkpaaapa
      481 aietddvhpe vsdippaq
//
LOCUS       WP_181674185            1659 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia fergusonii].
ACCESSION   WP_181674185
VERSION     WP_181674185.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 1659)
  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 1659)
  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 1659)
  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 1659)
  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..1659
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..1659
                     /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=182692
     Region          33..1658
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mrklnvvacm lllalsgcdn ndktsatgkt nlpaeqaase knntsteats pakpssqsle
       61 krqklaqqsa gkslalldls evqlegaatl lltfsipldp eqdfsrlvtv vdtrsgtvdg
      121 awelsdnlke lrlrhlepqr elvvavrrel kglnnatfgi dyqktittrn iqpsvgfasr
      181 gsllpgkvae glpvlalnvn svdvnffrik petlpsfvsq wnyrnsmenw qsdkllkmad
      241 lvytgrfdln ptrntreklq lplsdikplq qagvyiavmn qagrydysyp atlftlsdig
      301 vsvhsyqnrl dvftqsleng aaqqgievtl lndkgqtlsq aasdaeghvq lendknaall
      361 larkdgqttl ldlklpaldl aefdiagepg fskqffmfgp rdlyrpgetv ilngllrdad
      421 gkvlpdqpik levikpdgqv lrsvvskpen glyhftypld sgaatgmwhi rantgdnqyr
      481 mwdfhvedfm permalnltg kkkplspkes vkfsvvgyyl ygapasgnal qgqlylrplr
      541 eavaalpgfe fgdiaaenls rtldetqlsl dnsgraevyv ssewqethsp lqvifqgsll
      601 esggrpvtrr veqaiwpadt lpgirpqfat qpvydyssnt tvkkpmvden siasfdivya
      661 daqgvkkpvs glqvrlirer rdyywnwses egwqsqfdqk elveneqsld lqadetgkvs
      721 fpvewgayrl evkapneavs svrfwagysw qdnsaggstv rpdrvtlkld kanyrpgdii
      781 klhiaapaag kgyamvesse gplwwkeidv paqgldlsip vdknwnrhdl ylstlvvrpg
      841 dksrsatpkr avgvlhlplg denrrldlal etpakmrpnk pltvkikasn kngetpkqvn
      901 vlvsavdsgv lnitdyvtpd pwqaffgqkr ygvdiydiyg qviesqgrla alrfggdgde
      961 lkrggkppvn hvnivaqqaq pvtlneqgeg tvtlpigdfn gelrvmaqaw taddfgsses
     1021 kvvvaapvia elntprfmas gdtsrltldi tnltdkpqkl nvtvsasgll elvgespapv
     1081 elapgvrttl fipvraltgf gdgeiqanis gldlpgetfg dqhkhwkigv rpafpaqtvn
     1141 ygfalqpget walpaeslsn fspatlegql vlsgkppfnl aryikelkay pygcleqtts
     1201 glfpslytns sqlwalgikg dsdekrraav digisrllqm qrnnggfalw dkdsqeeywl
     1261 tayvmdflir ageqgysvpa tainhgnerl lrylqdpgmm sipyadnlka skfavqayaa
     1321 lvlarqqkap lgvlreiwgr hedaasglpl lqlgialknm gdatrgeeai alalktprrd
     1381 qrswwgdygs plrdnalmla lleenkllpa eqnsllftls eqafgkrwls tqetnalyla
     1441 artfenlpgk wqaqtslsae sltgeksqtr nlnsdqlstl qvtnngdqpl wlrldtsgyp
     1501 qsapepfsnv lqierhildt ngnskslesl rsgelvlvwl evkanksvpd alvvdllpag
     1561 lelenqnlan gsasleqsss kvqnlliqmq qaninhvefr ddryvaavav dkyqpvtliy
     1621 laravtpgty qvpqpmvesm yapqwrasga segfmvvrp
//
LOCUS       WP_181674408             273 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Escherichia fergusonii].
ACCESSION   WP_181674408
VERSION     WP_181674408.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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..273
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..273
                     /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=28939
     Region          57..273
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrktvavllg svcltamnfv dneaaatttn adevktlffg qddrvpvnap gkspwdaigq
       61 letasgnlct atliapnlal taghclltpt ggkldkpval rfisskgvwr yeihgiegrv
      121 dpglgkrlka dgdgwivppa aapwdfgliv lryppsgitp lplfsgdkaa ltaalkaadr
      181 kvtqsgyped hldslyahqd cvitgwaqts vmshqcdtlp gdsgsplmlh tddgwqvigv
      241 qssapaakdr wradnraisv tgfreklqal aqq
//
LOCUS       WP_181674759             281 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family transcriptional regulator [Escherichia coli].
ACCESSION   WP_181674759
VERSION     WP_181674759.1
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=30801
     Region          30..97
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 mlakvtflsc itmsdftfsg yelacfvths glsrsaghil sqcanlaatt seyfihkphr
       61 liaaetgysq stvvrafrea vnkgilsvei vigdhrerra nlyrftpsfl afaqqaknal
      121 iesklkissa atkvkavlak tlalfnflst spcqndtpsp cqddvaiknk ksqvkktkrs
      181 vsdgagtsrl kkltswiaea kakadnlrls kkraqkhefk qkveaaarky aylknkrspd
      241 iggisnfdnl phcmtvneal navlaknkdn eqwgipagfr g
//
LOCUS       WP_181672864             324 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Escherichia fergusonii].
ACCESSION   WP_181672864
VERSION     WP_181672864.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..324
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34129
     Region          9..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mikhltlpkk maamvllaga alstapvqaa swptkqielv vpyaagggtd lvarafadaa
       61 knhlpvsigv inkpggggai glseiaaarp ngykiglgtv elttlpslgm vrfktsdfkp
      121 iarlnaepaa itvrsdapwn syeefmtyak anpgkvrign sgtgaiwhla aaaledktga
      181 kfshvpydga apaitgllgg hieavsvspg evinhvkggk lktlvvmade rmktmpdvpt
      241 lkekgvdlsi gtwrglivsq ktpqdvvdvl akaaketaee pafqdalqkl nlnyawldga
      301 sfqtqineqe kyfdelltrl glkk
//
LOCUS       WP_181674943             262 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein, partial
            [Escherichia coli].
ACCESSION   WP_181674943
VERSION     WP_181674943.1
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: incomplete on the carboxy end.
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]"
     Region          11..261
                     /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 wq
//
LOCUS       WP_181675030             380 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenilisteria rustica].
ACCESSION   WP_181675030
VERSION     WP_181675030.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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..380
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..380
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42156
     Region          71..379
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mhvsrteraq kkrktrrlgi iftviacflf gglgsaylfm qahskvtade msmneestan
       61 vkanividph aslktkidli lkkhqfngaa yvvkdnktii nqgygvankt tgeantsqsl
      121 ffigsmekav vataimqlqe kgllnvedpi akyfpefpng qtikiknflg htsglegrkk
      181 gnnkvtsqqi leqieaagik rqpgtwdyqd dnyavmgrlv eklshqslea ylkqhvlapa
      241 gmkatsfgds ffthpnesvs ykstngaltk tsfvqdtsql fgagnmympp rdiylfnkal
      301 tdgklvnqas larmlkagag nygygfytrp nfyisrgvly nyetinsfsk dyrdavivfs
      361 nirmekdnga lvkeiysamq
//
LOCUS       WP_181675121             305 aa            linear   BCT 28-DEC-2024
DEFINITION  COX15/CtaA family protein [Paenilisteria rustica].
ACCESSION   WP_181675121
VERSION     WP_181675121.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..305
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..305
                     /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=34378
     Region          1..296
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mktflkvwsv ltilcmtfvv fggalvtktg sadgcgntwp lcngqfvrlt ditpekiiev
       61 mhrlttgiss ifvivlaila wiyikdrret kplaivavaf lvlqafmgaa avmwgqnpyi
      121 malhfgisii cyaaivllcl lifevdnkfd arnmvigtkl kvniylltiy tylsvytgal
      181 vrhekaslav pawpfvdgkf vmptnvqdyv qylhrfaali lvvwilyvtw ivfreyshyr
      241 vlkyamvlei ifvaaqaftg imsvvtnvnl yvalahslii tmmfalmtyl cllasrskqn
      301 rlrir
//
LOCUS       WP_181672637             263 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial [Shigella
            sonnei].
ACCESSION   WP_181672637
VERSION     WP_181672637.1
KEYWORDS    RefSeq.
SOURCE      Shigella sonnei
  ORGANISM  Shigella sonnei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 263)
  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 263)
  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 263)
  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..263
                     /organism="Shigella sonnei"
                     /db_xref="taxon:624"
     Protein         <1..>263
                     /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 wlkdapsqpl
       61 qqslkdlera yknffqnraa fprfkkrgqn dvfrypqgvk ldqensrifl pklgwmryrn
      121 srqvtgvvkn vtvsqscgkw yisiqtesev stpvhpsasm vgldagvakl atlsdgtvfe
      181 pvnsfqknqk klarlqrqls rkvkfsnnwq kqkrkiqrlh scianirrdy lhkvtttvsk
      241 nhamiviedl kvsnmsksaa gtv
//
LOCUS       WP_181675276             733 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Paenilisteria rustica].
ACCESSION   WP_181675276
VERSION     WP_181675276.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=78856
     Region          4..733
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 meakrqdlnv fgmtcaacst rvekslnkav gveranvnlv tesaavyydp eqiapeqlia
       61 ivkhagydaa ekmskeekda vlekqfkrev rrfvlsaila lpllltmvth ipylhhtafa
      121 mgvdtiispt iqlilatviq fyigwrfydg aykslrgksa nmdvlvalgt saayfyslae
      181 yvrqlvnpni eahyyfetsa ilitlillgk llesyatskt tqsiagllkl qskeavvlre
      241 nqewkvpvde laigdvilvr pgekvpidav vltgetside smisgepvpm ekkagdavig
      301 stvnfdgafq arvtkrmdet vlstiiqlve eaqgvkapiq rladrisgif vpivlviavv
      361 tfviwmivtg gvldqslqva iavlviacpc alglatptai msgtgkgaes gilfkggehl
      421 ertakvdtvi fdktgtlteg klrvtnmlen hadfkqfaga meaqsehpia kavlmhlegv
      481 dtdevraeki rakaghgmvg vlngakvslg syrfiaqsvd iekeaddtmq qwmeagqtiv
      541 amsidgifag afglldtprk eakeailrlr elgvkttias gdqrvvveni aaelgiddvy
      601 aeqlpndksd lvaelqkqgh ivafvgdgin dapalatadt gisigtgtdi aietgdvtlv
      661 ghqltlvpqt iqlsratmrn irqnffwala yncagipiaa igllapwvag lamagssvsv
      721 vanalrlkrv klk
//
LOCUS       WP_181675129             175 aa            linear   BCT 28-DEC-2024
DEFINITION  YceD family protein [Paenilisteria rustica].
ACCESSION   WP_181675129
VERSION     WP_181675129.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..175
                     /product="YceD family protein"
                     /calculated_mol_wt=20136
     Region          1..174
                     /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 mkwsliqlqk yrgkkvpfeq eidvteylke hnhdvrsasl vkvsgnitvr qdsvlidlvl
       61 dgtfvlpcar tfedvlypyh iesvetyvnk eekvldethh mmdgdkidal pvieelllle
      121 ipmqvysdnv enalsegndw nviteeeleq qakqeetkvd prlagladff ekked
//
LOCUS       WP_181675189             466 aa            linear   BCT 28-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Paenilisteria rustica].
ACCESSION   WP_181675189
VERSION     WP_181675189.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 466)
  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 466)
  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 466)
  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 466)
  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 466)
  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..466
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..466
                     /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=53530
     Region          2..446
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mqleqelerf lgfrdfrvgq revvthvldg kdcfamlptg tgktvcyqls gylldgtvli
       61 vspllslmqd qvermrange krvvalnsfl slqekqrale dlsaykfifv spemlanrqi
      121 rmaiqrltig lfvvdeahci sqwghdfrpd ylelgtvree lgspvtlvlt atatkkvrad
      181 ikrqlrltac vdvihsvdrp nialdvqkld srlekqaqll kwtgllkgpg iiyfsskkla
      241 eryaygiaeq hglrtafyhg dmsgedrvti qqqfiqnqlh licatsafgm gidkgdiryv
      301 ihfhmpgdle aylqeigrag rdgarsiail lyadgdeaiq lqlqdrdlpe eelvhlspal
      361 teqlpvterr flefyrelgl tpnqikekiq frkrwkrenl ytflnfikgi tcrrqfvrhy
      421 feeeakqesv snccdicgvd hsdfegenvv ieeqqdwqky leyllk
//
LOCUS       WP_181675743             381 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Paenilisteria rustica].
ACCESSION   WP_181675743
VERSION     WP_181675743.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=44529
     Region          62..378
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpikkldtgn yrvtaslgfd pitgkhrrky isnvktkaea eqiyadlksk ytnnelptln
       61 kisfrelsrm yfsdytlnqk ptyirtqegy aknhlipffk ntnitkitst eirqfqkkli
      121 kkktlsnnsi nkhlillkki fdvaiekkyi vtnpcinikk lkvekqkmkf wtlsefktfi
      181 kaveddylkt kdeqpekfvf ivfyytqylt glragestal lwedntfekq efdinktesr
      241 ihgkvvttsp ktksgirhvs ynakykdili qwkeiqnnil nsygievtpq thifqysdki
      301 pdrdnfstkk inkictstdi tairlhdfrh shvallidnk eeltaikerm ghasitttid
      361 tyghlfpnkq ksmsdkidel f
//
LOCUS       WP_181675980             294 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenilisteria rustica].
ACCESSION   WP_181675980
VERSION     WP_181675980.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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]"
                     /calculated_mol_wt=33174
     Region          61..281
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mvyllgaviv vllgwiflik kqlratsaki kdiatrrgsn erltmdiasp eirqlllhvn
       61 elleakskte rqfqtlnkel retienvshd lrtpltslsg ylqlmdrdtl tpeerdkynl
      121 iikskiqtlt elvenffvls klssdegklq lesvnlsdfm teavasyyed fskkgmtpel
      181 siaseisvna drkalqrmvd nfisnmlkhg egpmqitltk rsgkatllfa nkasqltead
      241 vprlierfyt adrvrsgnnt glglaiidll akklgasfkv ewkeevltfi vifk
//
LOCUS       WP_181676022             322 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenilisteria
            rustica].
ACCESSION   WP_181676022
VERSION     WP_181676022.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=35766
     Region          1..311
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklgvftplf anlsldemld kvaaaglgav eigtggnpgn hhcptdella seearlaylk
       61 kfedrgliis afschdnpis pdpeearaad eilrksirla smmgvpvvnt fsgtagdsde
      121 akapnwpvap wptvysdikk wqweeklipy wkeigrlaee ydvkigielh ggflvhtpht
      181 llelrtatsp aiganldpsh lwwqgidpvg aikilgkega ihhfhakdty ldqdninryg
      241 lldmqpygdv qtrawtfrsv gcghsvkews dmmsalrtfg ydyvvsiehe dplmsidegf
      301 qravtnlqti lindepldmw wa
//
LOCUS       WP_181675425             739 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Paenilisteria rustica].
ACCESSION   WP_181675425
VERSION     WP_181675425.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 739)
  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 739)
  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 739)
  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 739)
  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 739)
  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..739
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..739
                     /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=85061
     Region          3..739
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 makeqnltad qviemashym neehlavvkk acdyareahk dqfrksgepy iihpiqvagi
       61 lvelemdpat vasgflhdvv edtpitlqdl eeafspeiam ivdgvtklgk ikyksheeqq
      121 aenhrkmfia maqdirvmlv kladrlhnmr tlkhlpvekq rrianetlei fapiahrlgi
      181 srvkweledt alrylnpqqy yrivhlmkqk reererylrd vidgvnenld elnikadisg
      241 rpkhiysiyr kmseqhkqfn eiydllavri lvdsikdcya vlgiihtrwk pmpgrfkdyi
      301 ampksnmyqs lhttvigpqg eplevqirtl emhqiaeygv aahwaykegk vinsktsfdn
      361 kmswfreiie yqnesenaee fmeslkldlf tdvvyvftpk gdvfelpngs vpldfayrih
      421 teignktiga kingkivtld yklktgdiie iltskhsygp srdwlklvqt sqaknkirqf
      481 fkrqakeenv ekgrdmveke lrqldfdpkk vmttenmnkl gerlnfshed dlfaavgyng
      541 italqvanrl tekerrirel eeqaemltnk ieakpkhttd snnerlkikh nagvvvqgvg
      601 nllirlsrcc npvpgdeivg yitkgrgisi hrkdcpnvtg pdterlidvd wedadmtakt
      661 dynvdievfg ynrngmlndi lqvvnsltsn ingvnakvdn nkmatlvltl qihninhlqr
      721 vvdkikqvpd vytvrrlmn
//
LOCUS       WP_181675591             353 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Paenilisteria rustica].
ACCESSION   WP_181675591
VERSION     WP_181675591.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=38388
     Region          5..353
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mtklakiqaa ledrnmeavl vtsdynrryv adftgttgma litpskaffv tdfryteqaa
       61 kqavgfeirq nkgpifetvq aiiaelgiqk lyfeeayvtv aehklmqsff saklepfsdl
      121 fedmrkvkta selsaiktac eiadeafthi ltfikpglte levsneleff mrrngasgss
      181 fdtivasglr salphgvasd kiievgdfvt mdygcyyngy csdmtrtiai gepsaklkei
      241 yavtleaqlk vidalkpgmt gieadaiard hiaskgygea fghslghgig leihegpnls
      301 mkspnvlvag nvvtdepgiy lpgvggvrie ddilitetgn evlthsskel iil
//
LOCUS       WP_181676100             712 aa            linear   BCT 28-DEC-2024
DEFINITION  PBP1A family penicillin-binding protein [Paenilisteria rustica].
ACCESSION   WP_181676100
VERSION     WP_181676100.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02074.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..712
                     /product="PBP1A family penicillin-binding protein"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /calculated_mol_wt=77856
     Region          28..665
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mnnenktilt ylksfflflk kwlgigwskf rrfwknkhig kfltligltc ilifivslvi
       61 vaksadidal kkgletttvi ydkdndkage lsasdatfvs ikdispnlqn avisiedkrf
      121 yehggfdlkg ifrsvwglas tgnitgggst itqqvaknal ltqdqtftrk akelfmarei
      181 ektytkdeil emylntsyfg nnewgvenaa kkyfgtsasd ltipqaatia gllqapsayd
      241 pythgdkavn rrnivlgamy tngkitkeqm keyqatklvl tdksndpdny hypwytdavi
      301 nealketdlt qddimkqgyq iyteldqnyq aalestfend slfpsnaadg tlvqggavlm
      361 dpesggvral vggrgkhvfr gfnratqmka qpgstmkpla tyvpaleegw kvddmlqdkk
      421 ttygkytptn vggvyrgevp mykavaksin apavwlldki glqkgidsvk rfgiqltked
      481 eylgltlggl nkgvspvela tayatfandg akpeshiirk ivdptgkvvy eneastkqii
      541 skkvstdmts mlidvinngg tgenagvsgy emagktgstq vpfttdgtkd qwfvgytpnl
      601 vgsvwigfdk tdeahylktt ssdgvaslah yvmksglkyq kpvdfgtksa sakteeknqe
      661 navteqagdf wgsikdsakg agetikkgad kakeiggqia dgfnnildsf gn
//
LOCUS       WP_181676085             167 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Paenilisteria
            rustica].
ACCESSION   WP_181676085
VERSION     WP_181676085.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 167)
  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..167
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..167
                     /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=19463
     Region          83..158
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mkyayitsgt ehylrqilsd nptrnitllq nfgdsillee ttestvfreg aayrinhsfg
       61 eikghgtvtf eylylrseei pifqklyqsv altlheargl qcmqllqskt enkyliitfw
      121 nsgddyqhwk tgrehnkimd lirsnssqsg fshvdvfhfp eyfhdek
//
LOCUS       WP_181676298             310 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenilisteria rustica].
ACCESSION   WP_181676298
VERSION     WP_181676298.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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   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 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
REFERENCE   4  (residues 1 to 310)
  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..310
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..310
                     /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=36379
     Region          27..272
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          191..271
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtnefelieh skvqdihvfl iemhyrsmhl hmdmevvyll sgslnivtnn nkislekgdf
       61 illnscqlhe lhsknsalll ifqfspkife affpqinevy fdtipialea setgrrllen
      121 ivaasqayfk eeehfsllch gfssiimfdl mklvphkqmk eekkdqlllk lerikrisdy
      181 iskhyqekll lsdiakkeal sftylshffh enfgvtfqey vnllrcekak yllihtentl
      241 lticgvcgfs dlrylnsafk rfygvspkyf rkqnqncqnq vnmlkqdvtn kqyvfsknqs
      301 lekinqlftl
//
LOCUS       WP_181676853              96 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Paenilisteria
            rustica].
ACCESSION   WP_181676853
VERSION     WP_181676853.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=11249
     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 milesallqv tlgdtkqfen dfataskfis sipgyishel hhcienptdy lllvrwetle
       61 dhtegfrkst ayeewkkllh hyynpfpkvk hftrii
//
LOCUS       WP_181676405             370 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR/zinc-dependent alcohol dehydrogenase-like family protein
            [Paenilisteria rustica].
ACCESSION   WP_181676405
VERSION     WP_181676405.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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 370)
  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 370)
  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 370)
  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..370
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..370
                     /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=40457
     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 mcqektgnvv lgkdipqkmk aivayapgdy rleevavpei gpheilvkve scgicagdlk
       61 afdgapsfwg dakqpayika pmipghefig hvvgygdqvt efelgnrvis eqivpcwdcr
      121 fckrgqywmc ekhdlygfqk nvnggmaeym kftkeainyl vpddlpieka iliepyacsf
      181 havqranikl gdvvvlagag tlglgmigai kksgpqkliv ldlfedrlel akkfgadmvl
      241 npakddviti ikdltdgygc diyieatgaq ksveqgltli rklgtfvefs vfkepvtvdw
      301 siisdrkeld vlgshlgpyc yplviegiqn gdlptegvvt htlpledfka gfdlvrsgae
      361 slkvvlnpnl
//
LOCUS       WP_181676521             204 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Paenilisteria rustica].
ACCESSION   WP_181676521
VERSION     WP_181676521.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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 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 10140399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..204
                     /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=23277
     Region          5..141
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04692"
                     /db_xref="CDD:467574"
ORIGIN      
        1 mveklkifnl ehqqigtasr ddvhhkglwh etfhcwfvse dltrifiqfr seqkkdfagl
       61 yditaaghlt edetvldgvr evkeelgvdv afdelvslgv iatsyvspgf vdrefchvfl
      121 ykfagnladf rlqeeevggm vtadlqefrs ffkgesdglr vegfklrdag veivnevlgt
      181 rqftleendy ygklvramel rnil
//
LOCUS       WP_181676893             358 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Paenilisteria rustica].
ACCESSION   WP_181676893
VERSION     WP_181676893.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..358
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..358
                     /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=39444
     Region          28..356
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mansnklkds fkkttyklsq hgprnasvlk eafeavdgdl esdiygdgav ienfqdkiaa
       61 flgketavff psgtmaqqaa lriwadekgn kkiayhplsh leiheqnalk elqsmeplll
      121 gtaerlltmd dirnlsepvs cilielpqre iggqlpsfae leeisaycrn ngirlhldga
      181 rlwevtpyyq ksekeicalf dsvyvsfykg lggiagaila ggedftaeak iwkrryggdl
      241 islypyivsa dyyfdkrigk mgeyyeaakd lahrfnacdg vrtvpevpvs nmfhvyfeks
      301 aeaiepilak ihaetgvgcs gylqekpgga cgfelsvgda vaeipvasld qvfeklge
//
LOCUS       WP_181676946             255 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenilisteria rustica].
ACCESSION   WP_181676946
VERSION     WP_181676946.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=27998
     Region          1..>197
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mkytvitgas sgigyetala faargknlvv varreseltq lkaeivkira dvdvqikiad
       61 ltvaenvygl yeelkdlele twinnagfgn fdlvgeqkls kiesmlhlni ealtilsslf
      121 vrdyadvdgs qlinissggg ytivpnavty catkfyvsaf teglshelka nnakmqakvl
      181 apaatetefa krardeetfe ykgavakyht gkemagflld lydsekvlgi vetdnyafql
      241 kdpqfnyatr aqtsk
//
LOCUS       WP_181676666             140 aa            linear   BCT 28-DEC-2024
DEFINITION  YbgC/FadM family acyl-CoA thioesterase [Paenilisteria rustica].
ACCESSION   WP_181676666
VERSION     WP_181676666.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Feng,Y. and Cronan,J.E.
  TITLE     A new member of the Escherichia coli fad regulon: transcriptional
            regulation of fadM (ybaW)
  JOURNAL   J Bacteriol 191 (20), 6320-6328 (2009)
   PUBMED   19684132
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Angelini,A., Cendron,L., Goncalves,S., Zanotti,G. and Terradot,L.
  TITLE     Structural and enzymatic characterization of HP0496, a YbgC
            thioesterase from Helicobacter pylori
  JOURNAL   Proteins 72 (4), 1212-1221 (2008)
   PUBMED   18338382
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00051.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..140
                     /product="YbgC/FadM family acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16369
     Region          4..137
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mkyhestivv ryaetdqmgi vyhanylvwm eigrtdfles iglryfdmeq egyispvldv
       61 hisykramky gqkavvktwi ksydgfrvvy gyeirqeggn dihisgeteh iavrkvdfkp
      121 vstrrtfptw heayleamks
//
LOCUS       WP_181677026             445 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Paenilisteria rustica].
ACCESSION   WP_181677026
VERSION     WP_181677026.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 445)
  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 445)
  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 445)
  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 445)
  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 445)
  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 445)
  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 445)
  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..445
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..445
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51344
     Region          1..442
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mfskitisnf fsihdqislt ldhsyspadi fnqntlytyy dnqkkrsiln gailyganas
       61 gktnllyafe fmrimiqksh tynektdfdi apnafkfsta kettsrftit ftepnfqenq
      121 diqytyelai dagtleiqee sltykkilkt tlskpiivfe rlksqipkks sqlkslftki
      181 eqenityksi lsmlihdink ayfsketasl aykiveslat evtkgfqtkq fdgnsleafa
      241 eqinkdsdfk keiletlydf dfaiqdfsvt dmtdnlvesi eqatfsddvk aqliattkkn
      301 rrfeistahi vddvtyplsm smesdgtkkf lessirlfda lqneilfisd efdnkyhtki
      361 qegllnkfih qendkkaqfl iashnpllln pdrfakeqvi fiqkdrktqa sevfslsefh
      421 eitydnhnwt nlyldgrfga vpevf
//
LOCUS       WP_181677206             249 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenilisteria rustica].
ACCESSION   WP_181677206
VERSION     WP_181677206.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..249
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..249
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28391
     Region          7..244
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 maifsthfas qslqlrtslq vfipdiidtd kpmrllyllh glsdddtawl tnsslvryae
       61 nrniaivmpq vhrsfytdmq tgnrywtfls eelprlvhsw fklptepent yvaglsmggy
      121 gafkwalhyp ekfagmasls galdivalre arpegeaemq atfgdieshr gsdndlltll
      181 gkitakprvl qlcgtedfly ennlgfkahi eqtdlpytyq espgehdwey wdreiqtvln
      241 widqkgdfa
//
LOCUS       WP_181677008             199 aa            linear   BCT 28-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Paenilisteria rustica].
ACCESSION   WP_181677008
VERSION     WP_181677008.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..199
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=22800
     Region          6..197
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 maagemtpkv deylgkakry kdefaelrri alecgvtedi kwknicfmse gknvflihgf
       61 keyfailfmk gvlfkdpngi liqqtpnvqs arqirftsle qvlemepvik aymeeaiave
      121 ksgaevefkk qeevgipeel qlkfdempaf keafegltpg rqrayilffa tpkqaktres
      181 rieknvdrim dgiglndrf
//
LOCUS       WP_181677268             219 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Paenilisteria rustica].
ACCESSION   WP_181677268
VERSION     WP_181677268.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=24393
     Region          <5..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 mkegfavigl grfggsicks lveqgmevla idsseervne fmsiathavi cnstdenalr
       61 qlgirnfehv ivsigediqs silttlilke mgvkyvtaka tndkhaklld kigadrvvhp
      121 erdmgrriah yivsknmldy lelsdeyslv eisvsnrrfl gkslheldfr ntygvnivgi
      181 krdkqmiitp eatdilessd vlivigsddd ierlqeqiq
//
LOCUS       WP_181677365             254 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Paenilisteria rustica].
ACCESSION   WP_181677365
VERSION     WP_181677365.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=29940
     Region          1..237
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mievficede vnqrselvkh venyimmenf dmelalstgd peellsyvqf ggegmglyfl
       61 dvdlkhprld glelaqkire ydprgfivfi tthaelsylt ftykveamdy iikddfdkvr
      121 nrifdcmksv eervgrerke vgkfftmktd ekvihelydd ilflstlksk arriilhgqe
      181 rqvefygtlk sledslderf ykthrafivn tdkivsvnyv sgiitmvnqe ecllstrsnr
      241 dfrdfirrrr gdid
//
LOCUS       WP_181677463             248 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenilisteria rustica].
ACCESSION   WP_181677463
VERSION     WP_181677463.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..248
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27762
     Region          1..246
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mkmkapepfl fetgkravll lhgftgssad vrmlgrflqd nnytcyapqy kghgvspdvl
       61 lttgpddwwq dvlaaydrlk slgyeeiava glslgglfsl klgynrpllg ivamstptrm
      121 dssspiiqgf ldyvrnykky egkspdvida emlaykdapm dtiaklkdei qdvipqidli
      181 yapmmvvqgk kdlmvdvnga eliynkvesd qkelkwyens ghvitidkek aqlqddilaf
      241 ldtldwhv
//
LOCUS       WP_181677467             247 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenilisteria rustica].
ACCESSION   WP_181677467
VERSION     WP_181677467.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 247)
  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 247)
  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 247)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..247
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..247
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27452
     Region          4..241
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mstdrsfllk agsravlllh gfagttedvr elgeylaeng ytvyapnyrg hgeepaiflk
       61 ttpemwyeda kagykhlqdq gyheiaivga amggvfalkm aetfdpkaia plcanvnrkm
      121 ryipvekyll ksmsregiad aeaevmlany apeiktmtda rsafykavas dierievptm
      181 igqgcqdeei saddanyifk nihsddkqlc fyagsghdit tdcekdilae dlvyflddlm
      241 wleevvv
//
LOCUS       WP_181677494             135 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Paenilisteria rustica].
ACCESSION   WP_181677494
VERSION     WP_181677494.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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 10140416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=15456
     Region          7..114
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd04699"
                     /db_xref="CDD:467579"
ORIGIN      
        1 mkpifpavka viihngqflv lkkagvegdv welpggrmnf getkgetlfr evqeetglqv
       61 qpfilydtwe ffqpeyqitg viylcekpdg dvrlssehqa yewfpldass lermdvvfas
      121 rmvrwdfeai kgfms
//
LOCUS       WP_181677550             303 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenilisteria rustica].
ACCESSION   WP_181677550
VERSION     WP_181677550.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
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 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     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=34650
     Region          1..89
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mqldiskdsi hvyealasdt riqilnllsq ssmnikelah alhmssaiit rhinqlehak
       61 lirtekipgk sgiqkisklv vdkieitfpt tiypnfkmrs lelpvghytd ynvtptcgla
      121 sskdfighvd epkyfmdarr meaqiiwftq gyleykvpnp lqkeeqiell eisfeiasef
      181 pysnnvwpsd isfylnghtl gtwtcpgnfs dirgkytpsw wedsnsqygl fktiriskhg
      241 thfdgeilse ltlddldite elltfriave kdakniggtt ifgkgfgnhq kdmefkfyys
      301 ekc
//
LOCUS       WP_181677687             232 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-protein kinase family protein [Paenilisteria rustica].
ACCESSION   WP_181677687
VERSION     WP_181677687.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..232
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..232
                     /product="tyrosine-protein kinase family protein"
                     /calculated_mol_wt=26073
     Region          <40..232
                     /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 mlikrkeknt iitdgnemtm qknsvayekf ssiqtniqfm erkagsvqti avtsankgeg
       61 ksffitnyan tsalykqktl lidvdfynpk iskqyksklm pglsnvlvdm iafeeavipl
      121 enkylsflpi gtlppnplel lrsdefktll tklkeefdvi lldcppinlf tdarvvaaes
      181 dgtillvnsq ttseedvrks kslldqvdan ilgavlnnkr ynqkqmasyn yy
//
LOCUS       WP_181677724             867 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-mannosidase [Paenilisteria rustica].
ACCESSION   WP_181677724
VERSION     WP_181677724.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..867
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..867
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=98128
     Region          1..865
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mvkahivnht hwdrewyfts tdalvlseql ftevieelka hpeanfvldg qlsilddyva
       61 lypekmddik qliaakqlfi gpwftqtdaf fahgesilrn amigifdskk ygdymkigyl
      121 pdtfgfnaqm ptllaqagfd niifwrgihl geqvqstyfk wsglgdaaqi yainmpqgyg
      181 tgmlleptta yvdgrldpai dfiakysetq evlipsgndq lniitnfaek laeinkmgrh
      241 syelstyqdf idyvktlpdl eeyrgefrsp vlarvhktig ssrmniklks aeleqklltr
      301 iepllviaka sgipiserll mhtwkklleg qahdslagcv sdpvaddimh rmkeadelcd
      361 sientivkki addleleane ilvfntelat fdsykevqvi tknkhihfpe cpdamivqse
      421 yiesredvle etpagnrfik epgyyvlqvr mkielpglgy rvltfedset aleemkpvtd
      481 asisnpfyki tfedgtihle tatgdkqpaf ieledaanag dtydysplan dvprdfqftk
      541 viteksrqve rliltgvham pfdledrlip dgkqaellvk mtlelsrdsa llhcklkvnn
      601 qinshrlrlk intgvktdtn iaslpfgyie rkpgvpanwq dtysempvdi epleqsvtlt
      661 sktksctift rgikeyqqsg dqlaltllat tgqlgkpnla yrpgrasgdt tkkghvlipt
      721 egaqligdht fslaiylgaq gfnehetaqr srefnqttvs yqrqsynyfl hrldnkiqkt
      781 erkrglqrtl qlsdmpksyl isacypsyye sdkyiirien ptrtpqtidp thltkgsvtl
      841 vnaleepitn qdftipayda itirlpf
//
LOCUS       WP_181677799             306 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenilisteria rustica].
ACCESSION   WP_181677799
VERSION     WP_181677799.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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 306)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 306)
  AUTHORS   Rosinski,J.A. 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 306)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..306
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..306
                     /product="helix-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=35041
     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 mkierligii mlllqrelvs aaemasmfev tkrtiyrdvd tlsmanipvy tmpgvkggig
       61 imptykvdkk lltvedltai itglsgfeql lssadikktl qkmknmlghe nelpassisl
      121 dfsnlamkqe fnenverlhl aikkqqfval tyidrdgnqt irrvepyhll frnrswylqg
      181 yslerqdfrt fklsrviele vaaetfearp filkpfrast tttpfqmkea rliidkiare
      241 qialrfgvtt iepldesyfs akvtlpnhev gyrfllnlgt hvtvckpgef ydgfvaylqe
      301 iqckyd
//
LOCUS       WP_181677852             463 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Paenilisteria
            rustica].
ACCESSION   WP_181677852
VERSION     WP_181677852.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 463)
  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 463)
  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 463)
  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..463
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..463
                     /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=53243
     Region          127..263
                     /region_name="SIR2_2"
                     /note="SIR2-like domain; pfam13289"
                     /db_xref="CDD:433090"
ORIGIN      
        1 mmdqidkkev fqeifkacdy gnlgmfvgag fskavigesa lgwlgiidea rkkfelkalt
       61 deelkgaslp elatqtckki aenensdyse akqrfkaeis nisnwlpsie ageefekwfd
      121 smkpawvitt nydavmehil tgksisispk kyfsapknvi piyhlhgtrq epetivvtqe
      181 dyvsllrpnd yrqtklamti restvlvlgy slgdinvlsa idwsknigsg didyphgviq
      241 ilriekpnip keyayrdene niileiddls sffkqlteyi ndkqveaaln skiledlaer
      301 lskdnedfme sfinsedtrr illqalwqse ylmiipyiqf lnncldkvwe gtyvkdafym
      361 yekyldiild ilifypyekm ppklfqitmd aldkvlryvd ksasdrtpgn swsanacwhr
      421 rkkdipeatr tqifqyaekn qlrtlnqlid stvkedisvg ate
//
LOCUS       WP_181677694             170 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase [Paenilisteria rustica].
ACCESSION   WP_181677694
VERSION     WP_181677694.1
KEYWORDS    RefSeq.
SOURCE      Paenilisteria rustica
  ORGANISM  Paenilisteria rustica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Paenilisteria.
REFERENCE   1  (residues 1 to 170)
  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..170
                     /organism="Paenilisteria rustica"
                     /db_xref="taxon:2713503"
     Protein         1..170
                     /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=18352
     Region          36..168
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mlakltfsll nvfpmpnrlv lgrvvrhlkn qmaryffgsc aknsnlrpkl klrhpknihi
       61 gkrssigdna riiatapvhi gddvlmapdv viltdthcin gkekildsgt tqkpvfignd
      121 vwigtrvtil agaeipdgci vaagavvpak kyppysvigg vpakvikqer
//
LOCUS       WP_181678115            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181678115
VERSION     WP_181678115.1
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=166337
     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 kgsmahtgtv 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 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_181678063             169 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_181678063
VERSION     WP_181678063.1
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 carboxy 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          2..>169
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdikvkt akpkdkpykl adgggmylli ntngskywrm kyrfagkekm lsigvypdvt
       61 ladarekrse arkllaaggd pgeakkeeki aqqmslqntf eaiarewhqs kadrwslryr
      121 deiidtfekd ifpyigkrpi aeikpmelle alrkmekrga lekmrkvrq
//
LOCUS       WP_181678498             362 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Escherichia coli].
ACCESSION   WP_181678498
VERSION     WP_181678498.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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 10543770
            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="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          78..220
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
     Site            83..90
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(84..91,156,203)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            152..157
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            219
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mspqnnhlqr ppaavlyade laklkqndna pcppgwqlsl paarafilgd saqnisrkvv
       61 ispsaverml vtlatgrglm lvgepgtaks llsellatai sgdagltiqg gasttedqik
      121 ygwnyallin hgpstealvp aplyqgmrdg kivrfeeitr tplevqdcll gmlsdrvmtv
      181 peltgeasql yaregfniia tantrdrgvn emsaalkrrf vfetvfpimd faqelelvas
      241 asarllahsg iphkvpdavl ellvrtfrdl rangekktsm dtltaimsta eavnvahavg
      301 vrawflanra gepadlvdci agtivkdnee drarlrryfe qrvathkeah wqayyqarhr
      361 lp
//
LOCUS       WP_181678781             401 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia coli].
ACCESSION   WP_181678781
VERSION     WP_181678781.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia coli"
                     /db_xref="taxon:562"
     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=45239
     Region          5..394
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mskpaltaka ieaaqpqdkp ykltdsltpg lfllihpngs kywrfrywid kkerlqaigv
       61 yplislkear kraaesrlli aqgidpmeea rkekaidaln maasfktvae dwlatrvsgw
      121 senytkqvrs alekdvypml gkrsivdita rdvlallqkk ertapeqark lrqrigeifk
      181 favitelvnr npvadldtal karrpghnaw iqiseipafy kaleragsvq iqtairllil
      241 talrtaelrl mrwewvdles atitlpaevm karrphvvpl srqavellqd qftrsgysaf
      301 vfpgrfmdkp lsasailkal erigyksiat ghgwrttfst alnessrynp dwieiqlahv
      361 pkgiravynq aaylkqrram mqdyasaids ilagdgnple p
//
LOCUS       WP_181678802             707 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF2345 domain-containing protein [Escherichia coli].
ACCESSION   WP_181678802
VERSION     WP_181678802.1
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 10008437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..707
                     /product="DUF2345 domain-containing protein"
                     /calculated_mol_wt=78436
     Region          3..702
                     /region_name="COG4253"
                     /note="Uncharacterized conserved protein, DUF2345 family
                     [Function unknown]"
                     /db_xref="CDD:443395"
ORIGIN      
        1 mgiqnfdhsh hklkirgqqs pvdvltfegr eqlstpfryd iqftstdkai tpelvlmqdg
       61 afsltappvq gmpvqaplrt lygvitgfkh lsssqdeary evrleprmal larsrqnaiy
      121 qnltvpqive kilrerhqmr gqdfvfnlks eypareqvmq ygeddltfvs rllsevgiwf
      181 rfatdarlki eviefyddqs gyergltlpl rhpsglhdga teavwglnta yrvveksvst
      241 rdynyrtata emmteqhdat ggdnttygea yhyadnflqk gdneaaesga fyarirhery
      301 lneqailkgl stssllmpgl agtevsiafe egnpdrpyia gvkhdsahtd hvtiqnykrn
      361 vlrtpannki rlddergkeh ikvsteyggk sqlnlghlvd agkqqrgegf elrtdmwgav
      421 rakkgifisa daqdkaqgqv remadiisel nglsdkiqkl sddatmanad padmaaqial
      481 itsrindlta pvilmhapkg vavasgehlq laavknlqin agnnadigvv knmfigvgra
      541 lsvfvrkagi kliankgavs vqaqhdlmel lakksieivs tedeirisak kkitingggs
      601 yiriegsgie pgtpgdynvk avhygrqpga klkqemmafp miesgefntr ffftddndip
      661 yantkyiarl pdgttkdgit sddgrseiff sdkdgeilih lfveqdk
//
LOCUS       WP_181679238             262 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Escherichia coli].
ACCESSION   WP_181679238
VERSION     WP_181679238.1
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=28720
     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 lillpltaas nplipimktl ftdvtgtvpd aeeiahkael frqqtgiapf
       61 ivvlpdinne aslrqngkam lahassslsd vkgsvlllft treprlimit ngqvesgldd
      121 khlgllienh tlaylnadlw yqginnalav lqaqilkqst ppltyyphpg qqhenappgs
      181 tntlgfiawa atfilfsrif yyttrfiyal kfavamtian mgyqalclyi dnsfaitris
      241 plwagligvc tfiaalllts kr
//
LOCUS       WP_181679075             269 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Candidatus
            Protochlamydia amoebophila].
ACCESSION   WP_181679075
VERSION     WP_181679075.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Protochlamydia amoebophila
  ORGANISM  Candidatus Protochlamydia amoebophila
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia;
            Parachlamydiales; Parachlamydiaceae; Candidatus Protochlamydia.
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="Candidatus Protochlamydia amoebophila"
                     /db_xref="taxon:362787"
     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=29474
     Region          1..239
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mkqrlvlitg atagigqalv hlaaqkelkl litgrnqeel kkltdtfgsl ivqavaadls
       61 qeegvktiid lihkhcpdii innagfglyg ealsystvqq khivdvnvna vlqlslegar
      121 alisqvkqgv ilnvssaisf qvapnmavya atkafinqfs qsldeelkpl girvlvacpg
      181 mvktefsqna gmtrtrkfta vmsskfvara iwkqiesltp ltiidwkyrl ltwlsylipk
      241 kivtaiiknn iakriaprnv irlpscknk
//
LOCUS       WP_181679431             701 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Escherichia coli].
ACCESSION   WP_181679431
VERSION     WP_181679431.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 701)
  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 701)
  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..701
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..701
                     /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=80602
     Region          122..>452
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mlrkskltei ykrfgfteen tgnesiavys iktghyhnad ilplnnevnv nqtfeeyrql
       61 gyacqikkyq syeeahkelf ngffsvdstk erlikdyntf tdsivkihsp tatysyinsk
      121 yylngvigea nvvteileri qhrrpilfli eaaagfgktc tayellreii vnnigkiplf
      181 selsrnrqak ifryvlldei drsfpllssa lvrneiragn vpvildgfde llhestngie
      241 nnyektepml etiselltds akvvlttrrt aifdgdefhq wiashqedfd viririhepq
      301 iedwlpgqrl deisstgfpl nklsnpvlls flrciddtdf nkvisdptti vrkyfdsmle
      361 rerkrqdllm siedqytilk iiaddmvegn ytsesreyis lviteknqql leatrklytv
      421 derpttdelv nklashalld rsgsenqgig fvnefvlgnf vseniindks newigdkrfi
      481 epavqsympr iddekellwh slefalyfms gndkilyshl ligkvpldlk ndsvellsis
      541 klslgdinii hdtifvdcsf fssiftcgny knvtfvncsf idcsfnelsg rediyflgce
      601 cdndainkks veinsendhd itdcdiyile kfcprgsvsy hkhrpikglc snnnqfqlse
      661 ilhsldklrk dgllltpdkr sflelnmari seikailgrn f
//
LOCUS       WP_181679977             143 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Xanthomonas oryzae].
ACCESSION   WP_181679977
VERSION     WP_181679977.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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 both ends.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..>143
                     /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          <3..143
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 qahavrlddg qvlsgpvlva sgvslpqllp elalrprkgh lvitdrhpgl irhqllelgy
       61 adsahgaddt svafnvqprp tgqmligssr qfgehdrals mpvlqqmlqr afaylpvlre
      121 lqairvwtgl rpatpdgrpy lga
//
LOCUS       WP_181680266             207 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Escherichia coli].
ACCESSION   WP_181680266
VERSION     WP_181680266.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 207)
  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 207)
  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..207
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..207
                     /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=23181
     Region          3..201
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mslaarfkar rlelgmtqve vansagvsqq siesiesgrt rkprnlldla kalkcspdwl
       61 lngknimpla eistrripil syvqagelte arditdltge feyiladsdi petcfalrid
      121 gdsmqpefke gdiviidpdl ypapgefvva kndgheatfk kyrplgigid dfeliplnpd
      181 ypifrsadmn lqiigvmieh riyrrkr
//
LOCUS       WP_181680287             225 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181680287
VERSION     WP_181680287.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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 225)
  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..225
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>225
                     /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..>225
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkrlqafkfq lrpggqqere mrrfagacrf vfnralalqn enheagnkyi pygkmaswlv
       61 ewknatetqw lkdspsqplq qslkgleray knffrkraaf prfkkrgqnd afrypqgvkl
      121 dqensriflp klgwmryrns rqvtgvvknv tvsqscgkwy isiqtesevs tpvhpsasmv
      181 gldagvakla tlsdgtvfep vnsfqknqkt larlqrqlsr rvkfs
//
LOCUS       WP_181680288             183 aa            linear   BCT 28-DEC-2024
DEFINITION  YagU family protein [Escherichia coli].
ACCESSION   WP_181680288
VERSION     WP_181680288.1
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=20648
     Region          6..181
                     /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 inpvmvthii fslvfaigyc vvaeifpkvk lwqgilagli
      121 vtvtvhgifc palnltpplt qlpfdeyase ilghifwfwi ieimrrdlrn rithepdpev
      181 air
//
LOCUS       WP_181679268             300 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Escherichia coli].
ACCESSION   WP_181679268
VERSION     WP_181679268.1
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=34369
     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 rlsdgvlgqc snadlrhftr ilgieglfpr wddrllsill gntknnpfli kqrpyencgs
      121 fmsilnvlsd ailsqkkvnf nykdkefrav epyrlvndng lwylaaahds tlksfvissv
      181 kdvcmsnisf riipeineki ektdsiwyse dlievlisvs ahvapwfthr hllpgqeiih
      241 tsrsgdllvi srvthtdqim plmkywipdv eviqpasirq qlaediqsal krytqpsnap
//
LOCUS       WP_181680537             410 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Citrobacter sp. RHB25-C09].
ACCESSION   WP_181680537
VERSION     WP_181680537.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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 410)
  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 410)
  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 410)
  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 410)
  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..410
                     /organism="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     Protein         1..410
                     /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=46312
     Region          145..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 msihcltald lltfpvwivs pgteelifan ntakqlmqey tfsqlqkgmf sthaqdelan
       61 yitdlrhhrd iveiltvtln sthsalscrl svkelaefge vilfegiett ttqglkasrs
      121 tnyqrkkqgf yarffltnsa pmllidpsre glivdanlaa lnfygyrhdv mcqkhtwein
      181 mlgrqilpim heiarlpggh kplnfihkia dgttrhvqty agpieiygdr lmlciihdit
      241 eqkrleqele haalhdaltg llnrrqfyql tepgqthplt maqdysllli dtdrfksind
      301 lyghlkgdev lcalardlee sarkgdlvfr wggeefvfll prtpldvalq faesvrasva
      361 kisipglprf tvsigvahhe snesidelfk rvdaalyrak ndgrnrvlaa
//
LOCUS       WP_181679981             440 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181679981
VERSION     WP_181679981.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..440
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          6..193
                     /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          154..>254
                     /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 mtgsygaari rrlnletgqw qtlnypaqag dfdyaprysp dghwivflrn pqlgdlwrip
       61 aeggaaerlt hdtadiwgws wlpdgsgvif grrvdiearl yrldlldssl hdlgvddaqa
      121 pdvahghlvf aqrkpqfgvy qvirdtmngg yirrrlfsss grddqpmiap dgrqlvfasn
      181 rsgtyglwwg dvskpgsvrl ieglrpdsrq aadwsadsqr llvsgsdaag haalfevtps
      241 sgkvvrlpvp qprplqaihl pdpdqvlvla aaddghtfat lydrrsspwr alatlqdvsq
      301 vrldrisgqv lltrlsgggv wqvapslaad tlqaidskqp srwryrswap gahgdlhyls
      361 stdtcstydg elrsvggqcl davkftaing fsvdqhdgal yvalaeedgs siaymplpqr
      421 svasicvlan llsilrkias
//
LOCUS       WP_181680867             254 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Citrobacter
            sp. RHB25-C09].
ACCESSION   WP_181680867
VERSION     WP_181680867.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 254)
  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..254
                     /organism="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     Protein         1..254
                     /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=28431
     Region          34..127
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 miktlprlll ltfliasrya laatsteikq pqapvtaitp invspgdsds avnawnsrta
       61 sltkapgfis atlyqsvlpg spwplieivq wqsyttwtka hdnpgrnslt gfyrpavayf
      121 nlaarhesql peallnrvkk dpafshpesp fvfinlmema pedattfiad wkirsqltrq
      181 qagsmnatly ravlpderys iinvsqwqsy nafvdaqndp tysrqlqnnl nqtssiklir
      241 gffrpvayqi qtyd
//
LOCUS       WP_181681057             328 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Citrobacter sp. RHB25-C09].
ACCESSION   WP_181681057
VERSION     WP_181681057.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     Protein         1..328
                     /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=35719
     Region          1..326
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mtktnlitgf lgsgkttsil hllahkdpae kwavlvnefg evgidgalla dsgallkeip
       61 ggcmccvngl pmqvglntll rqgkpdrlli eptglghpkq ildlltapvy epwidlratl
      121 cildprllld eksvanenfr dqlaaadvii anktdratae sdqalqdwwq hnggdrqlvh
      181 adhgqidgql ldlprlnlae lpasaahshs hpqksglaal nlptqqrwrr slnsgqghqa
      241 cgwifdadtv fdtigllewa rlapvgrvkg vmriaeglvr inrqgddlhi etqnvsppds
      301 rielisnset dwnalqsall klrlaeha
//
LOCUS       WP_181681235             284 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Citrobacter sp.
            RHB25-C09].
ACCESSION   WP_181681235
VERSION     WP_181681235.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            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 13303747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     Protein         1..284
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=32344
     Region          <47..279
                     /region_name="PRK13500"
                     /note="HTH-type transcriptional activator RhaR"
                     /db_xref="CDD:184091"
     Region          197..279
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkesglpadq qffadlfsgl vlnpqrlgrv wfatqpatlp ggslcldlpr ldivlrgeyg
       61 nqleksqhrl aegemlfipa rsanlpmsdk plmllslvfa pawlglsfyd nrtasllrpv
      121 rrielshpqr gegeamltal thlsrspqeq aiiqplvlsl lhlcrsvvnt rpdtqrprae
      181 flyhsicnwv qdnyaqplsr esvatffnit pnhlsklftq ngtmsfveyv rwvrmakari
      241 ilqkyhlsis evaqrcgyqd sdyfcrlfrr qfgltpgeys arfq
//
LOCUS       WP_181681750             483 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Citrobacter sp.
            RHB25-C09].
ACCESSION   WP_181681750
VERSION     WP_181681750.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     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=52815
     Region          2..479
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mmvdwlfknv tvidgsggpq yrgdvavagd rivdiapsln vdaaqiinga gqvlapgfid
       61 vhthddinvi rmpeylpkms qgittvivgn cgisaaaatm kgavpdpmnl lgeaqhfiyp
      121 tveayaqave aarpalnvgt lightalrnn hmdnlfrpat vseitamrnd lrealkqgal
      181 gmssglayat afestteevm alaeelseaq gvytthlrse fepilealde afrigrhaqv
      241 pvvvshhkca gaknwgrtke tlaffdkmra qqeigcdcyp ysassstldl kqvtdefdiv
      301 itwsephpdq agkklqqiad dwqmsmleaa kllmpagaiy ynmdeqdvrr vlsypvtmig
      361 sdglpndpmp hprlwgafpr vlghycrder lfpltmaihk mtglsaarfq lpergliktg
      421 yyadlvlldp qtvrdvasfs dpqqpadgin avmvngvmsy grdkhiigra grflrrqsqs
      481 gke
//
LOCUS       WP_181681665             237 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Citrobacter sp. RHB25-C09].
ACCESSION   WP_181681665
VERSION     WP_181681665.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     Protein         1..237
                     /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=26739
     Region          18..146
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtthapftds ydsdflrdtm mgpnamrite emaatlpitp gmrildlgcg kgissillae
       61 kydatvfaad lwisptenae rfaqlgleek ivpllvdvtq tipfahnyfd miisidayqy
      121 fggnetmlst llpfvkkggf isvavpgfik dyspenlpev vksfwtpewy fypcnwwktl
      181 wekeagielt vvremdscql swdefmttkl aqemmvpvme agagayfnmi qlvgrkr
//
LOCUS       WP_181681680             269 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Citrobacter sp.
            RHB25-C09].
ACCESSION   WP_181681680
VERSION     WP_181681680.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     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=30518
     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 mennnsvynf yeshfdeanr cagnplefir sqeiiqrflt pspmliadia gangfysfwl
       61 aeqghqvhll dlsdkhieqa rqrgqqsavt lqsyncgdar qlpwdgntfd vvllmgalyh
      121 lqessdrmqc ikeclrvlkp ggmaifsyis rlaslvdgyk yqfiddpmfq rivetdlqtg
      181 nhenpegkpd yfttaffhtp pliiqelqqs gfqdirlfav egfasiidtd eimrvedkka
      241 lllkhlrlte elpellgiss hllavakka
//
LOCUS       WP_181681786             418 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Citrobacter sp. RHB25-C09].
ACCESSION   WP_181681786
VERSION     WP_181681786.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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 sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     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=47955
     Region          2..406
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdikvrt akpmdkqfkl tdgngmhllv hpngsrywrl qyryggkqkm lalgvypdvs
       61 ladararrdd arkllangid pgdkkkndki eqeeartfeq laiewhatnk kwseehsrrv
      121 lkslednlfp aigkrniael ktrdllapik avelsgrlev asrlqqrtta imryavqsgl
      181 ldynpaqemv gavassnrqh rpalqlkrip ellrridsyt grpltrlave ltllvfirss
      241 elrfarwsei dfetsmwtip aereaiegvk hsqrgskmrt phlvplshqa iailkdvykl
      301 sgdrdfvfig dhdhrkpmse ntvnkalrvm gydtkvevcg hgfrtmacss liesglwsrd
      361 averqmshme rnsvraayih kaehlderrl mlqwwadfld anrekaespf dfaklsme
//
LOCUS       WP_181681847              94 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Citrobacter sp.
            RHB25-C09].
ACCESSION   WP_181681847
VERSION     WP_181681847.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     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=10883
     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 msyelefdpr alkewqklgd nvknqfkkkl aevlinprie sarlhglpdc ykitlkslgy
       61 rlvyrvqdev vtvfviatgk reksavyqia dkrr
//
LOCUS       WP_181681851             636 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator [Citrobacter sp.
            RHB25-C09].
ACCESSION   WP_181681851
VERSION     WP_181681851.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     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=72687
     Region          14..608
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mrfpnqrlaq lfsmlqnetl pqdelaqrls vstrtvradi talnallneh gaqfilsrgn
       61 gyqlriddha sfktlqtqqp aalriprtsq ervhylmvrf ltsafslkle dladewfvsr
      121 atlqndmaev rewlqryhlt letrprhgmk lfgsemaira cltdllwtlt qqdpahplvt
      181 eealyagips qlqpvledif trfhirltde gdlflrlyca vavrrisegy plsdftteev
      241 eenvslaare iagvvqhlae hplsvseenw lkvhiaarqv qevapsaina ddeealvnyi
      301 lrfintqyny nllndqqlha dllthiktmi trvryqimip npllenikqh ypmawdmtla
      361 avsswgkytp yaineneigf lvlhigvgle rsynigyqrq pkvllvcdag namvrmieav
      421 larkypqiei vrtltlrdye qresiaedfv istariaekd kpvvqiapfp tdyqleqigk
      481 lvlvdrtrpw mlnkyfdath fliindamdq qtlfktlcdq lqregfvgse fldsvverea
      541 ivstmlgdsi alphalglla kktvvytvla pqgiawgdet ahvifllais kseyeeamai
      601 ydifvtflre ramtrlcasq nfaefktvam ecvsrf
//
LOCUS       WP_181682066             257 aa            linear   BCT 28-DEC-2024
DEFINITION  dimethyl sulfoxide reductase anchor subunit family protein
            [Citrobacter sp. RHB25-C09].
ACCESSION   WP_181682066
VERSION     WP_181682066.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            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 10007172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     Protein         1..257
                     /product="dimethyl sulfoxide reductase anchor subunit
                     family protein"
                     /calculated_mol_wt=26813
     Region          3..252
                     /region_name="DmsC"
                     /note="DMSO reductase anchor subunit DmsC [Energy
                     production and conversion]; COG3302"
                     /db_xref="CDD:442531"
ORIGIN      
        1 mhelplvfft vftqsavgaf vllliggtlg qiearrmavg lfcamclfgi gvvlgifhvg
       61 qplralnmll rvghspmsne ialsaafaal gglgslglli srgtnglcka lvwlaaavgv
      121 vfilaipqiy qlptvvtwrs syttvmmilt aligggmlaa lfglrlgllv svlailvsfc
      181 lrsgyistlm sadgvltaaq tnwftaqaal lalgivgvvi wvrlkanpai lavtavavia
      241 aelvgriafy nlwtlpm
//
LOCUS       WP_181682554             249 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Citrobacter sp.
            RHB25-C09].
ACCESSION   WP_181682554
VERSION     WP_181682554.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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 sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     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=27305
     Region          4..248
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqrkimvvta aygydtvrna ggqtamlpvi agagadgvei rremftdael salptlasai
       61 eifdllacys apqplfleng tlnpqlpall qeaqtlralw lkvslghfid atpfdtlrdw
      121 lessgmalvv endqtpcgrl epmqrfnaac qqqalpislt fdmgnwlwvg dspeesarql
      181 sssvgyvhvk aatahndsyr avppdradpr wlellehlpg dvprgiefpl egadltavtr
      241 ryvellrke
//
LOCUS       WP_181682773             197 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Citrobacter sp. RHB25-C09].
ACCESSION   WP_181682773
VERSION     WP_181682773.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     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=21200
     Region          4..185
                     /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 mtslylasgs prrqelltql gvsfervvtg ieetrgeges aqqyvsrlar ekalagvaqt
       61 prdlpvlgad tivilngevl ekprdaqhaa lmlhklsgqt hqvmtavala dsqyvldclv
      121 vtdvtfralt dadiadyias gepmdkagay giqgqggcfv rkingsyhav vglplvetye
      181 llsnfnslre krdkhdg
//
LOCUS       WP_181682736             160 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Citrobacter sp. RHB25-C09].
ACCESSION   WP_181682736
VERSION     WP_181682736.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 160)
  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 160)
  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..160
                     /organism="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     Protein         1..160
                     /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=17121
     Region          <3..146
                     /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 mvaalpflal yiflsialav ydlrsgllpd rftcpllwag lvyqqcifpg hlsdalwgav
       61 agyggfafly wsyriirkke glgygdvkfl aalgawhgwi alpllvfcaa llatmgvavm
      121 aitrgtailk nplpfgpfla aagfitgihn lvsgtinwsl
//
LOCUS       WP_181682970             385 aa            linear   BCT 28-DEC-2024
DEFINITION  CdaR family transcriptional regulator [Citrobacter sp. RHB25-C09].
ACCESSION   WP_181682970
VERSION     WP_181682970.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..385
                     /organism="Citrobacter sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     Protein         1..385
                     /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=43836
     Region          3..131
                     /region_name="Diacid_rec"
                     /note="Putative sugar diacid recognition; pfam05651"
                     /db_xref="CDD:461704"
     Region          77..371
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mlispelant ivkramdiih hnvnvidhqg iiiasgenhr igerhevace viknrqrmti
       61 etpqqaakyq nvqpginhpi ivddrvalvi gisgnpvaig ryaelailta ellvkqllei
      121 reinwqyrir dllikqfieq ddtkrkkdil lqlqqqnicl daayipilin ietggnllgk
      181 tidhilneis kilqsqnvil lshneilllv sepkrsdliv dkinafletq lshytiaigv
      241 estepeafrr svfmlkemqs qakslcsdqr ivngkqlafd gllneakssh ftlyyqhqln
      301 kiltsnsgkt lfktlstyin nnaevnatsq nlgihrntln yrlhqikeit aldpfmfkdl
      361 cqltialhyy qdreciaetd irhyl
//
LOCUS       WP_181683245              88 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Enterobacteriaceae].
ACCESSION   WP_181683245
VERSION     WP_181683245.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=9588
     Region          24..83
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mhtafsssss apaaplmpvs dvvqerfirl pevihlcgls rstiydlisr eafpkqislg
       61 gknvawaqse itawmaeria ernrgfda
//
LOCUS       WP_181683278             692 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Citrobacter sp. RHB25-C09].
ACCESSION   WP_181683278
VERSION     WP_181683278.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. RHB25-C09
  ORGANISM  Citrobacter sp. RHB25-C09
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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 sp. RHB25-C09"
                     /db_xref="taxon:2742624"
     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=75766
     Region          139..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 llswlafall pswsldygll estsdeilda ygwshfnisw
       61 lwyllpslll irpfhearre qrtrhtldag waflcmafiv isatvegrgl gyativlfva
      121 lgaimtlalt rlewlggdrf vigslvtiva ligvfivwps vaifipmftt sagefaplsf
      181 mtvlsqahii qviinsivls iavgvgctff glvlaiyttr iarrsaiigr ifsilpivtp
      241 pfvvglgvtl mmgrsgyvte lmvdwfgltn tnwlygftgi wlaqvlaftp mafmildgai
      301 ktihpsleea sytlrasrwq tfngvfvpll kpalanafli vivqsladfs nplvlggnfd
      361 vlatqiyfyi tgsqldyqaa stlgaflllf sllvfciqym wigkrsyvtv sgksyrgdvq
      421 plpvtlvwsv vailavwiaf nallygsify gsftvnwgvd ytltldnfik lfgqgmsdga
      481 wpslldtlly agiaapitaa fglliawivv rqqfkgkkti efttmlcfav pgtvagvsyi
      541 ltfnsapvyl tgtaaiviis mvmrnvpvgi ragiaglgqi dksldeasls lragslrtit
      601 hillpllrpa ilsaliysfv raittvsaiv flvtpdtrva tayilnrved geygvaiayg
      661 silivvmlai ififdwlige arisrskakn qa
//
LOCUS       WP_181686559             174 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome, partial [Xanthomonas oryzae].
ACCESSION   WP_181686559
VERSION     WP_181686559.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     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]"
     Region          51..138
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mrharvlvla alavpviaav afaqsavtpi pdpppvrlap levdlakttw gdakagqtka
       61 tacaachgpd gnpavamypr iagqteryva hqvaliasge rntgmsavmv pfvkdltaqd
      121 mrdlgayfat qkasagvadd aaiaegpyqg mkfyevgekl yrggdtargv pacm
//
LOCUS       WP_181687607             148 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181687607
VERSION     WP_181687607.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 148)
  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 148)
  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 148)
  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 148)
  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 148)
  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..148
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>148
                     /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..>134
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 msasyvsagr teqgnvrrrn edaillrddl glwavadglg ghsagdlasr mvvdalgalr
       61 rdgdlarfvd aidaqlnqvn rqlralarar rvdviastvv vlvhdhellm cgwvgdsray
      121 afeegrlqll trdhvagdkd dltqvgra
//
LOCUS       WP_181686817             448 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181686817
VERSION     WP_181686817.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 448)
  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 448)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..448
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          14..201
                     /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          162..>262
                     /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 arallfgsmt gsygaarirr lnletgqwqt lnypaqagdf dyapryspdg hwivflrnpq
       61 lgdlwripae ggaaerlthd tadiwgwswl pdgsgvifgr rvdiearlyr ldlldsslhd
      121 lgvddaqapd vahghlvfaq rkpqfgvyqv irdtmnggyi rrrlfsssgr ddqpmiapdg
      181 rqlvfasnrs gtyglwwgdv skpgsvrlie glrpdsrqaa dwsadsqrll vsgsdaagha
      241 alfevtpssg kvvrlpvpqp rplqaihlpd pdqvlvlaaa ddghtfatly drrsspwral
      301 atlqdvsqvr ldrisgqvll trlsgggvwq vapslaadtl qaidskqpsr wryrswapga
      361 hgdlhylsst dtcstydgel rsvggqclda vkftaingfs vdqhdgalyv alaeedgssi
      421 aymplpqrsv asicvlanll silrkias
//
LOCUS       WP_181687749             588 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181687749
VERSION     WP_181687749.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     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]"
     Region          6..555
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
      541 fhkvmegalr lmdvppddiq swlaaqaagk tgqpmvkpqs adldpalv
//
LOCUS       WP_181687796             139 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Xanthomonas oryzae].
ACCESSION   WP_181687796
VERSION     WP_181687796.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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 both ends.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..>139
                     /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          <3..139
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 qahavrlddg qvlsgpvlva sgvslpqllp elalrprkgh lvitdrhpgl irhqllelgy
       61 adsahgaddt svafnvqprp tgqmligssr qfgehdrals mpvlqqmlqr afaylpvlre
      121 lqairvwtgl rpatpdgrp
//
LOCUS       WP_181687857             430 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181687857
VERSION     WP_181687857.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 430)
  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 430)
  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 430)
  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 430)
  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..430
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>430
                     /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          30..>423
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtrptlsmig lavaaalsaq aqaqqadtas ntldtvivtg trasgrtvle stvpvdvlta
       61 edirkagvvn gelgsalqal lpsfnfphqs nsgggdhira aqlrglspdq vlvlvngkrr
      121 htsslvnids kigkgttpvd fnsipinaik rievlrdgag aqygsdavag vinvilddnp
      181 esgeleasfg ayntdvapin rritdgqtsy asakvgtllg ddggffkvgl elknreatnr
      241 agfdqippfe eqtpanlalk gqrnyvlgdg atkglnawln tkipfsasge fyafgtydqr
      301 dseganyfry pdssanwrei ypngyrpise genrdlqiva gargqwgnwd ydaslnygrn
      361 dftyrlrnsl naslgpgstt rfktgdfafa qtvgnfdltr vfdavgatht fgtgaefrre
      421 qyrthagdpa
//
LOCUS       WP_181687678              50 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181687678
VERSION     WP_181687678.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 50)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..50
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>50
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          4..>50
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mrelillrha haapadtgqa dfdrplsphg iaeaeaaglw lreqrlvpdr
//
LOCUS       WP_181687845             156 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181687845
VERSION     WP_181687845.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 156)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>156
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>154
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeylapr fregdyaggi saatat
//
LOCUS       WP_181687984             171 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181687984
VERSION     WP_181687984.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 171)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>171
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>169
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeylapr fregdyaggi saatatlagl iegealpppv s
//
LOCUS       WP_181688105             126 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181688105
VERSION     WP_181688105.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 126)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>126
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>126
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiad
//
LOCUS       WP_181688004             318 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181688004
VERSION     WP_181688004.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 318)
  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 both ends.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..>318
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          <2..271
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 kggglvyfdp ytgervappr lsaafafied lhrnltagkr gqavtgacal illffcasgl
       61 ylrwprrwws prtwwvvewr rqgrsflwsl havfgtwcll vyllvaltgl twsytwyrdg
      121 mlallgaapa irgdngdnrp atidvarvqr tldgipatrs aaldlriptr agqplnvrfl
      181 pdnpahdray nsldiapdsg allqrqdyal lprgqqlavs mfplhsgsff glpgrivvml
      241 aslgmsvffv tgwmlyldrr rkkrelraar vvlqgavpas qaapwviafa sqsgfaerla
      301 wqaaahlqaa glpvqvrp
//
LOCUS       WP_181689529             218 aa            linear   BCT 28-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181689529
VERSION     WP_181689529.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>218
                     /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]"
     Region          29..>162
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 macarypscl ahlrlrmkrh fsmlrdfqla dwftlanafc gtgavfaamr flqeehrgdl
       61 llgmalipla fvfdaldghv arwrkasstl greldsladv isfgvapaal gyacgmhggw
      121 dwlvlsyfvc cgvsrlaryn vtaeeiagea dkvpyfegtp iptslllvil lavaasighi
      181 getlwwgqwq lgpwqfhplv llfavsgslm isktlrip
//
LOCUS       WP_181689478             268 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [Xanthomonas oryzae].
ACCESSION   WP_181689478
VERSION     WP_181689478.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 268)
  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 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   3  (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]
REFERENCE   4  (residues 1 to 268)
  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..268
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..268
                     /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=30193
     Region          6..267
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mstataiteq efgrfqrfif eaagisissg kkamlcgrlg nrlrehqfst ytqylqlles
       61 rqdrdeiqta idllttnety ffrepkhfel lrkvagehrg glpfrcwsaa sssgeeaysm
      121 amvlddtlqg rpfevvgsdi strvlakart ghyalqridg ipqaylkryc lrgqgkydgt
      181 llverrlrdr vqfvhanlnt alpalgsfdv iflrnvmiyf ngqtkrdvil rvvsnlksgg
      241 hfcighsesl seldidlvqv apsifrka
//
LOCUS       WP_181689682             401 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181689682
VERSION     WP_181689682.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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 401)
  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 401)
  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..401
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>401
                     /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          30..>384
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtrptlsmig lavaaalsaq aqaqqadtas ntldtvivtg trasgrtvle stvpvdvlta
       61 edirkagvvn gelgsalqal lpsfnfphqs nsgggdhira aqlrglspdq vlvlvngkrr
      121 htsslvnids kigkgttpvd fnsipinaik rievlrdgag aqygsdavag vinvilddnp
      181 esgeleasfg ayntdvapin rritdgqtsy asakvgtllg ddggffkvgl elknreatnr
      241 agfdqippfe eqtpanlalk gqrnyvlgdg atkglnawln tkipfsasge fyafgtydqr
      301 dseganyfry pdssanwrei ypngyrpise genrdlqiva gargqwgnwd ydaslnygrn
      361 dftyrlrnsl naslgpgstt rfktgdfafa qtvgnfdltr v
//
LOCUS       WP_181690183             162 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181690183
VERSION     WP_181690183.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 162)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>162
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>162
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeylapr fregdyaggi saatatlagl ie
//
LOCUS       WP_181690257             431 aa            linear   BCT 28-DEC-2024
DEFINITION  ferritin-like domain-containing protein [Streptomyces sp. NBRC
            110611].
ACCESSION   WP_181690257
VERSION     WP_181690257.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NBRC 110611
  ORGANISM  Streptomyces sp. NBRC 110611
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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 431)
  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 10583968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Streptomyces sp. NBRC 110611"
                     /db_xref="taxon:1621259"
     Protein         1..431
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47135
     Region          26..253
                     /region_name="Ferritin-like"
                     /note="pfam12902"
                     /db_xref="CDD:403953"
ORIGIN      
        1 mphlttplav ramdgittld eladhlgdaa rielstippy lyaaysikts gysqwaqgaa
       61 aqrtligiai eemlhmalvr nvmvatrcet vktkngqgrk pfrfydpdsi ptypgdmshr
      121 tpplklhmqr istpavegfm evelpetvqq qrkilpsadd ytyhtlgely daigkgitdl
      181 tkakeitwgl tecrwqqqyl rafwnqwggp pkpipvvdqg saldalyiiv sqgegapdeq
      241 edshyekftr irdhvdgigv vyddngqqky tidddtgaav wpvvtdpkat dfpgalgkla
      301 vlsdavycyv lalldklylt paddpapdsa pgqhesapts eryalergfi aamqgvlspv
      361 agilvstplt sgqyagqhag ptfghydfng vppqqalldl ctdpdlakef pqlggtdgvl
      421 nqirllpyft i
//
LOCUS       WP_181690273             460 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces sp. NBRC
            110611].
ACCESSION   WP_181690273
VERSION     WP_181690273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NBRC 110611
  ORGANISM  Streptomyces sp. NBRC 110611
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  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 460)
  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 460)
  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 460)
  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..460
                     /organism="Streptomyces sp. NBRC 110611"
                     /db_xref="taxon:1621259"
     Protein         1..460
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=48040
     Region          5..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 mlhelkiinp atedlvatvp ttspdevdaa vrraataqea waavapgdra rilrrfadvv
       61 dahieplaal elaeaghplg narweagnvr dllhyaaggv erltgrqipv agglnitvqe
      121 plgvvaviap wnfpmpiaaw gtapalaagn avllkpaett pltalrlael aldaglsehl
      181 fqvlpgegpv tgtalvdhpg vakvvftgst atgrriaarc aaqtkrltle lggknpnivf
      241 adadleaaaa aapasfldnt gqdccarsri lversvydrf lellepavka fvagdpadsa
      301 tqmgplisaa qrervrsyvp edapaairgd vpagkgfwyp atvlegrpgd paateeifgp
      361 vavalpfdde adavrlanat dyglsgslwt rdvgrairvs ravaagnlsv nshssvrywt
      421 pfggfkqsgl grelgpdala aftetknifl stepstkess
//
LOCUS       WP_181690451             381 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Streptomyces sp.
            NBRC 110611].
ACCESSION   WP_181690451
VERSION     WP_181690451.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NBRC 110611
  ORGANISM  Streptomyces sp. NBRC 110611
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..381
                     /organism="Streptomyces sp. NBRC 110611"
                     /db_xref="taxon:1621259"
     Protein         <1..381
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          24..375
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 apatavvsda egddrvelqs lgtgrrargv lavgtgaplg tagryavhsa valltltter
       61 sralqdaeqr lgaavltmll agepdharav agrlygdlld tpfrmvvaeq vaaderpars
      121 gaaaaaapap sgasapvpps pspspaapts asspvsgasg agpgaldgla damesaaart
      181 geavltvldg grlialvtdg gaaadacaay agqaearasa parprgrpgs peagrggtev
      241 avglsaptgp taaanafrqa eqalsvarrr gralvehedv aagsvlplla ddavrafadg
      301 llralrehda tgrgdlvasl rawlarhgqw daaaadlgvh rhtlryrmrr veeilgrsld
      361 dadvrmelwl alkamsateg q
//
LOCUS       WP_181690463             320 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces sp. NBRC 110611].
ACCESSION   WP_181690463
VERSION     WP_181690463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NBRC 110611
  ORGANISM  Streptomyces sp. NBRC 110611
            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..320
                     /organism="Streptomyces sp. NBRC 110611"
                     /db_xref="taxon:1621259"
     Protein         1..320
                     /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=35671
     Region          45..211
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 msdtrgvirg nvrgvtgtar edqistardh ldakashive kygpgprvhy higlfdgdgd
       61 epdatssnal gtteagiegi rlritraqha lvrraaraws aeeilrpgae vidvgtglgg
      121 gaihwaeryg vivwavtnva shiahierfa aeagvgdlvr pvlsdardip apgrtidaav
      181 ameslcympr rlvfgrlael vrpggwlcvq dvflrrprwq pafdaywkts igtkdeyvaa
      241 ardagfvldr dedvsrwtse fwvqsmawae arivqleaqw erdaqlhhrl veslrwhagf
      301 hrawrdhaie vrllrfqrrg
//
LOCUS       WP_181690662             416 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181690662
VERSION     WP_181690662.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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 416)
  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 416)
  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..416
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>416
                     /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          30..>416
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtrptlsmig lavaaalsaq aqaqqadtas ntldtvivtg trasgrtvle stvpvdvlta
       61 edirkagvvn gelgsalqal lpsfnfphqs nsgggdhira aqlrglspdq vlvlvngkrr
      121 htsslvnids kigkgttpvd fnsipinaik rievlrdgag aqygsdavag vinvilddnp
      181 esgeleasfg ayntdvapin rritdgqtsy asakvgtllg ddggffkvgl elknreatnr
      241 agfdqippfe eqtpanlalk gqrnyvlgdg atkglnawln tkipfsasge fyafgtydqr
      301 dseganyfry pdssanwrei ypngyrpise genrdlqiva gargqwgnwd ydaslnygrn
      361 dftyrlrnsl naslgpgstt rfktgdfafa qtvgnfdltr vfdavgatht fgtgae
//
LOCUS       WP_181690517             871 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Streptomyces sp. NBRC 110611].
ACCESSION   WP_181690517
VERSION     WP_181690517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NBRC 110611
  ORGANISM  Streptomyces sp. NBRC 110611
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 871)
  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 871)
  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 871)
  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 871)
  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..871
                     /organism="Streptomyces sp. NBRC 110611"
                     /db_xref="taxon:1621259"
     Protein         1..871
                     /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=91916
     Region          24..837
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mkepehshgh parhrrvlgt rllienphal patevlrhld vdaelglddv evirrrslvg
       61 rnalagrkkl pawailvdqv rsavvvllva aavagllige vveaaavavv lvintivgfa
      121 telravrsme alrrlaatva dveredrrde ldavelvpgd iisveggdhv padarlieas
      181 dltvdeaalt gesepvaktv davavdapla ertgmlylgt tvragrgrav vvatgtatev
      241 griaemaast etmqaplqag lerlgrtlsl vvvgvagala glallrgldl heiievsial
      301 avaivpeglp avatltltvg mrrmarhral vrrlptvetl gsttviasdk tgtltanrmq
      361 vvdvalaega deqrlwqsav lcndadiapd gdpvgdptev allhaaqnag tdwrhlrkqh
      421 prcdevpfdp atkrmavvtd thvhtkgape vlldphrhte llsaaddmgg ralrtlvias
      481 gpapghpvdd qsllaaaevl gvvgladppr paaieavkac hqagirvvmi tgdqprtaaa
      541 vadqlglhaq qpvtgaeldr lddtalarvi dqtdvyarva pehklrlvqa lqtaghtvav
      601 tgdgvndapa lrqadvgvam grtgtdvare aadivlttdd fstiehavae grrvfdnirr
      661 fgqylfswhl avvlvvtaai algadaplag lmilwnniii dvipsfalal epssddamrh
      721 pprpknepvl gaatlrrilt qgalvgsvgl tsyllatttm nldldtartm tfvtlttaql
      781 lavfnartdt gsgfrgatan pylwaalalt taletialtv pdlrnllglt tlgaaswtta
      841 lalatlplll tqssrilrip rtrevarqhr a
//
LOCUS       WP_181690753             561 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181690753
VERSION     WP_181690753.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 561)
  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 561)
  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 561)
  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 561)
  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..561
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>561
                     /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          6..555
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
      541 fhkvmegalr lmdvppddiq s
//
LOCUS       WP_181689466             540 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181689466
VERSION     WP_181689466.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 540)
  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 540)
  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 540)
  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 540)
  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..540
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>540
                     /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          6..540
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
//
LOCUS       WP_181689576             472 aa            linear   BCT 28-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Xanthomonas oryzae].
ACCESSION   WP_181689576
VERSION     WP_181689576.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     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=53313
     Region          1..471
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 msyaivwfrr dlrlqdnpal raaldaghhp iplyidaphe egewtpgaas rtwrhrslav
       61 ledalralgs glviragdsa qvldaviaqt gavavywnrk yepatqprda qikralrerg
      121 ieaqscncal lfepwqlstq qggpykvftp fwrnaltqlq lpatapaprs lpplpamlkt
      181 daldtlqlvp slnwdqgfwe hwhageagah emleffidgg lsgyrknrdr pdrvgtsqls
      241 phlhfgeiap wriasaleaq rtarngaeid gyirqlgwrd fayhllhhfp dttnqnlnpr
      301 fegfdwakvd pvalqawqrg rtgipivdag mrqlwhtgwm hnrvrmivas flckhlrihw
      361 iegarwfwdt lvdadlannt lgwqwvagtg adaapyfrvf npvtqaekfd phatyitrwv
      421 pelgklpvke rfapwlhpls larfapeypr tpiiglaegr daalaaysks ra
//
LOCUS       WP_181693538             537 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181693538
VERSION     WP_181693538.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 537)
  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 537)
  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 537)
  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 537)
  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..537
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>537
                     /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          6..537
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvs
//
LOCUS       WP_181693685             583 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181693685
VERSION     WP_181693685.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 583)
  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 583)
  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 583)
  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 583)
  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..583
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>583
                     /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          6..555
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
      541 fhkvmegalr lmdvppddiq swlaaqaagk tgqpmvkpqs adl
//
LOCUS       WP_181693740             129 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181693740
VERSION     WP_181693740.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 129)
  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 129)
  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 129)
  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..129
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>129
                     /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..>128
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 msasyvsagr teqgnvrrrn edaillrddl glwavadglg ghsagdlasr mvvdalgalr
       61 rdgdlarfvd aidaqlsqvn rqlralarar rvdviastvv vlvhdhellm cgwvgdsray
      121 afeegrlql
//
LOCUS       WP_181693871              94 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Klebsiella oxytoca].
ACCESSION   WP_181693871
VERSION     WP_181693871.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
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="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     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=11116
     Region          26..84
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mqntiftppn peqrrtllee ygfkfdrrir edecseitsl srssrwkmeq qgrfpprchf
       61 grnscawlls dvlwwvrnpp avenvnnpys rksa
//
LOCUS       WP_181693939             336 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Klebsiella oxytoca].
ACCESSION   WP_181693939
VERSION     WP_181693939.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella oxytoca
  ORGANISM  Klebsiella oxytoca
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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..336
                     /organism="Klebsiella oxytoca"
                     /db_xref="taxon:571"
     Protein         1..336
                     /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=39421
     Region          5..308
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mrneitwdel leeyffahrl rpatewsynk vvrgfrrysg dtlpaqithr qvlewrryll
       61 qekqqsaqtw nnkiahlral ynygmeheil ppgknpfnks nvqrdtrkkk tltrsqlirv
      121 ylvmqqfeea eragrgirgg rnalwpawyw ltvldafryt gmrlnqllhi rlgdinlseg
      181 yldlclegsk threwrvpiv salkpglhhl meksaalgag sedylfdvnr iylnrhvewd
      241 aakvhqkirs ffrrlskecg ftvsphrfrh tlatelmksp ernlqlvkdl lghrsvsttm
      301 eyvelkmdiv gktleaelsl htdvtgernl hlltqa
//
LOCUS       WP_181694076             148 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome, partial [Xanthomonas oryzae].
ACCESSION   WP_181694076
VERSION     WP_181694076.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     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]"
     Region          51..138
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mrharvlvla alavpviaav afaqsavtpi pdpppvrlap levdlakttw gdakagqtka
       61 tacaachgpd gnpavamypr iagqteryva hqvaliasge rntgmsavmv pfvkdltaqd
      121 mrdlgayfat qkasagvadd aaiaegpy
//
LOCUS       WP_181694351             340 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein [Dietzia].
ACCESSION   WP_181694351
VERSION     WP_181694351.1
KEYWORDS    RefSeq.
SOURCE      Dietzia
  ORGANISM  Dietzia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae.
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="Dietzia"
                     /db_xref="taxon:37914"
     Protein         1..340
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35851
     Region          1..338
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtsggqgiag qveratdrls rrrvgvvmaa gppggvhtaa rgdtgrgatp dahtlfeigs
       61 vtkvftalll adgvvrgqwr ldtpvrdllp tgtdlpggdd dpitlqhlat htsglprtpg
      121 rlglrenlay vrtgadpyve ltepdvlagl rglrprrhpg qgtprysnlg fgllgiamts
      181 atgadfgalv rdricgplgm pdtvtedqmt ddqrrrtalg hrsrrrgaep wplrgmpgag
      241 alrstaadmt rflaahldps ttdledavrl tqatppsgpe rmglgwhrag pgtlwhnggt
      301 ggfrsitvvd tvgrtlavtl vnqtrgadlp tfrllraigs
//
LOCUS       WP_181694642             387 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181694642
VERSION     WP_181694642.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 387)
  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 387)
  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..387
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>387
                     /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          30..>384
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtrptlsmig lavaaalsaq aqaqqadtas ntldtvivtg trasgrtvle stvpvdvlta
       61 edirkagvvn gelgsalqal lpsfnfphqs nsgggdhira aqlrglspdq vlvlvngkrr
      121 htsslvnids kigkgttpvd fnsipinaik rievlrdgag aqygsdavag vinvilddnp
      181 esgeleasfg ayntdvapin rritdgqtsy asakvgtllg ddggffkvgl elknreatnr
      241 agfdqippfe eqtpanlalk gqrnyvlgdg atkglnawln tkipfsasge fyafgtydqr
      301 dseganyfry pdssanwrei ypngyrpise genrdlqiva gargqwgnwd ydaslnygrn
      361 dftyrlrnsl naslgpgstt rfktgdf
//
LOCUS       WP_181695948             592 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Nocardia sp. GTS18].
ACCESSION   WP_181695948
VERSION     WP_181695948.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     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=63315
     Region          27..592
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrefetpasy vipdnannsd svfrygresp dtvlfsvaga ditaaqfakt vtavakglia
       61 tgiepgdrva imaptryewv vldhaiwavg gctvaiydss aaeqakwilq dsgtvllivd
      121 sdkhrrvide ipadalpdlr eilqidkgvv aeltargahl ddqavhtrra gvgaespatl
      181 iytsgttgrp kgvllthanl yaesksdrla lgefvtegnr tlmflplahv faravtlaal
      241 dakvivafss dwatlvdqfa efrpdfilav prvfekvfna akqkahaggk grifdratet
      301 aivwsetldt ggpgllrkle halfdklvya qlrralggrc gaavsgggpl garlghffrg
      361 agipvyegyg ltettaaitv ntprntrvgt vgrpieghgv kiaddgelll rgpvvfgeyw
      421 gnpdatadaf vdgwfrtgdl gaidadgylt itgrkkeilv taggknvspg lmedalrahp
      481 vvgqamvvgd grpfvgalvt ldpealpawk qrnnipadtp vedlvdnptl radidqavad
      541 tnklvskaeg ikkvrilptd wteatgeltp kmslrraevm kkyaseveal ys
//
LOCUS       WP_181695991             175 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nocardia sp. GTS18].
ACCESSION   WP_181695991
VERSION     WP_181695991.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..175
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..175
                     /product="YybH family protein"
                     /calculated_mol_wt=19637
     Region          4..125
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 msgeseiref lesrtrahes kdidaamsfy sedivyydav aplrfsgtee vranflrwfd
       61 gydgpidlet helsiavdgd vafanmlhld sgkhkggiel siwvretvcl rrvegrwvit
      121 hehisipmsp ktfqiwcash kdapadggrt vfglaaralv arfvpwgrkm adrpv
//
LOCUS       WP_181696174             265 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardia sp. GTS18].
ACCESSION   WP_181696174
VERSION     WP_181696174.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     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=28144
     Region          1..259
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtttprtali tgasagigaa fahhlaangy qlllvarrad rlrelaaqls arhdvrcevf
       61 aadltdsaap aaivdyadgq gldvdvlinn aglsgktafa dtawdslage iqlmvtapte
      121 lahlvipgmk krhwgriinl ssvaafappg agllytgiks yvldtsqald melkphgihi
      181 talcpgftrt efhdvmgtrd kadhlprilw qqpdavvteg wdavmkgnpv cvpgivnkis
      241 aaamkplpvr lgyflgktfn pfkns
//
LOCUS       WP_181696179             500 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia sp. GTS18].
ACCESSION   WP_181696179
VERSION     WP_181696179.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 500)
  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 500)
  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..500
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..500
                     /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=54899
     Region          5..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 mairpvrapk iiiigagvag iasavtfkka gfddfvilek gsdvggvwfw nrypgltcdv
       61 psqlyqfgfa pkpdwsrvwa tgpeiqryha evvdkfglre hlrlnsevtd avfdgrgwvv
      121 tladgtelta dfviaatgvl hhpfvpeipg lhtftgdtvh tarwddslvt vdkriavigs
      181 gstgvqvvsa lqpgaaklsq ftrtpqwvlw apmgsaqskl vakllaaspt vhdrvyavsl
      241 wasgiladva lrptwrrtal qqlarlslra qvrdkdlrda ltpdyqplck rqvvsgtyyq
      301 aiqadnaelv tdkiteitpn girtadgreh pvdvivfatg fhphnymrpm nmrgrdglhi
      361 deawakgpra yrmtaipgfp nlftvlgpns ptgsislqys aeltaryitr wlhrfatgel
      421 dtvevteaat arfndavaea mgptvwntgc nswyftdqnt idlwpfdrkt mtamltepdd
      481 rdfligspah qgavaesttv
//
LOCUS       WP_181696211             434 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Nocardia sp. GTS18].
ACCESSION   WP_181696211
VERSION     WP_181696211.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 434)
  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..434
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..434
                     /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=48986
     Region          13..354
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 maitevavya hlsradveal geeldtirrd ieerrgapda dyirrtiafq rildasarll
       61 lagtgsrlgw lvgtsalaaa ksienmeigh nvshgqwdwm ndpeihsrtw ewdmagvssq
      121 wryshnyrhh mftnvvgmdd dvgfgvirvt rdqqwrprll lqplqnllla atfewgialh
      181 glyserdrae tatektahtr alvrkigrqt akdyvffpml sgrrwrrtlt asiaanalrn
      241 lwayvvifcg hfpdgaekft peaiehethg ewylrqmlgs anfdagpila flsghlshqi
      301 ehhlfpdlps nryaeiatrv ralcdkydlp yttgplprqy lltlrtinkl alpdtfllat
      361 tddapetase rkfatavpae pgtirrglrt alragarsgd hrgnfstrra misswismvp
      421 ppkrmagrpr kskv
//
LOCUS       WP_181696314             193 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Nocardia].
ACCESSION   WP_181696314
VERSION     WP_181696314.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nocardia
  ORGANISM  unclassified Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="unclassified Nocardia"
                     /db_xref="taxon:2637762"
     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: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=21644
     Region          24..116
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mstdpywnhn thyhpwlleq vpvhartald igcgdgllar klatrcdavl gididpevia
       61 napstphvhl dkadfrdldd tfdmvtavat lhhvpvregm aalrdlvapg gtlavvglwk
      121 mhpltdigyl pllpvvwatd rrhrreaggp natirdpeet lgeirraaee flpgarirrr
      181 llwrytllwq rpr
//
LOCUS       WP_181696329             418 aa            linear   BCT 28-DEC-2024
DEFINITION  lipase family alpha/beta hydrolase [Nocardia sp. GTS18].
ACCESSION   WP_181696329
VERSION     WP_181696329.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..418
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..418
                     /product="lipase family alpha/beta hydrolase"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44301
     Region          144..260
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
     Region          <216..>309
                     /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 mteqlsqsqa evqalarlag defvgaidgi aaihraisdr vftavragvg taadpvkvvh
       61 daitesvyav vggtghvvge masavqvsgl papsrtvwga gflaavqgli gdaleddapi
      121 laspmtirvd gapvpaeqla ahvpvpttkl vvllhglvet ehawrlggrp tygerleddl
      181 gytpvfvryn tglhisenaa qldalltrlv eqwplpvhei clighsmggl varsachrae
      241 qsdavwarsv rqvvclgsph lgapleqfvh yaaavldrlp etrplstllr rrsagirdlr
      301 qgslvdedwr drdvdalrae avrevplltg adhyfvtatv thspkhplgm vvgdgmvlrg
      361 sgsgvgrsrr igfdsgnglh vpganhfsll nhdavytalh gwlsgtphhp vqldtlgs
//
LOCUS       WP_181696418             325 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia sp. GTS18].
ACCESSION   WP_181696418
VERSION     WP_181696418.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     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=34819
     Region          14..305
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mssrlslrls rllnmvpyll ahpgisaaea aaelgvttkq lmsdlnqlwm cglpgygpgd
       61 lidlsfsees ievtfsagie rplrltstea tallvalrsi vempgmvdpt aahaaiakie
      121 saiaggdvsr ppaqvpverp vvatvraala dahalrlvyy sasrdevser vvdpirvvlv
      181 dnnsylqawc rqaegvrlfr fdriedatel deparppsha aadaaaldlf qddpdvplar
      241 lriradyawv ldqypmhrir srpdgsieag mrfasadwma rlllgfgtgv salgppelvs
      301 avreradaal aayaaagllg etepa
//
LOCUS       WP_181696420             497 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Nocardia sp. GTS18].
ACCESSION   WP_181696420
VERSION     WP_181696420.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 497)
  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 497)
  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..497
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..497
                     /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=53553
     Region          7..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(152,155..160,162..163)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(155,270..271,292..297,379,391,394,405,483)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(155,196..197,244,246..247,250,270..271,292..297,379,
                     391,394,402..405,464)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(196,246..247,250,270,402..404,458,464)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mnatlslasi laeparrrpe hlaliegehr itfadlwrqa raqaaaliar gvkpgdrval
       61 lcpntvdfpr ayfavlaaga tvvpvhlllt apemeyvlrd sgarllichp mvaqtggeaa
      121 raagiemvap edlagepipt fvsrspldta vvfytsgttg tpkgaelshl nmvmcatvnt
      181 fdaneihrdd ialgalplfh vfgqtvsmns hwrvggtlvl mprfdaaqai almtaervdl
      241 fhgvptmyls lieaaatate lpalklcvsg gaalpvsvle eferlfrapv legyglsets
      301 ptaavnqpvy gteagtvghp vwgvdveiad pdiadriell pvgevgevvv rghnvfsgyt
      361 grpeataaav idgwfrtgdl gtrdetgrir ivdrikemil rggfnvypte veaalmrhpr
      421 iaqvavigvp dehygeeiva vvvpdgevse qeviefarsr vakykyprrv efvtelplgp
      481 thkvlkrelr qrfgsge
//
LOCUS       WP_181696510             517 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia sp. GTS18].
ACCESSION   WP_181696510
VERSION     WP_181696510.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     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=57446
     Region          19..459
                     /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 msrkvtdnvv eprtvdnrar hvktiiigsg faglglairl aqqgredflv lergsevggt
       61 wrdntypgaa cdvpshlysy sfalnpdwtr sfsrqgeiqa yiksvaeryd vldrhvfdcd
      121 vrrvhwnnet srweisstqg eftadtvvsa vgalcepalp dikginefeg eifhsaqwnh
      181 dadltgkrva vigtgasaiq ivpaiadkva tldvyqrtap wllprmdrpy llperlafkh
      241 ipgvqrlsra aiyaaretqv vglakfpvlm kgfealsrak lqfeirdpel rkkvtpnyri
      301 gckrmlisne yypaldrdnv dvitdgiaev kpgsivtkdg tereidaliv atgfhvtdsp
      361 tynnivgrdg rtlsevfdei gqqaykgsai anfpnmfflv gpnvglghts mvymiesqin
      421 yvsdalatid klglktvevr edilreyntg lqnklaksvw ntggcaswyl dkhgnnttlw
      481 pdftfefrri tkhfdvsayn tttadasgad lkvvaaq
//
LOCUS       WP_181696106             270 aa            linear   BCT 28-DEC-2024
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Nocardia sp. GTS18].
ACCESSION   WP_181696106
VERSION     WP_181696106.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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..270
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..270
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28750
     Region          8..237
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mttteqvllt gdrngvrtlt lhrperknai dselwsalct aldaagndpd vrvlvltgag
       61 gafcsgadis apdprhpvyr mrvltevall lhelpmptva kvrgvavgag wnlalgcdlv
      121 vatpdsrfsq iftrrglspd lggswllprl vglqqakrla llaetidaae akalnlvtwi
      181 apepdidafv vrlaerlaag apvalaqtka llnegadrtl rdavanearv qginlatada
      241 peafaafaag repnftgrwa verrpdrhhq
//
LOCUS       WP_181696651             503 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia sp. GTS18].
ACCESSION   WP_181696651
VERSION     WP_181696651.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     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=55718
     Region          1..446
                     /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 mstidheiii vgagfsgiga aialreagfe dflmvddadg vggtwhwnty pgvavdipsf
       61 syqfsfdqrt ewsrvyapgr elkayaescv dkyglrprir fgttvvaadf dadadrwvlr
      121 tadgaelsar fvlsatgvlt rpklpdipgi etfagttvht arwdhgldlr gkrvaiigtg
      181 asavqvipei apvvehltvf qrtpiwclpr pdapmpppar walrlpggrt itrlisqtyv
      241 eitfplaahy hrslptaaig eraglahlrr qvkdpavrak ltpnyalgck rpsfsndyla
      301 tynrtnvtle tapiteitat gvrtedtehp advlilatgf kvmesgnmpt ydlhgvdgld
      361 lekwwdenrl qayegvsvpg fpnyfsimgp ygyngasyft lienqtrhil rclrrarstg
      421 atrvevrrea ndrffrevla rrggqvfwqd scadansyyf dkhgdvplrp sstleaawrs
      481 ghfdlsdymf taaprplsat vet
//
LOCUS       WP_181696398             116 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [Nocardia].
ACCESSION   WP_181696398
VERSION     WP_181696398.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     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=12002
     Region          9..113
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 minrtpataw lvlllagafe vgyalavggs hgftvltwsl vaivfflltl falsvalkti
       61 dvgigyavwa gigavgaall gpvffeetlt plkafwlavv iagvvwlkla draeaa
//
LOCUS       WP_181696806             364 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Nocardia sp. GTS18].
ACCESSION   WP_181696806
VERSION     WP_181696806.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..364
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..364
                     /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=38957
     Region          38..341
                     /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(48,50,183,203,275)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mhlrgvvlpg dqeldlwvvd gavtfepvvg aetlcrtgwi vpglvdahch vgirygggde
       61 thegaieqae terdagalll rdagspidtr fidehaelpr iiragrhiar pkryirelgi
      121 eldderdlpe ivaeqarfgd gwvkivgdwi dravgdlrpl wsddilkqai daahangarv
      181 tahvfgedal pglvnagidc lehgtgltdd tielmlangt alvptlinid tfpgiadsat
      241 kfpvyaahmr dlhrrvrdtv gkaheagvpi yagtdaggsi rhgriadeia altgaglsph
      301 dalgaaswna rtwlgresit egapadfvvy addprgnpaa ltdpqwvvlr glvvktpnpv
      361 tghr
//
LOCUS       WP_181696605             265 aa            linear   BCT 28-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Nocardia sp.
            GTS18].
ACCESSION   WP_181696605
VERSION     WP_181696605.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 265)
  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..265
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..265
                     /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=27167
     Region          129..230
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mriadtsprl admkrtaggv kvwvaigvyv attlaasvff lavqplsgid pavlslvqfa
       61 paagalvtwl vfrktvaavl paavsgrrva gnvaamvavc vgywsmlmva avvsgtatvg
      121 aaavgsvpfv vflvvqllga ggeeigwrgl mqpmlesria rlgavsvtga vwalwhvqal
      181 tagpvvavcf fvatmafamv lgylgtgsfg qrvlvasvgh wliniagyll agdattdrpq
      241 ivfvavaavl vavatmtvra vetrr
//
LOCUS       WP_181696814             380 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nocardia sp. GTS18].
ACCESSION   WP_181696814
VERSION     WP_181696814.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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 10790586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..380
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40554
     Region          25..369
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mtvmcalvaa sgatveagpg vtvlprpgge mlvgtttlhl vdaarpdpfe agrtrelmvs
       61 vfypatdvdr yprahyaste lipglektlg ielpgvltha hrdaparagt typvvlytpg
      121 agvsrvlgtg laedlasrgy vvvtvdhtye tgpavefpgg rivlptpapn gfdttireky
      181 iaarlldfrf vldsltrlss genpdseqda lptdlglvld mervgavghs sggytaveam
      241 htdrridaav dmdgqigvde afgravtegv drptlvltsa qieqvgdgnp sfdafwgkat
      301 gwkrhlaiad sahydftdmp afvpapakpa aaqyigtidt ermatlvrsy vaamfdkflr
      361 ertdtlldrp itepelttvr
//
LOCUS       WP_181696811             279 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia sp. GTS18].
ACCESSION   WP_181696811
VERSION     WP_181696811.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  AUTHORS   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19825230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..279
                     /product="helix-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=29775
     Region          <35..193
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          121..278
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <218..279
                     /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 mssllrprdg dalraeirwv arranvpvvf ggpvdedtll ltefvgtvtt glrglsvlrt
       61 sglggqamqy rrpaavadyr raptithdyd aavsgeglrs viavpvvvgd rpravlyaat
      121 rgasplgdra advimaagrr laneiavrde vdrrvrllel aepvaatpat eelreihael
      181 ramsaavdda tlrdrlagvs arlaavmtga padeaprlsr reidvlaqva lgctnqeval
      241 rlslgaetvk sylrhamskl dastrqeavv tarrygllp
//
LOCUS       WP_181696892             318 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Nocardia sp. GTS18].
ACCESSION   WP_181696892
VERSION     WP_181696892.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..318
                     /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=36159
     Region          4..253
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mnpklwavsd vhvghqgnkp iveqirpesp edwlivagdv gekaeevrwa lellrarfak
       61 viwvpgnhel wttpkdpvqm hgaarydylv amcrdldvlt pedpfpvwng pgaekfggsv
      121 tlapmfllyd yswrpagtnt kaealavare rnvvatdefl lhpdpyltrd awcharvqyt
      181 qrrldalapd tplvminhfp lvrqptdilf ypefslwcgt dltadwhtsy nvvcsvyghl
      241 hiprtthydg vrfeevslgy prewkrrgmp dpllrqilpe pvyaegdlna wgghfavtpe
      301 meaaaeemra kadrrrgi
//
LOCUS       WP_181696850             265 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Nocardia sp. GTS18].
ACCESSION   WP_181696850
VERSION     WP_181696850.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,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 265)
  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 265)
  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..265
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..265
                     /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=27161
     Region          5..243
                     /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 mlvwtprgkv lvlsvfglvv tvvfvapiat vvlaalagtw tgplpsdlgf anlgtavsge
       61 qaaslsvslq tallsgaval iigtwaalaa reaptwlrrl tdavfhlpva vpsvaiglgv
      121 liafnerpll lggtkwivil ahtvlvlaya fsaisaaldr ldpayrqaae slgagplrvl
      181 lqitlplllp algaaaglsi alsmgelgat imvypatwkt lpvsifaqtd rgevfdaaaa
      241 ttilvavtlv vlvvlgrlrg raavr
//
LOCUS       WP_181696658             190 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Nocardia sp. GTS18].
ACCESSION   WP_181696658
VERSION     WP_181696658.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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..190
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..190
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=20667
     Region          73..151
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mterrargts pggrgdrrts raarsrpspl dtpgrptaak rttrrrpeaa trkpsgkler
       61 tehtilglst gkavilaavl cglaltlavp trtyfsqrae aaalaeerae ldadlaalrd
      121 rraqqqdpay irtearerlr lvmpgetpyi vqvpgieapa pppmstrtae pdpwytdlwr
      181 sisepapegp
//
LOCUS       WP_181697004             221 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: potassium channel family protein [Nocardia].
ACCESSION   WP_181697004
VERSION     WP_181697004.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     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=23855
     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 myvvimgcgr vgsslaralt rvghevtvid rdpsafrrlg egfsgqevig vgfdrdvltr
       61 agieradafa avssgdnsni isarvaremf gvervvariy dakraevyer lgiptiatvp
      121 wttdrflrtl igdnstttwr eptgavavtq ltlheewfgr tvrdlerdlg vrvafilrfg
      181 rgllpesktv vqaddvvyva atsgsvgevv alaakapvse d
//
LOCUS       WP_181697057             294 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Nocardia].
ACCESSION   WP_181697057
VERSION     WP_181697057.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..294
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33193
     Region          25..88
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(31,35,60)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(34,59)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(41..42,53,56,60..61)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          112..289
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtaepheigr vqpivdrgpt vlrialggql rrlreskgit reaageairg shakisrlel
       61 grtgfkerdi rdlltlygvt dpvdreaffd larqanepgw whrysdllps wfstylgleq
      121 aasqirtyet qlvpgllqtp eytraivtvg lddaeterrv qvrqlrqdvl rrvdppvvwa
      181 videavlhrp vggrevhrnq lrhlielsll pnvtvqvlpy sagghaaags sfsilrfaep
      241 elpdivyleq ltsalylerr qdlalylsvm dqlsvqaahp drsreilrey aera
//
LOCUS       WP_181697011             176 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF1990 family protein [Nocardia sp. GTS18].
ACCESSION   WP_181697011
VERSION     WP_181697011.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..176
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..176
                     /product="DUF1990 family protein"
                     /calculated_mol_wt=19263
     Region          1..170
                     /region_name="COG4762"
                     /note="Uncharacterized conserved protein, UPF0548 family
                     [Function unknown]"
                     /db_xref="CDD:443794"
ORIGIN      
        1 mdtvpaestp ftypdvgatr attlpagyhr frlrrpigrg relfdragth ilafgmqkgv
       61 gifqradset aregteltvr lgagplgina pcrvvyvlde pnrrgfaygt lpghpergee
      121 lfaveydpad dtvyglvtaf stpaawytrl ggpvarllqh wfahrylrtl psntgs
//
LOCUS       WP_181696912             417 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Nocardia sp. GTS18].
ACCESSION   WP_181696912
VERSION     WP_181696912.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     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=42985
     Region          5..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 mnnevvitgi gavtpvgnta pdtwsalaag rsgvgrietf dpstfevqia gmvrgfspap
       61 ellttqrwdl lsrsggfgvv aaaqalaqag nmgshdeaar gvfvgghvgr pepqefaeig
      121 ltrrtsdgtv ihrrstdstw rcdqgvdlma iaevsrcrgp isgistacts athavgeamr
      181 riqageitma vaggqdsltt wldvagfsll galttryndn ptkaskpfda erdgfvlgeg
      241 svllvleerr iaeargaril arltgyastm nayritdspp dgggsitama daladagvag
      301 tevdcvyahg tstpgndvse taaikqvfga hayellvtsp ksmtghltag agalnvlaal
      361 ggiteglvsp tvnythpdpk ldldyvpnqa rkadvsvalv nsfafggtna slvvqap
//
LOCUS       WP_181697286             420 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Nocardia].
ACCESSION   WP_181697286
VERSION     WP_181697286.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..420
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..420
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45894
     Region          143..401
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mavttsiepf ltasgrpvst plkdvrtisr qmvvhfienv vpcatlpgea ldgdvttvtr
       61 vcleltrsml dgrdlpgrve rvqaaaadwa regipidtih havhegfklg fdlvitnvtn
      121 hdydtvvgva rrlmdaqdmi tsavsaayvr elravvsehh tavhtltsal lggqntstma
      181 recgievaae yhvmalelpp hpeesepgln akvvarrklr rvqaelanrc dgkvlsllsv
      241 dggtlllpat eftepeldel ivhlstaaqv pvravvmsaa pseipraaeq vhelveivhr
      301 lggpskvyrp helafeyqlt rpgpardyls svvdsleahp elmqtlevym stnmqrsrta
      361 rkmfihtntv dyrlkrisqm tgfdlndvtg lcylraalli rahrgtassd ispdrgsrag
//
LOCUS       WP_181696982             832 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Nocardia].
ACCESSION   WP_181696982
VERSION     WP_181696982.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 832)
  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 832)
  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..832
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..832
                     /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=92192
     Region          13..825
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mdltdlleip gtdadalyes falwaaeqgt tlypaqdeal melasgsnvi latptgsgks
       61 lvavgahlfa mangqrsyyt apikalvsek ffalcevfga envgmvtgda avnadapiic
      121 ataeilanla lregaaaevg qvvmdefhfy adpdrgwawq vpiielpraq fllmsatlge
      181 vdffatdleq rtgrptavva gterpvpltf syvrtpitet leelvtthqa pvyvvhftqa
      241 aaleraqalt svnfasraek daiaaaigef rfasgfgktl srlirhgigv hhagmlpkyr
      301 rlveklaqeg llkvvcgtdt lgvginvpir tvlltgltky dgvrtrrlka refhqiagra
      361 gragfdtmgt vvvqapehev enarliakag ddpkkqrkvq rrkppegfvs wseetfdrlv
      421 aaqpepmvsr favtnsmlln viarpgncfy amrhllednh eprpaqrkhi lrairlyrsl
      481 rdagvvqqls epdakgrmar ltvdlqrdfa ldqplspfal aafelldres ptytldvvsl
      541 ieatledprq llmaqqhkar gaavaemkae gieyeermel leevtwpkpl aeliepafet
      601 yraghpwvse fapspksvvr dmieramtfa elisfyeltr segvvlryla dayralrrtv
      661 pdaarteeld dltewlgeli rqvdssllde weqltnpgae idtdqvafga eqvrpisane
      721 rafrimvrna mfrrvelasr qrwyeldqlg tgpdwaeefa pyfeeyetig tgpdargpql
      781 frveqrpgfw hvrqviddpa gdhgwaltai vdleesdaag evvfdevtva pg
//
LOCUS       WP_181697334             202 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardia sp. GTS18].
ACCESSION   WP_181697334
VERSION     WP_181697334.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (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   2  (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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..202
                     /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=21536
     Region          44..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 msaskdrtps qweeivaadp shsaryvqrf rtlaaegtdi vgearlvdam lgrgarvlda
       61 gcgpgriggy lhdaghtvvg vdvdpvlida aradhpgptw lvgdlaeldl ptrdfdaivc
      121 agnvltflap striavlegf arhlapagrl itgfgaergy efadflddte kaglttdlll
      181 stwdlrpfrd dsdflaavfs rt
//
LOCUS       WP_181697345             330 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nocardia sp. GTS18].
ACCESSION   WP_181697345
VERSION     WP_181697345.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     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=34833
     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 mrdfgyerai gpeqavatml aepdavflga gtnlvdhlkl gitapgllvd vsrlpfddit
       61 erpdgavrvg atvrnadlaa hpiirarypm lsaallagas pqlrnlatta gnllqrtrcp
      121 yfqgvttpcn krtpgsgcsa iggydrdqav lgasdqciat hpsdmavamt aldatvrvlg
      181 adgereiplv dlhrlpgaep erdtvlahgd litavdlpal dwaanstyrk vrdrasyafa
      241 lvsvaaavdi adgqvrdcri afggvahkpw rahaaeaalr grpatetsfa eaadaelaaa
      301 rpqrhnafki plarkvlvat lrdlteqgar
//
LOCUS       WP_181697371             283 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MlaE family ABC transporter permease [Nocardia].
ACCESSION   WP_181697371
VERSION     WP_181697371.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..283
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..283
                     /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=29561
     Region          25..275
                     /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 mtsqpateps everiidsat glwrrhpqrs vetlgrqvll grsaivqlfl slvrrrfpfq
       61 efvkqcafma nvsalptvfv aipvavvvsi qvgalvnqvg attfigavag lgiirqgapl
      121 vtslmiagav gsaicadlgs rtireeidam kvmgvdpvrr lvaprlvaav vvsmllcgfi
      181 vfvgfatayl fnvyaqhgtp gsfissfasf avandllval fkaaifgalt aiiacdiglh
      241 tkggpggvan svnsavvtsa lmlfatniiv tqlynalfpa kvv
//
LOCUS       WP_181697522             551 aa            linear   BCT 28-DEC-2024
DEFINITION  (2,3-dihydroxybenzoyl)adenylate synthase [Nocardia sp. GTS18].
ACCESSION   WP_181697522
VERSION     WP_181697522.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..551
                     /product="(2,3-dihydroxybenzoyl)adenylate synthase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0008668 -
                     2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
                     [Evidence IEA]"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59124
     Region          10..546
                     /region_name="EntE"
                     /note="2,3-dihydroxybenzoate-AMP synthase component of
                     non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1021"
                     /db_xref="CDD:440644"
ORIGIN      
        1 mldltepafa gftpwpadla dryrahnlwt gdtfgdilaa raaatpdria vldtahswsy
       61 aelhhrarsl aaglarlgit pgdrvlvqlp nraefvevvf alfelgalpv fclpahraae
      121 lvpiaeaaaa tavitcgthq rfdyaalaat vrekvsslrh vllvldegqq lpegahdiae
      181 frdepvelrg psagdvaflq lsggstgipk liarthddyl ysvrrsaeic eldsdtvyla
      241 tlpvahnfpm sspgilgalw aggavamtpd ptpatafpli erfgvtitgl vpplarlwte
      301 raeagdtpdl sslrvlqvgg arcqdelarr igpalgvtlq qvfgmaeglv cytrlddpid
      361 vvvstqgrpm sefdqiavvd dngvevapge qgnlitqgpy tirgyydnpe adarsftaag
      421 wyrtgdivsi rpdgnlvvag ragdwvnrgg ekvsaeelea hllehpgird avivgtpdpv
      481 lgqricafvq ptdpeqrptl tsvrkfvrer gvaawkmpda vvvieqfpet gvgktsrkel
      541 rqllaegahg n
//
LOCUS       WP_181697539             435 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Nocardia].
ACCESSION   WP_181697539
VERSION     WP_181697539.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 435)
  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 435)
  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 435)
  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 435)
  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 435)
  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 435)
  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..435
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..435
                     /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=46931
     Region          147..410
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrrilrsil tvltittvvl gvpliytawl wveditrndl qsrleriaae viaqeqvdgy
       61 vhdgldvrai ralvpeggrl tvvyptptdn aartdigveq iddplvesls mgtsaslrle
      121 vpagpmharq eqavaavala vlaslgaafs vavvtarrva dplrdvaara arlamgdfrp
      181 dprrhgiael drvsdvldsa tveiagrlqr ehalvadvsh qlrsrltavr lrldelsthn
      241 dpevvheaee amaqvdrltd aiddlvrasr sedaadrdpv pvmaelrgvv aewthpfhea
      301 grelsligde slrapitgsr lreavavlvd nalmhgggtc tvsvrtvptm sardplicve
      361 vadegegird emaphifdrg fsaggstgvg lalaralvea dggrlelqrr rpalfavflg
      421 skvnrsqnat ltepr
//
LOCUS       WP_181697699             765 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Nocardia sp. GTS18].
ACCESSION   WP_181697699
VERSION     WP_181697699.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     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=83416
     Region          19..763
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mpdrladdra stdqggrgre ieqeqqyltv lydrldamrd yaqnrlktvl leaggtpqar
       61 seresftaly sedlakydaa ehglcfgrid ldatedaary igrlgilded ndyepllldw
      121 raplarpfyl attanpedvv rrrhirsrnr tvtaindeyl dlgaaerdga vgtddgvgge
      181 sallaalnaa rtghmndive tiqseqdaii rsehksvlvv qggpgtgkta valhraayll
      241 ytfrqqlaks gvliigpnat fldyigqvlp slgetgvlls tigdlypgvk avredslrag
      301 eikgsldmle vlkqavrdrq evpaepvrlt fdgypvlldr kiatrargra rssrrphnla
      361 rpifassvid altdqlaatm gadlsggtsl lssadlseig demradpqvq aaisalwpvl
      421 spqevladll adparldraa kslspedrae lvrpddgtfs aadaplldel aellgvddte
      481 ererarrrwr aqlaeaqdal diltgsapqd iedeldpeil maydlidatq laqrqefgnr
      541 qttaeraagd rtwtyghviv deaqelsema wrmvmrripn rwitvvgdva qtgdpagass
      601 wqrvlepyva krwklteltv nyrtpaeima vaadvltaid ptaqaprsvr etgnpprahr
      661 vspaevpdel arliaaeqap gtaavlapaa lvpelstlag esvqvltvhd akglefdrvy
      721 lvepqaivke sprglndlyv altratqrla vvhtedlpev lsala
//
LOCUS       WP_181697544             211 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Nocardia sp. GTS18].
ACCESSION   WP_181697544
VERSION     WP_181697544.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 211)
  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..211
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..211
                     /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=21817
     Region          2..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 mtrlvlasas parlgvlrta gidpvvrvsg vdedavsaal padtsaddvv valarakald
       61 vagsipelaa dcvvvgcdsm llvdgrlqgk phtpevarer wasmagrsad lltghcvlrl
      121 rdgevvaesa ecssttvhfa epgpdeleay iatgeplqva gaftldglgg wfvdriegdp
      181 ssvigiglpl lrrlledvgv gvtqlwrdar s
//
LOCUS       WP_181697524            2902 aa            linear   BCT 28-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Nocardia sp.
            GTS18].
ACCESSION   WP_181697524
VERSION     WP_181697524.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 2902)
  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..2902
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..2902
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=311090
     Region          <8..2782
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
ORIGIN      
        1 mgsverddvs adhpglpltg aqsgiwnaqr ldpeslsylv gevleisgae pvdvplldta
       61 irrtiaetdt mrlrfsetpe gprqritele pelrplvdlr geadpvaaah rlvaaerera
      121 atycrdmvdr qlytytllrl tdndvwciql yhhliidgys aamvsrrvaa hytalrrgte
      181 vprlrwgsve tlvaedleyr gsqahrqdre ywrdrltplp pldgrgrape gvveqthevr
      241 avlaadlmgr vktaatevgi twadvlvagy agfvhrllge tdvvialpvm arvgktaltt
      301 psmavnvlpl rvsvsgqdrl gelgkrvada lremrahqrf rgedlarefg gaqtgallhg
      361 igvnlkafdf aldfdgatgt lrnvaggppe dlgltvtpls edrvqlgfev darsldaata
      421 rrrmdalvtl itelvdadkp igaitlypae iaadiavera gaalpgrpdd vvevfdrmva
      481 aqpddivlvd gthrltaael garvhqlary lrgrgigped ivgialprsv dlviallavq
      541 hagaaflmld inhpaqrlad iiddadpali ltddivaeav faerlttdgs pdrtsaaqad
      601 apsmtgdvvn rhvatgmlll sdnevraait slpsgplsma elaaprsagh layvvytsgs
      661 tgkpkgvqis sgamaqllhh hrctvyadta grvggrqlhv ahtysfafda aldqlmwlwc
      721 ghrihlydvd iqkdasaqva alrtdridvv dttpsmatal idngllgsah rpellllgge
      781 atppalwtai vaskvvarnm ygpteatida lsapvtgavp hvggplagtr aylldgalqp
      841 vpdgeigely lagpqlargy lermvvtaer fvadpfacge rmyrtgdrar wlpghgydyl
      901 gradsqikvr gyrvelgeve aslgalpgva aaaatirksg dstrligylv petgrtldad
      961 qlrqllttlv pdhlvpsalm ildslpttvn gkldraalpa pqltstgrpp rteqeralcg
     1021 ivaevlglaq vnatddffgl ggdsitaigv ssrlralgwe vqpktllaqr nlatiaataq
     1081 maevrtgapt pdeptgavpi ppmvaallea ntdsrtiagy aqwtaltlhe dltvdhlttg
     1141 lqtlldrhda lrlvldgsgt darlevaavg tlrasdlvre ivpgvpghge maaliesvaf
     1201 alakelapae gvqiraalvr sghavadrlv lvanhlvvdg vswrilvpel yeacsaakee
     1261 rparlagkgs swrryatlla esgvageyra elahweralg dasaaplger aldpavdlve
     1321 saeqtrtfat paiteafltt lptayraktd dvllaalmla lnawrhesge slepgrpvtv
     1381 eghgrealrp dtdfagtvgw ftsefpvwtp atgiddpagl tealsggaaa ghllravkea
     1441 kravpgngvg ygvlrrldpe taprfagrrt pevllnylgr fggggtpgws lpehdafavt
     1501 epsekaltev lslnvfvhes aragaprlav ewtaasrilg adqvaeiqrh felalealaa
     1561 harlypgglt psdcpgvivd qdtidaledt hgplaellpl splqegllfh airdgaddvy
     1621 tlsarvdlhg pldgprlaaa fdtvvgrhpt maaafhfedl dqpvqavprs vgmpwrevdl
     1681 adlppriaqa aadrleaeai rhrfavdrsp mlratlirlp gdahrlvlnt hhlvidgwst
     1741 pivlrevlat yhgdelppaa sysdyltwlg trdreavraa wsqrlaglea ptmardliae
     1801 vahshrdrea rpwrnlasqq revrqrqvpl peslatalae lgrrrgltmn tlvqgtwalv
     1861 laalsgrtdv vfgatvsgrp aelpgvagmv glfantvpvr csftparpll dqwadlqenq
     1921 famqdfdhas laeiervagl gtlfdtlvaf enfpnsgpgq pdshdlrlge fhnhgnthyp
     1981 ltliappgdh lelmiwydra vvpepvlhhi adritailta vattpdtaan hfldpltpav
     2041 pqgrisapep avaarntias alndgeqcaa apivessalp gpsgttlaew gipvdpaapa
     2101 vtaegitidf gefdaranqa arwlisqgvg petvvavamp rtidsvvaah aicraggvyl
     2161 pidpeqpaqr iekildtasp amvlrsldea girsadersp dherggfada pltdvdrlap
     2221 lrpantacll ftsgstgvpk gvslshaaii stfewlqrev rfgpgdtmly rtppifdasl
     2281 memflplhvg arivltrpgg hrdpyyqaql msaervtamw mttsmltvla eeadlsgcad
     2341 lrcvltggev lpaataqrmr altgtavynf ygpteaaigf tfhetvdadt tsvpvgapad
     2401 tvrilddqlh pvpegtvgel ymtgvrlarg ylarpdltaa afvadpfgsg ermyrtgdlv
     2461 klnpdgeldy igrtdsqvkl rgqrielgdi esalltcpgv ahavvqlred tpgdqrlvty
     2521 lmaksgitld tdsireqlrn klpaymipaa vvvldhiprt atekidrral papesrtadg
     2581 dtldtiraam aavlsvpeig tdddffdkgg hsllavrlvg rltradlpvv lddvftastp
     2641 relaarigat dpttppkdgl aglgrrldpv lelraegsvp plfcihqigg tawkyaplar
     2701 llraerpiig lqmphltept trtrtlddla ryylaavrri qphgpyhflg yslggnlaha
     2761 maaileaege qvgyvgllds hplsnltera aatladpsgm aalvpeidey ptelasvvtq
     2821 aatellrmvt esespsysgp malycadngl epervhaqlt gwraagaqlv vrrlpythne
     2881 iamptgwiev aalidadpai rt
//
LOCUS       WP_181697741             323 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia sp. GTS18].
ACCESSION   WP_181697741
VERSION     WP_181697741.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 323)
  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 323)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..323
                     /product="helix-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=34727
     Region          15..321
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrlvqll lllqanggat agelarelev svrtvyrdve alsaagvpvy sepgrgggvr
       61 lvdgyrtrlt gltsdeadav llaglpgaaa dlglgtvlat aqlkmlaalp pelrgratri
      121 aervhidmpg wfhrpdetpt latiadavwh drrlaityrr gddvvertvd plglvmkagt
      181 wylvarvrsd irsyrasria taaptgetfd rppdfdlaah wqaaavdfgr smlkvsaqcr
      241 iatehlgllr lmndpaavha alaslgptap dgwaditips esyevlthal lpladhievl
      301 appefrahlr tiseamaary rtt
//
LOCUS       WP_181697782             293 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Nocardia].
ACCESSION   WP_181697782
VERSION     WP_181697782.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..293
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32420
     Region          23..289
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 midigpgept sdlrvlldll dleqisedvy lgnhpekvws rtfggqlvsq aivaagrtag
       61 drplhainah fvrggdvkkp ieyhvqrhrd gralanrtvt asqdgqelfv mlaafqdwgk
      121 glehahdapv vpdpeslpri eehfagfedk lemfinaphp idmrytndpa wilkgtgakl
      181 nhnrvwmrtd gtlpddpllh vaalgyssdt tvldsiitth glswgldril aatvnhsiwf
      241 hrpfrfddws lyatespvaa gsrglatgrf ysrsgellat tvqegvirhf par
//
LOCUS       WP_181697814             209 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardia sp.
            GTS18].
ACCESSION   WP_181697814
VERSION     WP_181697814.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   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 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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..209
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22580
     Region          4..97
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrsygqycgl araievvgdr wnllivrell laparyrall eglpgiatnl ladrlrdlea
       61 sgvverrltg egsiveyalt pwgaelrepi eglirwstpl msrgpaegds frpgwlalal
      121 pallnarvel rravtiglei daeffqlrgt rsgfevgrhd greldagvra dpgcllglaa
      181 galtldeara lqlveihgde svvdnvfgg
//
LOCUS       WP_181697983             151 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardia sp.
            GTS18].
ACCESSION   WP_181697983
VERSION     WP_181697983.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..151
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16939
     Region          4..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mryeeladap csitrplvil gdrwtllilk ycfagvrrfn afqsalgisr srlhdrldrl
       61 veheilvkrp vddgayeeyr ltekghaiyp ilmairdwgd tymapegppv eyrhhdctge
      121 ahvhltcdac haevtardie pqagpgitgv a
//
LOCUS       WP_181697914             272 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)-dependent oxidoreductase [Nocardia sp. GTS18].
ACCESSION   WP_181697914
VERSION     WP_181697914.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 272)
  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 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..272
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=27907
     Region          31..266
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 msnstavqrv sviglgamga alakallagg hevtvwnrta araeplvaeg atvattsaea
       61 maagdmvilc vlddaavreh vepaaeqlrg rvvvnltttt peqgrslgrw aeangvelvd
      121 ggimavpsmi ggpaafllys gitaafdrfr hvldlfgrae wvgtdygaaa mydlailggm
      181 ysmfagfqqg gkmvrttggs aahlatlmgp flqamagmfa qyapgiddpa tyvpeqsaef
      241 tagalttint aadeagtpse llqvllktvp gi
//
LOCUS       WP_181698053             323 aa            linear   BCT 28-DEC-2024
DEFINITION  COX15/CtaA family protein [Nocardia sp. GTS18].
ACCESSION   WP_181698053
VERSION     WP_181698053.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..323
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..323
                     /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=33778
     Region          16..307
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mlyrafiglv drlplpslrt qrlialavil sqagisvtga ivrvtasglg cptwpqcfpg
       61 sftpvgvsev pvlhqtvefg nrlltfvvtl caalivlavv rarrrkevlv yawlmpggtv
      121 vqaiiggitv rtgllwwtva vhllasmvmv wlavvlyaki gqpddgidtv qvpaplrwlt
      181 alsgvalagv liagtlvtaa gphagdksid rpvarlevei vtlvhlhsql ligylallig
      241 lafglyavgi tpairnrlfv llgivlsqal vgvvqyftdv paalvaihvg gaaactaata
      301 alwaslrire tvdapavsaa ath
//
LOCUS       WP_181698064             424 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Nocardia].
ACCESSION   WP_181698064
VERSION     WP_181698064.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..424
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45453
     Region          118..378
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtipvdrglt stlvthfvnn vatcrtlpgd aisgevtsvt rmcleicagl ldgrdeeakl
       61 hrlavaaagw aregvpidti lhalhegfri gfdaacagms lpdefrrlia isdvlcttvt
      121 rayirehrei agehhtavht ltsallagqp titmarecgi avaesyavla lsigehpdeh
      181 darlnssvva rrklrrvqaa lahrcgeqal sllsvdggtl lipadlladd qldglveals
      241 raarvdvtaa lvtspaaeip daaqrahell dmverldcep glyrfgdlal eyqltrpgpg
      301 rarlgellap ldkhpelyet lrvhiannmn rqrtarllhi htntvdyrlr rvaqltgldp
      361 aqasglwqlr samiarsfht gprvpaeqva stgfggamgt sgprrarada evcptpglgg
      421 vrsa
//
LOCUS       WP_181698118             345 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nocardia sp. GTS18].
ACCESSION   WP_181698118
VERSION     WP_181698118.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..345
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36379
     Region          45..344
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mntlafrtll aaacaaalat apvladgpqa taapgahlvs rgqtgqtaei svyspsmdrt
       61 ialrvlrpad tatpaptlyl lngagggeds anwagqtnaa effagkhvnv vmpmegafsy
      121 ytdwhqpdpg laknlknngv nkwttfltqe lppvidaafd ttgvnslagi smagssvldl
      181 aiqaprlyrs vasysgcamt sdpvgrefvs lvvrlgggkv enmwgpagda awrehdpyvq
      241 ahrlpdipiy iaagsglpgv hdtlanprvh vegknpasil qnqmlvgggi eaatmyctaq
      301 maqrtrelgr tnitynmrat gthswgywed dlhaswpmma talgl
//
LOCUS       WP_181698130             190 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Nocardia].
ACCESSION   WP_181698130
VERSION     WP_181698130.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 190)
  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 190)
  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..190
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..190
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20580
     Region          2..98
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msrrsydhyc avsraldlvg drwsllvvre lcsgprrysd lfadlpgist dmlatrlkgl
       61 erdgvlthhr ngmrssyelt elgrglrpvl dalagwgapl lgqrnptdav rahwlalplg
      121 ralaevvdeg tvtvhigdtv lhyvrtaegi thhdgpasaa dhelrldlae aidiatgaqp
      181 lspralspvr
//
LOCUS       WP_181698147             335 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [Nocardia].
ACCESSION   WP_181698147
VERSION     WP_181698147.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     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=34119
     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 mlwslivvgg faalavsili avtlgpadis pvnvrdvlln hlgltdvpvr vsknaivwee
       61 rlpralvaaa cgaglgicgv imqsllrnpl adpfvlgiss gastgavivg vlgvggaalg
      121 lsggaflgsl vafglvllla rmsggsndrv ilagvastql fsaltsfvif afadsdetrg
      181 vmfwllgsle gvrwddvtlc aivvlagaav clyfayvlda fsfgddvaas lgiavakvrm
      241 lllivtalit atlvsvagai gfvglvlpha arflvgprhs rlvpatallg avfmvwvdai
      301 srvafaptpl pvgvgtalvg vpafivilsr rrsvr
//
LOCUS       WP_181698220             257 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: pirin family protein [unclassified Nocardia].
ACCESSION   WP_181698220
VERSION     WP_181698220.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nocardia
  ORGANISM  unclassified Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (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   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14390632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="unclassified Nocardia"
                     /db_xref="taxon:2637762"
     Protein         1..257
                     /product="pirin family protein"
                     /EC_number="1.13.11.24"
                     /GO_function="GO:0008127 - quercetin 2,3-dioxygenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28112
     Region          24..151
                     /region_name="cupin_Yhhw_N"
                     /note="Escherichia coli YhhW and YhaK and related
                     proteins, pirin-like bicupin, N-terminal cupin domain;
                     cd02910"
                     /db_xref="CDD:380375"
     Site            order(30..31,47,52,70,72,74,76,95,97,99,101,131,133,
                     135..137,145,147,149)
                     /site_type="other"
                     /note="intramolecular domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:380375"
     Region          183..251
                     /region_name="Pirin_C_2"
                     /note="Quercetinase C-terminal cupin domain; pfam17954"
                     /db_xref="CDD:465583"
ORIGIN      
        1 mststtprie vhrggdrmkt riswldskhs fsfgehydpd nthhglllvn nedvvlpgeg
       61 fdthphrdme ivtwvlggsl vhqdslghng viypglaqrm sagtgilhse kndswrldgk
      121 lpehdepvhf vqmwvvpdep gvdpgyqqle iddelargdl vtvasglpry rdrtaisins
      181 shaamhvarl tadsapvtlp dapylhvfva rgevdmegvg tlaqgdavrl trsggqlirp
      241 hgdaevlvwe mharlgg
//
LOCUS       WP_181698221             283 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia sp. GTS18].
ACCESSION   WP_181698221
VERSION     WP_181698221.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   Wintjens,R. and Rooman,M.
  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 283)
  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..283
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31415
     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..279
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mapvsptaar welvlrlrdl reqrgfdsag fakrvgftpa nwshvekgrr vltrttiepv
       61 ldvldvpade rrellallea skqrgwwsts aaligpelqr lygmeagaqs irsydslivp
      121 gllqteayar alisadvmir pvqvdqlvai rlrrqrrlre pepleltavl geatlrqqtg
      181 gpevlrgqlr hlvelmreld tvdvrvipfs apegavlggs sfhlldfasd qlptfawaes
      241 avfgghvdda eqvrdlgyaf lrardqampr seslalisdy arv
//
LOCUS       WP_181698257             290 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Nocardia sp.
            GTS18].
ACCESSION   WP_181698257
VERSION     WP_181698257.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     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=31072
     Region          20..284
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtsvvaqqvp ydsaapyrsl slntattkrw tlaeavdgaa raglgaiglw rdrvdelgat
       61 taakivadag lrvsslcrgg fltgredgpa alddnrraid daatlgtrel vmvmggipdr
      121 dlagararve erlallvpya aergvrlale plhpmfcadr avistlaqal smaaphpaet
      181 vgvvvdtfhl wwdptlaeqi aqagadgris syqvcdwlnp mtadpllsrg mmgdgvidfa
      241 tigrwvrdag yrgdveveif natvwssdgh evietmkrry relvlpslvg
//
LOCUS       WP_181698343             463 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nocardia sp. GTS18].
ACCESSION   WP_181698343
VERSION     WP_181698343.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 463)
  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 463)
  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..463
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..463
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=50561
     Region          10..460
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mtapaphgis ghvagfvaal rsrgvpvgps etvdagqvlt vldlldreav reglacallr
       61 rpthrptfds lfdlwfpvtv gqrsaeapel prtpdgrvdl palreqlael latpdggnql
      121 ellaaqvveq lgryqsargp sfsayqalkd lapqtllara laglalppda serdaeiaqr
      181 llrmriagfr atveeetnrr vaeqigrerv atygvarqae dadflraser eladlrrgth
      241 rlarilasrl avrrkrsrrg eidlrktlra smstggvpid lvqrkprpgr pdlvllcdis
      301 gsvagfsgft lllvsalreq fsrvrifafv drtdevtdyf gpqtglddvl triftestvi
      361 dsdghsdygq aftsfadnfg davtsrtsll vlgdgrtnyr npkvdtlrgl vetakhahwl
      421 npephnlwgt gdsaapdyga viemhecrsa rqltdvvskl lpv
//
LOCUS       WP_181698223             671 aa            linear   BCT 28-DEC-2024
DEFINITION  M13 family metallopeptidase [Nocardia sp. GTS18].
ACCESSION   WP_181698223
VERSION     WP_181698223.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 671)
  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 671)
  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..671
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..671
                     /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=74245
     Region          2..671
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mtsdlsspsg idlsfrdqdv rvqddlfahv ngrwladyei padravdgaf rtlydqaeid
       61 vqtiitecae gsadsadark igdlyssfmn telvaaaglt pvadelhaia tvadasafaa
      121 llgrlqrtgv rgalayyvdt ddkdstryll hatqsgiglp desyyrsdef aeirdayrah
      181 ltkmftlaas dpalaglvpt dpadaanrvf elertlaagh wdvvrrrdae ksynlttfde
      241 latahpefdw aawadavaeg vdragtelfa elvirqpgyv gafarawsdv pqadwqawaa
      301 wqvlharapy ltdeivaanf dfygrtltga qeirerwkrg vglvqellge avgklyvash
      361 fppeakarmv elvanlqeay rrniaelewm gpdtraaalt klekftpkig ypdtwrdysa
      421 veidaadlvg nyrrgyaadh drdlgklggp vdrgewfmtp qtvnayynpg mneivfpaai
      481 lqppffdmna ddaanyggig avigheighg fddqgakydg dgnmqdwwtd ddraefgkrt
      541 kalidqynvl spadlsdeht vngeftigen igdlgglsia laaykisldg eepqvidglt
      601 glqrvfygwa qvwrtkarqe eairrlavdp hsppefrcna vvrnidsfye afevtpddkl
      661 ylapeervti w
//
LOCUS       WP_181698484             262 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardia sp. GTS18].
ACCESSION   WP_181698484
VERSION     WP_181698484.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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..262
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..262
                     /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=28329
     Region          30..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 mseavipaap vdathdplpl tgertvpgia eenywfrrhe iayarllahc tgktvleags
       61 gegygadmia gvaqrvigvd ydegavahvr aryprvemiq gnladlpldd esvdvvvnfq
      121 viehlwdqaq flreclrvlr pggrllistp nritfspgrd tplnpfhtre lnaaeltell
      181 veagftvsam lgvhhgdalk aldakhggsf idaqierala gepwpadlta dvaavtiddf
      241 dlregdidas ldlvaiaeka rr
//
LOCUS       WP_181698577             311 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase family protein
            [unclassified Nocardia].
ACCESSION   WP_181698577
VERSION     WP_181698577.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nocardia
  ORGANISM  unclassified Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 311)
  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 311)
  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..311
                     /organism="unclassified Nocardia"
                     /db_xref="taxon:2637762"
     Protein         1..311
                     /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=34414
     Region          22..288
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mrdqtlnpdl aglsrtvrss rpfdvgltva plrrgmgdpc hrtdpdgshw hasrlpsgpv
       61 tyrltqdgrd gvharawgpg aeeflsgldr mlcleenved fapehpklve ahrrvpglrm
      121 lrtglvlesl ipaileqkvh tkssfaayrt lvrefgtkap gpgdlmiapd adtwrripsw
      181 kfhranvgpq raqtivraar vadaiertar ldpreaatrl rsipgigvwt vaetaqrafg
      241 dadalsvgdy hlaatvgwsl lgrpidddam vayleplrph ryravrllml sgqahkpkfg
      301 prtpitdhrd r
//
LOCUS       WP_181698584             309 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Nocardia sp.
            GTS18].
ACCESSION   WP_181698584
VERSION     WP_181698584.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (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   4  (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   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 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..309
                     /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=32984
     Region          3..308
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mqvllagatg aigrpliral tahghtvtai vrnpanhglv relgaeplta dvldrdallr
       61 aldglradav ihqatalrda kpqrripadd ptgllrtvgs ahlleaaelv garrfltqsl
      121 ilgygyrdhg tvplterdtf gvydggvade vvracvsaee qafaapglea ialryglfyg
      181 pgafsdlfgd mmrkhqpvgp rgeggvnswl htedaaaatv aalergvagr aynladdtpi
      241 twgeffrlvr hskqaprpir lplwlirlgv pyiaalmgdt smrisselah aelgwqpkys
      301 svaeglaar
//
LOCUS       WP_181698679             346 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nocardia sp. GTS18].
ACCESSION   WP_181698679
VERSION     WP_181698679.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..346
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..346
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37456
     Region          80..338
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mlrpqqirni glvcldliaa tssgsattvp larlehstve wardgigvea ilhavhrcar
       61 iavdltgaqv yvvdllehta ttvasayvry tlelagrseh akdalanqvi agthsravar
      121 dcgveladey wvlalsiage ptdgpvdgvd ervrarrait rmraeldrrc dgeclvalst
      181 rggtalvpgn idadidvvaa altraagrqv tvavvlsdld evadatecah elleivrrlg
      241 rrggvhrfsd yaleyqltrp gpardhlatv lepltghpel letlrchvan nlnrrrtatm
      301 lhlhtnsidy rikriaeltg ydatrcadlw ylrsalvvsg lhdpaa
//
LOCUS       WP_181698133             407 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nocardia sp. GTS18].
ACCESSION   WP_181698133
VERSION     WP_181698133.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 407)
  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..407
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..407
                     /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=44363
     Region          22..406
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(59,66,95..96,103,107,114,240..241,244,248..249,252,
                     285,290..291,294..295,297,320,347..349,352..353,355..357,
                     361)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(66,89,91,94,96..97,179..180,189,239..240,243..244,
                     248,291,294..296,396)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 madtttaaap vetigadffd dphahyrrwr ttgpvhrvlf pdnvirwivi gypearaala
       61 dsrlrkdtvr adeilrakrd gtptdantmv llqhmlstdp pehtrlrklv nkafttrqva
      121 alrprveeit enlldamdgh devdlmqafa nplpvtvice llgvpfddrd dfqawtrslv
      181 gvvgeeegrp aaaaamaayl sslvrakqsr paedllsqlv ladedgdrlt drelvsmafl
      241 llvaghettv nligngvhal lreptqwaal cadpagvpea ieeflrfdgp vdmatlrfta
      301 epvtlggvei pageivnval aaanrdparf tdpdaltvdg ptsghlafgh gihfcvgapl
      361 arleaevaft allrrfpdlr ladpaatmhw qtstlirgll dlpvrlr
//
LOCUS       WP_181698768             209 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [Nocardia].
ACCESSION   WP_181698768
VERSION     WP_181698768.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     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: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=22521
     Region          41..138
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mkfaerydia apiydrtawf lslggidklh pglvegldlt gkkvadlgcg tglafpalls
       61 avgptghvig vdnnaailak aqkrvdenhw pnvtlltedi aelpvnqdvd vlfsciafsc
      121 vphpsdklae llgnltpgtq vriidalprt sglsryping ynfvksgivg shfrelhpfe
      181 qvfrdrltdv vvdylhggmy trltgvkga
//
LOCUS       WP_181698985             229 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardia sp. GTS18].
ACCESSION   WP_181698985
VERSION     WP_181698985.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 229)
  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 229)
  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..229
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..229
                     /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=25953
     Region          47..149
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mcvvrsqqdv tafyltalas geptaerlsa pvsdrfasfv navdrraprt aldlgygrgt
       61 ytlalaragf qvvavdqvpt hilqarlmgl pdwagrieav qqrienfsit rrfglvvakd
      121 vlhylrqdqv reiltrciqr apagtghfle vftditrtdr rgrrvliede aayaadtfrt
      181 tierlytgwd rhmsltphce rntdsahnyf eanritlray rtidvethr
//
LOCUS       WP_181698682             280 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Nocardia sp. GTS18].
ACCESSION   WP_181698682
VERSION     WP_181698682.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 280)
  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 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   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 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 10793067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..280
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29347
     Region          5..275
                     /region_name="PRK08278"
                     /note="SDR family oxidoreductase"
                     /db_xref="CDD:181349"
     Site            order(17,19..20,22,41..43,101..103,151..153,168,172,
                     198..201)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187663"
     Site            order(125,153,168,172)
                     /site_type="active"
                     /db_xref="CDD:187663"
ORIGIN      
        1 mttstsplag rtmimsggsr giglaialaa arqganiall aktdvpdprl pgtihtaaae
       61 ieaaggqala vvgdvrdeas vteavrrtve rfggidycvn nasaialapt eelpvkrfdl
      121 mqqiqlrgty lltstclphl rrsdnahils lspplnlapa wlgvhpaymv akygmslltl
      181 gwaaeyaehg vaanclwpet liataavqnl lggdeataka rtpqivadaa iailekdart
      241 vtgntfldve vlraegrtdf sayggsddle ydifvdppqa
//
LOCUS       WP_181699007             515 aa            linear   BCT 28-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Chthonobacter albigriseus].
ACCESSION   WP_181699007
VERSION     WP_181699007.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 515)
  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..515
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..515
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57810
     Region          1..515
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 mlfnsyafvl vflpvtllvf fslgrwsppw arlfllfasf afygywdify lgllivsila
       61 nygigaaitr lrtdapdrak kimlagvaan vallayykyt tfivdnvsvl tgydytvhsi
      121 vlplaisfyt fqqiaylidt wrsqtrpytl vdyalfvtff pqliagpivh hadiipqien
      181 prtyrfrprd favglcffii glakklliad tvgvladpvf dgalvnpptm aaawtavlaf
      241 siglyfdfsg ysdmavglar mfgirvaynf aspyqstsiv dfwkrwhitl sswlrdflyi
      301 plggnrrgrw rrhlnlmitm lvgglwhgag wtfviwgglh glylivnhrw rhfteiaatr
      361 grpivvspvl gwaitmgavg fawiffrapt ldhagvmivg llglnplpps lppetvasav
      421 tpllerpwne iairglrrfa eaypeavllv gagialflpn sqeildrpeg rrplmprlsv
      481 ptfrpthtwa aataflllva lsrmsdvkaf vyfqf
//
LOCUS       WP_181699062             270 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181699062
VERSION     WP_181699062.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 270)
  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..270
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..270
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28223
     Region          29..267
                     /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 mtvpsaqpaa stteiarrae aaariaenag rsamaffear dslvvetkes aqdfvsradr
       61 eveeeirrav aaefpedgll geeygletgr sdfvwvidpi dgtaafvsgq anwcisiavk
      121 gpdgvvigvi aapvfgetff avrgggatln grpiavdpka sltsgnvafg atqkspaats
      181 aafvqrlyee ggvlfrigsg almlayvasa rlagyydpyi nawdcyagiv lveeaggavd
      241 frgsddmmtg gplyagtafv trelrrlaeg
//
LOCUS       WP_181698629             286 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: segregation and condensation protein A [unclassified
            Nocardia].
ACCESSION   WP_181698629
VERSION     WP_181698629.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nocardia
  ORGANISM  unclassified Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="unclassified Nocardia"
                     /db_xref="taxon:2637762"
     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=31135
     Region          14..269
                     /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 mqavpeeavp aetsgfhlrl tnfegpfdll ltlissrkld vtevalhkvt defiaytkal
       61 taelaentkl radkildqtt eflvvaatll dlkaarllps gemtdaddle lleardllfa
      121 rllqyrafkq vaellaelea aalrryprsv aledqfagll pevtlgvdva afaeiaaaaf
      181 rprpiaevgl ghlhmhtisv aeqaelvlar lkergpggwt tfaelvsdct vpveivarfl
      241 allelyrgkt iafdqpdplg plavswlgel dpdaeaaalt feedyg
//
LOCUS       WP_181699216             557 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Nocardia sp. GTS18].
ACCESSION   WP_181699216
VERSION     WP_181699216.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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..557
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..557
                     /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=59715
     Region          28..548
                     /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 msdpvasase saasstaepi gagrterpll rveglrityq sgagpvaalr gasievapge
       61 vvalvgesgs gkstlahavi gllgdsarin sgriefageh vdpedekslr rlrglrvgfv
      121 pqdpglslnp vlrvgdqvae allvhrladr rtarlraldl leevgldrpe qrahqyphel
      181 sggqrqrvli aialacgpdl iiadeptsal datvarqvld rlaeriaarg tavllithdl
      241 avaaeradrl vvleggevve sgpiaqvlah pahpytrrll aaspalaptp frpararaat
      301 pllsvhalhk rfheggitav dnvefsldrg etlalvgesg sgksttaria lrltdadsgt
      361 vtfdghdltg arrkrlralr rrfqvvyqnp yssldprwdv gdiiaeplra fgiedrpqrv
      421 relldqvalp tdftrrkpae lsggqrqrva iaralalrpd llvldepvsa ldasvqaqil
      481 dlldglqsel dlgylfishd lavvcrisdr vavmrhgriv etgptaslft apqhpytrel
      541 laaipapafd idgketr
//
LOCUS       WP_181699296             426 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Chthonobacter albigriseus].
ACCESSION   WP_181699296
VERSION     WP_181699296.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=45146
     Region          1..409
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 maveitelps gitvvthgms hlastalgvw vgagsrseea sengishlle hmafkgtskr
       61 saveiaeeie nvggelnaat sientsyyar vlagdvalal diladilqds vfdpeelare
      121 khvigqeiga aldtpedlvf dffqeaafpg qpigrpilgs vetvtgfsda alksylnrhy
      181 tgsrtviaaa gkvehdelvn lalekfegyp aspppgeana ayrggekree rdlmeaqivl
      241 gfpgtsyyad dyttaqiaas vlgggmssrl fqeirekrgl cysvysfhwg frdtgifgvs
      301 aatgesdaqv lvettldeie raigtiseae varakaqlra gllmtlespa aragqiarqi
      361 lvhgreipld elvekidavt prlvsdylak mvvsasptla aigpiadvpr ldaiasrfgv
      421 apasaa
//
LOCUS       WP_181699304             365 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Nocardia sp. GTS18].
ACCESSION   WP_181699304
VERSION     WP_181699304.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 365)
  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 365)
  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..365
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..365
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=39580
     Region          63..236
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          160..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 mdvllgigtr kglflarsrd grktwevspp qfpvadvkal aidtrsetpr vlagvlnshf
       61 gptlvvsddl gqtwsepdda plafpddtdv alqgvwqikp ateaepdvvy agvepsalfr
      121 sedggrsfel vrglwdhphr tqwqpggggl alhtilphpa dtrrmavams tggvyqttdg
      181 geswrptnkg vtadfmpgel pewgqcvhkv aldaadpdtm ylqnhggvfr stdagerwqa
      241 iddalppsnf gfpivahprr pgviytfplv admdrfrfpp dakcavyrse dggqtwsals
      301 dglpevpfwa avmrdamcad daeptgiyfg trngevycsa degdhwqlva dklpdvlcvr
      361 aavig
//
LOCUS       WP_181699316             598 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Nocardia sp. GTS18].
ACCESSION   WP_181699316
VERSION     WP_181699316.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 598)
  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 598)
  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 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..598
                     /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=63747
     Region          4..>378
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mrvlrpwqqa aydewirkgr sgiveavtga gktvlgvraa idaveagspv vivvpdenvr
       61 drwlaileea mpscrigsla ttsqswqvav ltantvvrlr taglshlral lviddlhryg
      121 agfwptalae hfpyrlgftd tlphsghivd svlrpyfgsv iagcdyarar tdghlapvtv
      181 vhvgleltpk erarlnqaqa lieretdtlt gsygaperse efhgfveqlr rgrgsaahha
      241 nryvqalgdr atllaecrak mdlvrslpig vlsetqtvif agravaagtv aqalgasgit
      301 aamstpsmtp eqrsalaagl rdrstrvfve qrspdesvlv phaelglfla rshdraemir
      361 rlsrfvkqtp asrpcvvvig yvvgsiedpa sgtdgsltsi vhqladnivr tdvaglaqfl
      421 iewvrqvggv aaekdpaeta spsavhsaap ddaytdgvdd vepaedvavd gpeyidlldq
      481 ltkldfvaig devgdligvt dprelleqvh aaadagllty rplgeptddl lllsaavggt
      541 tatreqaata iahwaaesdd pvsdlravms qvgalavpph rliqvaaflr grtpsgll
//
LOCUS       WP_181699386             449 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Chthonobacter
            albigriseus].
ACCESSION   WP_181699386
VERSION     WP_181699386.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=46735
     Region          9..434
                     /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 mdaaprsssa lrvliadada darsvlrsal eeriarplmv metgdaasar vlaagrnfdv
       61 iaadlatlgg phaltpllsa agdttlyalg psedvtsavt avqvgaadyl skpldgaafa
      121 rrverqfgqs eavhaegfdg mlgrsesmrt lfeavgrvap slapvfvsgp tgsgkstlar
      181 vihgrsrrkh gpfvevdctg qesvalcdtl aaiggafdra hggtlhlkei srlspavqal
      241 llrlvdsgev lgsgvrrrls vrlvvstsea vqdgkvpgtl kpdlyfrlav lplrlpalaa
      301 rtediplial ealrraarer garsirllpa aesalmafgw pdnvaglkra cetlaehavn
      361 gvigpeavaa vlapagfvar teatgaaqrp iivrplhlee ariieeaiaa fdgniaraaa
      421 alqispstiy rkrrgregse agyaesaag
//
LOCUS       WP_181699490             214 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181699490
VERSION     WP_181699490.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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..214
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..214
                     /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=23496
     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 mtvlarvlap iaavcvtgfa rvvtgvrgnw fgctpapvpr vyfanhashg dfvliwtvlp
       61 aalrqrtrpv agadyweadr irrflgrevf ravlidrnpa arradpidam vsaldagqsl
      121 ilfpegtrnt tdepllpfka glfhlarkrp evelvpvyid nlnrvmpkge flpvpllctv
      181 tfgaptrlqd gedkasfldr trttlldlrr pggg
//
LOCUS       WP_181699586             389 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nocardia sp. GTS18].
ACCESSION   WP_181699586
VERSION     WP_181699586.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..389
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41740
     Region          10..380
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtraagfcrd dfaqvravfd eqlatgaelg aslcvtvdgd pvldlwggha dpdrtvawqa
       61 dtlvnvfsvt ktmtalcall lvdrgdldld apvarywpef aaegkdrvev rhvlshtsgv
      121 sgwerpiala diydteaaaa rlaaqppwwe pgtasgyhal nyghlvgelv rritgrtlge
      181 ffaaelagpl gadfyigtgp ehadriatlv appqrefdms aldpdsilvk tltsplldia
      241 etatpawrsa elgavnghgn arsvarvqsl vscggelggr rflspaties ifreqadgld
      301 lallaplrfg igyglprpqt yphipdgrvc wwagyggamv vndldrritf aytmnrmapg
      361 vigsdrcdny lkavfdavag tdrsrgrts
//
LOCUS       WP_181699617             687 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Chthonobacter albigriseus].
ACCESSION   WP_181699617
VERSION     WP_181699617.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 687)
  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 687)
  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 687)
  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 687)
  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..687
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..687
                     /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=75191
     Region          1..667
                     /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 msrdrsvqli aksyawviav lgllsvvnav avhstlkmql shsdlamtsn qqvqafiavq
       61 tviaavidta knealpdtrf ervkhrliev aanleqvnad vvaafaateg nivttvpeat
      121 rsayfskpfe larwmehtsg raraiasltr eeivsynnws ptevalasgt tlkgfrqaeq
      181 alkedaklwg araerfhqal tllalltlai eaalifgpli rkvrqeaerl eaahaeievl
      241 afsdgltgaa nrvrfrrals iaceaaskga pfavilsdln rfksvndgfg hqagdqllve
      301 vtnrlrasir pgdivarigg defailapgl dteegvqela laitaevarp whydgfdfdv
      361 sisvgaalcp rdsddpdrll ayadralyes kqeglpvsvf kfedralrdg dsallrglpi
      421 aiargefelh yqpkvrisdg amigaealvr wrhpqhglls pasflpivlr ggrmveltht
      481 ilhlagsnma cwrregidfg riavnipesm ltgrlgfdcl tevldcysld gdlftfeite
      541 dvlfsraaat iqaevenisa agvrisfddf gtgfaslshl rhfrfdelki drsfvseigr
      601 semsekivla lvslaqalgk eivaegvete dqlaflreag ctyaqgylya rpmpaadfea
      661 wtrtytssfq tgrtkpernt alrralg
//
LOCUS       WP_181699736             254 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia sp. GTS18].
ACCESSION   WP_181699736
VERSION     WP_181699736.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   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 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
REFERENCE   4  (residues 1 to 254)
  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..254
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..254
                     /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=25968
     Region          6..239
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          159..239
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 magvtappha sdsaarwrgd avftpgfmaf tgrigdadrh ahaavqvlfv argglvltda
       61 qgqathataa iippgvvhqv taepgtsgfa afldpdsata raalarlagl pgeaatswvt
      121 atsprspesp ldslgaarrr shpavadalr vaagwpggpp slvelaarvg msasrlahvf
      181 taevgsgyaa wrrwtrlqrg ftvvreggsl teaahaagfa dsahltrtcr eligitptea
      241 liatgwrppp aqvs
//
LOCUS       WP_181699799             682 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Nocardia sp. GTS18].
ACCESSION   WP_181699799
VERSION     WP_181699799.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..682
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..682
                     /product="PhoX family protein"
                     /calculated_mol_wt=72659
     Region          47..676
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mslkplalfv thdgqssrsa itceykcgna cfhevpntsd geyfgdivar lnrrglikgg
       61 aaavlavgaa smlaacgdds sdtgsagspg tgtgftpvap nkedavvvpe gyeqsvlirw
      121 gdaviegapa fdfekqtpaa aakqfgyncd fagllpiege adkyvlvvsh eystepmmfr
      181 gynkdaptre qfeialashg lsvvevhgqa gsgqlkpvfg kynrritatt efevrgpaag
      241 sallktkadp tgtkvlgtln ncsggvtpwg tvlsgeenfn qyfgnaekvt dadvakklkr
      301 ygieggaser rwenfdprfd ltqelnevnr fgyvvevnpw dassapvkht algrfkheaa
      361 tihvtadgsv vaysgdderf dymykfvsak kvqpgvgass mrhnmtilde gtlyvakltg
      421 dhaaeidgsg kvptggftgk gewirlletg adgkgksfvd gmsaeevavy trlagdkvga
      481 tkmdrpedfe tnpktgkvyv altnntkrge egkpgpdean prklnkngqv leltdnhtgt
      541 eftwtlllvc gdpaaadtyf sgfdkskvsp iscpdnlafd pygnlwistd gnalksndgl
      601 favvldgpnr getkqfltvp rggetcgpii tekqvivsvq hpgesddatv dkplsnwpdg
      661 gttqprpsva vvwkknggri gv
//
LOCUS       WP_181699811             654 aa            linear   BCT 28-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Chthonobacter
            albigriseus].
ACCESSION   WP_181699811
VERSION     WP_181699811.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..654
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..654
                     /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=69389
     Region          63..654
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mrmgrdfgva rpprraargg grpvlavslv aliaattfga gltpaaafel fgytffedek
       61 eplppdsqpy avevevatpd edveeriras sllwaereed pppstasfls rtraeygriv
      121 aglyadgfyg gtvritvdgk dpetidpdaa lpkpvpvrid vdpgprfafg evaisgrapa
      181 tsdpddqvee tpesfglvpg aiaksgivln seqalieewr qqgypkadie srdavadhps
      241 stldvtiaar sgqraaygpv svtgteymdp afvaymtgle pgveydpddi ekaekqlqrl
      301 gvfassrvve adtvnpdgtl pltvnvaerp rrvigggasy stvdgaglea ywehrnlfgq
      361 aeklrlegrv ggvastdpad ftyhlgatfl kpgvltpltd ltaeisarre pldtytetav
      421 rarvglahef feglsgtval nleaseiedp fgtnqfllls lpstltydar ddelnptsgy
      481 rttlglepff dfkggngalv adlegstyls lsgddsfvla araavgtivg asrdeipasr
      541 lffvggggsv rgygfrnvgp rigdevvggr syveaslevr akvtdsigiv pfvdvgqsfl
      601 ssvpdfsedl kigagiglry dtgigpirvd aavplnpgdd dpafalyigl gqaf
//
LOCUS       WP_181699822             418 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Chthonobacter
            albigriseus].
ACCESSION   WP_181699822
VERSION     WP_181699822.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  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 418)
  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 418)
  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..418
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..418
                     /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=47191
     Region          20..412
                     /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..414
                     /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..206,210,337..338,
                     375..377,379..383,394..397,402,405,409)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176893"
     Site            order(200..201,203..204,206..207,211,307..308,310,318,320,
                     327,329,359,362..363,369..370,373)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176893"
     Site            order(200..201,203..204,206..207,211,307..308,310,318,320,
                     327,329,359,362..363,369..370)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176893"
     Site            order(206,211,373)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176893"
ORIGIN      
        1 mldrstespr tllkrrkpnh sleqafytsp eifdldieai ffrhwiyvgv epdvpeagdv
       61 mvvdigrasv litrgdddvi rafhnvcrhr garlihdpkt tvgklvcryh awtydldgkl
      121 lhadhmgqef dtschglkpv hlkslegllf icladeppad fetmaaamgp ylaphdirnt
      181 kvafqsdlie egnwkitmen nrecyhcagn hpeltvplfe ygfgfspesm deakakeadr
      241 yacmvtdlhg ewegsgfpsa eiehlddmtt gfrterlpid ragesqtldt kvasrkllgn
      301 ltnpkmggls fwtqpnswhh fmsdhivtfs viplspertl lrtkwlvhkd avegvdydlk
      361 rltevwiatn dqdgqlvgiq hsgvispaye pgpyspyteg lvekfvswyc qrlaaylg
//
LOCUS       WP_181699903             360 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181699903
VERSION     WP_181699903.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 360)
  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 360)
  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..360
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..360
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=38901
     Region          45..234
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          154..341
                     /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 msgkvhllvg trkgafifda desrddwsir gpfcdmwpmn hvvgdpatgt iygaggnewf
       61 gpavwkstdl gatwthsseg igyaegetpv ksvwslapkg nrvyagvepa glfvsddgga
      121 sfthisglrd hpsrpewqpg agglilhslv lhpsdenqiw vaistagvfh tadggrtwqp
      181 rnrgtradfm pegqnypeyg qcvhclvmap gkpnrlyqqn hcgmyrsddg gqswesieeg
      241 lpstfgfpaa vhprdpdrly llplngdikg rfvpdakaav wctgdsgntw kdsraglpqe
      301 nayfgvlrqa matdsldpag vyfgtstgel ygsrdeggsw kpiaehlppi lsvetlvlrs
//
LOCUS       WP_181700020             430 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nocardia sp. GTS18].
ACCESSION   WP_181700020
VERSION     WP_181700020.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 430)
  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..430
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..430
                     /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=46035
     Region          13..341
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtaprqhalv igagvaglla arvlaerfdr vtvverdepd akaavrrgvp qawhlhglld
       61 rgrrimeely pgfteeavsd gatvaevlvg trwyvggsrl aagatgltsl iatrslletv
      121 lrrrtlrmpg ielltrttvq gligdaqrvr avrvtgpage qtlaadlivd asgrgsritl
      181 wltaiganvp deerlevdlg yasrffrhrp gqldgqasvi vstgadgrgg gavrvegdrw
      241 hvtlagmlgd hpptddqgfr ayaaslsapd ihtivvgsda lgepvpyrfr tavrrrfdrq
      301 sarpaglvvl gdaqcafnpl yaqgmtvaal qaaalrecld addlparfya saadavavaw
      361 qlaagsdlrn pgvegrrtlr trltdvfvtr vqrvahhdpr vartflrvah lvdppaalta
      421 pgtlrrillp
//
LOCUS       WP_181700045             642 aa            linear   BCT 28-DEC-2024
DEFINITION  ABCB family ABC transporter ATP-binding protein/permease
            [Chthonobacter albigriseus].
ACCESSION   WP_181700045
VERSION     WP_181700045.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 642)
  AUTHORS   ter Beek,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..642
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..642
                     /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=70804
     Region          7..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 mrkipptsdr pksvsaddst lvatvrnlwp ylwpsdrpdl klrvalavla livakvitvl
       61 vpylyawatd alapgsgtdr tmfllsvpam lvlafgvgrl llngfnqlrd alfaevsqya
      121 vrslayrtft hlhalslrfh lqrrtgglsr viergvkgid aivrftilna wptvlefals
      181 aaiiffqfgw tylvvvagtv wlyvwfsvry sdrrisirrr mndsdtdant kaidsllnfe
      241 tvkyfgnekm eadrydasma kyeraavetw tslswlnmgq tviftvgmta cmlmsaravm
      301 ageqtigdfv linsllmqla vplnfigfiy reirqgiadi eqmfgllnqp aeivdsptar
      361 pltvsggrva fedvhfaydp drqilngvsf evpagrtiai vgpsgagkst lsrllfrfyd
      421 vtggrvtidg qdvrdvtqes lraaigmvpq dtvlfndtia ynirygrpsa sdedvqaaae
      481 maqigrfves lpqgyktqvg erglklsgge kqrvaiarti lksppilild eatsaldtnt
      541 ereiqaaldr vsegrttlvi ahrlstvvra deiivlekgr iaergshadl iakgglyatm
      601 wdrqreaaea eerlkkaieg ddigivkrga ragepaalkp ae
//
LOCUS       WP_181700106             633 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Chthonobacter albigriseus].
ACCESSION   WP_181700106
VERSION     WP_181700106.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 633)
  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 633)
  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 633)
  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 633)
  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..633
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..633
                     /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=68143
     Region          27..625
                     /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 msrhhaaspe rgnpapqgst pvaspnivgr tvsvlvgata livaailpwa yysaaewrlr
       61 geieaelklh aqeagiavgq npdlwnalag tepvtrlihl pnqvrgdakn qtgfrlrilr
      121 pdgtpvvdep svqpllwpvi takagflrdl gvmeisgtlr pvlletlkva lgsaflalll
      181 fylvrelpir llnramaran flarhdvltg lgnralfieq leivlgsqrt sqrpaavffv
      241 didhfkavnd thghtagdcl lrafadrlkg avragdtvar lggdefavis tqlgdpgeam
      301 piaqrllait atetdpplpy aerlgisigv cvikadsglt paailknadv alyqakatgr
      361 graclfsael dgqirarrsl eedlqtavre gqfklafqpq vdlrtrriig aeallrwdrp
      421 ghgsvspaef vpvaestgii cdidrwalee acrvaaqlpg disiavnvsp mqfrrddfvp
      481 gviaalyrsg lpahrlelei tegmmlkdgp etfatldlln emgvrvavdd fgvgysslgy
      541 lsrfefdrik idrmfvmkvd sdpsalavvk aviglsqalg fkliaegiet haqaatlirl
      601 gcvegqgfly grpmpaadla dllaspfsra vsv
//
LOCUS       WP_181700144             332 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Chthonobacter albigriseus].
ACCESSION   WP_181700144
VERSION     WP_181700144.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=35691
     Region          22..319
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mdanqpatsp pgsttverer iaevartlek aligrtplve rlmialltgg hilvegapgl
       61 aktravkqls drldasfari qctpdlmpad ltgtpvwrpd agafefvagp lfhnlvlvde
      121 inrappkvqs alleamaerq vtaggvthpl pdpfivvatq npiehegtfp lpeaqldrfl
      181 fhvtvdmpda iaereildlv eretvtppaa agirlsvdev rlarteamrt hlspalkdyi
      241 vrlvtatrdg svgddvkaai ehavsprgtl slaaaakara ylrgrdyatp edvralaadt
      301 lahrlvltwr aaaegdtsrk viarlvdrva pl
//
LOCUS       WP_181700353             163 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Nocardia].
ACCESSION   WP_181700353
VERSION     WP_181700353.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 163)
  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 163)
  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 163)
  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 163)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 163)
  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 163)
  AUTHORS   Rosinski,J.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..163
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..163
                     /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=17562
     Region          80..>144
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdlderleal errvaalegt ahtderlpwa varlraefdd agdrnggvll agalklptge
       61 rvdwqaqyat daivgdiwti eaanclaala dpvrlrllre ivygrrtaad laaiaelgts
      121 aeiyqhlrql aavgwlqtag lgrfevpegr lvpllaalas aqr
//
LOCUS       WP_181700354             265 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Chthonobacter albigriseus].
ACCESSION   WP_181700354
VERSION     WP_181700354.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..265
                     /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=26998
     Region          1..264
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 myqttyhrps slseatslla saseakllag gqtliptmkq rlaapsnlid lgrldelkgi
       61 tvsggtvtig agtthyavst sadvksaipa laklasgigd phvryagtig gsvanddpaa
      121 dypsavlglg atvvtnkrei aaddfflgmf ttaleedeii vkfvfpvptk aayakfanpa
      181 sryamagvfv avtsggvrva vtgagsngvf rwadaerala anfsasaldg ltvdssells
      241 dihgdaayra nlvkvmgkra vtaag
//
LOCUS       WP_181700718             314 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181700718
VERSION     WP_181700718.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..314
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..314
                     /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=32863
     Region          12..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 migrgphpte erpmlaraff nrdsgtmrtl gekdveralv rafqskghai tvsfvagpdl
       61 edairaavse kpdaiivggg dgtvsssaal ladtgialgi vplgtmnlfa rtlglpleld
      121 aaadalasgq rrdadlaman grpfihqlsl glqprmvrlr eragayaskg gkilasaral
      181 glvlrrppsl dlvlvadgke rrletpgivv snnpygsghl pyadrpatgl lgvydvtsdr
      241 wgdlaqlaae ivlgtwqgda nvemttahqv tisagpsqqs saqatvdgel vrvefplais
      301 krpaalkvla pdqs
//
LOCUS       WP_181700360             221 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Chthonobacter albigriseus].
ACCESSION   WP_181700360
VERSION     WP_181700360.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 221)
  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..221
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..221
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=22563
     Region          1..143
                     /region_name="CoxG"
                     /note="Carbon monoxide dehydrogenase subunit G (CoxG);
                     cd05018"
                     /db_xref="CDD:176853"
     Site            order(3,5,7,16..18,20..21,26,30,36,43,45,47,49,54,58,
                     62..64,67,73,75,77,89..91,93,95,104,106,108,110,124..128,
                     130..132,134..136,139)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176853"
ORIGIN      
        1 mdmtgeyrip aprqavweal ndpdvlkaci pgcetlekng demaatvvak igpvkakfag
       61 kvrlenlnpp tsysivgegt ggvagfakgg advallddga gtiltytaka qvggklaqlg
      121 srlidgtakm madqffsaft ekvgaaaaag gvdatevepd ggptvlkeda ldravhtada
      181 verevearve taaiksgpsg pmvwglvtla vlivvlilat r
//
LOCUS       WP_181700806             215 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [unclassified
            Nocardia].
ACCESSION   WP_181700806
VERSION     WP_181700806.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nocardia
  ORGANISM  unclassified Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 215)
  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 215)
  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..215
                     /organism="unclassified Nocardia"
                     /db_xref="taxon:2637762"
     Protein         1..215
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=23089
     Region          6..191
                     /region_name="TerY"
                     /note="Uncharacterized conserved protein YegL, contains
                     vWA domain of TerY type [Function unknown]; COG4245"
                     /db_xref="CDD:443387"
ORIGIN      
        1 mtdsdrtlia vlldrsgsmq tikadteggl aayfeqqrev pkrievtlaq fdttyevvys
       61 nvpldqvppp nllprggtal ydavgklvts vgeelaarpe herpgtvivv vltdghenss
      121 rewthaavks litqqqevyn wtfvflganm davevgsnlg fdpgssitya pvaggvrgaf
      181 dalsaysara qaapagmarr arfsederrr agtds
//
LOCUS       WP_181700978             398 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Chthonobacter albigriseus].
ACCESSION   WP_181700978
VERSION     WP_181700978.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 398)
  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 398)
  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..398
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..398
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=43494
     Region          17..397
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 maaarlstrd digpavrrrl agfvrtlrda gfnvglaetr dalallasad rarlaevrpa
       61 lralfcgrrs dwdafdeifd afwtgsrvks rvamsgtsal asqktartla passaggepg
      121 paadvergvd qpeadaapeg rregasraen lartdfrria dpdalaeaha laerlarrmr
      181 vrltrrdraa argrrldlrr tvraslatgg tplrlvlrrp ryrplrlvvl vdasgsmsly
      241 tgvflrfvhg ildhfreaea flfhtrlvhv sdalrekdta raldrlglma egvgggtrig
      301 dslatfnrwh aarvihsrtv vmilsdgydt gepdrlgaem aalarrcrri vwlnpmigwd
      361 gyepsargma aalphvdlfa pahtleslaa lepylarl
//
LOCUS       WP_181701025             224 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Chthonobacter albigriseus].
ACCESSION   WP_181701025
VERSION     WP_181701025.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..224
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23448
     Region          8..193
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 maslkhlvif dcdgvlvdse ilsrrafadv lqaagvpatp dmvtpytgmk qpdilagiar
       61 etaseihpdv pgrlwpamqa lfreeltava gvaaflerld lprcvasssh perireslei
      121 tglahffade avfsshqvkh gkpapdlflf aaaqmgappe rciviedsva gvtaakaagm
      181 rvigfagash adathralla aaaptalves yeaavallsd wtag
//
LOCUS       WP_181701149             320 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [Nocardia].
ACCESSION   WP_181701149
VERSION     WP_181701149.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     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=35371
     Region          12..303
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtmplnvtvq rsdavlrelg rvvvgkrdem qlimiavlsg ghvliedlpg lgktliarsf
       61 aaalgldftr vqftpdllpa dllgstiydm ssgrfnfrrg pvftnvllad einrtppktq
      121 aalleamaeg qvsidgetyl lpqpfivlat dnpieyegty plpeaqldrf aiqlrlgyls
      181 eqdetqmirr rlergstppq vgqvvdaqgl memrqsvefv tvhpdvvnyv valasatrsh
      241 pqvevgaspr aeldlvqmsr aralllgrdy vipedvkala vpamahritl rpemwvrrir
      301 gedvitellr rlpvpratst
//
LOCUS       WP_181701012             361 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Nocardia sp. GTS18].
ACCESSION   WP_181701012
VERSION     WP_181701012.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 361)
  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..361
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..361
                     /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=37173
     Region          14..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 msarlrtplt eligiehpvv qtgmgwvagp rlvaatanag glgilasatm tfeeleaava
       61 ktksltdkpf gvniradatd aperiellir eqvrvasfal apkkeliarl kdagvvvips
      121 igaakhavkv aswgadaviv qggeggghtg pvattlllps vldavdipvv aaggffdgrg
      181 laaalsygaa gvamgtrfll tqestvpdav kqeylarglg dtvvsvkvdg mphrmlntel
      241 verlehsggw rglsaavgna akfksmtgmk wstlmrdgla mrktkdlsws qvvmaansam
      301 ltkaglvegr tdagvlpagq vtgiidslpt vaelidgivt daltriaavg tlvdtpvteq
      361 s
//
LOCUS       WP_181701192             258 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF1223 domain-containing protein [Chthonobacter albigriseus].
ACCESSION   WP_181701192
VERSION     WP_181701192.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..258
                     /product="DUF1223 domain-containing protein"
                     /calculated_mol_wt=27211
     Region          16..255
                     /region_name="COG5429"
                     /note="Uncharacterized conserved protein, DUF1223 domain
                     [Function unknown]"
                     /db_xref="CDD:444181"
ORIGIN      
        1 mmiedlprtv ttctravslc caalvfsgpv alageteavv elftsqgcss cppadstmae
       61 lardpkvlal tfavdywdyl gwkdtfarpe fskrqrqyaa argdsavytp qavingqadv
      121 vgsdgdkirk tiaslkasgg gltvdvkarv agdriiveip agtppaqgvs avwiaayrap
      181 esveigqgen sgrkvtytnv verwqvlgmw dgqamtvelp ladivqedta gcavilqskr
      241 drkpgailga tkidlsgs
//
LOCUS       WP_181700947             488 aa            linear   BCT 28-DEC-2024
DEFINITION  DHA2 family efflux MFS transporter permease subunit [Chthonobacter
            albigriseus].
ACCESSION   WP_181700947
VERSION     WP_181700947.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Colmer,J.A., Fralick,J.A. and Hamood,A.N.
  TITLE     Isolation and characterization of a putative multidrug resistance
            pump from Vibrio cholerae
  JOURNAL   Mol Microbiol 27 (1), 63-72 (1998)
   PUBMED   9466256
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Lomovskaya,O. and Lewis,K.
  TITLE     Emr, an Escherichia coli locus for multidrug resistance
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 8938-8942 (1992)
   PUBMED   1409590
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR00711.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..488
                     /product="DHA2 family efflux MFS transporter permease
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=49436
     Region          5..409
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(9..10,13..14,17,49,99..100,102..104,107,127,
                     130..131,134,257,260..261,264..266,269,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtigassmaf idgsvvpial saiqrdlsad fatlqwivni ytlflgalvl vggaygdrlg
       61 rrrvflagti lfvaasvacg lapnaialva araaqgvgaa lmvpqslali aatfpeetrg
      121 raigtwagas alttalgppl ggflmdtlsw ravflvnlpi glvvlwlsrg vpesraanag
      181 padllgglla tgglgaltia lvylpdrtit dplvwggflv favaapafia weartaapmm
      241 plrlfrdrif sgvnlltlll ygalggalfv vpytltglrg ytgaeaglal lplalaigll
      301 trffgsigdr vgtrlpmaig amvvavsigw lgateaagsy wtglfgpilg igigmsiaia
      361 pltttvmnav dqtesgaasg innaaariag llavaltgal mvgvfssell slpltpgvdp
      421 gvlssiaera drllqaadgm pgadasrsav eqafsaafra amvlnallai aaailaislp
      481 hkpaarvt
//
LOCUS       WP_181701193             362 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CaiB/BaiF CoA transferase family protein
            [unclassified Nocardia].
ACCESSION   WP_181701193
VERSION     WP_181701193.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nocardia
  ORGANISM  unclassified Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 362)
  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..362
                     /organism="unclassified Nocardia"
                     /db_xref="taxon:2637762"
     Protein         1..362
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38878
     Region          3..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 msttgqgpla gikvielagi gpgphaalll adlgadvvrv qrprqlpgfi erpqwrgrti
       61 veadlknpad vakvldlvek advllegfrp gvtermglgp ddalarnprl iygrmtgwgq
      121 ygpmadragh dinyisltgv lnaigrkger pvpplnmvgd fgggsmflvt gvlaalvera
      181 tsgkgqvida amvdgalals hfvwgmrgvg lwsdergenl ldtgmafydt yetadgkyma
      241 vgaiepqfye qllaglgidp eglpqqldpd gqeqlrklft ekfksktrde wtaifdgtda
      301 cttpvltfte atqnehirar eglieiedvv qhapaprfsr tqggtptppp saatpiedvw
      361 aq
//
LOCUS       WP_181701361             316 aa            linear   BCT 28-DEC-2024
DEFINITION  cell division protein FtsX [Chthonobacter albigriseus].
ACCESSION   WP_181701361
VERSION     WP_181701361.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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
REFERENCE   3  (residues 1 to 316)
  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 316)
  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..316
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..316
                     /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=32549
     Region          31..312
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 msaaapaedd aatrsepsrt rtpivppqti agraltlvia imtflaslti gavtmvdaaa
       61 rawqsdigre vtievrpldg tditaelska aalagefpgv asaralsdee trrllepwlg
      121 agvdlaalpv prlvvvtvdd palfdvagls eavrtqiqgg slddhaawvd rlramagsmv
      181 avgiavlvlv lvamvlsvvf atraamagnr qiievlhfcg aedrfiagef qhhflllgir
      241 ggliggglal vlfialailf ressglpgaa qmdtllggls iglpgflgiv vlvgavavlt
      301 aatsrlavrr slatie
//
LOCUS       WP_181701324             415 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Chthonobacter albigriseus].
ACCESSION   WP_181701324
VERSION     WP_181701324.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 415)
  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 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 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..415
                     /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=45265
     Region          21..386
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 msaphdnqas vssaeptrqp kapipvtvlt gflgagktsl lnrlvqdraf qhaafvinef
       61 geigldhlfv eakddgivel asgclcctir gdlvatlenf lrgldngrle ridrvviett
      121 gladpapvlh timahpylvm ryrldgvitv vdavngdatl daqaeavkqa avadrivltk
      181 tdlaagaara paliarlral npaapildaa kgeaegralt dtglwnpdtk sadvarwlne
      241 eayldrrpat shgpddhdhd hghhhhhnhg qshhhghdha hdvnrhdahi rsftlaadqa
      301 lpagslemfl dllrsahgpk vlrmkgivri aedperplvi hgvqevfhpp vrlerwpdgd
      361 rrtrlvfitr dlpegfvrrl fdafagvlrp dtpdrqsmte nplalsgfta psarr
//
LOCUS       WP_181701416             160 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Nocardia sp. GTS18].
ACCESSION   WP_181701416
VERSION     WP_181701416.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 160)
  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 160)
  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..160
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..160
                     /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=17284
     Region          1..145
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 middldsver rawgavvtla mrvpsvldsr lqrefglthf eyrvlallqd spshrmrlsm
       61 laarghgsis rvshvvskle rvgfvrrvav ttgrgvdavl tpnglakvve atpdylvair
      121 rlvldgldea qkaelavlae klshhligml gdspvgetag
//
LOCUS       WP_181700612             264 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Nocardia
            sp. GTS18].
ACCESSION   WP_181700612
VERSION     WP_181700612.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. GTS18
  ORGANISM  Nocardia sp. GTS18
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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 264)
  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 264)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 264)
  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 264)
  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 264)
  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..264
                     /organism="Nocardia sp. GTS18"
                     /db_xref="taxon:1778064"
     Protein         1..264
                     /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=28321
     Region          12..252
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mtwntddast alrvlavdde kpaldelvyl lneqvgvgev hgaseatgal rvlrahpvda
       61 vfldidmpgl tgmelagils efaeppavvf vtahddhava afdlgavdyl lkplraarla
      121 eavrriaaar aavpasppeq thpsevipve lggvttlvhr advawveadg dyarlhtrtg
      181 shlvriplta lesrwegagf lrvhrsylva lrlvtglrst gsgtvvclra egasgavelp
      241 vsrrqvrelk qrlvhgprqn wsqr
//
LOCUS       WP_181701451             274 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181701451
VERSION     WP_181701451.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 274)
  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..274
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..274
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=29816
     Region          6..272
                     /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 mpfsseelad litilrdaak aevlprfarl gaddvkaksh asdlvtiade aaerfiearv
       61 karygdvlfv geeiferdks ivdrlataer aividpidgt fnyangipaf amiaavvegg
      121 etvagvlydp irddwtsair gggsflegpn qprravrvam paplgemhga vswsyteepe
      181 rsrilagmgr fwgtyqyrcg gqemkmiveg gghfalygkl spwdfaasal ihreaggysa
      241 rfdgspyrpe hrtgglilap deaswhlire tllg
//
LOCUS       WP_181701449             743 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Chthonobacter
            albigriseus].
ACCESSION   WP_181701449
VERSION     WP_181701449.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=76336
     Region          14..738
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mnslplqqqr phvfdvrgmt caacaariet vlaktpgvag atvnlalera dvlldpgtdd
       61 svvveavdra gyeatprasd paerrrqrea eevarraayr stlaiftvsa lltapflgqm
      121 vamatggghw mspwlefala svvqavagar fyrgatkalr ggsanmdvlv algttaawaf
      181 sawmviargh haaghlyfea satvltlvll gklleeraka gttaavralm alrpdkatrl
      241 rdgveetvai eavaagdlvl vrpgeripvd grvetgegha deslvtgesv pvvkhpgdav
      301 iagsingega lvlrvsatge dtalaritrl vesaqsgkap iqmlvdrisa ifvpvvlgia
      361 vvvlvgwlia gagletalva avsvlviacp calglatpta lvagtgaaar agilikdidt
      421 leravavdav ifdktgtlta grpalvsiaa asgqteetvl aaaaavqhfs ehplakavte
      481 aaaaraidmp ratgfrslta rgvlatvegr rvavgnaall selgiepgpl agahrqfeaa
      541 artavfvaqg dhvigvlgla dpvrpearqa vadlrergie srmltgdnag vaaavasels
      601 lsgwrgpvrp edkasevqal qkagkvvamv gdgindapal aaadvgiamg tgtdvameta
      661 svtlmrpdpr lvaaaldiar atrakirqnl fwafaynvig iplaafgllt palagaamal
      721 ssvsvvtnag lltrwkpqlr tld
//
LOCUS       WP_181701579             446 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Chthonobacter albigriseus].
ACCESSION   WP_181701579
VERSION     WP_181701579.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 446)
  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..446
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..446
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47750
     Region          33..375
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrspwwrpag llsvspavif lwnallqpgt pvgiethvla dpyeenvevr lyvgvgasdd
       61 gddrqlahfv ehlvflkdrp peafrplalp gvsnnaftta tqtffifrgg sddlpemvda
      121 aaavldpldv dpdqarrerk vvareldwry rtdpfgglnq qitaalyagh pfgraaeldr
      181 idldgltlee aaafhqawyt vpnahlvitg avdptearrl aaaafasrps appperpalg
      241 slplpggaer isvvvegier prlriaaiap vsgdaaslqa daevlnrvlg gnlpgalatv
      301 lrddngmtla sgvdirffvp mpgwvhldid vtlavgadaa dvefktrswl gghraamide
      361 tafyrmrara vreaeqmasd vsargadlgt amamlppdta lgwgrslgea gpltarrilr
      421 aiadphrivt gwmmpgstpt tvgavq
//
LOCUS       WP_181701592             213 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Chthonobacter albigriseus].
ACCESSION   WP_181701592
VERSION     WP_181701592.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 213)
  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 213)
  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..213
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..213
                     /product="LolA family protein"
                     /calculated_mol_wt=23241
     Region          33..211
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mtitgrlcgt lttlaaalvc allatatvaa pnlaglnpeq rasldainny fnsirtiegk
       61 fvqtgpdggq vtgyfvidrp gklrfryypp aqldiiadgr tvaiddkklq eqtlvllset
      121 plrflvsqnv dltqeaviqe vsadadlitv vmedtalygs grltlifdsr tielkqwtvt
      181 daqgldttva lyevktgtet npkwfeinys kyk
//
LOCUS       WP_181701984             375 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Chthonobacter
            albigriseus].
ACCESSION   WP_181701984
VERSION     WP_181701984.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=40648
     Region          1..363
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mipflelgsa yrelkseidd avsrvlssgs yilgkevadf eeqfaaycea eacigvgngl
       61 dalhlallav gvgpgdeviv pshtfiatwl avaqcgakpv pvepdsrtfn idperieqal
      121 tdrtraivpv hlygqpadld pilsvarkhg lkvvedaaqa qgasykgrri gghgdavsws
      181 fypvknlgai gdagavttnd peiarrlrll rnygsevryy ndeigynsrl dpiqaailgv
      241 klrhldawna rrqvladmyl dslrdcielp ttipftrsvw hlfvvrhpkr delqrrlaea
      301 gvgtiihypv achqqkafad rgfrasdlpi aqklaetvls lpmgphlsta dcaaviervk
      361 stvaqmgepg apsga
//
LOCUS       WP_181701542             274 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181701542
VERSION     WP_181701542.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 274)
  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..274
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..274
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27995
     Region          20..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 mtststdlds rfvslqgvmr qagilalegf rkaksvptam kgpqdyltet daaverllrr
       61 elaalhpgdg figeeegggp agnvwvadpi dgtanfargi phfcislafv gdgvtelgai
      121 ynpaleelwl arrgagasln gapiavadtr dfqaasielg wstripntay ldvagdllal
      181 ganvrragsg alglayvadg rqdgyaelhm npwdclagll lvaeaggrvn dflangsgla
      241 sgnpvlavtp alaasvsaat giplapdatv draa
//
LOCUS       WP_181702042             124 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Chthonobacter
            albigriseus].
ACCESSION   WP_181702042
VERSION     WP_181702042.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..124
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13624
     Region          7..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvaanwnaye aecptravld riadkwtvll lgllaerpmr fnelrrhvdg lsqkvlsqtl
       61 kslerdglvt rrafatvpvt veysitplga slaettnalr lwaeahmdtv vasqaaydrr
      121 gada
//
LOCUS       WP_181702075             356 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Chthonobacter albigriseus].
ACCESSION   WP_181702075
VERSION     WP_181702075.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=34901
     Region          41..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 mtvaamssrt rpagdrsrra aavtaasaal avaaavlsla igptgvdlgh laaylggepi
       61 aerdriilea vrlprmalga lvgaglavsg ammqglfrnp ladpglvgvs sgaataavaa
      121 ivlgggvlap iagllgshfl plaafvggla ntvllyvmat rggrtstttl ilagiavgsl
      181 agaltglfif gaddaalrdi tfwslgslgg atavkvlavl pfvaaalati pfvargldgl
      241 algeaeamhl gvsverlkrv vilavaassg atvavtgaig fvgivvphll rlaigpghrf
      301 llpasafgga alllladtvc rvvvapaelp igivtaliga pvflaillnr ptedag
//
LOCUS       WP_181702093             278 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181702093
VERSION     WP_181702093.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=30974
     Region          20..>165
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqrlriyqsl waaehgrpgv ppepleeifn rvkaagyhgl aidlgvapve aarvavphya
       61 rtglgglvta fprsieglrp alhlakdiga pfvvvvgqim pvtvegmipv irdwlkvsae
      121 egmpiqfeth rncitndlfs tlqlldaipe mrlaadlshy vvdremklpl fpdlpaqvsr
      181 ilarsdsfqg riasrnqiql qidfpqhqkw vdlfkgwwae gfrawrarap edaelvflce
      241 lgppeyaitd sngeelsdrw aealviaewa reifakag
//
LOCUS       WP_181702245             407 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Chthonobacter albigriseus].
ACCESSION   WP_181702245
VERSION     WP_181702245.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 407)
  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 407)
  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..407
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..407
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45545
     Region          15..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 mnneavvipp ssrlpenvvh farllrragm pvgpasvvea veamtiagvg sredvywtlh
       61 aifvtrrehh ilfdeafrtf wrsrglvekm lqvfspvapp rapldkpkag aarlahalfg
      121 daaadrqver peveidarft vsdreilqkk dfaqmsadei alalqavrgl vmpvdkvpvr
      181 rrmaaprare idlrrtmqas lraggaiipl afrepkqvhp pivalldisg smtqysrlfl
      241 hflhalsstr rvttflfgtr ltnvtrqmrm kdpdealiac tnhvvdwsgg trigealhlf
      301 nkewsrrvms ggpivllitd glerddvagl aqetdrlhrs crrlvwlnpl lrfegfeara
      361 agvkamlphv defrpihnld avkdlcgala gddakrfdpr kwlrqia
//
LOCUS       WP_181702248             305 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Chthonobacter albigriseus].
ACCESSION   WP_181702248
VERSION     WP_181702248.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=33584
     Region          10..290
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msidspasid dtlalltrgg yvadralatv lflslkmqrp lflegeagvg kteiakvlaa
       61 tldrplirlq cyegldlssa vyewnyaaqm veiriaeasg vedrgeiasd vfsekflikr
      121 pilkaleptv dgrapvllid eldradeafe afllevlada qvtipefgtv raptppivii
      181 ttnrtreihd alkrrclyhw vdypdverem aivrtkvpka pdllarqvva fvqklremdl
      241 fkvpgvaetl dwatalaeld klaldpetvs dtlgvllkyq ddiarvktsd lgrvveeakg
      301 ralag
//
LOCUS       WP_181702320             392 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Chthonobacter albigriseus].
ACCESSION   WP_181702320
VERSION     WP_181702320.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 392)
  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 392)
  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..392
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..392
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=44968
     Region          1..392
                     /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 mfltfftdlr tagvpvtlre yldlmgamea dlaerrvedf yhlartvlvk deahidrfdr
       61 vfvrlfkgld lmsdavdvat lptdwlmkla ekhlteeekr rvealggfdk lmetlkqrla
      121 eqkgrhqggs kwigtagtsp fgaygynpeg vrigqdesrh rravkvwdrr efkdlddtve
      181 igtrqmkval krlrrfarhg apeeldlsst idatarqgwl dvklrperrn airlvlfldi
      241 ggsmddhvri tselfsavks efkslhhyyf hnclyegvwq anarrhgeri ptaellrtfp
      301 qdtrvvfvgd aamspyeith aggsvehwne epgavwlara vaawpklawi npvderqwdf
      361 thstrilrai vgermypltl egleratral gr
//
LOCUS       WP_181702338             364 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Escherichia
            coli].
ACCESSION   WP_181702338
VERSION     WP_181702338.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 10169520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..364
                     /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=39178
     Region          15..362
                     /region_name="THR_DH_like"
                     /note="L-threonine dehydrogenase (TDH)-like; cd08239"
                     /db_xref="CDD:176201"
     Site            order(51..53,56,169,173,193..198,217..218,222,238,
                     261..262,264,284..285,308..310)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176201"
     Site            order(51,53,81,169)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176201"
ORIGIN      
        1 mkinrivneg fmktmlaayl pgnstvdlre vavptpginq vlikmkssgi cgsdvhyiyh
       61 qhrataaapd kplyqgfing hepcgqivam gqgcrhfkeg drvlvyhisg cgfcpncrrg
      121 fpisctgegk aaygwqrdgg haeyllaeek dlillpdals yedgafiscg vgtayegilr
      181 gevsgsdnvv vvglgpvgmm amtlakgrga kriigvdmlp erlamakqlg vmdhgylatt
      241 eglpqiiael thggadvald csgnaagrll alqstadwgr vvyigetgkv efevsadlmh
      301 hqrriigswv tslfhmekca hdltdwklwp rnaithrfsl eqagdayalm asgkcgkvvi
      361 nfpd
//
LOCUS       WP_181702494             164 aa            linear   BCT 28-DEC-2024
DEFINITION  YcbK family protein [Chthonobacter albigriseus].
ACCESSION   WP_181702494
VERSION     WP_181702494.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..164
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..164
                     /product="YcbK family protein"
                     /calculated_mol_wt=17906
     Region          <59..154
                     /region_name="YcbK"
                     /note="Uncharacterized conserved protein YcbK, DUF882
                     family [Function unknown]; COG3108"
                     /db_xref="CDD:442342"
ORIGIN      
        1 mrrlavaalt vlsilawssa slagtreele glddevaaea edapelaqrt lvafvhqtrt
       61 vrsscltpkl ravlgklrdq fgrqiiltsg yrppgrarpg syhrrcmaad iqipgvapsr
      121 laraarnlag iggvgtycht rsvhvdvgpr rdwawgcrkk krrr
//
LOCUS       WP_181702570             336 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Chthonobacter albigriseus].
ACCESSION   WP_181702570
VERSION     WP_181702570.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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 336)
  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..336
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..336
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35987
     Region          32..326
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msapriagta adpdqivada eaavarivaa rdaiarvifg qesvverali tvlagghgll
       61 vgvpglaktk lvetmgtvlg lserriqftp dlmpsdilgs evleqaadgs rafrfvrgpv
      121 faqllmadei nrasprtqsa llqamqerhv tvagqrhdlp epfhvlatqn pleqegtypl
      181 peaqldrfll qidvlypdrq serrillett gaeearaerv lepaeiialq klvrrvpvge
      241 svveaildlv rsarpdsgig rhsnaiawgp gprasqalml tvraralaqg rlapsiddvk
      301 alaepvlqhr maltfaarad gvgvrdviad ltgrig
//
LOCUS       WP_181702587             299 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Chthonobacter albigriseus].
ACCESSION   WP_181702587
VERSION     WP_181702587.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 299)
  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..299
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..299
                     /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=32271
     Region          2..266
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mvrlvhlsdp hlgplpqasv sdlaskrilg yinwhrnrai amrgdllsrl veavraeepd
       61 hvavtgdlvn ialpaelepa rrfletigpg advsvvpgnh dayvpgavak ateawraymq
      121 gdhdpgapsw pfvrrrgdla iigvstaras apfmatghvs vrqatlladk lralrheglf
      181 rvvlihhppi rgstdwhkrl iggsrvraav raegaelvlh ghthlatrle ldgphgavpv
      241 igvpsasqep gghlpgagfn vfeidrtnrg wqlmmrarqa lhpggsfeet eeivwtlpa
//
LOCUS       WP_181702594             318 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181702594
VERSION     WP_181702594.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..318
                     /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=34517
     Region          18..316
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mtiveadver gaaegvgria vainakagaa rasdrrmlkd rireavepig tlqeivfvep
       61 rawmrtlqaf adrpdidtvi vgggdgsiss agqvfvgsgk tmgviplgtf nlfarslrip
      121 vgfdaalaal asarieavdt gsmtdglgre hvflhhvsfg ahphfievre ampygsrigk
      181 mlaslrvwgr tlrsleqvpl sfggdlqrik aryfqvavtv gsfregfgdf phaedltlgd
      241 ldvvllparg rwdfvlaait aalgrwrsns rlevqpvrnl tvashrrhlk vsidgelrrl
      301 pptltfrvqp kslkvlrg
//
LOCUS       WP_181702767             250 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Chthonobacter albigriseus].
ACCESSION   WP_181702767
VERSION     WP_181702767.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=26581
     Region          2..233
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrlalvtdih anlealsavl ddveaegvdr ivvlgdivgy gadpgpcvea vadlvdkgav
       61 allgnhdqaa flgpkgmset aatairwtip klgddhirfl kslplahheg dalfvhasah
      121 hpeswpyvme asdaaasfas tdarvivsgh thvpalfhti agalstgkml sfrpvadkav
      181 plspirryha vigavgqprd gdsracwgly dldgneitwr rvpydveaaa rkiehsglpe
      241 rlaarlftgr
//
LOCUS       WP_181702922             410 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Chthonobacter albigriseus].
ACCESSION   WP_181702922
VERSION     WP_181702922.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=42909
     Region          1..409
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrtlivgagl vgvaaahall degheveivd regfaagasf gnagwiahad ilplaspkaw
       61 anlprwladp lgpltirpsy lpklmpwlir falasrpaei etgiagiaal ntralpawer
      121 rldglvlshh lrrrgilhiw rdaglfaaag kvfdrqsgfg irldrldaag vrevepalan
      181 giaggvlygd gchvsdparl tqdlgvaalg rgarltvgaa raieptsnga tlvltdgrrl
      241 sadrivvaag awsralaatv gdrvpldter gynvtlapgt lglsrpvaye gegfvttpld
      301 sgdrvggave fagleaapny arvdamlgrl krvlpevdtn ggtrwmgfrp sipdslpvig
      361 psrasphvvh afghghyglt qaavtadiva alvagrtppv dpapysprrf
//
LOCUS       WP_181702560             430 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome b [Chthonobacter albigriseus].
ACCESSION   WP_181702560
VERSION     WP_181702560.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 430)
  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 430)
  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..430
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..430
                     /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=48227
     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 msghstyepr tgvekwidtr mpivrllhdt gvsyptprnl nyfwtfggil tfmlvvqilt
       61 gvvlamhyaa dsklafesve aimrdvnwgw llrylhanga smffiavyih ifrglyygsy
      121 kaprellwil gviilllmma tafmgyvlpw gqmsfwgatv itnfftaipv igqpiqtlli
      181 ggfavddatl nrffslhyll pfmifgvvil hiwalhvtgq nnptgvdvks tkdtvpftpf
      241 atmkdglalv wflvfylwfv fyqpnflghp dnyqvanplv tpahivpewy flpfyailra
      301 itfdigpins klggviamfg siailvflpw ldtskvrsar yrplykiffw vfavvcvflg
      361 wlgsrpaegt yvamaqaata yyfahflivl pllgfletpk plpvsilddv lakngghghp
      421 agataapdkh
//
LOCUS       WP_181703033             355 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Chthonobacter albigriseus].
ACCESSION   WP_181703033
VERSION     WP_181703033.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..355
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..355
                     /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=37044
     Region          1..349
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mnfssdnwag asapvaaaln avnhglaaay gaddttrtvs dwfaeiferp vtvffvstgt
       61 aanslalasv mrpggavich rnahvavdeg gapeffsgga klvpvdsarg kltpegvrsa
      121 iarfqppavh hgrpvavslt qatewgtvys paevaaiagi ahqaglkvhm dgarfanalv
      181 slnvtaaemt wkagvdmlsf ggtkngcwca eavilfdpqs addfayarkr agqlfsksrf
      241 vaaqfqgyfd rghwldnavh anamagrlaa gisaapgarv lfqpeanevf aiwsaktsqa
      301 lkaagalfye wpadglppad vpgegevlvr lvtsfattkh dvaefirvlm tgsav
//
LOCUS       WP_181703063             353 aa            linear   BCT 28-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Chthonobacter
            albigriseus].
ACCESSION   WP_181703063
VERSION     WP_181703063.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..353
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..353
                     /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=38811
     Region          8..322
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mtdtpvhtaf qslpivdisg laspdeadrk dvavtlgkaa rdcgflyitg hgidrdlrnr
       61 lltqaktffs lpheekmkvy iglsdnhrgy vppgeegfds qkpdskegfd laidlpsdhp
      121 avvagtpmcg anqwpdlpgf redvtayyea amslgrrlar alavaldvpe dtferhvnvp
      181 vsqlrllhyp fdpdqpedrp gigahtdyei ftillptapg levmngdgqw idappvedaf
      241 vvnigdmlev wtngalvats hrvrkvkaer ysfplffgcd fntlveplev frkpgeptry
      301 qplyagehlw aqtmqsfayl kkkletgels lpegsmalss fgqeakhgaa apt
//
LOCUS       WP_181702818             429 aa            linear   BCT 28-DEC-2024
DEFINITION  TadE/TadG family type IV pilus assembly protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181702818
VERSION     WP_181702818.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 429)
  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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15210410
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..429
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=46058
     Region          4..>65
                     /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          <276..392
                     /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 mntfskdrrg stavvlaval pvlimatgsl ldyssaysvr dkaqkttdaa vltiakmrfd
       61 ansktkgdkg kgavkkmlke avsddlefdv evgenlesge rtitvhaktv vrtdfmrlfg
      121 qpeiainvss taqyrddnya aeiafvintg atmmtarkst alhdalnatl dqfssinaad
      181 edrvrvavvp fqsgvtvpyv dmdsfyygnd fpdppslaah qanlfnasin mfptrcvver
      241 aypfetsiap vsasiasryr vvfdvvdpav pcpnativpv ttdfeavrst vatfnfdsgt
      301 ngavglvwgw nmltpdalfs esgniplgpd hkslkrilly itdgentatl snqtpsvvdd
      361 haltlctkik additivtin idgagseall kacasspdry kkvpapelpk vleglagdls
      421 gytpvrlmn
//
LOCUS       WP_181703189             320 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181703189
VERSION     WP_181703189.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=35506
     Region          5..242
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mnkailvvgg agfigthllr rlkreggrdl isidrrdpkr pvdgvtyika dvrdlsalaf
       61 eqpietiynf aavhttpghp dpeyyetnvl gaaevtalae rhgvddivft ssisvygpge
      121 dtkteetppa pvsaygwskf laerihrawl drapqrrlvi crpavifglg eggnftrlak
      181 lmkrgvfvyp grkdtikacf yvedlveaiq yahdqkrrfv lfngcypdry tleqiveafr
      241 arhftkartv mvprqavtga asalrpfsvm glgihpdrvt klirstdvvp gwlthegkat
      301 agrlpsaldr waadsdgrfd
//
LOCUS       WP_181703352             393 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181703352
VERSION     WP_181703352.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 393)
  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..393
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..393
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41920
     Region          11..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 mkgtvslete taaagllegi vvldmsqfls gpfaalrlad lgarvikier pdggdlcrrl
       61 ylsdteiggd stlfhainrg kqsfaadfkn padiaavral iaradvviqn frpgvierlg
      121 ldyasastln pgivyasitg ygsngpwrsr pgqdllaqar sglmwlngda dqgpvpfgla
      181 vadllagnai vqgilaalvr rgvkgrgahv etsllealvd fqfevltthl ndggripqrs
      241 afrnahayls apygvyetad gwlavamtpl dtlgallgle eivglpadaa frkrdgikkv
      301 iadrlrtvpt ahwtailepa diwcaevldw prlfasdgfk lldmlqtvsr ddgvairtts
      361 vplrvdgara hgalaaprig ehtealrref gln
//
LOCUS       WP_181703244             258 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Chthonobacter
            albigriseus].
ACCESSION   WP_181703244
VERSION     WP_181703244.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..258
                     /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=28257
     Region          15..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 massptaias hritnarihd mleplmsapp kildlgcgrg sflqtvakrf aeknwpvagn
       61 lmavdidlda yaapevpsqv vdlnaglpfa dnsfdvvtai evlehtrapy llieevfrvl
      121 kpggriifsv pnvmhmtsrf sflltghyym yptpsaklsn agrlcghisp lpvqywhygl
      181 rfagfeaitt ttdrikksar ilygllwpvl klaavrykak irrydadlrt eveavlpqan
      241 afgsaagrsl vfsavkpg
//
LOCUS       WP_181703588             318 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181703588
VERSION     WP_181703588.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..318
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..318
                     /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=34210
     Region          12..308
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 msftqykpvk trvqrselav pgsnpqmfek alnsevdfif ldledavapn dkvqarenii
       61 kalkempwra kgktisvrin gldthwmyrd vvdvveqage fldtilipkv gvpgdvymve
      121 amvaqireak sipneiglea liettlgman veaiaaarnl ealhfgvadf sasrrsrtvv
      181 igglnpdypg dqwhaaidrm vtacrayglr aidgpfgdfs spedyvkaak raavlgcegk
      241 waihpsqial andvfspppa evdrarrvlv aldeaaaqgk gaasldgrli daasarmaqn
      301 ivmvadaiea kgkaakaa
//
LOCUS       WP_181703354             281 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Chthonobacter albigriseus].
ACCESSION   WP_181703354
VERSION     WP_181703354.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 281)
  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..281
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..281
                     /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=31006
     Region          4..281
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mnlidthlhv iersrlsypw lagvpaldrd ftydayaaea rrvgvtdvlh mevdvadgdi
       61 erevemvral mlrpgslvrg aiaacrpene tfpafleavq dggvvrgfrr vlhvmpddls
      121 egplfrqnia rlsrtglpfd lvvlphqipk aialvdsapd vqfvldhcgv paikdraehp
      181 wreyvaeiar rpnvaakisg vvayadpaaw tladirpyve hvvscfgfdr vvwgsdwpvv
      241 tlggtlstwv aathalmaac sqdersalfa dnarriwrlp a
//
LOCUS       WP_181703625             392 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Chthonobacter albigriseus].
ACCESSION   WP_181703625
VERSION     WP_181703625.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..392
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..392
                     /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=41325
     Region          2..379
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqsydvviig gavtgssvay hlaadpdftg silvvekdps yqtcasalsa asirqqfssa
       61 vnvkislhgi aflrsigdil evdgdrpdvq lheggylfla tgagreilee nhaiqvglga
      121 diafldpaal katfpwlavd dlsagcyglt gegwfdgygl mqafrrkars lgveyraasv
      181 vdvrtaggrv vsvtlsdgse iacgtvvnaa gaggaaiara agveipihvk krmiftfkca
      241 dpvercplli dptgvyvrpe gdgflcgtap padqdpdveg dfevewglfe eviwptlaar
      301 vpaferirtg rawagtydmc afdhnvllgp travpnlila ngfsghglqq spavgrgiae
      361 livhggyrtl dlselspdri adgrpvvekn vv
//
LOCUS       WP_181703960             476 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [Chthonobacter albigriseus].
ACCESSION   WP_181703960
VERSION     WP_181703960.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 476)
  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 476)
  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 476)
  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 476)
  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..476
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..476
                     /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=51286
     Region          14..290
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
     Region          <354..445
                     /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 msvprqpdhd gpldpgfvdi krliiertgh ayyadkddil fervrrriqa agargfsdyl
       61 drlaggsdea ewsalvsevt igetfffrfr eqfaalknti lpdliarrgg drrlriwsag
      121 csngseaysl aitlseligp eildwrisvi gtdideaalq rarsgvfgaw slravdaagr
      181 dawfdagprs gtysvkrrfr pivrferhnl lsmldgtspl qftdfdlilc rnvliyfkte
      241 tviqlvaalg ealrpegwll lghaetnpaf taslvpveia gatvyrrpgp hlpttpalra
      301 sepsaavplp aiaeptrksa pravaratrt lsptpptgaa etkpislveq lrsladagdf
      361 agalavcreg eadrptdpll rfyeglihra lgdqaaaasa lrraiyldra falahyhlgl
      421 vllaqgdrta grravanagr laaampgtad laegdgltaa dlvavarlvl sdggpr
//
LOCUS       WP_181703986             468 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181703986
VERSION     WP_181703986.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..468
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49840
     Region          18..417
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtdivaetdr assrsaanrf yfaawrwhfy aglyvapfli mlaatgllml wsaalygrdg
       61 eavavaggtp lavsvlaeaa akavpngtvs qyiaptaadr aaafrvdadg asttvivdpa
      121 tgsvldsfer ragwydland ihgtlligvt gdrlieiaas lgivlivtgv ylwwprgrtt
      181 lgralvpeva arrrplwksl hqtigfyvag vlvlfllsgl awagiwgery vqawstfpae
      241 kwdnvplsda thasmnhggt kevpwaleqt plpasgsnag vtglpdgtpv tidsvvglar
      301 slgfdgrfql nlpkgetgvw tisrdsmsnd spdptsdrtv hvdqytgkvl advryadysp
      361 agkamavgva lhegdlglwn lafntvfcls viflsvsgvv mwwmrrpsga lriaappvpk
      421 dlplwkgavv lmlaisfafp laglvllavl tvdvlvisrv avlrnaln
//
LOCUS       WP_181704183             135 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Chthonobacter albigriseus].
ACCESSION   WP_181704183
VERSION     WP_181704183.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 135)
  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 135)
  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 135)
  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 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   5  (residues 1 to 135)
  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 135)
  AUTHORS   Rosinski,J.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..135
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..135
                     /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=14376
     Region          19..106
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mieqtagses smipsdlaet arrtssalra lshehrlmil gilargersv geletllhlp
       61 qpavsqqlar lrldnlvncr rdgrtiyysl ateriatica amtelltiaa enapaagvea
      121 vgeaahaikr faavs
//
LOCUS       WP_181704142             115 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181704142
VERSION     WP_181704142.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=12764
     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 miavifevrp aegetahyld laaalrpele tmdgfisver fqsltdpgkl lslsfwrdea
       61 aveawrnrpa hratqakgrg gvfagyrlrv aavlrdygld draeapddsr rlhgr
//
LOCUS       WP_181704188             127 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Chthonobacter albigriseus].
ACCESSION   WP_181704188
VERSION     WP_181704188.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=13132
     Region          27..126
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mkkslvltav liagfataah aagdaakgek vfkkcqacha vgegaknkvg palngvvgsk
       61 igahpadyqf skvlkemgda gkvwdeatlt ewlknpkafa pgtkmafagl kkddeladvi
      121 aylatfk
//
LOCUS       WP_181703827             299 aa            linear   BCT 28-DEC-2024
DEFINITION  class II glutamine amidotransferase [Chthonobacter albigriseus].
ACCESSION   WP_181703827
VERSION     WP_181703827.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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..299
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..299
                     /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=31739
     Region          2..295
                     /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(2,149..150,175..176,200)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238888"
ORIGIN      
        1 mcgivglflk dkslepelgr ylaamlevmt drgpdsagfa vygdgriglt kitvrlpkga
       61 datvltdkvg dalatgisaa vrgshvvlqv pedrveeala aiatvepgaa vtsvgnamev
      121 ykevglpadv avafglpqmr gthgightrm atesavttdg ahpystgpdq clvhngslsn
      181 hnlvrrrlir egidfrtend tevaagflsw rlregdqlgd aleaslkeld gfftfvvgte
      241 tgfgvlrdpi ackpavmaet dryvafgsey kaltvlpgie tarifepepa tvyfwdraa
//
LOCUS       WP_181704271             252 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chthonobacter
            albigriseus].
ACCESSION   WP_181704271
VERSION     WP_181704271.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=27171
     Region          7..250
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 malehtlsyq lytsrnfppl eaqlktlarl gytnvepfsa vygdvpalka aldanglscv
       61 sghfaldlme kdldaavaia rtlgisimva pwlppeqrpt daagwialge rlgavadklk
      121 plgftlawhn hdfefvalpd gsmpirhvla hpsvmleldv awvaragadp qqwlreyadr
      181 ivsvhvkdia pagqnadedg wadvgdgvvp waalwadvvk taaritvaeh dnpsdyerfa
      241 arsaaaiksf kg
//
LOCUS       WP_181702963             141 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Chthonobacter albigriseus].
ACCESSION   WP_181702963
VERSION     WP_181702963.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 141)
  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 141)
  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 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   4  (residues 1 to 141)
  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..141
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..141
                     /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=15537
     Region          6..130
                     /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(6..8,22,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133412"
     Site            order(53,56,60..61,70,81..82,85,88,92,98,102,105..106,113,
                     118..119,124,126)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133412"
     Site            order(81,116,124)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:133412"
ORIGIN      
        1 mqagvsigea arvsgvkvpt iryyeqvgll pepprtegnr rlyearhlsr lafirharel
       61 gfevdairtl ldlqdhpgqs cspadsiarl rlqdvkeria rlnalkaele rmiegcshgt
      121 vaecrvievl adhakcghpg h
//
LOCUS       WP_181704297             236 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Chthonobacter
            albigriseus].
ACCESSION   WP_181704297
VERSION     WP_181704297.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 236)
  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 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   3  (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   4  (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 18629734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     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=25506
     Region          62..232
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          167..235
                     /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 mntpdeilad avglrtcssa nrifdiierr lvshgashil vtglpmpgrp veplilhmkw
       61 pdvrsergql itiskgdpil ercrvahrpf lvdgvsisgh sdlvaaagpe asarivavpv
      121 ksiqpyqaav iglgtslslt eldlvafdfl cnqafrrlra lgflidsrpg dlsarerkvl
      181 eltatgktaq eiaellnisq rtvhahlqna gekldasnkt qtvvealryg qitldd
//
LOCUS       WP_181704317             597 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Chthonobacter albigriseus].
ACCESSION   WP_181704317
VERSION     WP_181704317.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter albigriseus
  ORGANISM  Chthonobacter albigriseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 597)
  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 597)
  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 597)
  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 597)
  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 597)
  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 597)
  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..597
                     /organism="Chthonobacter albigriseus"
                     /db_xref="taxon:1683161"
     Protein         1..597
                     /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=64088
     Region          235..569
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mridefrrvl ersfeplvhg satvdaarsa thrgfiaahm gsgiaalgmv plalvmqgaa
       61 apfsvtalai lgleslvaly vsrsgrletg fllsalvlts lvawvaaftg glssfaivwf
      121 aiapieaals nsrkviaksa lvggagllav alltlggslp ppvtfvggpa lmnaaaglvt
      181 lvyasmiair vetqhrdaet ransgegryr lladtmtdlv tchgadgdvt faspatarvl
      241 gvkpyellad glfrrvhiad rpafltalse aihrgmsave frvrrgddiq enwlwvemll
      301 rrtedaaltg gvvvavtrdi ehrklqedel lkarqdaeaa sfaktrflan vshelrtpln
      361 aiigfsdilg qeifgkfeye rhheyarlik esgehllqvv ndildmskie agnfdvvpep
      421 fdlravidrc gqlmahqafq agvnlrmqve dnlpelnadr racrqillnl lsnaikfsns
      481 ggevvygaqr egrrmalfvr dcgigisaed lprlgnpfvq aesgydrkhe gtglglsvvk
      541 glaalhggsm sieselgkgt tvtvylpitg dreptpfpkr aardtdaaap grtakra
//
LOCUS       WP_181704610             255 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181704610
VERSION     WP_181704610.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 18602469
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..255
                     /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=28205
     Region          26..139
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
     Region          <85..205
                     /region_name="COG4627"
                     /note="Predicted SAM-depedendent methyltransferase
                     [General function prediction only]"
                     /db_xref="CDD:443666"
ORIGIN      
        1 myldvvdlrd fytqdlgftv reiliqriae rwptvtgeri lglgyatpyl gafrpqaerv
       61 lafmpatqgv vnwpadgpst salviedmlp lpdaavdrvl lvhalemagd prellrelwr
      121 vlapggrlia vvpnrrglwa rvdtspfgyg rpfsrgqltq llreslfspi gwgealhmmp
      181 lnrrrfrrsa ntweqigrrl wpafagvivv eatkqlyqgl pvtrravrap afrpaliptp
      241 agagispavp appeg
//
LOCUS       WP_181704719             536 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Chthonobacter rhizosphaerae].
ACCESSION   WP_181704719
VERSION     WP_181704719.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 536)
  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 536)
  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 536)
  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 536)
  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..536
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..536
                     /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=56461
     Region          <34..526
                     /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 mtalspnagg pdgaapngrs avellsiagl cavlvflefr lglmsavavf lsreipfgst
       61 vvvavvgglw aglgvfsvgr rvelarahaa rstlmaafea hrltepvtgl pntygllayl
      121 dgllaeareg afvdlvavef anlplirdvh gtalqeamer eiadrltglv rtgdflargp
      181 gssfylvrav tgpaaftatd eevtailaaf rgglavdglv iparihvgta taragtigam
      241 alldradlav hhsrrkgpga vsafdaemkt afeyramiet siagalkage ivpyfqplid
      301 lsrnkvagfe ilarwqhptv gyiapsvfip iadeigilep ltldllgkac raasawgdhi
      361 mlavnvsptv lrnpaflagf revlkasrfd pkrleveite nafidevagl dlvvaslkde
      421 gvsisiddfg tgysslqrlr slpfdkikid qsfvkdmgen adsrriveai iglglslglp
      481 ttaegieaes nralleglgc stgqgflfap ampadevpgf ltryaaegvv alrrta
//
LOCUS       WP_181704795             310 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181704795
VERSION     WP_181704795.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=33837
     Region          22..267
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mlangvqgtg isahkrlndl sdfgaeldmi ealgvetiel ptydmdivvg grirrpqmea
       61 lkracagrsv vysvhgplai nfmdeayrlq rhfdvlaasl evaaevgagn yvihsglapm
      121 qqgagleaay arqrewlars gdmarqlglt lcvetlfagf dgtvhasspr rlaeelaaig
      181 hpavmatldf shaylkldyd gvrttfvdev aalapyakhl hmhdsfgrqd diwmfteger
      241 layghgdlhl pvgwgdipwd dlmdacrfpe gvvfnielkd rywyaaeecv aatkalaara
      301 vtlrsaeaae
//
LOCUS       WP_181704679             274 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181704679
VERSION     WP_181704679.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 274)
  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..274
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..274
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=29909
     Region          6..272
                     /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 mafsetelad liailrdaar veilprfanl aagdvkaksh asdlvtvade aaerfiearv
       61 terfgevlfv geeiferdat vvdrlasaer avvidpidgt fnyangipaf aviaavvegg
      121 etmagvlydp irddwqfalk grgaflegpk qprrairvak pvpldqmhga lnwayvdgpv
      181 rermlkgaar lwggysyrcg gqemrlineg gghfalygkl spwdfagsal ihreaggysa
      241 rfdgsdyrpe hrdgglllap dkatwdllrd vlfd
//
LOCUS       WP_181704872             352 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181704872
VERSION     WP_181704872.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=36719
     Region          1..313
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mnrfdylrpt svadavalaa epgsaylaag tnlvdlmkig vsrparlidi grlpgldrid
       61 wlpdggvrig alvrnsdlay darfaatfpa vaeallsgas aqlrnaatvg gnllqrtrca
      121 yfqdtasacn rrhpgsgcda lqgenrlhav fgwserciat hpsdfcvpla aldavveveg
      181 ragrreipld ifhrlpgdap ereteldgad livalripga saafsrnary lklrertsya
      241 falvsaaaal dldggtirga ritlggvaar pwraraaeda lagrpaders faeaagiala
      301 darpsgdnaf kielarrlva ralalalagt pavmpalpas pfaaaagadh aa
//
LOCUS       WP_181704915             148 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181704915
VERSION     WP_181704915.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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 10167422
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..148
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16488
     Region          3..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(4,6,8,18..20,22..23,28,36,44,46,48,50,60,63,69,
                     71..72,84..85,87,89,99,101,103,105,111..119,121..123,126)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 msdilhrvgi kassptatyq alstidglrg wwttdthges rpggvirfrf gppggfdmkv
       61 ldldqdarvl wevvdgpgew igtrvrfdlr qdgehtivlf rhqgwaepve fmhhcstkwg
      121 vflmslkslv eggagsphph dvkidnwn
//
LOCUS       WP_181704935             214 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181704935
VERSION     WP_181704935.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..214
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..214
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=22902
     Region          28..100
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          113..212
                     /region_name="COG3837"
                     /note="Uncharacterized conserved protein, cupin
                     superfamily [Function unknown]"
                     /db_xref="CDD:443048"
ORIGIN      
        1 mvetsrtava asddlstgsn apgtteytle raiggqirnq rkrlgitgae laaaaeisag
       61 mmskiengqi saslstlsal aralnmpiss ffaayeerrd csyvkagqgv sidrrgtkag
      121 hhyqllghsl gdgivvepfl itlseeakpy tafqhsgiel iymlsgkvay rhadqtyvle
      181 pgdtlffdag avhgpeelie lpmtylsiii ypnd
//
LOCUS       WP_181705040             278 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181705040
VERSION     WP_181705040.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29999
     Region          52..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 mdafraanra nwddraalha tdktgmygia avlagrsclh pvdragigdv tglrvahlqc
       61 higldtlsla hlgaspvgld fspnavaaar dfasragrpd vsfveadvya arqalsgdfd
      121 lvyvtwgain wlpdigrwaa vaasllrpgg rlflaethps alvldevdgr iearfswrta
      181 adapiatdde tsytgdprpi antrnyewih plsvilggvl daglrlvrfq ehetlpyrly
      241 psmvpadrde dgrvityrlp dgavrfplsf sltaekpa
//
LOCUS       WP_181705300             262 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181705300
VERSION     WP_181705300.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=27279
     Region          1..250
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtsrfssvvl tgassgigea lalelaapgr alllvgrdae rlaavadrcr raganvdtal
       61 vdvrdaeala atllafddrh pvdllianag vsaglapgrg peapgvsrrl ldinyggmln
      121 tvepllprli arrggrialv sslaglralp dmpsysgtka avrgygvalr gwlarygvgv
      181 tlvypgfvts pmsarhggar pfeisaekaa rlivrrlekg rrviafpfpl algiflgnll
      241 ppalsdltmk pfeadvapdd gr
//
LOCUS       WP_181705514             307 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181705514
VERSION     WP_181705514.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 307)
  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 307)
  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..307
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..307
                     /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=34233
     Region          9..207
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 magprpntfl iggpkcgtts lahylsehpd vflgypkeps fwsvdlkrse avvrlrgldd
       61 ylalyrrags akivldasts yllsevavar ilafapdarf ivilrnpaev ahayhmekvf
      121 nhqedvedfe tawslqqerr agrrvpptcv epaelqylav aslgrqlerv tslvrseqll
      181 vlftedmard pravylaalg flglpddgrt dfpvvggahf nrfrrlsrly qappailkpl
      241 vrsakrllra hlsaalksrm taaiaehrpr aaiprsfald lrrafaadva lteqltgrsl
      301 rhwidet
//
LOCUS       WP_181705529             325 aa            linear   BCT 28-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181705529
VERSION     WP_181705529.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..325
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..325
                     /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=35033
     Region          1..315
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 msipvidlsr alagdpaarl etaaaidaac rslgflvisg hgvpdalvaa iretsaaffr
       61 lpeaekakia vtpttyrgfi pieseslsls ldepapadlk evynigpvdv spedradlvg
      121 layfaenvfp davpgmreay eayyramtdl arelmrlfal glklpetffd gridrhitnl
      181 svlhypplnr pakpgqlrag vhsdygslti lqrdetpggl evlsegrwtp vpdipgafvv
      241 nlgdlmqdwt ggawkstlhr vvlppdlgmg drmsiaffhq pnhdavievl piegadpsgf
      301 vpvtsgahlm tkiakhrave heaae
//
LOCUS       WP_181705571             280 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181705571
VERSION     WP_181705571.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=30884
     Region          4..278
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mrlidthlhl vdrrrlaypw lastpaldrd yayatyaaea laggitdalh mevdvapedm
       61 eretavvaei aerpgnlvrg aiaacrpedp gfpaylerqr vqplvkgfrr vlhvvpddvs
      121 egalfrenia rlsgtgynfd icvdarqipk aialvdsapg dipfvldhcg vpavkdraeh
      181 pwaarmsema krpnvavkis gvvayagsdw tvedlrpfve haieafgwdr vvwgsdwpvc
      241 tltadltrwi eatmaltagc seeqraalfh lnaeriyrva
//
LOCUS       WP_181705598             382 aa            linear   BCT 28-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181705598
VERSION     WP_181705598.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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 382)
  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 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   5  (residues 1 to 382)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 382)
  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..382
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..382
                     /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=41543
     Region          28..382
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 msdrvrpkdp aagsatpadt pirfgseaai lnalphpvil vdarghirsa ndaaqsffqa
       61 saavlarhpl khfvpfgspl ltlidqvrdr gssvneyrvd igtprigger ivdiyaapan
      121 egaqdtvvml qertmadkmd rqlthrgaar svtglaamla heiknplsgi rgaaqlleqs
      181 vddpdraltr litdeadriv klvdrmevfs derpiereav nihavlehvk rlaqsgfard
      241 iriieeydps lppvwanrdq liqvflnlvk naaealtdtp daeialataf rpgvrlsvpg
      301 trervtlple ftvrdngpgv peeiqahmfd pfvttktngt glglalvaki igdhggviec
      361 dsqprrtafr vllpaftekm ad
//
LOCUS       WP_181705621             268 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181705621
VERSION     WP_181705621.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=28172
     Region          7..268
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 miapvfiddp adprvsaymn vrdrdlagah gglfvaeget vlsvlldspl faaesvlvae
       61 nringlagrl eaalevpvfv asqavmdriv gfpihrgvla vgrrgpdrda sslladrpdl
      121 vvgavgianh dnmgglfrna aafgagavll ddtacdplyr kairvsvggv lkvpfaragd
      181 gadlikllre hgylpiglsp rgrlrldevd patrpalilg tegpglpddl ldrtetvrid
      241 maggfdslnv attagialye lsrrrlsr
//
LOCUS       WP_181705733             351 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181705733
VERSION     WP_181705733.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 351)
  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 351)
  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 351)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..351
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..351
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36807
     Region          20..309
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mrhlllsial lvagtsaasa gvvefkafds palgrtlpta vyvpegappv ggwpvvyllh
       61 ghngnerswv dlgaieetld rlmakggdld palvvmpdae nswyvdseaa ggpgdyetal
      121 trdlrkavea aypvrtdrtg ravvglsmgg fgalrlglth pdlyavsasl sgaiwqnipq
      181 alagrslddl kavqnetyln rldeatmtag vilpsvgdhy egafgtpfda grfnalnvft
      241 llakqvaasa rlpafyiacg dddghglwrg avafytalka ngeqaelria dgdhiwpvwa
      301 rdvvgalayv eeqreagdav vtapvpaddr paatpaaavl aldekapvva r
//
LOCUS       WP_181705762             470 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181705762
VERSION     WP_181705762.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=48854
     Region          1..441
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mldaaldqin gliwnhlliy lligvgvwft vrtrfvqfrm fghslsalrr srshaeggis
       61 afqafcigla srvgtgniag vavaitlggp gavfwmwvva lvgmatafve atlaqmfklr
      121 qgdgtyrggp ayyierglgs rlwgsifavl livtfglafn avqantiadt lqsahavptw
      181 ataavlvlla apvvfggmrt iarvaewllp vmailyigla lvivalhvdr vpevvslivr
      241 safgldeava gtvggigaav lngvkrglfs neagmgsapn aaatatvghp asqgfiqalg
      301 vfvdtivics atafivlvsg lydpatatqv agasltqaav aeslgvagtv lmtvviflfa
      361 fssilgnyay adgnltylra pgpafmafrl iallavvggs lgtlptvwam advsmglmat
      421 vnlvailllg kwafaalkdy egslpgepvf nsrenahlpa rigtgvwrkd
//
LOCUS       WP_181705906             426 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181705906
VERSION     WP_181705906.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=44661
     Region          1..409
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mavevtelpn gikvvthdmp hlastalgvw vgagsrseea sengishlle hmafkgtstr
       61 taveiaeeie nvggevnaat sientsyyar vlagdvplal diladilqds lfdaeeltre
      121 khvisqeiga aldtpedlvf dhfqeaafpg qpigrpilgs vetvssfsdg dlrgylakhy
      181 tggntviaaa gkldhdalve laterfagfa pttgaaeapa sylggerree rdlmeaqlvl
      241 gfpgssyytd dyttaqiaas vlgggmssrl fqevrekrgl cysiyafhwg frdsgvfgis
      301 aatgetdahd lvettldevg kaiggiteae vsrakaqlra gllmtlespa aragqlarqm
      361 mvhgrpmpld elvakinavt pamvgdflar tvgtgsptla aigpvsgvps lsaiaarfgt
      421 rpasaa
//
LOCUS       WP_181705940             471 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181705940
VERSION     WP_181705940.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 471)
  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..471
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..471
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51365
     Region          43..469
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 matahalpav pgpdrrwrpl aalafgigla lsapgpalad dheapvigad vssftldngl
       61 qvvvipdhra pvathmiwyk vgsadepagk sgiahflehl mfkgtrthpe gefsrviaei
      121 ggeenaftsy dytayyqrva keklpvmmay eadrmqnlvl sdenvrperq vvleersmrl
      181 dsepgailas sldavlylqh pygipiigya deisrleked aiafydryyt pnnailvvag
      241 dveadevrrl aedtygkvpr raeppprtrp fapvletpre vshadpkvkq esvqvtwlvp
      301 syriakdgea ealdvlaeav gggstsllfr dlvidrklat aagvayqadf hdqaqftlya
      361 aprdgvslet mrtelvaafe raiatgltde eiarakarle adtiyaqdsq qalarifgst
      421 latggtveev ktwpaairav draaieaaak vfdprrsvtg ylrqadpeqr s
//
LOCUS       WP_181705941             442 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181705941
VERSION     WP_181705941.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 442)
  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..442
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..442
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47246
     Region          21..442
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mipfpfrsar irtavagafl lvasalpspa aattvtevvs pggikawlvs ddavplvamg
       61 fafrggasqd pagkgglanl msglldegag dldsaafqrr leetavrigf dadrdsfsgs
      121 lgtlstrkde afdllalalt rprfdeepld rirtqvtari rsqqtdpeti asklfaeatf
      181 pdhpygrppq gteesvasit rddllawhka hiakdnlvig vvgditaeel kplldrtfgg
      241 lpdtatqapv advvprtgqr ltatlanpqt iirfgaqgvt rddpdfmaay vvnhilgggs
      301 ftsrlyeevr ekrglaysvw saiatydrag vflagtstra dqapatvelm teeirrmaee
      361 gptekelada ktyltgnyal rfdssgkisq qlvglqldnl pidyftnrna lveavtledv
      421 kraakrilgs pltvitvgpa eg
//
LOCUS       WP_181706070             316 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706070
VERSION     WP_181706070.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 316)
  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 316)
  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 316)
  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..316
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..316
                     /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=35290
     Region          36..301
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 maehrrtaie iglnaaivav esgiprvytv pgeapalpfg pfdpvvhrtl eiglrawvee
       61 qtgleldyve qlytfgdrgr lappggaeph vvsvgylalt rllergaaen wlawydffpw
      121 edwrdgrpdi ldreilpald afvaeppppd apirpldrve rvrlafgtgg spwdeekale
      181 ryellyeagl vaeavadgrp vrpwaarfvg ramrhdhrri lataisrlra kikyrpvvfe
      241 lmppnftlta lqgtveaisg rhlhkqnfrr lvetgalvep tgastdrtgg rpaqlfrfrr
      301 evlrerpapg vrvgar
//
LOCUS       WP_181706122             282 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181706122
VERSION     WP_181706122.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=30465
     Region          33..240
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqgfgvhtsm wtmnwdraga ekaiaaavhy kmdfieiall napavdaaht ralleknnlr
       61 aicslglper awasvrpdaa veylkvaidk taemgceals gvifggiger tgvpptegey
      121 dniaraltaa arhakdkgil lgveavnrye nhlintgkqa vamvervgmd nvfvhldtyh
      181 mnieekgaan gildarehlr yihlsesdrg apgagnvpwd eiyatlaaig fkgglamesf
      241 inmppevayg lavwrpvakd eaevmgnglp flrnkarqyg li
//
LOCUS       WP_181706226             563 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706226
VERSION     WP_181706226.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 563)
  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 563)
  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 563)
  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 563)
  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 563)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 563)
  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..563
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..563
                     /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=63313
     Region          58..557
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 marrddavtn papargsalh raldtmpqmv wstrpdghhd yfnrrwyeft gvpqgstdga
       61 gwngifhpde qdlawerwrh slatgelyei eyrlrrhdgv yrwvlgramp vrdaegrier
      121 wygtctdidd lkaveqrlnr sekrfrslve atdavvwtar pdggfdteqp rwtaftgqpf
      181 ealkgwgwla avhpddrslt aqiwskallt rslyavehrl rrrdgvyrsm lvratplvga
      241 dgeveewvgi htdvtglkda easlrrlnet letkverrtt elvrartale aanrdlegav
      301 rartadlqqa neeikrfayi vghdlraplv nimgftsele tardelgrfy akaretapdl
      361 aspsldalfr eefdeaigfi rsstekmdrl inailtlsra errvltpepv amaaflaqvk
      421 agvahqaaav gatididpav pdivsdrlal eqvfanlven avkylsperp grirlsgrpd
      481 gdrvvytvkd ngrgieekdf ervfelfrra gvqdkpgegi glahvralvr klggritvas
      541 ihgegstftl dlprriadqf qss
//
LOCUS       WP_181706258             246 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706258
VERSION     WP_181706258.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 246)
  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..246
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..246
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=24663
     Region          1..140
                     /region_name="CoxG"
                     /note="Carbon monoxide dehydrogenase subunit G (CoxG);
                     cd05018"
                     /db_xref="CDD:176853"
     Site            order(3,5,7,16..18,20..21,26,30,36,43,45,47,49,54,58,
                     62..64,67,73,75,77,89..91,93,95,104,106,108,110,124..128,
                     130..132,134..136,139)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176853"
ORIGIN      
        1 mdmtgeyrip aprqavweal ndpdmlkaci pgceslektg demvatvvak igpvkakfsg
       61 kvrlenlnpp tsysivgegs ggvagfakgg advsladdga dtvlsytaka qvggklaqlg
      121 srlidgtakm madqffsafs akvgaaaaaa tpvavvadtp apatmaattt gaapasapms
      181 paerdggqva vkedaldrvv haaeaaerka etrvetaaik sgpsgpmlwg lialavlavi
      241 liigal
//
LOCUS       WP_181706284             418 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181706284
VERSION     WP_181706284.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  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 418)
  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 418)
  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..418
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..418
                     /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=46842
     Region          19..409
                     /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..413
                     /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..206,210,337..338,
                     375..377,379..383,394..397,402,405,409)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176893"
     Site            order(200..201,203..204,206..207,211,307..308,310,318,320,
                     327,329,359,362..363,369..370,373)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176893"
     Site            order(200..201,203..204,206..207,211,307..308,310,318,320,
                     327,329,359,362..363,369..370)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176893"
     Site            order(206,211,373)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176893"
ORIGIN      
        1 mldrspespr vllarrrpgh sleapfytsp eifdldieai ffrhwiyvgv epdvpfegdv
       61 mvvdidrasi livrgddgvi rafhnvcrhr garlvhdekt svgklvckyh awtydldgpl
      121 lhaehmgpef dtschglkpv hlksvegllf icladtpptd idemaaamgp ylaphairda
      181 kvayqtdlie egnwkitmen nrecyhcagn hpeltvplfe ygfgfspesm deakakeanr
      241 yacmvtdlhg ewegagfpsr eiehladrvt gfrterlpid ragesqtldt kaastkllgt
      301 ltnprmggls fwtqpnswhh fmadhivtfs viplspdrtl lrtkwlvhkd avegvdydlk
      361 rltevwiatn aqdgdlvgiq hsgvkspaye pgpyspyteg lvekfvawyt grlsaylg
//
LOCUS       WP_181706368             356 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181706368
VERSION     WP_181706368.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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 356)
  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 356)
  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 356)
  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..356
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..356
                     /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=40837
     Region          11..340
                     /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..>239
                     /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 miegigrdae wslpaafyrd eeryarerkl ifeanwllfs wserlrepgd yvtgqlagys
       61 ifvirgddgk arafhnvcrh rasellreea grcgklivcp yhswsfkrdg alhkaaefgk
      121 datfdpdewg lyaldceewr glvfvrirre gpsliewlgp vvdfaapfpi ekqhyftkke
      181 rvvdvdwkty genylecyhc ramhpglcat ldidryaidv hpehelfhlh apgraegltq
      241 gcylyrfpfl mlnlydwgss iatvepmgpg rlkhinwyff edvspekaea nqqsadwsaq
      301 iitedldiit gvqrnlnagv ytrgalskaq ehaviafdrm avealerpgp rrvaae
//
LOCUS       WP_181706377             328 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706377
VERSION     WP_181706377.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 328)
  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 328)
  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..328
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..328
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35043
     Region          44..315
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mdgatakaaq advhgriaal lrslegglvg rtpllerllv allagghvlv egapglaktr
       61 avktlashld asfariqcts dlmpadltgt pvwrpdagsf efvagplfhg lvlvdeinra
      121 ppkvqsalle amaerqvtag gvthplpdpf mvvatqnpie hegtfplpea qldrfffhvt
      181 vdfpdraaer aildlveret vepqaapvar lsvdeihaar daamrthlap alkdfivrlv
      241 matrdgtadt gtapvvehpv sprgtlslal avkarawlag rdhgtpddvr alavdclshr
      301 lvltwratae getprkvier lfdrvvpl
//
LOCUS       WP_181706466             398 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706466
VERSION     WP_181706466.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 398)
  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 398)
  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..398
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..398
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=43069
     Region          17..397
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 mtapaledpa digpaarrrl sgfvrtlrdn gfaiglaetr dglavlaaap fgrpatvkpa
       61 lkalfcgrrs dfdrfddlfd aywqgrgvka svavsgtspk asqrtlrtlq qgtgsggepg
      121 paidvdrrpd apdgdaspeg rregatrhes lartdfrkia dpdelalaha laerlarrmr
      181 arltrrdkas argggldlrg tirrslstgg tplrlvrrkp rhkplrlvll vdasgsmsly
      241 tgvflrfvhg vldqfreaea flfhtrlvhv sdalrekdaa raldrlglma egvgggtrig
      301 dslatfnrwh aarvihsrtc vmilsdgydt gepeplgaem aalgrrcrri vwlnpmigwa
      361 gyepvargma aalphvdlfa pahtldslaa lepylari
//
LOCUS       WP_181706490             294 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706490
VERSION     WP_181706490.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=32469
     Region          3..294
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mtvvdahhhv wrqadlpwll gpmqprifgp yepirrdypm aeyladiagl gigksvyvqa
       61 nwakdrfede aawvssvaae tgwphaivay admtvpdarp aldrlarhpl vrgvrmqlhw
      121 henpqyrfaa gpdlardpvv qanvarlady gwsfdlqvfa pqmagaadla dacpdvpfvl
      181 qhagmledls eagraawrgg mallaarpnv aaklsafgtf vhrvdpdlva fitretvalf
      241 gpdrclfgtn fpierlwtda gtllrahqda tahlpeeara mifagtatrl yrle
//
LOCUS       WP_181706496             272 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181706496
VERSION     WP_181706496.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..272
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..272
                     /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=28254
     Region          9..267
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mpitvkttat faeaadlvag nraarflggg tllmrdvneg svafetlvrt teparairta
       61 gsrieigaav tiaqiqaerd laflhgaarl iggpavraag tvggnlfaps pygdlatall
      121 aldgvatlqq gasrremplg dlfaqrgrdl rgvvvsvsil rpesadafrf rkvsrvkpkg
      181 aavltiaahl ptsggrigka rvaygamapt piraravera legrsldrdg vaaalaaaae
      241 gtdpaddaia sawyrrevap vylrrlllne pd
//
LOCUS       WP_181706562             354 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706562
VERSION     WP_181706562.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..354
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..354
                     /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=37471
     Region          30..351
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mnfssdnwag asapvaaait aatgglapay gtddatrkvd dwfaeiferp vgvffvatgt
       61 aanclslaav skpggvilch enahiandea gapaffsggs vlhgiagarg kitpegleaa
      121 lrrymppgvh hgrpvalslt qatewgttyt ideiaalaei ahkaglkvhm dgarfanalv
      181 grssaaadmt wragvdilsf gatkngcwaa eaivtfdrkl dedlayarkr agqlfsksrf
      241 vaaqfqgyfd lghwldnavh angmatrlaa siaevrgarv lfepeanevf avwpkaysrr
      301 lreagalfye wpadglsade mptadeevvr lvtsfatskh dvaafmrale dgsh
//
LOCUS       WP_181706585             199 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706585
VERSION     WP_181706585.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 199)
  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 199)
  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 199)
  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 199)
  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..199
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..199
                     /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=21435
     Region          105..192
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mhdllveapa lparttavdi lvaafandpa vraiypdehe yrrhfpgflt afggrafevg
       61 tadcdperga aalwyppgle pdgeavvehl aatvspdrfh mlmagfeiqa glhptephwy
      121 lpwigvrpea tgcgiggall rrgleradaa dlpvyleats rrnaalyarn gfeivgivea
      181 pgypeilamw rpartagrg
//
LOCUS       WP_181706782             159 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706782
VERSION     WP_181706782.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..159
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..159
                     /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=16704
     Region          56..153
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mdtspadrpn rlpwppmill gtlfagvtle alaptslpvp aavglalvaa alavdvwamv
       61 tmaraktnil phraadrlvt sgpfhfsrnp iyvgnaalia gcgiavgsvw llalapvaay
      121 athrlavlre erhlaarfge awaayarstp rwlgprgra
//
LOCUS       WP_181706712             290 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181706712
VERSION     WP_181706712.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=32069
     Region          1..264
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mspaeydflr qflkarsglv lsnekqylie srllpvarka glasiaalvs klrdpreaql
       61 adavveamtt nesfffrdkv pfdhftqlml pqllerraak rhlriwcaaa stgqepysla
      121 mclkemgprl agwrveilgt disnevldra ragvytqfev qrglpiqnll kyftqsgdqw
      181 tisaelrsmv qwrkfnlles faglgqfdiv fcrnvliyfd qptkadiinr igkllapdgy
      241 mvlgaaetvv glseafkpvp drrglyapnl vaaggaapia gvrvaglggf
//
LOCUS       WP_181707007             142 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181707007
VERSION     WP_181707007.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 142)
  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 142)
  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 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   4  (residues 1 to 142)
  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..142
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..142
                     /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=15598
     Region          6..130
                     /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(6..8,22,39..41)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133412"
     Site            order(53,56,60..61,70,81..82,85,88,92,98,102,105..106,113,
                     118..119,124,126)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133412"
     Site            order(81,116,124)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:133412"
ORIGIN      
        1 mhdgvpigea arasgvkvpt iryyeqvgll pepprtegnr rlyggrhlrr lafirharel
       61 gfeveairtl ldlqdnpgqs cspadsiarl rlkdveeria rltalkaelq rmidgcshgt
      121 vadcrvievl adhgacaspt hr
//
LOCUS       WP_181705790             286 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181705790
VERSION     WP_181705790.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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 286)
  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 286)
  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 286)
  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..286
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..286
                     /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=31894
     Region          10..>44
                     /region_name="Rieske"
                     /note="Rieske domain; a [2Fe-2S] cluster binding domain
                     commonly found in Rieske non-heme iron oxygenase (RO)
                     systems such as naphthalene and biphenyl dioxygenases, as
                     well as in plant/cyanobacterial chloroplast b6f and
                     mitochondrial cytochrome bc(1) complexes; cl00938"
                     /db_xref="CDD:445190"
     Region          98..273
                     /region_name="VanA_C"
                     /note="Vanillate O-demethylase oxygenase C-terminal
                     domain; pfam19112"
                     /db_xref="CDD:436978"
ORIGIN      
        1 msrttdpval ddwyvvglpg dvqagrpvtr rllgadltle rtaddvrvte aasgralpvq
       61 tayghlwttl gapkrplfai eefaeadrrl apcgavrvra sglrlvenfl dmahfpfvht
      121 dilgaedkpa vepydceirr dvdevwatnc rfwqpqaaah adggqmsdyi yrvaspfnvl
      181 lyktcpsdag rqdviglfiq peeedvsvah afvhvvdavs shtaivhfqq tvflqdrfil
      241 enqrprllpl spraetptra dmssiayrrw lkekglrfgi drrdaa
//
LOCUS       WP_181707173             415 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707173
VERSION     WP_181707173.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 415)
  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..415
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..415
                     /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=44879
     Region          162..399
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 msaiassaps ayglvsvkal rdgglwfavf lggfvivepa pyelalalli plyflgglkl
       61 rgafapllal vlvynaggfl svtqirpekf sdgllymavs lflgltsvwf aalvaedwrr
      121 irviertyvg tavlvsaigi lgyfrllpgs dqfllygrak atfqdpnvfg pflllpalil
      181 arrimtapla rnlgalamla vlaigiflsf sraawamlaf glpllaavvs atattnrarl
      241 rliglgaagi aaaavlvava msipavsdll vqraklvqdy daktgaelgr farhwvgfal
      301 saehplgigp yefplafvea thntylksil eygwlgfsay vtlvamtlvk glplafqprp
      361 wqpfaqcvlv sfvlhllvgw iidtdhwrhm ylafgliwgl vaveryhrag rfptr
//
LOCUS       WP_181707243             394 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707243
VERSION     WP_181707243.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=40664
     Region          4..392
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mttrdvvlvs pvrtpiggfn gafagvpatd lgaaairatl ersgldpsrl sgvvmgnvvq
       61 agnrmnpsrq aaigggvpvs vpavsvnrvc gsgaeaiaaa arevwlgfad amlaggmenm
      121 drapyllpsg rfglrlgpge vldamlldgl hdafsgrhsg whaedlirrm disreaqdrw
      181 aarsqqrfaa arsagafade ivpvtvkgrk gdvtvsddea prpdttaetl srlkpafrdd
      241 gtitagnapg lnagasamiv adrafaereg lrplgrlvat glaavepdmf glgpvpavhq
      301 aleragwtla dvdrveinea yaaiaiavlr avgfpeeivn veggavahgh pigatgavlt
      361 trllqsmrrd glkrgivtlc igggqgiala vetl
//
LOCUS       WP_181707364             336 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707364
VERSION     WP_181707364.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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 336)
  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..336
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..336
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36211
     Region          29..326
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msapfiasta tdtdrivada eaaverivaa rtaiarvifg qesvverali tvlagghgll
       61 vgvpglaktk lvetmgtvlg lserriqftp dlmpsdilgs evleqatdgt rafrfvrgpv
      121 faqllmadei nrasprtqsa llqamqerhv tvagqrhdlp epfhvlatqn pleqegtypl
      181 peaqldrfll qidvhypdre serrillett gaeearaepv ldpaeiialq rlvrrvpvge
      241 svvesildlv rsarpdsgvg rhgkaiawgp gprasqalml tvraralaqg rlapslddvr
      301 alaepvlqhr maltfaarad gvtirdviad ltgrig
//
LOCUS       WP_181707354             430 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome b [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707354
VERSION     WP_181707354.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 430)
  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 430)
  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..430
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..430
                     /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=48332
     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 msghstyepr tgvekwlerr lpivrlmhdt avsyptprnl nyfwtfgail vfmlvvqilt
       61 gvvlamhyaa nsavafqsve aimrdvnwgw llrymhanga smffiavfih mfkamyygsy
      121 keprellwil gviilllmma tafmgyvlpw gqmsfwgatv itnfftaipl vgepiqtlli
      181 ggfavdnatl nrffslhyll pfmifgvvil hiwalhvsgq nnplgidtks ekdtvpftpy
      241 atlkdvfalv vfclffgwfl ffqpnylghp dnyiqanplv tpahivpewy flpfyailra
      301 itfdigpins klggviamfg siailvflpw ldtskvrsar frplfkiffw vfaitcvmlg
      361 wlgsrpaegg yvlaaqlfta yyfahflivl pllgfletpk plptsitdav lakngghahp
      421 vgaaaspekh
//
LOCUS       WP_181707289             156 aa            linear   BCT 28-DEC-2024
DEFINITION  YcbK family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707289
VERSION     WP_181707289.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..156
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..156
                     /product="YcbK family protein"
                     /calculated_mol_wt=16967
     Region          <58..148
                     /region_name="YcbK"
                     /note="Uncharacterized conserved protein YcbK, DUF882
                     family [Function unknown]; COG3108"
                     /db_xref="CDD:442342"
ORIGIN      
        1 mqryvglvla iglmllaqpg rseglvkdaa avgntaarva erslvayvvq tksvrtncft
       61 palrtlltdl rrklgnrqit vtsgfrgaqr arrgsyhrrc maadvqvvgv aprkvaavar
      121 sipgiggvgt ychtrsvhvd vgprrdwsws crkrrr
//
LOCUS       WP_181707369             299 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181707369
VERSION     WP_181707369.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 299)
  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..299
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..299
                     /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=31923
     Region          2..266
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mfrlahlsdp higplpaasv adlaskrllg yinwhrnrav amrgdllsrl vdavkaeapd
       61 hvavtgdlvn ialpaelepa trflqsighg sdvsvvpgnh dayvpgalmk ateawraymq
      121 gdgdpgapnw pfvrkrgeva lvgvstaras gpfmatghvs vpqatllaer lealgregfc
      181 rvvlihhppi rgstdwhkrl iggsrvraav rqsgaelvlh ghthlatrme iegprgpvpv
      241 igvpsasqep ggpkpgsgyn lfeierrnag wriglrehrv lrpggdfvei gggrwdiaa
//
LOCUS       WP_181707466             392 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707466
VERSION     WP_181707466.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 392)
  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 392)
  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..392
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..392
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=44602
     Region          1..392
                     /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 mfltfftalk aagvpvsmre yldlmgamea dlparqvegf yhlartvlvk deknldrfdr
       61 vfasvfkgle stgdavtpea lpedwlrrma eryltdeekr qiealggfet lmetlkqrla
      121 eqkgrhqggs kwigtagtsp fgaygynpeg vrigqdesrh rravkvwdkr efrdlddrve
      181 igtrqirval krlrrfartg vpeeldlsst idatarqgwl dvklrperrn tvrvvlfldv
      241 ggsmddhvrv tselfsaars efkslhhyyf hnclyegvwq anarrhgerv ptvdllrtfp
      301 adtrvvivgd asmspyeith pggsvehwne eagavwlqrv vatwpklawi npvpedawsw
      361 thsiglvrel igdrmvpltl egldramral gr
//
LOCUS       WP_181707471             281 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707471
VERSION     WP_181707471.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=31947
     Region          2..271
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mrfqgttdyv atadltmavn aaitlerpll vkgepgtgkt vlarevaral gapfiewhvk
       61 sttkaaqgly eydavsrlrd sqlgdprvad ianyirkgkl weafespvrp vllideidka
      121 diefpndlll eldrmeffvy etgrtvkaar rpiviitsnn ekdlpdaflr rcffhyirfp
      181 dretmeaiva vhypdlkkrl lqealsvffd vravqglkkr pstselidwi kllvnedvdp
      241 etlrakdart aipplhgall kneqdvhlfe rlafmarreg r
//
LOCUS       WP_181707688             397 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181707688
VERSION     WP_181707688.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..397
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41375
     Region          1..389
                     /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 mttpkplagv rvlelarila gpwagqllad lgaevikver pevgddtrgw gppfvtaadg
       61 sawgaayfha cnrgkksvav dfetadgqgv vralaaecdv iienfkvggl vkygldmatl
      121 rtlhprlvtc sitgfgadgp yanragydfm iqgmaglmdi tgdpagepqk vgvavadift
      181 giyatvgila alrrrdttge gghvdmalld savgilanqa mnylvsgrap trlgnahpni
      241 vpyqvfavad ghvivavgnd gqharfcqvi gaehlaggpy aqnrdrvrlr delvpllspf
      301 vagfgrddll arleaagvpa gpintiadvf ddpqvvhrgl rldlraadgs rvpgvaspiv
      361 idgvrqvadg psprlgadta avlqafnisl plaeset
//
LOCUS       WP_181707690             392 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707690
VERSION     WP_181707690.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..392
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..392
                     /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=41852
     Region          3..379
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpsydvviig gavtgssvay hlaadpaftg rvlvvekdps yqrcasalsa asirqqfsta
       61 vnveislygi dflrrigdvl avdgdrpdvq lheggylfva teagmpvlae nhglqtrlga
      121 dialedpaal arrfpwlnte dlavgsfgrs gegwfdgygl mqafrrkars lgveyraasv
      181 vglgmdgerv tsvtlsdget igcgavvnaa gaggraiaal agldipvavk kriiftfkca
      241 epvpacplli dptgvyvrpe gdgflcgtqp pedrdpeved dfevdwdlfe eivwptlahr
      301 vpaferikpg rawagyydmc afdhnvllga paarpnlfla ngfsghglqq spavgrylae
      361 aivhgrpltl dlselspdrv aegrrvvekn vv
//
LOCUS       WP_181707761             311 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707761
VERSION     WP_181707761.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 311)
  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 311)
  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 311)
  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 311)
  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 311)
  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 311)
  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..311
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..311
                     /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=32541
     Region          73..300
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mlkaglatav vlaaagggvf wmltepdrve aaslpahtpd vangelvfha ggcvschaap
       61 naegeeklkl agglelntpf glfrvpnisp dpdtgiggwt agdlvnammh gtspegasyy
      121 psfpytsyar mrvedvidlk ayldtlppvr navadhdlgf pysirrgvgl wkrlyvdpsp
      181 vvalpadasd avrrgqylve gpghcgecht prnaiggldt arwlagaanp egrgvipnlt
      241 phaeglesws additysles gfkpdydsfg gqmvsvqanm aalpaedraa iaaylkavpa
      301 hpdavtrpaa e
//
LOCUS       WP_181707848             127 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707848
VERSION     WP_181707848.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=13153
     Region          23..126
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mkkslvlaaa llasfatgah aqgdaakgek vfkkcqacha vgpdaknkvg phlnnvvgap
       61 igkhaegfky sealsslgds gkvwdeasls ewlknpkafa pgnkmafagl kkedevadvi
      121 aylatfk
//
LOCUS       WP_181707849             421 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707849
VERSION     WP_181707849.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /calculated_mol_wt=44124
     Region          50..337
                     /region_name="FadH2"
                     /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur
                     reductase, or a related oxidoreductase [Lipid transport
                     and metabolism]; COG0446"
                     /db_xref="CDD:440215"
     Region          354..>402
                     /region_name="FCSD-flav_bind"
                     /note="Flavocytochrome c sulphide dehydrogenase,
                     flavin-binding; pfam09242"
                     /db_xref="CDD:462722"
ORIGIN      
        1 mtitrrrlle laivgsglla gagpgrsavp rlvvvgggpg gavaartasr lggdrvhvtl
       61 veanptyvsc ffsnwvvagl rtmadithrp aqagehgidv vtarveaidr egkalrlsdg
      121 srvpydrlil spgvdfrfdt vagysveaae rmphawkagp qtellirrla aldqgasvvm
      181 vvppnpyrcp pgpyeraalm ahvlktsgrg daritildak esfpkqalfq egwerhypgm
      241 iqwlppsvhg glravepagt avetefdrfd gdlvsvippq kagalaldag lgdadgwcpv
      301 eaasmrakad psiqvigdaa ragempksaf aaasqgrvaa vaaladllgg prpepryfnt
      361 cwsliapgda vkvgalygia egaiksvqgf vsqpgesaev rrvsaeeaea whaailadmi
      421 g
//
LOCUS       WP_181707533             472 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Chthonobacter rhizosphaerae].
ACCESSION   WP_181707533
VERSION     WP_181707533.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=51660
     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 mnseefelwa vraaewaaey rrtlrdlpvr pnvafgdiaa rlpvqapeta epmdaivrdf
       61 qdlivpgmth wqhprffayf panaapaavv aeilvsamaa qcmlwqtspa atelemtvva
      121 wlrdalglpt aftgvlqdsa statlsavlt mreralafqg ntrglsgqpa vrvycsdqvh
      181 ssidkacwis gigqdnlvkl pgrgpskald paeleaaiva drdsarlpag ivacvggtsv
      241 gasddvaavv avarrhglfv hvdaawagsa micpeyrslw agvedadsvv tnphkwlgap
      301 fecaahfird aeshvrtlai qpeylktyge krvinysews vplgrrfral klwfllrayg
      361 leglramirn hvrwaedmaa airdaerfdl vtnpvlslfa frwtpagatd ldaanlalve
      421 avnrdgrvyl tqtrhdgria iriqfgsfem teedaregwr virevaaglr lg
//
LOCUS       WP_181707853             127 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181707853
VERSION     WP_181707853.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 127)
  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 127)
  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 127)
  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 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   5  (residues 1 to 127)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..127
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..127
                     /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=14016
     Region          21..96
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(25..26,28,31,34..35,38..39,42,72,94..95,97..99,
                     101..103)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(26..27,31..33,46..48,57..60,62..63,66..67,69..70,
                     76..78,83..85)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(46,49,94)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mqhdpnitkq ttgigdiakk asdtlralsh ehrlmiigll argeksvgel erilelpqpa
       61 vsqqlarlrl dnlvtcrrdg rtiyysvtpa rigdlfnels villpgeahe asevtsfeqv
      121 qyraaar
//
LOCUS       WP_181708272             716 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Chthonobacter rhizosphaerae].
ACCESSION   WP_181708272
VERSION     WP_181708272.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 716)
  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 716)
  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 716)
  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 716)
  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..716
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..716
                     /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=77608
     Region          51..702
                     /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 mgnlkiqaai nwcmsafvvl lvimgvatvs glrivdqkid alegkwlngt qllgaissav
       61 sefrmaeisr alapdrdgrv eaqqrimest irvrdlldey ssllsnekpn eevhaflvaf
      121 hdyrranrvw vvadfagndd gpardgselh alytatkkav drlvkvnhel askdaqgade
      181 vsdvilisvg iislaigila tgllvfvqrr vtgplgemts alarlasgdr nagvpainrq
      241 deigvlaraf gvfsanaaal elahqavvea qraaeelarh daltglpnrr tfsaalasai
      301 ddpngtsvgy svllidldrf kpvndtygha agdqvlceva qrllrlagpd dmvarlggde
      361 failfrpedr anvlgtatgf agqviasmrt pisvgdaeve igasigiall stdgtdadev
      421 lraadiamyr akqggrntyr nfeplmdeer karakleedv ragllsgaie pyyqplldlr
      481 sghirgfeil arwndetrgs vspelfipvi eqlgladela trllsracqd trdwdvdlsl
      541 nisplqlqdp flptrilavl treafppsrl eievtetalm gdvdrarhvl sefrglgisv
      601 alddfgtgys slnhlrelkf drlkidrsfi mtmaenpese kivdavlgla eslgiavvae
      661 giesegarak ladrgcefgq gylfsrpvpa nearalvrgy apkmghprar mvklsr
//
LOCUS       WP_181708329             110 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181708329
VERSION     WP_181708329.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=12262
     Region          5..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkqvathlee slsgiayqnr llmmgllarg pmnvgqitka ldlpqptvsq nlarmkelgl
       61 iksevdgrsr vyrldrngie llktrlewll dtnyepssae rkdshaqdgd
//
LOCUS       WP_181708442             310 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181708442
VERSION     WP_181708442.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=32500
     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 mllscgdali dfvpvkaqdg rdayvpvvgg sclniavama rlgvpaglvg glskdmfgqm
       61 iadhataskv dlryvdrsdt eatlafvrfv dgephyafyd ettaarlwty kagsipfaav
      121 daihvgsttl indpvststl emakaardlt tvsfdpncrp slvrdkadyg rrmeafaana
      181 divrmsdvdf dylyggsdya pkaeallsgg atlvivtrgg kgviawhkta gcvevpapkv
      241 dvvdtigagd tfqgttlval keaqlierea legataadia nalgfgvkca aitcsragan
      301 ppwrreldaa
//
LOCUS       WP_181708590             750 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Chthonobacter rhizosphaerae].
ACCESSION   WP_181708590
VERSION     WP_181708590.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 750)
  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 750)
  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 750)
  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 750)
  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..750
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..750
                     /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=82596
     Region          69..736
                     /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 mrfdpadehq rlkelhryri ldtrrdaafd dlcelaraal dmpmagigfv dkdriwfksa
       61 igltapsfsr qgtlvgaavd hgghlevada cadprfvdhp lvvgpphlrf fasvpitvrd
      121 glvigvlcvg gteprrladn qrfvmeriah svvdrlrlhr lglerardnm rtrarnakia
      181 aqqseigkqr llleqttria riggweydvk arrlvwsdqi frildmpvgs pppfetvtrf
      241 yadgdrdmvh ahmkaaltqg ipfeaefkvi teqgrrrwvr cvceaertkt gvsrligtiq
      301 dvtdqraaee evqyvathdv ltglpnrrvf qdrleaglav ggrdarhgll mididhfkev
      361 ndglghhagd allaevalrl rrsagegaiv arlggdefav lilnlpnlan ldrvaglvad
      421 slsesvrygd esipvtasig vvigrtgdga dqllkdadia lyeaktagrn rvvrfhramr
      481 eemelkqsil rsmrqavanp gnlllyyqpk tclrtggllg fealvrwrrp dgavvgpslf
      541 mpaledpqls qiigdlvldq alrqaqdwrt rglafgtiai nvatsqfrrg dlagliltgl
      601 kshglppeal tvevtenvll akdirnvaet lnalsragvr islddfgtgy aslthlkdfp
      661 vdmlkidrsf vsnlvtspes haivramigl ahdlgvqvvc egveteqqrd ilvalgsdfa
      721 qgylfarpmp adlveqscft atgdkriqva
//
LOCUS       WP_181708564             461 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Chthonobacter rhizosphaerae].
ACCESSION   WP_181708564
VERSION     WP_181708564.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 461)
  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 461)
  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..461
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..461
                     /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=51269
     Region          129..453
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mltkhlplsp awddlfnllq seerhalsrl aryctaigia pgkvdketll gfynalvaes
       61 fvkcprkilk htialanmag krlsgewpvp rlsspfktqp fmmplsafpa sfgedvecwv
      121 tsattadpln lrarikparp atiksavyhi rraasalfre ghlrieeits lavlvqpanf
      181 vnalraflpa dssspptdaa riartlvgia kshvaveeav laqlkavsrr lqqrlppgmg
      241 krhrerveqf ddpenvrrll rfpaeeaara lqqknterra rgierslata ilvdtglrlh
      301 slrtlrtdts frrangvvfl hvhrdqsktd rpldyilpta tvalldeylr dhrqilsgsd
      361 gpylfpgrtg dpksesamrn ciseplhrht girlnphafr hvigkivver dpsayaivsr
      421 hlghtslntt lgsylgtetk vasrhlhkii dearnglpte v
//
LOCUS       WP_181708143            1162 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Chthonobacter rhizosphaerae].
ACCESSION   WP_181708143
VERSION     WP_181708143.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
REFERENCE   1  (residues 1 to 1162)
  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 1162)
  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 1162)
  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 1162)
  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 1162)
  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 1162)
  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 1162)
  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..1162
                     /organism="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     Protein         1..1162
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=123247
     Region          1..205
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
     Region          <281..>875
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <679..1151
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mrllalhldr wgpftdrtlp fpadrplvvv hgrneagkss alaglvdafy gietrsrfdf
       61 lhdygvmrvg atvetrdgrr lsfrrrkgnk atlrdetgdt piaddalvpf lgrvdralfl
      121 dafgldqdrl rkgaealakg egslgealla aapglgrlvd lrrtvaeeat aafterrsag
      181 kpvyaaidry ldarrrvqdl sltaesvara kadldaasar vadldrdrrq vrteearhqr
      241 laralphlaa ldrlaaerat madapdldpg fgdaltaaea erdrlatrra vlladrerea
      301 ealavlsvdd tliaaadrir rladgrrqre dasadlvdlq ariarltddl agqarrlglp
      361 daeavlqrrp taaaiarvrd laaartslda rasaaaeqaa dakarlaeld karaaalala
      421 dprslragld vlagldaalk laatrragva sasarfaeaa eqagvpadvr hvrgrrlpdr
      481 advedahrat eaaaraveta tqrladarar raeadrmlaa avasseipsl savaaaragr
      541 qeawaavrai lfgerdasps drlagardle aaidaadalv drrlsaadra avadrrreea
      601 ataadqvaaa eadlaaarea aaavaarwad llaatalppa ltprqalval drhadlvlla
      661 davgaaeaea asadadagrl lasldrlaad vgvaadradp lgslararae vtaleeawaa
      721 arrrdeaiad aarqveagne ttarvarala dwqgqwatav iavglpssat preaeaaldv
      781 waevpetesr laevrdrlar aerqaaafda aaedlrlgva pdlaadlrpa dvaqrlserl
      841 aaaeriadrr riaerrvaei dadlaradae srsaldtlar laaaagqppd adlravlraa
      901 gaaaalntri adhrdalare agddeatlra alagldadsl aaaladtadr larldaahee
      961 avaaramaek ayldviardg aetagqeaet aladlvdlae ewrilqaanr lagavveefr
     1021 rrhqnpvlte asgyfarlte gryrglapdy dangvarlla vraderrlgp dalsegtrdq
     1081 lylalrlatl adharrsepl pfvgddlfvt fdegrtaagl etlaafgesa aqailfthhe
     1141 hvariaedrl dgraavlrld ta
//
LOCUS       WP_181708984             522 aa            linear   BCT 28-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Burkholderia sp. MBR-1].
ACCESSION   WP_181708984
VERSION     WP_181708984.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 522)
  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..522
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     Protein         1..522
                     /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=57524
     Region          26..522
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 msfsrsaadp adtlpdlaat laapgddafv tlgdafhtrl paaplpapyv vgfsaevaql
       61 lglppslaah aqfaelfagn ptrdwpahal pyasvysghq fgvwagqlgd graltigelp
      121 gsdgrryelq lkgggrtpys rmgdgravlr ssireylcse amhhlgiptt raltvigsdq
      181 pvvreeiets avvtrvsesf vrfghfehff sndrpdllrr ladhvierfy ptcreaddpy
      241 lalleaamlr tadmvaqwqa vgfchgvmnt dnmsilgvti dygpfgfvda fdanhicnhs
      301 dtsgryayrm qpriahwncy claqallpli glqhgiaddd araeravdda qavlakfper
      361 fgpalecamr aklglelere hdaelanqll etmhashadf tltfrrlaql skhdasrdap
      421 vrdlfvdraa fdawanlyra rlseetrdda araaamnrvn pkyvlrnhla evairrakdk
      481 dfseverlaq ilrrpfdeqp eheayaalpp dwagslevsc ss
//
LOCUS       WP_181709136             732 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Burkholderia sp. MBR-1].
ACCESSION   WP_181709136
VERSION     WP_181709136.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 732)
  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 732)
  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 11420499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     Protein         1..732
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=79135
     Region          6..725
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          38..66
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          71..99
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(72,75..76,79..80,82,106,109..110,113..114,116..117,
                     140,143..144,147..148,151)
                     /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..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          172..202
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          207..234
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..270
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          245..307
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          275..303
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdgtgqalqt alahhqsgrl aeaktlydai ltaqpgqpda lhflgllacq lkqydaglal
       61 mkqslverpd asyfnnlgnm lresgrldda iahyrravtl rpdypeahnn lgnalrdagd
      121 ptaamascar aielrahyaq aynnlgnalq dlgdldgaat hyeraielda smamahanls
      181 avrhkqlrca ealthaldai rlapnlgeah nhagnayhgl nrlddalach rtavtlnpad
      241 agachnlsvv llklqrldea lvycrqalqa gapavlmhvn lgdilraqgn vdaavhayrd
      301 alalvrddad dvaatvlsrl lfsaaasacv spddyladal rygrhlaars tryahdprer
      361 aaraqgrplr vgfvsgdlrl hpvgiflesv lahldrtrid lrvyvttdee daitaklkph
      421 asvwrsiaal ppeaaarmih ddgidvlvdl aghtqssgla afgwkpapvq aswlgffatt
      481 gcdaidyfig drytlpdada hhfveapwrl pdsflcftpp adevevgplp maahghptfg
      541 cfgqlvkigd dvvhawsril havpdarlll kahelgregv rdatvarfar hgigadrlil
      601 eagsprteyl naynridval spfpypggtt taeamwmgvp vlgmkgsrfv thicesllha
      661 agmgewiadg edayvakaia avrdrerlat lraglraqvl asplcdarrf athleaafla
      721 mwqrytnseq ea
//
LOCUS       WP_181709211             405 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia sp. MBR-1].
ACCESSION   WP_181709211
VERSION     WP_181709211.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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 405)
  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..405
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     Protein         1..405
                     /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=45763
     Region          2..395
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mpltdtairt akpgpkiqkl ydgnglflqv mpsgqkywrl kyyfakkekl lalgvypdvs
       61 lavarrkrde arskladgid psearkmekr estlnadntf kaialawlen rktvveigqy
      121 tktlarmnkd vfpwlgtrpi keitppeils vlervdqrga rytahrvrse isrifrfait
      181 kgaakidpar elfdaiepav ekhfaaitdp kkvgemlraf dgfsgtfpvl calklapmlf
      241 vrpgelrkae wsqfdldkge wrylvtktkt dhlvplakqa vvilrelhal tgrgryvfpg
      301 arsaerpmse aainaalrrl gydtrteitg hgframarti lheeleqkpe viehqlahav
      361 pdalggaynr tkfikerram mqlwadyler qkvgaevipl saraa
//
LOCUS       WP_181708427             132 aa            linear   BCT 28-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Chthonobacter
            rhizosphaerae].
ACCESSION   WP_181708427
VERSION     WP_181708427.1
KEYWORDS    RefSeq.
SOURCE      Chthonobacter rhizosphaerae
  ORGANISM  Chthonobacter rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Chthonobacter.
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="Chthonobacter rhizosphaerae"
                     /db_xref="taxon:2735553"
     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=14082
     Region          1..132
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mfavevrdhm miahslprpv fgpaqglhga tyvvdaafft ealdddglvv diglasealk
       61 ailkpltyrn lddvpafagk vttteflaka lfdqlaaair dgalgpggar irrlkvtlhe
      121 shvarawyea al
//
LOCUS       WP_181709302             429 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. MBR-1].
ACCESSION   WP_181709302
VERSION     WP_181709302.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     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=47108
     Region          31..391
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mfvqsdrhva syyaaahpap ipqrpelder idadvlvvga gfsglhtalr lalagrrvvv
       61 leasrvgwaa sgrnggqall gwscdmqple dalgrdgarl lwdsmrwaaa evrelpvrhg
      121 fdidyrpgsl waavrprrva llaqardeaa erwsydrlrv idkdempawi gsarylaalh
      181 dpeaghlnpl klalglaqti eragariyeq srvldcretp dghiartarg evradvlvla
      241 cnayvdrldp alsrrllpvg tyqvatapla palarsllph dscvidnqfv pdyfrlspdn
      301 rllfgggcty lggipadiaa atrprlervf pqlagvrldy awgghidism rrtpdigrhg
      361 qrfwlqgfsg hgvlptlaga ravadavlgd drllaqyqri rnprfpggdr faaplealgk
      421 awyrlrdtv
//
LOCUS       WP_181709455             474 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Burkholderia sp. MBR-1].
ACCESSION   WP_181709455
VERSION     WP_181709455.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 474)
  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 474)
  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 474)
  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 474)
  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 474)
  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 474)
  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..474
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     Protein         1..474
                     /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=50333
     Region          91..326
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
     Region          251..439
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mnrtmnsrna arrvfplrra allgaawaai gvagapavaq pasqsvapap tathaaqsad
       61 adlvkrgayl aragdcvach tasggkpfag glkfdtpiga iystnitpdr ntgvggwtld
      121 dfaravregm rkngdtmypa mpypsysrls dddvkalyay fmhgvapveq qnravdivwp
      181 lsmrwplgfw rkmfapapkp fdaaqygdpv vargaylvqg lghcgachtp raatmqeral
      241 tdaggldfla ggaaidgwvp tslrgeprtg lgtwseteiv rflktgrtlr taafggmtdv
      301 vghsmqhlsd ddltaiaryl ktlpprvqge qphvydaaaa talragdask pgaavyrdnc
      361 machrsdghg ytrvfpalag npvvqgddpt slihvvlegs alqgthtaps tftmppfgwr
      421 lsdqevadvs nfvrtswgns gtpitaeqva klrkrvpstr pepppgarfp qasr
//
LOCUS       WP_181709566             461 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Burkholderia sp.
            MBR-1].
ACCESSION   WP_181709566
VERSION     WP_181709566.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
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="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     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=48230
     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 masilivddd aafrdglaet lgdlghrvve aasaraalat lrdgarvdcv fldfrlpdld
       61 glavlaqlrd dpalaaipvv mltahatsdn tidamrlgaf dhltkpvgrd diarlleriv
      121 sahaplpagd aeparfages asdrprllga saamrdvqkq lgraatsdat vlitgetgtg
      181 kevaarvlha asarhagpfv avncaavpae lleselfghr rgaftgahad ragrlveadg
      241 gtlfldeigd mpaamqakll ralqerqvtp lgadcpttid lrvvaathrd laaavangtf
      301 redlfyrlnv iplhlpplae rvadilplaa hfleraagar alhltndaqr allahrwpgn
      361 vrelrnvmer aaalapgpai gaadlalgva sapasaapdd alpaylfdlp lpdalatver
      421 aailralala ngnraqaarq lgigrqslya rmaslgierd d
//
LOCUS       WP_181709723             277 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Burkholderia sp.
            MBR-1].
ACCESSION   WP_181709723
VERSION     WP_181709723.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 277)
  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..277
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     Protein         1..277
                     /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=30180
     Region          34..205
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mspvahasrw rtdtqhlhac glwrdvptrr lsadvpqasi ecrvwsvahg dwddrgcaal
       61 ldarerermr rlplerqaay arhhaalrvl laewlgvasr alviapdahg kpalpdhprl
      121 hfnlshsgpf ggvalgefpv gfdleapdga aydrlawrly afeaaalakr ggtprdpraf
      181 arlwtakeay lkatgqglrr rldsfrlrvg adarafalld dgaapparas hflvldeppa
      241 payvgtlavl aaapqddrft ygdsrsgdra spltige
//
LOCUS       WP_181709635             913 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Burkholderia sp. MBR-1].
ACCESSION   WP_181709635
VERSION     WP_181709635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 913)
  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 913)
  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 913)
  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 913)
  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..913
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     Protein         1..913
                     /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=99852
     Region          242..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 mkfvllsrap aavrrwwqrh vvdgarlpvt lglafvglam fasglgyiti shnrlnaqrv
       61 halharndid alqalylran adflqgfgst raasfawpve rvgaavaafr rleqsyagdr
      121 ggietihalr qetarwawll aeitvnaqva ggrasvdsag lleanrllaq iigqltalre
      181 gqtrilrams drasrneaie gsvlalssll tcallsyafv aryrarlerq rgrlvaaene
      241 rrfrqyfehh plpmlifdve tlaimavnva aaaqygypag elcrrdmasl yaqadmpafl
      301 rdlqhlrtsg tgsgsagicr hrrndgramy vdlsyhflty tkrdacfita idvterknae
      361 lalrlrsral daigngvlit rieageeive yanpafetit gytsaqvvgr dhaglaragq
      421 qgllfeqmaq alaagsagar llrsrradgs afwgqlyvap vrddltyhic visdltelid
      481 srdqlvrqar rdaltglpnr atlrelieqa vaeqrafall fmdvdrlkdi ndslghgagd
      541 rllreiaqrl sgcvgddgtv tryggdefva mlgrpddgdr lpallrriar alerpvqigd
      601 aqsrvqlsig vacypadgld aetllkhadl amyqakargr ntvelfqpsf aeaaerrial
      661 shrlraaleh dgfelayqpq idvrtsrvsg veallrwhdp emgavspatf iplaedigli
      721 gqlgewvlrs acgqakrwad tlpalrvsvn vsprqlasgd fcsvvrrvld asglpahqle
      781 leitegalva pgalpalral neigvliaid dfgtgyssls ylrtfhadrl kidmsfvrgi
      841 gtncadeaii railalarsl hfevvaegve rsdqlsflva egcpivqgyh fcravpaaei
      901 ptyvrsfsml sta
//
LOCUS       WP_181709776             415 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: citrate synthase family protein [Burkholderia].
ACCESSION   WP_181709776
VERSION     WP_181709776.1
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..415
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..415
                     /product="citrate synthase family protein"
                     /calculated_mol_wt=44415
     Region          4..52
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
     Region          60..381
                     /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(60,216,219,249..252,254,257,283..290,293,298,325,
                     328,330,351,355,371,374)
                     /site_type="active"
                     /db_xref="CDD:99856"
     Site            order(60,249..251,254,257,283..290,293,325,328,330,371)
                     /site_type="other"
                     /note="coenzyme A binding site [chemical binding]"
                     /db_xref="CDD:99856"
     Site            order(60,216,219,250..251,283..284,286..290,298,328,355)
                     /site_type="other"
                     /note="citrylCoA binding site [chemical binding]"
                     /db_xref="CDD:99856"
     Site            order(62..63,65..69,216,220,223..224,227..228,231..233,
                     237,244..245,248..250,290,371..379)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99856"
     Site            order(216,219,251..252,289..290,298,330,351,355,374)
                     /site_type="other"
                     /note="oxalacetate/citrate binding site [chemical
                     binding]"
                     /db_xref="CDD:99856"
     Site            order(251,289,330)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:99856"
ORIGIN      
        1 mqnwitltea arrlgvraqt vyayasrgsi avmqdpddpr kslyraedvv alcrkkqvgr
       61 kraalaasti fgaepciysg ittfskgraw yrgrdsvqla dtatleetaa llwqattpvs
      121 fdppalalpp gerdrqcaft mlatlaahgh stlgrldsal hieagqlvai vsrafgahdd
      181 agasplhthq rlaagwglds hgadllrram vlvadheits safaaritas tgaslagcll
      241 tglatlsgpl hgdasgrvra vfddvqrlga ervvdhhlks aipipgfghh lypdgdpraa
      301 allarldppt elahfvdkvt tltgqrptid valamlsvql qlprdaafgl fsiarsvgll
      361 ahcieqlrvg kvirprsryt gptlddrhlr paadddgkqt kvgvinknrl fkvve
//
LOCUS       WP_181709915             351 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia sp. MBR-1].
ACCESSION   WP_181709915
VERSION     WP_181709915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 351)
  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 351)
  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..351
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     Protein         1..351
                     /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=39774
     Region          29..340
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mptdqhavvg nqaanddavm ngwvarfqkr phtariyrre isrlrlfmar egvtlraftv
       61 ehrqryvefl lrppedligp rrprssptwk pftgcmnggs lkhaisviai ffkyakergy
      121 iesdpmlggi dlpevdappa radryfddrq lqiltdairr vgegirwnrg aarwkfernr
      181 wifhlllhtd lkraqacgar msdlqlqyid ggdqwmlsvp nrsgspvllp vgegaiealv
      241 rfrrfmqlpe lpergetlpl vplesgpdar plsetgmyqa lrtlldrale fvpasethlr
      301 ervrqatpnw mrhsfattka ainrpapsvp agadarevre dfthagavdp e
//
LOCUS       WP_181709789            3169 aa            linear   BCT 28-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Burkholderia sp.
            MBR-1].
ACCESSION   WP_181709789
VERSION     WP_181709789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 3169)
  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..3169
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     Protein         1..3169
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=346376
     Region          157..>2772
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          <2810..3000
                     /region_name="entF"
                     /note="enterobactin non-ribosomal peptide synthetase EntF;
                     PRK10252"
                     /db_xref="CDD:236668"
     Region          2897..3110
                     /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 mqdnnvlvtd hryahiarfw reslsqvagv yriaphgpgr qpahrlsrtv pltrasvdvl
       61 rrigdgdlge favaaagiaf llwkyfripv tvlgtpglaa qpsaraaaip livevrpder
      121 vddylarvaa ivedsyaaph fpldtlvrne kdmdvaqltr vvladdrvhq aptlrdddlq
      181 lqlrlargei elhhsdaiep fvidgfansl gavleaferl daavgdivas tpaerrllas
      241 fnetatagpr hptvvemfea qvartpaapa lvtdtslmsy adlnaransl ahrlredhgv
      301 gpealvgvmf drsewmivai lgilkagaaf vpldpaypae ridhiladtg lalllthsdq
      361 laqwyefsga tllldqelpg wtplpdnppc raqpaqlayv iytsgstgkp kgcllehrnl
      421 ahyigwaady yfpesttgsf glysslcfdf tltnifcplv rgktlriypq sesidtilar
      481 mfqpgsgvdt lkltpthihl leymnlgrsg vrkvivggee lapqhiatlr kidpaieiyn
      541 eygpteatvg civervddvp stvligrpia ntrvyivdda lrpvplgvpg eiciagagla
      601 rgyhqrpdvt aakfveqpyp depriyrtgd igrwlpdgri qcygrvddqv kirghrielg
      661 eveaaiaahe evvgaavivr esahgarkla ayvkgsanls madlraflaa klpdymvpsd
      721 lvpiaefpln angkldrpal laltpaaapd daavdadatp iqlellriwr dvldnpavdl
      781 agrffdyggd slqamqlvsr iwssfaveig idaifelqti gavsdlieas spragstags
      841 ivprpragdl plsfpqqrlw flaqlegpss tynvssalrf egeldverlr aavseicrrh
      901 eilrttfpav dglgvqriap paavaldvvd vateadaler laqqadrpfd laagplhrva
      961 lyrvharlhv fgivmhhivs dawssgillg elaalyagrs lpelavqyad yavwqherla
     1021 sadthrelal lsaaladapd vialptdrpr paiqqfrgav lpfqldrdra gglralaras
     1081 gtstymvvla ayalllsrys nqqdlvigsp ianrrssmte pligffanml alrvdlsgnp
     1141 sfgellarvk rvaldaysrq eipfeqvvda lalerdlsrt pvfqvvfaye kaqpdalnfp
     1201 glvttpvqve shtskfdltl hvedaddgla gaieynldlf dgstiermaa hfrtlldavi
     1261 aapdrplgel pltsdaeral vtvewnrtdv dfgdaaaqpl hrlfeqqver tpdavaavyd
     1321 gaaltyaeln aranrlahrl ialgvapdtl vgvamersld mivallailk aggayvpvdp
     1381 dypaervrfm idhaqlrwll tqqhllaalp dtgartivvd rdtsefdaal tsnpaldlsn
     1441 dnlaymiyts gstgrpkgal nthraivnri lwmqhayvld addavlqktp fsfdvsvwef
     1501 fwplvtgarl vfarpggqre tdymvelidr erittlhfvp smlrafldhp qldahctslr
     1561 rvvcsgealp hdlqqhcfer ldvklynlyg pteaavdvta wecrrddpqr ivpigrpian
     1621 triyivdaql qptpigvpge lliggtpvgr gyynepnlsa ekfitdpfsd dpharlyrtg
     1681 dlaryrpdgn ieflgridhq iklrglriep geieavlrty pavddcvvia ktedartfli
     1741 ayvatasrdi aglrdhlrgk ladymvpsqf valaslpllp ngkinrkalp apaaaddaar
     1801 pyapavtpre mllasiwqqv lqlpsvgihd nffelggdsi lsiqviaran raglrvtaqq
     1861 lfqyqtiaql aaapdahaap apvasplgda pltpvqhwff eqdldmpshy nqtvlievpa
     1921 dldaarlada frqvcehhda lrtrfsrgad gwtqevlgsg ampavfavqt vagdaaerlt
     1981 amraaaadaq rgidivhgpl laarlfraag eplarlfvai hhlavdgvsw rvlvedlhaa
     2041 yhgrplpekt tsfrewalhl qqlagsqava deaptwqall aqpvepmpvd ypaagtnnav
     2101 gdaasvsfel deaattallr rlpraydtri ndvllvalaq acsmatgnvr tridleshgr
     2161 hvadaaldls rtvgwftsih pvvlevdamq apgdalraar qqlrripadg lgyallryls
     2221 pdaavrasla alpkadilfn yhgqldtvlq qsddwrpagd dlgalraers qrthafeiva
     2281 avadgklqvd whygerlhrr qtvenlaahf kdrlldfaas vrdtawdgvd dsyplsslqq
     2341 gilfhslydl dpaayfqqfs fvvsgplqvp alrqawanam arhpvlrtaf awadrerpvq
     2401 tvlhtvdlpw sfvdwrhrda trraqdfdaf laddrqrgfd lrhaplfrct liqetdtrhr
     2461 fcwsahhiil dgwstailmk evfddylsla rsgapvavap vpgyrayldw larhpraade
     2521 rwwraeltgf raatpiagga aqpaagdaar rdtlrkqqfv lddaltarlq allrahrvtl
     2581 nvliraawal vlwrraatdd vvfgvtvsgr ppalegvesi vglfintlpl rvriaperpf
     2641 vdwlaalhaa qaamephsys slvdiqswse lpagdslfds llvfenfpva aapdlgpdei
     2701 eildvrafae snypltltvh pnerigfels hdarrvapev vrqmldtlra llerfaddpq
     2761 qltgqlvdaa saagrpgtph gapghaapav epaadaaata ravvapsade rtlleiwqri
     2821 fkrddiavtd nyfdlgghsi iaiqlmanve kafarrlpis clfenptiek lgaalatqat
     2881 sartdvlvpi rdggpaaplf llpgaggnvv yfhplahhls aahavyglea lgldgscepl
     2941 thvediaarh veriwplvga gpyylaghsf gahvalemsr qlvakgavvk llaifdasap
     3001 vdstaaaywh dwddtdwlva iaheigtflg adlqvtrddl valdpdgqag lilarigarg
     3061 swfadadsdr lraylrvyqa nfksryapqa eplpvpiall rsvehdpgdh apspeiaqlr
     3121 ldptwgwsrf stlpvavmdv pgdhltmlld phagavaahl npflektps
//
LOCUS       WP_181710128             300 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Acidithiobacillus
            ferridurans].
ACCESSION   WP_181710128
VERSION     WP_181710128.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus ferridurans
  ORGANISM  Acidithiobacillus ferridurans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
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="Acidithiobacillus ferridurans"
                     /db_xref="taxon:1232575"
     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=33436
     Region          62..274
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mmrrrkpapv lvpypgrrwr rsrpkavrri wrlpvlvfyl llafplavwt carkpapdag
       61 syrafawwsr qalrifgihl rvggvipeap vlvaanhvsy ldilalatli psrfvakkem
      121 rawpffgimg awlgtlfidr sdarasqril rqageilaag tsvtifpegt tsdgrevgdf
      181 faapfeaacw agtptipval ryedvlrpgq pdalcpfvgd dslfghlwrl aaaapltlrl
      241 eflpalapgl grrelataar qaitealqrm eqgasvtylr dprrhslrda wvawrrrhgg
//
LOCUS       WP_181709791             816 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Burkholderia sp. MBR-1].
ACCESSION   WP_181709791
VERSION     WP_181709791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 816)
  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 816)
  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 816)
  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 816)
  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 816)
  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 816)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..816
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     Protein         1..816
                     /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=88392
     Region          18..454
                     /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          589..788
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 msspetsrpa easaplaaii igagfagigm avalqragih dfvivershd vggvwrdnry
       61 pgaacdvpsh lysfsfepna nwsrvfapqp eihaylqhca rkyglarhlr fgaeveqary
      121 deagalwrva ladgttlsaa vlisgtgqls rpalpklpgi dtfrgrafhs aqwdrdypla
      181 gkrvavvgtg asaiqfvpai agdvarllvf qrspayvlpr pdrpyrrwer tlfrrlpgam
      241 klhrasiylr yesraiaftr lhglmdfavg rpfrkllard vrdpalrskl tpdypigckr
      301 illssdylaa lgrdnvelvt rgirrvtetg ietddgvhhq vdaivygtgf aateflspmr
      361 itgrdgldln dawrrgaqay lgvtvpgfpn ffmlygpntn lghnsivyml esqiahvmrc
      421 lramqrdgas aidvdprryr rynahvqqrl egsvwsgcks wyvdasghns tnwpgftlsy
      481 rwitrftgls ayrfsrplag dtaptqavvv appagrveal aaaslrgflr aafrpligpp
      541 fgarvqrrvv amlsplmpga ggtlryrtaa agvpveviap krgdaggail ylhggafcvg
      601 sprthrsvtt rlaaeaglpv wapdyrlapk hpspaavdda laaydalraq gyaphrivia
      661 gdsaggalal alaialrerg epaaaallli spvtdaalgg atlasrrhdd pmirrgwleq
      721 glrwyhgaga gasrgpldad lrglppmlvq vgdqevllsd aqrlaahara cgvpcrleih
      781 aarwhvfhlq afylqsarda lrtlagfaaq rvaapv
//
LOCUS       WP_181709956             245 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            MBR-1].
ACCESSION   WP_181709956
VERSION     WP_181709956.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 245)
  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..245
                     /organism="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     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=27391
     Region          57..244
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mdgttigava kikrlrdsds eidlhcrvhp iiralggqsy vftmvqygld anapphyryf
       61 adcapewiqi ytyrcwyaid pfleyartnl tpsvgsriel asngqremia taarygfkss
      121 lvvplhgttq etlgllhvgt dteperggee lleasaliyr llatemldir lrqlrqhaie
      181 efglqpkdlt vlqmaywnrt aaeiaatmdl sistihalnr eisgkfstkt lrqavqiaft
      241 rgllt
//
LOCUS       WP_181710133             571 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat-containing sulfotransferase family protein
            [Acidithiobacillus ferridurans].
ACCESSION   WP_181710133
VERSION     WP_181710133.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus ferridurans
  ORGANISM  Acidithiobacillus ferridurans
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 571)
  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 571)
  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 571)
  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 571)
  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..571
                     /organism="Acidithiobacillus ferridurans"
                     /db_xref="taxon:1232575"
     Protein         1..571
                     /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=64857
     Region          10..>225
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          37..65
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(38,41..42,45..46,48,72,75..76,79..80,82..83,106,
                     109..110,113..114,117)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          70..100
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          105..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          337..511
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 msmrnaildl qkgryreaig afqmvwgndr apvmmrsdal snaavchlrl hewksaedsa
       61 raavemdpah vdawfnlags lkeqgqvlda lnafrkvcel hpqrmdgwry waelaeglgl
      121 weeaadawsv vyqkmangra fegrivcmvh agkaplvdee talyldqhkt enlarylrvl
      181 vlsdlqrfde avilthkmhg pavdqlvawv lihagyliea rerikglpes arahalrima
      241 aegpevleri adartylsas rkdnpqdiad lhfrlariae eqstpaaamq hydaahrima
      301 vsqpfseegh hqldtwirlr pwlqlaplah sdgpqwifiv gmprsgttll eqildmhpaf
      361 hgagelhdma tmaqryyats ngeavsqacd afsrkvskla praawcidkm phnfvhagml
      421 lhlfprarvi wcrrdpldnc tsiyrqhfrg ihpyahdlgt lgryfrwhee vmegyrkdyp
      481 qrvlevsyet lvddmpgtvt gllralgkdw dtacarfhen prriltasqg qvnkpiyrda
      541 vgswkryrgf vepllleepg msdpanesqr r
//
LOCUS       WP_181710246             447 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Xanthomonas oryzae].
ACCESSION   WP_181710246
VERSION     WP_181710246.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..447
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47270
     Region          54..405
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 maiglfgall plalsstaqt paptaaalqp arvaqsstap lpyrtslpan qvlapaagfd
       61 vaafesmadq ltygnrvpgm amaivqggkv lsargygvtd vnhpqpvdgh tvfrlaslsk
      121 afagtmagll vndgvlrwds kvvdyvpgfq lsdgaatrql tvaevlshrv gltrnaydrd
      181 iesnvdyysl shklavaplr capgdcyayq nvafslvgdv vfaasgsfye qlverrifkp
      241 lgmndaslgl agiqasphwa rphvrsrngw vsltpkptyy rlapaagvna sasdmaqwll
      301 ahtghrtdvl papllatlha pvistpgemr sgwrhervda asyalgwrvf dyaghqvvfh
      361 agavqgyrgl vallperdlg iailwngesg lpsgmlptil dralglpakr wldidvdgdf
      421 gsenmlaekp dpagkgassg ksvaspr
//
LOCUS       WP_181710437             394 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181710437
VERSION     WP_181710437.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 394)
  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 394)
  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 394)
  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 394)
  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..394
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>394
                     /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          30..>384
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtrptlsmig lavaaalsaq aqaqqadtas ntldtvivtg trasgrtvle stvpvdvlta
       61 edirkagvvn gelgsalqal lpsfnfphqs nsgggdhira aqlrglspdq vlvlvngkrr
      121 htsslvnids kigkgttpvd fnsipinaik rievlrdgag aqygsdavag vinvilddnp
      181 esgeleasfg ayntdvapin rritdgqtsy asakvgtllg ddggffkvgl elknreatnr
      241 agfdqippfe eqtpanlalk gqrnyvlgdg atkglnawln tkipfsasge fyafgtydqr
      301 dseganyfry pdssanwrei ypngyrpise genrdlqiva gargqwgnwd ydaslnygrn
      361 dftyrlrnsl naslgpgstt rfktgdfafa qtvg
//
LOCUS       WP_181709066             526 aa            linear   BCT 28-DEC-2024
DEFINITION  cation:proton antiporter [Burkholderia sp. MBR-1].
ACCESSION   WP_181709066
VERSION     WP_181709066.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. MBR-1
  ORGANISM  Burkholderia sp. MBR-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
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="Burkholderia sp. MBR-1"
                     /db_xref="taxon:2732364"
     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=55848
     Region          67..519
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 msnvelfhyl lllicgagal twlaervsip pavvllvggc vvavagkrvp dmdpalllaa
       61 vlppllmssg fytawkefrh elasiaslal gavafttvav alavhaansa lpwaacftlg
      121 aivsppdava akailqrhpl parlvavleg eslvndasgl llyqmavsaa lavtittaga
      181 talffsltli givtglvcgh amcwvlqrvr epmlgivvtf amawgsygia eavhgsgvls
      241 vvtcglvlgv rqhrvfgadl rikakatwea vvfvldalvf iliglalhai larvnqegav
      301 lmaglrvalp ataaaiaarv vwvfvamwlp arlrapragh ppwswreavv lgwsgmrgvv
      361 slaaaialpa dfpardlilf stflliiatl vvqggtlapl irvlklrpav rhtmsehavr
      421 ahtfgaalaa ldargpdgdg lerasrerll teyrnrvafn erahrdgaqp aqvrarmlgv
      481 elemvgvsrd allalhrdgr vddavlhrie seldfeelrl qrllep
//
LOCUS       WP_181710490             431 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181710490
VERSION     WP_181710490.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..431
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          1..184
                     /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          145..>245
                     /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 irrlnletgq wqtlnypaqa gdfdyaprys pdghwivflr npqlgdlwri paeggaaerl
       61 thdtadiwgw swlpdgsgvi fgrrvdiear lyrldlldss lhdlgvddaq apdvahghlv
      121 faqrkpqfgv yqvirdtmng gyirrrlfss sgrddqpmia pdgrqlvfas nrsgtyglww
      181 gdvskpgsvr lieglrpdsr qaadwsadsq rllvsgsdaa ghaalfevtp ssgkvvrlpv
      241 pqprplqaih lpdpdqvlvl aaaddghtfa tlydrrsspw ralatlqdvs qvrldrisgq
      301 vlltrlsggg vwqvapslaa dtlqaidskq psrwryrswa pgahgdlhyl sstdtcstyd
      361 gelrsvggqc ldavkftain gfsvdqhdga lyvalaeedg ssiaymplpq rsvasicvla
      421 nllsilrkia s
//
LOCUS       WP_181710583             425 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181710583
VERSION     WP_181710583.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 425)
  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 425)
  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 425)
  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 425)
  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..425
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>425
                     /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          30..>423
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtrptlsmig lavaaalsaq aqaqqadtas ntldtvivtg trasgrtvle stvpvdvlta
       61 edirkagvvn gelgsalqal lpsfnfphqs nsgggdhira aqlrglspdq vlvlvngkrr
      121 htsslvnids kigkgttpvd fnsipinaik rievlrdgag aqygsdavag vinvilddnp
      181 esgeleasfg ayntdvapin rritdgqtsy asakvgtllg ddggffkvgl elknreatnr
      241 agfdqippfe eqtpanlalk gqrnyvlgdg atkglnawln tkipfsasge fyafgtydqr
      301 dseganyfry pdssanwrei ypngyrpise genrdlqiva gargqwgnwd ydaslnygrn
      361 dftyrlrnsl naslgpgstt rfktgdfafa qtvgnfdltr vfdavgatht fgtgaefrre
      421 qyrth
//
LOCUS       WP_181710699             212 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Vibrio tarriae].
ACCESSION   WP_181710699
VERSION     WP_181710699.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..212
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23215
     Region          2..172
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtfqaaifdm dgllldterv cmrvfqeaca acglpfqqev ylsvigcnak tingilsqay
       61 geelprlhne wrqrynavvl heaiphkdgv iallewlkar sipmavatst qkevaliklq
      121 lagldhyfan ittgcevtqg kphpeiylla aerlgvepqq clafedsnng ikaamaaqmq
      181 afqipdlvkp slevialghp ictslndvid ll
//
LOCUS       WP_181710749             413 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Vibrio tarriae].
ACCESSION   WP_181710749
VERSION     WP_181710749.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..413
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..413
                     /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=47352
     Region          64..403
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mlnsssmeis gsltswqkga rsvihralqy legnltvieh fpdqsqtkhe qfgqnksdai
       61 havievkhpd fysrvlkggs iaaaeaymeg wwespnltal mqlmaanlgt ldklesqssp
      121 vtqwlnrfth wlkrntldqa kdnihqhydl gnelyqlfld eemlyssalf aqpeisleqa
      181 qqakmerlce qlqlkptdhv leigtgwgam aiymaqhygc kvttttisee qyayaqqkit
      241 algldnqitl lkqdyrllsg qydklvsiem ieavgkaylp tflsqcyall kprgkmaiqa
      301 itiadqryes ysnnvdfiqk yifpggflps isvltelatk rtglvlrnlh digmdyaltl
      361 qhwrdrfeqq lpkvrdlgyd erfirmwryy fcyceggfla rsistvhmtf erd
//
LOCUS       WP_181710801             477 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Vibrio tarriae].
ACCESSION   WP_181710801
VERSION     WP_181710801.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 477)
  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 477)
  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 477)
  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 477)
  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..477
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..477
                     /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=51998
     Region          2..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 maqskvlive ddeglreali dtlalagyew leadcaedal lklksnsvdi vvsdvqmagm
       61 gglallrsik qhwpnlpvll mtayaniqda vsamkdgaid ymakpfapev llnmvsryap
      121 vksddngdav vadtkslkll aladkvaktd anvmilgpsg sgkevmsryi hnasprkegp
      181 fiaincaaip dnmleatlfg yekgaftgav qacpgkfeqa qggtilldei semdlnlqak
      241 llrvlqerev erlgsrksik ldvrvlatsn rdlkqyvqag hfredlyyrl nvfpitwpal
      301 cerkddiepl anhlierhck klglpvpsia pnaitkllny pwpgnvreld nvvqralils
      361 enghiqsehi llegvdwhda sslqqavage smaapqikpv aepevfkplv qgggqssssq
      421 ssglggelrd qefaiildtl aecqgrrkem aeklgisprt lryklakmrd agidipg
//
LOCUS       WP_181710912             951 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Vibrio tarriae].
ACCESSION   WP_181710912
VERSION     WP_181710912.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 951)
  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..951
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..951
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=106087
     Region          40..468
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          508..934
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrkvglfgfs llllvgcsss dssltlfssl pkgvtlveev kaepgkvmip yskyrldngl
       61 tvilspddsd plvhvdvtyh vgsareeigk sgfahffehm mfqgskhvgd qqhfrlitea
      121 ggslngttnr drtnyfetvp anqlekmlwl eadrmgflld avsqrkfeiq rdtvkneraq
      181 nydnrpyglm wekmgealyp eghpyswqti gyvsdldrvd vndlkafflr wygpnnavlt
      241 iggdldvkqt lawvqqyfgs ipkgpevvda pkqparlsed rfitledrvq qpmlligwpt
      301 qylgaedqva ldalatalgs gnnsllyqel vktqkavdag afqdcaelac tfyvyamapa
      361 gakgklaply qetlqvlekf kqqgvsasrl eqiigseeas avfalesveg kvsqlaanqt
      421 ffdqpdries qlekiravtp esvqqvftry ldgqpkvtls vvakgktdfa vrpatfitpe
      481 rqlpeyqrig deqlsyrevk dsfdrsqmpq vaqavqprlp klydvyfdng vqllgtqtre
      541 tptvlieiel pagerqvamg keglanltas llqegsqnrs aeaiqaqldk lgssiqvvag
      601 aystsivvss lkknlpetlq iveemllkpa fkqsdfarlq qqmlqgvvyq hqqpswlasq
      661 atrqvlwges lfarsgdgtq asisaltlkd vkqfyrqhyt phgaqiavvg disareirqq
      721 lqfiadwkge aaplinpqvv ptltkqkiyl vdkpgapqsi irmvrkglpf datgelyltq
      781 lanfnlagnf nsrinqnlre dkgytygags yfasnreiga ivfnapvrad vtieaiqemi
      841 kemrhfsqtg mtdeemkflr lavgqqdalm yetpaqkaql vssiltysld rdylqqrnei
      901 vksvdrstln elaakwfnpd dyqiivvgda erlkpqlekl giplegleii r
//
LOCUS       WP_181711392             581 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181711392
VERSION     WP_181711392.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     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]"
     Region          6..555
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
      541 fhkvmegalr lmdvppddiq swlaaqaagk tgqpmvkpqs a
//
LOCUS       WP_181711496             413 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SAM-dependent methyltransferase [Vibrio].
ACCESSION   WP_181711496
VERSION     WP_181711496.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..413
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..413
                     /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=47448
     Region          138..403
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mlnsssmeis rsltswqkga rsiihralqy legnltvieh fpdqtqtthe qfgqdkpdai
       61 havievkhpd fysrvlkggs iaaaeaymeg wwespnltal mqlmaanlgt ldklesqssp
      121 vtqwlnrfth wlkrntidqa kdnihqhydl gnelyqlfld eemlyssalf tqpelsleqa
      181 qqakmqrlce qlqlkptdhv leigtgwgam aiymaqhygc kvttttisee qyayaqqkit
      241 alglnnqitl lkqdyrllsg qydklvsiem ieavgkaylp tflsqcyall kplgkmaiqa
      301 itiadqryes ysnnvdfiqk yifpggflps isvltelatk rtglvlrnlh digmdyaltl
      361 qhwrdrfeqq lpkvrdlgyd erfirmwryy fcyceggfla rsistvhmtf erd
//
LOCUS       WP_181711627             951 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: M16 family metallopeptidase [Vibrio].
ACCESSION   WP_181711627
VERSION     WP_181711627.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 951)
  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..951
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..951
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=106103
     Region          40..468
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          508..934
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrkitlfgfs llllagcsss gsslplfssl pkgvtlveev kaepgkvmip yskyrlengl
       61 tvilspddsd plvhvdvtyh vgsareeigk sgfahffehm mfqgskhvgd qqhfrlitea
      121 ggslngttnr drtnyfetvp anqlekmlwl eadrmgflld avsqrkfeiq rdtvkneraq
      181 nydnrpyglm wekmgealyp eghpyswqti gyvsdldrvd vndlkafflr wygpnnavlt
      241 iggdldvkqt lawvqkyfgs ipkgpevvda pkqparlsed rfitledrvq qpmlligwpt
      301 qylgaedqva ldalasalgs gnnsllyqel vktqkavdag afqdcaelac tfyvyamaps
      361 gakgklaply qetlqvlekf kqqgvsasrl eqiigseeas avfalesvkg kvsqlaanqt
      421 ffdqpdries qlekiravtp esvqqvftry ldgqpkvtls vvakgktdfa vrpatfitpe
      481 rqlpeyqkig deqlayrevk dsfdrsqmpq vaqavqprlp klydvyfdng vqllgtqtre
      541 tptvlieiql pagerqvamg keglanltas llqegsqnrs aeaiqaqldk lgssiqvvag
      601 aystsivvss lkknlpetlq itqemllkpa fkqsdfarlq qqmlqgvvyq hqqpswlasq
      661 atrqvlwges lfarsgdgtq asisaltlkd vkqfyrqhyt phgaqiavvg disareirqq
      721 lqfiadwkge aaplinpqvv ptltkqkiyl vdkpgapqsi irmvrkglpf datgelyltq
      781 lanfnlagnf nsrinqnlre dkgytygags yfasnreiga ivfnapvrad vtveaiqemi
      841 kemrhfsqtg mseeemkflr lavgqqdalm yetpaqkaql vssiltysld rdylqqrnei
      901 vksvdrstln dlaakwfnpd dyqiivvgda krlkpqlekl gimleeleii r
//
LOCUS       WP_181711419             314 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181711419
VERSION     WP_181711419.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 314)
  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 both ends.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..>314
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          <3..274
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 lsgkggglvy fdpytgerva pprlsaafaf iedlhrnlta gkrgqavtga calillffca
       61 sglylrwprr wwsprtwwvv ewrrqgrsfl wslhavfgtw cllvyllval tgltwsytwy
      121 rdgmlallga apairgdngd nrpatidvar vqrtldgipa trsaaldlri ptragqplnv
      181 rflpdnpahd raynsldiap dsgallqrqd yallprgqql avsmfplhsg sffglpgriv
      241 vmlaslgmsv ffvtgwmlyl drrrkkrelr aarvvlqgav pasqaapwvi afasqsgfae
      301 rlawqaaahl qaag
//
LOCUS       WP_181712311             145 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181712311
VERSION     WP_181712311.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 145)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>145
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>145
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeylapr fregd
//
LOCUS       WP_181711903             364 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Escherichia
            coli].
ACCESSION   WP_181711903
VERSION     WP_181711903.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 10169520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..364
                     /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=39192
     Region          15..362
                     /region_name="THR_DH_like"
                     /note="L-threonine dehydrogenase (TDH)-like; cd08239"
                     /db_xref="CDD:176201"
     Site            order(51..53,56,169,173,193..198,217..218,222,238,
                     261..262,264,284..285,308..310)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176201"
     Site            order(51,53,81,169)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176201"
ORIGIN      
        1 mkinrivneg fmktmlaayl pgnstvdlre vavptpginq vlikmkssgi cgsdvhyiyh
       61 qhrataaapd kplyqgfing hepcgqivam gqgcrhfkeg drvlvyhisg cgfcpncrrg
      121 fpisctgegk aaygwqrdgg haeyllaeek dlillpdals yedgafiscg vgtayegilr
      181 gevsgsdnvl vvglgpvgmm amtlakgrga kriigvdmlp erlamakqlg vmdhgylatt
      241 eglpqiiael thggadvald csgnaagrll alqstadwgr vvyigetgkv efevsadlmh
      301 hqrriigswv tslfhmekca hdltdwklwp rnaithrfsl eqagdayalm asgkcgkvvi
      361 nfpd
//
LOCUS       WP_181712539             202 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Vibrio tarriae].
ACCESSION   WP_181712539
VERSION     WP_181712539.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..202
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22800
     Region          3..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(9..13,109..110,142,166..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 mairnvvfdv gnvivkwapq diaqltfgeg eesavmatav fksefwrdln kgkytetevk
       61 ralhqelgls fdtleqlffh ikntqvllsg tqqlmddllk agyrlyaltd nvneivtylk
      121 kqydfwpkft gavvssecgl lkpdpaiyqh ltdsqrilpq esvfmddmpa nvegarhqgf
      181 haiqfvdaqq araqlaqmgl hf
//
LOCUS       WP_181712625             413 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Vibrio tarriae].
ACCESSION   WP_181712625
VERSION     WP_181712625.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..413
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..413
                     /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=47438
     Region          138..403
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mlnsssmeis rsltswqkga rsiihralqy legnltvieh fpdqtqtthe qfgqdkpdai
       61 havievkhpd fysrvlkggs iaaaeaymeg wwespnltal mqlmaanlgt ldklesqssp
      121 vtqwlnrfth wlkrntidqa kdnihqhydl gnelyklfld eemlyssalf tqpelsleqa
      181 qqakmqrlce qlqlkptdhv leigtgwgam aiymaqhygc kvttttisee qyayaqqkit
      241 alglnnqitl lkqdyrllsg qydklvsiem ieavgkaylp tflsqcyall kprgkmaiqa
      301 itiadqryes ysnnvdfiqk yifpggflps isvltelatk rtglvlrnlh digmdyaltl
      361 qhwcdrfeqq lpkvrdlgyd erfirmwryy fcyceggfla rsistvhmtf erd
//
LOCUS       WP_181712575             477 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Vibrio tarriae].
ACCESSION   WP_181712575
VERSION     WP_181712575.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 477)
  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 477)
  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 477)
  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 477)
  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..477
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..477
                     /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=52085
     Region          2..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 maqskvlive ddeglreali dtlalagyew leadcaedal lklksnsvdi vvsdvqmagm
       61 gglallrsik qhwpnlpvll mtayaniqda vsamkdgaid ymtkpfapev llnmvsryap
      121 vksddngdav vadtkslkll aladkvaktd anvmilgpsg sgkevmsryi hnasprkegp
      181 fiaincaaip dnmleatlfg yekgaftgav qacpgkfeqa qggtilldei semdlnlqak
      241 llrvlqerev erlgsrksik ldvrvlatsn rdlkqyvqag hfredlyyrl nvfpitwpal
      301 cerkddiepl anhlierhck klglpvpsia pnaitkllny pwpgnvreld nvvqralils
      361 enghiqsehi llegvdwhda sslqqavage smaapqikpv aepevfkplv qgggqnsssq
      421 ssglggelrd qefaiildtl aecqgrrkem aeklgisprt lryklakmrd agidips
//
LOCUS       WP_181711913             342 aa            linear   BCT 28-DEC-2024
DEFINITION  segregation and condensation protein A [Xanthomonas oryzae].
ACCESSION   WP_181711913
VERSION     WP_181711913.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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..342
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..342
                     /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=38162
     Region          85..315
                     /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 myvdlwdrag tgttliaitq gkalqarlrp qpatvrpdvd lmnselahva tppatsappq
       61 qqemplavvh gqpvlqipqd lyippdalev ildafegpld lllylirrqn ldildipvae
      121 itrqyvdyin vmqelrfela aeylvmaail aeiksrmllp rppsqdgeed dpraelvrrl
      181 qeyerfkqaa edldtlprmg rdsapvqahl peraavklpp pvelkemlma lydvlkrael
      241 ftghaikrea lsvrqrmgdv lsrlddgkfy rfeslftaee gklgvlvtfl allelakeql
      301 ldivqeapla piyvkslalg ntnaplqfss efddsdaane pl
//
LOCUS       WP_181712102             473 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181712102
VERSION     WP_181712102.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 473)
  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 473)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..473
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          39..226
                     /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          187..>287
                     /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 tgpaaarevv rcdradmlsf swspdarall fgsmtgsyga arirrlnlet gqwqtlnypa
       61 qagdfdyapr yspdghwivf lrnpqlgdlw ripaeggaae rlthdtadiw gwswlpdgsg
      121 vifgrrvdie arlyrldlld sslhdlgvdd aqapdvahgh lvfaqrkpqf gvyqvirdtm
      181 nggyirrrlf sssgrddqpm iapdgrqlvf asnrsgtygl wwgdvskpgs vrlieglrpd
      241 srqaadwsad sqrllvsgsd aaghaalfev tpssgkvvrl pvpqprplqa ihlpdpdqvl
      301 vlaaaddght fatlydrrss pwralatlqd vsqvrldris gqvlltrlsg ggvwqvapsl
      361 aadtlqaids kqpsrwryrs wapgahgdlh ylsstdtcst ydgelrsvgg qcldavkfta
      421 ingfsvdqhd galyvalaee dgssiaympl pqrsvasicv lanllsilrk ias
//
LOCUS       WP_181712668             951 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Vibrio tarriae].
ACCESSION   WP_181712668
VERSION     WP_181712668.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 951)
  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..951
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..951
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=106063
     Region          40..468
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          508..934
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrkvglfgfs llllvgcsss dssltlfssl pkgvtlveev kaepgkvmip yskyrldngl
       61 tvilspddsd plvhvdvtyh vgsareeigk sgfahffehm mfqgskhvgd qqhfrlitea
      121 ggslngttnr drtnyfetvp anqlekmlwl eadrmgflld avsqrkfeiq rdtvkneraq
      181 nydnrpyglm wekmgealyp eghpyswqti gyvsdldrvd vndlkafflr wygpnnavlt
      241 iggdldvkqt lawvqqyfgs ipkgpevvda pkqparlsed rfitledrvq qpmlligwpt
      301 qylgaedqva ldalatalgs gnnsllyqel vktqkavdag afqdcaelac tfyvyamapa
      361 gakgklaply qetlqvlekf kqqgvsasrl eqiigseeas avfalesveg kvsqlaanqt
      421 ffdqpdries qlekiravtp esvqqvftry ldgqpkvtls vvakgktdfa vrsatfitpe
      481 rqlpeyqrig deqlsyrevk dsfdrsqmpq vaqavqprlp klydvyfdng vqllgtqtre
      541 tptvlieiel pagerqvamg keglanltas llqegsqnrs aeaiqaqldk lgssiqvvag
      601 aystsivvss lkknlpetlq iveemllkpa fkqsdfarlq qqmlqgvvyq hqqpswlasq
      661 atrqvlwges lfarsgdgtq asisaltlkd vkqfyrqhyt phgaqiavvg disareirqq
      721 lqfiadwkge aaplinpqvv pmltkqkiyl vdkpgapqsi irmvrkglpf datgelyltq
      781 lanfnlagnf nsrinqnlre dkgytygags yfasnreiga ivfnapvrad vtieaiqeii
      841 kemrhfsqtg mtdeemkflr lavgqqdalm yetpaqkaql vssiltysld rdylqqrnei
      901 vksvdrstln elaakwfnpd dyqiivvgda erlkpqsekl giplegleii r
//
LOCUS       WP_181711502             142 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HIT family protein [Vibrio].
ACCESSION   WP_181711502
VERSION     WP_181711502.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 142)
  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 142)
  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 142)
  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 142)
  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 10472213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..142
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16130
     Region          9..101
                     /region_name="HIT"
                     /note="HIT domain; pfam01230"
                     /db_xref="CDD:395984"
ORIGIN      
        1 mahfelhpql qkdtdvighf plcvallhkd savpwvilvp qradlrelhh lpmdeqqqfl
       61 vesqlvcqtl etlfypdkln lgalgnmvpq lhihhiarft hdmawpgpvw grtqgvfrtq
      121 qeqaalltql rdalakhalf ka
//
LOCUS       WP_181712939             216 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Vibrio].
ACCESSION   WP_181712939
VERSION     WP_181712939.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
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="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..216
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23680
     Region          2..172
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mkfqaaifdm dgllldterv cmrvfqeact acglpfqqev ylsvigcnak tingilseay
       61 gedlprlhne wrqrynavvm heaiphkdgv iallewlkar siptavatst qkevaiiklq
      121 lagldhyfan ittgcevtqg kphpeiylla akrlgvepqq clafedsnng ikaamaaqmq
      181 afqipdlvkp spevialghp ictslnevid llspnh
//
LOCUS       WP_181712948             420 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Vibrio paracholerae].
ACCESSION   WP_181712948
VERSION     WP_181712948.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 420)
  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 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   3  (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   4  (residues 1 to 420)
  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..420
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..420
                     /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=47497
     Region          1..410
                     /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 mkstvllidd dqdvldsylh lmsiagltak avidptqams hiqpdwngvv lldmympqlh
       61 gmellkqika vdekipvivi tghgdipmav eavkmgacdf lekpinppql ltlikqhlel
      121 rrsfieqkll lsrsvkrelv gksaqmeqir shvaqyalln shvvivgesg cgrhtiayli
      181 hqltinnghl plvelvasak tewstvepkv qesaggtlli dhieqlseev qrnlvqslln
      241 qerlnrprtr viavidrppe qliaqnqllp elyyllnqgq idvpmlrqrp ddiaalfhyf
      301 lkqscyklgk pmpnvephyl allrahqwpg nvrelrnvae lyaigivkla gkervynqee
      361 mlspldelvd dyekqvieda lflfsgrvad aanylqvprk klylrmkkhg lekdafkarg
//
LOCUS       WP_181713163             142 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181713163
VERSION     WP_181713163.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 142)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>142
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>142
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeylapr fr
//
LOCUS       WP_181713220             554 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181713220
VERSION     WP_181713220.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     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]"
     Region          6..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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
      541 fhkvmegalr lmdv
//
LOCUS       WP_181713445             413 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Vibrio tarriae].
ACCESSION   WP_181713445
VERSION     WP_181713445.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..413
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..413
                     /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=47267
     Region          64..403
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mlnsssmeis gsltswqkga rsvihralqy legnltvieh fpdqtqtkhe qfgqdkpdai
       61 havievkhpd fysrvlkggs iaaaeaymeg wwespnltal mqlmaanlgt ldklesqssp
      121 vtqwlnriah wlkrntieqa knnihqhydl gnalyqlfld dsmlyssalf tqpelsleqa
      181 qqakmqrlce qlqlkptdhv leigtgwgam aiymaqhygc kvttttisee qyayaqqkit
      241 alglnnqitl lkqdyrllsg hydklvsiem ieavgkaylp tflsqcyall kprgkmaiqa
      301 itiadqryes ysnnvdfiqk yifpggflps isvltelatk rtglvmrnlh digmdyaltl
      361 qhwrdrfeqq lpkvrdlgyd erfirmwryy fcyceggfla rsistvhmtf erd
//
LOCUS       WP_181713588             175 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181713588
VERSION     WP_181713588.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 175)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>175
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>175
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeylapr fregdyaggi saatatlagl iegealpppv sghad
//
LOCUS       WP_181713681             549 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181713681
VERSION     WP_181713681.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 549)
  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 549)
  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 549)
  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 549)
  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..549
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>549
                     /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          6..549
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
      541 fhkvmegal
//
LOCUS       WP_181713747             138 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181713747
VERSION     WP_181713747.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 138)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>138
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>138
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeyla
//
LOCUS       WP_181713848             167 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181713848
VERSION     WP_181713848.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 167)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>167
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>167
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeylapr fregdyaggi saatatlagl iegealp
//
LOCUS       WP_181713858             591 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181713858
VERSION     WP_181713858.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     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]"
     Region          6..555
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
      541 fhkvmegalr lmdvppddiq swlaaqaagk tgqpmvkpqs adldpalvpd p
//
LOCUS       WP_181713932             305 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Xanthomonas oryzae].
ACCESSION   WP_181713932
VERSION     WP_181713932.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..305
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..305
                     /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=34215
     Region          23..304
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 masitsaarv qtprdasspv qrsgvriapf dgplgaevig ldlsqpldad afarlhrahl
       61 dhhvlvfrdq rispaqqvef srrfgalqih vlrnfqlrgh pevlvvsnik engepiglgd
      121 aghdwhsdls yretpslgsl lhaqqlpseg gdtlfanqhl awqtlpeslt rtvqdlraeh
      181 sylaryealr arnpwcpalt peqiaevtpv hhpvvrthpe tgrkalfvse hfttrilglp
      241 edesrallqt lfahstrpal vyrhrwqpyd mvfwdnrsvm hlaagtpdhl rrrlnrttie
      301 gdapl
//
LOCUS       WP_181713976             893 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-mannosidase [Xanthomonas oryzae].
ACCESSION   WP_181713976
VERSION     WP_181713976.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 893)
  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 893)
  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 893)
  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 893)
  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 893)
  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..893
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..893
                     /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=99976
     Region          39..>704
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          711..799
                     /region_name="Mannosidase_ig"
                     /note="Mannosidase Ig/CBM-like domain; pfam17786"
                     /db_xref="CDD:465505"
     Region          806..879
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; pfam17753"
                     /db_xref="CDD:465483"
ORIGIN      
        1 mplfrprsvp aaarlglala faisqawaap psavtldagw qvrlvpgqeq aktypkaaaw
       61 lpaqvpgavq tdliaakivp dpfyrdnegk iqwaglsdwq yqthfnvdaa tlkrehvelv
      121 fdgldtfaev tlngkqllsa dnmfrqwrvd aksllkrgdn vlevklyspi kkiqpwlakq
      181 pyalpgayds afgdepearh sstyvrkapy nfgwdwgprm vnagiwkdvr veawdavrvd
      241 glhiaqqrvd aesaqlqaql elqagrsgpv qvtldvlgpd gqnvgqftqd avvdpgqnri
      301 alavriakpk rwfpagygaq drytfvasvr dadgdsqqik rvtglrsvel rrekdtfgks
      361 meivingipi fakganlipl dafparvthd rmrstlqdar danmnmlrmw ggghyqddyf
      421 ydvadalgim iwqdfmfgga vppydvefre ntrqeaieqv krlrdhpsiv lwcgnnevqt
      481 gwenwgdrvk fkqsvdpeer sriergmttl fgtvfrevva tydsdvpywa tspgtdfdga
      541 adqandgdmh ywkvwggpal pvteylnvtp rfmseyglqs fpdmrtvraf aepgdldpes
      601 pvmrvhqkfd kgngnkrlml yirrefgepk dfesfvylsq lmqaegihia ashlrasrpq
      661 smgslywqln dvwpgaswss vdyygrwkal hyharrfyap emiaalrndk gqtevslvsd
      721 rttplaarwr mrvmrmdgkv lskrednasv kplsslqvgn fsdkqllgsa dpkhtyavfe
      781 lfdgntllsr emvffapakq lalptakids qwrtdgdgya ltltsntlar nvwlsfgdvd
      841 atlsdnafdl lpgepltvhv sskvaltqlq salkvrdlaa tlagappepa eak
//
LOCUS       WP_181713711             180 aa            linear   BCT 28-DEC-2024
DEFINITION  segregation and condensation protein A, partial [Xanthomonas
            oryzae].
ACCESSION   WP_181713711
VERSION     WP_181713711.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 180)
  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 180)
  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..180
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>180
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
     Region          85..>180
                     /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 myvdlwdrag tgttliaitq gkalqarlrp rpatvrpdvd lmnselahva tppatsappq
       61 qqemplavvh gqpvlqipqd lyippdalev ildafegpld lllylirrqn ldildipvae
      121 itrqyvdyin vmqelrfela aeylvmaail aeiksrmllp rppsqdgeed dpraelvrrl
//
LOCUS       WP_181714238             150 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181714238
VERSION     WP_181714238.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 150)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>150
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>150
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeylapr fregdyaggi
//
LOCUS       WP_181714015             432 aa            linear   BCT 28-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Xanthomonas
            oryzae].
ACCESSION   WP_181714015
VERSION     WP_181714015.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 432)
  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 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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..432
                     /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=46313
     Region          28..432
                     /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 mppspaplpr llpasvigrg qmwlaacvla ctllgslgas aqsqreterk lqqlrdelkt
       61 isadrreleg krgtaaqqlr qadekvakta ralneteaam raqaqhlstl qqeraqlqrg
      121 lqnqraqlaa llraadqvgr naplkvllsq dtvgdatrml adhryvqnar aqrihalttq
      181 lhaltkveqd iatrrqalda araqqkaqaa tlqkdlsqqa atvaqlddry kqraerekai
      241 gqdakaleql lanlraaaak aeaerraaak raaaeaaaqa rrgktdrpdr pgktppkvva
      301 sapapkvggl swpvsgnlla rfnatlpdgh tskgvligap kgttvtavad gtvvfsdwmt
      361 gygmilivdh gngymslyah ndtllrdaga sikrgeavak vgssggqgvp alyfelrrng
      421 qpvdpsswlq rr
//
LOCUS       WP_181714268             151 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181714268
VERSION     WP_181714268.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 151)
  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 151)
  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 151)
  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 151)
  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 151)
  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..151
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>151
                     /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..>134
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 msasyvsagr teqgnvrrrn edaillrddl glwavadglg ghsagdlasr mvvdalgalr
       61 rdgdlarfvd aidaqlnqvn rqlralarar rvdviastvv vlvhdhellm cgwvgdsray
      121 afeegrlqll trdhvagdkd dltqvgraqp a
//
LOCUS       WP_181714288             576 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181714288
VERSION     WP_181714288.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 576)
  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 576)
  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 576)
  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 576)
  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..576
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>576
                     /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          6..555
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
      541 fhkvmegalr lmdvppddiq swlaaqaagk tgqpmv
//
LOCUS       WP_181714410             104 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181714410
VERSION     WP_181714410.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 104)
  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 104)
  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 104)
  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 104)
  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 104)
  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..104
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>104
                     /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..>103
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 msasyvsagr teqgnvrrrn edaillrddl glwavadglg ghsagdlasr mvvdalgalr
       61 rdgdlarfvd aidaqlnqvn rqlralarar rvdviastvv vlvh
//
LOCUS       WP_181714459             141 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181714459
VERSION     WP_181714459.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 141)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>141
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>141
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 egaiaditan riiqeylapr f
//
LOCUS       WP_181714513             138 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181714513
VERSION     WP_181714513.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 138)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>138
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>138
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvarddr rvriqpgygl
      121 egaiaditan riiqeyla
//
LOCUS       WP_181714665             951 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Vibrio tarriae].
ACCESSION   WP_181714665
VERSION     WP_181714665.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 951)
  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..951
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..951
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=106078
     Region          40..468
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          508..934
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrkvglfgfs llllvgcsss dssltlfssl pkgvtlveev kaepgkvmip yskyrldngl
       61 tvilspddsd plvhvdvtyh vgsareeigk sgfahffehm mfqgskhvgd qqhfrlitea
      121 ggslngttnr drtnyfetvp anqlekmlwl eadrmgflld avsqrkfeiq rdtvkneraq
      181 nydnrpyglm wekmgealyp eghpyswqti gyvsdldrvd vndlkafflr wygpnnavlt
      241 iggdldvkqt lawvqqyfgs ipkgpevvda pkqparlsed rfitledrvq qpmlligwpt
      301 qylgaedqva ldalatalgs gnnsllyqel vktqkavdag afqdcaelac tfyvyamapa
      361 gakgklaply qetlqvlekf kqqgvsasrl eqiigseeas avfalesveg kvsqlaanqt
      421 ffdqpdries qlekiravtp esvqqvftry ldgqpkvtls vvakgktdfa vrsatfitpe
      481 rqlpeyqrig deqlayrevk dsfdrsqmpq vaqavqprlp klydvyfdng vqllgtqtre
      541 tptvlieiel pagerqvamg keglanltas llqegsqnrs aeaiqaqldk lgssiqvvag
      601 aystsivvss lkknlpetlq itqemllkpa fkqsdfarlq qqmlqgvvyq hqqpswlasq
      661 atrqvlwges lfarsgdgtq asisaltlkd vkqfyrqhyt phgaqiavvg disareirqq
      721 lqfiadwkge aaplinpqvv ptltkqkiyl vdkpgapqsi irmvrkglpf datgelyltq
      781 lanfnlagnf nsrinqnlre dkgytygags yfasnreiga ivfnapvrad vtieaiqemi
      841 kemrhfsqtg mtdeemkflr lavgqqdalm yetpaqksql vssiltysld rdylqqrnei
      901 vksvdrstln elaakwfnpd dyqiivvgda erlkpqlekl giplegleii r
//
LOCUS       WP_181715210             192 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Vibrio tarriae].
ACCESSION   WP_181715210
VERSION     WP_181715210.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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 192)
  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..192
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..192
                     /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=20946
     Region          5..166
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mahdwdeyaa nwekdpatha faqsvfehlt kilplqgkhi ldfgcgtgll sqrmsplard
       61 ivaldsseam ieeldrkelr nvepvvdslt rglvaqhpaf rkqfdlvvas svcaflpnlq
      121 dvadiiftlv deggyfvhfd wladgksetg lattdiesvl hiagfssvet qmafdvttaq
      181 gtqsvvvgia rk
//
LOCUS       WP_181715410             300 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-methyltransferase [Gammaproteobacteria].
ACCESSION   WP_181715410
VERSION     WP_181715410.1
KEYWORDS    RefSeq.
SOURCE      Gammaproteobacteria (g-proteobacteria)
  ORGANISM  Gammaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Gammaproteobacteria"
                     /db_xref="taxon:1236"
     Protein         1..300
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=33443
     Region          27..288
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mpkaktaaps gveriqrpep ltlrgstlfe gdaltvlrrl psgsvrcvvt sppywglrdy
       61 gieeqigleg tmpqflhrlv aifaevrrvl tddgtlwlni gdgytsgnrg yrapdkknpa
      121 ramdvrpdtp eglkpkdlig ipwrlafalq ddgwylrsdi vwnkpnampe svkdrpsrsh
      181 eflfmltkse kyyydwqavr epadggglrn rrsvwhvntk pfagahfatf ppdlirpciq
      241 astepgdyvl dpffgsgtvg lvcqdenrqy vgielnpeyv alaadrlqgq dsnviriaaa
//
LOCUS       WP_181715487             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181715487
VERSION     WP_181715487.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..190
                     /product="TolB family protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          <2..119
                     /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 lfastrpgga ggsdlyrapv daqgvvgavq svgtainsag neraptlsld gmrllfasdg
       61 hggaggmdlf vahwdgkafs qpvalvdins aadeldaawl gdgralvwtr gktdgpsqll
      121 latckdghfa qglplplsfn gpqertfgav vdtakpgell vtgsarapra gqldiyrmka
      181 paadgdascr
//
LOCUS       WP_181715546             212 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Klebsiella pneumoniae].
ACCESSION   WP_181715546
VERSION     WP_181715546.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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 10106962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..212
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=22716
     Region          1..180
                     /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(11,13,15,81,118)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238741"
ORIGIN      
        1 mrrlpvylli dtsgsmrges ihsvnvgvqa mlsalrqdpy alesvhisii tydnepreyv
       61 pltatadfqf sdievpsagg tftgaalecl iqcvdrdirr sdgeqkgdwr plvflmtdgt
      121 psdaraygea vkevqrrsfg siiacavgpk aghehlkllt dkvvaletld stafsgffkw
      181 vsasvasgss sagvttdsdt lpppppeiql vl
//
LOCUS       WP_181715953             137 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181715953
VERSION     WP_181715953.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 137)
  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 137)
  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 137)
  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 137)
  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 137)
  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..137
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>137
                     /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..>134
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 msasyvsagr teqgnvrrrn edaillrddl glwavadglg ghsagdlasr mvvdalgalr
       61 rdgdlarfvd aidaqlsqvn rqlralarar rvdviastvv vlvhdhellm cgwvgdsray
      121 afeegrlqll trdhvag
//
LOCUS       WP_181715983             123 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181715983
VERSION     WP_181715983.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 123)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>123
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>123
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriqpgygl
      121 ega
//
LOCUS       WP_181716173             139 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Cryobacterium sp.].
ACCESSION   WP_181716173
VERSION     WP_181716173.1
KEYWORDS    RefSeq.
SOURCE      Cryobacterium sp.
  ORGANISM  Cryobacterium sp.
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Cryobacterium.
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="Cryobacterium sp."
                     /db_xref="taxon:1926290"
     Protein         1..139
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=14311
     Region          9..139
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 msnekihdsi slddarrvid aaiaraeeig qpqdiavvda ggnlkahvrm dtanigsihi
       61 ainkaytsia fqtqtkdlse atrpsgdlfg lndahggriv vfpggiplvr dgrivgaigv
      121 stgsieqdqt vaeagaaal
//
LOCUS       WP_181716430             251 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Psychrobacter sp.].
ACCESSION   WP_181716430
VERSION     WP_181716430.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp.
  ORGANISM  Psychrobacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
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   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 251)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 251)
  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..251
                     /organism="Psychrobacter sp."
                     /db_xref="taxon:56811"
     Protein         1..251
                     /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=28870
     Region          1..244
                     /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 mrnielinnl firtydsqln ghthdyyqvl mplmgdismi igdrtikvsy gealvikkgi
       61 yhqfqaredf rflvanieni dflqlsldei hfamdektll yisfiekqli sahnqkiegm
      121 mfellkellg tikmskrldt rltavvytlk tniatnhtvk slaeiaclse sqfkvlfkeh
      181 lgctpnayit dlrmqaalgl ilntdtpiti vaercgydnv safirrfstv yhqtpyrlrc
      241 hnqnmkhpti s
//
LOCUS       WP_181716475             115 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Xanthomonas oryzae].
ACCESSION   WP_181716475
VERSION     WP_181716475.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 115)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>115
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          24..>115
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mrrtylkvvw mmallllpas llaqelaaip plrspvvdvt gtldagqiqq leqqalalqq
       61 rkgaqlqili vpttqpeaie qytqrvfdqw kigrkgvddg vlllvakddr rvriq
//
LOCUS       WP_181717000             434 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Psychrobacter sp.].
ACCESSION   WP_181717000
VERSION     WP_181717000.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp.
  ORGANISM  Psychrobacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  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..434
                     /organism="Psychrobacter sp."
                     /db_xref="taxon:56811"
     Protein         1..434
                     /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=48962
     Region          12..417
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makpittvtq iqkairqvkq tgeqtalpla gykglemrir psgddvtatf rhrythpyta
       61 krpymtigqf pamtleqark ahhdnmalla qridpltnre qqkqaqaaam nngfndiatr
      121 wiadktnnkd smpaaktike wqrviamavn ewgntpikdi tppmvlklcn nlqgdrvdtg
      181 rrvrsmceri ftyaighgli dvnpalqikg llktaqtthq haitkplefa qllkdidalk
      241 dsnertalql iallftrggd tvaakwadid ldaalwtlip qkgqgrsdmv delliplpaq
      301 aiailkeqhk ktgmyehvfh thrtrktkht nieklsvtls tmnnerykgk hvphgfrasa
      361 ltmiqeqlgy ahnlpdmqlg htvkdnngaa ynrakfiter temlqkwady qdelrtgtsl
      421 iranfkqpke qkqg
//
LOCUS       WP_181717029             413 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Escherichia coli].
ACCESSION   WP_181717029
VERSION     WP_181717029.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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 10669663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..413
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=44999
     Region          1..161
                     /region_name="TerD_like"
                     /note="Uncharacterized proteins involved in stress
                     response, similar to tellurium resistance terD; cl18957"
                     /db_xref="CDD:473128"
     Region          212..413
                     /region_name="vWA-TerF-like"
                     /note="vWA found in TerF C terminus; pfam10138"
                     /db_xref="CDD:401947"
ORIGIN      
        1 mnlqsgqnip lqqsairlnl qypaksgfkg epdtclflln aqgkvtgdsd fifynnlssp
       61 egavklvtgs qqssieiald rvpanvskia itvvidgedt isglsllsiq apgiadfqae
      121 tqgrsekaii lgevyrhnga wklralgqgf nggleplais fgvdvaqpap qpvkparisl
      181 ekkletrspr lvslakkasv sltknkldtl eaavafvlda sgsmsgqfsk gnvqsvldri
      241 avlaaqfddd gemdvwgfge khkkypnvtl dnldtyiqsi rgsgkrsawe nlpglggtnn
      301 eppvmeeivd yfkdskipvy vvfitdggis ktraikdair rsanypifwk fvglggssyg
      361 ilknlddftd rrvdnthffa mddfgsisde klydnlleef rpwidetkrl gil
//
LOCUS       WP_181717375             246 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase, partial [Xanthomonas oryzae].
ACCESSION   WP_181717375
VERSION     WP_181717375.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 246)
  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 10536543
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>246
                     /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]"
     Region          27..74
                     /region_name="DUF1289"
                     /note="Protein of unknown function (DUF1289); pfam06945"
                     /db_xref="CDD:462046"
     Region          117..245
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 msgsdvetdv dvdvdpdpdf aagrlpspci gvcsldaqsh cvgclrslde iarwmsmsda
       61 ehqnylhtvl paraltaqlp eyaqlrraly pldtapagpg wnhaelidlt dgdasaeaav
      121 lcglvpreqg ttvlltrrtd slrhhagqvs fpggrmepsd adaaaaalre sceeialgaq
      181 qvhalgyldp fltvsgfrvt pvvavidpaf vavpqpdeva dvfevplayl mdpdnlrsve
      241 lefrgc
//
LOCUS       WP_181717886             249 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family transcriptional regulator [Sporosarcina sp.].
ACCESSION   WP_181717886
VERSION     WP_181717886.1
KEYWORDS    RefSeq.
SOURCE      Sporosarcina sp.
  ORGANISM  Sporosarcina sp.
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Sporosarcina.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 249)
  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 249)
  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 249)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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   8  (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 10581578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Sporosarcina sp."
                     /db_xref="taxon:49982"
     Protein         1..249
                     /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=28349
     Region          36..104
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 mtltnttety qslqpfftin elndntklir erhakdltrs tyrvldvlhr ysskyygvsy
       61 rskskiavel gisrktvtra cqqleslgii qqhelkrhng drrrssnaiv firlepskie
      121 nvptecpkee tplntnnnpk itldtkrgfr gdkipafiyd alspflsesa mykaysallr
      181 gkaaidrtit fesneglftd ailsvingyk rgvvrsisav lytvafdtaa qiyrkenykv
      241 pdwleiath
//
LOCUS       WP_181717937             138 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Sphingomonas sp.].
ACCESSION   WP_181717937
VERSION     WP_181717937.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp.
  ORGANISM  Sphingomonas sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 138)
  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 138)
  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 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   4  (residues 1 to 138)
  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..138
                     /organism="Sphingomonas sp."
                     /db_xref="taxon:28214"
     Protein         1..138
                     /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=14853
     Region          7..132
                     /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(8..10,24,41..43)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133412"
     Site            order(55,58,62..63,72,83..84,87,90,94,100,104,107..108,
                     115,120..121,126,128)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133412"
     Site            order(83,118,126)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:133412"
ORIGIN      
        1 mrdekglaig elsrrtgvni etiryfervg ivatpprtsg grrvygashv ralgfirrar
       61 elgftpaevr ailslgdpaq ascsevrdia ahhlervrak madltqlesl lattidrceg
      121 dgaascavie lldqhtta
//
LOCUS       WP_181718156             344 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)H-dependent flavin oxidoreductase
            [Pseudoalteromonas].
ACCESSION   WP_181718156
VERSION     WP_181718156.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 344)
  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..344
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..344
                     /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          7..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 mnlcsilgie kpiiqapmag vqnwelaaav snsgglgsip cgmltkdqvl feiinfrkhs
       61 nktynlnffc hkmpeinhqt leaweeqllp yyesfsikpl neisglrvpf danladaiep
      121 hkppilsfhf glpsaelvtr ikswgtviis sattkeegvw leengadivi aqgyeagghr
      181 smfmtsdast qlptlelvac lkhelsvpvv aaggiatstd ikemirlgas gvqvgtsyll
      241 cdeaktsaih rqaiksknsv taltnifsgr largitnkim kelnfitska pefpyasiai
      301 gplrskaesq gksdftplws gtdrsgckei satkltyelw gdgi
//
LOCUS       WP_181718470             437 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Psychrobacter sp.].
ACCESSION   WP_181718470
VERSION     WP_181718470.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp.
  ORGANISM  Psychrobacter sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 437)
  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 437)
  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 437)
  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..437
                     /organism="Psychrobacter sp."
                     /db_xref="taxon:56811"
     Protein         1..437
                     /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=49216
     Region          6..418
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 msisittdtq lrkairqvvq tgkqaalpla gykgleirir ptgndakatf rhrykspytn
       61 krpymtlgey pfmsleqarr ahhdnmamla qridpmvhre qerlaqiaam nngfadvanr
      121 wlvdrvnnqg skpapstlks wenaineavk ewgdtpikdi tapmvlklck hvqtdrvslg
      181 lrvrgiceni ftyaighglm dtnpasnikg llrttktvhq haitnpvkfg qmlkdldalh
      241 dsyertalll mallftrsgd mvaakwsdid ldkaqwelvp qkgqgrsdmv dsliiplpaq
      301 aiallkeqhk ktgmyehvfh shktlkaphi gkhrlnyain sikdgyykgk hvphgfrasa
      361 ltmiqeqlgy phylpdmalg havkdingga ynrakfiler remmqayady qdalragkfa
      421 nvihasfkqq tqtqkhg
//
LOCUS       WP_181717044             175 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase, partial [Xanthomonas
            oryzae].
ACCESSION   WP_181717044
VERSION     WP_181717044.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 175)
  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..175
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>175
                     /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          14..>175
                     /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 mtgfsnvdaf qqrfglrlpi llspmagacp vplsaavada ggmgamgavl sqpqdivawm
       61 aafreagagp aqvnlwipdp apvrdaaaea rlraflsqwg pmvpetacda mpvdfdaqfd
      121 allaarpava lsimgvfqpe qvarlkgagi awfacatsld ealvaqaaga davva
//
LOCUS       WP_181718628             518 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Pedobacter sp.].
ACCESSION   WP_181718628
VERSION     WP_181718628.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp.
  ORGANISM  Pedobacter sp.
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 518)
  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 518)
  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 518)
  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 518)
  AUTHORS   ter Beek,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 518)
  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 518)
  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..518
                     /organism="Pedobacter sp."
                     /db_xref="taxon:1411316"
     Protein         1..518
                     /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=57210
     Region          61..509
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mgraiktyvi hylltlvlll lllvpllmvl fqwllnagki nalsfldrda lllimnslll
       61 satvallatv igtacgflly kthlkgrriy llllivpili spyifavawk dllfllfgga
      121 asvystagvi avhtliyfpl allitgnaft tisssledag lmitsfrkmv fkillplirp
      181 aftssfllil ifslsdfsvp affgvktftv eiftqfsafy nynaaitksm llvgvclill
      241 lsearylsaa affsvstrgs sskvyempdk ryffhaafai liilsmlmpv fillyqslsg
      301 reivldsawe llkpavfqsi klafwgamli siiglyagyr qerlkspfin illlilfilp
      361 stilgiafir fynrpetgfi ysslfivllg yigkygfias ritgngirqi pvsleeaaev
      421 lgvspvsrfi killpllsps lfvsfvltfv lclgelgtti mvyppgtelm pvkiftisan
      481 apqaltssma ligllitlff itlfsmagrl ifnryshg
//
LOCUS       WP_181718705             176 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Nocardia gipuzkoensis].
ACCESSION   WP_181718705
VERSION     WP_181718705.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 176)
  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 176)
  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 176)
  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 176)
  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..176
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..176
                     /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=19649
     Region          74..163
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mreppwlvqp laaeytysla echiscwrea yrglvpdhvl dafdierrae lwerdrvryp
       61 grthiaived vvigfagagp pddadavtpl elhalyvrsr whgsgvaddl iraaldpaap
      121 cslwvferna raqafyrrhg fvldgtrkle sftaavevrm vrtptmhadf apggap
//
LOCUS       WP_181718757             458 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181718757
VERSION     WP_181718757.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..458
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48180
     Region          146..456
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
     Region          <306..>333
                     /region_name="EfeO"
                     /note="Iron uptake system EfeUOB, periplasmic (or
                     lipoprotein) component EfeO/EfeM [Inorganic ion transport
                     and metabolism]; COG2822"
                     /db_xref="CDD:442070"
ORIGIN      
        1 mrsgrligla lfviaalvag csesnppept igdwhgaiev pgqplqigvs frddgtatid
       61 iplqgvtgaq lkdvssdrng vsfaipdipg dpvfrgeyes gtdritgdft qagqsfrlal
      121 srgkveppar pqepkppfpy ktedvtyrng ditlagtlte pqgsgpfpai lmitgsgpqd
      181 rneelmghkp fllladtftr agyavlrsdd rgvggtggkl ddanyadlae daaagvrflr
      241 arpdidpari glfghseggy laplvaarpd sgvafavlma gpgvpgsdvl veqtrliaaa
      301 ngtppdqvda rvrdtaelaa llkagdldga kqlavrqnqa lpadqrvpdd qaaaqitpyl
      361 aalvgydpap alvalrvpvl affggrdlqv paaqseqpmr dhlaadpdat vhvfpglnhl
      421 mqptetgrps eystiettva pevldyvtgw lrqrvpak
//
LOCUS       WP_181718713             320 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nocardia gipuzkoensis].
ACCESSION   WP_181718713
VERSION     WP_181718713.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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 320)
  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..320
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..320
                     /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=35048
     Region          23..148
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
     Region          158..306
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mnartgfeqe ggpfwdprit anihaagavl wrttaggaie ialvhrpkye dwslpkgkld
       61 pgetpilaav revreetgle srlgrylghv typipghrkl krvdywaaev vsgeftanse
      121 vdllswhpld rvmdqlsypm drqvvraftr lpartktlll vrhgkagrrd ryhgpdelrp
      181 ldregegqar alvsnllafg asevysadpl rcvqtvapla eklgveihte plfsesgyae
      241 qpgeagerlr alvsdsavrv vcsqgkvipd llsglaerdg lalpsarnrk gsvwvlsfag
      301 prlvaadhld rslsayvvps
//
LOCUS       WP_181718820             315 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181718820
VERSION     WP_181718820.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=34608
     Region          18..296
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mtavhetpvs natdhavrva pvagyigadi sgvdlreplt dqqvaaitda lhtykvlffr
       61 dqhidhaqqi afsrrfgavt pshpydddap tehpeilavd srlyekrfgv rkfsytnhwh
      121 tdvsalinpp aasilraeia perggdtgwt nlvaayenlp eslqrfvegl raehrfggsr
      181 pawdadsdya kkvaatplit ehpvvrvhpv tgeralfvnp gfttrivglr psqsdavlkl
      241 lfdevtnlay tvrfrwetgs lafwdnrata hlapsdldhl dvtrvlyrtt legdipvgid
      301 gepsksvagv kftga
//
LOCUS       WP_181718866             246 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Nocardia].
ACCESSION   WP_181718866
VERSION     WP_181718866.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 246)
  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 246)
  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 246)
  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 246)
  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..246
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..246
                     /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=25535
     Region          1..232
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msartalitg gsrgigaeva rrlagegyhl tlaartaetl eetaarlrge tgaevhpvva
       61 qmndldqvra lvqaheerfg gmnalvlsag tgtagnvadl aakayermld vnfrapltli
      121 qaalpllrks adtdrergak iialasitgv ageaglaayg atkaalislc etvsleesgn
      181 gvsatavspg yvdtdmtawk rdvldrsaml tpgdvaemvl aitrlsrnav vpnivlsrag
      241 dqlwra
//
LOCUS       WP_181718925             484 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181718925
VERSION     WP_181718925.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 484)
  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 484)
  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..484
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..484
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50845
     Region          20..375
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msntmnwdet gawqvrgdwg stdsagrrfs varwqakldr llaehhvpga alavlvdgqi
       61 yeiaagvlhr gtrvpvttds vflcgsiakv ytatlimrlv dageldldap vvdvlpefat
      121 pderatasit irqllshtgg vtndfnhdtg rgddclaayv eaardvaldc apgtamsygs
      181 lgyvvlgrvv evltgktwde avhdmlavpl gldrlvtlpe qalkfrvams hlgaagvdpd
      241 papewdampr svapaarvit sagdmvrfar mhldggraad ggevlsaasv aamqrrevdv
      301 pdkwtvsadg wglgwtlydw dgvkgfghdg aaigqyaylr avpgagvava lltngggarp
      361 lcsalfgell aeladvrvpd afgpadppva vdiapfvgty rragveitvt krddgtghmr
      421 yefvdgmagl spalsmdltp vgptvfaasg agpsfsddym pvvfatladg teccyvgmra
      481 tpkv
//
LOCUS       WP_181718889             454 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181718889
VERSION     WP_181718889.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..454
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..454
                     /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=48597
     Region          8..451
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtdvdfcvig ggfagltaal rlrqmgrsva lleardrlgg rtftevredg swidrggawi
       61 gpgqdriqal mtefgvpsyk qytdgeammv vdgkqhrytg tipwtmspwa amnlgavfle
      121 lghmcksvpl eapwaakkad kwdqvslahw lesnilskpa hdlletaiag cytsaasevs
      181 llfvlyqmas gggpsfvlgv kdaaqdarpv ggmgaiyrpm aaelgdsihl sqpvrcihqd
      241 adgvrvraed ltvrarraiv avplaiadki sykpmlpvdr sflhqrmpsg siiktsvvyd
      301 epfwrgdgls gqsaapgspa titidactdt grpgvlcvii egpiarhvgr lddaerrgav
      361 lgalverfgr kagspvdyie qdwsaerysg ggmlshaptg vltqfghalr epcgrihwag
      421 tessavmcgw idgairsger aasevlehet avvg
//
LOCUS       WP_181718958             283 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MlaE family ABC transporter permease [Nocardia].
ACCESSION   WP_181718958
VERSION     WP_181718958.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..283
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..283
                     /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=29446
     Region          17..238
                     /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 mafviesrfp rtvrrmrrms dsldslgkha vfyaqaigai pralihyrte tirliaeism
       61 gtgalavigg tvvivgfltl faggtiavqg ysslgnigve altgffaafi nvriaapvis
      121 giglaatiga gstaqlgamr vaeeidales mairpvpylv atrvlagmia ivplyalavi
      181 asflasrfat vviygqsagv ydhyfstfli psdilwsfaq aifmalavmm ihtyygynaa
      241 ggpvgvgvav gnavraslva vvtvtllisl aiygtsgnfh lsg
//
LOCUS       WP_181718992             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181718992
VERSION     WP_181718992.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..295
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32827
     Region          14..77
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(20,24,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(23,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(30..31,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          101..288
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mderdtgstl prrqlghylr dartalnlsl eklaeltdls ssvlqrlekg eatrlkvrdi
       61 halcealels dqmskaligl flqgtaksww heygtlipan fdvyvgleta arrlavyqps
      121 lvhgllqtpd yaralirvgk ptesaaehdr rvelrtkrqt mitrkyqpla ldvvlhesvl
      181 rsavggpkvm apqlhhlaev gklpnvtvri lpfmagapvg dpvgqfaile fdknlkgvav
      241 sppviyletf tgcmylekpd dvqrydrvhd slrraaldea dsrsllrqva kefsa
//
LOCUS       WP_181719018             493 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nocardia gipuzkoensis].
ACCESSION   WP_181719018
VERSION     WP_181719018.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 493)
  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 493)
  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 493)
  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 493)
  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 493)
  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 493)
  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 493)
  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..493
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..493
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54051
     Region          6..335
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 mrkpsdifdr drewealtrf vddsapgatl gvvsgrrrqg ksflleavce vadgfyfsaq
       61 eatdaeslaa igealsrhld lvapftpahw gqvidvllrm giegntpvvi defpylaran
      121 palpsiiqga yaprraerta srtrlllcgs alsfmgslls gnaplrgras lelpiatlny
      181 rraaefwgit darlallvhs vvggtpayrt emirydapad ladfddwvvr ailspgspmf
      241 learyllaee pdlrdgalyh svlnaiatgn tgrggiaghv grpvntlahp ltvledagfi
      301 trepdafran rsdfriaepl vtfyhaimrp fwpqltlaad thriwqrash rfasnvigph
      361 fericrewam lfaqeptgrn rlgdlpvqvs sgtvndpanr tthevdvvai gyaedgrppl
      421 lgigeakwne vmglghldrl rrlrelvaag gkfdvtgmrl lcfsgagfse dlqraerdge
      481 veligldely grs
//
LOCUS       WP_181719029             320 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Nocardia gipuzkoensis].
ACCESSION   WP_181719029
VERSION     WP_181719029.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=35444
     Region          12..303
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtmpmdvtiq rseavlrels rvvvgkqdel qlimiavlsg ghvliedlpg lgktliarsf
       61 aaalglqftr vqftpdllpa dllgstiydm ssgrftfrrg pvftnvllad evnrtppktq
      121 aalleamaeg qvsidgetfm lpqpfvvlat dnpieyegty plpeaqldrf aiqlrlgyls
      181 eqdetqmirr rlergaqqpq vnqvvdangl lemrqsveyv tvhpdvvsyv valasatrgh
      241 pqvevgaspr aeldlvqmsr aralllgrdy vipedvkala ipamshritl rpemwvrrir
      301 gedvitellr rlpvpratvt
//
LOCUS       WP_181719054             106 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [Nocardia].
ACCESSION   WP_181719054
VERSION     WP_181719054.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     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=10959
     Region          2..99
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mswvvlvvag lveivwsqsi kptenftrlv ptlvcfvlga tavyllsram qtlpvgtaya
       61 vftgigalga itlgivvnrd plsagrvlal alilggivla ritnpe
//
LOCUS       WP_181719102             383 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Nocardia
            gipuzkoensis].
ACCESSION   WP_181719102
VERSION     WP_181719102.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..383
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..383
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40549
     Region          4..382
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 myefgdaeia aatrvltsqr lfrymddaee tssfeaefaa tigaghglat ssgtsalicg
       61 lsalgvgpgd eviipaygfv adviavlavg avpvvceide sltmdpadva aritprtrvl
      121 mpvhmngfas dmagitelaa ahdlavleda cqaiggsfrg rrlgtfgaag afsfnqakii
      181 tageggmlvt ddrdryeraf iehdascvhd glafgrpvfg glggyrmnev saailraqll
      241 rldsilerlr vrrdllagal adlpgltrip erdpagscgt hvgyrlenae avtalrella
      301 dekafamptn afghsffewn mlherrgaah pgrnpladrf vqgadalpvs reildrsvvv
      361 gfgldldeaa tegihralsk efg
//
LOCUS       WP_181718898             209 aa            linear   BCT 28-DEC-2024
DEFINITION  YceD family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181718898
VERSION     WP_181718898.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 209)
  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..209
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..209
                     /product="YceD family protein"
                     /calculated_mol_wt=22182
     Region          23..190
                     /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 msagsgstsr pqsakrrspd agfvldvrsl grrpgtmrel rrtvtteeri gldliavpvg
       61 aqveldlqlq avsegvlvtg tvsapiegec srclepftse valrvtelfa ypdstteqtt
      121 eddeiyrlvd dlidlepvvi davglelplq plctpdcagl cpecgirmai aesghrheil
      181 dprwaglaef asgspgagsp degaadrdh
//
LOCUS       WP_181719182             411 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181719182
VERSION     WP_181719182.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 411)
  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..411
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..411
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46470
     Region          137..200
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(143,147,172)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(146,171)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(153..154,165,168,172..173)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          226..403
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mnlhllvrqs hvgvtadvgq neqsirrsvt pvtarpgvvt rraarisfpc rtvryefefc
       61 svffghvhml rsapttggsk rpepsnrcvc aerlsrwahv dsrrgkkqvi pwesrgghng
      121 mvgtksdisr ttlprrqlgr alrdarqang ytleqvaevl eisrsslgrl elgqnekvkv
      181 rdveficeyy glpenrieyl kslvsqsstk vwwqdyrsli rpgfntylql eaaatelhff
      241 qslvvpgllq taeyarnvea ypptstvdev errvalrmrr sailtrrhkp vraefllhea
      301 vlrtvvgsdr tmalqhrhia dlstrdnisi rivpfsagfp agsaippyii ldflrdepsv
      361 aytegavgtm ifeedgdvsr frtifdalrg aalqeqpsrd llrtiarrce q
//
LOCUS       WP_181719286             310 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TauD/TfdA dioxygenase family protein [Nocardia].
ACCESSION   WP_181719286
VERSION     WP_181719286.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..310
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..310
                     /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=34028
     Region          12..281
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mtvatatpst asvtrlgari garidnvrlg gdldaatvdv ihrallehkv iffrgqdhlt
       61 edgqyefaql lgspttphpt vtshgvksla idsengrans whtdvtfvdr vpkasilrav
      121 hlppyggatt wastvaayes lpeplkrlae slravhtnvy dyaartgeeq rpnsavyrae
      181 festyyeteh pvvrvhpetg eralllghfv khfvglsste shalfrlfqd rvtrlentar
      241 wnwapgdvai wdnratqhya iddyddqprk ltritlagdv pvgvdgsast iiagnaehys
      301 iiedtqplas
//
LOCUS       WP_181719021             187 aa            linear   BCT 28-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181719021
VERSION     WP_181719021.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 187)
  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..187
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..187
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=20452
     Region          8..186
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 mnqldgtdil tcvevaewee wlavnhhraa gvwlkiakkg aagttitite aldgalcfgw
       61 idshrrglda dhylqryspr rpkspwsqvn vgkaealiat grmrapgfaa iaaaqsdgrw
      121 saayapqrta tcpadlrdal ganpparnsf dqldrtaqya yflrlmkart steradqlrr
      181 mvaelag
//
LOCUS       WP_181719298             102 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Nocardia
            gipuzkoensis].
ACCESSION   WP_181719298
VERSION     WP_181719298.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=11252
     Region          6..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 mtddgvtfin vfeipaeqid efvenwhera rimrtapgfr dvrlhrallp dtrfqlvnva
       61 hwdsaeacea agahsavlas vadarktada npalyevvae yn
//
LOCUS       WP_181719401             223 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Nocardia
            gipuzkoensis].
ACCESSION   WP_181719401
VERSION     WP_181719401.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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..223
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..223
                     /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=24436
     Region          6..212
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mwyplfkyvl lgpvlrllgr pavtgldnip rtgpviiaan hlavidslyl alvvprrvtf
       61 lakqeyftgk glrgrfnrwf ysvsgqvpvd rtggsaaada laaatrilta dgvwaihpeg
      121 trspdgriyr grtgtlrvam atgapvvpvt lagtdrvnpr gsrlprfgkv riefgaplry
      181 pateqrhlvr aatdelmrem aarsgrhyvd ryaatfrtpa srr
//
LOCUS       WP_181719607             396 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nocardia gipuzkoensis].
ACCESSION   WP_181719607
VERSION     WP_181719607.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..396
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..396
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43305
     Region          139..392
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msrttpprai vdvaailler idelglrlaq rfiaeldtyr nqtqvpfeti htsctrnltl
       61 mvrhftstap ldpdppketg rlraqqgvpl aetlhafrig feflwselva earrhpsvtd
      121 amlvdlaaev walsgeysva vaaayremss elmlqreher svlvealftg viadpatlge
      181 atrilglppt gryvvvaadv pgagrealpg ietalrgaqi tsawrllpdq qigvlsvpeh
      241 realairtlr ksrarvgvsp pydaltetpq alhfarlals glgrrafgva rfddnplaml
      301 vaaapaeaer mvrlrlgpll alpyeertrl letletwfqa ggsaastger lylhansvry
      361 rlrrieeltg lsltnpaavr dlgaalealp vltrtl
//
LOCUS       WP_181719615             313 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181719615
VERSION     WP_181719615.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=32940
     Region          2..312
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 mlvvlnprsn agtalrrwkp vesvlrarhp dlsvelpada rhatelvraa varpdppavl
       61 vaaggdgmvn lvlnalmdpa tdrpravgsa lgavglgssn dfhkpvpdsa rvgsipvrid
      121 aaradlvdvg kasvlladgt ravryfllna smglvaagnh sfnqaaglig wlksrsvdaa
      181 ilatalatia thrplpvavr ggdwmhaapi tnigvlksvh faggmhydta vtradgrfdv
      241 niwaeagrlr tlglvaglya grfrrsrlav cyrdavvdlr pdrpapleld geitmvesar
      301 levlprvlkv caa
//
LOCUS       WP_181719707             233 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DsbA family protein [Nocardia].
ACCESSION   WP_181719707
VERSION     WP_181719707.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 233)
  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 233)
  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 233)
  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 233)
  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 233)
  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..233
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..233
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24179
     Region          65..221
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mssattyalg avalalivli viaairwgrd eaavrndgyg svrdpavhsv leqngsillg
       61 rpdakktidi fedplcpgcg sleriygqei aqkidagala vryrlvnfld grsrskdyst
      121 ravaanqcva eagsgpvysk fhtelfttkr pseggadlsn eelaaiagda gaaesvrqci
      181 angakvdfar ttamaqtaal gaalggsaat pavfdgttrv dtndenwvvs ltd
//
LOCUS       WP_181719766             166 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Nocardia].
ACCESSION   WP_181719766
VERSION     WP_181719766.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     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=18075
     Region          78..>147
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msledrvael errlsaleen lrpenlpadt eqwavtrlqd efaaadepng gvvfagsvrl
       61 pndqqrewqa rfttgdlied dwaetaecla algspvrlrl lreimggrrt aaelagvdgv
      121 gtsgqiyhhl rqlaavgwlh tagqgrfevp aarvvpllva lasarr
//
LOCUS       WP_181719771             490 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Nocardia
            gipuzkoensis].
ACCESSION   WP_181719771
VERSION     WP_181719771.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 490)
  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..490
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..490
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=52570
     Region          31..448
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mtvsttetit sdadlpepsd spaarrttar nslyalamrl hfyagvfvgp fvliaavtga
       61 lyaisptles ivsrdlltvt qtgtpkplte qvgaavatrp dlhlvavapa ggaedttrvl
      121 fsdpslgese rravfvnpyt aqpvgdsvvy gssgalpmrt widrlhrdlh lgepgrlyse
      181 laaswlwlva laglvvwvrr vrgrrarngw grlfavdrsq rargrtmtwh gavgmwvlpl
      241 vlllsatgmt wstyagenit elreqlswtt pavstalpgt vasghdsgsd hhggghaeha
      301 ptdstdriaq ldrvyatara egitqaaeia vpaapgnafa vkerrmpgty tvdavavdga
      361 sgavtdrlay adwplmaklt nwgiqfhmgl mfglfnqlll laamiglitv vvrgylmwwr
      421 rrptrdagrf algraprrga lrktslwvvv plvaaalvvg wfvplvgvsl laflaidvli
      481 glagrmrata
//
LOCUS       WP_181719792             512 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardia gipuzkoensis].
ACCESSION   WP_181719792
VERSION     WP_181719792.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 512)
  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 512)
  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..512
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54356
     Region          145..500
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 msawarparr isavplrvgl vivlllltat alfasgaavt salsrsltqr tdeqlydaar
       61 swaqprpmrq vitsdgraqw ipadlpaapv pprsageqpr rffelrtgad gqvyqdlpgg
      121 ngagspdlgg ttagtpktvp ssdgssmdwr vltttnqygs ttiglpltdn qetvsrliff
      181 eigtgaaall algavgylvi rrslrplrev eqtaaaiagg dlhrrvpvrg vdtevdhlar
      241 slnemlariq hgvaatease eaarrsearm rrfvadashe lrtplttirg faelyrqgas
      301 tdagmvvgri eaeaermgll vedllllarl dekrplerks vdllalagda vhnaravaar
      361 qkpspdapdr pitlaigdge gtmdvigdqa rlrqvlanll gnalthtpre aavgvrltpa
      421 pdrvridvid agpglspeat srvferfyra dasrtrgsgg tglglaivqa lvtahggrvs
      481 vqsepgrgst ftvvlpreps aapttdqpvr sr
//
LOCUS       WP_181719821             351 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181719821
VERSION     WP_181719821.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 351)
  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 351)
  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 351)
  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..351
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..351
                     /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=37436
     Region          50..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 mfgdrarglg ltsrpdfalv gllripevqt spwisltrrv lfaiallfga alvvyvgrng
       61 yhdnsgnels fldafyyatv slsttgygdi hpvspearla niviitplri lflivlvgtt
      121 lgvltersrq afkiqrwrht vrnhtvvvgy gtkgrtaida mlgdgvqpad ivvvdtdvva
      181 leaaanaglv tvhgsatqsd vlrlagvqns esvvvatnrd dtavlvtlta relnktakiv
      241 vaireaenth lvrqsgansv vvssetagrl lgiatttptv vemmedlltp eegfavaere
      301 vesseiggsp rhlgdivlgv vrdgvlhrvg epevdaidag dkllyirrsg k
//
LOCUS       WP_181719297             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia gipuzkoensis].
ACCESSION   WP_181719297
VERSION     WP_181719297.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=35959
     Region          16..317
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mndtparllr llsllqtprd wpgselaerl gvtdrtvrrd idrlrelgyp vtatlgatgg
       61 yrlvagtamp pllveddeav aiavglraaa gsavagmeea svralakleq vlppklrrrv
      121 rvlaaaltpp sgdglavdae vlatlaatvt nrervrfayr deagaetrrn tepvglvsar
      181 rrwylvgydl dradwrvyrv dridrpqpta arftprplpa adaaayvagr rtdwgtpvfr
      241 lhstihtsad rvagrlgddp gevvaidgst cridalrdda pewlahrllg lgvdfevhep
      301 peliahlrai adraeraisp npgdrpprsa ga
//
LOCUS       WP_181719374             207 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Nocardia gipuzkoensis].
ACCESSION   WP_181719374
VERSION     WP_181719374.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 207)
  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 207)
  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..207
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..207
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=22516
     Region          71..149
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mterrargts pagrgdrrts raatsrpads aakrgrrrse aaekpkprks aarsaadrhd
       61 htflglstgk avilamvvcg laltlavpmr tyftqraeaa qlaqqraele adlarlrdrr
      121 aqqqdpafir teardrlrlv mpgetpyivq vpgieapapp paptrarepd pwytelwrsi
      181 sepqptpaaa ppaaprpqap eglegpr
//
LOCUS       WP_181719891             439 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181719891
VERSION     WP_181719891.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=45944
     Region          15..431
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mgsrvgvvga gyvgltsaac lahlghhvvc vdndeskvet lrtgtvpive pglpelvreg
       61 lsenrlvfts dpralhecev vllclptpmg tggtadlgvi edaletlstv lppdcvlvtk
      121 stvpvgtaar ipalsglast avvsnpeflr eghavedflr pdrvllgaae qdresadrva
      181 alyagtgapv lrsdsasael akyasnafla vklsfvntla elcerfgadi tkvtdamgmd
      241 drigsaflap gpgwggsclp kdtrallraa eaagvdfamv raalrandrq hamvlrkirr
      301 aatgavdgsl sgtrigvlgl afkagtgdlr espavavarq lsrhdatvta ydpcvpesga
      361 pgldgirvvd dpylvakead aiviltewpe frsldwaria taveravivd trnllderll
      421 ngtgftllst gtdrrdtcs
//
LOCUS       WP_181719934             156 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Nocardia].
ACCESSION   WP_181719934
VERSION     WP_181719934.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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
REFERENCE   2  (residues 1 to 156)
  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 156)
  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..156
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..156
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17293
     Region          10..101
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtlrrpvdds vtrvvellgd rwtilliaea ffgvhrfsdf arnigitnrn lltsrlrmli
       61 dagiftrtdh gggrvdyhlt aagrelypiv tammvwgdnh lvgpegrpiv lehrscgqet
      121 spmlvcdhcr epidprdvep kagpgfhqpp gaeqae
//
LOCUS       WP_181720042             323 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia gipuzkoensis].
ACCESSION   WP_181720042
VERSION     WP_181720042.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 323)
  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 323)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..323
                     /product="helix-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=34867
     Region          20..306
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mrasrlvqll lllqtrgrlt apelarelev svrtvyrdve alsaagvpvy sepgraggvr
       61 lldgyrtrlt glttdeadav llaglpgaaa dlglgtvlat aqlkvlaalp pelrgratri
      121 aervhvdapg wfhrpdetpt latiadalwh drtlrvrygr kdtvverlld plglvlkagt
      181 wylvarsgrt phsyrvgrii saeptgesft rpaafdlrah wsdaaddfar smlrvrarcr
      241 iatthlrllr lmndpaavae aqasagppda egwvevivps esfevlahal lplgefvevl
      301 eppqlraqla ataaamhary sgg
//
LOCUS       WP_181719956             501 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia gipuzkoensis].
ACCESSION   WP_181719956
VERSION     WP_181719956.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=55457
     Region          6..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 mtesvavpeh ldvvivgagl sgigaayrlq tecrgktyav leardalggt wdlfrypgir
       61 sdsdmftlgy pfkpwrdaks iadgpsilry itetatehgi drhiryrtrv laadwdsgta
      121 rwtltlaqrd asggtetrtl tcgflyacag yydyeqpytp efpgissftg evvhpqfwpe
      181 dfdyhgkrvv vigsgatavt lvpamaqqaq lvtmlqrtpt wisavpgrdk vadkirellp
      241 prlahrvirt knilfgigfy qycrrrpeaa rklltglttr ilkddkavae hftpsynpwd
      301 qrlcavpdad ffkamkkgka evvtdhidtf vpegirlksg rvleadvvit atglkllafg
      361 giapsvdgar velseqfvwq gtmitgvpnf avcigytnas wtlradltsr lickvlnhmd
      421 rkgyaavmpq pqgelaehpl ldlasgyiqr sigdfprqgd rnpwkvrqny lldsattlrt
      481 dldktltatp ksavrqpvpv a
//
LOCUS       WP_181719830             191 aa            linear   BCT 28-DEC-2024
DEFINITION  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase [Nocardia
            gipuzkoensis].
ACCESSION   WP_181719830
VERSION     WP_181719830.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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 191)
  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 191)
  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..191
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..191
                     /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=21130
     Region          1..186
                     /region_name="Adi1"
                     /note="Acireductone dioxygenase (methionine salvage),
                     cupin superfamily [Amino acid transport and metabolism];
                     COG1791"
                     /db_xref="CDD:441396"
ORIGIN      
        1 mtllqvmaaa daadvrvrtt dderigtela rhgitfgrwp vvenaasvss eellthyakh
       61 vaelnesgry rhidiarihp ddadpqwpei akgargkfld ehrhaedevr ffaagrgcfy
      121 lhlgeevlav vceggdllsv pagtlhwfdm gerpdfiair ffeeedgwvg dftgdkisag
      181 fptldellta p
//
LOCUS       WP_181719858             459 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181719858
VERSION     WP_181719858.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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..459
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..459
                     /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=49904
     Region          19..456
                     /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 maagwsvrhd gyvseivrrr ssrnaklaki plgiagraav gfgkklaggd kseinaqlnq
       61 raaeqlftvl gelkggamkf gqalsvmeaa vpeefgehyr ealtklqaaa ppmpaatvhr
      121 vldqqlgtqw rsrfsefddt paasasigqv hravwadgrt vavkvqypga dealradlkt
      181 lsrmsglvas vipgadvkpi laeitertee eldyrneaan qrsfakgfdg hgeivvpkvv
      241 asapkvivte wldgvavsti ikqgaedpeg sralrnrvag lmgrfhfssp evvgllhadp
      301 hpgnfmmlpd gklavidfga capmpegfpp vlgrmlalav eerfaeltel lydhgwvipg
      361 rvvthqeiad ylrpftdpiq tdsfhftrrw mqrvagkase fsspemktar alqlpaeyvm
      421 ifrvlggsvg ilaqldaelp fmqlvrtwmp gfseertas
//
LOCUS       WP_181720235             308 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181720235
VERSION     WP_181720235.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (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   2  (residues 1 to 308)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 308)
  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..308
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..308
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34155
     Region          28..82
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(33,37,62)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(36,61)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(43..44,55,58,62..63)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          117..299
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgesdtnagi rqlkadihgt ggvphrslgr clrgmrqeag lsievaarai grgagtlhrl
       61 etgapnvivr dedlrrlckl yqrvdmlpvl kslaaqgrtp swldefpdlv nptfnayiqm
      121 eaaashltsy rpdllpgifq ipeyaraldr ayfpmdtaee ierrvrvrrn rqglitrdia
      181 plnavlflde amtrrvvggp rvmsaqlrhl adlppnvrvq vlpfgagypl gtstgpftil
      241 dfaadndgra leppvvyvqs ytgdiylerp stvrryraai dvmqrvaldv psskrllrqa
      301 akefdcvr
//
LOCUS       WP_181720248             131 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardia
            gipuzkoensis].
ACCESSION   WP_181720248
VERSION     WP_181720248.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..131
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14185
     Region          11..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mslrpgtvfl adcparsaie iiaskwavvt lfalsegpqr hgelveligg vsrkvltqtl
       61 rrlqehglve rrvyaeappr veysltelgd tlrepiaalt twarsngasi atfresteas
      121 rtaigktilt n
//
LOCUS       WP_181720184             794 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-glucosidase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181720184
VERSION     WP_181720184.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 794)
  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..794
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..794
                     /product="beta-glucosidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0015926 - glucosidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=84678
     Region          43..396
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          <550..667
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          717..783
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 medrieella kldldgklrl isgaslfrma gdpaiglaem pvsdgpsgvr genwderdps
       61 vslpsgtava atwdpallte igaliaaear rkdvyavlgp tmnlhrspls grhfecfsed
      121 plltaemaga yvravqahgv sacpkhyvan dsetdrftvd vrvddralre lylypfertv
      181 eagawmimda ynavngitmt enplldeplk gtwgfdgvvv sdwtavrtte saargtdlcm
      241 pgppylwgep laaavragei aesaiddkvr rilrfaqrvg aldgtpqptp vftdgqaqal
      301 vrrvaaqamv lvrndgvlpl apdmtvallg psageprflg ggsatvipgh tttpveglag
      361 rlplthtagv hlsedlipap laimtdpetg epglsarylt gdtvlgtqhr ttsrlvllge
      421 plaaqsnmve mrtrlradmg gdwqigfggv ghirldidge nvldenvald sgdpaaalln
      481 ppqrhvtrtl avgdevevrl vtsiedampg lgiilgatlg irrpqrddde efaaaielar
      541 aaevavvvvg tteqiesegv drtslrlpgr qdelvaavaa vnprtvvvvn sgapvempwr
      601 ddvaavllaw fpgqefgaal advltgtaep ggrlpttwpk tmadvpvldt tpvegvldyt
      661 egihigyraw lragnepayp fghglgyttw stddlvidgr tvsitvtntg dregkqviqv
      721 ylsrpnsavd rpdrwlagft avtlapgdsr tvaitlpera fqhwgptgwe tepgefvvrv
      781 gtsvadlpht asiy
//
LOCUS       WP_181720044             322 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia gipuzkoensis].
ACCESSION   WP_181720044
VERSION     WP_181720044.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=35265
     Region          16..303
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mletsarllk llallqthrd wtgaelaerl gvtgrtvrrd vdrlrelgyp vhatqgaagy
       61 rlgagaalpp lllddeeava vavglrgasa gavtgleeas lraltkleqv lpprlrhrvr
      121 tlrgatlrvg apgsevrpdt llaiaeacqr herlrfdyra ldgapsvrtv ephtlvhfsr
      181 hwylvawdvd radwrtfrad ritpriptgp rfapheppeg dvaaylsmrl strawpqqat
      241 vllhgsaeya aervwpgmgv leavdehscr llvgaetpeq lvwmitsvdl dftllagppe
      301 lvealraqaa rcaravrafp ap
//
LOCUS       WP_181720268             279 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Nocardia gipuzkoensis].
ACCESSION   WP_181720268
VERSION     WP_181720268.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   ter Beek,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 279)
  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 279)
  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..279
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..279
                     /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=28783
     Region          23..245
                     /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 mtaalkeeat agqvlrrnft dtvisslatl gralrigaea irigstdair lrfqvhetlt
       61 qawflirvta vpsilmaipf gvivsaqvgn ivsqlgadsm igaagglgvv kqgapmatam
      121 llggagaaai asdlgartir eevdamrvmg vdpiqrlvvp riaammlvap llniliifvg
      181 iasgfvvavs aldvtpgsyw esfgsfttpi dvwvsvvkal ifgflvvvia cqrgleakgg
      241 prgvadgvna avvmsvaava vlniaitqvv tmffpvrma
//
LOCUS       WP_181720291             425 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181720291
VERSION     WP_181720291.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..425
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..425
                     /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=44664
     Region          6..>62
                     /region_name="AdeC"
                     /note="Adenine deaminase [Nucleotide transport and
                     metabolism]; COG1001"
                     /db_xref="CDD:440625"
     Region          46..398
                     /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 mstetvvlra arwvdvatge vhtpavivvr geyieavdpa vepadatvld lgdttllpgl
       61 mdmeinllig gpenpsglps pmhgvqddpv yrtlratina rttllagftt vrnlglmvkt
      121 ggylldvdlh raieqgwfpg privsaghai tptgghldpt mfqrlaphim plsveeglan
      181 gvdqvrhavr yqikygagvi kisasggvms hstapgtqqy sdeelraivd eahraglkva
      241 ahahgdagir aciqagvdci ehgslatddt iammvehgtf lvptsylseg ldvskappal
      301 rekaatvfpk arrmlgkaie agvkiacgtd apavphgdna kelwamvdrg mtpaqalraa
      361 tvtsaelvga edrgrlapgl ladiiavpgd ptrditvteh vrfvmkggvv hknttadraa
      421 avpvr
//
LOCUS       WP_181720630             277 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Nocardia].
ACCESSION   WP_181720630
VERSION     WP_181720630.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 277)
  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 277)
  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..277
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..277
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29053
     Region          21..268
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrsleqirew pvrhaasavv tadgataseg svervfplas vtkplvayav lvaveegave
       61 ldqpagppga tvrhllahts glafdttdvq arpgakriys sagfevlaaf vteqtgiafd
      121 eylrdavfrp lgmtdsvlag saghagrssa adlarfaael lnprlisaqt haeatsvqfp
      181 gvngvlpgyg sqrpndwglg feirdgktph wtggtnspqt yghfgqsgtf lwvdpktgla
      241 clalsdenfg dwaraawppl sdaviaevta trntvak
//
LOCUS       WP_181720641             432 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181720641
VERSION     WP_181720641.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 432)
  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 432)
  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 10669663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..432
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=46731
     Region          1..159
                     /region_name="TerD_like"
                     /note="Uncharacterized proteins involved in stress
                     response, similar to tellurium resistance terD; cl18957"
                     /db_xref="CDD:473128"
     Site            order(27,29,66)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:132992"
     Region          229..431
                     /region_name="vWA-TerF-like"
                     /note="vWA found in TerF C terminus; pfam10138"
                     /db_xref="CDD:401947"
ORIGIN      
        1 mgaalikgqn galdmarvlv svrteapvdv sallvteagr vrsdadfvff nqpsapgvtl
       61 dqgtpaalsv slsdlpadia qlravltldd peqtfgrfap pvatvadaag nvlyeyrveg
      121 lgsesvvial elyrrqgvwk vravgqgyag gfaalvtdhg vsvddepvrg eapsahpaap
      181 dpqamvipta dvftvpgeak lsfdkrakld lrkravakvl idkdafgira rvvlvidktg
      241 smkrqyhdkv vhrvvqrmip vatqldddgt leaylyalsf aklpditveh gdewartflh
      301 ltgthagidy drlggrndel pimrdvidsl rpggrptlvl fftdggfakk reiaalmrea
      361 sqlpafwqfv glgranygll rtldelsdra vdnagffald didqvddgql yarllgefpd
      421 wlraartagi lr
//
LOCUS       WP_181720723             146 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181720723
VERSION     WP_181720723.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..146
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..146
                     /product="YybH family protein"
                     /calculated_mol_wt=16525
     Region          1..126
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtaneseira flerraaaqq skdidrlmeh yapdivyydv vpplrfrgve evrrnflrwf
       61 dgydgpisle thdltvatsg dvafanmlhl dsgtrkggfq saiwvretvc lrqsngtwli
      121 ghehvsipin penlqiwlas dkdqpa
//
LOCUS       WP_181720730             685 aa            linear   BCT 28-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Nocardia
            gipuzkoensis].
ACCESSION   WP_181720730
VERSION     WP_181720730.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 685)
  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 685)
  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 685)
  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 685)
  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 685)
  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..685
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..685
                     /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=76290
     Region          8..680
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 msgveqnvtd pylwledvsd eraldwarah navvrarfad sdrfrelerr ildmldtdtk
       61 iayparrgpw lynfwrdagh prglwrrttf aeyaedapnw dvlidldava aaedenwvwg
      121 gaavlrpeqs ralislsrgg adakvvrefd lerrvfldpa dggyflpeak seirwidids
      181 vyvgtdfgpg sltdsgypri aklwrrgtpl deaetvfege pgdvavsagy drtpgyerhy
      241 vgratdffne evylladdgt lrhldlpsda seswykdwll vrlkspwevg gasypagall
      301 aadfekflag ardfeviftp dahtslhgyg wtenhlllvt ledvqtklyv ltpgadgwrr
      361 epladtppma ttsvlnldpl eggdefmlnt sgfttpstll asavggrter lkqepgffda
      421 dgveteqffa rsddgtpvpy fvirhrdrtd gpgptvmsgy ggfevsrtpg ysgasgmgwl
      481 erggtwvmtn irgggeygpq whtsvqkanr hkvyedfssi aadlvargit tadqlgavgg
      541 snggllmgvm ltrypelfga ivcqvplldm kryhlllaga swmaeygdpd epeeweyigk
      601 yspyqnarad rayppilltt strddrvhpg harkmaalle eqghefwyhe niegghggaa
      661 dnkqsafqaa liyefftqml ierra
//
LOCUS       WP_181720624             463 aa            linear   BCT 28-DEC-2024
DEFINITION  protoporphyrinogen/coproporphyrinogen oxidase [Nocardia
            gipuzkoensis].
ACCESSION   WP_181720624
VERSION     WP_181720624.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 463)
  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..463
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..463
                     /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=49776
     Region          10..441
                     /region_name="HemY"
                     /note="Protoporphyrinogen oxidase HemY/PPOX [Coenzyme
                     transport and metabolism]; COG1232"
                     /db_xref="CDD:440845"
ORIGIN      
        1 msartsmcdt dvlvigagpt glaaaadcvr aglgvtiier gatvgglars aeiagfevdp
       61 gghrllatta rqrrawskla ndlgrlplht vgrrsgilrr grvlsypvdw pqfaqvtpwg
      121 trlraaasma hrrvrplpde dslsawvrnr ygdyltnalm dpharkvfgv eptdipaawa
      181 aqriavpplr evlktalprl pychhasaea dhflypdggl grlwsrfaes lagsnllfgs
      241 hpvaigrags gelsvavsgp ggsstitarr iistapaedl ascigltsls arlahhairr
      301 dlivalvrls slprmwanyq wlythdvgvr anrfqnysaw rglacppgli gleytvpsgh
      361 aadytdqvhr dlsiiyggey ellgfdtlpn ayanfeatrd lldeldadla rfgpglistg
      421 rqgagvyinl dqalrlgrra asvpadyagv lgggeyssyq erk
//
LOCUS       WP_181720789             665 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Nocardia gipuzkoensis].
ACCESSION   WP_181720789
VERSION     WP_181720789.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 665)
  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 665)
  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..665
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..665
                     /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=70563
     Region          3..457
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          591..656
                     /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(613,622..624,631)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            623
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 meitnvlvan rgeiarrvfa tcrrmglgtv avysdadaaa phvteadaav rlpgntpaet
       61 ylrgeliiea avaagadaih pgygflsena efakavlaag lvwigppvea ieqmgskvas
      121 kkmmdaagvp vlaeldpaev teahlpvlik asaggggrgm rvvreladla pqiegarrea
      181 esafgdptvf ceryletgrh ievqvmadth gviwavgere csiqrrhqkv ieeapsplve
      241 rtegmrarlf eaarlaagai gytgagtvef ladeqgefff lemntrlqve hpvtecttgl
      301 dlvrlqldva aggalpaepp amrghsievr lyaedpahdw qpqsgtvhci eipsvrtefd
      361 lldrpgvrld tgvvdgsvvg vhydpmlakv isyaetrgea arllaaalhr akihglvtnr
      421 dllvrvlrhp aflagdtdta ffathgldal aaplvsesde tlsivaaala daaanrdsar
      481 aggglpsgwr nlpsqsqrks yesratgthe vgyrfgrtgv tvdghdglel vasaadrvvl
      541 svpgdrgpvl rrfevarygd qvyvdsplgp valrrlprft dpadqvatgs llapmpgsvi
      601 rlgaevgshv eqgqpilwle amkmehtiaa paagvlsavn vtvgqqvdvg avlavvepee
      661 iqeqr
//
LOCUS       WP_181721056             167 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RrF2 family transcriptional regulator [Nocardia].
ACCESSION   WP_181721056
VERSION     WP_181721056.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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   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..167
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..167
                     /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=17744
     Region          2..156
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mhitakvdya vrtlleiasa prldqsvagl gaplvqvapa vkaeaiataq rippkvlesv
       61 lgelrraelv isrrgpdggy wlarpaaeis iadviraieg plasvrgarp edvhypgaaq
      121 plqrvwialr vnirsvlenv tiadiasdql pgfvdalted pgawarr
//
LOCUS       WP_181721184             417 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721184
VERSION     WP_181721184.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..417
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43848
     Region          18..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 magpaqhsap daesprprta qgplagvtvv aleqavsapm ctrtladfga rvikvehprg
       61 gdfaryyddv vhgqaahfvw vnrgkesvtl dlktsagvdv lhrllsradv lvsnlapgat
      121 arlglapadl aarhpdliav eidgfgaggp lshkraydll vqaesgvcav tgtadapakp
      181 gppvadvttg lyaalsilaa lcgrardash gntisvslfd tmaemmgyhl tyarhagvdq
      241 qplgmsspav apygayptad grivvlgttn drewqrlate vldrpdlaad erfrtnpgrv
      301 rhraeiddai tawclrhdla riqkiaddag ignscynrpt evldhpqlta rdrwrsietp
      361 agsipsllpp ailtgfeppm gpvpglgaht davltelgct avelaalrds gvigarr
//
LOCUS       WP_181721232             291 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721232
VERSION     WP_181721232.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=30895
     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 mkpaafeyha pataaeaval laelgeeaki iaggqslvpm lalrlavfeh lvdlrrvdel
       61 rgietrpdav rigagtthaa vgrsedvrrg apllaratpl ighfqirnrg tiggaiahad
      121 aaaeypvval tldadietls prgrrtipas afftgmwttd leqdeivtgi vfpvwhgrcg
      181 faieeftrrs gdfamagatv avrldadsrv ercaiglfgl aptpvratet eaeligrpae
      241 atqaeeigrs atagldavss dvhgsadyrr rvgaamvara wrraveearn d
//
LOCUS       WP_181721244             374 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Nocardia gipuzkoensis].
ACCESSION   WP_181721244
VERSION     WP_181721244.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=39900
     Region          18..371
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 matevvpddr alrhgrrdra laqmeahdld vlvlgrqana ryvsgtpqlw vagtrpfgpv
       61 atvvretrav hllstwdegv pediphdhly giawnpmnti gvlqgiegaa tarrvgtdal
      121 sptfakllpi afpnaelvdg elamraarri ktdqevqvlr atlriaeagl saavaelapg
      181 vteqaligvl leamaaggvs tpasqdsawv tsrehpwrra gadrrvqpgd lvafssgvlg
      241 egyigevgrt wpvggegdds vrklyrrwdg lwarlieacr pgsagtdlla ayeiaveplp
      301 pmpvarglgm gfdppvvtsh lrasaeaerm epgmvlavtg yvwepgvgav fgrdavlite
      361 dgaevltvap hweh
//
LOCUS       WP_181721333             475 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [Nocardia].
ACCESSION   WP_181721333
VERSION     WP_181721333.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 475)
  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 475)
  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..475
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..475
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=52212
     Region          20..472
                     /region_name="CoxE"
                     /note="Uncharacterized protein CoxE, contains von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG3552"
                     /db_xref="CDD:442773"
ORIGIN      
        1 msagsvppda aplsaphglp ghlvgfveal rargipvgps etvdagrvmt vldlmdrevl
       61 reglacallr rtthraiydg lfdlwfpval gertaaedei eiprtptgdv dipalrella
      121 elltqeaatq qlealaaqlv erlgryqsag gssfsayktl kevqpqtlla kilaglslgp
      181 dtsdfdmeva rraarqriag ftasveaetr rraaerfgre rvasysvarq aeevdflras
      241 qaelaelkrg vqrlarilaa rlaarrrhar rgeidlrrtl rksmstggvp idlvnrkprp
      301 grpdlvllcd vsgsvagfsn ftlllvsalr eqfsrvrifa fvdqvdevtr ffdphtqlee
      361 amtriftead vtgpdghsdy ghalagfard fpdavtsrts llilgdartn yrdprlatlr
      421 slvevakhah wlnperrdqw gsgdsaadky rdviemhecr sakqltavvs rllpv
//
LOCUS       WP_181721579             225 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardia gipuzkoensis].
ACCESSION   WP_181721579
VERSION     WP_181721579.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=24576
     Region          34..132
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mavlslldrf nqrhpwshnd hygrwvvgrv assgarhvld vgcgtgnlva rlrhrvttvt
       61 alepdpvtag vaaerftddp avtivhadfa grdprrrwda itlvavlhhl plvptlrelr
      121 dclapggrlv ivgcyrragp idlladlpam vanpvmglie hparaavlpp hmtaptadpk
      181 etlaeiraaa elelpgarir rrlfwrytlv ydapsdratd smnqg
//
LOCUS       WP_181721621             298 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Nocardia].
ACCESSION   WP_181721621
VERSION     WP_181721621.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..298
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33420
     Region          26..87
                     /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          113..289
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mnndddsgdp adfpaaergp tvlrialggr lrqlregcgi sreaagdair gshakisrle
       61 lgrtgfkerd lrdllslygv vdpaeretyf elarrandpg wwqhysdllp awfetylgle
      121 qaattirtye aqfvpgllqt adyaraviql gnsdeterrv airmrrqeil drvaaptlwa
      181 videnalrrp vggmevlreq iehllvmadr psiriqvlpy sagghsaagg pfsilrfpep
      241 eladivyteq ltsslyfdkq rdvelymsvm nrlsvealsp vdsvrflrdl ltemrsge
//
LOCUS       WP_181721660             519 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721660
VERSION     WP_181721660.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=55129
     Region          6..513
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mtptrssydv vivggghngl vaaaylarag rsvlvlerqs htggaavsar vfagvdarls
       61 rysylvsllp raivqdlglr fetrrravss ytpvgdrgll vssaqartea sfarltgser
      121 efrawrrfya ttnqlarrvf ptltrplpsk ealrhivdda atwealferp lgetiestfa
      181 ddtvrgvvlt daligtftha hdpslrqnrc flyhvigggt gdwdvpvggm galtdalaea
      241 araagaeivt gcevmsiend setaevgyad grvgagyvla nvapftlagl lgeplppkpe
      301 gaqlkmnmll rrlprlrdae vdpreafagt fhigesyaql draygeaaig ripsappael
      361 ychtltdpti lapdlaeega htltlfglha raklfatdhe aakdqmvkat laqldsvlve
      421 pivdclatde ngapcleakt pielerevgl pgghifhrdl afpylpedad padpaarwgv
      481 atghrnvflc gagairgggv sgipghnaam avldsgqag
//
LOCUS       WP_181721720             341 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD-IIIC family phosphatase [Nocardia gipuzkoensis].
ACCESSION   WP_181721720
VERSION     WP_181721720.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..341
                     /product="HAD-IIIC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36899
     Region          4..341
                     /region_name="FkbH"
                     /note="Predicted enzyme involved in methoxymalonyl-ACP
                     biosynthesis [Lipid transport and metabolism]; COG3882"
                     /db_xref="CDD:443090"
ORIGIN      
        1 maatvkclvw dlddtvwpgv vlesdggapk pevlralral dgrgilhava srgelsagta
       61 hlrrhgiedm fsaveigwgp kseairriae slnigretia fvdndpvela evatacpevr
      121 cypadripdl pdlpeftpet vtsearhrrs yyraerarrv geaefagsda dflaslglvm
      181 tvraaaeadl aradeltvrt hqlnttgvtf didelrelca sphhevlvas lrdrfggygi
      241 iglavseirg sdsvlllllm scrvmsrgvg talireivrr araagrrpta efmatpvnrv
      301 mlvtlrfagf evlesdgdra llvctvpped iggtghvevi e
//
LOCUS       WP_181721794             409 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721794
VERSION     WP_181721794.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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 409)
  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..409
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..409
                     /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=44884
     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..89,96,100,107,238..239,242,246..247,250,
                     283,288..289,292..293,295,318,346..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..176,185,237..238,241..242,
                     246,289,292..294,395)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mdtqplvldp tgadihgesa rirargpmar velpggvqaw svtdagvlkr lladtrvskd
       61 akqhwpafin geipqdwplf lwvavnnmft aygtdhrrlr klvapafthr rtqamrpmie
      121 qitadllael aatpqgeavd lregfayplp iqvisvlmgv peslnaglrk cvdgifdtsl
      181 gpeesqanyl emyrilgelv ahrrenpadd mtsllishrd eedgsqlteq elidtlllvi
      241 saghettvnl ldqavfallt hqqqraevte gratwsdlie ealryeapva hlplrfaadd
      301 ieidglriak gepilasyaa anrdpnlhga tadefdvrra skehlafgyg ahhclgapla
      361 rmeaeialpa lfrrfpnmrl aagpaelgtv ssfisnghar lpvylepad
//
LOCUS       WP_181721783             278 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Nocardia
            gipuzkoensis].
ACCESSION   WP_181721783
VERSION     WP_181721783.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..278
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..278
                     /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=30373
     Region          35..180
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtvhdqapvl lsenlltdnp alyertfpdt gernarfvad lvarfgagap helldvgsgt
       61 grdaarlael gyrvrgvdis prmvdyartr ypaidfsvgd aralrpgvpv dvltclgstl
      121 lhlhatadlv aaldgfaagl raggllilem rngaflltdr grrelldeel vrqvdwegmt
      181 ytsrtsltvd lpaqllrrqr iwtwpgcpep vtqhtawrll fpqelrhllt gagfevlalf
      241 dapgplttps wpadgvlser ldgdrlhvva rrtgtgpr
//
LOCUS       WP_181721799             201 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GTP-binding protein [Nocardia].
ACCESSION   WP_181721799
VERSION     WP_181721799.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 201)
  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..201
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..201
                     /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=21806
     Region          14..200
                     /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 mgsvlspsdr avdyvpetvt rsvkllvagn fgvgkttfvs svseikplrt eetiteasvg
       61 vddmaglpgk sqttvamdfg ritlspklal ylfgtpgqqr fvplweelar galgalvlvd
      121 trrieksdev lsvleergvp ysvavnqfeg arpypleevr daldlepgtp ltaldardrg
      181 tclrslitlv eflfhrlesr i
//
LOCUS       WP_181721122             110 aa            linear   BCT 28-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Nocardia
            gipuzkoensis].
ACCESSION   WP_181721122
VERSION     WP_181721122.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 110)
  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 110)
  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 110)
  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..110
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..110
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12253
     Region          1..108
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 markvtvelv ddydgkspae etvtfaldga ayemdlsvln asqlrglfeq wtpharrvgr
       61 vrrgksesrp tsdreqtqai rewarkkgle vssrgrisae vaeaykkand
//
LOCUS       WP_181721834             135 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardia gipuzkoensis].
ACCESSION   WP_181721834
VERSION     WP_181721834.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 135)
  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 135)
  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 135)
  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 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   5  (residues 1 to 135)
  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 135)
  AUTHORS   Rosinski,J.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..135
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..135
                     /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=14303
     Region          6..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdrstakife algdpvrrfi lelvaadeqp agavvaavqq rapisqpgvs qhlkvlrdag
       61 lvsvraegtr rlyaldpegv daarawltgl adplhqfaqp ldalateiar gkrarrsaas
      121 grsgdedsgr rarqa
//
LOCUS       WP_181721853             381 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721853
VERSION     WP_181721853.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=42633
     Region          5..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 mevdnrkrlp sltglrffaa fsvfifhvml pnspippykp vnlfsdpdia ynaavvvgka
       61 gflgvsfffi lsgfvltwsw kpgssklqfi rrrmvkifpn hltlwvasmv lfaaaitswk
      121 awlpniflih awfpqnyina gvntpswtls cellfyvlfp flipavlrid vkylwygaaa
      181 mvagmclivl ltvfvvpsse kseltpipvl qlwfgylfpp srlfefflgv fvarivmegr
      241 wiriplwaav gavgvgylva mytpfyigfv latavplall igsaaksdld gssrflssrl
      301 avwlgeisfa fyicqgvtvf yvrramgaat fsapvavlli vllfclnifa awllftfves
      361 pamrrfarpk rrpvvveqvv n
//
LOCUS       WP_181721900             465 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721900
VERSION     WP_181721900.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 465)
  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 465)
  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..465
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..465
                     /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          6..>352
                     /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 maagqlprgr larggrlgrl vagqavrgvg trlsmigrpd earqilaers alqaaqqmvt
       61 vlggmkgaam klgqmlsvld vdlvpeshre lfrvklaelr drapevpfta mrkviegdlg
      121 pmsrvfadfe etpvaaasig qvyraklhdg rmvavkvkyp gvdeavqadm rnlqlfaklw
      181 rsvlpsagda avldeiarni ggeldylrea rtqhgvasrf cehpfitvpd svgehcthhv
      241 lvtefvegrs fqeiqalpga drdrigeliy rfyisslfsd yefcgdphpg nilldgggrl
      301 afvdfglyyr mnpvdaefer asllaagehr agdlyqawvg rgiidpdasv tpqecleyvw
      361 aasgwqllde eititpelat aavvlavdpr adefrgmrhq llpaehvfsr raelftfaal
      421 gqlettnnwh rlarewlyge ppvtdigrat aqwragqlsg phfhr
//
LOCUS       WP_181721907             349 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721907
VERSION     WP_181721907.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 349)
  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..349
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..349
                     /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=38679
     Region          19..347
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtreqdgrrp vvmesavvpr gseyavllrr vqgagllkrr lryyawksaa tavalaagwt
       61 vfvmvgdsww qlgvaaflav vfaqiaflgh daghrqifgs rranyvfgvl fgnlgigvsi
      121 gwwtsnhnrh hahpntegad pdvmgvlahs gdrarasrgl rrlifrnqaw lffpmllleg
      181 wslhfasara vmrwaiphrg wealllavha tgylcavflv lspvkavvfi vvqqglfgly
      241 mgctfapnhk gmevltaads rgflrrqvlt srnvrgsrlv dtalgglnyq iehhlfpsmp
      301 rpnlrraqpl vaefcaelgl pycetsllgs yiqalrhlys vgrlarplt
//
LOCUS       WP_181721932             452 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Nocardia gipuzkoensis].
ACCESSION   WP_181721932
VERSION     WP_181721932.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..452
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..452
                     /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=48330
     Region          15..315
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 msekhrgatg grrrverrlv ivgggvsalw lalyaarsgi pttlvgidrf ggyastgnqg
       61 wlhsgalyam ngahdlaaac rsgaeevlrs ahstgaglts pdvvgafipg deqqldegir
      121 rlrtsridfd vrdisempda yflypgdrrr kvvvtgdrai dtrllvqeml aqvarhggrv
      181 gicrspvrla eaksgwtvea enellsaeav vlalgaglpg flseqlphls lpayrvtrsr
      241 viamavpkln tivvpptvgs paivpiwhgg kirgvtictl adndagsgdp adfdpsdayq
      301 lvdyyahsip glarllgrgn lhigmygcqk lhmsgdegte slrlykldny apglygfyag
      361 kmssapvaaa acldrlvtdg iirdegveel praewkprge niaartacea igvgthtrvt
      421 seqwrawrea ssgqsaespp rpsprdsfdq lg
//
LOCUS       WP_181721974             290 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721974
VERSION     WP_181721974.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..290
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32348
     Region          14..75
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(20,24,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(23,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(30..31,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..280
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 magkrtvltv rlrrlaamlh emrenaqlsk eevsaktgin vttlyrieta qarpqrrtlm
       61 amldlyrigd eqredalell sdalkpgmsr ayegsvsevy aayinfesea lsarhyqtsf
      121 ipgllqtyey atavidtsmp kleasvmesr akarmdravn ltkeeplelw vvmdeaairr
      181 ivggpavmrg qldrllqeik rknvilqilp fdagahpgma gsftlldfpd padpelvyve
      241 gmagdelieg hteirrfgvi fdqlramals prdsaamive aarrmdgmel
//
LOCUS       WP_181721984             292 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721984
VERSION     WP_181721984.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   Wintjens,R. and Rooman,M.
  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 292)
  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..292
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33287
     Region          13..75
                     /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          99..283
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msptgstlpr rmlgrqlrel riksgvsaey ardainvgkq tlwrietgqp vrlnplfier
       61 lckvygasee rtavllnlve etkrsgwwha ygdtiaeefs lfveleavak rlvsyqttll
      121 pgllqtdeyr raliwvdlpa ipgqeverri emfrqrkarl ddsdpvlvea videstlrra
      181 iggpsvmeqq lrhlmrvger shvsirvvpl aadaysglga gsfvmldfpk hptahltepp
      241 vvyiqeltgd lylekpeeir ryrqtyadiq rsalnqersr aliyriakey ae
//
LOCUS       WP_181722026             299 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia gipuzkoensis].
ACCESSION   WP_181722026
VERSION     WP_181722026.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 299)
  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 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   3  (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   4  (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 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..299
                     /product="helix-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=32153
     Region          114..298
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <238..299
                     /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 mwvtspchyp rkgvslvtht allrprdsda lraeirwvag aagvpvafgg evhgdallls
       61 efvgtltngl rglavvrtsg lggrvmesgr paavsdyrra ssithdydgp vsgegirsvl
      121 avpvvvdqrs ravlyaatrg vsplgdrtad lavqagrrla teiairdevd rrvrmlelaa
      181 psaeaapait eelrdihael rgmarsaedd rlrgrlhavc erltrvmage phpdsprlsr
      241 reldvlsqia lgctnqeaaq rlslgpetvk sylrnamvkl darsrheavv aarrhgllp
//
LOCUS       WP_181721340             707 aa            linear   BCT 28-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Nocardia gipuzkoensis].
ACCESSION   WP_181721340
VERSION     WP_181721340.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 707)
  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 707)
  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 707)
  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 707)
  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 707)
  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..707
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..707
                     /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=75820
     Region          17..571
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mttatgassi dltapdlreh aeqllrelag agaalredqw taiealvvrr rralvvqrtg
       61 wgksavyfia akllrragrg ptvivsplla lmrnqvaaaq ragvvaatin sgnvtewdei
      121 haqvaagavd vllvsperln npdfrdqvlp rlaadaglvv ideahcvsdw ghdfrpdyrr
      181 irtliadlgs dvpvlattat andrvvtdva tqigtdtlvl rgtldreslh lsvvrfddav
      241 ertawlsghl hrlpgsgivy tltvaaahdl advlnshght vaaytgqtdp aerealeaal
      301 lnnevkalia tsalgmgfdk pdlgfvvhvg apsspiayyq qvgragrgtd raevvllpgp
      361 edariwsyfa svafprehiv ravldaldsd ralstaalep lvelnrsrle mvlkvldvdg
      421 avrrvrggwi atgepwtydt eryerlsvar eaeqqamidy qstadcrmef lrrqlddpgl
      481 sagsadspgc grcdnctgsr pdrtvaaeav aatkarldrp gidlaprkqw ptgmaklgip
      541 lsgkitggae tgrvlgrltd lgwgqrlrvl ldgpddpvpd avfdacvavl rewdwaarpt
      601 svlalespry pvltatlaar laevgrlhdl gtlrtrpdrp pvsaansahr vaglfdswei
      661 pdltqvsgpi llvdtvtdtg wtftvaahal raagadailp falatpt
//
LOCUS       WP_181721816             544 aa            linear   BCT 28-DEC-2024
DEFINITION  carboxylesterase/lipase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181721816
VERSION     WP_181721816.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 544)
  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   2  (residues 1 to 544)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 544)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..544
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56870
     Region          18..529
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mrtataltva tglwfagtpa pviasappav fvtggeisgr aadgvveyfg ipfaaptggq
       61 arfapprpvp pwpgvrpard hgpqcpqngy lpglpplgpt sedcltidvy apdrardrpl
      121 pvmvffhggg ylsgsnteyd gptrmaadgd vvvaipnyrl gpfgflslpe laaesggatg
      181 tvgiqdqqaa lrwvrdnaha fggdpgnvti fgesaggvsv cthfaapgsd alfakaiiqs
      241 gpcaraplap gdrdaafars qryadsvgcg daatrlaclr alpaatllda ssvqsdgrtp
      301 iwapsidgvv itrtldaglv gdarktpiiv gttsgegalm vaetdyalgh vpdaesyerf
      361 vrqsfgadad rvlarypvdr ypspaaaqia vitdsglacp tmatsrtard aghplwqyef
      421 dqaplgaanp vlpgafhsae llylftrfmg vpipwtgasa afaaqmqrww ttfahtgdpn
      481 apgspewwaw peptghssdg palimratgn ymtddfatrh dcafwselgv dpamnrrrga
      541 gpvk
//
LOCUS       WP_181722154             342 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Nocardia].
ACCESSION   WP_181722154
VERSION     WP_181722154.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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 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 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..342
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35351
     Region          56..337
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mslrvpitva amaliavtta apvpaapvpp tpppavdpam trtgllsieq vapgrerlsi
       61 asaamrrvit vdvlrgsgea prpvlylldg vdgdatsawl tkggaaeffa dkpvdvvltg
      121 ggtgsmysdw arhdtalgln rwetflttel ppivesllrt dgrraiagvs mgaqaammla
      181 qrhpgwyrav agmsgcysta dplghavtti tvasrggnvd nlwgpptspe waahdsllqa
      241 ealrgtaiyl saatgvptga dlvavanspt iaealrtagg gaaleagara cterfvarld
      301 elkipatvey taegmhtwpd fqaqlpkawr vlaqalgvat ss
//
LOCUS       WP_181722159             314 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181722159
VERSION     WP_181722159.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 314)
  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..314
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..314
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35316
     Region          30..89
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          116..294
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mraskprqdt gsagadpvsg ggptvlrmvl ggrlrrlres rgltredage airgshskis
       61 rlelgrtgcr erdlvdlldl yrvtdpeerq rylelarqan asgwwardnd wlpkwfdtyl
      121 gleqaarrir syepravpel lqtpeyaral ltlshpgese esierrvalr mrrqdilsgp
      181 hppqlwviie eaalrrrigg stvwraqldh llrmearpni tvqiladdvg gpaltdgaft
      241 ilrfaetdlp divylqqlts alyldkiadl dvyyavlnql lvlapppehs rgllqllrdg
      301 vvptvdepvd rmrg
//
LOCUS       WP_181722213             147 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181722213
VERSION     WP_181722213.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 147)
  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..147
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..147
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16227
     Region          3..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(4,6,8,17..19,21..22,27,35,43,45,47,49,59,62,68,
                     70..71,83..84,86,88,98,100,102,104,110..118,120..122,125)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mvdilhrvgi espvsevyaa lttteglagw wttdtrgngg evggvlefrf gaggfdmkvr
       61 alepgrrvlw evidgpgdwv gtqldwdlgq addytivlfk hqgwkepves myhcstkwav
      121 fllslkslie tgkgapepyd vkidnwn
//
LOCUS       WP_181722358             296 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181722358
VERSION     WP_181722358.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 296)
  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..296
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32848
     Region          10..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          103..289
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 magstlprra lgrllrdlrv nagksqlaag laievskqti grvedgrpar istaqfrdll
       61 dfyeadeaar aelldliqev kaakgdpagg wwrayadlvn shfdhfmsle qacdrmttcq
      121 ltllpgllht payrrwiest tnpamsavei errleltarr qqrlsedqef rlevllseaa
      181 lrhqvggpav iseqllhllr vgtlpnvsir vvpfgvgghp glivqsftmf efpplrssrm
      241 qeppvvfveg ytgalfleea svieqhraav salrevalnq edtrrlvqei aeehva
//
LOCUS       WP_181722470             324 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: COX15/CtaA family protein [Nocardia].
ACCESSION   WP_181722470
VERSION     WP_181722470.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..324
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..324
                     /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=33906
     Region          16..307
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mlyraflrlv dklplpslra qrlialavil sqagisvtga vvrvtasglg cptwpqcfpg
       61 sftpvavsev paihqavefs nrlltfvvtl caaaivlavt rarrrrevlv yawlmpggtv
      121 vqaiiggitv rtgllwwtva thllasmvmv wlavvlyaki gepddgidvv rapaplrwlt
      181 alagvalgav liagtlvtaa gphagdksie rqverlqvei vtlvhlhsql lvgylallvg
      241 lafglfavgi ppavrtrlfv llglvcaqgl vgvvqyftdv paalvvvhvg gaaactaata
      301 alwaslrtre rvaapkpdpa aqaa
//
LOCUS       WP_181722578             473 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardia gipuzkoensis].
ACCESSION   WP_181722578
VERSION     WP_181722578.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 473)
  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 473)
  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 473)
  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 473)
  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 473)
  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 473)
  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..473
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..473
                     /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=48362
     Region          137..470
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrrllvalt lfaaiavlaf avplsltiat nrtqqlvlar sgdadrfatl addavtagds
       61 raladevlry helygenvlv vdargatavn agadvndpgi aaavvaarrn qrphavdklt
      121 pwgaptvlva rpvgtgvqvn gavvieasta rargdiaraw avivlggvga malfvllavt
      181 igrwvlrpla alshgvaelt atlpkpradt vapvsisgry ggppemrala esfdamaaav
      241 adsadaqrql vadtahamrn plaaltirld slepaipasa agtfrsasae vdrltalldg
      301 llslavaetp aafdvartae dadqcdavqv vadrfdawcs afeaagqrlr vapaaesadv
      361 aapadvlaqm ldvplsnatr yagagahadl ivetepgwvt vtvrddgagv rpdeidkltt
      421 rffrgssaat ggsglglpia aalaqargga ltvasvpphg lavtvrlpaa ear
//
LOCUS       WP_181722141             347 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Nocardia gipuzkoensis].
ACCESSION   WP_181722141
VERSION     WP_181722141.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 347)
  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 347)
  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 347)
  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 10229716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..347
                     /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=37753
     Region          10..>142
                     /region_name="LemA"
                     /note="LemA family; cl00742"
                     /db_xref="CDD:469899"
     Region          188..321
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mtfsattvlv laliaavvva iglwaystan rldrlhvrsd qswqaldaal arravvarav
       61 amaiagpvsd palaeqarql ssladraera grveretven rlssalsavd igtlrpqlva
      121 eladaearvl iarrfhndav rdtlalrtrr pvrilhlggt aplpsyfeit eratpaastg
      181 lavdtirtta rivlfdendr tllmrgndpk tpevsfwftv gggvepgesl rvaavrelye
      241 etgcradpae lrgpiwrrva vfpfngdlir seelffalrv rgfephaanq tvierrsitg
      301 nkwctaadiv aldrsgetvy pyhldellae aaeaasgnad pevrsir
//
LOCUS       WP_181722645             317 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181722645
VERSION     WP_181722645.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 317)
  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 317)
  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 317)
  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 317)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..317
                     /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=32712
     Region          78..191
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msrnpsgtra frhgllaaaa vlsalfgggv vapahadppp aqpypvsnqf lidairaslq
       61 ggataspagt nnwtckptaq hpepvvlvhg ilanrnnnwq tygpllanag ycvyaltwgg
      121 pggdpdgfig glgsmrngaa aldafvdrvr hatgaptvam vghslgatmp ywylkaggga
      181 gkvskmigla gavqgfdrnv mtsgsvdivq geglpnstfm relhdggiav pgiaytqivt
      241 rydevlpyta glieepgvan yilqdmcaqd yadhlsinsd pvtarlvlna ldpehpqpve
      301 ctlvlpaigv pstspgr
//
LOCUS       WP_181722671             426 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Nocardia gipuzkoensis].
ACCESSION   WP_181722671
VERSION     WP_181722671.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..426
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47003
     Region          145..418
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtstwipglr pdphqpvper isppelieaa ereigvqatw waaqtaqriv devttrfrds
       61 espamvtgfe regceasllt vliglhkqip svsrsgsate svhqsvhrgv aintvlqtvw
      121 tchalaqdal ltevekvvpe qrlveevrql nramngyits yagelireye eelalwkgrv
      181 qaeqlriftq liagvdpgen aeeilgvrlt dthlvasvws ratghvpdkd gqiasfahta
      241 gealgaartl vlpqddvtev wwswrsapps eyvarlrqlt rptwmhvavg tpergaggvl
      301 sshqaclqav rvgrrsevls lwpyeelriv allsadpeaa rrftraeltg lsdadaktvt
      361 lretlrvwlq sggsrtvtae rlfialntvs yrvakasdll grppgertve tllalelahy
      421 fpdflt
//
LOCUS       WP_181722767             299 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181722767
VERSION     WP_181722767.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   Wintjens,R. and Rooman,M.
  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 299)
  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..299
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..299
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33510
     Region          13..74
                     /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          105..290
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mteiesptll rrqlgrflre aregrgltia vaakevqlsf nglqrletgr avkprrqdvr
       61 elcmlyevnp ehteqavgla sraatarded gitplgglfs dafnmyvgme rsarrltsye
      121 vqvpgllqta dyaraligaf lhdgsadeie qrvrvrlnrq vavtrktrpv dlhvlldeaa
      181 lyrmvggpkv maeqhrylad vstrpnvtlr ihpwsagytr gilhgsfvll dfgtdskgsp
      241 ieppvvyldg gmssdlyler peivqrytem adairqtald ekttrdllrr varsydsdr
//
LOCUS       WP_181722828             304 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181722828
VERSION     WP_181722828.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   Wintjens,R. and Rooman,M.
  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 304)
  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..304
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..304
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33423
     Region          3..54
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mvsvrewtgk esralrdafr lsqqtwarkl gahertvkhw eagrairpay qavldttlsl
       61 appevvaafr erlhpkeddv drrqlfkvga lgagglamlg iadgerarwl msgagqpdaa
      121 avevvrntly samqlddtlg spaaqglvia qqqlteamlr essvslrpaa lslyaewtgf
      181 agclawdsge ydtatrlykl aretaheaed adlgaymlch lsqlaiwqrr prvavdhava
      241 arswvaqsed aplrayvamr aaepprspgs grpaswrwtk ptrlspessr atrrsrvpts
      301 cprr
//
LOCUS       WP_181722908             457 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia gipuzkoensis].
ACCESSION   WP_181722908
VERSION     WP_181722908.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 457)
  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..457
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..457
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=49842
     Region          31..84
                     /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(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 mnvheasavv iapavwespv mraalarrdl krvfellqrg gfsqreigrq aglsssevyq
       61 vlhrnrrisa ydvlakiadg lkiprgymgl ayddstennl dlaaatcsti gserdevrsl
      121 lshaanvtmg taaediahww qplereiapa ptrigrsdvd riraltaamr aidyrhggga
      181 crdaiaaqvr wsqqllnadg gdqvkeqlkc aladlhnlag wtsfdvglys parkhfgral
      241 elarsandfs lsanilyrtg rlhlhrgmpn ealrffqlgq iaaqdsgcal tvamlcvnea
      301 wtygqlgdre qmrrsvgraq defsraeren apvwvrffgd adlnasigva lvstvkvtkr
      361 dladgieflq aalarrspdm nrskafelta lasahldaga redglrvgrs avatastvrs
      421 vravdrlapl rkaatkypnd aglkdlarsi nsleavk
//
LOCUS       WP_181722985             269 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardia gipuzkoensis].
ACCESSION   WP_181722985
VERSION     WP_181722985.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=28297
     Region          13..260
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 miehphprlp gatrpvalit gptsgighgy atrlaslgyd lvlvardeqr laalatdleh
       61 rfgtrsqvlv adlalatdre qvvarladgv eflvnnagfa hsgefwtvpp drlqaqldvn
      121 vtsvvqltra alppmiaaan gcvvnvasva glipgrgsty saskayvvsf teglagglag
      181 tgvrvqalcp gfvrtefhqr agiemsslpk alwlsvdrvv agslrdlekg rvlsvpgmqy
      241 kalttvagmi prtlgarlnr glfdargrt
//
LOCUS       WP_181723116             285 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Nocardia].
ACCESSION   WP_181723116
VERSION     WP_181723116.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     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=30373
     Region          8..269
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mprtrrplsg rpvmitgaas gigrslaqll srrgspvaia didgvglket aaaltgpvlt
       61 rvldvrdaad qlafadevrd wltaplaavf nnagvatsss vldavpedde wlrrinfdgv
      121 vngtraflpl lveqdhgvvv ntssvfgllg mpnqsaycaa kfavrgftda lrqelrgtgv
      181 savnvhpggi rtniarnarv rkdpegrgrt heqmaaefea vtlttpqkaa eiicrgvehg
      241 ksrilvgpda ylfdllarvt pthyygvval lerslrtrdt tgara
//
LOCUS       WP_181722967             385 aa            linear   BCT 28-DEC-2024
DEFINITION  FUSC family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181722967
VERSION     WP_181722967.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 385)
  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..385
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..385
                     /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=40502
     Region          27..221
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mtggldpdsr vgsarassva rlraswarlr rsvlpivqca vgaalawfla hhvighalpf
       61 faptaavvsi gisfgarlrr svelvvgvav gigigdlfis ragtgvwqia lvvavamaaa
      121 vfldggsiit mqaagsavlv atllppsagg glsrmldalv gglvgvvvva aiplhpvrra
      181 rtlaadilgv mgksitdcad glleqdpekl hraltamrat qpqidalrat leggreisri
      241 splywnsrpr ldriratadp ldnairntrv llrrsltlvr ddeildpgli deverlgqav
      301 dvvrrmmltd pgeqpdraea arvlrsvakg arpelvagag lsahvvfaqv rstlvdlmqv
      361 cgvqrisaia llpptvknpy vrpev
//
LOCUS       WP_181722283             488 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: peptidoglycan D,D-transpeptidase FtsI family protein
            [Nocardia].
ACCESSION   WP_181722283
VERSION     WP_181722283.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 488)
  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 488)
  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 488)
  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 488)
  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..488
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..488
                     /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=50821
     Region          <74..487
                     /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 mntplrrvav avmvmvvall anatyvqvik addlrsdprn srvlldeysr qrgqisaggt
       61 vlassiatdd rykylrtypt epeayapatg fysmqygstg leraedsvln gsdsqlfgsr
      121 lvdlisgrdp rggnvlttld pvmqqvaydq ltskdytgsv vaiepstgki ltmvstpsyd
      181 pnrlsghdga rgtqawetls adprhpmlnr aisqtyppgs tfkvvvtaaa langlatpdd
      241 qftaapnftp pgtsvpmeny ngstcgpnpt aslfeafrrs cntafaelgl kvgsarlkde
      301 aaafgvgphr gipmpvaest vgpiadeaal aqssigqrdv altplqnavv aatianggvr
      361 mepylvdqlq gpdlseltkt kpvsvgqavs aevastltnl miasesntag ggqtpyqias
      421 ktgtaehgsn prstpphawy iafapaqnpk iaiaviveng gdralaatgg svaapvarav
      481 lnaglrgg
//
LOCUS       WP_181722873             245 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Nocardia gipuzkoensis].
ACCESSION   WP_181722873
VERSION     WP_181722873.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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..245
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..245
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26086
     Region          5..241
                     /region_name="EcfT"
                     /note="ECF-type transporter transmembrane protein EcfT
                     [Coenzyme transport and metabolism]; COG0619"
                     /db_xref="CDD:440384"
     Site            order(27..28,30..31,34..35,72,76..77,80..81,96,100,107,
                     110..111,116,139,143..144,146..148,150..151,154..155,
                     158..159,182..183,185..187,189..191,193..194,196..197,201,
                     204..205,211)
                     /site_type="other"
                     /note="S component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(142,146,149..150,152..153,196,199..200,202..207,
                     210..212,213,215)
                     /site_type="other"
                     /note="A' component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
     Site            order(171..178,184,187..188,191)
                     /site_type="other"
                     /note="A component interface [polypeptide binding]"
                     /db_xref="CDD:410987"
ORIGIN      
        1 mstvllrqvp vaspvhrlwa gtkmigvfli slllmflpsw pvlgvmtafl vfvgvtarlp
       61 lgtlprlpww fwalfvvggl itvpvggaav lryaqiatft lilvaasfli awttpmgdia
      121 palaklgapl rrlrlpvdew avvvaltlrg lpllmeeirv lraarrlrpk dgmlaraadn
      181 plidiltaam avstrragel geaitarggt gqltahpsap grrdalalal vfgvclgsva
      241 lhllf
//
LOCUS       WP_181723345             900 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Nocardia gipuzkoensis].
ACCESSION   WP_181723345
VERSION     WP_181723345.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 900)
  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 900)
  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..900
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..900
                     /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=99072
     Region          3..898
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtddrsrtge ldvfsaelkf rldpfqrdac aaleeghsvl vcaptgagkt vvgefavhla
       61 laaggkcfyt tpikalsnqk fadlterhgr asvglltgdq sinpdapvvv mttevlrnml
      121 yassdalrgl syvvmdevhy ladrfrgavw eevilhlppd vrlvslsatv snaeefgawm
      181 etvrgdtavv vdetrpvplw qhvmvgrrmf dlfdtrsteq kvlvdedlvr firqreatdr
      241 mnswgaprng rggprrdfrp lprpevlakl ddegllpait fifsragcdg alaqclrsrl
      301 dlsrpeerde vdaiidkhtg dlpksdlevl gywewrealh rglaahhagm lpafrhtvee
      361 lfvnglvrav fatetlalgi nmpartvvle rlvkfngesh aeltpgeytq ltgragrrgi
      421 dveghavvlw qpevdtsava glastrtypl rssfrpgynm sinlidrmda desrallers
      481 faqfqadrsv vglvrgiern daalrklrdq lggadggfle ylalrerikq rerqltqqsr
      541 adrrgaavda lgalrrgdvv aipsgrragl avilepdatp gdprplvlte dkwagrvsva
      601 dfpvpaealg hmrlprrvdh rtartrrdla salrstgisv pgrprrgrqs aaaddrelat
      661 lrrtlrahpa harpdreqls rvgerynrlq reteamrqkv aattnslart fdrilgllee
      721 rgfvhesevt pdgrrlariy aesdllvaec lrkglwrglg aaelagvvsi lvyesrqegg
      781 ylgasgptap irravgatig vwselrsdea rhklpptrep dlgfvdgvyk wargdglaes
      841 llasgdqgap lsagdfvrwc rqvidlldqi hntaddpeia ataakavrai rrgvvavdaa
//
LOCUS       WP_181723349             325 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia gipuzkoensis].
ACCESSION   WP_181723349
VERSION     WP_181723349.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=34928
     Region          8..317
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mssrlsvrls rllnmipyfi ahpgisaaea aadlgvttkq lmsdlnqlwm cglpgygpgd
       61 lidlsfsees ievtfsagid rplrltstea tallvalrsi vempgmvdpt aahaaiakie
      121 saiagsaapa edgrsrtppq eapavaavrs alalgralrl vyysasrdvv serivdpiri
      181 vlvddnsylq awcrqaegvr lfrfdrieaa aelgeparpp ehatqatagl dlfqddqavp
      241 larlrihady awvldqypmh rlavhpdgsl eatmrfatld wmarlllgfg sgvtvlgppe
      301 lvaavrersn aalaayeeag ylear
//
LOCUS       WP_181723457             203 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Nocardia].
ACCESSION   WP_181723457
VERSION     WP_181723457.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 203)
  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 203)
  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 203)
  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 203)
  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..203
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..203
                     /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=22804
     Region          120..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 mtavkpnhtp apavidlsva alrsrlhdal avyvaamdyp hgtenhrapm wtehttrpgw
       61 qavaavlpdd sgridlrrap ivaiaygyrg aahqwwhqqv hsgmrrsgwp ehstrellsd
      121 yfeltelhvh ptaqgrgiga tllerllrdr teravllstp evagednraw rlyrrqgftd
      181 vvrnfvfagd nrpfailgrr lpl
//
LOCUS       WP_181723492             243 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Nocardia].
ACCESSION   WP_181723492
VERSION     WP_181723492.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     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=26831
     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 mfywllkyvl lgpfihlynr ptvegvenip adgpaimagn hlsfadwlfa pllsprriny
       61 lakaeyfttp gikgrfqkff fsasgqypid rsgadaaeda lnaarklldq grlvglypeg
      121 trspdgrlyk gktglarlal etgvpvipva vigtdevspp gpfrwrrrkv tvkfgepidf
      181 sryegmggnr fveravtdev myelmqltgq eyvdvyahsl kkdvpsgsrp eavsvripdt
      241 aag
//
LOCUS       WP_181723557             406 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PucR family transcriptional regulator [Nocardia].
ACCESSION   WP_181723557
VERSION     WP_181723557.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
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="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..406
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=43944
     Region          143..404
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msvdssarqs ltlsgkpmss plkdvrglsr qmvghfvenv ipcgtlpgda iagdvttitr
       61 vclelavsml dgkdlpeklq rlgdaaagwa regvpidtih hsihegfkmg ldlvvsgatm
      121 kdyddlvdga kmvvemldmi nsavsmayvr elravvsehh tavhtltsal lgghststma
      181 recgiaiaps yavlavaipp hreernpmvd gkvvarrklr rvqaelatrc geaalsllsv
      241 dggtvliptg hldndqldtl vtqlshaaqv gvtatmveat pekiptaadq ahelldmvqr
      301 leavaglyrf delaleyqlt rpgpgreylg slldpldahp elletlqrhi annlnrqrta
      361 rvlhvhtntv dyrlkrigql tgfdpsqpsg lwylrsalva rtyrtt
//
LOCUS       WP_181723496             521 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181723496
VERSION     WP_181723496.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 521)
  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 521)
  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..521
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..521
                     /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=55844
     Region          9..509
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtgspsgpsr rtvlrasalg lvaapaltac ssdsgpglvr qrpvlthgva vgdprtdgal
       61 iwaradrpat livetaates ftdakrftgp lltpdsdgtg rvrvnglpag qqvhyrvtls
      121 gedgatsepv tgvfrtapta aadirlqwsg dvagqgygin pelggmkifa amaardphlf
      181 vhsgdsiyad gplkesvplp dgriwrnvvt eaksavaqtl dqfrgnyayn ltdanyrrfn
      241 ssvaqvvqwd dhetvnnwyp gglvaeskgy sersmdtlaa rswqafhewm plepreavdg
      301 rlyrkiaygp lldvfvldmr ankdindann gpsgrilgpa qtkwlsdslr sstatwkiia
      361 sdlplgvivp dgeqknttay egpangdpga ptgrereiae vlssirankv anvvwltadv
      421 hytaahrysp eravftdfde fwefvsgpln agafgpnqld gtfgpeavyv happvqnssp
      481 ldafqhfgev ridgksrelt vdlcdaagsv lfskslapas r
//
LOCUS       WP_181723689             609 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia gipuzkoensis].
ACCESSION   WP_181723689
VERSION     WP_181723689.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 609)
  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 609)
  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..609
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..609
                     /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=68820
     Region          61..549
                     /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 mqeckptvtp dvdrdalrar ylaerdkrlr pegqkqyllt egefadyyee dpytpveprd
       61 tmtdeievai lgggfaglit ahrlqqagvd dfriielggd fggvwywnry pgiqvdsdsy
      121 cylplleetg ylpkekfsfg decyehaqri gkhfglyeka vfhtlirsle wderierwri
      181 atnrgddira rfivmcqgpy nrpklpgipg itrfeghtfh tarwdyeytg gtlkggldkl
      241 gdkkvaiigt gasgigtiph laegaehlyv fqrtpsyife rgntatdpew vkslrpgwre
      301 erqrnfhnaa yafyspgepd licdgwteva rnvaahldat ggwaelatnp mkvmelkeae
      361 dyramervrr rvdqivadka taealkpyyr hlckrpgfsd nylqafnrpn vtlidvsdtk
      421 gveritekgi vahgveyevd civfasgfei ssdidrrlai qpfagrggrs lyehwnegfr
      481 tlhgimshgf pnhfatgfvq ggvtasttrm feqqadhiay iiqqasarga ttvepsaeae
      541 eawiatiran sfdnsnfvre ctpgyynseg epngrsflgd pfwggfyvle dllrswreeg
      601 rlaglvlga
//
LOCUS       WP_181723748             944 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Nocardia gipuzkoensis].
ACCESSION   WP_181723748
VERSION     WP_181723748.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..944
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..944
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=99053
     Region          <10..943
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mvslpvcgaf vgraaelaal qdayrdpavq tvlvggeagi gksrlvaeft trldartavm
       61 sgrcpefgak glpftpfvav mrallreqgv aglaallpis epalarwlpe laaragaaep
      121 etdrirlfge iltvleqfsm tkplvvvled lqwadeasle llaflvanla ggdlflvgty
      181 rpadsgplrk lvaglrreeg vrlltppplt rhevgrqlaa lrggepepgt iarvferskg
      241 iplfvealgp apeatpaels elllgylsdl pdqaasvlrl aaaagspvrh sllaaasdlg
      301 edaltaalhk lvgqqllvpt etgyefrhvl irdavygdll paerkrlhai israllgfrn
      361 rdsdpgpsge lahhayaage lplaleaawd aaanaesvga qrvqvrhldq vlelwdrvpe
      421 aasrvdadri dvveavvaac yrggviergi aaadealsal daatdperaa rlhhyraglr
      481 nqssgggedd llaalaylpp drptllrgev laelaaarvf sgaaaaaend araavevaeq
      541 lgagplaara yaylglatad rrevamahfe rahaaaktag dpgtlltvvl wesallvsag
      601 aneaaiatiq qglraahety rfaeaapill vkwaqaltal grwnealdli deslterlpp
      661 lstaalllch arimlargdv daaatsaata qpllgdrkwa rqyqiqlhtv qteitraagn
      721 pqraaeigaa tlaaddlaah hheawalada vartrcapmv lgsvtaklpv ttavdaayrd
      781 schavrsgra adwaaavssw rtlrqpfela rsllesgeae laagdraaar dalrsvlela
      841 devaaaplaq qarqladrag ivlaevggpa raqpattagl tpreldvlrl vstgasnrqi
      901 gaelfisant agvhvsrilt klgassrtea aatarergll gsag
//
LOCUS       WP_181723672             106 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Nocardia gipuzkoensis].
ACCESSION   WP_181723672
VERSION     WP_181723672.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=11306
     Region          6..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 matngvralt aladptrrai fealpqaars vgelaeeigv sssavsqhlr vlrearlvmm
       61 hpegnrrlys ldprgladar dyleqfwpsa iaaysaalrt aatata
//
LOCUS       WP_181723594             312 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nocardia gipuzkoensis].
ACCESSION   WP_181723594
VERSION     WP_181723594.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..312
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33751
     Region          20..308
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 maspsasadt asitgswped drtvqlrvhs aamgqdimvk vlrpadrsvp rptlyllngg
       61 gggqdsatwq kntdvlrfla ekevnvvqpv ggrwsyytdw rapdpklgvy kwktflteel
      121 pplidaefgt tgvnaiagls tsgtsvlqlp iakpglyrav aaysgcaqts dpigrefiel
      181 aveswgggdt enmygppgdp mwaandpylh aeqlrgirlf lstgtgvpgm ydvyngthmq
      241 pgprgflnql vlggvieaav nwcthnmrdr lnalgipaty dfqptgthsw gywqealkns
      301 wpvlaeglel pl
//
LOCUS       WP_181723774             257 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Nocardia
            gipuzkoensis].
ACCESSION   WP_181723774
VERSION     WP_181723774.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=28514
     Region          1..208
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 marepvydil tglaraiffa qglridiegq ehiprsggav lavnhtayld fmevglvgrk
       61 sgrnvrfmmk aelehglvgf lmkhckaigv drtagaesyv ravtalrege lvvvypeati
      121 srsfelkefk sgaarmavea gvpivplviw gahrvwtkdi pkqlgrhnfp vhirigepip
      181 paepteelta tlrtrmneql eraqknypmq pgarwvpvrl ggtaptlaqa avlereemer
      241 rrakarrrgd sdpstrh
//
LOCUS       WP_181723808             240 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardia gipuzkoensis].
ACCESSION   WP_181723808
VERSION     WP_181723808.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=25586
     Region          1..>185
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtktiaifgy gpglgvgtgr rfgregfrva vigrdpekar rhaeeltaeg ieaaafpadv
       61 tvaaqvtgvi ekieatfgpi dvamhgaagn msdrqpstle vdipsldapi alklhspilm
      121 tralapgmva rgdgallfss gssehfvapy lanfgialaa qrgylrqlev elrgtgvyvg
      181 llnigvlidr skaaqiideh pelipeglei vrmsgdelgd hywrlyterd kveldvgfpv
//
LOCUS       WP_181723842             144 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardia
            gipuzkoensis].
ACCESSION   WP_181723842
VERSION     WP_181723842.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 144)
  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 144)
  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..144
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..144
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15951
     Region          20..120
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdtvcdrsgt aglvesylhh cpareilavl adkwvmlvls vlrdhdgpir fselrrrldg
       61 itqkmltrtl rnlereglvr ravyptvppr veysltelgk sigalshamg mwavehqdri
      121 laaraefdar aatepeplpa gpsl
//
LOCUS       WP_181723832             490 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia gipuzkoensis].
ACCESSION   WP_181723832
VERSION     WP_181723832.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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..490
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..490
                     /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=54382
     Region          4..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 mteaadpehv piavigagia giglavslre agiedfllle ragdlggtwr antypgcacd
       61 vpshlysysf apnpdwsrty gtqreileyl rsvaarndvv rhmrfgvell earwddaatl
      121 wrlrtgrgdl tadvlvsavg pfseaqiprv pgaetfegtq fhslhwdheh dltgervavi
      181 gtgasavqfi peiqpvvgtl tvfqrsapwi vsrldrrtls aerallrrmp vlgkairgly
      241 ytgiegfglv gfvdkrfrhp yealgrlqll rqvrdpalrr kltpdyvigc kraifsdayy
      301 paltrpnvev vtegieeira rsivtadgae havdtiiwgt gfgvppavfd rvhglggqsi
      361 gdryrerpss ylgttmagfp nffctlgpfg aagnqsaiym ieaqvryivd avttmraqni
      421 qridvreevq rafldevter srdtawltgg crsyyqtadg gnaglypnws feyrrrtsrf
      481 dpesyrlrag
//
LOCUS       WP_181723779             749 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Nocardia gipuzkoensis].
ACCESSION   WP_181723779
VERSION     WP_181723779.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 749)
  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 749)
  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 749)
  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 749)
  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..749
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..749
                     /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=77443
     Region          11..745
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttatqpppa gqvelviggm tcascaarie kklnrldgvt atvnyateka rvevtgeisp
       61 qeliatveqa gytavlpaap kpqetaapee dpaaalrtrl lvslvlsvpv iamamipalq
      121 ftnwqwlslt laapvvvwga lpfhraawtn lrhgaatmdt lismgtlaal gwslyalfwg
      181 tagtpgmthp feftisrmdg tgsiyleaaa gvttfllagr ffearakrra gaalrallel
      241 gakevsvlrn gterripveq ltvgdrfvvr pgekiatdgv vvegssavda smltgesvpv
      301 evgpddavvg atvnvggrlv vratrigsdt qlaqmaklve daqtgkaqaq rladrisgff
      361 vpivialsva tlgfwlgtgg svaaaftaav avliiacpca lglatptalm vgtgrgaqlg
      421 ilikgpevle strrvdtivl dktgtitagk mtlldvvpae geqvarilql agaledsseh
      481 piaqaiakga rervgelkpv ddfanvaglg vqgmvdghav lvgrarllad wsqhldeels
      541 qairaaeaeg ktavavgwdg kargvlvvad avkptsaeai sqlralgltp imltgdnqaa
      601 aaaiaaqvgi deviaevlpq dkvdtvkrlq aegkvvamvg dgvndaaala qadlglamgt
      661 gtdvaieagd ltlvrgdlra aadairlsrr tlatikgnlf wafaynvaai plamagllnp
      721 mlagaamafs svfvvsnslr lrgfrstaa
//
LOCUS       WP_181723987             390 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Nocardia
            gipuzkoensis].
ACCESSION   WP_181723987
VERSION     WP_181723987.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 390)
  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 390)
  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 390)
  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 390)
  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 390)
  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..390
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..390
                     /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=43148
     Region          37..377
                     /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..>283
                     /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 mttqiepgfa gltedltrra lrlvlerttd maagplrvpl hyyrdpkite veesqilrrt
       61 plmivpsari pepndyvvrt vlgdsllvtr drdgtahvll nycrhrgaqp acgsgnatrf
      121 tcpyhawtyr ntgelagvpg kegftgmdrg dyglvelpsq erhgfiwavl saegsididd
      181 hlgamgpela qlnyasygyh ddreftsevs wkgaleafae syhfpfvhgq svigqntvan
      241 tsthdafgrh hrmgfpfnwi taldtdptgs wdplmnmgvi ywiypnlila nspvgvevld
      301 mlpagaptrc tvrhswmakv pattdeqrav ydgiyaqvha avrdedfaml pqcgegvrhg
      361 qhdhmiigrn eigvqhmitt fatelgvals
//
LOCUS       WP_181723999             229 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Nocardia gipuzkoensis].
ACCESSION   WP_181723999
VERSION     WP_181723999.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 229)
  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 229)
  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 229)
  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 229)
  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..229
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..229
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24761
     Region          3..199
                     /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..13,115..116,145,169..170,173..174)
                     /site_type="active"
                     /db_xref="CDD:319790"
     Site            140
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319790"
ORIGIN      
        1 mktravfvdf ggvlttsvfe gfrafarsig vapelpfrll vsdplvhsaf iefetgrltd
       61 ehfetvmata ltqhggtvea tgllqrmrsg irpdvamiel iagikaagnp valvsnslgr
      121 gcydgvdlra lvdvaivsae vglrkpsram yqlacrklgv dpanvvmidd lphnidgarr
      181 agidgivhgd aattaeelat rfgvfpqlpp tpdqhktiwr rhrpthwmr
//
LOCUS       WP_181724104             502 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia gipuzkoensis].
ACCESSION   WP_181724104
VERSION     WP_181724104.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 502)
  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 502)
  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..502
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..502
                     /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=54887
     Region          1..427
                     /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 mtrhvdvlii gaglsgigma chltkeqtgr syailerrta iggtwdlfry pgirsdsdmy
       61 tfgygfrpwn gtkvladgpn irryieetaa eygvtehirf grkvttarws sdtatwtvea
      121 ldeqtgetev htsnflvgct gyydydngyr pkfpgeenfg gqivhpqhwp edldysgkrv
      181 vvigsgatai tlipamseaa ahvtmlqrsp tyitalpadd pvavgmkaak vpaklayrig
      241 rarnialqra sfqlsrtnpe aakklllaav rmqvgsgidm rhftpsynpw dqrlcvvpng
      301 dlfkvlrsgk asiatdriet ftetgirlas geelpadlvi satglsvqml ggmslevdge
      361 pvvtrdrvvy kgamldgipn ammvlgytna swtlkadlaa eyfcrvlnhm kengftrvep
      421 vatdrdrgtd svmggaltsg yiqrgdavmp rqgtngpwqv innyfrdrkl lrkgaledgv
      481 lsfaraeqap tgvrplegsr sa
//
LOCUS       WP_181724468             497 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181724468
VERSION     WP_181724468.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=52274
     Region          10..481
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mamasaasak tsewsverkg aewvtdeerr grpraqfwpw agtscnvllv sfgpyvmalg
       61 ldwhlaalaa aagavlsfll lalvslagqr ggaatmvagr aafgfhgnkv ptlisylalv
      121 gwetfsavla tlaartvahr ldpdmdtrpl mvvtlclvvl astvvgiygc hvilriqkwf
      181 alvftalsvv ycvltlpeis fathgragfg aftggimlta sllglswvnc aadytrylpr
      241 etgkralvgw itfggtapav vlmgfgtlla agdpevaara atdpisalsa hlptwflvpy
      301 lilalvgfvs gsiiglyssg lalqtlgvrm prhytvlida vliasaggyv vfaapgffap
      361 fqafltttav vmaawsgifv vdlwqrrhig ydrtalfspv gaygrvnrag igcltvativ
      421 gfglitspdp hvgpllgylf tpaaragslg ssnlgifaal ilatagyaal hrvrppaepk
      481 tteqienrdt dlirata
//
LOCUS       WP_181724439             163 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SixA phosphatase family protein [Nocardia].
ACCESSION   WP_181724439
VERSION     WP_181724439.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 163)
  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..163
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..163
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17649
     Region          5..162
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 martlilmrh gksaypqgvd dherplaprg rreaglagdw lrdtqppida vrcstatrtr
       61 etltatgita pvvfeagiye aapetlielv rlsdddvatl lvighapgmp wtawelagnr
      121 dgtaavelsr kfptsalavl rfdrawadvd tgtgelthfh ipr
//
LOCUS       WP_181724523             631 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Nocardia
            gipuzkoensis].
ACCESSION   WP_181724523
VERSION     WP_181724523.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 631)
  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 631)
  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 631)
  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 631)
  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..631
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..631
                     /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=66856
     Region          59..617
                     /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 mthprpaprp rrgpsgaraa grprqpatav pdgplrlrlg vgrvvmlval avvalqllwv
       61 qsvaapglsa qaasqrtthq pdpatrgpit drngkslaft vsakaltfqp vrvrqdlaea
      121 kaendkapdp dqrlrdiart ihekvkdaps eadllaklrs desfvylarn vdpriaseii
      181 ekfpqvgsdh qsprvhpggs laanvigatg wdghgtvgle ssldsvlagt dgsytydrgs
      241 dgavipgswr deqpavngsa veltldsdlq yyvqqqvqqa kdmsgagsas avvldaktgq
      301 vlamandntf npdlgpqkwa dtdlsnpsvt dvfepgsvnk ivtaaaavey gltdpdevhq
      361 vpgaiqmagv tvhdawthgv epytttgifg rssnvgtlml aqrvgedrfa dmahrfglgq
      421 rtgiglpges aglmpdrdqw sggtfanlpi gqglsmttlq magmyqaian dgvrippriv
      481 rakiapdgtr teetqpdgvr vvskqtaatl rtmfqavvqr dpmnanqngt gwpaaitgyq
      541 vagktgtaqk vdrncrcyst ssfwitfagm vpadnpryvi glmldapvrs sdgsgggsva
      601 plfhniaswa lqrdrippsp qpsrqfvlqa g
//
LOCUS       WP_181724087             389 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181724087
VERSION     WP_181724087.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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 389)
  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 389)
  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..389
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..389
                     /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=40243
     Region          1..389
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mrdaviveav rtpigkgkpn galhnvnavd llahslrevv ersgidpali ddviggvvtq
       61 fgeqganmtr raalaagype svpattvdrq cgssqqaihf aaqgviagay divvaagves
      121 mgripmganl vgsddisgvg fterypeglv sqgisaelia akwgltrtql defalashek
      181 aalatkngsf akelapingl atdegirvgs tletlgalrp ayydpamaar fpqigwaita
      241 atasqvsdgs aavlimtser akelglrpla rlhsfavagd dpllmltavi patakvlrra
      301 glqlsdidli eineafspvv lawaqdtgad lakvnvngga iaighplgas garlmttlvh
      361 amrergaryg lqtmceaggl anatiierl
//
LOCUS       WP_181724496             376 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide)
            pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
            [Nocardia gipuzkoensis].
ACCESSION   WP_181724496
VERSION     WP_181724496.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 376)
  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 376)
  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 376)
  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 376)
  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 376)
  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..376
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..376
                     /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=39132
     Region          1..376
                     /region_name="MurG"
                     /note="UDP-N-acetylglucosamine:LPS N-acetylglucosamine
                     transferase [Cell wall/membrane/envelope biogenesis];
                     COG0707"
                     /db_xref="CDD:440471"
ORIGIN      
        1 maaggtgghi ypavttvral reelagrgrr levlwvgqag glesrvaage sirftavatg
       61 kirraanplk mitranavdm lrvplgiaqa wravgrfrpd vvvatggyvt vpvglaawlr
      121 rrplvvheqt vrlglanrvl arlasrvaas sessvallpr raaaksvvtg npvrpelfdg
      181 dadkavvalg adgfdrslpt iyvtggaqga vqinrvvrel lpwllqranv ihqcgrasit
      241 elrehatald avlgaryvvt efvgpeladv faladvvisr sgagtiaelt algkasvlip
      301 lassagneqa hnatilaehg aavallggvs aqalrdaiep lladssrraa vaararehgr
      361 pdaareltql lisvag
//
LOCUS       WP_181724658             293 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nocardia gipuzkoensis].
ACCESSION   WP_181724658
VERSION     WP_181724658.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..293
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31232
     Region          17..280
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msateqtsap sessvkrmle ifdvapvgan tftgtsdggp rkvvdgtqll aqsvvavakr
       61 lpgrsirsah avfvrvadpd eplefvvdvt hegrsiaaas vavnqhgrrc asvsvladta
      121 asdvirhhap rprvagpaes iqadmpmagr elrivgvadv ndpaevgppe lfawlryepi
      181 pvredlakal lahftghlsv sttmrahagv gtsqahhtis tavmtvtvsf hepvgwddwl
      241 lyshestqvg agmsyvrgqv htedgrlias ftqeamirpl rrehsaipan arl
//
LOCUS       WP_181724120            1060 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl-CoA carboxylase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181724120
VERSION     WP_181724120.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 1060)
  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 1060)
  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 1060)
  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 1060)
  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..1060
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..1060
                     /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=111078
     Region          3..450
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          478..543
                     /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(500,509..511,518)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            510
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     Region          562..1056
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mqvvvvnrge vavrvlrtar ergwrtlavy taeeqhalhv rladeavvlp gvgaaayldv
       61 aavvaaagma apgalvhpgy gflsesaefa racataelvf vgpspealev fgdktaarga
      121 aeragvpvip atrrdadvae iealltahpd gvmvkatagg ggrgmravra aaslaeafer
      181 craealagfg dagvyaealv tdarhvevqi vadgraatav gdrdcsvqrr qqklvevapa
      241 pelsaalrer lhgwavrvae svgcrgvltv eflvrgedaw flevnprlqv ehtvteavtg
      301 idlvavqcdl argatladla lpgpgtargy avqarlnaei ltaggevlpg tgtlaqfapp
      361 tgsgvrvdta afagmrqdar fdsllakiia sgpsypaalr rcadalaetv vagvdtnaav
      421 lravlaelad grvvpttwfe rhldelvgra gdfpspvsvs tlaevaatav tladdeqavl
      481 spmggtvvai aepgaivpag gevavleamk mqhvvraeqd lrvhrhvvap gavvdphapl
      541 lvfvaaehdg avidevavdl dairadlaev htrhrvglde srpeavakrh rlgrrtaren
      601 iadlvdadsf veygalavaa qrlrrsqedl iantpadgli agvatidaer fgpdrsravv
      661 lsydytvlag tqgmrnhvkt drmlelareq rlpvvffteg gggrpgdtdy pgisgldvtt
      721 framgalsgr vpligivsgr cfagnaallg mcdvviatpd anigmggpam ieggglgvya
      781 pedigpievq rrngvvhvva adeadavata rrylayfqga iedwaapdpr larhvvpenr
      841 lrafdiraai esvadvgsvl elrrdwavgi vtalirvegr pfgliannch hhggaidapa
      901 adklsmflrl cdthglpivs lcdtpgfmvg pdaekdgtvt kfsrlfidsa alsvplgtvi
      961 vrkgyglgaq amaagsfrap rfvvawptge iggmglegav rlgfakelaa iddpverqka
     1021 fdnlvqlaya ngkaltaatv levddvidpa dtrrwirtlr
//
LOCUS       WP_181724871             420 aa            linear   BCT 28-DEC-2024
DEFINITION  type VI secretion system ImpA family N-terminal domain-containing
            protein [Vibrio paracholerae].
ACCESSION   WP_181724871
VERSION     WP_181724871.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536173
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..420
                     /product="type VI secretion system ImpA family N-terminal
                     domain-containing protein"
                     /calculated_mol_wt=48039
     Region          27..117
                     /region_name="ImpA_N"
                     /note="ImpA, N-terminal, type VI secretion system;
                     pfam06812"
                     /db_xref="CDD:429132"
ORIGIN      
        1 msnvifidnv cyrltndsee irglepyakv reeinrrfnp iaggtdwpvv keyceqlacn
       61 qgmdflicgy yavaclktqg lagyatgmel msaslanqge cdvksakvrk eildwvnarv
      121 vqelkalkpt yeslrdlyra erhcerlhql feqqqteykv dfegvgfalf ehidrietqy
      181 hsllkkqeka qppklkfwqr gyalftlgvl gvavgvvvgy wgwpwfyttp yaapqrittl
      241 neasqtqall ndsstterar wqhdliplyr dtlqqnltis fsepkrhait qlnllrtlyp
      301 eneqvnalsq efalqqqqal eqtalfvakf seirtkmani sllakrgkwa elekqtksle
      361 efavslspiy grvdyvqgll eqgdvtnaqk efailkqrld slswkiadle qrigdaallq
//
LOCUS       WP_181724877             383 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Vibrio paracholerae].
ACCESSION   WP_181724877
VERSION     WP_181724877.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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..383
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..383
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=41935
     Region          192..220
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(193,196..197,200..201,203,227,230..231,234..235,
                     237..238,261,264..265,268..269,272)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          196..>355
                     /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          225..255
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          291..321
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          326..353
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msvvnealak saqrshsrla nieridvakp karpawlwvm lgfgvslavg gwsislqsvd
       61 tisssaevvr pevssptqkt tqqsialyqa pvnsealvkn etlvqkatlp knetavknav
      121 lakvesspts lkqtvnrqqe qtalgtelna epvlnladns elsffeeevs slpssspvmi
      181 veqvsltpeq laqkalqraq kamesnelqt avsaytealr ytphdemvrq klaalyygkg
      241 dgrkafdlmq agiernpdge vlrlalakll vkekqdaaal vplaylpsqp sieylslraa
      301 laqktkqdei aresyqqlte kdpnngrwwl glaiqqeral qwpaaqhayq qalnkvglss
      361 qsqafihqrl qllasleetq gan
//
LOCUS       WP_181724919             223 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nocardia gipuzkoensis].
ACCESSION   WP_181724919
VERSION     WP_181724919.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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..223
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..223
                     /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=24052
     Region          <51..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 mdaadwdery aqtelvwgap pnntvvehvy glerraplqt tpegeapefp raldlacgeg
       61 rntlwlathg wqvhavdysq vgidkgrtva srlsrsvrnr itwqcadvtd ldeagitgpf
      121 elvlmvflhl paeqrralvr qaagllapeg tllvlghdtt nitdgcggpq dpailftpdd
      181 vvadlgplaa asrisvriad rvyrptetgd aidalviatr pae
//
LOCUS       WP_181725079             391 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181725079
VERSION     WP_181725079.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..391
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42466
     Region          1..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 mahsgplsgv rvvdltamvm gpyctqimad mgadvikiep pdgdntryis vgpergmsgv
       61 fvnvnrgkrs vvldlrsedg krslrelvgq advfihsmra saiarlgfgy ddvaalnpsi
      121 vytncygygr rgrdagltay ddtiqaecgl pfvqeqltgt agyvgtimad kiagmtalya
      181 ttmalfhrer tgegqeveva mfetmaafml vehangamfd pplgpaaypr avtpnrrpyr
      241 tadgylsalv yndkqwtafi eavgppwagp efatleqraa ridtvyarlg etfrerttre
      301 wldllrsldi paapvrslde lfdnphltda affetvnspy gtvrfpgppt wfsrtpgrva
      361 aaaprlgadt aevlgrlpsa adgrpngrvq r
//
LOCUS       WP_181725080             413 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Vibrio paracholerae].
ACCESSION   WP_181725080
VERSION     WP_181725080.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..413
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..413
                     /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=47505
     Region          138..403
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mlnsssmeis rsltswqkga rsiihralqy legnltvieh fpdktqtthe qfgqdrpdai
       61 havievkhpd fysrvlkggs iaaaeaymeg wwespnltal mqlmaanlgt ldklesqssp
      121 vtqwlnrfth wlkrntidqa kdnihqhydl gnelyqlfld eemlyssalf tqpelsleqa
      181 qqakmqrlcd qlqlkptdhv leigtgwgam aiymaqhygc kvttttisee qyayaqqkit
      241 alglnnqitl lkqdyrllsg qydklvsiem ieavgkaylp tflsqcyall kprgkmaiqa
      301 itiadqryes ysnnvdfiqk yifpggflps isvltelatk rtglvlrnlh digmdyaltl
      361 qhwrdrfeqq lpkvrdlgyd erfirmwryy fcyceggfla rsistvhmtf erd
//
LOCUS       WP_181725094             477 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Vibrio paracholerae].
ACCESSION   WP_181725094
VERSION     WP_181725094.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 477)
  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 477)
  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 477)
  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 477)
  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..477
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..477
                     /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=52019
     Region          2..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 maqskvlive ddeglreali dtlalagyew leadcaedal lklkshsvdi vvsdvqmagm
       61 gglallrsik qhwpnlpvll mtayaniqda vsamkdgaid ymakpfapev llnmvsryap
      121 vksddngdav vadtkslkll aladkvaktd anvmilgpsg sgkevmsryi hnasprkegp
      181 fiaincaaip dnmleatlfg yekgaftgav qacpgkfeqa qggtilldei semdlnlqak
      241 llrvlqerev erlgsrksik ldvrvlatsn rdlkqyvqag hfredlyyrl nvfpltwpal
      301 cerkddiepl anhlierhck klglpvpsia pnaitkllny pwpgnvreld nvvqralils
      361 enghiqsehi llegvdwhda sslqqavage siaapqikpv aepevfkplv qgggqscssq
      421 ssglggelrd qefaiildtl aecqgrrkem aeklgisprt lryklakmrd agidipg
//
LOCUS       WP_181725101             338 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardia gipuzkoensis].
ACCESSION   WP_181725101
VERSION     WP_181725101.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=34405
     Region          33..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 mtrvdtpraa pvrsripvlg ivfaalvlcv alslalgars vplgsvveal lgrgagrdam
       61 vitgmrlprt ivglavgaal glagavvqgi trnplaaptt lginagagla vviaiyalal
      121 shpiqyvwfa fagaagaatf tmalgrragd ldpvrlvlgg tmlqlvlvsw tsavllfser
      181 tldearfwla gsiaerdlev llpmlptlll gavvglaivp alntlalgde aaqalgmpva
      241 rirlagmvav vllagsavav agpiafigla aphlvrlvvg tdhrllipgc liagplllls
      301 adivgrliar psevevgivt aflgapllav larrkerr
//
LOCUS       WP_181725116             363 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardia gipuzkoensis].
ACCESSION   WP_181725116
VERSION     WP_181725116.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=36654
     Region          42..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 mslsqteaar pvtpvptsrs rsrlvlvfvv asaglvalal vsaaigqvpt tpaevagsvl
       61 hrigleigpm pahpsgevtl wqvrfprvvl avlvgaalat agallqgvfa nplaepgvig
      121 vsagaavgag tvivvggafv aawsvaaaaf vaglattllv yllarsggrt evvtlvltgv
      181 ainafaggli alllfvaspa ardqivfwql gslngarwes vgvvapltav gvvaavllap
      241 rldllalges aarhlgvdve rlrrnvivvv avlatagvaf tgiilfvgli vphlvrmlvg
      301 pahrvlipls aivgavvlla advtarslvd nadlplgmlt sliggpvffw llrrtrarsg
      361 gwa
//
LOCUS       WP_181725283             610 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Vibrio].
ACCESSION   WP_181725283
VERSION     WP_181725283.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 610)
  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 610)
  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 610)
  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 610)
  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..610
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..610
                     /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=70520
     Region          <164..592
                     /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 mltkytqlaa wslaqlevet lnfthrlety llngsrenhq amslnydilw nrfdlfltsk
       61 etqelrqqhd aqaiiqevft qlkryelavs rgdepvlqel lklldpynak irnlaivnft
      121 gesansnirm inenkqqlly ffaaillmli llsymtyrsa dyqqflawhd pltrlknrnf
      181 ivkklkkrrr sqqepialil fdlnrfkeln dtmgyafgdk lliniadllt qrcrafayqc
      241 arigadefav llhpctgnad ffirnlwndl tklvqendpt krlsvamgvv tcqtqdftes
      301 ssklrassll nnadlalnia kkapegqvvy ytrdiesayn kkrilaeqlq qllldpnqss
      361 lylsyqpils rnpdrlgcea lirwqhsdfg yinpqyliei aeeygfgkkl gewimqqvyl
      421 alqndwkpyn rrldvsinls nslfdetlpa lvttifghhe nflnaiilel tetmtiddfp
      481 qslaiiesle kmkvrfaldd fgtgwsslyq lnhlkfsklk idksfvdnmn qnqqqaifia
      541 sivnlshqlg mqvvaegveq laqleqlkql gvdefqgyyf srpvtktefa tfcdryfsse
      601 ntslstqinq
//
LOCUS       WP_181725089             254 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181725089
VERSION     WP_181725089.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=26992
     Region          2..235
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mlrpnqvkrk ldagalvhgl fcslpepalv emiacggydf vvldtehali dpqqldhlir
       61 taeaagltpf vrvpagdsga ilraldagam givvpqvssr advdaavrat yfapvgmrsl
      121 gggraagfgl idhaqylhra nteimliali edaegvaaid dilagscidl vmpgpadlsq
      181 sygvpwqlrh prvqeaverl hhactthhvp fcamtrtper yeqwraadvr afacgdvadl
      241 aaaaigrslt dmrg
//
LOCUS       WP_181725286             118 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Nocardia
            gipuzkoensis].
ACCESSION   WP_181725286
VERSION     WP_181725286.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..118
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13106
     Region          9..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mgakrsgpyf cgidaamdvv ggkwkalilw elenhgvrrf gelrkglpgv sekmliqqlr
       61 eleedgivsr tvyrevpprv eyrlteigga lnaalaplgd wgraridrig arrvhqql
//
LOCUS       WP_181723962             111 aa            linear   BCT 28-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Nocardia
            gipuzkoensis].
ACCESSION   WP_181723962
VERSION     WP_181723962.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 111)
  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 111)
  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 111)
  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..111
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..111
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12165
     Region          1..109
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 markvvvtlv ddydgksqae etvsfavdgv ayemdlsaen agqlrgffdq wvpyarkvgr
       61 trrgrggvlr sandreqatv irewarkngi dvsargrisa evveaykkan g
//
LOCUS       WP_181725352             199 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [Nocardia].
ACCESSION   WP_181725352
VERSION     WP_181725352.1
KEYWORDS    RefSeq.
SOURCE      Nocardia
  ORGANISM  Nocardia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (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   2  (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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Nocardia"
                     /db_xref="taxon:1817"
     Protein         1..199
                     /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=22191
     Region          38..124
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mrtsliyrng tvyevlmrgl ygkhytaryr aiaelvprga svvdlccgpa tlytrylrhk
       61 svdytgldln erfvarvnea ggrgevwnlr aedalptady vimqaslyhf lpepqplidr
      121 mlaaanrqvi vaepirnlat sdnpllatig krftdagdge qahrftertl dalftayepr
      181 varqsliagg reklyvlta
//
LOCUS       WP_181725447             413 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Nocardia
            gipuzkoensis].
ACCESSION   WP_181725447
VERSION     WP_181725447.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..413
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=45211
     Region          23..399
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mnatavvpep gkrivrarkr srkpvrrtli sihrwsalll glvlvvqsts gaillyhael
       61 fraqhasfyr htdappvvdt eravalvraa dpgfdtgwvg rdggvivvgn ttftaaysid
      121 pgtgrinerv nltdgvlgwl vnlhdcafgc lrysgalpil enqapligit waasilcalg
      181 lllislavsg aiiwwpslsr lrngfrvrlr kgrfardrdl hsvlgvlavp fllmwgitgi
      241 tmewpavara wlvatggtan lertekyfvp rsdgagrtpi tigeagaiah qaapgrlayl
      301 llptdsapyy rasvagaysp rehrlfysgd vlvyvnaydg sdikvvdash grplantfya
      361 kvfepahfgw mvngwcrlvw lafgltplal altglstwlf rrrtkyrrdr att
//
LOCUS       WP_181725538             314 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nocardia gipuzkoensis].
ACCESSION   WP_181725538
VERSION     WP_181725538.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..314
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..314
                     /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=33214
     Region          <38..314
                     /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 mrrssghngd lfaaythhld qvmvqtfpei addditcvdr nafrhalltg maddvhfgkr
       61 lagyqltdsg rvrvefadgg gdegdvlvga dgvgsavrrq llpdatvrdl glrclygrmt
      121 itetteplip qdlhrgfswv gdgdgcgagf apvrfrarpd gtadylmttl vatpqrlgva
      181 dadlfafsse qlwklavdtt aswhsairel yahadsgtff pitiraaerl daipsgpvtl
      241 lgdaahampp tggagantal qdaatlagel lgaargdkpf seavaayerv mlprgfaavd
      301 dslrmaghlf gnag
//
LOCUS       WP_181725553             232 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Nocardia
            gipuzkoensis].
ACCESSION   WP_181725553
VERSION     WP_181725553.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 232)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..232
                     /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=25169
     Region          16..>148
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mpsfadfdrr dyrtvdvatg ydgwaptyeq tvldemdlal lgrlrldlgr vrraadlgcg
       61 tgrtgtwlre rgithidgvd vsqgmlalaa ergahttltr advratglpe gaydlviasl
      121 idehlpelap fyaealrlaa pgarcvlvsy hpqfimvsgm pthytdpsge pvaisthlhl
      181 isehlsagla agwaltevae avvddawlar kpkwaalrgh pftlatvwsr qe
//
LOCUS       WP_181725664             558 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Nocardia
            gipuzkoensis].
ACCESSION   WP_181725664
VERSION     WP_181725664.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     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=60274
     Region          7..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 msesarplle itdlnvsfta dgkpvpavrd vslsvypgqt vaivgesgsg ksttahaiid
       61 llpgtgrits gsiifdgkdl taaskrqiva vrgsgiglvp qdpmsnlnpv wkigfqiret
      121 leangiakgk aaakravell eeagmpdagr rvnqyphefs ggmrqralia iglscrpkll
      181 iadeptsald vtvqrqildh leqltadlgt avllithdlg laaeraehlv vmyrgrvves
      241 gpalrilrdp qhlytkrlvs sapslaaqrr savrrrteih aqavqvaadd ttvpdevvva
      301 etltktfrir grapwkssef vavddvsfrl rrgsttaivg esgsgkttva rmvlglleps
      361 sgsvtfdgkd vatldrkgaf afrrrvqpif qdpygsldpm ytiyrtieep lrthgigspa
      421 ereatvrell dkvalpvgvm rrypnelsgg qrqrvavara lalrpevvvc deavsaldvl
      481 vqaqilqlln dlqaelglay lfithdlavv rqiaddvlvm qhgkvveaat tdevfddpqq
      541 eytrklldai pgrdllag
//
LOCUS       WP_181725952             317 aa            linear   BCT 28-DEC-2024
DEFINITION  YbgA family protein [Vibrio paracholerae].
ACCESSION   WP_181725952
VERSION     WP_181725952.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..317
                     /product="YbgA family protein"
                     /calculated_mol_wt=36026
     Region          70..314
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mqttplkigi sacllgakvr fdgghkishf vtneldryae fvsvcpeigm glpvprptlr
       61 lisenerial vetkdssrdh taalesysqq kvaelqhael cgyivcaksp scgmervkvy
      121 khngtekdgv glytrilmek mpwlpieedg rlndpvlren yitrvfclhd fytsmgdaps
      181 akkivefhsr ykltlmahnp qayralgrlv anvkqyplds fiqeyrlglm qalahrasrk
      241 nntnvlmhlq gyfkrslnkl qkaelaqvie syrvgelpll apitllkhyl alfpdaylaq
      301 qrylnpypqe lklrygl
//
LOCUS       WP_181725825             413 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Vibrio paracholerae].
ACCESSION   WP_181725825
VERSION     WP_181725825.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..413
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..413
                     /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=47534
     Region          138..403
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mlnsssmeis rsltswqkga rsiihralqy legnltvieh fpdqtqtthe qfgqdkpdai
       61 havievkhpd fysrvlkggs iaaaeaymeg wwespnltal mqlmaanlgt ldklesqssp
      121 vtqwlnrfth wlkrntidqa kdnihqhydl gnelyqlfld eemlyssalf tqpelsleqa
      181 qqakmqrlce qlqlkptdhv leigtgwgam aiymaqhygc kvttttisee qyayaqqkit
      241 alglnnqitl lkqdyrllsg qydklvsiem ieavgkaylp tflsqcyall kprgkmaiqa
      301 itiadqryes ysnnvdfiqk yifpggflps isvltelatk rtglvlrnlh digmdyartl
      361 qhwrdrfeqq lpkvrdlgyd erfirmwryy fcyceggfla rsistvhmtf erd
//
LOCUS       WP_181726116             118 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Polaromonas
            sp.].
ACCESSION   WP_181726116
VERSION     WP_181726116.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp.
  ORGANISM  Polaromonas sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
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="Polaromonas sp."
                     /db_xref="taxon:1869339"
     Protein         1..118
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13191
     Region          6..107
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mprkshytcg ldialavigg kwkpliifhl ggerrrfgel krlvegisek vliqqlrdla
       61 edgviarhdy revpprvdye ltafglslae alkplcawge vnrkevgtlq rpettkda
//
LOCUS       WP_181726131             100 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Polaromonas sp.].
ACCESSION   WP_181726131
VERSION     WP_181726131.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp.
  ORGANISM  Polaromonas sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
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="Polaromonas sp."
                     /db_xref="taxon:1869339"
     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=10979
     Region          2..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdllevfkal snrtrleilk glkdpeknfp pqdegdvltv gvcvssiqeg vglsqstvsd
       61 ylatlqragl vevrrigqwt yykrneatis vlaeiigkel
//
LOCUS       WP_181726153             265 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Polaromonas
            sp.].
ACCESSION   WP_181726153
VERSION     WP_181726153.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp.
  ORGANISM  Polaromonas sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
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   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 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   4  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Polaromonas sp."
                     /db_xref="taxon:1869339"
     Protein         1..265
                     /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=28306
     Region          4..235
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mdcivltgaa grlgrslrpa laaacrelrv ldrsplvseh anetalqldl ndqaalasal
       61 tgasavvhfa gypreadwpt llaanvvgva slweaarvag verilyassn havgmyprse
      121 klsqgalpap dsrygvtkvf meslaslyaa khglrgfgir ighcapqpsd armlshwihp
      181 edlsalvqvg lqadyeneyv ygvsanslsw wlndraealg yrpahsadrf igslqaqtsa
      241 spvaeyfqgg sfaaaefdnp rfrpa
//
LOCUS       WP_181726191              89 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Polaromonas sp.].
ACCESSION   WP_181726191
VERSION     WP_181726191.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp.
  ORGANISM  Polaromonas sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 89)
  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 89)
  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..89
                     /organism="Polaromonas sp."
                     /db_xref="taxon:1869339"
     Protein         1..89
                     /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=10226
     Region          3..89
                     /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 mvwkveldpa aereldkldp qnarriltfl hsrvavlddp rslgealkgs rlgefwkyrv
       61 gdyriissie dgalrifvvk vgnrrevyr
//
LOCUS       WP_181726385             212 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [Klebsiella].
ACCESSION   WP_181726385
VERSION     WP_181726385.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..212
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=22488
     Region          1..189
                     /region_name="TerY"
                     /note="Uncharacterized conserved protein YegL, contains
                     vWA domain of TerY type [Function unknown]; COG4245"
                     /db_xref="CDD:443387"
ORIGIN      
        1 mrrlpvylll dtsgsmhgep ieavkngvqt llttlkqdpy aletayvsvi tfdstarqav
       61 pltdllsfnl psfsasgtta lgealsltan ridaevqktt aetkgdwrpl vflmtdggpt
      121 ddwrkgvnef kaakkgvvva caaghdadta vlkeiteivl qldtadsssi eaffkwvsas
      181 vsvgsqkvda gkkevigldd lpppppevnv vl
//
LOCUS       WP_181725577             463 aa            linear   BCT 28-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Nocardia gipuzkoensis].
ACCESSION   WP_181725577
VERSION     WP_181725577.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 463)
  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 463)
  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..463
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..463
                     /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=50697
     Region          4..459
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 merltgldas flyletgtqh lhvcallild pssgdysfeg fkaelarrlp lipqmrrrvy
       61 evplnldhpv wvedenfdld yhvrriaiaa pagrrelael vgdiasrpmd rdrplwemsv
      121 veglddgkva vvskyhhaav dgitganlmm hlcdpepgvt ktvpedewrp epkpndwqml
      181 aeavvkfptr agivgmlpkt vgvvagfaqr rrenkagmai pfsaprtpfn laitphrava
      241 ftdaeldaik eirsafsvkv ndvvltvvag alrtylaerd elpdrslias vpvsvhestr
      301 htagvnkvst lfarlgtdva dpvqrlreva ennrgakeeh eamgadflqd wskyappntf
      361 rlaarmyssl klaemhpvvh nlvvsnvpgp pmplyflgvr vdgmypfgpv fhgagltvtv
      421 lsnndklnfg fiackelvpd laaladavpg vvaellsaar ksg
//
LOCUS       WP_181726576             286 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SRPBCC family protein [Micromonospora].
ACCESSION   WP_181726576
VERSION     WP_181726576.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 286)
  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..286
                     /organism="Micromonospora"
                     /db_xref="taxon:1873"
     Protein         1..286
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=32105
     Region          17..143
                     /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(18,20,22,31..33,35..36,41,48,56,58,60,62,72,75,81,
                     83..84,95..96,98,100,110,112,122..130,132..134,137)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mddhggdrsr rlpgappvrt aitvpvgvde lwaaltdpvr laawfgttrg dwhvrtpwri
       61 dfgdgdffvv tpvrvtddrl ieftwsflgv gpeqhitwra aptaggarlt vedadpvrpp
      121 aeieqmragw tdflrrldgy lrtgrstryd wrsdidgsvd lplgwdafep sllyrwlpva
      181 sdgfrpawff vvdadgprrf plddwsvreg tvtftvqvte rgagttaela vhrladrqrl
      241 efshqgwrhl glpdnrahal rrrfaaawta aadcarelar lsvppg
//
LOCUS       WP_181724842             802 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Nocardia gipuzkoensis].
ACCESSION   WP_181724842
VERSION     WP_181724842.1
KEYWORDS    RefSeq.
SOURCE      Nocardia gipuzkoensis
  ORGANISM  Nocardia gipuzkoensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 802)
  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 802)
  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 802)
  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 802)
  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 802)
  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..802
                     /organism="Nocardia gipuzkoensis"
                     /db_xref="taxon:2749991"
     Protein         1..802
                     /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=88446
     Region          74..800
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mtqhlgeakv eqstsgpqsn gagatdaaqv aksqtpanat pprqpgtsaa vptsasrrvr
       61 arlarrmtgq rgiaavkpvl eplatvhrel ypkanltllq rafdvaddrh khqfrksgdp
      121 yithplavan ilaelgmdtt tlvaallhdt vedtgysleq ltqdfgseva hlvdgvtkld
      181 kvnlgaaaea etirkmiiam ardprvlvik vadrlhnmrt mrflppekqa kkaketlevi
      241 aplahrlgma tvkweledla failhpkkyd eivrlvadra psrdtylarv raeivntlaa
      301 srinaivegr pkhywsiyqk mivkgkdfdd ihdlvgiril cdevrdcyaa vgvvhslwqp
      361 magrfkdyia qprygvyqsl httvvgpdgk plevqirtqd mhrtaefgia ahwryketrg
      421 khsndtaevd dmawmrqlld wqreaadpae fleslrfdlk speifvftpk gdvitlpqks
      481 tpvdfayavh tevghrciga rvngrlvale rqlengevve vftskaqnag psrdwqnfvv
      541 sprakakirq wfakerreea lesgkeqisk evrrvglplq rlmsvdamta vahelhytdi
      601 stlytavgeh qvsahhvvqr lmaqlggigd venelaerst psttpsrqrv tgdagvlipg
      661 atgtvaklak cctpvpgdei mgfvtrggav svhrtdctna gslreqaeri ievswapsps
      721 svflvaiqie aldrtrllsd vtkvladekv nilsasvath gdrvaiskft femgdpkhlg
      781 hllnvvrnve gvydvyrvts aa
//
LOCUS       WP_181726961             187 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Escherichia coli].
ACCESSION   WP_181726961
VERSION     WP_181726961.1
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=21143
     Region          53..148
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mhsqlrerir lmrarldnar pvieipaefq lfvtpapvcd rlvtlaeisn rdhilepsag
       61 tgailraird tapgamcdav einsglvryl renfngvrvq hgdfmewqpt qyysriimns
      121 pfshgqdirh ilrafsllrp ggvlvavcln gprqqekllp fsdvreelpr gtfaytrvpt
      181 miirlra
//
LOCUS       WP_181727361             263 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Streptomyces sp. PT12].
ACCESSION   WP_181727361
VERSION     WP_181727361.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. PT12
  ORGANISM  Streptomyces sp. PT12
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 263)
  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 263)
  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 263)
  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 263)
  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..263
                     /organism="Streptomyces sp. PT12"
                     /db_xref="taxon:1510197"
     Protein         1..263
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27908
     Region          100..258
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mpvsrtrkpk qkpreparpq argrgnaprr laaaliaafl vcvlavggls alsggeadgg
       61 ggadgegdas vqplpsdhpa ldvarrdadd plalgdadap vvmieyvdfq dafsgiharq
      121 thdalvaeyv esgdvriefr nypingpesd aaaraawaag rqgrfwefya aalgeefhrd
      181 sgrfeeegar alaeeagvad vdrfaadmes deafdavqrd adegfdlgvs stpsfmingq
      241 aiegarplde frelldqlie sap
//
LOCUS       WP_181725193             470 aa            linear   BCT 28-DEC-2024
DEFINITION  SLC13 family permease [Vibrio paracholerae].
ACCESSION   WP_181725193
VERSION     WP_181725193.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 470)
  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 470)
  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 470)
  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..470
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..470
                     /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=50596
     Region          109..465
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mrpylkyiip llipilvlml patafpfegl tviqqrviai fllaallwvf epipiystsv
       61 viivlevlml sdkgfilfrl gegtsefgal lksteimatf anpiimlflg gfflamaatk
      121 yrldvnlarv llkpfgnnpk yvmlglmmit avfsmfmsnt attammlsil tpviavfgpk
      181 dpgrvafalc ipvaaniggi gtpigtppna ialkylvgdn litfaewmaf gipfvvilma
      241 lawlliefmy raeqktiels ikgkflktpk aiivyitfas tillwmlgsl hgmnsysval
      301 ipvavfsvtg iigkedlkmi swdvlwlvsg gialglaldk tglaelvvhs ipfdqyspyv
      361 vilgaailcl lmanfmshta tanllmpima algasmtsln pldgevtlil vvtfaaslgm
      421 slpistppna lahatgnvqs qqmakvgiil gilgvlmsfv mvwllnmvgh
//
LOCUS       WP_181727416             108 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces sp. PT12].
ACCESSION   WP_181727416
VERSION     WP_181727416.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. PT12
  ORGANISM  Streptomyces sp. PT12
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. PT12"
                     /db_xref="taxon:1510197"
     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=12070
     Region          <7..64
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mprhtrlsag eiagrfavsr paisrhlrvl resglvtdea dgrrrlyald psrlaqltaw
       61 laqfeqpspw aqrfdalgte vararrdrrh repaeegrsg gtarrdta
//
LOCUS       WP_181727459             944 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp. PT12].
ACCESSION   WP_181727459
VERSION     WP_181727459.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. PT12
  ORGANISM  Streptomyces sp. PT12
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 944)
  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 944)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 944)
  AUTHORS   Rosinski,J.A. 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 944)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..944
                     /organism="Streptomyces sp. PT12"
                     /db_xref="taxon:1510197"
     Protein         1..944
                     /product="helix-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=103128
     Region          <3..892
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          881..931
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 malverdyel kllnelftet hrghgriali sgavasgkte llhafsdacg dgggrvlrat
       61 atsadtgvpf gvlrqlvepl dlpadlvdgl aappvgpkal qaltarvlel sereplllcv
      121 ddvhhadess mdsllrlvkr mrsarvmlvl teaacawsvh pafrielvrq tqfrrfrltp
      181 lsvdgvaeml aqhlgqpaaw tlarethlat ggnqllvral iedytdsvgl pgqvdgyamg
      241 esfgqavltc lhrsspetld varamavldt tgsadrvael ldrepksvar alqalrsvgl
      301 veggrfrhpq irsaiydald qhqltrlhtr aarllhdgag svtdvadhlv aarqveadwa
      361 itelqraaer aladddeqaa lryaefalsm cavarqraal rmlltriewr snpeaaarhl
      421 pplfeaqreg hldtvqtaal lrsvmwhgrt qdatelierl phlragetgq pseplastrh
      481 wlrhdcpqll ppetetaaqp atggaaahgr aaasppgqqa qaaavlravl gqgrdedgrl
      541 trvaeqilqt talsdhtlea vcsalqtliy teqlpmaarw cdslldeada rkvtwwqail
      601 sccraeisvr hgelaeaerq alralrligv rgwgvavgap vgillevats mgdfdsarky
      661 lrepvpevmf qtryglsylr argryylatd qlqaalanfr ycgdlmtawg idapafvpwr
      721 sdlaeaylrl geqeraqqla kdqiarsgsr tsrtygyslr vlaatanhla rlrmlkesve
      781 vlqargdrmt laqaladlsr vhhslgdfgk armisrrarr ltkecqaqpa radeaaarpe
      841 kplvvvadda eawtppaepg pqtrpparpe patgggggev ltlserrvaa laslgytnre
      901 isgklhitvs tveqhltkvf rklrvkrrtd lpvdlelrae rsac
//
LOCUS       WP_181727784             218 aa            linear   BCT 28-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181727784
VERSION     WP_181727784.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>218
                     /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]"
     Region          29..>162
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 macarypscl ahlrlrmkrh fsmlrdfqla dwftlanafc gtgavfaamr flqeehrgdl
       61 llgmalipla fvfdaldghv arwrkasstl greldsladv isfgvapaal gyacgmrggw
      121 dwlvlsyfvc cgvsrlaryn vtaeeiagea dkvpyfegtp iptslllvil lavaasighi
      181 getlwwgqwq lgpwqfhplv llfavsgslm isktlrip
//
LOCUS       WP_181727767             587 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein, partial
            [Xanthomonas oryzae].
ACCESSION   WP_181727767
VERSION     WP_181727767.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 587)
  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 587)
  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 587)
  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 587)
  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..587
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         1..>587
                     /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          6..555
                     /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 mktgrnrtrs nfnlrgrltl vgialglcsv tligraafvq lvnrdfyqrq gearylrelp
       61 iatsrgmitd rngeplavst pvesiwvnpq ellrnpdrip elakalgqpl delnaklaqk
      121 agkefmylqr rinpdkahai vdlkipgvfs qrefrrfypq geamahvlgf tniddrgqeg
      181 lelafdewlr gkpgskkvvr dargaivesv dlvrpaqpgk dltlsidrri qflaykelrn
      241 alvennaagg smvvmdvatg evlamvnlpt ynpnsvtgin psarrnravt dlvepgstmk
      301 pltvatalta gvvtkdtvid tnpgymsvgr ftirdvphnn gvlnvtgvit rssnigaaki
      361 aakvpdqtfy qsirnfgygs aphsgfpges agvvlqparw sgpskttmsy gyglsvtplq
      421 iaqayatlgn ggkltpptfv rgqhnetrqv itpevarqvi dmmetvvtqg gakgaailgy
      481 hvagktgtar kngasgyerg hynalfaglv patrprfatv ivindpqgkv yygglvsapv
      541 fhkvmegalr lmdvppddiq swlaaqaagk tgqpmvkpqs adldpal
//
LOCUS       WP_181727836             467 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Parageobacillus
            thermoglucosidasius].
ACCESSION   WP_181727836
VERSION     WP_181727836.1
KEYWORDS    RefSeq.
SOURCE      Parageobacillus thermoglucosidasius
  ORGANISM  Parageobacillus thermoglucosidasius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Parageobacillus.
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: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Parageobacillus thermoglucosidasius"
                     /db_xref="taxon:1426"
     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]"
                     /calculated_mol_wt=52979
     Region          9..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 mnkrdlerar kerlkllrei egllsfitdp vlvvdvkghi vhtnsaaeqm lersqiimig
       61 khvtefvqsa slsqyikqgk paanlavcmm nakgarlefs crlhpllvda qvegailfft
      121 kpalrqeqek sfrygtrfsl ddvigsspai talkeqvmki aksestvlir gesgtgkevl
      181 aqsihrlshr nkgpfvainc aaipealles elfgyeegaf tgakkggkpg rfelakggtl
      241 fldeigdmpl ylqakllrvl qerriervgg tksievdvri iaathkdles miannqfred
      301 lyfrlnvipl yvpplrerke dlyeliqyym hkfckrfgke pkrfssqalk kifdyhwpgn
      361 irelenmvey ivnleigdlv tvsslpapir empedqhrdm aeethepqtv shlskslykv
      421 neveeqliiq alqrfgtste gkrkaaealg islatlyrkl ekmkrrr
//
LOCUS       WP_181728089             441 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Glutamicibacter soli].
ACCESSION   WP_181728089
VERSION     WP_181728089.1
KEYWORDS    RefSeq.
SOURCE      Glutamicibacter soli
  ORGANISM  Glutamicibacter soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Glutamicibacter.
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="Glutamicibacter soli"
                     /db_xref="taxon:453836"
     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=46321
     Region          31..414
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mnqhninyae hslatvplpr klrrdrltst igatcltfcv sfviafgllv psgtahfnvn
       61 vsayliqytl lagvsglcfa lvgklvprfg irrliiiggt ittlsifams lttnlylfyv
      121 faavhgvgws actlvaatvv vngwhvhrrk gtvlglvlag navggmvwgf vlppvirsfg
      181 wsggmqllai iaavmmvlpg ifliknppra intgnpdapv klptlrkael vgvmalltlg
      241 tfciclegga iqilptlleh rgidtakaga lvsmyaiggi fakplfgyly dkigplrsvw
      301 vaslayvvaf pgialtqsva syylfiplma lalatftvlv plivadavgq arfpdaygkv
      361 mtvgslglai atplwglafd itgsftpaly aaavlgvlgl vllhlgrtrg ravalrttrq
      421 aqaamasest apdateaaag r
//
LOCUS       WP_181728158             461 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Glutamicibacter soli].
ACCESSION   WP_181728158
VERSION     WP_181728158.1
KEYWORDS    RefSeq.
SOURCE      Glutamicibacter soli
  ORGANISM  Glutamicibacter soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Glutamicibacter.
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="Glutamicibacter soli"
                     /db_xref="taxon:453836"
     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=48603
     Region          206..426
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 maeklirgsi tqtsddgrgy yllkialfsi faipssmvle pigasgsvpm llalslsavw
       61 fassifglhn pledkhpgrf algalviatc lsyvamfsgw tggsnittra aadrwlllia
      121 asaglmltvt haarsvdgil rivrpfiaga vvcsviaaiq ftlrinpvew iqqampgfty
      181 nggdttfqvr gtflrvagtt ftsielavvs amvlplaiwr alydpkgskm lhwlgcallt
      241 fsmvatvsrs silglvvsll iffpflpala rkwatliipv vgalvfltip gmvttltgsl
      301 fsgtsdpsis trtdnyprva rmidanpvlg lgpgnyipdf aiyfldnqyl saavtlglvg
      361 mvatimyfav pavstavaac slkdpalkcf agavtagisv gaacsltfds lsfpvfalaf
      421 pvlsglggva wnlargrpsh khklsgatts tkkhnrrkvg t
//
LOCUS       WP_181728383             136 aa            linear   BCT 28-DEC-2024
DEFINITION  segregation and condensation protein A, partial [Xanthomonas
            oryzae].
ACCESSION   WP_181728383
VERSION     WP_181728383.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas oryzae
  ORGANISM  Xanthomonas oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 136)
  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 136)
  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..136
                     /organism="Xanthomonas oryzae"
                     /db_xref="taxon:347"
     Protein         <1..136
                     /product="segregation and condensation protein A"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
     Region          <1..109
                     /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 qahlperaav klpppvelke mlmalydvlk raelftghai krealsvrqr mgdvlsrldd
       61 gkfyrfeslf taeegklgvl vtflallela keqlldivqe aplapiyvks lalgntnapl
      121 qfssefddsd aanepl
//
LOCUS       WP_181728516              74 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Parageobacillus
            thermoglucosidasius].
ACCESSION   WP_181728516
VERSION     WP_181728516.1
KEYWORDS    RefSeq.
SOURCE      Parageobacillus thermoglucosidasius
  ORGANISM  Parageobacillus thermoglucosidasius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Anoxybacillaceae; Parageobacillus.
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="Parageobacillus thermoglucosidasius"
                     /db_xref="taxon:1426"
     Protein         1..74
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8389
     Region          10..58
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     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 mwgigkprsr lgkwldkngl eqqdlakaak vskntiskac ndknyiprqd vmkkilkavr
       61 kidpnakmsd fwdm
//
LOCUS       WP_181726514             136 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RidA family protein [Micromonospora].
ACCESSION   WP_181726514
VERSION     WP_181726514.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087367
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Micromonospora"
                     /db_xref="taxon:1873"
     Protein         1..136
                     /product="RidA family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=14003
     Region          19..131
                     /region_name="YjgF_YER057c_UK114_family"
                     /note="YjgF, YER057c, and UK114 belong to a large family
                     of proteins present in bacteria, archaea, and eukaryotes
                     with no definitive function. The conserved domain is
                     similar in structure to chorismate mutase but there is no
                     sequence similarity and no...; cd00448"
                     /db_xref="CDD:100004"
     Site            order(19..20,23,25,32,34,36..37,77,79..80,82,84,95,98,
                     108..115,126,128,130)
                     /site_type="other"
                     /note="homotrimer interaction site [polypeptide binding]"
                     /db_xref="CDD:100004"
     Site            order(19,91,95,110,126)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:100004"
ORIGIN      
        1 mrltldnpas vaapfgdrfa hvaridvggg allmlagqva vdddgtvvap gdagaqaeri
       61 feivggvlaa hgasfddvlh irtfmtdlad lpayaavrrr lfpgtpppas ttveisklfl
      121 pgavlevevt avvrsr
//
LOCUS       WP_181728062             286 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Glutamicibacter soli].
ACCESSION   WP_181728062
VERSION     WP_181728062.1
KEYWORDS    RefSeq.
SOURCE      Glutamicibacter soli
  ORGANISM  Glutamicibacter soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Glutamicibacter.
REFERENCE   1  (residues 1 to 286)
  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..286
                     /organism="Glutamicibacter soli"
                     /db_xref="taxon:453836"
     Protein         1..286
                     /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=30957
     Region          3..277
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mmridahlhl weldgpvphp wlgpqlgklh adfpavqagd vlrehgidga vlvqasdsea
       61 eteyllaaaa thawvagvvg wvdlsdpraa eaqlerwlpg gmlvgvrhli hdepdpafil
      121 rpavrdslgl laeagvpldi pdayprhlhq apvlldavpg lrlvidhlak ppfirgaeam
      181 adwermlrli avypavtskv sgldfgpgfs aesvrvaiev aldcfgaerl myggdwpmtv
      241 aghgygqnlr aissavdels laeresiwsg twkrvygrnr snaeii
//
LOCUS       WP_181728716             322 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Staphylococcus aureus].
ACCESSION   WP_181728716
VERSION     WP_181728716.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..322
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..322
                     /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=34233
     Region          24..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 mmttkiirry slitillivs ifislcvgsv mihpidaikg iftqddfiln eyriprtllg
       61 iiigsslais gaiiqavirn plaspdvigi skgaslaavi iimifttapl fvlpigsflg
      121 afavslflsf liskydvkgs klaliglaig aictaivqfl lirnpleank alvwltgsly
      181 ghdmsniyti lpwflitipi iillsyqldv lnlgdavata lglkvktikm lllilavila
      241 gsaisvvggi sflgliaphi arqlignktl hviimsglig ailltfgdgl argihppldi
      301 pvgviiaiig apyflillrr mk
//
LOCUS       WP_181728880             351 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Streptococcus
            suis].
ACCESSION   WP_181728880
VERSION     WP_181728880.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 351)
  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 351)
  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 351)
  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..351
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..351
                     /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=40121
     Region          21..351
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mkrkvfehyq pykikqkarf dlgnnenrii dwsflpqetl enldvnqlsf ygdntyseli
       61 ekyatylgvn pkqvtvgvgs dhlihmivst fmekddtflt vnpdffmyet ynhmhgsrfe
      121 tidleekndt lvlpveklla raeevkakii mlsnpnnpss vaysledlek laisfkgllv
      181 vdeayiefan vesfisrlqh fdnvlvlrtl skafglaglr vgfavgseel iyeldkvips
      241 fslsnltakm aavalnytdk vletvgviqn lreemilflq gldncqvlps qasfvtfkap
      301 waeefyqqal aqdwnfkyyp tgkleghirl sigrpeemdm mkkmieklve a
//
LOCUS       WP_181728983             419 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein, partial [Enterococcus faecium].
ACCESSION   WP_181728983
VERSION     WP_181728983.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 419)
  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 419)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..>419
                     /product="vWA domain-containing protein"
     Region          <290..>409
                     /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 mtttgkklkv ifmliilsls nfvplsaiad ttddptvlet isaevisdqs gkkalnikln
       61 anntsaekie keiglvenyl sdverkegdg yayqvnsgki tleissntkq tidlsfpidp
      121 alyhsqankl ivdnkeydii detenkkdtd vsvpkpdeie eesskenens vspftlptls
      181 lpavsvpsnq tipteyttdd qgtypkaswq ptgntnvldh qgnkngtnqw dginswngdp
      241 ndrthsyiey ggtgnqadya irkyaketst pglfdvylna rgnvqkditp ldlvlvvdws
      301 gsmndnnrig evkigvdrfv dtladsgitd kinmgyvgys segysysnga vqmgsfdsvk
      361 nqvksitpsw tnggtftqka lrdagnmlsv pnghkkvivl ltdgvptfsy kvqrvhaqs
//
LOCUS       WP_181729335             375 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium sanguinis].
ACCESSION   WP_181729335
VERSION     WP_181729335.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            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 sanguinis"
                     /db_xref="taxon:2594913"
     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=40062
     Region          7..368
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnhgpgltfr fltaqvvvvv isllvaatva tmvgptlfhd hmlmagredp slelfhaeqa
       61 yrdanlitla valptalisa llaslwlsrr lrtplqdltr aatsltagny rirvpageag
      121 pevttlahaf ntmadrleht eqvrrqmlsd lahemgtpls vltvyldglq dgavdwnnat
      181 htimadqltr ltrlmedidd vsraqehrie ldlaeeglgd llhtaaaaag eayadkgvdl
      241 qvetitdtar vlvdrqrfgq vmsnllsnal rhtpaggqvr isvhrqgast alihvaddge
      301 gippgqlghi ferfyrgdaa rsrdnggagi gltiskalve ahggtltats pgpgrgavfa
      361 lrlplsppds eeaar
//
LOCUS       WP_181729339             440 aa            linear   BCT 28-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Corynebacterium sanguinis].
ACCESSION   WP_181729339
VERSION     WP_181729339.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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 440)
  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 440)
  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..440
                     /organism="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     Protein         1..440
                     /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=48864
     Region          2..438
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mstptivwfr ddlrladnaa ltwaaergpv vglyvhetvg rgigraaaww lrhsldalre
       61 slpapliela gdpreivprl arelgatvtw nrryhltdid aevkeatgav shpgylltep
      121 wevratpyrv ftpffnaars vlldapptpl pvpdltpadv apatvdapae pawaaslaqh
      181 ntpgegaahk rlaefiaasa dydnnaldgv tsglsphlrf geispaevwl aavdagawaf
      241 arqllwrdfa whryyhladm etknvrekfg rfdwewtpna vpgttaaafa hqemdpdaqh
      301 ltelaawqsg rtgiplvdag mrelwatgrm hnrvrmvtgs wltknlgihw rhgeewfwdt
      361 lvdadaasna fnwqwvagsg ddaapyfrif npltqaekfd phgsyvsrwl petadypepm
      421 advkqsrlra laayddikng
//
LOCUS       WP_181729532             922 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sanguinis].
ACCESSION   WP_181729532
VERSION     WP_181729532.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
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="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     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=102050
     Region          8..920
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mstpspqthf defrahqgfe lddfqvkacq aveqdrgvlv captgsgkti vgefavslal
       61 srgtkcfytt pikalsnqky hdlvaehged avglltgdvs ingsaevvvm ttevlrnmiy
      121 aespqlalls hvvmdeihyl adrdrgavwe evilnlddsv sviglsatvs nseefgewlg
      181 tvrgdtaviv sehrpvplsq ymmvgrkvfp lfepgtdgrv nrdleyaier iesgraeegr
      241 rdfeegrgfr sraagrrsgr erpvdrtkpv grpevvsalq grdmlpaivf ifsragcdga
      301 lfqclrsrke lttpeeqeri aeivdkgikg ipdedlqvln yrqlrtawmr gfaahhagll
      361 pafkhiveel fvqglvrvvf atetlalgin mpartvvlek lvkfngeahv dltpgqytql
      421 tgragrrgid hignavvqwa pamdpkevag lastrtypli spftpgynma inmlkmngfd
      481 asirlveqsf aqfqtdrsvv gevreierlr akvgslreql erdiasfapp sddpaadlvd
      541 ylqlrrelte aekkaraaal tdrhtetvkl larlqvgevi alpgkkkpel aavvqaagkh
      601 ddprpwvtte rgwsgridas afrntpvvvg rvkiprhlad qprrharkvv sliqrgnfts
      661 prklkeqarv rpskrvtalr eairehpvha wpatdremla rvgeqlvreq rrlqkmqrav
      721 dsstdslgrt feriigllte mdyveivdge pqvteegerl asihsvadll vaqclkrgvw
      781 dsldpaelag vasmcvfenr ksifgspevp tepmavamna tmriynelvs deqrhqlpvs
      841 rmpdasfsls vhqwtagapl gyclaaaaes gaeltpgdfv rwcrqvidll eqvvktgynp
      901 eirhsankai dairrgvvai gs
//
LOCUS       WP_181729530             434 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Corynebacterium sanguinis].
ACCESSION   WP_181729530
VERSION     WP_181729530.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            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..434
                     /organism="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     Protein         1..434
                     /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=46832
     Region          186..316
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mltapdvpeh lvtvdahawp gllaiptgpa aglkarvaea kfagacaaag ieldpgrgae
       61 lrveydmlfr riaesgwvgl aegfmagewf atssevlvdv ltkllqsnyr pktptispkh
      121 ldgggeipae lvqhfagdgm sgfaghfatg vpttqrvrvk sqqsrsapay fvdvteysep
      181 idasrddlgd vqqrsvqmll dacatsrgth llefpssgga vslaaagrga vvdawaadeh
      241 aadalrdrvv yagvggavhv elmgpewtra tnrrsfydav vsverletlt paskaqylsa
      301 vghlvdpggr vavqtamrta aftpaadaal qslrayiwpg lsfstpdelt rivdrrtplr
      361 ivaqtrapah laaslrlqre mfdsrlreaa adgfdqvyrr lwqwqfalre alarlemldv
      421 vqvtlvprdr rgrr
//
LOCUS       WP_181729583             238 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein, partial [Corynebacterium
            sanguinis].
ACCESSION   WP_181729583
VERSION     WP_181729583.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 238)
  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 both ends.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     Protein         <1..>238
                     /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          82..234
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 pgetysyqig sdaggfsape sftiddgdds wkfvavsdaq igvnlkvaeq gamwrttagn
       61 aaaanpdasl fvslgdqveg wgdligrygq yneffsapql rnyrfaaieg nhetypsgas
      121 trhfkehwnl pnelgetsny ffeqnnalfi alnsnrkdda glaeqaqfvr dtvaahggdk
      181 dwiivlnhfa fhshggrytd ddivrmrnvl spvfsevgvd vvlnghdhmy nrsylmng
//
LOCUS       WP_181729616              65 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial
            [Corynebacterium sanguinis].
ACCESSION   WP_181729616
VERSION     WP_181729616.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     Protein         <1..65
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          14..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(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 trrstpqprd lrrdelkelr iakhltqvvv akhlgcapar isnietgkrp ltelasayek
       61 flksa
//
LOCUS       WP_181729791             333 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease
            [Corynebacterium].
ACCESSION   WP_181729791
VERSION     WP_181729791.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
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 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..333
                     /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=33562
     Region          1..332
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mrktsrliga tvlfaaiaaa ayiallgqga velspaqvlh vlrgggtsre iavvwdlrlp
       61 vavatllvga algmagewtq tmarnplasp dilgvtsgaa llvvlgtvty rpefsqalpd
      121 fwwravlalc gaagvvvllv alggvgtsdr ivltgfalsl mlhaavsyll lkaevlrave
      181 aqtwlagstg fvrmdgvial svgvlpfval glwcgrdlpl lahddtsata lgvnlkarra
      241 allvaatgis avvvsvvgpi gfvallaphl grivartpnp apvvsaaaga allavcavva
      301 glipaaapvg avssaiggva lvllvwrqsr str
//
LOCUS       WP_181729811             418 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Corynebacterium sanguinis].
ACCESSION   WP_181729811
VERSION     WP_181729811.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            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..418
                     /organism="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     Protein         1..418
                     /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=44028
     Region          1..416
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mspkavvvga gingltaaln laragwsvev leredtiggk crsaqlfpgt vsdlgaaafp
       61 fgaqtldadw vraprpvahp larntalida lgrdqkawda lhlpvardvd khlanilgpt
      121 mlrvpphpva marfgvrgal patalgnllf rteeakallv gnavhsmssp trpmtaafgv
      181 lfgalahang wpvarggaqt vaetlavqar dagvtirtgv evetlpqada vvlnmtarea
      241 qrfgarplhp gpgvfkvdwl lnnpvpwrdp rvgqaatvhv ggtaaeiaha ekqiarglmp
      301 nrpfvmvcqq yvadpsrgtt lwtyahvphg ytgdatghia rqikrfapgf rdcvedthvt
      361 gyiediagge mnvrqmvfrh phhvaggvfl asgstapgag vhgmaglwaa qavlkraq
//
LOCUS       WP_181729959             656 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Corynebacterium
            sanguinis].
ACCESSION   WP_181729959
VERSION     WP_181729959.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 656)
  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 656)
  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 656)
  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 656)
  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..656
                     /organism="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     Protein         1..656
                     /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=67154
     Region          32..631
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtsacgceps vpmadeeept pwwrdravll pvasgvslli glilewfvpg aglvatglfw
       61 lalllgasqf vpgalkglvt rvklgigllm tisalgavll gfieeaaala flysiaeale
      121 dkamdkarsg lrallalips tatiishgvt rsvaveelvp gdvlrlaage rlatdgiirs
      181 ghssldvsai tgesipvevg pgdavlagsi nttgalevea taggtdnslt tvvalveqaq
      241 hdkgqraria drlarplvpg vlilailvav igswlgdpgv wieralvvlv aaspcalais
      301 vpvtvvsaig aaskfgvvik sgaaferlgg irhlaldktg tltrnrptvv dvlttggatr
      361 advlgwaaal eahsthplaa aitaatpqap aaqqvdeaag qgitglidga qiavgsprwl
      421 spgplagqve dlekqgmtvv vihrdgqpvg aigvrdelrp evpevirtlt degfqvtmlt
      481 gdnsrtaaal areagitdvr aelrpedkat avaglgtrgp vamigdgind apalaradig
      541 iamgakgsda aiesadvaft gddlrlipra lrharrgrai inqnivlsla iiivllplai
      601 tgvlglaavv lvhevaeviv ianglraart khldlkpvea atvtadeday grsrvs
//
LOCUS       WP_181730144              85 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Corynebacterium
            sanguinis].
ACCESSION   WP_181730144
VERSION     WP_181730144.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
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="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     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=9505
     Region          2..85
                     /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 msymityvps aakairkldr starrlldai eslasdprpp gsiqlkggsg efrirvgdyr
       61 vvygihhdel vvlvlrvghr revyr
//
LOCUS       WP_181730214             188 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease, partial [Corynebacterium
            sanguinis].
ACCESSION   WP_181730214
VERSION     WP_181730214.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   ter Beek,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..188
                     /organism="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     Protein         <1..188
                     /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          <1..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 rllmggvavg yaltavtsll vfasdnaqga rsvmfwllgs lsmaafgpvl watiavvcac
       61 clafwvlgtr idaltlgdda artlgvhpdr trlifvvvcc lvvgavvsva gsigfvglvv
      121 phiarrlvgg lhrhvlpvaa algagltvaa dvasrtllap qeipigvlta lvgapllvvl
      181 varsgekq
//
LOCUS       WP_181729445             137 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GlcG/HbpS family heme-binding protein
            [Corynebacterium].
ACCESSION   WP_181729445
VERSION     WP_181729445.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 137)
  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 137)
  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..137
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..137
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=14025
     Region          7..137
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mtirlesvsl edaqrviaaa qakaeeigsp sniavvdaga nlvshirmdn awvgsvdisi
       61 nkaftarafd iatkdlaena qpgeqfygiq nsnpgrvmvf aggiplrrdg lvvgavgvsg
      121 gsgeqdqtva eaavaaf
//
LOCUS       WP_181730125             567 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Corynebacterium sanguinis].
ACCESSION   WP_181730125
VERSION     WP_181730125.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 567)
  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 567)
  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..567
                     /organism="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     Protein         1..567
                     /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=61625
     Region          36..542
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mssqsfprrs fivgsgvaaa svaaapyasa qlssdlssaa qgssiasgrv lpgapesvys
       61 hfmhgvasgd ptpvsvilwt rvtvspeatp gsgvgeaatv gwevatapdf atvvrsgsvt
      121 ttadvdhtvh vdpnglqpgt vyfyrfsyng vysavgrtkt apayeatvdq vnfalascan
      181 weagyfaayr dmaeraerde fdavvflgdy iyeyetggyv gksgtsrvht phnetitltd
      241 yrarhgrykq dlalqrahaa apwiviwddh etannswrdg aenhtagseg pwlerrnagq
      301 qayfewlpvr atrpsegghi yrnlqfgslv nltimdlrty rdeepsrfaa taegremlgs
      361 eqfdwlssvv rnsnttwnvm gnsvmiaplt lgamaetsse asmvnrlied fstlvagipm
      421 npdqwdgyaw arnrlfdela addanvlflt gdihtewvns ivhngqeigc elvtssisaa
      481 nvgdtvttyt kvyhpennpv sllaedflrk lnpavkhvdl dahgyavari rptevgmefy
      541 rvadyenses pvgvaatytw ragvgyv
//
LOCUS       WP_181729800             242 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphate signaling complex PhoU family protein [Corynebacterium
            sanguinis].
ACCESSION   WP_181729800
VERSION     WP_181729800.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sanguinis
  ORGANISM  Corynebacterium sanguinis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 242)
  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 242)
  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 242)
  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..242
                     /organism="Corynebacterium sanguinis"
                     /db_xref="taxon:2594913"
     Protein         1..242
                     /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=27504
     Region          7..210
                     /region_name="PhoU"
                     /note="Phosphate uptake regulator PhoU [Inorganic ion
                     transport and metabolism]; COG0704"
                     /db_xref="CDD:440468"
ORIGIN      
        1 mrtnyrehld afsrdliemc qnvrtlmdna tvalltqsld haedalsfsd gldvirqrce
       61 trgmqllale spvasdlrqv vssiyivedf ermgalathi arlarlrhph pvlpepmvvl
      121 veelarlahe lgsqtedlly apdadaavgl rnaddevdtm tsyilnvvtn rhwehstrea
      181 vdlallcryf erysdhcvnv aartvflvtg mkpeaylehr rsgdsfdmde rfavieqrfd
      241 rt
//
LOCUS       WP_181730465             284 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein, partial
            [Clostridium sporogenes].
ACCESSION   WP_181730465
VERSION     WP_181730465.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sporogenes
  ORGANISM  Clostridium sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 284)
  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..284
                     /organism="Clostridium sporogenes"
                     /db_xref="taxon:1509"
     Protein         1..>284
                     /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          1..>284
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdflnavkgi nnvlwnyvli fllcgtgvlf tvslkfvqvs kfkesfkkaf ggmslkgkka
       61 gkdgmssfqs latavaaqvg tgnlagaata ivsggpgaif wmwisaflgm atifgeavla
      121 qvfkekvnde vtggpayyis kglkskflas ffsvsiilal gfignmvqan sigaafskis
      181 nvpslvigii vailglivfi ggigriasvt ekmvpimalf yiigsiiilv snytnilpal
      241 klifvsafnp kaavggvagv tvkqairygv arglfsneag mgst
//
LOCUS       WP_181730509             284 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein, partial
            [Clostridium sporogenes].
ACCESSION   WP_181730509
VERSION     WP_181730509.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sporogenes
  ORGANISM  Clostridium sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 284)
  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..284
                     /organism="Clostridium sporogenes"
                     /db_xref="taxon:1509"
     Protein         1..>284
                     /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..>284
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mdllnavkgi ndvlwnyili fllcgtgiif tvslkfvqvs kfkesfkkaf ggislrgkka
       61 gkdgmssfqs latavaaqvg tgnlagaata ivsggpgaif wmwisaflgm atifgeavla
      121 qifkekvnge vtggpayyis kglkskflas ffsvtiilal gfignmvqan sigaafsnis
      181 nipswiigii vailglvvfi ggigriasvt ekmvpimalf yiigsiiila tnyinilpaf
      241 klifvsafnp kaavggvagv tvkqairygv arglfsneag mgst
//
LOCUS       WP_181730631             246 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Clostridium sporogenes].
ACCESSION   WP_181730631
VERSION     WP_181730631.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sporogenes
  ORGANISM  Clostridium sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (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   2  (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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Clostridium sporogenes"
                     /db_xref="taxon:1509"
     Protein         1..246
                     /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=28631
     Region          12..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 minyygslct tmyellhaha pedelqfylq yakkemkile plcgsgrflv pfvergfnit
       61 gfdmseemlk elykkapkak vfqssiekfs pkekydyifi tsgsfslfld ediafnvlvk
      121 mkealapkgk fvfaaettan iipdrekylk ncavktkegy diifksksfy dkhkkilstp
      181 slyelydgdn llgkeemdfr iklydsgeld klilkagfkr rhvfsdfnrr esidkntetf
      241 lyecyi
//
LOCUS       WP_181730728             316 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TolB family protein [Thermoactinomyces].
ACCESSION   WP_181730728
VERSION     WP_181730728.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 316)
  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 316)
  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..316
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..316
                     /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=34860
     Region          35..179
                     /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          64..101
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          105..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          116..281
                     /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          145..186
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mkkvskkvtg mmgalilsts lalpvyanqe qpgtilfsgg lhtqsiyqfn petlqtkrit
       61 sgnsvdvsps gdmityikhd svyvadssgk navrltrshf phfdssprfs pdgekivfar
      121 sdgnlytidl enkkvtqltk aedgvfhssp dwspdgkkiv fhstdkdgnt glyimnadgs
      181 qispltghhd pksseysphf spdgksvlfe ksqngqtdiy vmnlatkqar nitadldkaa
      241 sgavwsedgk qilftvnekn ekekdsssfy imnkdgsnkk mlqmqvkyat pskwkalnls
      301 eqeegflkkv knflld
//
LOCUS       WP_181730834             586 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Thermoactinomyces intermedius].
ACCESSION   WP_181730834
VERSION     WP_181730834.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 586)
  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 586)
  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 586)
  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 586)
  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..586
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..586
                     /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=65124
     Region          6..572
                     /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 mgsmfkkskr rslliglvwi vgfiivigrl fwlqavdhnk llaaaketwi kedalrpkrg
       61 tvydrtkqqq lawevdayyf vadtrqvkdp ektakylapv lkikedelvk llskdsdsve
      121 lryngkykyp ketlnqvesl kkdgliqgiy afptfmrqyn gtmaahvlgf lryddtavgg
      181 ieeyydpwlr gkegyikylk arngvmvtdq peknqppqhg kdlvltidsr iqhqveleld
      241 eaiktheakg gtaivadpkt geilamasrp tfdpnryaet lsdensinra vqsqfepgst
      301 fkivtlaaai eegifnpdqt ypsgsirvdd rvihdwngsg wgnitfrdgi klssnvafvi
      361 lgqklgaqkl tdyinrfgfg niteqygkkt gidlpaegrg yffgrnlyat elattsfgqg
      421 isvtpiqqva avsaianggv wktphimksi wepglkkevk sfqpesrriv kestakqvre
      481 llrgvvqngt gveadlpgyg vagktgtaqk pdpdggymen qyivsfvgfa pydkpevvvy
      541 vaidepsssq natggtvaap iareimkksl qirqvqpndk faetik
//
LOCUS       WP_181730854             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Thermoactinomyces
            intermedius].
ACCESSION   WP_181730854
VERSION     WP_181730854.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..190
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21173
     Region          52..190
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mnkrqaviva vlaaavagav fmtvdkpken pasamnravc qgepkpvqgf capnfklptl
       61 sgeevelyqn egkptvvnfw atwcppckee mpyfqklhet ygekinvimv netamerdes
      121 dvkpyldnhr ytfpvaldrg rngtvvgvdq yqlfnipatf iinengkitr hfmggvsekq
      181 lfsavqelmq
//
LOCUS       WP_181731002             569 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Thermoactinomyces
            intermedius].
ACCESSION   WP_181731002
VERSION     WP_181731002.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..569
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..569
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=66416
     Region          <351..>541
                     /region_name="CCDC158"
                     /note="Coiled-coil domain-containing protein 158;
                     pfam15921"
                     /db_xref="CDD:464943"
     Region          392..>457
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mlwenetwqr khtkeiaalr erdpsrftki kgefycfgcw kryiqehatp psrselpkvs
       61 hyhfkkskeh hfrlrpnqkh ipgcvfrdag ylrevaqrhg ltvlhdqvic lpdlekslrl
      121 dtparspesk paagktdrrs flfqelfdgm qddwvhqrvq adgkttdlgq ilyshesahq
      181 atgqsaiitg vvqnlslnrh hgveltlgpe gnfkvtvspg hlydrdflsp llgrkiaiyg
      241 kvtqteaqpp gmelismekq lvfldldekp fpafdlpkik dqrlhdtihq vlsryhaqpl
      301 apedfpfrfq tgliqqreeq reqleekydr lkqqaedlqq qqtdllqqqs eyeeqkekya
      361 qekstkeave nqlkkeirql sgffkrlfrs gklkqkqqel iavqtelqyl trqiyetrsk
      421 iqkladeqkk ihremetlka emekiqseme svksslgllr qhdelvrswq kvanhaehsy
      481 lfsshirgfh lclnisrdpd narfvhvqsc lqpyesegte krlmqpfakq eihlepdllk
      541 pygklfnqlk awiasqtenl egemattpv
//
LOCUS       WP_181731044             717 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Thermoactinomyces intermedius].
ACCESSION   WP_181731044
VERSION     WP_181731044.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 717)
  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 717)
  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 717)
  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 717)
  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 717)
  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..717
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..717
                     /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=82333
     Region          1..717
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mpidalidia esylskedvm clkaayefaa kaherqtrks gepyihhpve vaiilaelkm
       61 dlttliaall hdvvedtsvt leeveekfgp avgklvdglt klrkrmkfks nqehqaenhr
      121 kmfvamakdi rvilikladr lhnmrtlkym pekkqreksr etleiyapla hrlgiskikw
      181 eledtalryl npqqyyrivh lmkkkraere qyldeiistl serlegsdvp vldisgrpkh
      241 iysiyrkmvt qnkefneiyd lmavrvivnt vrdcytvlgi ihtiwkpmpg rfkdyiampk
      301 anmyqslhtt vigpkgepie vqirtmkmhr taeygiaahw aykegstien skfeeklkwf
      361 remmelqqet kdalefvesl kvdwfsdsvf vftpkgdvie lpqgsvpldf ayrihtdign
      421 mcigakvngk ivpldyqlht gdiveiltsk hsygpsqdwl kivkssnarn kirswfkkqr
      481 reesivkgre mveallkkhd fkvsevltne riqevtrkfn fqdpddlfaa vgyggittaq
      541 vvnrltdglk eeeqpvvlpd vktmrhrnhk adqgvrvkgv dnllirlsrc cnpvpgddia
      601 gyvtqgrgvt vhradcpnln nvpkerriev ewdsqtsqhy qvdievsgfd rqgllnevlq
      661 visdtqtsls avsakgdrrg iasihirvgi qninhlksvv ervkgvrdiy svrriiq
//
LOCUS       WP_181730988             191 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Thermoactinomyces
            intermedius].
ACCESSION   WP_181730988
VERSION     WP_181730988.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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..191
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..191
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21785
     Region          56..191
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mdkkkpllqi flllflavlt vyaiwsfrds psksrapqnm tveeyiasha lpkqsqapdf
       61 elpgiaqetv rfskdsgkpa iinfwatwce nckremplle kvyqtkrdqv qiimvhtthl
      121 drkeaaqqyi kqygytfpag ldtdgrvsdl yrvsalpqtf fidkngriih hqigeltqav
      181 ldqqlsrltg s
//
LOCUS       WP_181730462             235 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Clostridium sporogenes].
ACCESSION   WP_181730462
VERSION     WP_181730462.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sporogenes
  ORGANISM  Clostridium sporogenes
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 235)
  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 235)
  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 235)
  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 235)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 235)
  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 235)
  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 235)
  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..235
                     /organism="Clostridium sporogenes"
                     /db_xref="taxon:1509"
     Protein         1..235
                     /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=27901
     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 mlnvaicdde kyqreeivgi ivealrlrnk qykifqfdng edlissmndf diyfldikmn
       61 kltglevakk irlvneeaii ifitglkdyv fdafdvkafh yilkpidesk lkdvlysall
      121 qfdkkdkfii gktisqatki flkdimyies qhrklkihtk nniieyyhki sdiekelygc
      181 nffrchksyi vnlkyvesyd nvfitlinse kiyvskyrld dfskafmyyl knevq
//
LOCUS       WP_181731066             359 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD(P)H-dependent flavin oxidoreductase
            [Thermoactinomyces].
ACCESSION   WP_181731066
VERSION     WP_181731066.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
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="Thermoactinomyces"
                     /db_xref="taxon:2023"
     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=38454
     Region          12..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 mpwyqtrlte llqisspiiq agmaggitsp rlvaavsnag glgslgagym spedirqair
       61 eirkqtdrpf avnlmvpapy etnaeqerlm knhlkrfeea agasgqetts haaisfeeqi
      121 hvileekvpv acftfgipsp aviqemharh tvvigtatsv reaveveksg mdavvaqgse
      181 agghrgtfls aefpyvgtma lipqvvdhvr ipvvaaggim dgrgvlasla lgadgvqmgs
      241 aflptlessa hdkhkeaalq stdestvmtt vfsgkparai qnefiremkn yphplppypv
      301 qnaltkylrq aaskkgntdy malwagqaaa lsrcepaeel ikrimsqvnq clsqlageh
//
LOCUS       WP_181731144             161 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Thermoactinomyces].
ACCESSION   WP_181731144
VERSION     WP_181731144.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 161)
  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..161
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..161
                     /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=18180
     Region          17..155
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mkiawmdqap eqwlekfrff tpiqvrfsdt dqlghinnvs yfsyfeygri aylealdltk
       61 slldasrssa qgvivtasle cqylkqvhfg ekvslgvris rlgrssadfe yalvtgenkt
      121 lsaagrgavv yidpktgksr pipeevkdri rayeqmmepi e
//
LOCUS       WP_181731283             167 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Thermoactinomyces intermedius].
ACCESSION   WP_181731283
VERSION     WP_181731283.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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 167)
  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 167)
  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..167
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..167
                     /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=19399
     Region          80..161
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mefakaapsq tdkvfqvyke atkimnanni yqwsenypgr ediekdiqsg nlyvltsegd
       61 ivacvvldqh qepeyeqipw edssgrflvv hrlcvnpkyq gkgisrtlla eierfakkeg
      121 yasirldtqm inekamylye scgykkrgkf yfprhdepym afekrvt
//
LOCUS       WP_181731335             371 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Thermoactinomyces
            intermedius].
ACCESSION   WP_181731335
VERSION     WP_181731335.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     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=41447
     Region          3..366
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mkkiplldlt aqlqpireev lqavervids gqyimgpevk afekevaqyl gvkhaigvgn
       61 gtdalllald aagikagdev ittpftffat aetisqvgat pvfvdidpkt ynidvnqike
      121 kinektkaii pvhifgqpan meeimalaee hqlfvledaa qgmgseykgr kignwghaat
      181 fsffptknlg gygdggmvvt nddqlaekir ilrvhgsnpk yyhsmigyns rldalqaavl
      241 riklrhldaw ndgrrkkaal ynellkdtpv vtpyeaedrk hiyhlyiiqa edrdelmahl
      301 keqgiscgvy ypvplhqqev ykdlgyeegs lpvseymakr tfalplyael ededirlian
      361 tiksyyanks k
//
LOCUS       WP_181731339             472 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Thermoactinomyces intermedius].
ACCESSION   WP_181731339
VERSION     WP_181731339.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 472)
  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..472
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..472
                     /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=52763
     Region          169..450
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 msellfskqk rldrlfylmi vfaligptlg vpitsgfnlt ffriafllla agialrfaae
       61 kkletsymyp vrwygafflf wfaygvials wsaslsagvr ylfllgmmlp laysfpfflk
      121 ttdhfwkalr ilfwvyaaii lfavfesitl ihlpqsrafg risasvtsvf tnqndlatci
      181 tlglpflass lyildlkrkh kwfiyiigvl siytliatgs rsntffalpl aalplvvllp
      241 mvmdrskitm knvgkgiiav lvafilangl smvflsaear eqaktklsst fgflmdvqns
      301 pwtvdegged pidaetgrsa tvrkfliing lrflhqshym gvgpgnvevy mdgapkvdkv
      361 nmhnwwgevl vnfgviifil ymslyflmlw rlwklaslkh spqlnpvlrw gaystmaalt
      421 gyffggmaps taihytpmwi cygiglaiia igetlkkkhs gselekgslk gv
//
LOCUS       WP_181731397             161 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase [Thermoactinomyces].
ACCESSION   WP_181731397
VERSION     WP_181731397.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 161)
  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..161
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..161
                     /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=17906
     Region          45..159
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mrkterfkvs gpnslwqvyr tvpfwkvfkn tlvivmaryl pwmglkrrvy rkltgieige
       61 ctavafmvmm dilypdkihi gkntiigynt tiltheylid eyrlgdvyig dhvmiganst
      121 ilpgvtigdr avvgagsvvt kdvppgtfva gnparvikst n
//
LOCUS       WP_181731517             371 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Thermoactinomyces].
ACCESSION   WP_181731517
VERSION     WP_181731517.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..371
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..371
                     /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=42335
     Region          14..304
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mtsvksdihk vgrvhyldni rwvtvilvli yhvfylfntv gvpfpvadda gvrafdtfsy
       61 ivypwfmvil fliagisary alykrthref lkdkvnkllv pstlglfvfh wisgylnikw
      121 gggldsipvw mrypvfamag tgplwfiqml flfsvflvli rkmdkndkiw afcgkinivm
      181 ilslvfviwg aaqvlnppvi ttyrfgiyga ayligyfvfs hdevqnavek iripmllaav
      241 ilgvaftvry fgesfvstkc ltsfltncyl waailailgc gkawfnktsa fasymtrssf
      301 gfyvvhylvv qvvcfyvhhf splpkslnyf lalaielpgt fllyeglrri pvirylvlgm
      361 krkkvkqpap v
//
LOCUS       WP_181731531             335 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Thermoactinomyces
            intermedius].
ACCESSION   WP_181731531
VERSION     WP_181731531.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     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=35045
     Region          28..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 mlknkssfpf vlkltaglai lflsfviamv mgaadtslre vwlaitggek setitmirei
       61 rlprevaavf vgaalsvaga vmqgltrnpl adpgllglta ganaslafll afhssagyfv
      121 ltmacfvgaf agvclvfgis avkkggfspf kivlagaavt aflqgiaeai glyfkiskdv
      181 smwtagglig tsweqlkvii pfiaagilia lylsrqltil slneevavgl gqktrqikav
      241 lfmvvtilag aavaiagnma figlmvphiv ravvgtdyrf vlpmsavfga afmlladtlg
      301 rtihapfetp vsaivyilgl pffllivrkg grtvl
//
LOCUS       WP_181731562             341 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease
            [Thermoactinomyces].
ACCESSION   WP_181731562
VERSION     WP_181731562.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
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="Thermoactinomyces"
                     /db_xref="taxon:2023"
     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=36674
     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 mtigkmkwlw gggllialil svslgvflgs thvgfwtvwk vilqhtglmd gvnmdeadaa
       61 iiwelrlprv llvglvgacl atagviyqgl lknhladpyi lgvssgaavg aalaiitgwg
      121 nrsgwmlplf aflgaclall lvlqlgrgrg asqatslila gvviqaffsa vltlaistsp
      181 eemqriqfwl mgsfafrgwq higlmlpffl igffvcwrfs relnlmalge rsahhlgvhv
      241 ekmrifllii aslmtsaava vsgmigfvgl vvphimrmlt gadhrfllpl salfgasfli
      301 wadglsrmvl apqelpigvv tafvgapffa gilrrhqrsq g
//
LOCUS       WP_181731381             340 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: murein hydrolase activator EnvC family protein
            [Thermoactinomyces].
ACCESSION   WP_181731381
VERSION     WP_181731381.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 340)
  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 340)
  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..340
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..340
                     /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=38676
     Region          41..339
                     /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 mvrkwfvttm mlvqailfsl asplsvkans ehqknpawtg leearkqvma rerqvaalne
       61 eiaqkkmnlv ekqkklsmle arfeavlvhi ykrshknqyl yyllsadsvs eflmrldils
      121 mfvenesavi kqylkekksl enevamieks kkekeallke arqhltryta lyqqqsrtld
      181 pvrepepetm qpvrqedknr qvrnsrppan sspdrqenda lawpqpggkv ssefgerngn
      241 hegidiknsm gspivaaasg ivvltksdpd gygyyvvidh gnglktlyah mypstvqvev
      301 gdrvekgqqi asvgnypqlv pylhfeihen gkpvdplqyy
//
LOCUS       WP_181731349             626 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Thermoactinomyces intermedius].
ACCESSION   WP_181731349
VERSION     WP_181731349.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 626)
  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 626)
  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..626
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..626
                     /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=69949
     Region          <128..402
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mfillllavt lpmmstpgar sksqkwvvkw rqpvpssfwm eaelleegge glylvrtkpg
       61 tdderwvetw kedpgiesig pdiryelgde kkrsrfrvvf gknyylqqth vskawayfrk
      121 kadpdrikpv tvavvdtgvd lshpalkpfl tegvnvknpd lppqdhfghg tkvagviast
      181 wgaregkavg kgrimpvkvm endgdgeify tvkgireair rgadiivlsq gswtysklme
      241 daveeaerqg vlviaaagna efekgellfr qplyypaafp svlsvgatdf qgnheplsnt
      301 gygldivapg dmiytmsndg dyafdsgtsf stpqvagvaa liwqlrpdyt pgdirmllrq
      361 tassprwnek tgfglldadr alrspldpdm aepndseqta tpfflsqeir lvlqkgdpdw
      421 yvldlnkagr lqvdvevldg pgedvflsii qattgqtrsf slsawsgkqr iitpvsqgki
      481 llkwsvsqts krevalrfha aylpeedeye andllsqatl lplsenkkvf satisrpgda
      541 dwyqlsipke grlvvqvqpl tprfdpvifk irqddwenmr qdeeregrte tlsldvkpgp
      601 fyfrvtdyag nliedpyqli isfepv
//
LOCUS       WP_181731317             172 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NuoB/complex I 20 kDa subunit family protein
            [Thermoactinomyces].
ACCESSION   WP_181731317
VERSION     WP_181731317.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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 172)
  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 172)
  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 172)
  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..172
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..172
                     /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=18998
     Region          1..169
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 mgvnferfap veeqelkrnv vttnleqika warssslwpl tfglaccaie mmgtgaphyd
       61 ldrfgvifra sprqsdvmiv agtvtkkmap llrrlydqmp epkwviamgs cataggpyvk
      121 sysvvkgvdq ivpvdvyipg cppnpaaliy ginklqekir yeakygkkvt nr
//
LOCUS       WP_181731047             124 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: group I truncated hemoglobin [Thermoactinomyces].
ACCESSION   WP_181731047
VERSION     WP_181731047.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 124)
  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 124)
  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 124)
  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 124)
  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 124)
  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..124
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..124
                     /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=14051
     Region          11..122
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(13,18..19,22..23,26,57..58,61,90,93,97,100,111,114)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(27,36,39..40,43,47..48,51..52,55..57,59,67,69..72,
                     75..76,79,81,85..86,89,114,117,121)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(29,32..33,92,95,99..101)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mlrstkstly erlggeqait aviaeffnrm mqddrvnhhf igvnieelrq kqitnfmsya
       61 isgtplydka tlreahtgln itseeyeiai khlnsslrky nvglgdiaki eaflrsvkph
      121 iink
//
LOCUS       WP_181731774             239 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Thermoactinomyces intermedius].
ACCESSION   WP_181731774
VERSION     WP_181731774.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 239)
  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 239)
  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..239
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..239
                     /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=26586
     Region          <22..219
                     /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 mplneyglwm aagisglvay wipglaywig sgkcgepvhc sfrlkplsrv ffaifaagls
       61 wtvqwklgtg weswmatvlv wlllvialtd icfflipdvv tysgfflfms wrffvdaanm
      121 pvylaggffi tsglslvswi srglgwgdvk lvamaswvve wpqlllsiwf atlssmlhva
      181 grlrsrgraa vreplpfgph laagmflsll cgdvlrdwyg eqflqfflpc fgsivpmns
//
LOCUS       WP_181731804             578 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Thermoactinomyces intermedius].
ACCESSION   WP_181731804
VERSION     WP_181731804.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 578)
  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 578)
  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..578
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..578
                     /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=66710
     Region          28..488
                     /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 mgvsvvsake vsdleldqar reilemrlki trsqryrtia gifakhgllh lledrglfrl
       61 ffkkrtreee eklhrfgrrl rmvfeelgpt fiklgqvlvs rqeiipepvt telsellnev
      121 ppmpfrymaa vmedglpegl kefewidpep vgsaslaqvy raqlkdgrvc avkvvrpivd
      181 klfetdisii qkfagrlqkr lpppyaasvd lnglvrdyys sstneldmla eartmkehre
      241 mmkdfetisv pevykvsknv lvmeyvdgwn lkefpvdflt feerfmrmvd lahyyvktfs
      301 egyyhgdphg snimidkhtk kayvidwgmv grvdslhtea ifrmllhtrl nqaedaaeav
      361 ldiiqptpyt dpirlkdqlr shfvhyvnsd qagkynwgnl liqaivigvk nhcripnama
      421 lwakgftaae gtarwlcpei syhtvvesad vqilkswlsr rfnyranasw isevakltgt
      481 lprrlnkile rlawndwkvv venrtddhlv rqmnkmvnrm alawlasglf vgsavflafg
      541 newmqsvqsi kwlmqgmlwg asalsvyllw rvfrskra
//
LOCUS       WP_181731884             541 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Thermoactinomyces intermedius].
ACCESSION   WP_181731884
VERSION     WP_181731884.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 541)
  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 541)
  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..541
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..541
                     /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=60005
     Region          25..531
                     /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(190,193..198,200..201)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(193,311..312,333..338,418,430,433,444,524)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(193,236..237,284,286..287,290,311..312,333..338,418,
                     430,433,441..444,505)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(236,286..287,290,311,441..443,499,505)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 makvtvvggv shakgqpfay eklslpqmfd rtverhpdrt avyfydreis ykmlqdmskr
       61 vsgalracgv kkgdrvgiml pncppyvisf fgvlrrgavv vqinpmytrr eleailtdsg
      121 advlivsgdl yprvqninsf srlrkviive tdsfrlenpl shevswtafl hasapvpdep
      181 veperdvavf qytggttgrs kgamlthqnl vanvqqihah asenplteqd kiltviplfh
      241 vygmtcamnf gfflgsslil lprfeplevl etiqkhrpay fpgvptmyva lnaypgaeky
      301 gvdairiins gsaslpveli qsfekktgav myegyglsea sptthsnprs gqrkpgsvgi
      361 plpgteakiv dletgtrtvk igetgelvir gpqvmrgywn mpdetkqtlr ngwlytgdia
      421 rmdedgyfyi vdrkkdliia ggyniyprev eevlythpav leaavvgvpd pyrgetvkay
      481 lvfkpgakat iqelevfcrk hlapfkvpkq feirsslpkn avgkilrrvl rdeakkggdn
      541 p
//
LOCUS       WP_181731968             278 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TrmH family RNA methyltransferase
            [Thermoactinomyces].
ACCESSION   WP_181731968
VERSION     WP_181731968.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 278)
  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 278)
  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 278)
  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 278)
  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 278)
  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..278
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..278
                     /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=31044
     Region          7..264
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mkkteritss enrqwkqwkk lktkkgrkqq dalliegehl ieeavqaeqv fqavifseaa
       61 kekkadwlkk vpgnvpvfel psslfqqlae tttpqgimav ircprwslde vwkqnhsgkt
      121 fllldsiqdp gnlgtlirta katgmdgifl gkgtvdpfng kvvrasmgai fkvplwqedl
      181 scvipglker nvtvvntsph atrsyfhypl psrvaillgn egrgvdrrle eyvddhvtip
      241 mpggteslnv svtgallmye rirqgslrgn gefdynik
//
LOCUS       WP_181732039             367 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DUF1648 domain-containing protein
            [Thermoactinomyces].
ACCESSION   WP_181732039
VERSION     WP_181732039.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467976
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..367
                     /product="DUF1648 domain-containing protein"
                     /calculated_mol_wt=41937
     Region          1..365
                     /region_name="COG4194"
                     /note="Uncharacterized membrane protein, DUF1648 family
                     [Function unknown]"
                     /db_xref="CDD:443348"
ORIGIN      
        1 mstsvllmcl imipvlislc fipywtrrte sfgvsipekv yhlpelkkmr kqyawimagi
       61 glavlamfvp gsmicddees lglwfvfllv aylavnflay lifhrkmkal kkqadwgkek
      121 kqmvvvdtgf rqqkltyshl wflipfslal atliyfihvy eqipekipmq ydlngkvtry
      181 aeksyrtvlf ppvmqvyltl lflwiniiig kakqqigaen peksirqnvi frrrwslfti
      241 lsgtvlvsml slssfswihp vsaglvtavs lvitigilia alilsfttgq ggsrvktvsg
      301 kngdminrde dqywklgqfy fnkndpaifv ekrfgigwtn nwahplswif illvvglaft
      361 ipyflgn
//
LOCUS       WP_181732121             171 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: D-glycero-alpha-D-manno-heptose-1,7-bisphosphate
            7-phosphatase [Thermoactinomyces].
ACCESSION   WP_181732121
VERSION     WP_181732121.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 171)
  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 171)
  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 171)
  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 171)
  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..171
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..171
                     /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=19031
     Region          5..158
                     /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 mkgqnkavfl drdgvinevm tgrvdhvnrp qdfyllekvp eaiaklrglg ykifvvtnqg
       61 gvglgyiqek tlkkihekmq ndliaghpga iiddilycph kpfegcscrk pqagmilela
      121 kkhqvdlsrs wmvgdrqvdl eagkragcrs vlvsseytlw dfacsldske e
//
LOCUS       WP_181731594             135 aa            linear   BCT 28-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein
            [Thermoactinomyces intermedius].
ACCESSION   WP_181731594
VERSION     WP_181731594.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 135)
  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 135)
  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..135
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..135
                     /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=15854
     Region          4..127
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mrgkytmvkh fwiscahsip gagkcerihg hnykvtfcve gfeldekhml idfrqvkhai
       61 ekkydhhyln dfpefdpdqt gvapstekva evffriiegl crqksnqprc kwveveetne
      121 ayarfervde qeems
//
LOCUS       WP_181732133             256 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: arylamine N-acetyltransferase family protein
            [Thermoactinomyces].
ACCESSION   WP_181732133
VERSION     WP_181732133.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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 256)
  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 256)
  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..256
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..256
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28971
     Region          4..251
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mipqylarig vqppvpvhls gltglmqkhq qhihfenldi lsgrsiqldp kslfqkiivk
       61 krggvcfeln glfhwllnel gfdvqmvagt vyessrgewg legthltnlv clnrekylvd
      121 vgfggnaprr pvplsgevvq diagryrirs npdhyvlekk epgteswqvl yrfagdaktf
      181 qdfheacrli etsprspfnr siyiskmtpd grvsligrkl vqvtpsgkek revsenelpa
      241 lireifqirw espeaq
//
LOCUS       WP_181731636             251 aa            linear   BCT 28-DEC-2024
DEFINITION  segregation and condensation protein A [Thermoactinomyces
            intermedius].
ACCESSION   WP_181731636
VERSION     WP_181731636.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     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=29450
     Region          1..248
                     /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 meevkikldm fegpldlllh lietsevdiy evpiaqiteq ymqvlneake rkldvasefl
       61 vmaatllaik srmllpkqev leedfmmeed ewfedprtel verlleykky krlgevlrqr
      121 eeerskiysr pamdltaytp evnpvegltp ddllqafvea lknrethepe akltreeisv
      181 sdrmneidel ltekgqllfs klidwktatk ervittflal lelmklkriv cyqehmfgdi
      241 rverlqaevq p
//
LOCUS       WP_181732428             264 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Thermoactinomyces intermedius].
ACCESSION   WP_181732428
VERSION     WP_181732428.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..264
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29850
     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..127,132,155,159..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 mkgfvvgsyl pgnsfvhrld praklgfvfv fmlyvfflka vlpstlfllf tlaavraari
       61 pyklffsalk pvlwiillss flhlwmnkgg dvvfsfsfit vyeegirqag miairlsllv
      121 aiaslltftt spmdltdgie kilspfkkfg vpahelalmm sialrfiptl weetekirka
      181 qmargvdfea gnlltrlkky fpiliplfvs sfrraedlal amearcyrga egrtkwrrlq
      241 ltprdgwlva vlillggivw mfgr
//
LOCUS       WP_181732615             775 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FtsK/SpoIIIE family DNA translocase
            [Thermoactinomyces].
ACCESSION   WP_181732615
VERSION     WP_181732615.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..775
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..775
                     /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=86219
     Region          21..179
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <301..765
                     /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 makkrnkkkq sigtkkeilf eiygivllal slvtiasyga igrnltylar fvvgtwdfli
       61 pvlgmglsvy vmahhkwpdh wssrwtgvvl vfmalitfnh yltfhtiqtd kgiidqtwym
      121 lleernsavp ldvgsgmlga fsyallhflf ddtgtlivla avvccgflli adfsftkaal
      181 iskavykkak qrgkdflidw irqydrrqkr tskqkrvrek nvpdvevske pidpvvydfe
      241 dvayqdreqp engkkpvheq mklklqpsep qpqpkqpepd egsgepievh fqsqqkmdhy
      301 vlppatllnp tkkrqgreqe nvhekaqtlq dklesfgvka tvgeihrgpa vtryeirpek
      361 gvkvsrivnl addialalaa kdirieapip gksavgieip nskvalvglr dvlesaeylg
      421 sqsklsialg rdvygkpivd nlakmphllv agatgsgksv cingiivsll ykarpdevkl
      481 mmidpkmvel nayngiphll ipvvteprka avalkkvvae mekryelfak hgardierfn
      541 qlvkekglee taplpyivvi vdeladlmmv apadvedsic rlaqmaraag ihliiatqrp
      601 svdvitgvik sniptriafa vssqadsrti ldmggaekll grgdmlylpt gaskpiriqg
      661 aflsdeever vvkfvkeqqe pdyqeemipk spdknkssvd delfpqakkl vieaqtasvs
      721 llqrrlrigy traarlidml eakgivgpye gskprevlvs sldnetgerk keavk
//
LOCUS       WP_181732198             178 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
            [Thermoactinomyces].
ACCESSION   WP_181732198
VERSION     WP_181732198.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 178)
  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 178)
  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 178)
  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 178)
  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..178
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..178
                     /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=20427
     Region          16..174
                     /region_name="Adi1"
                     /note="Acireductone dioxygenase (methionine salvage),
                     cupin superfamily [Amino acid transport and metabolism];
                     COG1791"
                     /db_xref="CDD:441396"
ORIGIN      
        1 maqiyirnsg krleseevrs fleeqgvlye qwpteklpeh lrekfvlnee eqeeilkayq
       61 eeiqslakrn gyvqwdvval seatenldel lkkfenvhth sedevraivs gngiftikgk
      121 egtgyfdvel spgdvisvpe ntphfftlme nrkvvavrlf idpsgwvahp yqdpefta
//
LOCUS       WP_181732653             290 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Thermoactinomyces
            intermedius].
ACCESSION   WP_181732653
VERSION     WP_181732653.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..290
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..290
                     /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=32072
     Region          2..290
                     /region_name="LCB5"
                     /note="Phosphatidylglycerol kinase, diacylglycerol kinase
                     family [Lipid transport and metabolism, General function
                     prediction only]; COG1597"
                     /db_xref="CDD:441205"
ORIGIN      
        1 milfvvnpes gkgkgkvfwe kaeaylkars vayevwhtkq nekltsqird eakqkkwqav
       61 vaiggdgtvn evgsgligga vpfgiipsgt gndfafahgi psrpekalar ilnfqpelvd
      121 tatvngqpmf gstgvgfdvs vvdrvnrsgl kkwfgsfsyg meamkclfsy karsmtlkmd
      181 gkeyrlekcw mvsvanirqy gggiricpqa dtqdgyldvc cvqnlskgqf irafpltyfg
      241 whtrhpairf eraqqieipg pesfpyhidg evkgttpvri kvqprsllll
//
LOCUS       WP_181732690             358 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Thermoactinomyces
            intermedius].
ACCESSION   WP_181732690
VERSION     WP_181732690.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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..358
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..358
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=40154
     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          160..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 mkrlllgmer ellvadlddg esagttsrlk gmqptciaqd pfrperlycg tfgrglwcsd
       61 dfgdswypvg dgcdyfeplk ekgilyekit avavsphqke ngygmvyvgt epsalfssed
      121 ggktwrehke mkfvpshrtw sfpprphthh vrwitpdpeq seriyvsief gavlrsldgg
      181 ktwedkkfqg pldahtllmh pgqpdrlyaa cgdglfregc gymesrdggq swiplgqdlk
      241 hpylygmavd akkpdwvlvs asihpnhghh armeqassti yrkegdrwle avdglpgpeg
      301 mlisalandp sesgvfyaln nlglfrsvdv gktwekinlg wkeeyrsqhp htllvvdc
//
LOCUS       WP_181732648             119 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HesB/IscA family protein [Thermoactinomyces].
ACCESSION   WP_181732648
VERSION     WP_181732648.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
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="Thermoactinomyces"
                     /db_xref="taxon:2023"
     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=13007
     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 miklteqaal kvkdmlseqe hpenlylrvg veyggcsgfs ysmgfdeekk endleldqfg
       61 vrilidqrsq pllkgtvidy ketvmgggfs idnpnatvtc gcgssfrtat esgrpdenc
//
LOCUS       WP_181732707             151 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Thermoactinomyces intermedius].
ACCESSION   WP_181732707
VERSION     WP_181732707.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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 10140382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     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=17477
     Region          10..144
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 matrrftapv tihlffirdh qilllrrfnt gyedgnysvv aghldggetv kqaavreake
       61 eagvhlteen ieivsvmhrk agderidffa tvkewegeik nqephkcddl rffpldqlpv
      121 ntipyilrai enykkgkwfd sfgwterkrs i
//
LOCUS       WP_181732763              95 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: antibiotic biosynthesis monooxygenase family protein
            [Thermoactinomyces].
ACCESSION   WP_181732763
VERSION     WP_181732763.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
REFERENCE   1  (residues 1 to 95)
  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..95
                     /organism="Thermoactinomyces"
                     /db_xref="taxon:2023"
     Protein         1..95
                     /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=10916
     Region          1..95
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mylvnnhiki qseehlkhlk egfsrapesm kqvpgfvsfr lllsedeshv vaetvfaske
       61 dfinwiqseh ferahggrkg dverqelsay hiivk
//
LOCUS       WP_181732825             299 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Thermoactinomyces
            intermedius].
ACCESSION   WP_181732825
VERSION     WP_181732825.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 299)
  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 299)
  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..299
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..299
                     /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=34459
     Region          33..289
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mefslplsyp ysfklttkrl qffeksiyrc qhgrfqrtih gkhgplllsv scdeeevalk
       61 veitgkvgeq eeeglrkkva rmfstevdlq pfyeqmeqvp elapvilark glhfvldpdl
      121 hecliktiig qqlnvsfaav lirrlielag deaefqgerw avfptpeqia rlryedlqai
      181 qfnrrkaeyi idlsrriagg kldlealdqc sdeevfarll pirgigrwta ecvmlfglgr
      241 pdllpaqdig lrnavkqfys meerpdestv rqlgrswspy asyvtfylwd alrdlknek
//
LOCUS       WP_181732868             268 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase
            [Thermoactinomyces].
ACCESSION   WP_181732868
VERSION     WP_181732868.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces
  ORGANISM  Thermoactinomyces
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae.
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="Thermoactinomyces"
                     /db_xref="taxon:2023"
     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=29803
     Region          1..249
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msnpvvlvtg atsgigeaia rklpdqgyvp vllgrrasrl keihrelnrg syypcditne
       61 aevkpvveei iqtygrvdvl innagygcfg gfldvspedy rgmmetnylg avrmvrhvlp
      121 hmlraghgri iniaslaglt gipnlagyca skfaligfse alnleyapvi rvgvlcpgpv
      181 mtpffrgenp rrhfppliag qmlkaeevar yalkmikhpk tvvipkklkw alqlrkwfps
      241 lyfwatrriy rqldpnphks pshsvsei
//
LOCUS       WP_181732913              77 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Thermoactinomyces intermedius].
ACCESSION   WP_181732913
VERSION     WP_181732913.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 77)
  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 77)
  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 77)
  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 77)
  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..77
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..77
                     /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=8722
     Region          2..59
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 midaiyvfpe sqgqgigtml laqalknlke wtvdveagnk tgirfykare fqaveeykep
       61 ffgydlktir mttdili
//
LOCUS       WP_181733063             117 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Thermoactinomyces intermedius].
ACCESSION   WP_181733063
VERSION     WP_181733063.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 117)
  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 117)
  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..117
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         1..117
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13834
     Region          21..>93
                     /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          31..63
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnsslklhee galeeeieri ldqhlikypd dveawvrlsv lvfespigdf eksinclrka
       61 vevkpdylea llilmrmqny iyreieedly kllhkkskrk sqitffkrnv kekkkpg
//
LOCUS       WP_181732796             120 aa            linear   BCT 28-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Thermoactinomyces intermedius].
ACCESSION   WP_181732796
VERSION     WP_181732796.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     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=12811
     Region          1..114
                     /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 mrmiiavgig gavgtllrfg vaqafndpvf pfgtlmanwt gclglawlne qrkisfspvw
       61 qkglgpgllg ayttfstlcv eahllpplls lfyivatttg gllfarlgvw laqrgkadwk
//
LOCUS       WP_181734513             186 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein, partial [Klebsiella pneumoniae].
ACCESSION   WP_181734513
VERSION     WP_181734513.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 186)
  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 186)
  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..186
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         <1..186
                     /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          <55..178
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 ghwlnarrep nleviakifn ilkmpgfvvn adgtisdsra dhnvsfnsin eskgsypvis
       61 wvsagdwmea vepyhrraid rwydttvecs edsfwldvrg dsmtspagls ipegmailvd
      121 pqveaingkl vvakldgdne atfkklvida gqrflkplnp qypiipingn criigvvvda
      181 kitnlp
//
LOCUS       WP_181736433             104 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Marinobacterium marinum].
ACCESSION   WP_181736433
VERSION     WP_181736433.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
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="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     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=10922
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mswvylvlag lfevgfaval kesdglsklw psvtfivlgg csfflltram asiplgtaya
       61 iwtgigalgt vlvgifwfgd sanglrlmfl amllcslvgl klvs
//
LOCUS       WP_181736628             639 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Marinobacterium marinum].
ACCESSION   WP_181736628
VERSION     WP_181736628.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..639
                     /product="PhoX family protein"
                     /calculated_mol_wt=69922
     Region          19..633
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mnqhphidpe dhpelehtdf drltakgvsr rsfllgsaga mglflaanpl tqavaavtrp
       61 msspllgfka vpastadtfv vpegyvakpl iawgdpilkg apafdesgtq nanaqagqfg
      121 dntdgmsffp ltedrallav nneytnyeyl fahqgkqaln adevqksqaa hgvsifeirr
      181 naqgewqvas asdhnrrita ytpmeltgpa aghslmrtah dpegkyplgt fnncangqtp
      241 wgtyltceen fhkyfaaped apdvelpard kryglksgnr dfqwyrhder fdlskhpnep
      301 hrfgwvveid pmdptstpkk rtalgrfkhe naaltidpsg hvvvylgdde rgehlykfvs
      361 kglynaddqk anrdlledgt lyvarfsakd getkglgewi elthgknglt aengfadqae
      421 vlifareaat rveattmdrp ewvavhpnnk avfctltnnk nrgqdgqpvg gpnpraknny
      481 gqivrwwphe gshvdnrfsw dlfavagnpt takglyagsd ninaenmfns pdglgfddag
      541 rlwiqtdgky snageyagmg nnqmlcadpe sgeirrfatg pvaceitgla fspdqrtvfi
      601 gvqhpgedla pshfpaggts kprstimmvq rkdggiigs
//
LOCUS       WP_181736754             459 aa            linear   BCT 28-DEC-2024
DEFINITION  class II fumarate hydratase [Marinobacterium marinum].
ACCESSION   WP_181736754
VERSION     WP_181736754.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 459)
  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..459
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..459
                     /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=48771
     Region          1..456
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 mpntrieqds lgelevpena lygaqtqrai nnfpisgqam peafirslll ikkaaaqana
       61 nlgcltqsva naisdacdsl ldsntlqlhf pvdvyqtgsg tssnmnanev iatlasralg
      121 dhvnpndhvn fgqssndvip taihvsavlq leealfpaln hliealetka levghhcktg
      181 rthlmdampv tlkqvldgwr dqleqdlerl rhaktqlgql plggtavgtg inthpdfada
      241 fslqlnsltg qgftrasnff srigaqdnav alsgqlrtta vsimkiandl rwmnsgplag
      301 lgeitlealq pgssimpgkv npvipeaaam vsakvigndt titlggqsgn felnvmlpvi
      361 adslldsikl lanvstllad raiatftina eqlekplain pilvtalnpv igytkaaeia
      421 kaayreqrpi idvasehtdl preelkalld pakltrggf
//
LOCUS       WP_181736923             449 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Marinobacterium
            marinum].
ACCESSION   WP_181736923
VERSION     WP_181736923.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 449)
  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..449
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..449
                     /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=46925
     Region          1..448
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 metiesaira ingvvwgpmm lvlilgvglf lslglklvpi lkigtgfkll wggrtaasgd
       61 eekgeippfq almtamsatv gtgniagvat aiflggpgal fwmwitalig matkyseavl
      121 avryretdek gqhvggpmyy iknglgknwa wmgvvfaifg acagfgignt vqsnsvadvl
      181 hanfsiptwv sgvimatlvg avliggikri gqvagalvpf maisyliagl vvlainahll
      241 pqafelifth afspvaaqgg fagaavwaai rfgvargvfs neaglgsapi ahaaaqthnp
      301 vrqglvamlg tfldtlvict itglvivssg vwtggesgaa ltsqafatal psfgnylvav
      361 alaifaftti igwsfygerc ieflfgikav lpyrilwiia iplgatlsld fvwlvadtln
      421 ammaipnlva lallspvvfq ltrdyfskh
//
LOCUS       WP_181737020             457 aa            linear   BCT 28-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Marinobacterium marinum].
ACCESSION   WP_181737020
VERSION     WP_181737020.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
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="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     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=51170
     Region          1..456
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mqlvwlrndl rlvdnpalsa acatgepvmv vvcltpaqwa ahnesaarin ywqarlewle
       61 rqlsaggiev rrlmleyfad cppailqqak alranavhfn yeyplneqqr draacqllaa
      121 egivarghhg dliippgrvm tgqgtpfkvf tpfsrawmrv llqvlhdplp apvgasvepq
      181 agsalpwplv geqatpypva dsqlsaqlyr fvherepdyr rwrdfparha tsglsaalti
      241 galsarqcla alkqaasade wqqstwlnel iwrefyrhll vafpdlsrla pfrpeveari
      301 gwlnndaafa awkvgetgfp ivdaamkqll atgwmhnrlr mivasfltkl lrvdwrhgea
      361 yfmsklidgd fasnlggwqw sasvgadaap yfrifnprlq sekfdpdgey latwlpelrq
      421 lspqarhepg agqaygrpap iidyrqarqa alddyng
//
LOCUS       WP_181737245             296 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Marinobacterium
            marinum].
ACCESSION   WP_181737245
VERSION     WP_181737245.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 296)
  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 296)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 296)
  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..296
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..296
                     /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=34577
     Region          12..254
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          176..254
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msqsgtltll wldlrsfdrs atfyelfdkr feierldlhn pvydrqhltp taicvdfdyp
       61 dmhglmlvrd lheryhlpii mmteqhsesl mvwalrariw dillkpmqas aaeyqvnely
      121 qrleqasqtp drlddvspml rlpeesrfhg ssteartvhp alsymqlhlg erineeqlaq
      181 lcnlrplqfs rqfkkafgvg fqellqqlri qeatrllenp dlpildvala vgyrdhsyfc
      241 rvfkkylgvt pktfqeqrqw qseqeqqqfi avklqavagl nqpttppstr airrsc
//
LOCUS       WP_181737404             190 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Thermoactinomyces
            mirandus].
ACCESSION   WP_181737404
VERSION     WP_181737404.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..190
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21488
     Region          47..189
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrkrqiaivg vllaavigai fmtvrgardn paasmgrvec qgetkpaegy capnfklptl
       61 sreelelyrn hgkptvvnfw atwcppckye mpyfqklyeq ynneinvimv nqtameskee
      121 dvgsylkknr ftfpvvldrl qdgsvvgidq yrlfsipatf ivdengkivh qfmgtiseeq
      181 lfsavkevlh
//
LOCUS       WP_181737301             103 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Marinobacterium marinum].
ACCESSION   WP_181737301
VERSION     WP_181737301.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
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="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     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=11528
     Region          1..96
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mfvvanrimv nsgyeeafae rfrqragqve qqpgfvrlev mrpanegcpw vvmthwrdkg
       61 afeawvssed fkrahreqsl pkeafgaggg lemhevelca gda
//
LOCUS       WP_181737462             603 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Marinobacterium marinum].
ACCESSION   WP_181737462
VERSION     WP_181737462.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 603)
  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 603)
  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..603
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..603
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=67825
     Region          72..315
                     /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 mpplidllqp sklhwltvpr yaviavplll atgssasgqg tvalplllia tlgcvrlvwl
       61 krlphewarl dkakhalnaa qpdraigill kplalagthy qvkravllar aychqgdfik
      121 ahevlsahdt ryllpdeqls lqiawaqlfi eadnpaearr rladisdqec qanlnclllk
      181 aelalqdehy pqartllesg ldhckepadr vllhnnmarl eglqghrdaq lrhlqsarve
      241 fskapraglt divhhnlaia lvrkgqpeda kavlreafaa gdtsglahvi avlnnhlhta
      301 reagyadwvr niyaefdrql erlkprtsre qlalditqlr mmrndgisct idnypelieh
      361 lldrlatttp avpiservag lvelrhdlkr eietelqqtn kvpvqlinlm qqsaqqllkh
      421 tatietylsn lspkligplt lwhryrtdad karielaegs tnlqaafnal fdhlrekaew
      481 laeqgtaqqt ieawliicde lvayhdqwpp aaqpswraqy sdlaqhaldq atalmaglkh
      541 hrqqvdqlig layfnlrlre dkvaaarwmr vvkmyepsld hyaswlrghy gfvcgeldga
      601 fyv
//
LOCUS       WP_181737512             134 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Marinobacterium marinum].
ACCESSION   WP_181737512
VERSION     WP_181737512.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
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="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     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=15547
     Region          2..130
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 myqytltpaf ydtdglghin ntrvpqwfea arndlfrift pdldmkkwql imarievdyl
       61 gelfygrdve vrtfvskign ssftvlqeaw qdeklaargk afmvrydfan gramslsdeq
      121 rgmleihfka detv
//
LOCUS       WP_181737551             130 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Thermoactinomyces mirandus].
ACCESSION   WP_181737551
VERSION     WP_181737551.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 130)
  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 130)
  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..130
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..130
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=15344
     Region          41..130
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mpfqhgkdki ltfqrplnpd rqqkpqsspk pvrplhpavr rrrmiwlviv vvficwaviq
       61 sfiqqlrvwe qekelaakqe qlaqlqlkqk elkqevqklk sedymlelah kmgygkpgee
      121 iyslekkese
//
LOCUS       WP_181737606             107 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Marinobacterium marinum].
ACCESSION   WP_181737606
VERSION     WP_181737606.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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..107
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..107
                     /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=11416
     Region          32..97
                     /region_name="Cytochrome_CBB3"
                     /note="Cytochrome C oxidase, cbb3-type, subunit III;
                     pfam13442"
                     /db_xref="CDD:463879"
ORIGIN      
        1 mkalkrqfmr pvmlgaalil gsgqalaadd sqwesgeqiy akvcghchea gvgptikgrs
       61 lppsyitaiv rhgframpaf rasfiddqal qsvaeyists papqnee
//
LOCUS       WP_181737661             600 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein
            [Thermoactinomyces mirandus].
ACCESSION   WP_181737661
VERSION     WP_181737661.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 600)
  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 600)
  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 600)
  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 600)
  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..600
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..600
                     /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=67295
     Region          2..597
                     /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 mkykwrsvav nivivllfgg ilarlymiqv sstrsfqivd eqvdliamaq tsqkkevviq
       61 sgrgsildrn gkpfvggsdw hllvfpqsek qwrlradqfr kiseiinvpy wefrqqllhl
      121 kspvilsgln geeitlsple rktiealrvp gvmvvqsdqr mtlnqlaeqv igqvarspll
      181 lkkwyfdkik nkewhsesli gisgleqafe pflhgeeeql liytatrggk plngvqmtrk
      241 ntvraeedpp rilvttldke iqqkvekilr eeeveegavv vqeirsgdil amgsmpkgts
      301 akrelnpwkn ravmeatpgs ifktvvavaa leqglvnedt vfhcdgkldh yhlsdakpgg
      361 hgkitfaeay akscnvvmgt vaktlgpekl etyarrfgln qkviwdgkvf hdssfvqlpe
      421 eqtglifakk tdkkdggvlv qtgigqrdvr mtpvqaanmv tslfhqgktp eprlveeiqd
      481 vqgrtvfrfp rqviegakpl rsntirsmkk fmqkvvesgt atqarqakwk lagktgtaqi
      541 gqkgdsynkw migfgpvnqp rysiavvlnr vsdaddprai kifekvmnel avlektkkek
//
LOCUS       WP_181737719             453 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Marinobacterium
            marinum].
ACCESSION   WP_181737719
VERSION     WP_181737719.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 453)
  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 453)
  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 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   4  (residues 1 to 453)
  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..453
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..453
                     /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=50889
     Region          9..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 msepipspvi lvddehhirm aagqtlelag hevttlerae palelidadw pgvlvtdinl
       61 pgldglelmr rvraidadlp vilitghgdi smavsairdg aydfiekpfa sellldvvrr
      121 aldkrtltle nrhlrealev qnapgpriig ntpsmlalrq lgrtvadmpa dvliqaetgc
      181 gkdllarflh eqgkrrehnf vaincgavpe nlieselfgh eagaftdakt rrigkfehan
      241 ggtlfldeie smplplqvql lrvleersie rlgsnnvipl dlrivaatki dlkqaaaegr
      301 fredlyyrln vvrmdipplr erredisllf qhfaliassr ygreipqlsa armhslmvhd
      361 wpgnvrelrn laeryvllge nctfdfenrp italegsltl peqveqfekm liqielerhg
      421 gsikdtlhsl glprktlydk mkkhdldknd ykp
//
LOCUS       WP_181737744             218 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Thermoactinomyces
            mirandus].
ACCESSION   WP_181737744
VERSION     WP_181737744.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 218)
  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..218
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..218
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24753
     Region          <20..>194
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mlvgwrrrap sctllrlppv daepetgnid vedlkkkitk rtkaivvthi wgypcemdei
       61 mevaknhglk viedcshahg atykgqlvgt fgdvscfslq gnkivsageg gilltnsqei
      121 yerstllghf rdrsqqcvcs nfykqfaktg yglkyrmhvl aaalarvslw klderiktrt
      181 enlnyfskll skiphrttny qklryqrsil wvqafvse
//
LOCUS       WP_181737848             456 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Marinobacterium
            marinum].
ACCESSION   WP_181737848
VERSION     WP_181737848.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 456)
  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 456)
  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 456)
  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..456
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..456
                     /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=50121
     Region          6..>126
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(6..7,10..11,13,37,40..41,44..45,47..48,74,77..78,
                     81..82,85)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          6..30
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          35..65
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          73..101
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          140..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          251..456
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mslpslneal almnqgafta acaicrqhla qrpddfnarh llgliqfkng nqlaatkelt
       61 kasrlnpapa fkaqafnnla lvlqargkqe qavnacrtai qlqpreqafh lnllgaleql
      121 erwpeicdhm yahpvlarqi earlchavae rhlqhyqaal dllttlpdtl eveseralnl
      181 cltenaqtvi erwtskdsdp qtlirmadyi aeegfavaat piyqaaalaa pdnsgvrhml
      241 dairgdctaa apadyvrtly dthadqfesr lqqqlgynap velcrqlari mpanrpvsaa
      301 dlgcgtglcg relrsqlpir hlqgcdlspr mlqlaadkhv ydalscspll dylptltatq
      361 litatdvliy tgdlqpilaa lpgalapqgl faftveqheg pdeislhasg ryrhslqhie
      421 rlaaqydfti kllnpfplrf engvsikglm vilqka
//
LOCUS       WP_181737974             240 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Thermoactinomyces mirandus].
ACCESSION   WP_181737974
VERSION     WP_181737974.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 240)
  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 240)
  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..240
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..240
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27696
     Region          33..>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"
     Region          41..71
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          76..100
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          144..174
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          179..207
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvgpmidvdl icegkkghrf aagsyrrnrs riekmlqddp hvedylmlav leakkgywnr
       61 aqtavekame lepdnhdall llaqileikg elreagityq tlfhkhpdft kgsreyaryl
      121 ithtdaiala qnilfhnlel dskdaishtl laeiyltrgk tgqallhlel aahyyqahpl
      181 yhqqkakvfm emnkyeeaar qlklalrmdp knkvirsqfd kalkaskvpk iflfwkkwvi
//
LOCUS       WP_181737854             472 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Marinobacterium marinum].
ACCESSION   WP_181737854
VERSION     WP_181737854.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 472)
  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 472)
  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 472)
  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 472)
  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 472)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 472)
  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..472
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..472
                     /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=53269
     Region          14..440
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
     Region          233..468
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mirfkwhths lkqlvllaff laaiplaili fqsgnalvdq sdrarmlare mlqssqqtee
       61 lrtlaeditr sarqyeivkr selrdrlthq lqnyrtllqq lqlptrltds aaklktlldn
      121 iqlqsdqdta prfepadlda litatqslih atdqafnsrl seleqqvkae qqrtvwqasa
      181 lilastilil ffsarinrpv qhlikhiral gegertpspy lsgplelvqv neqlnwladr
      241 lsgleedkar flrhishelk tplttlrega dilseelagp ltqnqqeivh llqqnsitlq
      301 elieqlldyn rlqqphrlqk etvalpslle riitpfklqi eqkqlqlkle lnnidgwitd
      361 shmlqriltn lisnavhysn qggvicitts qtgsvlelev antgpqipda dlpqlfepfy
      421 qgknrrrgpl kgsgiglsia aqassalnak llvsrnsdgw vafslflpsl eh
//
LOCUS       WP_181738014             359 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Marinobacterium marinum].
ACCESSION   WP_181738014
VERSION     WP_181738014.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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..359
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..359
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39222
     Region          80..218
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
     Site            84..91
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(85..92,157,201)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            217
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mnelikplae drfqdeieil kawdaengha rpyawqlspq avvlfitggv agdtpisaky
       61 fgadrsvqva vatlttdral llygppgtgk stlsellaaa icgnsqlivq gtagiseekv
      121 lyewdyayrl skgtdtgalv ktpiframee gklarveelt ripsdvqdal itilsekmmp
      181 ipelntsvma srgfsiiata ndkdkgvndl skalsrrfnt vrlelpddeq teikivehqv
      241 gklckaedlp lpvnlpeeiq rvvrifrelr egqsgsetie kpsatlspae aisvisqais
      301 msayfggdda iqadhiasgl egvvvreaed rlvfrnyadr ilknraadrd ldealrqil
//
LOCUS       WP_181738165             140 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Thermoactinomyces
            mirandus].
ACCESSION   WP_181738165
VERSION     WP_181738165.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..140
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15603
     Region          1..139
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkatefslpd lsgkihqlgn yrgqivwlef wvswcaacqv slsnrnvlyc slntrevafl
       61 tinvtgrean pdrvrdfikr agfqfpvlcd rgtetydayn issvpadvli tpqgeihgiy
      121 detvpltsii qevgfllsks
//
LOCUS       WP_181738254             144 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Thermoactinomyces mirandus].
ACCESSION   WP_181738254
VERSION     WP_181738254.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=16989
     Region          1..121
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mmenlaetkl rvryqetdqm gvvyhanylv wfevgrtemm rergfsykdl earglllpvv
       61 dihckyeypa ryddpvivrt kigefnrski ifsyevihqe tgrrlakges ihlwvnqemk
      121 rvnlkhsfpe lymqlsrlta kgge
//
LOCUS       WP_181738459             398 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Thermoactinomyces mirandus].
ACCESSION   WP_181738459
VERSION     WP_181738459.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 398)
  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 398)
  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 398)
  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..398
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..398
                     /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=43805
     Region          17..396
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mhtlprvpen eirnriarfq ttlqeleadg alitqnvdly yltgtmqngi lfvpqtgepc
       61 fyvkksvtra eyetilpvqp lgrmrelggi ietrfgsvkk laiemdvlpy glatrylgmf
      121 pqaeaidisf plrlqraiks eyelqqikka avyvneivas lpgylqkgkt elelsanieh
      181 vlrlkgnigi yrmrgynqel clgmvasgsa aatptyfdgp agglgvqlas pqgaspkplk
      241 tgepilidia ttvegylidq trmavigdld pemerayeva vsiiremeqm gkpgvewqal
      301 ylrslemaek aglsnhfmgy gpdqakflgh gvglemdelp ilakgfrqpl qegmvlaiep
      361 kftfpgrgva gientylvtk dglqpltiap eeivripe
//
LOCUS       WP_181738302             140 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Marinobacterium marinum].
ACCESSION   WP_181738302
VERSION     WP_181738302.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     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=15153
     Region          1..140
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mkfqrqrree ininltplid vvfllliffm itttftresh lsislpeaat navnaaseid
       61 aidvvigaeg qysvnelplv tsdaltlrra viklagekrd lpfvitadan akhqsvvtvm
      121 dvagqlgfsr lsiatqkagd
//
LOCUS       WP_181738461              72 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Thermoactinomyces
            mirandus].
ACCESSION   WP_181738461
VERSION     WP_181738461.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 72)
  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 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   3  (residues 1 to 72)
  AUTHORS   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..72
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..72
                     /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=8177
     Region          1..72
                     /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 msnrkgnsll tnrerevfel lvqdkttkei aqqlfisekt vrnhisnvmq klnvkgrsqa
       61 vvelvrlgel ki
//
LOCUS       WP_181738220             153 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein [Marinobacterium marinum].
ACCESSION   WP_181738220
VERSION     WP_181738220.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 153)
  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..153
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..153
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16545
     Region          3..150
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mrllvlrhae avsgadldpc reltpqgrvq aqmmasrles llgdfrllss pwvrarstaa
       61 eltaseneis saleliptas vaavavrlep lfatdrplvl lthqplcgrl ihwltegqdq
      121 plsvapcsga lleldwpaag marlvrwldp htp
//
LOCUS       WP_181738625             447 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Thermoactinomyces
            mirandus].
ACCESSION   WP_181738625
VERSION     WP_181738625.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 447)
  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..447
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..447
                     /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=46757
     Region          1..437
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mesftgilde vsnfvwgppl lillvgtgiy lsfrlsflqf sqlplalkta fsrrqdkqst
       61 gdishfqslm talaatigtg niagvatavv aggpgaifwm wvtaifgmat kyaeailavk
      121 yrvagkrgem aggpmyyier glgwkwlavl falfgsiaaf gigsmvqsns vaasiessfa
      181 inpwitgivl tgitgiviig giksigraag ylvpfmsily vaggliiill nieklpsaig
      241 liftdaftgq aiaggaigtv irygvargvf sneagmgsap iaaaaaitdh pgrqalvsmt
      301 gtfldtiivc sitgitllmg gfymdgdltg aalttqtfns llpgpggwiv tfglilfays
      361 tvlgwsyyge kcfeylfgsq aipgyrivft lsvfigsgld ltavwsiadi fnglmavpnl
      421 igliglsgvv vaeskafani iqnekrd
//
LOCUS       WP_181738636             317 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Thermoactinomyces
            mirandus].
ACCESSION   WP_181738636
VERSION     WP_181738636.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=36387
     Region          31..287
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 msqtaakktq rasktaefaa lfraleyafp kerrlfedpf aihflsydlq llaclaripi
       61 lgklilqlvd rtepgarasg vartrliddh lthalskgiq qvvilgsgyd crafripecr
      121 qirvfevdqs gilnlklarl nkllpglprn vifvrtdlni dkleqtlirs gydknlpaff
      181 iwegvtqylt eqavqhtlqf igetapgsfl lftyvhkqai dswltgqkkr lirqfvnqig
      241 epwifglfpe elsailsshg leliedvdsm afrkrymnph gphinryrfy raalacvkrk
      301 stepqirffr sffrete
//
LOCUS       WP_181738806             789 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Marinobacterium marinum].
ACCESSION   WP_181738806
VERSION     WP_181738806.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 789)
  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 789)
  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 789)
  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 789)
  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..789
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..789
                     /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=86787
     Region          19..783
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 msridqwlla pirsgerlie hmlfdyrrlm alvfacltla lgwqavqirp dasfvkmips
       61 shpyvanyle hrddlaglgn sirvvvaake gdilqasfqq qlqaitdelf flpgvdrsal
      121 ksiwtpnvrw tevteegfag gpvipedydg spaaleqlri nilrsgqlgr lvandfrsal
      181 ievplferip etgeklnyqq lsaqletlvr eryqsdqiai hvtgfakivg dliegagyva
      241 iffgiaflvt lvllylyshs lagtlipllc sltaviwqlg llrwlgygld pysmlvpflv
      301 faigvshgvq ivnnvrieaa agadkmtaar kafrtifiag ftallsdglg fvtlmvidiq
      361 viqdlavaaa lgvlvivatn llllpllisw agigqkaihk erhgressav vwralvrfsr
      421 prgaliaigi avmlawygwt vsrdlqigdl sagapelrad srynrdnafv tshysnssdv
      481 fvvmvktpee scsrfdslql vdrfqyfmnd vagvqsslsl vdvaervtag lnegnlkwrs
      541 vsrnqyvins slryapsglm nascsllpvi lfledhkavt lqrvaqavdh faerhnrddi
      601 rflmgagnag feaatnevia daqyemllwv ygvvsllcll tfrsvrtvac iilplaltsl
      661 lcqalmarlg igvkvatlpv ialgvgigvd ygiyiqsrln tylqqgmalp eaywetlrtt
      721 gksvaftglt laigvvlwvf spirfqadmg illtfmflln mlgalillpa lscvlnyrrq
      781 prevaqtvl
//
LOCUS       WP_181738686             578 aa            linear   BCT 28-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Marinobacterium marinum].
ACCESSION   WP_181738686
VERSION     WP_181738686.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 578)
  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 578)
  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 578)
  AUTHORS   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 578)
  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..578
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..578
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=65163
     Region          25..577
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mtrmplpsik nsidrvihai egrytqglsp asltlayldw lthtshspgk inemlentlr
       61 kcsaftlwaa rasldsdapp fisplpgdrr faddawkrfp ynvmaqsfll qeqwwhyatt
      121 gipgvakhhe nvvsfaarqw ldmfsptnyp mtnplvveka vqtggqslan glqnllddiq
      181 hslldeadpd slpyaagknl amtpgkvvfr nrlieliqys pttdkvaaep ilitpawimk
      241 yyildlsehn smvrylvdkg htvfmiswhn pdardrdmgm gdylrrgvmd alrvinavvp
      301 erkvhlvgyc lggtlatiaa aamardnddr lqsltlftaq tdfteagelm lfidesqlsy
      361 medimwdkgy ldtqqmagaf tllrsydllw srlvseyllg esprmndlma wnadstrmpy
      421 kmhseylrrl flnndlasgr frvgdrpisl rdirvpvfcv atqkdhvapw rsvyklhdlm
      481 ntevtfalts gghnagivse pghprrsyql gvqtakdkhi paddwlvrhd skegswwepw
      541 vewlakhsst qvtppatgnt dagypaigpa pgtyvfer
//
LOCUS       WP_181738903             499 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Thermoactinomyces mirandus].
ACCESSION   WP_181738903
VERSION     WP_181738903.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=54365
     Region          10..485
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mlrekvkllq ekydlvingq evpgtsheyf avfnpatgek isevakatke dvdkaveaar
       61 ealanskwar wpaarrgqil nkiakimrsr fqdlveleil ntgkalsaaq gqvmqaiedm
      121 elyagattti qghtkpvpng ffhysvkepv gvcaqivpwn yplmmtawki apalaagcti
      181 ilkpasltpl talaladich eagvpagvin vvtgsgaeig sylvghpgvd kvaftgettt
      241 gkdimakase tlkrvtlelg gkspnivfpd adlegavngs vfgiyyntgq scearsrlfv
      301 heeiydefve kfvektkklk lgdpfsketh vgavisrgqw etidgyvkla ekegarviyg
      361 gkrpdgeefs kgywymptvi vdvtndmrva qeeifgpvvv imkfreeiev irmandtiyg
      421 laaavwtqnh glahritsql kagivmvnnp istfpglpfg gykqsgfgre lalesldlym
      481 etksvlsyvg pkplnifgi
//
LOCUS       WP_181738931             189 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Thermoactinomyces
            mirandus].
ACCESSION   WP_181738931
VERSION     WP_181738931.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..189
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21019
     Region          51..187
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mnwrnlligi liviavggaf wtansgkgds pnqttssrte qasvqrdesp qekmkapdft
       61 lqtldgktvq lsknggkpsl infwaswcpp ckvempyiqk ayekygnqvn fmmvnltamd
      121 dkakmeqflk egsydfpvll detgkvgemy qafsipttyi vdengiiinh imgamsesql
      181 teimekise
//
LOCUS       WP_181738963             268 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Thermoactinomyces
            mirandus].
ACCESSION   WP_181738963
VERSION     WP_181738963.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=29746
     Region          1..249
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 msepivlitg assgigeaia rklavagyfp iltarnlarl hqlqqelnkg avlscditre
       61 edvkklidqi iqkfgridil insagygrfg daldisledy qgmmetnflg tvrmihhvlp
      121 hmlengggri inissmaglt gipnlagyca tkfaligfse slrleyspai qvgvlcpgpv
      181 rtpffgeedp nhhfpsliar qmldaedval etlkmiqrpr iviipkklkw alklrhwfps
      241 lflaltkqly srlniknrks tfqhisks
//
LOCUS       WP_181738980             470 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Thermoactinomyces
            mirandus].
ACCESSION   WP_181738980
VERSION     WP_181738980.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 470)
  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 470)
  AUTHORS   Rosinski,J.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..470
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..470
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=53851
     Region          1..83
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          242..>424
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          289..317
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(290,293..294,297..298,300,330,333..334,337..338,
                     340..341,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          328..358
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          369..397
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mefdrieigk fikktrkakr lrqqdladen isqvvisyie tgkpeiseek iryllnklki
       61 resdykefyv ednkeaskel eeemklrlia letiidltap eqgleelrsi glpngsplda
      121 diyylkgkyy lykrnlkran kyffqairlv ddkypemigs nlkaasyfgl akleyanndl
      181 nkaleyckkg essfiidggr sylqagflvs kviflqklnr ledaqsaldk lnslnsgkpc
      241 fiesreiiln ayelqatiwa kgnmtnnaii hakkgielar idkaydrsce lwttlgsiys
      301 nknklhlaei cfltalklkn kiqreyllsy antqlgnlyt kkkkfskaek mfqkaisisk
      361 ktndayqete almglgecyi hqnnsahaik clkhalelak qsgftkqknq lllklghylk
      421 tignpgfqey vfdffesnve alfnrkgges ampyyfsqtk rhsagdppdl
//
LOCUS       WP_181739006             319 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Marinobacterium
            marinum].
ACCESSION   WP_181739006
VERSION     WP_181739006.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
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="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     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=35903
     Region          <119..312
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          233..312
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mkqnalrlgl dipkdvsdmg egwrrlqlpi dlghcysdhl elesglslvr vnyqpkchli
       61 eetacphker vlvitlgltg esdfhqtnqn slafkaghtt ittfsntpge rvyqantpvs
      121 qlrlivnepw lqrylgaerc eqvlgnghly llsnhsstsn trthalalsr hiqtdmhhsp
      181 nklnthihal silceqldgi apenlksqas lnvhelerie rarqlmsehl etpltlasls
      241 qqvslsqhkl kqgfkqlydt tpsqmltelr mqkaytlltt ghqvaqaawm vgyrypnnfs
      301 vaftryfgrs pksvmghng
//
LOCUS       WP_181737728             124 aa            linear   BCT 28-DEC-2024
DEFINITION  group I truncated hemoglobin [Thermoactinomyces mirandus].
ACCESSION   WP_181737728
VERSION     WP_181737728.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 124)
  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 124)
  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 124)
  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 124)
  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 124)
  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..124
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..124
                     /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=13993
     Region          11..122
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(13,18..19,22..23,26,57..58,61,90,93,97,100,111,114)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(27,36,39..40,43,47..48,51..52,55..57,59,67,69..72,
                     75..76,79,81,85..86,89,114,117,121)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(29,32..33,92,95,99..101)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mlrstkstly erlggeqaia avitefynrm mqddrvnhhf vgvniealrr sqityfmsya
       61 lggspqyegs tlrqahagln itseeyeiai khlnsalrkf hvglseiaki eaflrsvkph
      121 iinr
//
LOCUS       WP_181739267             325 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase [Thermoactinomyces mirandus].
ACCESSION   WP_181739267
VERSION     WP_181739267.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=35764
     Region          5..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 mnqfeqfhlf lenadpilvv ahlypdgdai sstlamgyvl rqlgkkvtmv nespipqkfs
       61 flpgveeikl adsvseifpy aialdcadae rmgscrslir ekaivvnidh hatndrygti
      121 niiqpqaaat aeiifdwvee adfpvdrqla aciytglltd tggfrysnts skvftqaakl
      181 letgieshki adavletvtm eqlqllqtal stlqksedgl vawmdlrkqd idrfanshed
      241 ldgivnyarn iygvdvgilf hetndrtikv sfrsremvdv gnlaksfggg gharaagcsi
      301 sgtlqeahhr vlslvqsklk qecev
//
LOCUS       WP_181739279             417 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Thermoactinomyces mirandus].
ACCESSION   WP_181739279
VERSION     WP_181739279.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 417)
  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..417
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..417
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46606
     Region          1..408
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mivkytlnng vrivaekiph vrsvalgiwv gtgsenetpa nngishfieh mmfkgtknrt
       61 arevaeafda igghvnafts keitcyyfkv ldehfatald vladmffesi faeneiekek
      121 kvvleeiymv edtpddlvhd llsevsigdh algypvlgna etvqsfkred lfqyknqfyv
      181 psnvviavag nlpdgyleli deafshhqgk tppvnkevpv ftprlkvrkk dteqthiclg
      241 lpglpvghdd lytlvllnnv lggnmssrlf qeireergla ysvysyhssh rdtglfavya
      301 gtkhgqedev fsciyqvfdd ilngglsene lqkakeqlkg simlglestn nrmsrlgrde
      361 lllnrnftld eiieqiesit ledvnrlaqk tfsspmslal ispdgkipas frrnsia
//
LOCUS       WP_181739479             279 aa            linear   BCT 28-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Thermoactinomyces
            mirandus].
ACCESSION   WP_181739479
VERSION     WP_181739479.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 279)
  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 279)
  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 279)
  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..279
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..279
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=31625
     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 mrklsvflim amlivvsacs qekaeknesf vlvkggtftn tksnyygksv tisdfyisky
       61 evtqkewiev mgknpsqfkg dnlpvemvsw ydaveycnkr sikeglqpyy kidknkidpn
      121 nkseydnikw tvtinagang yrlpteaewe yaasggqmsk sytysgsnna devawywrna
      181 gdkyltgnwn wsiiennrnk tkpvgvkkpn elglydmsgn vrewcwnwyg dldsnsgsfr
      241 ivkgggwigd isnneisfrg kfeasgigpd qgfrvirge
//
LOCUS       WP_181739568             242 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Thermoactinomyces mirandus].
ACCESSION   WP_181739568
VERSION     WP_181739568.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..242
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27437
     Region          <3..239
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mfkrtikrea lksvcldetk eiliflpgee qslqknypll vlhdgndyfn lgrivtqavq
       61 middgqldpf vmvaipvdke krsseyspag nrqplhmqmv mdellpfire kypvsskked
      121 lviggsslgg tvslhialky pdqvnnvlsq sgaffkatse eimrqhslsh lqiyqsigts
      181 etavpthmgk ldllarnrei yrnlkkkkaq vhyieadgdh twgfwqrdlp nalnyffgna
      241 lk
//
LOCUS       WP_181739657             773 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Marinobacterium marinum].
ACCESSION   WP_181739657
VERSION     WP_181739657.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 773)
  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 773)
  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 773)
  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 773)
  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..773
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..773
                     /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=85050
     Region          91..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 mspplerdpv smtppqwgva lfallvlgav wlfmayqlkd nreqvearqt atlanlsfiv
       61 aenlgqlldr artlrmlvcd vreghisggd agiaalilsd pvftrlslyd argalnysss
      121 agapeqldaa wrvapdqdta dirvlpsaaw qqqdslplll pdqsggessf llleldlgyf
      181 lklyqkldfg aqasiqllsa sgqtlaqvda gglvveggdl dnslitnsrl qsgrfinrge
      241 aggatlvgyf qrlesfpfav virqlesdll ahhqaqrsry iltvlllsgv vlagvawllr
      301 tmhgrdahlw alerseqrnl allerlqkeh rqtleaasrd altglynrrl fmelayshll
      361 gakrqgrfaa vlfidldrfk aindslghkv gdlllqavag rlnsclresd ivsrfggdef
      421 vvmltgvkrr ddiaprvqql vdilaapyae legsglstsp sigialspqd gmdietlvkh
      481 admamytakr ggrgryalfd tapsardlnt vglaeqlpsa itrqleihlq prlllpdyrl
      541 agfealvrwe hpdfgllppa qllplaeaqg lmaevtcqvi rkvceqwqlw rqegttvvpv
      601 avnlglsqlq dadlpqriig llddygveya wleldvnead lkqlqpeqld qlralrqlgi
      661 glniddfgsc glspeqlrrl pfnriklaqs firdiynsyd dnvllsatis laqrlglkvt
      721 akcletpdql vylklagcde vqghllsral sasevrtyrr qtepvsgvsg gml
//
LOCUS       WP_181738573             685 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Thermoactinomyces
            mirandus].
ACCESSION   WP_181738573
VERSION     WP_181738573.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 685)
  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 685)
  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 685)
  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 685)
  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..685
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..685
                     /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=75604
     Region          1..676
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mkniaagiik hkktvaitfi ilavictlaw favsvnydik dylpddapst kampvmeqef
       61 egnvptnrvm ikdvtiqeal afkeklaaid gvsdvtwldd aidiktplem addeivesyy
      121 kdgnalfsfs irdrdevavt daiynligee namsgeslnt atqqkmtgre siyatvllip
      181 iiililvlst nswieplffl taigisvlin mgsniflgei sfvtqsvapi lqlavsldya
      241 ifllhsfady rkkiadplqa melamkksfp aiaasasttf fgfialsfmn feigsdlgmn
      301 lvkgillsfi svmvflpalt lmfykwidkt qhkpllpsik nigshiikfg ipslllvfil
      361 vvpaflaqsh tnftygigeq pettragsdl akirehfges tpivllvpkg niakeeklvh
      421 dlekiehvts vlayvntvsa aippeyldps vtdqfyseny sriilqtdtk negeeafhli
      481 eqvqrtaeny ygkdvhllge svtlydiknt vqkdnklvnl ltiitiaivl lmtfksvsip
      541 lilllaiqsa vwinlsvpyf tgtslvyvgy llvsiiqlaa tvdyailltd aykeyrkkmp
      601 aleaikktad kkifaiavsa silssvgfil gitssnpiva siglllgrgt llafimvvff
      661 lpamllvfdk liakttwkan fykek
//
LOCUS       WP_181739778             153 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Thermoactinomyces mirandus].
ACCESSION   WP_181739778
VERSION     WP_181739778.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 153)
  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 153)
  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 153)
  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..153
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..153
                     /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=17608
     Region          10..144
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 mskdrftapv tihlffired qilllrrynt gyedgnysvv aghldggetv kqaavreake
       61 etgvslredd vkivgvmhrk tgderidffa avknwegeiq nrephkcndl rffsldnlpa
      121 nmipyivrai hnyrkgrwfd sfgwesvtvd str
//
LOCUS       WP_181740105             476 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Thermoactinomyces
            mirandus].
ACCESSION   WP_181740105
VERSION     WP_181740105.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=54095
     Region          1..475
                     /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 mkralvvdde vevssffkyf leskncdvvv ansgrevekl lfqqvpafhl alidlkmpda
       61 dgldllakik akypvcevfi mtgystvksa vsaiqlgard ylekpfddld hlekmidsvl
      121 vntflkeekl nktakkygii fspespmqkl laladklark ainilieget gtgkeliarf
      181 ihgsslrsey pfvgincgai peslleself ghekgafsga vknrkgffel adngtlflde
      241 igeasasiqv kllrvletge fmrigseeir ksnvrfisat nrnlerevnn nrfrsdllyr
      301 legvklfips lrerpedipl iaqhyldkky gghcrldpdt ahilktyhwp gnvrqlhnil
      361 nqthaihdck rltpdhlpky llkesqypvr etsfemrtae fiekeaqqfv qriisglgtv
      421 enldlkkvlk rirkmegeig rkiiekglse tkgnrkllse klnitsrtlr yilnek
//
LOCUS       WP_181740042             220 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Marinobacterium marinum].
ACCESSION   WP_181740042
VERSION     WP_181740042.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 220)
  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 220)
  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 220)
  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 220)
  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 220)
  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 220)
  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..220
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..220
                     /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=23225
     Region          14..116
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          116..217
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mlkrywrltl asallvsgav qaqgvaangq qivmqgdgsg apclachgmd gagnnlasfp
       61 rlagldaeyi akqirdynsg krvsvvmqpn vdnlteqqil dvaayyasqp vpkveaatad
      121 aevmalgeki akrgdwnnyi paceschgpd nqgmgvsfpg iagqhanyik qqlnawrsge
      181 rhndpnqlmt gvaerlseqq leavaaylga qqavaaeggq
//
LOCUS       WP_181740358             426 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Thermoactinomyces mirandus].
ACCESSION   WP_181740358
VERSION     WP_181740358.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..426
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..426
                     /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=46706
     Region          13..425
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 msvstvthve teslnpyeiv qsqidqagkr lgireevlni lkkpkrvlyv sfpvkmdngs
       61 irmfegfrsq hndavgptkg girfhpnvtm devkalsmwm sfkcavahvp fgggkggvic
      121 nphelskgel qrisrgfmea iadivgpekd ipapdvytna qtmgwmmdty srlkghfspg
      181 vitgkplslg gskgrneata rgcvyvieqa mktlekpleg atvaiqgfgn agrivadlls
      241 ekrckivavs dtsgaiyqkd glnldqvkrl kdgqtssivd npdaqrienp eelleldvdi
      301 lipaalenvi thknadrvka kivaeaangp ttpkadeilf nngilllpdi lanaggvtvs
      361 yfewvqnlmn yywseeevns klqkimvhsf sevyslakeq qtnlriaaym vaikritdam
      421 eargwi
//
LOCUS       WP_181740480             422 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidase U32 family protein [Thermoactinomyces mirandus].
ACCESSION   WP_181740480
VERSION     WP_181740480.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..422
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..422
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=47854
     Region          8..317
                     /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          328..407
                     /region_name="Peptidase_U32_C"
                     /note="Peptidase family U32 C-terminal domain; pfam16325"
                     /db_xref="CDD:465094"
ORIGIN      
        1 maertklkkp ellapagnle klkfavlyga davyiggqky glrskagnfs yedmkegvaf
       61 ahqhgakvfv aaniiahned fdgmtdyfqt lyqigidavi iadpavvdic reaapnleih
      121 istqssitnw qtvqfwadeg iprvvlarev sldevqkikq htdieietfi hgamcmsysg
      181 rcvlsnymts rdanrggcaq scrwkydlfe dldgeenalf eegdqsftms skdlcmiehi
      241 pelinagvds lkiegrmksi hyiatvvnsy rrvidayced pegfqfkpew keeilkaanr
      301 plttgfyfnn psekdqifgl ppkmaaydfa glvldydpet qtalieqrnh fkigqevefi
      361 gpkrekflqq ideirdekgn pldaarhpmq kvkvkvdlpv qpydlmriek eqeiikkkhf
      421 lt
//
LOCUS       WP_181740507             404 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Marinobacterium marinum].
ACCESSION   WP_181740507
VERSION     WP_181740507.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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..404
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..404
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=45950
     Region          64..347
                     /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          214..245
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          250..278
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkrmirwlpl wlllstaaga esltlppgvl vqlnaaqkam aeenypqadk vlkalsgkel
       61 sapakayvlq frgnlalvrq qektalkhfs aayaldalpa vdqrrvlhtv aqlqlsqeqw
      121 ragvnsmsaw igqvrakgtk aervraedyl mlaqgysqle qwaqviapvk tairmkgrap
      181 edwyklqlaa hfelkqwkga tavlellvnr ypqrasyweq lasvyqirdr hadalstlra
      241 awlagkfkqe rqyiwlsqlf lqqglpqraa ellqesmaak kvrrtlkher llaqtqlqak
      301 mydagrgtle riaqrkpdys twrqlayldm qlrhwdamkr sidqavafkp daaelyllgg
      361 iadinrshye qarssfvkas rhdatraqaq nwlnyldqvr gsss
//
LOCUS       WP_181740656             346 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Thermoactinomyces mirandus].
ACCESSION   WP_181740656
VERSION     WP_181740656.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=36597
     Region          6..345
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mkryfplrig rfslmmdtka vfvislliiv sfavlvgslt igetptsfld vikglfgmge
       61 nsfvimtlrf prvliallsg aalamagail qavirnplas pdiigvtgga sagavlvitf
      121 fgdissnlsv slfwvplaaf lgagsiglli yllswkkgvs pfrlvlmgig fytatqaltn
      181 liilmgpvfq asqakmwitg tvygsnwdqv avlwpwlsil ipvallfarh lnvgqlgedv
      241 ikglggnssr qrifflllst glagsafafa ggisfvglia phaarrlvga syeallpvsg
      301 llgaifvmva dllgrtlmap leipagvfta vigapyfiyl lirnrn
//
LOCUS       WP_181740798             401 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Thermoactinomyces mirandus].
ACCESSION   WP_181740798
VERSION     WP_181740798.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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..401
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..401
                     /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=45309
     Region          171..397
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mmiaavlvif mmvgqifvkl iaddykqnmi ehdyavagyl drngvdsfqi trafihekil
       61 adrkagqell qvaayhvgtq nnlipevdrf hqkyallfvm lsglfsiail gglwlfavrq
      121 nkrlqkvnmd issfmdghiy mrledvgegs lsklfasvnk matsltshii kekrskeflk
      181 dtisdishql ktplaalqmy neimqdektg nevvddfilk serelkrien liqnllklar
      241 ldagaielek nthilkkfle evigrfstca elegkmitld cddrlvlafd eewlleavsn
      301 iiknaldhtn sgdridlqce atpvtteiti kdtgtgihpe dihhifkrfy rsryskdkhg
      361 igigltlska ivekhgglii vesklgegta fhlffpklsn l
//
LOCUS       WP_181740725             176 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein [Marinobacterium marinum].
ACCESSION   WP_181740725
VERSION     WP_181740725.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 176)
  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..176
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..176
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19818
     Region          4..160
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mktltlirha ksswddpfld dfdrplnprg rhdlplmcar mlahgpapdq lihstalrth
       61 ltasalidtf rltdravcgt driyeadvsv leallrqqsn ehqhlmlvgh npgllllahw
      121 lcqqapdrlp taaiiqlelp ltywrdlapg cartvwfdyp klhrplaper dtlass
//
LOCUS       WP_181740827             309 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Marinobacterium
            marinum].
ACCESSION   WP_181740827
VERSION     WP_181740827.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (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   2  (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
REFERENCE   3  (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
REFERENCE   4  (residues 1 to 309)
  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..309
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..309
                     /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=35106
     Region          66..309
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          226..305
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqnrydstpa eariftdqdl ltfgeryald yrfpdryrsg nimrgqveef gfrsgmqlvy
       61 snvqvmesym sssldpapln iiimlegyvs lslgpeviel seqmaltvsl dkevqldarq
      121 ltgqhlkvlt lsldyaalel lqapvqsgtg whlwrlpphl yqgllayrqn mdlsrlyleg
      181 lslqvlshgl aqteelaplk eprispqerv rleqirdrvv ddpraeyslt dlsrlaamsp
      241 sslrskfkac ygqtlfdfik eqrlnmardy llqgfsvqqa ahfagysyat nfttafrkhf
      301 gvapsslir
//
LOCUS       WP_181740835             506 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Marinobacterium marinum].
ACCESSION   WP_181740835
VERSION     WP_181740835.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 506)
  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..506
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..506
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=56234
     Region          7..383
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 miaplgrhvr qrmaqlhrwt gvlliwllfv ifltgtlsff rqeltqwmqp erpqgrelaq
       61 peaalehalp ylwqhasaas hwtivlpger sglldvswrg aegrgqaylh pdtgegvqvr
      121 dtrggeffyr fhfqlhylpv ltarylvgia ammmllalis gvlthkkilr dfftfrwgkg
      181 qrswldahng fsvlalpfhl mitytglvtl mtlyvpwgmd kafpeqeqrq qligeifafm
      241 pstpssgqva altsvpalve qaraswqgah vgrvqiahpg dlsakvlvea qtgqadrlgi
      301 sghppfmlfd gvtgellkak asrpaydayg tllglhlgrf adwpgrwlya llgaagcgml
      361 atgmllwtsk rrrkpghsrv glwlverlnv atlagfpvav valfwlnrll pvemtaraqw
      421 eihglflvwl gmgihallrp lqsgwreqlg lagllllglp vlnllttdrg fpaslaagdg
      481 vfigfdllsv llallmfrca rrrrgv
//
LOCUS       WP_181741072             327 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Marinobacterium marinum].
ACCESSION   WP_181741072
VERSION     WP_181741072.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 327)
  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..327
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..327
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35887
     Region          21..313
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtiemedarv ardvtgkidf lrssigslli gqdevvdqvl iallcrghvl legvpglgkt
       61 llvralatcf dgrfrriqft pdlmpadmtg haiydmkegr fhvrkgpvft nllladeinr
      121 spaktqaall evmqehqvti egkayalepp fmvlatqnpi eqegtyplpe aeldrflmkv
      181 fidypafdde trlvrqvtgg elsmaaissr lngaldaddi qalqqaaerv tlddqvlaya
      241 vrlvqatrna ssilkgagpr asiglvsaak awalmngrdf vlpddvkqva lpvmrhrill
      301 apeseiegft pdrvlqqlmq tvdaprt
//
LOCUS       WP_181741185             550 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Thermoactinomyces mirandus].
ACCESSION   WP_181741185
VERSION     WP_181741185.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 550)
  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 550)
  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 550)
  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 550)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..550
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..550
                     /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=60725
     Region          73..186
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mlrrlwyfvl csllicfvlp agfvfgqngd ipqpvrmgna hgqviaeqlp ppsndttpgt
       61 wflgatppda dltkppivfv qglnsqaqsw wdetfyhgmn dmyetaynhg yrtafvqlhd
      121 aggnpsspwd ngkllarmle eiyshfrqkv nivahskggp dtqaalvhhg afpyvhkvvt
      181 lgsphhgshl adlayswwag wlaellgqks datyslqtge makfrevtdn hpnapkntyy
      241 taagtnwgpt fsalwlggvy lsshgendgl vnvwstglpy ghhlftsdvd hdgirtgtas
      301 fakmdpvlrt mqvadseker nrqsssvvve pltnhfvrgg plvanqpktv tipadgssds
      361 mvfavltksp htevklisps gkvysetssq ffqttdkyff kgaaiqlfqi kdresgnwvm
      421 qmnspqsday llvatfpgse elsvslpvit dqlklplhve wdhvkqwnpg qirgtvkvip
      481 pqaqtdrksl nletipltea gknrpelyae lkletagtyn ltieiegktl dgkpfartii
      541 rsvhvekatk
//
LOCUS       WP_181741220             346 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Marinobacterium marinum].
ACCESSION   WP_181741220
VERSION     WP_181741220.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
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="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     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=35508
     Region          26..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 mlarahlgrq vlvvlgvlll mvmlfsttvg pmhilwrdsl dvliglggsn gpadtiitsi
       61 rlprallgml vgaalaasga aiqglfrnpl adpgligvsg gaalaavavi vlggttlgsl
      121 vnwmgpyslm laafgggfat tlivariatt rtggtstntl llagiainii tgagiglfty
      181 maddtqlrtl tfwsmgslgg alwevvlsag slivlvllll pglarplnal llgesearhl
      241 gvnvdrvkrr vmllsalavg aavaaagmig fvglvvphlv rltlgpdhry llpasallgg
      301 lfllvadmla rtliapaelp iglltsiigg pffialimlq rrrysl
//
LOCUS       WP_181741008             172 aa            linear   BCT 28-DEC-2024
DEFINITION  NuoB/complex I 20 kDa subunit family protein [Thermoactinomyces
            mirandus].
ACCESSION   WP_181741008
VERSION     WP_181741008.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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 172)
  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 172)
  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 172)
  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..172
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..172
                     /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=19147
     Region          1..169
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 melnfenitp feeqefkrnv ittnldqlkg wvrsnsmwpl sfglaccaie mmatggshyd
       61 fdrfgvifra sprqadvmiv agtvtkkmsp llrrlydqmp dpkwvvamgs cataggpyvk
      121 sysvvkgvdq ivpvdvyipg cppnpaaliy ginklqekir yeakhgkkvi nr
//
LOCUS       WP_181741256             468 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Thermoactinomyces
            mirandus].
ACCESSION   WP_181741256
VERSION     WP_181741256.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=52780
     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 mkpcvliidd epaigsslhf aledhfrtfa ctnvsdayki lqkhevhvil ldlrldnadg
       61 ldllseikem ypaipviimt afgsiessve aikrgafhyi mkppevdell llvkkslehq
      121 nlynqvrels kqiekmkgyd qiigksppmk rvfsiidqvk didsnvlitg esgtgkelva
      181 raihhngkrr ngpfiainca aipesllese lfgyakgaft gasssrtgki eaaqngtlfl
      241 deigemtpql qakllrflqe kevtplgssd tikvdvriis atnqnlldli ekgdfredly
      301 frlsviplhi pplrerkddl kllipyylkk haevmnrpvp alssealqcl eqfsypgnvr
      361 qlanileyav amaknrqiqs sdlpflitdp lksdfktekd enknnlqipi pstlkevekk
      421 liqavldyck gnrrktasll kisernlrnk lnqykkeden fkigkncr
//
LOCUS       WP_181741317             327 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Marinobacterium marinum].
ACCESSION   WP_181741317
VERSION     WP_181741317.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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..327
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..327
                     /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=37059
     Region          34..>327
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 madtkaitts kqiaalrlee grsvqrfrvh tsmgsglfve lrkgrtqkvw lyrfyianks
       61 gdyrmgtfpa islkqarelh aeavqlvkkg idprtyraae vakntqawtm qeaferwlah
      121 ytasptrtgh lptektikqr krrwrlhlek qlasmrvqdv traklievls daateareea
      181 rqclimlkgi layaedleqi eespaasitp akikarpspp rdrylslgel tevlqvfndp
      241 ngrtsvtvrn vmrmliatga rrsevsqmqw gevnmqagiw tlpasrtktr qvrrvalsay
      301 sleilkqqqq lshsgfvfes pdipgqp
//
LOCUS       WP_181741343             153 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Thermoactinomyces mirandus].
ACCESSION   WP_181741343
VERSION     WP_181741343.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 153)
  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 153)
  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 153)
  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 153)
  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..153
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..153
                     /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=17363
     Region          65..151
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtiqtlslqn nkeliqilst qqaayqveae liqayniptl netiesirnc ketfigiyek
       61 eqlagflsyi qdpnqiticr lavhpsffrq giasrllnrv lniagitrwk vttgkgnipa
      121 ircyekhgfq lveeimtkeg ipivrmlkkv dkk
//
LOCUS       WP_181741494             264 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Thermoactinomyces mirandus].
ACCESSION   WP_181741494
VERSION     WP_181741494.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..264
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30037
     Region          5..245
                     /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..127,132,155,159..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 mngfivgmyl pgdsfvhqld praklgfafi fmfmvffadr llacaiflaf vlvaihiakv
       61 pyrlfftalk piifiillss llhlwmtkgg emilafpgit iyeegirqag iisirllllv
      121 aiaslltftt spvdltdgme sllsplrkig vpahelalmm sialrfiptl weetekirka
      181 qmargidfee ghilkrlkkh lpiliplfis afrraedlal amearcyrgs egrtkwrqlh
      241 ytrrdlwlll ilillgmvll ifrh
//
LOCUS       WP_181741526             424 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Marinobacterium marinum].
ACCESSION   WP_181741526
VERSION     WP_181741526.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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 424)
  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 424)
  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 424)
  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 424)
  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..424
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..424
                     /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=47920
     Region          114..423
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrwfqrlfwk mflviwvvsl vgmgsvflll sshydqthrl ellearakgq allmlerfee
       61 gapdwykqsg rrhasslwly dartqaslmp wlpeptrktl qlelttgsgr ayharvalpr
      121 dvffvnrllg rlfslqmvli llvsglaglv lgalvvrpir rlrdhvrdlh qaqdmslrad
      181 eglsrrrdei gdltrefdrm vasveqtlla qqrllqdvsh elraplarlq aaaglieqrl
      241 gdgeplmdri nrecerldtl iseilsfsrq qrdgldhefs lhalcreleg dvelrqpqrp
      301 ftlelptqei lyrggrellr ralqngieni lrhtpeataa glvvrlledg rvelclfdtg
      361 pgvapdvlpr lfepfvrden gsgegfglgm siarraieql ggdisasnrp egglvlrvll
      421 psas
//
LOCUS       WP_181741542             406 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Marinobacterium marinum].
ACCESSION   WP_181741542
VERSION     WP_181741542.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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 406)
  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 406)
  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..406
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..406
                     /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=45886
     Region          <154..402
                     /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 mpvrttptds splrpalili shsvsletcw rdwlpaewad rlcryhsiea alpilqqpht
       61 pivllepstp dqtpealqql rrhrnplpvi vlhrsprapd wqplladpwn dhlhlptstp
      121 etahralryc cqllqphtvt paynptvepg ydpalwralq hqefelyyqp rinlrtgtfc
      181 gaealtrwhh pkrgllspdh fipacessgl ivplgywvlq evgaalpsmq aaglegrigi
      241 nlsfrqfqdr qlaptierlm qqqhmdarnl efeltetaly hdekhlcstv sqlsdqgvef
      301 slddfgtgys sfsllqklpi atlkidksfl dgipgnsdne eivraiisla hnlnkqviae
      361 gvetraqldf lmrqdcdqaq gyffsrpval tpflnllsts hrqqal
//
LOCUS       WP_181741762             363 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Marinobacterium marinum].
ACCESSION   WP_181741762
VERSION     WP_181741762.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..363
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..363
                     /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=38921
     Region          23..347
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mnvfshpefd nheqvcfftd pktglkaiva ihnssrgpal ggcrmfpyas deealrdvlr
       61 lsrgmtyksa lanldlgggk sviigdprqh ktealmeamg rcleqlggry iaaedsgtsv
      121 vdlqimgrht tqvagtsehp gfdgrpsngd pspvtaygvf vglkaavrhk lgrndlaglt
      181 vavqgignvg yrlarhlhea gaklwvydih qdqmdravqe fgatpvsadd iltlpvdvva
      241 pcalgavlnd tsipklqakv vagaannqle rpdhdallmq hgilyapdfv lnaggiidvf
      301 hsrtdyepdr vrahvdsida tlseiftrsd rdgrptgvia nelaeerfkp aatpqdstla
      361 qvs
//
LOCUS       WP_181741875             541 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Thermoactinomyces mirandus].
ACCESSION   WP_181741875
VERSION     WP_181741875.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 541)
  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 541)
  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..541
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..541
                     /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=60192
     Region          25..531
                     /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(191,194..199,201..202)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(194,312..313,334..339,419,431,434,445,525)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(194,237..238,285,287..288,291,312..313,334..339,419,
                     431,434,442..445,506)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(237,287..288,291,312,442..444,500,506)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mkmvtvvgsv shakgkpiqr rllslpqmld qtvrqhgdrt avqfyeteis yrklqdlsrl
       61 aagafrrlgv kkgdriglml pncpqyvvaf ygilrcgaiv vqvnpmytkr eiefvlqdsg
      121 advlivfgdl ysrfkktnlf srlrkvvvvk pdesvfpgla qntvswdnll agtsfmadde
      181 pidperdvav fqytggttgr skgamlthfn lvtnvlqlnd hsrgnsltet driliaiplf
      241 hiygmtcamn lgilngstii llsrfeplev lqtikkyrpt cfpgvptmyv alnsypkaeq
      301 ygidsiricn sgsapipvel iqsfekktga smyegyglse asptthntpr tgqkkpgsvg
      361 iplpgteari vdlktgtetl pigeagelvi rgpqvmkgyw nmpeetkqai rdgwlftgni
      421 armdqdgffy ivdrkkdlii asgyniypre ieevlythpa vmeaavvgvt dpyrgetvka
      481 fivlkpeaqv tgkeieqfcr rnlapfkvpk qiefrkslpk tavgkilrrv laeeekkrng
      541 n
//
LOCUS       WP_181741406             410 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Marinobacterium marinum].
ACCESSION   WP_181741406
VERSION     WP_181741406.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
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="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     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=43913
     Region          6..407
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mpimirlfip falgywlsyv frvinavvap nimqelgids aslgfissay fltfaacqip
       61 lgilldryqt rhvapvlllf aaagsltfal ansstllwig rgligmgvsa clmaafksya
      121 twlkteqlpl inglqlacgg lgaltatapa ewalqhsdwr tlfillalas lliaallysc
      181 ipltprnhtd irlptllrqt lavirtpafy qlapasmlsq svfiatqslw agiwlqrvnq
      241 lsasdaaqml lvsalgmmag flglggiasr lnrfgigtqs isfcgmagfl lvllwiqlhp
      301 gradtlawaa fgffgtsgtl mfaglaqqfp aaisarvsts lnlgiflgaf ivqwgmgaii
      361 arwpsangvd ysaeayrtal gcatalqals lawylicrwr psqlsnadst
//
LOCUS       WP_181742125             368 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Thermoactinomyces
            mirandus].
ACCESSION   WP_181742125
VERSION     WP_181742125.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=41357
     Region          35..367
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 miidffglnk ayveqknkil yiidstltke eflrgqsvqq lekecsivle rkyaiavnsg
       61 tdalllslrs lgigkgdevi vsafsfiasv spilmvgatp vfididpety lmdleklesa
      121 itaktkaiia vqlygqcidp aqlesiaeky nlwliedaaq afgsergnkv agsignisav
      181 sfdvskvvgg lttggmvltd dyelytvatk lrshgrdstt gdfrklgyns qmssinaavl
      241 iwkisqeekr rerriglaqr ymknlvhlpe ikcttivdng vhnfhkfvir anhrddlkef
      301 lkktgietki hyikplphye fikeksriys divhtekask evlslpiype lqeeevdyit
      361 dqiiefyk
//
LOCUS       WP_181742208             283 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Thermoactinomyces
            mirandus].
ACCESSION   WP_181742208
VERSION     WP_181742208.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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   Wintjens,R. and Rooman,M.
  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 283)
  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..283
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31749
     Region          6..69
                     /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 mskpfeelkr arnekrmslv qvaemtgidt eylaalenae fsllpdplyv rgfirryakt
       61 vgvnakpild ayreweqevn fieetnqqvs lpsrssryqk nrkagwkspg saiekfktln
      121 vkkkrilvss avflilaasa viwliidkvy sgaetvqlnq ssssapdsss aamvkkrpvv
      181 rlaqpaeksd ygdvysiena dkvevrisav klaeiqvrsg gptgekiaek tlrakktemf
      241 sdpkwlslrv dhpdhvkiyv ngvlidtskq kevslyqlki kek
//
LOCUS       WP_181742126             324 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein
            [Thermoactinomyces mirandus].
ACCESSION   WP_181742126
VERSION     WP_181742126.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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 324)
  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 324)
  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 324)
  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..324
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..324
                     /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=35884
     Region          4..317
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msetvliigg agfigsklsq vlrneghkvv vldnfqqysn pleinyasvl ayrkqllegc
       61 eivrgdatvs fdlinvienf kpdrvihlga vtradindan itnsvmftim piihlmqilq
      121 rhpikrflyv sssyvygnfq yspcdenhpl nptstygstk lsaeiytkal gqrfnvpyti
      181 vrliavygpg dvngklsmqn iksaldsgei pvmgsldela dysyiddtvs glmkalfsgq
      241 tdgktlniss gqgvemseli kifdelgyav kpkmmpvtks rpkrgylsik faqelidyqp
      301 ttplnkglkk ciefiknnkv fige
//
LOCUS       WP_181742211             414 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Thermoactinomyces
            mirandus].
ACCESSION   WP_181742211
VERSION     WP_181742211.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 414)
  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..414
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..414
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46226
     Region          1..67
                     /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 magigdylkq vrqqrgysle emnrltniht kylyllendr fdllpspfya kaflrtyaks
       61 lgidakplld hldkllknkm psrkpvrntv tspqilpryn knflptsprg klpegsvtgk
      121 asypgderqt tgqnhyrnqs agtrhnrmnm pmtdtqripv mpnsgmnpnt npnmnnmnpn
      181 tnpnirqnlq ppymapknvs pttgpqhevp qstmsfpple atqqhlltpr svamaakelq
      241 nkgkkvtlrk krykiiaiav gallllgggf yyffmdhdka sqstnnntat tdiysgasfe
      301 nvnaeskktp alvegeastd pkvgqtylir nvdklevvlk grsgtstlly aptpndkpke
      361 ltlkerqtvt ldtagknyiw frlgtpsnve ilvngqqint daqdaeksyi vkve
//
LOCUS       WP_181742236             477 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Thermoactinomyces
            mirandus].
ACCESSION   WP_181742236
VERSION     WP_181742236.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 477)
  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 477)
  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..477
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         1..477
                     /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=54485
     Region          2..462
                     /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 mgqkrvhflh tndlhshldq fgkiytlves lrsqfeadge pcflldigdh mdrfrleteg
       61 tdgrvnrall ertgydmvtf gnnelltfsk eqlgilyhdv pfsvvstnvf dlkgdhqpdw
      121 ivpyqwkvvn girccflaat ipyplvyemm gwqvknpfpi ieeavlsvrh qadvvvllsh
      181 lgldkdqlla ekidgidvii gahthhlfeq aekigntylt aagkfgqavg qisitvdpdr
      241 rsiedvsacc hfveqhpsae siedlmdwyk lqaeqnmsqp vtwleeplei nwneespfan
      301 lladsirdwv gsdlalvnsg qllcdlprgt itqriihqac phpinpvlme isgrdlkdtl
      361 eesllnefkq kpirgfgfrg kilgmmsvsg ievrydpdre pfqkitslwl gekewkenek
      421 ylvgmidmfm fgagylrlrs gklikyflpe flrdllahql kkptairkcr qrrfltg
//
LOCUS       WP_181742300             149 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Thermoactinomyces mirandus].
ACCESSION   WP_181742300
VERSION     WP_181742300.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
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="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     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=17495
     Region          1..132
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrqnqfqirv nwgdtdkagi vyypnyfkwf diaghqffrs aglspaelad kqqiilplld
       61 arctfekply yddiitiktr veeihrktik lshevyrdee rtgygyelrg wvkeedgkif
      121 avpipdevkd lllkereken lsvnpwlsa
//
LOCUS       WP_181742409             201 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Terrilactibacillus laevilacticus].
ACCESSION   WP_181742409
VERSION     WP_181742409.1
KEYWORDS    RefSeq.
SOURCE      Terrilactibacillus laevilacticus
  ORGANISM  Terrilactibacillus laevilacticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Terrilactibacillus.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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 201)
  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..201
                     /organism="Terrilactibacillus laevilacticus"
                     /db_xref="taxon:1380157"
     Protein         1..201
                     /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=23709
     Region          5..148
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04692"
                     /db_xref="CDD:467574"
ORIGIN      
        1 maewltifnd dginigiker dqvhldgdwh etfhcwlfet dhqrinlyfq krshtkkdfp
       61 slyditcagh idqdekviea glrelqeelg vilkekdiiy dadfketiql dsffdreich
      121 lffmnlteck lnllnigdev esiakvdinl feqlikkerm dipmleltke gfiqkkvtks
      181 sfcphdheyf nhiiqvckkl s
//
LOCUS       WP_181742452             108 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Terrilactibacillus
            laevilacticus].
ACCESSION   WP_181742452
VERSION     WP_181742452.1
KEYWORDS    RefSeq.
SOURCE      Terrilactibacillus laevilacticus
  ORGANISM  Terrilactibacillus laevilacticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Terrilactibacillus.
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="Terrilactibacillus laevilacticus"
                     /db_xref="taxon:1380157"
     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=12347
     Region          5..71
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(8..9,11,14,17..18,21..22,25,55,75..76,78..80,82..84)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(9..10,14..16,29..31,40..43,45..46,49..50,52..53,
                     59..61,66..68)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(29,32,75)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mdksaqvlki lgdktrltiv allmkrelcv cellevfems qpsisqhlrk lkdaglvkea
       61 rkgqwvyysl nemaeyypli qtvinyipdq sdkirqieks nptlrcgc
//
LOCUS       WP_181741816             220 aa            linear   BCT 28-DEC-2024
DEFINITION  anthranilate synthase component II [Marinobacterium marinum].
ACCESSION   WP_181741816
VERSION     WP_181741816.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 220)
  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 220)
  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 220)
  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..220
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..220
                     /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=24168
     Region          3..217
                     /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 mkvyiidnyd sftynlyqyi geilhteqhq grldsfdivv krnnevtldd vraaapdrii
       61 ispgpgsped payfgvcaev irelgpqipl lgvclgmqgi vhvfggkvvk aplpmhgkis
      121 pishtaegvf antpdqleim ryhslmaeae slpecldvta vvgdlpvdsf tdharihrgg
      181 dfeimgvkhr qhpihgiqfh pesfateggk elianflfqa
//
LOCUS       WP_181742368             460 aa            linear   BCT 28-DEC-2024
DEFINITION  transketolase family protein, partial [Thermoactinomyces mirandus].
ACCESSION   WP_181742368
VERSION     WP_181742368.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces mirandus
  ORGANISM  Thermoactinomyces mirandus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 460)
  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 both ends.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Thermoactinomyces mirandus"
                     /db_xref="taxon:2756294"
     Protein         <1..>460
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016744 - transketolase or transaldolase
                     activity [Evidence IEA]"
     Region          1..460
                     /region_name="TktA"
                     /note="Transketolase [Carbohydrate transport and
                     metabolism]; COG0021"
                     /db_xref="CDD:439792"
ORIGIN      
        1 ghtdgveatt gplgqgiama vgmamaeahl aatynrkdfp vidhltyalt gdgdlmegis
       61 heaaslaghl klgklivlyd sndisldgel nrsfseniqq rfqaygwqvl rvedgnnvee
      121 irrairaaka hteqptliei ktvigygspn ksgssashga plgeeevklt kefygwthep
      181 fyvpeevyad feekvvkpga qkeaewkklf aayeeaypep arelkqaiag klpegwekel
      241 pvfeagkdpl atrassgkvl naiarqvpyf lggsadlags nkttingedd fssrnyagrn
      301 iwfgvreham gaalngmalh gglkvyggtf fvfndylrps irlaalmkqp viyvlthdsi
      361 avgedgpthe piehlaalra mpglslirpa danetqaawr lalestdkpt alvltrqnlp
      421 tlegtrekay egvkkgayvi sdadketpda lllatgsevs
//
LOCUS       WP_181741801             644 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Marinobacterium marinum].
ACCESSION   WP_181741801
VERSION     WP_181741801.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium marinum
  ORGANISM  Marinobacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 644)
  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 644)
  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 644)
  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 644)
  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 644)
  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 644)
  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..644
                     /organism="Marinobacterium marinum"
                     /db_xref="taxon:2756129"
     Protein         1..644
                     /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=73897
     Region          374..634
                     /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 mhkrelrypw rwyfwsagla vlvllaivta lsllvnlrqe qrlqqqqhdy flsrlnhsih
       61 ttldsveldv srlaysplly nyleqpdtiw lkllqqsyls larlrpeydq irfldrhgte
      121 ivrinrlmgg dayvvpdegl qnkshryyva ealrldagel ylspldlnve rhevevpykp
      181 mlrlsmpvyq qdqlqglivi nyqgqtlldn lsevlpapls pllwdesghw lhgsdgrdwq
      241 fmfaehtgla vemptqwqqm qtrqrgevaa gdecyvyqwa eygqshlhgp rlllglkagq
      301 rcsalesryl ergiqlmaag sgvgllvlwg wyrlrrrqwh ldqrirrseh klrlitnevg
      361 sglimvdrng cvcwlnpeae rllgwteael lgqelhptih mtlsgqvlhe hacptlealr
      421 tgerqhaerd ffrtreghil pvhttvtplp gdgadggavi tfsddsghla tenrlreqam
      481 tdeltgclnr ratmqlldrl leapdsypgv vlfdidhfkr vndryghaag dqvlayyaqe
      541 vrellragdg fgriggeefl ivfdnvsldn llqlaervrn rfderrcpvd ehrlhvtasf
      601 gvavrqpges srtlmaradm alyrakdqgr nrveqaneel letg
//
LOCUS       WP_181743269             383 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Vibrio cholerae].
ACCESSION   WP_181743269
VERSION     WP_181743269.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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..383
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..383
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42012
     Region          192..220
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(193,196..197,200..201,203,227,230..231,234..235,
                     237..238,261,264..265,268..269,272)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          196..>355
                     /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          225..255
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          291..321
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          326..353
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msvvnealak saqrshsrls nieridvakp karpawlwgm lgfgvslavg gwsislqsvd
       61 tipssaevvr pevpsptqkt tqqtialyqa pvnsealvkn etlvqketlp knetavknav
      121 lakvesspss lkqtanrqre qtalgselna epvlnladhs epsffeeevs slpssspvmi
      181 veqvsltpeq laqkalqraq kamesnelqt avsaytealr ytphdemarq klaalyygkg
      241 dgrkafdlmq agiernpdge vlrlalakll vkekqeasal vplaylpsqp sieylslraa
      301 laqktkqdei aresyqqlte kdpnngrwwl glaiqqeral qwpaaqhayq qalnkvglss
      361 qsqafihqrl qllasleetq san
//
LOCUS       WP_181743273             610 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase [Vibrio
            cholerae].
ACCESSION   WP_181743273
VERSION     WP_181743273.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 610)
  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 610)
  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 610)
  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 610)
  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..610
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..610
                     /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=70478
     Region          <164..592
                     /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 mltkytqlaa wslaqlevet lnfthrlety llngsrenhq amslnydilw nrfdlfltsk
       61 etqelrqqhd aqaiiqevft qlkryelavs rgdqpvlqel lkllepynaq irnlaivnft
      121 gesansnirm inenkqqlly ffaaillmli llsymtyrsa dyqqflawhd pltrlknrnf
      181 ivkklkkrrr nqqepialil fdlnrfkeln dtmgyafgdq lliniaellt qrcrsfayqc
      241 arigadefav llhpctgnad ffirnlwndl tklvqendpt krlsvamgvv tcqtqdftes
      301 ssklrassll nnadlalnia kkapegqvvy ytrdiesayn kkrilaeqlq qllldpnqss
      361 lylsyqpils rnpdrlgcea lirwqhsefg yinpqyliei aeeyglgnkl gawimqqvyl
      421 alqndwkpyn rrldvsinls nslfdetlpa lvttifghhe nflnaiilel tetmtiddfp
      481 qslaiiesle kmkvrfaldd fgtgwsslyq lnhlkfsklk idksfvdnmn qnqqqaifia
      541 sivnlshqlg mqvvaegieq laqleqlkql gvdefqgyyf srpitktefa tfcdhyfsse
      601 naslstqine
//
LOCUS       WP_181743369             216 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Vibrio].
ACCESSION   WP_181743369
VERSION     WP_181743369.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
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="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..216
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23701
     Region          2..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mkfqaaifdm dgllldterv cmrvfqeact acglpfqqev ylsvigcnak tingilsqay
       61 gedlprlhne wrqrynavvm heaiphkdgv iallewlkar sipiavatst qkevaliklq
      121 lagldhyfan ittgcevtqg kphpeiylla aerlgvepqq clafedsnng ikaamaaqmh
      181 afqipdlvkp spevialghp ictslnevid llspnh
//
LOCUS       WP_181743448             446 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Klebsiella pneumoniae].
ACCESSION   WP_181743448
VERSION     WP_181743448.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 446)
  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 446)
  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 446)
  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 446)
  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 446)
  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 446)
  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..446
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..446
                     /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=47623
     Region          <1..131
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
     Region          222..408
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mmkmqwlsal vlgalscaaf aeeapadsnl ikqgeylara gdcvachtng kagkpfaggl
       61 pmetpigtiy stnitpdkeh giggytfeef ddavrkgvrk dgstlypamp ypsfarisea
      121 dmramyayfm hgvepvnvan kdtdipwpls mrwplafwrg ifaptpsdfv anpqvdpvle
      181 rgrylveglg hcgachtprs ltmqekalse segdeylags napidgwvas slrgenrdgl
      241 gtgseaelae flktgrndks vvfggmsdvv ehslqylsdd ditaiarylk slpprggkqt
      301 papvedsvak dlwkgndskt gaalyvdnca achrtdgagy krafpslkgn pvvqtedats
      361 lihivltgst tpavkdavsn ltmpsfgwrl ddqqvadvvn firtswgnna pavsasdvak
      421 vrkgtaahde kalgnadisk lpgagq
//
LOCUS       WP_181743535              82 aa            linear   BCT 28-DEC-2024
DEFINITION  BolA family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181743535
VERSION     WP_181743535.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            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 10000955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..82
                     /product="BolA family protein"
                     /calculated_mol_wt=9242
     Region          1..79
                     /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 miadeirerl rsltpatlev ldeseqhhgh sgwreggqth fririsapal tglsrierhr
       61 lihrtlgdiv prihalaiev qd
//
LOCUS       WP_181743571             469 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181743571
VERSION     WP_181743571.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 469)
  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..469
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..469
                     /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=51432
     Region          195..449
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 miaaasrmis srilprwlvi llivatifnd lqpflplgel skdafvylfp laflmllrnp
       61 grvalpplfs vlllifiili vvsiavnyea vstayfkgrs gmsrvitqgm avllgplvtl
      121 lffnlassan rrdisrgaev alwvmavvav fetaswsgvp gfsqiyegms vfihaetney
      181 yplrmrltaf easwaavmlt fifpfamtra tpvklflyag fvilsmflaq srtamlvigi
      241 qylvllaafm rrrkdyivhc vtaiciaamt vlatpgvges vatkvsnlie fgsvdgmidk
      301 dggvenvsni trlaavragm smfrenpvfg vgfaqygfny pshihmddmr ssevrsyvte
      361 adielawppa yslhvrllae lgiigylswl slilpvllrs lmmadgttyl grmhlavamt
      421 ligwmllgvs idsfrffggw ialgvglalp rpprsfgdrp vvsrtaaas
//
LOCUS       WP_181743618             129 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Paracoccus sp. S1E-3].
ACCESSION   WP_181743618
VERSION     WP_181743618.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 129)
  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 129)
  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 129)
  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 129)
  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..129
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..129
                     /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=13202
     Region          <4..114
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkrislavfa avtvlagaas aqdfvqsgta aklpqtegka iynaicsgch mpdgqgavga
       61 gqypalagna nletpdypiy lilhgqkamp pvgdvmddaq iaavvnyirh nlgnnyeget
      121 taedvaaar
//
LOCUS       WP_181743451             157 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Klebsiella pneumoniae].
ACCESSION   WP_181743451
VERSION     WP_181743451.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 157)
  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 157)
  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..157
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..157
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=16579
     Region          <2..151
                     /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 mnsgligtnt aewlpggtll vpealppnvt hiliklgtnd rgmatgpgym agaqgtfvnl
       61 nvivnslrtt ypgvrtilia ppyaptdsay gssdeiarav rraarvlecg fidlysptle
      121 lelqgetwls dglhpndygy rtmfkavqaa ivsagsk
//
LOCUS       WP_181743275             142 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HIT family protein [Vibrio].
ACCESSION   WP_181743275
VERSION     WP_181743275.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 142)
  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 142)
  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 142)
  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 142)
  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 10472213
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..142
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16009
     Region          9..101
                     /region_name="HIT"
                     /note="HIT domain; pfam01230"
                     /db_xref="CDD:395984"
ORIGIN      
        1 mahfelhpql qkdtdvighf plcvallhkd savpwvilvp qradlrelhh lpideqqqfl
       61 vesqlvcqtl etlfspdkln lgalgnmvpq lhihhiarft hdmawpgpvw grtqgvfrtq
      121 qeqaalltql rdalakhalf ta
//
LOCUS       WP_181743751             364 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Paracoccus sp. S1E-3].
ACCESSION   WP_181743751
VERSION     WP_181743751.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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..364
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..364
                     /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=39688
     Region          8..335
                     /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 msnlaykidi ivigggqagl ssayhlhqmg lqggkgylvl dksprpggaw qfrwpsltmk
       61 tinrlhdlpg mgfaevldpg qtevraaeav payfeayeqr fqlpvyrpvt vrvvcrrgdr
      121 frvetdqetf sargiinatg twdapqipyy pgrelfrgrq mhthdyrtad afagkrvliv
      181 gagisalqml deisrvtevi wvtrrppefr agdftpedgr aavaiveerv rqglipgsvv
      241 svtglpmtpa iramrergvl nrlpmfseit ptgvrwadgr eeavdvilwa tgfrsaldhl
      301 apldlrepng givmagrlat qvakdprvhl vgygpsasti ganraggaaa qelartlglt
      361 parp
//
LOCUS       WP_181743760             294 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paracoccus sp.
            S1E-3].
ACCESSION   WP_181743760
VERSION     WP_181743760.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     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=32434
     Region          3..244
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mgrlgihsfv wtggqtqqgl enaleksaeh gyrtiefayl rpelfdldrl akkaqsldvq
       61 igvtmglprd kdvsatdaqt veggkrmlad avhavrdigg nklggilysa htkydrqpte
      121 dgwknsveai aetaeiaraa gvdlvlevvn rfetnllntt aqglkflddt grddvrlhld
      181 tfhmnieean paaairlagd rlgyfhiges nrgylgdgvi dfdrifdall didyqrdivf
      241 esfstavvde glslacaiwr dtwtendpla ahakgfieqk maeakrrrat narp
//
LOCUS       WP_181743957             100 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181743957
VERSION     WP_181743957.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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 10475648
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..100
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10888
     Region          31..78
                     /region_name="HTH_3"
                     /note="Helix-turn-helix; pfam01381"
                     /db_xref="CDD:460181"
ORIGIN      
        1 mrtktgtfvp ktgtnvhlea dvadyrtaia aalrdelglt hravktamrw tgasertvky
       61 wiagergpsg ehlialakns divfhmvlml adrhddadae
//
LOCUS       WP_181744109             122 aa            linear   BCT 28-DEC-2024
DEFINITION  HesB/IscA family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181744109
VERSION     WP_181744109.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 122)
  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..122
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..122
                     /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=12849
     Region          9..112
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mfsipgqapv titpaaerqi srlmagkeay glkiglkkgg cagmeytmdl vpaadaadev
       61 veqngarili aptaqmflfg tqidyetgll esgfkfrnpn vtdacgcges vsfkldrdtp
      121 da
//
LOCUS       WP_181744152             902 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paracoccus sp. S1E-3].
ACCESSION   WP_181744152
VERSION     WP_181744152.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 902)
  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 902)
  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..902
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..902
                     /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=96490
     Region          2..902
                     /region_name="PRK10490"
                     /note="sensor protein KdpD; Provisional"
                     /db_xref="CDD:236701"
ORIGIN      
        1 mnddnrphpe aflpeanaea apeasprgrl kiflgaspgv gktyamleea aarskagsdv
       61 vaalvethgr tetaallarl dqiprreisy rdrrltemdl dallarrpav alidelahtn
      121 apgsrhpkrw qdveevlaag idvyttlniq hveslndvva ritgiqvqet vpdavlqmad
      181 eiklidlpad dliqrlhdgk vympaeagra lanffskpnl talrelalrt aasrvdaeml
      241 altrgmgrtg vqdrlmvcld dpatakglvr agrrmtdrar ipwvvahvlt pgieargaaa
      301 sgamidalql aerlgaetrt lhaehdvaga fldaarqlnv trlvvsrpas vgwldrlksr
      361 ffpplterlv eaagnfevti ltplggrala aprgtrprng qrwfrilves laaaafctli
      421 swpfwhvlpv aslaviylvg vlavgmrrgv aaaitasiis fltynfffte pyysfkvsae
      481 esvvallvft isalftgtla grlkrqvefm rdaqsrtetl ydfarkiasa sttddvlwaa
      541 aahiartlec hslilmpgse ghltqvqgfp sieedldpis daaalwafqr gqaagrdtdt
      601 lpaagwmflp latqgapmgv iglrftdpkr rmdpdtrrll navegqvava verikvgddl
      661 erarltsete klraallnsv shdlrtplvt vigalsaved gglspaqdra ltgqaldear
      721 rldrfvgnll gmtrlghgal vprlrgveaa eliaaaradl arvldgfava vevapdtppv
      781 lvdplligqa lsnllenask yapegstiri taapegaqva itvsdegpgi ppaergnvfd
      841 lfhravqgdg qpagtglgla ivkgmveang gsvaaieppa grgaairlll padlsspeda
      901 dd
//
LOCUS       WP_181744193             330 aa            linear   BCT 28-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Paracoccus sp. S1E-3].
ACCESSION   WP_181744193
VERSION     WP_181744193.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            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..330
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     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=36137
     Region          9..318
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(14..15,17,57..59,80,108..109,112..113,115..116,119,
                     123,125,133,135,137,139..145,147..151,169..170,173..174,
                     276,282,288..294,296..299,301)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(58,81..83,106,245,292,295)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(82..83,110,159..163,181..183,187,215..217,221..222,
                     243..245,269..270,292,294..295)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mtgtnsrlrv avtrrlpdpv qarmsalfdv tlneddhhlt rdelvealqn ndvivpslad
       61 rldgplldqa gprlkliany gagtdhidln harqlgitvt ntpgvltedt admtlaliia
      121 vtrrlaegla vmqsgnwegw sptaflggri ggrklgivgm grigqavarr arafgmevhy
      181 hsrtrlrpet eaelgaiwwe sldwmlshmd ivsmhvahsp atfhllgarr lkllkpsavv
      241 intsrgevid enaltrmlra deiagagldv yehgheanpr lrnlpnvvll phmgsatveg
      301 riemgervie niqtfangds ppdlmrpeml
//
LOCUS       WP_181744161             241 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181744161
VERSION     WP_181744161.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..241
                     /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=26375
     Region          <102..233
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mnrpisvaps ippmmvmaps dlwgqafhds vdiwqseqam fafhfalkga peyplatgws
       61 vtgaeasime rpesiyqlnq dlargemelg dyplqivhaa gydrtrapag ysllkieggm
      121 pyalkegpeh wdaikaqvad evldrylryt pnltrddvla rvimspldie rmnpamwrgs
      181 vhhldkrwgn fapyrlpipg lyqtgactap ggsvtgqpgr naaiailedd gkklgdivgk
      241 g
//
LOCUS       WP_181744359             383 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181744359
VERSION     WP_181744359.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..383
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39844
     Region          1..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 mdnrplagll vvsveqavaa pyctsrlada garvlkierp egdfargydr aaagessyfv
       61 wlnrgkesva ldlgapadra lflsmtdrad vfvqnlkpgt lerkglgsea lrarnprlit
      121 caisgygetg pyaarkaydl liqaesglcs vtggpeapar vgisvvdiat gaaaqaaile
      181 allargragq gcdirismfd viadwlavpf lhaaagqppq riglahpsis pygvfttadg
      241 qdllisiqnd rewatfaakv lkkpalaqhp dfatntarva hraavdaeva avigrhdkaa
      301 mgailqaadi afagvndmag lmshphlsti avttpgaisv plpapparfd gqrhigaapa
      361 paldqhgaai raefaapvrs hra
//
LOCUS       WP_181744620             156 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Paracoccus sp. S1E-3].
ACCESSION   WP_181744620
VERSION     WP_181744620.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 156)
  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 156)
  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 156)
  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 156)
  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 156)
  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 156)
  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..156
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..156
                     /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=16245
     Region          21..136
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
ORIGIN      
        1 mkasliatlt vfalaspsla qdaakgekef nkckachmiq ddagtdivkg gktgpnlygv
       61 vgrpiasveg fkygdgilkl aaanpgavwd ihslkayvtn ptgyldqysg dekakskmtf
      121 kmsknqddlv aylltispna ppqpaegdga pmapaq
//
LOCUS       WP_181745090             622 aa            linear   BCT 28-DEC-2024
DEFINITION  GumC family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181745090
VERSION     WP_181745090.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 622)
  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 622)
  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 622)
  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..622
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..622
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=69435
     Region          10..622
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mndpirrprq pskaipsrve rmdseefiql lrqnvwlilv vvaavmggtf wylqretpvy
       61 taqsamaltn sevrisqvdt qmevydltra rveteldrlr srnfaeevae sldlfdntkf
      121 lpldpngpam gsrergravi dkllgsyslq rsgeslvisv madaeqpqla adianavvet
      181 firlssaqqv teieksteyl rrqiettgeq laleqmqmad firenvlddt elperlrrer
      241 shqasvlavm dgrgqndpae rarleknlae vedqlaartr nemqlsrmer svdlmstryq
      301 tmverlnqle pqrdqiqpda rqvtvaevpf epswpniptt lalalpaglm lgfilallrs
      361 sfsrqiwtga qathvsqlpn lgnlprirgr gllgrrlapa wtlrrfprse yseairalvt
      421 iwssqaardk grklamvtsa lpnegkstva tslasvaald gmrvllldfd phragaslmi
      481 dgnlktssls qlndgtlpve daiaavpdyt nfdmlridrd srltpraidd faanilpqlt
      541 daydliiidt ppvlgvadaa rvgmladetl ivvrsgktpe ralqncverl edsgvqlsgt
      601 vmndieqrry rqmnlgggyg yy
//
LOCUS       WP_181745204             322 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Paracoccus sp. S1E-3].
ACCESSION   WP_181745204
VERSION     WP_181745204.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     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=33927
     Region          10..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 mslppvlshl ripviaspmf ivsgpelvia qckagivgsf palnarekeg epiqldlwlt
       61 riaeeldrhn qanpdnpaap favnqivhrs narlerdiei cvkhkvplwi tslgarpevn
      121 eaahsvggvv fhdiinntfa rkaiekgadg liavaagagg hagvqspfal iqeirawfdg
      181 pvalsgsiat gravlaaqam gadfgyigsp fiateeahai peykqmives gaedivyssl
      241 ftgvhgnylk psirnagldp ddlehadass mnfaqgaskp kawsaiwgag qgigairqvq
      301 paaayidqla reyaeakaal ag
//
LOCUS       WP_181745345             635 aa            linear   ENV 28-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase [uncultured Paracoccus sp.].
ACCESSION   WP_181745345
VERSION     WP_181745345.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Paracoccus sp.
  ORGANISM  uncultured Paracoccus sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus; environmental samples.
REFERENCE   1  (residues 1 to 635)
  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 635)
  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 635)
  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 635)
  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 635)
  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 635)
  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 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="uncultured Paracoccus sp."
                     /db_xref="taxon:189685"
                     /environmental_sample
     Protein         1..635
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70626
     Region          143..632
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mtlflentwt phplpagtwt vtlmnlseea ltdftlsltt itrimpehrl egarllrrva
       61 nfhefappeg lvlapgacwr fsaeglnrsp fhrndaakta cvtlksgqhl pvqlsdlvqg
      121 havpvlpppr lpegrltlpf asipwpnrie aeagpapvvi haaegtsrad lrlmlsidal
      181 harlfpaark lfqispapgs laltfaddag ipaegyrldf tperitltas aeagrryglt
      241 tlaqmlhgaf vdpqmrfpat gqivdspryd wrgnhldcsr hfwtadqvmr vidilgwykm
      301 nvfhwhltdd egwraeiray peltsvgatr gydcpgmlpq lgdgpepqgg fytqdqmrav
      361 vahagalgie vmpeietpgh aacvlaalpf lvdpdetpds yhpvqgypnn swnpglpetf
      421 evletiiael veifpsrhfh iggdevakna wlespraril mqreglsgtf elqswfarrv
      481 kqildrhgkv lvgwnelshg ggvdpentll mawerpevgi elartgydvv mtpgqayymd
      541 mvqgpdwlen gagwagpvpp aqtygyeaeg efpeelqhrm rgiqsciwce hfttvdwfnd
      601 lvfprlpava eaawtlkank dwlrfaaqvr lhpkl
//
LOCUS       WP_181744910             584 aa            linear   BCT 28-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181744910
VERSION     WP_181744910.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 584)
  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 584)
  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 584)
  AUTHORS   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 584)
  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..584
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..584
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=65501
     Region          40..583
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mdqnriaeqt tefvdlmqra qglagrasan aaakasgqef svldaatiaq ayaragmqia
       61 adpfalprfq mqlmtdsaqa wmrawtgpag etagdrrfrd drwngdplsr glrdvhlaie
      121 naaeqligdl pdddkdslrv rfytrqllsa lspanylaln pvardrflet egrslldgfr
      181 nllddlergd grldinmtdr hafevgrdla itegqviwqn elmqlihyap ltetqfkrpl
      241 lfvppwinky yifdmkpdns mvrfmleqgh svfliswvnp trehaalsfe dymrlgplea
      301 ldkieeatge kefdilgfci ggilvtatla ymaaigdkrv ktattlatmv dftdvgeigv
      361 fidrdrlkvl rdhmaekgyl enhhlqdmfs mirendliws fhvmnylmgk kppafdllfw
      421 ngdstrmpaa mllwylekiy ienglrqpgq ltmdgvaidi skitipfyvl atkedhiapw
      481 rsiypttgll ggktsfalgg sghiagvinp pgkrqkygfw tgepypadpd ewlahadkhd
      541 gswwphwadw iagnstgkkv payqpgagpl kpiepapgsy vrad
//
LOCUS       WP_181745450             192 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Paracoccus sp. S1E-3].
ACCESSION   WP_181745450
VERSION     WP_181745450.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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..192
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..192
                     /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=20630
     Region          33..183
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mliarlqaal aaetapssdf danprlspep plrdagvlaa fheddgrlfl ttraatmrhh
       61 pgqialpggk vdpgdadaia aalreaqeei gldprqltli gtlpphltvt rfritpvvav
      121 irgpftpiae pgevaevfal pfdhiaspan yrlegriwrg ewraysvapy gpyylwgata
      181 rillglaerl sa
//
LOCUS       WP_181745514             106 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paracoccus sp. S1E-3].
ACCESSION   WP_181745514
VERSION     WP_181745514.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     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=10851
     Region          5..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpqndhladl akglahparl rilrhllatp gciggdivda vglaqstvse hlrilkasgi
       61 isgeidgprv cyalnpaala plaefiaslt pppgdaccvp trketa
//
LOCUS       WP_181745551             281 aa            linear   BCT 28-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Paracoccus sp.
            S1E-3].
ACCESSION   WP_181745551
VERSION     WP_181745551.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..281
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=30763
     Region          59..226
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mlirygydit iesdgplpli lqmsarperq idlrgieafs tdpaipfaty ldgygnacrr
       61 ltapagrfrm tqtaviadsg laepalpdaq empiealpdd vltflmasry vdtdrvsaaa
      121 wdlfgqepag wgrvqtimdw vhdhitfnyq dadasrtafd aleqgkgvcr dfahlaigmc
      181 rslniparyv naylgdigir pppdpmdfaa svqvylsgrw wnfdprnnmp rigriavgyg
      241 rdagdvalis sfgqhqlvnf tvitdevdaa griippqaap a
//
LOCUS       WP_181744687             437 aa            linear   BCT 28-DEC-2024
DEFINITION  SufB/SufD family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181744687
VERSION     WP_181744687.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 437)
  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 437)
  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 437)
  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..437
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..437
                     /product="SufB/SufD family protein"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=46717
     Region          46..437
                     /region_name="SufB"
                     /note="Fe-S cluster assembly scaffold protein SufB
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0719"
                     /db_xref="CDD:440483"
ORIGIN      
        1 maetavltre agaadpglaa rlgaldlpag gftaaarkaa larfekmglp rgrdeywryt
       61 dpaafnaavp aplqiadsgp dgplfedidr lrlvfvdgif daeasddpal egvqidtlaa
      121 aegqadhwaa pvygtleaag hdrvarpfga lntavardga lirvsgrpar pihlihrrad
      181 dgadvyfhhv ivvepgaevt vletgmtgar snyvievdvm egarfhhisa kragyqklgw
      241 ggifarvaak alfksfnlsl ngtlmrheav idivgddava hiagavlgdg kngdfvhddt
      301 vfithgaerg esrqvykkvl kngakgvfqg kilvkpgaqk tdgyqisqal lldensqflg
      361 kpeleiyadd vkcshgsttg aidetvlfyl rsrgvpkgra ivlmvlsfla dalaevedea
      421 lreqiserld awltrha
//
LOCUS       WP_181745828             599 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Paracoccus sp. S1E-3].
ACCESSION   WP_181745828
VERSION     WP_181745828.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 599)
  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 599)
  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..599
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..599
                     /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=66673
     Region          183..526
                     /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 mldarvtdqv qqvlddfgaa laaadadraa gmfvsdcywr dlvaltwnlr tmegrdqvad
       61 mlrhqlasaq psgwkvdpve patedggiit awihfetavg rgyglirlrd gqiwtlltal
      121 qeikgheeak gfarplgakh gagknrpswl eereaeaael gytrqpyvlv igggqggial
      181 garlrqlgvp aiiidkherp gdqwrkryks lclhdpvwyd hlpyikfpen wpvfapkdki
      241 gdwlemyakv melnywskte aksahydeaa gewvvevnrd grdvtlrpkq lvlatgmsgk
      301 pripdftgad sfkgdqhhss ahpgpdayag kkvviigann sahdiaaalw ehdadvtmvq
      361 rssthivrsn slmeiglgal ysekavqdgm tteradlvfa slpyrimhqw qiplydqmre
      421 rdkdfydgle kagfkldwgd dgsglfmkyl rrgsgyyidv gasqliidgd vkvvqgdvar
      481 ilpegvelas gqvlpadliv yatgygsmng waadlmgqei adrvgkvwgl gsdttkdpgp
      541 wegeqrnmwk ptqqealwfh ggnlhqsrhy slylalqlka rmegidtpvy rlqevhhls
//
LOCUS       WP_181745938             455 aa            linear   BCT 28-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181745938
VERSION     WP_181745938.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 455)
  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 455)
  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 455)
  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 455)
  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..455
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..455
                     /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=48909
     Region          4..452
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mggtiwwirr darqadnaal aaaaaagpvt avfliepvlr aqgaatrwrl gralaaldad
       61 lrarggaltv rtgaaedilp rlaaelgaae vhalawpepk rivadeaart alngaavqlv
      121 lhdgatllpp aairnaqgkp frvqsafsra aralgvsppv rmpahiewrp apseqlgdla
      181 pdmnrgaavl aaharpagea aalmqlhafl dgpvedyahs reridrpggc talsealavg
      241 eigprtiwaa vadhsgegpq kllselmwre fawsllvarp dlpvanfrpe wdrfpwqgdg
      301 paaeawrrav tgiplvdagm remfvtgtmh nrvrmvvasf lckhlltdwr vglawfgdcl
      361 tdwdpasnam nwqwvagsgp daapyfrvfn palqaekfdp tgayrsrwls pnsgyfeavp
      421 rswglqpstr lhpvislaeg rgraldalsr mkgag
//
LOCUS       WP_181745642             339 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181745642
VERSION     WP_181745642.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..339
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34489
     Region          39..336
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkrdligvsn sasgglaftr raalaaaaaf alaapafaqd wptgpvhvyv gfpagsspdl
       61 lariitepls qklgqpvvve nkpgaggvig vqqmlaagpd ghafgtting plttagrlmp
      121 dlgydvakdi qpvaliatsp lvlavagdae atdlagfiel akaepgalsy gsvgqgsgah
      181 ltaelfneaa giemlhvpft ayaevttsii greidagfma psaalphvas gklkmlgvts
      241 aepfaqipdv pviagnagmp adfqaelwna fiapagtdpn vvarlntein ailadpevqk
      301 klldmgwqaa ggtpedlakr itddtrmwga vidkvgtak
//
LOCUS       WP_181745566              97 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181745566
VERSION     WP_181745566.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 97)
  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 97)
  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..97
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..97
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=10870
     Region          10..97
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 msqrlslsai vifllaalas lyfafaavqg psglmrriql qaeteqlrsd raalqaevdr
       61 mknlthrlsd dyldidllde rarevlglmr pdeviir
//
LOCUS       WP_181745961             255 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181745961
VERSION     WP_181745961.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 255)
  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..255
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..255
                     /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          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 meaprnefkr rlltgealdg lwlslaspis sealsligfd wllfdtehap vdlgalqpll
       61 qaaaagrsaa vvrpawndkv likraldmga qtllipfvet peeaaaavaa trypphgirg
      121 vaggtrasrf gltsdyfeva ndqiavlvqi etssalerle eiaavpgvdg vfigpsdlaa
      181 smghlgrtga devqamlrdt aarlgalgka pgilatnatd arryrdwgyq fvagavdlgl
      241 llkgaqgvla emrag
//
LOCUS       WP_181746128             420 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Paracoccus sp. S1E-3].
ACCESSION   WP_181746128
VERSION     WP_181746128.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..420
                     /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=47256
     Region          115..378
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mntllrlfle khmqlgqltv isargeelrl gdgsgppitv rfnttraera vasnpalklg
       61 ecfmdgeidm vqgsiydlim lgyanggrgl mpavwmkafe rmriltrrlh qintriqarg
      121 nvqrhydlsa dlyrlfldpd mqyscayypr pdiplaqaql lkkrhiaakl qldpgmevld
      181 igcgwggmgl ylaqvagarv dgvtlsdeql vvaqrrarte glaidfrlkd yreigrdydr
      241 ivsvgmfehv ginhydgffr kaasmlrpdg vmllhtigrv dppgatnpfl rryifpggyt
      301 palseimqai eksglvvtdi evlrlhyaet lrawrlafma rrdqakalyd eafcrmwefy
      361 lagceaafre ggmvvwqiql ahrvdavpvt rdhlssaeaq laeaearrgl pgpawpedwp
//
LOCUS       WP_181746086             272 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Paracoccus sp.
            S1E-3].
ACCESSION   WP_181746086
VERSION     WP_181746086.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     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=29993
     Region          7..>204
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msprfdtili tgaagrlgte lrrglaplar klrladvari tdcgpneevl tfdladmeaa
       61 maacagvdai vhfggapher pweevlnani rgsyniyega rkhgvprviy assvhamgyn
      121 eleehvntaa phrpdtlygl skcfvedlgr lywdkfgies vmirifssfp epadrrmlws
      181 wlsfddcvrl vtaaltaprv gftvtvgmsd nkvkpvdnsr aahlgyhpqd nterfragme
      241 artdtpdpra pavrclggwf vdighpddea rd
//
LOCUS       WP_181746284             234 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA (guanine(46)-N(7))-methyltransferase TrmB [Paracoccus sp.
            S1E-3].
ACCESSION   WP_181746284
VERSION     WP_181746284.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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 11415463
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     gene            1..234
                     /gene="trmB"
     Protein         1..234
                     /product="tRNA (guanine(46)-N(7))-methyltransferase TrmB"
                     /EC_number="2.1.1.33"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008176 - tRNA
                     (guanine(46)-N7)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25927
     Region          24..232
                     /region_name="TrmB"
                     /note="tRNA G46 N7-methylase TrmB [Translation, ribosomal
                     structure and biogenesis]; COG0220"
                     /db_xref="CDD:439990"
ORIGIN      
        1 msdkpfdpnp thrnfygrrh gktlrrsqkg yladdlgalr pqgitlsdnp drnpvdpaaf
       61 fdgqppvwle igfgggehmv hmaatypgig ivgcepfing vamlvgkika agvsnvsvhp
      121 gdardlmdvl pegsiakafl nypdpwpktr hhrrrfvtpe hliplhrvma pgaefrvatd
      181 ipsyvrqtls evpkagfelv slragawpdw pstryeqkal regrtptyis frrv
//
LOCUS       WP_181746051             323 aa            linear   BCT 28-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181746051
VERSION     WP_181746051.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     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=34374
     Region          6..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,
                     215..216,237..241,261..264,311,313)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176189"
     Site            order(134,230..231,244..245,246..248,256..263,266..267)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 msrmyrihel ggpevlslvd aplgnpgpge vrlrhayvav nfidiyfrtg rypmplpngl
       61 gsdavgviea vgdgvtefrp gdrvgyllgp qgayadmrim paevlipipd gvsdstaatl
      121 mmrgmtaqyl frqvyplkgg etilyhaaag gvgliacqwa ralgvemigt vstdekaeia
      181 rangcahviv tsreniaerv reitngkgvp vvydsvgkdt lmasldslap rgalvsngts
      241 sgpveidttl lavkgslwvt rpamihyatp rphmlamare mfdlveagki vsepgqvydf
      301 adaaeahral egrrtigstv lki
//
LOCUS       WP_181746355             198 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181746355
VERSION     WP_181746355.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     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=21462
     Region          8..189
                     /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 mtrthqarli lgsasprrld llaqigitpd eirpadidet prrnedaray vrrmaaekae
       61 avsaapddiv laadtvvtag rrilgkpeda aearafltll sgrrhrvmta itlrrggrew
      121 srlvetqvrl rplsareied ylasgewqgk aggyaiqgra gafvnwiegs fsavvglpla
      181 etatllraaq aarpsked
//
LOCUS       WP_181746396              75 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paracoccus sp. S1E-3].
ACCESSION   WP_181746396
VERSION     WP_181746396.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     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=8010
     Region          10..70
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtntptepkt hdpllrlrni igpygilpvs rstfyalvaa gkipkackls arisawresd
       61 ilayiasaea ddagr
//
LOCUS       WP_181746431             475 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Paracoccus sp. S1E-3].
ACCESSION   WP_181746431
VERSION     WP_181746431.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            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 11417382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..475
                     /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=52333
     Region          5..475
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 msnphpsfrd svdrmfthaa slmklppgle ekirvcnsty tvrfgvrlrg aihtftgyrs
       61 vhsehmepvk ggiryamsvn qdevealaal mtykcalvev pfggskgglr inprewdede
      121 leritrrfty elsrrslisp sqnvpapdmg tgeremawma daykrlhpdd inakacvtgk
      181 pvtiggilgr veatgrglqy alreffrhpe alkragvegs lsgkrvvvqg lgnvgyhaak
      241 flqqedgcvi vtvveyngtv snpdgldiea lkahvnetgs vagfpgatfr eagleglede
      301 cdilipaave sviteenapr ikaklvieaa ngpvtaegde ilkkrgivvi pdmyanaggv
      361 tvsyfewvkn lsqislgrle rrheearnrm lveeitrlsa dsgvkwtlsd gfkeaylhga
      421 delelvrsgl ddtmresymk mqevwfgddr vedlrtaayv vairrianvy gslgl
//
LOCUS       WP_181746532             460 aa            linear   BCT 28-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181746532
VERSION     WP_181746532.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 460)
  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 460)
  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 460)
  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 460)
  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..460
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..460
                     /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=47749
     Region          2..442
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mtpefaapta darpiwlvqg alpddldpaa rawaqatgfa gkpgqvcllp gadgalsgal
       61 vgveqasgrp srerfalaka amalpegawr ivawpegldp aeaafgwlla qyafgryrka
      121 egakarlvap egvdaarlla maeaefltrd lintptndmg pdaleaaara maaqhgfavk
      181 vvtgdelldq nfplihavgr aaaqaprlie ltrgeggpal slvgkgvcfd tggldikpaa
      241 smglmkkdmg gaatvlglaq mlaatgaadg irlrvlipav ensisadafr pgdiltsrkg
      301 ltvevnntda egrlvladal alaaedepdw lismatltga arvalgpdvp pfycdddaaa
      361 aaisaaarsh wdplwrmpfw epyeemiepg iadldnapsg gmagsitaal flrrfaegag
      421 hyahfdiygw qpkpapgrtk ggvqqgaral laalpellgk
//
LOCUS       WP_181746698             224 aa            linear   BCT 28-DEC-2024
DEFINITION  YcbK family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181746698
VERSION     WP_181746698.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            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 11459704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..224
                     /product="YcbK family protein"
                     /calculated_mol_wt=24732
     Region          19..129
                     /region_name="YcbK"
                     /note="Uncharacterized conserved protein YcbK, DUF882
                     family [Function unknown]; COG3108"
                     /db_xref="CDD:442342"
ORIGIN      
        1 mttrfyrhwr dvpkdiwhwp nfspaeiacr gtgsiliheq aldrlqalrt rlgkplivns
       61 ayrspehnar vrgakrskhl egtafdisma nhdpaafeka araegfmgfg typrsgfmhi
      121 dlgparrwgv pfparaipfa edqpparehl adsrtmkgss avglatvgaa gieiaqdtls
      181 daqsaiqpli pyldtlrwaf ialalagigl tvwariddwn rgqr
//
LOCUS       WP_181746845             198 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181746845
VERSION     WP_181746845.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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 sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..198
                     /product="LolA family protein"
                     /calculated_mol_wt=21526
     Region          1..191
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mkklalavap viallatapa alaekiplnt isnylnglst lqseftqvnp dgtisagtvy
       61 iqrpgrvrfe yknsrqlmla sggqvavfda ksnqgpqiyp lgqtplsiil dqnvnlarkg
      121 mvtghserkn ttvvkaqdpa rpqygsiemv ftsptelrqw vvtddtgkkt tvilgemkkg
      181 vrfkpstfai qneinrrk
//
LOCUS       WP_181746882             154 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Paracoccus sp. S1E-3].
ACCESSION   WP_181746882
VERSION     WP_181746882.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            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 10002890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..154
                     /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=16285
     Region          1..150
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 maagghrrpg lilprrnrry rfsmtpladv mfqlliffml saniapysml dlrtgalsgg
       61 gaapapetgt epgrttdirs tavwtldetg tilasgqrfe parlpalada lmaqgtrdvl
      121 vvlrhdvavq qlvtvlqtla argitsvqia sggt
//
LOCUS       WP_181746888             254 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Paracoccus sp.
            S1E-3].
ACCESSION   WP_181746888
VERSION     WP_181746888.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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 254)
  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 254)
  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 254)
  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..254
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..254
                     /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=26879
     Region          10..250
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mnaettplif qtaalshqgr vrshnednya tlpelglwvv adgmggheag diasaiivqe
       61 msslgvavta adqrarfmer lhrahqrira haaeheldtv gttvaallvf gaelscawag
      121 dsriyllrkg eltamtrdhs evatllaega itaeearssp rrnvitravg igndprpemv
      181 tgvarpgdrf licsdglteh ltdeelgill dsghdaqhta eqligltler gakdnvtvlv
      241 idaaaggedp gegg
//
LOCUS       WP_181746936             475 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paracoccus sp. S1E-3].
ACCESSION   WP_181746936
VERSION     WP_181746936.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. S1E-3
  ORGANISM  Paracoccus sp. S1E-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 475)
  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 475)
  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 475)
  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 475)
  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 475)
  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 475)
  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..475
                     /organism="Paracoccus sp. S1E-3"
                     /db_xref="taxon:2756130"
     Protein         1..475
                     /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=51379
     Region          139..466
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrsidtltgr faaltllfva laelfvlipa msnfridylq trlekaqias lallaapede
       61 nittdlesel ldnagvynvv lrrddvrqlv lssplpgpiv atydlrsnst lamaadalrq
      121 lfdrkdevvr vigapvnhag qlieitlsta plrkamvdfg lpvlvwsavl illtaallnl
      181 aaqrlilkpi rrvishmasy saapedtrli itpdarivev reaesalasm qttltqalkq
      241 kerlaglgqa vakishdlrn ilttsqifad rledsadpav rkaapklvns itravnlcet
      301 tlafgkaeep aptlsrfdlr alvdeiaeae allaeapngt plvdfvidis pnlviradrd
      361 qlhrvlsnli rngrqaieaa grpgtieiag aetdhdwqir vgdngpglpq kaqdylfkpf
      421 tgttrkggtg lglaiaadli rghggklelq rtdengtcft itlprgalie nfeae
//
LOCUS       WP_181746999             424 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Brevibacillus halotolerans].
ACCESSION   WP_181746999
VERSION     WP_181746999.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 424)
  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..424
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..424
                     /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=48317
     Region          1..>74
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mtqddihewm qrdldddlsk eekrilqakl aenpeymlqy erlkkvsdgl tnlprvtppf
       61 sivdallpql eqsretpepa avtqtelprl elkqtedksv gkkrrlplwm akvgsgvaaa
      121 clllgifvma nkdknepial tngasghvqe dvsknssgdp ivketpktek pkstptdkkt
      181 tddekdqnpq daskevpdvt pndtstelkg eqkqkenkpd hhqggssdsk sdaetsvamg
      241 qtdgrlkggn qtdenqtqhe iaispkikdn htsasdkqas aheqsisega lfslipdqvd
      301 nynkldqegk iqaweeaske vqeflqehpd lqnvknqkdl ekviqnaier alkeqkkree
      361 ekkqraeqqa kdkqkelekk qkelqkewek qmkewekqqe kqrkdtekhl eewtnqqngw
      421 kwqk
//
LOCUS       WP_181747163             276 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Brevibacillus halotolerans].
ACCESSION   WP_181747163
VERSION     WP_181747163.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 276)
  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 276)
  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..276
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..276
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31134
     Region          6..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 mlnkvmfgry idtnswlhrl dprskllgmf lfvllimmtn sllaciavfl faigimassr
       61 ipfgffvkav kplrflilfl flfqlffike grfllsigpf sfyaegvrla cmtawrmill
      121 laftslltft tkplslakgv egilqpfrft gispeklglm isislrfipt ifeetqkimk
      181 aqasrgadva dlpwrekgkm llsllvpvtv ssfrraedlv ysmeargyvl gaprisyeml
      241 kwkrqdsifl glllainilv gfilndcggl tygslf
//
LOCUS       WP_181747205             336 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Brevibacillus halotolerans].
ACCESSION   WP_181747205
VERSION     WP_181747205.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     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=35903
     Region          30..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 mscllqsrra kvwalltgil lllvsmlmsi lfgyhmftfh mlldmlyqfd gskehlllrd
       61 vrlpaafiaa svgaslaiag vlmqnltknp laspslfgin agavlfivlt lfffdpdltl
      121 tqmvwiafvg agvtavlvli lgtmgkdgfl pikvtlagaa vsvfassfts gimlinnesl
      181 nqalfwlvgs vtgrkmehlt tvlpymvigw iialclshal nlmamgddma kglglhtafa
      241 klliilvvil laggsvslag piafvglivp hicryivgvd hkwlipfsgl igaillvsad
      301 tasrfllmpk evpvgvatal lgvpfliyia rrssye
//
LOCUS       WP_181747341             295 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Bacteroides fragilis].
ACCESSION   WP_181747341
VERSION     WP_181747341.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
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="Bacteroides fragilis"
                     /db_xref="taxon:817"
     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=34019
     Region          <159..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mklhykkehi sctnyksesy egfgigtlts gsnfnsqtls vktnflifil egeveiipke
       61 gkikrviaqe fffisalsty eiqvrvpgry iymsflyndi klcekhmles ylkevrease
      121 evgilsvrhp lnlflelmda ylragvnckh lhsikekelf iilrtsyskq eivnlfheii
      181 gtnmsfkaav llhvdrvnnr eelaqamgms itdlarkfkv efgesvyswl lkqknkkiiy
      241 rlaqpgasvk eivyefgfss aasfnkyckk nfgnsprela rqlkdkyidn qnlki
//
LOCUS       WP_181747432             555 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Bacteroides fragilis].
ACCESSION   WP_181747432
VERSION     WP_181747432.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
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="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..555
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64713
     Region          11..>250
                     /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 mtrvpftqny rwhlpllllv fccsffinng aifadimesr niitaremvy dhnwlvptmn
       61 gelrlekppl ptwiaaitem ispdnlplqr amagfaavml vlffykfatk ltdnrtyalv
      121 sslvlctsyn iilmgrtatw diychafmmg aiyylylalr qnpckwtyfi gagifmglsf
      181 lgkgpvsfya lllpfvcayi lyyrketqmk gkwialavmi ligivlstww yayiyiyhqe
      241 masyvfhkes sswsnhnvrs wyyywqffle tgvwslltlt tllvpfwkkr vesskeylfc
      301 lswmllilff lsllpekktr yllpillpaa ltmghlfvyw irqakqkmpq lkdrvlyrin
      361 aylivvaala lpialylfmy regrmgtgmf vwlvvlfltv avwlfrsafk lqpfsflmgi
      421 valfavaelf vmpyigsfvs nsdpksisat rknpelqplp fyhskdevlr ielvyeahkk
      481 igdmdlsnke eiikalpfvl isqkpaelli pdsirkdlnl rfidcydnnr wakghkryds
      541 vfisnvtive pikeq
//
LOCUS       WP_181747442             428 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [Brevibacillus].
ACCESSION   WP_181747442
VERSION     WP_181747442.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus
  ORGANISM  Brevibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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 11441044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Brevibacillus"
                     /db_xref="taxon:55080"
     Protein         1..428
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=46979
     Region          64..287
                     /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 msqkkisllm vfcsliggii gfvvgemivn llsnelpqwv imglyfgqya lfvglmclia
       61 elisprlngq gwrqryvgfs wkmlvpstfi mlgvvamllq ffygtnfqka sgsnnivmll
      121 disssmqesd kdnqlfksaa dvvrrmdant rvavitfnqq asvlqplvll snqkvrddvi
      181 qklnshegps ggtdieealq talnhinret nnsgnntvil msdgysdvdl dkslqpfkqs
      241 qiivhtvgms tvsadgtqll kriaeetngn yydiehtdqi tgvfgqiydm srqdrelvke
      301 rvgatehslf yailrvvsll vigallglav glffdnkyia kgftlggivs gllaglilek
      361 glasgmypam gvrlvadlll aavmplftif ipmpnqalas eksrftggry lsaknkeakq
      421 istnkfdr
//
LOCUS       WP_181747322             599 aa            linear   BCT 28-DEC-2024
DEFINITION  IucA/IucC family protein [Brevibacillus halotolerans].
ACCESSION   WP_181747322
VERSION     WP_181747322.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 599)
  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..599
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..599
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68500
     Region          4..582
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mkhvkdiaeh aamqsflncy lretgngrwv ttngekylhv plvsqkmdly vkasyqsptg
       61 rhqfdypafy qsreeapave adyvtmtvll vkelslqhgt kavpdelvlr viqscqnmer
      121 ylaaryddre elygfemdfi taeqallfgh lfhptpksrq gipdtkqavf speqkgafpl
      181 hyfaahhslv legsglkqsa teiikaelgq evleqdgirq yaknedysli plhplqaewm
      241 ldqhsvqkyi kcgllhnlgl lgecyqatss lrtvyhpdks fmiklsipvk vtnslrvnkr
      301 aelesgveak kvldmfeeem skqfpgfafi hdpayitlkl deqdesgfev ilrhnpfqgs
      361 aaenatvlaa liqdplpgqk srlaviilql aqqegrtpse vslewfrryl eislkpmvwl
      421 ylkwgiglea hqqnsivklq dgypsqfyyr dnqgyyycqs mkellsrnfp nlgemsknvt
      481 edslvderlr yylifnhmfg lingfgsagl ideqqlldem rsvlqeflpl nrepsqflhs
      541 lltseklack anlltrfhdv deleseesns aifvkidnpl akarerqiel eavnqlalr
//
LOCUS       WP_181747481             659 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Brevibacillus halotolerans].
ACCESSION   WP_181747481
VERSION     WP_181747481.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 659)
  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 659)
  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..659
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..659
                     /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=76109
     Region          417..635
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mdtkskgkft plvalivsfy llalpflvti dvlnnipqls kdyyfttndf grdvnrfsdl
       61 lvrrfvdfkd yekkpfaeqa eefkrtkfrl sildntfhyh iqdqqtkdvy enidktptee
      121 elktktlfya kfpmlnppdn ledvnylfkh fdwwgyitvp ltlneenlel kyytyflssr
      181 drlmneclvg lasligiisi giylfkqkni tvlllekmar vlrcipidir ifllaivcit
      241 tiislnrtsf fylqpgivhv lvltgfallf ayiilhiyea cyilnnreql qlqwqksflh
      301 qlkilyqest lyksllfkvv llailsagfg fscllifwgi rgmvdirrip vicgffyslf
      361 yllfvvpltl rrigalnkim kateyiaagq lslhieepka gnfkelvqnl nnmreglkks
      421 ldsqmksekl ktelitnvsh dlrtpltsim nyvgllkqdt ltpeeskeyl nildkkthrl
      481 kvliddliea skvasgavem hveqvdival ldqalaeftd kipasglifr lhvdqpkilm
      541 hvdgkktwrv fenlisnvik yslpntrvyl slneeadrvl ftiknvsaye isyevselfe
      601 rfkrgdqsrh tegsglglai aksimdlqgg elhididgdy fkvtaifpkq irhevksqs
//
LOCUS       WP_181747501             280 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Bacteroides fragilis].
ACCESSION   WP_181747501
VERSION     WP_181747501.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 280)
  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 280)
  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 280)
  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 280)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 280)
  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 280)
  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 280)
  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..280
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..280
                     /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=31406
     Region          <136..277
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mdihpiqess rrwmtalila vvaagiqttl lwgyagadtl paaidgilsv gllcllayla
       61 wyviglvsil qtdlliaala llfwlvggfa vqyvleqnmg qvyapfgetl pfrilfgala
      121 wgvmmlwyrl qslntvqeei leeavsreea lreelrqiec redkalpeea ecidritvkd
      181 gthihlirtd ellyiqacgd yvtlvtpsgq yvkeqtmkyf dahlpsagfv rvhrstivnv
      241 tqisrvelfg kenyqlslkn gvrlkvsnsg ykllkerlel
//
LOCUS       WP_181747241             864 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Bacteroides fragilis].
ACCESSION   WP_181747241
VERSION     WP_181747241.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 864)
  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 864)
  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 864)
  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 864)
  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 18682358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..864
                     /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=96683
     Region          41..>596
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          605..702
                     /region_name="Glyco_hydro2_C5"
                     /note="Glycoside hydrolase family 2 C-terminal domain 5;
                     pfam18565"
                     /db_xref="CDD:436582"
     Region          743..848
                     /region_name="F5_F8_type_C"
                     /note="F5/8 type C domain; pfam00754"
                     /db_xref="CDD:459925"
ORIGIN      
        1 mnftlhtlng iklwlvllll sgainvcrad sprqtinfnr gwkycqgdfd haarpgfdds
       61 ewekiglphs fstpyfmskd fyvgygwyrk afpvkkeilg kksflefdgv fqeaeifvng
      121 hlagthkggy tgfsidisay lkegknlvav rvnncwrpdl apragehvfs ggiyrnvrlv
      181 ikpptyidwy gtwvttpnla enkgksgsvh irtdvcnasg ktdtyrlltt vvdaqgkevs
      241 svstsqvlpd natytfeqqt keiqapqlwh pnhpalykvi sslyhgqeli dryetafgfr
      301 wfewtadrgf flngehlyfk ganvhqdhag wgdavtetgm rrdirlvkea gfdlirgshy
      361 phspafsqac deigmlfwae nafwgigghk gdgywnasay pvnesdraef ensvkaqlke
      421 lirihrnhps iivwsmsnep fftapetidp mrklleetvk lskqldptrp aavggaqrpl
      481 gekridklgd iagyngdgsy ipefqqpgmp tvvseygstt adrpgeydpg wgdlaknnaq
      541 ngfpwrsgqa iwcafdhgsi agsalgkmgi idyfripkra wywyrnaykg itppewpqeg
      601 tparislvad rtdnikadgt ddvmlsitil dasgkpvsns pavkldilsg pgefptgtsi
      661 lfekesdiri ldgkaaiefr syyagetvir atspglepae vkirftgstp yteafkvker
      721 pytrfetptk tdnlqtfgpn nptfcsssvn ghssafaadg destywqase ndperswtld
      781 tekglsirhi riafpdltpy qykvevsmdr ehwslipdqt nnkqnenirm iqvvpgiqgr
      841 fvrisftgek aaitdvqvig tvid
//
LOCUS       WP_181747529             336 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Brevibacillus halotolerans].
ACCESSION   WP_181747529
VERSION     WP_181747529.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     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=35239
     Region          30..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 mgksilerpf vkaiglllgl lvllacmlvs vvygvittdi htlieaythf ngsnehivil
       61 etrvprsiia aaiginlgia gcilqaltrn pigdvgifgi ngaasfaivc svgflgansm
      121 qaltwagftg allggiavyi lgsigrdgmt plkmtlagaa ltalfssftn gilvtneqal
      181 eevlfwlags vadrklsylm evlpfmiaaw iialllapai ntfmlgedva kglgqrtlll
      241 kigmgavvii lsgcsvavag pigfvglftp hvaryltgnd mkwtilysgl fggillvisd
      301 ilaraiampq elpigvmtal fgapffiyvi rkgmlr
//
LOCUS       WP_181747594             610 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Bacteroides fragilis].
ACCESSION   WP_181747594
VERSION     WP_181747594.1
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=66703
     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 lallmavisl atvsaqaitv sgtvtdakdg tplvgcsvqi kgttkgtvtn
       61 mngqytiqsk kgetllfqyi gykqekrvvk sstldvkmka delvleecvv vgyghelrat
      121 ksmstaymav cpasgimyna vnaeeygeiq engfknvsda plstfsidvd aasysnmrrf
      181 inkgklppvd airteelvny fsydypkptg sdpvkitmea gtcpwnadhr lvriglkake
      241 iptdnlpasn lvflidvsgs mwganrldlv ksslkllvnn lrdkdkvaiv tyagnasvkl
      301 eatpgsdkqk ireaidelea sgstaggegi mlaykiaqkn fisggnnrii lctdgdfnvg
      361 vssdkelekl ieqkrksgif ltvlgygmgn ykdskmqtla ekgngnhayi dnlqeanrvl
      421 vnefgatlht vakdvklqve fnpaqvqayr ligyesrlla dedfnndtkd agemgaghtv
      481 tafyeviptg vksdfagkid dlkyqkkqkp stplnesdel ltiklrykap dsntskkiel
      541 plidhksnrv sadfrfaaav amfgqllrds efkgnatydk vislaktgle nnekgykref
      601 irlaetaksl
//
LOCUS       WP_181747775             257 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Brevibacillus halotolerans].
ACCESSION   WP_181747775
VERSION     WP_181747775.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 257)
  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 257)
  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..257
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..257
                     /product="LolA family protein"
                     /calculated_mol_wt=28956
     Region          64..247
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 mkkkmiavvl vgatlvatga yaqeavydky vktnvydatg kvigqtrags eslpevknsk
       61 ltmdqvyeel lkkmemvply keitvkreqq gkvvtstake wyspldrgyr ieekdhtgvv
      121 tysvfngtss lsyregtksa seitaapdqk vvnndvfylr elknnhklqf lgeetinnra
      181 tyhimaiptq kddlqvelwm dkdtgvamks ittvfglqgi tevtkldfyp aftkelftlt
      241 lpsdvkvykd mqfdpqk
//
LOCUS       WP_181747830             344 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Brevibacillus halotolerans].
ACCESSION   WP_181747830
VERSION     WP_181747830.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     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=36188
     Region          35..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 mqsvtatkte rlkskhgfta iailsilivi afifsmntgf irlsplellq tlfgagtdkq
       61 nlilfefrlp rivislliga glavsgcvmq gisrnaladp gilginagag lmvmlfisfy
      121 pttaaapifl lpvlaligag ltaaliysla ykryeglstt rlllsgiava agisaamivl
      181 tlkispekyq fvatwlagsi wgtdwkfvls llpwillllp yvyykarvmn vltlgeqaav
      241 glgvsvsreq laliatavgl agscvavsgg igfvgligph larrlvgprh qiliptaala
      301 gallvitadt igrwmlqpse iptgivvavi gapyflylla rska
//
LOCUS       WP_181747918             801 aa            linear   BCT 28-DEC-2024
DEFINITION  GumC family protein [Bacteroides fragilis].
ACCESSION   WP_181747918
VERSION     WP_181747918.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 801)
  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 801)
  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 801)
  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..801
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..801
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=88260
     Region          11..763
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mkedlyddly eekeekidfh allfryvirw pwfvasviic lagawlhlrq ttpvynisas
       61 viikddkkgg nsggnlaale glglvnsvsn idneieilrs ktlvkhvvse lnlyttysvk
      121 gsfnevelyk sspvlvgltp qeadrlpgpa vfeltlspgn rldvkatvge tsynkkfskl
      181 pgllvtpagt ftftlagdsa gvsepqtlta vvsnpmqtak ryaaalsvep tsqttsiviv
      241 slkntnkrrg edfinrliev ynrntnndkn evaekteefi agririinde lfstekelet
      301 fkrdagltdl asdaqlavse nsayekqrve ngtqlnlvry laeyisapdk inavlpvnvg
      361 ltdqslssli gqynemvlqr nrllrnsses npvivnldsg iramrenilt tihsvqkgll
      421 itkaeldrqa skfnrrisna paqerqfvsi srqqeikagl ylmllqkree nsialaatan
      481 nakivdeama dngpvspktk tiymialvmg mgipvaiiyv mgllqfrieg radvekltsa
      541 piigdiplae egngkaggia vrenenslma etfrgirtnl qfmlgeenkv ilvtstisge
      601 gktfvatnla islsllgkrv vivgldirkp glnkvfnlsq kekgitqfla gpqttdlmsm
      661 vqpsgisrtl silpggtvpp nptellarqa lveaidilkk hfdyivldta pigmvtdtqi
      721 iarvadlsvy vcradythka dytlledlrl gnklpnlctv ingldmkkrk ygyyygygky
      781 gryygygkky gygygygqkh n
//
LOCUS       WP_181748028             418 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Brevibacillus halotolerans].
ACCESSION   WP_181748028
VERSION     WP_181748028.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 418)
  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..418
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..418
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46678
     Region          1..406
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 miqtytcang vrivtekias vrsvalgiwv gtgskyeneq nngishfleh mffkgtttrs
       61 akeiaeafde iggnvnafts keytcyyarv ldrhaplaln ilsdmyfnsv fdaeelekek
      121 nvvleeismy edtpddlvhd liarasyadh slgytilgke dvlkgmkred lltyieqryl
      181 pentvitvag nfddelitlv qslfstyqra gktmdiatpt ftgqsivhqk qteqahlcls
      241 mpgyavghdn vysliilnni lggsmssrlf qeireergla ysvysyhssy kesgtfniyt
      301 gtapehvgkv fdivsnvlhd vrtngiteke lnkgkeqlkg slmlslests srmnrlgkne
      361 llhgrhltld eiiakvdrvs qesvlavake lfhskmamam vspleafpen vdanvflt
//
LOCUS       WP_181748138             320 aa            linear   BCT 28-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Brevibacillus halotolerans].
ACCESSION   WP_181748138
VERSION     WP_181748138.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     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=35013
     Region          5..312
                     /region_name="GDH"
                     /note="D-glycerate dehydrogenase/hydroxypyruvate reductase
                     (GDH); cd05301"
                     /db_xref="CDD:240626"
     Site            order(11..12,14,54..56,76,104..105,108..109,111..112,115,
                     119,121,129,131,133,135..141,143..147,165..166,169..170,
                     268..269,277,283..289,291..294,296)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240626"
     Site            order(55,77..79,102,239,287,290)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240626"
     Site            order(78..79,106,177..179,182,209..211,215..216,237..239,
                     263..264,287,289..290)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:240626"
ORIGIN      
        1 mttkpfvyvt rkvaeeamnl latiatvevw dqeypvprdi llekakrsdg lyvmlsdrid
       61 reiidvaphl kvistlavgy dnidleacke kgivvtntpd vltdatadlt fgllmaagrr
      121 fieanrvlmn gewktwspyf magqrihgat igiigmgrig eavakraagf dmrilyhnrs
      181 rrveaeqtyg atycslpdll cesdyvvllt plteatkglm gaeefammks tavfinasrg
      241 atvdeealyq alkqgtiwaa gldvfgqepi ptnhpllslp nvvalphigs atyetrdrma
      301 mlvsenlvav lskgeaitpv
//
LOCUS       WP_181748238             409 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Brevibacillus halotolerans].
ACCESSION   WP_181748238
VERSION     WP_181748238.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..409
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..409
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=47354
     Region          103..408
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mqqnlfeqyq hsdideladv igellqnpit iedldhrlia ysshgdstdp arwstimgrr
       61 vpetvlarlw kdgvfqqlfs qkdpvhipek keiglgkrva iairrgndil gyiwaqevnr
      121 altswddeil rqaakeavpr llqrqgkrka eqdrqkeflw elllgghsee tklrqkainl
      181 hmkivpplmv ctievlegkg eqlhqllypl lmrdkmyslt dgsqlillmq hpkgqaated
      241 vlvtyseqfl gecmskltdk fgkgkahigc grpvcslieg rqsyqealqm nvikrlfpqe
      301 terilrfqql giyrflpqmn swnkeqaykn dqlakllyyd qenqtnltet levfldhvgk
      361 vnrtaahlhi hintlsyrlk rieeimqidl ddpnqrysly idlkvmklg
//
LOCUS       WP_181748242             231 aa            linear   BCT 28-DEC-2024
DEFINITION  3-oxoacid CoA-transferase subunit A [Brevibacillus halotolerans].
ACCESSION   WP_181748242
VERSION     WP_181748242.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02429.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..231
                     /product="3-oxoacid CoA-transferase subunit A"
                     /GO_function="GO:0008410 - CoA-transferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25179
     Region          1..223
                     /region_name="AtoD"
                     /note="Acyl CoA:acetate/3-ketoacid CoA transferase, alpha
                     subunit [Lipid transport and metabolism]; COG1788"
                     /db_xref="CDD:441394"
ORIGIN      
        1 makiyesynd mvadihdgat llvggfglcg ipenliialr dkgvkgltvv snncgvddwg
       61 lglmlqqkqi kkmvssyvge nkeferqfls geleveltpq gtlaerirag gagipafytp
      121 agvgtpiaeg retrifndke yvletaitgd falikawkad tlgnliyhkt arnfnpmmaa
      181 agkitlveve eivaageldp dhihtpsiyv qrlikapsfe krierrtvqk a
//
LOCUS       WP_181748205             640 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Brevibacillus
            halotolerans].
ACCESSION   WP_181748205
VERSION     WP_181748205.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 640)
  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 640)
  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 640)
  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 640)
  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..640
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..640
                     /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=67756
     Region          1..599
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mlqkgmmils gvcvliswlw gsiagidpaw iaivvcgvpi aitagkelwe qrslnsdvlv
       61 tiaiiaatci gellaaaeva fimmigmwle ektvakatsa lkemvemtpe qarvmrggqw
      121 ieakadsvlv gelvlvkpge qipvdgivva gqaaidqail tgeslpvekr qgdevfvgtt
      181 ntngsleiqt trvgeetafa kvtrlveeam ekrapvqrll dkwavwivga slllailvyl
      241 vtndmvrsvt vlivfcpcal vlatptaima gignaakngi liksgvaleq lgsintvlfd
      301 ktgtltkgal svagiahaeh saqevmrwaa aleqhsehpi atailhqakk welelpaves
      361 fimhagsgie gvvegkriyv gnpsfmkglg igleqvqgll ttkekegktn iliasehkll
      421 glisvsdqlr pearetvetl aeagvevavv tgdnkgaaqf maeqlgitqv yaeqmpdmky
      481 mqverqlkag rkvamigdgi ndapaltlad vgismgvhgt qiaaqasdvv lmsndlrkia
      541 dvmrlgqkav qvirenliis tainsaaill allgvlgpvf gafvhnitsv lvvlnsarli
      601 gflstpknsr pssphhgahs sagyatdtgk lqsinkfvgl
//
LOCUS       WP_181748434             251 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Bacteroides fragilis].
ACCESSION   WP_181748434
VERSION     WP_181748434.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
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="Bacteroides fragilis"
                     /db_xref="taxon:817"
     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=28957
     Region          1..247
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mykviiidde kaaietlrrd levqadleik gtagngakgk klimdihpdl lfldielpdi
       61 qgirllseir eqvlwdmkvv fytaydkyll qalresafdy llkpydieel nliieryrkt
      121 mvsaqplpsf asavgtlmpg rdlfmistvt gfrflrleei gyfeylkdkr lwqvelfnqt
      181 klclkkntta gdiigysdvf vqisqsaiin inylamiksk qcllyppfsd kedliisrgf
      241 lkelqerfci i
//
LOCUS       WP_181748740             516 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Brevibacillus
            halotolerans].
ACCESSION   WP_181748740
VERSION     WP_181748740.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 516)
  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 516)
  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..516
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..516
                     /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=57891
     Region          14..512
                     /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 mstsrlmdgt tflamvahil demnegvhvi dadgtsilyn rkmaelegmq kedvlgkkll
       61 dvfqfspgqe stllqalhkg eslrqirqty lngkgqeitt isntlplqqh gknigaveia
      121 ndvtkmermi renyfvkkem gntrytfasi ignspairem iehanrvart sssvlivget
      181 gtgkelfvqs ihnasmraks pfisqncaal pdsliegllf gttkgaftga ierpglfeqa
      241 eggtlfldel nslnlslqak llralqekti rrigdtkdrt invriiaain edpieaisan
      301 klrkdlyyrl gvvtllippl rerredippl vthfiekynr lfqmdvvgit edvqrffgdy
      361 dwpgnvrele hfiegamnlm ltdetsiald hlplhhirrk lpgstsipss pafegqeqkg
      421 idhkeaplss ipssraystg ttntqpilhe symkdtlhll qqdslslkev lqsfeaiylq
      481 kkldqfagni shtaehigms rqslqyrlrr lqqenh
//
LOCUS       WP_181748826             229 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Brevibacillus].
ACCESSION   WP_181748826
VERSION     WP_181748826.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus
  ORGANISM  Brevibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 229)
  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 229)
  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..229
                     /organism="Brevibacillus"
                     /db_xref="taxon:55080"
     Protein         1..229
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=26500
     Region          63..197
                     /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          63..89
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(65..66,69..70,72,96,108..109,112..113,115..116,139,
                     142..143,146..147,150)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          94..133
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          138..161
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          172..197
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mhyfqmtlpa tltglavvlf vgllrlqwpf ryyyrtllck rnpermqtil easylknkkr
       61 svalldkssq qllqgkydaa esyitqaiil ckesptlfhr allqhlfynl avacyyrgry
      121 rdalqigihl ykrdprmhsa lgviiccqar mgdlpaakha lsllqrrrir palqyfclae
      181 ieaaagrytl avehiekirn yaysqtlflr keeldlrlqe wtkaashag
//
LOCUS       WP_181748288            1051 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_181748288
VERSION     WP_181748288.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1051)
  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 1051)
  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 1051)
  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 1051)
  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..1051
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1051
                     /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=116871
     Region          30..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikkhilip lmvlllfgsm damaaieqai qvkgkvvdni gepviganvv vkgtttgvit
       61 sidgsfaida vkgstivvsf igylsqevkv tgnflnitle nntelldevv vvgygvqkka
      121 nltgaiatvg akeledrpvt naaaalqgkv anlnisngdg gpgkkasfni rgyagldaty
      181 splviidgvt gyfddlnpnd ietltvlkda aasaiygaqa aygvilvttk sgkknektvi
      241 nynnnfsfns ptvlpktags lefsrlfrea dingggsgii dletmeriek yyydptsipn
      301 nvpqrdnpdr wadwgdgrsn anedwqkamf knnqlnqqhn isirggsdkt tyvmslgylk
      361 degklryydd hyqrynalak ittdvmkwlt vglnvryshe ksvspaygmn pggsvndmig
      421 wtqvvwptip vrdpnghfsp agrmvfiada npqtsytdnf wgtanvvikp lkgwtinadf
      481 tynkwmnkrs yskgliysys vsnepylegg fgtedtrvwq esnnddftsm nayttyekef
      541 kghnfkimag mqseykknfg lyankmgmvl pgqpsistst gkieawdsld hyatlgffgr
      601 fnydyksryl fefdlrrdgs sryakghqwg tfpafsagwn vakeaffepy tsilselrlr
      661 gswgelgnmr gknyqyistv pynattdyim gdkrisafga pnmiayntwe knrtldfgvd
      721 iaalnnrltm sfdwyrrdii glitkgvtlp avlgvnspdt nnadirnegw eltlgwrdqf
      781 slasksfnys vsfnlsdyqg tvlkysnpkg liydyyvgkk mgtiwgyttd himtdpaeak
      841 aindsgvqnk fggdwvvgdi kyvnldddpn indgnqtled hgdlsiignd tprynfgfgf
      901 nadwngidfs mflqgtmkrd lwlegpvafg lgggqwgsnv wkntldcwre dgsnpdpwlp
      961 rlylwstskn lqkqtrymdt gaycrlkniq lgyslpgaii nkvglekvri yfsgdnlltf
     1021 sginenfdpe apwggaypis ksisfgvnvt f
//
LOCUS       WP_181748813             242 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Brevibacillus
            halotolerans].
ACCESSION   WP_181748813
VERSION     WP_181748813.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 242)
  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..242
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..242
                     /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=27866
     Region          1..241
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mhtliyahrg asgmypentf pafhaaylqg sngmeidvqv tadeqlivmh dtnvehttdg
       61 vgevrhltye qiyrlnaaak srkyypptkv pelsdvllfv kttglrliie lknfivpqpq
      121 leehvirlih dlrlhkqvvi ssfnyhslfh vkeldpqirt gmlyfgqlhk pweiakqfra
      181 delhapeeqv nkallqaarq hhlsllawtv ntpermqelf slqidgiitn ypnvarkyln
      241 kk
//
LOCUS       WP_181748116             444 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Brevibacillus halotolerans].
ACCESSION   WP_181748116
VERSION     WP_181748116.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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   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 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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..444
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..444
                     /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=49601
     Region          19..409
                     /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(29..30,33..34,37,70,120..121,123..125,128,148,
                     151..152,155,263,266..267,270..272,275,303,307,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mklrhplkkn gthryhitiw irmfgafits lsgsmlapfl llylhdklng avlvpmlivg
       61 lqpltdimvt llgggitdrl grkpvmllal imqsiamagf mladsilsfa llymlhgagq
      121 slfvpaqraq iadvttesqr vevfgllnti sytglalgpv ggmllyqydp twlfgieals
      181 ifiymlvcww klpetapvsa tapfsssdqv evsetaeket rsserigvsh askgtgkhry
      241 fsfhrmtali trykhvlklm iytlpisffy aqtetsfriy lqesfvnyvs iiatlstika
      301 ilavilqlpl vklterlsfq rvmllscscf mvtaaaygfs ksilvlilvq lswtvgetig
      361 ltrlhtyisd iappeergry fslhgihwdi srtfgpflgg vmlltfggei lfsiclilll
      421 lsgilffrsp nfhkltrqdv dfrk
//
LOCUS       WP_181748886             647 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Brevibacillus halotolerans].
ACCESSION   WP_181748886
VERSION     WP_181748886.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 647)
  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 647)
  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..647
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..647
                     /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=73202
     Region          <96..198
                     /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          220..>440
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
ORIGIN      
        1 mrkksfqrwi avfamattli ssvnpvfaan ydeekisvng dttataygmd fdgdyavwve
       61 esgknysvvl ydvddesiak kissnsskkv apriegntvv waqeeksgye lyaydlkknk
      121 ervltnqhar vtdpeeiafk dgvvawkdkr dggtniyale vrndkeyris tggkashpsi
      181 yddqivwqde rngraelyqn kvgsskefkt ywgkaktakp iisdddivyl neasgniekt
      241 qvesskskvl thekgdeelf dfngrylvyg sgstlyyldt nkddlvkinn dfnrklppvm
      301 sgryvlyatg ktnnltlklf dtkkeksqtl gkdeniknma spaasknyva fvkegkresr
      361 vmlynvkdrk titispekhe aehpvvsdsy vvyydnddra lvsydietge stkittkktd
      421 vveglyaiyk dhlvwvsggk rsntvnltnl kknktselhd sklgvrsvai nnqavalidg
      481 eddryqdivi ydyvdggrim keeaesakgi glgdkfaaws aynsdtkskd ifvysfklnr
      541 tdllyeeegd qenpivsnni ifyetevekg gdavdkyvmy drdkhrfrap fgsdadpsei
      601 aiggnrlvwl ddrddeegly tsvlgssddd dddddydddy dyfygkd
//
LOCUS       WP_181748526             273 aa            linear   BCT 28-DEC-2024
DEFINITION  SPL family radical SAM protein [Brevibacillus halotolerans].
ACCESSION   WP_181748526
VERSION     WP_181748526.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 273)
  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 273)
  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..273
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..273
                     /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=31538
     Region          6..>206
                     /region_name="SplB"
                     /note="DNA repair photolyase [Replication, recombination
                     and repair]; COG1533"
                     /db_xref="CDD:441142"
ORIGIN      
        1 mkseffykyp ktllnkgtgf lsdythslnp ytgcsfgcsy cyvrqmpvsi frreewgtwv
       61 dikreaanvl rkelrreksk gkvtifmsss tdpyqpiehk ekvtrsllev mlenppdflf
      121 iqtrsplvsr didlllrlek kvrvsmtiet dredirkhft phappiparl ealqrladag
      181 vptqatiapl lpsseefpdk lrtlvdcici ddyfmgdgsg grrtrnlgid sfyhklnave
      241 wyhpsayqlv yerftrvfpt dqvflsqkgf apy
//
LOCUS       WP_181749025             141 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Brevibacillus].
ACCESSION   WP_181749025
VERSION     WP_181749025.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus
  ORGANISM  Brevibacillus
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Brevibacillus"
                     /db_xref="taxon:55080"
     Protein         1..141
                     /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=15693
     Region          <10..140
                     /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 miwpsqklny kvskttrlll dsigvvgvfm llalindtnk fddslyrggf lklsfitaav
       61 iavlvhsasr vgnfigckpl rwigvrsysl yiwhfpiivl ssspvntega silrivlqla
      121 asfiiaaisy kyieqpfrrl e
//
LOCUS       WP_181749104             456 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Brevibacillus halotolerans].
ACCESSION   WP_181749104
VERSION     WP_181749104.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     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=51281
     Region          <167..455
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkhkgmkrql flshlgvalv sllviiiivn isvsitfgky venqlkaead ailqdltesy
       61 vkanewsrqt lmgvghramq rdmtvilldv egnviwdltk mgmhmerqgt khscavddkl
      121 phstystpii igdqqvgmlh vglpdgqfqe qerefitrfn gmvggalliv ivgvyyysvr
      181 isrgishpll hmkekanrmr tgdltarvet dtlhgeiqel gqavnhlaes lqkqerlrkn
      241 ltadiahelr tplatiqsym eafedgiwep tseklqicqe qtsqlvllik dleklteaen
      301 pmlrlqkqqv nlpaiiaeaq ksiaelwdkk riryvppftd nifvhadyrr llqvftnlls
      361 naykytpedg evsvaievqq snivinvadt gvgireeelp yvferfyrge ksrsrksgga
      421 giglaivkai ieahggevrv eskvgkgttf lvrlpm
//
LOCUS       WP_181749266             338 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Brevibacillus halotolerans].
ACCESSION   WP_181749266
VERSION     WP_181749266.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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..338
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..338
                     /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=37997
     Region          5..334
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mstdvyiltg ylgsgkttll qqllaylrdq ssnvvvmmne mgeedvdgeq vegfgfpvkk
       61 mlngciccsi rgeltenvke imqnikpehl iiettgvadp ievvdamthp elydrmnvkg
      121 iinvidasry leltsffqag galiktirnq vkyadlliin kvdlvdedil tkvktklqet
      181 nshapihvti rtemdlekll qvkrlaqsre msnspsipvq ktigrfspld klkqtlglkt
      241 nqpslfhsid tfsyhfkgpv daeafedfly dlpktiyrak gyvqfigqdd lisfqqtqtq
      301 vhlfpfsnfg pkmvavfige gidkdniiea lekcyrts
//
LOCUS       WP_181749195             548 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Brevibacillus halotolerans].
ACCESSION   WP_181749195
VERSION     WP_181749195.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 548)
  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 548)
  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 548)
  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 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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..548
                     /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=60774
     Region          63..171
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrisklyhav icitltssll lpipmfstka laaapaptlh denphgafgd wytgaippna
       61 sldkpvilfv qglhatykkf yrdgglyeaa ynsgyrtafv qlrdadgdgg nmytngekla
      121 evikkvadyy nvkqiaivah skggvdtqaa lihygaapyv htvhqlatpn kgseladlay
      181 sswfswlaei lgkkddavys lqtsymanfr kqtdnhrdin ktrtymaagt gddgiftkyw
      241 fahavlpged dgavtvdsaf glpygiktfk knishtaitd akhvwseves nirksskelq
      301 pnfapeldre yqlneeentp asivsntivr ggkikgktqd tfllesgvsq mmvdvmtane
      361 ktkvklisps gkeytpkrlg dsdfdsetdv dgdetqelfa saihhgfkid dpekgkwklv
      421 asgkndayfm faqvesdqpm evvsekkiye pgergeirve lpeatikkqa ianvsmvetk
      481 nrqllaaedy lkikekndei qgtfkaprep gvynicleit gvnefgeefs rsvwynfavi
      541 dedaeeel
//
LOCUS       WP_181749291             790 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Brevibacillus
            halotolerans].
ACCESSION   WP_181749291
VERSION     WP_181749291.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 790)
  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 790)
  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 790)
  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 790)
  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..790
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..790
                     /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=89274
     Region          9..787
                     /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"
     Region          <125..>183
                     /region_name="modC"
                     /note="molybdenum ABC transporter ATP-binding protein
                     ModC; PRK11144"
                     /db_xref="CDD:182993"
ORIGIN      
        1 mqiepeqqrk kdpeivfrvn imflavficf vvvilrlayv qvvqgelfaq elekyslkel
       61 pipaprghil drngvvlvdn kpvftvkfmd rpeekinker vaeelatlld wkqeergddk
      121 kladlgiqlq asfpiilsfe qrqrlrtqiq tkldalplpe kmellqsvel lrlakevhip
      181 ikyaftdver tkalellrkk tgkilsyeqg andrvllgel lqhqipfpyh lekkqsddla
      241 rkikssieil ratpvtkqsd rklienarff fldvnlglse iqreqtwrkl lvlermvgmg
      301 vpafmprqik rnitaaedar ieerlaqlpg vyveveplrk vktdanggpl athilgyins
      361 idprfvkeyk skqysgnelv gvaglenyye sqlrgktgam tvqvnrnsef vnetikrvae
      421 pgndliltld wrfqdkveei lhknlsqknl kvghavvmap dtgeilalan ypdydlnlyy
      481 dretfskvyk tdiwpyednk itrgayapgs tvkpisvmla lqeglvtpse tiidrggllv
      541 gnrfknnwlr sghgavdarr alqvsnntym yemglrlark gnregkhyse qfnvldyyns
      601 qfglgvktgi dlpgektgyl andkylgnlv dafigqynsf tpmqlcqyvs tianggyrik
      661 phlvkeirkg asnpteritl tkvepyvlnk vdidpkwikv vqegmakvtq pngtayrnfk
      721 gfpfpvaakt gtaqtggnad nalivgyapv knpqiafavv vpggghgadm sgviakqile
      781 eyvkmygieq
//
LOCUS       WP_181749166             384 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein
            [Brevibacillus halotolerans].
ACCESSION   WP_181749166
VERSION     WP_181749166.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 384)
  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 384)
  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..384
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..384
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42120
     Region          8..380
                     /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 mfkekitlri pgptpipprv qqamnrpmig hrsgqfsqml sdvvekikpa fgtaqqvyvi
       61 agsgtsalem svvntlqagd eaivtisgaf gerfakicer yqikvhrlev awgeaitpel
      121 lqdflvqhpm akavfatyce tssgvlnpip elsrvvkkhs nalfivdavs clgavpcemd
      181 ewgldivvtg sqkafmlptg lafiavsqqa wkrieqitpq afyldlkayr ksmadqttpy
      241 tpavslvfgl eevvamldee glpqvfarhe lmknmtraam ralglplmte deyasptvts
      301 vdpgdlfdae elrkilrtky nvviaggqqh lkgrifrigh mgycdpqdvl tvislievsl
      361 kqigyeitlg agvraaqevl iqhg
//
LOCUS       WP_181749398             295 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Brevibacillus
            halotolerans].
ACCESSION   WP_181749398
VERSION     WP_181749398.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     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=32480
     Region          2..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 miwfivnras gngkghkvwk yverlliekn ikyqvafter prhaieiaks iskqngtnvv
       61 iaiggdgtvh evanglvgse iplgsipags gndfarglqv pkqsnkalek alygkkrkid
      121 ivsindevfi naagmgfdgq vakvtnqaky kkwlnhlglg kfcyivsffk vlflyratev
      181 sividdreqt fsdvwliava nipfygggmm icpnakcddg ifdvcivhgi srwklvkllp
      241 rvfrgthifn raittltgkq ltimstspmi thgdgeivge tpiqltikke glyiv
//
LOCUS       WP_181749417             365 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Brevibacillus halotolerans].
ACCESSION   WP_181749417
VERSION     WP_181749417.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     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=39080
     Region          41..358
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mqqttttapr svnsigtqyt knwiaklmgs gvvlflsltv aimlgpvqid pvivwkvigs
       61 hvpfvqqwvg tdvsnaqmhi vwdirlprvl lsavvgagls ivgiaiqali rnpladpyil
      121 gvssgasvga tavllfgslg vfgsyalsla aflgalasvi lvfllslvgg rvqlirllla
      181 giavsimlsa ltsffimlap raeslssvly wmmgsftrak weslvlptia vlsffiflwv
      241 narnlnllil geetstllgl hpenmrkill itislvtgll vavsgsigfv glmlphifrl
      301 wvgsdhrrli plcacggaif miwadvlarl iiapeelpig ivtalcggpf fiwmlrrray
      361 tfggs
//
LOCUS       WP_181749470             357 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Brevibacillus halotolerans].
ACCESSION   WP_181749470
VERSION     WP_181749470.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     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=39387
     Region          6..355
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mshrleklra vlkeqnvdal iiesevnrqy isnfsgstgw vivsldqakf vtdfryieqa
       61 tnectgfevi nnkrqalpti kqvlqdmkva kvgfeaehts yatfeawkqk ldhvelvatk
      121 glveklrlyk deaeiaimrq aaqlsdaafa hvikmikpgi reidvasele yyirkhgakg
      181 sgfdiivasg krgalphgra sekvieagdm vtidfgahyk gyhsdmtrtf avgepdpkmk
      241 eiyeivlrae legvnrvevg mtgkevdalt rdiikeagyg dyyghaaghg lgmdvheapa
      301 vsmlsdtvle pgmvitiepg iyveglggvr ieddvvlten gieilnktpk ellilpv
//
LOCUS       WP_181749482             104 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Brevibacillus halotolerans].
ACCESSION   WP_181749482
VERSION     WP_181749482.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
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="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     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=11088
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mgwlfvflaa ifelmgvigl krfstnktli ntalffggfg asfaflytal qylqlsvaya
       61 vwigvgtaga vlvnmiffne srsigriisl iiivigvtgl kavs
//
LOCUS       WP_181749831             135 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Brevibacillus halotolerans].
ACCESSION   WP_181749831
VERSION     WP_181749831.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..135
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..135
                     /product="YybH family protein"
                     /calculated_mol_wt=15284
     Region          2..124
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mehelkelik kcdlaikqed fdtlmnyytd dailvvkpgm iargkeeikk afiaiakyfn
       61 nsivptqgem iiletgntal vlsqtlldad kedsefsmdr raiyvfkknr qgewlcaidn
      121 sygtelinke tlkgl
//
LOCUS       WP_181749968             206 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF47 domain-containing protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181749968
VERSION     WP_181749968.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..206
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=23963
     Region          6..206
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mlfnrskdql fyqlmvdata niceavqlfr envetleeke kyaerikele skgdeythll
       61 ikelnqtfvt pldhedilkl atnlddvldg veacaarfvy mhvdkstpyl vkfaeileec
      121 arqlqdsfia lekrdyatir kisieinnle negdklmres vstlfeepvn pvelikmkei
      181 yerledvtdt fedlmdlmes vvmkya
//
LOCUS       WP_181750093             427 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181750093
VERSION     WP_181750093.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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 427)
  AUTHORS   ter Beek,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..427
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..427
                     /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=46886
     Region          27..378
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mnhwlskklt vflslllils lalaaagcta gsddgkiqlr ivtmfsgtdp atkvyqqale
       61 dfkkkhpnve itdesmtatg dpfrtkvktd ftsgnapdvt ffftgadaqs iiksgavvpl
      121 ndlmakdqew nsvltdnvkk qiiekdgkiy afpitgfyeg lfvnkdlfdk ynlelptdwn
      181 kfvkavevfk kngiipiags meesfylieh filsaggpeg hnsayqngvd psweqglnrl
      241 keiykmgafp kdantmkdad avqlfvnkka ammvngswti gqmqdkenvk vmpfpvmpgg
      301 kakpadliag ftsgyylskk syedqskkgm alelikflts kemikkfaea nggvpaadvt
      361 idglspvaae gqkmvkeans lnlpidaqis peafteirkn iayivqekkt akevleaalk
      421 veeqark
//
LOCUS       WP_181750090             147 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Paenactinomyces guangxiensis].
ACCESSION   WP_181750090
VERSION     WP_181750090.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 147)
  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 147)
  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 147)
  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 10140416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..147
                     /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=16955
     Region          4..124
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd04699"
                     /db_xref="CDD:467579"
ORIGIN      
        1 mkpykiaaka iifdqdrvli lrksaeerna kdshgwdfpg gglepsepim ealarevmee
       61 tglqvkvvap ayiydeiqee khliiikfac dqpvgelils sehesyhwvr ldqlqegafp
      121 dwmkeeirra yriytdfrgm gryvqsl
//
LOCUS       WP_181749747             591 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Brevibacillus halotolerans].
ACCESSION   WP_181749747
VERSION     WP_181749747.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus halotolerans
  ORGANISM  Brevibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 591)
  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 591)
  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 591)
  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 591)
  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..591
                     /organism="Brevibacillus halotolerans"
                     /db_xref="taxon:1507437"
     Protein         1..591
                     /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=68125
     Region          5..473
                     /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 mshiriehil venyrsfgdq ivvnfpkedy kkpvaivgyn nsgktnfins ilygitekyv
       61 tkdsftindf hkrsydnlpr ivtkinssse ikvdgsianl sgyhfleikl dgieiesaki
      121 ksfndsgqtn knysafgaak yfkifyinfh eikkeistkk tswgnlssfl akhiksivdk
      181 dtimggkkdi fkgevksste rvladsslnd flhkiqtnys inlrqnkchi efglpeyedi
      241 flemifkigl ngdmdnlvpi dhfgdgyism fvmaviqaia esnetdkclf lfeepesflh
      301 enhqeyfykt vlcglaekgh qviytthsdk mldifdtcgl irfefdeisk qtvlkynehd
      361 kflegeekde vlseiddynn yikliepnln kiifskkvll vegpndlmty keiirrkvld
      421 ltgdnkyaet ylnfkniavi phhgkitasi lirlckhlgi dyfaindfdf eddfvsklsf
      481 esidelqkse iyndeladir asnskgepls dktkramitt nwrlinessf dkihfnipkl
      541 eavlgydsnd knsagiwnti kettdfgeei fpqkleefle lnefknkdnf v
//
LOCUS       WP_181750260             306 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181750260
VERSION     WP_181750260.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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 306)
  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 306)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 306)
  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 306)
  AUTHORS   Rosinski,J.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..306
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..306
                     /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=34598
     Region          2..96
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mihikdlrsg lpifkalgse iririielll qyesfnlnel agklkltnga itphikklee
       61 sglitisttv gkhgiqkicy lsddkllvdl adrstdnlye vdikighyvh yeatptcgla
      121 tkesiigefd dpryfadpqh ihseivwltq gcleywipny lkanqqfeei qlimelssea
      181 psynnnwpsd iyfylngiel gfwtspgdfg gkkgifnphw wpphlnqygl lklvrvnreg
      241 sfidgckisg vtiediglhn kskikfkiav pahaknaggl tvygehfgny kqniiarvly
      301 sqrprp
//
LOCUS       WP_181750261             430 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181750261
VERSION     WP_181750261.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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 11447308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=49185
     Region          1..341
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 mkksviasll illicfyslt gcthsqatqs ngkteltlwt fvpqhvefyq kmakrwnelh
       61 pdrqitlkad nfpyadmhnk lllslysgvg apdladiein rfpnylkgkp qlvplndlie
      121 pvkdkvilsr feiyskdgky ygidfhvgat vmyynteils qagvdpdqik twddyveagk
      181 kvkaktgkmm ttveitdlws ywpmviqqns dfidrhgnvt ldnktniktl qflydmiekd
      241 kiaqpaprgf hhsedyyafm nkgeaasvmm pmwymgrftd fmpdlkgkii vrplpawtkg
      301 gmrsagmggt gtavtnqskh vklakeflaf sklskegnie iwktlgfdpv rwdvwdlpel
      361 napnkyteyf gsdifktlls ikdeihsphl sdkspqmnql lrsevffntl qrrsqtpaes
      421 lkavaeemrr
//
LOCUS       WP_181750318             430 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181750318
VERSION     WP_181750318.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..430
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..430
                     /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=48481
     Region          16..366
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msekvvvvgg glaglsaaar lahygyevtl lekapklggr aitiplkgfn fnfgahaiya
       61 rdksvlrkfe seihlhvdwk dfsaskafyd mgsyttpmpa tleglyrtki ldsqnklrfa
      121 yevfktmasi ergedgvpig eylqkepeqv rdllltvass nfftnepeki psplffeyyk
      181 rlfsthravs yigggwqaiv nsfaeiiekn ggkivpkekv tgldwngnri tavhgkeqty
      241 eadtfifcip pkelcnlfsd tpqqkyfdey sryaatqvvv ydvglkeria spftyvyqka
      301 qrvfitdisy ydttcvpegg qlmqavayln eeeiangkad ekigiietvy dkhfpgwrdr
      361 lvakrvskka tvqeikcidd qrlmpvkfys lpnayfagdw cqgegqlsel sfssayevts
      421 riikhpieea
//
LOCUS       WP_181750596             339 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181750596
VERSION     WP_181750596.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=36461
     Region          1..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 mktlvwtgpn tmkveqqdip svqqgevlim vetvgicgse iegflghnsl rkpplvmghe
       61 fcgriaklge dagsfsigsk vvvnplihcg qcdrcrrgve nlcdnreiig ihrpgafaey
      121 vvvpassvtv vpedlnsnra slaeplaccl ravrrvlsiy pfanvliyga gaigllsglv
      181 akilgankvi ildlnnerlk tvqqagidfv inpktedvpa riskiagekg idviidaagf
      241 lptrtqafel inpggvimni glgidetplr inhlirseit vlgsfcytrq dfhdavqllv
      301 dgkiseegws etrpleagqd afseivagka teskiflqp
//
LOCUS       WP_181750615             144 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Paenactinomyces guangxiensis].
ACCESSION   WP_181750615
VERSION     WP_181750615.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 144)
  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 144)
  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 144)
  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..144
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..144
                     /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=16560
     Region          10..144
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04683"
                     /db_xref="CDD:467566"
ORIGIN      
        1 msenrftapv tihlffiqdd silllrrynt gyedgnysvv aghldggetv kqaavreake
       61 eagvqlkeed vemvgvmhrk agdervdffa vvrnwegeiq nlephkcddl rffpfnelpa
      121 nmipyilrav nnykegrwfd sygw
//
LOCUS       WP_181750899             351 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenactinomyces guangxiensis].
ACCESSION   WP_181750899
VERSION     WP_181750899.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 351)
  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 351)
  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 351)
  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 351)
  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 351)
  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 351)
  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..351
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..351
                     /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=40919
     Region          21..345
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkqavriflr ermgwitlvy vnlglvflli alvlsfektq meiikqeigy gllfstvlll
       61 lflviqfwrr fpyyrvlqkg ayhvetvddf aewgetgsde rklvtdvvqn lyrlavaerq
      121 qfqearkqhl efinlwvhqm ktpvatlslf tqqtkgmtne ererlkgmee eieklnegld
      181 mvlsmarltd faidyqirpv slmesvrdvi qtkkkqfirn gifprleaee kdwtvltdpk
      241 wnrfvidqiv qnalkyasqv nqrsyvhigl qydekmitls irdegpgipa hdlsrifhpf
      301 ftgengrkya qatgmglylv kkvldqlnhe ikveskqgqg ttvcikykkp s
//
LOCUS       WP_181751145             124 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181751145
VERSION     WP_181751145.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=14530
     Region          8..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mssqpkhdif qaiadptrrq llrlladkel pvtviskhfp msrtavskhl rilseaglvg
       61 eqkvgrekry rlqaepliel kqwlsfyerf wenkismlkh fveneetadr klvtsdrnkr
      121 esee
//
LOCUS       WP_181751042             408 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Paenactinomyces guangxiensis].
ACCESSION   WP_181751042
VERSION     WP_181751042.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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   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 408)
  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 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 13023665
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..408
                     /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=45650
     Region          14..389
                     /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..145,148,223,226..227,230..232,235,263,267,316..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 mkgflrefhp ivsvllfgnv finlfksmsy pyfaiylagr teldikvigl vigigaftgi
       61 igsfwggyvs dvigrrkmml lsllisgvvy mgytwiksey livifiiigg ffislfepvs
      121 kalisdmtpp dkrlrafsyr ytgtnigyav gpllgsfmgi tgnampfllm aiayfiylli
      181 lqvllkifgi qkieeesieq ihlkqvwkai rsdfalqyfi aggilstivy glwsvplsiy
      241 ltnqveqgek lfsillsvna atviflqpll arkmekispf llimagsalf algeigfgmt
      301 amwwvfifsm lifsigeilv ipseymlidq itpngmrgsy ygaqsfiglg lvigpwlsnl
      361 ildlfgaktm flimafiais silfywrgmh hskmnlrnhp lqkakatr
//
LOCUS       WP_181751224             335 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181751224
VERSION     WP_181751224.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=35524
     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 mtnsaqlkrv rltmisalvl llalfvisva tgyislspaq lgrtilgqgt grenlilfgf
       61 rlpriiitil agmglavsgs ilqsitknpl sdpgvlgina gaglmvvfyv mlftaesthf
      121 lyvlplfalt ggiltaaiiy imaykkgkgv dparlvligv giaaamygai ftlttrlere
      181 endffanwma griwgddwtf vlvllpwill lipivfaksn vlntlnlden vsvglgvhvk
      241 rerlilifia valssasvsv sggiafiglm aphiaralvg prhqgflpia amlgaillla
      301 adtlgraild pggipagiiv tiigapyfmy lmakk
//
LOCUS       WP_181751290             104 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Paenactinomyces guangxiensis].
ACCESSION   WP_181751290
VERSION     WP_181751290.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=11271
     Region          3..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mdwvflilag vfemvgvtmi nrfhresnwq slvlllagcg asflflnlam ktlpmgtaya
       61 vwtgigasgg ailgmvlyge skdwrrilfi imvlgsavgl kwis
//
LOCUS       WP_181751272              77 aa            linear   BCT 28-DEC-2024
DEFINITION  indolepyruvate ferredoxin oxidoreductase subunit alpha
            [Paenactinomyces guangxiensis].
ACCESSION   WP_181751272
VERSION     WP_181751272.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..77
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..77
                     /product="indolepyruvate ferredoxin oxidoreductase subunit
                     alpha"
                     /calculated_mol_wt=8589
     Region          1..63
                     /region_name="IorA"
                     /note="TPP-dependent indolepyruvate ferredoxin
                     oxidoreductase, alpha subunit [Energy production and
                     conversion]; COG4231"
                     /db_xref="CDD:443375"
ORIGIN      
        1 mpyvitspck dekaaecvev cpvdaihgdd vqyyidpntc idcgacepvc pveaifqeel
       61 vpekeqdyir inteffe
//
LOCUS       WP_181751380             255 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181751380
VERSION     WP_181751380.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..255
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28538
     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 mkslslyvdr dsfvhnidpi skiwfiifsi avpvilptip vsfvcmmitl sllllakvfk
       61 qaipvygfif lilstviiiq glfnegnetp lyhigplify regflyglli slrvinitga
      121 fmllvlttkp sdlvealvrk glsprlgyvl hsvfqiipqm asamrtimda qrsrgmeteg
      181 nlivrikafl pliapvvfhs lintkerala levrgfqssg kktflneekk spyswpiqwg
      241 liciivaaig wrmia
//
LOCUS       WP_181750819             492 aa            linear   BCT 28-DEC-2024
DEFINITION  FGGY-family carbohydrate kinase [Paenactinomyces guangxiensis].
ACCESSION   WP_181750819
VERSION     WP_181750819.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 492)
  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 492)
  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 492)
  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 10167383
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..492
                     /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=55440
     Region          7..443
                     /region_name="ASKHA_NBD_FGGY_YoaC-like"
                     /note="nucleotide-binding domain (NBD) of Bacillus
                     subtilis sugar kinase YoaC and similar proteins; cd07798"
                     /db_xref="CDD:466804"
ORIGIN      
        1 mgmqagylif digtgnarvv vagsdgtiha veredlpykr dhhypdslyf epealwqqlk
       61 rmakkavels snvkikaits tsqrqgivlf dengnhylgl pnidnrgkay eariadldti
      121 yqqvgrrptt lfsalkltav kheqpdlwhr fkaftsisdw vtyllsgelv yehsqatetl
      181 lydvrknews lslcdtfgip vdklpplvds gsilgklkpe yvsewnlgkd vavivggadt
      241 qlaikgtnpl indyvivsgt ttpvtkvmde yrfdceqrtw tnghvekgqw ifetncgvtg
      301 lnyqrlkaif ypnedysvie keineledfs ciatlgsils deqeplktgg fvfetpvshe
      361 lkrahfalas lgdiacsiae nyrvlhdvtg depeyiwgcg ggfqsktlrq llanllqkei
      421 rirkgyrqss vsgailicne ilgieaaian dfevtnlned driakwfekw kwarktlrnc
      481 kqditqkrik gr
//
LOCUS       WP_181751450             370 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Paenactinomyces guangxiensis].
ACCESSION   WP_181751450
VERSION     WP_181751450.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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..370
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..370
                     /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=42090
     Region          12..347
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mseqkwvnqk ldrirhwlgq kgldgvllck krnfswltcg kanhielnte qgvadllitq
       61 nraicittrm eaeriaseel dglgfemvvs ewiegrekti qhlcrgkkia tdvspeligl
      121 dqgicldrei arlsyaltde eaaryrnicl naakalestc reiepdmtef eiqatlakkv
      181 ftrgmrpvvm lvatderiyr frhpiptskr lqtyamlvlc aeqsglianm trfvhfgpls
      241 pelsenrykl aqidvamnsa trpgteikqv fqsgirayqe aghgedwhyl hqggptgyat
      301 reflatpdce gvvqlnqafa wnpsirglks edtilvkeeh neilthtdew iyitikkdgq
      361 efkrpdilir
//
LOCUS       WP_181751601             417 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181751601
VERSION     WP_181751601.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=47378
     Region          35..408
                     /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(145,147,267,269,301..303,344)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mkkkllvisf vfimlltacs dhrpstdknn ngiitityyq pgledplakk emnetigrfe
       61 qkhpnirvkv qssgwdeayq klvtsfmada ppdvfyggtr wvtsfvtmka vlpldkyake
      121 rlslypqplq kavqvdgksy aiprafsart liyrsdlisr ppqtweellq takkvqaenk
      181 niyglgisga khvstttqfl nylfqnggev fdekgnvkln speavealtf yadlyrkhkv
      241 vpnpleynre qlpilfkqkk iamyvcgpwa knlmaaeenh pntpykaapl pkgkmmantl
      301 vsdslmissk tkhpeaawkf iefitspeeq kkhdmtlnvl plqteeakdp ffnndpymke
      361 finmikvgkp eptpvswesf edilttaiqk tfngedaqta lneavqkike eklepkr
//
LOCUS       WP_181751172             141 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine dioxygenase [Paenactinomyces guangxiensis].
ACCESSION   WP_181751172
VERSION     WP_181751172.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 141)
  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 141)
  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 141)
  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 141)
  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..141
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..141
                     /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=15823
     Region          35..133
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
     Site            order(35,37,51,62,64,113,127,129)
                     /site_type="active"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mtqptlrelq eaissigcts ekilsyvtep dilpygrnvi yqsnnleavv icipgmrkts
       61 vhdhgnstgc ayvvegslin klyvlekdnk pfcyeknkfm kgeffyatkg qihsmcnssg
      121 eklitfhvys ppirdmrvyg e
//
LOCUS       WP_181751697             124 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Paenactinomyces guangxiensis].
ACCESSION   WP_181751697
VERSION     WP_181751697.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 124)
  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 124)
  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 124)
  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 10140416
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..124
                     /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=14332
     Region          3..116
                     /region_name="NUDIX_MutT_Nudt1"
                     /note="MutT homolog-1 and similar proteins; cd04699"
                     /db_xref="CDD:467579"
ORIGIN      
        1 mnfpvsikgi iirednvlll knernewelp ggrlekgeap qkclireike elnidctvkq
       61 lvdtwvyevl pgkqvfiviy ycecddfsql kiseehveyg wvslsklkqs qipegylnsi
      121 fkvi
//
LOCUS       WP_181751704             111 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Paenactinomyces guangxiensis].
ACCESSION   WP_181751704
VERSION     WP_181751704.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 111)
  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 111)
  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 111)
  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 111)
  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 111)
  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 111)
  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..111
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..111
                     /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=12196
     Region          <12..107
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkwiryslac slmlislsal agcgtanqnq yptgqasavt epeeiytrhc anchggnlqg
       61 sygpslknis rkytqeeilq iiqkgkgkmp sqdyvskeeq qkladwlsgq r
//
LOCUS       WP_181751622             325 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase [Paenactinomyces guangxiensis].
ACCESSION   WP_181751622
VERSION     WP_181751622.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=35760
     Region          6..316
                     /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 mtiqlekanh figeadhllv vshlhpdgda vsstlaaaqm frllgkrvtm vnespipkkf
       61 tflsgveeil qpervmnkfr yvvaldcada ermgnsrelf agdvkilnid hhptndhfgt
      121 vnvvepgaaa tveilfqwie nnkipwnksl ataiytgllt dtggfrysnt ssrvlrqaah
      181 lieigipahi iadtvlettt ieqlqilqta lqslqrtkdg liawmslrlq dlqriraand
      241 dldgivnyar nilgvdvgil freteqqtvk vsfrsrsrvd vgsvakslgg ggharaagct
      301 fqgtleeaqr qilsrvqael erdgk
//
LOCUS       WP_181751782             156 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Paenactinomyces guangxiensis].
ACCESSION   WP_181751782
VERSION     WP_181751782.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 156)
  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 156)
  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 156)
  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 156)
  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..156
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..156
                     /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=17287
     Region          64..148
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 miqlldvkdr tvaqkvlkvq klsyqveadl igfqgipplh dtleslmqcn etflgyfftd
       61 qlagfisyvk dgktldihrl avspaffrkg vasalitcll kqeqdmkkav vstgakntpa
      121 knlyrrfgfs evgevevapg vsltlferfm gddlhi
//
LOCUS       WP_181751783             237 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181751783
VERSION     WP_181751783.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 237)
  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 237)
  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 237)
  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 237)
  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 237)
  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..237
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..237
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26514
     Region          72..234
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msknkkeraq qqakqnlist itmatvilaa iglgffalfq pgsdgkndsa nqatvqkisy
       61 egqpgtgnpn apvklmefgd fkcpackyfh deiypqlkkd yidtgkvqmf ftnyqfiged
      121 svtagmagea vyhqnkdafw kfyeaiythq gneadvwatp efltelvkkn vpnidinkls
      181 qdlnnktyek avlednqmar slkiegvpal fingknvgei sgyeelkkmi deelkkk
//
LOCUS       WP_181751811             193 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181751811
VERSION     WP_181751811.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=22514
     Region          13..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 melspglyhg fvrprwltki yihdmiqrhf dltgkavldf gsgtgscsci ctpkhylgid
       61 pdpkrvayar rlypdynfav legsslpasd ksfdyiliva vlhhippdtl paylqefhrv
      121 lkptgkilvm epcflknslf nnrfmaffdr gkyiryesgy rsiftkhhyr ieklkefkkm
      181 lfynelffma ipe
//
LOCUS       WP_181751607             179 aa            linear   BCT 28-DEC-2024
DEFINITION  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
            [Paenactinomyces guangxiensis].
ACCESSION   WP_181751607
VERSION     WP_181751607.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 179)
  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 179)
  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 179)
  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 179)
  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..179
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..179
                     /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=20390
     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 maqihirnsg vrleseqevs sfleeqgvly ehwpteklpd hlrekfvltd aekeeiltvy
       61 qeeieslarr kgyvewdiva lseatpnlde llkkfenvhv htedevrait agngiftikg
      121 neetgyfdve ltagdvisvp vntphfftlm enrkvvavrl fidpsgwvah pyhdpqfta
//
LOCUS       WP_181751815             365 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181751815
VERSION     WP_181751815.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..365
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40906
     Region          2..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 mlegvriidf tqtlpgpfas mrladrgaev ikieplkgep arymgemkdg vgllylannr
       61 nkksialnlk teegkqialn larhcdvlie sfrpgvmerl glsyqevsrv npiviyasls
      121 gygqnglmsr qashdlnfma lsgalaqlrd qkgslihpti lladmvggis asetilaalv
      181 qrgikkrggy ldisileemv rlmgthaaiy netgnkhgpv llaggmisyg lygtkdertv
      241 alaalepkfw thfchavdrs qwipaqmtpq tdsnpvylel cqlfqsrtwe ewlefglkad
      301 ccltpvieag ewewhphfle rkqkirdeds pspvkvgqht reilqewlra deeqidkwie
      361 nriil
//
LOCUS       WP_181751844             496 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181751844
VERSION     WP_181751844.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..496
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..496
                     /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=56279
     Region          14..482
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mkkgvviggg isglvaaihl aargyeinll ekqeklggki qevrlgkyqf dfgpsnitlp
       61 wvfervfrea gqkidpalrl iplavnsrnf fnngtvidlt adpdymseql agfspenrqg
      121 fldyltevqr myeiaedhlf ehlwvewsdv fsprylkafm svhpfqsmds fhrryfddpr
      181 llaimnrfat yvgaspyqlp atlsligyme lvqgvyyieg gnyrlieafe rlavslgvri
      241 ytgckvdeim ikgeqvtgvr sgmdsweadf ivsnadvrtt qelllsekrk petqdslgvs
      301 sflclfgvkr vyphlhhhnl ffpqdvgrqy idifeqkews lsptiyicns afsepdravn
      361 gsnlsvlihv pavheqrqed laakygeyrn hliywlennw glsglseeie vekvygpaei
      421 eqicgapggs lydpvschrr tffrpvmker kvkglyytsg ppflcggaam aalrglniaq
      481 miqldherel qkragk
//
LOCUS       WP_181751834             565 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Paenactinomyces guangxiensis].
ACCESSION   WP_181751834
VERSION     WP_181751834.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 565)
  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 565)
  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..565
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..565
                     /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=63647
     Region          27..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(212,215..220,222..223)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(215,332..333,354..359,438,450,453,464,544)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(215,257..258,305,307..308,311,332..333,354..359,438,
                     450,453,461..464,525)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(257,307..308,311,332,461..463,519,525)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 msvtekiwvr hyppsipetl eypdvpltqf lldavkdfpd rdailflgkr mtfkelqlev
       61 frfanalkdl gvqkgervgi mlpncpqsvi ayyailfvgg ivvqinplym erelehqlvd
      121 sgaetiisld lvyqkianvq entrlkriiv tsmkdylpfp knwlyslkei iegtklkipy
      181 gekvrsfvql iskalptple asyesgddia llqytggttg lakgtmlthr nlvvnccqaa
      241 awiykakrgq dtilgalpff hvygmtvvmn famrmaatmi lipkfdrdlv lkmisthhpt
      301 lfpgaptmyv glinhpeihr ynlssiqacl sgsaplplev qekfeeltgg llvegyglte
      361 tspvthanli wdrvksgtig lpwpdtdcri vdpetgevlp dgsvgelqik gpqvmkgywn
      421 rpeetekvlk dgwfstgdiv rmdedgyfyi mdrkkdviia ggfniyprev eevlfehpai
      481 qeaavvgvpd pyrgetvmaf vvfkqgkqva keelekfcre klasykiprl yefrdelpkt
      541 avgkilrrvl qeeaketlsa skvet
//
LOCUS       WP_181751900             315 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181751900
VERSION     WP_181751900.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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..315
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..315
                     /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=34510
     Region          31..175
                     /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          60..94
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          101..136
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          113..268
                     /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          143..182
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 mkkamgltcs filtstlllp nlanasapkq ilfsggslhk pgiykmnedt tavtritdgv
       61 svdaspdgkk lafikndsly isdidgkhqv rltksrfpvy dssprwspdg kkivfsrsdg
      121 niysidkngk nltnltntde tvinsepdws pdgskivfhs nrngnshifv mnadgssvkq
      181 ltgnkqssey sahfspdgrk ilygrsikad sdiyimnadg knprnltkdi qeaaasplws
      241 ddgkkivftl nepritdhgy llimnadgsg katiklpinf vnpydwnqle ttqsaskqss
      301 gikatinyls dflfd
//
LOCUS       WP_181751976             172 aa            linear   BCT 28-DEC-2024
DEFINITION  YceD family protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181751976
VERSION     WP_181751976.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..172
                     /product="YceD family protein"
                     /calculated_mol_wt=19179
     Region          1..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 mqislhhlnq akdqqmelse tippdslavk vpglirlepv kvtaqvlkld shlievkaeq
       61 sthatltcsr clseieipvq tewveqftdv enqageteeh eihliegnil dltpyireal
      121 llsiplapvc redckglcpk cgvnkntdac ecriesidpr laklqellnk dr
//
LOCUS       WP_181752103             300 aa            linear   BCT 28-DEC-2024
DEFINITION  EamA family transporter [Paenactinomyces guangxiensis].
ACCESSION   WP_181752103
VERSION     WP_181752103.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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..300
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..300
                     /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=32645
     Region          5..297
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mlgasqtlar vkgfalvltg avlwgvsgtv aqhlfqndgf tpewlvvirl lvsgilllsa
       61 arfqnkhglw aiwksrhdri slllfgiigm lgvqytyfaa iqagnaatat llqylapvli
      121 tcylavrsrr lpsgkesvav ilalsgtffl vtdgrvkdls isewalfwgi gsaftlafyt
      181 lqpskllaqw gatlvvgwgm ivggvgfsfi sppweiqgew nlktalfvvf vilfgtliaf
      241 ycyleslkyl rpsetsllsc aepltaaims vvwlhvsfgt iewmgalcii atiillskse
//
LOCUS       WP_181752142             242 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenactinomyces guangxiensis].
ACCESSION   WP_181752142
VERSION     WP_181752142.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..242
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27613
     Region          <5..242
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 meqkvykrii kkenlyskhl eeakeilvsl ppgydesrsy pllvlhdgnd yfnlgrivtq
       61 anqmmvngei epvimvavpv qkerrtseys pkgsrhsqhm kmvveellpr irdhyptdds
      121 perlvlggss lggtvslhia lhypevsnri lsqsgaflea tneailhaks lehfriyqsv
      181 gkaetavsth mgsldlvarn revlrhlkek hahvhyvede gdhtwgfwqr dippalrfff
      241 gr
//
LOCUS       WP_181752254             685 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181752254
VERSION     WP_181752254.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=76504
     Region          <118..>236
                     /region_name="PRK11086"
                     /note="sensory histidine kinase DcuS; Provisional"
                     /db_xref="CDD:236839"
     Region          226..684
                     /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 mqrflivggg kegnailqtl stvefvkvig ivdvsadtpa iqeakkqgil tgreiepflr
       61 lspdvilevt gdpavysrlc qldlpdtlvi sgeianlmvr lveekdrwfq awrqrqrelq
      121 ailnsthdgm iavnkkgqvt llnraaerml qlkaaealgk pvaelvpntr leivlkrgvq
      181 elnqkqqlsg dmeivtnrvp vkdpegkvig avavfrdvse lqsltqqvtd legmksllqa
      241 iinssddais vvdadgmgml inpaytrltg lppedvidkp aetdiseges mhmrvlktrq
      301 pvrgvhmkvg pqrkevvvna apiiindelk gsvaiihdms elqqlnrdle rarriirkle
      361 akytfddiig tseamriaqe qakqaaktra tvllrgesgt gkelfahaih nasdrkynqf
      421 vrvncaalse slleselfgy eegaftgakr ggkkglfeea sggtlfldei gelqpstqak
      481 llrvlqekev irvggtksip vdvrviaatn vyleraiqek rfredlyyrl nvlpiqiapl
      541 rhrkedlydl sthlikkynq eygrsveeid pgalailsry swpgnvrele nvlgraminm
      601 afnekiikpi hlpslnlsrt algekesqat ngdkektlke vlaeterefi krvyvscgrn
      661 ktesarrlgi svrnlyykle ryhll
//
LOCUS       WP_181752558             479 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Aeromicrobium phoceense].
ACCESSION   WP_181752558
VERSION     WP_181752558.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 479)
  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 479)
  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..479
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..479
                     /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=51965
     Region          1..424
                     /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 mtrvrvavvg agfagvamar rlaaagesfv vlerrpgigg twhdnrypgv acdvpahlyg
       61 ysdiahpgfs rvfapgaeir eyleeaaapv gdrimlstrl esaawdgegw rlttsrgpvq
      121 aevlvmaagr lteprlpevp gafdgpivht arwdddldle gkrvavvgtg asgiqvipel
      181 arqaesvvvl qrsapyilpk gdrayadaei alfeqqperl adlrgdlmre teevfdqrag
      241 dgraqarara ldhlagqvpd pvlrdaltpd hefgckrvlf sddyfttlrl phvrlvpsal
      301 tayepgavva adgsrhdvdv vvaatgfhst rqpyaelvtg rdgisldqyw sqgmrayast
      361 vvhgfpnlfv ldgpnatlah nsavlmieaq adyaasalpw tshgplevsv daeqdyidei
      421 qersgvwtsg csnwyvders grqvllwpgk aqefrdrfgw fdpapfgmah qepsesaga
//
LOCUS       WP_181752706             107 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Paenactinomyces guangxiensis].
ACCESSION   WP_181752706
VERSION     WP_181752706.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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 107)
  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..107
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..107
                     /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=11153
     Region          33..103
                     /region_name="Cytochrome_CBB3"
                     /note="Cytochrome C oxidase, cbb3-type, subunit III;
                     pfam13442"
                     /db_xref="CDD:463879"
ORIGIN      
        1 mrklaigfag llsfvllagc npqqqtnrap andtamepkd iytnncasch ggnlqgsigp
       61 slekiggkls keeianiian gtgsmpgqtq isaqqrekla awlaeqk
//
LOCUS       WP_181752830             263 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181752830
VERSION     WP_181752830.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=30247
     Region          1..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 mpdhsiydwp dyydwtspgl erdltyyiel akqtggpvle lgcgtgrcsl aiarlgipvv
       61 gvdlsspmlq karqrakkln lsdrvrwvea dmsrfslner fplviipyrs flhlltvrdq
      121 istlkrirqh ltdgglfafn ifvprirdly qmegkysfrg sflasggker vdlydltefd
      181 yfnqtayitr yaerfdekgh slgrirmafr lryifpaeln hllalcgfki inrfgsfhrt
      241 pfdarseeli ieavkrpgqt gsg
//
LOCUS       WP_181752842             119 aa            linear   BCT 28-DEC-2024
DEFINITION  fluoride efflux transporter FluC [Paenactinomyces guangxiensis].
ACCESSION   WP_181752842
VERSION     WP_181752842.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=12819
     Region          1..116
                     /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 mkqicfvgvg gfigtllrfa vsrllhqpgf pwgtlfvnwt gcfllawlla vntrtgrisp
       61 ewqtglgtgl lgsyttfsaf saetiqlgnw kwqavyvavs viggialavl grtigkekr
//
LOCUS       WP_181752205             453 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Paenactinomyces guangxiensis].
ACCESSION   WP_181752205
VERSION     WP_181752205.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 453)
  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 453)
  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..453
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..453
                     /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=47420
     Region          52..>449
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mkklistglt avltisllvs gmgtaaaaga gkeiytvnfk gntlpshvqk iiqdtggslv
       61 ksdaelayvq avsndpqflr nirknpsved agrtlkvvqe aavekaalea ddahpiydqy
      121 qwdikqvtqe gasyqlpkgk gtrdvvvavi dtgidlehpd lkanivdaks fvpgenaqdy
      181 dghgshvags iagngkalgi gpelgiaalk vfpkdgggas tasiaealky aadqdydvvn
      241 mslgsyaylq dpaydtndir adinlfkkai ayahkkgvti vgsagnasad isspgklsry
      301 lfdengathr dpasnllirv sagskgktlt fysnygvgki dvmapggdlg pnydpvnktg
      361 rdnaylcyst vpvvdsnyqi ighgyagyag tsmaapkvag iagviiakhg knklspaqvk
      421 siiqqsaedi ykngydaesg fglanalnal qyr
//
LOCUS       WP_181752672             350 aa            linear   BCT 28-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181752672
VERSION     WP_181752672.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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..350
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..350
                     /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=39147
     Region          32..350
                     /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 mkrellvgvl avslafstwv aepafatgtn pekklkeiqq dkkkaktdln ktqaelnekk
       61 kklqaleeqv gkldeqiash tkklldnqkl lekqdkqfke tlvrmyqkne ldytaqllas
      121 dsfsefltry etlrvilkre railegyiet knkiekekaa veakkekqap ilkaaqkeyq
      181 siksvlakqt nnleklehqe eltkeaieek nrlvreangm ysgrgtgvlq wpangkvtsg
      241 ygwrsgrmhe gidvansigt piyaadsgtv sltksnpggy gyyvvinhgn glstlyahmy
      301 rstvtvsvgd kvrkgqrias ignngrssgp hlhfevhkng npvdpmkylp
//
LOCUS       WP_181752739             772 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Paenactinomyces guangxiensis].
ACCESSION   WP_181752739
VERSION     WP_181752739.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 772)
  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 772)
  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..772
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..772
                     /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=86893
     Region          <156..438
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mvkkirreri agftticila lslllvplwn skpapslmie spegrewvir wrqkvnpafl
       61 qtvvvihrsa erddgetmlv qvkkgldpel wtkrwakdpg veylhpnhky klegnehttg
      121 tesfddfyyl ekiranqawk vlrskqkqyt klhrpvvvav idtgvdfrnp klapllmpgv
      181 nlknrslppq demghgskva gvvaavwgaf skegpvgngk ilpikvmedg tdgdiyftae
      241 gireavrrra diivlaqgsw tysqmmadav keaeragilv vsaagnasyd ingkvvynhp
      301 lyypaalpnv lgvgsvslng thelssntge gidvaapgew ikttgndgdf hfdsgtsfaa
      361 pqaaavaami lqlhreysaa dlrhlisqta lkgpgeprwd ermgfgqlda yralttplsp
      421 dlsepnnrpe lsmpvstaqe lkasltekde dwyhmdvkra gilllqfhkk kgewgdsclk
      481 vtiaenghss lyrldqwqni rltvpagrvh lqiigpkkpa keivyrwqat wippadeyen
      541 ndyqwnaadi dlfegltayq gtihkkrdmd wyrlvipkqg qleigvqtft prmdpvlyiq
      601 tkqdwkgmrv daggegereq mqmkveegsl ylrisdyggn viddfyqltf hyqadiqdpt
      661 epnqtsneaa tilmgqemqg qltevtdidw ysfymeqeqq teyvllaldq lkgvnftlyd
      721 aerrviqtws gdqerneavs lsasvppgry llrvraenkt glgayririq tk
//
LOCUS       WP_181752923             409 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181752923
VERSION     WP_181752923.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..409
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44972
     Region          51..402
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrlpvrwfsl algiflllsg misilvlskg ksgspslrhe dpkglkmegn qlkyidkime
       61 dairdgvfsg gtvlvsrkea ivyekafgfa vrykdhqktp adklirastr tiydiasisk
      121 iftatavmql aekkkislde pvsrhlpafa angkekitir qllthtgglp atlplyevqg
      181 grgdrikaal scklvakpgs kmiysdisyi algqlvekvs gmplqrymkt yifqpldmst
      241 gyqpppflkk riaateyqpg lqrglvwgev hdenawaldg vaghaglfst aedlakfgla
      301 iinqghlngn rilkpstvee mtrlqtgslp gafrglgwel nqewymgsfs gdgayghtgf
      361 tgtsimidpk rdvmiilltn rvhpgrtgpn vseirkqiae tvyssfrek
//
LOCUS       WP_181752411             563 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Paenactinomyces guangxiensis].
ACCESSION   WP_181752411
VERSION     WP_181752411.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 563)
  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 563)
  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 563)
  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 563)
  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..563
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..563
                     /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=63033
     Region          <1..>563
                     /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 mghyetllka iaanpkqkis siplltemek rklltewngt dtwfpnkkci helfeeqvdi
       61 nphaiavidr emrysyleln kranklayfl qqkgvgpnvf vgicmdrtfd mivgllgilk
      121 aggsyvpldp dypkerlayi indtkmnflv tgqrntdkhg vinrktnadq layviytsgs
      181 tgqpkgvmiq hkqavamisw aknvfsdeel agvlastsic fdlsifeifv plcrgkkvil
      241 aenalylael pnaqevtlin tvptaiaell kvegiprsvk vvnlageald eklvqqiyqk
      301 ewiekvnnly gpsetttyst yaliprdpel kvhigkpian tqiyildseh qivpigvpge
      361 ifiggaglsq gylnqpelta ekfiahpfrs hqgeklyktg dlarflsdgn ieylgrqdyq
      421 vkirgyriet kevevvlkqh savkesvvmv kegpdgnkrl iafltgkqpv ptikeirsyl
      481 leklpgfmvp ssfilldsfp ltlngkidrk allqmsqema eeeaglilpr dwvelkmalk
      541 weellgvksv gvndnffylg gds
//
LOCUS       WP_181753015             241 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Aeromicrobium phoceense].
ACCESSION   WP_181753015
VERSION     WP_181753015.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 241)
  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..241
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..241
                     /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=25853
     Region          5..240
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mttapritah rgqsathpen tipalreavr lgadalefdv qptadgsivl mhdrsplrtt
       61 nirhvqtskv glsvqrftla elaqldagsw kspafagtpv ptlrdvvhal rgtevrlvve
      121 mksapvdprs yvravldelg ghsrvtlmsf drdvaeaalp vhhavglvsr grpnaadidr
      181 fdefhvsarr vdralvdrvh agggtltawt vddprqverl aalgvdgitt ndvsaarpal
      241 v
//
LOCUS       WP_181753001             261 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Paenactinomyces guangxiensis].
ACCESSION   WP_181753001
VERSION     WP_181753001.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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
REFERENCE   5  (residues 1 to 261)
  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..261
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..261
                     /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=29648
     Region          1..261
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mywevirirf lmmlayrvny ysgiviysln igvyfflwma iygdqsslqg ltavqmatyi
       61 avswmarafy fnnldreiaq eirdgtvaiq lirpyhyllv kafqgfgegm frlllfsvpg
      121 mivvslifpi hlpvnaevwy kfalslvlgf ivnvqvnilt gicaffilnn qglirakrva
      181 vdllsglvip ipfypewaqt ilsylpfqai sylpsmvlvk glagtefiha ilvqaawcvl
      241 lwipiraiwk karktlivqg g
//
LOCUS       WP_181753211             318 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Paenactinomyces guangxiensis].
ACCESSION   WP_181753211
VERSION     WP_181753211.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=35771
     Region          15..304
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mnpspnwdqg nkliekmvnn iekvligkqs viqlclvall akghvlledv pgvgktmlvk
       61 alarslgcky rriqftpdll psdvtgvsif nqktlefefr pgplmsnivl adeinrtspk
      121 tqaalleale egsvtvdght yqlespffvm atqnpieyeg tfplpeaqld rfllklslgy
      181 pdtgqememi krfqyehpin evaevwsrnd lhflqqqvln vyvddaivey mvnivkqtrn
      241 epdlflgasp raslaifrss qalalirgrm yvvpddvkyl ipftlshril lsseahmngk
      301 tpeqvlerll rqipvpvt
//
LOCUS       WP_181753281             427 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181753281
VERSION     WP_181753281.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..427
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..427
                     /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=47132
     Region          21..426
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 meqqsvatgh qpeeqenldv lvstqtvikk aldklgypdp vynllkeplr vltvripvrm
       61 ddgtvkvftg yraqhndavg ptkggvrfhp dvtesevkal siwmslkagi vdlpygggkg
      121 givcdprnms frelerlsrg yvraisqvvg ptkdipapdv ftnsqimawm mdeysriref
      181 dspgfitgkp lvlggsrgre tatakgvtlm ireaakkkgl smegarvviq gfgnagsfla
      241 kfmhdsgakv igisdaygal hdpdgldidy lldrrdsfgt vtklfkdtit nqellelecd
      301 ilvpaavenq itaknahrir adivveaang pttleatril dergillvpd vlasaggvtv
      361 syfewvqnnq gyywsedeve qkledimvra fenvyrtsqn rrvdmrlaay mvgvrkmaea
      421 srfrgwv
//
LOCUS       WP_181753491             437 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Aeromicrobium
            phoceense].
ACCESSION   WP_181753491
VERSION     WP_181753491.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 437)
  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 437)
  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 437)
  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 437)
  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 437)
  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..437
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..437
                     /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=46862
     Region          6..246
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mapltyryva ltdvglrrsn nqdsgyaspr llviadgmgg aaagdlassa alaeirdldr
       61 eldddtdgda ldamrtavan anhrlaqlia ddpavegmgt tleamlwdge klavahigds
      121 rayrlrhgrl sqlsidhtfv qslveegrit peearvhphr slllkailgr ddfepdftwl
      181 qpaagdryll csdgltdmvd detiertmkl etidaaatel vrlaleaggy dnvtvvvaef
      241 vpgdepided lvcadgkpql vgaatsqprr rtgsvsassa pavhvagapg avepdpeelr
      301 yaplpvprrr wvrwllgslv vlgllggaaa yaydwsqrqy fvapsdgmva iyrgvdvdvp
      361 gltlktvdev trieidtlpp yqrdrvaagi aaadhdeakr ivtnlsiqvt eptptptptp
      421 tptprrtpat sapteap
//
LOCUS       WP_181753585             622 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Aeromicrobium phoceense].
ACCESSION   WP_181753585
VERSION     WP_181753585.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 622)
  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 622)
  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..622
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..622
                     /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=68711
     Region          4..612
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mnttatntla rrirtraeet pdriamrekn yglweevtwa dywdrselvg hallalgvgi
       61 gdrvavhsen rcewlwsdvg itavragtvg lyptnpapev lhvlrdsgac vliaedqeqi
      121 dkyleiadel pdlrtvvyid prgiegrydd prlmswddfl algeqhrtdh pgavtervea
      181 aepgdlatlv ytsgttgppk gamlsisnie fvietlqsgg afvdppasdr dlvvsylplc
      241 hvaervfttw fnaavgsqvn faesietvqq alrevqptll fgvpriweki aagvhirmsg
      301 aswlkrknfd fwmkraawig rtlvenqgnh taatkavyai gwvclyrplr erlglakvry
      361 aasgaapiap evleffmgig ipmhevygmt ensaiatanm agrvkvgtvg epqvgaeiri
      421 ddetgeiltr hagtfagywn npeataktvd adgwlhtgdv gewvdgthik itdrikdiii
      481 taggknisps eienslkssp yikeaivigd rrkyltalig ieldtvgnwa qarklgftty
      541 rdlsekpevi elvqsvvdet nrkfasveti krfamlpkel dheegeltat qkikrsaine
      601 rfaeaiegly sdtdraahev ka
//
LOCUS       WP_181753586             333 aa            linear   BCT 28-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing protein
            [Paenactinomyces guangxiensis].
ACCESSION   WP_181753586
VERSION     WP_181753586.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 333)
  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 333)
  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..333
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..333
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=37077
     Region          2..47
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 mkihivrpgd smwdlaqkyn ipverlhean pqikeanhlq pgmkirvptg ripivsqkre
       61 estnispgka gvakealqnk eseeftekpe qktaysepqs esschysysa teaesshttt
      121 vseegapyhs hsqeeeriyq qyplpeqqtl ypyppserdl pvdssarypa pglespdryp
      181 lpqeespkqy aspyfstypy vatpemsgsd vagyesqfas esplmdssay dlppvppgls
      241 qypdgtegry vplyypmifg ptafvaappp plvpaaehys syfyapgqev nwqppsaepw
      301 shpttppsft pttplpffas piqrekesss red
//
LOCUS       WP_181753677             717 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Aeromicrobium phoceense].
ACCESSION   WP_181753677
VERSION     WP_181753677.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     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=75009
     Region          12..715
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mtthetevep tttyrldigg msctscaari ekklnrldgv eatvnyatek atvhahhavd
       61 pdelvqtvek tgytaqvhdp hagheghaah gglhsaesmr krlivatilt lpvlaismvp
      121 glqftgwpwv alalttpvvl wcaypfhwsa vlnlrhgaat mdtlismgvt aayawslvql
      181 wigvtghgve hghyyfetaa avttfilagh yleatakgrs saalralmdl gakqvtllrd
      241 grevevpieq lhagdtfvvr pgekiatdgd vvdgasavde smltgesvpi dvatgdtvtg
      301 atvnqsgrlv vratavgqdt qlaqmarlve eaqegkaevq rladrisawf vpgviaisav
      361 tllvwllvap gigafeaava vliiacpcal glatptalmv gtgrgaqlgi likgpqvles
      421 traidtivld ktgtittgtm tvahvdpapg vdvdelhrla asveaasehp varaitalae
      481 plpvtafrnh agqgvegtvd ghvvragrpg wigaedrpdr tgtviavsrd gevlgtitva
      541 drvkessrea vadlrrlgle pilltgdner vatavaaevg idrvhaevtp qdkldvvrdl
      601 rdqgrvvamv gdgvndaaal agadlgiamg tgtdvaiaas dltlvhgdla tavtavelsr
      661 atlrtikgnl fwafaynvaa iplaalgfls pmiagfamaa ssvfvvtnsl rlrrfgh
//
LOCUS       WP_181754099             489 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Aeromicrobium phoceense].
ACCESSION   WP_181754099
VERSION     WP_181754099.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     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=53362
     Region          2..421
                     /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 mtlqrdvdvl ivgaglsgin mayriqqacp gltyaiverr driggtwdlf rypgvrsdsd
       61 fftlafpfrp wrgkdaivdg dqileyledt areagidrhi afgrrvdsad wssvdsrwsv
      121 easgpegpet wsarfvvact gyydydspyd pgfagvedfd gtlvhpqfwp edldhtgkrv
      181 vvigsgatav tivpamaeta ehvtmlqrtp syllaqpkgd piadvvrkia pptvahhvvr
      241 tknmllqwal fqacqrapka mrslllkgva hgtgsaeiae qhfnppydpw dqrlcvtpqg
      301 difaaikagt asvttaridr fvpegvried gtvlpadivv tatglsikil ggakvsvdge
      361 prdpsdsfay hgtmltglpn lafcvgyinl swtmrsdlts rlvakvlrrl vdsgassvvp
      421 eftgsgptap lmdmqsgylq rgahlmprat dsypwsfrqn flvdswstnr adlddglvwt
      481 apdraeapa
//
LOCUS       WP_181754194             338 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Paenactinomyces
            guangxiensis].
ACCESSION   WP_181754194
VERSION     WP_181754194.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=37523
     Region          29..320
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mnsvqelenk laepsvglvk tladldgdil ilgvggkmgp slarlaknal neagvqkkvi
       61 gvsrfssgnl rqilesdgie tiaadllnee qleslpdvkn viymagnkfg ttgreyfswa
      121 mnaylpgrva ekyrhsrmvs fstgnvyplt pvamqgtsed hptgpvgeya qsclgrervf
      181 eyfsrkygip mvqfrlnyai dlrygvllev arsvfekkpi dlrmghvnvi wqgdaneyal
      241 rslsicdspp rilnvtgpet vsirwlakkf geqfgiepef ihseektall snaseshrlf
      301 gyprvtlrqm iewtadwvaa ggetldkpth fqerkgaf
//
LOCUS       WP_181754292             296 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Aeromicrobium phoceense].
ACCESSION   WP_181754292
VERSION     WP_181754292.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 296)
  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 296)
  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 296)
  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 296)
  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..296
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..296
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31987
     Region          39..263
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 msprrphdap rnlqsrsila gqaaaaaaev eqalaqpadp taaaffdvdn timqgasifl
       61 larglhrref fttrdiaraa wqqayfkyvg vedpehieqa rnaalqfiag hevseleeig
      121 eevfdeymaa kiwpgtrama qwhldrgqrv wlmtaapvei aqviarrlgl tgglgtvaeh
      181 vdgvytgrlv gdmlhgegka iavralaese gldlercyay sdssndipml slvghpcavn
      241 pdgallshak angwlvrdyr tgrkvvaaga kagaaaalat tawlltrlav rrlrrs
//
LOCUS       WP_181753857             264 aa            linear   BCT 28-DEC-2024
DEFINITION  energy-coupling factor transporter transmembrane component T family
            protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181753857
VERSION     WP_181753857.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..264
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29663
     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 mnqpvigqfi pgnsllhrmd prskllfvla fmfvvflann aasyglllaf iaigvyfsri
       61 spiilyravk piffllllts ilhlwmtkgg dvllklpfvt iyeegvrqav fisvrffllm
      121 aaaslltftt spidltdgme rlikplervg vpahelalmm sialrfiptl weetekikka
      181 qmsrgadfes ghvitrvksy ipvfiplfis afrraedlal ameargyrgg agrtkfrelr
      241 yskpdgvllv ffvamlaglw vlrk
//
LOCUS       WP_181753901             318 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: EamA family transporter [Aeromicrobium].
ACCESSION   WP_181753901
VERSION     WP_181753901.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium
  ORGANISM  Aeromicrobium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 318)
  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 318)
  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..318
                     /organism="Aeromicrobium"
                     /db_xref="taxon:2040"
     Protein         1..318
                     /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=33868
     Region          1..316
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mpqphvrrgy alvvtaavff ginagvtrip meaglptaty ttirvtfafl tffliavafd
       61 rsalrrprgr dlllvlalgv vgvafvqwty niaimrlpig vallleylap vlvvlwvrfv
      121 rrepvhprvw paialallgl alvgqvwdgl sldgigvlma laaavcfaay fllgeeltss
      181 aaepltalrt vvwsfgvgai vmnvlggweg tsalandasm lgrlaeftvp awlamasvvl
      241 lgtvlpffly laslrdlsss kasvtamlep vvavivgwlw fsetldavqv igvlavlagi
      301 vlaqtarhvp adelpppl
//
LOCUS       WP_181754304             205 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181754304
VERSION     WP_181754304.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 205)
  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..205
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..205
                     /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=22581
     Region          3..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 mqpelvlasg sprrqellsq lglsfriqts qadetveqnl spatfveqla lkkakavars
       61 cqsalvigad tvvvlddeil gkpgdqtvvk rmltrlqgre hqvytgialv qvhdekvvre
      121 ltdhkrttvw mrrltpekie wyagtgepld kagaygiqgf gacfvekieg cyfnvvglsi
      181 slldemmeki gfslvedfrs gtkvl
//
LOCUS       WP_181754419             330 aa            linear   BCT 28-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Paenactinomyces guangxiensis].
ACCESSION   WP_181754419
VERSION     WP_181754419.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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 330)
  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..330
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..330
                     /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=36452
     Region          <38..156
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mklideaika vnrdtyvlrq dgtqitqsta traivkslel ldiqpgmkvl eigtgsgyst
       61 allkylvgde gsvvsidiep emtiwakqlf qhqsnvsfft gdgrkgyteg apydrivawe
      121 taqyfpkqws kqlseqgliv spfktfpiad ttviarfkke nchiqgdvvi pggyilmnds
      181 pdyesfgpel dadiviksek etvawasstw lksrkswmdw vsllnekevk sgpikggdea
      241 refrayllal nleglttayd desgsligis spsgfallal dgsayfrsgs skeadqlesc
      301 lkdwcnrgkp gysalkpvve neevrvklkf
//
LOCUS       WP_181754631             251 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Aeromicrobium
            phoceense].
ACCESSION   WP_181754631
VERSION     WP_181754631.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     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=27220
     Region          2..209
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mrdvtyppii gtaktlfrvl gisfqtsgte hipreggail asnhvsyvdf ifnglaaqpa
       61 grlvrfmakk eafehkvsgp imrsmhhipv draqgeaslh eaadyarrge ivgifpeati
      121 srsmevkeik tgavraaaeg gvplvpmvvw gtqllktkdh eadlwgrgkt ialhvgepip
      181 vtgedpvaet allhdsltal ldkaiheypv spegqwwapa ryggtaptpe earrldleek
      241 aardarraer g
//
LOCUS       WP_181754814             272 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Aeromicrobium
            phoceense].
ACCESSION   WP_181754814
VERSION     WP_181754814.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     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=28544
     Region          4..267
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtyftgkvav vtgagsgigr alamglarrg arvaisdvda tglaetaqal ealgatvrad
       61 hldvsererv layadeiagh fgvvhqvynn agiaftgdie amdfkhleqv mdvdywgvvn
      121 gskaflphli asgdghvvni ssvfgiisvp tqgaynaakf avrgftealr memvargrpv
      181 kvtcvhpggi ktnvarnagq vdgldhdsla ssfdriartt pdqaaevilr gvekgkarvl
      241 igadarvidl larvtgphyq rlvarfagka gl
//
LOCUS       WP_181754921             447 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Aeromicrobium phoceense].
ACCESSION   WP_181754921
VERSION     WP_181754921.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     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=47054
     Region          3..442
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mrptypdvel allsrwpetr lepsldrira icelmgdpqr aqpviqltgt ngktstsrmi
       61 dallraldlr tgrftsphlq rmnericvdg eplsdelfvd ayadvaiyad lvdqgqphpl
      121 sffemlvamg yaafadapvd vavvevgmgg awdatsvada svavitpidv dhasflgdtp
      181 adiavekagi ikpgsrtvla sqpeevlevi mgranevgsm lvlegadfgv esrtaavggq
      241 vltiqgvkgr yedillplhg afqarnaala vaavevftgd aeldpdlira gfgavtspgr
      301 levvrrsptv vldaahnphg vramvesise efafspligv vgvmadkdae eilrelepvv
      361 ahlvctqnst erslaaadla evasgvfgpe ritvvprldd aleraiglad asgedfgdsi
      421 gsggvivtgs vvtvgeartl lrggesq
//
LOCUS       WP_181755099             110 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Paenactinomyces guangxiensis].
ACCESSION   WP_181755099
VERSION     WP_181755099.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
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="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     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=12837
     Region          12..88
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msliaktpnp pyyaviftse rtevtkgyeq maermltlas eqpgflgees frdengfgvt
       61 isywdsleai kqwkensfhq vaqnlgkkew ykryktrvck vekdyfflse
//
LOCUS       WP_181755149             502 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Aeromicrobium phoceense].
ACCESSION   WP_181755149
VERSION     WP_181755149.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..502
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..502
                     /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=53417
     Region          1..501
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 maervvivga ghnglvaaal laragvevlv lerlgrvgga avsgapfaeh darlsrfsyl
       61 vslfpqalid dlglelelrs rdtasftpwh rdgrdgglvv etrpgeatra sfaeltggdd
      121 eleawnrfya eigtladaia ptlmqplphi gdlrdrvema iwtdlvehpi gtvirrrfad
      181 dvvrgvvatd aligtfasle dlslvqnrcf lyhligngtg ewrvpvggmg avtaelarva
      241 teagatirln sevdgidvsd vdvtvcgdgf veradhvlfg aapyvlerll ghtptskpag
      301 aqlklnllls rlpalksgad pavafagtfh ldesydqlqr awataasgdl ppatgefych
      361 tltdrsilgp dlrdsdaqtl tyfglhtppg vldapgakde avarvlaald ahlaepiepl
      421 ilgleaktpt eiehelwmpg ghifhgdltw pwleederpy spaqrwgvat ahprvllcgs
      481 gtrrggavsg lgghnaaqal ls
//
LOCUS       WP_181755253             559 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-70 family RNA polymerase sigma factor [Aeromicrobium
            phoceense].
ACCESSION   WP_181755253
VERSION     WP_181755253.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR02937.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..559
                     /product="sigma-70 family RNA polymerase sigma factor"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=58217
     Region          10..178
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
     Region          194..228
                     /region_name="zf-HC2"
                     /note="Putative zinc-finger; pfam13490"
                     /db_xref="CDD:463895"
     Region          <265..438
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mtdqetlaap pdtelvegvr sgdehamaql yerhradalr varivsqdtd addlaaeafa
       61 rvitkitegg gptsgfrpyl htvirnlnie rrrqagreqa asdkpwllds tdevepevfd
      121 evdadraara lrslpdnwqq llwkldvqgs kpaevarele ipvasvsstv yrareglrva
      181 yldqhvprad dgdcawtrar lsrlargslt sratakvhlh lnqcaecaal yddlhrlntk
      241 lgafvwplvl aggvsaggfp wsvgavaspp psgqssgaag gagtsvgtsv ggvvagapva
      301 avaagivgfv avvaagalwl tsssaepsaa rvvtpvlesv veespakpkp aaptlagplg
      361 llatplgvtp lpsgddpttp aptdpppsde papetspgpt peptpepspq ptepqptepq
      421 ptepqpteep pvepvdlgvg eptvvatged shweltvpis aqegaaaesf tlsvdltmnd
      481 vtgfverrsa gwscgpieeg gsngdpyffd tvtcdytyqp gqavtplqlv lmavepsgav
      541 tvrgagnadp dassdsrqf
//
LOCUS       WP_181755286             611 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AMP-dependent synthetase/ligase [Aeromicrobium].
ACCESSION   WP_181755286
VERSION     WP_181755286.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium
  ORGANISM  Aeromicrobium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
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="Aeromicrobium"
                     /db_xref="taxon:2040"
     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=66105
     Region          15..611
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mavseadqll ivqnrarnvg elffgrveas gpreafrypd adeswhsltw nqageqvskl
       61 aaglvalgie peervaiasg triewiladl ainsagaatt tvypstvtpd vvyilsdsds
      121 rvvfaeddaq vaklrdgrse lpqvmkvvaf egetdgdwvi slddllaqge kyladhpgvv
      181 qeriaatgpe slatliytsg ttgrpkgvrl vhdcwtyega avaapgllti ddleyrwlpm
      241 ahsfgkvllt tqlavgfpca vdgrvpkive nlavvrptfm gaaprifeka ygrivgmmee
      301 eggaklklfh waervglqks rleragkpvp lplkaqhala dklvfskvrd rfggrvrffi
      361 sgaaalstdi aewfhaagil vlegygltet sagavvghpd dyrigtvgrp fpgtevkiat
      421 dgeilikgpg vmrgyhnlds esasalvddg wlatgdigef dadgylritd rkkdlfktsg
      481 gkyvapshie gafkavcpla sqmvvhgndr kfcsalitld pdavdawaan hgmegksyqe
      541 ivsspgiqqq iaqdieelna klnpwetikk wavldhdlsi esgeitpsmk vkrrvvedry
      601 sdvldgfyag a
//
LOCUS       WP_181755333             115 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor
            [Aeromicrobium].
ACCESSION   WP_181755333
VERSION     WP_181755333.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium
  ORGANISM  Aeromicrobium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
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="Aeromicrobium"
                     /db_xref="taxon:2040"
     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=12249
     Region          32..109
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(37..38,42..44,60..62,71..74,76..77,80..81,83..84,
                     90..92,97..99)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mttrttlpla detaccspvt ggvldveeaq rlarmfkalg dptrvrllsi iaagadreac
       61 icdltepvgl sqptvshhmk qlvdaglvtr eqrgrwafyr vvdetlaslg aaltp
//
LOCUS       WP_181754983             405 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Paenactinomyces guangxiensis].
ACCESSION   WP_181754983
VERSION     WP_181754983.1
KEYWORDS    RefSeq.
SOURCE      Paenactinomyces guangxiensis
  ORGANISM  Paenactinomyces guangxiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Paenactinomyces.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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 405)
  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..405
                     /organism="Paenactinomyces guangxiensis"
                     /db_xref="taxon:1490290"
     Protein         1..405
                     /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=46205
     Region          23..405
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(59,66,91..92,99,103,110,239..240,243,247..248,251,
                     284,289..290,293..294,296,319,346..348,351..352,354..356,
                     360)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(66,85,87,90,92..93,175..176,188,238..239,242..243,
                     247,290,293..295,395)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mpestdkvwe inlfssefke nayqiykqlr lndpvhritm psghhgwlit ryqdalavlk
       61 ddriiknprk vlntdkpnrv laesdlltnh mlssdppdht rlrslvqkaf tprmveglrg
      121 rieeiahtll ndvqdkgkmn viddfafplp iivicemlgi paedrdkfre wsnaiisatn
      181 qpdkmrqiqp qvqefidylh dlitkrrqtp rddlvsrlvh aesegdqlte kelfamifll
      241 iiaghettvn ligngilall ehpaqmeklk qqpelihsav eemlryyspv eiatnrwase
      301 diflggkkip kgdmvlvmlg sanrdpeqfa npdqlditre nnrhiafglg ihyclgapla
      361 rlegeiaiqt llarmpdiql avnpatlkwr ptflmrglee lpvtf
//
LOCUS       WP_181755359             342 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Aeromicrobium phoceense].
ACCESSION   WP_181755359
VERSION     WP_181755359.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 342)
  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 342)
  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 342)
  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 342)
  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..342
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..342
                     /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=35652
     Region          1..342
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mqpdtvtvia grpakqpgap lnapitlasa fvpggsseyg rhgnpayeaf eavlgelegg
       61 ralafasgia tsaatlglle pgavvvlprh gyngttslve sgpyevrlid psdtegsiea
      121 fagadlvwle sptnpamevg dlptlvaaak eagalvavdn tfrtplrdrp lsygadivch
      181 saskllgghs dlvlgvlatr ddalferllt hrslhgaipg alecflaarg vrtlavrldr
      241 aessaaviad rlkahpavae vrypgfgsmv cfvvddaeha qratessrii shatslggve
      301 stwerrrrfp aepetipagl irlsvgieav edlwsdieaa lg
//
LOCUS       WP_181755387             220 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Aeromicrobium phoceense].
ACCESSION   WP_181755387
VERSION     WP_181755387.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     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=23817
     Region          16..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 mtdshdhddh qqdapdyfeq pgwdkryags ekvwsgqpnp qlvaevsaln pgtaldlgcg
       61 eggdviwlaq qgwtvtgadf saqgldraar haeeagvadr tswwqvdart fdagsrrfdl
      121 vtthflhpgg smvdvvrrla tavapgghll vvghapsetf aqlsaeqfra mwhaedllpa
      181 lddsfepvvv eerprvverd gktveigdat llarrvgldg
//
LOCUS       WP_181755442             413 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Aeromicrobium
            phoceense].
ACCESSION   WP_181755442
VERSION     WP_181755442.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 413)
  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 413)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 413)
  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..413
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..413
                     /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=46679
     Region          53..412
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mrfrsspprg lfrrfligsl lvqlgavvsl mtatsirkrm rgkgteplpr ieaehftigg
       61 gnevqvyvsg ealyddmlaa iagahrrill esyiikgdem grrfrralrd aadrgvevcv
      121 iydgfanlvv ppaffrfghg vhmmrypilp hrlaffspra wgrnhrkilv vddaigfvgg
      181 ynigslyade wrdthvavtg pavwdlenaf idfwndvrph esmtplsest wdphvrahrn
      241 vprqliypir gmyleaidra tksieitqay fipdknilqg lvdasrrgvq vrilvpkvsn
      301 hvvadfvarg yfgqlldagv eilrysdhmv haktmtvdge wstigtanid rlsltgnyei
      361 nleilddgla egmsriferd aqsaqvldvq awrdrptiar lyerllspwr plv
//
LOCUS       WP_181755432             433 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Aeromicrobium phoceense].
ACCESSION   WP_181755432
VERSION     WP_181755432.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 433)
  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 433)
  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 433)
  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 433)
  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..433
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..433
                     /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=46791
     Region          1..428
                     /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 mmyalgvvlf ligvaasial hevghmwpak kfgikvtqyf vgfgrtlwsv krgeteyglk
       61 aiplggfvkl vgmlpperee rdrdghlvvr ssntglftqm atdaraaeye didpadedrl
      121 fyrkpwwqkv ivmaggptvn lfiatvlfsi sfmafgvptp tttvsavsdc aitdaeagra
      181 ctdadpvtpa rqaglepgdv lttfngepld dwtevttlir rngdseatig ferdgaerev
      241 tvntsvlara avddperten vgflgvsptf vterqgpgfv vvqmgdmiga tanalvhlpv
      301 rmvdvakaaf gaerdaegpv svvgasrvag elvtyddptw aertqrlisl laslnlflwl
      361 fnlipllpld gghiagalwe qirrtfarlr grpdpgfvdv akmlpvaygv glvlivmgvv
      421 liyadivnpv rls
//
LOCUS       WP_181755326              91 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: type II toxin-antitoxin system RelE family toxin
            [Aeromicrobium].
ACCESSION   WP_181755326
VERSION     WP_181755326.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium
  ORGANISM  Aeromicrobium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
REFERENCE   1  (residues 1 to 91)
  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 91)
  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..91
                     /organism="Aeromicrobium"
                     /db_xref="taxon:2040"
     Protein         1..91
                     /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=10467
     Region          5..89
                     /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 mtdepwrvef saaavrtldr lphkiavavv efctgtlpqd pyrmtkplry elegwsvarr
       61 gdyrvtlril dddhclligr iehrstiyrg p
//
LOCUS       WP_181755132             524 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SLC13 family permease [Aeromicrobium].
ACCESSION   WP_181755132
VERSION     WP_181755132.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium
  ORGANISM  Aeromicrobium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
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="Aeromicrobium"
                     /db_xref="taxon:2040"
     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=55104
     Region          114..520
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mstaeerptt yrtfdevqet lspaeqrfer irrttglfag pvlgivvyla cssldepaqr
       61 lagvlawvav ywiceaipip vtamlamaav ialgiapadd vfgsfgnsti fvfiggfila
      121 esmskhgldr rfafgilnlp giarsttriv vafgvitavl sgfvsntata ammmpiaagi
      181 vgfmasamrr sgdgdvdvnp qrlrfatalm lmvaysasvg glltpvgspp nligraylee
      241 elditipffq wmllafplvl vmfavlcvll vrlnkpelkh vegvegyite ereklgsmgt
      301 ggrntliafg vavtlwilpg avglvtgges atydwllehl degavaifaa sllfllplnw
      361 ekreftlnwn davkidwgti ilfgsgialg gllsstglae tmgtslgdll gtetlvgiti
      421 latviaviis ettsntasvv vvapiaaqla laadvnpaip vlaaifgasf gfmlpvstpp
      481 naivygtgmv pitkmlrsgi vfdvigivii vtgvtvmanl lgig
//
LOCUS       WP_181755523             199 aa            linear   BCT 28-DEC-2024
DEFINITION  D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
            [Aeromicrobium phoceense].
ACCESSION   WP_181755523
VERSION     WP_181755523.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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 11415520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..199
                     /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=21091
     Region          26..>153
                     /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 mwsaeallgr dtseippper dvpwdlvlld rdgtlnvhrp gyiaspaelr lrpgaahavg
       61 qltraglrtv lvtnqrgiat glltesqlve vhaalvsrla raggrldaie vcphqtgtcs
      121 crkplpgmll ralarapwar pervvmvgdq psdeaaahaa gvawldagps gvgsariadv
      181 lisrdphrsg svvlrsrer
//
LOCUS       WP_181755731              74 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Aeromicrobium].
ACCESSION   WP_181755731
VERSION     WP_181755731.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium
  ORGANISM  Aeromicrobium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
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="Aeromicrobium"
                     /db_xref="taxon:2040"
     Protein         1..74
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8100
     Region          10..72
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mppeddehrv hcrldellad rgmtltrlae ivgvtvvnls vlkndrarai rfttltaice
       61 aldceigdll viae
//
LOCUS       WP_181755848             404 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Aeromicrobium phoceense].
ACCESSION   WP_181755848
VERSION     WP_181755848.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..404
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43270
     Region          20..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 mrlplegvtv vaveqavaap latrqladlg arvikverrd ggdlsrgydh vvdgtgahfv
       61 wlnrgkesva vdlktaegrd ivrrlvdsad vfvqnlapga akrlglgtde lrsnhpelit
      121 vdlsgfgtgg pheqrkaydm liqaeaglis itgtpetavk tgiptadias glycaqavla
      181 allrrwrfge gasievsmle atvewlghal ytqmftesap prmglghtsi apydafptrd
      241 gevligvqnd rgwrslvrdv ldapeladdp rfvtnvdrva hraacdaava shtrrwatdd
      301 litsleaagv paaqvkqmsd vvshpqlrar grwrevateh svvpallppa tfsdveaamg
      361 avpalgehtr tvlqglglrd qqidelvkhe ivtsdprlpa ltss
//
LOCUS       WP_181755872             638 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Aeromicrobium phoceense].
ACCESSION   WP_181755872
VERSION     WP_181755872.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 638)
  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 638)
  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 638)
  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 638)
  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..638
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..638
                     /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=65863
     Region          30..630
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msaacgcehd svamtgedfd esgrpwwrdr gvmvpvfsgl afllglvaer sgaetpalvl
       61 fwvglllgas tftpaairnl fkgklgigll mtisaigavi lgyveeaaal aflysiaeal
      121 edkamdrarg glrallklvp etatvlrdgv aeqvqakdlv vgdvmmvrpg eriatdgivr
      181 sgrssldtsa itgesipvev epgdpvsaga insagaleie ttaagtdnsl ttivelveqa
      241 qaekgdrarl adriarplvp gvlilavlva llgsilgdpd vwitralvvl vaaspcalai
      301 svpltvvaai gaaskfgviv ksgaaferfg tvrhvavdkt gtltrnepav tavlvvegit
      361 eaqglawaaa leqhsthpla aaitaaaqdv plaaevteqa ghgidgtvdg mkitvgsprw
      421 ldagelgarv edlemqgmtv vivhrdgvpv aaigvrdelr pevpdvvrtl tdhrvgvtml
      481 tgdnartara laaqagiddv raelrpedka aaitelseag svamigdgin dapalaaadi
      541 giamgatgsd aaiesadvaf tghdlrlipr afeharrgrr iinqniilsl liiaallpla
      601 lfgvlglaav vlvheiaevi vilnglraar tpaprleg
//
LOCUS       WP_181755916             459 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Aeromicrobium phoceense].
ACCESSION   WP_181755916
VERSION     WP_181755916.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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..459
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..459
                     /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=47881
     Region          6..458
                     /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 mdrppdasea larahqhals wlatlpdrpv ppaasvadvi aalgadlpeg ptdpvevvdl
       61 laraaepglt ampsgrffgf viggthpaam aadwltsawd qnsgmrtvtp aataaddiae
      121 awvldllglp adgavgfvtg gttanftcla agrdavltra gwdvgtrgla gspgvrvlag
      181 aeghgsvdla lrylglgape lvpvdaegrl laealgtmld egddeqpamv vlqagnihsg
      241 afdpfdeait vahehgawvh idgafglfag aspsfrhlvh gyeaadswat dahktlnvpy
      301 dcglaivrdp aalraamsmh gdyliqdaag dpfekvpels rrgraftvwa vlrslgrrgv
      361 aelvdrmagh arafadgiag iesaevlndv vftqvcaafg dddrtrdvvr lmledgtawt
      421 tgsvwhdrav lrisvsnwst tdtdvertld alraavaat
//
LOCUS       WP_181755978             152 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Aeromicrobium phoceense].
ACCESSION   WP_181755978
VERSION     WP_181755978.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 152)
  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 152)
  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 152)
  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 152)
  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..152
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..152
                     /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=16593
     Region          58..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 mvilepatae nwrdiakvra sdaqggwvae ptyylclsay dglwrscavr tedgttvghv
       61 mwavdpddds hwigglmida erqgeglgra tvealltlwe reepalsgtp yreaalsvsa
      121 dnevalglyr slgfvetgel sddeivlrrp rp
//
LOCUS       WP_181756028             152 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RrF2 family transcriptional regulator
            [Aeromicrobium].
ACCESSION   WP_181756028
VERSION     WP_181756028.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium
  ORGANISM  Aeromicrobium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae.
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   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..152
                     /organism="Aeromicrobium"
                     /db_xref="taxon:2040"
     Protein         1..152
                     /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=16672
     Region          2..139
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrvstksdya lralielaae pgdkpvtade lgrrqdiphg flqsilgdlr kagillsqrg
       61 qsggwrmarp pyavtvadvf ravdgpivsi yglrpeavey ngraeilkpv wiaardalre
      121 vletvtieql aegalpssvm krtehieawr sr
//
LOCUS       WP_181756087             133 aa            linear   BCT 28-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Aeromicrobium
            phoceense].
ACCESSION   WP_181756087
VERSION     WP_181756087.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 133)
  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 133)
  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..133
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..133
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=13420
     Region          79..129
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
ORIGIN      
        1 msitldhtaf apldlarrpv vtrttyasat aapsapvrlt grgrvaivav alaiittlvi
       61 vfgsavvatg sasdpgivtt vtvqpgqtlw siaaearpna diratvdeiv klnaledgap
      121 lpigstlavp vqd
//
LOCUS       WP_181755991             267 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Aeromicrobium phoceense].
ACCESSION   WP_181755991
VERSION     WP_181755991.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 267)
  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 267)
  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 267)
  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..267
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..267
                     /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=27802
     Region          2..264
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mrcavvgspi shslspamhr aayrqlgldw sygafdvqdg eltefvsehr egwrgysvta
       61 plkreaagla aerdayveal gvantlvaid ggwsahntdv pgavsalhei gvgslrsvri
      121 vgagataasm alacrrlgar evelrvrdta raastartie glglavtvvp lhvevlesvd
      181 llvntvpdgs lagrehgfvg atnavfdavy dpwptalmrs arsegrslat gldllahqav
      241 lqvslmagdt vepavlvtaa mealasr
//
LOCUS       WP_181756387             252 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Aeromicrobium
            phoceense].
ACCESSION   WP_181756387
VERSION     WP_181756387.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     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=27192
     Region          1..250
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtrtalitga tagignafar qlarrgthlv lvardtvrle qvaaeltdah qvevevitad
       61 latlqgmdrv adrlsesgrp idllvnnaga slagwfgsta iadedrqldl lvrapmhlmd
      121 aaiksmsgrg rggiinvasv aaftprgays ahkawlvnis qwanwhyadv gitvqalcpg
      181 ftrtefhqrm gaeisnvprw mwlkadavvk dslrdlergk aisvpslryk vlmavaryap
      241 atvvakiaqr gr
//
LOCUS       WP_181756486             317 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Aeromicrobium phoceense].
ACCESSION   WP_181756486
VERSION     WP_181756486.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 317)
  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..317
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..317
                     /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=32950
     Region          10..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 mslptvlqnr lslpvvaspm fiasgpelvi aqckagvvgs fpalnarpas llgdwldrie
       61 selegtdaap favnqivhrs nnrleedmat ivehqvpivi tslgarpein eavhsyggiv
      121 lhdiinnrfa hkaiekgadg liavaagagg hagtlspfal vqeirqwfdg plllsgsiah
      181 grsvlaaqaa gadlayvgsa flatdeanvv egykqmives saddivysdl ftgvhgnylr
      241 gsieaagldp rnlpagdpst mdfgsgstsd akawkdiwga gqglgavdat vpaaelvarl
      301 treydaakre llaavpa
//
LOCUS       WP_181756433             556 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Aeromicrobium phoceense].
ACCESSION   WP_181756433
VERSION     WP_181756433.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 556)
  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 556)
  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..556
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..556
                     /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=60478
     Region          8..455
                     /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 mtilddnryv alarlvrrhg rsdllagaql defdiddetp lgdaeraeaf addlermgpt
       61 fiklgqllst rfdllpasyt talerlqdev dpiefeavre vvetelgatl rerftefdpe
      121 plaaaslgqv hravlrngre vvvkvqrpgv rdvvredmkv lgrlarladk rtevghrfgf
      181 grlldqfrrs lageldyrre arnlvtfgel taaydlllvp qpvpayttsk vltmdfvkgr
      241 kvtdigqlgl vdldarpive qlfsaylrmi ldagilhadp hpgnllltdd grlalldlgm
      301 tasvpprvqh diiklllais dgdgeetasi lasmghpldg fdagafrddv shlvseaias
      361 gadvavgavl vdlsrlsgah glrppaemsm vgkallnldr stshldpgfs paeairenvs
      421 diftagltmt pggivaaaie sktfvaelpk ranrimdala egefrvkvda mdeqrlhmvl
      481 qrianrltlg iiiaatilga altmrvpsew sllgypglam llflfavcsg iamavwilmt
      541 drkvartqhp tgppps
//
LOCUS       WP_181756704             416 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Aeromicrobium phoceense].
ACCESSION   WP_181756704
VERSION     WP_181756704.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     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=46119
     Region          137..408
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mttlsplaap qwpslvlpps trtsdlraam arrlftsavd rldvtvefdg hilgaggprm
       61 tihrpeeffr rlgsqpstgf gesymtaawd addlggfltv laagirtlvp rplqvmrsav
      121 mprpprderg dkadtqrvvg hhydlsndlf etfldptmty ssalfdetvt gtpvvggdle
      181 qaqerkldrl ldlarvgdgt qlleigsgwg slalraarrg arvrtitlsv aqqqlareri
      241 aeaglqdrid vdlcdyrdve grydavvsie mieavgwrhw stylatidrv lepggnaaiq
      301 aitmphdrmk atrntqtwvt kyifpggflp svraleeata gtslrltste aigahyaetl
      361 rqwdeaflar adevralgld dtfsrmwhfy lqysragfss gylddhhlvy tkesgr
//
LOCUS       WP_181756640             701 aa            linear   BCT 28-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Aeromicrobium phoceense].
ACCESSION   WP_181756640
VERSION     WP_181756640.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 701)
  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 701)
  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 701)
  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 701)
  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 701)
  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..701
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..701
                     /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=75824
     Region          8..559
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
     Region          <664..>699
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
ORIGIN      
        1 mttiatttad ealerlralt grpdarfheg qleaiaalvd qqrralvvqr tgwgksavyf
       61 vatallrsrg agptvlvspl lalmrdqvaa aeragvraaa insatveewd diearlaadt
      121 idvllvsper lnnptfreqq lprlldrmgl lvvdeahcis dwghdfrpdy rrlahviesl
      181 gpqvpvlatt atanarvvad vadqlggdvl tlrgslards lrlgsltlps akqrlgwlva
      241 hlgdltgsgi iyaltvsaae dtarllreag fevraytgrt dpsereeleq alkdnrvkal
      301 vatsalgmgf dkpdlgfvvh lgapsspvay yqqvgragra tdradvlllp gpedrdiwry
      361 fatasmpdpe radrvisqlg sepistpale alvdikrtql elllkvldvd gavrkvrggw
      421 iatgqpwvyd aeryeriaaa reheqqamlt yergqtcrme llqrdlddps atacgrcdvc
      481 taawyptdvp eatvgratea ldrvgvpiep rgqwptgadr rgvevkgria aeeraetgrv
      541 iarltdlgwg gtlrelfaag apdreipepl vgaavralrd wpweqrpvav vgmpsvtrpt
      601 lvastaetis rlgrmpllgt ldldphipra etggnsafrl asvwgrfsvg pelasalrna
      661 pgpvllvddl vdsrwtitva arelrragat avlpfalatv a
//
LOCUS       WP_181756652             324 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Aeromicrobium phoceense].
ACCESSION   WP_181756652
VERSION     WP_181756652.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (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   2  (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   3  (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   4  (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 10790899
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..324
                     /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=32038
     Region          3..324
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mfalvatlva aglavmalti gdyglspsqv lralagdgsd plaeffvreq raprvvcall
       61 vgaalgvsga iiqqvsdnpl gspdivgfti gaatgaliqi tvlgggpdat apaalvgglv
      121 taavvgalaw qggrhggipg vrlvlvgigv aavlqavntl lvvradlsaa qdaahwlags
      181 fnamtwqdva rlglvlavva pftaalartl pvlalgddaa rgigvpvess rlalvvcgvv
      241 lvaaatavag piafialaap qlarritrta gsglasaalm gaaltlasdi vaqrlfaptq
      301 lpvgvvsgsl gglyliwllt rekr
//
LOCUS       WP_181756765             259 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Aeromicrobium phoceense].
ACCESSION   WP_181756765
VERSION     WP_181756765.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phoceense
  ORGANISM  Aeromicrobium phoceense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
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="Aeromicrobium phoceense"
                     /db_xref="taxon:2754045"
     Protein         1..259
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27965
     Region          14..257
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 msdssargas pvrpgaepff apggrvgvll shgftgspas mvpwgrrlae tghtvtvprl
       61 pghgttwqem ntttwrdwyg eldtaltdlr sqcdfvavcg lsmggalalr laeqrpddvd
      121 alvlvnpaia lkrrdlklvp llsrvlpsmp gvgndiklag qdevaydrmp lkamasqlql
      181 wrdvrenlds vtapllmfrs tedhvvdatt aglvmkgvss pvrelvelnd syhvatldhd
      241 aefimersaq fladhapva
//
LOCUS       WP_181757196              96 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Bacteroides].
ACCESSION   WP_181757196
VERSION     WP_181757196.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
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   Rosinski,J.A. 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 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 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     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]"
                     /calculated_mol_wt=10962
     Region          20..79
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mrkeiedelt aikqllllgt knvlnmddas lltgfskshl yklvcakeip hfkskggkit
       61 yfkkdeletw mlnhrvathe eieqqvanys itrkkg
//
LOCUS       WP_181757211             834 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Bacteroides sp. CACC 737].
ACCESSION   WP_181757211
VERSION     WP_181757211.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            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 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     Protein         1..834
                     /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=92363
     Region          33..211
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <346..827
                     /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 makknstakd telslsffgk vaalfrsetv hfviglvlvi fsvylllafs sffftgaadq
       61 siidggsaqe listnngvkn yagsrgaqla sylindcfgv ssflilvfla vaglklmrvr
      121 vvrlwkwfig cslmlvwfsv ffgfvfvdqy kdsflylggm hgynvsnwlv sqvgvpgvwl
      181 lllvtaicfl iylsartviw lrrlfslsfl krkekaesvq getpeefkts wgakekaaap
      241 tpeaaepekv lekeeeiate eeepeslnei tldlggsdgk ikpaksaded vtmtfetpvp
      301 epvppfreqp vekepafqve kaeeeeyvgt ekepynprld lenyhyptid lmkhyddngp
      361 tidmveqnan kdkiintlrs fgieistika tvgptvtlye itpeqgvris kirgleddia
      421 lslsalgiri iapipgkgti gievpnsnpk ivsgqsiigs kkfqestydl pialgktitn
      481 evfmvdlckm phvlvagatg qgksvglnai itsllykkhp aelkfvlvdp kkvefsiysv
      541 iehhflaklp dgedaiitdv tkvvqtlnsi cvemdtrydl lkaahvrnik eynekfinrr
      601 lnpekghkfm pyivvvidef gdlimtagkd velpiariaq laravgihmi iatqrpttni
      661 itgtikanfp ariafrvsam vdsrtildrp ganqligrgd mlflqgadpv rvqcafidtp
      721 evaeitkfia rqqsyptafy lpeyvdenag gdlgdvdmgr ldplfedaar lvvihqqgst
      781 sliqrkfaig ynragrimdq lekagivgpa qgskarevfc idendlemrl nnlq
//
LOCUS       WP_181757273            1049 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. CACC 737].
ACCESSION   WP_181757273
VERSION     WP_181757273.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1049)
  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 1049)
  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 1049)
  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 1049)
  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..1049
                     /organism="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     Protein         1..1049
                     /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=115643
     Region          30..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqvnlriyr tiltlllglf lsagayaqqi svkgtvkdqt gepviganvl vkgttngvit
       61 didgkfllsa akdgvlvisf vgytsqevpv tgkeltvilk edtelldevv vlgygasark
      121 qdlsasvgvv snteelaarp vtstesmlqg qlpgvtiqad ggdptsspsi virgqgsqdg
      181 dnvlwvvdgv pgapiasmnd iesivvlkda asaaiygaqs gaggvvlvtt kkakegapsl
      241 tydgtfgirq atnlieplna eqqlemrkms yanagltlpd gwdinknpwi gttrtdwmde
      301 ifrtafyqrh nvalnvgten fthrlslayd ndegvlintf kknlslryns klklnkwvsi
      361 sedftwqnts srtkstdnda ftgpiisaiy mpasatvynp ldgsyggttt edpeyikkyg
      421 snfadahgda vnpvrlleae nvydktsdvw sttslnidnv ipglkfvsrf tynlrtnhfk
      481 kfnpirdevg kpvlsnnlqe ttyradawkt entltydntf gdhtigvlla ttadhsetrg
      541 levtgtdlad esaylqylay akslkgtdyl tgpdanvsli grlaysyadr yfltasfrrd
      601 yagrlpkenn ygdfpaftlg wkisnesffk ksdlisllkv raswgrigni ssvpiayksp
      661 vldktswneq aqygvasntv wgnivfiptd alnvdltwet seqtdlgldv emfnnrlsls
      721 mdyfdkrtfn liqtrttgwp qtigvkrqli nlgevrnrgf evsvnwsdki nknlsyfvsg
      781 nfsylknwvs digvknadgt sgvwtsdktf rnlpymiqsa egkplnsfyl iktdgifqsd
      841 eeaanyknkd gkpiqpgaqa gdlkfvdyng dgeisdedrq ymgnampktt faftlgvtwk
      901 klsisamfqg vggaqalyvg ksmllsdveg sfnrsaeiln awsptnkgsd iprlsklddn
      961 knftrpsdyf lenssylrfk nltvsydlsd vfrkwshlne rnsrlsvyfs genlvtftgy
     1021 sgmdpecggw dalkypvsrv lsvgvklty
//
LOCUS       WP_181757265             345 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase [Bacteroides sp. CACC 737].
ACCESSION   WP_181757265
VERSION     WP_181757265.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 345)
  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..345
                     /organism="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     Protein         1..345
                     /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=38807
     Region          14..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 mltkvieqsk idhftkwfdr adkivivshv gpdgdaigss lglwhffssq gktanvivpn
       61 afpdflkwmp gskdillydr ykefadklia eadviccqdf naihridamg davlaspark
      121 ilidhhlhpe dfckiiishp eisstselvf rlicrmgyfs disregaeci ytgmmtdtgg
      181 ftynsnnrei yfiisellsk gidkdeiyrr vfntysesrl rlmgyvlsqm kvypdyhaal
      241 isltkaeqsq fdyvrgdseg fvniplsikg vifscflred tekpmikisl rsvgtfpcnq
      301 laaeffgggg hlnasggefy gtmdearkvf eqalekykpl lnakg
//
LOCUS       WP_181757291             457 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Bacteroides sp. CACC 737].
ACCESSION   WP_181757291
VERSION     WP_181757291.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 457)
  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 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 10165816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     Protein         1..457
                     /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=50069
     Region          173..428
                     /region_name="Peptidases_S8_9"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 9; cd07493"
                     /db_xref="CDD:173818"
     Site            order(180,216,278..280,320,322..323,394)
                     /site_type="active"
                     /db_xref="CDD:173818"
     Site            order(180,216,394)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173818"
ORIGIN      
        1 mkrlvllsaf vlfaagasaq qdtlkyrisl kdkaattysl ehpeaflsek aierrrkqnl
       61 pidstdlpvc rkyvdeirrq gakivvtgkw enfvtvscnd salieriaal pfvrktekvw
      121 iapggdgpfm aterdslinr psvhpdsiyg lavdqirlsn gdklheegfk gqgmtiavid
      181 agfhnadkit amqnirilgt kdfvnpqsdi faesshgmav lsciamnrpg vmtgtapeas
      241 fwllrsedey sehlveqdyw aaaveyadsv gvdvlntslg yyafddkskn yklrnldghy
      301 almsrqasri adkgmvlvcs agnsgtgswk kitppgdaen vltvgavdke avlapfssvg
      361 ntadhrikpd vvavglgadv irtdgnqgra ngtsfaspim cgmvaclwqa cpeftakevi
      421 elvrrsgdrt dypdniygyg vpdmwkayqd yqsernk
//
LOCUS       WP_181757358            1011 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. CACC 737].
ACCESSION   WP_181757358
VERSION     WP_181757358.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1011)
  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 1011)
  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 1011)
  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 1011)
  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..1011
                     /organism="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     Protein         1..1011
                     /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=111707
     Region          35..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknlnlpkk kigrlknlfl tvcllasvaa saqektvtgt vtdtlgdpli gatvlvqgts
       61 ngvitdidgr ysiqatpent ldfsyvgmvk qavkvgsqsv invqmkddsq mlaetvvigy
      121 gsakkrdltg sitnikgdei ankpvvnpvs alqgkiagvq vinsgkagsd peirvrgtns
      181 ingykplyvv dglfndninf lnpqdiesme ilkdpsslai fgvrgangvi iittkkakeg
      241 qtrvningsf gfksvtdkia ltdaegfkll yneqlknegn peynfsdwtg ntnwqdeifq
      301 tgfitnnnis itgasdknsf ylgagyayeq gnikhekysk itlnisndyk vtdnlkvgfq
      361 fngarmlpad tksvatalra apvahvfnse yglytslpgf qkaqmnnpmv dvdlkanttk
      421 aenyrgsgnv ygqwdflksf qfkamfsldy asnntrtytp iiqvydasve gdiatlgngk
      481 tgvsqakete mkvqsdyllt ytnswgdhnv tatagfttyy nklenlngar tqgvglvipd
      541 npdkwyvsig daatatngst qwerstvsvl arvlynykgk ylfngsyrrd gssafsytgn
      601 qwqnfysvgl gwlmseeawm kditwldmlk lkgswgtlgn qnldraypae plltnaysav
      661 fgtpsaiypg yqlaylpnpk lrwekveawe agaeanflrn rlhfegvyyk kktkdllaev
      721 pgisgtvpgi gnlgsiensg velalswrdr igdwnynigm nlatiknkvl slvqegysii
      781 agdkqqsytm agypigyfyg ykvegvyqtq eeiehspknt latvtpgdlk frdvngdgei
      841 ttadrtmign ptpdvtygft lglgyknwel avdmmgqggn qiyrtwdnyn wsqfnfmeqr
      901 mdrwhgegts ntqpllntkh tinnlnseyy iedgsffrir nmslaynfdk aliskigmqa
      961 lklyvniqnl ktwkhntgyt pelggsaiaf gvddgsypmp aiytfgfnlt f
//
LOCUS       WP_181756993             576 aa            linear   BCT 28-DEC-2024
DEFINITION  apolipoprotein N-acyltransferase [Leptospira noguchii].
ACCESSION   WP_181756993
VERSION     WP_181756993.1
KEYWORDS    RefSeq.
SOURCE      Leptospira noguchii
  ORGANISM  Leptospira noguchii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Bork,P. and Koonin,E.V.
  TITLE     A new family of carbon-nitrogen hydrolases
  JOURNAL   Protein Sci 3 (8), 1344-1346 (1994)
   PUBMED   7987228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Leptospira noguchii"
                     /db_xref="taxon:28182"
     Protein         1..576
                     /product="apolipoprotein N-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016410 - N-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=65487
     Region          27..571
                     /region_name="Lnt"
                     /note="Apolipoprotein N-acyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0815"
                     /db_xref="CDD:440577"
ORIGIN      
        1 mfysfiskds ilyrlilcfg igigtlfgls pfsffsagvi vsisciflff slnrtsiwka
       61 llwllvlsqi vnfsafywip gaisrisgtn tfvsvlffll yglishlkff pfyslfrfsk
      121 iesisktcil lvfpaagtls dmitfqifpw ywgnlisgsi vfeqfasifg vyglsfllll
      181 isstfiifln yykhksskef iisitslvci tfvfgyglyr igytnqsqne vktkdlsvli
      241 vqpdtspgtk ilkadasyls atmskvfsla lpssenspsl ivipesaipf hgtidseenr
      301 kekiyspsme givlylskht gadilfneln lnenklknqi slfknldgkt erydkrrllp
      361 fgeylpmekk fpflrsifqe tsnyipgefp kllignkiqn qkpillteis klnepetyrs
      421 efssiekrtn kirnleysys ilpllcyeam ftelvldyfq ngqkpevlin itndswfnse
      481 leayqhsgav rlraietglp lirsavsgis evwdargipl ivpmgfhetg trsfsiqlga
      541 veptiytrfg nsflwifcvl ilisrlifvl rierks
//
LOCUS       WP_181757578             621 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidase U32 family protein [Bacteroides sp. CACC 737].
ACCESSION   WP_181757578
VERSION     WP_181757578.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            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 10002826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     Protein         1..621
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=69907
     Region          5..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          437..504
                     /region_name="DUF3656"
                     /note="Collagenase; pfam12392"
                     /db_xref="CDD:463557"
ORIGIN      
        1 mikqrkiell apaknlecgi eavnhgadav yigapkfgar aaavnsledi aalvehahly
       61 nariyvtvnt ilkeeelket ermiwelyri gvdalivqdm gitrlnlppi plhgstqmdn
      121 rtpekvrfla dagfrqvvla relslqeirg iheacpdvpl evfvhgalcv sysgqcyvsq
      181 acfgrsanrg ecaqfcrlpf slvdadgkti vrnkhllslk dlnqsevlee lldagatslk
      241 iegrlkdvty vknvtaayrr rldaifarrk eyarassgtc rfdfqpqldk sfsrgfthyf
      301 lqgrggeits fdtpkslgee mgtlkeqrgg yltvagikpf hngdgvcfld eqgrlqgfri
      361 nrvdgnklyp agevprikpr trlyrnfdqe feriltrkss erkigvcwel adnsfgfslt
      421 aadeddnrvt lsfpypkela rtpqadnlrs qlaklgntpf evaghlseea sgirlnlsan
      481 wfipasvvad wrrqvidkli earrvtyrre lavwkptsha fpatsltylg nvmnsaarsf
      541 yrehglssia payeaqavpe avlmfckhcl rfsmgwcpty qkghspyrep yylvetdgkr
      601 frlsfdcknc qmkviaheep l
//
LOCUS       WP_181757650             326 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Bacteroides sp. CACC
            737].
ACCESSION   WP_181757650
VERSION     WP_181757650.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 326)
  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..326
                     /organism="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     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=37395
     Region          145..305
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mkhtflflll tfllgltacs kpagrtlmny eqalshadsl vqcgavdsar avrlisglhr
       61 eysqikelsd grhvrlkpvs gyerffwgvf svimfsisga mlfslvrfkk erhhrnylit
      121 lseneqrlrn nerereelee clkemlltde ereevhsslt nlmehgsrld keneslrarl
      181 keyednpvpr elellrkege rvrmldgqvq alasavidad evvkqlriqp kfladsqwny
      241 lqkltdrvyk gaskrlvmrf pqltpadsql cmlirlhfsn aqiatliavs pasvsqqkfr
      301 lkkrmmqadg glfadgetld tvvchv
//
LOCUS       WP_181757716             437 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Bacteroides sp. CACC 737].
ACCESSION   WP_181757716
VERSION     WP_181757716.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
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="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     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=49593
     Region          30..436
                     /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 mrikffffil vlfllglggm lvyllsgkpl lylyvlegii gfiliylivf ynkivkpmnt
       61 igsgmellre qdfssrlsrv gqyeadrivn ifnrmmeqlk nerlrmreqn hfldlliqas
      121 pmgvviltmd devsqlnpma vkmlgvrmee amakrldqmd splaaelssi pkdetavvrl
      181 ndaniykcth ssfidrgfkh pffliermte evmraekray ekvirmiahe vnnttagits
      241 tldtveqals teddmedicd vmrvctercf smsrfitrfa dvvkipeptl vpvqlnelvs
      301 mckrfmegmc ndrnielrle cdpevgmvrm daslfeqvlv niiknaaesi egdagengqq
      361 geiivrttap asvevvdngp gisketeakl fspffstkpn gqgiglvfir evlsrhgctf
      421 slrtyndglt rfrilfn
//
LOCUS       WP_181757771             277 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Bacteroides].
ACCESSION   WP_181757771
VERSION     WP_181757771.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
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="Bacteroides"
                     /db_xref="taxon:816"
     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=31250
     Region          <193..277
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mefpqvdlpv dmiawtevte dilniykqsc rlkacifalc iegsitvsin lmdteikqgd
       61 fitllpgtii qfyeqkgkvc lgfvgfsshc lngvnliqst lssfsniley pvlavnptva
      121 syfkdyfalw arittgpypp dtkmaqsals mllsgvdkmy chrpqmqkgn ksrkeeiche
      181 lvqlvienyt rerraqfyad klgislqhls ttvrqvtgrn vldiiahvvi vdvkaklkst
      241 nmtiqeiays lnfpsasffg kyfkrhmgms pleyrns
//
LOCUS       WP_181757817             303 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Bacteroides sp. CACC
            737].
ACCESSION   WP_181757817
VERSION     WP_181757817.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 303)
  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 303)
  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 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   4  (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
REFERENCE   5  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..303
                     /organism="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     Protein         1..303
                     /product="helix-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=36115
     Region          6..301
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mgkklerlqr mlviinklkg lqryvpreel enyvthrmee rggipvdlrt lqrdfnaiee
       61 mfgiricfdk krngyyinee ddtkkeqyer lllnfdilna ldtssglhty vvaehhrpvn
      121 neylpllika ikfshpiifk ymyvrengkm rekevlphyl kedqyrwyll ayeenvlktf
      181 svdciidpqi lygktfkrnm didinslfkd cygiwnqtni pieeielsys pldgsflksv
      241 plhhsqeiiv ddekefrikl hlritndfvm allsrsrslt vikplhlreq vkaiyeealk
      301 rnr
//
LOCUS       WP_181757347            1058 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. CACC 737].
ACCESSION   WP_181757347
VERSION     WP_181757347.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. CACC 737
  ORGANISM  Bacteroides sp. CACC 737
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
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="Bacteroides sp. CACC 737"
                     /db_xref="taxon:2755405"
     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=117143
     Region          37..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklhanvcsq wewtklrqll vivllglgiv stygqtktvs givksesgge plvgatvkvk
       61 etntggitdi dgrytiqanl gqtlivsyig yrtkevkver ttridillqe dnemldevvv
      121 vgygtmkrsd ltgsvvsvtg delkksvvts ldqalqgraa gvqvtqnsgt pgggisvsir
      181 ginslngnep lyvidgvais gnntsnnsvl ssinpadivs mevlkdasat aiygsrasng
      241 vvlittrqge egktkvsyeg yyalqqlpkk letltlpeya vyqnlraati gfgareefkd
      301 psllsrgtdw qneifrtapm hnhqinisgg sksmkyslsg gymkqdgivf gsdferfsfr
      361 vnmdndinkw lttglrasva rtqqtnnvdg sgaiynalnq lpevparnpd gsfgmqtenm
      421 ygtyfsnpls dliqnenysr stqvyvnafa diklwkglvf rteyaanfny sndykftpsy
      481 dyehfkqqss asrgasngsn wtlktyftyn ntfgkhglsa mlgheaqenk yeslsgsrtn
      541 flfnsvheld agdattakan ssrgssaies yfgrlnynyn drylltatlr adgsssfake
      601 srwgwfpsva lawkvnneaf lkdveainsl klrlgwgvvg nqwagsyayg vtmasaasiw
      661 gtgfyagnyp nrelkweetn sfnvgldlal fnnriefiad ayykktdnll mqaslptyvs
      721 glirapwvna gamtnkgvef tlnthniqtr dftwtsgltf sinrnevtkl ysessaisgi
      781 ngsetltytm vgepvgqfyg ykvigmfkee gdfykkgadg nflldetgnr iqvaipkdqt
      841 igksgiwvgd yiyedrdnng videkdrtfl gnpapkftfg fnnylsykgf dlniflngsv
      901 gnkainlirr tftdpmrnsn llkeatgial iamydpevgd evlsnvyvan adaakvqrit
      961 tssandnnri sdrfvedasy lriknislgy tfpqkwlrhl qidhlrlyvn iqnlctitgy
     1021 kgydpeigal nynvllrgvd darypsqriy tfglnfnf
//
LOCUS       WP_181758186             335 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Cytobacillus solani].
ACCESSION   WP_181758186
VERSION     WP_181758186.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus solani
  ORGANISM  Cytobacillus solani
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Cytobacillus.
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="Cytobacillus solani"
                     /db_xref="taxon:1637975"
     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=35174
     Region          31..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 mkekqrsipf ifkltagtlv figmfvmacv fgaadiavkd vwlaltsdat sdkisiirei
       61 rlpreiaavf vgtalavsga imqgitrnpl adpgllglta ganaalaisi afipstnylg
      121 imiacfigaa igailvfgig smkkggfspl rivlagaais aflyalsegv giyfkisknv
      181 smwtagglig tswaqlqviv pfiligiivs lffsrqltil slneevavgl gqkttqvklv
      241 lfiviillag aavalvgnmv figlmvphiv raivgtdyrf iipmsaiiga sfmlladtlg
      301 rtinspyetp iiaiiamigl pfflfivrkg gkafs
//
LOCUS       WP_181758293             222 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Stappia taiwanensis].
ACCESSION   WP_181758293
VERSION     WP_181758293.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23483
     Region          1..167
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mkelfffdcd gvlvdsevls aattseilae qgitlsvqds iriftgktig daarlvaery
       61 dvtlpedyaa rheaallrrf teelreiagi rqvleactap vcvtsnstrs rlaltlqttg
      121 llryfgrnvf saedvaapkp apdlfrhaaa afgvdparci tiddsvsgia garaagarai
      181 gfcggshitd gtpaqllaag aeiclhsmae lqdylhsaap nr
//
LOCUS       WP_181758303             366 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DUF917 domain-containing protein [Stappia].
ACCESSION   WP_181758303
VERSION     WP_181758303.1
KEYWORDS    RefSeq.
SOURCE      Stappia
  ORGANISM  Stappia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Stappia"
                     /db_xref="taxon:152161"
     Protein         1..366
                     /product="DUF917 domain-containing protein"
                     /calculated_mol_wt=37810
     Region          1..356
                     /region_name="COG3535"
                     /note="Uncharacterized conserved protein, DUF917 family
                     [Function unknown]"
                     /db_xref="CDD:442756"
ORIGIN      
        1 mrrtltekdv epavrggsvy aaggggwadh grklgyaavg agapelvsid elndddwvat
       61 aaaigapast tpwemrgvdy vkavrmlnea lgtpvsgliv gqngksstln gwlpsailgc
      121 kvidavgdir ahptgdmgsi gmagsqeqmi qtavggnreq nryieltvrg atakvspilr
      181 tasdmsggfi asarnplras yvarnaalgg ismaldlgha ilaaepkgta avidtiveqt
      241 rgailiedvv tkknvvytne afdvgtvvvg sgdkaltlhv mneymaidda ggnriasfpd
      301 vittlstdae plsvgqleeg mrvhilhvpk sviplgagvl dpavypsvek amgielakya
      361 lepsna
//
LOCUS       WP_181758333             388 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Stappia taiwanensis].
ACCESSION   WP_181758333
VERSION     WP_181758333.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=40734
     Region          11..373
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mtdtpitapq pdtllahagg gldpstggvv paiqpattfa rdaeyrlisa shlyarddnd
       61 lsrqienlvm rledardtrv fgsgmaaiaa ivravkpgds ivvqsgiywg ttawmrahca
      121 hvgialvead ateterftet iresgpalvf levpsnpfla iadiraiaea thaagavlav
      181 dattatpllm kplalgadlv chsgtkalng hsdvlaglvs tadadsdmwr firaerhdag
      241 avlspfdgyl lqrgmrtlal rmermctsaq kiaehldahp avekvlypgl ashpghglak
      301 aqmnggfgyl msflvkgdap ealavigrln lilratslgg veslaehrhs legdssgvpr
      361 nlirlsvgie apedlladld aalsglpa
//
LOCUS       WP_181758311             612 aa            linear   BCT 28-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Stappia taiwanensis].
ACCESSION   WP_181758311
VERSION     WP_181758311.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 612)
  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 612)
  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 612)
  AUTHORS   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 612)
  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..612
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..612
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67968
     Region          60..611
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mtahkarkta rpagkdqaga qlralicpqs dpppkpdtet apahphenld rtvrataarl
       61 tggvsphafi eawsdwalhm arspgrqlel iehaqenvfk ltnyllnidd aaeppfapka
      121 hdhrfahagw nrapfeiwaq gflaaqdwwn yatdhlrglq pddadrtrfm mrqmldlmsp
      181 snfpalnpei ieatvqtrgr nlsegavhfa rdflhtmtqa hipappgyqv gkdlactpge
      241 vvfrndlfel iqyapkggtv qaepilivpa wimkyyildl sprnsmvkyl veqgftvfvi
      301 swcnptaeqa elsledyrkh gvmealnaid aivpgekvqa vgyclggtil aiaaatmard
      361 gddrlasitl maaqvdfaea gelllfldes qvafledmmw dqgyldrpqm arafatirae
      421 dliysravrr yflgqedapt dmgvwyadtt rmparmhsey lrglflenrl sagrfavegq
      481 vialkdirap mfvvgteadh iapwksvykt klftdndltf vltnrghngg ilsepghpgr
      541 hyrisprpag alyvgpdawl arhaprqgsw wgewsqwltd nsrgkadvpa mgapekgyap
      601 iaaapgayih qt
//
LOCUS       WP_181758471             715 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Stappia taiwanensis].
ACCESSION   WP_181758471
VERSION     WP_181758471.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 715)
  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 715)
  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 715)
  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 715)
  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..715
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..715
                     /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=78526
     Region          17..709
                     /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 miqrirlanw pillkvmaap latlgflall svhgwqtlkt qravltagye efapvlahay
       61 eipqslarid ahlyrlsvws qigvkgaele rtlksineel rqadggiqml esagvagtsr
      121 lrdafnayrd ntsqvmllil rnatlgavaa rggdaifsrv eslahqaaan asqhfqqran
      181 gasrdarema rkfiwqslla galavlasyl asraiihpir elvqtinrll hgklkgevpy
      241 sgrsdeigsi smsvrelqrv lienrkleee reekrvkley lalhdgltdl anrkafdlfl
      301 egairaphte kdnlicllid ldsfkpindt ygheagdavl relarrfsll arptdmvari
      361 ggdefgiait sddrpldaas iatrfldatr dpidhdgkvl rvgasvgavr lsdidgdgea
      421 lmaaadqamy aakqdkrpsf svftrnttpe rvgvhdreel eealrsgafv pyyqpkidlr
      481 skthagfeal arwhhptkgv ltpedflpri srfglqgdft gaittqvlad lggflqqgld
      541 pggvainiee atlashsgld dlcqliesvp hlaplitlei tedvfiaraa emirqnvetl
      601 aamgvrismd dfgtgygsfq hlrqftfhem kidtefvagi gkdrssevii egflsiangl
      661 gadvvaegie teaqerymrq rgchfgqgyr fgapmprata eiylrddkaa rqass
//
LOCUS       WP_181758631             394 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Stappia taiwanensis].
ACCESSION   WP_181758631
VERSION     WP_181758631.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 394)
  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 394)
  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..394
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..394
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45092
     Region          1..394
                     /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 mfitfltnlr dagvpvslre yltlmealka dladkkvedf yflaraclvk deinldkfdr
       61 vfgatfngle lgaggdgtep relpedwlrk laekhlteee kaeiealggf eklmetlrer
      121 lkeqegrhqg gskwigtagt spfgaygynp egvrigqaes rhrravkvwd krtfkdlddt
      181 velgtrnikv alkrlrrfar sgaaeeldld htiqstahkg lldikmrper rnaikvllff
      241 diggsmddhi rvceelfsaa rtefkvleyf yfhncpyefv wknnarrhse riptfdvlht
      301 ygpdyklifv gdasmspyei ayaggsvehw neepgsvwle rltshyaksv wlnpvpeqhw
      361 sfthsidmiq tlmggrhfpl tldgldnamk elsr
//
LOCUS       WP_181758545             144 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Stappia taiwanensis].
ACCESSION   WP_181758545
VERSION     WP_181758545.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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 10440481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=14544
     Region          56..138
                     /region_name="Cytochrom_C"
                     /note="Cytochrome c; pfam00034"
                     /db_xref="CDD:459641"
ORIGIN      
        1 mtgkgkvlal lavlavgiag vllfrggeap psapgaggaa lasvkvptrl sdveragegl
       61 faancatchg vnaagrdgqg pplvhkiyep shhadgaffl aatrgvrqhh wtfgdmapvp
      121 gvsqtdvaai vayvralqre ngif
//
LOCUS       WP_181758596             323 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Stappia taiwanensis].
ACCESSION   WP_181758596
VERSION     WP_181758596.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..323
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..323
                     /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=33438
     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(33,246,249)
                     /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 milvcgealf dlfaeedgdr ltldariggs pvnvaiglar latpvsyfga lsgdlfgrrl
       61 rttlaaegvr ldhvlatdap ttlsivglsa agspeytfhg egaadrqvrp adlpdlppei
      121 acihigsfam lvppvgdsla alvarehgrr miaydpnirp tvvadlaawr arlgallphv
      181 dllkisgedl atlypdrdaa tlaaawlarg pslvvvthga egaeaftgka hvaipghpva
      241 vvdsvgagds fqaamlarlg ergqlsaeal arldaedlgd llhfaasaaa ltctrrgadl
      301 prraelasac hsapfpspqn rgp
//
LOCUS       WP_181758707             258 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Stappia taiwanensis].
ACCESSION   WP_181758707
VERSION     WP_181758707.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=26267
     Region          9..244
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mtasssspsl aerlrhdeai vtawsslamp mlaealgrsg ygavtldmqh gqhdiasvre
       61 giaatrlsga hsvvrtpvdd fasvsrvldf gaeavimpmv nsvddalalv gaakfppmga
      121 rswgphraam lkgespaayl aganretlal amietpaala alddilavdg ldgvfvgpgd
      181 lsltlsagae vvpgsdrvqt vaadiavrtr aagkiagifc naaedargaq kmgfrfmahg
      241 vdmsllmeaa gaasavld
//
LOCUS       WP_181758647             250 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Stappia taiwanensis].
ACCESSION   WP_181758647
VERSION     WP_181758647.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=27458
     Region          56..164
                     /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 mtsiidccla lygardyfvr yparpaaeey wdgkadpdgr vrdlaserdq rkadlayiae
       61 avnarpsgrv vdvgcglgel leqiddrher igidpsekav evaaaqsgaq tlrgeltget
      121 fpagscdail ahhviehmda pvefvrsaak alkpgglfvv gtpnfasaaa rlfgdryrll
      181 hdpthvslft deslmrlmrd cgfrilsvey pffgtrfata eawermlrpe egvspafwgs
      241 fvtvfaekeq
//
LOCUS       WP_181758715             422 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Stappia taiwanensis].
ACCESSION   WP_181758715
VERSION     WP_181758715.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=44339
     Region          2..411
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrsvdvivlg agiagisaal hlqargrqvl lldrgpagee asrgnagvia rdgciphrls
       61 aspmvlgaqa lglrsdahvs wwgmrhhlpw lrafrdasas vgvsryvral apvqaaavge
      121 hlalaraana lrffrptglv klhdardaea aeleahfari ygtgyselss velarlephl
      181 varglravyw pdgqsvsspg gvtkayarlf rerggiidtg dalsltgahg vwsvrasrga
      241 veagtvvval gswsadlltp lgyafplaal rgyhlhlraa agaslsrpva dvargfvlsp
      301 mergirlttg velaprdapa rprqmaqala aareifplgs pvdaapwlga rpclpdslpv
      361 igpapahpgl wfcfghadtg falgpatgrl laemiagetp fadpdpfsar rfaagwemlr
      421 fa
//
LOCUS       WP_181758784             148 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Stappia taiwanensis].
ACCESSION   WP_181758784
VERSION     WP_181758784.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=15245
     Region          25..147
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mlklcargla ialplallag paaadpietr qnimksvgaa tgtlgkmikg eipydataan
       61 mamrvlftap sgfvhqfpdg tqtggkteas pkiwedragf ekiaadmema alaaipaasg
      121 gldqlkgafg svarnckach egyriqkn
//
LOCUS       WP_181759033             233 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Stappia taiwanensis].
ACCESSION   WP_181759033
VERSION     WP_181759033.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 233)
  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 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   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
REFERENCE   4  (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 18629734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=25025
     Region          53..231
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          164..231
                     /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 madpteiqsk aaaiaeaqtg khvldvieaq lrrmgashil vtglpmpnrp ieglvhrlrw
       61 aderlggier sgidaedsal mlglmrsraf iwdvtagdtt hselfasiga dsqvvvvpit
      121 eahpfqalvl gggaringgk lelsnlelic naafrrliel gvistqrpgd lsarerrvle
      181 ltalgktand iaslleisqr tvhahlqnas aklnasnkth tvvealrygq irl
//
LOCUS       WP_181759097             251 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Stappia
            taiwanensis].
ACCESSION   WP_181759097
VERSION     WP_181759097.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..251
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..251
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26156
     Region          <92..144
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          <189..236
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 msraqrkapr rktpaakpep sglgamaldn pvaaggwlvm vltgcliian atafqsgphp
       61 aplfatrkaa pppapaltpa eerarsaqrv lvrdvqvelr rlgvyegsld glkgpatdra
      121 vrayqrsrgl rdtgqidegl larlamdtgs gapeaglppl pvpppeppaa hqqtgsqset
      181 tlsgerarva riqaalvrlg ygplnvdgys geqtanairr feldrgkpit galspalvte
      241 iekvtgrplg g
//
LOCUS       WP_181759199             235 aa            linear   BCT 28-DEC-2024
DEFINITION  corrinoid protein [Stappia taiwanensis].
ACCESSION   WP_181759199
VERSION     WP_181759199.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..235
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..235
                     /product="corrinoid protein"
                     /calculated_mol_wt=25357
     Region          21..221
                     /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(112..118,121,158..160,162..164,193,209,212,215)
                     /site_type="other"
                     /note="B12 binding site [chemical binding]"
                     /db_xref="CDD:239021"
     Site            115
                     /site_type="other"
                     /note="cobalt ligand [ion binding]"
                     /db_xref="CDD:239021"
ORIGIN      
        1 mseeddldla slsdeelveq mhddlydglk deicegvnil lergwtpykv ltdalvegmr
       61 ivgvdfrdgi lfvpevlmsa namkagmgil rpllaetgap kmgkmvigtv kgdihdigkn
      121 lvsmmmegag fevidiginn pvenylaale ehkpdilgms alltttmpym kvvidamvek
      181 girddyivmv ggaplneefg qavgadaygr daavtvemak dliarkhnql aartg
//
LOCUS       WP_181759286             608 aa            linear   BCT 28-DEC-2024
DEFINITION  cation:proton antiporter [Stappia taiwanensis].
ACCESSION   WP_181759286
VERSION     WP_181759286.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 608)
  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 608)
  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 608)
  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 608)
  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 608)
  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..608
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..608
                     /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=63704
     Region          19..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 mdpvvigvav vamagvaaqw lawrfqlpai vlllvagavv gpisgiiept aefdtlvkpv
       61 vaiavaiilf eggltlnfhq isetskavrr lvvlgaptaf vlgalnayyv aglslwpalv
      121 fggilvvtgp tviipllrqa qlakrpasll rweailadpl galiavfvye tflvlsgqhh
      181 vdtlvlrivf alalgagggw llgralvwaf vrghvpeflk tplilasvla ayagsnvvle
      241 esglltvtvf glalgnsria slgevkrfke imtillvsav fivltaslkp eelvsalepr
      301 tlafvavlll vvrpasvwls tlgtglsvne rllvgwiapr gvvavavsgl fagllaargi
      361 adgerlvpla favvvvtvva hgfsigplar rlglssggag glfivganrf tvalaeklks
      421 levpvlvadr nwgrlrsarq agvathygev lsevaehtls lgsyshllaa sdnddynalv
      481 ctnfgpeigr sqvlqigrsd deaahqqlmv tlggrpflpd agglwaletk iaqgwrisat
      541 alreefdfaa mkaaraegaf tvlvvtgggr llvgpfeear tpkpgdtvln mvppeeppra
      601 arngavpq
//
LOCUS       WP_181759324             336 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Stappia taiwanensis].
ACCESSION   WP_181759324
VERSION     WP_181759324.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 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   5  (residues 1 to 336)
  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 336)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..336
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..336
                     /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=37207
     Region          <33..86
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Region          143..279
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
ORIGIN      
        1 mntapllsad qllaglrtvg eetrlrllal ladgeltvkd atailgqsqp risrhlkllt
       61 eaglvqrfpe gawvyyrlgd gpmgdlarll ltrldpeeal fsadrvrlaa trrakaeeaa
      121 ayfanraktw dqerslhvpe eavekairea vgtrpfdaml dlgtgtgsll slfsdqyara
      181 lgldashdml avaranldrq glrhaqvrhg diyalnvpke sfdliaihqv lhylddpgra
      241 iseaaralrp ggrmlivdfa phgleflrdt hahrrlgfaq dqmrrwlrea gldlvmtrdl
      301 vpdshdkehl tvtiwlardp rvvsdlpvln paqeva
//
LOCUS       WP_181759331             270 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Stappia taiwanensis].
ACCESSION   WP_181759331
VERSION     WP_181759331.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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   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 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   8  (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 18598964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..270
                     /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=29617
     Region          18..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     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"
ORIGIN      
        1 mvwlaqdsqf dpdsvcqpvf giaardlshh dsglhahrva qllfarrgcm titleaklcl
       61 lpptravwip aglvhraqmr tavdyrsvyf rppfaqdmps qievfevsdv lqatleriav
      121 apldvdwtmg aarnllavcm deirraprvp tllplpsdpr larldtaslp pslgqlasdv
      181 gagektigri frretgmsyq ewrqqwrllk ayellsagts iscvsqelgf agdsafisff
      241 khaagvtpkr yvrslnpgan aaatqetgaf
//
LOCUS       WP_181759406             385 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Stappia taiwanensis].
ACCESSION   WP_181759406
VERSION     WP_181759406.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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 385)
  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..385
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..385
                     /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=41729
     Region          15..380
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mplpftrqef sarldalcal mteqkldaml lfaqesmywl tgydtfgfcf fqtmvvtrde
       61 rivlltrsad lrqaqhtsvv gdiriwedra gaspvlqlre llfeldllgg rigveydthg
      121 mtgkvaldin qhlasfatlq dasalvpllr avkspaeiah vrraaeltda afvaglekia
      181 pgadegeila amqgavfagg gdypgnefii gsgqdallcr yksgrrvlaa ndqitlewag
      241 vyrryhvaam rtvvvgepts rhvalhtaar ealaaveanl rpgctfghvf dahaavvdah
      301 kltphrlnac gyslgarfsp swmdwpmays gnsaeivpdm vifmhmilmd sdsgtamtlg
      361 qtylttngap eclsnlpldl pvkag
//
LOCUS       WP_181759475             417 aa            linear   BCT 28-DEC-2024
DEFINITION  cation:proton antiporter [Stappia taiwanensis].
ACCESSION   WP_181759475
VERSION     WP_181759475.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=43493
     Region          1..>390
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mstgllmlam fvmvytmlak wlsstvltap ilflgfgyal agtglmpvge teallhvvae
       61 valilllfld aaqtdvtalr rhhvwplrml viglplavlf gtlaawpilp glplaavalv
      121 aailaptdaa lgqavignpk vpkrerqalt vesglndgla lplvllfasl saeamdgaat
      181 dwlafglkqv llgplvgaaa gwiggsvflt akdkgmttet megigtisla ggaylaagei
      241 ggngfiaafv aglafgnvvl grcrfiyeft dnegqmlawg affliglalv pqavmhlelw
      301 mlaiilpsmf lvrplaiwls ligtdapart rlffgwfgpr glatalfall vvpqidpelg
      361 epllmlavna vwisallhgv savpgarwyg alrhhgkadk tgkpgknggt pvpggra
//
LOCUS       WP_181759520             332 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase, partial [Stappia
            taiwanensis].
ACCESSION   WP_181759520
VERSION     WP_181759520.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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]"
     Region          3..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 ttnaggfgfl aaasippggi daaiaavkaa tdgpfgvnfh mfqpnaeevi eaillhrvra
       61 vsygrgpdaa tigrfrdagi ecmptvgavk havravelga siitvqggeg gghtgsvpts
      121 lllpqvldav dvpvvaaggf ydgrglaaal awgadgiamg trflltsdsp vhpatleryl
      181 ktgdpaairv skavdglpqr fidneelrrm egmrgparfl aslrhslswg raqgmsyagm
      241 vrlalralka deagfaatvm apnlprlveq glvsgdtrgg llpsgqvaal igelescdal
      301 iarivreaee rlavlrhlpg sdretvkqga ra
//
LOCUS       WP_181759569             275 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Stappia taiwanensis].
ACCESSION   WP_181759569
VERSION     WP_181759569.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=28960
     Region          206..273
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 maiiapeaer sgiaapavpl srvrtieean lngfpsdrql idgqwflrls pgnparrvns
       61 lnvfdpaddv dcaarlaaar tvfaragvaf hlrwtplvpq altghvdalg wlrigetgvw
      121 srpidadevm sgesagverv tladwlaafg atggtrpeav tplalsrlga slervaadli
      181 clvarsadga paavavavad rdllgiydla vapscrrsgl grqmvracla hgaaagcrea
      241 wlqvtaenas aralyrglgf seayryhyra ppdad
//
LOCUS       WP_181759714             263 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Stappia
            taiwanensis].
ACCESSION   WP_181759714
VERSION     WP_181759714.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 263)
  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 263)
  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..263
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..263
                     /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=29778
     Region          27..241
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mlllrsllfh alfylvtlgl milfspvlil prrwgwpvvp fwartclall rwivglkvev
       61 rglenipegg yivaakhqsa wetfallplf asptyvlkre lryiplfgwy takyrqipvd
      121 rgkrsvalar mtekageava egrqilifpe gtrrpagaep rykhgvahly rslecpvlpi
      181 alnsgvywpr rgwtlypgtv lveilppiqp glelhacyeh lvsavegasd ellreaarrd
      241 pdspvlalve erwrargrvf pra
//
LOCUS       WP_181759850             238 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Stappia taiwanensis].
ACCESSION   WP_181759850
VERSION     WP_181759850.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25309
     Region          62..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 mnaspkdpdf agrrnaardr ldglfgakgg dradrsawfh avyetaggdp aavpwadlaa
       61 kpellawlad npgggadapl raldvgcglg dnaealaaag yattafdlas aaidwarqrf
      121 pqstvdycaa dlfdppaawi gafdlvhecy tlqaldgalr aaafpatarl lapggrllil
      181 trsraegtea dgppwplmps eltrfeelgl ekvektpyel rkgerviphi ravfrrpd
//
LOCUS       WP_181760315             471 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Stappia taiwanensis].
ACCESSION   WP_181760315
VERSION     WP_181760315.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 471)
  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..471
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..471
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50375
     Region          21..450
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mltlapvlpa qaeltraasa adfatirvgg dmtsftldng lqvvvipdrr apvvthmiwy
       61 kvgaadeppg msgvahfleh lmfkgtkanp dgafsqrvaa iggvenafts ndytayfqrv
      121 akehlgemma leadrmenlv ltdevvaper dvvleerrmr vdsdpgarls etldamlyvn
      181 hpygtpvigw paeiealssd naiafydrfy tpnnailvva gdvdaqevra laektygavr
      241 rraepgarsr papqlvpgtr qvtlndarvn qpnvrqvwlv psyttaegrd alaldllaei
      301 lgggstsrly rqlvaddaia asaggwyqst slddtsfmiy avprdghtle elgtairqti
      361 dtlvadgvsa eelerakksl lssalyaqds qstlarmfga amttgssiqd vrdwpakvsa
      421 itaeevqaaa akylvrppvt aylrpqvvae gpaptadaaa pseagattaq p
//
LOCUS       WP_181760120             268 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Stappia taiwanensis].
ACCESSION   WP_181760120
VERSION     WP_181760120.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..268
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..268
                     /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=27743
     Region          1..268
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mngfayltpg dlaealallr qgdeasplag gqtlvptmkq glaapetlid lgglaelagl
       61 rvtpthvevg amcphavvaa dpevraacpa ladlagmigd aqvrnrgtig gsianndpaa
      121 dypaaclgln avirtdrrdi daddfflsmf dtalepgeli vsvafprcre aaylkfrnpa
      181 srfalagvfl arhedgvria vtgagtdgvf rwseaeaalg reftatalag lavpvedmlg
      241 dlhaaadyra hlvkvltara laaisqra
//
LOCUS       WP_181760377             184 aa            linear   BCT 28-DEC-2024
DEFINITION  IMPACT family protein [Stappia taiwanensis].
ACCESSION   WP_181760377
VERSION     WP_181760377.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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..184
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..184
                     /product="IMPACT family protein"
                     /calculated_mol_wt=19946
     Region          1..182
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mplmtitrey egyledrksr flahlvpval feqrleelhk qhrkanhivt ahrrlldddr
       61 ieesgkddge pagtsgmpvl rvlqgaelin cavlivryfg gvklggggla raysgaaqda
      121 ianaepipfq rvavkqvsad fassselerq veqlgltvaa rdftqagvtl tlegpeenla
      181 rlga
//
LOCUS       WP_181760410             287 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Stappia taiwanensis].
ACCESSION   WP_181760410
VERSION     WP_181760410.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 287)
  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 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   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 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 10793067
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..287
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30566
     Region          1..272
                     /region_name="PRK08278"
                     /note="SDR family oxidoreductase"
                     /db_xref="CDD:181349"
     Site            order(12,14..15,17,36..38,96..98,146..148,163,167,
                     193..196)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187663"
     Site            order(120,148,163,167)
                     /site_type="active"
                     /db_xref="CDD:187663"
ORIGIN      
        1 mslkgktlfi tgasrgigka ialraardga niaiaaktae phpklegtiy taaeeieaag
       61 gkalplivdv reetqvkeai dkaaatfggl dilvnnasai qltplaatdm krfdlmhqin
      121 trgtlvcckh aldhlaradn philmlsppl dmqekwfapf tpyaiakygm slavlglage
      181 lrpkgigvna lwprttiata avrnliggdd mvsksrtpei ladaayeift spaksfsgnf
      241 liddtfltar gvtdfdryrv dpaqplmpdf fvpddseppv glgpake
//
LOCUS       WP_181760429             137 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Stappia taiwanensis].
ACCESSION   WP_181760429
VERSION     WP_181760429.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=14752
     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 mltigelara tgvkvptiry yeklgliaep trsegnqrry agparerlsf irhardlgls
       61 ldairellhl senpdmpcae ahviagahla atrariaqlq rleaelarit sgcdtstigd
      121 chvihaladh glcggdh
//
LOCUS       WP_181760445             321 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Stappia taiwanensis].
ACCESSION   WP_181760445
VERSION     WP_181760445.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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 321)
  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..321
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..321
                     /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=36291
     Region          33..306
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mieiglnavi vavddpqplv ltvatpiaqq apslpfgpfd perhrtfeig lrewveeqta
       61 ltlgyveqly tfgdrgrhhi hsdegphvvs vgylalarqt seseealare natwrswydf
      121 fpwedwrsgc pgivtehilp alerwvaapv pagsppraqs redrmhqafd iqdgiwdeek
      181 vldrfellfe agllaearrd grpaalerac lpplgqamly dhrrilatai srlraklkyr
      241 pvvfelmprt ftltdlqrcv eaisgrhvhk qnfrrlvdka elveptgets tqtggrpaal
      301 frfrrevlke rpalglrvgg r
//
LOCUS       WP_181760846             378 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Stappia taiwanensis].
ACCESSION   WP_181760846
VERSION     WP_181760846.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 378)
  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..378
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..378
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40751
     Region          7..376
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 msiaddflpv agpsitdrev ayaadaarna wyqnhnafna rfealfaetv gakhavslph
       61 ctaaihlala argigpgdev ivpdvtwias vapvsyvgat pvfvdslket wcidpdavva
      121 aitdktraii avdlygsmad wqrlraiada hdlflledsa ealgstyagq qagslgdigv
      181 fsfhgsktva tgeggmlvts ddalharvmt lrdhgrppgd rfflntevaf kykmsavqaa
      241 lglgqmerfd eliaqkrqif awyrdrlanl qgvalntepa gtsnsywmvt ivpdadygld
      301 kfaimeglka rgidsrpfft plstlpayae rpesarflps dpvgheiarv gvnlpsgyhm
      361 deakvnrvaa aleeilrr
//
LOCUS       WP_181761002             266 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Stappia taiwanensis].
ACCESSION   WP_181761002
VERSION     WP_181761002.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=27231
     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 myettyhrae svadaatrla gaedgkllag gqtllptmkq rlaapsdvid lthiadlkgi
       61 aetgggvrig aatthaevas seivkrllpg laslaghigd phvrhrgtig gslanndpaa
      121 dypsavlalg avvhtntrql paeeffagmf etalddgeii tavefpaata sayakypnpa
      181 sryamagvfv akradggvrv avtgagqdgv frhegmeqal agnfsaaald gisvdademl
      241 sdihgsaeyr ahlvtvmakr avaacg
//
LOCUS       WP_181761168             359 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Stappia taiwanensis].
ACCESSION   WP_181761168
VERSION     WP_181761168.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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..359
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..359
                     /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=41561
     Region          72..344
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mptkrlknhr hvyerissdg rltgyqvkir qkgfpvytkt fdrladadaa vvqvlndrnh
       61 gsrrdhrape ritlgevlen airevqqsek kgkdgeaarl stfikrhpaf chmsmanitr
      121 hdwedwkslr leevksstvr remnllmpvm rqaaidlemv gspldqvsrp qvrderiirl
      181 epdeedrlfh efacarnkll lpaarfalet gcrrsellrl rwsdyshngg tiylhdakng
      241 rgrdilltya aqviieelpg rekreghifp isaealknaf erarlragva hwrwhdfrhe
      301 aisrcfdhgw taeqvmdfsg hvdiksllry rhprvsdava rlrkmeserq aagslriav
//
LOCUS       WP_181759306             233 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: J domain-containing protein [Stappia].
ACCESSION   WP_181759306
VERSION     WP_181759306.1
KEYWORDS    RefSeq.
SOURCE      Stappia
  ORGANISM  Stappia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae.
REFERENCE   1  (residues 1 to 233)
  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   2  (residues 1 to 233)
  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   3  (residues 1 to 233)
  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   4  (residues 1 to 233)
  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   5  (residues 1 to 233)
  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 11437593
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Stappia"
                     /db_xref="taxon:152161"
     Protein         1..233
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=25472
     Region          47..149
                     /region_name="terB_like_DjlA"
                     /note="N-terminal tellurium resistance protein terB-like
                     domain of heat shock DnaJ-like proteins; cd07316"
                     /db_xref="CDD:143585"
     Site            order(59,66,130,137)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:143585"
     Region          168..233
                     /region_name="DjlA"
                     /note="DnaJ domain-containing protein [Posttranslational
                     modification, protein turnover, chaperones]; COG1076"
                     /db_xref="CDD:440694"
ORIGIN      
        1 mtiwdrisav vsaigaggvq vvdrlvqfiv nagdgrtgdr svaftvamia lsakmakadg
       61 vvtgdeeiaf ldvfdipage ernvarlfnl akqdvagfet yaqrlaalfp ddpetrvdil
      121 dvlfhiakad gvvhehelay lrrvgeifgl darafnqlla rhtrgggdpy rvlgldetvp
      181 teelrrhyrr lvgethpdrl iargvpeefv kiandrlaal naayaqiaae rrl
//
LOCUS       WP_181761269             642 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Stappia
            taiwanensis].
ACCESSION   WP_181761269
VERSION     WP_181761269.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=70758
     Region          21..610
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtvaacrigm fglglfcavp alaqdlelee vvvsagrtpl gaekvgrayt vitgedlers
       61 qtryladalr kvpgvsvsrt gsvggltqvr lrgseanhvl vlidgvevsa sssgefdfgg
      121 lqvadverie vlrgpqsaly gsnaasgvih iitkggvrdg yevsgrtevg tdrtwlgave
      181 lrgggenfdl alagafrrtd gfnlsdygse kdgdrnltly gkgawdlset vrldanlryv
      241 drksdtddqd ysfpptpteg qvidtpgyna trefsggvga swslfedrfv qktrfeltdv
      301 errgygsgse ngnhdrryha syqgtfafet peflsaahsl tgaveweqet frnthpgtps
      361 qvptrsrdlf gyvaeyrgef ydnlfisgal rfdqnddfkn altysasaay lvpetgtrfh
      421 asigtgvtnp tffeqfgfip ssfignpnlr peqnfgwdig ieqtfwedrv vadvtyfner
      481 ledeiqtryl pgwvstpvnl dgtsrrqgve valgvdvten lhakvsytyl datepsglqe
      541 vrrprhsgsl glvygfdegr gnlfldavyn gqmqdlefis stpwtrvtld qywlvnvgad
      601 yqlndhvqlf grvenlfdqd yqevygyntq gltafvglkg tf
//
LOCUS       WP_181761120             218 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Stappia
            taiwanensis].
ACCESSION   WP_181761120
VERSION     WP_181761120.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=23323
     Region          9..200
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mqviatqadl veglerllal dprlrpvara agplplrrqp adlaglvqiv taqqvsvasa
       61 aaifqrlrll idpferdtla rledaeltaa glsrpkirtl ravvaamgeg ldlaalaecp
      121 aqdahrrlce irgigpwtad ifllfcaghp difpsgdlal reavrqafdm perpgpkavd
      181 glaqrwaplr giaarlfwsy yravsgrsgl pvaaagae
//
LOCUS       WP_181761343             325 aa            linear   BCT 28-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Stappia taiwanensis].
ACCESSION   WP_181761343
VERSION     WP_181761343.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=34367
     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 mvhaitvhet ggpdvlrwee vsvgapgpge vrlrhtavgl nyidtyfrsg lypapaglpf
       61 ipgnegagvv eavgegvthl sagdrvayag plgayseerl iaadrlvrip egiddrtaaa
      121 mmlkgmtary llrqtykvts etvllfhaaa ggvgliagqw aatlgataig tvgsdekael
      181 arangyahvi nyrtenfver vkeitggklc dvvydsvgkd typgsldclk prglwvsfgq
      241 ssgpiedfnl amlsakgslf atrptlfsyi aeradleeta ndlfdvvgsg avtiavnqdy
      301 plkdakrahe dlqgrkttga svllp
//
LOCUS       WP_181760863             358 aa            linear   BCT 28-DEC-2024
DEFINITION  C45 family autoproteolytic acyltransferase/hydolase [Stappia
            taiwanensis].
ACCESSION   WP_181760863
VERSION     WP_181760863.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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..358
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..358
                     /product="C45 family autoproteolytic
                     acyltransferase/hydolase"
                     /calculated_mol_wt=38292
     Region          17..328
                     /region_name="C45_proenzyme"
                     /note="C45 family autoproteolytic
                     acyltransferase/hydolase; NF040521"
                     /db_xref="CDD:468523"
ORIGIN      
        1 msslpdvial dgcpltrgqq hgrqaagria aflddglarl dtflgpdirl sdlgqdiaay
       61 gaaieretpe lyreiaglse gagismdeav llqvrrelag fsrfntsgdc ttfartgega
      121 vigqtvdlag dlddqvtllk vrdaasghra lvmsftgllg ylgvndrgla vglnlvlagd
      181 wrpglppyla irhlldtcgs veeaiaclqe ldlassrcfm lcdgkaaafv eamegklavh
      241 rgaelthtnh fldpafaphd elnifaqngs rkrfeacrdw lashdanrep gsyfdlfste
      301 pvrvkdsgnr avektvasvv ldpvnrslhv ragdpfgapt asfdmvgwge nrhecana
//
LOCUS       WP_181761419             369 aa            linear   BCT 28-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Stappia
            taiwanensis].
ACCESSION   WP_181761419
VERSION     WP_181761419.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 369)
  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 369)
  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 369)
  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 369)
  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 369)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 369)
  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..369
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..369
                     /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=39981
     Region          15..368
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mtsgalmpgg gsqvqildal phplvlvgpq geieeantaa enffrasaqv lrrhpiahfv
       61 pfgsplllll tqvrergtpv neykvdigsp rigaekvvdi maapvadrpg fvvlmlqerg
      121 maekidrqlt srgaartvsg latmlaheik nplsgirgaa qlleasaded drpltrlimd
      181 etdrivklvd rmevfsderp iereplnihv vldrvqrlat sgfarnqtin vdydpslpqv
      241 lanrdqlvqv flnlvknase alsgqehgei tlttayrpgi rlavpgsrek vslplefcvr
      301 dngidgvpee llphlfdpfv ttkangsglg lalvakiigd hggviecdsq pgrtvfrilm
      361 pahvpgder
//
LOCUS       WP_181761373             753 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase NtrY-like [Stappia taiwanensis].
ACCESSION   WP_181761373
VERSION     WP_181761373.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 753)
  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 753)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 753)
  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 753)
  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..753
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..753
                     /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=81965
     Region          21..284
                     /region_name="NtrY_N"
                     /note="NtrY N-terminal region; pfam19312"
                     /db_xref="CDD:437144"
     Region          285..726
                     /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 msddlqmerg grnrrirklg lvfviaalis itatffvlmg vtpiapdgma ttvamiingi
       61 lvagllvlia lefisllqar rrgraaarlh grivtlfsvv aavpavlvai latitldrgl
      121 drwfedrtrl iidnaltvaq aylqeharvl rgeliamand vdraktvydf eptrfdsffq
      181 tqtslrsllg aflmrsdgtv itrvivnpdv evlppppeaf gqadggepvl iapgisnlvg
      241 gvmklsaydd mylyvaramd krvvdymrla qegasqytvm eqsrfgvqva falvytgvtl
      301 vlllssvwig fgfanmlvsp irrligaadq vskgnlyvqv etdksagdla nlgatfnnmt
      361 aqlrgqreal laandqidrr rrfteavlsg vtagvigvdd ggritlvnrs alalldveed
      421 dlldqpvgta vpelaemlge vlareddrmr eeqislhrqg rertinvrvt seqstrsehg
      481 fvvtldditd lvsaqrtsaw advarriahe iknpltpiql saerirrryg kkitddrtvf
      541 dqcvdtiirq vgdigrmvde fssfarmpkp tkssadlrnt vreaaflqtv anpdisistq
      601 lpeeparacf darlvgqalt nviknaaesv salppeqleh gritvtlrnq gdllaievvd
      661 ngiglpvenr qrllepymtt rekgtglgla ivkkimeehg ggielldapa nadgsgggrg
      721 amvrltmate rqdtatdatd ehltsgtvat dgl
//
LOCUS       WP_181761423             110 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Stappia taiwanensis].
ACCESSION   WP_181761423
VERSION     WP_181761423.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=12492
     Region          16..110
                     /region_name="sulf_sens_BigR"
                     /note="sulfite-sensing transcriptional repressor BigR;
                     NF040642"
                     /db_xref="CDD:468610"
ORIGIN      
        1 mslprvedle cssdlekiid rakiasdflk alahesrlli lcilaegeks vteleallsl
       61 rqptvsqqla rlrmdklvit rregktvyyr landdarrii eavydvfcrd
//
LOCUS       WP_181761457             192 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NuoB/complex I 20 kDa subunit family protein
            [Stappia].
ACCESSION   WP_181761457
VERSION     WP_181761457.1
KEYWORDS    RefSeq.
SOURCE      Stappia
  ORGANISM  Stappia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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 192)
  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 192)
  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 192)
  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..192
                     /organism="Stappia"
                     /db_xref="taxon:152161"
     Protein         1..192
                     /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=20892
     Region          27..186
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 mgltsgeplv aqapkgiidp ntgkpvgand pffleindel adkgfvvtat dnliqwartg
       61 slmwmtfgla ccavemmqms mprydaerfg faprasprqs dvmivagtlt nkmapalrkv
      121 ydqmpepryv ismgscangg gyyhysysvv rgcdrvvpvd iyvpgcppta eallygvlll
      181 qkkirrtgti er
//
LOCUS       WP_181761582             321 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Stappia taiwanensis].
ACCESSION   WP_181761582
VERSION     WP_181761582.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..321
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34026
     Region          28..319
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkiaalkycv aglllassaa ladvtapeci apakpgggfd ltcrvaqtgl aaqfdkpiqv
       61 tfmpggigav afsqfnttrt ddpnaivafs sgsllniatg kfgeftendv rflatvgadf
      121 gavvvradsn fetlddlmav fkenpaevvv gaggsvgsqd wmkgalllks vessprdmry
      181 vsfegggeal aallggsidm vtadvgevit hleagnirvl avlsperlda pfdqiptaie
      241 qgydvewtim rgfymgnnvp dadyqtwada fakayeteef rkireekgll plnlsgaeld
      301 tkvkqrigel rqiardagli k
//
LOCUS       WP_181761734             317 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Stappia taiwanensis].
ACCESSION   WP_181761734
VERSION     WP_181761734.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=34773
     Region          99..313
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          230..302
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdqgvdapew rmvggnaiai pgaqgrverl vfdkgvavyr seieavadcr ftvpnqlpqp
       61 wigfsvqlag saalstlggk tcamaedtla lmrvgpsgfv ldlpagmlir htgvavslri
      121 lkqqlngtmp lrlapfmerg ktlerfetlp lpasvktlat dlfgpsldgp lramtieglg
      181 kqlfsqalra fcehnpvgqp ftawelmrfd emlahirdhl ddtlagrtfa aqaglklarv
      241 eqmfkalrgv slaafvrser lraarrllhe eklpvsevai rlgyrhvanf srayraqfge
      301 apattlhrpr nrapqrr
//
LOCUS       WP_181761789             131 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Stappia taiwanensis].
ACCESSION   WP_181761789
VERSION     WP_181761789.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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..131
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..131
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13102
     Region          7..130
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mqqniirtvi dtararaaka gfavniavvd asaqlagfer megavlgaid vsqkkartaa
       61 lfqtdsialg aearpsgaiy tiensnggli sfgggvvlrd aegaflgavg vagatvedde
      121 diaqaaaavl r
//
LOCUS       WP_181761796             446 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Stappia taiwanensis].
ACCESSION   WP_181761796
VERSION     WP_181761796.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..446
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..446
                     /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=47867
     Region          31..>92
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          71..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(89,91,261,281,348)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mtmrknflat ilalavsapv caqeatdpgt litgarifdg igpdliegqd vlvqdgliae
       61 igagldapeg atiidaegrv mspgfidmhy hlslcsvpis dqqgayapdl dyigilasqe
      121 aervlmrgft svrdvggasw gaklaadrgq iagprvwpsl rtlsqfgghg danprymnpr
      181 efggpqnnle rlgysriang vddvltatre nlkrgasqik mhlaggvgte fdpidgrqfv
      241 rdeieaavev aegfgtyvta hvyttdgirq aieagvkcie hgnlideeia qmmaendvwl
      301 spqvlvyrtf spdlgpvrla kgqmveagld smfrlakeyg iktvfgtdvv vnpeacaeqn
      361 kefaarldwf tpaeiltqat ansgellqls gdrspypgiv griiegahad lllidgnple
      421 ditiledhet vidlimkggt iyksel
//
LOCUS       WP_181761799             444 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Stappia taiwanensis].
ACCESSION   WP_181761799
VERSION     WP_181761799.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..444
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..444
                     /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=47937
     Region          28..>88
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          68..421
                     /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(86,88,255,275,343)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mtlgknlfaa alifstttal aqevsqtlin nvqvfdgena dlienasvli egnliksvss
       61 dpisaegatv idgggrtiip glidvhwhts yccaaqstvv tgdilevair galgsestlm
      121 rgfttvrdvg gnpfatkkmi dkgeligpri lpsgppigqt gghfdyrpyq svptnpadsq
      181 wywyavglms madgvpevtk rarevmrmga sqikisgggg vssvydpldv rqftreevea
      241 fvevadtynt yvashiftdd aariaveagv ktiehgfllt eetlqlmkek gtwlsiqpll
      301 ddedgfsfdd pgsqqkwiev tngtdtiypl akkvgvkiaf gtdilfdpal aerqgaflak
      361 lkrwftpyev lkmatsenae llelagprhp yqdgalgvik pgayadlilv dgnpledidl
      421 vadphtnfdl imkdgviykn eigk
//
LOCUS       WP_181761599             518 aa            linear   BCT 28-DEC-2024
DEFINITION  formate dehydrogenase beta subunit [Stappia taiwanensis].
ACCESSION   WP_181761599
VERSION     WP_181761599.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=54429
     Region          3..93
                     /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..509
                     /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 mtptifvpcd aaalavgadk vaaaitaels arglnativr ngsrglhwle plievrtdhg
       61 riaygpvrpa dvpglfdagf lsggdhplrh grtkdmpflk gqtrltfarc gvtdplsled
      121 yrhyqglkgl ekavtmppad ivrevtdsgl rgrggagfpt gikwntvlga pgaqkyivcn
      181 adegdsgtfa drmimegdpf vliegmaiag iatgatkgyi ytrseyphav aimrraieia
      241 rragilgpsv lgsahafdme vrvgagayvc geetsllnsl egkrgvvrak pplpaleglf
      301 gcptvvnnvm slasvpvild rgaafyrdfg vgrshgtipi qlagnikhgg lyetafgltl
      361 gelihdiggg tasgrpvkav qvggplgayf ppalfdtvfd yeafaarggl ighagivvfd
      421 dtadmlkqar famefcaves cgkctpcrig avrgtevldk iakgespean ialledlcnt
      481 mklgslcalg gfapypvesa lthfpddfdk npflqaae
//
LOCUS       WP_181761838             105 aa            linear   BCT 28-DEC-2024
DEFINITION  Rieske (2Fe-2S) protein [Stappia taiwanensis].
ACCESSION   WP_181761838
VERSION     WP_181761838.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=11523
     Region          2..103
                     /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 mielcnstdv vegeilrrdv egfpavaltr hegqifvfpd tcphaeesls egwvedgrvv
       61 cgvhfaefel gsgevhnrpa gcpnltfftc edrdgkvfar lkeea
//
LOCUS       WP_181761958             160 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Stappia taiwanensis].
ACCESSION   WP_181761958
VERSION     WP_181761958.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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   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..160
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..160
                     /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=17726
     Region          2..141
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrltnrtdia irtlmylaid edriitidei vekslshrsq vvscvqtlrk ngyinstvgr
       61 sggislakkp dqivissivr liepdfflae cdekarrsrc aiyescrlkm vlhealscff
      121 khldtvtlad ivsnrdelrh aiaqsrlpaa hsslvgaagt
//
LOCUS       WP_181761947             243 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Stappia taiwanensis].
ACCESSION   WP_181761947
VERSION     WP_181761947.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 243)
  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 243)
  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..243
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..243
                     /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=27589
     Region          5..230
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msngktisda crawlkrcel delecatlrs yrnhvdhhie paigelclas lsrsdvrdfi
       61 ddmldknsra mtdkvlrslr salnealdre wvdnnvalsv klrrssrnap drviptkeei
      121 ktmlraaptk hrplivtaiy tgmrmselrg lrwvdvdftr siiqvrqrad rfneigkpkf
      181 sfhalrhaaa slfieqgwpa kkvqtilgha sitmtfdvyg hlfdnaeddv nlfakleadl
      241 eaa
//
LOCUS       WP_181761971             396 aa            linear   BCT 28-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Stappia
            taiwanensis].
ACCESSION   WP_181761971
VERSION     WP_181761971.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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   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 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   4  (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   5  (residues 1 to 396)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
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 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..396
                     /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=42156
     Region          16..382
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mdedqsgggp vtpsvsearl ssvlgtavdg ivvmdhqari llfntacekl fgytadevrg
       61 qnvkilmped falahdrfvs nylttgekri igigrevrgk hrdgrefpie lsvgeavtpe
      121 grqfigimrd isarkaveqr laqaqaqlvs mtrisaldem gaaiahelnq pltaimlylq
      181 aakrqassgs gadsklveiv dkgvneaera skiiqrmrrf vekreperra vavaplirec
      241 lelvtlgnac dgvafaidve ddlpqisadp vqvqqvlvnl irnaleavra vedkrvsvsa
      301 gvrerdmiir vsdsgggvpa elvpnlfkaf sgskkkglgl glaisrsiaq nhggdlaveq
      361 agsgggaafv lrlplsvgra saeaqdageg mkgsse
//
LOCUS       WP_181762097             446 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Stappia taiwanensis].
ACCESSION   WP_181762097
VERSION     WP_181762097.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
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="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     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=48677
     Region          3..436
                     /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 mdkatvllvd deadlreala eglelaghqv safagaagva ehlardlygv lvtdirmpkt
       61 dglalmrhal eidpalpvil itghgdvpla veamrsgayd fmekpfpvsr lanvierale
      121 krrlvlenri lreqlaqrtg legrlvgrsp vmerlrglva tladtdadil ivgetgagke
      181 vvaralheeg hrhggpfval ncgglpaevi eselfgheqg aftgasrqri gklehaqggt
      241 vfldeiesmp ldlqvkllrv ietrtierlg snktialdir flaatkddlv vagnegrfrk
      301 dlfyrlnvvs vevpplrark edipllfhhl areararyrr eipdaspafi tglmardwpg
      361 nvrelrnvad rfvlglesae gpsgfeagqs laervgayer aviqdelarn ggglkatyea
      421 lgvsrkalye kirkygldre aplaeg
//
LOCUS       WP_181762227             294 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Bacillus sp. B4EP4a].
ACCESSION   WP_181762227
VERSION     WP_181762227.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. B4EP4a
  ORGANISM  Bacillus sp. B4EP4a
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
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="Bacillus sp. B4EP4a"
                     /db_xref="taxon:2590665"
     Protein         1..294
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33860
     Region          <95..292
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mlenlkqkfp naltnkmdtg eisdyvwfed srsllgihrs eitaeeirll ellfapsinp
       61 ynlnahpdss wktflsepna plpltswenv rflhfkltha dfsnsdfeea flafvpsdat
      121 ivwenetagv lietdedepl stkeliaiss tlesdfyvkt rmftgrfhpi nqdlhqhwtq
      181 ekkcfdlaqv hlpdlkvadl adiiphslin dpsvkdakwy ineilgktkq dteliktikt
      241 yiecnsnaty aakqlyihrn slqyridkfs ertgldirnf rhaltaylil llnd
//
LOCUS       WP_181762418             424 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pandoraea pnomenusa].
ACCESSION   WP_181762418
VERSION     WP_181762418.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea pnomenusa
  ORGANISM  Pandoraea pnomenusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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..424
                     /organism="Pandoraea pnomenusa"
                     /db_xref="taxon:93220"
     Protein         1..424
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45727
     Region          127..419
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 myverhsrpa garlttwrtw renthaalca tglsaasvrr gvlrvllsav flssatpals
       61 qgassapaas qnsvvvalpa sgpakpirpa vpigqstlaq gvaqlkerfn lshvwlrtes
      121 dtgvaleaat adddvgallp vaslsksvta igiallvqeg klsldaklgd lldayskqhg
      181 kpldpslrel tvrrllahra glptngfndp vnglfsglai rrvggsadff kyldageagh
      241 stgksdfvys nvsylllgmv ieavsgqayk dfcetrifgp lgitdaqlpd nwrllapfag
      301 wqmstgallk vwrvfdirrp sllteqtlrt llldrqsgpv nadrdvyytl gvfllprage
      361 rsyrishdgi adffrtqaty ytvveknvpg dswalvvspi psrgqfgalq revrriirqa
      421 rlvp
//
LOCUS       WP_181762397             339 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family NADPH-dependent oxidoreductase [Pandoraea pnomenusa].
ACCESSION   WP_181762397
VERSION     WP_181762397.1
KEYWORDS    RefSeq.
SOURCE      Pandoraea pnomenusa
  ORGANISM  Pandoraea pnomenusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
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   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 339)
  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 10169684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pandoraea pnomenusa"
                     /db_xref="taxon:93220"
     Protein         1..339
                     /product="MDR family NADPH-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /calculated_mol_wt=36604
     Region          1..322
                     /region_name="ETR"
                     /note="2-enoyl thioester reductase (ETR); cd08290"
                     /db_xref="CDD:176250"
     Site            order(43,123..124,127,148,150..153,173,215..216,237..240,
                     262..264,319)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:176250"
     Site            order(53..54,236..239,245..247,249,252..254,257..261,263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176250"
ORIGIN      
        1 mkkvvvaqyg dpqryvrcie apdiahpged evlfdvlafp inpadisfcw gryrlkpelp
       61 avpgaecigq vvavgtsvrh isigdlvinl drenwtqrrl vkasrvivvp keidvaqaam
      121 mrinpptahl llsdvvklgr gdwiiqnaan savgrmiiaf akergintvn vvrrdeareq
      181 llglgvdvcl tdsedlassv kvltnnasiv lgidavagsa tnriascvad ggvvctygsv
      241 sresivlsps hvvyrgltft gfllgrfldk kredevaaiy qeifqrvtqg lrvdiervyp
      301 ienivealah adrardggki lvaphgpdrl nlagatsaa
//
LOCUS       WP_181762651             175 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Pseudarthrobacter sp.
            B4EP4b].
ACCESSION   WP_181762651
VERSION     WP_181762651.1
KEYWORDS    RefSeq.
SOURCE      Pseudarthrobacter sp. B4EP4b
  ORGANISM  Pseudarthrobacter sp. B4EP4b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Pseudarthrobacter.
REFERENCE   1  (residues 1 to 175)
  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 175)
  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 175)
  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..175
                     /organism="Pseudarthrobacter sp. B4EP4b"
                     /db_xref="taxon:2590664"
     Protein         1..175
                     /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=18057
     Region          <5..168
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 maeqfdgagf vrgalrkgfd phgkralvvg ngsvgspiaa slaglglagi glfdpdtgas
       61 etlaqrisah ypdvqiamgs kdpegydliv natplgmkdg dpvpvdidri tpgsyvgdvv
      121 lkagmtpflq aakqkgctvq vgsdmlfemi payleffgfg tataeelrtt aqlpl
//
LOCUS       WP_181762086              72 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Stappia taiwanensis].
ACCESSION   WP_181762086
VERSION     WP_181762086.1
KEYWORDS    RefSeq.
SOURCE      Stappia taiwanensis
  ORGANISM  Stappia taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 72)
  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..72
                     /organism="Stappia taiwanensis"
                     /db_xref="taxon:992267"
     Protein         1..72
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8152
     Region          3..>53
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 marqrgltqk elskllelec ytmisgveng nnrvppealv swakalrvnp sefakrllsh
       61 yepryfeaif gk
//
LOCUS       WP_181762778             570 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Rhodococcus spelaei].
ACCESSION   WP_181762778
VERSION     WP_181762778.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus spelaei
  ORGANISM  Rhodococcus spelaei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 570)
  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 570)
  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 570)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..570
                     /organism="Rhodococcus spelaei"
                     /db_xref="taxon:2546320"
     Protein         1..570
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=60748
     Region          23..569
                     /region_name="COG4425"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443540"
ORIGIN      
        1 mtttvsaaes lpgspapvsd rttgrldgvr rygrslhpvg lavallffvw smtpsllpra
       61 wylqavatgi svaigygigc laawlvrkcg iapdyaartr rigwwslaiv aavavptfli
      121 lgswwqqivr dlvgverinr anyllillia laiaalilai argiragtng ltrfglryvp
      181 apaarlaslv vvvilgalvv ngvvyqglig manrsaqasd hstapnveqp qipersgspa
      241 saeawdslgr egrtfvaggp taeqitavtg rpartpirvy agresadsva atadlvvael
      301 ertgafdrkv lavatttgrg wvnsrvassl eytaegdsai aamqysflps alsfiadrdt
      361 pqqagralfe avhtawearp egsrpklvtf geslgsfggq gafsgaqdml artdgalwvg
      421 tpnfapqwaq itadrdagsp erlpvvdggt nvrfaasasd ldldgapwgt privywqhas
      481 dpitwwsfdl llhqpdwlre plgadvdpgm rwipfvtfwq vtmdmvfsad vpaghghtfg
      541 pdaanmwaai lhpegwtdad tehvravlae
//
LOCUS       WP_181762918             333 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Rhodococcus spelaei].
ACCESSION   WP_181762918
VERSION     WP_181762918.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus spelaei
  ORGANISM  Rhodococcus spelaei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 333)
  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 333)
  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 333)
  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 333)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..333
                     /organism="Rhodococcus spelaei"
                     /db_xref="taxon:2546320"
     Protein         1..333
                     /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=34930
     Region          75..201
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 miarlravsa rlatvalfav aaasfpsaaa faesvatgsa gapddvpaaf aplagamrnw
       61 gkspagvndw ecrpadaqhr pvvlvhgtgr gmqeswgnla dpnikgplve dlandgrcvy
      121 alnygsafdf ptlsmkwgfa aiensaadlg afvdavlaht gatqvdvvgh sqggtvtrey
      181 lrtspdrtki hslvmlapps hgstlggeft seadarnkla piavqqqaid saflkrlneg
      241 qetfpgidyt viatksdqti tpsdssflvp apatsvhnmy vqdvcgnqdl vvwhsrpfpn
      301 sseskgpgll dhdvprflvr qaldptlsgt ppc
//
LOCUS       WP_181762941             162 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein [Rhodococcus spelaei].
ACCESSION   WP_181762941
VERSION     WP_181762941.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus spelaei
  ORGANISM  Rhodococcus spelaei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 162)
  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..162
                     /organism="Rhodococcus spelaei"
                     /db_xref="taxon:2546320"
     Protein         1..162
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17144
     Region          6..161
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 maprililmr hgksayppgi adhdrplapr gereaglagd wirrtqppvd avlcstatrt
       61 rltldatgie aparyeesly gtnaagvlhe iartddgvht llvighepgi pdaavaldps
      121 gatadriakr fptsaiatls vtgswsrils traaltnfhv pr
//
LOCUS       WP_181763109             404 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Mesorhizobium sp. B2-4-13].
ACCESSION   WP_181763109
VERSION     WP_181763109.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. B2-4-13
  ORGANISM  Mesorhizobium sp. B2-4-13
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
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="Mesorhizobium sp. B2-4-13"
                     /db_xref="taxon:2589936"
     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=44054
     Region          6..380
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mkirvtkrsv dalvgaekds fwwddtlkgf gvkvtpigkk vfvlqyrvgk spaprritig
       61 eygqpwtpdl ardeamrlrg lvatgidpad kpveklqltv sqlweryadq asahkkpsti
      121 ardrssatrh iiplmgdldv gslskpeiqt ffsgvrsgkt aadektgfrg raivtggpgt
      181 anrtldllss mmtfaidlgl rqdnptkgik kfalrtrdry lngeelkrlg kaldaeqsag
      241 anplalaair flllsgcrks ealglqwkwv dlenalvslp dsktgarqlh igsaardllk
      301 niprfanspw vfpssrgsgh vigirkiwda vrqraqlgdf rlhdlrhsfa ssavssgqsl
      361 yvvgkllghs qarttqryah lakgpvqsaa davsdeiskr lags
//
LOCUS       WP_181763118             602 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Mesorhizobium sp. B2-4-13].
ACCESSION   WP_181763118
VERSION     WP_181763118.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. B2-4-13
  ORGANISM  Mesorhizobium sp. B2-4-13
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 602)
  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 602)
  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 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   5  (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   6  (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   7  (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 11439550
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Mesorhizobium sp. B2-4-13"
                     /db_xref="taxon:2589936"
     Protein         1..602
                     /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=62954
     Region          16..575
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mvlnrnaagf tggvgsrrpp rlglavllrq ggpiavyavf alliglplsl vllqavmpgl
       61 fggeaasvfs leplkrvfss pyiagsvlhs lelgvlaaft ttvlggafav lvqrcdvplr
      121 gaisivpwlv fltpsylkal awvllmssgg ylaqlgllpp algadffgla glvfvhtlsl
      181 fplaafiigs alaglgsele daarlsgagp lrvwlrvngp llapaialsf iatfaevlsd
      241 fglastiarm ssfgvltygi yaaasdypvd fpaagaqalv llalvllvva vdrllrrrad
      301 phlisgrakp arlydlgrwr wlalaaalav vflalilplg aiaaraltst lghglvpenf
      361 tlanlaaalt lntaandglv rslfyaglta viastlalll saqlgrsspf mrtmvlglsl
      421 gavaipgivl gfgyilvwnr lpgfrdwpfp hygdgsllvm gyvaaalpyc lvvilsaigq
      481 lapsltdaar lhgvgalrrl lsvtlplivl svvtaflltf irtvfelpms qmlipqsgpp
      541 aptlilklfs hdrdglacai alvamtvagg taaliwypln rfvgpgrrra hgrrevalek
      601 lp
//
LOCUS       WP_181763461             210 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Mesorhizobium sp.
            B2-4-15].
ACCESSION   WP_181763461
VERSION     WP_181763461.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. B2-4-15
  ORGANISM  Mesorhizobium sp. B2-4-15
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
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="Mesorhizobium sp. B2-4-15"
                     /db_xref="taxon:2589934"
     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=22019
     Region          20..178
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 madskhqgal gavyaakrpe evaalydsws qtydadmsaa gyrhpticla llarhlprgs
       61 aplldagagt gligewldit gypevealdi sqgmldqaar kgvysalhcl algarlplad
      121 hayagvisag vftsghvgae gldeliricr pggvivltvk ntlwdqgfaa riaeleaqgl
      181 virveetrpy vsmpgeadtv psrglalrvs
//
LOCUS       WP_181763502             609 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Mesorhizobium sp. B2-4-15].
ACCESSION   WP_181763502
VERSION     WP_181763502.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. B2-4-15
  ORGANISM  Mesorhizobium sp. B2-4-15
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 609)
  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 609)
  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 609)
  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 609)
  AUTHORS   ter Beek,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 609)
  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 609)
  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..609
                     /organism="Mesorhizobium sp. B2-4-15"
                     /db_xref="taxon:2589934"
     Protein         1..609
                     /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=63250
     Region          25..561
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mtilqhsgaa afargagark pplgrlsalt ryggpfavya vfglliglpl alvlvqavmp
       61 glfaaqdasn glsfeplarv fnspyvagsv lhslelgmlv actttalgga failvqrcdi
      121 pgrtaisivp wlvfltpsyl kalawvllms sggylaqfgl lpawlgsaff glaglvfvht
      181 lslfplaafi igsalaglgs eledaarlsg atplriwlri ngpllapaia lsfiatfaev
      241 lsdfglasti armsnfgvlt ygiyaaasdy pvdfpaagaq alvllalvll vvvadrllrr
      301 radprlisgr arparlynlg awrwlamaaa laiaflalal plgaiaaral tqtlghglvw
      361 snftsanvva alslntaand gllrslfyag ltaliassla lllsaqldra gpvlrsavvg
      421 lslgsvaipg ivlgfgyilv wnrlpgfrdw pfphygdgsl lvmgyvaaal pyclvvilsa
      481 igqlapsltd aarlhgvgti rrllaitlpl vllsvvtafl ltfirtvfel pisqmlipqs
      541 gppaptlilk lfshdrdgla saialvamaa agigaalvwy plrrfvkprr saghagvgsg
      601 qtagtgtls
//
LOCUS       WP_181763530             106 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181763530
VERSION     WP_181763530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=10894
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mhwlylsvav ifeitvaiaa gkaagftnrp wtiatllsga iatwflsral ltfdvgvgya
       61 lwtsvagigi tvlgalligq rldwrkalgi avviagvvgl qlsgaa
//
LOCUS       WP_181763564             120 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181763564
VERSION     WP_181763564.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=13193
     Region          3..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maddrlslvf saladptrrd ivarlaagda tvnelaapyd vtvqavskhi kaleeaglvs
       61 rsrdaqrrpc hleaevfdlm tkwieryrre aedrfrrldv lleqmggqpa tgaptteaas
//
LOCUS       WP_181763524             191 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181763524
VERSION     WP_181763524.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 191)
  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..191
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..191
                     /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=20506
     Region          1..186
                     /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 mrvefpdfrl gnvlatsftg tlserhgdav eriptphrlv dwlavnglav dscstaqldl
       61 arelresiha aataaairea lpasavqvin drsaqgraaa vltpegerrw qlssascved
      121 alsviaadai siiagerdgs lalcasptcq aaffdtsrsr trkwcdmntc gnrqkkarfn
      181 anqrknprsa k
//
LOCUS       WP_181763811             348 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181763811
VERSION     WP_181763811.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=37225
     Region          78..346
                     /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(141,145,165..170,188..189,193,215,232..233,235,
                     255..256,282..284)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176217"
ORIGIN      
        1 meqvvqftgp rqvevaehgr eplppghlrv rtrysgisag teltayrgtn pyltrtwdae
       61 trlfregeag iaypvtgwgy sevgevtevs peltgspgip atgdlvwgiw ghrsegivpa
      121 ermaghtlpr gleplagafa rvgaiafnav lgadihlged vavfgqgvig llttrlaqln
      181 garvtavdal dvrlahareh gahftlnart devaervref tegrgadaai eisgaypalh
      241 ealrsvavgg rvvasgfyqg dgaglrlgde fhhnraqlic sqiggvpqql agrwsverlq
      301 qtflrlvaee avevqslvsh lvpvadaaqa yellderpsd alqivlef
//
LOCUS       WP_181763552             653 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Streptomyces albidus (ex Kaewkla
            and Franco 2022)].
ACCESSION   WP_181763552
VERSION     WP_181763552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=68592
     Region          9..479
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mkrltaedpr riggfrllnr lgeggmgrvy larsdrgrtv avkvvknela rqpdfrrrfa
       61 reitaarrvg gawtapvlda dpeaetpwva tgyiagpsla evvkvqygpl pegsvtglas
      121 glfhalrdih gaglvhrdlk psnilitidg prvidfgiar alhpmvetag gltrtgmlvg
      181 spafmspeqv rgrtvtaasd ifclgvvlay aatgrmpfgt adngvhglmf riaeeepdlt
      241 glsgklldiv ssclaknpeq rpeleelips tkdalsgtwl psallaqlgr havqlldsed
      301 pevtgeirig aaapstaqvs alpatrpsvt afggigapal asevaggdss tretatlpsl
      361 pgavphtvpg apaddlvsls pgtpeeppal prrskrrlav gavaavvvag aafaapgsgl
      421 lgsdggtqts sdvpeeyvgt wsgpvertge ggagqyrrfv iargdvgeiv trnvdlgady
      481 qctsngklas akgsltieak viksvpegkc sapgtnrlsl gpdstlqwea dgrrallhkv
      541 rtperlpkef lgtwqrqssg ggtqrvtvkq lsadrksidl vlqsadrkce aqasvfsvgg
      601 esepvligps vvdwrtsadd cptantsrlr vedgrliref ldadkkytyd rvs
//
LOCUS       WP_181763812             267 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181763812
VERSION     WP_181763812.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  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 267)
  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..267
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..267
                     /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=29125
     Region          2..257
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mftiacqeql lpgetlqqkw efaqaagyda velrgkgdfa frerlpelrg aladgvvmpt
       61 vcvdmlhffg afdeelrrda vaqmksqlsv iaelggtgaq tpasygmfsr rlppfepprs
      121 eqedrevllt glaemgehar regvtlylep lnryedhmvn rlgqavelir evgldsvrig
      181 idsyhmniee tgpaaailda apyighaqvs dsnrfqpgag hldwpawlaa ldsagytgpl
      241 alecrltgdd paealravpp fltrsaa
//
LOCUS       WP_181763515             222 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181763515
VERSION     WP_181763515.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=23602
     Region          9..205
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mqnellvved lmllmmddks gavagegtly ytlggavlve lglgghvtvd qndrgltglk
       61 vravpgsrlp dpilkdahdk varrvrgvqs llaeigptlr gtvldrlvkr gvlrrdtkkw
      121 lglfsstsit iadtrrkkal vekvravlvd haepdartaa lvgllsasgt lttlhrsipw
      181 sgkvykrake leleswgaea vnsavmrtma sisagsaaav ts
//
LOCUS       WP_181763732             214 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181763732
VERSION     WP_181763732.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 214)
  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..214
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..214
                     /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=23773
     Region          8..179
                     /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 melnyysdma vrlvnteepe rgedtltsve svrelcganq qmarratesd vprlrgvrtr
       61 lravfsaase geetravdll nsllmefpts pqisghgdld qdgrprwhmh laehpvttaa
      121 gytatacmgl afhltdlgve rlgicqatpc rmayldtstn rsrrycsdrc atranvaayr
      181 arkrreseee rsgrtatsgr taetaqrttg qker
//
LOCUS       WP_181763966             962 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181763966
VERSION     WP_181763966.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 962)
  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 962)
  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 962)
  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 962)
  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..962
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..962
                     /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=103998
     Region          3..246
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          116..962
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          673..701
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          712..740
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(713,716..717,720..721,723,753,756..757,760..761,
                     763..764,793,796..797,800..801,804)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          751..781
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          792..820
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          832..860
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(833,836..837,840..841,843,867,870..871,880..881,
                     883..884,913,916..917,920..921,924)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          865..901
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          912..940
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mgeptfgvlg plqvrvdgvp vriggpkpra vlatlllqps gfvsldllte vlwpggaprs
       61 avanvrtyvr alrqalatag vdtdglrtep sgyaldvasg dvdmllfeer leraraerdh
      121 gneaaalrsy esalglwrgg vlqdvpssvv wdpavtrieg lrsvavdecl eirlrlgdyt
      181 slvadlrsrl tenplredlw rmvvqalhns grttearaay aeaeriiaae lgiepseplr
      241 tmgeeingya grrrsatpap vcqlpmdvpd ftgraeeiav lerllaaagr qpvvatvsgp
      301 pgcgkstlav hvahrvsdaf pdgqlyvdlg gtsdqprepa dvlaemlrgl gvidstipge
      361 lseraalfrs rlaqrrfliv lddasgsaqv rpllpgtggs avlvssrrrm pglpayqspl
      421 gvmkredara lfgaivgpdr lrlveaevdr vvagcgslpl avriagarla nrpgwtvgal
      481 adflhdergr ldqlrtgeme vragaelsyr hlpesaksvf rafgqladva vagwtaavvi
      541 ghadeasgal etlldehlve vvgtdrvglq ryrmhdllrc yarelaeadg rtervrqqll
      601 vtdaliglar tansampnrf lgvlgdptpl tgpesalaet vrarpvewfe serrilvgav
      661 daavrlgqts raadlavela sffdmrgyyg dwlrthqlvl dampdasdar aaallrnlgq
      721 lhlyqdryad alasfersre ifadighlpg eavasagigs vyrvvedlds aldafvhalh
      781 afgkagdphg eavahnaias vwlerkdpqa asgwldgale lsravgdrhr eaqvrrriae
      841 lhelrgephv aqaeleralg ifddlsdthc aayvqqsige lclrqgnare asalltgala
      901 vqqqlgdrra earvacllge lhhatgreqt arryfhrsls twrrldapdq aelvdaklrs
      961 lr
//
LOCUS       WP_181763993             220 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Streptomyces albidus (ex Kaewkla
            and Franco 2022)].
ACCESSION   WP_181763993
VERSION     WP_181763993.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 220)
  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 220)
  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 220)
  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..220
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..220
                     /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=23381
     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 vgrsiagell enghevllid kaptaisver vpqaewllad aceitsldea
       61 alercnvvia atgddkvnlv vsllakteyg vprvvsrvnn pknewlfnes wgvdvavstp
      121 rlmsalveea vsvgdlvrll rfsqgdanlv eltlppeaal agtrvgdvsw pedtalvtii
      181 rgnrvlvpdk ddalevgdel lfvaaparee qledllsvrg
//
LOCUS       WP_181764057             152 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181764057
VERSION     WP_181764057.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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..152
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..152
                     /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=16118
     Region          2..132
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrisakadya vraalelaaa qddgpiktea iskaqgvphk flesilndmr rgglvisqrg
       61 gqggyrlaap aesitvadvi rvvdgplvsv rgerppelty tgpaesllpl wiavranvra
      121 ilsevtladv aaadlpehih rltelpeawt np
//
LOCUS       WP_181763848             422 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Streptomyces albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181763848
VERSION     WP_181763848.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  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 422)
  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..422
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..422
                     /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=44663
     Region          3..417
                     /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 mnrrvvitgm gvtapggvgt ddywklissg tsatrtislf nadgyrsria aevdfepefh
       61 gltplqirrl drggqfalvc lreaiadsgi eidealaart gvsigsaiga stsldqeysv
      121 vsdsgrdwlv ghtdvvpqlf eymvpvrfas diaweagaeg patvistgct sgldavgyaf
      181 eliregsadv mlagatdapi tpitvacfda iratsprndd pehasrpfdf drdgfvlgeg
      241 aavfvletle sarrrgahiy aevsgfagrs nayhmtglkp dgremaeaid aamrqarvna
      301 edidyinahg sstkqndrhe taafkrslgd vayhrpvssl ksmlghslga igsielagca
      361 laiehdavpp tanletrdpe cdldyvplta rdqpvntvls vgsgfggfqs avvlnsyrge
      421 aa
//
LOCUS       WP_181764220             222 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181764220
VERSION     WP_181764220.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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: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=24167
     Region          49..150
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mpltskslpe ywdtykphkg kgkpppppvd sfewtqhpah gpgerflgrp rtalelgcae
       61 gkeavylars gvevtaldls paqiararlw wegtpgvsfv naeacdflan tpstfdavfs
      121 rwgavwftdp adlvplvrqr lnpggvfavs qaepiegfyg pqamygngls grrltvlrws
      181 yspemwsdvl gsngfvdvda hilpapdpen vgtlmvrahv pk
//
LOCUS       WP_181764222             106 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181764222
VERSION     WP_181764222.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=10798
     Region          4..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mglawvvlvv sgvletvwag aleasgnfhk lwpsvlflgs lalsmtglsy avttiplgta
       61 ygvwvgigal gtavygmvvl gdpvtmarll clllivggvv glkflh
//
LOCUS       WP_181764260             125 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181764260
VERSION     WP_181764260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            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..125
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..125
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12826
     Region          47..112
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mklnrtagki attafavlal taagatgsaa aaeapsnpaa necnystarp tlqlgdtgpa
       61 vkqaqcyllh tliiddliev sgnfdaktql rvrqfqscag lasngvvgas twsvfeqyms
      121 tgrvc
//
LOCUS       WP_181764299             324 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181764299
VERSION     WP_181764299.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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 324)
  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 324)
  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 324)
  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 324)
  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 324)
  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 15747257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..324
                     /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=34698
     Region          40..195
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          252..324
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mkvdtgrlpv eqfefgtsdp alaesvtkem ygecrqnggs aeeftfgirr tsaggmsldh
       61 lvhtmdtsad cgvlddlmfv fltggslsvt srdlearltv gdtalypagv piriswdrlr
      121 aeilsvpvpa aeraaaeygd gdgpvrfvgt lpvspamdrf wrstvgfvth qletpdspls
      181 aplvqaqtln llgaaavrvf pnttmtadyl pgpgqvspaa vrraaefiea hadrpltsad
      241 iaaaasaspq alqaafvrhh dttpleylrr vrlerahrdl qitdpttgat vasiatrwgf
      301 skpatfaehy hdvygqppgh tlra
//
LOCUS       WP_181764308             339 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181764308
VERSION     WP_181764308.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            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 albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=37204
     Region          5..318
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 madvtermla llstlqtgrs fsgeeltrrl sisprtlrrd vdrlrgygyp vetrpgpggy
       61 yrlaagrtmp plvldddeav atllalasla atgpstgggi ddaatraygk ldqflparlr
      121 pralalrssl etspqrapsv taqqlglfad aiarqetmtf tyssargert errvepyrqv
      181 hhllrwyvlg wdlerqdwrv frldrvtepl rtgeryeprp lpagsaseyl rqglnrgkqt
      241 vrlqvdalaa dvadalkfqd aeirpvgdrr tdvtlaldsw qwlvlhlafl dadfriaegt
      301 qfteacgifg erlvaaasde pgaqkppgtg qgghasgsg
//
LOCUS       WP_181764420             246 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181764420
VERSION     WP_181764420.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 246)
  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..246
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..246
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=27368
     Region          6..129
                     /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..24,29,39,52,54..55,57,60,66,68,
                     80..81,83,85,96,98,100,102,110..118,120..122,125)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mderrlekei elaaspeqvw qaistpegms vwfvphehtd gelegdfggg ntqagqvlew
       61 epgrrvvyga pgpdgepsmt feflvegreg gttvlrlvqr gffgddweae ydgfgkgwgm
      121 ffhnlaeyfr yfpglpvanv vatgfttlpg etlwadliar lgaapalger vrltpeglep
      181 iegvvdqrdt mllgirtehg fyrfmaddlh hmvstvqyfy gvtvdresrt aawqswldsl
      241 tgdegr
//
LOCUS       WP_181764422             201 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181764422
VERSION     WP_181764422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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 201)
  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 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   5  (residues 1 to 201)
  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 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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..201
                     /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=21647
     Region          18..108
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mhdvaviddp gaaevsldpv rarllaelse pgsattlaqr vgltrqkvny hlralerhgl
       61 velveerrkg nctermlrat atsyvispsv laavepdpar srdqmsarwl lavaarlvrd
      121 vgelitgaar arkrlatfav dgevrfasaa draafaeela gavtslvsky hdesaaggra
      181 hrivvavhpt vqreekpeer g
//
LOCUS       WP_181764477             104 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181764477
VERSION     WP_181764477.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=11190
     Region          7..87
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mltsvdtdli rvladplrlq ivtllahetl ctthlveetg arqtnlsnhl rvlreagvvd
       61 tepcgrftyy klrpdvieav assfstlaaa arataaadkk racp
//
LOCUS       WP_181764481             112 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181764481
VERSION     WP_181764481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=11959
     Region          16..88
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(20..21,25..27,42..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 mkevepldra taqeyaswfk vladatrvqi vsllarrgrp msvgeivdav qvgqstvsah
       61 lkqlaevqfv laeyagtasy yrindecvtc fpsaadvvmg rpapggpppe ha
//
LOCUS       WP_181764566             720 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181764566
VERSION     WP_181764566.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 720)
  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 720)
  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 720)
  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 720)
  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 720)
  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..720
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..720
                     /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=77364
     Region          16..714
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mrslrrlsha allgqaprrd glpdamehva kvhrahhpqa dlaalrrayv laesshrgqm
       61 rksgdpyith plavtlllaq lgaetttlta sllhdtvedt dvtleqvrke fgeevsylvd
      121 gvtklekvdy gaaaepetfr kmlvatgndv rvmsikladr lhnmrtlgvm rpekqvriak
      181 vtrdvlipla erlgvqalks eledlvfail hpeehalare liaehveqpd pltgvatsvr
      241 hvlreagiva qvlirprhtv svhrlrlkrg elgpcdfgrl limveedadc yavlgelhtc
      301 ftpivaefkd fiaapkfnly qslhtafade egrvaevlvr trqmhriaea gvialgdphg
      361 aqaaenegaa epggpgwlsr llewqshatd tetfwaelrd elaqdreitv ycaspgvasa
      421 psggalplpa gatcvdaaya rygeaahrci garvngrlta lstvlrdgda lqlflepaas
      481 apsgpspewl qhartpaari airhwlaanp pvseaelttv gagtaligeg phrafapaas
      541 aaanvadgra easvstvpra aheasvphsa asvvaddpha vvrlarcctp vppdsvtgfa
      601 vrggtvtvhr dgcqsvtrmt stgrrpvpvr weqgaagcrv tlraealgrp hlladlteii
      661 aaqgaavvsa dveppreqrv lhtytlqlpd aaglpdlmra mrrvpgvydv tratrplpar
//
LOCUS       WP_181765180             303 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181765180
VERSION     WP_181765180.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            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..303
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=31238
     Region          1..283
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mdvgrallfv pgdrpdriak alatsadava vdfedavgda ekasaraata dafsglpdap
       61 rpavyvrind ldtseaeedl aavasmltat rlaglivpka esskeigllq gvlttaeraa
      121 riepgslali piietargvl eaaataaasp rvrtllfgtl dlagelgvep tvegrellha
      181 rsqvvlaara aglagpldgp ypalddeagl irsstaarel gytgrvvlhp aqvgpvqrlf
      241 aptdselvra revlaayeea qkqgvgalrl pdgtfvdrpv vnraaalvee aalhagdrae
      301 aar
//
LOCUS       WP_181765181             388 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181765181
VERSION     WP_181765181.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..388
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40841
     Region          3..381
                     /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 mtsgrrlple gitvvaleqa vaapystrql adlgarviki erpdggdfar gydhavrggs
       61 saflwlnrgk esvqldlkds adredldrll eradvmvanl apsalgrlrl dadtlrerhp
      121 dlivclisgy apggplaekk aydaliqaea gvmsltgtpg apakvgvsia diaagshals
      181 gvlaairhrd ltgealpvrv slfdaltewm ahplyytlhg gsapvpmgts hpaiapygaf
      241 taadeaalli avqnerewvr lcadvleapg laaderfrsn pdrvanraal daalgerfaa
      301 ypsstlterl dgagvawgrm tamtdlaahp elarddrwmd tptaqgsvrt lrppgipgdr
      361 aaeggavpal gqhtasvlae ihaaegdr
//
LOCUS       WP_181764562             405 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181764562
VERSION     WP_181764562.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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..405
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..405
                     /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=42895
     Region          167..>327
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 msanlrpprr rpalavaavv aalaltatac gpeddnaggd pgasdsaqpd kkekrdlglp
       61 eelpkdlpss ledldkwrng awknwdrdew lrrakefvnp iiddlwdpdr mkdadgndrk
      121 vdedeiddge sggdngtged egvtdptpsr vaakpvklpy tkatppvgkv fmdtpqgsmv
      181 csgtvvtdpa hpgksnlvat aghcvhagkt ggwfrnvvfv prynpkglsn aelgkaskkd
      241 vapdgvwwak yagttdhwik egsktggrga pqdfavlkvq pedkksgpsl qeivgkaakv
      301 nfntprvkai psltphgypa appydgskml tckdkpgrlt idpseptmyr vgcsmtggss
      361 gggwlspsgr qllsvtsigp vgggwlagar igkeskdvfd siakk
//
LOCUS       WP_181763590             124 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181763590
VERSION     WP_181763590.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 124)
  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 124)
  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 124)
  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 124)
  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 124)
  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 124)
  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 124)
  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..124
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..124
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13534
     Region          30..124
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mengtgnars spdqraater idearasgvr lieslrrlwd gvveaseqan iddehdpega
       61 tvaferaqlr dvlkqahadm ddldraaerl rtgdywvcdi cggpiaverl aarptattci
      121 rcar
//
LOCUS       WP_181765322             456 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181765322
VERSION     WP_181765322.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 456)
  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 456)
  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 456)
  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..456
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..456
                     /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=50970
     Region          8..453
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mtktqvvray rfaldatpsq veilrryana sraafnfalg mktasherwk rgrdplvaad
       61 mdmaeakkka pkvriprkpq vhrhfiatkg kgpigplrqg eerrtpypww egvnansfqe
      121 affdadaawk nwldsmtgkr agapvgyprf krkgsresfr ltntavrfag yrrlwigggg
      181 gqaaftvrlh eparrlvrll dagqarilra tiardghrwf aavvveeiav lpnrptrrqa
      241 nagrvgvdlg vksaaafsdp vvlahgapgv lelanprhvr ntekklaraq rvasrrfvkg
      301 aqkqskgyhe akarvaklha qlaarrastq hlltrrlveq yaevaleklm vknmtrsakg
      361 saenpgknvr qkaglnrail dvgfgeirrq ieykaawygs stryvgtyfp ssktcsnchw
      421 knkeltladr vfkctqcgmi mdrdanaaqm ikkhaq
//
LOCUS       WP_181765561             191 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-class carbonic anhydrase [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181765561
VERSION     WP_181765561.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            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: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..191
                     /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=21080
     Region          49..183
                     /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(49,51,58,60..62,74,77,96,101,111,114,173)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:239474"
     Site            order(58,60,111,114)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:239474"
     Site            order(59..62,68..69,74..76,78,80,91..92,95..96,173,
                     175..176,178,180)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239474"
ORIGIN      
        1 mstpqrrhqp lhqspaddlr gsgtvtdrli eanaryaaef ndpgmdarpv lkvavvacmd
       61 aridlhevlg lelgdchtir naggvvtddt irsltisqra lgtravvlih htgcgmlslt
      121 enfrhelele vgqrpswave afpdldqdvr qsmervrtsp fllhtedvrg fvfdvktgll
      181 reidpeiape p
//
LOCUS       WP_181765562             343 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181765562
VERSION     WP_181765562.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 343)
  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 343)
  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 343)
  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 343)
  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 343)
  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..343
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..343
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37267
     Region          16..307
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mttfderadl sdlsttadrv rrsmesvieg kpevvrlslt vliaeghlli edvpgvgktm
       61 lakalarsvd csvrriqftp dllpsditgv siydqqrqef efkpgaifaq ivigdeinra
      121 spktqsalle smeerhvtid getydlpspf mvvatqnpve megtyplpea qrdrfmarvs
      181 igypspaael emidvhggas pledlqpvah aheiskliea vrgvhvadqv rryavdlvaa
      241 trthqelrlg aspratlhll raaraaaals grdfvlpddv qslavpvlah rllptaqaql
      301 srrtaeqvvt eilqrvpvpt gapgvattpl htdgygqqsp rgy
//
LOCUS       WP_181765571             480 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181765571
VERSION     WP_181765571.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            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..480
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=50658
     Region          1..444
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mariavigag lgamaasarl avaghevtvh ertetfgggv rlherdgfrf dtgpgllhlp
       61 avyrdlfvkt greplekcve lvrldpavrh vfadgtavsl phasragvie aldgalgkga
      121 gerwtdllar artvwdatrr plleeplsaa dvpaaralsa rdpypalrrk gllrrrtptl
      181 aevaadelrd prlaamltgc ahaygldprr apagaavlay lehtfgswhv rggmrrlaea
      241 lyerclergv dfrfgtevlr vreengrasg leladgpdvd adavvagscr psadaatpda
      301 dvsgvpaasr ltvllalrga rptgtahrtv vhradapgtp ltvlrpddpt lrpdaehesa
      361 vlsvtvrade vpdreeasll adrlitaadt aglnlgerml wrvvhtpedi eretgvpggl
      421 vpapalageg ivrppnrtat kglyraggwg hpgggpahag msgalvagli vegddwrgsr
//
LOCUS       WP_181765355             295 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181765355
VERSION     WP_181765355.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 295)
  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..295
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..295
                     /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=32066
     Region          38..292
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 msmrravaaa tgvllgvsgl sfiatpaqaa sqqkkadsap itvahrgasg yapentlsav
       61 ekadklgmdw vendvqrtkd gelvvmhdtt larttnvekl yperspwnis dftakeikrl
      121 dagswfsddy agekvptleq ylkkitktgq rlllelkspe iypgielqtl relsshgwld
      181 skhtksklii qsfnadsvkt thflnsavkt gflgnpkvse ldsyakftdq inpthsaatk
      241 dyikavhark gplgkqmevf twtvndasta rtvdkagvdg iisnfpdvvr datgg
//
LOCUS       WP_181765805             160 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181765805
VERSION     WP_181765805.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=17208
     Region          4..146
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 matpefirai rataghqlly lpgvsavvfd degrvllgrr adngrwaiig gipepgeqpa
       61 taavrevqee tavhcvaerv vlvqaleqpv tfpngdvcqf mdicfrcrat ggeakvndde
      121 slevgwfsld alpameeftv trikhatgdg ptwfegagqv
//
LOCUS       WP_181765595             604 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181765595
VERSION     WP_181765595.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..604
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=65547
     Region          26..223
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          304..592
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mahmdsgtqr aadndelasy rlrrerelss lyatarsmaa lgevdevlps ivrhahelig
       61 sdfaylslld aegnltlras agtispefss armppgdglg grviesrapf wvsnygeara
      121 lshnptfdll vageglmall gvpllvgera vgvlfaadrt erpfendeva lfsafadhaa
      181 ialnnarlye esrisvqrlq eayrtiedqv ttveraaavh ealthvvltg ggpgdlaqvl
      241 vehlrgmvtv ldrddkvvas rsfggdaadt gwepapelle aarrtgrcat aegedgavhs
      301 vaviqaggsh lgslsltrha apeppdirml ersaqimgll ilmrdarvea eervcgellm
      361 ellsrppvhp aqrdraltrg vdvdhldvlv vadcpgkspg dvvrqlnavs pewsglagey
      421 lgqatmllra ddvqeaagal hhrlrrtlge pvlvvadrit gqersrsftl trrclevmrs
      481 lgetdrgstt qqyamyalvf dperahdldq fldevlgpll aydrrrstdl vtttaayfah
      541 agnlsqtars lhvhmntllk rldrigtllg ddwrspdsal rlhlavrlhe lrgalegrss
      601 gars
//
LOCUS       WP_181765722             233 aa            linear   BCT 28-DEC-2024
DEFINITION  bleomycin resistance protein [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181765722
VERSION     WP_181765722.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  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..233
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..233
                     /product="bleomycin resistance protein"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=25882
     Region          6..124
                     /region_name="BLMA_like"
                     /note="Bleomycin binding protein (BLMA) and similar
                     proteins; cd08349"
                     /db_xref="CDD:319937"
     Site            order(6..8,38,45..47,49,64..69,74..75,78,123)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319937"
     Site            order(29..30,38,49,51..52,66,105,112,114,118..120,122)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:319937"
ORIGIN      
        1 mservipilp crtlqpvldf ytalgfevtf qqkspnpfav vqrgaielqf fgmkkfepte
       61 sfstcyvltd dvdplyetfr aglksaygki ptrglprigp lrdmsygvrq flmsdpggnc
      121 irigmktsed qrhrpapket faralhnatl fadshedpeg aakiidrvlk ledeeptrvq
      181 llrllvlrsd vagrlgddgt aadllkkaaa vqlteeeaes arddlarlqe lrg
//
LOCUS       WP_181765829             450 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181765829
VERSION     WP_181765829.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=48586
     Region          8..448
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 msdraplkit vigtgylgat haaamaelgf evlgldiste kiallerget pmyepgleel
       61 lrkhvaghpg ssgrlrftts yeevgefgdv hficvntpqr hgeyacdmsy vdsavdslap
      121 hlkrpalvvg kstvpvgsaq rlalrlaela pagedaelaw npeflregfa vkdtlhpdrv
      181 vvgvrserae qqlrevyatp laegspfvvt dfptaelvkt sansflatki sfinamaevc
      241 eaadgdvakl aeaighddri gkkflrsgig fgggclpkdi rafmaragel gasealtflr
      301 evdsinmrrr vhmveltrea vggtllgtri gvlgatfkpd sddvrdspal nvagqlhlqg
      361 aqvtvydpkg menaralfpt lryapsavda vrgadvvlhl tewrefqeld paalgevvav
      421 rhvldgrntl dpalwrkenw kfralgrpta
//
LOCUS       WP_181765921             189 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181765921
VERSION     WP_181765921.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 189)
  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..189
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..189
                     /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=20477
     Region          1..183
                     /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 mptalkilva ggfgvgkttm igsvsevppl etdeymtqas lgvddlagtp dkstttvamd
       61 fgritldpdh vlymfgtpgq drfwfmwddl algslgavvl adprrltdsf asvdffeqrr
      121 ipfavgvncf ygrcdfsaee vqtamnlrtp apvvmcdvrh rnsskqvmla llesartqaa
      181 qrmmsshgg
//
LOCUS       WP_181765841             302 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181765841
VERSION     WP_181765841.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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..302
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..302
                     /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=33185
     Region          26..280
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mpatrtwtap psydlrsnlr vlrrgpydpc yrveggavwr atrtpdgpat lritaeaaga
       61 tvraeawgag aewalerlpa mlgadddpsa fiahhpltre ahrrhpglrl prtglvmeal
      121 ipsvleqkvt theayrawrl lvrrhgerap gpqdgmfvmp dhrgwcrips wewhragvdn
      181 krsatviraa qraprleeaa smelaaamar lqlipgigpw taaetlqrsn gdpdaltvgd
      241 lhlpsivgys ltgardvdda gmlellapye gqrhraarli liagraparr qprfpigdia
      301 rl
//
LOCUS       WP_181766048             304 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181766048
VERSION     WP_181766048.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 304)
  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..304
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..304
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34257
     Region          29..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          115..295
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msaqregdss vrrildhprg gptilrivlg tqlrrlreer gitreaagda irgshakisr
       61 lelgrvgcke rdiadllsly gitdeqdrde ylvlarhsst pgwwqkysdv mspwfdrlig
      121 leeaasvirm yevqfvpgll qtedyaravm rlghpraste eierrvelrs drqailtrph
      181 spklwavvde aalqrplggp svmreqikrl lwaaeqpnvt lqiapfaigg laaaggpvti
      241 lrfqepdlpd ivyleqltss lylekrdeve nymvvmdrlc ataeppsmtv eflerllsrh
      301 eaqg
//
LOCUS       WP_181766116             118 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181766116
VERSION     WP_181766116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=13782
     Region          5..81
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrapaaladp vrreilvllh arprnvseit ghfdvsrpav srhlrvlrea glvvaedrgr
       61 ervyrletap lvelrqwleq fsnrweqrfd aletevhrtr rerrrqaqst deakekpa
//
LOCUS       WP_181766126             185 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181766126
VERSION     WP_181766126.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  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..185
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..185
                     /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=19387
     Region          15..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maehrtmqra alldaarall seggtealtf palaqrtgla rssvyeyfrs raavveelca
       61 vdfpvwaaev etamaeaeta egkieayvrq qlalvgdrrh ravvaisage ldagarekir
      121 aahgglvamv vealgalghe qprlaamllq gvvdaavrri elgaaedpeq iteaavsmal
      181 sgvgn
//
LOCUS       WP_181766128             509 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181766128
VERSION     WP_181766128.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 509)
  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 509)
  AUTHORS   Rosinski,J.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..509
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..509
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=56011
     Region          3..>69
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          74..504
                     /region_name="MurA"
                     /note="UDP-N-acetylglucosamine enolpyruvyl transferase
                     [Cell wall/membrane/envelope biogenesis]; COG0766"
                     /db_xref="CDD:440529"
ORIGIN      
        1 mtddylarig qlirdarqhr gwtqvklaea lgtsqsavnr iergnqnisl emiariseal
       61 dseivslgys gpmhlrvvgg rrlsgsidvk tsknacvall casllnsgrt vlrrvariee
      121 vfrilevlss igvrarwind gadleivppa eldleaidad aarrtrsiim flgpllhrmd
      181 qfripyaggc dlgtrtvqph mialrrfgle itateglyha vversvtper pivltergdt
      241 vtenallaaa rhdgvtvirn assnymvqdl cffleelgvk vegigtttlt vhgvseidvd
      301 vdyspsedpv eamsllaaav vteseltvcr vpvefleiel avleemglea erspeytadn
      361 grtrlidltv rpskleapid kihpmpfpgi nidnvpffaa iaavaegktl ihdwvydnra
      421 iyltdlnrlg grlqlldphr vlvegptrwr aaemmcppal rpavvvllam laaegtsvlr
      481 nvyvinrgye dlaerlnevg aqietfrdi
//
LOCUS       WP_181766253             542 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181766253
VERSION     WP_181766253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 542)
  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 542)
  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..542
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..542
                     /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=60046
     Region          20..541
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mtqplsaese fraaarhlcr rrlltgtaat valalgtnlp qpahavqrld ptaihkdpft
       61 lgvasgdplp dsvvlwtrla pepfepdsgl tahavsvewe lasdelfkrt vksgkvtahp
      121 efhhavhvvp eglsprtryy yrfrvgawts pvgrtrtapa atddpeslrf vfvscqayhd
      181 gyftalrhla kekdvdavvh lgdylyeyav dsqggdradg slhlpdrfnk etvtledyrl
      241 ryalyhsdpd lkaahaahpw ivtwddheve nnyadevpdg sppeaflarr aaayrayyen
      301 lplrppqqps gpdlllyrrl qfgrlaqldi ldgrqhrddq tagdgwrvpt adterpdrtm
      361 lgstqerwls dgwkgskavw nvvpqqcvls rrrnrtagpf plsmdawdgy paarkrfvda
      421 araagvdnlv vltgdvhvhy amdikedfdd kssrtigvel vttsvasggn gvakpgdwqt
      481 mmdanphlkf ydgrrgyvlv tldqrqlrad yrtvdlvtkp gaplvtaasf isragspgla
      541 pa
//
LOCUS       WP_181766328             283 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181766328
VERSION     WP_181766328.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 283)
  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..283
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31158
     Region          17..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          90..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 manikeldpg asplhyfgae lrrlrersgl tlaqlgkivf ctgsligqve taakaptlef
       61 iqradaalga egallrlwpl lkrsrlpykq rrvaeieapa iqicafqpqa vhgllqtegy
      121 aramlgisqr edieeelaar mhrqgilrre dsplfwvvls eavlhqqvgg pevmaqqllc
      181 lldyrhvdnv qiqilpfavg ahqgmigaft lfsyedqpni ayaegydgvd atanpqefra
      241 rslrydllra salspgdsad liarvleery eyragavgpp pma
//
LOCUS       WP_181766368             271 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181766368
VERSION     WP_181766368.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  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 271)
  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..271
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..271
                     /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=30476
     Region          53..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 mtdadgdwlw hnrqnwndrv rvhsasdfyd lprfregvst lrpfeipevg dvagrrlvhl
       61 qchmgqdtls warlgadvtg ldfsedairt arelaadigm adrarfvvsd vyeapsaldg
      121 elfdivytgl galvwlpdlt swartaasll keegalylae fhpltelleq dgrtvehdyf
      181 qsegrtsesp ftytdgptlt rttsvqwqht lggvvtalag aglrieflhe hetllfkrfp
      241 qmerhgsldy rfpeghprlp lmysiravkg s
//
LOCUS       WP_181766456             279 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181766456
VERSION     WP_181766456.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 279)
  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 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   3  (residues 1 to 279)
  AUTHORS   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..279
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..279
                     /product="helix-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=29453
     Region          116..278
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <218..279
                     /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 mtdpieagav raalcrlrrt ssvpvafagm tgegrgfris emtgtrthal rglaiapgng
       61 lggkavtlar pasvtdyrss rvisheydaa vateglrsvl avpvvvrrrv rgvlyaalre
      121 slalgdrald taadavrele qtlavreegq rlaavqqlpa adprtweeir aahadlrtla
      181 qrvpdgelrq ellgacgrla tacrpeqqad gqpgavaltp retdvvscva gggtnaavaa
      241 rtglqpetvk aylrsamrkl gthtrmetvv earrlglip
//
LOCUS       WP_181766382             320 aa            linear   BCT 28-DEC-2024
DEFINITION  complex I subunit 1/NuoH family protein [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181766382
VERSION     WP_181766382.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  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 320)
  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 320)
  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..320
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..320
                     /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=34506
     Region          2..320
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 mmdvldvlwr llavllaflv lplvvgqaeh kamahmqgrv gpmyaggfhg waqlvadgvk
       61 faqkedivpd gadrrvfqla paiallpylv vlivipvgkg dmvgqvvdag vffvlavmgv
      121 gvlgslmggw asnnkfsllg glrtaaqlma yelpmllaaa svamaagtls lpgildawew
      181 wwlpwqiigg lvffvaglae lqrppfdapv adseiifgay teytglrfal fllaeyagiv
      241 vlsaltavlf lggwhgpfed glgwvwtllk tavlafvviw lrvsyprlre dqiqrvawtv
      301 lvplalfqia ltgvvkvviq
//
LOCUS       WP_181766485             341 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181766485
VERSION     WP_181766485.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=38065
     Region          58..336
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mrrtpqdpel strlrrrgfl gvaagtamas llgaaapaha aataadrdrc dplvpkgrlg
       61 iqlytlrdkv qalgfaavfk elarhgyeqv efagytqgtg ditlaglrkl lrehglrgig
      121 shvgyhsdnp ddytfatqle kvvddaaalg lphvgtaasp drygrtvdaw kraaedfnty
      181 gaaarkrglk fyqhnhqmef gfaedrpdvr lydvllaetd pelvylemdi ywayagqyrf
      241 svrpdgtpap fepldyvlkq phryplfhvk dgehdetsdd gyrmvdvgdg didyrrfltk
      301 vgrthggkrh nwlvehdqpe dsfrtarrsa ahlrslrgsg h
//
LOCUS       WP_181766481             302 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181766481
VERSION     WP_181766481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=31990
     Region          7..281
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtghaplrya ygtngladlr ledalgvlad lgydgvgltl dhmhldplap glprrtaavr
       61 kaleryglsv tvetgaryvl dprrkhhptl ldpdpdarar rldlllkavr vaadlgahat
      121 hffsgvlpeg tdkhtawprf adgvdallsa anatgvplav epepghlldd laafhrlrtt
      181 lgepeglglt ldvghclcle prspqacves agpwlrhvqi edmrrgvheh lpfgegelev
      241 apvlaalrgt gyaglvtvel prdshagpsr aqdairflrd aegsdrahgs gtgstspgga
      301 pc
//
LOCUS       WP_181766614             870 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Streptomyces albidus (ex Kaewkla
            and Franco 2022)].
ACCESSION   WP_181766614
VERSION     WP_181766614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 870)
  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 870)
  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..870
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..870
                     /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=96148
     Region          96..842
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mepatvatrl assavtpivk klfvsegaga glvdkpvris slvsfkgeqr tlnekdlakl
       61 aaelteraak asgpheapge etrrelasal ttalhsmgdl emddvqavrl gpqglarqla
      121 ypaslsatae ayfgpllhta clhilnffsq rstfiprtlt eqahqldrlv svsdlllerv
      181 parsaedarf eqryaehiar khgeltiygl dfvhtrewrl dsayisleat qdagssldia
      241 kslsadrvla dhervllrgp agsgkttllq wlavtaarqa ydehlahllg rvpfilplrr
      301 vvrdglpptp drflhavrss lagsqpagwa ervlaagrgl llvdgldevp ggqreetrrw
      361 lrelmgdfpg nlwlvtsrps avredwlage gftevslapm srhdvaafis rwhnaadaep
      421 gladslisav rthpdlgrla vnplmcgllc alhrdrrgcl pygrrdlyda alslllegrd
      481 rdrsvavpdg lrlskdsqiq llqrlahwmi rngrsemeqe davaqldrfl srtahieatp
      541 yelfrhlldr sgvlrepadg rvdfvhrtfq dhlgakaave egdfpllldn ahkdqwedvi
      601 rmavaharpa drarllrglv aevpangagg grreegpeqg efegsvrnll laaacleqat
      661 dlhpevraev tsktsrlfpp rsmaaarhva diggpmllgl lpgpegltda eaacavvaas
      721 rtgtdaalpv laryrnhssl dlrrqlvwaw hrfetdeyak eviahldetd lyftahhvdh
      781 lralrqmggr eriqivgryh prqlsehiea drlthlwlrd gyahhngedw lsafphlhtl
      841 vvpgtmsrym wstlpvrlkv vteselsghp
//
LOCUS       WP_181766615             893 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Streptomyces albidus (ex Kaewkla
            and Franco 2022)].
ACCESSION   WP_181766615
VERSION     WP_181766615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 893)
  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 893)
  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..893
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..893
                     /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=99354
     Region          292..>858
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mepvvrlass vvdpligrli aaapaafpss pdseqlmarl vsfrgeepvl sweellevaa
       61 elvrlgvvat gqrlaeaees gvaavlartl wvigeldttd tqavrlgpqd yarrlrsavp
      121 gadrelssea awfhdsllvt iclhflhlli lrspelaerl pershrigql vdlndvealr
      181 grpqpsrqda efearylrhv adqysrvtiy gidlpnpntp dnwsldatyl slaaefsses
      241 rsgatptanp agetqtgpas qgssstreva tqpdetapap aepvmtadra laghervllr
      301 giagsgkttl iqwlavstar aalpeelqtl rgripfvlpv rrfardgmps pddflaavrh
      361 plaeeapegw avrvlaagra vllvdgidea peiqrdavge qlrrllriys gtlclvtsrp
      421 pavdadwlae egfteltlap mnrdqvaafi tawhtaartd egkdhgrlde yrdmllrsip
      481 lfrelrvlat nplmcglica lnrdrsgmlp kgrkelyeaa memllqrrdp errvlyadti
      541 vmqrsprerl lrklayrmlv degsvldhat algeitrhvs aipavagqgt peeifdhlll
      601 rtgllreqad rsvefvhrtv qdylaakeav eqgnldllld haheaeweev irmavaharp
      661 kecslllqgl lapgrtgmkr nrrrllaaac lehvteldpe tharvrretr hmvrpsddra
      721 arglgwvgpi vlemlpdpdt vsdteayrla ltvtriddda avdylarlrh rrpltlrael
      781 ahgwrnfete ryaaeviqhl dpeglyfpvs dreevavlrk lggreriqiv ghftpdqlld
      841 glvrdrlthl wvaydlgagm smdwlshfpg lttlrvnprl rvtdvpehir iit
//
LOCUS       WP_181766629             634 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181766629
VERSION     WP_181766629.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 634)
  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..634
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..634
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=67725
     Region          65..245
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          316..629
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mprarpdaay lelltrrapa eaydeplaea raagaspeel aslesgklla lriraelegr
       61 rrreaeltal ietvhdlagl rdlddvlrai vqrarsllgt evaymtltdn ergdtymrvt
      121 egsvsarfqq lrlgmgeglg glvaqtarpy vtddypader frhthtidsa vgeeglvail
      181 gvplllggrd vigvlyaadr rarvfereqv allgsfaana avaidnarll setrdaladl
      241 etanemiera sdvhdrltel vlrggdvtdv agavaevlag rvefvepvva sartaversr
      301 sdgyavrdgd swvtavsagg ellgalvlhg hpaldpvdqr tferaamvts llllarrsas
      361 eaeqrvrgel ldelldatrh dprllrdraa rlhadldaph vllsarldgh tggdaeesmg
      421 rqrlwaaash lavtrhglaa ardggtvlll plaqksrdsa aqdltasrla qdvaaqlgva
      481 agspvtvgss atvpapaaqp gavaaaypea rrcvdalrll grsgqgaaae dfgflgmllt
      541 dsrdvgsfvr rtlgpvldyd arrgtdlvtt meayfacgms parakdelhv hvntvaqrle
      601 rvarllgddw qaperaletq lalrlhrlad avgg
//
LOCUS       WP_181766659             132 aa            linear   BCT 28-DEC-2024
DEFINITION  VOC family protein [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181766659
VERSION     WP_181766659.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 132)
  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 132)
  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..132
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..132
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14402
     Region          9..130
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 msdqiptpsv vpylfyddpa girdfladaf gftavstheg pdgevlniel rvgdkflmls
       61 raradmgmss paglpaaham vlvyvedvda hfararsaga qiwyepqdmp ygqreygard
      121 pengfwsfat ll
//
LOCUS       WP_181766758             590 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Streptomyces albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181766758
VERSION     WP_181766758.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            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 albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=62182
     Region          1..459
                     /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 yaepdrdalh vrvadeafal ggdtpaasyl
       61 dmdkvlkaaa dsgadsihpg ygflsenadf aqavldaglt wigpppdair glgdkvaarh
      121 iaqragaplv agtkdpvsga devvafaeeh glpiaikaaf ggggrglkva rsldevaely
      181 dsavreavsa fgrgecfver yldrprhvet qcladkhgnv vvvstrdcsl qrrhqklvee
      241 apapflsdeq naelyraska ilkeagyvga gtceflvgqd gtisflevnt rlqvehpvte
      301 evtgidlvre mfriadgeal eyadpqlrgh sfefringed pgrnflpapg tvttfdppsg
      361 pgvrldagve sgsvigpawd sllaklivtg atrqqalqra araldefgve gmataipfhr
      421 vvvrdpafap evngrqdapf dvhtrwiete fandikpfag vgdaeedegs retvvvevgg
      481 krlevslpss lgvsaaptag ggskkpkrka akkagsaasg dalaspmqgt ivkvaveegq
      541 qveegelvvv leamkmeqpl nahrsgtvkd lhaevggsls agtviceikd
//
LOCUS       WP_181766981             409 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Streptomyces albidus (ex Kaewkla
            and Franco 2022)].
ACCESSION   WP_181766981
VERSION     WP_181766981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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 409)
  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..409
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..409
                     /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=43898
     Region          19..407
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(55,62,90..91,98,102,109,240..241,244,248..249,252,
                     285,290..291,294..295,297,320,348..350,353..354,356..358,
                     362)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(62,84,86,89,91..92,178..179,188,239..240,243..244,
                     248,291,294..296,397)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 msdapeaphr ldpsgagqha vndllrehgp asqvllpgdv eavavtghae lkdfltdpkv
       61 sknachfaal regrlpegwp lavfatvsgm stadgadhrr lrglvtraft arrveslrpr
      121 vekltaella alpdaveedg tvdlrrhfay plpmsvicel lgvepglrer lhhlsgvlvs
      181 tsaapeqmia agletaeila lvvstrradp gddltsalia areedgdrls erelvdtlll
      241 miiaghettl nlianavral cahrsqlkll rsgsaswadv veetlrydsp vsffpfrypt
      301 tditvgetvi ragtpvlagy taagrdpray gpdagrfdit reqgrhlsfg hgahfclgap
      361 larmeatval galfarypdl dlavpdeell plpsfvgnsk qilpvrleg
//
LOCUS       WP_181766989              73 aa            linear   BCT 28-DEC-2024
DEFINITION  FmdB family zinc ribbon protein [Streptomyces albidus (ex Kaewkla
            and Franco 2022)].
ACCESSION   WP_181766989
VERSION     WP_181766989.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 73)
  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..73
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..73
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7054
     Region          1..46
                     /region_name="CxxC_CxxC_SSSS"
                     /note="putative regulatory protein, FmdB family;
                     TIGR02605"
                     /db_xref="CDD:274226"
ORIGIN      
        1 mpryeyrcrk cdtqfelsrp maesgapatc pdghgdtvkl lstvavggga sapamsapqs
       61 gggggccggg ccg
//
LOCUS       WP_181767161             460 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181767161
VERSION     WP_181767161.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  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 460)
  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..460
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..460
                     /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=50318
     Region          1..447
                     /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 msdlprkavt rtaklaalpl gfagrsawgl gkrigglsae lvghdlqqrt aeqlfrvlge
       61 lkggamkfgq alsvfesalp eeiagpyrat ltklqeaapp mptrtvhevl aermgedwrd
      121 lfqefddkps aaasigqvhh gvwhdgreva vkvqypgage alisdltqlg rfarllgpli
      181 pgmdikplis elrdrvteel dygleaeaqr tyaeefahdt dvvipdvvhq ceqvlvtewm
      241 ggrplaqvis kgteeerdra gqllarflfs gtartgllha dphpgnfrll padepeagae
      301 qwrlgvmdfg tvdrlpdglp pmigtalrmi idgeaeavye llcaegfvkd sielepaevl
      361 dylvpiiepa raakfhfard wmreqaaria dprspahqlg kqlnlppsyl lihrvtlsti
      421 gvlcqlgatv rmreemeawv pgfaqddgeg dslevteapa
//
LOCUS       WP_181767331             132 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181767331
VERSION     WP_181767331.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..132
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14239
     Region          18..122
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 madlgertqk gvelgaaeqc tepessitrv fqvlgkrwtg lvlaalmngp ghfaqlrrav
       61 pgisermlsd rltelgtlnl vvrtveegpp lrvsyrlsaa gqalkpamte ltrwadthlp
      121 eeaagcpeef rg
//
LOCUS       WP_181766282             529 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-N-acetylhexosaminidase [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181766282
VERSION     WP_181766282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 529)
  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 529)
  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 529)
  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 529)
  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 529)
  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 529)
  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 10261875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..529
                     /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=57677
     Region          59..176
                     /region_name="Glyco_hydro_20b"
                     /note="Glycosyl hydrolase family 20, domain 2; cl03741"
                     /db_xref="CDD:446174"
     Region          181..509
                     /region_name="GH20_DspB_LnbB-like"
                     /note="Glycosyl hydrolase family 20 (GH20) catalytic
                     domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and
                     related proteins. Dispersin B is a soluble
                     beta-N-acetylglucosamidase found in bacteria that
                     hydrolyzes the beta-1,6-linkages of PGA
                     (poly-beta-(1,6)...; cd06564"
                     /db_xref="CDD:119334"
     Site            order(191,220,268,325..326,381,402,431,481,483)
                     /site_type="active"
                     /db_xref="CDD:119334"
ORIGIN      
        1 mgpkwpkklv gsttalvtga vtvltlsacs teeagggsgs qsgssavptp ttpartgpap
       61 aaipsvrdwq pvrgpgweps kytrvvadpd gpladeakll arelkvpfag gaahtadvel
      121 alddaskegr egyelrsrng qvkisgsada gvfygtrtll qsvrarggva dgvvrdepdr
      181 pqrglmldva rkhfsaswie eriremgdlk lnqlqlhisd dqafrvests hpeivskprl
      241 tkkqmrsive laesrhitvi peidspghlg avlkahpelq lkdesgtpte gaidisnpda
      301 akiiddllre yadlfpgkyw hlggdeylal akrdpdasyp qlakkareed grdagvqdla
      361 tswlndraev vreegktpqv wndgvhedga vrphrdrqia ywtgreager npveflkegw
      421 klinlndeyl yyvlgqpnnf typtgrriye qwtpavlrgt kpvpkslsgp khipggrfav
      481 wcdqagaqtp eqvatgirmp lratsqklwn pekpalswed fkklgagvg
//
LOCUS       WP_181766662             434 aa            linear   BCT 28-DEC-2024
DEFINITION  M50 family metallopeptidase [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181766662
VERSION     WP_181766662.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  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 434)
  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..434
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..434
                     /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=46615
     Region          4..428
                     /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 mttlmtilgi vvfivgllfs iawhelghls takmfgirvp qymvgfgpti fsrykgetey
       61 gikavplggy irmigmfppg edgtlrarst spfrgmieda raaayeelkp gdekrlfytr
      121 spwkrvivmf agpfmnlila vviflvvlms fgintqtttv ssvskcvipa saksdkcpan
      181 akdspakaag mlpgdkivaf dgkrvgewst lqqqirdttg pasitvereg arktlqadli
      241 snkvaksdgr gsyvegqyvt agflgftpas gvvqqtfpqs vdrmsdmmas gvqalvalps
      301 kvpdlwdaaf gggerkqdsp mgvvgaarvg gevfsldipp tqrvatmlfl vagfnlslfl
      361 fnmlpllpld gghiagalwe svrrafakvf rrpdpgpfdv aklmpvayvv agificftll
      421 vlvadvvnpv rlag
//
LOCUS       WP_181767513             306 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181767513
VERSION     WP_181767513.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  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 306)
  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 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
REFERENCE   4  (residues 1 to 306)
  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 306)
  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..306
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..306
                     /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=31207
     Region          1..252
                     /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 mdlsgksavv tgsgrglgla yaealaaaga svvindvdaa aaeaavkkit daggsavavv
       61 apvgdtatan slvetavdaf grldvmvtna gilrdrvlwk msdddfdavv dvhlrgtftc
      121 araaavrmre qgtggrlilv sspagqrgnf gqtnyaaaka givamartwa lelararita
      181 navvpvaate mtrtipafap lieeaektge plpgwlrrde gfgtaqdaap lvvylasdaa
      241 sevtgqaigi ggdkltlwth pqekapavya dggwdadsia eawaagpgsq petygipapr
      301 ppeerg
//
LOCUS       WP_181767531             309 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181767531
VERSION     WP_181767531.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  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 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   3  (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   4  (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   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 11418686
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..309
                     /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=32849
     Region          4..304
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtlrvvltga tgfigtavln rltgedaavr altrrelrlp pdveqvradl trpesltgac
       61 sgadvlvhaa pfvgsdeqqc vqvndlgtaa lmeeaaragv grivqvstta vygrgphrge
      121 avgdlepapg satsrtrlag ekhalkrgal vlraglvtga gdrwvvpala eltrrvpgyw
      181 lggearlsmi avedlarivt haalrlpapa hgvhhavhpe pvrnrdllds laslallppv
      241 egeltweqcl tlmrehsgri getqlellay dhfysgaslw kacelapgpg plarldeaad
      301 wyrghltrs
//
LOCUS       WP_181767647             315 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181767647
VERSION     WP_181767647.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=35018
     Region          4..314
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mshpttrvla mlelmqahhr msgsdlaerl gvdertvrry agrlaelgip vtaergrygg
       61 yrlmpgyklp plmlnddeat avvlglmagr rlglpgeaae salakvqrvl prslrervqa
      121 lqetlgftlt sregdapatd tvltlaqaar errrvrmryr swqgqdsere vdtyglvfhs
      181 grwyfaghdh rsgqtrtfra drvvavemgt atfdmlddld pvqyvtrsla avpythevev
      241 vlettlreag rrippsaasl setpdgvlvr araenldgma qmlaglgwpf kirrpdelrd
      301 avrdlaarlt erada
//
LOCUS       WP_181767588             335 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA desaturase [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181767588
VERSION     WP_181767588.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  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 335)
  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..335
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..335
                     /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=37105
     Region          30..323
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mttsppevld sspeaenktt agasvspadi atlggdkrhs aeqialllfi vvpflaliaa
       61 vpltwgwgvs wldlglltam yfigchgiti gfhryfthgs fkakrplria lavvgslave
      121 gpvvrwvadh rkhhkfsdae gdphspwrfg etvpalmkgl wwahigwmfd eeqtpqqkya
      181 pdlikdpair avsrqfvlwt tvslllpaai gglatmswqg altaffwgsl vrvallhhvt
      241 wsinsichav gkrpfksrdk sgnvwwlail scgeswhnlh haeptsarhg vekgqldssa
      301 riirwlekag waydvrwpar dridsrrkeq psqaa
//
LOCUS       WP_181767825             726 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181767825
VERSION     WP_181767825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 726)
  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 726)
  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 726)
  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 726)
  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..726
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..726
                     /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=79709
     Region          30..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 mtpgphepeg lekdglrrfa tiwsravypv tqtsmtrael edylhplavk lcdaihehpf
       61 saapgrevgv alveghctsp dalphllgvi daylvlygrd panknlsvee ararcsrlqh
      121 tiaagftqal rdrtlgeqea lsraalaaqt aveealhase trfravfnda tigisiadmd
      181 grirdanetv armfgrsvee mrrrnvnewv hpddapevwk qhrqlvrger dhfrvekpyq
      241 rpdgtvlwtn ltvsllrdpe gepryqlall editerrllh lrlryeathd eltglpnrtl
      301 faerldrlls asggvkrfgl cyldidgfka vndslghavg dqllvavaer lqsctagsgh
      361 lvariggdef aalvtdpsgp edvaelarqv laalatpigi dgrelsvras igivegpsge
      421 lrpeevmrsa ditmyrakda ggnryeladp dsdaraidrh sltnhlpaal erdeffleyq
      481 plirmsdghv dgaealvrwk hpvhgrlgpd rfiplaehtg livplgrwvm eqavrqacaw
      541 heqrdaekvk gaaaeaplrv nvnlsprqlh hpdlvpdtva vleaagmaps slclevtesa
      601 ligadedelk plrqlaelgv eialddfgtg ysnlanlrrl pattlkldrs ftrglqqhpa
      661 dpvdvtfveg ivtlahalgl avtvegvete hqasqlremg cdtaqgwyya rpgpastfqh
      721 gfavtp
//
LOCUS       WP_181768079             322 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768079
VERSION     WP_181768079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            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..322
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=34277
     Region          1..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 mrallvvnpv atttsvrtre vithalasdl kldvattesr gharelarla avngetelvi
       61 alggdgtvne vvngllhegp dpeglprlav vpggstnvfa ralglpnhav eatgqlldai
      121 etgrertigl glasgvpdtd dagvrsrwft fcagfgfdag vvgrveqqre kgkrsthaly
      181 vrqvlrqflk eqhrsggtir leregaapve dlvlsivcnt apwtflgnrp vyaapeasfd
      241 taldvlglsr ltslavgryg tqlltssptr gphgrhavtl hdvsdftlhs qvplpfqmdg
      301 dhlgvrtsvn ftgvrralrv ia
//
LOCUS       WP_181768108             456 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181768108
VERSION     WP_181768108.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            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..456
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..456
                     /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=47774
     Region          <53..128
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
     Region          131..456
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mgidpgrayg gsggperrrv lalgltaaaa ggvagsgrtg atarragrpg avpepvsflr
       61 tswstdpyar gsysflapsr lgvkartlla aavdgrlhfa geacsseapa tahgalesgr
      121 raakeivrgs regrhvvvig agfaglgcar aladagfevt vleardrvgg rvrtrriggv
      181 paetgaswih gskgnamtrv lrqsggrgle fdygsvtgrd adavaelarh rrrlddvenp
      241 dttpvsavlp rspsaalrha anihyaqeya adpdrlavta eregrdlrgp dlllpdgyds
      301 lvahvrgglp vrtgavvtav rhssagvtvt lrnspavead havvtvpigv lkadtiafep
      361 slppvkrqav dalgsglldk lwlefphvfw drdadvieff dreapgrwsw wvnghkafga
      421 pvllgfnggr aahalarvsd eallascgna lhsmrr
//
LOCUS       WP_181768163             282 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181768163
VERSION     WP_181768163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 282)
  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 282)
  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 282)
  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 282)
  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..282
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..282
                     /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=28144
     Region          1..282
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrplraiplp slisvllgal laillapqpa aardrivvgg hpvdaathpw vvalasrdrf
       61 gdsrsgqfcg galvgvrtvi taahclstev lgvkhgevdd lraisgrgdl gtregrempv
      121 skvwinpgfd pesnagdiav ltladampeg ataamagsgd aayaagtaae vfgwgdtsga
      181 gkyasglrsa qvkmlkdsac akaypagthg ssggafesrs mvcagvaagg rdacqgdsgg
      241 plvaggrvvg lvswgagcge egrpgvytrv samaelvrah sg
//
LOCUS       WP_181768224             401 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Streptomyces albidus (ex Kaewkla
            and Franco 2022)].
ACCESSION   WP_181768224
VERSION     WP_181768224.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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 401)
  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..401
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..401
                     /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=43988
     Region          19..401
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(56,63,88..89,96,100,107,235..236,239,243..244,247,
                     280,285..286,289..290,292,315,342..344,347..348,350..352,
                     356)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(63,82,84,87,89..90,174..175,183,234..235,238..239,
                     243,286,289..291,391)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mvarpvgltq lspdfvcdpy pvyaklreeg pvhhvrgpdg velwlvvgyd acrtaftdpr
       61 lsrdwlksgs lgqltgaedv ptpalahmlm sdppdhtrlr rlvareftpr rveslaprvq
      121 qitdelldam qarperaadl iasfafplpm tvicellgvp eldreafrgw snemvaptgq
      181 eaqgrayvem paylseliga krkapgedll samihvvdeg gdrlspdeli gmcvlllvag
      241 hettvnlign gmralfahpe qlaalradfg lldgaieeml rydgpvesct erlaledvem
      301 dgvtipagsi vlismadadr dparfeeper fdvrrdargh iafghglhhc lgaplarleg
      361 riavgsller fpgltpdvde arlswipgml irgvrelpvr w
//
LOCUS       WP_181768279             273 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768279
VERSION     WP_181768279.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 273)
  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..273
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30032
     Region          17..72
                     /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          90..268
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mtqdadgeas gaflkcfgkq lkllrerael tqaelgsrig ygadqvasve rgrripkpem
       61 ieaadrvlda ggllsamkee vararypaff rdaarleaea velhaydthv lngllqtedy
      121 aralfrmgrp lldeetveqr ligrmarqdi farrpaptls fvieepvlrr plgglhvlrg
      181 qleqvllvgq rlnveiqvmp tsrednagmg gpftllspkg geqvaymegq grsttvtard
      241 evrsissryg iiraqaltps eslafieell gel
//
LOCUS       WP_181768434             487 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768434
VERSION     WP_181768434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 487)
  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 487)
  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 487)
  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 487)
  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..487
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..487
                     /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=52071
     Region          1..487
                     /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 mnkplrriai fcgllvlall vrdnwiqlvq adelksdpkn rrvsiaryaq prgniivdgk
       61 aitgsadtks gdfrykrtyk ngpmwapvtg yasqafganq iealndgilt gdddrlffnr
      121 tidmltgkpq kggnvvttln akaqraafeg lgdnkgavaa inpktgaila lastpsydps
      181 sfagngdadt sewsklqkqk nedepmlnra lrqtyppgst ykvvtaaagl esgrydldka
      241 tetpdpyrlp dsstdlgndg dipcknatvr nalryscntv fakmsnslgn gemikmsekf
      301 gfndkeldtp vraaesvype dnkpqnamag igqasnratp lqmamvasav anngtlmkpy
      361 mvdqlvapnl nvvqqqkpke lsepvssena qklqqametv vekgtgttaq ipgvtvggkt
      421 gtaqhgenns knpyawfisy akdkdgsapv avavviessn tlrddiaggk laapvakrvm
      481 navlegk
//
LOCUS       WP_181767752             424 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Streptomyces albidus (ex Kaewkla
            and Franco 2022)].
ACCESSION   WP_181767752
VERSION     WP_181767752.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 424)
  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 424)
  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 424)
  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..424
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..424
                     /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=46322
     Region          32..420
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(68,75,103..104,111,115,122,252..253,256,260..261,
                     264,297,302..303,306..307,309,333,361..363,366..367,
                     369..371,375)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(75,97,99,102,104..105,190..191,200,251..252,
                     255..256,260,303,306..308,410)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mgehgqpvap tgrletsadr pvvidpaggd ihaeadrlra fgpaalvelp agihawsvss
       61 mellkqlltd prvskdprqh wpawqrgefh dswirswvgv tnmftsygae hrrlrklvap
      121 aftarrteam lprveritgq lldamadlpd gepvdlrsay ahplpmgvic elfgipddqr
      181 aemarlveqi mdtsvtpeea artaqevqra fgalvalkre qpgedltsvl vsarddygsr
      241 lseaelldtl llvigaghet tvnlignavh allthpdqlr lvldgkvpwn dvieetlrwa
      301 psianlplry avedielrgg vtirqgeail atyaavgrdp grhgreagqf dirrtdvehl
      361 afghgahfcl gaplarmear talpalfgrf pglrlavpae epepvgsfia hgyltlpvll
      421 kgkr
//
LOCUS       WP_181768232             324 aa            linear   BCT 28-DEC-2024
DEFINITION  polysaccharide deacetylase family protein [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181768232
VERSION     WP_181768232.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  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..324
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..324
                     /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=35841
     Region          57..306
                     /region_name="CE4_HpPgdA_like"
                     /note="Catalytic domain of Helicobacter pylori
                     peptidoglycan deacetylase (HpPgdA) and similar proteins;
                     cd10938"
                     /db_xref="CDD:200563"
     Site            order(63,65,135,139,271)
                     /site_type="active"
                     /db_xref="CDD:200563"
     Site            order(71..72,78..79,81..83,85..86,90,94,113,116..118,
                     137..138,140..141,144..145,148..149,152..153,156,176..177,
                     179,197..203,222..224,229..231,233..235,250..251,254..255,
                     258,277..279,281..282,285)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:200563"
ORIGIN      
        1 mstddapspd tapaapsvad drpswqwpes vwrghaeavr agrsltpprw peaarvaval
       61 sfdsdhetip lrdaetspgr iaqgeygarv gavrvlelle rfgvpatffm pavsallhpd
      121 earryvregh evgvhgwihe rntllgaede ktlirrslet ltevtgaapt girtpswdfs
      181 dstlqtildl gfdydsslma ddepyevvar gtatglveip vdwirddapy ftmdrftavr
      241 pytrprdvle iwkdefdaay rdggvfqltm hphvighrsr lvilrelldh isahagvwfa
      301 thaqlagaar eqldrpavpt epda
//
LOCUS       WP_181768508              62 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768508
VERSION     WP_181768508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=7324
     Region          1..62
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 marqkmlklq evleeidmsr aafyrmrarg eaprliklpn gqlrvrradl ddwwerceqh
       61 aa
//
LOCUS       WP_181768478             858 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181768478
VERSION     WP_181768478.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 858)
  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 858)
  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 858)
  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 858)
  AUTHORS   ter Beek,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 858)
  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 858)
  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..858
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..858
                     /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=89714
     Region          1..858
                     /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 mtvfkaslrn ffahkgrmal savavllsva fvcgtlvftd tmnttfdklf aatsadvtvs
       61 akkskdrdsr qetdkpptvp asalskarsa egaksaegvv ssekvtvvde ddknvgsstg
      121 aptiagnwtv gdrrtmeits graprgpadv mvdadtakkr klelgdelrt itvtgdftak
      181 isgiatfqvt npgaaivyfd tetaqrkllg atgaytglav sadsgvthgl lkknvkaslg
      241 adtytyqtqk eaadssrdqi gsfldvmkya llgfagiall vgiflivntf smlvaqrtre
      301 iglmraigss rrqvnrsvli ealllgvags vlgvgagvgl aiglmelmgy lgmnlstsel
      361 tiawttpvag lvlgilvtml aaylparrag rvspmaalrd agtpadgkag alrgvlgvll
      421 cggggaglya atkaekaaeg svwlgvgvvl tligfivvgp llagglvrvl svvtlrpfgr
      481 vgrlaernal rnprrtgata aalmiglalv aslsvvgssm vasatkeldr svgadfiiqs
      541 gngqpitrtv ekklkasknl etvtsykivn aritapggkp dgaqltatdp symrdlrret
      601 ksgdldaayd rdsmsvgday akkndvkvgd tlkvafgsgr takltvaavt sddssvdkgs
      661 mytdiatarr ylpagqvppn timfgsakdg qedaaytalk kemkpypqyq vrdqadfkqt
      721 lqdqvgqmln mvygllalai ivavlgvvnt lalsvvertr eiglmraigl srrqlrrmir
      781 lesvvialfg amlglglgmc wgaaaqklla leglkileip wptigsvfig salvglvaal
      841 vpafragrmn vlnaiate
//
LOCUS       WP_181768583             297 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768583
VERSION     WP_181768583.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10007181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..297
                     /product="helix-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=32224
     Region          73..131
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mdyeflfvve gvsaesdldv gvvfdefdgl lashrgrqll tvsgdgsgav daahrlsvrl
       61 rrvlpavrlv rldpdlvgva diaertrrsr qnvlqwtkse rrrsetfpep egtagrspvw
      121 rwgevnawln avgegddvhv plreealaid vmlpqwqram degrpvvavv vpqddrtder
      181 vaiaqllhga lhdaavlktv salprmehsr lvvacalptd rlrtvleqit pedmsgllat
      241 rvdegelkli gvasralpgt rpiaelglsq eatvgdlllq laqgdgedss ptplala
//
LOCUS       WP_181768591             213 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces albidus
            (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768591
VERSION     WP_181768591.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 213)
  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 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   3  (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
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..213
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..213
                     /product="helix-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=23139
     Region          61..213
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <153..213
                     /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 mnqhtsvdrv tvdvraqdpi sqaglashlr trpevrlvep entetpevvv vvadavdedv
       61 lralrqihrt savrgvlvtt hideqqllsa aecgfigivr raeatperlv rvigavakge
      121 ghvppdllgn lleqvgrlqg evlgprglnf tglanreiev lrlvaegcdt adialklays
      181 ertiknvlha vmtrlnlrnr shavayalrq gli
//
LOCUS       WP_181768824             284 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768824
VERSION     WP_181768824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=30085
     Region          8..274
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msaaglarfs inqetvkqls lpeladacgk lgvtqvglwr apvqeygpea aarlvreagl
       61 tvtslcrggf ltaldpaera ralddnraav deaatlgtgt lvlvsgglpe gsrdlrgare
      121 riadalgela pyagergvrl aieplhpmfa sdrcvvstla qaldlaerfp pdqvgvvvdt
      181 yhvwwddqap aqiaragegg rlaafqladw vtplpegvll grgqlgdgsv dlrafremtd
      241 aagyegpvev eifnpglwar dglevlaeta qryvrhalep aaki
//
LOCUS       WP_181768956             206 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein, partial
            [Streptomyces albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768956
VERSION     WP_181768956.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  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 206)
  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..206
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         <1..206
                     /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..>138
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 vldalgisld avggplrvpd tatgtlivan hvswldvvaa lavepvplla krevagwpvi
       61 galsrragtr fvdrdalrel vgvvreltth lerggsvmvf pqattwctap ggpfrraafq
      121 aaldagapvr pvaidfsqhg gisraasyvg ddtleasvrr vavseglvar vtacaplqpn
      181 ghdrrslaaa ayaavcdavg rpapee
//
LOCUS       WP_181769023             376 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Streptomyces albidus (ex Kaewkla and Franco
            2022)].
ACCESSION   WP_181769023
VERSION     WP_181769023.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            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 albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     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=39957
     Region          94..232
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 mcgggpvtvf raeetdarpv lrphaedafa delsalaaad drprparwrl spwavstyll
       61 ggelpggtvi tpkyvgprri vevavstlat drallllgvp gtaktwvseh laaavsgdst
      121 llvqgtagta eeavrygwny aqllangpsr dalvpspvmr amaegrtarv eeltripadv
      181 qdslitvlse ktlpvpelgd eiqavpgfnl iatandrdrg vnelssalrr rfntvvlplp
      241 etaeaevdiv arrveqlgrs ldlpappdgt aeirrvvtvf relrdgvtad grtklkspsg
      301 tlstaeaisv vtggmalaah fgdgvlragd vaagvlgavv rdpssddvvw qeyleavvre
      361 rdgwkdfyra crevsa
//
LOCUS       WP_181769096             287 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase, partial [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181769096
VERSION     WP_181769096.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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 287)
  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 287)
  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..287
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..>287
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          61..282
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 masrpspala whwltrrsra atarsvlage asaeaarkqe lelvasappe vefpvvgdth
       61 aaaffdldnt vmqgaalfhf grglykrdff ekrelarfaw qqayfrmagr edaghmadvr
      121 ssalsivkgh rvseltamge eiydeymagr iwpgtralaq ahldagqkvw lvtaapveta
      181 tiiahrlglt galgtvaesv dgvytgrlvg eplhgpakae avralaaaeg lelercaays
      241 dsandipmls lvgypyainp dsrlrdhare mgwrlrdyrt arkaarv
//
LOCUS       WP_181769155             470 aa            linear   BCT 28-DEC-2024
DEFINITION  nitrate/nitrite transporter [Streptomyces albidus (ex Kaewkla and
            Franco 2022)].
ACCESSION   WP_181769155
VERSION     WP_181769155.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 470)
  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 470)
  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 470)
  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 470)
  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 470)
  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 470)
  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 470)
  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..470
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..470
                     /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=48894
     Region          40..433
                     /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(50..51,54..55,58,90,144..145,147..149,152,171,
                     174..175,178,248,251..252,255..257,260,288,292,344..345,
                     349,353,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mtaataapga rkggrwierw epedetfwre kgsgiahrnl llsvfsehig fsvwtlwsvm
       61 vlfmgpqygi dpagkfllis matlvgavar vpytfavarf ggrnwtvvsa alllvptvaa
      121 wlvmepgtsy ttflvvallt gvgggnfass mtninsffpl rrkgwalgvn agggnvgvpv
      181 vqlaglavig tagaghpril lgvyiplivi aavcsalwmd nlapvrndsg aareavrdah
      241 twimsflyig tfgsfigysf afglvlqtqf artpleaasl tflgpllgsl irpvggqlad
      301 rfggaritlw tfaamaaatl vvvaasltes lpvfvlgftv lfvlsgvgng stykmipaif
      361 hakalargit gedaavrgrr lsgaamglig avgalgglgi nlafrqsfet vgtgtaaylt
      421 flvfygvcca vtwavylrga sapiadgadg saassaaape qekrpvyagv
//
LOCUS       WP_181768791             227 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Streptomyces albidus (ex
            Kaewkla and Franco 2022)].
ACCESSION   WP_181768791
VERSION     WP_181768791.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 227)
  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..227
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..227
                     /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=24718
     Region          4..223
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mslltvghrg vmgvepentl rsfvraereg fdvieldlhl skdgalvvmh dadvsrttds
       61 sgaiadftla elreldagqg eripvfeevv eavrsplqae ikdraaarvl vgvinelglh
      121 drvtvisfhd ealrevrthl pemplvlvtg rstptapera relgavmvsc elrwleaetv
      181 erchadgikv iswtvntdee lslarelgld gvvtdmpeik raagrga
//
LOCUS       WP_181768464             529 aa            linear   BCT 28-DEC-2024
DEFINITION  xylulokinase [Streptomyces albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768464
VERSION     WP_181768464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 529)
  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 529)
  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 529)
  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..529
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..529
                     /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=57336
     Region          7..506
                     /region_name="XylB"
                     /note="Sugar (pentulose or hexulose) kinase [Carbohydrate
                     transport and metabolism]; COG1070"
                     /db_xref="CDD:440688"
ORIGIN      
        1 msghlslgid igttnvkaci ldtstgkvva saaaehplhh phpgwaeqep ddywravtyc
       61 iarcveqcpg pasaiagvsv sglvgvtlpv drdgrplrra miwmdsraqr eceeirelvg
      121 eerikavngn rvaswfiepk amwlrrhepe vfdsihklls pagyctmrlt geyamnhgda
      181 glfypyehrh srwdhsltea lglppgiypd ihtsdtvigt vtshaaretg lregtavvag
      241 gtdigaaalg agaveagqay ysmgtgsnlg vlvpreelpe eyrilkwphv ldgmtlfdap
      301 maftgaslkw frdkfadpes alaarmgrnv fdlvtaqaeq itagadglly lpylgnslsp
      361 rwdenacgvf fgmqpftsra hviraliegv aydlysnvri aedggavfpe lvlnggptks
      421 plwnqitanv tnrrllipdv deaaplgdav vaatgaglya gmrepmkdla pirhvvepdp
      481 elhemyvdff glwsqlyedl kpsmkrhhal vqrysdpaps amsgaggss
//
LOCUS       WP_181768727             219 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-ketoglutarate-dependent dioxygenase AlkB family protein
            [Streptomyces albidus (ex Kaewkla and Franco 2022)].
ACCESSION   WP_181768727
VERSION     WP_181768727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidus (ex Kaewkla and Franco 2022)
  ORGANISM  Streptomyces albidus (ex Kaewkla and Franco 2022)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 219)
  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 219)
  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..219
                     /organism="Streptomyces albidus (ex Kaewkla and Franco
                     2022)"
                     /db_xref="taxon:722709"
     Protein         1..219
                     /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=23739
     Region          13..217
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
ORIGIN      
        1 mdaliprppa rlgpgavhrp gwlpkeqqrq lvtacrewaa gpvplrhtrl prggvmsvqt
       61 vclgwhwqpy rytrtagdvn gsrvaafpew laelgrrala dayddpdage gydpdtalin
      121 fydgrakmgm hqdkdeqsga pvvslsigdt clfrfgnttt rgrpytdvel asgdlfvfgg
      181 psrfayhgvt rvfegtgdpa tglasgrlni tlrvtgltd
//
LOCUS       WP_181769272             602 aa            linear   BCT 28-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Bradyrhizobium sp. UNPA324].
ACCESSION   WP_181769272
VERSION     WP_181769272.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 602)
  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 602)
  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 602)
  AUTHORS   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 602)
  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..602
                     /organism="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     Protein         1..602
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67327
     Region          51..600
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 msmattdtpk petkfdaeaf amnvarames ggkalaaylk presgevqdr ppaelaevvk
       61 tftsvaeywl sdtsrssdlq tklakdyldl wgsavrrmag qdappaiaps prdkrfadpe
      121 wksnqffdfv mqlyllttkw aqelvrdaeg ldpqtrrkae fyvqqvtnal spsnfvltnp
      181 evlretvass genlargltm laediaagkg mlkirqsnpd nlvvgvnmat tpgkviyqne
      241 mmqliqyspt tetvlrtpll ivppwinkfy ildlkpeksy ikwcvdqgit vfviswvnpd
      301 krlgnkswed ymkegpltam dviekvtgem kvhtagycvg gtmlattlaw laekrrqrvs
      361 satffaaqvd fthagdllvf vdeeqisale kdmkaagvle gskmamafnm lrsndliwsy
      421 vvsnylkgqq psafdllhwn sdatrmtasn hsyylrncyl enrlstgtmv ldntlldlsk
      481 vrvpvynlat redhiapaes vlygsqffgg pvkyvlsgsg hiagvvnppa snkyqywtnd
      541 nikdvnvaqw mkdavehkgs wwpdwrqwlg eldpeqvrar apgneafppi edapgsyvrv
      601 ra
//
LOCUS       WP_181769318             513 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Bradyrhizobium sp. UNPA324].
ACCESSION   WP_181769318
VERSION     WP_181769318.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 513)
  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 513)
  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..513
                     /organism="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     Protein         1..513
                     /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=56748
     Region          5..502
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mnfpfsrrrf ltagagalgt iampylsraa drplvthgvq sgdvtvdggv vwartdrpaq
       61 mlvevattdt frdaralppi aalpesdfta kmlienlpgg qdifyrvrfr dlshsavege
      121 avvgrfrtap adrrdvsfvw ggdvagqgwg inpddggmft fsamrrhrpd fflhsgdtiy
      181 adgpiasevk ladgkiwknl tipekakvae tldeyraahk ynltddnlra fnaevpifvq
      241 wddhevtnnw slskelpaay kerdiallaa rgarafhemy plresinepg rvyrqisygp
      301 hldvfmlder syrgpngpnl eaaygpasyf lgpdqiawlk rgllnsratw kviasdmpls
      361 lvisdtpkgg seafaqgdgp vrgrefeiad ilrfikmapi hntvwltadv hyaaahyydp
      421 nkaqfrefep fwefvsgplh agtfgpnald ntfgpevrfv kapgkdsqnl ppsagmqffg
      481 hvkidgasgq mivtlrdrad valwsttldp kqs
//
LOCUS       WP_181769357             178 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein [Bradyrhizobium sp. UNPA324].
ACCESSION   WP_181769357
VERSION     WP_181769357.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 178)
  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..178
                     /organism="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     Protein         1..178
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19488
     Region          4..172
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 mrrlmllrha ktetdapsgr dqdrrlddrg qrdaarigdw iaahppfpdt vlvshavrar
       61 qtwdiaweam kdrvpapqve ilpelygadp aqildsirta tapadpkrll lvahnpgmhe
      121 aalmlmgsgd pagaraladn lptsglaifd fdvkdwgdva yrrgklvlft spkllrsg
//
LOCUS       WP_181769346             536 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Bradyrhizobium sp. UNPA324].
ACCESSION   WP_181769346
VERSION     WP_181769346.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     Protein         1..536
                     /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=57379
     Region          1..530
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 msetdvviig aghngltcaa ylamaglrvr vverrkvvgg aavteefhpg frnsvaaytv
       61 sllnpqvird lklaeqglri verraqnflp apdgsylltg egrtkasvar lsahdagald
      121 gfsreledia dvlrqfvlra ppnlvdgfgt aairegvnaw ktanilrglt leqsrslldl
      181 ftrsagemld erfehdlvka lfgfdaivgn yaspyaagsa yvmlhhafge vngkkgvwgh
      241 aiggmgaitq amaraardrg avidtdagvr eiiverdrav gillengsai rakyvaanvn
      301 pkllythlia aealpadfla rirhwkngsg tfrmnvaldr lpsftalpge gdhlssgiil
      361 apslpymdra yldaraegws rspvvemlip stlddtlapa gqhvaslfcq hvaptlpegk
      421 swddhrdeva dlmiatvdky apgfwasvlg rqilspldle rqfglvggdi fhgaltlnql
      481 fsarpmlgha dyrgplkgly hcgsgahpgg gvtgapghna aqailrdhrs lfgsrg
//
LOCUS       WP_181769386             531 aa            linear   BCT 28-DEC-2024
DEFINITION  Y-family DNA polymerase [Bradyrhizobium sp. UNPA324].
ACCESSION   WP_181769386
VERSION     WP_181769386.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 531)
  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 531)
  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 531)
  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..531
                     /organism="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     Protein         1..531
                     /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=58065
     Region          12..351
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(15..16,19..20,58,61,115..116,168)
                     /site_type="active"
                     /db_xref="CDD:176458"
     Site            order(113,116,189..195,224,248..253,284,310..314,316)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 msassvsrrr ilslwlprlp idriqrffgn vglvknsnep sivvikdnna lvihaldeaa
       61 erlglyigqp lanaramcpd lkvfdadvva daktlsdiad wcdrftplva ldpphglfld
      121 itgcahlfgg eaallktlvr alarqgfavg aaiagtsvca rtltrqasgs ivadgnetaa
      181 ierfpvsalg agevittglr raglktigdv aarapseita rfgarfstll ahalgqgdap
      241 isprkpppdy ivekrfaepi atdtmiamtl srladtlias mekqgkgarr leaaffrtdg
      301 vvraimvetg rpvtksavid rlfrerldal adpldpgfgf dmvrlsasrt eivvqeqrdl
      361 dahvhdndel aalidriaar iggkrvvvhl pedthipeca vmvapaqhyl aaamqaewpa
      421 rvesepplrp lrlfdkpepi kvpfaavpdg pphqftwrra lhavvrvegp eriamewwrq
      481 dgkqltrdyf riedaeglrf wifrdglyeg evfdddgkpa spnwyvhglf a
//
LOCUS       WP_181769432             784 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Bradyrhizobium sp. UNPA324].
ACCESSION   WP_181769432
VERSION     WP_181769432.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 784)
  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 784)
  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 784)
  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 784)
  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..784
                     /organism="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     Protein         1..784
                     /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=85167
     Region          101..784
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mfsirivrpc svllasaalt sfaasdipaa laqqareplp pvevtpaqsr kqakpagrga
       61 qsprraaahr paaasapkpi gpaaaaqtpl nsnavaesas rlgltvretp atvevisaet
      121 mreqgyrtvs dvaqgavgvt sgdnpaepsa fsmrgftnsq intlyngiki gpqnmtsrim
      181 dtanldavef lkgpaslisg egaaggainf vtrqphsgps rneadfswds lnslrahygs
      241 ggstnvqgld yrfdvsrsal ngfaddtntk tldvsgqlny risdslkvsg aieyredrsk
      301 aywgvplvpi afsgshatsg ivsgnyvsny sktnlgavti ddrtfntnyn vldnrnvaqe
      361 vwlrggfelk lapdltlksq aygygaertw fnneveafns ttnlvdrerf yvahsqrlvg
      421 nitdliwdtn iagfdnrlvt tlsssyldfv rpgaanfpgd svdlvdpnrg fygllttkqq
      481 taridneals vedrlkltrt faligglrve higldrnstd knglenvgfp ytkdwapvtg
      541 rigytweavp gltffsqyat gadvsannif lltptqpldl ttartyetgv khlfwdnrae
      601 wsfsaydilr knvyaagggq alniagrqes rgvelaasfr pieplrlwgn iayvdaryad
      661 ynfvggsfsg ntppnvpriv anagasyrlf tpwpvelgit grhvgdrynt dantvtmkay
      721 tvadvyafvd iprsvfnavd qarltfrvrn itdkryaiwg dpfypdqvll gaprtyelsa
      781 afkw
//
LOCUS       WP_181769344             205 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CGNR zinc finger domain-containing protein
            [Bradyrhizobium].
ACCESSION   WP_181769344
VERSION     WP_181769344.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 205)
  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..205
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..205
                     /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=22832
     Region          2..204
                     /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 mdrppamfia dslgldflns vatpidtpvd widdgeglid wlsqaklvpa eeldalkarv
       61 rrgeldevad qtralrewfr gfvlkhagrp ltaqalqelg plnsllgrde afsriepaqe
      121 gggvlalqrk rrwrspealm lpvgealakl vceedfsnvk aceghnctmv fadhtrrhar
      181 rwcimavcgn rakqaahrsr lksrq
//
LOCUS       WP_181769450             252 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Bradyrhizobium sp. UNPA324].
ACCESSION   WP_181769450
VERSION     WP_181769450.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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 252)
  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 252)
  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..252
                     /organism="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     Protein         1..252
                     /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=25371
     Region          5..249
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mkklatlvia allivgpaha ivgggtpqad gvaravvtiv gsrgnfctgs liaprvvltv
       61 ahcvqpgady kivdrgadgt pqllnvrava ihpnfnmqam qshratadva llqleiplkg
      121 kstvtigmpt ipiqvgsrfv iagigvtvrg dgksggttrv aalvatgqpg tlqirlvdpl
      181 tngvregiga ctgdsggpvl edkpngavlv glvswstgpn gaagcggltg vtpltlyrdw
      241 ilqtarswga al
//
LOCUS       WP_181769518             433 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Bradyrhizobium sp.
            UNPA324].
ACCESSION   WP_181769518
VERSION     WP_181769518.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 433)
  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 433)
  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..433
                     /organism="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     Protein         1..433
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47389
     Region          122..433
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkrealwrpr gwralalsvi vaaavlappa yaqddrsspr epgpvfsdsg pdaelygaam
       61 gypvgargta tqvdklvgvy shfgeiypsr pvgramapwq fkrapepsia ysfgnerlni
      121 gdylkrnpvt glliarddti lyehyqyart drdrflsqsm aktlvamlvg iavsegriks
      181 iddivstyvp glagteygnt sirallnmss gvefsevydg hddiarlgra lfvdepkdpa
      241 aivaqfnirt appgtkwhya sveteilglv lraatgtpva dylhdriwdp igteadaswa
      301 idgsgqeiaf ccfnatlrdy arlgrllahd gawegrqlip rqwlldattv rpgdghlapg
      361 vatsyfgygy qvwllprepr rfallgirgq vilvdptskl imvhtavrqk psepgalrep
      421 lalwsavlqq lgq
//
LOCUS       WP_181769549             166 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Bradyrhizobium sp. UNPA324].
ACCESSION   WP_181769549
VERSION     WP_181769549.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 166)
  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 166)
  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..166
                     /organism="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     Protein         1..166
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=16894
     Region          48..160
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mnvrcwsvat alliasigpm raeealvayk plspelaldl araaldscrs rgyqvavavv
       61 drsgvtqvml rdrfagphtp ltasgkawta vsfktsttel naisqpgmmq agirdlpgav
      121 iiggglivet ggslvgavgv sgapggdade acakagieai rdklef
//
LOCUS       WP_181769590             272 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Bradyrhizobium sp.
            UNPA324].
ACCESSION   WP_181769590
VERSION     WP_181769590.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPA324
  ORGANISM  Bradyrhizobium sp. UNPA324
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
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="Bradyrhizobium sp. UNPA324"
                     /db_xref="taxon:1141174"
     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=31410
     Region          43..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 mpdiqinyhf ldtgktfehy anrrssfqsi yadllssepr lsgkvldigc ghainptlek
       61 iiskvgtldg vdpfplidpp lhlrnrwtck ledvpverdt ydmaysynvv ehvenvesfl
      121 akaieilapg avywslspna hhpftwatrl aerlglkkty vkninqkand ypayyrlshd
      181 erivraital klpvsqidfy fvpnvhwdty fpralriiah lfdrcwllrr pkrsfifmfr
      241 lrkrpllgev lsensieqgk lssdraniah qt
//
LOCUS       WP_181769782             359 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181769782
VERSION     WP_181769782.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            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..359
                     /organism="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     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=40016
     Region          29..355
                     /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 mlsnsfnldr tkndtstlld llralaaqmv cvghtwnltf apfggarptl ipdigvllff
       61 vlsgfviayt lhdrtgygsy sllnysverf ariysayapa lfliaaldyv aftlgvplfq
      121 ldsltsfvrn lfmlqgypge wgggtfgsag qlsslaiefh iyffvgglff fckgrnriag
      181 lllaiaaaal plfhfaerpd ashslfvlwl lgfggyfvai nmkidrlstv vsaalsfllf
      241 wrwrvahvrg deyalaaqpy famwfvslai aaqgqnwllr srpvieffag ysytlflvhy
      301 tivkivvglk paplwmtfti aiavsnsaaw lfalateakh krfagwilrk fdcfrmpvr
//
LOCUS       WP_181769825             324 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181769825
VERSION     WP_181769825.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
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="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     Protein         1..324
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34139
     Region          18..320
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mtarsfmlal aagllamvpa apssaqdyps havrivvpfg aggpadvaar lignvlqesf
       61 gqpfvienrt gaggvigtve aakspadgyt llmmsntqta neslltpdkr kyelmrdlap
      121 iapvnysdlv ivvnpqvpak tlaefialak aqpgkpnyas sgqgtpyhma gelfkamagi
      181 dlvhvpyrns gearsgvigg qvqmmidavp amapniaesq vralattgkq rstvlpnvpt
      241 aieagvpgye atiwlglmap sgtprpvidk lnaavnamvk rpdivklwte qgavpmsmtp
      301 eefdkflrgd iekwadvvkk fdks
//
LOCUS       WP_181769835             435 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181769835
VERSION     WP_181769835.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            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..435
                     /organism="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     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=47186
     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 mtrdwsalps vnslweatae parefpvlsg eqqadvviig agytglsaah hiarsglspv
       61 vleanrpgwg asgrnggvit akfrlsfrev davhgramak rmyeiahest dmveelvcey
      121 giasanlvrt gqvkaahnet tlraaidean wmtremgsav vrildrdgvr eetgsdifvg
      181 gvlnpgsggi hplnylrgla ngvasrgvpi fqespvvklr regdgivaet prgtvrakqa
      241 iiatnsysdl tnatahlqrt lvpfrsamva teqlprnlag klmpsgrtyt etkrmmrwfr
      301 mvdnrvifgg rgafgkqdsq aafdalrkam vgifpdladi playkwsglv amtldsvphi
      361 grlddrtlvs lgyngagvam sslmgrylaa fvrgetpdvg lldirrmkti pfyplrepav
      421 rmvagwyqfl daigq
//
LOCUS       WP_181769870             608 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181769870
VERSION     WP_181769870.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
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="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     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=65972
     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 mpepisqpdp laevrtlpel lrwrvnatpa aeayrhydag aerwvgqswr eidaefelwr
       61 ralaaenfap gervailmpn giahiamdqa alsrglvpvp mhavdnpdsi ayvlvdsgal
      121 llfvdtlerw qaivatgqpl dhlkrvvcad agglitpdar ivgldhwlaq apgasaplpd
      181 vaiepddlaa ivytsgttgr pkgvmlshgn vvanvkaiah riaaaphdvf lsflplshtf
      241 ertggyyypi aagacvayar svpqlsedlk hvrptvlvsv priyeriyal imqhrasagf
      301 veralldlti avggrrfdar qrhgapslpd rlvwpilerl vadkvlaqlg grlrvavsgg
      361 apiaepvirl flalgldvlq gygmtetspv vsvntvddnd phsvghvldg vevrlgdnde
      421 llvrgpsvmi gywhkpdetr rvkdadgwlh tgdqariedg rititgrikd ilvtstgeki
      481 apvdietail adplfeqalv vgeqrpflsa lvvlnakawv eekerlaarg qqggaaeraa
      541 llariaaavk aypsyatpra vwwtldpwti aaglltptlk nkrpalerrf adeiehvyak
      601 kpaaitpt
//
LOCUS       WP_181769900             423 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181769900
VERSION     WP_181769900.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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..423
                     /organism="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     Protein         1..423
                     /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=48793
     Region          68..368
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msrhellggm vqvyrrsgrt whcsasidgr qyrattgedd lvlakqaaed wflalrgksk
       61 agilknektf kqaadqflke yeiitegqrs pkwisgyrdr lrlhllpffg nmalseitpg
      121 raqeyrvhri etsrtgkapa rstihdeivt lrqvlktair hewlahlpdf sppyksqgkv
      181 vhrpwfspee yrrlfettrl hakeaqpqhk wdaeqlhdyv lflgntglrp deaknlqhrd
      241 vtiveegrag erileievrg krgvgyckst pmavvpyerl lgrakfvplg ktrertrkrn
      301 prqvpppefp kptdrvfpgn higqfnrlle kselkldrdg kprtayslrh tyicmrlmeg
      361 advyqiaknc rtsvemiekf yaahiknmld avainvmrpk vkkraspkdl ydapvdpdvl
      421 nql
//
LOCUS       WP_181769905             454 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181769905
VERSION     WP_181769905.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
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="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     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=48840
     Region          24..436
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtypflrrva fslaagaals laaispslaa akiqrlvspg gieawfvqda tvpliameys
       61 faggsgqdpk dksgvanlvg dlldegsgdl dsktfherld rraielsfsa srdtfrgslr
      121 mlrdnkdeaf dllrsaltsp hfdpadveri rsqvisglrr ettnptslas rkflevafgd
      181 hpygrqtngn ldsvpsitia dlkdyvgrvi akdglkiavv gdvdpatlgk lldhtfgslp
      241 akanltpvpd vdaakppqrv fvtldvpqtv itfggpgvkr sdpnfmaayv vnhilggggl
      301 ssrlyrevre krglaysvye allwmehsai figntgtrad ragdtidaid kevrriaeeg
      361 ptqkeldeak sylkgsqmla ldtssklaqa llqyqqdklp idyierrnai vdavtlddak
      421 aaakrlwgqg lltvvvgrap qaaaqpappa tksn
//
LOCUS       WP_181769922             796 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181769922
VERSION     WP_181769922.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 796)
  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 796)
  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..796
                     /organism="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     Protein         1..796
                     /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=87210
     Region          140..>404
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          294..740
                     /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 mtsaetsaah fdtapaeepr rwsarrwlap favalalgsa lltflvltgl ttieptpevv
       61 rsfylinatt illlvviivr elwqlilarr rgraaarlhv qivslfsiva vlpavlvavv
      121 anvtiergld rlfsgptkev iqnsltiara ymqdhaqlir gdilgmandi aharplydqd
      181 rrsfremlta sagsrnlpga miidkntnil esadtgmrla ysppapdfls nvnesepeia
      241 vlpdasfvaa virlrafsdt flyvarpldp nvvaqlkqte vsvaeyaqie srrlgiqvaf
      301 almfavialt ilmasvllgl nfanslvspi rrlmnaahtv stgdlhvqvp vhqsegdlaq
      361 lgetfnkmtq elrsqrdelv nasdlidsrr rfieavlssa sagiigvdas gsvgilnrsa
      421 eklighaese tlghplsdvl peldemmkaa regtqrlvqg qititrdgte rnlsvrvsae
      481 knqphdsyii tldditelvs aqrtsawgdv arriaheikn pltpiqlsae rirrkfgkdi
      541 teakdkqife qctdtivrqv ddirrmvdef srfarmpkpv megedvadtv rqavflmkva
      601 hpeidieaef kqdplraqfd rrlisqavtn ivknateaie qvppeelgkg ridvvvsreg
      661 edvlidvidn giglpkvars rllepyvttr akgtglglai vgrvledhgg rielkdasdf
      721 regqrgawmr mrfaisgqpa kaegaelapi akdttkeavt epakdaapet kepaaetkea
      781 aektydstki eastgi
//
LOCUS       WP_181769946             820 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181769946
VERSION     WP_181769946.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
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="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     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=90506
     Region          154..814
                     /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 mtaakkmpgk paaemfddip vlrrkwraal kpgdrlprye dvmlgslgrl adhiallrnd
       61 grlelsrsgr yvqrwlgeer wdiavaelsp dcatalseaa gialatgqph qasahcvrdg
      121 mvrtydvlal ptasrwgatl vgayinerga qynlldaifa atddavisla tmrdaggkpf
      181 dlqvvhhnns agtllnvakg sllwrrigeg atllalpeim dfllkavags rgeqleiehg
      241 drhlrfsata fadvvsltis dvtalkrrda sfrllfdnnp mpmwvfdaes keflsvndaa
      301 iqhygysrat flrmklheiw pkdewdshte alervgdayh ssrnwrhlra dgseievltf
      361 grrvafddrd gylvavvdit errkaearia hmahhdgltd lpnreyfqer lkqaleqagd
      421 krvgvlyidl dlfknindsf ghpvgdrllk qvaerlttav rganlaarlg gdefavilaa
      481 dvspneasac agllidmlka pydldgqemv igasigials pgdgttpeel mrnadmalyr
      541 aksdgggvhh fferemdlqa qkrrdmeldl rrafangefe lhyqplvsia sdrisgfesl
      601 lrwrhpdkgm ispaefipva ediglitqlg ewvlreacae aakwpadikv avnlspaqfr
      661 srnlvqivis alaqsglspr rleleitesi flaetdanla ilhqlrelgv gismddfgtg
      721 ysslsylrsf pfdkikidrs fvkdlaerpd cgaivraisg lgrslnittt aegvetedql
      781 dwlraegcne vqgflfsaar paaeiaklla dfgqrasraa
//
LOCUS       WP_181770191            1101 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl-CoA carboxylase family protein [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181770191
VERSION     WP_181770191.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 1101)
  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 1101)
  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 1101)
  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 1101)
  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..1101
                     /organism="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     Protein         1..1101
                     /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=117487
     Region          3..474
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          498..563
                     /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(520,529..531,538)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            530
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     Region          583..1098
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 msfkkllian rgeiairiar aaadagiatv aihpaddals lhvrvaddav eipgrgaray
       61 ldieavvkaa ksvgcdavhp gygflsenaa fakacadagl tfvgpkpaal elfgdkvaar
      121 qlakrcgvpi iagtsgpslm eeitafftsl gsnaaivika maggggrgmr vvenasdlae
      181 ayarcqseak aafgfdgvya erlirqarhi evqiigdkhg aishlwerec tiqrrhqklv
      241 evapspslsd plrgriieaa kqlataasyd nlgtfeflvd gtaedsfafi eanprlqveh
      301 tvteevlgld lvraqlavaa gaslaslgla qgsipkprgy amqlrvnmet ldvsgathpt
      361 ggvlavfepp sgpgvrvdsf gyagyktsaa fdsllakviv htpgeawhdv vakasralre
      421 fridgvvtni aflqavlahp dfrinriatd fidrniaklv eaadgaakpl yfaatehsga
      481 hgteahvaqm vpegtvmvaa plqgtivtiq vregeivrpg qqlaviesmk mehlvmaeqg
      541 grvmklvagd gvtllhgepi mylepldvaa dsaaaeadvd ldhirpdlae liarqantld
      601 anrpasverr rntnqrtare nvaqlvddgs fmeygslaia aqrrrrkldd likntpadgl
      661 imgvatvnge kfgpegarci vvaydytvla gtqghmnhkk idrmltlaed wrvplvfyae
      721 ggggrpgdtd rlgmtgldgp sfvqfarlsg lvpvigvvsg ycfagnaaml gccdviiatk
      781 nasigmggpa mieggglgvy hpaevgpvsf qspngvidil vedeeeatsv aqkylsyfqg
      841 avtewqaadq rllrraipen rlrvydirsv idlvadkdsv lelrrdygvg mitalirieg
      901 kpfgliannp rhlggaidad agdkaarflq lcdafdlpvv slcdtpgfmv gpeaektaiv
      961 rhvsrmfvtg asltvplfgi vlrkgyglga qsmigggfha sfftaawptg efggmglegy
     1021 vrlgfrkeme aiadpeeret yyrnkvaely angkavsias vfeidnvidp aetrrwimag
     1081 lrsvpkppar tekkrpcidt w
//
LOCUS       WP_181770429             267 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Amycolatopsis
            pittospori].
ACCESSION   WP_181770429
VERSION     WP_181770429.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 267)
  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 267)
  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 267)
  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..267
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..267
                     /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=28447
     Region          24..>150
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 migeanagdd padgwfpesv aasydapggv nspdvvttav dvledladgp vlefavgtgr
       61 iaaplaargv pvsgielsra maarlvdkpg gdavevtigd mtttrvdgrf slvylvfnti
      121 snvttqdgqv dvfrnaaahl rpgglflvev glpdlrrlpp gqdtvpftvt pgyvgfdqyd
      181 vvtqeftsnh vtvspdgtgr frripfryaw paemdlmari agmrpkyrwa dwdrseftae
      241 stkhvsvwea dpgmlsvpfe dggisgg
//
LOCUS       WP_181770390             316 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA desaturase [Amycolatopsis pittospori].
ACCESSION   WP_181770390
VERSION     WP_181770390.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 316)
  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 316)
  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..316
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..316
                     /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=35361
     Region          28..310
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mtatldrsqt pakgpkpvle ghrssgvqls vylgvvfpla allaavpfaw gwgltwvdvg
       61 lfvffyaisg lgitvsyhry fthgsfkakp wlrvamaiag smavqgpvit wvadhrrhha
      121 fsdrdgdphs pwlfgtspla iakgfwhahm gwlferdqtn aerfapdlvk dpaikkvddl
      181 fwlwslltlv lpavlgglit wsfwgavtaf fwaglvrvcv lhhvtwsvns vchmigerpf
      241 aardksanfw plaifsfges whnlhhadpt sarhgvqrgq idlsarliwi fekfgwaydv
      301 rwptpqrlar iaaesk
//
LOCUS       WP_181770235             530 aa            linear   BCT 28-DEC-2024
DEFINITION  Y-family DNA polymerase [Bradyrhizobium sp. UNPF46].
ACCESSION   WP_181770235
VERSION     WP_181770235.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UNPF46
  ORGANISM  Bradyrhizobium sp. UNPF46
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 530)
  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 530)
  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 530)
  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..530
                     /organism="Bradyrhizobium sp. UNPF46"
                     /db_xref="taxon:1141168"
     Protein         1..530
                     /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=58074
     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(112,115,188..194,223,247..252,283,309..313,315)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 msassvnrrr ilslwlprlp idriqrffgn vglhknneps ivvikdnnal vihaldetae
       61 rlglyigqpl anaramcpdl rvfdadvvad aktlsdiadw cdrftplval dpphglfldi
      121 tgcahlfgge aallktlvra larqgfavga aiagtsvcar tltrqasgsi vpdggeaaai
      181 drfpvsalga deaittglrr aglktigdva arsrseitar fgarfstlla halgqgdapi
      241 sprkplpdyi vekrfaepia tdtmiamtls rladtliasm ekqgkgarrl eaaffrtdga
      301 vraimvetgr pvtrsavidr lfrerldala dpldpgfgfd mvrlsasrte ivvqeqrdld
      361 ahvhdndela alidriaari ggkrvivhlp edthipeqaa lavsaqhhla aamqaewpar
      421 vesepplrpl rlfdkpepvt vpfatvpdgp phqftwrrak havvrvegpe riamewwrqd
      481 gkqltrdyfr iedaeglrfw ifrdglyege vfdadgkpap pnwyvhglfa
//
LOCUS       WP_181770437             115 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis pittospori].
ACCESSION   WP_181770437
VERSION     WP_181770437.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=12185
     Region          6..114
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mnatgpsgde llrllgtlan phrlrivaal raerayvsql arelgisral lqlhlrklea
       61 aglvsatlel sedgkamkfy evepflvels pdaiaaaapt lstpglsdve qgerp
//
LOCUS       WP_181770476             413 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Amycolatopsis pittospori].
ACCESSION   WP_181770476
VERSION     WP_181770476.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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 413)
  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..413
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..413
                     /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=44526
     Region          17..404
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(53,60,88..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(60,82,84,87,89..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 mesrcpytld iagtdihaeh anlraqgpva qvelpggvig wsvtgyqaar qvlsdnrfak
       61 dpqkwpaytn geipsnwplv gwllmdnmtt ndgedhmrlr klvsrgftpk qveltrpliq
      121 kivddlldgl ssagpdevid lkgrfatplp arvicdmfgv pesarasalr gagvnvtttt
      181 tgdeaeanve lwhqeltela efkrehpgdd ltslllaare edgsrltdee mvgtlhlmlg
      241 agsetlmnal saavvallsq peqkelldsg qvswddviee alrvnapvaq lplryaledv
      301 evagvtirkg dpvlmgftgi grdpeihget agefdaarad kthlsfghgt hfclgaplar
      361 lelrialpal farypdlkla vgvdelegqg tfimnghkev pvtlgepvia atv
//
LOCUS       WP_181770495             349 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis pittospori].
ACCESSION   WP_181770495
VERSION     WP_181770495.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 349)
  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 349)
  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..349
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..349
                     /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=36713
     Region          125..349
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 migsgesfge mlahawhilp fallfalpvv llgvvalyll rrgslastmt ilvlipvlat
       61 ltavlgisgf mftpalttmt lvcllvalvt vppalalgra iarrsvwere arereraaea
      121 srrelvawis hdlrsplagi qamaeavadg vvaepievtd yarrisgett rlsgmvgdlf
      181 elsritagal qltmasvplr dvvsdavaaq aplaeqkrvr mvenanvwpv vsgsdpelar
      241 ivrnlvsnav rhtppdgtva vqigieggea llavddgcgg ipddeigrvf dvafrgtrar
      301 tpergglasg gglglaiakg lveahrgrig vrnhgpgcrf evrlplata
//
LOCUS       WP_181770500             203 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181770500
VERSION     WP_181770500.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=21809
     Region          <50..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 mtafdrgllg hrcwlelatg ervdlpverw taipcdgddv lldacggpti digcgpgrlt
       61 aaltergvas lgvdisatav rlthargava vrrdvfdrvp gegrwrhail adgnigiggd
      121 plrlltrtae liadggtvlv eldppgrgvr qdrvrlrpds dgawftwawv gveaiaelaa
      181 rsafrvawst rrghrwfacl eka
//
LOCUS       WP_181770580             370 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Amycolatopsis pittospori].
ACCESSION   WP_181770580
VERSION     WP_181770580.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..370
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=39345
     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 mgsgvigscv slflaqrgvr vhcvdrgrpg glttdvsfar lsayqqptyr rfelshagii
       61 ehahfaglfd sapwwhptgs lawaaadgrc gvstrsfvee aerlrswgyr viwhdaakvg
      121 relepaipfs paqtpvaqlp eegwidgprm vssvldaaks igeltlsnad vqeielrggq
      181 vtalrldnge rlevdavvna agpqapavaa tlgspmvrgi adrsslvldl agdgdplrhv
      241 lrgaelharp agpgrvrvrs eqvdavltgk tesdlgrdnv enlldrayrt ipalkaftie
      301 rkrigtavfp adglpsvgpl stvsgyyeaf ansgvilapl igralatqit tgevpsllrd
      361 cspdrlrvaa
//
LOCUS       WP_181770562             273 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181770562
VERSION     WP_181770562.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..273
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28035
     Region          49..119
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mrkvataamf taltgaalmg ttagqtavaa ptvnmeavvk aamwdpykad qsitpgsgps
       61 vkvveealaa knmldkkqvd ghfgtstvaa yqkfqkslgh sglaasglpg kgsltelgkg
      121 rytvtapisv gskttvdgkt lnkrtaemit aaekkagvkf tvtqgsynag gvgasggthd
      181 gggavdisvn niknkdaavk alrevgfaaw hrtpsqgdwv ehihgiaisd tdmspqaqaq
      241 agdyfkglng lashakddgp kvkkvtfeef krg
//
LOCUS       WP_181770526             329 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181770526
VERSION     WP_181770526.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 329)
  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 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   3  (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   4  (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 18524816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=35982
     Region          9..255
                     /region_name="YrhO"
                     /note="Sugar-specific transcriptional regulator TrmB
                     [Transcription]; COG1378"
                     /db_xref="CDD:440988"
     Region          <271..329
                     /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 mtpsdglgaq lirlglgeva agiyrrmleg apvtadellr rhgdaetvhl alkeladagl
       61 avssgkdgte ylpanpseal salstrrqae lhdariavqt ayrtfrrahs gmphaqdlle
      121 vvtgeaivpr lqhlatmvrh qvrrldsppy ftgghrnlle edqlrrgigy rcvysgaslg
      181 dpgyftgnil pclrageqar llpelpvklt lfddraatia ltireadrnq sivivrpcsl
      241 fsaleglfet swaaalpldq hgrtsgqpir pierellill aagrkddeia aelgvsrrtl
      301 fryletlmdr agvssrfqlg vfaahnewl
//
LOCUS       WP_181770586             204 aa            linear   BCT 28-DEC-2024
DEFINITION  anthranilate synthase component II [Amycolatopsis pittospori].
ACCESSION   WP_181770586
VERSION     WP_181770586.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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 204)
  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..204
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..204
                     /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=21888
     Region          3..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 mkvlvvdafd sfvhiidqyl rqlgadtvvv rsgtrtpeel aatrpdavvl gpgpghpads
       61 ghvalarrfa gevpllgvcl ghqaialafg gavrladnlm hgrtsviehd grgvyaglpe
      121 rhevtryhsi vvaeplpadl vrtarslddg yvmgmrhral piegvqfhpe svatvdgtrm
      181 manflagvrt radrrprpar srat
//
LOCUS       WP_181770721             458 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181770721
VERSION     WP_181770721.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 458)
  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 458)
  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..458
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..458
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48684
     Region          10..351
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpnsvrttfd rahwqarldg lraghhvpga alavlidgei helasgilhr gtgveatsds
       61 vfqlgsvakv ytaslvmgla eegrldldap vievlpefat vdpeatktit arqllshtsg
      121 ltcdftddtg rgddclakyv eaargvgmdc ppgtaasyss vgynvlgriv evltgltwdd
      181 alrerliapl gltetmtlpe ealrfrvamg hlgpdpepta vwdllprnag pygrvlatag
      241 dvvrfarmlv dgvaadgtrv laeetvaamr rrevevpdkw tlgsdgwglg lsifdwdgvl
      301 gfghngssig qrsylrvvpe agvafallsn hgttdrlyts larellgela gvvlpadfap
      361 ptsppsvdva sfvgtyrreg viitvtdtdg klhfvyefad alegiappie adlvpvsegv
      421 fagmnpmfgd dwmpvlftel pdgtpccfts mrvapkia
//
LOCUS       WP_181770761             133 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181770761
VERSION     WP_181770761.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..133
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14792
     Region          21..120
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msqgntdvta qarvvdpekl evctvlevin risgkwaigi lleatrgpvr ftelersveg
       61 isrrmltltl rnlerdglli rtvyptvppk veyevtamak elyaslsgll hwaerhrdsi
      121 aasrvvydek vsa
//
LOCUS       WP_181770777              99 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181770777
VERSION     WP_181770777.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 99)
  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..99
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..99
                     /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=11019
     Region          4..>64
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mttveltrfk vpadradell raraamladf radregflda qlirvddetw ldvvwwrsse
       61 dfaasrekga nlpgikaffa piaelvsaee gttadyraq
//
LOCUS       WP_181770910             587 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Amycolatopsis pittospori].
ACCESSION   WP_181770910
VERSION     WP_181770910.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 587)
  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 587)
  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..587
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..587
                     /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=63573
     Region          3..587
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mpravstprt lceafqtvaa ldpdavalrd lggdvaitwr qyrdrvrsia aglaglgigr
       61 gdtvalmltn rpefhlcdta tlhlgatpfs vyntnpaqml ayqfdnadnr vvicerrflp
      121 vireavqqgg kvehivcvdg ealsleqlea apapefdfea awravephdl ltlvytsgtt
      181 gppkgvelth anflenaril vdfgvrdqpn rmisylpdah aanrwfshya qllyggqitt
      241 vadpkgvlda ltqvrptyfl gvprvwvkir aglqaalaqq dpvkrrlaaw aigtgrarar
      301 arseareqhp larlryavad rlvlaqvrqr lgldqivaav sgaapiprev heyilglgip
      361 lsegwgmsec taavtvnplh rikigtvglp vpgaritlad dgevlargpm vtrgyrkdpa
      421 rtaeaidadg wlhtgdvgef dsdgylrivd rkkeliinaa gknmsptnie navlancplv
      481 stvavigeqr pyntmlicld pdaapsfadq helpadlatl aenpqlvaav qagvdaanvt
      541 lsrveqikkf tvlpevwqpg salltptgkl krapiathya qtieamy
//
LOCUS       WP_181770993             413 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis pittospori].
ACCESSION   WP_181770993
VERSION     WP_181770993.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..413
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..413
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45414
     Region          156..398
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mhyrsvlreg saaivaelav everqlpali ettveqirse mpvyrdaqfv slaelrtsvr
       61 nnleyvmrtl rgteepdlaq aratgraral qgaplpellr ayrigltevw nrfveltalg
      121 ehqdlrglva atsaiwalvd dyaealttty rdttaevmla hqsrrsalve alfaggaate
      181 gtlwdiarvl elsldgtyvv vaaetprvgh eplpqienrl rerhhasawr ltpdlqvgvv
      241 smrdpeasqv iiellrensi grvgvspvft glgntaralh larvalssmm pgssgmvqfn
      301 esplaglvas apeasvqlah hvlrpildlp gddrnvlllt lrawfecqgs tkltsermfc
      361 hpntirhrlk riteelgrsl tdpadiaelg aalralhmfp dtshlpsprd plr
//
LOCUS       WP_181770986             325 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis pittospori].
ACCESSION   WP_181770986
VERSION     WP_181770986.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 325)
  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 325)
  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 325)
  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 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   5  (residues 1 to 325)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..325
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..325
                     /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=35664
     Region          240..>306
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlriyfsted llrirllaep hpmwevllsl hlvqtgqgqp vfggwrrklr prlpsstgll
       61 talarpsgys pdfltppgdi pdletgidll lgttrtrlkt diavlarhrv lptwvaeiad
      121 geveslrrla ealrayhrea iepfwpgirh hveldrrsra dvvaiagfea vltglhpair
      181 wrppvlevdy pveqdlyldg rglvlapsff cwggpittls ddsatpmlvy pvercpgwaa
      241 dpdeeavrvr sltallgrtr atvlrtiadl pqvnttdlan algislagas qhatvlrnag
      301 lvqtartnga avhrisqrgs allrp
//
LOCUS       WP_181770976             115 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis pittospori].
ACCESSION   WP_181770976
VERSION     WP_181770976.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=12785
     Region          3..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mhafdvlgdp vrrrilella ngelssgdvt tvvrgefgis qpavsqhlrv lrengfttvr
       61 aegarrlysv dpgplkeidg wleqyrrfwt gpldalatei argrrerrka aeetg
//
LOCUS       WP_181771007            1104 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF885 domain-containing protein [Amycolatopsis pittospori].
ACCESSION   WP_181771007
VERSION     WP_181771007.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..1104
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..1104
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=120821
     Region          6..549
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
     Region          556..1102
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 msevstlade fvealfdaep vmpalqgfrp estgltdlse aagdafrakl aglaeraeai
       61 daaglgaeek ttrdvliama rarialldsr fveftisdlf ispaaevltv lpmlsvgagt
      121 qaeahlgria avpeylrqaa qrhrdgvarg lvpvaylvda avahldryla dpsadpllrq
      181 papdedfetr raellrdvvr paiteyrevl akeiapngrp edkpgvcwlp dgeriyalla
      241 emhtttdrtp relhqtgldv ianlaaeyre ygsnvfgttd laeifsklrt dpalrwssad
      301 emldsaraai traeaeapnw fgrippqpwt vepvpaesap gapaayymwp aidgsrpgiy
      361 fanthkaeer frhaaeataf heaipghhfq lslaqgltel pvlrrigdft ayaegwglyt
      421 erlademely sddvaklgml tmdsmragrl vvdtglhalg wsrrqaidfl tentpmalve
      481 iesevdryia fpgqalsymv grleiqrire eaeltlgsrf dikafhdvvl gggslplsvl
      541 dgvvrdwvag hgdtpnslae elmalkfeey plwrsllglp gdhgalpdps aaaaaaqras
      601 aaaiadraea lgveglstve avtrevviqq akamidvads rsadisvsdg laspalsvln
      661 elamlaltde ervrgylerl egigsyldal ivrqraaaae glvppgflve sgvayveryl
      721 gdeagdplal tasvsvegye terdrllaev vrpayrryrd flatelrplg kpeeepglca
      781 lpggqekyaa lirahtster taqdlhdtgl dmiakladqy relgekifdt gdlgeiferl
      841 rtdpalrwrd gdelldaard aitraeavap qwfstipeek cqvepvppae apggtlayyl
      901 eaaldgsrpg tyyantyead qrpkhtseai afheavpghh fqiciahhlk glpmlrshad
      961 vnayvegwgl yserlademg lysseltrfg mltqdsmrag rlvvdtgmha fgwsrqravd
     1021 ylventpmar veieaeidry aaypgqalsy mvgrleieri raeaeaalgd rfdikgfhev
     1081 vlgngilplr vldnvvkewv sahk
//
LOCUS       WP_181771095             199 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181771095
VERSION     WP_181771095.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 199)
  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..199
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..199
                     /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=21562
     Region          11..195
                     /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 mtpgtrllvn aqgeryrfdp gslslelllt ggpgpyerye iahtpadlae wftgsrlalt
       61 apltdvqirp aelaalkelr galyrvapal ahgeaqssdd vvllndataa tprpilapet
      121 rrlawappvt gkqllgavar daigliager sgrvrecsas dcyllffdts rsgnrrwcsm
      181 ercgnrakir ayrartetv
//
LOCUS       WP_181771144             366 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amycolatopsis pittospori].
ACCESSION   WP_181771144
VERSION     WP_181771144.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..366
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..366
                     /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=38453
     Region          1..338
                     /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 mkaviigggi sgtvtamalk ragieasvhe ahptggedag afltimhngm dalraigadg
       61 pvvensfaad glelvtpdgr tverrsfdld glagprtltr aslylalqee aisrgitfer
      121 gkrlvsatsg talfedgtsa egdiligadg lhsivrnlid pscppprstg ldvvygyttd
      181 tsvpqapsly rmvqslhaff gytstpdgtt ywfarlptae gvrsglsaee wrstafaafd
      241 geplpaaeii hstgdevfgg hsydvpstpv wsdstmvlvg daahaaspaa gqgasmaled
      301 svvlaqclrd lpdaptafaa yerlrrarve klvassaavs sgttsdrdrn wlyrhhiewd
      361 akisas
//
LOCUS       WP_181771166             299 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Amycolatopsis pittospori].
ACCESSION   WP_181771166
VERSION     WP_181771166.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 299)
  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..299
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..299
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32823
     Region          23..299
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtemareaaa gfdetggvgg qpvldrlval ldlekieeni frgvspahsp vrvfggqvag
       61 qalvaagrtv peerkvhslh ayfirggdps vpivyevdri rdgrsfttrr vvgiqhgkai
      121 fslsasfqkd eggiehsegm pdvpdpeslp tlqeraegyf ighhdrprpi dlryvndppw
      181 vtrksgelpa rnqvwmradg klpdqqllhv cvltyasdmt lldsvlarhg vywdldkvig
      241 asldhalwfh rpfradewfl ydsasptasg arglatgrff aadgthiatv vqegllrvv
//
LOCUS       WP_181771145             598 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Amycolatopsis pittospori].
ACCESSION   WP_181771145
VERSION     WP_181771145.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=63734
     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 mreysapaan pvtddenlad vvwanaerfs dvvsfrrqvd gtwldvtakd faaqvlavak
       61 gmaqagiapg driglmsktr yewtlidfai waagavtvpi ydtssaeqvh wilsdseaka
      121 vfvetdehla tldsvkgrld rlehtwqiea akpavddlta qgaelsdddl herrrsvkag
      181 dlativytsg ttgrpkgvel thrnllaeir adiaafpqlm eqgnsllvfl plahvlarai
      241 avtalsarvt lghtsdvknl vadlgtfrpt fvvavprvfe kvynsakqka hgdgkgkifd
      301 aaeatavays qaqdtggagl glkvkhalfd klvfsklraa lggrcvaavs ggaplgvrla
      361 hffrgigvpv fegygltets aaacvgtqtg frvgtvgrpv agtsvriadd geillkgdvv
      421 fggyfnnpea taealedgwf htgdlgelds dgflkitgrk keiivtaggk nvapsgledt
      481 ikasplisqa mvvgdqrpfi galitideey fpswksqhnk padatvsdla adaelraevq
      541 qavdqansav sqaeaikkft ilskdfteag geitpslklk rnivnknyat diealykk
//
LOCUS       WP_181771200             380 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181771200
VERSION     WP_181771200.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 380)
  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..380
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..380
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39502
     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 mkagplsglk vvelaglapa pfactiladl gaevvrvdra tpgndvigfp ndplargrrs
       61 igintktpeg velvlkladd advliegfrp gvaermgigp eqvharnprl vygrmtgygq
      121 dgplapvagh dinyigisga lepighagqr pvvplnlvgd fgggglllam gvlaalferq
      181 ssgkgqvvda smvdgaallt tslhglldsg lwpggrgenm ldggapfydt yetadgkyva
      241 igaiemrfwg dlvkvlgldp eetpvhvdkn ewpklrkiva eavakhtrde lvakaegtda
      301 cltpvlapre apshphnvar gtfvdiggvv qpapaprfdr tpaetpeppr pkgadtadvl
      361 aelgvdadgi erlkaggtiv
//
LOCUS       WP_181771259             284 aa            linear   BCT 28-DEC-2024
DEFINITION  YfdQ family protein [Amycolatopsis pittospori].
ACCESSION   WP_181771259
VERSION     WP_181771259.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 10009413
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..284
                     /product="YfdQ family protein"
                     /calculated_mol_wt=31535
     Region          1..278
                     /region_name="yfdQ"
                     /note="Uncharacterized conserved protein YfdQ, DUF2303
                     family [Function unknown]; COG5532"
                     /db_xref="CDD:444283"
ORIGIN      
        1 mpntndqtaa vvadiqrrad eatppqpfel apeksvvvrt lrndervdtt dleslldqpr
       61 rprgtalltd psdfaayvar lattsttvwa dqdnlkvtat fndhangfsa gwrdhqavlk
      121 lkhdedwkaw lrrdgtlmdq edfaehledr ahtivnpdta tmleialtfq trrnasfsrg
      181 arlnsgdvql awseettaka gasgrlevpa eftiavapff glpatevtar lrwriregql
      241 gigyrldrpd lvhrkafadv rqmladtlda pvllgsaphi epvy
//
LOCUS       WP_181770940             145 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Amycolatopsis pittospori].
ACCESSION   WP_181770940
VERSION     WP_181770940.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..145
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=16182
     Region          26..139
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 msgghanlda elerlcrrva gaaevtldlr nrpdlrhvrs vvaehigfgr reneplgpll
       61 lvvdelvsna yrhtigpgel rierrlhglm vevsdddpdl dplcsdqahy glrlvgqlsl
      121 dwgfrtertg kavwalvpvp lyyer
//
LOCUS       WP_181771391             213 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Amycolatopsis pittospori].
ACCESSION   WP_181771391
VERSION     WP_181771391.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=23775
     Region          6..196
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mrrltlvdsl fflahdeftg kpalrrtglg igmagsalcd lllaeritve rkrirplsrr
       61 righpvldra fseilgerew htvrewvdhl rqdigetvan nlldagvinr etdrglmrki
      121 hrypprdllm staarskara avlgterpdp hsvclallaw tiglddlcep eldraalrdw
      181 aeathrdlpr sladlisgid avgaavvytg drh
//
LOCUS       WP_181771498             470 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis pittospori].
ACCESSION   WP_181771498
VERSION     WP_181771498.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=50480
     Region          <100..465
                     /region_name="MtrAB_MtrB"
                     /note="MtrAB system histidine kinase MtrB; NF040691"
                     /db_xref="CDD:468655"
ORIGIN      
        1 mrvlsglrpr lilafaamtl igaaaaagas yvsarnailg avqdaamnql kdrvaaygrp
       61 lstpptqeql ndfagslrln avavyrsmrs vngpdlttfs telretvstd nriqfqrldr
      121 davpellvgm pvlsrqpdgs mgpsglqvys ltslaqqqqa ieelakyawq maalalplaa
      181 alallaarqv lrpvralnta aaqlgegrld vrlpakgsde laelvttfnn taaelertvg
      241 elrsmeadar rfvadvshel rtplaamnav tdvldedaea lppdtavaar lvsgetrrlt
      301 rlvqdlveis rfdagraelv ldewdlatai rdsldargwr dgedlvtdlp egviarvdrr
      361 rldlivanlv gnafrhgsgp vevrlrthdd gvtlevddhg pgidpevlph vfdrftkadt
      421 srarsegsgl glaialenar lhggditaan tghgarfvlr ipnraegvtr
//
LOCUS       WP_181771502             407 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Amycolatopsis pittospori].
ACCESSION   WP_181771502
VERSION     WP_181771502.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 407)
  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..407
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..407
                     /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=44390
     Region          23..406
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(60,67,95..96,103,107,114,240..241,244,248..249,252,
                     285,290..291,294..295,297,320,347..349,352..353,355..357,
                     361)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(67,89,91,94,96..97,179..180,190,239..240,243..244,
                     248,291,294..296,396)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mpeaaydaea gpvmfgpefd rnpspayewl ranapafrlp lpgdtwtwll trhadvvsam
       61 adprlskcps vasehwrkan lglpadhrpt lighmnnveg deharlrkac agafgprrlh
      121 hmrdrthrla nelldpiler gegdlvedfa yplgirsice ligipdtlld evrppalvva
      181 agdvtdmasm lkatdeldel ladvvarkrt epgadlisdl ltqeadgklt dqevaatafl
      241 sliaghetti sliastaltl ithpeeaara radgahltlv ieevlrrdtp lqntswrfvt
      301 epmelagqrm eagdpillsl laanrdpevh pdplafrpge rpvrhvafgv gphicigaal
      361 armqasaale tlfdrapsmt ltvpedrlvw wpsaitrglh nlpvkls
//
LOCUS       WP_181771514             174 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181771514
VERSION     WP_181771514.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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   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 174)
  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..174
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..174
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19399
     Region          2..104
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkrtsfaqwp csiartmdll gdwwtplvlr eafygirrfd efqqelgiar ntladrlrrl
       61 vgegllekra yqadpvrydy vltekgadfy gvlaamtrwg drwlsgeagp pvtlhhdacg
      121 hdthaevvca hcagpltgen trarlgpgyp pklasrpdvv rrfaaqespe gltt
//
LOCUS       WP_181771526             397 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Amycolatopsis pittospori].
ACCESSION   WP_181771526
VERSION     WP_181771526.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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 397)
  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..397
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..397
                     /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=43182
     Region          18..391
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(55,62,83..84,91,95,102,227..228,231,238,271,
                     276..277,280..281,283,306,335..337,340..341,343..345,349)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(62,77,79,82,84..85,167..168,175,226..227,230..231,
                     277,280..282,381)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 msdvpeillt dpgvlndpft aygparersp vaklvapgfg pmwavlrheq arkmlsdprf
       61 alsqasyqrm eipehcrpym rtmqevegpe hlrlrrlvap aftprrasal rpgierivdg
      121 lldgfagrdr idlvtdfarp lpidticalv gipegdrprw reygtaiaag dgaglmkavp
      181 givedslaai ahrklepged vvsellriqa edgdrlsete lvalvwqlvl ggqvpgnlia
      241 nsvealfahp aqlaelredp almpgaveel mrwcspqllt vprlttedvr igdvlipege
      301 pvtvaiaaan rdprafpepe vfdirraagp awhlafahgp hfclgaalar vqtevaltal
      361 lrrfpdlapa dgpsripdpg twrlhtlpvt lhapvan
//
LOCUS       WP_181770658             305 aa            linear   BCT 28-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181770658
VERSION     WP_181770658.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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 305)
  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 305)
  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..305
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..305
                     /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=34294
     Region          17..289
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 mtstdmprta gaaaagrqet aqrlldssam lsydpatevd wetpldkdfh gaspewstly
       61 gtsywaemtp eqqkeltrqe aasvastgiw femilqqmvl rdfyakdptd pafqwaltei
      121 adecrhsimf argaeklgap pyrprrlave lgrvfkatas geaayaailv aeevldvmqr
      181 dwmrdervvp fvrtinnihv veesrhmkfa reetreqlkg agflrrrina lvvaiasyfi
      241 vssmvnrdvy enagldsara lreaktnehh kammrsscag lmeflnscgl ltrpalvfyk
      301 ranli
//
LOCUS       WP_181771585             413 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis pittospori].
ACCESSION   WP_181771585
VERSION     WP_181771585.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..413
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..413
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44598
     Region          143..396
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mshndpgfli ggrplaerlt dvlpsltkav lgeivtripe ygllpaeels gdithvieqn
       61 lrsfidtlrt gampareeid flresaarra eegipidivl tayhigiqvv wasltpdvrp
      121 eevtdvlavh qltlrylevv tpavgagyld errtmfdder sarhtvlsal ldgesadvaa
      181 gqaglrlppc yvvlaasvga hpdeeangvd plvagrrklr rlrvelerqi rgtvltsltp
      241 eggiallphe dtagelsthd warlerilad vartagaevi agaaaaepaq lpaaaklaqd
      301 vlavatasgr ppglyrlddv lleyqlsrpg paldrlatrl epldgneell qtletflrrg
      361 grrqtaaalh vhpntvdyrl rriadltgld ptrlehiall naalaartvt grk
//
LOCUS       WP_181771638             210 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181771638
VERSION     WP_181771638.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 210)
  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 210)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 210)
  AUTHORS   Rosinski,J.A. 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 210)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..210
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..210
                     /product="helix-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=22953
     Region          46..210
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <151..210
                     /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 mfepnrtpvv vratdpilhn gvcmtlrsrd dvrlvdgeta dptmvallvt drldeamtrm
       61 lsalhhqgft rivliagevd dneilgaieh gvcavarrse agadvlvrli kaaaagegal
      121 ppdllgrllh rvsrlqrqvl qprglhlggm snretevlkl vasgfstqei adqlcysqrt
      181 vksilhdvtn rfqlrnrsha vayalregli
//
LOCUS       WP_181771702             130 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181771702
VERSION     WP_181771702.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..130
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14428
     Region          <36..85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msphqtfaek lsalidsmra degaphsyre lsaaidragg pamspaylqq latgkrinpk
       61 ihyvealarl fgvpityffd dqeaqplgea klmamraqel spqgrrqvmd llelveryek
      121 aerdlpgesr
//
LOCUS       WP_181771822             871 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Amycolatopsis pittospori].
ACCESSION   WP_181771822
VERSION     WP_181771822.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 871)
  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 871)
  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 871)
  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 871)
  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..871
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..871
                     /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=94252
     Region          183..856
                     /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 mpdtngrpvs aaqatpgkgg avteartder rfrvytfavl tmgiaaaaav slwldfeasd
       61 dllwigpila lafllaeqlg invdvrsgis wtisfteipl vigffvapfe vvlaahlaag
      121 igtllarkva grvlynagaf lleitgafav aglvkqasga qdmtwiaala gtltaplvst
      181 llalaavrvl rrrmrvstai rltgrilvvg fvnasvglsg ylvisgtpka wplvlavflg
      241 ltalywaysd llreqrdmea lsdvslmvar sgqqaaarpa gradelvggv dvrewatiae
      301 rikdqlaagr vvlrlrlepk dtmrmvvagd elppvdpaad dpllrlpgah vrhfritean
      361 pdvrsalldr gaqealvvpl rsanqllgvv eahdrlsrwr gfgkydvqll gtmashlats
      421 ldnrrllatl rhdayhdplt gllnrpgfrq vakeplreqv navvlrvdld vfstvsdalg
      481 yvwadrmvia agrrirdalg pdvplarleg asfaallvgc aperaqaaae llraelvapy
      541 pvdrlsvean amigyatssa ddddqvdvdg llqradvavr atkggeevrg ymasmgqifm
      601 rrfqmvtqfr qsleegqlsv hyqpkitlpn rqiqgvealv rwvhpefgrl gpdefvpaie
      661 aagligvlts fvleeslkrv rkwldeglri saavnlsvrn ladedfptkv areldrfgip
      721 pelltfelte sgvmsdpqka lpilrelhsl givlavddfg tgysslaylr qlpvdqvkid
      781 ksfvlgmgtd lgdlavvrsi velghslglt vvaegveedv ardqleamgc dvaqgylisr
      841 plpedrleaw lqartarspg rhsetvltll t
//
LOCUS       WP_181771722             446 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181771722
VERSION     WP_181771722.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=48026
     Region          30..435
                     /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(142,144,270,272,306..308,359)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrktvallav llltltgcag agalgtgdrt lvvgivanpq mkdaielsge fekanpgvtl
       61 kfvslpenqa rakitastat eggefdvvmi snyeapqwaa ngwlenleph iaanpsydsa
      121 dfipsikesl shngsmyavp fygessflay rkdlfeqagi tmpakptwsq iaefaakldd
      181 kskglagicl rgkpgwgesl apfttvantf gaqwfdkdwn akltspefka aaefyvnlvr
      241 nhgevgassa gfsecgtryt qgqaamwyda tvmagtnedp saskvvgksg yapapvektq
      301 asgwlytwal aipkvakdkd aafkfmawmt dkayvqrvaq qfgdwnrvpp gvrkstydip
      361 qyreaakaya qptldgiada nqqkamanpv pypgiqfvgi pefqdlgtrv sqqlsaaiag
      421 qitvdealkq sqeyaqtvgk syqevq
//
LOCUS       WP_181771951             565 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Amycolatopsis pittospori].
ACCESSION   WP_181771951
VERSION     WP_181771951.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..565
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..565
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59503
     Region          30..483
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtgtlpttgs petappnrty aplaanenre dyslrfaphs frrwspfvva ttalggiayl
       61 adfaigasiv lsygftsgvl ailaaalvif vtgvpiahac akygvdmdll trgagfgyfg
      121 stltslvyas ftviffsleg simaqafela mgiplpvgyl lstlivlpfa lygmgavakm
      181 qawtqplwia glvlpfvvia vrepgkfaef asfggtegag sgfsaigfgf gmgvalslig
      241 qigeqadylr fmpqktdsnk rawwgavlaa gpgwvvlgaa kqiggallaf lalgvvgkth
      301 alepiapyle avepalgpaa ltfaalfvvv sqikinttna ysgslsfanf fsrvlhrhpg
      361 rvwyvlvncg ialalmefga fgflnkilgf ysnvaiawig avcadlvivk plglspryie
      421 fkraylpkin pvgfgsmvva stisiiayfg afgqflaafs pllalviamv lvpalavatk
      481 grtylarpns virqklspee lrathictvc qdefelpdia dcakqsgaic slcctldatc
      541 hdlcqtagpv dlpmptlptl ptskp
//
LOCUS       WP_181771903             396 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181771903
VERSION     WP_181771903.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=42253
     Region          159..352
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mpkavalvwa llilntlgst gattvipipr sviqlvtmgs lvlafcvalv lnarlrirps
       61 aylllltvlv vlslmaslnl evgygalfrc frfglfvatl wlltqwwdgg irlvrhhirt
      121 ysvvlvtvvv glaaspgial aeeyggrltg tiwpltppqv gqyaavvigl tvllwlggel
      181 drlnaliviv psfailllth trtamlglia gvliallslw mssararkvf avvglagavv
      241 avalgsllqa wflrgqseen fssltgrakv wdallsdprt lgeylfgvgl tnksyiglpi
      301 dnswlavyhe qgyvgiaiva afmlvlivva alrppslsra caiflityci sasyteaglg
      361 daspyllhla laasllvrsp setvvekkfi pakepa
//
LOCUS       WP_181771975             448 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181771975
VERSION     WP_181771975.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 448)
  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 448)
  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..448
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..448
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47788
     Region          8..315
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlattemall rrlaheqssc rapslvaavv rdgeiawsga rgrvngespg ddtqyrlgsi
       61 tktlvatavm rlrdegkldl ndpleqhlpg tafgaatiaq llshtsglta espgswwert
      121 vggdwdalve slkdgatrhr pgsrfhysnv gygvlgelvs ryrgqswldv vraeiltplg
      181 mnrtsphpeg ahadgfavhp fadilmpeps pdagamapag qlwstvtdla rwtaflgght
      241 gdvlsaetva emremvtvdd gdtwttgfgl gvmlvrtqgr rlaghtgsmp gflacslida
      301 narigalvlt nstagvgitq lcldlitlte ehepslpaew qpstvdpkll eltglwhwgp
      361 tpyhlrvlpd glislaptdg pgrasrftpl gddtwvglda yyagetlrig rdaagnpshl
      421 dlatfifsrt pydpaapipg gvdpdgwr
//
LOCUS       WP_181771989             271 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181771989
VERSION     WP_181771989.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 271)
  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 271)
  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 271)
  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 271)
  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 271)
  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..271
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..271
                     /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=28989
     Region          26..267
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 maelitiddr ddprlddfrd lstadrrpdr pggrglviae gtvvverllr srypvrallg
       61 verrfrelga eldrvdapgy vtsaetmaev vgfhlnrgvl avadrpvppp tvegiidgar
      121 vlavlegvgd henlgslfrn aaalgvdgil lgagcsdply rrsvrvsmgh vlrvpfatfg
      181 swpddlnllr ergfriaalt pradsvslrq lrdqapekva lmlgaegagl teeaiaaadl
      241 avripmpdgv dslnvataga iafyetrppl s
//
LOCUS       WP_181771994             252 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181771994
VERSION     WP_181771994.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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 252)
  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 252)
  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..252
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..252
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27975
     Region          1..245
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mdaaayldrl gldrpatadv aalrtlqerh lavvpfenls ihlgepivld pealfdkivr
       61 rrrggfcyel nglfaallre lgfdaslrsa kvfrpdgtlg ppfdhaairv eldepwladv
      121 gfgrfsrfpl rlaateaqad pggeflflda pygdidvlld gkpqyrieqr arnldeftpt
      181 awwqatspds hftqgpttsl ptehgratla gdklivtthg vreetrlssd qevldvyrke
      241 fgidlvrvpv rp
//
LOCUS       WP_181772049             289 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181772049
VERSION     WP_181772049.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..289
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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]"
                     /calculated_mol_wt=31777
     Region          16..167
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtaltpqeay qatnkhyelp aelfeiyldr rlkysaglys dagtdldqaq tdklhfvarr
       61 lglrggerll digcgwgsli lfmakeygch atgvtpsrpq aeyirqraee agvaglvtlr
      121 sgsfseleva gkfdavtmlg sivhmpdrtq vlrkvhgllr rngslylses cfrddatyqe
      181 fsrrpgtvhv tesifgfadm vpvsalvaai esagfsltgl tdltahyhrt ieqweeraqa
      241 aldrveevap gmgepliryl qtanagwgyt tkhyaltalk srmgpaeap
//
LOCUS       WP_181772060             317 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181772060
VERSION     WP_181772060.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=34469
     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 mradrlvatl llmqargrvt aselaeelei svatarrdle alsaagvpvy pqpgrgggws
       61 lvggartdls glsateaqal fllagpaasi spevksalrk lvralpdtfr adaqaaadav
      121 vidpsrwger ekerpelltv lqagivrrrk vrfgyakkga epvervvdpw glvdkddiwy
      181 liagtekgqr tfrvdrmsda evsdlpaarp ddfelsqawe qvvdqverrr sgldatvlia
      241 erhlpilqdh fgrqsvveet lddgrvrvtv sapvawmiaq qlagwgsmie vlgppsvqre
      301 larigaelve ryatpvg
//
LOCUS       WP_181772072             223 aa            linear   BCT 28-DEC-2024
DEFINITION  response regulator transcription factor [Amycolatopsis pittospori].
ACCESSION   WP_181772072
VERSION     WP_181772072.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 223)
  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 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   3  (residues 1 to 223)
  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 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 13308614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..223
                     /product="response regulator transcription factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [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=24084
     Region          18..194
                     /region_name="PRK15369"
                     /note="two component system response regulator"
                     /db_xref="CDD:185267"
     Region          <150..211
                     /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 mlvkvevgvt tmrivercid lvlmggndlf hnglralldr dpsfrlvadv edavqvdvii
       61 vdldsidvde slriidrwhs cgivligger ehgrvgellt rgasaylrrt vlfdqlaati
      121 ksasagsddi vitisredlp lfasaasvrl saretavlel vcralkndei arqlfisqgt
      181 vkrhlaniyt klgavsrida lnkavaagll strqagpdsv rat
//
LOCUS       WP_181772088             155 aa            linear   BCT 28-DEC-2024
DEFINITION  peroxiredoxin family protein [Amycolatopsis pittospori].
ACCESSION   WP_181772088
VERSION     WP_181772088.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 155)
  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 155)
  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 155)
  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 155)
  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..155
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..155
                     /product="peroxiredoxin family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16624
     Region          10..153
                     /region_name="Bcp"
                     /note="Peroxiredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG1225"
                     /db_xref="CDD:440838"
ORIGIN      
        1 mleigstvad laledtagra vrlsdfrgtd nvllyfmrst tcpvcnghvk dlvgragewe
       61 aagvrvlvav pegraeaevw rakralpfqv vtgrsgtphe avglvkkvfg alqqsgslli
      121 dregvvrhah aatlpingyd rrgieravae lvrvr
//
LOCUS       WP_181772115             319 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Amycolatopsis pittospori].
ACCESSION   WP_181772115
VERSION     WP_181772115.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..319
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..319
                     /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=33647
     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 mrpfeliape tveaavsspg tflaggttlv dlmklnvltp rqvldinsvp lrgidtsdgl
       61 rfgalermgd iaghpgvypa isralllsas qqirnmasig gnlmqrtrcs yfrdvampcn
      121 rrdpgsgcpa isganrmhav lgtsdscaat hasdvavalv aldaklrlvs etgtrtvelg
      181 sfyrlpgdtp evendlrpge liaevivpkl dwasnstyvk vrdrqsyefa lcsaavalhv
      241 ederivdarv aaggvatvpw rlpaveealr gapatvasfe aaaalatega rplsgngfkt
      301 sllprtlvra lleltegsr
//
LOCUS       WP_181772280             192 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis pittospori].
ACCESSION   WP_181772280
VERSION     WP_181772280.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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 192)
  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 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   5  (residues 1 to 192)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..192
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..192
                     /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=20994
     Region          6..81
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maglpprkri edvelmrala hplrsalvdh lmavgprtas ecatavgsta sncswhlrql
       61 aqhglverve gedgrerpwr acqvgiefgd dpelhgaqla vvgttlarer elveryldaa
      121 dgldkewqda sgintyslrv taaeleelir gmdalvrpyv stiredvpeg arpvhlglra
      181 flridaegkp se
//
LOCUS       WP_181772284             226 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Amycolatopsis pittospori].
ACCESSION   WP_181772284
VERSION     WP_181772284.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..226
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23886
     Region          10..>177
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msapstldgl aavlwdmdgt lvdseklwdv alyeavetlg gtlteeqrls lvgsnmddta
       61 afllevcekp vtpesvaemg ewirkrtanl fdgvipwrpg aqellellrs egvpmalvts
      121 tersltelal ntigreyfaa tvcgdevdgl nkpdakpyql atellgvqas rcvaiedspp
      181 gaasaaaagc tvlvipndve vqpgerrvfr sslvgldvpg ltallg
//
LOCUS       WP_181772331             192 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis pittospori].
ACCESSION   WP_181772331
VERSION     WP_181772331.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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 192)
  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 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   5  (residues 1 to 192)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..192
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..192
                     /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=21697
     Region          14..85
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mgkserylar vdgrvlrals hplrvkilel lredgpatas glakrvgess gttswhlrql
       61 aecgligeda ergsrrdrww kavhegdqmr ardfiddpdl agpfnayaht mierryaaea
      121 qfvaevrdwa dewidkvsfh dsplsltpde aaalgdeile viaryrrper egdtpvrvhw
      181 aafprksrpe tp
//
LOCUS       WP_181772349             146 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181772349
VERSION     WP_181772349.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..146
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16586
     Region          6..103
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mtegprdcsi anameviger wsllalrevf fgarrfdqiv rntgasrdil tarlrklvet
       61 gilekrlyee hppryeyvlt eaghalnhvl lnlmawgdky vtegpaptvw rhscgeelap
      121 etvcahchep vrekdmtlvr strrtt
//
LOCUS       WP_181772309             348 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181772309
VERSION     WP_181772309.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 348)
  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 348)
  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..348
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..348
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=35916
     Region          49..222
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          207..>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 mrrallvvlg avvplaltgv ahaapecpdp awtetptgtd aqlrglsavd srtawvsgsk
       61 gtilrttdrg rtwksvappd tadldfrdie afdadhaval sigpgeasri yrtddggksw
      121 rlsfrnsdpa afydcvaffd rhrglamsdp vdgkfrlqst sdggrswkpv padgmvpale
      181 gefgfaasgq clttsgprda wiatgggara rvlhsgdggk tweaadtplp sgasagvfsv
      241 tfrdprhgva iggdyaapna pgpavalsad kgrtwrtpse apvgyrsgla wlgntiiavg
      301 pggsdlspdg grhweafdtg sldsvdcarg acwasgakgr aarlggva
//
LOCUS       WP_181772350            1000 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181772350
VERSION     WP_181772350.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 1000)
  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 1000)
  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 1000)
  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 1000)
  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..1000
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..1000
                     /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=106734
     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          105..990
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          817..845
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(818,821..822,825..826,828,856,859,862,865..866,
                     868..869,898,901..902,905..906,909)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          854..886
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          897..924
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdfrvlgpir lytggqavti geprrqavla vllleagrtv gvdvlvdrvw gesppkqvrr
       61 slqahitrir raleeadpgg arvsrdsggy rldvppgqvd lfrfrdtlre spadaaalha
      121 alglwqgepl aglrgdwaer tretltqerv aavvawadaa iqagdapatl trlteladdh
      181 plqetvaatl mralyavgrg adalaryeri rrllrddlga dpgrelagvh eavlrhelps
      241 gtapvapvpa qlpalvsaft gradeldald rlvadatgep vvvcltgtag agktatavhw
      301 ghrlrdrfpd gqlyldlrgy dpgepmapve algafltalv ppgteiplgl teraarfrte
      361 laarrmlvml dnaatveqvr pllpgtgdcv vvvtsrdslg glvalhgahr vtlgqlpdpd
      421 avalmrrlag prvdaepeaa aalaercvrl pltlrlaael avsrpatrla rlvdelraaq
      481 htldllsgga dqraavravf swslrelded tvrafavlgl hpaprfdaha laalagrple
      541 warirldtla ranliepsga drygmhdllk ayaaesgged dacaalgrvh ryyhatiaaa
      601 mdrlypgeah rrpavtgtas papsftdadg artwldeelp avqalsaqav aggfpehavt
      661 lsallfryld ghheaialsi hgyaraaara gddrsaeada lialgglhmr agrpepaaad
      721 lwaafaayge ignplgqarv lgtvgmleec agryrtssgy yaqaltlfdr lgdvigrahi
      781 ltrlgtiear lgvpeaedrl rqamglhgqa ghrfgeawvk vglgelaaee gksadahrlh
      841 eeaadlfarl ghreseawai dalgraeala grpveaatrh rralhlfrrh gtrdgeawal
      901 nglgeachac gyadaaranh aealtvatri dsreqaarah rglarvavad advvaarrhy
      961 dqaitiytgl glaaartars elasyvderq frsisrnsag
//
LOCUS       WP_181772423             376 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181772423
VERSION     WP_181772423.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=40446
     Region          54..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 mssvlprraw wrplshtdyl asswfpgltg vralaavavv ffhygghvtd rlqgwiavql
       61 ffvlsgflit tlalreegrt gridlrefyl rrsfrilpvy flllalttva vilggtyqss
      121 rladampyyl vfgnelvdfn tpyptswslg veekfylvwp allvltsfar tgktalrllf
      181 gasavlgvvl falplapsht waslsvhycs lvigcllamv lhhprgfavf rpltspavat
      241 aigcgfvvfq fsvgplakal gghwqfvvpv yaagsalllv avvspgpvrg llssrpltfv
      301 gdrsyalyla qtgaagvsgw vlpsglakaa vttvvallia calrrwveqp aiaygrkvvk
      361 rrapagppae atagar
//
LOCUS       WP_181772427             587 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Amycolatopsis pittospori].
ACCESSION   WP_181772427
VERSION     WP_181772427.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 587)
  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 587)
  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 587)
  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 587)
  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 587)
  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..587
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..587
                     /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=64646
     Region          10..324
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mpefsigetd flldgkpfqi isgalhyfrv hpdqwadrid karrmglnti etyvawnahs
       61 pepgefdltg gldldrflrl iadagmyaiv rpgpyicaew dngglptwll rdpglrvrhf
      121 epkyltavrg ylddvfrvva phqidrggpv llvqveneyg afgddkryla althytraag
      181 itvplttvdq pthemlangg ldgvlhrtas fgsqstarlk tlrehqptgp lmcsefwngw
      241 fdhwgahhht tsvadsaadl dallaagasv nlymfhggtn fgltngandk gvyqplvtsy
      301 dydapldeag dptakyhafr eviaryqkvp dsvppearpa ptptaplrdp vslldsprrw
      361 gtaqvherlp afdeltptpr laflrttida stagvltfce vrdqatvffd gdrvgtllre
      421 hhdravrlpr argellvlve dqgrvnyger igepkgivgg arlhgeplkg wevvpidlaa
      481 lpgllpeesa ddappgpisg pvvvrggfdl deptdlfldt ghwgkgmvwi ngfllgrywr
      541 rgpqrtlyvp gpvvragrnd vvvleldtml epearfvarp llghtea
//
LOCUS       WP_181772441             324 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis pittospori].
ACCESSION   WP_181772441
VERSION     WP_181772441.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=35136
     Region          <144..239
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          <262..>314
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtvelgvael aatrfaispl setvasllqi sgldqnmvnl pwlrwaqeel erepldlstt
       61 wpllvngkps wpeflvpapr daggsierdl aalrrtpesr vraslqrvfe gklpraaaal
      121 aenpasglra iagelrathd rliaphwpri ravldadiah rarqlaagga eklfadlhph
      181 lrwradrlsl trerrertnl vvtrgpgglv lmpvvlgspy vlikantstq ttvrypargi
      241 gtlwtagtra aapnavrllg rvraellqal sspatttdla raldvtpsav sqhlkvlrds
      301 glvarersgr svlylttplg esll
//
LOCUS       WP_181772518             216 aa            linear   BCT 28-DEC-2024
DEFINITION  response regulator transcription factor [Amycolatopsis pittospori].
ACCESSION   WP_181772518
VERSION     WP_181772518.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 216)
  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 216)
  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   3  (residues 1 to 216)
  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]
REFERENCE   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14435700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..216
                     /product="response regulator transcription factor"
                     /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=22957
     Region          4..119
                     /region_name="REC_NarL-like"
                     /note="phosphoacceptor receiver (REC) domain of NarL
                     (Nitrate/Nitrite response regulator L) family response
                     regulators; cd17535"
                     /db_xref="CDD:381090"
     Region          152..208
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mirvvvvdde pmvcahlrti lgsaddievv aqaqdgaeav eavvrhrprv vlmdlrmpgv
       61 dgltaieria klpeppavva lttfdadtyv iralragaag flvkstpped liglvrvaad
      121 ghtvlspeaa qrlvamssdg rrrgddarrk teglteretd vlaclgegls nadiaarlhl
      181 aeatvksyvs rmlvkldcan rtqagllahe aglvkr
//
LOCUS       WP_181772575             414 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis pittospori].
ACCESSION   WP_181772575
VERSION     WP_181772575.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..414
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=45243
     Region          156..410
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mvqsaaapwp slspearelf rrgaeivlhp raewieelha aslggdsmra vaedpvlteg
       61 tkranmanll hwaaanvqhp grrvnanlnq evlegardmv rrgfdsggld ayrraqgvaw
      121 rrwieicfdl tsdpvllrel ldvsslsitt fiedtvaavs ermaaertel trgahaerra
      181 tvtlllegap isrsraeaql gyplagphta aivwsgsatp ssqqlesaae tlmraggash
      241 rltvvasaaa lwvwlpgrtq pradrlteel tphpdvrval grpgsgidgf rrshldaaat
      301 qrmlarltsp qqiaryqdiq llalltvdpa qadefladtl gelrhadaet retvrtyvhe
      361 lgnttrtaer lythrntvir rlaradellp rplaenavdv avaletlrwl gsgv
//
LOCUS       WP_181772592             458 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181772592
VERSION     WP_181772592.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..458
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=49066
     Region          2..452
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 msktvdaaiv gaglsglvsa yrlqragadv vvleakdrvg grlmtsasrs gigvdsggsw
       61 vglrqqavla lleefgiglv pqyadgvnll riagreyryq geiprlrphe mldlgramwv
      121 ldriakrlga ppwtgdfaar vderslgawm rrnvrtaasr lvlemvtaas fgcrptelsl
      181 ltfsahvhgs gglsdligvs dgalayriag gaaalparla eslgdrvrlg havtgierha
      241 dhviltgpgr ppvrarrviv aadpatvaci ahrpalpagr aelqrrwqmg sgikahvvyr
      301 rpwwrerglt gaaitdagta ritfdvsppe tgegvlttfl glpvsddpal lapeagdrrr
      361 qrvledlaal fgpdvwtfed yiekdwtres wqsgcllrvp tgvlsvgrpw ltepvgalhw
      421 agsesshfge ghmdgavrag traaeevlae lalkqlrt
//
LOCUS       WP_181772500             207 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Amycolatopsis
            pittospori].
ACCESSION   WP_181772500
VERSION     WP_181772500.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 207)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..207
                     /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=22475
     Region          1..182
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mdrpataeel fdtigsayed vfgrppvvgr avrhlletlp pssrvldigs gtgrpvaedl
       61 taaghrvtgl dvssvmigia reqvpaatfv radvrewtsp pesweavcaf fpflqmprkd
      121 teavladvar wlvpgglfal vtvprdyedv pvqffghtfh etsfmpddlv rrvgaaglev
      181 tgthseifta depgtppeeh llitarr
//
LOCUS       WP_181772656             322 aa            linear   BCT 28-DEC-2024
DEFINITION  COX15/CtaA family protein [Amycolatopsis pittospori].
ACCESSION   WP_181772656
VERSION     WP_181772656.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..322
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..322
                     /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=34130
     Region          19..303
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mpfqslvarl pypsfavqra vamaaviaqa gigvtgsvvr vtgsglgcpt wpqcvegsiv
       61 pvahpefdal tqwiefsnrm ltgvviavaa lcvitawrvq iehpnrrrlv klawtmpagv
      121 mlqavvggit vlaklewwtv alhflastpl vwlavlllra fkegdeparw lipdagrktl
      181 ivlavamwav lvagttvtga gphggdpgth rlqapietlt qvhggllvay livlavfglq
      241 lmrgstpkql wrrytivwvi alaqgvlgsv qyalgvpeal vsfhvlgsaa viiataalwc
      301 gsrdrgpvts atapdrelat sn
//
LOCUS       WP_181772727             274 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181772727
VERSION     WP_181772727.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 274)
  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 274)
  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..274
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..274
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28704
     Region          32..271
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mesvreieqw pvdtaatavv taagdvvgth gdttkvykla svtkpltaya aliaieegvv
       61 eldtpagpeg stirhllsht sglafnehks maapgnrrly snagfeqlad altehsgipf
      121 adyqaealfq plgmkatkla gspaagaest vddlvafaae lqapkliaae tvreatsivf
      181 pglsgvlpgf ghqkpndwgl gfeirdhksp hwtgsssspr tfghfgqsgt flwvdpdaga
      241 acvaltdraf gpwaaevwpp ytdavlaelr gltp
//
LOCUS       WP_181772797             321 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Amycolatopsis pittospori].
ACCESSION   WP_181772797
VERSION     WP_181772797.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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..321
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..321
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34598
     Region          <79..>276
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          103..184
                     /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 mtdpeaggrr lrtqveshdv ealekqtkal ravdyrcggg mcreavmarl hhghrllgms
       61 isdavrprlf savadlhnla gwtcfdsgrv vgahhhlala lgfaadggdh elaanihyrr
      121 grvhlhhgap dealtqfrlg rraaarsgsk laasilsane gwahakkgea dlavglldra
      181 rdefaekgdv eppdwarfft aidvsamags ihtdlalchg grhvglaist ltyavgaygp
      241 emrrsrslcl imlaighlld rdtdqalavg iealetagtl estrtrdrlr pleeevakhl
      301 ddpdcralse vvtwfagpad t
//
LOCUS       WP_181772870             605 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Amycolatopsis pittospori].
ACCESSION   WP_181772870
VERSION     WP_181772870.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 605)
  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 605)
  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..605
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..605
                     /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=67504
     Region          185..>521
                     /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 mtqtvdriea tgspqarvda wlgrfeaala ardveaaaal favdsywrdl vsftwtiktv
       61 egrdgvagml gacldridps gfrttetpte adgvteawle fetatgrakg hlrlkdegaw
      121 tlltslrelk gfeenqrdrr pkgvehgvvr grkswaekre eqqarlgyee qpyvvviggg
      181 qggialgarl rqldvpalvl ernerpgdsw rkryknlclh dpvwydhlpy lpfpdnwpvf
      241 apkdkiadwl emytrlmevp ywastevtsa swdeekqqwl vivvregeev vltprhvvfa
      301 tgmsgkpnlp sfpgmesfag dqhhssrhpg pdayagkkav vvgsnnsahd icaalwehga
      361 dvtmvqrsst hvvksdslmd lglgdlyser avragittdk admifasipy rimprfqipv
      421 ydairerdkd fyarleaagf qhdwgddgsg lflkylrrgs gyyidvgase lvadgkvela
      481 hgqvdhltrd svvlsdgtel eadlvvyatg ygsmngwvad lvgqetadrv gkcwglgsgt
      541 tkdpgpwege qrnmwkptqq eglwfhggnl hqsrhyslyl alqlkaryee iptpvfglqe
      601 vhhks
//
LOCUS       WP_181772875             563 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181772875
VERSION     WP_181772875.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 pittospori"
                     /db_xref="taxon:2749434"
     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=61973
     Region          47..540
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mtsavptaih hdepagrpit mfgpdfpfay ddflkhpagl gtvpaerhgt evavigggls
       61 givtayelmk lglrpvvyei aeiggrlrtv nfpgcpddvv aemgamrfpp astalfhyid
      121 kvglettpfp nplapgtpst vvdlkgeshy artpdelpev fgkvaaawdr tltekaafae
      181 mqtairdrda ktvkrlwnel vprldnqtfy gflcespafa sfrdreifgq vgfgtggwdt
      241 dfpnsileil rvvytgadde hrsivggsrq lplrlwehap edlafwpagt slsslhggsp
      301 kpgvarlhrt apnnitvtdt egrirtypaa vftaqswmll sniecdaalf pidhwtaier
      361 thymasskvf vpvdrpfwld pdpatgrdtm smtltdrmpr gtyllgddpd spaviclsyt
      421 waddslkwlp lsvservevm lqslreiypg vdvrrhiigd pvtvswedep hfmgafkanl
      481 pghyryqhrl fthfkqdgle prhrglflag ddvswtagwa egavqtalna vwgvlnhfgg
      541 etdpanpgpg dvyddiapve lpd
//
LOCUS       WP_181772909             279 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MlaE family ABC transporter permease [Amycolatopsis].
ACCESSION   WP_181772909
VERSION     WP_181772909.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis
  ORGANISM  Amycolatopsis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   ter Beek,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 279)
  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 279)
  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..279
                     /organism="Amycolatopsis"
                     /db_xref="taxon:1813"
     Protein         1..279
                     /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=29432
     Region          13..269
                     /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 mtsvperare afkrpgnslf elgdqllfyv ralaaipmav tryfrevvrl laevtfgsga
       61 laviggtvgv mvglcvftgi tvglqgfsal nqinisamtg fltayfntre iaplsaglal
      121 satvgagfta qlgamrisee idalevmavr smpylvttri vagfiaiipl yvigllisyl
      181 gsrvttvvff gqsggtydhy fslflppedv lwsfgkvlvf svgvilthcf ygyrasggpa
      241 gvgvavgrav rtsivlisvl dlflslaiwg atttvkvsg
//
LOCUS       WP_181772926             748 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Amycolatopsis pittospori].
ACCESSION   WP_181772926
VERSION     WP_181772926.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=77105
     Region          15..740
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mttsaptade aaavrtvelt vsgmtcaacs arvertlnkl dgvrasvnya teratvqvpg
       61 aladdvlier vrksgytaei rgeegpdtgf arvrdlrrrm vvaallaipl gnlsitlalv
      121 prlrfpgwel lclalavpvv fwsalpfhra tlrnlrhrss smdtlvslgv lasfawsawa
      181 afgggaepgy wigfgptaag adaiyldvaa gvttfllagr yfesrsrrsa agllaaldal
      241 aakdvrvlrd gaermvpige ltvgdlfvvk pgesiaadgv vesglstvdv savtgepvpa
      301 etgegdrvvg asvnrdgrli vratavgayt qlaqmtalae raqarkaavq rlvdricavf
      361 vpvvlgvavl tlaiwlfsga paregfaaav avliiacpca lglatptalm agvgrgaqlg
      421 ilikgpdale asrkvdtvvl dktgtvttgk msmiacrpad gftvpevlrf agavetgseh
      481 aiaaavvtaa raelpdlppv ndfgalpglg argtveghev lvgnarlfad reigvpddfa
      541 aaaqdgatai lvavdgrvag qlairdvvkp saraavdalh alglrtvllt gdneaaarvv
      601 adevgipdvr agvlpaekaa vveelragga rvamvgdgin dgpalatadl gmamaqgsdi
      661 alrsadvvlv redlrvvpda irladrtlri irgnlawafg ynvaaiplaa fgllnpliag
      721 aamslssvlv vsnslrlkdf grsdrraa
//
LOCUS       WP_181772933             104 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Amycolatopsis pittospori].
ACCESSION   WP_181772933
VERSION     WP_181772933.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 pittospori"
                     /db_xref="taxon:2749434"
     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=10583
     Region          2..104
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mswlvlivsg fleavwatal gkseglsrlt psvifgvtlv asmvglgyam kdlpvgtaya
       61 vwvgigaslt vgygmwsgae taslakilli mgivgcvvgl kilh
//
LOCUS       WP_181772880             532 aa            linear   BCT 28-DEC-2024
DEFINITION  purple acid phosphatase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181772880
VERSION     WP_181772880.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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   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 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 11244734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..532
                     /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=57521
     Region          78..190
                     /region_name="Pur_ac_phosph_N"
                     /note="Purple acid Phosphatase, N-terminal domain;
                     pfam16656"
                     /db_xref="CDD:465220"
     Region          197..445
                     /region_name="MPP_superfamily"
                     /note="metallophosphatase superfamily, metallophosphatase
                     domain; cl13995"
                     /db_xref="CDD:472684"
     Site            order(207,209,234,278..279,368,404)
                     /site_type="active"
                     /db_xref="CDD:277317"
     Site            order(207,209,234,278,368,404)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277317"
ORIGIN      
        1 msetpenprs qayrrlslae khdkfhnrys rrtlfrvgav ggaalaaggv llpgtaaasp
       61 gptvllnsdk tagsalrpfg rhiafgadps qqvvvswqvp avvtapfiri gtvpgdfspp
      121 iaaevralts qmswqhpvee vppnspksit qyylharidr llpdttyyyv vghqghdpag
      181 rlgemasfrt apapggdgtf tftafgdqgv gynavatssl iagldpafhl amgdlsyale
      241 gegghpeedq ydarlwdsff vqnepvtagi pwmmalgnhe megwysedgy ggvrarftmp
      301 dnawngstci yswryqnvgm isldgndvcy nspsnlgytk gkqlkwlgrt laafrvdpti
      361 dfivvychqc tystchsnga elgaqtdwap lfdryqvdlv lnghnhiyer tdpirggkag
      421 kkvpsrgttd pvkdgttyit agggggsvse fpapdtylgh etsndspvpm kysekdghsl
      481 tkkvtwsrvr frgyslvavd viagtgttpp kmdvraisad gtlvdqiivq rt
//
LOCUS       WP_181772963             172 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Amycolatopsis pittospori].
ACCESSION   WP_181772963
VERSION     WP_181772963.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 172)
  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 172)
  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 172)
  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 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   5  (residues 1 to 172)
  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 172)
  AUTHORS   Rosinski,J.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..172
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..172
                     /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=19140
     Region          6..77
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mpespdldgl rvlahpvrlr ilslltgvam saaeaarelg ethanvsyhl rrlheaglld
       61 vaeevrirgg makryrhdpe sgmrfssknp geeqllvatm aeelkrrsef ravgkrgstt
      121 daemwvdret wekalghare lsrilheaar pprtrgtipv natvslfemt kp
//
LOCUS       WP_181773037             517 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis pittospori].
ACCESSION   WP_181773037
VERSION     WP_181773037.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..517
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=54941
     Region          222..489
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mvsvrsvvdr vgptllhalq vpeespavgd vviaepgttl aagdlvlgva itetsdaael
       61 vklsaskgaa avllkpplaa kpsvkraaks adialievrs atswaqlvwl lrtvldalad
      121 esdaledggg pgsgdlfrla davasvvdap vtiedtnsrv laysarqdlt dsarvstimg
      181 rripddvlar frsrgvfrel srgrqtifvp aqrdgtlprl ivpirmggel lgsmwavvag
      241 pvsderaaaf adaapvvalh llrrrahtds qrrvsaellr avlegkaspr kaiaeldlse
      301 ephrvvviev sggdgrddeg lrlalleris qgvgqrpvat elggvlyavv pdgdgwselr
      361 aalealpasr rggtpraaag saceigelat sraqadeals llraklvpgr vvvfdeawta
      421 lslhrgataa stakvaelgp lgllrthdet hetgyvdtly qwlrhpgdpr aaakelrihp
      481 ntlryrmrrl ldlvpldldd pdvrlalitq lvsvrws
//
LOCUS       WP_181772783             200 aa            linear   BCT 28-DEC-2024
DEFINITION  formylglycine-generating enzyme family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181772783
VERSION     WP_181772783.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 200)
  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 200)
  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 200)
  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..200
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..200
                     /product="formylglycine-generating enzyme family protein"
                     /calculated_mol_wt=22622
     Region          1..200
                     /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 memitipage vtlsdrrter swtvgiasfl lapvpvtase tsrfprvdvs wldairfcna
       61 lseregltpa yevdedvkwd vaangfrlps eaewehacra gttgprygpl devawyrens
      121 aesvhevggk apnawglhdm lgnvwewcwd vydaevygey rvlrgggwfd ehwscrasvr
      181 rrshptfrvd dvgfrlartl
//
LOCUS       WP_181773056             212 aa            linear   BCT 28-DEC-2024
DEFINITION  IclR family transcriptional regulator [Amycolatopsis pittospori].
ACCESSION   WP_181773056
VERSION     WP_181773056.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..212
                     /product="IclR 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=21521
     Region          3..208
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtregsltld rglallqava daggeaatis elavaigasr aavyrllvpl serglvwrdg
       61 nkvrlgvgll rlagqvlpql reaarpvlre laekvgatah lsvvqgdqaq avavvepswt
      121 sfhvayrvgt rhplsagaag kamtlrpggd gwvtstgele agasgvaapv rgvpglrasl
      181 gvvsleplda svvgpavvga aqrlaevlkq pe
//
LOCUS       WP_181772956             458 aa            linear   BCT 28-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181772956
VERSION     WP_181772956.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 458)
  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 458)
  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..458
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..458
                     /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=49854
     Region          8..453
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mpfmpvtdsm fllvetrehp mhvgglqlfk kpedagpdyl rdlrrkllds dnmrdvfhrr
       61 parpvntagh iawatdndle ldyhfrhsal pqpgrirell eltgrwhstl ldrhrplwei
      121 hlveglqdgr faiyskihha lmdgvsalrh lqgtlsddpt dldcpppwgq rpkpdggrng
      181 kavpsvfqtv gktvnqlagi apaamkvare afqehtltlp aqapktmlnv piggarrfaa
      241 qswsldrvrk vataagvsrn dvvlamcsga lrdylieqsa lpdapltamv pvslrrkdsg
      301 daagnnigal lcnlathltd paarlatina smrngkklfs eltplqtlll sginvaqlgv
      361 spipgivnnt kppfnlvisn vpgprkqmyw ngasldgiyp asvlldgqal nitltsngdn
      421 ldfgitgcrr svphlqrilv hldtalaele haasvgrg
//
LOCUS       WP_181773111             368 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Amycolatopsis
            pittospori].
ACCESSION   WP_181773111
VERSION     WP_181773111.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 pittospori"
                     /db_xref="taxon:2749434"
     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=39220
     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 vkrfedafat vsgtkhaiav nngttalvaa
       61 lqaldlkpgd evvtspftfv atlnaileag atvrfadirr ddfaidpdav aaavtdrtkv
      121 lmpvhlygqt admgklapla aehglqvied saqavgasfe gkqagsfgig cfslyatkni
      181 ttaeggvitt dddkladalr vlrnqgmrar yqyevaghny rmtdlhaavg ipqlekldql
      241 taarqsnakr lseglagtpg ldipqvlpgr ehvwhqytvl vgphaflsrd elaaalterg
      301 igngiyypki vfdydcyrnn plipdakved fpvaasvaaq alslpvhphl sesdldtiie
      361 tvrevlga
//
LOCUS       WP_181773122             244 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181773122
VERSION     WP_181773122.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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..244
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..244
                     /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=26889
     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 maelvyppvi maaklmfrvl dnrirvegte hipaeggavi acnhvsyldf ifcglgaqpa
       61 krlvrfmakk eifsnriagp lmrgmhhisv drgaglasyq eaverlkage vvgvfpeati
      121 srsftvkdik sgavrmaaea gvpvvpmalw gtqrlwtkgh pkdltkrhvp isilvgepmh
      181 pkaeedaevl skdlrvrmsa lvervqadyp ekpssdderw wlpahlggta ptpeeaarld
      241 rerr
//
LOCUS       WP_181773153             399 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amycolatopsis pittospori].
ACCESSION   WP_181773153
VERSION     WP_181773153.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..399
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..399
                     /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=42305
     Region          1..373
                     /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 mkiviigagf ggmacaiwla eaghevelye qapqlrtsgn gvlllpngtg llsdlgvels
       61 glgarmdsvd glyhdgslsl rvqlskiaak fgspvlvgsr glivermaac lldgslrlnm
      121 rctgieqngd gpvrvtfadg sevkadlvig adgqrsvvrt klfgedpavy lgdatwhgit
      181 elpgafaegh avhsifgneg icvmhpvgdg kvywafelpf ddgdilppga pgdtaslkep
      241 gsavanlrar fgqwtapglr nlldamkded vsvfphiihr elpqwgegpi tlvgdaahvv
      301 pprvgmglsq aledawvlsr alagggrdpi arvrayeqvr ikrvrgmqka aralgrktvp
      361 appwllrafg rllpvtklnm aqvrgssnyl nndlpeeva
//
LOCUS       WP_181773294             617 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181773294
VERSION     WP_181773294.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 617)
  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 617)
  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 617)
  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..617
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..617
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63671
     Region          22..>248
                     /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 mttalasrve papveetvek ppdrwvrpav fgllaatall yfwnltasgy gnsfyaaavq
       61 sgtqdwkawl fgsldagnvl tvdkppaalw vttafarlfg fssftvlapq almgvasvgv
      121 lyltvkrtsg pvaglfagaa laatpvaalm fkfnnpdall tlllivgayc tvraiekasp
      181 kwlafagvai gfgfltkmmq aflvlpafgl ayliaaptsm rkrllhlvga vlsvvvsagw
      241 fialvdlwpt dsrpyiggst ddsllelalg ynglgrifgr gggtmaggtg ggmgggnvgf
      301 ggesgltrmf gasfggevsw llpaaliglv aglwftrraa rtdktraali vwggwmlvts
      361 lvfsymsgiv hpyyavalap siaavvaisg tslwrgrahl aprvflslmi aasavwayil
      421 ldrdagwlpa lrwivaglgl vtatfvlvgv ppirklvavv atvtvltigl gttayavets
      481 sqahsgsipt sgpatngerg mgggmgmdme gssselgtvl aatttkwaaa tsssqsaanl
      541 elasgksvig iggwsgqdpa ptlaefqqyv angdiayyve ggrgggpggg sneisewvaa
      601 nftattvgeq tvynlfs
//
LOCUS       WP_181773489             377 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Amycolatopsis
            pittospori].
ACCESSION   WP_181773489
VERSION     WP_181773489.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..377
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..377
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40099
     Region          4..376
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 madflpygrq sisdediaav tevlrgdwlt tgpavtrfee dlaehtggtp avavtsgtaa
       61 lhvayaaagi gpgdevvtsp mtfvataata allggkvvfa dvdadtgnld paaasaavts
      121 rtkvvaavdy aghpaaldel griahdngal lledaahsvg gswqgrpvgs ladlttfsff
      181 ptknlttaeg gavvtgsdel larargfrnh glvrdkaaqr ypdegawhqe vhefglnyrl
      241 pdvlcalgss qlrrlaefkv rraeiharyt aalssldgvs tpavldgadp vwhlyplrvl
      301 egrrralfdh lrakgigvqv nyipaywhpv fedlgyrrgl cpnaelyysq elslplfpal
      361 tdadvdrvid evhaffg
//
LOCUS       WP_181773506             251 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Amycolatopsis pittospori].
ACCESSION   WP_181773506
VERSION     WP_181773506.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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..251
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..251
                     /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=25785
     Region          44..240
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrralllvlc vllagcsaas dpaettdtgg pleatpvspr ynpaigalfv egthfctasv
       61 vhsgpgdlll taahclhdge ggeyatgisf apgyhdgvap ygywdvsdpq vpegwadssd
      121 pdldvgfata hqagntktle svtganaltt gggfahpitl tgypdereap vvchgtsaqa
      181 dtyqmrvdcp gfstgtsggp wvidadpate lgtvvgvigg ylyggddpdt syssyfdtdv
      241 atlyrkmdsr g
//
LOCUS       WP_181773634              83 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181773634
VERSION     WP_181773634.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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 18824274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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]"
                     /calculated_mol_wt=8629
     Region          1..73
                     /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 mraqlgecia alsdretevl alitgdktdr eiarelgige rtvrahvsri llklgvasrv
       61 gaavaatkvg laqdvigrdr hgg
//
LOCUS       WP_181773692             317 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Amycolatopsis pittospori].
ACCESSION   WP_181773692
VERSION     WP_181773692.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 317)
  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 317)
  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 317)
  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 317)
  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 317)
  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..317
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..317
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34269
     Region          11..300
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mnqpaatavy ravaenvqrv lrgkpdvvrl aiaallsegh lliedvpglg kttlarclar
       61 siggswnriq ftpdllpgdv tgvmvyhqnn ekfefhpggi fanivladei nrgtpktqsa
      121 llevmserra tvdsvphdvp hpflviatqn piemegtyrl peaqldrfmm risvgypdhd
      181 aevrvimsdc arvspdelep vvdleilrra idqvrdayld paicsyavrl aaatrdhasv
      241 rygasprgsi alvraaqgia atdgrnyvtp ddikavakpv lahrlvltad aelnqrpate
      301 ivdealaatp apavnav
//
LOCUS       WP_181773924             205 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Amycolatopsis
            pittospori].
ACCESSION   WP_181773924
VERSION     WP_181773924.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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 205)
  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..205
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..205
                     /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=21945
     Region          6..188
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtthldatre sydtvaedya trvgrlfgqe pigrsmlaaf aelvrgsvld vgcgpghvta
       61 hlaslglsvs gvdlspkmie iarhqypdlr fdvgsmtald lpdgalgglv awwsifhlpp
      121 aelpavfaef rrtlvpgghl lvgfhvgder lspdrayghp vsydayllqp davadllgra
      181 gfevaarltm egrkwpqacl lakav
//
LOCUS       WP_181773928             213 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Amycolatopsis pittospori].
ACCESSION   WP_181773928
VERSION     WP_181773928.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 213)
  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 213)
  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 213)
  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 213)
  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..213
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..213
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22688
     Region          1..204
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 meavifdldg vlvdsetmwd evrravvdef hgtwraeatr amqgmstpew aaylahdlgv
       61 rlrpadvaev vidrmarrya akppiipggp dvvrevakhw pvaiassspp llikafldit
      121 rlpvptavss eqvgagkpap dvylraaell gaepkncaav edttnglraa laagmtvyav
      181 pnphfppdpa vlaqttvvet itdlpaalqt pkd
//
LOCUS       WP_181773953             586 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding and vWA domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181773953
VERSION     WP_181773953.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 586)
  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 586)
  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 20696117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..586
                     /product="substrate-binding and vWA domain-containing
                     protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=64196
     Region          45..347
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          308..579
                     /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 mrgsgwlslv fgtvvgaivi vvlatavtap snaartdcvr lvtssstekg dlihelaery
       61 natnrtfgsg kcakveaykk tsgaaldlia ggwndideqq pepqvwlpss slwldllrqr
      121 gkgdlidggp rtslatspmv iampkpmata mgwpgnsigw rdvlavnqng gwaskgadka
      181 qwgnltlgkd nprrstsgla atiatyfaat ggdydkieta eavqfvrgve asvayysdds
      241 vaflrtlyee drkkptpyis amamqeqmvy lynhgaptgd pkqlqddpad ldrplvavhp
      301 aegtmlidhp flttakatae qraaakdfsd flrapgqqqr frdlgfrdpd grgnaklakd
      361 tgtegipesq pigtptgdqi qkmldgwdyt qrrgrillvl dlsasmnekf drnrsdkpys
      421 drridllkpk iveqlgllhp edevglwtfs tdgpeermpi gkvkdvrtsm idlirnlqpk
      481 gdtalyrsvv danakmrref dpnlinaivf ltdgkdtegg ytkeqvlndv daarldnsvr
      541 iftmaygpea dgrvmdeiaq kskarsykav dpqsidkmfv nvfsnf
//
LOCUS       WP_181773975             324 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181773975
VERSION     WP_181773975.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=35835
     Region          16..316
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mletsarllr llsllqtprd wtgtelaerl evssrtirnd verlrslgyp vnatrgsagg
       61 yrlgagadlp plllddeeav avaiglrtaa ggsiagveet slralakleq vlpsrlrrrv
      121 nalqaytipv prdepgprvd aatlttltaa crdheqlrfg yrahdgsesv rkvepyrlvn
      181 wgrrwylvaw dldrgdwrty rvdrltprvp igprftprdl pedvtdrvrr gvssaawrhr
      241 advivhapaa evtarinpav gtveaidatt cllrtgadsi etmavylgll gcpfevtepp
      301 qlvdylrtla dryrdatdhp grgy
//
LOCUS       WP_181774066             143 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Amycolatopsis pittospori].
ACCESSION   WP_181774066
VERSION     WP_181774066.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=15967
     Region          7..138
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mteprkpiie mplrvryhec dgqgivfnan ylayldmatf everalfgsh dealahgadv
       61 vvaesnlryr apcryddelv vsaflnhlgt tsliidfeir rggmvcteat nryvfvdpet
      121 lrkaappasv reayaaflpv qed
//
LOCUS       WP_181774199             557 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Amycolatopsis pittospori].
ACCESSION   WP_181774199
VERSION     WP_181774199.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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 11467399
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..557
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=58991
     Region          238..544
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mltpvpskph tslgrvledl gdvllepivl grttrkqlgg vvihdphdes efpakavvlg
       61 vgvreqdeva rllhdvgarg avalvvrspv tptpelkraa dssgvallgl argaswaqla
      121 allrtllaeg dvgdvspqtl ggmpsgdlfa lanaiaalld apvtiedrns rvlafsgrqd
      181 eadpsrveti lgrqvperft rglerdgvfd rlyrehtpvy vdpqryddne ialprvalav
      241 ragdevlgsi waavreplse ertqalidaa klvalhmlrl ragadverrl radlvstale
      301 ggagapeaia rlgllgqpsi vlamgllgap apdddlrlva drqrvadala mhlsavqprs
      361 avalvgdvay givpmpgshg dcqerstrva stflertgrr aaaaigigpl aldasglras
      421 rdgadralrv lltnggakrv asvedvhvda lmleladlaa argdvatgpv arllaydvqh
      481 qsqlvhtlrc wldafgdiga asaaayvhpn tfryrlrrla evgeidldda gerfaamlql
      541 rllprdartg ppaaees
//
LOCUS       WP_181774196             462 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181774196
VERSION     WP_181774196.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 462)
  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 462)
  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..462
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..462
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49484
     Region          8..352
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msklseidaw ldqnlpalla ehqvpgaava vfangevidh aagllntgtg vestvdslfq
       61 igsitkvwtt tlamqlvdeg mldldkpvrd ylpefvladd daaeritvrq ltchtsgfeg
      121 diftdtgqgd dcvaklvatl sdvpqlfgpg emfsynnagy cvlgrivevl rgksyddclr
      181 dhlfaplglt hsaagpydai ryraaighlq ptpedapvpa pawaltrsna pagshlamrp
      241 rdlltfvrmh lnegraddgt qvlkpetara mwerqvelpy lglmggawgl gwmifdwdgg
      301 pvighdggti gqsaflrvvp gsnvavallt nggkplhlyl difrkvlgdl agvevpplpe
      361 pnaaeapada srfvgeyssq vadivvsqde dgalwlertp kgifaelggp peksrlqgyk
      421 gdtlvaehdg lglhmphafv gddgtgralf vhtgradrrv nr
//
LOCUS       WP_181774207             436 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181774207
VERSION     WP_181774207.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=45609
     Region          33..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(148,150,277,279,316..318,359)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mrigkiapal vlalaaaatt acggdtsssa pkelvywasn qgtsldndka vlqpeldkfe
       61 kasgikvkle vvpwtdllnr ilaattsgkg pdvlnigntw saslqatgaf lpfddaalek
      121 vggksrflgp slaatgangq ppvgvplygq vyglyynkkl faeagitkpp atweelvedg
      181 kkltkpdkgq wglslqagqv tenshhaail gaqqgaqffs pegkpqlasd psvaavqqfv
      241 dlmqkdkivn psnaeyadta kslkdlsdgk aamfmnqasa gsfknigmdm anlgvapipl
      301 patppsagrk vtsfvaginm svfkgtknpd aaldfvkfmv sapeqallnk tygslptvqd
      361 aysdaafqte dvkvfqsvla nssepmpqvp qesqfetlig tamkamfadv aagkpvdgak
      421 irdqlnqadq qiaags
//
LOCUS       WP_181774273             415 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181774273
VERSION     WP_181774273.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..415
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=44285
     Region          1..71
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <10..414
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mgdevggrvr rlraergltq relaephyta ayvssvetga rtpsgdalrh faarlgvdtg
       61 ellgvtsprd dvrldldiaa aaldflagng sapkmrklar raerigrtrq aglawlwlar
      121 ytdgdtrprl vaaaeaalgg diapyrelav alrasvligw gephhamhll rtaldaclgs
      181 hphpvllltl haflaeghlr lgettqaahh asaalrltrg dvlaelienq rrlteaylae
      241 gqvtdavaav avlhdllher alrpvlarcl yaralvrrad dpegaladlr asrtavpdha
      301 vtleladvcr elgrlddada llaeaaeaip adsphtaslt fqqgslalar gdldaaeagf
      361 ahaidvavlr dsrgvlaasv dkagellrdq grveeaadll rrgllllgae edlrk
//
LOCUS       WP_181774269             443 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181774269
VERSION     WP_181774269.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 443)
  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..443
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..443
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=48067
     Region          8..88
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <21..436
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mppsppapte aeplgarirr lrkargltqr elaeprydrg flakvesgdr apsdevldhl
       61 arrlgltade lrfgrppgaa eeltealeta yrklqqggle taerefaqve rraaayrlpd
      121 vqcharfylg evqwqrydip saakgfahal elseaasprl samivnrvaa cralsgdlga
      181 svalvetala glraagpvdp daelalltal ihpliemgal rrarraaeeg rrtlasahrk
      241 disaryhrqa aqlwqaigla draekdlsra lrlftsigyd rdaarsrwar gflwrrlgkl
      301 ddahaelrla rdllaeagsq egvlgatiel advrrrqgal deaeelaegi rplldrspdi
      361 earaevlrll glvarargdl paatalleea aaaqesaelr galvatslhl gdtlrerglp
      421 geameayrrg vraaalsdsg ppd
//
LOCUS       WP_181774308             585 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181774308
VERSION     WP_181774308.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 :: NF008453.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11308
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..585
                     /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=63695
     Region          1..575
                     /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 mtllelrelt vgviadeter elvrelsfdl eqgrtlcvvg esgsgktvta lsiirllefv
       61 apvrtrgeit vdgvdltrls ademrayrgp rigmifqeal dslnpsqrvg kqlieayrkp
      121 gslprqaark gtplhreaet kargllkevg ltdtdrvlsl yphqmsggmq qrvmialalm
      181 adpslliade pttaldvttq aeiltlfdrv rrdhgtacvf ithdmgvaaq vadriavmyr
      241 gelvelgske dilhapkhpy tkalldcvpk lgvsrrdgfp tisealleaa mngesavate
      301 trtlagrkta agegtalvid svskvyghrg rfslsrepev havkdvslei apgeffglvg
      361 esgsgkttlg rlvsaletpt agtitfgehr ctskgldgde rafrrraqli fqdpqssldp
      421 rhsaariiae plreltglrg adldrrvtel idevglpsdt akklpsqlsg gqrqrvsiar
      481 aiaaepdliv adeptsaldv svqgqvmnll lelrrtrals flfithnlsl vlsvadrvgv
      541 myrgelietg dpdeirlrpr hdytrrllaa npelpahpht gvrnp
//
LOCUS       WP_181773380             268 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Amycolatopsis pittospori].
ACCESSION   WP_181773380
VERSION     WP_181773380.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=26977
     Region          39..268
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mdikrrfsll kktliavaaa gtlaglatap qaaaaqppst dvvggtraaq gefpwmvrls
       61 mgcggalyts qivltaahcv srtgantsit atlgvvdlqs gsakkvksty vhrsptypts
      121 tggdwalikl aspvtgiatl piatttayns gtftvagwga ateggaqqry llkanvpfvs
      181 datckaqggs yadlidsaei cagnvnsggv dtcqgdsggp mfrrdsagaw iqvgivswge
      241 gcarahapgv yaevstfata iknaaagl
//
LOCUS       WP_181774463             405 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Amycolatopsis pittospori].
ACCESSION   WP_181774463
VERSION     WP_181774463.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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   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 405)
  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 405)
  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..405
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..405
                     /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=41654
     Region          11..376
                     /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(21..22,25..26,29,63,113..114,116..118,121,141,
                     144..145,148,226,229..230,233..235,238,265,269,318..319,
                     323,327,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mspaaarswv vplawtavll dgfdlvvlgt vlpallrdhv wgltpgtasv istfgligmm
       61 igamaigtit dvigrrkali iavaafsvct alcaiapsaf vfglfrflag lglggclpta
      121 ialvteyark gkggsatttv mtgyhvgavl tallgiwliq plgwramfva galpalvlvp
      181 lmikylpese sferaretqe ksatqvvggl frggllrati afwvtsfmgl llvyglntwl
      241 peimrqagyp lgaalglllt lnlggvvgll vagrvadkvg vrpavifwfl gaavflalls
      301 vklpavglyv avfltggfvf saqvlvyayi gktypdamra tgigwaagvg rigaisgpil
      361 ggalltagia ypwgfyafaa vgalgaaavt gvragraqet atpvp
//
LOCUS       WP_181774443             490 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Amycolatopsis pittospori].
ACCESSION   WP_181774443
VERSION     WP_181774443.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 490)
  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 490)
  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..490
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..490
                     /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=54825
     Region          1..443
                     /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 mterfkvviv gtgfsglgqa iqlekagird yvilekadev ggtwrdnsyp gcacdvqshm
       61 ysfsyeqnpd wsrsfspape ifeylkdvtd kyrlrdkilf gveltgadwd etarrwhvht
      121 kagktieaqf vvsgvgglhi pqvpklpgie kfkgqtwhsa qwnheydlrg kkvavvgtga
      181 savqfvpeia pevteltlfq rtppwimpkp dhampgwakt afrripgvqr lyrnalywfl
      241 earaigfngh pammkagevi akrhigkgvk dsalrkkvtp dytmgckrvl isndyypaia
      301 rsnvdvnteg vrevkahsvv dgngvehevd aiiygtgfkv tdaleyldit gidgrdlake
      361 wategmhthk gisvsgfpnl ffllgpntal ghnsvvfmie sqsryvvdai rladsrgaaa
      421 ldvrpgvqdk fqreiqrklv kgvwtqggck swyldakgvn rtiwpgftwr ywletrkvdp
      481 sdyelsgrvs
//
LOCUS       WP_181774401             611 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181774401
VERSION     WP_181774401.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 611)
  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 611)
  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 611)
  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..611
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..611
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62976
     Region          <88..>247
                     /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 maqhrgdapp ghvpattsgr rrtaaaarrl lsvdvvltll vvtggvrvly lasptpspas
       61 epatvahvfa lshlasftdt gdtgtspfgw lqlagyalvs rafdrntvpv tavretmvlt
      121 avlcavllwv larrlglpfw aattavvlma vsplaiglqr vaivehlavt wvlaalvlva
      181 tprerakpwh dvlaasclla avltspfall alpaagwllv rrreasrvaf tavvftlglg
      241 vafgpaasal rpdlpelgpp giaiwvaldp vlvvlsmvai vagmvlprtr plavsallia
      301 avlawpavpv elplalllpl tpllvaevaa tiaasrpqag hrlvplrhpv saivlatilv
      361 lvsvagwvhg ygrlrpdpsg glaltqarew lrdnasgavv lvddaswtel aaggwptgsl
      421 vplgtcsavc atpewavlta sgqrdrprfp aasaflsgta kvavfgsgpd tvtvsrfgep
      481 sdlpgagdet gartragaal asskrvqcdg ptrdaltsgt vdprliatva alatlgpvrl
      541 vdfpsipgev aagqplrrlv vsggdeasia efytgqratf epasvtrvpg gvlvtyplfp
      601 ppglltpfsa p
//
LOCUS       WP_181774477             334 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181774477
VERSION     WP_181774477.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=37308
     Region          4..318
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msrpitlftg qwadlpftev crlasewgyd gleiacsgdh fevdralsee dyvpgrlkll
       61 adhglkvwai snhlvgqaic ddpiderhqa iipsrvwgdg epegvrqraa kemadtaraa
      121 aklgvdtvig ftgsktwkyv amfppvsqav iddgysdfad rwnpildvfd evgvrfahev
      181 hpseiaydyw ttkraleavg drpafglnwd pshfiwqdld pvgfildfad riyhvdckdt
      241 rkrfdgrngr lgshlpwgdp rrgwdfvstg hgdvpwedcf ralnsigyag pisvewedag
      301 mdrlrgaaea vtylrgllfd kpsaafdaaf snqk
//
LOCUS       WP_181774253             491 aa            linear   BCT 28-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181774253
VERSION     WP_181774253.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 491)
  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 491)
  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 491)
  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 491)
  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..491
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..491
                     /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=51385
     Region          52..490
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mrnplppvpg kllelevsdd lrrgtplatl iaapseedgd agleeiegvr ptgkagdvqt
       61 vptggtrwla gvgdgeprqy rkagaalira vssaldedvk aglkafrtfa velpedagae
      121 hieelafgll lggyrftvta eepkpsprtv rlltryerav payekalerv relaaaaafa
      181 rdlanapsni ktpawladta arvagdlpnl tvavrdekwl aeqgfggvla vgggsasppr
      241 liemeyrprg asthlllvgk gitfdtggls ikpadgmhlm rtdmaggaai iaavraiaal
      301 rlpvrvtglv paaenhvsgs syrpgdivrh yggkttevgn tdaegrmvla dalvygikkh
      361 kpdvvvdaat ltgamkvslg vrtggvfatd dslaervtka gervgeawwr mplledlaet
      421 vqgslgdvrq apggpggiva alflrefvgd vpwahldiag paradktyad vvpgatgfaa
      481 rtlvelvasy v
//
LOCUS       WP_181774507             301 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181774507
VERSION     WP_181774507.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=33263
     Region          43..296
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          207..289
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mrgttvlprt pclqpkagel plhrlevrap dalpftvgtf dtigpmsraa fphrhtfyei
       61 vhitggsgdh vvdftrwelg ppqlaviapg qvhhwdardl sgfvvlftdd fllehpadre
      121 tlrrlsqqpw rlderaaeet trliaeldee frcggqgtds vlralmhvli vragrlpgla
      181 dprpparaqa vgtefarllg rpdlglwsvg alaerigvtp gyltdavkta tgrtaaqlmr
      241 eartreakrf llgtdltvrq vasrvgfadp ayfcrffrre tglspgdyrr tgdaapeihh
      301 d
//
LOCUS       WP_181774743             264 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Amycolatopsis pittospori].
ACCESSION   WP_181774743
VERSION     WP_181774743.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=27134
     Region          24..259
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrtrslvagl lagaaavlgs ampasaaepp sgvqplivgg vdatetysfm asmqnksgdh
       61 ncgasliapq wlvtaahcve geepanwqyr inttdhtkgg evaevdkfvv hekydgsgpy
      121 diavvhltkp aeaapieigq spkpgtdvre igwgltcptr gcgdapvnlq qldttiaeds
      181 gcsgsgayda qtelcmdnqg gkasacygds ggpavvkagd kwtlvgatsr gqtascpemp
      241 giytdvtafa dwvgqqtgkq dtrs
//
LOCUS       WP_181774769             274 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181774769
VERSION     WP_181774769.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=30172
     Region          52..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 mteyldvnra nwderapaha esvdygykkf vadpahlsgv vtfdrpllgd vsgargvhlq
       61 chigtdtlsl srlgarmtgl dfsapaleia rrlaaetgae idyhesdvyg atdvlgagef
      121 dlvytgigai cwlpdiarwg kvvgallkpg grlfirdmhp mlgtldetqp litphypyfe
      181 qsepmvfdep gtyvdtdvsf qqnrthewnh gigeivmsll dagltltklv ehdsvpwnal
      241 pgfmtldeat eewrltkdpq rlaasftiea vkrs
//
LOCUS       WP_181774810             466 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181774810
VERSION     WP_181774810.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 466)
  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 466)
  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 466)
  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 466)
  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..466
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..466
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=48965
     Region          11..465
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mteydaasag gntsavfevi npateevvss vaptsaeetd aaiaraqaay pawravspsd
       61 rarllrrfad avdadienla qlevtnsght ignarweagn vrdvltyysa sperlsgkqi
      121 pvpggvnmtf qeplgvvgvi vpwnfpmpia gwgfapalaa gntvvlkpae ltpltairlg
      181 elarqagipe hvfqvlpgkg svvgqrfvdn pavrkvvftg stevgkqima gcaaqvkrvt
      241 lelggknani vfadadleka aatapygvfd nagqdccars lilvqasvyd rfmellepav
      301 hgvvvgdprl evtemgplis aghhakvssy vddsapvafr gsapagpgyw fpptvvtppd
      361 lghplaadei fgpvvavvpf aeeadavtma nhteyglsgs iwtrdvgraf rvargvesgn
      421 lsvnshssvr ywtpfggfkq sglgrelgpd avdaftetkn vfiste
//
LOCUS       WP_181774894             253 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181774894
VERSION     WP_181774894.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 253)
  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 253)
  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..253
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..253
                     /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=27387
     Region          2..249
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mirpglcsvt lrrldaeeva rraeeaglkv vewgadvhvr pgddwaadrv leamaryglt
       61 cdsygsyfra tpiesgkfge iaatavrlda srirvwagka gsadvdpder eqvvtglrea
      121 advaaghgle valefhggtl tdtaestvrl ldevgrdnlg tywqppqdlp depalaglel
      181 vldrvlavhv fswwpsnerh pltartdlwt qafallakag rpldallefv pdndpdlvpg
      241 eadslrklie aga
//
LOCUS       WP_181774935             201 aa            linear   BCT 28-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181774935
VERSION     WP_181774935.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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..201
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..201
                     /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=21071
     Region          <37..188
                     /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 mtmttcsrpv trhsfaldrs ggrhrrpgrp rrlprlaila tllaifassa mpgtargaps
       61 pqgrlswpvs papsvtryfe ppatpygpgh rgvdlaaapg anvlaaaegv vmfagqvagr
      121 gvvsidhegg lrttyqplal tvtagdqvyr gqvlgtlvvg hpgcpeqacl hfgvlrgeey
      181 vdplaligep seirlkpweg l
//
LOCUS       WP_181774948             369 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amycolatopsis pittospori].
ACCESSION   WP_181774948
VERSION     WP_181774948.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..369
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..369
                     /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=39282
     Region          17..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 msiaivgagl gglalarvlr vngvdavvye reasrdargq ggmldihsgq ralreaglie
       61 efhaiargeg qdmrllepdg tlllqedtpd daplarpevd radlrdllvd slpegtvrwg
      121 raftsaengv lcfadgstvk ydllvgadga qsrvralltd arpahigqni vevgipdidr
      181 thpdlaamvg rgnywvlgag lslgaqrngd grvriglsfy ntdedwfaas gipfddpaaa
      241 karlidlldg wdprfialie acddtvvprs itslpvgltw psapdvtlvg daahlmppvg
      301 eganmalldg allglelaar pddfpaavke yeremfertg aaarmsaemq ellmspdaar
      361 rllaffqpg
//
LOCUS       WP_181774974             392 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein, partial [Amycolatopsis
            pittospori].
ACCESSION   WP_181774974
VERSION     WP_181774974.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         <1..392
                     /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]"
     Region          <1..351
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 glepgaqyyy rfqalgkvsr vgrtrtapvg pvrrvrfasa ncqafhdgfy aahagiared
       61 ldfvvhlgdy vyehgqvggn plrdhegpev ltlpayrrrh alyksdpslr dahaahpwfi
      121 twddhevvnd ysgttpslra rrsaayqawf ehmpvrpdhp atprihrqrr wgdlldlsil
      181 dlrqyrsaqn lpdgtilgad qkawlkdqvt gageawhcwv nsimlsqlae pggggymftd
      241 qwdgflaerk evlthvaqsg ledlvvitgd whsafvddir pdfadpagpv igteftahsv
      301 ssgayspewn atngpkmgaa nphlkyfegd rygydvyevt prrwsthmrv igdrrdprsp
      361 vstlttfhvd rgrpgsyedr atitspahyr rh
//
LOCUS       WP_181774978             112 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Amycolatopsis pittospori].
ACCESSION   WP_181774978
VERSION     WP_181774978.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..112
                     /product="YybH family protein"
                     /calculated_mol_wt=11934
     Region          2..112
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 matepndlgr ffiergnagd vdglvalyep davlafppgs latghaeirk vyeqfvaaap
       61 ellpgrqhpp lvsgdlaltv atltsgemtv eiarrqpdgt wlwvldqpml vp
//
LOCUS       WP_181775002             231 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181775002
VERSION     WP_181775002.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=25436
     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 mtlfrtflte qtdpdgfysi laddsvrqla ghtplngrti vdvgggpgyf sdafraagat
       61 ylgidpdvge ltargeagen mvrgsgtelp vrtgsvdicy ssnvlehvse pevmldemcr
      121 vtkpggtifa sftpwyspwg ghetapwhff ggsyarrryl ertgkepknk fgeslfafsv
      181 gaalrwgkat pladlqeayp ryhpswaqwi vhvpgvreia swnlvmvlrk r
//
LOCUS       WP_181775006             704 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Amycolatopsis pittospori].
ACCESSION   WP_181775006
VERSION     WP_181775006.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 704)
  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 704)
  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 704)
  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 704)
  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..704
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..704
                     /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=76020
     Region          58..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 mtapfpdgde ypaspnapki tassaspkrk nsaptratla rkwaylvtsa vylpythaqi
       61 eehftalldq vfaavlsdea epaqateaga rlvalrcvgp dslrrtmevl gkgllhepel
      121 rsvrslperv lqvlgalaag ygealresiq rqqedlsrtl vtleretrre lvltqarfeq
      181 lfsgsstgva vtrvdgrvqr vnpaladlln rpvadvigln lydllhveda dglregyrkl
      241 legesqrlel srrlvgeegd tmwaaftgav irdpagepqq litlvegdtd vsllqrqlsr
      301 qalhdpltgl pnrqffstrl eralrhadpa fgvtvyhldl dgfsliaggl gqkpsddllk
      361 nvaaklravv ggeeaivari ggdefgillq ntaaspdvat vigminqels epvyleggsg
      421 vavsacigvv hrpprdiapt ellrvsgmtl rraqangyrq wamsdsaldt rerhefglav
      481 smasaweige ievvfrpltw lanstpagie arlawnhprh grighdtcvr fadetglivp
      541 lgewlirtac qeaddrlpmv vgltphqaad pdlvgtmrrv ltetglgpsr lrlgfpagav
      601 lgdlgetvdn lnllaeigvd aelqdfgaag dvlclvdvpv rtvrisprla errteplaer
      661 slrslidtvk sagatviadg idttgdagww qsvgadigtg ryfg
//
LOCUS       WP_181775086             276 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181775086
VERSION     WP_181775086.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 276)
  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..276
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..276
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28576
     Region          18..272
                     /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 mtllssrppq pvepgllsra levagrland atdvitatag rgahpdlkds pfdwvtdtdr
       61 ilerhtrrvl taefpgipvv ggefgadhga dvaeyrwvvd pvdgtanyva gvpwcaysla
      121 lidasgpvvg vvadpyraqi yaaargrgar angkpirltd rcgtagaivc teltrkgvwp
      181 gmgdfieraa aahagvrvlg saalsiaqva lghaaaavlh syrewdvags valaieagav
      241 vldrhgedta lpvdallvaa pgvadeilgw wqtsvg
//
LOCUS       WP_181775175             338 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Amycolatopsis pittospori].
ACCESSION   WP_181775175
VERSION     WP_181775175.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 338)
  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 338)
  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..338
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..338
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36304
     Region          8..235
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msansllpal svvipvyneq nwidrsvgal iasaqaanwp vevvvvddgs tdatpdklaq
       61 lqelygitvl sqpnsgrfea rragiakasg rqillldsrv ivdqssltfl rdqlvdhper
      121 tvwnghvnva sehnpyagfm aglvkipwrr ycadprlmsf gieefdvfpk gtgffsapkd
      181 vledssnafe slfedvrfas ddtgvlrwia erhriflape fsatyhgrds fkkfigqsyf
      241 rgttfvdsyl aspgparngl faamavgvlg lgvaakrpka avalaaagst aagfavtkfg
      301 atkaeakava qltpvfaagf gagalrglfm alrarlrr
//
LOCUS       WP_181774943             400 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Amycolatopsis pittospori].
ACCESSION   WP_181774943
VERSION     WP_181774943.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=41731
     Region          18..396
                     /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..121,124,144,
                     147..148,155,225,228..229,232..234,237,265,269,324..325,
                     329,333,349,352..353,356..357,360)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mavtellglp strgrfplia aqsvdalgtg lflpfavvyf hvakglpltv vgaalsiaal
       61 ialpagplag rpidrfgpsr tviaanllra vtftgyvfad eawhlvvlaa vtfwgegmfw
      121 pstgalvaqv addgqrarwy ameralrnvg iglggllgaf lvawggtggy tvivlvnaat
      181 fvvaaglvas wrapagtprp aeappaggyr kvfadrifrg vlvtvfvfal cdlaltvlls
      241 ayvldglelp awqpgvlfai ntvlvvlaqt vvasrverrg mprtlqvaag vwalsfllfa
      301 fvpagqptta fplltlamiv ftgaellqap tssaltvaia paplrgrylg leelvwsaar
      361 vlapatftwl lshgsglpwl vligccgvai vvlgklnral
//
LOCUS       WP_181775326             396 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Amycolatopsis pittospori].
ACCESSION   WP_181775326
VERSION     WP_181775326.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..396
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..396
                     /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=42877
     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 makvliaggg iagtitaial hetgheavih eaydrtaegv gafltlavng lgaleplglk
       61 glvknlgfdt prikmhlgng reladfalgg mladgttsqt vlrsdlyvgl rdeavrrgie
      121 vrygkrlada retasgvlat fedgsssegd llvgadglrs rvrriidpqa pspryvplln
      181 tgglaegvrl ddepgvlhmt fgkrlffahv vhpdgrvwwf anvprkqdps qtelatmtgd
      241 awrgelirql avdrtpavdi vratreiyrp watydfpsvp twrtdkmvii gdaahatspa
      301 agqgaamaie davtlarclr dvpsipkala tyeglrrkrv eavvergkrn gdakavgpvg
      361 rvirdffitr afknppqedp nafmwqhrie weapvg
//
LOCUS       WP_181775369             289 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Amycolatopsis pittospori].
ACCESSION   WP_181775369
VERSION     WP_181775369.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..289
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..289
                     /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=30875
     Region          1..280
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mdflrpsslt ealavkaerp davpiaggtd vmvelnfdhr rpgalldlnr vtelaewtet
       61 dgrirlgasv pyvrviaelg evlpalamas rtvgspqirn rgtvggnlga aspagdthpv
      121 llvlgaevev asvrgtrlip aeefylgvkr naleqdelit avhlpaaagp qqfakvgtrn
      181 amviavcsfa valhldtrei raavgsaapt prrataaeef lttelpwstk asiadsvkrr
      241 fgelvsraas piddvrgsad yrkhalsvla rrtltwawnd fqkgereca
//
LOCUS       WP_181775399              93 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Amycolatopsis
            pittospori].
ACCESSION   WP_181775399
VERSION     WP_181775399.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 93)
  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 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   3  (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
REFERENCE   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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 amino end.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         <1..93
                     /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          26..79
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 levprveelg srfglvpgqw pgpdpaaglt eaermvaala arghtnrqia dtlvitistv
       61 eqhltriyrk lrvqrraelk pllwaepala der
//
LOCUS       WP_181775614             129 aa            linear   BCT 28-DEC-2024
DEFINITION  (deoxy)nucleoside triphosphate pyrophosphohydrolase [Amycolatopsis
            pittospori].
ACCESSION   WP_181775614
VERSION     WP_181775614.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 10130752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..129
                     /product="(deoxy)nucleoside triphosphate
                     pyrophosphohydrolase"
                     /EC_number="3.6.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13630
     Region          1..122
                     /region_name="NUDIX_MutT_NudA_like"
                     /note="MutT pyrophosphohydrolase; cd03425"
                     /db_xref="CDD:467531"
ORIGIN      
        1 mvivgaaivr dgkllaqqra wpadhagrwe lpggriedge gdeaalarec leeldvavtv
       61 ggrvgddvpl pggkvlriya aslvsagdep ravehkdvrw issgdlddld wlpadrillp
      121 alhtllasp
//
LOCUS       WP_181775661             182 aa            linear   BCT 28-DEC-2024
DEFINITION  HD domain-containing protein [Amycolatopsis pittospori].
ACCESSION   WP_181775661
VERSION     WP_181775661.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 182)
  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..182
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..182
                     /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=19824
     Region          4..147
                     /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 mealarfgfe lgvlkrirra gwwqagvrdp esvaehttrv aqlagllaae ggadparaay
       61 lalwhdtqet rtgdlphtik gfvekpdpra itaaqtsalp gaardsvrea vdeyetaesp
      121 ealyardadk lemllqavey rdigvknvde wiasatkslq tdlarrvaea altlsslswr
      181 vr
//
LOCUS       WP_181775688             284 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Amycolatopsis pittospori].
ACCESSION   WP_181775688
VERSION     WP_181775688.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..284
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=29320
     Region          3..283
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mipapfeyva pstvdeavna laeagedakv laggqsllpv lrmrlatptt lidlgkvgel
       61 rgvredgdvl figsmtthyd vqrdalvaeh aallkaatdt vadpqirhrg tfggaiahad
      121 pagdllapvl algcelvvag pngrrtvaaa dffqdmftta laadeilvev rvpkhtgwsa
      181 hyekfnrvaq awsmvavaac vrteagtiee arvaltnmgs tpvraagvea alvgvpatae
      241 airgaaeraa egtnptadgn sdvayrqhla rvltgravla aags
//
LOCUS       WP_181775759             269 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181775759
VERSION     WP_181775759.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=29270
     Region          15..247
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mfalhqdens arrapaiwrt mlnidrglvn fvgkltvtgr vpaelrrkpl lmtanhigvf
       61 dafvlmaack riginprfml aggildapvi gpalrvsghl rvdrkessta igqfaeatea
      121 lrttrdpliv ypegrishdp glwpergktg aarlalaagv pvipisqwga heavywgtet
      181 vngpadlvpl aksglsapmr rprfqvhfgd pvdlsdvepe rpgagvraha kimqaitdgl
      241 vplrrgeldk prfhdptrpt dtvspwkkh
//
LOCUS       WP_181775794             288 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Amycolatopsis pittospori].
ACCESSION   WP_181775794
VERSION     WP_181775794.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..288
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..288
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30468
     Region          64..287
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mrrpgaegvg havsrrglll gaaalggtal lagcgaekkp ilgpppvapp tsptplteav
       61 tvqqmrsaar nknvnlviia pegvskvgmp vcvalhgrga dartfldldl qkaldqvvaa
      121 glpgfavaav dgdnywvdvg kgddpqrmls delpgwlaqr elqppsamfg ismggfgalr
      181 yardhkelka vavasaalfl swpdaksrkv fadraqwesh epllhtddid pastgvwcgn
      241 sdpfvradrk lvkaldpava kltpgehndd ywreilpevv kfvgeria
//
LOCUS       WP_181775805             371 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181775805
VERSION     WP_181775805.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 371)
  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..371
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..371
                     /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=41954
     Region          17..356
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtglqdkltp hqveefgrel deirqrivad lgqvdvdyih nviktqrale vagrgllfag
       61 ffppawiagv talsvakild nmeighnvmh gqydwtrdpa lssqkfewdt vapsenwrhs
      121 hnyihhtytn ildkdrdigy gvlrmdpaqk whpyylgnpv yatalalffq wgvmlhdlef
      181 drvvkgerkw sdnkevglkm lkkagrqvgk dyvlfplltg plapltflgn atanltrnlw
      241 afsiifcghf padvesftee etenesrgqw ylrqilgsan itggklfhim tgnlshqieh
      301 hlfpdiparr ypeiagevra icekyglpyn tgplhkqlls vakkivklam pwngapreaa
      361 tvesdktlra a
//
LOCUS       WP_181775828             954 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Amycolatopsis pittospori].
ACCESSION   WP_181775828
VERSION     WP_181775828.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..954
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..954
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=102451
     Region          <7..929
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mviggcrrrt sspvlvgrdv elrrildgam rspaviileg eagvgktrla tellacpelg
       61 grpvlsgscq plrepfpygv vfdalkdvrp sgelspvtgv lgpylpelaa flpeppprlg
      121 dpraerhrlf ravrellgsl gphvlliedl hwaddgsrrl lrflmtdppt gltllltyrr
      181 eetpggiplg sayrpapgte hvhvtlrpld rdgvqalasa llgepnvsae faarlherta
      241 gipfvveetl haigevegav hadgitarrl ldavevpall reatverlaa lppaarrite
      301 aaavlgtpst sellsaaaal tperahrali lalernvlve agegeygfrh alaqqavyrt
      361 ipgpdrqelh rraarllrdr lpqslvrlae hcrkagdrag alkfgeaaad qasavgdlat
      421 atdllrtlld epglqpsdvd rlavkfssva cnglgqaevi palerlltdg rlsgrlsgev
      481 rlglglllvr qaggleaart eielavndlp drpdlagrgm gvlaqpwvga tplrehrrwm
      541 drvdelvera tdrrlriilm annvasrlhi gdargwdmld rvptgvgsad eqrhlarlhc
      601 nsadacawig hhrrarsllr sgmqlaadcg apyvvstart tavhtdwltg nwdglaerad
      661 alideyrdll pvtselclvl gllaaargew deaavrfagt aadqpenaft pvviaahagm
      721 agmllaqdlg eaavtqaekg ldllrakgvw awgadlvsaa vdaycvtgrd daaqaltdef
      781 ereiggldap lthaalsasr glvaasrgdh aeaieafeqa rtrydalpap yhaalvaera
      841 arcrlagned vaetfaalae tfdqlgatrd aarcrhafrs tgavapsrrg rrgygdelsp
      901 rerdvarlla aghtnreiae vlflsrrtve qhvasvlrkl kvrsrselag lrsa
//
LOCUS       WP_181775853             372 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Amycolatopsis pittospori].
ACCESSION   WP_181775853
VERSION     WP_181775853.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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
REFERENCE   2  (residues 1 to 372)
  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 372)
  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 372)
  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..372
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..372
                     /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=38931
     Region          5..371
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mtatlrtrav hagrddltdl gvhaapldls ttypsrdsve eagridefat tgslsglpvy
       61 grlsnptver fekalaeleg fddavafatg maavsaslla avaqgkrhiv avrpvygctd
      121 hmltsgllgt evtwadpegl aaalrpdtgl vlletpanpt lrevdiaeiv raagdvpvlv
      181 dntfatpvlq rpgrhgarfv lhsatkflgg hgdvmggvva cstedagvlr qirfatggvl
      241 hplagymllr glstlplrvn aasataaelv qrlrshsnvs avhypgiggp liafevdgdp
      301 haligavrli tpavslgsvd sliqhpasis hrivaeddrr gagvtdklir msvgledved
      361 lwhdldqalk ac
//
LOCUS       WP_181775918             307 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase, partial [Amycolatopsis pittospori].
ACCESSION   WP_181775918
VERSION     WP_181775918.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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 carboxy end.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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          68..306
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnlsgarslr grvtllatgl valvsllllw ltwnlvgdav savpqlppgt tvrvdgvdvd
       61 asavtehlri yarnrvllfg avafcfvvla agilawtfta rvllplreit gtarrlsies
      121 mgerigevrt kdelaelaet fddmldrlqa afdaqrhfva nashelrtpl avirteldvt
      181 ladeqadeae lrrmagvvrd ateraerlvg sllllartdg aglvarepvd lavivasawr
      241 avradaekrg iraefataga pafgdpalle riagnllena irhnvdrgwl dvvtqagpqw
      301 svlrvrs
//
LOCUS       WP_181776016             346 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Amycolatopsis pittospori].
ACCESSION   WP_181776016
VERSION     WP_181776016.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 346)
  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 346)
  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 346)
  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 346)
  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..346
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..346
                     /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=35909
     Region          6..346
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mntndwsprt lavaagrpeg pgeplnvpiv aastfdagad raysrengtp twealeaaig
       61 alegghataf asgiatlsav vdtlkvgakv cvptfsyags rgllahahrt grvvvteiap
      121 ddtdawvaaa dadllwlesp tnptldvidi etiaaaangl vavdntfatp lgqrplelga
      181 divvhsatkl igghsdlllg ltiaadeava kelrdartrm gatpgaleaw lalrglrtlp
      241 vrlaeqtrta allaarlldh paitrvrypd sgtmiafelp daqiadkvig slrliraats
      301 lggveslver rawlagdahv paglvrfsvg ledpedlwtd lasalg
//
LOCUS       WP_181774742             273 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181774742
VERSION     WP_181774742.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 273)
  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 273)
  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..273
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..273
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30422
     Region          15..254
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mtlapeqvde wtvdtldlda ylgrigqera kpsadalrel akahilavpf envdvvlgqh
       61 kgialdavig klvrrhrggy cyehgslfaa aaeqlgypvr rlvarvqpqk ngpythmtlv
      121 veadgvqhlv dvgfgagmlv pmplvdgavv dqagwphrmv adgdrwrlqk legddwtdlh
      181 aftltpmhri dyevyhhyts thprspftgr lvimrleegl srkligdefi verpdgtket
      241 ttipperlda tlreldvvlt eeelakllki ypg
//
LOCUS       WP_181776122             489 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Amycolatopsis pittospori].
ACCESSION   WP_181776122
VERSION     WP_181776122.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=52513
     Region          129..485
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrfglrarvt aavvavttta tavmafsaak iqeddaldkf taaaktsfga mfgqawphle
       61 qfmtgspyal dffsqgmdka gadwmlvtsy pqstnddfka pegppvivks asesfdwttg
      121 trnanppdrr aalesvkdvv llrttgpgkl lsaitvdpas grklfvvsan fvaywvvqff
      181 dltlfeqdla aqrwklvyia lgvtalgvaa avfaagrirr pvlrvasaar dlgdgtfdvr
      241 vpvkgrdela dlarsfntma ervsesiedl rakdrqqqrf vadvahdlrt plasmvatvd
      301 sldsttpetr tratellgaq arrlaklved lmeisrfdag sadfrpepvd lpalvedaig
      361 agvpetpiev rstgdttvva dprrvhtivc nllvnavrhg rtpitvtldg evdgvtirva
      421 dsgpgipeel lpilfdrfvr gdharqateg sglglsiare nalihggsle vhndggavft
      481 vnlprgsre
//
LOCUS       WP_181776130             631 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Amycolatopsis pittospori].
ACCESSION   WP_181776130
VERSION     WP_181776130.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 631)
  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 631)
  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 10144877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..631
                     /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=63673
     Region          192..624
                     /region_name="Peptidases_S53_like"
                     /note="Peptidase domain in the S53 family; cd05562"
                     /db_xref="CDD:173798"
     Site            order(234,240,287..289,313,315..316,566)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:173798"
     Site            order(234,240,566)
                     /site_type="active"
                     /note="putative catalytic triad [active]"
                     /db_xref="CDD:173798"
ORIGIN      
        1 msrfsrvvtc svpvavgall lstavsgaqp seeartqagi talqsikksl tpaelkqssq
       61 lviekrlrad kglagklpey rtglgvsnag tvavdikgag qslvdavkaa ggsvryaspa
      121 gairadlplg avdaiagrgd vaevkaasqa mtwnesapqd rrqatasqaa aalqvaegdk
      181 ahgndtartk ygvtgagqkv cvlsdgiksl qasqtagelp avdvlpgqag sgdegtamle
      241 iihdmapgaa lgfataftse qsfadniral rttgkctiiv ddvsyfdesp fqdgpvaqav
      301 ndvtaagaly fssagnsgnl tdgtsgyyeg dfrgssskis gitgtphdfd psgttqlyna
      361 lspgslgryv tlfwsdpwak atsdydlfvl nssgsvvass egsqngtqnp yeiaqvpatg
      421 tgfkvavvky sgadrfialn virgrfvasg slkafstngv tsghsaavna fsvaaapaag
      481 afgraletgd panptgpfpg lftaaskwer ftsdgrrkqf ynpdgsvitp gnvsatggai
      541 rnkpditaad gvatsvtgfq pffgtsaaap saaaiaalll qgkpgatpaq irsaltstai
      601 dlgapgfdpv tgagvimtdp alaalgvapk k
//
LOCUS       WP_181776305             224 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181776305
VERSION     WP_181776305.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 224)
  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 224)
  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..224
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..224
                     /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=24275
     Region          14..209
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msakglpega sdpfhtfgrg iskfivrpaf rvrvhgaerv pasgpvvfma nhssmaepal
       61 lfgmfsrrta flvkaelfkg fvgwffpklg qipvkrgavd rkplmmavkv ledggavgif
      121 pegtrglgda enfergaafl vragnatvvp vatrgtykpa gakrrwrphv dimvgepftp
      181 aigkgrtgle egterlrial adlvkaldew rlehglqdtr qnvk
//
LOCUS       WP_181776335             428 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Amycolatopsis pittospori].
ACCESSION   WP_181776335
VERSION     WP_181776335.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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 428)
  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 428)
  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 428)
  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 428)
  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..428
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..428
                     /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=44882
     Region          152..421
                     /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 mvgdslvatg sggrssrfav prrllgtwsl welprrglig ylllvdaaal aattylfalr
       61 ppapsallpf sallagmils seisrpiers radtrlgagl daawifagal llppalaatl
      121 vvasavyrwl rirrgiphrq vfaaaatmms alaasllpil vgaapfadat rdfqgfalvf
      181 gtglvflsvd aalaapaaef gaepsgfafd aamvafglli awsavdwpfv tivlavalvv
      241 lhragmmral rghagtdagt glltasswld gartqfdllr grgtdlsllm ldldhfarln
      301 dehgrsvgdd vlravadtlr aevraadlvg rfggeefvvl lpgttrfdah aiaerirlri
      361 astsvslggr qpddplfagt tisigvsshp adgetldrlv gaadqalraa kvagrnrtvv
      421 feaeesld
//
LOCUS       WP_181776359             282 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Amycolatopsis pittospori].
ACCESSION   WP_181776359
VERSION     WP_181776359.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..282
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..282
                     /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=29451
     Region          4..282
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mkaapfsyfr assldeaiea latpdsrvla ggqslvplln lrqarpslvv dinrvddlsf
       61 lrkengrlei galtrhrvve tsevvrsevp llaealayvg hvairnrgti ggslahadpa
      121 aelpavmlal daefvvrgps gerivaardf flgphrtala sgelltrisv plsrgvcave
      181 elsrrsrdla lvavfavvsm sdgvcetari avagagptpi raiaaeesla ggaltadait
      241 daaesvaaat dppddlhapa gyrremaavl trraitrakg ra
//
LOCUS       WP_181776146             493 aa            linear   BCT 28-DEC-2024
DEFINITION  apolipoprotein N-acyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181776146
VERSION     WP_181776146.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Bork,P. and Koonin,E.V.
  TITLE     A new family of carbon-nitrogen hydrolases
  JOURNAL   Protein Sci 3 (8), 1344-1346 (1994)
   PUBMED   7987228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..493
                     /product="apolipoprotein N-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016410 - N-acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0042158 - lipoprotein biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53102
     Region          5..483
                     /region_name="Lnt"
                     /note="Apolipoprotein N-acyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0815"
                     /db_xref="CDD:440577"
ORIGIN      
        1 mnqrllwwlg tallllavht dwnvplaawv fpvfllryar raparravvm vgsslligql
       61 fwlgvtgllf visallafil ltllqtaafl adrlladrag plrtlvfpvt lvageylftf
      121 tgfgdfgalg stqsgnlpll qvasvtgvyg ltfvlawfas vvntvwtegf ppvrrtvlvh
      181 acvlglvfaa ggarllfdvp ttqtvriagi spssdadras saaldrigvk ywraqevsta
      241 dpvavgaafa pvtenlvelt rkqaaagaei vvwpetharv lerdqaalln rvgvearqag
      301 ihvglayaly taqapyirnv avlvgptgev awtydkthpt pmepmapgpg ivpttdspyg
      361 rlatvicyda dfrdltrqaa dkgtalllvp andwegfasl haekatfrav engyslfrhs
      421 thgkstavdg qgrvlghadh frtgqqtlva dipvqprtrt vyasigdvfa wlclaaatlc
      481 plwtytrkrt gnr
//
LOCUS       WP_181776167             684 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional MFS transporter/dTMP kinase [Amycolatopsis
            pittospori].
ACCESSION   WP_181776167
VERSION     WP_181776167.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 684)
  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 684)
  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 684)
  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 684)
  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 17682176
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..684
                     /product="bifunctional MFS transporter/dTMP kinase"
                     /EC_number="2.7.4.9"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004798 - thymidylate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006233 - dTDP biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=72510
     Region          32..454
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(42..43,46..47,50,86,136..137,139..141,144,165,
                     168..169,172,273,276..277,280..282,285,309,313,366..367,
                     371,375,391,394..395,398..399,402)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
     Region          479..667
                     /region_name="Tmk"
                     /note="Thymidylate kinase [Nucleotide transport and
                     metabolism]; COG0125"
                     /db_xref="CDD:439895"
ORIGIN      
        1 mqsvpeagtg gptnrdasti hrvrrvlaik pfrrlwgvty lcsvadwlnl ltltglvtkl
       61 tdsyaaqnfa fvgvvltsll pgllfaplgg lladrfdrrk vmvlcdlgrc gfllsiafvg
      121 tpwwvfvgnf lvgccsmmwi pskdaavpnl lrrpdqveta nqlgmvmtyg lavitaagan
      181 avltgsnttf hffqgdaqlg iakvavvitg llyltsaivi atripelslr nvhstdkpkv
      241 ksadeekfgf rqmisdgarf vrttplvrgl migafgafaa ggavigsakp ysssllagda
      301 afnllvlavf lglatgmava pklarrlahd rlfglsivaa glclivvals phlavslvav
      361 aavgvwagta fltgvtiigs riedairgri naiyqslmki vlfgstilvp vvisavqqte
      421 lslwggtiti dgtrpvmigg gvlallagii ayrqmddrra epiladlrna lrrsprrvng
      481 llialegtra intetqaarl aewlragtrp vvlaadpald dqrlakllsg asltgaraqa
      541 laaaavradi verdiqpald agsvvvmerf vdsplahlsa vagldsqele gladwatnrl
      601 rpditvllda dpgtvmrkse sldaqwrvqh lltemaaadp dryvvvdadg tedevsdrvr
      661 aavravlvgr laglapaeek vear
//
LOCUS       WP_181776499             294 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181776499
VERSION     WP_181776499.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 294)
  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 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   3  (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   4  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..294
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..294
                     /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=30969
     Region          2..287
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrvmvigatg vlgrplvrrm lagghevsgl argedrvaav rvtgakpvtg slfdvdslag
       61 alrghdavln vatripdarh amtlsgwaen drvridgsrt laaavrrvde lgivvqegis
      121 fvyadggdre ldedaplelr gniasstvah aniaelaeeg rtairlrlgl lvsddamtta
      181 mlaaarrgsp liigsrtdwt aaihpddaaa gaiaalraps gvynlaadpt rkqdlgeama
      241 taagvkrara lpkwlanrls lmsvlarsqr vvstrltdat gwrperptpd pswf
//
LOCUS       WP_181776502             255 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181776502
VERSION     WP_181776502.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 255)
  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 255)
  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 255)
  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 255)
  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 255)
  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..255
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..255
                     /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=26242
     Region          16..251
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mgdesaispk drfltvygrk pvlealddaa levdkvilad tvrgpnaaei qraakaagvp
       61 vqrasahrvk vlagngkqdq gvladvvapr mrslhaalse gkppsrvlll dgittpanvg
      121 milrtataag legvvvprrg vaaldpmvvk asagvafrap vlrcgsarea aemlteagyg
      181 iyalgasats svfdvelpqr aafvlggetn gvgeevgelv tewvsipmpg eveslnvsaa
      241 aavlsfelvr rstrg
//
LOCUS       WP_181776515             376 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Amycolatopsis
            pittospori].
ACCESSION   WP_181776515
VERSION     WP_181776515.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=42230
     Region          16..373
                     /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 mtrterpptt ssliptlggr yytdpgifaa eqeklfermw fcavrsadlp sagdyrtvri
       61 gresvivsrg rdgglrafln icrhrgarvc peesgtvkra fqcsyhawty gldgkliaap
      121 nlanlpdidr tayglhtvhl rewlgyawvc laedppsfet dvegavrerl gdlesikryg
      181 ldglsvgrri tydvkanwkl ivenfmecyh catihpelte vlpefadgya aqyyvghgae
      241 fgegvdgftt dggsgferld gvaseqdrry yaitirpqvf vnlvpdhvif hrmyplapdr
      301 tvvecdwlys aevvtsgrdv srsvelfhrv neqdfdacer cqpamasray agggvlmpte
      361 hhigefhdwl larled
//
LOCUS       WP_181776567             370 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181776567
VERSION     WP_181776567.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=40571
     Region          9..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 mmtheqylat krfpaldglr aiaallvvvf hyggpswtma ngwigvhlff vlsgflittl
       61 alreedrngr islanfyirr afrilpvyfa vlgiivvfty lrgqytssgl sgampyfltf
      121 tnefahnapf gqswtlgveq kfylvwpfla fgiaalsfpk rlglaiglia lmialipvmp
      181 yagayspiii gcalaiglhy rkgfaalrvf thpiasfvll palvvlqlhv tdieaffqdg
      241 gtvggttyav lvalfitsli prgpiawvfs tppmrflger sysvyllqgv aatvvalsip
      301 qlgthrtlta vavtvvalvi sdvlyrwvev pmidvgrkvv arrktrsedr trpsapdptm
      361 reaepaltrg
//
LOCUS       WP_181776624             124 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Amycolatopsis pittospori].
ACCESSION   WP_181776624
VERSION     WP_181776624.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..124
                     /product="YybH family protein"
                     /calculated_mol_wt=13143
     Region          20..121
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mthstsvplt adpaehpfvf qaafntgsae ildslyepda vfirrdgaqv tgadrrsang
       61 rilalgqpiv vaprqvrvag dlallivdwv ieghlaatat dvarrgpdgl wryvidnpfg
      121 vdap
//
LOCUS       WP_181776666             317 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181776666
VERSION     WP_181776666.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 317)
  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 317)
  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 317)
  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 317)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..317
                     /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=32642
     Region          65..179
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrttkslaaa claavlalic tslantanaa dklpvpwtla aalpaqaanp ggpppgsndf
       61 dcrpssthpn pvvlahglga nqtvnwqtfg pllknngycv fsltygvpga plpiyqpggl
      121 lpmeqsakel skfvdkvlda tgaskvdilg hsegtlmpsy yvkflggask vdkyvsltpl
      181 wdgttlfgas hlyalavtlg lspgingild pacgscrqfl rgseflsnlr ggngifqpgv
      241 tytniltryd eavvpytsgl gkgpnvkniv lqdsclldla ehggvaadrn aaghvlnald
      301 pahakpvpcv paspigs
//
LOCUS       WP_181776674             198 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Amycolatopsis pittospori].
ACCESSION   WP_181776674
VERSION     WP_181776674.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..198
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20235
     Region          71..176
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mtrvtklalg aavlvvaliv alltarddke pvrtsgdlta arskaalaac pppgpgevak
       61 lrgvdveclg dgsrvdlarv lsggpvlvnl waswcepcra elpllqeyaa qpgaarvllv
      121 qvassgadgl gllselgvrl psvfdgdgqs gpvrtalkvp sslpatylvt aagevrlien
      181 prvflnteqv raaaegtp
//
LOCUS       WP_181776573             128 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Amycolatopsis pittospori].
ACCESSION   WP_181776573
VERSION     WP_181776573.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 128)
  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 128)
  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..128
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..128
                     /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=14464
     Region          1..124
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 msdvaepell rewhelsarh aavfgrlecr lqerhglgvt efealerlvn cvvgkcrtad
       61 ltevvhlsqs atsrlvarle reglvqrslc esdrrgifvi vtdegrrrye eakpthratl
      121 eetltika
//
LOCUS       WP_181776501             468 aa            linear   BCT 28-DEC-2024
DEFINITION  WS/DGAT/MGAT family O-acyltransferase [Amycolatopsis pittospori].
ACCESSION   WP_181776501
VERSION     WP_181776501.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 468)
  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 468)
  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..468
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..468
                     /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=50668
     Region          5..466
                     /region_name="acyl_WS_DGAT"
                     /note="acyltransferase, WS/DGAT/MGAT; TIGR02946"
                     /db_xref="CDD:274360"
ORIGIN      
        1 mpdrlsalda sflyvedhst pmhvggvaif erprdgftye qlldligqrl aylpryrqrv
       61 levpghlarp vwvddvdfdl nyhvrrsalp qpgsdgqlfd lvarlmsrrl dpgrplweay
      121 fveglagdrv alvtkthqsv vdgigtidlg qlildatpqe pepfddnwhp rrepsrtqli
      181 ldavaetvqr pteivenvrs mahdaaaiag kvtetvgdva salktmvnpa psgplnvrts
      241 ggrmfavvrt rledfrkvra ehggtvndvv laaisgalre wllsrgsnlt atttlralvp
      301 mavrdaetae ystpallgnq vdaylvdlpv gepnavlrlq highamadhl dsgrsvaarg
      361 lltvggfapa tlhslgaraa gsmsgrifnv litnspgpqv plyagqakmv emfpvmplvr
      421 nqalaigvts yhggvyfgln gdrkavsdvd llagmieesl eelkgahw
//
LOCUS       WP_181776870             358 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Amycolatopsis pittospori].
ACCESSION   WP_181776870
VERSION     WP_181776870.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 358)
  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 358)
  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 358)
  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..358
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..358
                     /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=38456
     Region          48..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 mrvlkrfpvr lsdrpdhelv gvirmpeltv splrsilkri igamlallat vlivyldrdg
       61 yrdangdgls fldslyyatv slsttgygdi apatssarlv nvlvitplrv lflivlvgtt
      121 levltersrq afkiqkwrtk vrdhtvvvgf gtkgrsavna llgdenvepd hivvvdtdqq
      181 aleaatslgl vtvhgsatra dvlrvagvqr akavvvapnr ddtavlvtlt arelapkahi
      241 vasvreaenv hllkqsganq vvvssetagr llgmatstpl vvdmvedllt pesglaiaer
      301 pvepseeggs prhlpdivlg vvrdgvlyrv dapqadaiep gdkllyirkv taaetier
//
LOCUS       WP_181776907             918 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181776907
VERSION     WP_181776907.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 918)
  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 918)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 918)
  AUTHORS   Rosinski,J.A. 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 918)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20189366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..918
                     /product="helix-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=98040
     Region          <66..631
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          738..909
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          848..902
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mgatavtnag pddaqaaldr vltgpgaiwv vhgpsgsgrg tvlagmaqrg rrsgavvlav
       61 pagtdpdtvl lrlttqlvel igaldrpela smlsaaawlr arlesgtgtg pqttahdlit
      121 vlatlsprsr ivlqfddfdl lppdvatvlt lvaegaratg tvtvattlgh apvsgparkl
      181 laladgtvdl rpltaaetta llpgwttrgg riatdpalvt alraalgplf gnpgtvcatv
      241 eslrdrerla vvdehvclvg aptpivlpdr hpealrlrrl gphaqrlaai iavlseqgap
      301 tleklswlas aaamelpaag qaldelvrag ilrtgtggev efavpalaer lrlergmrwr
      361 tvlhrriard llerrgadpa eiaphlaelp psppdheave vllaaaasnr telptarryr
      421 maalrrleps ddrfpevlra lladsfaaga yglladdlat vlapkltaar lpvrlsatvl
      481 acwlgalahe qriaeldavr pfaralgagr llaavdrgdk avaidamqaf artcdaeddd
      541 vfvlgarill gslpgdgcrp vepgqaltdt pledvteaae vldsvsvlav ylrgsyqppt
      601 tgfafgwhav rqayrdgdwd talsltrrle gerlwwdppr rhrfasvfaa eicaqrdqpd
      661 raadwlrrlp frtsadayva waryrlhhsa grhdeaaerg wrdyvdcrer gvrpgmerll
      721 arlllgarrr gdtesvtrll aelegtaarc ptasvqeaal vcgglvrgdl esvragvrla
      781 rqsgdvfria eactafgels pvpapsllea yrtlkrldav aalatvsdll eqhriafspe
      841 rtdrvdragl dplerhivgl iasgrtnrqi aaalqvsekr iearltslfe rtgsqsrvel
      901 aaawlqgrlg aatvpags
//
LOCUS       WP_181777340             144 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Amycolatopsis pittospori].
ACCESSION   WP_181777340
VERSION     WP_181777340.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 144)
  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 144)
  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 144)
  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 144)
  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..144
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..144
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15567
     Region          34..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"
ORIGIN      
        1 mskikrfvcv lagvlalvtg fgsgaasaap kaenvvtvts anyaevmnis kqklvimdfg
       61 atwcppcrqm kpvierlaae yggrfllgev dvdqsrdlss rynirylptl vgvrnttelp
      121 ssrnigypge srlrawidaq laks
//
LOCUS       WP_181777375             231 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Amycolatopsis pittospori].
ACCESSION   WP_181777375
VERSION     WP_181777375.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 231)
  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 231)
  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 231)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..231
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..231
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25159
     Region          7..199
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mseadpavrt wrargqakav vlvlhggaeh sharvapwrl ayqrmvplak dvhragrehg
       61 vevrllrnri ygwnddgada ladarwalkr irddhpgvpv imvghsmggr valrvaddpa
      121 vvgvcalapw tppgepigav egravliahg tkdrmtdpva shafaeraek vtsrsarfei
      181 ggeghamlrr srvwnrlvra ftlelieagg tdetvsaawd rpsserlrip v
//
LOCUS       WP_181777446             718 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Amycolatopsis pittospori].
ACCESSION   WP_181777446
VERSION     WP_181777446.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 718)
  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..718
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..718
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=78740
     Region          6..706
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          497..525
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(498,501..502,505..506,508,538,541..542,545..546,
                     548..549,572,579,582,585..586,589)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          536..566
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          571..602
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          616..646
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          657..685
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlftmesgdr renkvtgdvs gtsvqvgavh gdvflhqgak pvvprqllpv sasftdrere
       61 ltaltrlled dhrqgpalav itgsggmgkt alasrwitnh adrfpdgqly vnlgafsadg
      121 pttpddvlgg flralgvpse qvpaeiaeqa amyrsvtagk rfavladdad saaqvrpllp
      181 aspdsvvvvt srwrlgaltm dgarvlvvdp ldeaagltll krtvgvqrvt telerarelv
      241 alcggmpial cvaaarlstr prwpisrlvg vladekrrls alsiadeaiv qasfdlssee
      301 ldtetarvyr llglhpgrdf gvglasaaid rtaletedal dslvvssllt digpdrfqfh
      361 dlarvharqq aarvddqatr vsalrrmldw yldnvveadl viiphrhrls pryaqvrels
      421 sqfsgtrdal dwveqelanv vatmraavdh gwwnevwqfc eglwgfflyr khyhhwekth
      481 kwavdaarhc edpaaearmh iqlgyaylnt eryedarrqf saslkaaqti edisgeataw
      541 ehlgvvaqst gghqnalecf tralrlaeqa gqrrgvalhl rrigeacaal grmrdaigyl
      601 drsaaealai gdtvlharaq mrigtsyltl grigdasrll eeaatalnhs gadpyfaeal
      661 eslaesrlre gdthtarvhl rqaleiyrks rdlkahrves riaaiasete rssepqse
//
LOCUS       WP_181776471             410 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Amycolatopsis pittospori].
ACCESSION   WP_181776471
VERSION     WP_181776471.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 410)
  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 410)
  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 410)
  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 410)
  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..410
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..410
                     /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=43035
     Region          16..404
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 maegatplap nartvrnvaf vegvrtpfgk agekgmyagt raddlvvnai rellrrhpel
       61 ppervdevai aattqigdqg ltigrtaall aglpksvpgf aldrmcagam tavtttasgi
      121 gfgaydiaia ggvehmgrhp mgegvdpnpr iiadklvdpt alvmgqtaen lhdrfpaitk
      181 qrtdafaars qekyaeavkt gkigpelvpv atrskelgwg latedepprp gttveqlagl
      241 ktpfrphgri tagnaaglnd gataallade dtarelglpi gmrlvgysfa gvepevmgig
      301 pvpateklfk rtglsiddig lfeineafav qvlafldhfg iadddprvnq wggaiacghp
      361 lassgvrlmt qlsrqfaerp dvryglttmc igigmggtvi wenpafegak
//
LOCUS       WP_181777178             611 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Amycolatopsis
            pittospori].
ACCESSION   WP_181777178
VERSION     WP_181777178.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 611)
  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..611
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..611
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=64031
     Region          54..233
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          321..605
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtsvdgsaql rrllellasg agseqlahvp vdpkatelal rirdtvaehr rreaelaalf
       61 dtasdlarld dpdavlrsiv rrarallgvd vsylslknea egntyvrvtd gsvsalfqdi
      121 vlgmgeglgg lvaqtarpya tsdyfndkrf hhtssidtgv ldegltailg vplaigskvi
      181 gvlfasdrtv refspeeval lssladhaai aldnahllde trravaelnd anatisahne
      241 amrraedahd rlmdlvlrgg dlaevaaava gvlgggiavy dadgavlart dgglrlsrta
      301 vsasrasgra vstedgwvca vqagkeflgs lvlgggpslg eadrrlfera gvvtavllmq
      361 rrsvaraede vrgellsdll tapgrnpaal margrrlgvd lstphavlia hsddvsrrrl
      421 ataaarradl vgvhadevvl lvkgedpgel arsvaaelas tmdcvvtvga agpaaspqgl
      481 aeahaeaarc vasllalgra gegasmadlg fvglllgeha dlaayvtati gpvldyderr
      541 gtdligtlla yfscggnltr akdllhvhvn tvvqrldrva sllgeewqap eralelqlal
      601 rlhsltndrn g
//
LOCUS       WP_181775268             359 aa            linear   BCT 28-DEC-2024
DEFINITION  J domain-containing protein [Amycolatopsis pittospori].
ACCESSION   WP_181775268
VERSION     WP_181775268.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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..359
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..359
                     /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=39356
     Region          5..>106
                     /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          197..>270
                     /region_name="NERD"
                     /note="Nuclease-related domain; pfam08378"
                     /db_xref="CDD:462454"
ORIGIN      
        1 mpdvdyyevl gvgkaasvte iktayrrlak shhpdaggsa ltfqlvreay dtlsdpmrra
       61 gydadgrsvr mpirprprrr fgdepgyvpe avvidpddle wwefaaqdhr vrhgrrrgpg
      121 htpvvaavgg mvlvllpvlt gvgfsaptli vwliltagta llvqrlargy laasraknrf
      181 aaefggkrvf gspgtesdel aerltadlle ryltrlpgar ifhglswpds vfadvdhavl
      241 cgkrlvlves klwlpghyet ddddrllrng safrgggsrl aeslaeyrri lpgvtlrgam
      301 ivypsrtgev ttdhddpslt ppmtpeqflh eiggwlaaep stvdsatmri vrdrvvgtv
//
LOCUS       WP_181777561             234 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Amycolatopsis
            pittospori].
ACCESSION   WP_181777561
VERSION     WP_181777561.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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 234)
  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 234)
  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 234)
  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 234)
  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..234
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..234
                     /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=24262
     Region          1..>183
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtktlaifga gpvlglslar rfgregfria lvarttenld alvaelaadg ieasafvadv
       61 yepaqigaav taigridvva fnpgggnmgd givsvldvdp enlrlivdrf vvsavalvra
      121 vlpdmvergd gailftggqs glypapflgn agmaqaalrn yfhnlnavla ekgvyagavn
      181 igaliegsvp hlaltsgpld fepevihpdv fadafwtlha krevpeilvg sfgk
//
LOCUS       WP_181777570             364 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Amycolatopsis pittospori].
ACCESSION   WP_181777570
VERSION     WP_181777570.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..364
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..364
                     /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=37199
     Region          43..358
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 mvnvpaetlr lfaepddeta rplrltgpvi llsaalllsl iagialgptt valpdvlryl
       61 gkaivggtit tddvtgysiv wqvrtprvll aavvgaglav vgvavqalvr naladpfvlg
      121 issgasvgaa avvvfglfag lgvlalstaa flgalgatal vylaarskfg ltplrlvltg
      181 valtyafqav msvlvylspn gqaaqtvlfw llgslgsatw aslplaalgv vvaivvllry
      241 gtaldvlsmg detamslgtd avalrrwlfl ltavvtgllv avsgsigfvg lvlphvvrmv
      301 agsghrrvla laplvgavfl vwvdllartl vapeelplgv italigvpvf lvvmrrrgya
      361 fggr
//
LOCUS       WP_181777597             162 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-class carbonic anhydrase [Amycolatopsis pittospori].
ACCESSION   WP_181777597
VERSION     WP_181777597.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            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..162
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         1..162
                     /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=17415
     Region          26..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(26,28,35,37..39,51,54,73,78,88,91,151)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:239474"
     Site            order(35,37,88,91)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:239474"
     Site            order(36..39,45..46,51..53,55,57,68..69,72..73,151,
                     153..154,156,158)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239474"
ORIGIN      
        1 msvtdellan nadyaagfsg plplppakhi avlacmdari nvygvlglqe geahvirnag
       61 gvvtedeirs laisqrllgt eeiilihhtd cgmltftddd fkksiqedvg vkppwaaeaf
      121 gdldedvrqs iarirnspfi pkkdsvrgfv fdvatgklne va
//
LOCUS       WP_181777598             221 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Amycolatopsis
            pittospori].
ACCESSION   WP_181777598
VERSION     WP_181777598.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
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 18629734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     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=23693
     Region          29..205
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <149..206
                     /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 magirtispi gqrtfdagri arpgiisefv egadmplaal saglrlgggn aafyrllgrr
       61 paevlgesfp elvttgpdhl rhrlnrvaeg weqrfrgsva glgssgpdrl tivagrmrap
      121 gaailltvlp etgpaeerae qlgsvndiea kilqgiasgl sslemadkfy lsrqgidyhv
      181 arlqrkfkar nrvelvsraf atglldstaw pprvpesrra s
//
LOCUS       WP_181777639             707 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein, partial [Amycolatopsis pittospori].
ACCESSION   WP_181777639
VERSION     WP_181777639.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis pittospori
  ORGANISM  Amycolatopsis pittospori
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 707)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Amycolatopsis pittospori"
                     /db_xref="taxon:2749434"
     Protein         <1..707
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          <1..706
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 ladapsaept driiaavrdr evllildnce hviesaaafa hrvlgecrrl rilatsrepl
       61 gitgealwpv vplalpdkda gpgeieaspa irllrdrasa vrkdftvdda tlatmlrvcq
      121 vldgmplaie laaarlrtms idqlanrldd rfrlltggsr talprhrtlr amvdwswell
      181 sdaervvlcr lsvfsggasm eaaekvcsgd vveeyevlel lttlteksll vasgdgapry
      241 rmlgtikeya sqrldeaget elarqahlty ftelaetaep llrraeqlew latlnsehdn
      301 itfamrgala agethaamrl aaaagwywwl sghraegmel vsaavempge vpgevgamvy
      361 glvslfvssg fadentaakw iheayrlgqe gaanhpllgl vvplvrmleg adplsawept
      421 lenendwvra larlhlgkmr islgrpgdea eayleralae frvigerfgi sfalteladr
      481 iatrgefata ceyyeqavtv vtevgavedl irlrsrqaql ywllgdeeas aaataealrr
      541 aegvtwpgal gmlalsrael ahwrgeaeea arqlavattv mgdearlghv raithdlrgy
      601 laddleearr hrasafeaaa elrhvpllah vlvgvadlal rrdepeqaar llgaadelrg
      661 lpnrahpdga rieetalrrl getkfaeaar egaqagwqkl aevtlas
//
LOCUS       WP_181778017             350 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Rossellomorea
            aquimaris].
ACCESSION   WP_181778017
VERSION     WP_181778017.1
KEYWORDS    RefSeq.
SOURCE      Rossellomorea aquimaris
  ORGANISM  Rossellomorea aquimaris
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Rossellomorea.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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..350
                     /organism="Rossellomorea aquimaris"
                     /db_xref="taxon:189382"
     Protein         1..350
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39233
     Region          7..350
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 midrilvedt vrslreryql pgisvcltds tgedfpvaag vrhiasdtkl epddhlrigs
       61 itkifistlf lklkdagivs feqtvdsllp gilkdgihit irqllqhrsg lkdyiwmdva
      121 gtkciqhavn slqdvfppqs lirlvanhdl efepgtefny sntgyillgm iaeklsgksi
      181 eyllnqwifq plhlertyfp itndlrkpya tgcsratadl tdfsdeisei mnlnisiiwt
      241 agalisnpie iqtfmkalfk gqllteeslt dmmcfleadd pkhsyglgiq qytfedgrqa
      301 ighqggihgy esvtlyypdc emsltvivnq mpigvvaiad qlfreitkri
//
LOCUS       WP_181778026             741 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Rossellomorea aquimaris].
ACCESSION   WP_181778026
VERSION     WP_181778026.1
KEYWORDS    RefSeq.
SOURCE      Rossellomorea aquimaris
  ORGANISM  Rossellomorea aquimaris
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Rossellomorea.
REFERENCE   1  (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   2  (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 13208672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Rossellomorea aquimaris"
                     /db_xref="taxon:189382"
     Protein         1..741
                     /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=84571
     Region          146..365
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            order(168..174,334)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          <227..606
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mkttemieew qtaldmeilq lkkretsgvl ieegrcirke enayiywftl sypaslpegg
       61 gvvykrkqtr itgvvissed recmieldqf igdtisygqi lhepwetlek lierleeake
      121 rtgktqriqh mmnpmketrh pktafnnplh eayvrskynp vtylwgppgt gktytlarva
      181 ayhysegkkv lllshsnaav dvlieemyhf lsshnrwkrg evirygtsrk aysedvtdls
      241 vlqlleqldp slaeekgkve tyrrrlknkl tktyssydse rlsqlevhyq kikekfkrre
      301 gelvtdarvi gttlskaaid gilfeeefdl vivdeasmay ipqvafaatl gkkiiicgdf
      361 kqlppistsf hpmvtkwlke difhsaqvan avdkgkdhsq llllpeqrrm hpsisaftnh
      421 fiyhskvgdh hsvrqmraei tnkmpfpshg avlfslkegt ewaetqkgsr wnvlsslati
      481 nliseaiedg iqsigivtpy rvqakwynll ldelvktthp qtnlyaatvh gfqgsendmi
      541 lfdlvdgash gkpgalltrk gsdrllnvai trargkfvli andqfiqekt hssqpihqfi
      601 rhlqqeghke tsssltpfst kkmkwmdvsd lnrlvkdfka akqkivvnvg lvtdipeeil
      661 sildtvsrei nviiqcknss asqagnsiki ekattdipfi aldekviwfn sfskernrfp
      721 yhvrilskri tgqflkmiee k
//
LOCUS       WP_181778062             628 aa            linear   BCT 28-DEC-2024
DEFINITION  cation:proton antiporter [Rossellomorea aquimaris].
ACCESSION   WP_181778062
VERSION     WP_181778062.1
KEYWORDS    RefSeq.
SOURCE      Rossellomorea aquimaris
  ORGANISM  Rossellomorea aquimaris
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Rossellomorea.
REFERENCE   1  (residues 1 to 628)
  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 628)
  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 628)
  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 628)
  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 628)
  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..628
                     /organism="Rossellomorea aquimaris"
                     /db_xref="taxon:189382"
     Protein         1..628
                     /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=69871
     Region          4..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 midsilfnim lvgvlgiasq wiawrfrlpa ivvmsivgll vgpifglinp kddfgevfkp
       61 iismavaiil fegslnlnfr evkglgkplf rivtfgalla wilgslgahy vaglswavsf
      121 vigglfivtg ptvilpllrq aklkprpaai lkwegivvdp fgallavfaf eiinflisdd
      181 vtgltlllff aaslfavvfg walgkftgfi fenghvpefl kspvvfalvl acftvsdqit
      241 hetgllavta mgmtlanmhi ssiddmrhfk enisvllist ifvmltaslt vdtllrifnw
      301 nivafvllml fivrplsiwl stigtdlsnk ekllvgwiap rgivaltvss yfasvllekg
      361 fedaailtsl tfalvfstvc ahgfsikwma kkldlaiddr pgvmivggsk fstefaktlq
      421 dlkipvlisd sswqrlfsvr kagipfyrge ilseqteyyl dmtpyeymia ateldsynal
      481 vcttfvpeig rnnlfqlslr sqrdddledm vhtiggrilf qnhvtweeln kriergdvfr
      541 ktnitekytf esylqerden tllifalkpa griefftega spkieqgdvi vsltkpckek
      601 nkiqekltvq rekeiikaqn etnqesad
//
LOCUS       WP_181778106             209 aa            linear   BCT 28-DEC-2024
DEFINITION  YczE/YyaS/YitT family protein [Rossellomorea aquimaris].
ACCESSION   WP_181778106
VERSION     WP_181778106.1
KEYWORDS    RefSeq.
SOURCE      Rossellomorea aquimaris
  ORGANISM  Rossellomorea aquimaris
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Rossellomorea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..209
                     /organism="Rossellomorea aquimaris"
                     /db_xref="taxon:189382"
     Protein         1..209
                     /product="YczE/YyaS/YitT family protein"
                     /calculated_mol_wt=23143
     Region          2..203
                     /region_name="YczE"
                     /note="Uncharacterized membrane protein YczE [Function
                     unknown]; COG2364"
                     /db_xref="CDD:441931"
ORIGIN      
        1 mkiywqisyf vigllifsyg ismsikvqyl gihpwdvlni alfekfglti gtwnimvgat
       61 liagtlvlkg kyvrigtiln gvmvgmlvdf flfydllppq tnlvadilil lsaiilmgvg
      121 gglysaahlg tgprdgfmlt isdltnlsis rvrimcecav lliglllsgp vfiftfiytf
      181 iqspifqksf lfftnrlhtr fpehgnism
//
LOCUS       WP_181778219             360 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Rossellomorea aquimaris].
ACCESSION   WP_181778219
VERSION     WP_181778219.1
KEYWORDS    RefSeq.
SOURCE      Rossellomorea aquimaris
  ORGANISM  Rossellomorea aquimaris
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Rossellomorea.
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="Rossellomorea aquimaris"
                     /db_xref="taxon:189382"
     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=42481
     Region          75..337
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mmdhiqlnpn mdpetickqy gielkdflnl lqgyrrldss knaseiieef kgkikkdlen
       61 ekksettyty ytyflnrfkt fltnktsnfc lldvneelmd effntatnke kispgtknty
      121 qaivnsliey aytnryised iryrfetlky etlpryipts iikemlsysl ktsspffnyt
      181 viyfligtgc riselvniri edfkveenvi firkakgnkq ryipmypevk nviikflsrt
      241 gvreiksnds rhvfskriyd nrrpvlirti qkmvetmlla lgieedycvh sfrhsfavqs
      301 ikqgmrieil qqvlghtnie ttriytklfp qdlqeevigk ypfpfeklls hmigfeglde
//
LOCUS       WP_181778347             225 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Oligella urethralis].
ACCESSION   WP_181778347
VERSION     WP_181778347.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
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 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..225
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25380
     Region          4..225
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 mttrtlalfd ldhtllpidt dyewiewlsr nhlagdpaev arrnqeimdk ydagqltiee
       61 saafvlsfla mhnpfdlgky herfmaevvr pnmteaafel vdqhlragdl cclvsatntf
      121 viqpvgrafg fehiigttpe yingrytgqf vgtasyqegk itrveqwlns lggaledfet
      181 iyfysdsmnd lpllekathp vatnpspalr eiaeknnwai idlfk
//
LOCUS       WP_181778551             397 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Brevibacterium].
ACCESSION   WP_181778551
VERSION     WP_181778551.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
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="Brevibacterium"
                     /db_xref="taxon:1696"
     Protein         1..397
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42040
     Region          1..393
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msnegpaaea lparvrkavv etfdrhaarc cggmqfsvyr agepvlqlsa gvagrrgdts
       61 akpwgprtlt vffsgtkglv amiaakaage glldvdapvc eywpefaaag kdtatvahvl
      121 dhtvglpyvd pdpsldadgr pqegeakwaf ldsrrmaail agqrplwepg tkiayhgvty
      181 gylmseiilr ttgrtvarwl redlveplgl dlhlglpaad edrvapiiqm pgysvapevr
      241 dperravidr myasllspsl pmnsrefhaa elaagggigt adslarlysl lvdpdrpggs
      301 iidpealeqa vrtwsegtdc lndrglrfgl gfeladakgt ygpvssafgh sgaggslhga
      361 wpdvglgfsf ltnemlsddv dtrakdllaa lagedvg
//
LOCUS       WP_181778639             244 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycerophosphodiester phosphodiesterase
            [Brevibacterium].
ACCESSION   WP_181778639
VERSION     WP_181778639.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
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="Brevibacterium"
                     /db_xref="taxon:1696"
     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=25783
     Region          25..243
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mslilatvag iacapkpsgp vvdaeypila ahrggshvwp qntmtafraa laarpgvale
       61 tdvralkdgt lvlahydtvd qisangetgr vadmtpaqws alriksptgg tsapaatlnd
      121 llteyggtdt vlvievkdpa lvnafieavw phrqqviaqs fdpatvkrlv ksglhvlqlg
      181 dystvqlipg ihsvgvqtln itpdlisrah eqgakvwawg nevttaqyaa hdrgldgymv
      241 ndpr
//
LOCUS       WP_181778679             373 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FUSC family protein [Brevibacterium].
ACCESSION   WP_181778679
VERSION     WP_181778679.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium
  ORGANISM  Brevibacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae.
REFERENCE   1  (residues 1 to 373)
  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..373
                     /organism="Brevibacterium"
                     /db_xref="taxon:1696"
     Protein         1..373
                     /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=39997
     Region          32..197
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 msgraltrvg esfwpmvqga laaaiawwia lrlaghpqpf fapiaavial nanpgrrgtn
       61 aihllfgvll giivgevals ffgtgfavmg iatlvgmaaa tafdgsrlvi aqgavgailt
      121 vaggqpefgp eriidaliga gvalvfsqil fparpiallr raeadvlggm atsleltaes
      181 lrhevddrae qaigglrslr dklteladtr enssrtvrha pvwwwrsapi vresenagql
      241 dllnnsllml irsvfalpee drddfapvtg riaevlrala vdpgdqgarq kaaegalesy
      301 rmleadesdp qksaqaravv rttaidimvf agvepdqarg liekhdaevd vpdpprlsll
      361 parlkrlwrr rrk
//
LOCUS       WP_181778820             255 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Pseudonocardia pini].
ACCESSION   WP_181778820
VERSION     WP_181778820.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,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 255)
  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 255)
  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..255
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..255
                     /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=26799
     Region          13..248
                     /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 matpvlskai kpvggffaft ldtfvamfrr pfqwreflqq twfvasvslg ptillgipfv
       61 alvtfqfniv lvelgaidls gagsgfatit qigpvattfi iagasstaic adigarkire
      121 eldamevlgi dpvqrlvapr vlatalnaam lngvmiligl aggyvfgvyl qgaspgqyvd
      181 sldllvsfkd lvhgeiravc fgvvgaligc yrgmtcgagp rgvgnavnet vvytflalfp
      241 lnimltqipy slgiv
//
LOCUS       WP_181778846            1116 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Pseudonocardia pini].
ACCESSION   WP_181778846
VERSION     WP_181778846.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 1116)
  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 1116)
  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..1116
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..1116
                     /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=123827
     Region          12..751
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 meqfvrsggd vartfgyhpl stdlpallha spfsrlvvvg ggvpdvtssv aqirtaptve
       61 lpngvywfsg iespvamvvd gglatedgsa iavddltqda plmsayewae hlwdeghavp
      121 rprfgigesv vtrsdgkdse iksrrfvagv wryevrldgr sqrftesale sapefggpae
      181 wvrsapaaid rfgatltrgk laasltdtvf sfratrtvfr pyqfkpvlrl lhtgatrili
      241 adevglgkti eagliwtele arraadrvli ispsslvgkw qhemeerftf eleeldtkgl
      301 arfleqhrqd rlpkrfryit slerlrkwgg leefddappq ldlivvdeah qmrnpgtksh
      361 elgvrlndwa darvfltatp vnlgyhdlas mlellapedf ddphvlelrl epnavlhrie
      421 slllnrtang aerlavlddl kdmtfgsalm srpdykvlre lvgqdildpa qvvearrila
      481 dlnalssavt rtrkaeidda kalrdphter vvwtdaerdf yseylnwcrr raeavnmplh
      541 famqmplrla saclpaaraa vlghteqwap qdeddpaaas aastvpphsd llaaakalps
      601 gvdskfdvll pilkdlirqg kqtllftfsr ptltylrnrl sgearvavlh ggvpreerrr
      661 vmtqfrkgef dvvlanrvas egldfefcst vinydlpwnp meveqrigri drigqreqki
      721 rivnfynedt idekiltrvl erigvftrai galepiiqse lsslreavys fdldvaqrea
      781 kadqvmtaia akkaeaerla gaaadllvsn dvdvtglere lvragryvgq kelahllhdw
      841 adtagapgit raddvhvtlr gnaamgdqlq dvarrgdrlq tevvelaral rdeadlplal
      901 dqedarttgg alltathplv laavsvpghr qarfaqvrvh dpdgvaepgr yavvlarveg
      961 ggeravrelw gaavdlngre aptavphall aalargelre adgpadagql vgpisratdl
     1021 lderqwdeeq rrsaegaala dsrrlsleeq lrrkegvier rmqtarangr galqlfegqk
     1081 rrarerhrea lrlledkkst elrmehiavc ylevar
//
LOCUS       WP_181779004             382 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudonocardia pini].
ACCESSION   WP_181779004
VERSION     WP_181779004.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 382)
  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 382)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 382)
  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..382
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..382
                     /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=40818
     Region          151..>335
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtltpeekrv raarrfgwig liwttlsfvf apafalvpgw dppgaivvlg vllvasvalh
       61 vwrirqhirv lgtvappwfa vaaavvgval vwvgvsssvt gwmwsilagi llgdvvaglr
      121 grfialwvgs atvvctvlay faglyvgdge aaivqaitaa vvtaiyvgsf wildverlww
      181 lkavtdlddq rrtaaelata rerlrladdl hdilghalev vafkselaar lqevdparar
      241 aemeevqqva rqsltevral vrsgrdtdla aelagaravl gsagialevt gdptvveapa
      301 rnvlgrvlre amtnilrhaq ptrcsieiap drlvicndga vgggdgtgtg lvglerylee
      361 yegrltaged grggfrleav lr
//
LOCUS       WP_181779026             401 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Pseudonocardia pini].
ACCESSION   WP_181779026
VERSION     WP_181779026.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..401
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..401
                     /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=43737
     Region          27..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 msgsgvivvg ggphgllhal alarahidvt lldvrrptpt atpramtfhw smmkgldelg
       61 ilddalargl vhriwslnvl dggermffdl dvladdveyp ftlhlpqesl seivvgrlqe
      121 msnvhlawdt rltgldqddr gvtvraaspd gdqvfrggwv vgadgpksav rravglglpg
      181 itwperfvaa nvrydfaalg yevsaiqldq rdgalvaqid atglwrytya envtlpeetv
      241 germrevfgr vlptgdepev qawaahrmhq rvadtfrvgr vlllgdaahv tnptsgygla
      301 ggffdsvslv ealsavvhdg asdeivdrys vvrrrvftei tspvssdskq llwnsdgpgr
      361 leaelerlrr atstrdrqrq ylivgcgles pslrspsvtp q
//
LOCUS       WP_181779098             262 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudonocardia pini].
ACCESSION   WP_181779098
VERSION     WP_181779098.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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   Wintjens,R. and Rooman,M.
  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 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 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..262
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27165
     Region          27..77
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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 mpetpieqgr dtpqrfcadf adelssrgvs vrdaadrsgw sksaignart gprlprrelv
       61 advlsaiglt eaqvqdwtlr haalsmtgad paasdpaapp papprrrpgl pvaagvaalv
      121 gavlagsivy llvrpatapp savasavvtv qnkvalgaed lvedttpayl ssrpepfcgr
      181 tgckvegtev vsgallpavc tvtgaemwny nldspaddnp grarsalwyr ltwpdgragy
      241 lsevylepas rgglglptct ap
//
LOCUS       WP_181779199             298 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing GNAT family N-acetyltransferase
            [Pseudonocardia pini].
ACCESSION   WP_181779199
VERSION     WP_181779199.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 298)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..298
                     /product="helix-turn-helix domain-containing GNAT family
                     N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31988
     Region          30..107
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          136..292
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
ORIGIN      
        1 msspsrtaps sstvlplsdv snpdptqlsp ldattyaewf aclaeptrvr llhaiasagr
       61 dttvgelrtg lgisqstcsh hlrkladvgf vtmrkegtat lvavnpacct glphaadavm
      121 gmlgprpccp ddvpadvtvr alepgdwadv rriyaegiat ghatfetevp erreldrkwl
      181 pghrwvaevd griagwtalt aastrpvyag vaetsvyvge efrgrgvgka llhkqvtaad
      241 tdgiwtlqts ifpenrasva lhqsagyrtl gvrerigrhh giwrdtvlle rrgavdpv
//
LOCUS       WP_181779329             540 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Pseudonocardia pini].
ACCESSION   WP_181779329
VERSION     WP_181779329.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 540)
  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 540)
  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..540
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..540
                     /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=60822
     Region          5..481
                     /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 mdtdattply daivigagin glnqihrlrd rsgldvrafe agsdvggtwh anrypgarld
       61 sesytygyff seeiyrewrw pehyasqadv erylrfvadk ldlrrsidfd ttvtsaryva
      121 aenvwevrtd rdethraryl vtalgtesap qmpenltgld efegewhhta rwpqqpvdya
      181 gkrvavlgtg asgvqvitev aktaasltvl qrsanycvpl rnspitdeqh qalqgqsrsl
      241 fekcnqsfig fmyawdprsg hdfdaagrre vyeqlwerpg fakwhngfse vytddtinee
      301 fgefvrekar ariddpavae klmprypfst rrvtmdsgyy eaynqdnvrl vdlketpyer
      361 ftpkgmvvdg vehefdliif atgfdaftga ftridivgen gvalkdywad gprtllgigv
      421 agfpnffmvt gphtkgvfcn vpicgeqnvv witeliahld agghtyidpr paaqeewgeh
      481 vmdlyqgtml aksgtesyfl gtnvpgkakt vygyfgsvpq yaarcdevak agytdhfvir
//
LOCUS       WP_181779362             122 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudonocardia pini].
ACCESSION   WP_181779362
VERSION     WP_181779362.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=13569
     Region          5..86
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpdpldrvla alanphrrai vhslgqqpha ihqlaamrel slpaihkhve vlgsaglvhr
       61 hkrgrttflt lerkalhqlq dwvgqfhpyw gsdeatyeny erylgvapps dtvtdegqet
      121 gs
//
LOCUS       WP_181779409              97 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Pseudonocardia pini].
ACCESSION   WP_181779409
VERSION     WP_181779409.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=10477
     Region          1..94
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mvreiafltv adgagpales allsvrdvld adsgclgftl drclenpley vlvvewrsle
       61 ahtedfrssp drsrflkall gcvsepprsa hyvvavs
//
LOCUS       WP_181779443             199 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional class I SAM-dependent methyltransferase/NUDIX
            hydrolase [Pseudonocardia pini].
ACCESSION   WP_181779443
VERSION     WP_181779443.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 199)
  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 199)
  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 199)
  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   4  (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   5  (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 18603314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..199
                     /product="bifunctional class I SAM-dependent
                     methyltransferase/NUDIX hydrolase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /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]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=22096
     Region          36..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"
     Region          <160..195
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
ORIGIN      
        1 maepdedtta gsytdrlnrl qtarwkqvld vqrpyrwnlr rllgerrvld vgcgigrnla
       61 hlsaesvgvd hnqhsvdacr elgltafttd eflaapperp fdgmlaahlv ehlppdgaae
      121 ilrpylpsla pgarvvlicp qergyasdat htvffdharl relaeelgle vseersfpfp
      181 raagrvftyn efvsvahvp
//
LOCUS       WP_181779598             318 aa            linear   BCT 28-DEC-2024
DEFINITION  GDP-L-fucose synthase family protein [Pseudonocardia pini].
ACCESSION   WP_181779598
VERSION     WP_181779598.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (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   2  (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   3  (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   4  (residues 1 to 318)
  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 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 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..318
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34472
     Region          9..307
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(14,16..19,40,43..46,66..68,70,90,109..111,140,144,
                     167..168,170)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(87,111,140,144)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(111,140,169,188,205,213)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 mrpvhqddri yvaghrglag saiwralega gftdlvgars aevdlrdraa tfdflgdtrp
       61 svvvlaaakv ggiaandasp adflsdnlri qtnvmdaarq agiekllflg ssciypkfae
      121 qpiressllt gkleptnday aiakiagima vqatrrqdgl pwvsamptnl ygpgdnfdpe
      181 kshvlpalir rfheaaeaga eqvtlwgsgt prreflhvdd lgraivrlld vyddpepinv
      241 gvgedvsire laelvadvvg frgeivqdrt rpdgtprkll dvsrinalgw qasiplregv
      301 estyrwfvsh raearlag
//
LOCUS       WP_181779700             556 aa            linear   BCT 28-DEC-2024
DEFINITION  cation:proton antiporter [Pseudonocardia pini].
ACCESSION   WP_181779700
VERSION     WP_181779700.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 556)
  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 556)
  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 556)
  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 556)
  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 556)
  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..556
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..556
                     /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=57918
     Region          45..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 mellligllg llaiaaasal sdrvgvaapl vlvvvglgvs lvpgvpafei dpewilagvl
       61 ppllfssava mpamdfrrdl gaisglsvll vvlstavigf vvhalvpdlg laasfalgai
      121 lsptdavats ivkkvgvapr ittvlegesl lndatalvvl raaiaataas vsvggvladf
      181 aiavvvavvv gllvgrlgll vrsrirqapv stvvsyaipf aasipaealh gsglvaavva
      241 glvtgqgair ylspqhrlsd rqnwrtvevv legaifllmg lelttvlgdl redggsawlg
      301 iglaalalll tvavraafia pligvqrgla rrseslrpdl agmderlrlg ntlefrgrsr
      361 eiddperaee frtrlrrkia didyllaepl garegavivw agmrgavtla aaqtlpedtp
      421 lrsllvfvaf lvaagsllvq ggtlawfvrl vrpagpdped laaergella rmraasrevl
      481 ekhsanpava tflertsddv qrpdpadfra lmlemieaqr atlvaaraeg tfasaaltsa
      541 lenldaeqin lelrgg
//
LOCUS       WP_181779826             220 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Pseudonocardia pini].
ACCESSION   WP_181779826
VERSION     WP_181779826.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 220)
  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 220)
  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 220)
  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..220
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..220
                     /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=23472
     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 myvvimgcgr vgaslsagle rlghevavid qdvqafrrlg tdfrgrqvig fgfhrevlie
       61 agiekadafa avssgdnsni lsarvaretf gvervvariy dakraavyer lgiptvatvp
      121 wttdrfmrmv lpdgvatawr epagtvailp lplhedwvgh pireleevaa crvafivrfg
      181 tgvlptrdta vqaedtvyva avsgtvsdvt aaaaappqea
//
LOCUS       WP_181779934             390 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudonocardia pini].
ACCESSION   WP_181779934
VERSION     WP_181779934.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 390)
  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..390
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..390
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40363
     Region          8..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 mapldegppp tgplagvvva dfsrvlagpy atmllgdlga tvvkvegpgg ddtrswqppt
       61 vergdgpeat yylsinrnkh svvldltdae dlaaaqalaa radvlienfm pgslarfgld
      121 eptvraandg vvycsisgfg deggaglggy dllvqatsgl msltgeadgp pvragvavfd
      181 vitglhaava vvaalrhrdl tgegqhvktn llsaalsslv nqtsavvagg vvptrmgnah
      241 lslfpyeplp tgdgelivia andhqfrrlc gaieapella dprfgtmvdr trnreelrpl
      301 llaklavrga hewfdvlsaa gvpcgpintv degialaesl gldpvvhpgg gvgtvrnpvd
      361 ysatppdyrr tppalgadte avkkwlqtgr
//
LOCUS       WP_181779997             254 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudonocardia pini].
ACCESSION   WP_181779997
VERSION     WP_181779997.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25739
     Region          7..253
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtypepfdlt grvavvtgag gglgrafagv laeagatvac aerdlaaata taaplgavav
       61 eldvtdedqv aevvprlaae lggldvlvnn agigdlrsvp lhrvrtehwr rvlavdldgv
      121 flcsraalav mveqgsgkiv nvasmfglsg arispipays aakgavvnlt relglqyaaa
      181 giqvnalcpg fvrtglsggv yenpeflarl qaqvpmgria epaelrgall llssaasdym
      241 tgqtlvvdgg ctag
//
LOCUS       WP_181779963             128 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Pseudonocardia pini].
ACCESSION   WP_181779963
VERSION     WP_181779963.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..128
                     /product="YybH family protein"
                     /calculated_mol_wt=14305
     Region          3..124
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mdteirelve rwaaairtgd letvvadhad divmfdvppp qdgvrgiaay retwppffef
       61 lasggsfdil elqvtagtdv ayafallrcg saeererrpd qrlrltlglr reggrwvvah
      121 ehhsfpvd
//
LOCUS       WP_181779036             445 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Pseudonocardia
            pini].
ACCESSION   WP_181779036
VERSION     WP_181779036.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 445)
  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 445)
  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 445)
  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 445)
  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 445)
  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..445
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..445
                     /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=49670
     Region          20..413
                     /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          <397..>441
                     /region_name="PRK09303"
                     /note="histidine kinase"
                     /db_xref="CDD:236462"
ORIGIN      
        1 mtqpssrpvr yidddrdlpr frvnraamvd pdvfareqer ifdkvwlyvg heteltkpnd
       61 fktrtvagrp lifardrrgv vqvwvnscph rgamicrepa gnarfmtcfy hgwsfdtsgr
      121 lvsvpgdtay gpdfvrpgla appqvdsyrg fvfvsfnpdv epladylaea tefidlvcdq
      181 sesgmqvleg theysvkanw kllvensydg yhavsthqry femvmasgae ldatalgdsi
      241 gvalgnghaa svggpntggm fgrplsaaaq aerqgrfesl rgrhgaawvd rmtgarnlvi
      301 fpnlviidlv mgvvirkidp vrpdymevta welvppeega elrkqrldnf ltfwgpggla
      361 spddvealet cqrsfaahre lpwsdvsrgm vsavplgsde lqmrtwwrrw nelvndevlp
      421 pephdppgdr frgerlelqd qgtsv
//
LOCUS       WP_181779257             500 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Pseudonocardia
            pini].
ACCESSION   WP_181779257
VERSION     WP_181779257.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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   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
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..500
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=53770
     Region          3..490
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mqigdlirra grqfgaapal vdgervvtfa efddltdrlg hallsrglaa gdrvavlmpn
       61 gidgvvvyya laksglvrvp lnaretahel afkiedsqar glvvageapa pveitiaaee
      121 lpgliegapa gpcdvrrdpd eplrlaytgg ttgrpkavvl ttrselaevn nflvdlvpnl
      181 rpdsvmlhaa pithgsgaff lphlvkgaan vivskfspga fleaaqkhra tttfmvptmi
      241 gmlledlata qadlalerlc yggapiattv lqrgidvlgp vftqlygqae aplaitclqp
      301 wehtperlts agkpytfvev dirdaegnsl gvdgvgevlt rgphtmeryw rrpeataetk
      361 qadgwvhtgd igrwdaegyl hlldrrhdvi isggfnvypr evedallahp avveaavvgl
      421 pdekwgervt aavvvraaad pdeirafcad rlagfkrpka veiwpdlpts pvgkslrrev
      481 rdrmlttars lserainsed
//
LOCUS       WP_181779561             522 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Pseudonocardia
            pini].
ACCESSION   WP_181779561
VERSION     WP_181779561.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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   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
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..522
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=56147
     Region          17..522
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 msspgpsdva aatgttvdal frrafrifad rvavtsdqpc eepwtyrelg graerlaagl
       61 hasglrrgdr vavlsetrpe yvelyaalar lgvavvtlnv rlhpdelahi vgtagprali
      121 tsgsfaasae airdrspsvk awysldpreg flpygslres gaevpepaaq pgdlhnvlyt
      181 sgttglpkga mitqqaaavr glrlaqwfgl taddgfvgwl pmfhcagdes lyatmvtggr
      241 faclrkadpa rildlverdr lswtlllpgv itdvlaepta grdltsfrfa igyanmmptv
      301 veqltakyri sfcdafgqte tsyalahgfs gpgerphlrk tptplldvrl vdtemnevpv
      361 gvpgecvvrg pgvmsgyldd paataeafrg gwlhtgdvlv raedgtlsfv drtkylvktg
      421 genvypaeve haiaghpavq evcafgvpde rwgetvkvvv vrapgaqvsa aeivahcreh
      481 lasykrpryv eflaseelpr sttgklqrhv laergateae ra
//
LOCUS       WP_181780295             256 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudonocardia pini].
ACCESSION   WP_181780295
VERSION     WP_181780295.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=25928
     Region          1..255
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mtrldgkvav vtgaagglgr agallfaaag arvvcvdvae aglaetvrei gasggealav
       61 rtdvsrlgev eamvgaalaa ygridvlwnn aavlnglyss aeeiteeewn aalavtltga
      121 ffcikavvph mkergggaii ntasvaglva hrvgraayva akgglialtr qlslelgphn
      181 irvnaiapga irtgmtatvs rpdeptfdvs rdepvadavr raepvevart alflagddlg
      241 pmtgailahd gglsvr
//
LOCUS       WP_181780134             375 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Pseudonocardia pini].
ACCESSION   WP_181780134
VERSION     WP_181780134.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..375
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..375
                     /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=40714
     Region          1..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 msrhveiagg giagltiatl faregwtatv herqdairev gsglvvhqss avvfeeigal
       61 eeiaagatrf rtsalgdeqg rilwkktlge esrtynplrt svinavhkaa vgagveirtd
      121 smalsavpag vlrtsareer padlviaadg lhsavrdslp itvekkmlna gctrtviprg
      181 dfdrhdgfle lwsgslrlgi cptsptqsyi yyaaredder gsavpvdvdy waanfpglpq
      241 efldrlpqgd airhayslvr ldrwsagkva vigdachtlp ptlgqgvgla vgnaralvhd
      301 vahaddvpaa larwerrirp vidttqdwsm ryellssrwp rfgqglrkkv lqasrhpriq
      361 rgmtaadraa kqwaa
//
LOCUS       WP_181780080             102 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein
            [Pseudonocardia pini].
ACCESSION   WP_181780080
VERSION     WP_181780080.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=11063
     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 mavvkinaih vpenagpele krfanrkhav dgqpgflgfq llrpvkgder yfvvttwesd
       61 eafeawrqgp aveahagsrd pnagprpvas gadllefevv dl
//
LOCUS       WP_181780310             308 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pseudonocardia
            pini].
ACCESSION   WP_181780310
VERSION     WP_181780310.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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..308
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..308
                     /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=33750
     Region          7..293
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maasstirig sapdswgvwf psdpeqtpad rflgevsaag yewieigpyg ylptdpnela
       61 drlathslkv sagtvfehlh rpdswedvwk qvtdvaslta avggkhivvi pdtwrdhktg
      121 apledrtlsd erwgllttgm delgrrilee yglavqfhsh adshvghqhe ierfventnp
      181 eyvnlcldtg hvsyyggdnv alikkypsri gylhlkqvnp dviarveaed lsfadavklg
      241 amiepplgvp dmpsllaave elgtdifaiv eqdmypcppd hplpiaqrth tylagcsgrl
      301 digtpkgl
//
LOCUS       WP_181780303             629 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Pseudonocardia pini].
ACCESSION   WP_181780303
VERSION     WP_181780303.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..629
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..629
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=69014
     Region          <12..104
                     /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          370..624
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mepklidved ffsdpvfaga slspdgtria ylapkdgrrn vwvrgideeh edavcvthdt
       61 rrgigkyhwt ddprwllyeq dtdgnedwhl yrvdleapte pavdltplpp gsrvfgfeal
      121 egvpgsilvv mnkrplyldr frvdvatget tlhleqpspg etvltdrrge pafhsrltdd
      181 gttvfsavdp ggelrplyrv ggaehpygav pqyvtpdgqg lllgsyqdsd dlrlvridra
      241 tgeqtvvaav eghdlcalga ldsrlppivf tsrrtgevla arfvgdrphi evvdpefaev
      301 yaelsalsdg vlgtvssdes erywiaafih drepavtwlh dretkqsrvl frpyphldpa
      361 dlapmtavgf aardglplhg fltlpvhvhp rrlplvllvh ggpwahdtwg ydpqaqflan
      421 rghavlqvef rgstgygrrh ltaavgelag amhtdlidaa dwavaegiad perigiyggs
      481 yggyaalvav tvtpdhfaaa vdyvgisnlv efmravpefa rhglvnnwyr yggdpdvpeq
      541 eadllarspi tmvdrirtpl lvvqgandar vpqaesdniv aslrgrgvpv eylvaddegh
      601 gfenpenqir fyramerhfa ahlggrtgg
//
LOCUS       WP_181780381             611 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Pseudonocardia pini].
ACCESSION   WP_181780381
VERSION     WP_181780381.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 611)
  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 611)
  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 611)
  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..611
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..611
                     /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=66025
     Region          63..>304
                     /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          230..565
                     /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 mgnpllsfwl rllgqdeppp rrgpsgrlrr ripmasavea eatiflilrr mrtplivlit
       61 ifavsvlglt lvpgasgrgm sffdafyfms ytastigfge lpdpftaaqr lwvtaaiylt
      121 vigwayaigs llalvqdraf rralalqhft rkvkrlrepf llivghgrtg ellchsfdam
      181 gkrvvvidva edrivalelg syrgdvpglv adgrdpghlg vaglrnprce avlaltddde
      241 anlavamtaa llrpdlpvia rtvsptaaer irafgtptvv nafdrfgdhl rvamrapasy
      301 qlmtwlesgp gaelpdrgrp pgeghwvvcg ygrfgrevta dlraeglevt vvetrtgagd
      361 aapadggvat vqgsgsdpdv leragvegav gfvagtdndt tnlsmvadar rlnpsifvaa
      421 rqnrpasapl faamevdsll vpaevvahev faqlstpllw rflqqvpaqg drwatqlidr
      481 itaqcghrlt spwkvrlnrg eapalvgwlg tgearlgdvl rdperredrl avvvlmilrr
      541 dadgdeeclm apaddvvlap ddeliliggt aarrgldvtm lvdaareyvq tgrrvpnswl
      601 wrklartgpa g
//
LOCUS       WP_181780445              70 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Pseudonocardia
            pini].
ACCESSION   WP_181780445
VERSION     WP_181780445.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 70)
  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 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   3  (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   4  (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 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         <1..70
                     /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          3..68
                     /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 ttranpaglt grqleilqlv aagltnaeia arlvlsvrtv dhhvsavlqk lgvasrrdaa
       61 aalaereipa
//
LOCUS       WP_181780400             460 aa            linear   BCT 28-DEC-2024
DEFINITION  FadR/GntR family transcriptional regulator [Pseudonocardia pini].
ACCESSION   WP_181780400
VERSION     WP_181780400.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 460)
  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..460
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..460
                     /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=48747
     Region          2..231
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
     Region          243..455
                     /region_name="FadR"
                     /note="DNA-binding transcriptional regulator, FadR family
                     [Transcription]; COG2186"
                     /db_xref="CDD:441789"
ORIGIN      
        1 mtgtlasris reiegeimrr gwpvgevlgs epglcehygv srgvlreavr lveqhgagrm
       61 rpgrnggliv capdsgavtq alviyfehlg lgvqevleaa illeplaagl aagrvdelgi
      121 grirrilqge serrdergva alhalhvelg klsgnpalel fvavlnrlgt rfaatgrais
      181 qdeldrvkla teerhsaiad avvsgdrpra eattaahlda vsgwmtaldp rvdgrrprlp
      241 avlhgskraa gvagalydei vasgwpvgrr lgseyevmar fgvnravlre avrilefhgv
      301 lttrrgtggg ffvaaprvga svdsvalyld hrgvgpgdlr avreaveigv lglvakrwte
      361 psvaarlaag pqgpdglhte laelsgnrvl avflrilqel werlygpdpv agvdldtaad
      421 tpaqvataha divdallagd ggvarlrmrr hlaglsgwdr
//
LOCUS       WP_181780566             388 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudonocardia pini].
ACCESSION   WP_181780566
VERSION     WP_181780566.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..388
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40957
     Region          1..379
                     /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 msaapldgil vvameqavaa pfatrqladl garviklerp gtgdfargyd gkvdglssaf
       61 lwlnrgkesv eldaksadgr rlldallgra dvflhnisps aaarlgidsa tlstrfprli
      121 agsvsgygtr gpladakayd llvqgetgli sltggedspa kvgisiadis agmyayasvl
      181 aaihhrsrtg ealpvdvslf dsltewllyp myytahggaa prrmgashat iapygpfttg
      241 dgaqvllavq nerewvrfca evvrmpelae dprfgsqerr vgnrdvldai iadrlagldr
      301 dtvlkrldaa diasgrlnpi erlpdheqla grwtrtgtqs gpvstvlppw appgidgygd
      361 vpglgqhtaa vrdwlglnas gaegkdsp
//
LOCUS       WP_181780564             267 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Pseudonocardia pini].
ACCESSION   WP_181780564
VERSION     WP_181780564.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..267
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..267
                     /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=27991
     Region          4..257
                     /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 mepvrqlesl gdqlslytra iawiprtlrr ypkeiarlla evsfgsgali vilgtagvma
       61 alslfvgslv glqgfralds lgvealtgfi tayfttrdia plvaasalta tlgagftaql
      121 gamriseevd alevmavpsv pflvttrvia givavvpmyt igllmsfaaa rinvtvingl
      181 pggtydhyfd lflpvsdila sylkvivfat vvilihchyg yhakggpagv gvavgravrl
      241 sivstaildf fltlvlfgtd tsvrvag
//
LOCUS       WP_181780617             592 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Pseudonocardia pini].
ACCESSION   WP_181780617
VERSION     WP_181780617.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 592)
  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 592)
  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..592
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..592
                     /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=64850
     Region          8..127
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
     Region          177..563
                     /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 mteaavadap qdhadptrva aewlsafera agagdldale rlfvadcwwr dllcvnwdlt
       61 targvasvre sfgkrlaatg frdmvvatdv pagvadgvlt afhefdtaia hgrgvlrlmq
      121 qedgewrawt fltamqdlhg heeqrtsvhd aarekhnqpv eqretwtqyr ererefadse
      181 ptvvvvgagh aglniaarlg hlgvptlvle qtprvgdvwr nryhnlslhd tkwygqmpyl
      241 sypdnwpvfa pkemiadwfe ayawmlqlnv wtnsavqsat ydeaagrwtv tvtrdgetre
      301 lhpkhvvfat gafagapdip elpgvdrfrg iavhssahag grglqgkkvv vvgtgasahd
      361 vaqdacemga dvtmvqrgpt yvissqygvp amhealyses sppveqsdlv alsfpwhlfl
      421 etagpgvqql aeidkelldg lraagfrltd gingsglfgl slirgggyyi dkgcsrliad
      481 grialqhgev erftpdgvvy sdgteapadi vvfatgwpnm rdtirpivgd dladrlttvw
      541 gldeqgeikg vfrpsghprl wfmaggfqqs rygskllalq ikaveeglhe fa
//
LOCUS       WP_181780653             348 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pseudonocardia pini].
ACCESSION   WP_181780653
VERSION     WP_181780653.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 348)
  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 348)
  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..348
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..348
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=36457
     Region          <9..125
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          81..328
                     /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(208,211..212,214,236,239..240,243..244,246..247,268,
                     271..272,275..276,279)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          234..264
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          267..293
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          302..327
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtaqldpdap rpaprgpvlp aaipdprdap vepgpvdpta palttvpggp ptiaeavaea
       61 vaevrpilvp deptptplsd agralleegr aegaleplrr avasaepgga dllvrayldt
      121 gawaavidwl tplvadgrte fagrlgvala efgdlvraed mlrtavahge vaaandlall
      181 lrddrrlvea arvlthaada gdpqapdnlv alhledgdlt gaaeaaerya ddrrpdalva
      241 ladvraaqgr vdeadalyrr gaelgavrah tayagflvar getadaehef reaerhnepg
      301 wpltvgrflv etdrpdvarw yletgvragd reagallael dgvdptdd
//
LOCUS       WP_181780655             309 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Pseudonocardia
            pini].
ACCESSION   WP_181780655
VERSION     WP_181780655.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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..309
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..309
                     /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=34202
     Region          42..290
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mierewrpef rldlpgvlgp lrrgrgdpsw rsvgegagmv taiwrtsttp dgpatvrlar
       61 rtdgtvvakg wgpgaaweld glptllgaad dpesfvahhp liadvarrrp girfpatrrv
      121 wdqlvpaile qkvtgtearr swrelcwrfs dpapgpgelm prgmripptp aqirsvpewe
      181 whkagvdsar rrailaaaav ahrleaavel ggeegrillr kipgigvwta aevaqrswgd
      241 pdavsfgdfh iptvvgwalv grplddagml evlepyrpqr qravryvels gfrrprfgpr
      301 fsprdfram
//
LOCUS       WP_181780849             296 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudonocardia pini].
ACCESSION   WP_181780849
VERSION     WP_181780849.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 296)
  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..296
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..296
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32892
     Region          13..76
                     /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          107..286
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mapqqgpagp rrrlgaelrr lrlkadmtld evaelmtcst skisrletgk gipkmpdvne
       61 liriygvsad aerdmlhrlv regrthgwwe pfvegvqpek fvmdaparyp sleaeatsvs
      121 sfdlaflhgl lqtrdyarav laallphhgr raieklvelr merqraldrp dpmhlqvvld
      181 egilvreagg ravmrrqlev laeqaarpnv dlrvlpfsag ldrahlgefv llgfadpsvs
      241 dvvyvegpsg esyldapadv elyehvfgev aeraldpaas ldrieqhlss pertrs
//
LOCUS       WP_181780854             442 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein, partial
            [Pseudonocardia pini].
ACCESSION   WP_181780854
VERSION     WP_181780854.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 442)
  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 amino end.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         <1..442
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          41..387
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 rrdeggppgt alrplarrvh flaailvapl llllcltgla yvfspqihdd lyakqlyvge
       61 vgevprpvae qiatamarhp eaelrsvvpp qaadrttqvn lstpgqepgt artvyvdpyt
      121 nyvdgeltti ggrlpanvwl refhsnlhlg efgrlyseta aswlpvialg glvlwlvkqg
      181 rkprsaaevl vpkvrgknpq arlksvhgpl glwlagglvv mavtglmmsr fagsglfawr
      241 aprlraapvd vppgpnpvgv dtvlevarsh gldgalqvdv ptapgevftv aqtapglpir
      301 rdtiavdpys aavtehlrws dypflaqvrv lgtslhtgtl fglanqvlla lfaigtivll
      361 vggylmwwkr spyrgqlppa pqaalratpw pwtvvalvva aalawylptf gvtlvlfvaa
      421 dvsigavrri rarskvppaa gr
//
LOCUS       WP_181780425             264 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Pseudonocardia
            pini].
ACCESSION   WP_181780425
VERSION     WP_181780425.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=27353
     Region          5..248
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 malglrsaig sdvgrrrtan edsgaagdrl lvvadgmggh ahgelasalt igamlelder
       61 lpadasgldl laelriavdd asarlaehak rdpdtqgmgt tvvallldgd rlalahvgds
      121 riyrcraggl eqlthdhtmv qqlvdegqit peealvhprr svlmralstd hpvdadvayl
      181 dlvpgdryll csdgatavlp daaildlmaa ptsaevvveq litlsndggg pdnitcivad
      241 vveqesaapq pvrlvgaaae vqtg
//
LOCUS       WP_181780669             132 aa            linear   BCT 28-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Pseudonocardia
            pini].
ACCESSION   WP_181780669
VERSION     WP_181780669.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=14167
     Region          1..132
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mfgitvrdhm mvahsftgev fgpaqrlhga tfvvdatfrr peldaddlvv diglasealk
       61 avlaeltyrn lddvsefagr ntsteflaqv vadrlagria adelgpgarg ltalvvtlhe
      121 shiawasyer sl
//
LOCUS       WP_181780885             207 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudonocardia pini].
ACCESSION   WP_181780885
VERSION     WP_181780885.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15841257
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22366
     Region          31..73
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          94..204
                     /region_name="TetR_C_24"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam17932"
                     /db_xref="CDD:465574"
ORIGIN      
        1 mtkaaakgra vagtrppgrp rkeidpaava eaagrlfssg gyeavsieav aeqlsvsrat
       61 lyrtvptkeh llailferst qrldeqatal vaegrepaae leglvrlhvv aaietrryma
      121 vffggaglpg dvyerwqrfs hdfemlwrgv veramaagvl aagdpvlttr lvlgaviwvs
      181 rwyrpgedys aeqiadaale liahrpg
//
LOCUS       WP_181781207             194 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudonocardia pini].
ACCESSION   WP_181781207
VERSION     WP_181781207.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=20756
     Region          19..>88
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mtnrtavied aasaavaldp vrarllgalr epgsatslaa tlgltrqkvn yhlraleahg
       61 lvelveerrk gnmterllra tagafvispq swalvapdpd repdklsaqw llalaarllr
      121 evarlitaag srrvatfaid geitfataad raaftrelge svrelvarhh aaegrphriv
      181 vavhaamppe etsp
//
LOCUS       WP_181781144             297 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase, partial [Pseudonocardia pini].
ACCESSION   WP_181781144
VERSION     WP_181781144.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 297)
  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 297)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 297)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..>297
                     /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          <180..>297
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtvqgfrera wrgvgpnlvl plvwipialv aarnipnfvp dqrpldavgi alivlgplll
       61 vvrfalprav llgcaavllv ylglgyafgp vvvpslvava qvvaigdrrl aygatvaava
      121 vglllqvtvr ggvvswegtl tllawlsayv agcelwrarq erraqaraar eeterrqage
      181 erlriarelh dvlghhvsli nvqagvalyl idedpeqarr alatikdasg dllremrstl
      241 gvlrgideep praptaglgv ldrlvadnet aglpvdatva apdlpptvdl aayrivq
//
LOCUS       WP_181781210             471 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudonocardia pini].
ACCESSION   WP_181781210
VERSION     WP_181781210.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=49787
     Region          71..463
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mteavdreln gryprldrvs lrarigilaa avaaavvvlv saaaffivrg silatlddnl
       61 eqralaaaqs elarpqllat vpseilgaad irvallyssg laqsaegaas applsesele
      121 vargeidqsv rsaggyrvva vqagegralv iaqkmdstqa vlselatalp vvgaigvvla
      181 gfagaavara glrpvqrlte atervaatgr ltpirvsgsd elarltqsfn emlgalaasq
      241 eqqrrlvada ghelrtplts lrtnlellaa aekpgapslp redredmltd vraqveeltq
      301 ligdltelar ddapnaarep velvdvvera ldrvrrraga digfdvtlvp wtlvgeapal
      361 eravlnlldn avkwsppggl vrlrmirlde wtvvievads gpgiaeedrp hvfdrfyrad
      421 tsrtmpgsgl glaivrqvav rhggavwadr apeggallsl rlpgrpgele l
//
LOCUS       WP_181781142             204 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Pseudonocardia pini].
ACCESSION   WP_181781142
VERSION     WP_181781142.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..204
                     /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=21759
     Region          6..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvglrerkkl etrralswaa irlvvergia gvrvedvaee agvsertfrn yfatladava
       61 drhlerslqi adelrrrpag eplwealrra vetrfglgaa dsapdpvwva gvramvtepg
      121 lhgamqktaa taaetlaaav adrtgtdper dlypklvaaa vgaavgaate hwlradppvp
      181 mgpllveald rlssglpeps eeda
//
LOCUS       WP_181781288             751 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Pseudonocardia pini].
ACCESSION   WP_181781288
VERSION     WP_181781288.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 751)
  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..751
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..751
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81206
     Region          <34..749
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mtsfvgrrte vagvkrslet yrlvtvtgtg gvgktrlarr vaadvggafp dgvwlveldd
       61 ladgpllast vllgiggrdd gvtavddalp aylrdrqall lldgcdrvve acaelverll
      121 qaapgvrvlc ssrrplripg eavvpigpfp appetaaria dpasydavtl fveralavrp
      181 tlrtsaddld liaricrrld glpiaiefaa drldvlslee lgdrlddayr llvtakrgap
      241 erqrtlqalv dsshqlcsep eqllwarlsv ftgrfelpav edvcaddrlp rdavldvvag
      301 lidksvlvrd ehpggswfrl prllrdygal rldeldewdr lrsrhvrwcq wladhaaegl
      361 lttrsdgwmg qvrgnhanvr aaleyclgsp arvqdglrla aalwyywima grvaegrewl
      421 crllraapep ttarasalga aaylaladhg radellaegt alaerlaept vtgelryvag
      481 llelhrgdaa aarthlaval arfreggdgm gtsktlclsa vacvmdaapr eavslcdefl
      541 ampgassenw gfayiqwtra laawreglpt ealglhrqaa alarrfddrf gmgvcvqsaa
      601 vhleaagrhr eaavslgaae vhrvsgfgml ddlrrrcaed vrgalgpvry aelveegrgl
      661 sldravdrlv gqeggaapap lpgtellskr ewevaelvae grsnkeiaaa lvistrtaeg
      721 hvqrilgkle flsraqiasw mteqrvrgat g
//
LOCUS       WP_181781304             256 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pseudonocardia pini].
ACCESSION   WP_181781304
VERSION     WP_181781304.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 256)
  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 256)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 256)
  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..256
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..256
                     /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=27666
     Region          1..256
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          172..254
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtlavqappy eghagddald mwicrfglae pggwglhrhh qhqiawvseg lttavvegrs
       61 wvlpptralf ipahavhdtv nrppsalhcl yvwphacpld wtaptvigvg pllrelllal
      121 sgpalqaved sartllfglv gavpdpgvev rmptdrrarv vaetltadpa dprslddwap
      181 algtsvstlr rafadtgttf tdwrtqvrlr talplladgv pvagvarrvg yaslngfvda
      241 frrqfghtpa ahfrer
//
LOCUS       WP_181781108             272 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Pseudonocardia pini].
ACCESSION   WP_181781108
VERSION     WP_181781108.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 272)
  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 272)
  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..272
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..272
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=29777
     Region          9..241
                     /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 madsrltipa npriavlgds laaglgvren syprllakdl qaeailmkak asrrvdecte
       61 lvprldkfkp dlvlistgqt eslvhpprfv eeaierhgpe nwkgvvglda rpyysedrak
      121 rareiattva kivvknvtir laggyprmph deyrrelttf ldlmeergwp vvvagvgfpn
      181 avlyprskks latveqlqqe liatrpnary lrlnglvdfa rdtladrchp svaghrkiad
      241 ahhalldvvp rvdagpvaaa asngrapsps ah
//
LOCUS       WP_181781464             546 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Pseudonocardia pini].
ACCESSION   WP_181781464
VERSION     WP_181781464.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 546)
  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 546)
  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..546
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..546
                     /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=59556
     Region          7..489
                     /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 msapvdpapd ydvvvvgagf aglyalyalr aeglsvvgfe sgsdvggtwf wnrypgarcd
       61 tesldysysf dkdlqqdwtw seryatqpei lrylnhvadr falrplirfh tevtsavyde
      121 dsatwtvgts tadtvraryv vmaagvlssl keldfpgler frgtrlhtar wphegvdlsg
      181 qrvavigtgs sgvqlvprla pqtahlhvlq rtanfsvpar nrpvlpeeaa rekagyderr
      241 aeirvsragm keipaegsal dhdaaertri fewrwayggg ptflrtftdl aldeqanata
      301 adfvrakire tvadpetads lspkgfpigt krlcvdtdyy atfnrpdvtl vdlrktplve
      361 ftengirtta geieldavvf atgfdaltga itridvrgrg getvaehwad gprtmlgvav
      421 agfpnlftvt gpgspsvlgn vvasieqhve wivdclrhar evgavsveat reaeedwsrq
      481 aaeaaaqtlm arnaswytga nipgkarqll pyaggvgrfr eicddvaarg ypgfhftvpt
      541 ptghqa
//
LOCUS       WP_181781482             124 aa            linear   BCT 28-DEC-2024
DEFINITION  HesB/IscA family protein [Pseudonocardia pini].
ACCESSION   WP_181781482
VERSION     WP_181781482.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 124)
  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..124
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..124
                     /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=13308
     Region          19..124
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
ORIGIN      
        1 mtventveag patteethgv eltdtaafka rslleqegrd dmhlriavqp ggcaglryql
       61 ffddrsldgd lfreynglkv gvdrmsapyl qgavidfvdt iekqgftidn pnaggscacg
      121 dsfn
//
LOCUS       WP_181781492             401 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudonocardia pini].
ACCESSION   WP_181781492
VERSION     WP_181781492.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..401
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42575
     Region          3..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 msetrtgpla gmkvvelaqw vfvpsaaail adlgadvvri ehpvhgdpys alttagskng
       61 asaqsarsaq anrgkrsvgi dlrrpggrel aytlireada fltsfradal drlgmteahl
      121 talnprlvya rgdafgpegd esglpgydit afwarggvga lvtepdatel arqppsfgdr
      181 issvglaagv lasllgrerg hapqpvsasl mgaaawvtas eiithdpeag pgarvtmppl
      241 tgsyrcaggg wimlnlmqsd rywddfckhi gapelrlder fadaaardah aaelrpalaa
      301 vfarrtrdew saafatfdgp wapvqdvtel addpqivang fvrpvpeieg mrlvrtpftv
      361 geapetlprg pelgehtetv lldagvewde ierlkdagvi t
//
LOCUS       WP_181781535             312 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Pseudonocardia pini].
ACCESSION   WP_181781535
VERSION     WP_181781535.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 312)
  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..312
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..312
                     /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=32403
     Region          11..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 mafanrvtql lgveipilqa pmgyiakppl vaavseagam glvpgslgia evredirrtr
       61 dltdkpfgln lplafvkdva ivdmiveegi tfvttsagsp tahtprlkea gltvfhvvps
      121 lrgaqkaida gvdglvvegs egagfkapre vssmvllplv asqvgvpiia aggiadgrsm
      181 aaafalgaeg vqmgtrmvat lesgvhvnmk navvsatetd tmlinkhngk qvrvlrttat
      241 apfelategd pmallgnier lyrdgdvdas laqlgqvagr ieaiepvadv iartvdefte
      301 tlagmakryl ea
//
LOCUS       WP_181781753             284 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Pseudonocardia
            pini].
ACCESSION   WP_181781753
VERSION     WP_181781753.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=30447
     Region          29..281
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msgellvatc wttagdaapl rgderspvpl rtrievaara gfrgfgvtha dlraaltehs
       61 ladlrgilad ngmehrevel ladwwttgpa reasdrvrhe lfeaaealga rlvkiapdvs
      121 gtawererwv aelaalgpaa eahgtrvale flpwsnvadv hqglalveaa ghpavgllvd
      181 awhvgragtp padiaavpld rlfgvelndf ddepvgtlfe dtrdrrrycg egtfdleglv
      241 ralrrtgyag pwgveilsae hrgsdlatav akahdtaadl lrra
//
LOCUS       WP_181781827             150 aa            linear   BCT 28-DEC-2024
DEFINITION  flavodoxin family protein [Pseudonocardia pini].
ACCESSION   WP_181781827
VERSION     WP_181781827.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..150
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=15526
     Region          4..145
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mavllivhht pspacqelld evrrgasdpe itgvevrtra alaatasdll aadavvlgtp
       61 anigtmsgal khffdqvfyv cgedtrglpf glyvhgnqgv egavrdvgri tdamgwtqaa
      121 qtvevmgapd raareacwel gavlaagisp
//
LOCUS       WP_181781574             416 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Pseudonocardia pini].
ACCESSION   WP_181781574
VERSION     WP_181781574.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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 416)
  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..416
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..416
                     /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=45356
     Region          18..409
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(58,65,98..99,106,110,117,240..241,244,248..249,252,
                     285,290..291,294..295,297,320,350..352,355..356,358..360,
                     364)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(65,92,94,97,99..100,180..181,188,239..240,243..244,
                     248,291,294..296,399)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mtvldapalt dpelladpwn afgrlreqap vlrsrfgmgg detplwlvtr yadvkavlad
       61 prfvndaars pagrdtrael maavgvtpdl aeyltksvld fdgadharlr klvsraftvr
      121 rvgdlrprve eiaaglldgl sgevdlvesy ayplpitvic elvgigeedr anwhvwgrel
      181 vsadptripg alratvehir elvarrrvep tedllsgmir aqeedgdrls dfelvtmvla
      241 lvfaghetta hlvansiaal lthpdqldrl qadpslwpta vhelmrlygp vsqvrvryat
      301 eaveiggvvi pagatvqpil lsangdpref ddperfdvtr vpdrgeghvg fghgahyclg
      361 aalarqegev alralftrfp dlrlavapee lvwqpvpgsr rlaalpahlp grimap
//
LOCUS       WP_181781537             249 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein, partial [Pseudonocardia pini].
ACCESSION   WP_181781537
VERSION     WP_181781537.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..249
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         <1..249
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          2..241
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 gevhalvaap agegpfptvf alhggphaad edrfsparaa wvdagfavve vnyrgstgyg
       61 sawrdaiegr pglteladva avhdavvasg ladparcvve gwswggylal laagtqperw
      121 aavlggvpva dylaayedem eqlrafdral fggspdevpe tyrtasplty vgevrapvlv
      181 lagendprcp irqvdnylaa latradlpye varfdaghgs lvvaealrhm ateidfarra
      241 laritlptt
//
LOCUS       WP_181781712             110 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudonocardia pini].
ACCESSION   WP_181781712
VERSION     WP_181781712.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=12458
     Region          3..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maraatttda fnavaeprrr eilevlarge rsvgdlvgel elaqpqvskh lkvlhevglv
       61 avredgrrrl yrlngrglkp ihdwvarfeq hwedrfgvld avleelqeep
//
LOCUS       WP_181781968             844 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Pseudonocardia pini].
ACCESSION   WP_181781968
VERSION     WP_181781968.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=92712
     Region          15..837
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtsalltdrl ppgddpealv etfaewafee rglslypaqe ealleiatgg nvilstptgs
       61 gkslvamaah aaalargart fytapikalv sekffalidv fgadkvgmlt gdaavnegae
      121 iicctaeila nialrqgara dvgsvvmdef hfyadphrgw awqvplvelp qaqfllmsat
      181 lgdtaffrdd ltrrtgretv eitsverpvp lfyryvvtpl hetitellqt heapvyivhf
      241 tqqsaveraq slmsvnvtsk eekaaiaeli gsfrftagfg ktlsrlvrhg igvhhagmlp
      301 ryrrlvetla qagllkvicg tdtlgvginv pirtvlftal akydgvrtrp lkarefhqia
      361 gragragydt lgtvvaeape heienarrla kagddvkkrr rvvrvqapdg fvgwsqtsfe
      421 klqaaqpeal tshfqvtfam ilnvisrpgd aftamrhlle dnheprprqr rhilraiqiy
      481 rallaagive klpapdaegr svrvvgdlql dfalnqplsp falaafelld respsyaldm
      541 vsvveatldd prqvlhaqqn kakgeavaam kadgieyeer malleevtyp kpldellsga
      601 letyrrgapw vedarlspks vvrdmseram tfheyvshyq larseglvlr yladcyralr
      661 qtvpshahte eltdliewlg elvrqvdssl ldewaelaag ggvadetapp sidavgaapa
      721 gvtrnarafr vlvrnalfrr velaslnrwd llgeldsaag wtadrwrsaf epffalhgyg
      781 gigigpdarg pkmidiveep erwlvrqvid dpeddhdwai taevdltasd eageavvwis
      841 gfgd
//
LOCUS       WP_181782074             150 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein, partial [Pseudonocardia pini].
ACCESSION   WP_181782074
VERSION     WP_181782074.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 150)
  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 150)
  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 150)
  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 150)
  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 150)
  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 150)
  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 150)
  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 10588955
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..>150
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          4..141
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
ORIGIN      
        1 mpdllerqdd ldsllgavda vragagrvvl ltgeagigkt alvralraal dpevrvlaga
       61 cddllapral gplrdaahgt ggpleraldt espdavfaaa laqlsrptll vvedvhwadd
      121 atldvlryla rridtvpall lltlrdegag
//
LOCUS       WP_181782186             261 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Pseudonocardia pini].
ACCESSION   WP_181782186
VERSION     WP_181782186.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=26690
     Region          23..244
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mdailratll gvtvspkdaf itvygrkpvl ealaddalav dkvilaegtr gesareiera
       61 aqrrgvpvqr asahrvkvla gngrhdqgvl advvaprmap vsvflsdlga rrpaavlvld
      121 rvtnpsnvgm ilrtatgagl dgvllprrgv paidplvika sagvafsapv lrsgtaeegl
      181 valkeagfgv fgldaggssl laadlpprva lvlgnetdgl sagvralldd vlaiplfagv
      241 eslnvasaaa vaayelhrrr s
//
LOCUS       WP_181781985             366 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudonocardia pini].
ACCESSION   WP_181781985
VERSION     WP_181781985.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 366)
  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 366)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 366)
  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..366
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..366
                     /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=38722
     Region          140..366
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlafipfsal vlaplaglsa palfllqlaa lavvpfvfai gllhggfart apleelglwl
       61 gsvddgrppv rdalaavlgd eslelyfpsg pdgrlldagg rdavperfgs tvsvdaahga
      121 vaviayddal iadpwpvqqa grvvalaler erltvellar rrellesrsr lvqvadeerr
      181 rfaqdlhdll qsrlvlatlr agtlgaapgl daelrqdaea lreelteair elrrlvhgvm
      241 palllerglf aaaedlldrc pipveadwrg ssaelpaavs tgaylilaea tanavkhsra
      301 saitvrvera gdtllldfad dgvgsaaptg aglrgvrdrv dvleghfelv sppgggtrlr
      361 vrlpca
//
LOCUS       WP_181782141             244 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudonocardia pini].
ACCESSION   WP_181782141
VERSION     WP_181782141.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 244)
  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 244)
  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 244)
  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 244)
  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..244
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..244
                     /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=24613
     Region          1..234
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtapaalvtg asrgigalia eklatagwdl tvsarsagpl qeraaalagh ggtvravtad
       61 mgseeevlal adahveafgr vdalvlnagm gsigaiadfp arrfdklyav nvrsafvlvq
      121 rllptlrtsa agergtakvi avssltgvag eplnsaygas kaaltslcet lnteeseggv
      181 tatavcpgyv atdmtaplad qvapeamida advaelvval trlgrsvvvp sipmtrpgph
      241 lwra
//
LOCUS       WP_181782264             250 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pseudonocardia pini].
ACCESSION   WP_181782264
VERSION     WP_181782264.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 250)
  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 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   3  (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   4  (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 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..250
                     /product="helix-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=27181
     Region          74..250
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <179..250
                     /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 mgvtrterew lelvatlfae plvdmpvdri gpmlmttfet agvtfsevep eslrhrwwdg
       61 glgalapdla qwsvhradre hpllrfylat glwtprqvad vpdtfqdrwt adggraland
      121 csaaqqlalp lrataamsrs fvlgrqdpwg pgelafaerl wrllsglekq vsalaavtgg
      181 qgvsaaeipl tpreqavlgl laqgltagti arrlgisprt vqkhlercyl klgvtdrlsa
      241 vlraqalglv
//
LOCUS       WP_181782313             696 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein, partial [Pseudonocardia pini].
ACCESSION   WP_181782313
VERSION     WP_181782313.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 696)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         <1..696
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          <1..692
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 rafadgvrvv elaslrnpal lpqavfdglg ighrdqpdrs avdalvehvr trhmlivldn
       61 cehvrdaaar fvdevlrats rvhflttsre llnlpgerit vlhplaalgp atalfesrar
      121 dvvpgfvvdd tnraavrqvc erldglplai elacarlrvl svheladrls dsiellstrg
      181 rggterhqsl qaamawshel ctreqqllwa rvsifaggfd traaeavcad aalpaavvld
      241 clydlvgksi lqreesrgrv rfriletire fgqamlspae sarlhrrhle wcaglvtesv
      301 rrwfsdeqfa iserlranla nvrtaletal vidrptaael vsapwflwac glsarehamw
      361 ldrvleqels pgrraaalgt vglvrtmqgy rdtaapvvae aldlaraapd ppaeafalda
      421 qglaaffdge hrraetllge slalyetdpq vrgdlpcavr vhlgmllcfe grtgeaqrff
      481 ddvrarceev gerwmlsyai fgqglvavte erhpeaiala reslglkrqf edsvgtplav
      541 ellgwaeaga gsaaraavli gassvlwraf gqqlygsaew marrerfvlr arselgnaaw
      601 etgarrgaam glaelldfal aeeatelrpe sdviavlsrr erevarhiaa grtnreiaaa
      661 lvlshrtveg hvehilqklr lqnrnqvava llsdqk
//
LOCUS       WP_181782320             293 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase family protein
            [Cytobacillus].
ACCESSION   WP_181782320
VERSION     WP_181782320.1
KEYWORDS    RefSeq.
SOURCE      Cytobacillus
  ORGANISM  Cytobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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..293
                     /organism="Cytobacillus"
                     /db_xref="taxon:2675230"
     Protein         1..293
                     /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=33478
     Region          16..291
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mikdgfflek iqvegpynfd lvlnrlsndp lnsvdigsrs vkvpmmlshq pvvaevkaig
       61 ttdkpeffit gtdgplkeka aerlseifqw hlplerihkh fqntelqpif dahygtpivl
      121 dfdpyscilk ciihqqlnla fahtlterfv kafgferdgv wfyplpekva elkvedlrel
      181 qfsgrkaeyv igiaketasg klnfdelksl sdeeiydkli klrgvgpwtv qnflmfglgr
      241 pnlfpaadig iqnalkklyk leakptleem etfskswspy lsyaslylwr sie
//
LOCUS       WP_181782475              43 aa            linear   BCT 28-DEC-2024
DEFINITION  FmdB family zinc ribbon protein, partial [Pseudonocardia pini].
ACCESSION   WP_181782475
VERSION     WP_181782475.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 43)
  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 10560705
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..43
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..>43
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
     Region          1..43
                     /region_name="Zn-ribbon_8"
                     /note="Zinc ribbon domain; pfam09723"
                     /db_xref="CDD:462856"
ORIGIN      
        1 mpryefrcre carrggratf evdrpmaaas dpadcpqgha dtv
//
LOCUS       WP_181782654             285 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein, partial [Pseudonocardia
            pini].
ACCESSION   WP_181782654
VERSION     WP_181782654.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 285)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         <1..285
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
     Region          <7..285
                     /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 wraggapgle grvhctisaf gagpvdgrpv tdpdsedllv qalsgnmdlt gfeggppces
       61 gipiadlgtg vyaaigvlag vvsggarrie vakidvaval lsymavgyfa dgevparvgt
      121 ghstifpyns feaadgevvv apftarfwrn fatatgradl agddryrsfa rrlrakeell
      181 aefvpilrer tveewvstfa aadvpagpvl tlagalsleh tvtrgmtasv aapdgaavpt
      241 vaspfhlhgp dgtrfrpapg avpergadta avlaglttdd ertar
//
LOCUS       WP_181782639             118 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Pseudonocardia pini].
ACCESSION   WP_181782639
VERSION     WP_181782639.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=12553
     Region          19..94
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(23..24,26,29,32..33,36..37,40,70,89..90,92..94,
                     96..98)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(24..25,29..31,44..46,55..58,60..61,64..65,67..68,
                     74..76,81..83)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(44,47,89)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mhegipdfam pseqqvrraa dslrlladpt rikilwallq getsvaclae lvgaaptavs
       61 qhlaklrlag lvegrregtf vyytaesahv ralltealgq artaappqls rtpsatpr
//
LOCUS       WP_181782735             692 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA-transferase family protein, partial [Pseudonocardia
            pini].
ACCESSION   WP_181782735
VERSION     WP_181782735.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 692)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..>692
                     /product="CaiB/BaiF CoA-transferase family protein"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
     Region          6..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"
     Region          398..>692
                     /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 mdvetplagv rvleagdtpa layagrllad lgaevvvveg aegsplrtlg pfaggvpdae
       61 rsasfayfha gkhsvrhtda etaalaarad vvlrstrdgh ellsdaever lqradpgliv
      121 ldvssfgrvg tgsgpypsde llalaaagll avnsttltgp dpeplryrge lssmhaacga
      181 viavlgalfe rrrsghgqri dvsqqaavas vlatalsrwa ytgsmpvrqg nrsvgpwgfy
      241 evkdgrvlmq itrdeefrrl vhllgdpdwg aielfettag rdenhdvldv fvresladft
      301 lrefldlayt hriaacpihg ardilewdhl aarsslppva fekapdesvp vpcrpwrfgg
      361 avppargpap algssdpstl wttaaertpv aptdspvpgp lagvrvvdlt vvwagpfsam
      421 qlahlgadvi kvesatrlet trglgpyade ivgfnrsgyf nqnnqgkrsv alnlktergr
      481 ellrdliaea dvvidnmsag algrmgfpfq rlveinpriv avsmtgfges gpysghtayg
      541 slidalcgia tsngavrggp tdlvmslpdp magittaiat igalyraqat gepvrvetam
      601 feaclsafpw pvlyagatgg evpvihnrde lrsphgtfrc rdedtwvavs vaddaafaal
      661 advigepgla adprfatlaa rrlhedelea av
//
LOCUS       WP_181782647             567 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Pseudonocardia pini].
ACCESSION   WP_181782647
VERSION     WP_181782647.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 567)
  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..567
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..567
                     /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=60959
     Region          3..567
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 maeydlvvrg gtvvdgnggp prtadvavsg driaevgrva gtgrreisad gavvapgfvd
       61 vhthydgqat wesrlqpssw hgvttvvagn cgvgfapalp ehrdrlidlm egvedipgia
      121 lheglpwtwl sfpeyldvle arhydvdlav qvphaalrvh amgeraaahe eatpdevalm
      181 aklaaeavra galgfstsrt lnhksidgel ipsyglgaae lvaighavge tgtgvlqlvs
      241 dfpeperefa lirelaeaag rplsfslnqf pldperhrtv lrlleqavad gleiraqvaa
      301 rpvglilgle ntlnpfmtnp vwrriadltp geqaarmrep glraeileaq treknrsrlg
      361 gnlihkyelm yeledppnye ppvstsvaar aaaqgrdpve laydivaggg mlyvvsanya
      421 dgdldavrem lvhpdtipgl sdggahvgti cdgsfpttll ahwtrdrage ripleyivrq
      481 qsrdtaravg ltdrgvlepg lradltvidm aalrlrrpem radlpaggrr llqraegyvh
      541 tvvagqetya dgvetealpg rllrgar
//
LOCUS       WP_181782775             711 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Pseudonocardia pini].
ACCESSION   WP_181782775
VERSION     WP_181782775.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=74745
     Region          38..710
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mprvlsdaag rlrlgvpelt grvslavave davdvvggvr qvhayprtgs vvvwydatrc
       61 drrelleald kglgadpeat aertprsadv rngdlvrlvv ggaalaalgv rrfglrrppm
      121 lgptsrtvat gvtiftgypf lrgalrslgg grgagtdalv saatvaslvl renvvaltvl
      181 wllnigeylq dltlrrsrra isdlltgaqt rtwtrladgt evevdidavs lgdevvvheh
      241 vvlpvdgevv dgdgivdqaa itgeqlpvsv gpgvrlhags vllrgrivvr atavgrdtai
      301 griisrvesa qddrapiqtv genfsrrfvp asfalsaltl lvtrdvrram tmllvacpca
      361 vglstptais gaigngarrg ilikggahle aagrvdaivf dktgtltlgr pvvtnvisfd
      421 dgwspeqvla yaasseihsr hplaqavirs teerrieipp heecevilgl gmrvrsdgrt
      481 mligsrellr tqkvpvsraa sgwvtrlqka aetplllavd grlvglvslr dtvraesrev
      541 laalradgvr rivlltgdnp htaaavaael gidefraqvm peekqdvvra lqaeghtvam
      601 igdgtndapa laladigiam gvggtdvave tadvalagdd lrtlldlrdl grrtitlirq
      661 nygmsiavna aglavsaaga lspvvaavlh nassvavvgn ssrlirytlr p
//
LOCUS       WP_181782270             506 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Pseudonocardia pini].
ACCESSION   WP_181782270
VERSION     WP_181782270.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 506)
  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 506)
  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 506)
  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 506)
  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..506
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..506
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=54084
     Region          1..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 mtattvrhfp mlvggeqvdg enlleirdpq ngelmataaa ggakeidaav daaktsfaag
       61 ewsratpahr aqvlnavadk lgeqldelve leimangati rqatgfhvgy aaphlaffad
      121 laakyefetp mpratfpvlg qstmrrepig vcgaiapwnf plllalwkfa palavgnsvv
      181 vkpdektplt tlefgriaee cglpkgvfnv vpgpgpeaga rlashpdvgk igftgstdig
      241 revmrlaagt vksvtlelgg kspalvleda didlavdgvl ygcmlysgqi cesmtrlllp
      301 esihdefver lvarastiql gdtrdwetdm gpvvsakqhe rilgyiasgk degatlalgg
      361 gvpkgeqfer gywieptift gvrndmriar eeifgpvlsv isygseregi elandtpygl
      421 assvwssdns halevaekiq agsvwindsh qincevpfgg ykqsgvgrel gphaldpyte
      481 vknvhldlsg rrdarpydvl lshadd
//
LOCUS       WP_181782733             463 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Pseudonocardia pini].
ACCESSION   WP_181782733
VERSION     WP_181782733.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 463)
  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 463)
  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 463)
  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 463)
  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 463)
  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 463)
  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 463)
  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..463
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..463
                     /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=47922
     Region          19..420
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mrtsgaettt snghrpavwv vwgaavlvyl fgvtqrtslg aagldaadrf gidpgtlslf
       61 vflqisvyaa gqipagmmvd rygprvmllv gglllglgqg llafattlpl algarvlvga
      121 gdavafssam vlvarwfpar rvpvatqvtt ivgqlgqvls alplllllha agwstaftva
      181 agasvvsavv aaalvrngpv gwhpprpapa relvrqvgev wrrpgtrlgf fghlgtqfsm
      241 mtfsllwglp ylvsaqgvep lvagalmtll viasvvvgpl vgvltarhpm rrswillgvi
      301 gltagtwtvv lalpgpaptw llvvlvvvla vggpasvvgf diarttnpgg nlavaqgmvn
      361 iagysasvvv lmvmgavlta tggftaegfr tawlvqypvw afavvgilvt rrkarrvage
      421 agpdggtsgp arrrespsap rrrdarrave pagrlvgrse rta
//
LOCUS       WP_181782996             278 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Pseudonocardia pini].
ACCESSION   WP_181782996
VERSION     WP_181782996.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..278
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..278
                     /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=30910
     Region          10..163
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mttvehptnq hydldprvfg lfldesrkys agyydtgtes ladaqrrkmn lvadlvhvdd
       61 rsrvldvgsg wgalvlhlag vrgctvtgis paprqrefve grarrrglan rvrmvtspfe
      121 taeelprgld avtalgsvvh msdlpavfak argllrrdgr myvsescfrn qairarfdrv
      181 dgtdfvreai fgngelrpls elvaaaedag fsvettvdlt rhyhrtieqw ienvqanaaa
      241 lnriqpgiaa rlehyldvsn tgwgyttkhy alvlrnar
//
LOCUS       WP_181782961             144 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Pseudonocardia pini].
ACCESSION   WP_181782961
VERSION     WP_181782961.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 144)
  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..144
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..144
                     /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=15056
     Region          2..132
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrlststdla lrilmrlava pphtelttrq vadgvaitys havkvvarlq klgvvdarrg
       61 rggglalsea grtaslgala rtlegvgdvv gceddppcpl rhactlrgll rqaqeafyrt
      121 ldpvtvgdli hndlsaallg arps
//
LOCUS       WP_181782869             311 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA desaturase [Pseudonocardia pini].
ACCESSION   WP_181782869
VERSION     WP_181782869.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 311)
  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 311)
  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..311
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..311
                     /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=34807
     Region          7..301
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mtvaeprrkt isspyihrlq rrhfllfdia pilgtvaava flwvhpfgwt elglllgfwl
       61 ltglgvtvgy hrlfthrtfk atpaveavla vlgsmagqga viswvalhrr hhefsdkegd
      121 phspnlsggg lrgalkglah shflwmrrhe ypnvvhyapd lirnrrlvkv grlyywwval
      181 glavpalvgg lvdlswqgav sgllwgglvr ifvlehivwa insflhrvgt rpyesrensr
      241 nggifalvtl geswhnnhha fpespsfgld wyrldpgfwl iktlaaagla wdlktpsder
      301 rdsrrvrpag a
//
LOCUS       WP_181783222             437 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Pseudonocardia pini].
ACCESSION   WP_181783222
VERSION     WP_181783222.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..437
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..437
                     /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=46628
     Region          17..390
                     /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 mtitaehapv patgpapgsa ttelraltgl rivaaawvvl fhfhftalpg valvvaalgp
       61 vvtsgalgvd lffvlsgfvi aytyleklgp kmtaeqtgrf vwaracriwp ayalvfhmfg
      121 iwlvaravyg sdpdiafqat qptlsagewv eqlfmvqlwd qpyfdgaswv gstwsisaew
      181 layllfpgva lvfhrmrnlp fvvlaggava lmapiavayl qtgspyypws wlvrilcgfg
      241 ggilaylavr klratdarvr rgaswvatat pvaivaglma gelvgpgrgg avillfpllv
      301 gslaladgga arwlstpamv lggrisyaly lihipmfevy wlamaylpel vgstvlahla
      361 glsmlvatvp aawllyrwve eparvamkkv peflhlpfpa apakhepale llsagpitpp
      421 peptppadpn vravpsa
//
LOCUS       WP_181783242             147 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Pseudonocardia pini].
ACCESSION   WP_181783242
VERSION     WP_181783242.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..147
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..147
                     /product="YybH family protein"
                     /calculated_mol_wt=15775
     Region          14..146
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtvhspaptv sdptdhtadv aairqvvadv etgmntndpe lltrhfaana vavgvngrpn
       61 vglaalreah taavgpggfl rdqyvryeva dvtfvrpdva larklarait edgepidldh
      121 amsalyvlvk eqerwwvvar qntlips
//
LOCUS       WP_181783300             132 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Pseudonocardia
            pini].
ACCESSION   WP_181783300
VERSION     WP_181783300.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..132
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14824
     Region          9..115
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msqrntrvph ealgeicpln evldrvsgkw aigvltltga egvvrfteye rgipdisrrm
       61 ltltlrnler dglltrtvyp tvppkteyrl teaaheltet lslltdwakr hqahvhvsrt
      121 eydathaapr ps
//
LOCUS       WP_181783298             126 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter ATP-binding protein, partial [Pseudonocardia pini].
ACCESSION   WP_181783298
VERSION     WP_181783298.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   ter Beek,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 126)
  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 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..>126
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /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]"
     Region          9..>112
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mteqtppgpa lvvrglrkty eagtapvral rgvdltvrag efvalmgpsg cgkstllhll
       61 agldrpdegt vavdgtried lapqrlarlr rrsvglvfqf fhliehmsal envalaalva
      121 garpne
//
LOCUS       WP_181783318             216 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Pseudonocardia
            pini].
ACCESSION   WP_181783318
VERSION     WP_181783318.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 216)
  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..216
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..216
                     /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=22782
     Region          1..167
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mvdvwwarpv dpagaphlla lldaherari drfrrpadqa rylgahalar lvlgsrlgld
       61 paavvidrtc rcgeqhgkpr vpglefslth sgdrvgvavs aagpvgldve elrdlaaldg
      121 laehalspae prppdghafl rvwtrkeall katgeglssp mnaitlagar vvswsagpaq
      181 awlvdlhagp dhpaalaglg teppevrvhe gdpllh
//
LOCUS       WP_181783408             400 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudonocardia pini].
ACCESSION   WP_181783408
VERSION     WP_181783408.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..400
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42591
     Region          4..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 mdsaephlpl agvrvldast viaaplaaml lgdlgaevik iehpthgdpa rhhgydrdgv
       61 plwwlmlgrn kksvtlylgs eegqeifrsl aatadvvven frpgtmerwg lgyeqlaaen
      121 pglvvahvsg fgrrgplvdd pgfgtmgetm sgfafrngdp tsephlppfg ladgvtgiat
      181 algimtalfe rsasgrgqev dlsiiepllt llepqlvtqd qlgrtlhrtg nqaemnaprg
      241 myrtkdeawv alsastagta tsvvrlmgap elaeepwfah asgrrahtdt idaaivpwfa
      301 artaeqavad craagvpvap vhsaadilqd pqyeaigsig tfdhpvlgpv rmpdvmfrls
      361 rtpgavrwlg telgrdtdev ltglgvtter larlraakvv
//
LOCUS       WP_181783409             419 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein, partial [Pseudonocardia
            pini].
ACCESSION   WP_181783409
VERSION     WP_181783409.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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 419)
  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 419)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         <1..419
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
     Region          1..419
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 rgtpakrrge ilwaisdlvl ahadelarie vldngmpiam arglldgvve gfryfagact
       61 rlhgrtadmg edleyhafav sepvgvaglv vpwngplasl gnklapalaa gcsvvvkpae
      121 qtslstlrla elvleagvpp gvvnvvtgtg paagaalvhh ddvdkisftg slevgrgiva
      181 asagnlkrvt lelggkspvf vfddadldaa vpvvgagifa nsgqvcfags rvyaqpgivd
      241 dlvaglveha kglrvgngld agtqigplis erqrarvldy vasglaegge vvtggvasgg
      301 vgyfveptif tgtradmriv reeifgpvlt vmpfggldel pgignagpyg lgaglftrdl
      361 gvahravrll dagnvwvncy grrdrslpfg gfkqsgwgre ngpegldayl ekksvylhl
//
LOCUS       WP_181783345             278 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Pseudonocardia pini].
ACCESSION   WP_181783345
VERSION     WP_181783345.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 278)
  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 278)
  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 278)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..278
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..278
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30183
     Region          9..268
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mtgnrpdtvv lvhglwmtpr swehwvshye akgltvlapg ypgfeievea lrenpqliad
       61 ltvpatvdhl asvvealdap piiighsfgg tltqlllarg lgaagvvids aptegvrvnp
      121 vsqarslfpa lknpanrhra vgftpeefhy aftntlsaee sravwdryai papgfwvwey
      181 glfanfkpgh qdtwvdysad rapllfiage qdhimppsvn rsnakhyaes paltdyvele
      241 grdhwtcaap gweavadral awalehaapl gstapaeg
//
LOCUS       WP_181783316             169 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Pseudonocardia pini].
ACCESSION   WP_181783316
VERSION     WP_181783316.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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 169)
  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 169)
  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 169)
  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..169
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..169
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18630
     Region          19..169
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mldpplgpyd hvqghadapl tllkygdfec pycrdaapvi ekvreelgdr lrfafrhfpl
       61 hdlhphalaa atasemagle grfwpmhasl yapgpprltq adlrehavna gvdpekvvwp
      121 rtrvvedrve adfnsgvrsg vrgtptlyvn gevyqgpvtv erlvdalte
//
LOCUS       WP_181783577             538 aa            linear   BCT 28-DEC-2024
DEFINITION  class I adenylate-forming enzyme family protein [Pseudonocardia
            pini].
ACCESSION   WP_181783577
VERSION     WP_181783577.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 538)
  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 538)
  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
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..538
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=57718
     Region          8..538
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnypevpvga vlagaarrwt drvalhygdr eltytalyer acafahalre qgirpgdvva
       61 ihlpncpqya iayygiqlag atftpanpll pppdlaaqla dsgavaivsw eqasaavpre
      121 glrfalvtnr eqgldpsvrl pgqdfeefha gspttppeve idlaglahla ytggttgrsk
      181 gvmlphrnvv tnvlqyaclg tgtrpaldde ggivlvdqgp pedypvrlge svvvnitpwf
      241 hamgtvggln ipllsgttsv lherfdpaay ladaerfrvt slggapplya allrhpdldg
      301 rdlssvrslt sgaaplavem iealhrrlgs dvvvvegygl tevtmgatqn ptarsaerrq
      361 gtvglpvpdt evrvvdaegn pvptgepgev cirgpqvmtg ykdrpeetaa tlrdgwlhsg
      421 digvldadgy lrivdrtkdm llykgynvyp releellfrq dgvvgaavvg rpdpevgela
      481 vafvvapgrs redaeairet vnaqvlpykr ireirlvaei pvsaagkvlk relrellr
//
LOCUS       WP_181783728             255 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudonocardia pini].
ACCESSION   WP_181783728
VERSION     WP_181783728.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26656
     Region          5..253
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msgeldgqva lvtgassglg rrfaavlaea gaavavagrr lerleelake ieaaggralp
       61 vqldvadaga ipgavdavea glgpvdilvn nagipdakra hrmplevvda vlatnvrgpw
      121 qlstevarrs iaaerpariv nissmgahdy ghggaaglys vskaaierms evhavewaky
      181 rinvnaiapg afltemmegm igrlktseqe maeawprhrf prpelldstl lylcspasea
      241 vtgtvvkvdd gqhgr
//
LOCUS       WP_181781868             266 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Pseudonocardia pini].
ACCESSION   WP_181781868
VERSION     WP_181781868.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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 266)
  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 266)
  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..266
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..266
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29216
     Region          8..257
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mtdewgihrl dlaaylarig ctatddlarl hrahvaaipf enldvvlgrg idpdleavqd
       61 klvrrrrggy cyehatlfga alerlgypvl rllsrvggdg tvptprthmv laveaagerw
      121 fadvgfgsgv ltpipwrsda vehqgdwlvg lqlgadgetw elwertpegg ravlhrvtee
      181 pqhaadvrma nhftatypss pfvrqvvair kdehtrwtla grelttarpd gteekrtlsg
      241 eevaaaleed fritltaadr aavasl
//
LOCUS       WP_181783825             157 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Pseudonocardia pini].
ACCESSION   WP_181783825
VERSION     WP_181783825.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..157
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..>157
                     /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          1..>142
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mpevvivggg legcatawal tqrgitdvvi verdtvgsgg tgkssgivrc hygvsslaam
       61 atqalevfen aaevlgadig fhqtgyvvgv gpenvaalha smadqravgv rtedisadev
      121 qrlwpvadle pfgafaweer gamtwsltvp ltgvlvg
//
LOCUS       WP_181783886             651 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudonocardia pini].
ACCESSION   WP_181783886
VERSION     WP_181783886.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..651
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=72428
     Region          <47..>453
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          292..651
                     /region_name="COG4867"
                     /note="Uncharacterized conserved protein, contains von
                     Willebrand factor type A (vWFA) domain [Function unknown]"
                     /db_xref="CDD:443895"
ORIGIN      
        1 madprrrrrr yaygpyaggp dplappfdir samdqigrdv megssprqal qellrrgleg
       61 rrglddltrq vwqrrrdlqr dnrldgtlqe vrellarald aereslghed sddarfremq
      121 ldalpndtgg avrelneydw rssearqaye dirdllgrem ldqrfqgmkq amenatpedv
      181 erinemltdl ndllanhaqg qdtteqfaef mqkhgdffpe npqntdelad ilaqrsaaaq
      241 rmlnsmsaeq raelmelsqq afgdprlaqq marldaqlqa mrpgedwqgs grfrgdnpmg
      301 mgeatralee lgqldslaeq lsqsypgarl ddidlealte mvgeqagvda rtlaqlerel
      361 qrqglferaa dgslllspka lrrlgqsilr dvaeqlsgrt gqrdtrraga agdatgqtrp
      421 wafgdteaws vprtmlnaql rrasgdsral dvtdveivet eqrtraavsl lvdtswsmva
      481 egrwvpmkrt alalhqlvst rfrgdalqlv tfgrhaqsve lgelvglega yaqgtnlhha
      541 lllagqhlrk nsdaipvvlv vtdgeptahl epdgeayfdy ppsphtlrat igeldrlsgl
      601 katftffvlg ddprlaafmd dvahrvggrv vtpsldglga evvadylkrr s
//
LOCUS       WP_181784149             192 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase, partial [Pseudonocardia pini].
ACCESSION   WP_181784149
VERSION     WP_181784149.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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 192)
  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 192)
  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 192)
  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..192
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..>192
                     /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          7..>192
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 maiittvadp adprlddyrd lttadrrpdr pggrglviae gvvvvrrlld spypvrsllg
       61 vprrieelsa elahldvpay aadadtmatt vgfhlnrgvl avadraapvd aatlarsarv
      121 lavceavndh enlgslfrna aalgvdgill gprcadplyr rsvrvsmghv lrvpfahlpd
      181 pwpdslellr ga
//
LOCUS       WP_181784172             212 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase, partial [Pseudonocardia
            pini].
ACCESSION   WP_181784172
VERSION     WP_181784172.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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 212)
  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 212)
  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 212)
  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 212)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         <1..212
                     /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]"
     Region          2..202
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 yresgvavev lpadltepaq larvgrrlad pdvapvdllv nnagmgqrgs flttsvddlq
       61 rqhdlnvtsv lrlthavlpg midrgrgavv nvssvagflp gsgstytadk awvtaftegv
      121 aasltgtgvk alalcpgfvr tefheragid pgsrtgplwl daarvvddcl adlaggrvvs
      181 vpslqykais svvgvlprrf vrrlvatfdr er
//
LOCUS       WP_181783524             143 aa            linear   BCT 28-DEC-2024
DEFINITION  VOC family protein [Pseudonocardia pini].
ACCESSION   WP_181783524
VERSION     WP_181783524.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 143)
  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 143)
  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..143
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..143
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15445
     Region          6..125
                     /region_name="PhnB"
                     /note="Zn-dependent glyoxalase, PhnB family [Energy
                     production and conversion]; COG2764"
                     /db_xref="CDD:442048"
ORIGIN      
        1 mtrieqlypr lpvrgadaai afyrdafgad lveryaaptg evvhallrag dvvwavkdgd
       61 eydpapsegg gsailalyva dadavgaale kagatvrfpi sdqpygergg rftdpyghqw
      121 mvaqrtedlt peeveertra mfe
//
LOCUS       WP_181784225             652 aa            linear   BCT 28-DEC-2024
DEFINITION  M13 family metallopeptidase [Pseudonocardia pini].
ACCESSION   WP_181784225
VERSION     WP_181784225.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 652)
  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 652)
  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..652
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..652
                     /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=71968
     Region          4..652
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mtiaddrtrs gldlrwvdta trpqddlfth vngkwlaghv ipddraqdga frdlrdraee
       61 dvraivegaa aaegpearqi adlyaafmdt erieeqgtap lqpllaeiaa atdkaelaav
      121 lgarqrqgra alfgafvgtd akdssrylvh lsqaglglpd esyyreeqya eiraaylthl
      181 arlaslvgle dvsatvmdle tqlaaiswdr vtnrdaekty tlmtwpavqa napefdwapw
      241 yaalrapegs fdevvvrqpa fvlaaarlwr dlpleqwkaw lsvrvasaca dylsdavvee
      301 dfdfygrtls gtpalrerwk rgvsvvegav geavgklyvq rhfpassker mvelvanlve
      361 ayrqsistld wmspetrera leklgkfrpk igypdrwrdy stlsvsaddl lgtmlraaew
      421 dfdfdlarig gpvdkdewlm tpqtvnayyh prmneivfpa ailqppffdp eaddaanygg
      481 igavigheig hgfddqgsry dgdgnmtdww etadraefdq rskalidqys glspaglpeh
      541 kvngaltvge nigdlgglti aikaykiata gsdapvldgf tglqrvlvgw aqvwraatrd
      601 aeavrrlavd phsppdlrcn avvtnldafh eafsvaesda lytapearvr iw
//
LOCUS       WP_181784239             147 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Pseudonocardia pini].
ACCESSION   WP_181784239
VERSION     WP_181784239.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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=15940
     Region          3..125
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 msapathrte ltvrgyeida lghvrhtvyl dyaeharwea laaaglsapt llqhaimpim
       61 lettisyrre lryddvvavg cefewgtgkt aritqpltrv edgtvaaevr svsglldltt
      121 rtlvadpldr lcalatdpev lglgrva
//
LOCUS       WP_181783888             345 aa            linear   BCT 28-DEC-2024
DEFINITION  adenosine deaminase family protein [Pseudonocardia pini].
ACCESSION   WP_181783888
VERSION     WP_181783888.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 345)
  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..345
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..345
                     /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=37702
     Region          11..335
                     /region_name="Add"
                     /note="Adenosine deaminase [Nucleotide transport and
                     metabolism]; COG1816"
                     /db_xref="CDD:441421"
ORIGIN      
        1 mnladylrll pkvelhchfv atirpttlie larakdvplp sydpeilfgy ddivdflvaf
       61 eaanhvftdk gvfervayes vedavaagnl rhreyfvnad lfpigygevl damvaglsaa
      121 erdfgvgfgi ipaiarqrtp adavalvrtv lddgrpevvg igqdylttdd tespelwtea
      181 ydlakrhgln rtahvaeipg stadavtial eqldcsridh gyhvmddpav vevarelqvp
      241 ftctpystqv lsgwemtpeh pvarmiragl nvtlstddpt ffrtdigrey aealpamgfg
      301 aadgariala gveatwlpqd rkdrlraeft aqiraldaal gstrn
//
LOCUS       WP_181784301             146 aa            linear   BCT 28-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein, partial
            [Pseudonocardia pini].
ACCESSION   WP_181784301
VERSION     WP_181784301.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 146)
  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 146)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         <1..146
                     /product="transglutaminase-like domain-containing protein"
     Region          <1..97
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 aaaelcrrih ddfdyvsgst tvrstvtdll tggegvcqdf ahlavaglrs rglparyvsg
       61 yletlpppgk pklrgvdash awvsvwtgdg wldldptndr vvdeqfvvla hgrdygdvpp
      121 lkgviftdsa ksvmavsvdm erlsag
//
LOCUS       WP_181784506             438 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Pseudonocardia pini].
ACCESSION   WP_181784506
VERSION     WP_181784506.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 438)
  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 438)
  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..438
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..438
                     /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=48433
     Region          1..435
                     /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 msdiprrtvs rtaklaglpl gvagraaagw grrlaggdrd qisaqmmaks aeqlfavlge
       61 lkggamkfgq alsvfeaavp eemaepyrea ltklqtaapp mpsadvhrml aeqfgrgwra
      121 rfrefdeepa aaasigqvhr avwrdgreva vkvqypgaee avlsdlrqls rmsrllqpla
      181 pgmeikplit elkermveel dyrdeaenqr afaaeyaddp eirvprvvas apramvsewv
      241 tgrrlsdvir ngtqeerdra gallagfhys apyrvhllhs dphpgnfqil ddgrmlvvdf
      301 gavarlpegl prplttmtky alenrpadli allrsagflq pgtevaaeev laylspftep
      361 lrterfrfsr swlqgqaerv gdlrspefdt grslnlppqy llihrvtlgt lgvlcqlqad
      421 vplreivgrw qpdlfvag
//
LOCUS       WP_181784687             251 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Pseudonocardia pini].
ACCESSION   WP_181784687
VERSION     WP_181784687.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 251)
  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 251)
  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 251)
  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 251)
  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..251
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..251
                     /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=26064
     Region          1..248
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mndltglvav vtggnggigl gmatgiakag gsvalwardt aksadaveal tdlgaraiav
       61 scdvadedqv aeamdrtvae lgplgclvsn agtsdrtsvv dlsletwrqv havnldgafl
      121 tcreaarrfv dqgsggsiiv vgstisrfgg agqaayassk tallgltrtl avelarhrvr
      181 cntlipgwtr tglsergyqd erfrqattar tpvrrwadpa eygqvaayla dpsltfhtgd
      241 evvvdggyci f
//
LOCUS       WP_181784845             361 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein, partial [Pseudonocardia pini].
ACCESSION   WP_181784845
VERSION     WP_181784845.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     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]"
     Region          48..340
                     /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 mrdrprrptv dpqvigalrm pdnperplva llkrvavafg allaaalivy igrdgyvdnn
       61 gegdisfnda lyyatvslst tgygdivpft atarllttvv itplrllfli vlvgttvell
      121 tersrqsfri qrwrqrvrhh tvivgygtkg raavetllgd gvepeqivvv dtdrtqldaa
      181 salglvtvtg natrsavlri agahhataii vatnrddttv lvtltarela pktrivaavr
      241 esenvhlvrq sgadsvivsa etagrllgva trtpsvvevi edlltpeagf aiseravepd
      301 evggsprhla divlgvvrde klyrvdasav dalergdrll yvrkatpade dragpgrtar
      361 r
//
LOCUS       WP_181784869             214 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Pseudonocardia
            pini].
ACCESSION   WP_181784869
VERSION     WP_181784869.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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..214
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..214
                     /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=22377
     Region          6..208
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mtimdlpaga npalhdlarw igtwvftpay rvqvhhperi ppegavvlva nhsamvdgpl
       61 lfgllgrrsv flvkqemftg vlgkglrgig qlavrrgepd rapltaalgv lrggglvgvf
      121 pegtrgtgdv raaqqgaawl srtsgacvlp vvcrgtrrpe gsgprlrprv dvlvgeplpa
      181 ptgkgraela aatetirgal aalvtelddv rsrt
//
LOCUS       WP_181784943             112 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor, partial
            [Pseudonocardia pini].
ACCESSION   WP_181784943
VERSION     WP_181784943.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 112)
  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 112)
  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 112)
  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 112)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 112)
  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 112)
  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 112)
  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..112
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..>112
                     /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          5..>112
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mpdrlrvlav ddvapalael trllaasscv revvpaadal salkllkdtr fdavfldiam
       61 pgmdglelag llarmtdppe lvfvtafeeh avsaygvgal dyvlkpvaae rl
//
LOCUS       WP_181785195             416 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Streptomyces
            phytophilus].
ACCESSION   WP_181785195
VERSION     WP_181785195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 416)
  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 416)
  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 416)
  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..416
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..416
                     /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=45592
     Region          19..415
                     /region_name="RsbU"
                     /note="Phosphoserine phosphatase RsbU, regulator of sigma
                     subunit [Signal transduction mechanisms, Transcription];
                     COG2208"
                     /db_xref="CDD:441810"
ORIGIN      
        1 mtsqidykal fmaapnpnlv lgpdlvivdv neaylqatgr tradligqym fdafpsnpad
       61 phatgmqdld aslhrilrtk tpdtmaltky diprpgrpgt feerwwspin tpvlgpdgqv
      121 awiihrvedv tpfilaraaq pddnddrdra lgereamdae lyvrarelqr lneelrraha
      181 rerqvavtlq etmlrspdla hhqhitvryl pasgslnvcg dwydvidlpd ngfavavgdv
      241 vghglqaaat mgmlrsalsa gvralrepgk aldlldlysy avegalatta vkavidperr
      301 rityssaghl ppvllhpdgt cdlldkstdp plgtrprhip rphaslpyrt gdtlvlytdg
      361 lierrgedid aglhrltdtl arystaater ladsllarlg vaggarddia liivrl
//
LOCUS       WP_181785280             133 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces phytophilus].
ACCESSION   WP_181785280
VERSION     WP_181785280.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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 phytophilus"
                     /db_xref="taxon:722715"
     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=14538
     Region          20..109
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 marpaklrva vsdpaqwige rerarmlapk lraladetrl mlilliaqrp rtvkelqeat
       61 glsqtlvshh laplreqelv eavpkgrsnq yvmccqtlae plrmfaslaa mdpetvaacl
      121 qpeadqagtv qna
//
LOCUS       WP_181784881             324 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidylprolyl isomerase, partial [Pseudonocardia pini].
ACCESSION   WP_181784881
VERSION     WP_181784881.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia pini
  ORGANISM  Pseudonocardia pini
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Pseudonocardia pini"
                     /db_xref="taxon:2758030"
     Protein         1..>324
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
     Region          <80..163
                     /region_name="Tig"
                     /note="FKBP-type peptidyl-prolyl cis-trans isomerase
                     (trigger factor) [Posttranslational modification, protein
                     turnover, chaperones]; COG0544"
                     /db_xref="CDD:440310"
     Region          185..315
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 msllrslfsv rdvprpvlav vggclvaava vgvgaaasgl padaafevgd tvvteedlag
       61 rldvldalyg vreptdadrr defrresakt valgmvldea aadeqvevpd seveaayarf
      121 taerfpdgqa gmvrllgtvg aseadvrdei rrqlltkrly dtavagalet pteeevrayy
      181 dahadrfaqp earhlrnivv adetvavqvl esarrgtdfa elartysrdt etrdsggdlq
      241 fvarsqvedg yagpafdaap galfgpvqta ggwnvgqvae vrpgrrlafe evaqqaraal
      301 enerritawr qwvddrvaav gvty
//
LOCUS       WP_181785796             149 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Streptomyces phytophilus].
ACCESSION   WP_181785796
VERSION     WP_181785796.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 149)
  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 149)
  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..149
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..149
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=15237
     Region          5..>112
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mhrihrltle dalvmlaaae aeaarigvrq ticiaddgah pialhrmtga rltgveiaia
       61 kaftaaghqr athlfneepk gpalpgneaf giqhmhpgrf aafvggfpiv yegevvgavg
      121 vsggngdqdk avgaaalaaf erkvatgaa
//
LOCUS       WP_181785645             348 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            phytophilus].
ACCESSION   WP_181785645
VERSION     WP_181785645.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 348)
  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 348)
  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 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
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Rosinski,J.A. 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 348)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..348
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..348
                     /product="helix-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=36851
     Region          6..319
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mavspsrmlh llsllqsrrd wpgrvlserl gisdrtlrrd idqlrglgyr itavkgpdgg
       61 yrldagaqlp pllfdddqav alavalrtaa asgatggeaa lralttvrqv lparlrhrvd
      121 avafttlpsg sgavagpavl lavsaavrar evlrfdyvpm drapdagpdr rraeprhvvf
      181 grghwylvaw dldaggwrvy rldrmsprtp tgpgfvprtv pggdvrdfla ghfkgsdrgd
      241 awpctgevvl hlparevipf agdgiveelg pdrcrltags wswtalaasl grfdaalsda
      301 aprpladafa llarrcadas srtvpaapvp pgpggekdts gpdpaaip
//
LOCUS       WP_181785691             222 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Streptomyces phytophilus].
ACCESSION   WP_181785691
VERSION     WP_181785691.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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=23645
     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 vgrsiagell dnghevllid ktptaiaver vpraewllad aceiasldea
       61 alqrchvvia atgddkvnlv vsllakteyg vprvvarvnn prnewlfnea wgvdvavstp
      121 rlmsalveea vsvgdlvrll rfshgdanlv eltlpeesal igtavgdvdw padttlvtii
      181 rgstvltpkp ddtleagdel lfvaaqaree qleellsvrr eg
//
LOCUS       WP_181785832             185 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces phytophilus].
ACCESSION   WP_181785832
VERSION     WP_181785832.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  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 185)
  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 185)
  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 185)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 185)
  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 185)
  AUTHORS   Rosinski,J.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..185
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..185
                     /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=20568
     Region          1..79
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtedrskass pealkalahp lrlrilrhls vhgpatsttl aaaldentgt lsyhlrmler
       61 ggliediper sagrerwwrg vpgldirrpp mddvtagera viaeldrlrg aedlelarrf
      121 aagqkeesee gwlrgsrgls hltkeqldaf hddylkllak yrhtpedaap garpillrwf
      181 gipgd
//
LOCUS       WP_181785848             418 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Streptomyces phytophilus].
ACCESSION   WP_181785848
VERSION     WP_181785848.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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..418
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..418
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=46713
     Region          <208..392
                     /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          233..261
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(234,237..238,241..242,244,274,277..278,281..282,
                     284..285,314,317..318,321..322,325)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          272..302
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          313..341
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          354..381
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mttldtdghm taaacnlplr qadltlksla eaglledrga hpvrgriytl hdelreharr
       61 csrqqdgtav idrtrrrtld wlltvstaie kqvtphhrtd dvgrdfrypp apetlpqfgd
      121 ntsalawfea lhhnfmaalr aaaaanprqa viyqlvhaww pwwhhrqhyv lwaeahqlaa
      181 eaaqlsgdll aereilnasg iglrgdaryd eaisrfsrvl qmardaednr svsqaehelg
      241 vayqsagrpe ealhflrdal qlrqaigysr gvaltrivlg qvyldlgqae ravaawtkar
      301 ralrelgetf esaralaflg hasaqqhdfa taeehlhqar eevlqsgghp rwlariweml
      361 gqcaadqghq eaahdhyqqa mhlfesinpr daqrirdrla dlgaapgdsa tvsrppad
//
LOCUS       WP_181785933             284 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181785933
VERSION     WP_181785933.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..284
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30864
     Region          20..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(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          114..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mspaspsssa qaartavavr lrelrkdagl tvtelanrcg whhaktsrie nartppnatd
       61 irlwcracda adqaadlvaq sihaesmyte wrrkirtglk qlqesyaply krtrhfrvys
      121 pgivpgllqt egyvaallgg iaefhaapdd vaaaasvrme rarvvhepgk rfafvieeaa
      181 lhyrigdsda maaqlghllt vgalpavslg vipsatsdrq lrpletfhif dealvsvell
      241 taqvnvvqps eidlylkafa qlhqlavyga earalilnai etld
//
LOCUS       WP_181785990             405 aa            linear   BCT 28-DEC-2024
DEFINITION  LolA family protein [Streptomyces phytophilus].
ACCESSION   WP_181785990
VERSION     WP_181785990.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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..405
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..405
                     /product="LolA family protein"
                     /calculated_mol_wt=41006
     Region          <122..286
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
ORIGIN      
        1 malipperpa deaedraadl aaarrrkavr ygvplgiagl aaatiglvpa laqddgpsad
       61 dvtakeliak alasdvesvd gtvkvstdlg lpslpfgggg ggadlsqlla gdtklhvaad
      121 gpekqrvtlt gsdgdrtvvh ngkdvwtfgg gsdevshstv pedggkdsak hdgfalpkdl
      181 adatpqelad kllkaaddtt dvtvagtaqv agqdayelrl tpkqdestvr ditvavdadn
      241 gvplrvalta ddgkavvdvg ftkvdfnkpd adlfappaga evterdlged fggdfgkgfg
      301 gdfgkglggd waggedwagg draeggksag ledvevhgeg wgsiaelplp ggalgedgvg
      361 aaldfftdkt dagrvfesrl vnvlitddav yvgavtpeal qaaad
//
LOCUS       WP_181786059             762 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Streptomyces phytophilus].
ACCESSION   WP_181786059
VERSION     WP_181786059.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 762)
  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 762)
  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..762
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..762
                     /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=79820
     Region          131..>470
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mqgrsvralt svagvmvlla scssgdfwek atdprrgdgg qqaeldpsir mpalsaavqd
       61 ghvrlqwrpv krisryridd grsqmdvpaa icaqtctlgl pprpeggrqe favsavtaag
      121 afskastatv qapepeadep vgplqevvvi rqdhlpedpe nnsptverip vdsgaaarre
      181 iektwsdpdv isasvnhrit ttdgddppag stptnvlwqr damefdrlpg dprgegitva
      241 mvesggvdat hpslkgavee gasitgdgtg istptlhgta tsslivgqpa gdipgvapga
      301 eimpvalged akaadlvegi iwavdhgadi inisagtscn gpelsgcpds lraasayaee
      361 agvvvvaaag nngpgtncar gtnhpwspai vdsvisvgay radgkrwecs plrsdidila
      421 pgahlmhawl gggygtnsgt sfsaplisgl iatilaerpd lepsdirqml pkwrladgrl
      481 styamlvdld iietddqqpr vgdmdlagif pfeafigigt ghpirkelea akklqfgnpg
      541 grrihtsvsi pwwdgtgsgf ggslpnqree pwgygaitgq vylhkdgsvs aagwmslnri
      601 spgldygldl tgwhrmvcda afvnparkqf rwdtpvkvgv sgftagndtt parakltfsl
      661 gtgattgkhg qlppvtvgkd tlgdcpgqia aqkgrdpaas gtpqelaavf deyarsieri
      721 ehmlvqatpv ttaeavplsg tdaptetrae qdpnlhlnid vs
//
LOCUS       WP_181786106             333 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Streptomyces phytophilus].
ACCESSION   WP_181786106
VERSION     WP_181786106.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..333
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=36740
     Region          2..321
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mtlltgdata alralpddvv dcvvtsppyw rlrdyatgaw tggqpdcphp paahtepagq
       61 hrcsrcaatw hdrqhglept ltsyidhlrq aftelrrvlt ptgtvwlilg dsyaansdgy
      121 htsgplhyrq phyrpradlp pknligvpwh tafalqadgw ilrnaavwhk pnaapfpvrd
      181 rlalqhetvf llvkqthhyf ephppcstts edtdrassag srtasaaisp tddrrgdvwr
      241 vpvrprrhqq hpatfplaip qrciqhgspp galvcdpysg tgttglaalt lhraylgidl
      301 nptytkiaae qlshyraprp dhdeteqqsg dep
//
LOCUS       WP_181786154             271 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181786154
VERSION     WP_181786154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  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 271)
  AUTHORS   Rosinski,J.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 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..271
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30743
     Region          17..>61
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          90..266
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mttlensqpp vqwrycgnqt krwrtragvs reelateagy aydtvkmmeq grrrptprll
       61 qvademcdaq gllvaalgyl qpekfasysq eymlyeaeav alsfyqphyi pgllqtdeyv
      121 ravlaafvpp ldaetleerv karlerqvll aigsrsfsfv veeavlrrrf sseeaherql
      181 rrlldvaeqr nvtlhvmpsd rglhpglrgp lviletpehe hlvyaesqag gvlyadaerv
      241 niamrrrdmi agealcpgds vrlitkllee r
//
LOCUS       WP_181786315             433 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces phytophilus].
ACCESSION   WP_181786315
VERSION     WP_181786315.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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=46317
     Region          102..410
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mglsrlhltv lkrvgamsaq ltprrvrvrl tllygslfvl sgavllaity llvarpsggl
       61 vtfkdvqygs srssaqadtr tyrldedlgs qeggiveemr qqawhqream ldrllmqsgl
      121 alaimsviai glgwvvagrv lrplrtmtst irhisarnlh erlatggppd elkdladtvn
      181 gllgrldtal esqkrfvana ahelrtpltl ehalleetli drgatlesfr anferlltis
      241 kqqatllesl ltlsssdrgl dnpepldlaa lthevlpafr peigrrelav asameparis
      301 gdsalihrlv anlldnaidy nvpggsveia tgvrdggafl svrntggavp pdqverlfnp
      361 fqrlrrtagd ghhglglsiv rsiatahdat ltaearsggg lavtvafplr ddgpgengrv
      421 agfaapgaap adf
//
LOCUS       WP_181786377             276 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181786377
VERSION     WP_181786377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30394
     Region          20..73
                     /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(24,28,53)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(27,52)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(34..35,46,49,53..54)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          95..269
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mteqlpelhg epgnglewfg revaaalahk ganqrqlada tgykepyvsk vksgkarasm
       61 hfakgcdrff etsgyfarll vrvserghpg wfvpyinlek qasrienysn alimgmlqta
      121 dyaeatfrat hpreadeqir arvearlvrr eimerdappl lwailqestl rtevggravm
      181 adqlrhlasd agnphitlqv lrfnagapas slpfilltpa dgatvlyses rgqghvtdsa
      241 aavdsartty drlracardp deslalirei aeeyat
//
LOCUS       WP_181786472             334 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family NADP-dependent oxidoreductase [Streptomyces
            phytophilus].
ACCESSION   WP_181786472
VERSION     WP_181786472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 334)
  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..334
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..334
                     /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=35545
     Region          1..328
                     /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 mtdtaltvhq tarprgfptp ghfafvesav papgpgtalv enlywsvdpy hremmdgdft
       61 ldaplegrti grvvhsrhps lreggivfhr lgwrthavvt pdqarpvprf egvplsahlg
      121 ilggtgltay vgltriaelr egqdvfvsaa gggvgtatgr larlmgagrl vgstgraska
      181 ahltehvgyd evfdyhagpv agllagaapd gidlyldnvg gehleaaiss lreygrivri
      241 gtlaqynstg tpyalrnlpd ivekslrmeg flvrnhghvq kelyefvvph lqsgrvglde
      301 tvvdgfgriv daflgmlrge nqgkiivraa gtav
//
LOCUS       WP_181786508             237 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces phytophilus].
ACCESSION   WP_181786508
VERSION     WP_181786508.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..237
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24706
     Region          5..212
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mpgaielvif dcdgvlvdse riaaaaqatv gaelgwplte adavdlfmgk sqesvgamvv
       61 erlgpgadkt wrtryyeeff agldrleavp gvvdaldaia aaglptcvas sgdhermrrt
      121 lgrtglydrf agriysaadv ggrgkpapdl flhaaremgy apqacavved srygvqaara
      181 agmraygftg glspagwlag pgtvlfddmr klpvlletet etegegegeg eaagtad
//
LOCUS       WP_181786244             252 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Streptomyces phytophilus].
ACCESSION   WP_181786244
VERSION     WP_181786244.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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=26646
     Region          7..>173
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mpprttdrrr ayaawlsdpg fataeivaaa gygavvldie hgafdladle rfipflrrld
       61 ldvlakvlgp ergpiqqald fgatavvvph vesaahaaev csygkfpplg drsfaggrta
      121 gyggfdddwi arqdretrvy pmiedagaie eiekilglpv vdgvfvgpsd lsmrrsrgay
      181 trseadfadl aaiadaaraa gkpwvlpaws aaekafalah gadqlvltmq hgallagfsa
      241 avaetdelag rp
//
LOCUS       WP_181786381             281 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Streptomyces phytophilus].
ACCESSION   WP_181786381
VERSION     WP_181786381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 281)
  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..281
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..281
                     /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=29050
     Region          4..269
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mttliigasg flggelarqa tatghtvtgt fttapgplpe iqwlpldvrn rdditvvldk
       61 vqprlvinaa arrgdwaata egpgrlamaa adrgvrllhv ssdavfsgvq tvydeaatpd
      121 pitsygaaka aaetavrlvs paalvirtsl iigdgtskhe klvhdvsagr apgplftddi
      181 rrpvhvsdla aailelassa qsgirhvage davsrhelgl liarrdglda aalpagrrta
      241 tgasdaqdir ldssatqsal rtrlrgaref lspatgtgtl r
//
LOCUS       WP_181786678             233 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            phytophilus].
ACCESSION   WP_181786678
VERSION     WP_181786678.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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   4  (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 11437015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=24385
     Region          1..229
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msdrthvvvi ggtsgigrhf aqtcadrgsd vvvtgrdedr tkaaaheigg rtrglaldla
       61 dpeaaiaala gvervdhlvl taldrdqntv rdyrpdaatr lltvkltgyt avlhalapkm
      121 pghgaavllg glashrpypg sttvttangg iaalvrtlaf elspirvnal hpsivadtpf
      181 wsdkpaaraa aeekaltkrp vtmrdcthal tfllenrain gvnlnidggd vli
//
LOCUS       WP_181786776             199 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Mycobacterium shimoidei].
ACCESSION   WP_181786776
VERSION     WP_181786776.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium shimoidei
  ORGANISM  Mycobacterium shimoidei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 199)
  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 199)
  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 199)
  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 199)
  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..199
                     /organism="Mycobacterium shimoidei"
                     /db_xref="taxon:29313"
     Protein         1..199
                     /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=22095
     Region          117..198
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mttfvidlaa hdmqrrlgda lgvyvnamhy ppgtehqraa mwlehtrrrg wqavaavevd
       61 aepqqtpsag qlsnapllgv aygycgapdq wwqqqvvsgl qrggfpgqei adlmnsyfel
      121 telhihpraq grglgealvr rlladrgean vllstpetng esnrawrlyr rlgftdiirg
      181 yyfagdprpf avlgrklpl
//
LOCUS       WP_181787037             107 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181787037
VERSION     WP_181787037.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..107
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..107
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11410
     Region          14..93
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 mtqpkfdeli hpstrlslva tlaavdwaef aflkdrlels dsalskqlat leeagyvate
       61 rrvsggrrkv rarltpagrd afeghiaalq aivgdaarpl sgpaprs
//
LOCUS       WP_181787063             352 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181787063
VERSION     WP_181787063.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..352
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          7..324
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 lpeldpaalq aaiddldhpp staaqlrvag tsgrwygtsg vadtgtgrpv sayhrvrigs
       61 vtkvfvatvv lqlvaegrvl ldapvrrllp gllparfapv tlahllthts glpdhvgipe
      121 prtaeevfrh rfdhwtprew vatathgplk fapgtgqeyr ginyvlaami idrltgrpyg
      181 havatrilrp ldltrtavpg ddrhikgrhv hgyltmadgt lrditaydqs sargegdmis
      241 taddldrlla alfagellpp ellrlmftlp pddvrmpdgs parysvglqr avvagiplwg
      301 ktgetygykn aafstrdgrr rfvlayhptt vggdqsepva rvaallvagp as
//
LOCUS       WP_181786846             106 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine dioxygenase, partial [Streptomyces phytophilus].
ACCESSION   WP_181786846
VERSION     WP_181786846.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 106)
  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 106)
  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 106)
  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 106)
  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..106
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..106
                     /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          1..82
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
ORIGIN      
        1 vwlltwlpgq gteihdhgga agaftvvagv lterafpgsg gaprarelaa gglrsfgpry
       61 vhevvnagte pavsihayap alaamsyyae qpggglrpvr tdpvtd
//
LOCUS       WP_181787182             271 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181787182
VERSION     WP_181787182.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  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 271)
  AUTHORS   Rosinski,J.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 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..271
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31032
     Region          17..>61
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          91..266
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mttlensqpp vqwrycgnqt krwrtragvs reelaneagy gldyvkmmeq grrrptprll
       61 qvademcdaq glllaalayl qpekfasysh efmayeaeaa sliwyepryv pgllqteeyv
      121 ravlsafvpp ldeetfeqrv tarlerqkll gilnrsfsfv ieeaalrcrf ggeevyerql
      181 rrlleaaeqr nvtvqvmsaa sgihpgfrgp fvivetpqhe hlayeegqtt gvlyadpekv
      241 stvmrrhdmi arealspqds lrfitqllee r
//
LOCUS       WP_181787180             282 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181787180
VERSION     WP_181787180.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31676
     Region          7..>72
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          107..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mstdyqqare algarlrelr ystpdgrltg ialaralgwp nskvsklelg kqtatpedlr
       61 awadacgqpe syqelrarla gfeshirswr rqlvgghapv qnthnqvqaq aavlrawess
      121 wivgvlqtpd yaravltrav elhrsprdve eavrarirrq ellyqpgrry hillwegvlr
      181 alvcpravla aqldrlvgvi gldtvelgiv pftaplkqpp avgfwiyddr qvivetwhae
      241 lwlddtdsva tyvrawkair dsavygaeah rviararsml np
//
LOCUS       WP_181787153             540 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Streptomyces phytophilus].
ACCESSION   WP_181787153
VERSION     WP_181787153.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 540)
  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 540)
  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..540
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..540
                     /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=59729
     Region          25..516
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mlgtggalal gtlgaagapa llapstataa ersgtadglp sglftlgvas gdplpdgvvl
       61 wtrlapdpla gggmparpvp vqwqvsdtps ftrirkggaa larpeqghsv hvevhglepd
      121 reywyrfrtg retspagrtr tapaadarvr hlrflfascq nwqdgyftaw hhaaqedvdf
      181 iaflgdyiye svprdttvrk hegtdepysl tdyrnrhaqy rsdanlqaah ahapwivtld
      241 dheidnnwad eipqdpesqt peafrarrva alqaywehmp lrrasmpdgl dmqlyrslry
      301 gnlatvhvld trqyrsdqit tleeaqdpar smtgaaqerw lvrgmersga rwnllanqlm
      361 waqndrkagp eqvfdfdnwd gyraqrrrll effgsgrtdn pviltgdrha twvadlkpdf
      421 ddpaspvvga eltgssissg gdsdpaafha tydpimaesp hwkyidnrra yvlcdvtrer
      481 mtaalrtvdt vwrpegttat tsaefvveag rpgvtaastp apprpmrlad rrydvdddqv
//
LOCUS       WP_181786768             548 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 27 protein [Streptomyces phytophilus].
ACCESSION   WP_181786768
VERSION     WP_181786768.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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 phytophilus"
                     /db_xref="taxon:722715"
     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=58036
     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 mltrsrrrla rllaataaal alsataphqp valaapgspa vtpplgwnsw nsfgcgvted
       61 mvrqaadamv ssgmrdagye yvvvddcwfd pqrddqgnlr ahptkfpggm kalgdyihsr
      121 glkfglyqvp tertcaqrvg tfpgstgsmg hevqdartfa swgvdylkyd wcspegtrde
      181 qvarfslmrd alrdtgrpiv ysinpnsfha itgstydwgq vadlwrtted lldiwqngnv
      241 nsypmgvgnv vdvnaplaaq agpghwndpd mlvvgrpgls ltesrshftl walmaaplma
      301 gndirtmsad vsavlrnqrl lavnqdtlga ggrrvrddga tevfakplad gsvavglfnr
      361 gdgtatvsas atqigltggs faltdlwtga tsstsgqita svpahgvtaf rvtggtplaa
      421 etsrirgtgs grcldvenss tapgagvviw dchtaanqlw ttwaggeirv ygdkcldaen
      481 qgtadgtrvi twscngqdnq kwtlatdgsv rnvhaglcle pdggatanga rlvlgvcngq
      541 adqrwtrt
//
LOCUS       WP_181787250             109 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            phytophilus].
ACCESSION   WP_181787250
VERSION     WP_181787250.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 109)
  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..109
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..109
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12266
     Region          1..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkkrsytcgl daaidvmggk wkglilfwlg eeplrfgelr rtvdgiserm lilhlrelea
       61 gglvhrevhe qvppkvvysl tdfgrslvva ltplgewgee hmerleall
//
LOCUS       WP_181787269             245 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Streptomyces phytophilus].
ACCESSION   WP_181787269
VERSION     WP_181787269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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..245
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..245
                     /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=25937
     Region          64..223
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mprtpesrdp gartpesrtp esrtpvavsd aglpgwlapv adaartvrpe elssflpped
       61 dggrpaavlv lfgdgddgpe lllteragsl rshagqpsfp ggsldpedgd pagegplraa
      121 lreaeeetgl dpagvqvfsv lprlyipvsg fvvspvlgww repspvgvvd paetarvfsv
      181 tvadltdpan ramavhprgh lgpaflvgsa lvwgftagvi drilhlagwe rpwdrerrvp
      241 ldwha
//
LOCUS       WP_181787284             417 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181787284
VERSION     WP_181787284.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 417)
  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..417
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..417
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=46802
     Region          23..83
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mpypleeqea igrrikrlrl rlgmaqadla vavgktqgwl srvengrlel drtglinqia
       61 aalhchpndl ldrpytsnvp enqwqvaats imrelrrfdl tptfdgtprp srqlwqdvkr
      121 lhrlrdaaan tailrempdl frearalaev stghereeaf avytvcckat htaahalghs
      181 elialacera mwsaqlsgdp lmpavadymr iwdmwatadw ndamvladra ldsvedyaer
      241 ddqmalrlrg ilhlraavsa aragdvaesr ariadateta vrigryegpp vfdrqsvtfs
      301 agnvtvhgia taleagdhvr slelnddadp eeidslphsr rgnhhmdmar aflwngdrht
      361 alnqlrkaed lapqlvrnhp iaratlrkiv yaertstreq lrgmsnrfhl ddqglfr
//
LOCUS       WP_181787330             184 aa            linear   BCT 28-DEC-2024
DEFINITION  NuoB/complex I 20 kDa subunit family protein [Streptomyces
            phytophilus].
ACCESSION   WP_181787330
VERSION     WP_181787330.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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 184)
  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 184)
  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 184)
  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..184
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..184
                     /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=19963
     Region          1..156
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 mgleeklpsg filstveeaa glarkssvfp atfglaccaf emmtagagry dlarfgmevf
       61 rgsprqadlm ivagrvsqkm apvlrqvydq mpnpkwvism gvcassggmf nnyaivqgvd
      121 hvvpvdiylp gcpprpemli dailklheki rheklgvnre eaareaeeaa lkalptiemk
      181 gllr
//
LOCUS       WP_181787352             515 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Streptomyces phytophilus].
ACCESSION   WP_181787352
VERSION     WP_181787352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 515)
  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 515)
  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..515
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..515
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56465
     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 msvviaayna mpyltrcves vleqslppaa veivavddgs tdgtgaeldr farahpgrvr
       61 vvhqensggp aaprnagiel argryvffld addylgpeal ermtamadan gsdvvvgklv
      121 gvggrkppts mfkrdqpdad lyssrvfwvl npmklvrrel ierhglrfpe dlrtgedqvf
      181 vtkvylhaak isvlasydcv yyvlrddggn ltttvrkspr paagnfgpla amfalvgent
      241 pagprrdhll trlygvnlqr alrgvrkesd persrrmfaa vhepvarwys etamaglpai
      301 vrlqgelvrr glyeeavavv ryigkrrdvl dreggakpvr wlapadftve ggrvfahypy
      361 frdsrlglpd svfdvtrqvg arsfvrpasv tvaqdrrdsr vlsvrgrrrt rlpavalelt
      421 atresdgrtv tvavpapaed pvkdltsgpg tagkrtftar irvphpgiwh lslriagnsr
      481 selplqavrv esanparall awlgrdgrra vrpas
//
LOCUS       WP_181787400             389 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces phytophilus].
ACCESSION   WP_181787400
VERSION     WP_181787400.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 389)
  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 389)
  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 389)
  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 389)
  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 389)
  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 389)
  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..389
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..389
                     /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=41461
     Region          82..382
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mpdtasepar rtgrrlrwtv rlrltllyga lflvsgvall aityalvarg nvtkgilvrf
       61 dspqpggqgd pdirhvater heaalqalla qsgialalmt avsvalgwvm agrvlrpvrt
      121 magrarrise hnlharlaia gpddelkdlg dtfdgllsrl daafeaqrrf vanashelrt
      181 pltlqramve valsrpgada aslravcerv vasgeeqerl iealltlags qsglvaaepv
      241 dlarvvrevl hdrtraapgt ldlhsslrpa lasgdvrlia rlagnlvena lrytpaggwv
      301 rvatdvretg ypmlrvvnsg pripaeripd lyepfqrlqp raagggyglg lsivgavaaa
      361 hraelttvpg pegglsvtve fpppdpaew
//
LOCUS       WP_181787421             290 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Streptomyces phytophilus].
ACCESSION   WP_181787421
VERSION     WP_181787421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   ter Beek,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 290)
  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 290)
  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..290
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..290
                     /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=29892
     Region          40..282
                     /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 mtatlppvpq ppdppdpdpg gepeaapket apgwsvpgag alretgklfa lalsvarlsf
       61 krpfqlrefv eqfwfiasvt ilpaalvsip fgavialqvg sltqqfgaqs ftggasvlav
      121 iqqaspliva llisgaggsa icadlgsrki reeldamevm gvspvqrlvv prvlatmgva
      181 vllnglvsvv gtlggyffnv ilqggtpgay lasfsalaql pdlyiseika lifgfiagiv
      241 aayrglnprg gpkgvgdavn qsvvitflll ffvntiltsi ylqvvppkgg
//
LOCUS       WP_181787514             420 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Streptomyces
            phytophilus].
ACCESSION   WP_181787514
VERSION     WP_181787514.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 420)
  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..420
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..420
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44097
     Region          24..394
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mtnssatsla llggkpeiat pgshfswppi dsrdieavtg qlmeavsipd rsgivadled
       61 alaawlgvrh vvttstgtaa lhsmyaaagi gpgdevlvpa ltfhatatpl lhlgarpvlv
      121 dagtdgqpdl daavrllspr tkalvavhlw glpenadala afadehsvml ledgshahga
      181 sfngrlvgty gqaaafslng pktlsagegg fvatddtdqy yrlllhgqyn krcrteiptr
      241 hplakyattg qglklrihpl aaalaraqlp rlegclsgra acaerlcaal edvpglrvpr
      301 ldpaaraswy alplryesaa lgglplarfl aavhaegate vdhpgstrpl gdhplfrtpr
      361 eliphypvaq dptlgdcsga arvhastvkl pvwhrpedsa ladayaaala kvarhhkell
//
LOCUS       WP_181787618             490 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181787618
VERSION     WP_181787618.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..490
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51095
     Region          25..346
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrtraaalvl lllaalaplp aharsatsqv daylrerara tdtpglayai vgpggtertg
       61 afghdgdggp vtprtpflwg siakpvtata vmtlaesgav gldepvrtyl prftladpga
      121 aaritvrhll qqtsgipeht gvtdrfgdrd dpygqavadl adteprsapg erhgyssany
      181 lllgalveav tgrpyeaylr dhvlgpldmr gavttprrar avprghsyff gqvvaadthy
      241 dpagasygyl ggtvrdlarf aaahlgggty dgervlspas vaqlhrgtad sggtqryglg
      301 wrddtrnddl gtrtvwhtgg apgyhamvvl lpgadravvv lqnaygyfqa adlnaagfga
      361 arilaggdpe qppgdapyta flaalaavlt lttaatawta friarpaagr rtrrrilatt
      421 aawtlaalta aalagvvapr sfgvdlrlir lyspdlgwll tltalaacal aaarlaaggl
      481 alrragrgrr
//
LOCUS       WP_181787370             234 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase [Streptomyces phytophilus].
ACCESSION   WP_181787370
VERSION     WP_181787370.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  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..234
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..234
                     /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=24540
     Region          70..216
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mregygdrvp nqqrnsvtsr llsravhrgw rwvrstgavs agrpgpyrfr gigegtvlpf
       61 pqgtifgegr ielgahciig eqvtltvgla pgaplgpeaa lrlgdgvvlg rgshviadls
      121 vtlgdkvycg pyvyitsinh syddphepvg eqwprsapve igsgswlgvg avvlpgarlg
      181 rnvvvaagsv vrgevpdhav vagaparivr rwnpesgwhp plrpappgtl eaat
//
LOCUS       WP_181787665             108 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces phytophilus].
ACCESSION   WP_181787665
VERSION     WP_181787665.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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=11772
     Region          12..95
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrevsqpaag sirmvdvlra ladpvrlevv lrlaatgees cnaiggdldv hqttmshhyr
       61 vlreagvtwt tvqgrtrlvr lrrddleerf pglldsvlng aaadvtpr
//
LOCUS       WP_181787738             248 aa            linear   BCT 28-DEC-2024
DEFINITION  aminoglycoside phosphotransferase family protein [Streptomyces
            phytophilus].
ACCESSION   WP_181787738
VERSION     WP_181787738.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 248)
  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 10007009
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..248
                     /product="aminoglycoside phosphotransferase 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=26760
     Region          2..220
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
     Region          <136..194
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
ORIGIN      
        1 mdevevvvah seratlrvgd vflkvdadqa ridveveama lvpvptpevl wrkpsvlaia
       61 alpgtvlgrl gepsaaspaa waaagaairq lheaplppwr grrrqgpdel aaeldgecel
      121 lvangvlpad lvtrnrqvad aairpwtavf thgdlqiehv fldgdevtgi idwseagrgd
      181 alfdlatltl gheghlddvi vgygtdvdrd virawwslrs llgvrwlveh gfdafapgce
      241 vdvlrsrm
//
LOCUS       WP_181787799             275 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Streptomyces phytophilus].
ACCESSION   WP_181787799
VERSION     WP_181787799.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 275)
  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..275
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..275
                     /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=30226
     Region          2..272
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mpridahhhl wditrrpqpw mdgswadplr rtftladlap hlaehridgt vlvqtsssye
       61 etlelceepd ppvhlvcgwl dltasaldaa alrrtparlg alrhqaegep dprwlvrpdv
      121 lralglagec glvydllvtp relpaaiaaa ravphtrfvl dhagkpqiaa gewqpwadlv
      181 aelarlpnvs cklsglvtqa dwehwrpadv lpyarhvidv fgpgrilfgs dwpvctlaag
      241 ygqvvelaee avadltaaer eaffggnarr iylpd
//
LOCUS       WP_181787843             805 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein, partial [Streptomyces phytophilus].
ACCESSION   WP_181787843
VERSION     WP_181787843.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>805
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          <7..805
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mrgnhterlr ttpplvgrde elhrlvaava nppgvavieg eagigktrlv gelaarldss
       61 grrmllggcr qirepfplgp vldalrgigd vlpgrrlsav vgalrpllpe laehlpdape
      121 pledraaerh rvfralvsll aevgdavlvv edahwadeqt vdflgyllad pppalcvvlt
      181 yrgeeadeal ravttrlaae vgrehivlsl ldpdqtsala aaildtgqsv srnfaihlwe
      241 rtsglpfavq ellallrerg mlvrrergws rraideldvp agvrhsvler vrrltpagqa
      301 vaeaaavlre rvsvevltat cpvpradale gledvlgsgl leergsmvgf rhmlaaqsvy
      361 aslplprrqd lhgraatavr slvppplgqv ahhlreahly dqwvdaaeaa aeqaaelndd
      421 teaarvledv lrtapldpar rgaltiklgw vaiearhfva vldlfeqala lgqpravrgq
      481 lrfftiplqe qlaaepamlw rtataaledl egqpelsawa mlslalpygl dppaaehlaw
      541 anralelvpq irdrafavfi lgkvamllin vgdprwsvlt eqvleltggt pvhtrevnay
      601 asiaeaamhv gnhawaerll daaadapvgp rldlltdalr lvldhrrgrw dgleeaaapl
      661 rstlrdrpgl wiivesvsac lalsrgeldg vdarlsgave aaldasgvev lpalttaylr
      721 lstatgeadr alaatrdplr lwevkemwpv avralpalve allavgrave aaerlagfea
      781 glrdrdapfa paalahargh laaaa
//
LOCUS       WP_181787858             294 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181787858
VERSION     WP_181787858.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..294
                     /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          4..273
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 lhtlrrdkaa vshhydvgnd fyslvlgpsm vyscaywddg dtledaqaak ldlvcrklgl
       61 kegdrlldvg cgwgsmvlha areygvravg itlsaeqaay arkrvadagl gdrieirvqd
      121 yretadgpyd aissigmaeh vgstrygeya rglhrllrpg grllnhqiar rpladeedya
      181 idefidayvf pdgelspigt tvdqleragf evrdtqalre hyaltlrrwv anlearwaka
      241 valttpgrar vwrlymaasa lsfehnrigv nqvlavrtpg tgdsglplrq pgwr
//
LOCUS       WP_181787382             515 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Streptomyces phytophilus].
ACCESSION   WP_181787382
VERSION     WP_181787382.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 515)
  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 515)
  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..515
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..515
                     /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=54869
     Region          14..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 mrshllndrt agtyrrtvta gvehiaarla hadrpftgia ppalapvvda vdldhplgda
       61 daalaeldrl ylrdavyfhh prylahlncp vvipavlgea vlsavnssld twdqsagatl
      121 ierrlvdwta ariglgpaad gvftsggtqs nlhalllare eacdgvrkeh gadlrtaeil
      181 prlrilasah ghfsvrksas llglgeeavv evpcdaerrm rpaalaaala dlqrdglvpm
      241 avvatagttd fgsvdplaqi aelcagygvw lhvdaaygcg llvsgrrrhl lagieradsv
      301 tvdfhksffq pvsssavlvr draalrhaty hadylnperm aaeqipnqvd kslqttrrfd
      361 alklwltlrv mgadgvgalf devcdlagag wrlldedprf evvvrpqlst lvfryvprga
      421 rpdpalvdaa nlharerlaa sgaamvagtk vdgrhylkft llnpettted laavldliaa
      481 haadhtgesl vpdvpapsta spvqaaqaap avpar
//
LOCUS       WP_181787861             414 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Streptomyces phytophilus].
ACCESSION   WP_181787861
VERSION     WP_181787861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..414
                     /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=43462
     Region          51..335
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mtdaddlmtr rratwaaaeh tlsaslptis arlarlatar pggvdldqqv dvyaggivge
       61 leertagllg cddaaffptg tmaqqvalrc waertgsrav ashplahlev heraaysvvt
      121 glravhptre priataaeva algepfgtlm lelpmrepgf vlpeweelee vvaaarerea
      181 vvhfdgarlw ectthfgrgl aeiagladsv yvsfykslgg lsgaalagpa gfveearawr
      241 hryggqlfqq wpaalaaleg lqlelprlps yvvharvvag alreglaaag vpffrvhpev
      301 phthqfqvwl pygaealmea gtalaeetgv clfrmwtepg dppglsvtev tvtepglaws
      361 aedvareaga lvervrrvaa araepagsgd agttgsggag pagsgpgdsg aads
//
LOCUS       WP_181787236             482 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-amylase [Streptomyces phytophilus].
ACCESSION   WP_181787236
VERSION     WP_181787236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 482)
  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 482)
  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 482)
  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 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..482
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50389
     Region          55..402
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(100..101,104..105,140,143,194..197,227,229..230,
                     232..233,260,262,267,319..320,325)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(142,199)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(229,260,320)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          408..481
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 mahpvrarlr garlllgtal aalvlallpa atrastaaea gaaeapaaea aaggdvianl
       61 wswnwksvaa ectdvlgpag yaavwvappa eslahpqhhw wdvyqpysyg ltgrlgtead
      121 ftamtaacdg agvavytdav vnhtaaqtgt gyagtalgdk yappmysrad ynvdvcnrei
      181 gnwddkwevq ncellglpdl ktgsdavrdk iagylnsqia rgvsgfrvda akhipaadle
      241 aiagrlddta agarpfvfhe vfpgstpapd eyygsgrvld fffgdrvksa fqsdiarlen
      301 lgdqgllpar nsvsfvtnhd terngrhlty kdgdtavlan vfqlgwtdap ptvyagfafa
      361 gnddsppadg ggfvtgtdcg agwycldrdp ritgmvgwrn aaggaevtdw qsprgnvvgf
      421 grgdrgfval nntgepvsqe fgtavadgty cnvldgcate vtvaggrval dlpakgavaf
      481 hp
//
LOCUS       WP_181787884             202 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces phytophilus].
ACCESSION   WP_181787884
VERSION     WP_181787884.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..202
                     /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=21825
     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 mpdsdlapyw ntnvarhpgi lravpegcrd aldvgcgdgl larklavrae rvtgvdnspe
       61 miasareqaa grpgldfvag dfltadlpap gydficsvsa vhqmdftpal armrdllrpg
      121 gvlvvvglar ersvgdwaam vaaapvvrta kllrrasfpp gmpfisphms ygevraearr
      181 vlpgvryrrh vlrrysltwq ap
//
LOCUS       WP_181788044             240 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein, partial
            [Streptomyces phytophilus].
ACCESSION   WP_181788044
VERSION     WP_181788044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 240)
  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 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   3  (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   4  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..240
                     /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]"
     Region          <1..239
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 gagivvnatg gwlasaeenr qaharlvdhl ldaarllpap prfvqigsih eygpvpegtd
       61 igesrpphpq tpygrsklag snavlrasra ghvqgvvlra vnvygpgaaa gsflgsvvrr
      121 lralapgdrl hlevngdrrd yvdvrdlada vvraaesplt grsvnigrge algmrrlltl
      181 lvaeagldag vleladqpva shgggwtrad irlaerllaw rpktsvgqsl rdmwqhtaat
//
LOCUS       WP_181788215             632 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces phytophilus].
ACCESSION   WP_181788215
VERSION     WP_181788215.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 632)
  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 632)
  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..632
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..632
                     /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=68807
     Region          1..629
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mtetetqtkl dsrppsvatl fldrvestpd reafqypvpa aggsgegdew rsltwaqsae
       61 rvfaiaagll dlglqseerv avacntrlew iltdlgilca gganttvyps tnaeetayil
      121 adsgsrvlva edaaqlakvr emraglpdla hvvvveaada vateddpdgw vlslaelerr
      181 gaeylekhpe avrehigalr pdqlatliyt sgttgrpkgv rlahdswsym gyaiegielv
      241 mpddvqylwl plahvfgkvl taghikvghv mavdgridki ienlpvvrpt qmcgvprife
      301 kvyngvaaka kagggakyki flwaaevare yarvtqdnhr rtgkrtapvg lttkhaladk
      361 lvygkfraaf ggrmrgmvsg saalapeigy ffdgagvpil egygltesaa asfcnrmety
      421 rtgtvgkplp gcevriaddg eillrgpgim qgyhglpeks aevleddgwf htgdigelsd
      481 dgflritdrk kdliktsggk yiapsevegq fkavcpyvgs ilvigadrnf ctalisldea
      541 alagwakeng ledrpyaelv asaearelve gyvkqlnerl qrwqmikkfr ilprdldveh
      601 geltpslklk rpvvekeykd liedmyagar ea
//
LOCUS       WP_181788253             282 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181788253
VERSION     WP_181788253.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31516
     Region          20..93
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          99..277
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgkvgnvsly ggeaeagdsl ktfgamlkvl rdeagltqea laeglgyshd hiskiergvr
       61 fpprdldkla edvlgplaar llketrrslt rkaglasrfr hwaviekeav tlyayecrvv
      121 pgllqpepyi rvineavlpp lveeqieqrv aarlerqvvl nerphtyfgf iveqmllerq
      181 vggaeitrsl idhllaiger rnieiqvmpr rmekhvgsag siylaetvdh kwlgysegqq
      241 ssnlisdltd vgtlqqryrk lssqalshea tvelleqmrg dl
//
LOCUS       WP_181788265             120 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181788265
VERSION     WP_181788265.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..120
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..120
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <3..113
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 aglkacsawe daprpvladd llperaiagd paareqlvee iysplaeags alletlsvyl
       61 eqasslegaa rmlfvhpntv ryrlrrvtdv tgwspsdvrs aftlrialil grltdaepqp
//
LOCUS       WP_181788306             289 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces phytophilus].
ACCESSION   WP_181788306
VERSION     WP_181788306.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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..289
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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]"
                     /calculated_mol_wt=31607
     Region          22..183
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 masdahdsnl appspeevgs aydrfgalyd ltqgtsaihv grwsaggtgl pattlgelad
       61 ramdrqtdyy iealapgptd hvldigsgtg gpavrlaert earvtgitvs etqvararer
      121 aaaasladrv tfaladvlel pyedasfdaa waidsfahia drlgglrqvw rvlprggrll
      181 mteftrrgep sraqldtfrq vwtsppplpl aegvrlacea gfelvrlenq thdvlmnaev
      241 mtvlyrdhhd eireryglet taamdasipl frtfvrdhlg yflyvlrkp
//
LOCUS       WP_181788378             265 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces phytophilus].
ACCESSION   WP_181788378
VERSION     WP_181788378.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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=28757
     Region          50..156
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 magttdsvtp vgadwqgwqa swdrqqewym pdreerfrvv ldavealvgp eprvldlacg
       61 tgsisarllr rfpgarttgv dldpallaia rgtfaddpra qfvtadlakp dwtarlphga
      121 ydavltstal hwlfsdqlat lygqiagvvr eggifvnadh mpdpatpgin eavrnwskvr
      181 qdreraegvl dwadwwrvva adpvlggpaa erfvifgdpn dpneghadgd vqapawhaet
      241 lraagfaear tvwasardaa vlalr
//
LOCUS       WP_181788353             455 aa            linear   BCT 28-DEC-2024
DEFINITION  IucA/IucC family protein, partial [Streptomyces phytophilus].
ACCESSION   WP_181788353
VERSION     WP_181788353.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  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..455
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..455
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
     Region          <1..453
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 leghqtghpw lvankgrigf saadaaayap earvprrlpw lavhrslaey rgvpaldrpe
       61 elyaqelppa travfadavv aagrdpdgyl wlpvhpwqwd etvatlyapq vaaglviplp
      121 adggpadmwl pqqsvrtfln lsrprarsvk lplsvlntlv wrglptertl aapavtrwvh
      181 glrdgdpyla eetrvvllge tasvtvrhpl ydslpgvpyq yrellgciwr epigplldpg
      241 erartlaall wtdadgrslt aelvrrsgla prawlarlfa allppllhfl yrygtvfsph
      301 genavvvfdg advpvrlavk dfvddvnvss kplpehagmp devrrtllte apeflpqfih
      361 sglfigvfry laplcadelg vpeaeffglv raeilcyqrr fpelaerfal fdllvpridr
      421 lclnrnrlyl dgyrdrarrp haavdgtvpn plhst
//
LOCUS       WP_181788395             300 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181788395
VERSION     WP_181788395.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..300
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33142
     Region          29..88
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          115..295
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msaspeqtss vrralsqqhg gptvlrillg thlrrlreaa gvsreaagda irashakisr
       61 lelgrvgykd rdvsdlltly gvtdeqerse flalarrass pgwwqkygdv lpgwfetllg
      121 leeaaglirn yqvqfvpgll qtadyaravt llanagaaeq eiqrkvdvrl rrqqvldrpd
      181 apklwvvvde aalrrplgga dvmrgqvrhl lemgsrknit iqiapfdigg laaaggpihi
      241 mrftepdlpd vvyleqltsa lyldkpdeve nyklvmdrlc ataethagsm rilerladef
//
LOCUS       WP_181788427             455 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            phytophilus].
ACCESSION   WP_181788427
VERSION     WP_181788427.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 455)
  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 455)
  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 455)
  AUTHORS   ter Beek,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..455
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..455
                     /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=49167
     Region          42..443
                     /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(154,156,282,284,317..319,360)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mltptrskrt irtlvpvata aallaacsga ggggssggdd svnvvmvnnp qmvelqklta
       61 khftkktgie vnftvlpene vrdkisqdfa nqagqydvat isnfevpfya endwllplde
      121 yaaddaefdq edvlapmres ltaedgklya epfygessfl myrkdvfaen glempdkptw
      181 qqvadlaaea dgaepgmkgi clrglpgwge viaplttvvn tmggtwfded wearldspef
      241 teavkfyvdl vrehgeagaa qsgyaeclnn ltqgktamwy dataatgsle aedspvrgki
      301 gyapapvdrt essgwlytwa wgvqkaserp esawkfiswa sskeyeelvg kelgwanapa
      361 gkrastysnp dylkaagafa ditreaiega dprdpgtqpr papgiqfvgi pefsdlgtkv
      421 sqeissaiag kqsvedalan sqelaeevgg eyrdr
//
LOCUS       WP_181788467             422 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces phytophilus].
ACCESSION   WP_181788467
VERSION     WP_181788467.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 422)
  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 422)
  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 422)
  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 422)
  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 422)
  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 422)
  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..422
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..422
                     /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=45765
     Region          111..420
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mddnrrsasd elpagtppkp twdpreaaap ywlrptirir ltliyggmfl magmvllaii
       61 yllaatalds fatpfklles sgtvqvasgp cpevsdakty dqfngileac ierrrqlald
      121 sllrksllal lgmtvlafaf gyvvagrvls plgritrtar svagsdlhkr ieldgpddel
      181 keladtfddm ldrldrafns qqrfvanash elrtplainr tllevqlsdp easpelqqlg
      241 ktllatners ellvegllll arseneivdr kpvdlaevas qamdqargea qtrgvelrgv
      301 rkpayvqgng vllervglnl vqnavrynvp eggwvevgte aqpgvavltv antgpvvpay
      361 evdnlfepfr rlrtertgsd kgvglglsiv rsvirahggt vtaqpreggg lvirvalpmq
      421 tv
//
LOCUS       WP_181788537             155 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase, partial [Streptomyces phytophilus].
ACCESSION   WP_181788537
VERSION     WP_181788537.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>155
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          1..>155
                     /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 mdpviivgag pvglalalal arhavptvll ddrpagdaee dgrpagprpa rtavlrphta
       61 afldrigaae agergarltg wrvlrggrtq vrvefgeaag paplhvaqsa ltaslaalae
      121 nshhvevfrg srvtelaqep ygikartrag twwrg
//
LOCUS       WP_181788668             282 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181788668
VERSION     WP_181788668.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30869
     Region          16..>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(20,24,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(23,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(30..31,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          101..275
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msspsssvqq arealgqrlr eirkdagita relarragwh eskcsrlehg rtppsdadir
       61 awtlhcdaag qaddliatar gidgmyvewr rmeraglkra qqsvaslfer thrfrmyqsw
      121 vvpgllqtpa yttailrtva elrdvpddva davavrmerq rvlhtgvhsf avlveewvlr
      181 tvigdaevma gqlghliavg tlpavslgvi plgaargigw pvesftmydd vqvnvelvsa
      241 hltvtqprei eeyaqsfanl aqiavygpra ralitsaida lg
//
LOCUS       WP_181788725             147 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181788725
VERSION     WP_181788725.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  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 147)
  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 carboxy end.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>147
                     /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          51..147
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mgedlsaaaa kgwavrwelq reqrepgred rftvvgdlve rvtdgrhrpa vldlgcgtgs
       61 laarlkrrmp aldvvavdad pvllglgrrm hgtqirfvdt vvggirwqdd ldldrpldaa
      121 vsatmlhrlp ermllevygr lhallrp
//
LOCUS       WP_181788342             372 aa            linear   BCT 28-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Streptomyces phytophilus].
ACCESSION   WP_181788342
VERSION     WP_181788342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  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 372)
  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..372
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..372
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=42035
     Region          1..372
                     /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 msltlqpisr eqhlayirsl paashcqipa wadvksewra enlgwfeadg rqvgaalvly
       61 rqlpkvkryl aylpegpvid wyapnldawl tpmlahlksq gafsvkmgpp viirrweapt
      121 ikagiadpdv krlrdvnadv vepqafevae rlrrlgwqqg edggagfgdv qpryvfqvpl
      181 agrsldevfk gfnqlwrrnv kkaekagvev vqgglehfge wqrlyeitae rdkfrprpqg
      241 yfermwkvln aeepgrmrly falhqgecla attmltvggh vwysygasan hgrevrpsna
      301 iqwqmmkdah aagahvydlr gigdalvdsd hlfgliqfkv gtggqaaeyl gewdyplnkl
      361 lhkaldiyms rr
//
LOCUS       WP_181788794             192 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181788794
VERSION     WP_181788794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>192
                     /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]"
     Region          3..>190
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mipaafdyvr pesvgdavga laaaeaagse akvlaggqsl lpllrmrlaf pdlvvdvgri
       61 pglrgvrddg dalvigamtt hhdvvadplv rrhagllaaa tatvadpavr hrgtlggsla
      121 hadpaadlpa valaldaelt avgprgrrtv parefftdyl ttalapgell aeirvpkydg
      181 wgfryekfsr aa
//
LOCUS       WP_181788434             270 aa            linear   BCT 28-DEC-2024
DEFINITION  IclR family transcriptional regulator [Streptomyces phytophilus].
ACCESSION   WP_181788434
VERSION     WP_181788434.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..270
                     /product="IclR 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=28816
     Region          29..262
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mavlhpdpgd qppgrrpepa ddasaapfpa vrhafrvles asrhggegvs vallaretgl
       61 ppgqlaqlll tlrgqryler ledgsyaige avallgaggs rtravhdklq rgmndlrkat
      121 raaiylgrye dgevrvtqia dapgtprvne wvdfrsaaha taigkclltq ldhdarrehl
      181 srhrtarlts rtitsekavl aaldrqvatv ptldlqeyav gtvcaavplt agrevgcval
      241 slpvhqthrl raaaeklnte agnlllalsl
//
LOCUS       WP_181789027             428 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase, partial [Streptomyces phytophilus].
ACCESSION   WP_181789027
VERSION     WP_181789027.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 428)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>428
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          3..428
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mgqtatpqan sggltleehr ldnglrvvls edhltpvasv ciwydvgsrh evagrtglah
       61 lfehlmfqgs aqvsgnghfe lvqsaggsln gttsfertny fetmpahqle lalwleadrm
      121 gslltaltee sldnqrdvvk nerrqrydnv pygtafekla amtypdghpy hhtpigsmad
      181 ldatsladcq effrtyysps navlsvvgdi dpaqtlawvq ryfgsipahe gkqpprdgsl
      241 pdtlggaqrv plaeevpsra lmasyrlped gtreadaadl altvlggges srlynrlvrr
      301 drravaagfg mlrlagapsl gwldvkasgg vevpaienav deelarfaeq gptpeemera
      361 qaqlerewld rlatvggrad efcryavlfg dpklalgave rilgvsaeev qavakarlip
      421 enraalvy
//
LOCUS       WP_181789061             167 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease, partial [Streptomyces phytophilus].
ACCESSION   WP_181789061
VERSION     WP_181789061.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 167)
  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 167)
  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 167)
  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 167)
  AUTHORS   ter Beek,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 167)
  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 167)
  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..167
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..167
                     /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..159
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 allmlplgts avtvgfgfli aldtppldlr sswilvplaq alvgvpfvvr tmlpvlravd
       61 drlreaaavl gasplrawre vdlplvwrav lvaagfafav slgefgatvf iagpdrptlp
      121 vavarllgra getnygqama lstilmavca asllllervr knqagef
//
LOCUS       WP_181788797             309 aa            linear   BCT 28-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Streptomyces phytophilus].
ACCESSION   WP_181788797
VERSION     WP_181788797.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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 309)
  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 309)
  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..309
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..309
                     /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=35216
     Region          19..292
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 mttttghlal tdalgplkdr ekvaerllaa sekhsfdpdk eldwdapiee gkwfwppelv
       61 slygtpmwrr mseeqqkela rleaaslasl giwfeiilmq llvrhiydkp vtsnhvryal
      121 teiadecrhs mmfarmiskg gaepypvsrf hhnlarilkt vsttpgsfta tllgeeildw
      181 mqrlvfpder vqtlvrgvtr ihvveearhv ryareelrrq mltaprwern ftrltsgeaa
      241 rvfsvsfvnp qvytdaglnr aeavaqvkas phrrevmqtg akrltdfldd igvlqgvgrr
      301 lwrssglla
//
LOCUS       WP_181789193             347 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181789193
VERSION     WP_181789193.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..347
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36858
     Region          37..322
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnirdqplka vaaaaepraa vavavsvtga yrtlcrggid rkgtasvtdr trfevgsvtk
       61 tftallladt aargevslsg riaerlpyaa lprghgrait yehlathtsg lprlppglll
      121 kglpswfanp yrsftpdmll palgravvhh ppgtltrysn lgvgllgrll adgagtdygs
      181 mlrtrvldpl elkdtgtaap adpdpdyavg ywhgrrrppw vipalpgaga irssardlir
      241 flrahldped rdipgalrrp laevvrirel paqddeksgl gwsartvaga tlyfhsgatr
      301 gctafvglsp erevcvaalt nsgvtlrsgf iqsaylllrg lalgeak
//
LOCUS       WP_181789327             264 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces phytophilus].
ACCESSION   WP_181789327
VERSION     WP_181789327.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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..264
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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]"
                     /calculated_mol_wt=28343
     Region          <49..153
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 myhssspprl trltfhgpls edralrmirr lsapaaptap tasaapvsvl digcgwgefm
       61 lrfleatpga tgvgidlned dlargragae arglaervrf vrgsavdiah gpadlvlcfg
      121 ashalsdarp pehtsaalha lrrlvspggr vvlgegiwqr pptaaelsam wpdasaaehl
      181 dlaglvdlav sagfrpawie tasngewedf esayqsdvee wlaahprhpl aketrdrvdr
      241 hrsmwlrgyr gvlglayltl vpit
//
LOCUS       WP_181789305             285 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181789305
VERSION     WP_181789305.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 285)
  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..285
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32379
     Region          13..70
                     /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..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 masnvnptvr rrrlgqelrr lreqknmtae qvadrllvsq skisrlengr rsisqrdvrd
       61 lcgvyevdde rivgslmqma kesrqqgwwn afgdvpysvy igletaaasl riyqslvvpg
      121 llqtrayaea viagsspevt aadvekrvnv rmrrqdrire teqplrlwav fdeaalrrvv
      181 gneqimreql dhlveaselp hvtvqvlpfe tgahpgvtgq yailefpees dssviylegv
      241 tsdlyleksd dvhnysmmye hlraqalnae qtrkfivdaa kkyar
//
LOCUS       WP_181789398             296 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces phytophilus].
ACCESSION   WP_181789398
VERSION     WP_181789398.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..296
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32392
     Region          5..294
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mddaaltelv dlldleqieq diyrghsrta vvprvfggqv aaqalvaagr tvpadrpphs
       61 lhayflrpgd pgaplvytvd rirdgrsftt rrvvavqhgq pvfnlsasfq lheeglehqv
      121 pmppapdpek lptaeeampr yavnfldpal arrllearaa vdlryaappp wggepgvpre
      181 prsqvwfrtn grltgaidtp llhvclmtyv sdmtlldsvl lahgrggwav gdvvgasldh
      241 amwfhrpfra dewllydqes ptsqggrgls tgriftrdgr laasviqegv irvpra
//
LOCUS       WP_181789506             573 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein, partial [Streptomyces phytophilus].
ACCESSION   WP_181789506
VERSION     WP_181789506.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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 10790020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..573
                     /product="PhoX family protein"
     Region          1..565
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 vviawgdpvl rgapafdgar qsaaaqagqf gynndfltll plrgerdrql lvanheytde
       61 qimfpgydpe nvtreqaeig waahgmsvva veeegrrggk gggslravpr hplnrritat
      121 tefelrgpaa gsdllktsad atgrrvlgtl nncaggttpw gtvlsgeenf nqyfanaeav
      181 tdpvakqrla rygfaggasq rkweqfddrf dvvkepqesh rfgwvveidp ydpdstpvkh
      241 talgrfkheg anvrltrdgr avaysgdder fdylykfvsd krmmrgnsrw arahnmtlld
      301 egtlyvakls gdspageidg sgtlpadgef dgagewikla sgdrsfvpgm taeevyvftr
      361 laadkagatk mdrpedveps pnsgkvyval tnntnrgtgt nakadeanpr nankhghile
      421 ltekrndpas trfdwrlflv cgdpadpsty fagfpkdkvs piscpdnvtf dpygnlwist
      481 dgnalgnhdg lfgvattgry egqvkqfltm ptgaetcgpv vqedrvlvav qhpgevdgat
      541 yenpgsawpd gpgrpnrpav vnvwrsgggr iga
//
LOCUS       WP_181789435             102 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181789435
VERSION     WP_181789435.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>102
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          7..>102
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mnmgegvewg lhscltlawl rdsgpvpirk laawfdlpqe ylkkrlqala ragilasapg
       61 arggfslara peritlmdvv talegplepf vcteirqqgh gg
//
LOCUS       WP_181789807             341 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            phytophilus].
ACCESSION   WP_181789807
VERSION     WP_181789807.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  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 341)
  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 341)
  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 341)
  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 341)
  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..341
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..341
                     /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=36309
     Region          2..306
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrvlltghqg ylgtvmaprl raaghevagl daglfadcvl gpppadppgr qvdlrdvtaa
       61 hlagvdavvh laalsndplg slapeltydi nhhasvrlar lardagvrrf lyastcsvyg
      121 aagggelvae eaplrpvtpy aeskvrvedd lhaladgdfs pvymrnataf gfsprlradi
      181 vlnnlvghal lsgevlvlsd gtpwrplvha adiaraftaa laapreavhd rafnigsefn
      241 nvtvaeiaeq vaaavpgsrv vitgetgadp rsyrvdfsrf rtalpgfdce wtvkqgalel
      301 adayrahglt redferrftr lavlreasaa gavdatlrrr r
//
LOCUS       WP_181789832             260 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            phytophilus].
ACCESSION   WP_181789832
VERSION     WP_181789832.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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..260
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..260
                     /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=28561
     Region          1..217
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mfysamkmsl gnslrlvfrp wvegmenvpd tgaailasnh lsfsdsfflp smlhrkvtfi
       61 akaeyfttpg vkgrltaaff kgvgqlpvdr sgsrgageaa iksgldvler gelfgiypeg
      121 trspdgrlyr gkpgglgrla llsgapvlpv amidtekiqp pgqvvpkvmr pgirigrpld
      181 ftryqgmehd rfilrsvtde vmyeimklsg qeyvdeyata akrrmadeak rrkaeekaek
      241 aekaenaena eksdrrdaaa
//
LOCUS       WP_181789833             265 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Streptomyces phytophilus].
ACCESSION   WP_181789833
VERSION     WP_181789833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 265)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..265
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..265
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28589
     Region          5..247
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mpvlpgaepf rqpggetgvl vchgftgspq svrpwaehla argltvsmpl lpghgtrwqd
       61 lqvtrwqdwy atverelrel sdqcervflc glsmggtlvl rlaalhgdav agvvavnpln
      121 klhgllpkal paarflvrss pgviddiakk gaaetgydrv plhaahslrq llarvdaelp
      181 qvtqpllvlh srvdhvvspv dsarilgrvs srdvtetvle dsyhvatldh daeriftatd
      241 dfidrltvpa ggteqrkear argga
//
LOCUS       WP_181789961             158 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181789961
VERSION     WP_181789961.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..158
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..158
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <20..151
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 lrrtldtavt vgaaaasagl etiveahpda vrcldvllal drdgegaspd elgvygllfh
       61 qtgrdelrrf vrrtlgpvld yderrggdla rtmttyfacd anltrtaael yvhvntlyqr
      121 idritallgp qwrhgdhglq ahlavkvham lsppaapg
//
LOCUS       WP_181789932             205 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces phytophilus].
ACCESSION   WP_181789932
VERSION     WP_181789932.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  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 205)
  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 205)
  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 205)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 205)
  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 205)
  AUTHORS   Rosinski,J.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..205
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..205
                     /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=22920
     Region          4..85
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 mgreperite leqlkafthp lrielyrllt aartatashl aeqadeavsl vsyhlrklae
       61 hgfieeaaeq grdgrerwwr vsaqrsfsfr sadfddtpeg taaltgvtre llatrtrtyl
      121 nyldqqagwg rewtraafts eytlrltage lqelaeemga fvrrwrerae aaaeagadda
      181 gaegaegsag retvalhlyg fpfrp
//
LOCUS       WP_181790168             116 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Streptomyces phytophilus].
ACCESSION   WP_181790168
VERSION     WP_181790168.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 116)
  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 116)
  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 116)
  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 116)
  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..116
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..116
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12296
     Region          16..116
                     /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 mttpqtqtaa hgvpyvtdet fteevlradv pvlvqftaqw cpsckqltpv lgalaaelgd
       61 rvkavrldvd hnpqttvahg vlavptllvf qggepvrsvv garskarllr dldgvi
//
LOCUS       WP_181789917             147 aa            linear   BCT 28-DEC-2024
DEFINITION  Fur family transcriptional regulator [Streptomyces phytophilus].
ACCESSION   WP_181789917
VERSION     WP_181789917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 147)
  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 147)
  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..147
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..147
                     /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=16466
     Region          1..136
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mettdwkrdl rkrgyrltpq rqlvleavds lehatpdgil ievrktaagv nistvyrtle
       61 lleelglvsh ahlnhgppty hiadrhhhlh lvcrvcdrvi eaenavaepf aeelrqrfgf
      121 esdvrhfail grcatctesg kpdasap
//
LOCUS       WP_181789710             399 aa            linear   BCT 28-DEC-2024
DEFINITION  lipid II:glycine glycyltransferase FemX [Streptomyces phytophilus].
ACCESSION   WP_181789710
VERSION     WP_181789710.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 399)
  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 399)
  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..399
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..399
                     /product="lipid II:glycine glycyltransferase FemX"
                     /EC_number="2.3.2.-"
                     /calculated_mol_wt=43757
     Region          23..388
                     /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 msysepgrta hrqepgapga slavrpitpa ehlafvrrqr svsflqtpaw grvktewrse
       61 slgwydgrel vgaglvlhrp vprldrftla ylpegpavdw sgdvdawldp laarlkahga
      121 fairlgppvr tstwnadqvk egvadpgtgr ltelsghwad pvgthvtgrl rdagwlpqsp
      181 edgfgtghpq fkfeiplagr teddvltgmn qqwrrnikka aragvevavg egsadlaafh
      241 alyahtaerd rftprplryf etmfaalsae dperirlyla rhegdlvaaa vlvrvgahav
      301 yaygasstgk revrgsnacq wamirdslaa gcdvydlrgi tptldaddph vglitfkagt
      361 ggqavryvge wdlplrpvvy rafglylkrr esvrrrgrt
//
LOCUS       WP_181790239             267 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Streptomyces phytophilus].
ACCESSION   WP_181790239
VERSION     WP_181790239.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 267)
  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..267
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..267
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=27857
     Region          13..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(13,15,24..26,28..29,34,41,49,51,52,54,61,63..64,66,
                     69,75,77..78,92,94,105,107,109,111,120..128,130..132,135)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 mtdddptarl tghevvvpgt pdevwraiat gpghaawlfp adidpapgga mtvrrepyge
       61 tahatvtdwd pphrfgyeep agpdapplat eflvqaaggg scvvrvvngf rhggegwedl
      121 vdgagegwrm sltvlraylt hfaglpagnv dvlvglglpa aerpraaavl dlllgiagaa
      181 agtpfrtpar vpelagtved rspgyvllra aepypalyal scfpmapgap lsanllarly
      241 gappgaaare edrwrtwltg arsafdn
//
LOCUS       WP_181790174             346 aa            linear   BCT 28-DEC-2024
DEFINITION  3-dehydroquinate synthase family protein [Streptomyces
            phytophilus].
ACCESSION   WP_181790174
VERSION     WP_181790174.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Carpenter,E.P., Hawkins,A.R., Frost,J.W. and Brown,K.A.
  TITLE     Structure of dehydroquinate synthase reveals an active site capable
            of multistep catalysis
  JOURNAL   Nature 394 (6690), 299-302 (1998)
   PUBMED   9685163
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..346
                     /product="3-dehydroquinate synthase family protein"
                     /EC_number="4.2.3.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003856 - 3-dehydroquinate synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36300
     Region          11..339
                     /region_name="AroB"
                     /note="3-dehydroquinate synthetase [Amino acid transport
                     and metabolism]; COG0337"
                     /db_xref="CDD:440106"
ORIGIN      
        1 mttsketgaa rrivvrlger syavhigpgv rdllpgvlag igarrvavvs arpradlpet
       61 gvetlfltar dgeqdktlat vermcrafae fglsradavv scgggtttds vglaaalyhr
      121 glpvvhlptt llaqvdasvg gktavnlphg knlvgaywqp aavlcdtdyl rtlpprewtn
      181 gygeiarchf igagdlrgrp laeqiaasva rkadivaade rdaglrhlln yghtlghale
      241 ratdfamrhg egvavgtvfa grlagalgri gadrvaehld vvrhyglpwe lpagpadgdl
      301 valmrldkka tsglsfvldg pkgaelvsgv pesvvlsvla rmprrg
//
LOCUS       WP_181790347             334 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces phytophilus].
ACCESSION   WP_181790347
VERSION     WP_181790347.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  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 334)
  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 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  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 334)
  AUTHORS   Rosinski,J.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..334
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..334
                     /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=36317
     Region          257..325
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 magklhvhfn drdfrhvqla rtadpiweai lglhvaytpa pllparlrpf hrrarhrlrh
       61 hdlrrtcrll ngiapadaay fpdfltpves edgitaglrt lratpatrla reirlaarhr
      121 plppwtrrla agdrtvlgdl adalqhvhnr liapdwseie atvaadrtrq lealeagmpa
      181 vlatldpftw tdpvlsapyp vdstlhlhgr girlipsyfc httpvaiadh glppvvvhpv
      241 rrhpapdgtg ratphrdtal aallgtsrar ilaaltptsa pattgglaar lgmpassvsg
      301 hltvlrragl aesertgphv vhrltargrh lldg
//
LOCUS       WP_181790381             341 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Streptomyces phytophilus].
ACCESSION   WP_181790381
VERSION     WP_181790381.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 341)
  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 341)
  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 341)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..341
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..341
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36738
     Region          60..339
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mvpvltvrnr llllfsalll tfvpaapsla aaapeaapga aakgggprgd aevvgvtrvg
       61 erlvdlsvrs palggrtvpv rlltpdgwdp depgqkwptl wllhgccgdy tswtsatdve
      121 dtdslrdvlv vmpeagwngw ysnwwnfgkg gdpawetfht delrrllesd wgassdrvva
      181 glsmggqgal myaarhrgmf kaaaaysgaa hpllndesvn rimgffggqg ddprrvwgdp
      241 vdqraiwqah dpyylakklk stpvylscgd gtagpldppg atdaleadfn rqnqalaael
      301 krvgakkvit nlygpgthrw aywerelhas lpmllgalkv r
//
LOCUS       WP_181790373             226 aa            linear   BCT 28-DEC-2024
DEFINITION  YceD family protein [Streptomyces phytophilus].
ACCESSION   WP_181790373
VERSION     WP_181790373.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 226)
  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..226
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..226
                     /product="YceD family protein"
                     /calculated_mol_wt=24397
     Region          18..201
                     /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 mrrvhesrka lkahpdhrap lvfdtrdlgr rpgtlkrltr tvpapkdlgn evvgvpegdp
       61 velelrlesv megvlvtgta rgrvtgecvr cleplgqelr vdfqemysyp etdargrvar
      121 gggsgadaee adaeegtlyv eddmidlepe lrdavvlalp lqpvcredcp glcpdcgarl
      181 addpdhrhdv vdarwaalqg laetvsdgek ndasgavdga gekqek
//
LOCUS       WP_181790209              75 aa            linear   BCT 28-DEC-2024
DEFINITION  glutaredoxin family protein, partial [Streptomyces phytophilus].
ACCESSION   WP_181790209
VERSION     WP_181790209.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 75)
  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 75)
  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 75)
  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 75)
  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 75)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>75
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
     Region          4..74
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 magtvtmyst twcgycrrlk sqmdregipf eevnieqdpk saayvesvnn gnqlvptvvv
       61 vprqggesva mpnps
//
LOCUS       WP_181790427             320 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181790427
VERSION     WP_181790427.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..320
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
     Region          25..293
                     /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 ewfeterril vatvesalrl grttqaadla lelasffdlr gyygdwlrth qlvldampap
       61 sdaraaallr nigqlhlyrd ryadardsfv waraifgavg hpageavaaa gegsvhrilg
      121 dldaalatft dalsgfgdvg drhgeavarn aiasvwlerg npraaaswld galalardlg
      181 drhreaqvrr riavlhdlrg epdlaqaela raldifcdla dthcaayvqe sigelclrlg
      241 nageasalla dalavqrqlg drraeaslac llgelhratg rvqtardyfh rslstwrrle
      301 ahdradvvhe klralhsgqg
//
LOCUS       WP_181790355             156 aa            linear   BCT 28-DEC-2024
DEFINITION  RCC1 domain-containing protein [Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis].
ACCESSION   WP_181790355
VERSION     WP_181790355.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
  ORGANISM  Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 156)
  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 156)
  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..156
                     /organism="Myxococcus
                     llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogoch
                     ensis"
                     /db_xref="taxon:2590453"
     Protein         1..156
                     /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=15902
     Region          12..>155
                     /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 mraaegfarq gtvlggrnhs lalrsdgtvw awgdntqgql gvstpafsrt ppqvpglfgi
       61 taidggdght lalktggtvw sfgandtgql gdgslgvrrt spvqvqglfg mvsisagaqh
      121 slavksdgvv wgwgdnsqga lgngmssirl rpvrvf
//
LOCUS       WP_181790537             603 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis].
ACCESSION   WP_181790537
VERSION     WP_181790537.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
  ORGANISM  Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 603)
  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..603
                     /organism="Myxococcus
                     llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogoch
                     ensis"
                     /db_xref="taxon:2590453"
     Protein         1..603
                     /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=64780
     Region          19..510
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mltvihhpaq fppghtvhgw rivklvgaga ygavykvemn gkhfamkvam hratsgdeek
       61 adarlkrelg clvhlrhpni iaahahgrwp dfesgwlyvi lafvdgytla ewvervhpta
      121 qevvrlfvkl saavdymhgr gvfhrdlkls nvmvrasdne pfiidfsagd ythaedltda
      181 plppgtrryr speasrflre ngdnrdarye fkvtddvyal gvclfdvlta pqpasdsvkt
      241 pvegrmmpph prrlnervpg alsdavmrfi arkpenrppt aeavrrelea laketgpewv
      301 tplhtltakp lltpatgted aakparprrg ivlgalgavl tlaalvgffa prqsgqessa
      361 masvepsaqr dagtgapllv vapqedagmp lgtgvvspap vasspgvals pqgpvqkesp
      421 svkrapivas tsespamkap assggraefl kkcaaatavv alqmgcpsss qvrpgpsecp
      481 deareamfev lriregdsvv vtldksqpga mnergdysdg pvrgvvlngn relptgtvll
      541 grlwtrggal larytearys ngrtypvciv igengaeeae egaqpgtvyf prsaygyavk
      601 nwp
//
LOCUS       WP_181790566             210 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces phytophilus].
ACCESSION   WP_181790566
VERSION     WP_181790566.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..210
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22388
     Region          1..200
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 msrlhifdmd gtllhgssan ielarqlglv aefraldaaf gsgeidtyey aghahgmwss
       61 ltpeilgraf agapwlagir evwaditdrg ehcavislap gffverllew gvhaahgsrf
      121 palpfrepvd magilgppdk vriadllcaq ygltradcva ygdsmsdtdl favvprsvav
      181 nadhhvsgva shaysgrdlr gayaltrtag
//
LOCUS       WP_181790564             167 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Streptomyces phytophilus].
ACCESSION   WP_181790564
VERSION     WP_181790564.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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 167)
  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..167
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..167
                     /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=18086
     Region          13..137
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04669"
                     /db_xref="CDD:467553"
ORIGIN      
        1 mtvshrpvvk rtaravlldg demllikrtk pgrepywitp gggvepvdas vvaalhrevd
       61 eelgarvtgv vpvfvdtvpe gehgvkvqhf facrltsmdw trrhgpevde prgeyeavri
      121 pftregvdsv dvvppslray lrmniegvla vladdflpdg spaggpg
//
LOCUS       WP_181790645             253 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein, partial
            [Streptomyces phytophilus].
ACCESSION   WP_181790645
VERSION     WP_181790645.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 253)
  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 253)
  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..253
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>253
                     /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..253
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mfslaaqeql lpgdtlqqkw efaqaagydg ielraqgdlr faarlpelkr aladgvvmpt
       61 vcvemlhffg afdtgqrrda vaqlksqlsv iaeiggtgaq tpasygmfsr rlppftpprd
      121 eagdravlld glaelgehar regvtlflep lnryedhmvn rleqatelir atgldsvrig
      181 idsyhmniee adpaaaildn apwighaqvs dsnrfqpgag hldwpawlga lkaagytgwl
      241 aaecrltgdp aaa
//
LOCUS       WP_181790721             278 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            phytophilus].
ACCESSION   WP_181790721
VERSION     WP_181790721.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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=29804
     Region          9..253
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 msahrpprtv lltgaaggig tlmrgllhah ghelrlldhv aaapgperfv tadladrgal
       61 reavrgvdav lhlagisles tfekvlranv egtyhlyeav reegvrrvvf assnhavgfh
      121 prprhpgrvp aaeligpgaa hrpdtfygls kcfgedlaql ywdkhgietv svrigscfpe
      181 ptsvrmlslw lspadgarlf haaltapdvg htvvygssan trawwdlgta ralgyepqdd
      241 seayadklla elgpddtdap dqanlggpfc tdppiwph
//
LOCUS       WP_181790804             217 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces phytophilus].
ACCESSION   WP_181790804
VERSION     WP_181790804.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  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..217
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..217
                     /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=23180
     Region          44..210
                     /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 mdsatsdtra tsarpagaae raplartadn glkivvvggf gvgkttmvrs vsdirplnte
       61 etmtlagrgi ddrsavpgkt attvafdfgr isldartvly lfgapgqerf wflwdrlfsg
      121 tlgaivlvdh rrladswyai drlehhgtpf ivarndfggp pytgaevrea ldldphvplv
      181 dcdarsress kgvlialveh lqrlaaapvp tapetat
//
LOCUS       WP_181790853             202 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces phytophilus].
ACCESSION   WP_181790853
VERSION     WP_181790853.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     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=21987
     Region          20..199
                     /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 mnepdtrapd avrdtylppv kilvaggfgv gkttavgtvs eitplrteer lsaagvgvdd
       61 lsgieqksat tvamdfgrit ldvavlmlfg tpgqerfwfm wddllrgalg avvlvdtrrl
      121 drsfaavdff esrdlpfvva ancfhgeqdy dpeeirdalt lrepstpivl fdarrrdsvr
      181 gvllalmdhl iasaepahaq rt
//
LOCUS       WP_181790786             404 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein, partial [Streptomyces phytophilus].
ACCESSION   WP_181790786
VERSION     WP_181790786.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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 404)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..404
                     /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]"
     Region          3..400
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(40,47,71..72,79,83,90,234..235,238,242..243,246,279,
                     284..285,288..289,291,314,341..343,346..347,349..351,355)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(47,65,67,70,72..73,155..156,177,233..234,237..238,
                     242,285,288..290,390)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 tdpypayawl rthapvhrtt vpsgvdawlv tryadarqal adprlsknpa hhhsdktgip
       61 gergaglmth llnidppdht rlrrlvsqaf tprrvaafap rvqeltdrli dgfadrgead
      121 lihefafplp iyaicdllgv paedqddfrd waavmlhssg grppearnhg kgsrggvara
      181 vkkmraylae lihrkraalg ggdaadddli sglirasdeg eklteneaaa mafillfagf
      241 ettvnligng tyallthpae rarlaaepal lpsaveellr ydgpvelatw rfatepleig
      301 gqrvavgdpv lvvlaaadrd parfadpdel dlsrrdnqhv gyghgihycl gaplarleaq
      361 talgtllrrl pdlrlaaets elrwrgglim rglrtlpvhf gpsl
//
LOCUS       WP_181790364             100 aa            linear   BCT 28-DEC-2024
DEFINITION  GroES family chaperonin [Streptomyces phytophilus].
ACCESSION   WP_181790364
VERSION     WP_181790364.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 100)
  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 100)
  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 100)
  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 100)
  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..100
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..100
                     /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=10811
     Region          1..84
                     /region_name="Cpn10"
                     /note="Chaperonin 10 Kd subunit; smart00883"
                     /db_xref="CDD:197951"
     Site            16..29
                     /site_type="active"
                     /note="mobile loop [active]"
                     /db_xref="CDD:238197"
ORIGIN      
        1 mlhdrvlvri dtaegerrss ggivipataa vgrrltwadv vatgqnvrtv epgdrvlfdp
       61 edrgevevrg vgyvllrerd lhavaserle gsddstglyl
//
LOCUS       WP_181790861             206 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces phytophilus].
ACCESSION   WP_181790861
VERSION     WP_181790861.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  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..206
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..206
                     /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=22184
     Region          39..194
                     /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 mdsnsfdavv gprsedllpa sattsvkvvv vggfgvgktt mvgavseiep mtteetmtra
       61 gegvdhlagv pdksettvam dfgrislner mvlylfgapg qqrfwflwqg lfegalgavv
      121 lvdtrrleac fdvlgrleeg avpflvavnr fpdapyhsld eirsaldlpe hvplitcdar
      181 drdssrsvlk slvrflhsia ltteas
//
LOCUS       WP_181790891             190 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181790891
VERSION     WP_181790891.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 190)
  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 190)
  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 amino end.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..190
                     /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          <3..78
                     /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 gpvtgvepsa rmreqavaya ahprvsyvpg raealplpdg avdfalgflv whhvrdkpag
       61 arelhrvlrp ggtlllrtel tdslpdlwyl dafprgrevl aalyeplsal rgtfeaagwe
      121 laavgevalp apgtcagala rlrtrafsif ehmpeadiea gfaelerrva adpraparvs
      181 pgtvvtfrra
//
LOCUS       WP_181790931             555 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181790931
VERSION     WP_181790931.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  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 555)
  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..555
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..555
                     /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          2..555
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 afadevtava kglvaaglep ggrvaimsrt ryewcvldfa vwaaggqsvp vyatssadqv
       61 gwilrdsgtr fvvaetaane etvrtasgqa rvwqldagcv delkalgrdv pdheiakrra
      121 altpdtiatl cytsgttgrp kgcvlthgnl haeaansvel lhpiftevtg rtastllflp
      181 lahifgraiq iaclsariei ghwpsikpde lrpefkvfrp tflvgvpylf ekihhtgrem
      241 aeklgrgssf dradriavrf geahlhrflg tgkgpglrls lawglydllv yrrirkelgg
      301 rlnyaisgas pldrnlnlff yaagiviyeg ygltettaaa titpplrprp gtvgrplpgt
      361 airiaadgev likggivfge ywrnpeatee vladdwfatg dlgaldedgy ltitgrkkdl
      421 littggknvs pavledrlrs rppvgqvlvv gdkrsyvaal vtlereavah wlavrkrprd
      481 tplaelrddp elradvqrav dyaneavsra esirrfvivg gefteengml tpslkvkrha
      541 veaayakeie glyen
//
LOCUS       WP_181791135             917 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis].
ACCESSION   WP_181791135
VERSION     WP_181791135.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
  ORGANISM  Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 917)
  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..917
                     /organism="Myxococcus
                     llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogoch
                     ensis"
                     /db_xref="taxon:2590453"
     Protein         1..917
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=99176
     Region          47..473
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          501..907
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mssqilsrss prarrmtavv vvlsavlgac stlpqrgqvv mrdvsfplrd frmpsglrvv
       61 veqdtrapvv avvalvgtgg ssdpvgkegl ahvvehlafr srhagspsvw trledvgagq
      121 fnaftsldht lyqtlapkes laallkmegq rmsaplagvt pevfaverev vrnelrqrne
      181 tgyvgqvfsw mhaaaypaeh pysrpiigth esltalalad aqrfarnhyr pdnitlviag
      241 dvdlaaveav lmqnlppawv gtgaplavgt rmpqvteppl kaaspsipef kasvgspely
      301 lswvlprsfd easaihdfvr vnlnrnlqga mrndgdiagi gtqvvagtrs sllvvrvalt
      361 tgehprksad kvldqvhetw tqtinagavl grefdfqsmr rnvitgmvle sedlmartvr
      421 raelthfmld vrgytrsqma lmtidggkvt dfaykwlqrd rariilvrpg esagvsvaap
      481 pplpveystl taeqritpsm ltalsapvqt lkldngmevl laprpglpvv rvgavlgggs
      541 tygaragaaa ladygsfres wfeghashwg lhvwdsmrrd hqrievsgta gnvgnmlaml
      601 seqlsttrts ldavkylqeq vvpwrravda hpevraerel mkalygahay srdatgeema
      661 qvtwdevqsw igdvyrpant vvviagefdv ktveplvrey lggwkhgpat avsvpaapsl
      721 pepsakartl vtprpgasqg hlqlacrlpt atpeaearys lmaelvsaya fnelrsqqga
      781 sygfsastwl arggashlvv egvvdaqrma egaksvqaml snfatnvder elsrartrll
      841 arqavsyiss eawvqallda rvrgfppesl aqrpahlqav tsaalkqefd gclkrlvvgv
      901 vadegqarta lqalsvp
//
LOCUS       WP_181790969             537 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis].
ACCESSION   WP_181790969
VERSION     WP_181790969.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
  ORGANISM  Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
            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 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Myxococcus
                     llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogoch
                     ensis"
                     /db_xref="taxon:2590453"
     Protein         1..537
                     /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=57537
     Region          69..528
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mprtplfdlf rqttrkalaa aspeanalea rrvarmdrrs vlkgvtalgm gmavraarae
       61 earppaalrv givgaglagl acayelrcsg vqatvheare rtggrvfsmg gafggpvifp
      121 gqvverggef idsghstilg yarefhlere dllrvpgdvf yffggqlyse adileeycpl
      181 iaainqdlsr lseaptaadh teldrrfdll dlvtylearn tgplvkaaii aayeaeygqa
      241 adelsclnll fliqteqcrr fepygesder yrllggnqqi prelaarlpg qvrqgerles
      301 vrktptgals ltlrrgstsy tatydvvvla ipftvlrrve laaslglpaw ktrvirelgy
      361 gtnakmmvgy rgpvwrasgc sgasysdlmn hqatwetnpt ratagdavlt dfasgprgag
      421 mdpgnvagea erfvaamgrv vpgtagavkr gvdrrivahl ehwpsnpnal gsyssyrpgq
      481 ftslagtegt pvgnlyfage htssfyeaqg ymegaaatgk staqailama nvavasg
//
LOCUS       WP_181790981             567 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181790981
VERSION     WP_181790981.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 567)
  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 567)
  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 both ends.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..>567
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          2..>567
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 aaarggapvr elsadaayfh dalldtaclh ilhffsqrst fvartlveqs rrqadqiarl
       61 daliarnplp aardaafera yfayvakkhg kltiygvdla dspakwpldv aylrleaaae
      121 hhpaapshep lpyadlggla gsdplpdpvl padqalatye rvllrgaags gkttlvqwla
      181 lsatradtga ehtmdylagr vpfvlplrtl trhgqrlpap rdflpatgsp lagaqpdgwe
      241 hrvlsarrgl llvdgidevp raerdrtrrw lsdlidaypg nrwlvtsrps avgedwlaae
      301 gfseltlapm rpadlarfia rwhaavrtgd paaddaqlaa yeaqltaavr htsdlgrlat
      361 nplmcglmca lnrarrghlp rgrkelyeaa lsmlltrrdr erdmavpdlr depqlqvlqr
      421 laywlirngr teldraraes ivaaalpavp evaalgdata vlehfrdrsg llrepgpgav
      481 dfvhrtfqdy lgaraavedg digvlaahaa ddqwedvirm avaqgrprer eeilrellaa
      541 aearegvegv rirllaaacl ehaaela
//
LOCUS       WP_181791145             353 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis].
ACCESSION   WP_181791145
VERSION     WP_181791145.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
  ORGANISM  Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 353)
  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 353)
  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..353
                     /organism="Myxococcus
                     llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogoch
                     ensis"
                     /db_xref="taxon:2590453"
     Protein         1..353
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=39524
     Region          42..293
                     /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"
     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          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"
     Region          166..196
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          201..229
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          302..330
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrlarlasal slvltlplag clttpppher alinnelctq elhngdlvra dvycdlglef
       61 spqyadlwvn kglialangn ndeakkhfik alrynqehlq ayqslgviyn eegahgkahd
      121 nfrralkvnp dnletrynla ytlmkmrkft eakkelrtll avnpnlaaah htlgiiafge
      181 dqfedaaeam aqsvaldpnn pdawhdygnt lmelsryada reafsncaql npkatnctnn
      241 lalaqrkaal tdaafkevkd tqqaensapa lfmlarqfre kgllaeeett ykkcvklesk
      301 fapchyglfe lfqdankheh aeiacknflk yatseefpte yqacekylsn atf
//
LOCUS       WP_181791191             270 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis].
ACCESSION   WP_181791191
VERSION     WP_181791191.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
  ORGANISM  Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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 270)
  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..270
                     /organism="Myxococcus
                     llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogoch
                     ensis"
                     /db_xref="taxon:2590453"
     Protein         1..270
                     /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=29307
     Region          18..266
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mttlgfdell ttargvaaes vlvvtgagis lasgiptfrg tdpgavwane vtqkgtrayf
       61 klfpheswkm ylqrlelark akpnaahaal vdwerwqtgq gggftvvtqn vdslheqags
      121 qalvkvhgsl qlarcsargc elgpptgtip letldfsafh aspsaetvpr cpscrsrvrp
      181 hilwfdeyys ehlgyeierv ydlarqgrlv vfigtsfsvg vtesirafal krrtpmfsid
      241 psgvappqgi qavtgraeel lpelvrslrg
//
LOCUS       WP_181791034             269 aa            linear   BCT 28-DEC-2024
DEFINITION  CheR family methyltransferase [Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis].
ACCESSION   WP_181791034
VERSION     WP_181791034.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
  ORGANISM  Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 269)
  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 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   3  (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]
REFERENCE   4  (residues 1 to 269)
  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..269
                     /organism="Myxococcus
                     llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogoch
                     ensis"
                     /db_xref="taxon:2590453"
     Protein         1..269
                     /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=30094
     Region          1..263
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mkdddctell rwaaprlrlr legfhrvrgq vckrlgrrlh alglphlaay rerldsdpee
       61 wavldalcrv tisrfyrdar vfdalrdell pallesspvl rvwsagcasg eepytvsilf
      121 rlgllprfpr arlelvatea dgallarark gcyprgtlre lpadwrteaf pgsdtepclt
      181 peyrnglifl hedlrarmqe gpfqlvlcrn vaftyfapsl qrevlaglva rlapggllvi
      241 gtreslpegg vdlervagal pvfrvpvsr
//
LOCUS       WP_181791277             242 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein, partial
            [Streptomyces phytophilus].
ACCESSION   WP_181791277
VERSION     WP_181791277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 242)
  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 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   3  (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   4  (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   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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>242
                     /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]"
     Region          2..>242
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkilvtgatg algsrllpll taaghtvtgt ttseakadrl raagvepavl dvldaaavre
       61 tvanaapevi vheatalshk ielrprdlrr ldasfaptnr lrtagtdnll aaaaesgtrr
      121 fvaqsfagwp ykreggwikt eedpmetdpp agseeslaai khleeavtta pgmegivlry
      181 ggfygpgtsi spggqqaemv lkrrlpvvgs gdgimslihi ddaaaataaa vergapgvyn
      241 vt
//
LOCUS       WP_181791297             221 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Streptomyces phytophilus].
ACCESSION   WP_181791297
VERSION     WP_181791297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 221)
  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 221)
  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..221
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..221
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=23420
     Region          1..193
                     /region_name="TerY"
                     /note="Uncharacterized conserved protein YegL, contains
                     vWA domain of TerY type [Function unknown]; COG4245"
                     /db_xref="CDD:443387"
ORIGIN      
        1 mqilpfylvc desgsmggap ieainkalpe lhqeistnpt vadktrfali gfsddaqvlq
       61 pladlselnt lpalaaggvt sygqafralk acietdvgdl kaeghevyrp vafflsdgvp
      121 tdgqweealr eltesrycpk iiafgigead tatisrvanf rafmqqdsai spaaalrefa
      181 asltrsivrs assisadgsg dftlavddkv pgfetvtldk l
//
LOCUS       WP_181791442             278 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            phytophilus].
ACCESSION   WP_181791442
VERSION     WP_181791442.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..278
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31435
     Region          6..67
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(11,15,40)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(14,39)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(21..22,33,36,40..41)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          93..273
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mrriilgnnl rrlreqrnit fqaaartiga sqpklsrlel grggckehdi aalltlygve
       61 deaerehyla larganttgw whqysdvtpt wmetflglee aaslirsyqa qripgllqta
      121 dyarafaqia ypnadeaaie rhvdlrlrrq qilghadqpa rywvvldeaa lrrplggrrv
      181 mraqiehllr ilelsnitvq varlatgrfa avvspltilr faepdlpdva yieqltsaly
      241 ldkrndvery lltmdglcaa aekqessqem lekllaey
//
LOCUS       WP_181791596             144 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein, partial
            [Streptomyces phytophilus].
ACCESSION   WP_181791596
VERSION     WP_181791596.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  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 144)
  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..144
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..144
                     /product="sugar phosphate isomerase/epimerase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
     Region          <2..141
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 elaeaakraa ghglalgyhn hefelcqhvg gvpalevlad llaglgtsga tvqfevdtyw
       61 aavggqdvpa llgrlgervt hlhikdgpvt kddpmtavga grmpveavla agagarrhiv
      121 eldacatdml tavresfdwl egkr
//
LOCUS       WP_181791403             328 aa            linear   BCT 28-DEC-2024
DEFINITION  SMP-30/gluconolactonase/LRE family protein, partial [Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis].
ACCESSION   WP_181791403
VERSION     WP_181791403.1
KEYWORDS    RefSeq.
SOURCE      Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
  ORGANISM  Myxococcus
            llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogochensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Myxococcus.
REFERENCE   1  (residues 1 to 328)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Myxococcus
                     llanfairpwllgwyngyllgogerychwyrndrobwllllantysiliogogogoch
                     ensis"
                     /db_xref="taxon:2590453"
     Protein         <1..328
                     /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]"
     Region          25..263
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 ppapassasd vsaksrprvt eqlplppgft ipngiahavd gtlyvgsvad grvlrrapgg
       61 awtelfpgse qvfsatslrl daprnllwgt spdamgllrp kgtmggrrha rifaldartg
      121 alrklvhlpe galgndltva pdgglyvtds arasvlylrp ggehletwvt dprfkaqgtg
      181 msavgpagia laadgrtlav ntygpgrlfl ihpgassdap prvtevelpr rlenpdgmrf
      241 apdgrlllve gsiqsgdgrl irvevlgktq gpralevlas glespvnltv sdegtvwvte
      301 arlrdrllkg tsvplpenfw vasvplsr
//
LOCUS       WP_181791389             259 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfite exporter TauE/SafE family protein [Streptomyces
            phytophilus].
ACCESSION   WP_181791389
VERSION     WP_181791389.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..259
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25903
     Region          46..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 mpdiplstlv mlcvvaaaag widavvgggg llllpalllg hphlqpayll gtnkavaivg
       61 tsaaavtyar rspvdvrlav rigaaalags algaffaagv ssdvlrpvim gvllavlafv
      121 alrpsfgtda patgpvtprr vaaavalagl gigfydglig pgtgtflvla ltavlrlnlv
      181 qasatakivn vctnfgalvm fsvqgtvlws laallavfnl gggwfgahma lkkgsgfvrg
      241 vlvvtvvglv aklaydqwa
//
LOCUS       WP_181791266             454 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181791266
VERSION     WP_181791266.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  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 454)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..454
                     /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]"
     Region          1..433
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 wtrlapdpla adghggmpra gydvgwqvae derfrrvvrs gsavalpelg hsvhpqvrgl
       61 rpgrqyfyrf rthgrtspvg rfrtapdprs ahgsftfata scqawyhgyf aayrdmaaqd
      121 pdvvfflgdy iyeygitaan mwrnaplpga rhetetstla dyrlryalfk sdpglqavha
      181 aapwilapdd hevqndysde tsyyglseed fllrravayr ayyencplpa lalghgpdar
      241 lhrrlrygpa alhvldarqy rdpkpadaae qhapgrtmlg reqerwlyhg lrtsgarwnl
      301 llqqvglvrv tenrvdqwdg ypaarqrlld vlgepgvaps vvftgdchrs iagdlladfa
      361 dpgsrvvgse flgtsiasdg dgaptdnytk dwmqhpwmrf ydgrrgyvlg hadaaavtag
      421 yravpyvrad draagfaldr frvahgrpgm qkvs
//
LOCUS       WP_181791608             311 aa            linear   BCT 28-DEC-2024
DEFINITION  COX15/CtaA family protein, partial [Streptomyces phytophilus].
ACCESSION   WP_181791608
VERSION     WP_181791608.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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 10004065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>311
                     /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]"
     Region          12..300
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mlnplaliae rwtptqktvq ratlsavlms ivivvtggav rltgsglgcd twpkcsddsl
       61 latsemgmhg aiefgnrllt yvlcaavgwa iiaaratkpw rreltrlgwl qfwvvmgnav
      121 lggaavltel npytvaahfl latglitity ltwhraregd ggpdmlvgav vrrltralva
      181 vavlllaagt vvtgtgphag dssdvprmgw iswdhaakvh svtawavval tvaiwvtlkl
      241 vdgpagplsr trdlflvlms qavvgyaqyl tdvpevlvmi hlfgstlvwi avlrvvvslr
      301 hrphvepaev p
//
LOCUS       WP_181791690             315 aa            linear   BCT 28-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein, partial
            [Streptomyces phytophilus].
ACCESSION   WP_181791690
VERSION     WP_181791690.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 315)
  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 315)
  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..315
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..315
                     /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          <22..305
                     /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 eeseaterye aarrasaaqr vkiaklqrav rakhrrlvvl rgrigqlaar eyqsgglgpt
       61 aqllfsrtpe dlldkvflld kgeqaaagly hraeraerrl adererqava ladlraelrt
      121 qarvkrlies klaraqgrle klqsaqtars rssgcpraer sravtlstdg kalagrkwta
      181 pvarytlssr fdqaggmwss rhtgldfavd egkpvgsvgy gavygigcdd afgnsvtvrh
      241 ddgyytfyah lsevrakpge rvfpgqplgl agttgnstgp hlhfevrvtp qfgsgidpep
      301 wlrdkgvrlr gapae
//
LOCUS       WP_181791787             280 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181791787
VERSION     WP_181791787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 280)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>280
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
     Region          3..>280
                     /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 mgstghgplh gvrvvelagi gpgpfaamll adlgadvvrv drpggpglgi dpahdltnrn
       61 krsvvldlks aagaaaalal aeradilveg frpgvaerlg vgpgdcharn prlvygrmtg
      121 wgqdgplaat aghdigyvav tgalgmigpa dgppavpanl lgdyaggsly lvvgvlsalq
      181 harttgegqv vdaaivdgta hltsmihama aagawhdrrg anlldggapf ygvyetadgq
      241 ymavgalepa fyeefvrllg vsgtlpdrad paawaelrer
//
LOCUS       WP_181791770             331 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein, partial [Streptomyces phytophilus].
ACCESSION   WP_181791770
VERSION     WP_181791770.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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   5  (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   6  (residues 1 to 331)
  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 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 10543770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..331
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          49..187
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
ORIGIN      
        1 erwrlspwav styllggtlp dgtaitpkyv gprrivevav atlatdrall llgvpgtakt
       61 wvsehlaaav sgdstllvqg tagtpeeair ygwnyaqlla agpsrealvp spvmramaeg
      121 mtarveeltr ipadvqdsli tvlsektlpi aelgeevqav rgfnviatan drdrgvnels
      181 salrrrfntv vlplpasped evgivtqrva qigaslqlpp lpegvdeirr vvtvfrelrd
      241 gqtadgrtkv kspsgtlsta eaisvvtggl alathfgdgv lrasdvaagi qsavvrdpaa
      301 dsvvwqeyve tvvrerdgwk dlyracrels a
//
LOCUS       WP_181791833             231 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181791833
VERSION     WP_181791833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>231
                     /product="coiled-coil domain-containing protein"
     Region          51..>209
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 msahrrstrp cgagrlrtgv ltaaaaaals gspavfsgls daalaapddh aearervhdl
       61 yaqaeratek fnaareraee lrrkaermqd raardlarin rmrtelgsla gaqyrsggid
      121 pnltlilses pegylekaat lerignlqsg rlrqlvglqr rleqqrvrar dtlaelerer
      181 dalaghksev tdrlararql lnslpkeerp etrrsrasrs aptpdfgsap a
//
LOCUS       WP_181791731              91 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181791731
VERSION     WP_181791731.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>91
                     /product="RrF2 family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
     Region          1..>90
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mtegvewalh sclnlawagp drpvtaarla ayhelpapyl nkqlqalvra givastsgpr
       61 ggfrlvrpla ritlmdvvaa iegpgeafrc t
//
LOCUS       WP_181791983             375 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Mycolicibacterium
            parafortuitum].
ACCESSION   WP_181791983
VERSION     WP_181791983.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium parafortuitum (Mycobacterium parafortuitum)
  ORGANISM  Mycolicibacterium parafortuitum
            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 11467523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Mycolicibacterium parafortuitum"
                     /db_xref="taxon:39692"
     Protein         1..375
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=38681
     Region          22..373
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mtirrtgvry alkrttcgfa tavlvaamav ggaiadpaad alarlnelsq qavqsrqalt
       61 taqydaevkf aeqaaaaerh radqaaldaa tadvaalqga vdrvaamdym sgsrtefaal
      121 ltaaspqkli dqlamqrtlg triadqmraf rsareraaga aqaseksaad asaaaeaaaa
      181 iraelqakla ellqqiaaae aqyaaltpqq qaivdaappp valppaappp pvppiealpa
      241 ippgdvappp aapipdvpea lpmgvaveag lqpnailaar avsqqfpqia niggvrpdsk
      301 pwhpsglaid imipnhgspe gialgdqima yalanaarfg lqdviwrgty ytpagpqatg
      361 yghydhvhlt vtprr
//
LOCUS       WP_181791896             300 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein, partial
            [Streptomyces phytophilus].
ACCESSION   WP_181791896
VERSION     WP_181791896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         1..>300
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          174..240
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
     Region          241..300
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mttldevpql rragaadrpt rrrstsslps laprrrtvlq satvvgfaal gvfgaareay
       61 adgydiwega cpsyasehdc spgcgpstvh aaacetsgph agfhrndgvt wtlrpnqcys
      121 gsydgwlwaf sgacgacgcg ierrchdgyf nsgsgwvrsi crwttdcgce galawptlrd
      181 gsrgpdvsta qhllgfrafp tepdgifgpd tetavtgfqe aqglqptgtv nattwthlva
      241 tvrqgdsgaa vsaaqrqlvk hgypltvdgk fgtltadaar efqrgagltv dgvvgqqtwr
//
LOCUS       WP_181792017             386 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Mycolicibacterium parafortuitum].
ACCESSION   WP_181792017
VERSION     WP_181792017.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium parafortuitum (Mycobacterium parafortuitum)
  ORGANISM  Mycolicibacterium parafortuitum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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..386
                     /organism="Mycolicibacterium parafortuitum"
                     /db_xref="taxon:39692"
     Protein         1..386
                     /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=43693
     Region          91..338
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mmavlaadcp ldadvlhara reatglddfg pddyrerlnl ylaelreidm hapgivnfha
       61 qlqqwlknrl lltdlltrhp eiedielvap vviaglprsg tthlhnllaa aptfrslpyw
      121 esvepfplps eagiepdpri grmdlavqtm dllmphfalm hemttdhahe eiqllandfs
      181 tmlmetlahv prwteyywsh dqtstyryla tqlkalqflr gggrwvlksp qhlaqlpvid
      241 nvlpgakvvf thrdpvpval smiamityse rmhrdkvdva tvaaawvdrl ekmlaacvrd
      301 rdviaadrsl dirfddfmsd emgvaesiys ltgetfddps raavsdyles hrrgrhgrvh
      361 tsaemfgldp ddlrqrfasy ttrfls
//
LOCUS       WP_181791826             228 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein, partial [Streptomyces
            phytophilus].
ACCESSION   WP_181791826
VERSION     WP_181791826.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces phytophilus
  ORGANISM  Streptomyces phytophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 228)
  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 228)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Streptomyces phytophilus"
                     /db_xref="taxon:722715"
     Protein         <1..228
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
     Region          8..222
                     /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 haceplsdcp ekswstgdsk dvdslarrll dkpsghtwnf arsgaqvadl pvqtgeaiar
       61 rpdlvtilig andactdsaa amtpvadfrt avadsldrle adlprtqvyv ssvpslmrlw
      121 evgrgsaltr qiwslgvcqs mlaepsdlga tasdrrdgvq ervvefnavl qeecgehplc
      181 vyddgaafhy aftgdhlsrw dsfhpdedgq nvlaqiaydk lraaregr
//
LOCUS       WP_181792040             860 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Mycolicibacterium
            parafortuitum].
ACCESSION   WP_181792040
VERSION     WP_181792040.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium parafortuitum (Mycobacterium parafortuitum)
  ORGANISM  Mycolicibacterium parafortuitum
            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 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Mycolicibacterium parafortuitum"
                     /db_xref="taxon:39692"
     Protein         1..860
                     /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=92077
     Region          87..234
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          321..835
                     /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 masktaarst arqtrskapa rgkgksarpa aprrkparrt aspvasagna vgrgvragwl
       61 mlakgagsta rsvgrardle pghrrdgial allglavvia asswfdaarp vgewidtvvr
      121 mlvggavvlv pvvlavigvt lmrsephpea rprlilgfam ialpvlglwh mwsgapldpv
      181 arrhaggflg fviggpvadg ltvwiaapll iigvlfglll msgttirelp etvrdmfatr
      241 wqdyrdeydd eyddyeddeq vaadsddfsd dfsddfsdgy ydepvgdagd aaeawpsaaq
      301 ptvpltrfag pvgtpmdnyp ldeddaveap vpapvakprk kprkeeaakl vvdrvvegpy
      361 vlpsldllia gdppkrltaa nqamtdaits vlqqfkvdaa vtgctrgptv tryevelgpg
      421 vkvekitalh rniayavate svrmlapipg ksavgievpn tdremvrlad vltdpvtrsd
      481 hhplviglgk diegemisan lakmphllva gstgsgkssf vnsmlvslla ratpdevrmi
      541 lidpkmvelt pyegiphlit piitepkkaa aalswlveem eqryqdmqas rvrhidvfne
      601 kvrsgeitap lgsnrvykpy pyilaivdel adlmmtaprd veeaivritq karaagihlv
      661 latqrpsvdv vtgliktnvp srlafatssl tdsrvildqp gaekligmgd glflpmgank
      721 plrlqgafit deeihavvta tkdqaepefv egvtavkage rkdvdpdigd dmdvllqave
      781 lvvssqfgst smlqrklrvg fakagrlmdl metrgivgps egskarevlv kpdelagtla
      841 lirggsdang sdaeddepdf
//
LOCUS       WP_181792313             426 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Prevotella pallens].
ACCESSION   WP_181792313
VERSION     WP_181792313.1
KEYWORDS    RefSeq.
SOURCE      Prevotella pallens
  ORGANISM  Prevotella pallens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 426)
  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 426)
  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..426
                     /organism="Prevotella pallens"
                     /db_xref="taxon:60133"
     Protein         1..426
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49403
     Region          <47..273
                     /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          <197..402
                     /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          216..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(217..218,221..222,224,248,251..252,255..256,
                     258..259,284,287..288,291..292,295)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          246..276
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          283..311
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          317..340
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          351..380
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mhgqklkikd kiildeyfks dsfkhilhky eelcknnvss fldseeladi aeyyhiigkd
       61 eeakaaarya inifpgaiap lcfmarcamf idknidkaks iaeeildktd ldyyylnaei
      121 mivqmkteea niyllerfsy vaieeqqnyi fdvaslfcdy alvefaqkwl slyedvespe
      181 ykelkvrill wngggtesee ilnslidtnp ysttywnela kyyflnekye ksitaseytl
      241 ainpkdedal snkanalysi gnykeainyy krlqkitvgg lrkslnisia naylsennie
      301 eafkyftkai dysekkeeiy ikmaislmgn gyireayqif sdymenmsed wnigyacyar
      361 ccfelglmek ykkileiaik knlieteevl adlypegskp eeypqlspke rnvgtnsnfn
      421 nstfpf
//
LOCUS       WP_181792654             275 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            WELS2].
ACCESSION   WP_181792654
VERSION     WP_181792654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..275
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..275
                     /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=30134
     Region          37..275
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msvirqmtyq pagrpaasve tmtfgrlrel ndggtqradf hvlavidagp gsvavdfhrh
       61 pledrsavwi ppgavhrwdd iadvaghlvl fvptapvthv trelaaspdp aahwsipdad
      121 wpfvdtarsh llleasapps dsrtelpeil lsalitrlhp phtearltpq vfrlfrssve
      181 ahfrqhhdag yyartlgyap rtlsravqqa tgrtakayiv erivleakrl lahdrltaar
      241 cadvlgfpda snfsvffrka tgmrpgawqa tvaae
//
LOCUS       WP_181792721             306 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces sp. WELS2].
ACCESSION   WP_181792721
VERSION     WP_181792721.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            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..306
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..306
                     /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=33987
     Region          28..195
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mngtdepaye vlpshqsdpf rdhvvrayed tpadwqkvig gqlhfqwgvf ghpdaprpvs
       61 ldeaglryle qqlalatger sgptrprril dvgcgwgatl rhlaqvfpdc prldgvnisa
      121 eqlahcaglv rdvprpgrvh lylcdaadia elpdpeqpyd lalargvith lpprvyeaat
      181 ealsrrmrpg sllvvsetly seeflarepr lpadadhlal ehrkslryvt dvlrdsgfri
      241 rdervlpcae daarwvlelk snidvhfpee asppleairr maadlavall rreasvhsiv
      301 aervpa
//
LOCUS       WP_181792917             104 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase, partial [Streptomyces sp. WELS2].
ACCESSION   WP_181792917
VERSION     WP_181792917.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 104)
  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 104)
  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..104
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         <1..104
                     /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..87
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 tppgtpirig vgtvgrhavl evadqgpglt aterahvfdr fyrtddsrtr atggsglgla
       61 lvpalvtaha gsitldtapg qgctfrvllp lpallddrav datt
//
LOCUS       WP_181793113              97 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Streptomyces].
ACCESSION   WP_181793113
VERSION     WP_181793113.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=10890
     Region          17..72
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mpnslpapsr apigaafltl kdaaeylgls pqtlyvwrhr rqgppsfrmg prgrvmyrre
       61 tldawirdqe qadsrsntal npvsippqqr fsrtrsa
//
LOCUS       WP_181793219             148 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Streptomyces sp. WELS2].
ACCESSION   WP_181793219
VERSION     WP_181793219.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     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=15563
     Region          2..132
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrllrstdla lrvlmrlava agatpttrqv aadmevpyth atkvvaelqh lglvdarrgr
       61 ggglaltekg rttsvgavvr tfegegdvvd cegtpgcplr sgcllrgalr raqeaffasl
      121 dpvtvsdlvt dptgplllei srgpkerd
//
LOCUS       WP_181793280             290 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Streptomyces sp. WELS2].
ACCESSION   WP_181793280
VERSION     WP_181793280.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  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..290
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..290
                     /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=31340
     Region          35..288
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 myarvvaatv vaalgaaaal lgtgsdarag dgvvptviah rgasayapen tlaaidkaar
       61 lgfswvendv qrtkdgqlvv lhddtlartt nveevfpgra pwkvgdftaa eiarldagsw
      121 fsstyagvrv ptlkqymrrv ernhekllle ikspelypgi ekqtlkllrn egwldgrhrn
      181 rlivqsfsad svrtvhrlkp avttaylgap avtelkdfar ftdlinppng sltreyvsav
      241 hglrgphgrt lrvftwtvds aagalrvagy gvdgiitnkp dvvrdaldph
//
LOCUS       WP_181793439             604 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces sp.
            WELS2].
ACCESSION   WP_181793439
VERSION     WP_181793439.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     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]"
                     /calculated_mol_wt=65130
     Region          50..580
                     /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 mplnrrkflk ksavtgagva iagaaaapaa eaaqdqrpgk pghpvkryal tvmgttdlhg
       61 hvfnwdyfkd aeysdkagna mglariatlv nqvraekgrc ntllldagdt iqgtpltyyy
      121 akvdpitakg gpvhpmaram naigydaaal gnhefnygie tlrkfedqld fpllganavd
      181 akslrpafpp yfmktfhvpg akpvkvavlg ltnpgiaiwd kayvqgklaf pgleeqaakw
      241 vpklrsmgad vvvvsahsgt sgtssygdqv pyvenaaanv arqvpgidai lvghahveip
      301 elkvvneqtg ktvvlseplc yaerltlfdi elefrkgrwe vesvsaslrd srtvaddpei
      361 trlltgqhek vvayvnqvvg ratetlttve arykdapiid litkvqedvv kaalagteya
      421 slpvlaqasp fsrtseipag dvtirdlssl yvydntlvak lltgaqlray leysaeyyvq
      481 tapgavvdve kltnaggrpd ynydyvsgls ydidiaqpag srirnltfgg apldddrqfv
      541 lavnnyrang ggafphvasa kelwsestei rtriaewvta kgvldpkdfa svdwklvrgg
      601 tpvf
//
LOCUS       WP_181793658             331 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Streptomyces sp. WELS2].
ACCESSION   WP_181793658
VERSION     WP_181793658.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            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..331
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..331
                     /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=34865
     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 mngfgylrpg tlqeaveaya ahpgarylag gtnlvdlvkl gverptvlid vgrlpldtle
       61 elpdgslrag atvrnsdlaa dprvrdrwpa lsqallagas aqlrnaattg gnllqrtrcp
      121 yfqdldkpcn krepgsgcga rdgvhrdhav lgysarciat hpsdmavala aldaqvelyg
      181 pegtrrlpva dfhrlpgehp erdtwirpge litavllpga tagvpsayrk ardrasyafa
      241 lasvavalrv tdgvvdqagv afgglahrpw rarhtelalv gapatpeafe gavalelaha
      301 eplrdnaykv slarnlaldv lnrlapagaa a
//
LOCUS       WP_181793684             668 aa            linear   BCT 28-DEC-2024
DEFINITION  IucA/IucC family protein [Streptomyces sp. WELS2].
ACCESSION   WP_181793684
VERSION     WP_181793684.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 668)
  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..668
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..668
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=71580
     Region          61..667
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnatphpdgr sgapddqgdt tppaalprad svpqqkrraa dtswrtvpgp dplddpdpht
       61 aaqaaavenl lrcwvretgl aapateslti plpaggtali apvrywsptg whrfgpprla
      121 sapgtappvd avtlaallar etpartgppg gtaptpphtv shpgdegtpg apasvahpaa
      181 gadlvarvad svrrtaefir hrrahpadsp dlflsaeqal llghplhptp ksregltdae
      241 adryspeshg sfplhwlava psllatdsaw tergrpvpag rlvrslagtg lplpdgytpl
      301 plhpwqarev rhrpavaall dsgllrdlgp lgahwhptss vrtvhrsgap amlklslalr
      361 itnsrrenlr kelhrgvevh rllrtglagq wrtahpgfdi vrdpawlavd dpdgvpvpgl
      421 dvvirhnpft paddagcvag lvsprplavp tsntserplt wpvrsrlahl larltartgq
      481 plgavaaewf lrylehvvrp vlwldgeagv aleahqqntl llldgdgwpv ggryrdnqgy
      541 yfresrrtel tarlpgiger sdtfvpddva derlayylav nnvfgligal gsqrladerl
      601 llaafrrflt tlasgpdplr splpgrllds pvlrckanll trlhgldela gpvdtqsvyv
      661 tianplhs
//
LOCUS       WP_181793561             256 aa            linear   BCT 28-DEC-2024
DEFINITION  triose-phosphate isomerase [Streptomyces sp. WELS2].
ACCESSION   WP_181793561
VERSION     WP_181793561.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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..256
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..256
                     /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=27177
     Region          5..233
                     /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(10,12,96,165,171,205,224,226..227)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238190"
     Site            order(10,13,46..48,50,53,66,83,86..87,98..99)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238190"
     Site            order(12,96,165)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238190"
ORIGIN      
        1 mtttpvslts tkmnlglret eewindvllp radalarlrf caclphpvlp lgarllrdsg
       61 msagaqnvwy eagaftgevs agllaevgct hvmvghaerr rlfaeddrlv grkaraaaha
      121 glipvicvge perlghaetv ryvrrqasaa ldalphetpa ivlyepvwai gsaqgadphq
      181 aaavldalhr aagghhdvgm iyggavvpgt ysslrrlapw dgvalgraaq dsalldetlg
      241 ellssrpvdt pwvrve
//
LOCUS       WP_181793772             279 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Garciella nitratireducens].
ACCESSION   WP_181793772
VERSION     WP_181793772.1
KEYWORDS    RefSeq.
SOURCE      Garciella nitratireducens
  ORGANISM  Garciella nitratireducens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Eubacteriaceae; Garciella.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   ter Beek,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 279)
  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 279)
  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..279
                     /organism="Garciella nitratireducens"
                     /db_xref="taxon:218205"
     Protein         1..279
                     /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=30638
     Region          4..273
                     /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 mtnipqiplv dwidilvewl knnaqwffnp innflgtfvn flsnmlisis piifiivfvg
       61 isiyltkkiw glsifillgl lliwnldywe etmltlslil tssiisilig iplgiwmskn
      121 ntvkgivtpi ldlmqtmpaf vylipavsff gigmvpgiia svifamppvv rltnlgirqv
      181 prelieaads fgstgrqklf kvqlplaktt imqginqtim lalsmvvias migaeglgte
      241 vyraitrnna gqgfaaglsi vilaimldrl iqagnkksq
//
LOCUS       WP_181793863             254 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Streptomyces sp. WELS2].
ACCESSION   WP_181793863
VERSION     WP_181793863.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,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 254)
  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 254)
  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..254
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..254
                     /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=26515
     Region          1..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 mitgalrqsg rlfalaveva ramfrrpfqf refveqfwfv agvtilpaal vsipfgavia
       61 lqvgsltrql gaqsftggas vlavvqqagp livalliaga ggsaicadlg srkireelda
      121 mevmgvspvq rlvvprvlat mgvavllngl vsvvgtlggy ffnvilqdgt paaylssfss
      181 laqpadlyis elkalvfgfi agivaayrgl nprggpkgvg davnqsvvit flllffvnmv
      241 mtvlylrivp pkgg
//
LOCUS       WP_181793895             187 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase, partial [Garciella nitratireducens].
ACCESSION   WP_181793895
VERSION     WP_181793895.1
KEYWORDS    RefSeq.
SOURCE      Garciella nitratireducens
  ORGANISM  Garciella nitratireducens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Eubacteriaceae; Garciella.
REFERENCE   1  (residues 1 to 187)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Garciella nitratireducens"
                     /db_xref="taxon:218205"
     Protein         1..>187
                     /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]"
     Region          5..>187
                     /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 mdmikniinv iqknhnfllt thlspdgdal gsiialglal eklnkkvdyy idpsipekfn
       61 flpkiqnlsc nvldkqyeig iildcgdinh lydrtilkkc ntiinidhhi nnqnygnmny
      121 inskagatge iiyeiieflg veldhniska lytaivtdtg nfkysnvtsk thyivsellr
      181 ipidawk
//
LOCUS       WP_181793941             559 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Garciella nitratireducens].
ACCESSION   WP_181793941
VERSION     WP_181793941.1
KEYWORDS    RefSeq.
SOURCE      Garciella nitratireducens
  ORGANISM  Garciella nitratireducens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Eubacteriaceae; Garciella.
REFERENCE   1  (residues 1 to 559)
  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 559)
  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..559
                     /organism="Garciella nitratireducens"
                     /db_xref="taxon:218205"
     Protein         1..559
                     /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=64748
     Region          5..463
                     /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 mllknryhei rrvkeiisvf ikygfynqih qlgllkymki yplrknkksk nqkfsrgkrl
       61 rmaleelgpa fvklgqllst rrdlipkdmi eelenlqnkv vpisyesike qvekqlqgsi
      121 eelflefkkt plaaasiaqv hkatlkngkk vvvkvqrpgi qqklmtdlsi ieevasfley
      181 ktkygklydf tgivkdfkkn llkeldfrme grniitfqkn fkndknivfp ciykeyssqk
      241 vltmdfiqgi slknvellrk khldpsliar rfchcileqi lrdgffhgdp hpgnvrvlse
      301 nriafldmgi vgkvaeekre qffkmiagit lknsklives iremgvtkef idfkqlenei
      361 silrdeylei plkeikigef lteifrlafq ynisipneva miaktliive gtiteldpnl
      421 nileiaqpit kqlmkemysf qriakylqen ildtsrllhr lpdsftnile rlerhdfkli
      481 lsfknekqmi ktlnkianql sfsiallalg ivisgfilal aingnsfgfl dsrfvivgli
      541 islimglwlm isiiksgrf
//
LOCUS       WP_181793988             191 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GTP-binding protein [Streptomyces].
ACCESSION   WP_181793988
VERSION     WP_181793988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 191)
  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..191
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..191
                     /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=20413
     Region          4..186
                     /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 mdfassdagr attsakivva ggfgvgkttf vgavseinpl rteavmtsas agiddlthtg
       61 dkttttvamd fgritldqdl ilylfgtpgq drfwfmwddl vrgaigaivl vdtrrladcf
      121 pavdyfensg lpfvialngf dgqqpyspde vrealqigpd tpiittdarh radaksalit
      181 lvehalmarl k
//
LOCUS       WP_181793070             241 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Streptomyces sp. WELS2].
ACCESSION   WP_181793070
VERSION     WP_181793070.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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 241)
  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 241)
  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..241
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..241
                     /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=24147
     Region          39..241
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mrisrlapal aaaavsllal faptasaapt aapvtargsq piigggyags gpwaarlysn
       61 gqetctatii aptwvltakh cvagggslsf rvgsldqysg gtvangvqty thsadlalvr
      121 ldrsvpttya slgqpgtvrv gqnvqvygwg atsqcgsein cqsrylkvan vtvaggctda
      181 yggsaicayr gdgitaggds ggpmmangvq vgvastsdrq sntaytnvta yrswiqsvag
      241 v
//
LOCUS       WP_181794027             350 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            sp. WELS2].
ACCESSION   WP_181794027
VERSION     WP_181794027.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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 350)
  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 350)
  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 350)
  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..350
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..350
                     /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=36409
     Region          3..345
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mlilvtggvg figshvvttl tgaghtvrvl dallpaahrg appipegvdw rhadvrdaaa
       61 vadalrdvda vchqaamvgl gkdfadapdy vgcndlgtav llagmaeakv rrlvlagsmv
      121 vygegryecs rhgvvrpgpr epadlgagrf eppcphcgep lvpalvdeda padprnvyaa
      181 tklaqehlaa awaratggrv aalryhnvyg prmprdtlya gvaslfrsal argeaprvfe
      241 dggqrrdfvh vrdvaganla aldavdglaq galraynvgs geprtvgema aalaaahggp
      301 apvvtgefrl gdvrhitass rrlrdelgwr arvafaqgma efaaaplrag
//
LOCUS       WP_181794054             193 aa            linear   BCT 28-DEC-2024
DEFINITION  HD domain-containing protein [Streptomyces sp. WELS2].
ACCESSION   WP_181794054
VERSION     WP_181794054.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 193)
  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..193
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..193
                     /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=20913
     Region          11..174
                     /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 mgdqdladva hflwetgtlk tarrtgwwma gvrdpesvae hswrtsvias viatlegada
       61 araahlavwh dsqetrtgdv nhlgkkyaap gdpeavtadq tagmpevlra avravvaeye
      121 aretpeavca rdadklecml qgleykaqgy eaaqrwvdns rarivtesgq rladqllaqa
      181 pldwlraamg ess
//
LOCUS       WP_181794055             372 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            WELS2].
ACCESSION   WP_181794055
VERSION     WP_181794055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 372)
  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..372
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..372
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=41428
     Region          29..>62
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
     Region          30..100
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
ORIGIN      
        1 mgdqakqtpt ggqgttgrgr agiisgyvfr vireqlghtq eglaevfdva adtiagwetg
       61 rrpltslpvg qmlshrhrll rmgtapqlla alarameadm llagvledev sagpnllgaw
      121 vmqrdlvevl twplngvppt plrtlpappr prrgpvppap elaadyrrrf frrmretaeq
      181 acggrdfllr rqalylagfd qdpgtsdwla yqqrterpdd wltrwlnsrs vaavaarqgd
      241 rdrmthfitr tlgddtraea anlnywaywi getphiqlsd dfigdstpgp whgdrlmahl
      301 vrgltpwhgf fdlnvhtlwa liaarpnllr tqsaagrvlr erlpmmldds glssqarrel
      361 egiryairla ea
//
LOCUS       WP_181794089             164 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine dioxygenase [Streptomyces sp. WELS2].
ACCESSION   WP_181794089
VERSION     WP_181794089.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 164)
  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 164)
  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 164)
  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 164)
  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..164
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..164
                     /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=17879
     Region          61..146
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mnsdndlqia gdilevphll qpprehpatv aefaglarsi aadrdrwthl vrfdattrwy
       61 hrlrtgpgye vwllswlpgq gsgrhdhgrs sgvltvvegt ltehtvrgtr algagaqrvf
      121 apgyvhevvn dalepavslh vyhpgltemp mhtsphceas svtt
//
LOCUS       WP_181794144             357 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Streptomyces sp. WELS2].
ACCESSION   WP_181794144
VERSION     WP_181794144.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 357)
  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..357
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..357
                     /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=39420
     Region          14..352
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtfspqaval ltvpaepspv pgagsdfsrl srriteaglm rrrpgyyavr lglvvaltaa
       61 gwgaflalgd swwqlavagf lalmygqaal vahdlahrqv frrgrpsriw grlfgnlgig
      121 msygwwmnkh trhhanpnhe eldpdvapdi lvwstaqard srglarligg hqawlffpll
      181 tlegfnlhva svralrspsm khrtleagll llhiaaylsa lflvlppgka vaflavhqcl
      241 fgvylgctfa pnhkgmptls gderpdflrr qvltsrnvrg grltdvllgg lnyqiehhlf
      301 psmptphlrr aqavvrayca eigvpyhetg llrsyrealt hlhrvgepir rqrgmaa
//
LOCUS       WP_181794260             282 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            WELS2].
ACCESSION   WP_181794260
VERSION     WP_181794260.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..282
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30771
     Region          7..79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          104..268
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mgserreqmk algarlrvlr gesgltgavl aqragvgqpt vskietgrmv psrdvldrll
       61 galgadesvs revrellagv vaaeddepta vdvaegttvd eevrsaqsvr sfqcvvlpam
      121 lqsaeyarhv fqsaprstpe avgravaarv drqsvlyepg resvfvvtea vlrtwpgspa
      181 lmlaqfdrll aveslstvrl gvipwrrpvp vlprhgftlc dqravvietf dservstaat
      241 evaaydetfe rferaavfgd evrelllrvm kefrdlgdtl th
//
LOCUS       WP_181794410             378 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces sp. WELS2].
ACCESSION   WP_181794410
VERSION     WP_181794410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            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..378
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..378
                     /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=39711
     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 mavdvtiiga glgglmlarv lhvhgipatv heaepspaar sqggmldihd yngqlalkta
       61 glmdefgglv legrqamwll apdgtvlfdk addgtggrpe vqrgelrqml ldslppgtvr
      121 wgrkagrvrs lgggrhevvf adggtvvtsl lvgadgawsr vrpllsaatp rytgksvvet
      181 ylfdagrrhp aaaravgggs mivhapdrei fahrekgdtl hayagltepe dwfaaidftd
      241 aaaattriar efegwapelt alitdsdtap vlrrlyalpa ehrwdrvpgv tligdaahla
      301 apngeganla mldgaelgea laahpddtea alsayeqvvf prsaeaavle gggahgsetd
      361 sptphdliaa ftrneesr
//
LOCUS       WP_181794529             205 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Streptomyces sp. WELS2].
ACCESSION   WP_181794529
VERSION     WP_181794529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 205)
  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..205
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..205
                     /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=21397
     Region          7..198
                     /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 mtanrrrrlv lasqsparlg llrqagfdpe vivsgvdeda vtaptpaela lalaeakasv
       61 vaarpevqga lvigcdsvle ldgralgkpa daeeatarwk nmrgragvlq tghcvwdtea
      121 kryvsatast vvrfgepsda eiaayvasge plhvagaftl dgrsapfieg idgdhgnvig
      181 islplirrll aelgvgitel waper
//
LOCUS       WP_181794953             359 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family NADP-dependent oxidoreductase [Streptomyces sp. WELS2].
ACCESSION   WP_181794953
VERSION     WP_181794953.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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..359
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..359
                     /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=37055
     Region          9..353
                     /region_name="PGDH"
                     /note="Prostaglandin dehydrogenases; cd05288"
                     /db_xref="CDD:176190"
     Site            order(53,136,160..162,182..183,187,219,240..241,262..266,
                     268,297..299,342..343,345,347)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(54,268,300)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:176190"
     Site            order(57,61,256,261..264,267,282,288,291..298,301)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176190"
ORIGIN      
        1 mtslpqrisr evrlaalpag lptpadfala evpveaparg rvlvrnrrfl vygglrtllg
       61 gaakdtpvpt lrpgdtlygp avgevvlapp gsplrpgdtv thllgwreya lvpeaecarv
      121 dpalpdpvar lasgsaayga ltrvagvreg dvvlvtgaag gvgslagqia rllgasrvig
      181 ttgspgkagr lvaelgydav vtagswregr gsgnsreayr afagqlaeaa pdgidvlldn
      241 vggpqlsaav daarqgarfv lvgalsgqla aegsgavapa eidtfrlivk gvsvrgylgt
      301 dhpgveaewt arfadwlrsg rirlpltrft gidrapwalq eliegkrfgt vvvelpehd
//
LOCUS       WP_181794640             764 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Streptomyces sp. WELS2].
ACCESSION   WP_181794640
VERSION     WP_181794640.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     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=83017
     Region          19..758
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mragaelsna dltnsefpdd elrgeqefid glyarvdvlr geaetsvtda laqgdkpmqa
       61 rlerdilvae rsgllaalna vdgslcfgri dladgtthhi griglredda ertpvlidwr
      121 advarpfyla tghtpmglrr rrhiatesrt vtslhdeild lgdatrtghe dhngdavlla
      181 alnsartgrm gdivqtiqae qdriiraphr gvlvveggpg tgktavalhr aayllyehre
      241 llarravliv gpnpaflgyi gevlpslget gvllatvgel fpgvrataad tpeaaavkgr
      301 admaevlaav vrdrqalpdp viaiehdrev lmlddglvnv arertraakl phnaarehfe
      361 ghilntltel yaervgtdpy dgsslldpsd itqirdelae npevwdaidt lwprvtpqrl
      421 vadflaepdg ylpkedadai rrpvtrawtv advplldeaa ellgeddrta raraereret
      481 qvayaqgvld vsyasrtyef edkddeesev lsahdiidae rfaerqeead hrsaaeraaa
      541 drtwafghii vdeaqelspm awrllmrrcp trsmtlvgdp aqtaeaagvg swadilapyv
      601 edrwehtrlg vnyrtpaeim dlaaavvrag qpdfeppssv rstgvrpwvr hasgdlpgav
      661 aeavaeltpe egrlaviapr dlhralaarl dgvtagtepd ltrtvvlldp rqakglefds
      721 vlvvepaayg tsdlyvaltr atqhlgvlht gtlpagltpa aatp
//
LOCUS       WP_181795205             263 aa            linear   BCT 28-DEC-2024
DEFINITION  cell division protein FtsQ/DivIB [Streptomyces sp. WELS2].
ACCESSION   WP_181795205
VERSION     WP_181795205.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            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 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..263
                     /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=27587
     Region          17..259
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 magpttaerg erqqgssgpp pargavrrlr tivilavavf llgaggawvl ygsqwlrvrh
       61 vsvsgtlvlt paevreaadv pvgepmasvd tdaiearlrr klpridtvdv vrswprgial
      121 nvsertpvll irkggnfvev ddegvrfatv sqapkgvpsl elsasrngpg aaslrrfgtg
      181 rlvraavrva gdlpapvara artvrvrsyd avsvelgdgr tvvwgsdeqg rakaraltal
      241 mkaspgarhf dvtvptapas svs
//
LOCUS       WP_181795348             121 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces sp.
            WELS2].
ACCESSION   WP_181795348
VERSION     WP_181795348.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..121
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13695
     Region          3..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrskmdeasd hcavefamel lggrwklail kqlvsgthrf gelrralpgv tqrmltrqlr
       61 eleadglver tvyrevpprv eytltdvght ldsiteqlda wgrwyrdtvr reappgtgas
      121 d
//
LOCUS       WP_181795402             409 aa            linear   BCT 28-DEC-2024
DEFINITION  thiolase family protein [Streptomyces sp. WELS2].
ACCESSION   WP_181795402
VERSION     WP_181795402.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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 409)
  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 409)
  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..409
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..409
                     /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=42190
     Region          13..409
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mntahtppnp kavyivdavr tpfgryngal asvrpddlaa halrallart peldparidd
       61 vylgnangag eenrnvarma allaglptsv pgvtvnrlca sgleaviqaa raialgdasl
      121 avaggvesmt rapyvlpkpd gpfpaahtel ysttlgwrmv nprmdpqwti plgesaelia
      181 dkhgisreqq ddfalashrk aaaareqglf daesvsvpvp rrkgepvvfg tdecvrpdas
      241 laamaklkpa fraeggtvta gnasplndga aallladeeg lratgrepla risatglsat
      301 dpryfglapv eavnralaka gkdfgdlsvl elneafaaqv lgclaewpef dpavlnpqgg
      361 aialghplga sgarlagtva hqlarrgsgt gaatlcigvg qglalvler
//
LOCUS       WP_181795697             126 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Streptomyces].
ACCESSION   WP_181795697
VERSION     WP_181795697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 126)
  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 126)
  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..126
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..126
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13917
     Region          19..>115
                     /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          82..112
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpetsgstgr tpethvidfr aaeqllnard prgavklldg viaahpenta arllraraff
       61 aaaqlrpael eftivlerep dnafahfala rtyerqgrpd qakrhfrlaa aldpnpryle
      121 aarfda
//
LOCUS       WP_181795794             290 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease, partial [Streptomyces sp. WELS2].
ACCESSION   WP_181795794
VERSION     WP_181795794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   ter Beek,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 290)
  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 290)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         <1..290
                     /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          3..283
                     /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 atdwpaggtl diagpvnrav dwmtdhlysg vpvvggtadw aghfttwvld pvraglqamp
       61 wwsvllvvaa lawligtwrt altavlamaa igvlgvweps ldtlsqvlaa vavtlvlgva
      121 tgiaaarsar idrvlrpvld vlqtmpqfvy lipvvalfgv grapavaaav vyalpavvri
      181 taqglrqvdq aalesarslg atgrqqlwqv qlplarrall lavnqgvvlv lavviigglv
      241 gggalgydva fglaqgdlat glvagaaivc lglmldrvtq pagrragkga
//
LOCUS       WP_181796132             327 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            WELS2].
ACCESSION   WP_181796132
VERSION     WP_181796132.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     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=35785
     Region          1..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mraarlikmv lllqsrplmt aaelarelev sertvtrdaq alseagvpvy adrgraggyr
       61 lvggyrtrlt glargeaeal flsgvpgalr emgladvasa arlkvsaall pslrdapdta
      121 aqrfhldapa wfrepetpal lpvlaeavwd dgrvlawykr ardtverrle pyglvlkagv
      181 wylcarvagn gsfrtyridr ftavdrlger fdrdpgfdlp gfwaeqaerf arsilraevv
      241 vrlspegvrr lrhavdpaaa rsvleepgep daagwvtvtl pveseevaye qltalgpeae
      301 vlapaalrer faadaarava lyrredg
//
LOCUS       WP_181796345             503 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Streptomyces sp. WELS2].
ACCESSION   WP_181796345
VERSION     WP_181796345.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  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 503)
  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..503
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..503
                     /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=53223
     Region          6..497
                     /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(157,160..165,167..168)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(160,275..276,297..302,384,396,399,410,490)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(160,201..202,249,251..252,255,275..276,297..302,384,
                     396,399,407..410,471)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(201,251..252,255,275,407..409,465,471)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 matlsvaail aenarrrpgk talvegelrl tfaevwqral aragaltglg vrpgdhvalm
       61 apntaefpva yyaiaaaggv vvpvhlllsa gevehvleds gatvllvhpa qaetgraaae
      121 aagvqvvtlg eefdklaada eplpsyvsra addpavifyt sgttgvpkga vlshfnlvmn
      181 atvnafdahd iraddialga lplfhafgqt vslnstwrag atlvllprfd aaraielmae
      241 edvntfhgvp tmfvalaaaa adaerlpglr vcvsggaslp vavlerfeaa fgariyegyg
      301 lsetspaatv nqpvfgtkag tighplwgvd aeiaraeved riellppgel gevvirghnv
      361 fsgylgrpea taealvdgwf rtgdlgtkdd egflrivdrk kdiiirggyn vypreveevl
      421 mrhpeiaqaa viglpdelhg eevcavvvpa pgtapdaaal tewskehlgr hkhprrveft
      481 dalplgpsmk vlkrelrary tgr
//
LOCUS       WP_181796292             520 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA synthetase [Streptomyces sp. WELS2].
ACCESSION   WP_181796292
VERSION     WP_181796292.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  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 520)
  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 520)
  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..520
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..520
                     /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=54901
     Region          10..497
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(164,167..172,174..175)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(167,282..283,303..308,388,400,403,414,494)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(167,207..208,255,257..258,261,282..283,303..308,388,
                     400,403,411..414,475)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(207,257..258,261,282,411..413,469,475)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mrnqgigswp arrarktpdr iavvhedrei tyrhlhervl rlahalralg vargdrvayl
       61 gpnhpaflet lfaagalgav fvplntrlta pelayhltds gaavlvhape qaeaaaaaaa
      121 dagvshrial agpgsgalgy dellaaagte pldepvapdd pcmimytsgt tgrpkgavls
      181 hanivwnsvn vlvdldlaad evtlvtaplf htaalnmtcl ptllkggrvv llgafdpdrv
      241 lhlieshrvt cmfgvptmyd alaarprwpe adltslrsvn cggapvpert idvylargla
      301 faqgygmtea spgilfldre qtsakagsag vphfftdtrv vlpdgrdaap gergeilvsg
      361 pnvmtgywnr paetaaavtd dgwlrtgdva rtdedgfayi vdrvkdmfis ggenvypaev
      421 enavlghpav eecavigvpd aqwgevgrav vvlkpgarae eadilghlrg rlakykipks
      481 vvfaealprt asgklvkpav raayapatag adddrppapr
//
LOCUS       WP_181796611             172 aa            linear   BCT 28-DEC-2024
DEFINITION  SixA phosphatase family protein [Streptomyces sp. WELS2].
ACCESSION   WP_181796611
VERSION     WP_181796611.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..172
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18807
     Region          9..170
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 msvaeprriv lfrhakadwp qvpdherpla ergrmdapva grkladtgit fdlalcstai
       61 rtretwklav qelphrpktv yeeriyeasp geliavlnel pdearnvili ghnpgvhgla
      121 eilagsaagd ararmnrrgf paaafallsy dghwkgvepg vatltdywap se
//
LOCUS       WP_181796582             304 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces sp. WELS2].
ACCESSION   WP_181796582
VERSION     WP_181796582.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  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 304)
  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..304
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..304
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32758
     Region          51..273
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 maalgwltpr rrsatarsvl ageasaeaar kssqetatpe epefpvigdd kaaaffdldn
       61 tvmqgaalfh fgrglykrkf fetrdlarfa wqqawfrlag vedpehmqda rdsalsivkg
      121 hrvaelesig eeiydeymad riwpgtrala qahldagqkv wlvtaapvei aqviarrlgl
      181 tgalgtvaes vdgvytgrlv geplhgpaka eavralaaae gldlarcaay sdshndipml
      241 slvghpyain pdaklrrhar eqdwrlrdyr tgrkaakvgi paaagvgava ggtaaaials
      301 rrrr
//
LOCUS       WP_181795540             744 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase, partial [Streptomyces sp. WELS2].
ACCESSION   WP_181795540
VERSION     WP_181795540.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 744)
  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 744)
  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 744)
  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 744)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..>744
                     /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]"
     Region          4..>744
                     /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 metrveadrd ywsrvltagg atvvprwvpe pvpgvleqet avpeevtaav ralvrrsglp
       61 lsavllaaha kvlaalsgep evvtgytagv rgeplpcrlt vppgswralv taaeraeael
      121 lahrefpvag lrrelgltep pyevvfgpeg pegtegpega rgagaggpga degvlhvrwy
      181 drggglalrl ryrtdvldag aaariggyhl kalallaaap dadhgqqsll saeevreqlq
      241 glagprrelp darahelfer rarehpdrva avhgertwty gelnaranrl ahallerglg
      301 pedvvavvte rdldwlaatl avfkaggvyl pvephfpagr iaamltraec rlvltgsggt
      361 ehldealaav pgavrlpvet aysephpdtd pglpiepgrl ayiyftsgst gepkgamceh
      421 agllnhlyak igdlgigegs vvaqtapqcf dislwqllsa lltggrtllv gqdvitdver
      481 fvdtlvrgrv avaqlvpsyl evvvsyleqr pralpdlrcv svtgealkre ltqrwfalqp
      541 girllnaygl tetsddtnhe vldgvpdrvl lgravhnvrv yvvdehlslv plgapgliaf
      601 sgvcvgrgyv ndpertreay rtdpyhpger lylggdlgrw hpggkleflg rrdnqvkirg
      661 frieigeien tllrvagvrd gavvvaergg gnkhliafht grrippgtlr erlaaalpsy
      721 mvpsafhwre slpltangkt drka
//
LOCUS       WP_181796632             317 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein, partial [Streptomyces
            sp. WELS2].
ACCESSION   WP_181796632
VERSION     WP_181796632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 317)
  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 317)
  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 amino end.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         <1..317
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          3..316
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 iddhgrtyra trgvadrvtg raistedrfr igsvtktftt vvllqlvdeh rlaldapvnr
       61 ylpgllpddr itvrhllshr sglydysddm faasvsgfea vrkkvftyrq lvalslkkpr
      121 tnapgaaysy sntnfvvagm lvekltgqpv rtayqsriik plkltdtfyv hpdtaipgrh
      181 trgyltpdra gaplvdataq tvswaqsaga vissahdlda fygallkgrl lsaarladme
      241 rftkvnstta yglglrrrdl scgvsvyght gavqgyytya fgtkdggrtl tamantsnna
      301 kvlntlagal esafcgk
//
LOCUS       WP_181796733             359 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Streptomyces sp. WELS2].
ACCESSION   WP_181796733
VERSION     WP_181796733.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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..359
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..359
                     /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=38427
     Region          11..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 mgnslasggs prqipvvvla gflgsgkttl lnhllhrsgg srigaivndf gaieidamav
       61 agalgdstvs lgngclccav dageldlyld rlaapaagid vivieasgla epqelvrmll
      121 asehpgivyg glvevvdaae fddtrakhpe idrhlaladl vvvnkldrag dadrilglvr
      181 sltdraavvp vtygridpef lfdcrpseer vgqlsfddlh dhddpdhagh lhtgydslsf
      241 ssavpleprr lmrfldsrpe glyrikgyvd fgpydavnry avhavgrflr fypepwapgd
      301 erltqlvlig sgidadalrk elddcgndap hadehgmwgv lryvqgpdea davveeppa
//
LOCUS       WP_181796794             538 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces sp. WELS2].
ACCESSION   WP_181796794
VERSION     WP_181796794.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 538)
  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 538)
  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 538)
  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 538)
  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 538)
  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 538)
  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..538
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..538
                     /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=57300
     Region          25..503
                     /region_name="MtrAB_MtrB"
                     /note="MtrAB system histidine kinase MtrB; NF040691"
                     /db_xref="CDD:468655"
ORIGIN      
        1 mtgtreglrg waagrggsls rlrftslrlr lvvvfalval taavsasgia ywlnreavlt
       61 raqdavlrdf rqemqnraga lpehpsqdql qraagqmaas sqrfsvllva tdadgktvyg
      121 nsggingfal edvpstlraa vtkrqpvtgq nkepyhlywq rvvdhgtpfl vagtrviggg
      181 ptgymaksle peakdlnsla wslgiatgla ligaallaqa aattvlkpvh rlgvaarrlg
      241 egrldtrlrv sgtdeladls rtfnnaaeal ekrvaemaar deasrrfvad mshelrtplt
      301 aitavtevle eeleaetgsm dpmiepavrl vvsetrrlnd lvenlmevtr fdagtarlvl
      361 ddvdvadqit acidarawld aveldaergi harldprrld vilanligna lkhggspvrv
      421 svreaedsve irvrdhgpgi pedvlphvfd rfykasasrp rsegsglgls ialenahihg
      481 geitaansae ggavftlrlp rdasslteqd ggdggngred tggkdakagr dgageegs
//
LOCUS       WP_181796859             312 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AurF N-oxygenase family protein [Streptomyces].
ACCESSION   WP_181796859
VERSION     WP_181796859.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 312)
  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 312)
  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..312
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..312
                     /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=35685
     Region          22..295
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 mttlteadal dglrdalgll kdreqvaerl lassakhsfd pdkeldwdap feegkwfwpp
       61 elvslydtpm wrrmseeqri llsrheaaal aslgiwfeli lmqllvrhvy dkaatsahvr
      121 yalteiedec rhskmfarli thggtpwypv srahqnlgrl fktisttpgs ftatllgeev
      181 ldwmqrltfp dervqplirg vtrihvveea rhvryareel rrqmvtapkw sqeftrvtsg
      241 efarvfsvaf vnpevytnvg ldkreamaqv kasghrrevm qtgakrltdf lddigvlrgv
      301 grrlwrasgl la
//
LOCUS       WP_181796772             507 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein, partial [Streptomyces sp.
            WELS2].
ACCESSION   WP_181796772
VERSION     WP_181796772.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 507)
  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 507)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         <1..507
                     /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]"
     Region          1..484
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 apaflhgvas gdplpdgvll wtrvtpvpea ipgsglgpdt evgwvvardk altdvvargs
       61 vtataasdht vkadvrglap atdywfrfsa ggtdspvart rtapaadadv sslrfgvvsc
      121 anweagyfaa yrhlaargdl dawlhlgdyi yeyksgeyaa rgrvvrphap aneiltlady
      181 rtrhakyktd pdlqalhlta pvvaiwddhe fadnawqgga vnhtegaegt waarqaaakq
      241 ayfewmpvrp alagttyrrl rfgrladlsl ldlrsfrsqq astasgsvdd pdrtltgraq
      301 ldwlkaglra sdtkwrlvgn svmispfaig slsadllkpl akllglpqeg ialntdqwdg
      361 ytddrrella hlrsnaiknt vfltgdihma wandvpvdag typltpsaat efvvtsvtsd
      421 nlddiakvpe gtvsavaapv ikaanrhvhw vdtdrhgygv lditaeraqm dyyvlsdrtd
      481 pdaraawtrs yrtlsgtqkv ertydpv
//
LOCUS       WP_181797002             711 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces sp. WELS2].
ACCESSION   WP_181797002
VERSION     WP_181797002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 711)
  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 711)
  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 711)
  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 711)
  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..711
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..711
                     /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=77649
     Region          33..705
                     /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 msaepdgped rlhrlttiws ravypvtsts ltraefaeel lplarrlsel lrarsfdada
       61 akavgaalvg ahctdpeala rtldcvdayl ilycgedgpq delrmrssrl qhamaagyaq
      121 alrertraeq eaiaqaalra qgvvaqalha searfravfe gaaigigiad lhgnvlqvne
      181 allrmfglse qtlrgrrvqd wvhpedapqi rrlyeelvrg erehyhveka fnrpdgtvlw
      241 tnltvsllrd adgspqyqla lmedtterrl lnlrlryeat hdaltglpnr tlfferldka
      301 lnagegqrfg lcyldldgfk tindslghaa gdrllvevad rlqscatapg emvarlggde
      361 fvalttgpdt ergvdelaer imnalvtpis idgrdllvrg slgivegpag ertaaevlrs
      421 aditmyraks aggnraelad peadaraitr hglttalpta lergeffiey qplvhlgdgs
      481 vrgaealvrw lhpqhgvlgp drfiplaeht glivplgrwv leesirqara wrerhggqag
      541 plrinvnlsp cqlghpglvq dtvdilerag vapdalclev tesaligadd dllkplrrla
      601 emgvdialdd fgtgysnlan lrrlpvsilk ldrsftqgmq rfpadpvdlk ivegivslah
      661 sldlavtveg vetgaqaeql rilgcdtaqg wyyarpgppe rlhdltlvda t
//
LOCUS       WP_181797036             291 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein, partial [Streptomyces sp.
            WELS2].
ACCESSION   WP_181797036
VERSION     WP_181797036.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..291
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         <1..291
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          42..289
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 rrpgiwwlpd gatpvrtpws srdedavapg rppvrpvplr ptardalplh gwyyrapgra
       61 pgepapcvih lhggpedqer pvldplyhei lgrgvdvfap dvrgssgygr sfvdadlgrg
      121 rfaaiddvad caahavlagl adparlavmg rsyggyltya slvwhpdlfr tgiavcgmsd
      181 lttffegtep wiaqsaahky ghperdrall relspmsrvd alrapvlavh gehdtnvppg
      241 eseqfvraar ergvtaellt lpdegheflr adnrrlfrra aadwlqrqls t
//
LOCUS       WP_181797095             288 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces sp. WELS2].
ACCESSION   WP_181797095
VERSION     WP_181797095.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..288
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32579
     Region          4..288
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtnpterlvd lldleqievn ifrgrspqes lqrvfggqva gqalvaagrt tdgdrpvhsl
       61 hayflrpgrp gvpivyqver vrdgrsfttr rvtavqqgrt ifnltasfhk peegpfehql
      121 pparevphpe slptvsdeir khlgtlpeql ermarrqpfd iryvdrlrwn aeeikgaepr
      181 savwmravgp lgddplvhtc altyasdmtl ldavripvep lwgprnfdla sldhamwfhr
      241 pfradewfly dqespiaigg rglargriyd legrllvsvv qeglfral
//
LOCUS       WP_181797129             365 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Streptomyces sp. WELS2].
ACCESSION   WP_181797129
VERSION     WP_181797129.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     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=39276
     Region          48..327
                     /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 mklpghdaia rqadehlvth rvklprkvve rpirqvvkrl vmalavlvat alivyadheg
       61 yhdnadgtvd lldafyyatv tlsttgygdi tpvsdgarla niflitplrv lfliilvgtt
      121 levltertre ewrlnrwrsv lrdhtvvvgf gtkgrsaiqt vcatglkkeq vvvvdpsska
      181 idaataegya gvvgdatrse vlkraevhka rqiivapqrd dtavlvtlta rqlnrgakiv
      241 aavreeenap llrqsgadav itssgaagrl lglsvlspaa gmvmedliqq gsgldlverp
      301 vvrgevgktp retddlvvsv vrghrvlgyd dpavgtlqlt drlitivrat pgnhvtpdtr
      361 plphg
//
LOCUS       WP_181797013             322 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: complex I subunit 1/NuoH family protein
            [Streptomyces].
ACCESSION   WP_181797013
VERSION     WP_181797013.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 322)
  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 322)
  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 322)
  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..322
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..322
                     /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=34513
     Region          3..321
                     /region_name="NuoH"
                     /note="NADH:ubiquinone oxidoreductase subunit 1 (chain H)
                     [Energy production and conversion]; COG1005"
                     /db_xref="CDD:440629"
ORIGIN      
        1 mndvldvalr llvvfavflt fplivgqteh kvmahmqgrl gpmyaggfhg waqliadgvk
       61 faqkedvvpa gadrrvfqla pavallpyll vllaipigpg egavgqvlda gvffvlavmg
      121 vgvlgslmag wasankfsll gglrtaaqll syelpmllaa asvamaagtv slpgilhafh
      181 wwwlpwqivg avvffvagla elqrppfdmp vadseiifga yteytglrfa lfllaeyagi
      241 vvlcglttvl flggwhgpwg adglgwvwtl lktailaflv iwlrvtyprl redqlqklsw
      301 tllvplslaq ialtgivkvv is
//
LOCUS       WP_181797163             348 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein, partial [Streptomyces sp. WELS2].
ACCESSION   WP_181797163
VERSION     WP_181797163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     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]"
     Region          6..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 mpdrqasgtr qklpsltglr fyaaalvfcf htsltkmvdp fadrdfaddy gllfskagwa
       61 gvsfffilsg fvlawsarpg erlgsfyrrr llkiypnhvv twaltlllfs stvggvsvwl
      121 pnlflvhswi prlgtfvsvn qpswslcsel lfyllfpllw rwvkgigssr lwawfavtfa
      181 gllitqivig tavpgtprla ewplsetqww laynipplrl fefvlgmlma rilregrwig
      241 lgiapalalt gagyalalvv pwqyglnvtl avplallvta vaaadvtgrp tglrgrvmtl
      301 lgeisfafyl vhylvllavq dlldgrrfat paalavvaaa fvaaqllg
//
LOCUS       WP_181797176             273 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces sp.
            WELS2].
ACCESSION   WP_181797176
VERSION     WP_181797176.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 273)
  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..273
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..273
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30382
     Region          15..71
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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"
     Region          92..272
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mnrkelnpda spqaaygarl rslreargwt qddlgilmdy ssvhisavet grkpptlrfs
       61 rsadrafglt gtgnsferey rqiqhgnlle gfpefvkheg raaeirlyei giipgllqtp
      121 eyarvladsa vrrgtitpeq aeervsflae rqeavergrl ptmlvvmdes cirrqvggpk
      181 vmraqldrlm qfaelpntvl qiapfdmger rpfnlpmtll tmpdlsviay aesqvrghle
      241 retaavlpll adyhqlqada lsqaasvavi kea
//
LOCUS       WP_181797549             229 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces sp. WELS2].
ACCESSION   WP_181797549
VERSION     WP_181797549.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  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 229)
  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 229)
  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 229)
  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..229
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..229
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24349
     Region          9..>171
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 msdlgtlsvi fdldgtlvds epnyyeasrq tlaahgipgf twadhegyvg istretvriw
       61 reryglrasv pellaetnrr yldlartrtr aypqmrafve llaadnvpma vasgsspeai
      121 eavlagtgla ahlrttvsad evphgkpapd vfleaarrlg tppadcvvle daapgaaaah
      181 aagmrcialp yvpaqadape fttaslllrg gqadftarsa yawlrdgar
//
LOCUS       WP_181797644             334 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces sp.
            WELS2].
ACCESSION   WP_181797644
VERSION     WP_181797644.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 334)
  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 334)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 334)
  AUTHORS   Rosinski,J.A. 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 334)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..334
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..334
                     /product="helix-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=37034
     Region          153..333
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <273..334
                     /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 mrarenpsrg rqptdseake aylamrerig tsdaryater eelrglpaev trwlaerrll
       61 dpggerlstp eralrhvvse hrrrlretad glardarald dvlslltvpr pgaretvete
      121 fftdrertrr rleeldalsr eeflamrntf pgarvldasl ardlemaadg irmrvltsqq
      181 alrspapary laaladagve vrvaatvplh mnimdravvv igvgagprge ggdvilhsgp
      241 vaqcfarvfl hawdlarpht erpagpdrpg prlsvlerev ltllatgakd dtiarrldcs
      301 drtlrrlmhr imvklgtssr feagvtaarl glvd
//
LOCUS       WP_181797697             116 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Streptomyces].
ACCESSION   WP_181797697
VERSION     WP_181797697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=12341
     Region          <56..111
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(61,64,106)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mhlvpadrad rrtidghrvc eaiaaigdag rlrtwadrfs lladanrlal llalhrtgpl
       61 avsdlaiatg mndpavsqal rllraagvva gekegrvvry rvvdedvrgl lehcaa
//
LOCUS       WP_181797887              86 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Streptomyces
            sp. WELS2].
ACCESSION   WP_181797887
VERSION     WP_181797887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..>86
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <53..>85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 msnpvsdear viplrpapaq pkapesepap replwrdlvg evlrrerreq rrtlkdvada
       61 arislpylse iergrkeass evlaaa
//
LOCUS       WP_181797983             487 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Streptomyces sp. WELS2].
ACCESSION   WP_181797983
VERSION     WP_181797983.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     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=49204
     Region          20..473
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mastlpdphp gagptpagga svsgaaerag veahgidlip dserrgrpre lfsvwaaanv
       61 nylslvvgga lvlmglslwq alavivvgnl fwlltgllav pgpvagapse vvtralygvr
      121 gnrvnnavtg wlisvcyfal nlaaaataaf slvdraglpv ttavkaavvv liaavtlaig
      181 vyghaaivrl ylpitlvlsa vfavvgvavl rhtdfgytpg ppltgrdlwa tvaagtalia
      241 sgplsyttsa dfsrylprtt pakavagwta lggfvpsvlv cgvgacaata vdmndpetsl
      301 qtllpgwfrp vfllalvlgt valnaltsys aglalqavgl rirrtlsvlv dgavavsltl
      361 yallvsdfld avgdvlqltv lllgpstavy atdillrrgr ydgpglades pggpfwytgg
      421 vnrsgalalt agvtasalsv dsvytgpvaa alggvdlalp agllvasaay avlftrlgpa
      481 aprtgqp
//
LOCUS       WP_181798034             436 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein, partial [Streptomyces sp.
            WELS2].
ACCESSION   WP_181798034
VERSION     WP_181798034.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..>436
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          2..436
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 maqfveprsi dvvpdeerhg rafgqftlwl ganlqitavv tgalavvfgg dvvwsvlgll
       61 lgnllggavm alhsaqgprl glpqmiqsra qfgvrgavvp lllvvvmyvg ffasgsvlag
      121 qavgelthtd dttgilvfaa vtgviatagy rvvhalgrva stvcalafvf lavrllerad
      181 tsallhdahf slpvfllavs lsaswqlafg pyvadysryl prttsakatf wwtlagsalg
      241 sqwsmtfgvl vaatageafl dsqvgyvvgl ggtglvasfl yfvialgklt vnvlntyggf
      301 mslvtgvsgf rgqrrlsrag rvayialvmt agtavallgk dgflasfkdf llflltfftp
      361 wsainlvdyy lvskerydla aladphgryg awrwdalavy aagllaqlpf latgfytgpl
      421 veplggadvs wivgla
//
LOCUS       WP_181798116             386 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein, partial [Streptomyces sp.
            WELS2].
ACCESSION   WP_181798116
VERSION     WP_181798116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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 386)
  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 386)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         <1..386
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
     Region          1..381
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 levreaghtl gnarweagna rdvllyaagg aerllgrqip apggwdvtfh eplgvvgvia
       61 pwnfpmpiaa wgsfpalaag navvlkpaea tpltalrlag laleaglpeh lfqvlpgygt
      121 tagralvdhp dvakivftgs trtgrevmer carlvkpvtl elggkspnvv fadadltaal
      181 dpfsfldncg qdccartrvl vqesvleear allaealaav vvgdpadekt qmgplisarq
      241 rervrsyvpd dapalrgsap dgpgfwfppt vltgerpdgr aareeifgpv avllpftdeq
      301 davrlandtp yglsgsvwtr dvgralrvsq avragnlsvn shssvrywtp fggfkqsglg
      361 relgpdalta ftetknvfis tegpaq
//
LOCUS       WP_181797751             199 aa            linear   BCT 28-DEC-2024
DEFINITION  RICIN domain-containing protein, partial [Streptomyces sp. WELS2].
ACCESSION   WP_181797751
VERSION     WP_181797751.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19228254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..>199
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          36..162
                     /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(52..55,65,67,70,74..75)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(61,94..97,107,109,112,114,116..117)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(80,84,86,90,94..96,107,109,112,116)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(137..141,150,152,159..160)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Region          177..>199
                     /region_name="GH43_62_32_68_117_130"
                     /note="Glycosyl hydrolase families: GH43, GH62, GH32,
                     GH68, GH117, CH130; cl14647"
                     /db_xref="CDD:449341"
ORIGIN      
        1 mnrgsfsrrh psavlaavfa alaalaallv atpaqaassg alrgvgsnrc ldvpgavetd
       61 gtalqlydcw ggtnqqwtlt danqltvygn kcldvpghat tagtkvqiwt csgganqqwq
      121 vksdgtvvgt esglcleaag agtangtavq igtcnggsnq kwtgltgttt pptggtcalp
      181 styrwsstga laqpangwa
//
LOCUS       WP_181798163             295 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces sp.
            WELS2].
ACCESSION   WP_181798163
VERSION     WP_181798163.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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   4  (residues 1 to 295)
  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 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
REFERENCE   6  (residues 1 to 295)
  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..295
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..295
                     /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=31644
     Region          3..>149
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mntprvalvt ganqglgral veglaarmap qdlvlltgrd rrrvsdaare vaglpgtrar
       61 vegrvldvar tdaiarlaee lrerhggvdi vlsnavtrvl peesqaarad evidvsntat
      121 hailrhfgpd lrpggrllvv asslgtlgrl dprlhhlfdg vtldqvehav eswrraihdg
      181 tareagwpvw lnvpskvaqv aavraaaaer rerdlatgtl vaavcpgmid tatsrpwftd
      241 ysqaqspaqa aravldlvfa egvdpahhge lvrfgkalsw ydgtppveqe rlltp
//
LOCUS       WP_181798304             442 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Streptomyces sp. WELS2].
ACCESSION   WP_181798304
VERSION     WP_181798304.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 442)
  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 442)
  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 19797826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..442
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=46008
     Region          <41..234
                     /region_name="YfbK"
                     /note="Secreted protein containing bacterial Ig-like
                     domain and vWFA domain [General function prediction only];
                     COG2304"
                     /db_xref="CDD:441879"
     Region          388..434
                     /region_name="VWA_3_C"
                     /note="von Willebrand factor type A C-terminal domain;
                     pfam18571"
                     /db_xref="CDD:408355"
ORIGIN      
        1 manfakpdvp rfsvdvyqne ylpeggsqvd aivtvtatgg gilggadsap grpsaavavm
       61 vdcsgsmdyp pakmrgarea taaaidtlrd gtrfvviggt hvaqevypgg grlavadatt
      121 reqakqalrr lgagggtaig twlrladrll saadvtirhg illtdgrneh espedlratl
      181 dacagrftcd argvgtdwdv kevtgiasal lgtadivadp aalaadftrm metamgkeva
      241 dvalrvwtpa gatirfvkqv apavedlthr rteaapragd yptgswgdes rdyhlsvtvp
      301 paglgqemla arvslvvpqp dgtvqnlgaq glvravwtdd vaastamspq vahytgqael
      361 aqvirqgidl rkagdfdgat aklgravqla nasgnadtak llakvvdvvd aatgtvrlkt
      421 rvteademtl etrstktvrv kk
//
LOCUS       WP_181798530              99 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Streptomyces
            sp. WELS2].
ACCESSION   WP_181798530
VERSION     WP_181798530.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 99)
  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 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   3  (residues 1 to 99)
  AUTHORS   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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 amino end.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         <1..99
                     /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          7..62
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 tsaetglhal tpaehrtall aakgltnkei adrlyvtrrt velhlsrvyr klavagrgdl
       61 paavadqlpd parrplrrvd aavsppdrpa rsmtlrpas
//
LOCUS       WP_181798432             199 aa            linear   BCT 28-DEC-2024
DEFINITION  RICIN domain-containing protein, partial [Streptomyces sp. WELS2].
ACCESSION   WP_181798432
VERSION     WP_181798432.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Cummings,R.D., Schnaar,R.L. and Ozeki,Y.
  TITLE     R-Type Lectins
  JOURNAL   (in) Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M,
            Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL and
            Seeberger PH (Eds.);
            ESSENTIALS OF GLYCOBIOLOGY: 419-430;
            (2022)
   PUBMED   35536958
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Hazes,B.
  TITLE     The (QxW)3 domain: a flexible lectin scaffold
  JOURNAL   Protein Sci 5 (8), 1490-1501 (1996)
   PUBMED   8844840
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19228254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         1..>199
                     /product="RICIN domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          38..163
                     /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(52..55,65,67,70,74..75)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(61,94..97,107,109,112,114,116..117)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(80,84,86,90,94..96,107,109,112,116)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(137..141,150,152,159..160)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Region          177..>198
                     /region_name="GH43_62_32_68_117_130"
                     /note="Glycosyl hydrolase families: GH43, GH62, GH32,
                     GH68, GH117, CH130; cl14647"
                     /db_xref="CDD:449341"
ORIGIN      
        1 mrrrsfssgr lsvvlaaavt ilaalaallv aapaqaassg alrgvgsnrc ldvpgasqtd
       61 gtnlqiydcs gganqqwtlt danqltvygn kcldvpghat tagtkvqiwt csgganqqwr
      121 vnsdgtvvgt esglcldvtg aatangtave lwtcnggsnq kwtglsgttt ppgdgscalp
      181 styrwsstga laqpangwv
//
LOCUS       WP_181798974             152 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase, partial [Streptomyces sp. WELS2].
ACCESSION   WP_181798974
VERSION     WP_181798974.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  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 152)
  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 both ends.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         <1..>152
                     /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          <7..>151
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 raraegeart rrffadashe lrtplvgikg ytdlyrmgam ptredvdqtm sriaeesarl
       61 trlveemfll arldedtegt gtarepafal dlapmdlrtl aadalhdvqa ldatrpvtlt
      121 gpgggkptta pahadearlr qvvtnligna vt
//
LOCUS       WP_181799168             370 aa            linear   BCT 28-DEC-2024
DEFINITION  ferritin-like domain-containing protein [Kitasatospora acidiphila].
ACCESSION   WP_181799168
VERSION     WP_181799168.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora acidiphila
  ORGANISM  Kitasatospora acidiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
REFERENCE   1  (residues 1 to 370)
  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 370)
  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 370)
  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 10583968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Kitasatospora acidiphila"
                     /db_xref="taxon:2567942"
     Protein         1..370
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39697
     Region          16..237
                     /region_name="Ferritin-like"
                     /note="pfam12902"
                     /db_xref="CDD:403953"
ORIGIN      
        1 mtastidsrd dlisylhaam alehatipty ltayysihsa tnsdaahiir vvaveemlhl
       61 tlaanvlnai ggtpdltapg fvpsypaylp dgeddftvdl rpfspeavet fckierpgka
      121 psgssrlvra sdngrpllaa sptakgmrfy sigefyeeii eglekvaadd pglfcghpal
      181 qvgpeyfysg ggtvitvsdl dsarralrfi aaqgegldsg ihdadgelah yyrfrqlqlg
      241 ryyqvgdhpd apsgpplsvs wddvyrlkvs arladypags elagaarkfn adyeaflall
      301 tkafngkpdl lqdavwymfr lrdgfnrlvr nplpgsdglh aaptfeipna vgpgpdaart
      361 aggtaqavtr
//
LOCUS       WP_181799222             138 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Kitasatospora
            acidiphila].
ACCESSION   WP_181799222
VERSION     WP_181799222.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora acidiphila
  ORGANISM  Kitasatospora acidiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
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="Kitasatospora acidiphila"
                     /db_xref="taxon:2567942"
     Protein         1..138
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15456
     Region          23..115
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mederrpgrq vsvqevlara gdvreafdti antwsllill alrdgtlryn elkrtvggvs
       61 errlsqtlkv lerdgvvdrk lvrsipshve ysltptgevv vdslgellst iiefspqvaa
      121 arrrydekqa qaqenper
//
LOCUS       WP_181799110             281 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Kitasatospora acidiphila].
ACCESSION   WP_181799110
VERSION     WP_181799110.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora acidiphila
  ORGANISM  Kitasatospora acidiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
REFERENCE   1  (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   2  (residues 1 to 281)
  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..281
                     /organism="Kitasatospora acidiphila"
                     /db_xref="taxon:2567942"
     Protein         1..281
                     /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=30163
     Region          8..278
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mpsesrlril llgasgfvgg glwshlrarh evvgtfatrp vpglvqldlr derrlsalaa
       61 dgfdlvihaa glvplevaea dpelahrlnv rpievlldav rgsaaklvfl ssdnvfdgtr
      121 hqyteddhrs pvnvygrtka aaedllradg ghlvvriplv ygrgpwantf larlagsttp
      181 artdlvcapv ylpglgpava elwgrtgvvh yggrdvvtrf elmskvqqal elptrvvavq
      241 gdearagcrr pprlvlrstr hrllgpglda alahlagrpl a
//
LOCUS       WP_181799350              96 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Kitasatospora
            acidiphila].
ACCESSION   WP_181799350
VERSION     WP_181799350.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora acidiphila
  ORGANISM  Kitasatospora acidiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
REFERENCE   1  (residues 1 to 96)
  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 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   3  (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 10612959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Kitasatospora acidiphila"
                     /db_xref="taxon:2567942"
     Protein         1..96
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9977
     Region          2..>36
                     /region_name="HTH_Tnp_4"
                     /note="Helix-turn-helix of DDE superfamily endonuclease;
                     pfam13613"
                     /db_xref="CDD:463934"
ORIGIN      
        1 medrvllvav ycrtnltmrq lappfgtsha tahriigrhs pscvrrepph qrqeaaaasg
       61 aglagaepes sgiepvespe vgfevapple gavgar
//
LOCUS       WP_181798646             511 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase, partial [Streptomyces sp. WELS2].
ACCESSION   WP_181798646
VERSION     WP_181798646.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WELS2
  ORGANISM  Streptomyces sp. WELS2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 511)
  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 511)
  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 511)
  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 511)
  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 12220070
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Streptomyces sp. WELS2"
                     /db_xref="taxon:2749435"
     Protein         <1..>511
                     /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          1..78
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Region          95..>511
                     /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 repfladlvr ghvatilgyr sgqdvgrtla frelgfdsla avelrnrltt atglklpatl
       61 vfdhptpavl arhllgeltg tlapaparta prpaaddepi avvgmacrfp ggiaspedlw
      121 rlvaegrdav gefpadrgwd ldrlydptld rpgtsytrhg aflydaagfd paffamddee
      181 alvtdpqqrl lletsweale rasidpatlr gsdtgvfagv myhdyfgsyg sgsvvsgrva
      241 ytlglegptl svdtacsssl valhlaaqal rqgdcslala ggvtvmatpg tfvefsrhrg
      301 lsrdgrckpf adaadgtgfg egagvlller lsdahrngrr vlavlrgtav nqdgasngis
      361 apngpaqqrv irraleaagv aasdvdvvea hgtgttlgdp ieaqaliaty gsehtddrpl
      421 wlgsvksnlg htqaaagvag vikmiealrh etlpaslgvd rptrhveweg snvrlltenr
      481 pwpdpgrprr agvssfgisg tnahviieaa p
//
LOCUS       WP_181799392             158 aa            linear   BCT 28-DEC-2024
DEFINITION  glycine-rich domain-containing protein [Kitasatospora acidiphila].
ACCESSION   WP_181799392
VERSION     WP_181799392.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora acidiphila
  ORGANISM  Kitasatospora acidiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..158
                     /organism="Kitasatospora acidiphila"
                     /db_xref="taxon:2567942"
     Protein         1..158
                     /product="glycine-rich domain-containing protein"
                     /calculated_mol_wt=16832
     Region          12..137
                     /region_name="COG4278"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443419"
ORIGIN      
        1 mldprtllse eafsgvvatv rqnnpgmvse iaqritteal afvaacaefp elrlkpsrvv
       61 degwhalilh trlyaelctk lgvfvhhrpe apdvtrhdpn alkrtmrais tagypvdhal
      121 wagpadtsip vaadcehspp gpegsctgdc sntgpnva
//
LOCUS       WP_181799584             928 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Kitasatospora acidiphila].
ACCESSION   WP_181799584
VERSION     WP_181799584.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora acidiphila
  ORGANISM  Kitasatospora acidiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..928
                     /organism="Kitasatospora acidiphila"
                     /db_xref="taxon:2567942"
     Protein         1..928
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=100488
     Region          <3..924
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mtehgsadar hepaeleqph lyeresalqd aqqaldrlrv eyaaggvelg slllysgkag
       61 mgkttmlqqi ralagaqgit vlsgrageqr ikepfhllrq lllgelsals tgqldevlge
      121 whavagpalg lvpptgedld pqsvqqgldv vmtqlarvra plvmlvddlq wadqeslvwl
      181 eslavrcpel plllaiawrt gelpdrvrgf rslvagnshr hlefqgltpp avgklvrevf
      241 qdaedsfirq vwavtdgnpf lvnallakvr esgiepvqen mpllhdlaae aqgmdsdywm
      301 gklsiealkf aqaaamldte ilprvatria alspataaaa iaelrrhqvl tgpadgplef
      361 vhpllatsly qsirpairta mhgkaavele nagrplvess rhlletypdd erevvvklrr
      421 aarehlavga pdaavrcler alaeppedei rarviyelac atlltdpiat anqlklaldt
      481 vpglpadlrv davfrlsevl ahsgrlgeat dltlaeaqrt dpgpgrtrla vahfmwaafq
      541 rdeadgpgrs srladlasgm pgddvnaraa ralrawdltl rgssvtrvqa lldsaldqgr
      601 lpaelgwttn pwglelpgii althiytdrl draeqlidda iwafgvagwe gahlgiavfl
      661 mglakfrrga laeaevelrn alriarrvgp dlplqwdavg vladtllarg rveearklaa
      721 dysfappyhp daivlpdaat lygklllaqr dregavgvlr gvgeqltarg whntiwapwa
      781 ghlaqalype rpeearelae whvqrarifg vasavgsalr mnaavvegql avvcnadglv
      841 hrarrelnaa glrpnlprst grdalsrnew rvaelivdgl tpsqiaerld vsvslinrri
      901 aavhrktgsd veglaaalgl averpdsd
//
LOCUS       WP_181799604             275 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Kitasatospora acidiphila].
ACCESSION   WP_181799604
VERSION     WP_181799604.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora acidiphila
  ORGANISM  Kitasatospora acidiphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..275
                     /organism="Kitasatospora acidiphila"
                     /db_xref="taxon:2567942"
     Protein         1..275
                     /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=29432
     Region          <16..>253
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          41..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 mtdgacdgrp dtadryvfdr ewereherla aleavydgvt ldrlaglgva egwqclevgc
       61 gagsvarwla ervgargsvl aidldprfae ghglpnltvr rqdlltdplp adaydlvhar
      121 allehlpare qaldrlaaat rpggwvvved fdiegamaaa varywpaght glaerlysal
      181 qavfggaggd agcgrwlpda laraglteig alvhapllrg gtpflvltlr qlrapllagg
      241 litaqeldka leliqcqeir ytpnfmvtaw grrpg
//
LOCUS       WP_181799952             431 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Marinobacter pelagius].
ACCESSION   WP_181799952
VERSION     WP_181799952.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter pelagius
  ORGANISM  Marinobacter pelagius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
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="Marinobacter pelagius"
                     /db_xref="taxon:379482"
     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=48173
     Region          23..387
                     /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 mdtkegldli ivgggiggvi clkyakdagl nallleraer igglwrdlps wqdiqfrked
       61 wtlgtlplag edqpnilgni eawaerfkls pyirlnapvt sarpcengwh ittdaathea
      121 kwliaatggh nrpvvpqver idssileyhs salpdpeelr dkrvtvvggg asaydlldlc
      181 fahgarsvaw iyrstkwmrp trqskhlgtd mrvlaryqml clpasmlhrl snkdlrarya
      241 kaginevmpe vdfdirhdql ipgrpgmikn faqierhrge vsslsgktik lssgeeletd
      301 lllwgtgysv dfgflglevl nkarnlneis srcysrflsa dapnlfllap gvldtntstp
      361 wayahvaksi mshiggesvf vrppshaftn hfdlvkllap qdrgsypfgi wylkylwlal
      421 fhpwrrpmpi p
//
LOCUS       WP_181800172             464 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Streptomyces ipomoeae].
ACCESSION   WP_181800172
VERSION     WP_181800172.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     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=51250
     Region          7..432
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpmghtatae agsegltvke hrldnglrvv lsedhltpva avclwydvgs rhevpgrtgl
       61 ahlfehlmfq gskqvsgngh felvqgaggs lngttswert nyfetmpahq lelalwlead
      121 rmgsllvald qknldnqrdv vknerrqryd nvpygtafer ifrlaypegh pyrhtpigsm
      181 edleaasled areffrtyya pnnavlsvvg didpeqtlaw iekyfgsipk ydnkrerrdg
      241 slpdvigeql revveekvpa ralmaayrlp edgtracdaa dlaltilggg essrlynrlv
      301 rrdrtavtag fgllrlvgap slawmdvkts gdvevpviea avdeelarfa aegptaeeme
      361 raqaqlerew ldrlgtvagr adelcryavl fgdpklalta vdrvldvtae evqeiakarl
      421 rpdnravlvy epvageedea eaaeaeatep eaaettdene esak
//
LOCUS       WP_181800324            1010 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces ipomoeae].
ACCESSION   WP_181800324
VERSION     WP_181800324.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1010)
  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 1010)
  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 1010)
  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 1010)
  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..1010
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..1010
                     /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=108071
     Region          306..965
                     /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 msprpssapt lsptprtakp lpgvllpggp sperggaslr aqlvlallca ayavgaafgw
       61 gneqvalvmg dfglsaaaat aavscfryar srrsrfrpaw llfalssama algngvwgwy
      121 evvlerpvpn psyadlfflc fappaivgll vlakrpvtqa gwvclaldaw liggslvtls
      181 wslalaqtaq lddsdtahta lslayplldi alvsmvlalh frrssmhrsa vntaigalal
      241 tvmcdalfas pllhnsyrsg qlldagwfag slllayapwa gqrhgqpeee qharvvhehi
      301 pgqrhdadgh rhdgphgghv hvplqggghs rypvtrpiag slaaltpyla aavctlgily
      361 nvlngrsvdr vvlitactvv lalvvrqgim lldnitltqe laqkenhfrs lvqgssdvim
      421 iaapsgilry vspaaagvyg rpaeelvgke lasiihpedl gcvvhevrrf laaspaeept
      481 triecrfksg dggwlnvest vnrhhgglif nsrdvtervr lqaqlqhnae hdpltdlpnr
      541 alftkrvqqa lsgrrssdrg ialrntavlf idldgfkavn dtighqagde llvqaarrlq
      601 esvrqgdtaa rlggdefaal ivgdgsrdra areqhifela drlrvtlsqp ytidgndvrv
      661 aasigvafae aglgagellr nadlamyrak asgkgrvely qpqmqqdvvr kaelatrlra
      721 alhdgeflll hqpvveletg rissvatear wrssqgvlft paeflrvsed ndktaelgrw
      781 mleqavehas erlvnglhvp vsvrmsarrl ldrslppgsl etlltrhglp sgslvielsd
      841 tevkgslddl errlsqlrrl gvrvaldglg sgqaaitalr rlpvdvlkld rslvegvves
      901 trlhkitsgl lriagdlgle svaegvdlpe qvvalramgc thgqgaafsg pldeyrlrra
      961 lstgnypvpr gpaepafagg gagvytsgvp avygggsalr shnetpvppt
//
LOCUS       WP_181800538             332 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Streptomyces ipomoeae].
ACCESSION   WP_181800538
VERSION     WP_181800538.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  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..332
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..332
                     /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=32786
     Region          77..272
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mlllgacaaw slitaatrgg rpegvllavl alsagyaagr isgallpvla pgvgalaglg
       61 laitaphtmg gsplvpplgh tgataallal stgaaccaaw aarapglrla lwllavgvav
      121 taavldsttg lfacagvllc slaaarirhr glglsglalv talvtgtawa iaenilpsgp
      181 tdalegeltp hrislwrdal glahedpllg agpgrfgels ttitlsapsd dkphsapfql
      241 aaeqgligva llatvfcwvl yvlwrtprpt pvvltagaal talaaiaavg nalsfttvta
      301 gagllagmat arpltdeedg vgvperdapy gd
//
LOCUS       WP_181800562             339 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            ipomoeae].
ACCESSION   WP_181800562
VERSION     WP_181800562.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     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=36496
     Region          2..305
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mvigatgqig rvavgalard gwevtavsrg gdrdknwpeg vrvaradrad daalsaaigd
       61 gcdvlvdmva ygpeharqlt glaervgsav vissisvyed dkgrnfdtqa epdgfpeypv
      121 pltesqrtvr pgeasystrk aglerellav gerlpttlvr agaihgphcr tprelyfvkr
      181 nldgrrrrvi ayggesrfhp asvhniaeli rlaaarpgtr alnavdpdap kvteiaaaid
      241 avmgvrtenv lvdgpppvpa vgdtpwsvpa pvvcdmsaae qelgyrpvva rhaetlpetv
      301 awierqlagg rdwreaypkm fqtygdlfdy aaedawlks
//
LOCUS       WP_181800592             284 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces ipomoeae].
ACCESSION   WP_181800592
VERSION     WP_181800592.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..284
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32301
     Region          11..>58
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(17,21,47)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(20,46)
                     /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          113..271
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mnnqaqeare algarlrgfr kdagfasgra favatgwaes kvsrlengkq npseddirvw
       61 cvktnkhehv ddliatvrhi delwlewrrq lqtgaerrqr kalpvyaktk vfrvwhptlv
      121 wgtiqtadya aetfkqvvdy yeipddteaa takrlerqqy lyrgnrifnv vlgeqalytn
      181 fggpevmkgq ldrllavmrl prlslgiipr sapigiwpgn sfsmfddklv lvetysaefs
      241 vtqpreiely tkafallqqs avygsavrdl iltaihhfdq mpsd
//
LOCUS       WP_181800677             333 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Microbacterium sp. H6].
ACCESSION   WP_181800677
VERSION     WP_181800677.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. H6
  ORGANISM  Microbacterium sp. H6
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
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="Microbacterium sp. H6"
                     /db_xref="taxon:421122"
     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=39066
     Region          31..307
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mftrwidsyg pndistevrr khrrqgelhi lpfladvpia dldrervqrf lshdiaalpd
       61 gawrntykvv ktmltwatnn dliarnpitg vkqrtykaav hdddiqlidk rttialdllr
      121 wlkdeqhkhy vlilfmflgl rrsellgltw nciddddtdv garihvrqql srakgqgwfi
      181 dprtknnksr ivymphewwv dltwhkmtty pdigdwrddl vfrrddgmhi nytdvqkiwd
      241 dvldayfaar etkpekwrlh ynrhltasmm fragqnlqyv qellghsdat mtlyythfsa
      301 qakkdaitay gdalekgdwg rlakineanp vse
//
LOCUS       WP_181800691             422 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Microbacterium].
ACCESSION   WP_181800691
VERSION     WP_181800691.1
KEYWORDS    RefSeq.
SOURCE      unclassified Microbacterium
  ORGANISM  unclassified Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 422)
  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 422)
  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 422)
  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 422)
  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 422)
  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 422)
  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..422
                     /organism="unclassified Microbacterium"
                     /db_xref="taxon:2609290"
     Protein         1..422
                     /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=44854
     Region          113..422
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 msfrtrlvii itavfiaaga alltvqylvv qqlfstaitt teasclpmaa vlqvgegssa
       61 tdgpdvsevt plpdsssvlw gqastgcgyy vgsidaqlav psqtltfdav egavlqqssf
      121 ladevgngll lwsvvvlvaf tgvaaaiafw larrsldrig evtaaardis erdlgrrlal
      181 pgpddeikel gdtidgmldr lqsaftaqdr fvanashelr tpltttrtal eipleqgavp
      241 adlqanmqra lrateqserl itallalara rtgleevepv elrtliedqv ddldaqeiev
      301 htnlrdltve gdavllarav rnllengirh nvpggelwvr srrergravi eientgaqit
      361 patvqlltep fyrgdasrts agpdgtglgl aivqsiakth ggevrlrark gggliaaivl
      421 pl
//
LOCUS       WP_181800692             400 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein, partial [Microbacterium sp.
            H6].
ACCESSION   WP_181800692
VERSION     WP_181800692.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. H6
  ORGANISM  Microbacterium sp. H6
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 400)
  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 both ends.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Microbacterium sp. H6"
                     /db_xref="taxon:421122"
     Protein         <1..>400
                     /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          58..331
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 aqlrlpvtvp agasamtlrf vfdapgaags wmlddvqvvr plaalaegve antvvdifsd
       61 vqgattrlsq nvlpgframa qtadvlvsng dlvsngstan ytsylsalaa ggggeygtvv
      121 stignheyyg segsavyrer fldstgmrdi ggqgglwgev lvdgqlpliw igsefydyta
      181 ktgagpfvdf seeqftwlrd rlahwraqdq pvllfshhll pysvsgsyar fyendfgqee
      241 arfaallaqn pnvimfnsht hwsptlndws telrpdptra hgptvvntga vttmygpsgd
      301 weekavggad pvglraalyd drvrvtvysf stagateikh vdiprptdap vdpvdpvdpv
      361 dpvdpavals aqtvaaggrv tisgtgfpea aelaielrst
//
LOCUS       WP_181800972             236 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces shenzhenensis].
ACCESSION   WP_181800972
VERSION     WP_181800972.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 236)
  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 236)
  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 236)
  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 236)
  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..236
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..236
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25788
     Region          13..217
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtltahelfg wspeavvfdc dgtlmdserh wqearnrafr eyglqpprgf aeqatglhye
       61 dcgrlmarsv rkpelaeglt aalldhflal vtddpvtmpg avqlvrllsv rlplavasnc
      121 prvvvegsle raglsahfqh ivvpdagdgv rpkphpdvya vaarlcgvrp hralavedsl
      181 tgvksarsag lrvlgvgprp qddsetradl wlpalhepel lawarswdir rplpep
//
LOCUS       WP_181800978             472 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces shenzhenensis].
ACCESSION   WP_181800978
VERSION     WP_181800978.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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..472
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..472
                     /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=50770
     Region          37..416
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtssasssas gavnggisfw yaddglpavr eplagdasad vvivgggytg lwtayylkka
       61 apflrvtvle qkfcgygasg rnggwlyngi agrdryaalh greaavrlqk amndtvdevv
      121 avaaaegida dlhkggvlev attpaqlarl kafhqhelsy gekdrelyga getrerirva
      181 davggtwtph garlhpvklv kglvaaveal gvrihestpv teirpghavt pygtvrapyv
      241 lrctegftan lrgqkrtwlp mnssmiatep ltaeqwasvg wegretlgdm ahaymyaqrt
      301 adgrialggr gvpyrfgsrt dndgrtqeat iealreilvr ffpslagvav ehawsgvlgv
      361 prdwcatvtl dratglgwag gyvgsgvatt nlaartlrdl vqldsgqagr tdltelpwvg
      421 hkvrkwepep lrwlgvqgmy atyraadqre rrhpstassr larvadrvag rh
//
LOCUS       WP_181801149             328 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181801149
VERSION     WP_181801149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=35874
     Region          4..327
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 maiakaerlm nlalcllgtr rplskrelrd sieayveasg pgrgaasgpg sddsfnrmfe
       61 rdkddlrelg lvietvenld gevgylarrd snrlppitld aeeaaalgla akvwqqarla
      121 gaasgalqkl raaglpegvd pyeahgalep ripvheaafe plmlacrdrr pvlfeyrkat
      181 aahpetrnve pwalecwrgh wylagwdrdr gaervfrlsr itgkvrsrgt aftapvpdvv
      241 tvretvaswa geiadrsali rlrsgsgypl rakatavrel gdgwdeleip yghgldawlv
      301 efgpdvvvle paelradvvd rlravakg
//
LOCUS       WP_181801126             286 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            shenzhenensis].
ACCESSION   WP_181801126
VERSION     WP_181801126.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  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 286)
  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 286)
  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 286)
  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 286)
  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 286)
  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..286
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..286
                     /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=29625
     Region          3..247
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mstftdavvv vtggatgigl alareaaarg arvmiadved artaveslra dgatvdwsqt
       61 dtsdysqvkk lteatierfg avnvvcnnag vgvagalqdv dpdeakrlfd vnvlgmfhvi
      121 hafapllkea aargepayil ntgsehslgv pphvmpmsty taskyaalgl tdtarrdlkd
      181 fgvgvslltp gwvrterisa llaadphaaa aiapfaqepa evaaaafdgv lkgtaviatn
      241 phsrafameh ardlmadiqa lplldgpndh ahdgtgdasr cpfsqg
//
LOCUS       WP_181801282             286 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181801282
VERSION     WP_181801282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..286
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32173
     Region          29..90
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          103..281
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 metvergege redagprped epgsgvvtaf grqlkllrvr aalerpefgk lvgyagqsia
       61 sfeqgrripp prfidradev ldaggvlkal keevgraqyp affrdmarle aqavalhvya
      121 aqavpgllqt deyaravftm rrplldedti eqrvaarlar qeifsrrpmp tlsfvieesv
      181 lrrpiggwal lqgqleqiml hahrrnvevq impndrtehc glagpftlie drdgrrmayv
      241 evqrdsrlht drsavreiee qygilraqal tpheslafve ellgek
//
LOCUS       WP_181801358             427 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Streptomyces
            shenzhenensis].
ACCESSION   WP_181801358
VERSION     WP_181801358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11468605
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=49098
     Region          20..417
                     /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 mahfpkpseg swtehfkidt gpvsyadsis pefyelerda vfrrtwlnvg rveqlprkgs
       61 yftkeldaar asvvvvrgtd gevrafhnvc rhrgnklvwd dypreetkgt craftckyha
      121 wrydlegklt fvqqeseffd idksqyglvq vqtevwegfi fvnldpentt plkaylgkfa
      181 qgidgypfhk ltqvhkyrae igsnwklfid afaefyhapi lhagqyesge aakikkygye
      241 alsydidgph smvsswggia ppkekamvkp iervlrsglf gawdapdigm taeelppain
      301 ptrsevwgmd sfvffpnfml liwrpnwvlt yhywptsynt hifegtayfv ppkngfqrlq
      361 qelaavtfke yglqdgntle atqtmlesrt vdqfplcdqe vllrhlhttt qnyvreyqqr
      421 natapis
//
LOCUS       WP_181801369             401 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181801369
VERSION     WP_181801369.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..401
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42571
     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 mkplegirvl evamygfvps agavladwga dvikvehavt gdpqrglrqt gsfrveddpn
       61 pnvahanrgk rsvgldmsrp egrevlyklv kqsdvfltsf mpasrarlgi dvddiravnp
      121 rivyargtal gprgpeadkg gydmtafwar agtaasitpp gsdgmisppg paygdtvsgt
      181 nlaggiaaal lrrertgesp vvdvsllgsg lwalghaiav svrldraweg vtpsahgspt
      241 nplsglyrta ddrfiafvml qparfwpnvc rcigrpelad dprfataeai avhtadavki
      301 lreviasrtl tdwsedlsal dgpwapvqdt lqaaadqqvr angyigqage lelvaspvqf
      361 diqdtrlgpa pefaaqteev ltelgygwdr ilalkasgai t
//
LOCUS       WP_181801418             454 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181801418
VERSION     WP_181801418.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 454)
  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 454)
  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 454)
  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..454
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..454
                     /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=49245
     Region          21..415
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(58,65,94..95,102,106,113,245..246,249,253..254,257,
                     292,297..298,301..302,304,329,357..359,362..363,365..367,
                     371)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(65,88,90,93,95..96,182..183,192,244..245,248..249,
                     253,298,301..303,406)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mttqlppssc pfaidpagsd lhaearqlra lgpaarielp ggvaawsvtd palierllld
       61 drvskdahqh wpafvdgqip ekwplrlwvq vrnaltaygp ehkrlrrlig tgfqirrvra
      121 lapaikdiah allddleryg gtgspvdlre yfawvlplrv vnnllgvpdd lhdtfrelig
      181 gafatdlted eaearnlaly kaldqlvtak rempgddvtt dlikahdsat dtrlsqqeli
      241 dslllligag hettvnlidh aavnlmahpd qlalvaaeta sitmddvvde tlrhqapvan
      301 ilprfptvdi hdaetgltfd agdlvvinya aanrdarvht dpdrfdvtrp trknhqsfgv
      361 gahyclgagl arleariale slfgryprlt lataaedlrp lasfisnghq qipvhidgap
      421 aratgldhlt vqvtppaapg rtpprghtae tpaa
//
LOCUS       WP_181801426             177 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces shenzhenensis].
ACCESSION   WP_181801426
VERSION     WP_181801426.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 177)
  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..177
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..177
                     /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=19057
     Region          1..177
                     /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 mvagafsvgk ttligtmsei rplrteevmt aasvpvddle grpdksattv aldfgrlsls
       61 pelvlylfga pgqqrffpil rhlahgalga lvmvdtrhla qsypvigave elglayaiav
      121 nefpdaprht vdelraamdl seqtplvffd ardrpsskna lislvsyllt llpeptr
//
LOCUS       WP_181801834             269 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181801834
VERSION     WP_181801834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=28199
     Region          9..254
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mtsenqlitg strlfavigd pveqvqapsm mnalfarlgi davlvpahat parlaavvrg
       61 lqstgnvdgl litvphkrav ldladevspt aalsnganam rrapdgrwqa dnfdgegfvr
      121 glraaghepa grhvwlvgag gagsaiavsl lsadaeltit dldenrvrtl aerlsphftg
      181 rlhsaagpva adlavnatpl gmrpedplpf dpallpsstv vvdivmkprr tallrtaekh
      241 glkvhygsam lshqldlylg ffglgrqps
//
LOCUS       WP_181802041             344 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802041
VERSION     WP_181802041.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  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..344
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..344
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36042
     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 mngplaglrv levghilagp yatmlladlg aevtkveppg gdlsrqvsda yfaslnrgkr
       61 svcldlsasg gqdhlhelvr dadallvnlk psaverfglt yetlkpfner lvcvvltgwg
      121 mdagdrpafd yvvqaatgva altgdpdgpp alpgysavdn sagmaaalgl laqvvsgqgg
      181 qievslrdvm lsqlnyhaaa wlnegkaprr lggahayyvp aqlfptaegh lalfvthdgf
      241 wrsfaaeagv egyatmaera arreevvaav tkalsvdsal swerrlrplg vpaaavctlp
      301 qalvefpdav vragehrlva spfripghql sygpppslge hggv
//
LOCUS       WP_181802175             210 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces shenzhenensis].
ACCESSION   WP_181802175
VERSION     WP_181802175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 210)
  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..210
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..210
                     /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=22049
     Region          6..200
                     /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 mvlrpssrpr tgaptvlkvv iaggfgagkt tavgavseit plsteeylte asadvdslag
       61 veakqtttva fdfgrlnlpd apvplelflf gtpgqdrfvd lwydlcrgav gavvlvdtrr
      121 lessftpvgf fediglpfvv avnqfdgahr yhpdevrtal elpasvpvvt cdardpnhva
      181 gvlltlvgha lksasanlar pastttfqda
//
LOCUS       WP_181801855             270 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181801855
VERSION     WP_181801855.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..270
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30214
     Region          14..73
                     /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          87..265
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maeqddgasf lrcfgqqlkl lreragltra elgsrlgyge dqitsvelgr ripkpelidr
       61 adevlkaggv lramkeevar arypaffrda arleaeavel htydthvvng llqteeytra
      121 lltmrrplln eetieqrvaa rlarqeifnk wpaplfsfvm eesvllrrlg gtpvlrgqle
      181 qilligqkrn vevqvmpldr ednagvdggf tlftrkggeq igyteaqgrs tlvtdreevr
      241 alaarygiir aqaltpcesl ayiekslgel
//
LOCUS       WP_181802196             312 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AurF N-oxygenase family protein [Streptomyces].
ACCESSION   WP_181802196
VERSION     WP_181802196.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 312)
  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 312)
  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..312
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..312
                     /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=35646
     Region          22..295
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 mttlteadav dglrdalgll kdreqvaerl lvssakhsfd pdkeldwdap fedgkwfwpp
       61 elvslydtpl wkrmseeqri vlsqheaaal aslgiwfeli lmqllvrhiy dkaatsahvr
      121 yalteiedec rhskmfarli argdapwypv spahqhlgrl fktisttpgs ftatllgeev
      181 ldwmqrltfp deriqplvrg vtrihvveea rhvryareel rrqmvtaprw sqeftritsg
      241 efarvfsvaf inpevytnvg ldrreavaqv rasghrrevm qtgakrltdf lddigvlrgv
      301 grrlwkssgl lg
//
LOCUS       WP_181802313             416 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces shenzhenensis].
ACCESSION   WP_181802313
VERSION     WP_181802313.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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..416
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..416
                     /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=46192
     Region          82..405
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maghiqdrwy kteadtngrp rrvrtdrygt gmryraryig pdgteksksf pdgqkrladq
       61 wlahteadms rgqyidpaas rvtfrqyaek wlstqttdmt tresvdsair ghaipylgsr
      121 plgsfkpehi rdwlselera vpassyrrvi ynnvstvlna avddghlskn pchaqsvrpp
      181 aagtgrvvpw taervfavqa alperyratv dlgggcglrq geifglpvde igfdsgwlhi
      241 anqvkvtkeg lvfsppkrnk irdvplpdrv ahvlkrhmea fppvvvtlpw lrpdgplvtk
      301 rllftrldga gavrrtdfnd rawkpalvaa gvipapkrge rhqaarehgm halrhfyasv
      361 lldagenvka lsnylghndp gftlrvythl mpssdarark avdslydgal slpsat
//
LOCUS       WP_181802326             372 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces shenzhenensis].
ACCESSION   WP_181802326
VERSION     WP_181802326.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=41368
     Region          54..356
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maniqkrpng kwraryrdld gkeharhfdr kidaqrwide vtaslvtgqy vdprsakkpf
       61 keyaeewrai qphrpstaka vaqhlrcyvy pawekralga ikpgdvqswv tslttthgla
      121 astsrtvfnt vnavfraavr drmiphnpca eaklpsvprk kivplaveqv rtlseeipar
      181 ykglvllgaa tglrpgelfg lqlrhvdllh atvsveqriq qtakhgvyvc ppktarshrt
      241 vplprmavda mkahlrdfpa drpeswifta pqggpvvyth fmdgswrpac akagiakgtg
      301 phalrhhyas llikhgesvk tvserlghtn aamtlniyth lwpdseertr aavdkayadq
      361 sgdakpqvde aa
//
LOCUS       WP_181802333             230 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802333
VERSION     WP_181802333.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 230)
  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 230)
  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..230
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..230
                     /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=25229
     Region          49..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 mlaqaspwha haaqrtaagl teplsvparm ewttrpgqgp gadalgpdlr gkrllelgcg
       61 pghnaahlat rhgahvtgvd lvglqvrrar shygrlnnlt fvaghalhyl hasdeqfdai
      121 ysvfgaiglv apelllpaia qrltpgrvlt fsvphpqrgg rspsgddrpr rdhvtlpdrt
      181 rllvarwefs tdrwekhlsq agfwltsaqe fhdprmghwp ttllirarkl
//
LOCUS       WP_181802334             303 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181802334
VERSION     WP_181802334.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 303)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..303
                     /product="phosphotransferase 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=33516
     Region          <63..246
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mttnpsaell dnlltatgqt tavreevrvw smsgvervaf pdgstaifky akkpfdsedq
       61 tlrlahtlgv pvpqvhasav ldgwlgmlme dlgpsvread dldgvaaavi lhgtrtappl
      121 pvldqnrlrt lparalehle rlrkadrwqd addvedaldr iaqaaearsa gatlepfgwv
      181 hsefhptslh igdrgwrlld faraftgpgl ldlaswhgti epphpvrlrv fleqyvtagg
      241 tpdalaprgg ltaehwalgw hrmwavewfm eqsirwindp atdpayikav rrhltdvlhl
      301 lei
//
LOCUS       WP_181802358             462 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Streptomyces shenzhenensis].
ACCESSION   WP_181802358
VERSION     WP_181802358.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  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 462)
  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..462
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..462
                     /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=51520
     Region          165..450
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mksykvsvwk isvnkttkkp tylvrwvvdg qpfsesyktk tladrfrakl vgaldkgepf
       61 dtvtglpdsl rggkaalsfl dlavkyvdar waeasakqrd svtdalatvv pvlvkpgrgr
      121 papevlrral rsyvlpvprr ererpeeiaa avrwiekasl pvgelqeitr vhelidvlgr
      181 rldgkpaatq tyrrrravvf nvleyavele hlpsnplsrv rrkrgkravq evdrrvvvnp
      241 rqarelltal tyvggydras grrlraffgc lyyaamrpge alglrrsdck lpatgwgrie
      301 laetrptagk awtdsgeahd rrglkqrahg evrivpippp lvrllrdhlk dfgtakdgrl
      361 fssergnvia assysrawkq arelalvpdq vssvlafrpy dlrhagvsqw lnsgvpapev
      421 aaraghsvdv llkiyakcid gqeqemndri mqglreggds td
//
LOCUS       WP_181802435             283 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802435
VERSION     WP_181802435.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 283)
  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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31837
     Region          15..72
                     /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(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          101..278
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mpprqtptar qlrlgaelre lrenmgltar eagemiganq arisnietgr fglseqrvrt
       61 lahnyestds alidalvama ayrnrgwwee yrgtlpsrsl dlaemeyhav alrvaqvini
      121 pgllqtpeha rtlfrqvvpe lrpheieyri shrikrqail hrekptpyta iiheaalrmr
      181 fggrelaraq ldhlakmsel phvtvrvipf dgtvfptvgh gldyaygpvp aldtaqldaa
      241 hgselidsaa qlakyrlild rmqeatlepe dsrdlihria qns
//
LOCUS       WP_181802507             418 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces shenzhenensis].
ACCESSION   WP_181802507
VERSION     WP_181802507.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   3  (residues 1 to 418)
  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..418
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=44004
     Region          <196..395
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mstlerarcr agahplavda viaagalvcm avssfaaphg argvawgirt paplslvlmt
       61 laaaalvfrr hapktvlavt gaasvlecvm gdprapvama avialftvaa ttdrrttlra
      121 glltmtvltt aamvagplpw yaqenlaifa wtgigatagd avrsrrafvq aireraerae
      181 rtreeearrr vaeerlriar dlhdvvahhi alvnvqagva ahvmdkrpdq akealghvre
      241 asrsalnelr atvgllrqsg dpeaptepap glhlleelad tfrnaglqve varadqgttp
      301 paavdlaayr iiqealtnvq khagpdarae vsvvrvgprl evtildngsg qdtapeaggg
      361 hgllgmrerv talrgtlttg prygggfrvh ailpvktdtd ertngrprdr taalgdsa
//
LOCUS       WP_181802529             415 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802529
VERSION     WP_181802529.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 415)
  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 415)
  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 415)
  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..415
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..415
                     /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=45462
     Region          43..394
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mgrraggvgv aeaagtdgvg haryayrlrv ssaarsalsa ewgrcrwvwn ecvaksravh
       61 lrnratgqka acgpaqldrm ltgarartpw lregssvpqq qvvrdfgrsr akahkdirgr
      121 lpmarragmp khkkkreala slnytqrgfr lkggrlhlag givvtvvwsr elsaepssvr
      181 vyqdslghwy asfvvpaqaq plpetgrvvg vdwgvketat ttsddhdlph aghgrkaqak
      241 ltrydrmmar rrpqkgqsas kgyrearrlr akvykkaarq redtgrkwak kvvrdhdava
      301 vedfkpkfla rttmarkaad aaigatktal iemgrkhgrd irlvhpaytt mdcahcgara
      361 khalplgert ytctacrtvs prdknsarvm lvraglipag adgarppgal lqeaa
//
LOCUS       WP_181802533             288 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802533
VERSION     WP_181802533.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..288
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32622
     Region          33..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(37,41,66)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(40,65)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(47..48,59,62,66..67)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          105..283
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 matdvevvse adepgwevdp ddewglavia tvgrqlrlrr eargmrvpdf akavgygedl
       61 iykieagkri prpefldkad qvlradklia amkedvekvr ypkqvrdlat learavells
      121 ygnhnlhgll qteeyawall rtrrpvpped qleqavaarm arkaiydrsp apelsfvlee
      181 ttlrrpvggk mvwrqqlehl lqvaqlrhve iqvmpmdrwe hpgtagrvqv lkfgdgtaig
      241 rmddefngrp vsdlkqlril elrygiirae alttresgaf ieqllget
//
LOCUS       WP_181802583             447 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802583
VERSION     WP_181802583.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=47757
     Region          4..445
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mslkitvigt gylgathaaa maelgfevlg ldvvpekiam lergetpmye pgldellrrh
       61 vagfegstgr lrfttdwaev gafgdvhfvc vntpqkhgey acdmsyvdsa iaslaphltg
      121 palvvgkstv pvgsaerlaa yltanapagd daelawnpef lregfavqdt lhpdrlvvgv
      181 rseraekllr evyatpvseg tpfvvtdfpt aelvktsans flatkisfin amaevceaag
      241 gdvaklaeai gyddrigkkf lragigfggg clpkdirafm aragelgadq altflreids
      301 inmrrrgqmv emardalggg sflgkrvavl gatfkpdsdd vrdspalnva gqihlqggqv
      361 tvydpkgman arrlfptlgy agsaeecvrg advvlhltew refreldpaa lgevaaakvi
      421 ldgrnalepe vwrragwtyr amgrpta
//
LOCUS       WP_181802780             412 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Mur ligase family protein [Streptomyces].
ACCESSION   WP_181802780
VERSION     WP_181802780.1
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 13558984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..412
                     /product="Mur ligase family protein"
                     /calculated_mol_wt=43530
     Region          62..>186
                     /region_name="Mur_ligase_M"
                     /note="Mur ligase middle domain; pfam08245"
                     /db_xref="CDD:462409"
     Region          304..402
                     /region_name="MurT_C"
                     /note="MurT ligase C-terminal; pfam08353"
                     /db_xref="CDD:462442"
ORIGIN      
        1 magnsdpltp raklavtagk avaaasraag rgsgsviggr valkldpdll arlaqnldvt
       61 lvsatngktt ttrliaealk aagpvvsnal ganmpagits alaggseskf gvievdekyl
      121 agvardtdpk ciallnlsrd qldraaetrm laenwregla gskavivanc ddplvvwaas
      181 sspnviwvaa gqmwkddaws cpscggvmqr pgddwfcgec gfrrptpswv lsgdhvldph
      241 gsawpihlql pgrankanaa ssaavaavfg vppqvalerm yqvqavagry dvvqfqgrdl
      301 rlllaknpag wletfslidp ppapvilsvn argadgtdts wlwdvdytrl tghpifvlgd
      361 rkldlavrle vagqhfqvce sldqavqmcp pgrieviany tafqdlrrrv gn
//
LOCUS       WP_181802884             468 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181802884
VERSION     WP_181802884.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 468)
  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..468
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..468
                     /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=49946
     Region          169..413
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mhdhsemlll avlfvvclvg villaacirg avcwlwaaal vplflfgray atvgvspvyl
       61 ldlftglalv vtvrvwgpra freprlrgfr avavllaivt vqavcrgisa dypdplkgiv
      121 lglyplfgwf aatwlltrsp eefhhwrwil fvptvgtflk vplhlvttaa apglylaiag
      181 afgmhlhrqg dsrlltwtlv gtamltavas krgpllavvv ailatavagr snrrsaarlp
      241 vlswalavmg vaavigfstt grhpadlpvv gglatrleaa tqnpdseaah niglrfamwr
      301 kafeaarenp lfgggagrpi dvvfegvqld vsrsgphnsf vgyiyylgwp agiaftllvv
      361 vtllrtwrar shpagsvwfg aimgvcvtaf tnvafettfi glpswlvlgc afalvgvppq
      421 shgiaascpr qeanhswtsg grhriaqvpg tatradergt qksalsgt
//
LOCUS       WP_181802901             216 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802901
VERSION     WP_181802901.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 216)
  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..216
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..216
                     /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=23708
     Region          10..185
                     /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 melayysdya vrlvnseepg rgkdsltsve avrdlfggnq qaarratead ltrfrsvrar
       61 lravfeaadk geetlavdll nslllefpvs pqisghdfrd edgrplwhmh ladhpsnata
      121 gytaiaamgl afhlteygvd rlglceaapc rnayldtstn rsrrycsdrc atranvaayr
      181 arkrrleaer pdrpdrsast glaaasaqrt sasger
//
LOCUS       WP_181801597             694 aa            linear   BCT 28-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Streptomyces
            shenzhenensis].
ACCESSION   WP_181801597
VERSION     WP_181801597.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=75623
     Region          5..688
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mvrptlpvev pptrrvsegg ytlhgrryed pyvwlerldd getvdwiaaq eavtravlds
       61 vpgrdglraa varstryarl sppipagrng rtfhwqagad deksalmmrr stgapaetvi
      121 dpgawpagdv lvfaepspdg tlvalgrasg gthgavihvl dvetgqllpe rlrgtdhgsv
      181 awrpdsssff ytaypepgev ppdeqaywha vyehrigsdt parkvfgddr dkdhwctvda
      241 secgryavit vwdfvhandv tllrltddel ipaatgmrsv nqvqviddsv lvwtdldapr
      301 grlctaplte ptawrtlire gpdimqtvtg iggrlyavys haashrvavh aadgthlrdl
      361 alpslgsvnr negvgvvsgv tgswhgddvw vaftsfvqpp svykydyaqd rlepyhvpda
      421 gldpaayttq qiwyesaddt pvsmfliyrt dlprdgrrpv rlsgyggfni pveprfsavs
      481 aawlqlggvl ahanirggge ygrtwheaav gmrrqnafdd yiaaarhlva tgwttperia
      541 srgnsnggll vavtalqape afgavycrap lldmlrfptf pnlsgttvey gspddpdeca
      601 ylaayspyhn vrpdrrypvi aiatalndrt vppydplkmi aalqtdaakg gpyilvplrd
      661 sghgggttls alieqdvdel sflywalgip arpr
//
LOCUS       WP_181802902             259 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802902
VERSION     WP_181802902.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=28545
     Region          52..157
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mtdtpmttts tsgtdwgawq qswdrqqewy mpdreerfri mldmvealvg taprvldlac
       61 gtgtvtarll arfpaavstg vdldpallai aegtfagder vtlvtadlkd prwtarlpyd
      121 sydavltata lhwlhsepla alygqvaglv rdggvfmnad hmiddstpri naaeraqrhr
      181 rmdqakaaga ldwaewwrla aqdpvlagpt arrfeiygeh aegdmpspaw harvlreqgf
      241 gearpvwcsp sdtlllavk
//
LOCUS       WP_181802928             282 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802928
VERSION     WP_181802928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..282
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31361
     Region          28..84
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(30,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(37..38,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          102..269
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mnrpeladfl rrtrtrlgps dvglppgarr rtpglrreev aslagmsady ytrleqsrgp
       61 rpsrqmltal aralrltrde rdhlfhlage epprregtst hvgpglllvl drlhdtpamv
      121 ttdcgevlaq nalsralsgd vlarpprern llrryfldps ardlfppedr partrehvan
      181 lravaaarpt dpvpaalvae llagseefar lwaehevavr rsttkrflhp avglleldce
      241 vlvstdtrqh lvvhtarpgt dsherlrllq vvglqdmtps rs
//
LOCUS       WP_181802948             185 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181802948
VERSION     WP_181802948.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 185)
  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..185
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..185
                     /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=19367
     Region          15..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maehrsmqra alldaarall seggtealtf palaertgla rssvyeyfrs raavveelce
       61 adfpvwaaev aaameragsa egkveayvrr qlalvgdrrh ravvaisase ldagarekir
      121 aahgglvami vaalgelghe qprlaamlvq givdaavrri elgaaedpav itdaavamal
      181 rgvrg
//
LOCUS       WP_181803014             612 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces shenzhenensis].
ACCESSION   WP_181803014
VERSION     WP_181803014.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=64976
     Region          48..612
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 msvrgdlrra rrrtdladrs kvevvkdeag vvrearrapl aaplttgsla dlpytnaage
       61 phatairrgg gtvtaaafaa qvtsvakgfi aagvaagdrv avmsrtryew tvldfavwaa
      121 ggvpvpvypt ssadqvdwiv rdsgarhvvt etpqntatvi tgtashphrp rtweldggal
      181 adltllgegi pdeevtrrra altpgtvatv cytsgttgrp kgcvlthanl haeaantvel
      241 lhpvfqavtg qtastllflp lahilgrtlq laclmgriem ghfpsvkpde lrpalrefrp
      301 tfvvgvpylf ekihdtgrat aekigraasf draerigvrf aaahlakflg tgkgpgpgly
      361 avsggspldr dlnlffhaag ivvyegyglt etsaaativp pleprpgtvg qpipgtavri
      421 addgevlvkg pvvfgsywnn paataevlsd dgwfetgdlg eldadgylti tgrkkdilit
      481 sggknvspav ledrlrsrsp vgqclvvgdn rpfvaaivtl dpeavahwls vrklppdtpl
      541 aelvrddrmr aevqkavdha nlavsraesi rafalvegef neenglltps lkvkrhavsa
      601 ryaaeiealy rg
//
LOCUS       WP_181803079             328 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces shenzhenensis].
ACCESSION   WP_181803079
VERSION     WP_181803079.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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 328)
  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 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   5  (residues 1 to 328)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..328
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..328
                     /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=35977
     Region          <259..316
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mlrihftpad lqgirvarrp dplwelvcaa crlvtnqgpl efgawrrgvl ertvrdlear
       61 ralrlvgtlv ppvgyipdfl tptvsdeglp aaleqvratp rrrlhkelgi lattrplpaw
      121 tttlgkpgdr nmgylvkale vsfkallepr wghvrkavhd evdlrarsll dggvralles
      181 lrpfarwnsp vlevdypver dlylegrgll llpsyfcwrr ptaladpalg pvlvhpvtar
      241 pfdaaalssg glerllgrtr asvlaqvarg rarttsevae vvgialpsas yqlavlrdgg
      301 lvashregqf vrhsvtamgh rlleadag
//
LOCUS       WP_181803240             512 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding and vWA domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181803240
VERSION     WP_181803240.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 512)
  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 512)
  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 20696117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..512
                     /product="substrate-binding and vWA domain-containing
                     protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=54755
     Region          38..285
                     /region_name="SBP_bac_11"
                     /note="Bacterial extracellular solute-binding protein;
                     pfam13531"
                     /db_xref="CDD:463911"
     Region          249..509
                     /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 mtrhpllall aaaavvltgc takdhdddsa apkpgtlrvl asselsdmta vldrvrkdtg
       61 vtvrptymgt ldavdllarg kadgrydalw lssddylrlr pqaakkvvse tsimtspvai
      121 gvrtatakal gwkpdavtws rieqavvagr lsygmtdpar snsgfatlis vasalsgaqs
      181 altdadvaka tpqlkeffkg qkltsgssgw lasayqrrgd vdallnyesv lkgipgltvi
      241 rpsdgvvtad ypfsslagts aatredvrev tedlrgtavq klitdttrrr pvvasvppaa
      301 gldttrrrel pfpgsrsvad glisayenel rrpsrtvyvl dtsgsmdgdr lnrlkkaltd
      361 ltgdfrdree vtlmpfgsav ksvrthvvep adpkaglaai rkdtealtad gdtaiytsle
      421 kaydqlggga dtftsivlmt dgenttgdka gdfdhfyrel stdrqripvf pilfgdssra
      481 elqhiatltg grlfdarqgs ldgafeeirg yq
//
LOCUS       WP_181803107             136 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_181803107
VERSION     WP_181803107.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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   Wintjens,R. and Rooman,M.
  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 136)
  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..136
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..136
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14429
     Region          7..63
                     /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 ehldrkgwsy gdvarrggip rstvhhlatt drvvrmpqas tleglakgle
       61 ipleavrraa aeacgihvyd tapaadpngt agtgpadpev alliasvqkl saddrrhvta
      121 lveslldrsp rpaeek
//
LOCUS       WP_181803282             833 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein [Streptomyces shenzhenensis].
ACCESSION   WP_181803282
VERSION     WP_181803282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 833)
  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 833)
  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..833
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..833
                     /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=88616
     Region          256..>413
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mpfdgagfpa fadeaargdv ehlrgelpvv stslsdwvld crvwpdlglg gerpwagasg
       61 aaifcrdrlv gvavednrlm ggrrlqaapi healslpgfa dlvirhghpg ttvslekita
      121 vdagdgpipd lapvalvvaa lilfaygigp gvgpagalla llmmgmagaa mwrnrarrss
      181 ptavssngdd agwlrdlrqa etdriaedlr arsidvaaia vpwrilsaas gsgdgdppep
      241 edvhglfavw ssratprlvl sgsagsgksi alsllakril dedasdgpvp vviplsgwtp
      301 ssgfydwvaa qladrypeiv gedghltsss llralrgngq ivpfldgfde maperrrqlv
      361 talnqaagas gsfalasrtv elaeaehstg gfrdavslel lplsldhfrt fltdsgevar
      421 weplltlvkd geapvpacvf ktplmqwlgl qvvgrtgrdp asfadrsafp drsalerhll
      481 aslvravydp pdgqpgrtrw aaenagrwlr flaaqshqdd dairwwqlhr rhqflliavy
      541 galfaflaga aadlsrelgt alvagglwga acgggftvgy gfqrraerer rqvhrsgfrp
      601 daglgitwlr farvlpvlll aaaavqlmgg llrpvgdngs lwmvlgqgml vatglglvgg
      661 saaglilmrg allaanvtpa ysaspsqllt rdrwsteava vccfaavgls avaawwfgar
      721 slvpwgfalt aagagavlgp mmftswpvfr vthaacvvag ilpvsymafl draraggilr
      781 idgmvhrfrh ellrqsllnd vdtpeqlrrd rlglnrfevd erregtgrgn dpv
//
LOCUS       WP_181803316             411 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181803316
VERSION     WP_181803316.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=43764
     Region          21..407
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mstapyvsgt prpdkhdpst lafatqsvhv gntidkgtga vrtplvmans yllpedpstm
       61 dwsspeglvy trnsganqvn lqtklaaieg gedavafatg vaalhsvfft hlksgdhvvv
      121 snvtydavyr lfaelfpqky gieatfvdis dldavrdavr pntklvhaet ianptttvad
      181 iaglaeiaha agallsvdst wtpppfyrpl rdgadlvvhs ltkyinghgd amggvvvgar
      241 dlvdpirhea mvevggvisp fnawmimrgs vtlplrlsqh lasaekvaay lasdpriayv
      301 yypgleshpq hetarrqfag agfgammafa vdgdsdtqnr fvnnlqvits avslghdesl
      361 ivhvggsgrg gmenypepfr kyghlrlsig ledaddlvad iraaldatfp s
//
LOCUS       WP_181803451             494 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181803451
VERSION     WP_181803451.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 494)
  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 494)
  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 494)
  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 494)
  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..494
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..494
                     /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=52564
     Region          <78..494
                     /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 mnkplrriai fcgllvltll lrdnwlqyvk adtlredpan rrvtiaryst prgdiivdgn
       61 pitgstasgs sglndlkykr tykngpmwsp vtgyasqafg anqlesledg iltgnddrlf
      121 frntldmitg kqkqggnvvt tlsaaaqkaa ynglkaqggk gavvalepst gkilalasyp
      181 sydpsafagt sntdaeawkk lqkkynpndp mlnralrety ppgstfkvvt aaaalengly
      241 ksadentdsp lpyvmpgttt elknegsipc knatmrvalk fscntvfgki gadlgndkml
      301 aeakkfgfds eqftpvrssa svfsdnmnqs qtalssigqf ntaatplqma mvasavandg
      361 klmkpymidk lqssnldtis qtdpeemsqp lssanaqilq smmetvvqdg tgknaqingi
      421 tvggktgtaq hgvensanpy awfisyaklp dgskpvavav vieddqanrd disggglaap
      481 iaksvmeavi nskk
//
LOCUS       WP_181803382             105 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181803382
VERSION     WP_181803382.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 105)
  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 105)
  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 105)
  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 105)
  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..105
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..105
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11334
     Region          1..104
                     /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 maevtdadfa aevigaelpv lveftadwcp pcrqmgpvla alaaeegerl kvvqldvdtn
       61 pettnaykvl smptfmvfrg gepvrsmvga rpkrrlleel sdvls
//
LOCUS       WP_181803462             182 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Streptomyces].
ACCESSION   WP_181803462
VERSION     WP_181803462.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 182)
  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..182
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..182
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19234
     Region          12..>61
                     /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 mdaaqqeata rarelqrnwy geplgalfrk liddlglnqa rlaavlglsa pmlsqlmsgq
       61 rakignpavv qrvqllqdla qqvadgsvsa aeatermdei kksqggsvls nttqttsgsg
      121 aptvkrvvre iqsllrsvaa agdiidaadt lapthpelae flrvygagrt sdavthyqsh
      181 qs
//
LOCUS       WP_181802986             178 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces shenzhenensis].
ACCESSION   WP_181802986
VERSION     WP_181802986.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=19101
     Region          8..148
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mghtrwldde ekrawtaftt ahallyrrle qqlkrafgls glqyeilarl sgvpdremrm
       61 aelacalvns ksgltyqigq leksglvrrr scpsderavy avltdegmal leraapdfvg
      121 lvrellfdal tpeqvralad glgeasrrma agpvgtraaa dgtacpgaaa dvatgpgr
//
LOCUS       WP_181803501             307 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181803501
VERSION     WP_181803501.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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..307
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=32020
     Region          4..288
                     /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(32,240,243)
                     /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 mtavivgeal vdvvwpagsp hltphpggsp tnvavglrrl drqvtlmtcw gddppgelvr
       61 ahlgaigvav hrlpsdsdrt tialayldqa tgaarydflp twdparipid pnatllhtgs
      121 laavvepgas rvaaacrdlr srggavtvdl nvrpavlpdr dsyrrqasrl aevadvvkas
      181 dedlawlypg lhphtaaral ldlgpslvvv tqgaegafam tarhhvtvta pqvdvvdtig
      241 agdafqatll dslmgpggir lpttpeelmt hlrrctaaga lactrrgaqp ptqeeieatl
      301 vsspgsa
//
LOCUS       WP_181803740             306 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181803740
VERSION     WP_181803740.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>306
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
     Region          1..213
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mprlsvivpc frvqgflrec ldsvleqsfh dieviavddr spdgcgaild eyaahdprvk
       61 vlhlpenvgl grarnagiph atgdfllfld sddtltpgal raitdrlaet gdpdvlvfdy
      121 artywwggtr rnalaevlgv tadvftaaeh peildllmva wnkvqrrdfv eengfrfppg
      181 yyedtpwtfp vmlsaariat ldriclnyrq rrqgnilstt srkhfdvhdq ykrvfafvda
      241 rpelagwrpy lhrkmgehcl dilakpdrlp paakgeffrr taelyrafrp agagpagpag
      301 lgdlgd
//
LOCUS       WP_181803488             336 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA desaturase [Streptomyces shenzhenensis].
ACCESSION   WP_181803488
VERSION     WP_181803488.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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..336
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..336
                     /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=37434
     Region          21..315
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mtssgsnvie dahkptgstg tsatlggeqk gsieqltlll fivvpflall aavplawgwg
       61 vswldlgllv ffyylgchgv tigfhryfth gsfkakrplr ialavagsma vegplvrwva
      121 dhrkhhkfsd aegdphspwr ygetvpalik glwwahiawm fdeeqtsqek yapdlikdpa
      181 irtisrqfvy wtmlslalpp ligglvtmsw wgaftaffwg slvrvallhh vtwsinsich
      241 avgkrpfrsr drsgnvwwla vlscgeswhn lhhadptsar hgvergqlds sariirwcer
      301 lgwaydvrwp srsridsrrn tgeggsrqga esakaa
//
LOCUS       WP_181803770             518 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP and VCBS repeat-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181803770
VERSION     WP_181803770.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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 10608369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..518
                     /product="FG-GAP and VCBS repeat-containing protein"
                     /calculated_mol_wt=51550
     Region          44..120
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          101..132
                     /region_name="FG-GAP"
                     /note="FG-GAP repeat; pfam01839"
                     /db_xref="CDD:460357"
ORIGIN      
        1 mrtrthlagk laalagllla atggvtltsp qaaaatctag tasdfngdgv qdtviadpga
       61 tvngakragl vrvvlgggkg vseisqatsg mdatpeagdg fgtsyaayda dgdgcsdlvv
      121 gapyedvvrd ganlvdagai yiihgtptgi gtgstiqgys qngfdtattt eaydwfgyal
      181 kagttasgsp ylvigvpgeg vtfggttyad agcveyvqgs tkvslsqyst gvpgdpevnd
      241 rfgyslagtn ryfavgapge aigdeefagg vtvfshtlss gmptplvgla qdsdgiggts
      301 eagdrfgfsl smtgyrpsdq tynsdvllav gipgedvgtt pdaggvavvr iqpsgaytqv
      361 aafdnsvadv egdavagdfm gqrvviantd tsvvtttsvv rlavgepgkd tstvkdagav
      421 hvfrpldtal gandkelfrg sglpgtatar dytgvalvgg svnlyvgvpy skepatskgv
      481 ayvmpwsdid gttstgttvh vpgsgglpda gstfgvig
//
LOCUS       WP_181803825             116 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181803825
VERSION     WP_181803825.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..116
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12500
     Region          12..113
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 maveqahdpe ackgvdagit rvfhvlgkrw ngpilsvlmd rpthfaslrr aipgiserml
       61 sdrlaelgaa glvvrevdeg pplrvsyrlt aagaalepsl kalrdwareh lpdspc
//
LOCUS       WP_181803852             159 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Streptomyces shenzhenensis].
ACCESSION   WP_181803852
VERSION     WP_181803852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 19109193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=17482
     Region          4..145
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18879"
                     /db_xref="CDD:467590"
ORIGIN      
        1 matpdfirti rasaghqllw lpgitaivfd ddgrvllgrr tdtrkwsvig gipepgeqpa
       61 acavrevfee tavrcvaerv vlvqalepvt fpnadvcqfm ditfrcravg gearvnddes
      121 ldvawfdvda lpelhefgvf rikqamsdap twfdatafs
//
LOCUS       WP_181803872             158 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Streptomyces shenzhenensis].
ACCESSION   WP_181803872
VERSION     WP_181803872.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..158
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=18108
     Region          42..129
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mavkdrdrfs tatrlkllge qtaarvyrsq trrqarrsrl tgraallaiv lctmvvalay
       61 pmrqyvsqra eisdlerqrq qarqrveqlr dlkarwqdda yaeqqirerl hyvmpgetgy
      121 vvidpgaakr ahaylgaadr pwyanvwdgv dksdasdr
//
LOCUS       WP_181803868             431 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces shenzhenensis].
ACCESSION   WP_181803868
VERSION     WP_181803868.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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..431
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..431
                     /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=47888
     Region          20..428
                     /region_name="cyclopro_CfaB"
                     /note="C17 cyclopropane fatty acid synthase CfaB;
                     NF040703"
                     /db_xref="CDD:468667"
ORIGIN      
        1 madaasrlrr vaeqvlgvpl pvrlrawdgs qagppgapal virnrralrh mmfkpgelgl
       61 arawvagdld iegdlygvla amsgliwerg ddgrtvfeal rdpavrsavr ellrlagppi
      121 ppappreevr rprhlhtrhs drraishhyd vgndfyelvl gpsmvyscay wgaienaetl
      181 esaqrdklel vsaklgltpg qrlldvgcgw gsmaihaare hgvsvvgvtl sqeqaayark
      241 rvadegltdr veirvqdyrd vrdgpydais sigmaehvgs eryleyarel ygllkpggrl
      301 lnhqiarrpq rdesaynvda fidayvfpdg elapvgttvt qleragfevr dvesirehya
      361 rtlrrwvvnl eaewpravrl tspgrarvwr lymaasalaf ehnrigvnqv lavrtpesga
      421 sglplrtrtw n
//
LOCUS       WP_181803850             647 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181803850
VERSION     WP_181803850.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 647)
  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..647
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..647
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=69201
     Region          90..269
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          344..640
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msrdhvqpvr rpapapaaga ldldaevlgg aetaylella rgasaeayeq pvllaraenr
       61 pperiaaler akllalrvrt elegrrrrea elsalfetah dlaglrdvda vlqaivqrar
      121 sllgtdvayl slndpargdt ymrvtegsva arfqqlrlgm geglgglval tarpyvtddy
      181 fkddrfqhtl tidagvrdeg lvailgvplm lgphvigvlf aadrrarvfe reqiallgsf
      241 aalaaaaidt anlltetrsa mtgleranei ikahstvier aseihdrlae lvlrggqvhd
      301 vaaavsevlg gtveftdtad prpletsrte ghavrhgddw iaavaaggel lgalvlrghp
      361 gldpvdqrtl eraamvtsll llarrsaaea eqrvrgelld dlldardrep rqlsdraarl
      421 hadldathvv laarldgpaa daeetaaarr rlwsaashla ttrhglaaar dggtvlllpl
      481 gagrcaghlg tavhqpvtvg asapvadlat rpdtvavaya earrcldald llgrggdgaa
      541 aedfgflgll lagerdvaaf vtrtigpvva ydtrrgtqll rtldayfacg mspartkdel
      601 hvhvntvaqr lervtrllgd dwqsparale iqlalrlhrl gaqpqrr
//
LOCUS       WP_181803965             633 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces shenzhenensis].
ACCESSION   WP_181803965
VERSION     WP_181803965.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 633)
  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 633)
  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..633
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..633
                     /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=68415
     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 mrdyalapta astltgglad sifetadrnp alpvlarrpe aaerweevta aelrdevvdl
       61 akgliasgis pgqrvavmar tryewtlfgl alwsvgaeiv pihptssrdq vewilrdagc
      121 vavvvedeqa vmtvgtvceg lprlkhvwql dadalpelvr kgvfvplttv eslrrivmpd
      181 staaitytsg tsgrplgcal shrglaypsd tllagwghta arqgeqasvl aflpfshvyg
      241 lmimviclrg gilmghepem teaalaealr tfrptylyav psvlekvykt flrtsqqhgr
      301 galferaaqt ardfaaaler qrlgtgagpg fdlrlqhavy ertvyrklrg alggrvlrat
      361 sggsslsrel tlfyegigvy vhdgygltes sggitmqplg reksgtvgqa lpgtqiqvad
      421 dgeilvrgps vfqgyvgddy atraalrggw latgdigrld segyltitgr kkdiiitssg
      481 ksvapapleq rlrmhplvhq avvvgddrpc vgalitldpd flahwrgala vpgdapgrea
      541 reenalreei araiasansv vsrsesirvy rvlqepfapg ngmltpsmkl rrdaiarhya
      601 aeidamyqar sqavrragrp epadwddsdn vfr
//
LOCUS       WP_181803932             395 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptomyces shenzhenensis].
ACCESSION   WP_181803932
VERSION     WP_181803932.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 395)
  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..395
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..395
                     /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=42161
     Region          18..382
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mrrivvvgas aaglaaaetl rregydgtlt lvgdeprapy drpplskqil aaewvperla
       61 lrtpdalaal dldlrlgvaa tglepvgrtv eladgsalpy dglviatgvr prrlpgegah
      121 vlrtlddalt lrerltpglr lvvvgagflg aeaaavawql gvhvtllepa pvplthaigt
      181 evgrllaqah lergvdlrcg vtvaevtddg vrlghgelie adevlvaigs lpntewldrs
      241 glavrdgvvc deyceaaknv yaagdvarwy nplfgtsmri ehrttaaeqg maaarnllaa
      301 pearkpfapv pyfwsdqydm kiqaygylrd hdevavvegd laerrfvaay rtgdrvtgal
      361 avgmppkair qwrqaiatga awhdtvsttv pames
//
LOCUS       WP_181804044             428 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181804044
VERSION     WP_181804044.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..428
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45421
     Region          3..425
                     /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 mlaardlplh gvrvldfsqf lagpvaalrl adlgadvtki erpevgeigr tlafagrwad
       61 gdtlsfhamn rnkrsvvadl kdaadlelvk elvsradvll qnfrpgvmar lgldygtlra
      121 inpgliyvsa tgygddgpwa arpgqdllaq svsglpwvma tgdrplpvgl avadhlmsch
      181 iaqgvtallv rkvrtgvggl vqtslleaml dlqferltar lsepgelsep gepgepsenl
      241 aecdpatrpv hgrltapagi fatrdghial ahipvdvlgr vlgdpelvgy ddpgrcragr
      301 ahleaplraa faarstqdwv gllsgadgwc apvlsleell eheafdavrm tqevlrpsrt
      361 agtapvrvvt arspiridgh rllsakaapr vgedghvrde vlsdraryas avtskqnaal
      421 vgqgaddq
//
LOCUS       WP_181804119             306 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181804119
VERSION     WP_181804119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 306)
  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..306
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..306
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34392
     Region          30..92
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(34,38,65)
                     /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..45,56,59,65..66)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          117..297
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msaesprasr lepylsrtep aptllkmlvg vqlagirega gfaqeqaara lgfspaklsr
       61 ieagkgrrpp tesdvralle lyeaddyeas vllkllqrag epgwwqrydk rlmpewfdrl
      121 vglqeaaaai rtfeiqyvpg llqtaaytra vverglptap acevqrrvel rmrrrellhr
      181 adapqlwavi desvllrvlg srevmreqle ylvemaglph vtvqivpldl tnasapaipv
      241 tylrfggldl pdivylehik sanfledrde teeyrvaldr ladealnpre slallrdtle
      301 qrypap
//
LOCUS       WP_181804277             290 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181804277
VERSION     WP_181804277.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..290
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32036
     Region          9..88
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(34,59)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(41..42,53,56,60..61)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          107..265
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mkdeesdnql gsylrarrel vspaqaglpp ggnrrvpglr reevallagi spdyylrler
       61 grdknpspqv leslarvlhl ddvertyllg laaarprapr rkrpehvpar vhqllahlqi
      121 pafvegrafd vlasnpmava lsprlrpgen rlrsllldpe eqafqqdwak atadfiaalr
      181 ttigddtgnp rfvelvgela lssqrfrtlw arhdvrnldg gtttvhhpvv gelrlhrdkl
      241 pvddvilvvy ypdkdsdsdq klqlltalsp tepagtahsg padaphpktp
//
LOCUS       WP_181804318             259 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181804318
VERSION     WP_181804318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..259
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27018
     Region          5..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 msdidllapm teaahevgdf lraapvpapa atwaefahnf ealdkpaadq lrarlsglrp
       61 gaawgeelgd alpahgevwv vdavdgavql lqdlpywsvs vtlvrdlrpv atvlhspvrg
      121 etytaarghg arlngrliqp srktelglal latsqpptva aqpdavhaag rslsallpha
      181 gavrnlgpts wqvadaaggr idafweygld dvnllggslv ateaglrvtd iegnpwqaga
      241 asfitapaal hdqllklls
//
LOCUS       WP_181804382             848 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces shenzhenensis].
ACCESSION   WP_181804382
VERSION     WP_181804382.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 848)
  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 848)
  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..848
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..848
                     /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=91492
     Region          3..839
                     /region_name="PRK10490"
                     /note="sensor protein KdpD; Provisional"
                     /db_xref="CDD:236701"
ORIGIN      
        1 margklriyl gaapgvgkty amlseahrri ergtdcvvaf vehhhrprte vmlhgleqlp
       61 rkelqyrgat ftemdvdavl rraptvalvd elahtnvpgs rntkrwqdve ellaagidvv
      121 stvniqhles lgdvvesitg vrqretvpde vvrradqiel vdmspealrr rmahgniyks
      181 dkvdaalsny frpgnltalr elallwvadr vdaylteyrs ahqvstiwgs rerivvgltg
      241 gpegrtlirr aarlaekgag gevlavyisr sdgltsaspk elavqrtlve dlggtfhqvv
      301 gddipaalld fsrgvnatqi vlgvsrrrsw qyvfgpgvga tvaresgpdl dvhlithdea
      361 gkgrglpvar garlgrarvv wgwlvgvlgp llltwlltsa vpevglandm llflsltvaa
      421 alvgglfpal asavvgslll nwfftppvht ftiadpkniv aivifvgval svasvvdlaa
      481 rrthqaarlr aeseilsfla gnilrgetsl eellervret fgmdsaalle rtdettpwtc
      541 agsvgprpae ipedadvdvp vgdhmalslr grvlpasdrr vlaafaaqaa vvldrqrlqr
      601 eadrakelae gnrirtalla avshdlrtpl agikaavssl rsddvewseq dqaelleaie
      661 egadrldhlv gnlldmsrlq tgtvtpiire tdldevvpma lggvpedsve ldipetlpmv
      721 yvdrgllera vanvvenavk ysppeekvlv sasaladrve vrvvdrgpgv pdeakdrife
      781 pfqrygdspr gvgvglglav argfaeaidg tlhaedtpgg gltmvlavpt alererseea
      841 dlptpass
//
LOCUS       WP_181804454             394 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181804454
VERSION     WP_181804454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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
REFERENCE   2  (residues 1 to 394)
  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 394)
  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 394)
  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..394
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..394
                     /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=41154
     Region          24..392
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mdtassyddp apvrgrasra qralateavh agrddlarqg lhappidlst typsydsrae
       61 aaridafaad gadpvgppvy grlgnptvar feaalarleg tesavafasg maalsavlla
      121 raatglrhvv avrplygcsd hlltagllgt evtwtdpagi tdalrpdtgl vlvespanpt
      181 laeldlrava hacgtvplla dntfatpvlq rpaelgarlv lhsatkylgg hgdvlagvva
      241 cdeefagqlr rirfatggvl hplagylllr glstlpvrvr aasataaela rrltadprva
      301 rvhyprlgga miafevpddp hevvsrvrli tpavslgsvd tliqhpasis hrvvdaddrr
      361 gagvsdgllr lsvgledvdd lwrdldtalg earp
//
LOCUS       WP_181803104             290 aa            linear   BCT 28-DEC-2024
DEFINITION  PAS domain-containing protein, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181803104
VERSION     WP_181803104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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 290)
  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 290)
  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 290)
  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 290)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>290
                     /product="PAS domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          48..278
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
ORIGIN      
        1 mgnpdglppp ddshgtprqt gsarqahlid elrqeledtn rglialhtel entrraearl
       61 aaivassdda mlsldsdlrv qtwnpgarrl lghteeqiag qavgtlmpda araefgtave
      121 qirsggraes hqcrwrradg tevdvavtvs grrdadgalv gycatardit hqlaaqaela
      181 saradrevma erdriardlh dmviqrvfga glalqstaar lhgpdaermh tvideldati
      241 relrttifdl hqpaqkaasl raqvldeaaa aqprlgfapa vefegpvdas
//
LOCUS       WP_181804471             459 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Streptomyces shenzhenensis].
ACCESSION   WP_181804471
VERSION     WP_181804471.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=49203
     Region          34..450
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtsssstata rtssearava rtqtlikgen gigtvrkttl pgglrivtet lpsvrsatfg
       61 iwahvgsrde tpalngathy lehllfkgta rrsaldissa idavggemna ftakeytcyy
      121 arvldtdlpl aidvvcdmlt gslileddvn vergaileei amteddpgdc vhdlfahtmf
      181 gdsalgrpvl gtvdtvnalg adrirrfykk hygpthlvva aagnidhnkv vrqvraafek
      241 agafknsdaq piapraghrg irtagrvell grkteqahvv lgmpglartd drrwalgvln
      301 talgggmssr lfqevrekrg laysvysyts gfadcglfgv yagcrpsqvh dvlkicrdel
      361 dqvaeyglpd deigraigql qgstvlgled tgalmnrigk selcwgeqms vddmlariaa
      421 vtpdevrsva rdilgkrpsl svigplkdkq aarlhdava
//
LOCUS       WP_181804521             611 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Streptomyces
            shenzhenensis].
ACCESSION   WP_181804521
VERSION     WP_181804521.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 611)
  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 611)
  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..611
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..611
                     /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=65931
     Region          50..586
                     /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 mpvnpmnrre fvqksavtga avavagtvgt gsaqaaeagh ghtrppkapk twsfsilgtt
       61 dlhshvfnwd yytnaapkds kgntygiari atlvknlrae kgeervllvd agdiiqgtsl
      121 ayyyanvdpi tgkdgkrgpk hpmaiamnem rydaaalgnh efnygidvir tfekqcdfpl
      181 lganaldakt mrpafrpytv khikvphgpd ikvgilgltn pgialwdkdn vsgkmaftgl
      241 veqakkyvpr lralgcdvvf ltdhsgldgs tswgdelpyv enasnlvaeq vpgidailvg
      301 hthvdvptyt vknaetgedv llsepycygy rlsvfdfele hvhgswkitk ktattlnsnt
      361 vaedlritel ltadhelvvk yvntaigtst qdmstaeacw kdvpaidfih evqteavkag
      421 lsaadaalpl isvaacfsrt adipagnvti rdiaglyiye ntlygkkltg aqlkdyleya
      481 akyyhqvpsg tavdtatltn ansfwdymyd tasgvsyeid iaaaegsrik nltyngaaip
      541 ddqvfvvavn nyranggsgy phiaaaetay sstnqvrdlm iayatakgti dpstfaatnw
      601 kltqdgtpvf p
//
LOCUS       WP_181804649             268 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Streptomyces shenzhenensis].
ACCESSION   WP_181804649
VERSION     WP_181804649.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,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 268)
  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 268)
  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 268)
  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..268
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..268
                     /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=29759
     Region          27..268
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mttlthawra arvtplgely tpprvtaall rltvqvvlva slwhglyaqs gttaglsrdq
       61 avtfavlavl asrlreldqy aardtvvqhm yygtivywyl rplsphryya lralgeqlyg
      121 fawaatgyai claagvvvpp esaavaavfa lslllgqwvl hyvmllidql cfwtlrntaa
      181 llilifaqnl msgvyaplwf fphwflvlss flpfqatlnv plslyvgrip lsdagfqlgv
      241 qaawlvalrf ltrflwrraa rrvvsqgg
//
LOCUS       WP_181804919             393 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181804919
VERSION     WP_181804919.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 393)
  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..393
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..393
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41783
     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 msvlsgyrvl dlsiamagpl aamrlgdlga dvlkiepvtg ewqrhtsagg avgqkvnasf
       61 lslnrnkrsl avdlknpagr elvlglaaea dvflqnyrpg vaarlgldye avrsvrpdiv
      121 yvsmsgyged gpyadrpgqd lllqslsgal ysagraedip qagpyfvada itaysafegv
      181 laallhrert gegqkvevnm ldamiamqmq elsvrtvggv aqtrghgiha hsyirapygi
      241 fptsdscial afadlgllae ifgdptlarw daerdgfvhr daisaavarn litdttaswl
      301 erlggrgvwv gpvnsyadvv ddpqvkhngs fvtyrhpteg vvttpgfafr ltgtparver
      361 gaptvgehtd eilaelglte aevaalkqdk vva
//
LOCUS       WP_181804934             287 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181804934
VERSION     WP_181804934.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 287)
  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 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..287
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31642
     Region          5..84
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(30,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(37..38,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          102..271
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mdrqelaafl rsrrerispa evglprgprr rtpglrreev aqlayisaey ytrleqargp
       61 rpsrevlsgl aralrlsdae rghlhhlaga ppgpppgpsr evrqslldll rrlpqaaafv
      121 tsatfevlaw ndlaaalmed fsalpprdrn lvrrafltpr tqggrlygvs dvdafarlsa
      181 qrlraaagry pdspevtglv aellagseef rrlweshdvs aeptlcktfl hpvvgpvtvn
      241 cdaldvtdrd qqvviytatp gsrseealrl lsvigtqrmd qqvdfpa
//
LOCUS       WP_181804961             194 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HD domain-containing protein [Streptomyces].
ACCESSION   WP_181804961
VERSION     WP_181804961.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 194)
  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..194
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..194
                     /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=21137
     Region          15..177
                     /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 madteqeqtk gttgfllemg mlkrakrtgw wiagvkdpet iaehsfrval igsvlammeg
       61 adpartallg lwhdtqetrv sdiphigrry leaagnekvt adqvsaahpa vragaqqive
      121 eyengdspev icahdadkle cllqaveyre qgcsnvqpwi dsslaklkta saqsladaal
      181 smtsiewqqt ylpr
//
LOCUS       WP_181805038             125 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181805038
VERSION     WP_181805038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>125
                     /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          <22..117
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mttataprdd lpprltrltf hgplsearaa amvrrlagpr pgsvldvgcg wgelmlrllt
       61 avpqargvgv dvnaadlkrg rrtarargla grvefaeesa vgtgrgpadv vlclgaipve
      121 rkvll
//
LOCUS       WP_181805054             809 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Streptomyces shenzhenensis].
ACCESSION   WP_181805054
VERSION     WP_181805054.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 809)
  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 809)
  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 809)
  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 809)
  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 18682358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..809
                     /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=88849
     Region          10..581
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          559..653
                     /region_name="Glyco_hydro2_C5"
                     /note="Glycoside hydrolase family 2 C-terminal domain 5;
                     pfam18565"
                     /db_xref="CDD:436582"
     Region          705..796
                     /region_name="F5_F8_type_C"
                     /note="F5/8 type C domain; pfam00754"
                     /db_xref="CDD:459925"
ORIGIN      
        1 mnrrelinrn wkftygdpeg atleafddgd wydvglphsf gipyfmetgf yvgrgvyrrt
       61 fdlteadagk yvalefhgvf qdaeitvngv avdrhlggyt afvvdvseav rtgtnqltvr
      121 vsnewnprla pragehvfng giyrdvslii aertriawyg tgvvtlgvga dgagvevtte
      181 lvndtdapfd gllaarvtaa gtrpleaaaa vrlpprsttt hrqpllvddv rmwhpdsphl
      241 ytleqtlrts ggaelhraat efgirtieft atdgfhlnge rfaihganvh qdhagwsdav
      301 thagmrrdva likdagmnfi rgshyphheq fatecdrlgv lywseapfwg iggansegfw
      361 nasayppdea dqaefedscl rameemirvn rnhpsivaws tgnevffsdd hvvpaakklt
      421 rrlvdlahdl dptrpaavgg aqrrgfdelg dlagyngdgg elflnppwpn ivseygsvve
      481 drpgsythrf rhgseneyaw rsgvvlwcgf hhgsivpdmg rmgfvdyfrl plrswywyrh
      541 rltgteppaw pgpgtatalr itadrttvlt dgtddvhlvv eivddtgrvv aderpvriev
      601 vegggifptg tsieltpagk glldgrgaie frsyhagpnr lrataqglap ceilveavgp
      661 epwtgqrrnl apgppareha pdtrephqla emrpvfssgs rpdrparlvt dhsvdhgwis
      721 atddpgawls vdleglwsis tihvefgagp etpyvielsd dgrqpvplav gttrpttvrl
      781 dldnpqahav rvtfpqapae vinirvhgh
//
LOCUS       WP_181805094             300 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181805094
VERSION     WP_181805094.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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 shenzhenensis"
                     /db_xref="taxon:943815"
     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=33012
     Region          8..298
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mpraldrirv gsapdswgvw fpddprqvpw erfldevaea gyswielgpy gylptdparl
       61 adeiarrdls vsagtvftgl hrgpavwept wehvsrvaal tqamgarhlv vipsfwrddk
      121 taeileppel tgeqwahltk gmerlghevk eaygldlvvh phadthidte ehvehfldst
      181 dtdlvnlcld tghyaycggd svklietyge rigylhlkqv dpavladvqa kgtpfgpava
      241 qgvmceppag vpelapvlaa aqrlgvdlfa iveqdmypce pdkplpiavr trkflrscga
//
LOCUS       WP_181805340             714 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces shenzhenensis].
ACCESSION   WP_181805340
VERSION     WP_181805340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=78144
     Region          33..707
                     /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 mtaepggped rlrryatiws ravfpvtsts mtrpefeeql lplarrlsei llahgfdade
       61 arqvgaalid ahctdpealt rsldcvdayl vlycgedgpq delrmrssri qhamaagfaq
      121 alrertlaeq eaiaeaalra qgvvaqalha searfravfe gaaigigiad legnvlqvng
      181 allrmfggse qtlrgrkvme wahpedapqt wrlyeelvrg erehyhveka fnrsdgtvlw
      241 tnltvsllrd adgepqyqla lmedtterrl lnlrlryeat hdaltglpnr tlfferleka
      301 lsagegqrfg lcyldldgfk tindslghsa gdrllvevad rlqscatapg emvarlggde
      361 fvalttgpat qrevddladr imnalvtpis idgrelmvrg sigivegpag ertpaevlrs
      421 aditmyraks aggnrfelad peadaraitr hglttalpaa ldrgeffiey qplvhlgdgs
      481 vrgaealvrw lhpqhgvlgp drfiplaeht glivplgrwv leesirqare wrerygehdg
      541 agplrinvnl spcqlshpgl vqdtvdiler tgvapdalcl evtesaliga dddllkplrr
      601 laemgvdial ddfgtgysnl anlrrlpvsi lkldrsftqs mqqfpadpvd lkivegival
      661 ahgldlavtv egvetgaqae qlrilgcdta qgwyyarpgp perlhdlalv datg
//
LOCUS       WP_181804976             212 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181804976
VERSION     WP_181804976.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Chapman,E., Best,M.D., Hanson,S.R. and Wong,C.H.
  TITLE     Sulfotransferases: structure, mechanism, biological activity,
            inhibition, and synthetic utility
  JOURNAL   Angew Chem Int Ed Engl 43 (27), 3526-3548 (2004)
   PUBMED   15293241
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16049904
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..212
                     /product="sulfotransferase family protein"
                     /EC_number="2.8.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008146 - sulfotransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23909
     Region          2..202
                     /region_name="Sulfotransfer_4"
                     /note="Sulfotransferase domain; pfam17784"
                     /db_xref="CDD:465504"
ORIGIN      
        1 mkvigagfgr tgtlsvkaal etlgfgpcyh mvtaferpdh lrawraaheg ravdwealft
       61 gfgstmdwpa ctfweqllda cpqakvvltv rdperwyesf retlvplwgt daaahdrpsp
      121 efreylalvr rigtdtfggr lddrehvvaa yaahnrrvre kapadrllvy evgqgwqplc
      181 aflgvdvpdg vafprlndrd sfqemvrrrl sm
//
LOCUS       WP_181805406             292 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181805406
VERSION     WP_181805406.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..292
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32190
     Region          27..>85
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          109..287
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mvtdngvgag gstgqaggng scepelsdsl ktfgavlkal reearltqeq faplvrysaa
       61 yiakieqgkr fpprdllers eevlgavagr vlgaaarslt rkaglaswfr qwagieeeai
      121 slyayecavi pgllqpepyi ralferrlpp lseeqfeqqv tarlerqrll terpnstfsf
      181 iieqalldrr lasdivthtl ltsllevgrl rnveiqvmpr vqedhsgfeg plylaetven
      241 rwvgyveahd csmlvtdtka asamlqrygk mrsqalshqa taglleqmrg al
//
LOCUS       WP_181805104             211 aa            linear   BCT 28-DEC-2024
DEFINITION  TetR/AcrR family transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181805104
VERSION     WP_181805104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 211)
  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..211
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..211
                     /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=23891
     Region          26..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mptkkkphvt atrkpaaaaa qarrrellet aaevfaeqgy nattvrkiad hagmlagsly
       61 yhfdskesml eeilrtflde lwdgydtvld aglgpretle alvtesfrei drhraavaiy
      121 qkeskqlvaq erfgflaesq rrfekawlat lergvaarvf radldvrlty rfvrdtvwva
      181 aswyrpggqh speeiarqyl smvldgiavr t
//
LOCUS       WP_181803954             491 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181803954
VERSION     WP_181803954.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 491)
  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 491)
  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 491)
  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 491)
  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..491
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..491
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=52712
     Region          3..470
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mpttlptkal vdgswldgga gtfpvhspqs gellaevtrc daddverava aarraqpqwa
       61 atpliervki lrrvhalfae raedvartlt leigktvaea reevieyaap awqkageevl
      121 rhrglsfpst qeqtnnkrlv mnhrplgvvg vitpynfptd issialahiv aagntavwkp
      181 sefapvscnq vaeifteagl pdgvinvvhg fgdvgaalvd hpgvdglfft gstatgeria
      241 raaalrphll elggdgpfii lpdadidaav eaavngcfyy agqvctsaer llvheavhde
      301 fvtkltaraa klrigdpase etdmgpvrne aglrriaehv qdardrgadi vqfgkeeglf
      361 fpatiltgvt pdmriaqeet fgpvapvikv ssvqeaveia nssdlglias lwtrdlataw
      421 rvgealqhgt vninetsnyw dqlapfggtg ksgvgrelsg wfldtftesk llvfelgdse
      481 lrydrraegg w
//
LOCUS       WP_181805469             468 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Streptomyces shenzhenensis].
ACCESSION   WP_181805469
VERSION     WP_181805469.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=50962
     Region          19..436
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpmghtttae tgsgglaate hrlanglrvv lsedhltpva avclwydvgs rhevkgrtgl
       61 ahlfehlmfq gsaqvkgngh felvqgaggs lngttsfert nyfetmpthq lelalwlead
      121 rmgsllaald desmenqrdv vknerrqryd nvpygtafek ltalaypegh pyhhtpigsm
      181 adldaatled araffrtyya pnnavlsvvg didpeqtlaw iekyfgsipa hdgkptprdg
      241 slpdvigeql revvveevpa ralmaayrlp edgtrasdaa dlaltvlggg essrlynrlv
      301 rrdrtavaag fgllrlagap slgwldvkts gdvevpviea aideelarfa aegptpeeme
      361 raqaqlerew ldrlgtvagr adelcrfavl fgdpqlalta vqrvlqitpe evqevtkarl
      421 rpdnravlvy eplsaesaeh teeagrgenp eqeatveagn enneetak
//
LOCUS       WP_181805485             501 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA synthetase [Streptomyces shenzhenensis].
ACCESSION   WP_181805485
VERSION     WP_181805485.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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 501)
  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..501
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..501
                     /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=53719
     Region          10..490
                     /region_name="FACL_FadD13-like"
                     /note="fatty acyl-CoA synthetase, including FadD13;
                     cd17631"
                     /db_xref="CDD:341286"
     Site            order(158,161..166,168..169)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341286"
     Site            order(161,276..277,297..302,381,393,396,407,487)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341286"
     Site            order(161,201..202,249,251..252,255,276..277,297..302,381,
                     393,396,404..407,468)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341286"
     Site            order(201,251..252,255,276,404..406,462,468)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341286"
ORIGIN      
        1 mrneglgswp arrarktphr talvsgghsa dyrtlytrtt rlahalrarg irrgdrvgyl
       61 gpnhpaylet lfaagtlgav fvplntrlag peiayqlads gakallysps haglvaglpg
      121 tsdvrtyvev gaeyeellaa aaedpidepv vpddtciimy tsgttgrpkg amlthgnltw
      181 nalnvlvdtd liaderalvs aplfhtagln mlalpvllkg gtcvlveafd pattldlieq
      241 hritfmfgvp tmfeqvarhp rwpdadlssl riltcggspv ptpliaryqe rgltflqgyg
      301 mteaspgtlf ldaehavgka gsagvphffs dvrvvrpdlt rvdvgetgev vvrgphvmpg
      361 ywglpeetaa sfadgwfrsg daarvdedgy vfivdrlkdm iisggeniyp aeiedlllah
      421 pgiaecavig vpddtwgevp ravvvprega vldadevlas lagrlarykl pksvvladel
      481 prtasgkllk sqvrkrygtd s
//
LOCUS       WP_181805519             204 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces shenzhenensis].
ACCESSION   WP_181805519
VERSION     WP_181805519.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..204
                     /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=22287
     Region          35..202
                     /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 mgsatselps hrtplndtae tglkivvvgg fgvgkttlvr svseirplnt eevmtqasvg
       61 vdengavatk ttttvafdfg rislndsmvl ylfgapgqer fwflwdrlfs gtlgavvlvd
      121 trrmddswya idrlehhrtp fvvavnrfdd gvrhsldeir qalalpahvp midcdarsrq
      181 sgkdvlitlv nhlhdlaiaq eatl
//
LOCUS       WP_181805570             402 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces shenzhenensis].
ACCESSION   WP_181805570
VERSION     WP_181805570.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 402)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 402)
  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..402
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=41695
     Region          123..398
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mhtaydvava gvvacsasyy svgydqvigw amaltllfrr rwpmavlgav salallqyvl
       61 avvpdvaqag aptgydiavl vamvsvvtha ramwqvytag avvvagvvlg fggvgslftp
      121 gaasmdlvpf vaflgicvav wltavvlrtr rlyavgleek aaveererrh laqlaaaeer
      181 aeiarelhdv vahslavmil qadavgyvlk tdpdkagtal qtiaatgrda ledmhrivrv
      241 lragrapgdg eeegaelgdg rrraslsgle tlverartag llvtltvhgd rdrlptadql
      301 tvfrvvqecl tnalrhagpg aavavtlsce edvvhievsd dgggrlgapa pagaegvagg
      361 gnglvgmrer vevsggrfta gprlgagwrv eadlpakaga at
//
LOCUS       WP_181805711             126 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181805711
VERSION     WP_181805711.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14456
     Region          29..118
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mvtkqikgrs eeadlrrads lareifsdva nkwafliiet lgertlrfse lrneiegish
       61 kmltqnlrml ernglversv hptvpprvey tltepgqglr atvdgmcdwt hrylghieaa
      121 rhrfdv
//
LOCUS       WP_181805787             597 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces shenzhenensis].
ACCESSION   WP_181805787
VERSION     WP_181805787.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 597)
  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 597)
  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 597)
  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..597
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..597
                     /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=64730
     Region          27..383
                     /region_name="FAD_binding_3"
                     /note="FAD binding domain; pfam01494"
                     /db_xref="CDD:396193"
ORIGIN      
        1 mpmfndgise telptdavvt tdvvvvgsgp agasaallls tlgvgtimit kyrwtantpr
       61 ahitnqrtme vfrdlgveeq vladatehgl vgdtvfctsi sgdeigriht wgtrpdregd
      121 yrlaspcltv dipqtylepi lvrnaaqrga qtrfsteyls hvqdadgvtv rvldrltgqe
      181 ygirakylig adgarskvaa diglpfegam diagsmnitf kaditryvah rpsvlywviq
      241 pgsnvggiga glvrmvrpwn ewlivwgydi aeeppvvder tarqivrnli gipdleveit
      301 gtslwgnnem yatrlqsgrv fcagdavhrh ppsnglgsnt svqdsynlaw kiaavlngha
      361 gpglletyta erapvaeriv krankssref vdifaalgvl dagteaemaa aieerkantp
      421 agaakraalv ramelknyef nahgvelgqh ytsaavlsdg aeppaparda dlyyemstvp
      481 gahlphawvg dnvhrralmd lapydrwtll tgiageawqd aaekvghelg vplgtvvigp
      541 grevtdlyyd waklrkises gvllvrpdkh iawraaelpe hpadelrral lsllgrn
//
LOCUS       WP_181805828             164 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181805828
VERSION     WP_181805828.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 164)
  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 164)
  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..164
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..164
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18026
     Region          7..109
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mttprtdpye vpgrpcsiaa alqvvgdrws llaireimfg nhrfrqiakn tgaptdrlsa
       61 rlkslvadgi lerrplsdep rhdgyyltea grdllgvire llrwgdrwlt tsppmklrhh
      121 dhdftpraic ahcgepvaqg evqaevtaeg wslkgpvags pgqa
//
LOCUS       WP_181805967             201 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces shenzhenensis].
ACCESSION   WP_181805967
VERSION     WP_181805967.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 201)
  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..201
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..201
                     /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=22045
     Region          15..198
                     /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 mifgrsergk ppvepvtlki lvaggfgvgk ttlvgavsei rplrteellt eagrpvddts
       61 gvegkhtttv amdfgritlr enlvlylfgt pgqerfwfmw delaegalga vvladtrrle
      121 dcfaavdyfe rrsipflvgv ncfenaaryp veavrkaldl dpdvpvvlcd ardresvkev
      181 ligvvqyamr yaaghrqavt t
//
LOCUS       WP_181805996             172 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SixA phosphatase family protein [Streptomyces].
ACCESSION   WP_181805996
VERSION     WP_181805996.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..172
                     /product="SixA phosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18836
     Region          9..170
                     /region_name="SixA"
                     /note="Phosphohistidine phosphatase SixA [Signal
                     transduction mechanisms]; COG2062"
                     /db_xref="CDD:441665"
ORIGIN      
        1 msvaeprriv lfrhakadwp qvtdherpla drgrmdaava grkladsgit fdlalcstsv
       61 rtretwklav helahrpktv yeervyeasp geliavlnev pddvqnvili ghnpgvhgla
      121 eilaataetd arermnrrgf paaafavvty egswkalepg vatladywap se
//
LOCUS       WP_181805374             709 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181805374
VERSION     WP_181805374.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 709)
  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 709)
  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 709)
  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 709)
  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 709)
  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..709
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..709
                     /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=76659
     Region          47..708
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 msaeatnpvt pgpvapaaav rrkarpridl rrlgraallg naargrlpda ighvveahra
       61 hypdadlepl rrayvlaess hrgqmrksge pyithplavt lilaelgaet ttltasllhd
      121 tvedtdvtld qvreqfgeev rylvdgvtkl ekvdygaaae petfrkmlva tgsdvrvmsi
      181 kladrlhnmr tlgvmrpekq ariakvtrdv liplaerlgv qalkteledl vfailhpeey
      241 ehtreliaen aaragdplae iadevrgvlr eadipaevli rprhfvsvhr vsrkrgelrg
      301 adfgrilvlv nedadcyavl gelhtcmtpv vsefkdfiav pkfnlyqslh tavaradgqv
      361 aevlirthqm hktaeagvva lgnpyapaad apaadasdsp vdgeradptr pgwlsrlldw
      421 qkaapdtdtf wstlredlaq dreitvfrpd ggtlglpega tcvdaayaqy gedahaciga
      481 rvngrlatls tvlvdgdtvq llmgqdpase psrewlehah tpaariaiqr wlathpdste
      541 eppapapsrp vpdpaapsaa prtanalvvd rpgatvrlag cctpvppdev tgfavrggvv
      601 tvhrvecasv lhmkstgrpe vtvswgdsta crvtlvaesf grphlladlt eamaqegaei
      661 vsatveppsq qrvrhtytve lpdaahlpal mramrnvpgv ydvgraqhq
//
LOCUS       WP_181806464             107 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [Streptomyces].
ACCESSION   WP_181806464
VERSION     WP_181806464.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=10904
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawllvivag iletgfavcl klshgftrlw ptiafasfal gsfglltlsl rkldvgpaya
       61 vwtgigaagt aiygmvflgd lvsalkivsi slviagvigl qlsgsah
//
LOCUS       WP_181806516             166 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181806516
VERSION     WP_181806516.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=17941
     Region          2..164
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mrllltsdth lplrakrlpd qllaelprad avlhagdwvd eatldllesr srrligvygn
       61 ndgpglrarl pevayaelgg lrfgvihetg aapgrearca arfpdldvlv fghshipwdt
      121 tapgglrlln pgsptdrrrq phctyltata aggaltevtl hrlppr
//
LOCUS       WP_181806559             116 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Streptomyces].
ACCESSION   WP_181806559
VERSION     WP_181806559.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=12578
     Region          10..84
                     /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..27,30,60,79..80,82..84,
                     86..88)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238042"
     Site            order(14..15,19..21,34..36,45..48,50..51,54..55,57..58,
                     64..66,71..73)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
     Site            order(34,37,79)
                     /site_type="other"
                     /note="putative Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mstplyqlka effktlghpa rirvlellse rehavaemlp evgiepahls qqlavlrran
       61 lvvtrkegst vyyslvspqi aellrvarti lsgvlagqae lladlraaqt pakpps
//
LOCUS       WP_181806750             598 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces shenzhenensis].
ACCESSION   WP_181806750
VERSION     WP_181806750.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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 shenzhenensis"
                     /db_xref="taxon:943815"
     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=64207
     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 dvavmarkag gvwqdvtata flaevhaaak
       61 gliasgvqpg drvglmsrtr yewtlldfai wsagavtvpv yetsspeqvq wilsdsgata
      121 civeldnhsa avesvretlp alkhvwqiea galeelgrlg qgvtdatvde rssqakaddp
      181 ativytsgtt grpkgcvlth raffaecgni verlrplfrt gecsvllflp lahvfgrlvq
      241 iapmmapikl gcvpdiknlt delaafrptl ilgvprvfek vynsarakaq adgkgrifdk
      301 aadtaiaysk aldtpsgpal glrikhktfd klvysklrav lggrgeyais ggaplgerlg
      361 hffrgigftv legygltesc aatafnpwdr qkigtvgqpl pgsviriadd gevllhgehl
      421 fkeywnnpaa taealadgwf htgdigtlde dgylritgrk keiivtaggk nvapaviedr
      481 irahalvaec mvvgdgrpfv galvtldeef lhrwaaehgk pagataaslr ddpdliaavq
      541 davddgnaav skaesvrkfr ilssqfsees ghltpslklk rnvvakdfad eieaiyqk
//
LOCUS       WP_181806834             305 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces shenzhenensis].
ACCESSION   WP_181806834
VERSION     WP_181806834.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 305)
  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..305
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..305
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32524
     Region          18..304
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtaaaagpaa ptsaivtaal tlkpappghf dlsftattqp cpwpkayggd lvaqaaaaam
       61 rsvtdgktlh smhsyflrpa digaevryev evlrdgrgys trqvrgyqng kvlyvclanf
      121 aagepgaafh aefaadvpgp etlpgaaryl tdrtggtmta eskaywsggr gfdmrhvpgp
      181 vyltvdgdrv phqavwlrpf dplrpveglt daqrdlaala yvcdytilep vlrvlglawa
      241 dpglvtasld hamwfhrpap vgdwllyaqe avaadagrgl gsgrfftrdh rhlatvvqeg
      301 mirpa
//
LOCUS       WP_181806887             344 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181806887
VERSION     WP_181806887.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  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 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   3  (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   4  (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 18524816
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=36692
     Region          21..256
                     /region_name="YrhO"
                     /note="Sugar-specific transcriptional regulator TrmB
                     [Transcription]; COG1378"
                     /db_xref="CDD:440988"
     Region          <282..339
                     /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 mdvfssealw agtglgapar qaleylvghp dadedavaag igvpataara alrsleaell
       61 avrvgerptr wsaspprssl gallgrkrqe laraelyaeq lheiyrtapg rqiatdlfev
      121 vesgeqvgar yahllrssrh evlhfakppy vtsrtapada statgatvrp gvrlrsvyds
      181 dgisddgcle aalrsttaeg elrllpglpm klvifdgvaa implrgddpa agslvvhsst
      241 lldvltalfe svweravpls lesgpaapta saerqdgvvh srtrdilrlm sagmkddaia
      301 ralrlsrrtv qthisdlgrq lgartrfqia llahergwlg apek
//
LOCUS       WP_181805830             308 aa            linear   BCT 28-DEC-2024
DEFINITION  LysR family transcriptional regulator [Streptomyces shenzhenensis].
ACCESSION   WP_181805830
VERSION     WP_181805830.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..308
                     /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=32608
     Region          2..>182
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          95..299
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,123,125..131,232..237,
                     243..244,246..247)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mldvrrlril qhlatygtva ataevlhlta pavsqqlsvl ereaglpvve ksgrsvrltp
       61 agellvahae viladlaaae sdllalkggh hglirvaafa saartllpev yrliaehgde
      121 qartltvqlv eqepdpamea lkkrqvdvvl ahsysvlprd fpgnsqqevl madpvllclp
      181 tgraqrlela pgqpvdltrl ageawlapgp etscyqmiqr tcgvagfvpd vrvrssdfsv
      241 llslvaagag valaprlaig eqpgisvdpl ltpvtrtvft virtgtarrp dvhllsallk
      301 qaaaasmt
//
LOCUS       WP_181806902             617 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces shenzhenensis].
ACCESSION   WP_181806902
VERSION     WP_181806902.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=66787
     Region          11..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 msgtsegptp aadldrsavt esdniyrksy qktddetepk tyayafaaat lamavvdreg
       61 lvttaneafa tligadragl pgriaadlmd lasdartwha yrevlrgrqa klrctrrlkh
      121 pdghsvwvqv nvaplakdap gvlisasdis arrelqarlr hlqmhdpvtr lpnrtlffer
      181 lsaaleaesy ersgtgrigl cyldldgfka vndtlghrvg drllaavaer ltrvadeagf
      241 aragaplvar lggdefallv edstgteqla dlaesvlaal qapfdlagqr lslsasigvv
      301 erhaagttat glmqaadttl ywakadgrsr wtlfdperna hlvtrqalss tlrpaierge
      361 fvleyqplvg medgrlsgve alvrwhhpqf gtlapnrfig laeedgsivp lgrwalttac
      421 rqarrwqldh pgeppifvsv nvavrqvwds dlvadvaetl aetglaphll qleltesavm
      481 gsagrplqal qalsdmgvri aiddfgtgys nlaylsrlpv svlkldgsfv rgfqyddpgd
      541 rpnpadevvv eamiqlahrl gltvtaecve tsaqasrlrh igcdtgqgwl ysrpvtadri
      601 selldtraya dtpvgkp
//
LOCUS       WP_181806714             298 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181806714
VERSION     WP_181806714.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  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..298
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..298
                     /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=32446
     Region          8..290
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 msddpalida hhhvwdlarr aqpwldvpah tpinrsfrpg dlrsaatvpi agrslaatvv
       61 vqcvasvdet rellaladgd pllaavvgwa dltspalgdv ldelregagg grlralrhlv
      121 qdetdpdwlq rpaverglrt lqarglgydi lirshqfpea irlarrfpdl pvvldhagkp
      181 pladgelsdw ernvrvlagf pqvrckvsgl vteadhekws aaglrpvwev ladafgadrl
      241 mfgsdwpvcv laggwnrwas amdefltgas psetdavlrr tatrfyglsd tepregtt
//
LOCUS       WP_181806916             251 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Streptomyces
            shenzhenensis].
ACCESSION   WP_181806916
VERSION     WP_181806916.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..251
                     /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=27995
     Region          3..174
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mstatplapy dalsavydrw terndyarwa ahladrfrsh grvdrvldvc cgtgsitall
       61 qrqglevvgv dgspgmlera rartaagtel lqvrlpepvp apaasfdaav ccfdsvnyfp
      121 pdqlpdlfag varllrpggl fvfdvntrhk lehvfgdshy gddlddfayv wrnryhpser
      181 rcdfaislft qapggfarqt erhsqwwfha deirsaaraa gfehatvtdd yqdrapgpdt
      241 lretwalvrg r
//
LOCUS       WP_181806950             576 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181806950
VERSION     WP_181806950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 576)
  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..576
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..576
                     /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=61898
     Region          1..570
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mldhvikgas vvdgtgapah tadvgirdgr iavigavtee srtsedaagl vlapgfvdph
       61 thydaqlfwd pyatpslnhg vttvaagncg ftlaplnper padadytrrm mskvegmslv
      121 aleegapwsw nsfgeyldal egriavnagf mvghcalrry vmgadavggq psaeqldqiv
      181 rllheamdag awgfsttqss thsdgdgqpv asrhalpael lalsravgeh egtqieaiva
      241 gcldqfsdae ielfaemsav agrplnwnvl tvdaavperv prqlqasera rkaggrvval
      301 tmpiltpmnm slgtfcalnl ipgwgpvlgl pvperieklr dpevraellr raqskeagvf
      361 rrlanfgryv igdtyseana rlsgrvvrdi aqergqdpfh tlveicaadd lrtvlwpmpt
      421 dndpaswalr aetwrhedvm lggsdagahl drmcgapytt rfigdclrgr kllgleqavk
      481 mltddparlf glrergriae gfhadlvlfd periaagpat lvhdlpgdsp rldskaigvr
      541 avwvngveai rddvvsgavp gkvlrsgrdt rtvstr
//
LOCUS       WP_181807121             485 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181807121
VERSION     WP_181807121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=50380
     Region          7..484
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mtttfetgpg qlfiggqwre aadgartevt dpatgqvitt vaeagaadvd aavraaretf
       61 dagewpglsg rergrvlhrv aelirenaed iaalesldvg kpitlagavd vtnaandyeh
      121 faalahsldg avrdiplnal aytrreplgv vaaitpfnfp lilagskigp alaagntvvh
      181 kpadetplsa lymaglfqka gvpdgvvnvv tgagpvagea llrhpgvdkv aftgstaigr
      241 hvastagqal kpvtmelggn aahlvfqdad ldkavgavik afvfntgqfc mggprllvdr
      301 pvyatllril aeavpavpvg dprdpatavg pmagekhlrk veeyvelark eggrvvcgge
      361 rldlngghyy kptviadlpg dsrviqdeif gpvltvqpfd sedeavalan stpyglasgi
      421 qtgslarahr vaarlqagiv wvndwamldp avpfggvkas gfgreygpes ltayskvksv
      481 vvsld
//
LOCUS       WP_181807116             137 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces shenzhenensis].
ACCESSION   WP_181807116
VERSION     WP_181807116.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=16259
     Region          1..129
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mrhlyrcplr wsdmdayghv nnavfiryle earidflfrp dkdfkqgsvv arheidykrq
       61 lvhrhhpvdi elwiteiraa sftityevkd ddlvyvrast vvvpfdfeag rprritaeer
      121 dfleeyrddd keeavaa
//
LOCUS       WP_181807229             461 aa            linear   BCT 28-DEC-2024
DEFINITION  class II fumarate hydratase [Streptomyces shenzhenensis].
ACCESSION   WP_181807229
VERSION     WP_181807229.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 461)
  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..461
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..461
                     /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=49204
     Region          1..460
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 msdyriehds mgevrvpaha kwraqtqrav enfpvsgqri erahiealar ikgaaakvna
       61 elgvvdkdia qaiqeaaeev argdwdehfp vdvfqtgsgt ssnmntnevv atlaterlgr
      121 dvhpndhvna sqssndvfps sihiaataav trdlipaleh lagsltrkae efadvvksgr
      181 thlmdatpvt lgqefggyaa qvrygverlr aalprlaelp lggtavgtgi ntppgfsaav
      241 ieevarvtgl pfteardhfe aqgardgive tsgqlrtiav gltkiandlr wmasgprtgl
      301 aeialpdlqp gssimpgkvn pvipeavlmv aaqvigndqt iavagaagnf elnvmlpvig
      361 knvlesvrll anvsrlladr tvdgitahre rareyaessp svvtplnkyi gyeeaakvak
      421 kalaerktir qvvleggyve rgdltvgqld ealdvlrmtr p
//
LOCUS       WP_181807275             288 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Streptomyces].
ACCESSION   WP_181807275
VERSION     WP_181807275.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..288
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32554
     Region          4..288
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mtnpaerlvd lldleqievn ifrgrspqes lqrvfggqva gqalvaasrt tegdrpvhsl
       61 hayflrpgrp gvpivyqver vrdgrsfttr rvtavqqgrt ifnltasfhk pqpapfehql
      121 pqprevahpe slptlaeeir khlgelpeql ermarrqpfd iryvdrlrwh peeiagaepr
      181 savwmravgp lgddplvhtc altyasdmtl ldavrvpvep lwgprnfdia sldhamwfhr
      241 pfradewfly eqespiatgg lglargrvyd ldgrllvsvv qeglfral
//
LOCUS       WP_181807146             200 aa            linear   BCT 28-DEC-2024
DEFINITION  M48 family metallopeptidase [Streptomyces shenzhenensis].
ACCESSION   WP_181807146
VERSION     WP_181807146.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 200)
  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 200)
  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..200
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..200
                     /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=22542
     Region          <18..193
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mqrvqagliv rpggtrhrra ehppahpvre frdgepftyl grayrllidg egqapvrlha
       61 grivigeglt rdpvrarral vswyrqagqr waqgrlqpwa armevrepev vvrdvgnrwg
      121 tyrpgdggrg tmalhwalfq lpahlvdyvi ahelahirip ghgadywvll rqaipeceer
      181 kselddlgrr lwlggidgga
//
LOCUS       WP_181807297             251 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein, partial
            [Streptomyces shenzhenensis].
ACCESSION   WP_181807297
VERSION     WP_181807297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 251)
  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..251
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>251
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
     Region          26..>241
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mpiapsrard evphptvpaa spsrwaplrp lvlrlhfyag vlvapfllva attgllyacs
       61 fqaeklvyah eltvpvggtk lpvseqvaaa reahpegtvs airpspeada ttrvllsgvk
      121 gvnpdhtlav fvdpytgkvr galeqygstg alplrtwide lhrdlhlgdt grlysefaas
      181 wlwviagggl vlwfsrrral rkvrgtsgrr rtlglhgtvg vwaaagfvfl satgltwsah
      241 agahidelrt s
//
LOCUS       WP_181807031             598 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-galactosidase D [Streptomyces shenzhenensis].
ACCESSION   WP_181807031
VERSION     WP_181807031.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Kitaoka,M.
  TITLE     Diversity of phosphorylases in glycoside hydrolase families
  JOURNAL   Appl Microbiol Biotechnol 99 (20), 8377-8390 (2015)
   PUBMED   26293338
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Naumov,D.G.
  TITLE     [Phylogenetic analysis of alpha-galactosidases of the GH27 family]
  JOURNAL   Mol Biol (Mosk) 38 (3), 463-476 (2004)
   PUBMED   15285616
REFERENCE   3  (residues 1 to 598)
  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 598)
  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 14423458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..598
                     /product="alpha-galactosidase D"
                     /EC_number="3.2.1.22"
                     /GO_function="GO:0004557 - alpha-galactosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0046355 - mannan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63842
     Region          45..376
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(52,98..99,145,217,219,257,276,280)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          388..462
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          472..593
                     /region_name="CBM35_galactosidase-like"
                     /note="Carbohydrate Binding Module family 35 (CBM35);
                     appended mainly to enzymes that bind alpha-D-galactose
                     (CBM35-Gal), including glycoside hydrolase (GH) families
                     GH27 and GH43; cd04081"
                     /db_xref="CDD:271147"
ORIGIN      
        1 mrspstsalp vrglrtvlvl amtaafaaav paaqaqtpeq iaakpymgws swsmqsskyp
       61 glndkgdysy lteanvlkqt damasklkky gydhvnidag wwmdwnwkqg ydqygrqkad
      121 parfpsgmka vadhihakgl kagiylpagl ekgaygdgtt pvwnaegctt adivypdlrt
      181 tngwdssykl dfdkpcaqky idsqaqliag wgydflkldg vgpgsgksgd qydnvadvaa
      241 whkaisatgr pihleaswsl dfghaadwqk ytngwridtd vecycntlvs wensvddrwd
      301 dtpawtgkag pggwndldsl dvgngamdgl tkaerqsyat lwavaksplf tgdditkldd
      361 ygvslltnre viavdqsdnp parpvtpsdp qqvwaatnad gtytvalfnl adspsavtad
      421 wtalgftgka svrdlwnhen lgshqnkite alpahgsrlf tvtpkgsapa ytgyeaeasg
      481 ntlsgnasva gcdacsgqqk vgnlyqggkl tfnnvvvdka gtylvkvayv sgdsrpatia
      541 ansgggtshk fpstgdwgtv atvsvpvvlk agantisfds gtgyapdidr idvpkspr
//
LOCUS       WP_181807321             286 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181807321
VERSION     WP_181807321.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 286)
  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..286
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..286
                     /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=33096
     Region          3..274
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mfvvdtqihi wkeetpdrpw vpgarerirl nghredpfsy eealelmdea gvnralilpp
       61 swegdridya leaceahpdr fgimaripqn kpeegkamlt dfaqnphvkg trltfhrpqd
      121 rnwmidgtnd wywpvaeelr iptmvhapiw krelgeiaar hpelkiiidh mgimarcvdd
      181 aigywvseta dlhvhpniyv kvsalpgyst qpfpnsniqk yvremvdkmg pqrcfygtdi
      241 trllghgity tdtieqftkh wdftpeelew imgrgisevl nwpieg
//
LOCUS       WP_181807311             256 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            shenzhenensis].
ACCESSION   WP_181807311
VERSION     WP_181807311.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=26165
     Region          4..242
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 msrtrlagrt vvvtgaaqgq gaaeaaaaar egatviatdv ldeageklaa slradgldvr
       61 yvrldvtspa dwallaasld vvhglvnnag ipmrarlgqv elddwnrafa vnttgallgi
      121 qalaplmpag ssivnvgsva gltahhavay taskwalrgl srvaalelap rgirtniihp
      181 gyietplmat anpvfvaahl amtpqgrpgt vdevaplvvy llsdeaayvn gaeitvdggy
      241 aahgpvkait naldqd
//
LOCUS       WP_181807340             461 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181807340
VERSION     WP_181807340.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>461
                     /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]"
     Region          1..451
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mttavvvgsg pnglaaaltl aaagvrvrvi eaadvlgggv rsgeltlpgl vhdecagfhp
       61 lapgsafaqr fdlagagltw rwapvefahp laggrgaval rsvaetaagl gaggrgwrrt
      121 fgplaerfat iseeflqpvl hvprhplhla rfgayaglpa tllarrlrtp eaqalfagva
      181 ahafrpldtl assaigvalt taahafgwpv aeggtaaird ailaraaehg vrfetgrrvt
      241 sldelgapdv vmldtspaaa ariagdrmpp rvrraylryr hgpgafkvdf aveggvpwah
      301 egsrsagtvh lggdlaemat aekdvaagrm perpfvlvgq qyladrtrsa gdvhplyaya
      361 hvpagftgda teaitarieq yapgfrdrir atyvrsttel srhnenyvag divtgandpw
      421 qllfrprpal dpyatgipgv hlcsaatppg iwpsatastt a
//
LOCUS       WP_181807323             486 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181807323
VERSION     WP_181807323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 486)
  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 486)
  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 486)
  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 486)
  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..486
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..486
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=51490
     Region          1..477
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 mrtletllgg ewvttgqwid vldpadvrtp larvpalsak dvtraydhae rgfagwkrts
       61 pferarvlte aarlirerag eiaadvtaen gktlaeatge tlkaadfley yaglarqgyg
      121 tllhdvrpdh rthtqrepig vilvispwnd plitparkla pllatgnaav fkpatetpla
      181 glhfaralhd aglpagvlgv vtgrtaeiee tllddpriag itftgsnavg nrirrrladr
      241 nvrfqgelgg knasvvlrda dlpaaakava aasfgqagqr ctatsrvive qpvyddfval
      301 llaevraltv gpgtdpattl cplsspkqrd svvadlgrav aqgatvltgg radgerphgc
      361 yveptvlagv tpdmavwree vfgpvlalra vdgfaaavea vndsvfglaa avftrdlgsa
      421 yrfadeaecg qvavnttttg wdvhlpfggf hdsgtgykeq geevlrfstr vktvavnvgv
      481 perpra
//
LOCUS       WP_181807346             277 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces shenzhenensis].
ACCESSION   WP_181807346
VERSION     WP_181807346.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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..277
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..277
                     /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=30162
     Region          36..173
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mtdstqtlpv peavgklydr ltltalndgt fnpnihigfw dtpdstatle eavdrltdvl
       61 ierllvddsa hvldlgcgvg gpgirvaret garvtgisis qeqvktanrl aaeagladra
      121 efrhadamkl pfedgtfdav malesiihmp dreqvlteva rvlrpggrlv ltdvferapr
      181 kavphpsiek fcrnfmvtla daddyvamlh raglrlrgll ditehtmqrt ftelarptag
      241 aerpealgqt nlpdlfrpsd mvgvdefgcl lvaavrp
//
LOCUS       WP_181807414             206 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces shenzhenensis].
ACCESSION   WP_181807414
VERSION     WP_181807414.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 206)
  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..206
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..206
                     /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=22340
     Region          19..194
                     /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 mdfkssdtip gprsedhlph taqaavkivi vggfgvgktt mvgsvseirp ltteetmtqa
       61 gigvddnygs dsktattvam dfgrisitde lvlylfgtpg qerfwflwng lfegalgavv
      121 lidtrrlevs fdvmgrleer gvpfvvavns fpdaprhpve elrtaldlpp dvpivecdar
      181 rrassrdvlm tlmrflhsla msgalt
//
LOCUS       WP_181807011             838 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Streptomyces shenzhenensis].
ACCESSION   WP_181807011
VERSION     WP_181807011.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Gradowski,M., Baranowski,B. and Pawlowski,K.
  TITLE     The expanding world of protein kinase-like families in bacteria:
            forty families and counting
  JOURNAL   Biochem Soc Trans 48 (4), 1337-1352 (2020)
   PUBMED   32677675
REFERENCE   2  (residues 1 to 838)
  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 838)
  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 838)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Kannan,N., Taylor,S.S., Zhai,Y., Venter,J.C. and Manning,G.
  TITLE     Structural and functional diversity of the microbial kinome
  JOURNAL   PLoS Biol 5 (3), e17 (2007)
   PUBMED   17355172
REFERENCE   6  (residues 1 to 838)
  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 15505478
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..838
                     /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:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=88905
     Region          <93..201
                     /region_name="PknG_rubred"
                     /note="Protein kinase G rubredoxin domain; pfam16919"
                     /db_xref="CDD:435653"
     Region          201..458
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(201,226..227,254,259,264..267,285)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(208..209,211..214,216,230,232,262,284..287,291,293,
                     337,339,341..342,353..354,357,370..373)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(208..209,211..214,216,230,232,262,284..287,291,339,
                     341..342,353..354)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(212,291,293,337,339,341,357,370..373)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(353..361,366..373)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          473..836
                     /region_name="PknG_TPR"
                     /note="Protein kinase G tetratricopeptide repeat;
                     pfam16918"
                     /db_xref="CDD:435652"
     Region          577..605
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(616,619..620,622,646,649..650,653..654,656..657,680,
                     683..684,687..688,691)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          616..639
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          644..674
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          679..703
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 msqagetcqr pgcegsyedv gggelycdtc glapvvaagg apaaggmlgs sptgitaggk
       61 estgsgssgt gsrgstrtss qssksrrsvs grlsrsvsgt stgrsvsvrs sgssastsgr
      121 srlgaglvtv pqvpkpdpre mvlenpevpe rkrfcsrsdc gapvgrarge rpgrtegfct
      181 kcgnpysfvp klkggdvvhg qyevvgclah gglgwiylav dravsdrwvv lkglldtgdq
      241 damaaaiser rflaeiehan ivriynfveh ldqrtgsldg yivmeyvggk slkeianarr
      301 tpegrrdplp veqacaygie alealghlhs rnllycdfkv dnaiqsedql klidmgavrr
      361 mddeesaiyg tvgyqapeva evgpsvasdl ytvgrtlavl tfdfqgyttv fvdslpdpdt
      421 ievfrqyesf yrllvratdp dparrfasaq emaeqltgvl revvsvqtgt arpalstlfg
      481 pevkvtdtel fpkldgdvsr lgarrtasrt laleppgapa dpalvkpvav paaalalpvp
      541 lvdqndpnag flaglstslv gevsllgala aapaqtvetr lrqirallen gdseaalvsl
      601 grlederpdd wrvvwyrgva alvtgdhega alsfdavyda fpgetapkla lglcaevlgq
      661 ldnaaeyyrl vwatdpgfvs safglgrvql aagdrrgavr tlesvpeasi hytaarvaav
      721 rarlrhrtaa addtpflddl taaagqieal daygldparr eqlsaevlgc aldwilsggq
      781 dsqpavggrv llgsglderg lrfglersyr tlarlatgge eridlveran ryrprtwv
//
LOCUS       WP_181807517             204 aa            linear   BCT 28-DEC-2024
DEFINITION  GTP-binding protein [Streptomyces shenzhenensis].
ACCESSION   WP_181807517
VERSION     WP_181807517.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 204)
  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..204
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..204
                     /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=22095
     Region          19..199
                     /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 mvsehsdhse staddtsama lkilvaggfg vgkttlvgav seirplrtee mlseagqlvd
       61 dtdgvdqkvt ttvamdfgri tirsglslyl fgtpgqdrfw flwdelsqga lgavvladtr
      121 rledcfpavd yfehrhipfv vavncftgar sygahdvcra ldldqgtpvv lcdardrdsg
      181 kevlirlvey agrmhtarll dsvg
//
LOCUS       WP_181807553             286 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181807553
VERSION     WP_181807553.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..286
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32168
     Region          15..76
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(20,24,49)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(23,48)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(30..31,42,45,49..50)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          100..263
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mseprsaptv gqvvlgrrll dlreraglkr eeaarvlrva patvrrmeta evalkipyiq
       61 lllkaygvad deadlfvrla edankpgwwq rfhdilpswf smyvslegaa tlirsyephf
      121 vpgllqtedy argvlksgav ghtepeeier hvalrmqrqq lltrtdaprf wavmdetalr
      181 rpvggpevmr aqidrllevt klpnvtlqva plssgphpgt ygpfvlfrfa mpelpdmvys
      241 eyltgavyld artevathle vmdrmaaqaa taqrtkeilr dlrkel
//
LOCUS       WP_181807574             117 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator, partial
            [Streptomyces shenzhenensis].
ACCESSION   WP_181807574
VERSION     WP_181807574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>117
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          14..117
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mdtgfdlreh ggvevflrdc ptravldvia gkwtlpvlva ladgrlmrfa elrrrldgvt
       61 pkvltqtlra leregllsrt vyptvpprve yrltglgqea gglvqritdw sqanmaa
//
LOCUS       WP_181807578             152 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181807578
VERSION     WP_181807578.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 152)
  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 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   3  (residues 1 to 152)
  AUTHORS   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         <1..152
                     /product="helix-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..141
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          84..136
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 lfsaaaesfa tgglvlaesr vrlllgrala aagrlddaid cvgrakriad ahgaahlsrl
       61 avnaqrqiga rrprpgghgt phgalseqer ricrlvaggl snrdiasnlf vsvktveahl
      121 trifrklqvn sraalvgala qapaaegrrt ag
//
LOCUS       WP_181807638             269 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Streptomyces shenzhenensis].
ACCESSION   WP_181807638
VERSION     WP_181807638.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  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 269)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..269
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..269
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29182
     Region          7..265
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mtvplpvvfi hglwlhstsw qpwidlfrde gydpsapgwp gdpdtvedar qnpesiaghg
       61 iddvvehyaa lieelpappi lighsfggmi aqkllgqdra aaavaidaaq ikgvlplpls
      121 alkatlpvfk npankrrsvs ltaeqfrfaf gnaiseeesa elyerwtipa pgkplfeaas
      181 anfnphspak vdtdnsgrgp lllvsggkdh tvpevvtrat lkqyrhseav tdiinfpdrg
      241 hsltidggwr evadtvltwl rrqspetgr
//
LOCUS       WP_181807628             226 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces
            shenzhenensis].
ACCESSION   WP_181807628
VERSION     WP_181807628.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=24250
     Region          33..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 mregyegtgp gaitpdgcav elysrltvgd epdiieaavp agarilelgs gvgrmthplv
       61 ergftvtavd esaemlervr gartirstie gldlaekfdv vllasflvht gdvevrrgml
      121 rtcaahvaag gcvliqrega dyhtkvprer vdpsgytvrl vsaepvgggv nsvraeyefp
      181 dttwtqtfla rpltreqfee alaeaglevt eyltedgtwv kampsa
//
LOCUS       WP_181807671             422 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181807671
VERSION     WP_181807671.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=45864
     Region          45..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 mtteqftgri esgppvavtp aaagadvpsr tpggaaagsp aaasrlpslt glrapialav
       61 flfhaalpfa sirlfaddsl ehgfyravaq vggltmpfwf alsgfilvws yrgnekttaw
      121 wrrryvkivp pyivgwilar vlvegvdgsh ttltqgflsf fmlqswvpdv ptnfavnnvg
      181 wslsteaffy lvfpvvyplv rripaqrlky wiggvvlavc avplityavi pvgsavvpne
      241 pahsanyfwf ayifpparll dfvlgmlvar avlagrwrnv gmagsgvlla vsyvvalnip
      301 mlwglrvacl vpavmviaag amadsegrrs lfqsrfagwl gdisfafycv hftvleltrk
      361 llgdrlfstp atigllagql tvsvllawal fafverpvtr rfsrsrrara hsaarlpepa
      421 rm
//
LOCUS       WP_181807767             369 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Streptomyces
            shenzhenensis].
ACCESSION   WP_181807767
VERSION     WP_181807767.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 369)
  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..369
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..369
                     /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=38789
     Region          22..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 mqtelskalg vehavfgftp fpavaaaisr aggfgvlgav rytapddlkr dldwleahvd
       61 gkpygldvvm pakkvegvse adveamipeg hrqfvrdtla kygvpgladg easgwritgw
      121 meqvartqld vafdypirll analgspppd vvdrahdqdi lvaalagsar havkhrdagi
      181 divvaqgyea gghtgeiatm vltpevvdav aplpvlaagg igsgrqvaaa lslgaqgvwl
      241 gsmwltttea dlsspavtrk llaagsgdtv rsraltgkpa rqlrtewtda wddpsgpgtl
      301 pmplqgllva ealtriqkye vepllgtpvg qivgrmtser svqavfddlt rgfeqavdri
      361 nriagrsgt
//
LOCUS       WP_181807797             266 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal-phosphate-dependent aminotransferase family protein,
            partial [Streptomyces shenzhenensis].
ACCESSION   WP_181807797
VERSION     WP_181807797.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 266)
  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 266)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>266
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
     Region          13..>253
                     /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 mthpfldlpp ltaarfaaie drvarllgtr qdvvitqgea llplegaira tagpgttaln
       61 vitgpygqtf gnwlrdcgat vidlavpfht avtagqvrea faahpeidfv slvhaeaatg
      121 ntnpvaeige avreqgalfy ldavasvgae pvlpdawgvd lcvigaqkam agpagvsavs
      181 vserawarma anpnaprrsy lslldwkerw idggrkvlph apaqlemlal eacverieaq
      241 gletvtarhr taapppyfpa nrprpr
//
LOCUS       WP_181807816             415 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Streptomyces shenzhenensis].
ACCESSION   WP_181807816
VERSION     WP_181807816.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..415
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..415
                     /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=42783
     Region          16..396
                     /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..121,124,144,
                     147..148,151,225,228..229,232..234,237,266,270,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mrglraqvas fdrparllmv nqfainlgfy mlmpyladhl ahglglaawa vglvlgvrnl
       61 sqqgmflvgg tladrygckp milagcvlrt vafgllavas slpalivasa ltglagalfn
      121 pavraylaad ageerrveaf aafnvfyqag vlvgplagla llawdfgavc tvaalvfgal
      181 avlqaralpa rppadrgaep awravaadwr tvaanrpflr faaamsgsyl lafqvylalp
      241 lrarelfger tgvvtgavfa vsalaalsgq lkltawakrn lpgpraivcg lavmgaaflp
      301 mlrgshgava gvaaltvcaa llawggally pfemdtvvrl sgdrlvatyy gayntasgia
      361 islgnlavga lfdtgvrwlp waalggtglv caalvaqlhr aghltsepaa aavpv
//
LOCUS       WP_181807824             375 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Streptomyces shenzhenensis].
ACCESSION   WP_181807824
VERSION     WP_181807824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11457220
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..375
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40384
     Region          50..371
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mgltsnkmla lailfavllf vgtlwlwprl arrswravsg raglllatql alfvclgiav
       61 nqafgfyasw gdlfgtetdq gvvvdhtaga aagaplrvvs tsevhgmggs lprtagqiqq
      121 vgivgrtthi atpayvylpp eyfqqqyrtr tfpvvvvlsg ypgtaralvd klhyprtaqh
      181 lvragkmrpt ilvmlrptva pprdtecvdi phgpqtesff ardlpaavra hyraavkpgg
      241 wgivgdstgg ycalklamhh pgvyaagagl spsykaplda ttgdlfqgdr nlknranlww
      301 flkhepapdt sllvtsskvg etnykatlkf iasveatklt rissiildsg ghnfntwrre
      361 ipatlqwlsg rlsgg
//
LOCUS       WP_181807896             291 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181807896
VERSION     WP_181807896.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 291)
  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..291
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..291
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32830
     Region          21..82
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(26,30,55)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(29,54)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(36..37,48,51,55..56)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          106..285
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 msegrsnagg tsaptvlrmi lgrrlqerrq eagvsledaa ralrvtplti rrlekaevtl
       61 kplyvdklle tygadqqerd efvtfaeran epgwwhtyrd vlpawfsayv sletgattlr
      121 tyephyvtgl lqtpeyarsv lsggfpndsd edlerrvnlr lrrqvllers daptlwvvme
      181 eavlhrvvgg pevmreqier lleiselahv svdvvpftag ahvgacapft yfrfaepelp
      241 dvvyteilsg amyldqrsdv vahleahnrm alltsdaqsr gllnrmrkey s
//
LOCUS       WP_181807842              87 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181807842
VERSION     WP_181807842.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 87)
  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 87)
  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 87)
  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 87)
  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..87
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         <1..87
                     /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          1..73
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 elvklmvhrd argrgvargl lavaeeaaaa agitllhldt etdspaerly rsagwtragv
       61 ipdyaadpsg vlrpttlyyk rvaapar
//
LOCUS       WP_181807928             102 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces shenzhenensis].
ACCESSION   WP_181807928
VERSION     WP_181807928.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=11210
     Region          7..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mmtsvdtdlm rvladplrlr ivtllaretl csthlieetg akqtnlsnhl rvlreagvve
       61 tepcgrytyy klrpdviasl agqfadlaes arhaadnkra cp
//
LOCUS       WP_181808023             206 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF47 domain-containing protein [Streptomyces shenzhenensis].
ACCESSION   WP_181808023
VERSION     WP_181808023.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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 11443566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..206
                     /product="DUF47 domain-containing protein"
                     /calculated_mol_wt=23064
     Region          5..206
                     /region_name="YkaA"
                     /note="Phosphate transport regulator YkaA, distantly
                     related to PhoU, UPF0111/DUF47 family [Inorganic ion
                     transport and metabolism]; COG1392"
                     /db_xref="CDD:441002"
ORIGIN      
        1 mrfrltpret sfydmfaasa dnivtgskll mellgadasa raeiaermra aehagddath
       61 aifhqlnssf itpfdrediy alasslddim dfmeeavdlv vlynveelpk gveqqievla
      121 raadltaeam phlrtldnlt eywievnrle nqadqihrkl lahlfngkyd aievlklkqi
      181 vdvleeaada fehvantvet iavkes
//
LOCUS       WP_181808249             244 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces shenzhenensis].
ACCESSION   WP_181808249
VERSION     WP_181808249.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..244
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26003
     Region          9..240
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtalglpdti qaclfdldgv vtktavvhaa awketfdafl rgyegqrpfd qvadydeyvd
       61 grpradgvra flgsrgiqlp egdpddppda ptvhglgnrk narllekirt egveaydgtl
      121 ryleavrahg lrtaivsssa ncrdvlrsig aehffdvrid gvvaaerrlp gkprpdtfla
      181 aahdlgveps gaavfedala gmdagragrf gyvvgvdrvg qtdalyahga dtvvkdlael
      241 ggke
//
LOCUS       WP_181807915             396 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine-protein kinase [Streptomyces shenzhenensis].
ACCESSION   WP_181807915
VERSION     WP_181807915.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 396)
  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..396
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..396
                     /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=42323
     Region          9..275
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(9,33..34,64,69,74..77,93)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,72,92..95,99,101,137,139,
                     141..142,144,154..155,158,179..182)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(16..17,19..22,24,37,39,72,92..95,99,139,141..142,
                     144,154..155)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(20,99,101,137,139,141,158,179..182)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(154..162,175..182)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          343..>395
                     /region_name="growth_prot_Scy"
                     /note="polarized growth protein Scy; NF041483"
                     /db_xref="CDD:469371"
ORIGIN      
        1 mrgtllaerf ritdrlgvgg mgevwaaqde rmrrdvavkl vhplfgtdea atrarferev
       61 qlagrlshpg ivtvhdwgev paggrqvlyl vmelvhgvpl hrrldestpp wplavawaaq
      121 iaqaldaahr rgvvhrdikp analltpggt vkvvdfgvak flgdtlsarh ltapgdllgs
      181 phymspeqal gdgetghrgd lyslgcvlyh altgrppfds pnlvavlrmh rddvpappsa
      241 qvaglpgald dlvlallakr pedrpsdaaa vhdalttllv gqvrtgagad aldvaqlgha
      301 dsaagrflkk awerweragg dhaavsgeaa aaradalrea haeaerltis aerrlaeaen
      361 vlrraradae rilaearqra aatladaera avqrmd
//
LOCUS       WP_181808291             225 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces shenzhenensis].
ACCESSION   WP_181808291
VERSION     WP_181808291.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 225)
  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 225)
  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 225)
  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 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   5  (residues 1 to 225)
  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 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 18445957
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..225
                     /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=23742
     Region          9..99
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
     Region          121..222
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mrdatpggtk aalydafaas gkalasgkrl elldllaqge rtvdalakaa glnlttasah
       61 lqtlkqagfv atrregvrvh yrlagddvaq lfallrkvad rhqaavpaar daylgedgaa
      121 evtheellar vragnavvld vrpveeylag hipgavcipv aeladrvgel pgetevvvyc
      181 rgeycalayd avrlltdrgr ravrlsdgml ewrladlpvh agaaa
//
LOCUS       WP_181808366             307 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Streptomyces].
ACCESSION   WP_181808366
VERSION     WP_181808366.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 307)
  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 307)
  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 307)
  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 307)
  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..307
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..307
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32953
     Region          54..276
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 maalgwltpr rrsatarsvl ageasaeaar knqeatappk daaepefpvl gddkaaaffd
       61 ldntvmqgaa ifhfgrglyk rkffetrdla rfawqqawfr lagvedpehm qdardsalsi
      121 vkghrvaelq tigeeiydey maeriwpgtr alaqahldag qkvwlvtaap veiagviarr
      181 lgltgalgtv aesvdgvytg klvgeplhgp akaeavrala aaegldlsrc aaysdshndi
      241 pmlslvghpy ainpdtklrk hareldwrlr dyrtgrkaak vgipaaagvg avaggtaaai
      301 alsrrrr
//
LOCUS       WP_181808387             483 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181808387
VERSION     WP_181808387.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=52418
     Region          1..455
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 msteaeprvs gleirsidyv plderhgrlw hlgplwfmsn aqiatlavgl isiteggnli
       61 wsllaivagt ligtffmafh saqgpqlglp qmiqsrpqfg yvgallvwlf ayvqyagfnv
      121 fntvlagqal dttihggvrl wvvvvtaval vvalvgydii hkaerfltyt flvvfgiftv
      181 gvlvtlhypa gsfdlgafka tpflaqfgvv agyqiswaiy vsdysrylpp dvtvrktfyw
      241 tyfgsalggi wlmvlgtlla awagdsfgti psinaagdkv fdgfgaivll fsalglisvt
      301 alnmyggslt lisaidsfkr vrptlgvrlv tlgvtaalsl igalaatsdf ltnfnnflll
      361 vlylfipwts vnlmdyyvvr rghyaiaeif kpdgiygrwg wqgivsylvg favmipffsv
      421 gtlfvgpvak aldgadislf vglpvsally wwltrsidve aetrvaeaea aaleqaaheh
      481 rep
//
LOCUS       WP_181808421             329 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Streptomyces shenzhenensis].
ACCESSION   WP_181808421
VERSION     WP_181808421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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=35144
     Region          20..316
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mdpttdnags tgnpadaras lealraeiak avvgqdpavt glvvallcrg hvllegvpgv
       61 aktllvrala saleldtkrv qftpdlmpsd vtgslvydtr taefsfqpgp vftnlllade
      121 inrtppktqs slleameerq vtvdgtprpl pdpflvaatq npveyegtyp lpeaqldrfl
      181 lkltiplpsr qdeidvltrh aegfnprdlr aagvrpvagh adleaaraav akttispeit
      241 ayvvdicrat respsltlgv sprgatalla tsrawawltg rdyvipddvk alalptlrhr
      301 vqlrpeaeme gvtadsvina ilahvpvpr
//
LOCUS       WP_181808422             163 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Streptomyces shenzhenensis].
ACCESSION   WP_181808422
VERSION     WP_181808422.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..163
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=17610
     Region          <59..>151
                     /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          66..92
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          105..134
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
ORIGIN      
        1 mllfavsagv pvafvggavt gwtrsvigap twvswtiavl avitglplaw fsttpgirsa
       61 tnlllrayrr egleyveqqy lsrltpyrag iqlynlalal dhagdqdgal avyrsaadrg
      121 sppamvnlay wlsrhgeede aqewyrraae agytrvvpga ger
//
LOCUS       WP_181808209             142 aa            linear   BCT 28-DEC-2024
DEFINITION  thioesterase II family protein, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181808209
VERSION     WP_181808209.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         <1..142
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
     Region          <13..123
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 ieykrlvddl arrlddegll reiralsgtd arvfadeell rmvlpairad yriveshrav
       61 pdppldcrvi altgvddpkv taeearawre httsafdlvt fpgghfyltt qaaevarvis
      121 talapppatp gtppppelig rp
//
LOCUS       WP_181808535             225 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181808535
VERSION     WP_181808535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 18527459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..225
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=23926
     Region          17..81
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          96..223
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 maeqvrphta erpplgdlgr rvaarrkelg ltreetaeqa giaagylryl eehseaapgt
       61 gallrladvl httvshltgg dlgappgggr aghhprftel spaecrdllg shgvgrlgvd
      121 tdsgpvivpv nysvidgtiv frtaddttps laqghqvafe vdriddafge gwsvlvrgpa
      181 nrvteaeevq rltaafhstp waggernlwv rieprslsgr rigvs
//
LOCUS       WP_181808541             533 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces shenzhenensis].
ACCESSION   WP_181808541
VERSION     WP_181808541.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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   4  (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   5  (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   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 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..533
                     /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=57203
     Region          <3..521
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          343..382
                     /region_name="HAMP"
                     /note="Histidine kinase, Adenylyl cyclase,
                     Methyl-accepting protein, and Phosphatase (HAMP) domain;
                     cd06225"
                     /db_xref="CDD:381743"
     Region          <393..>497
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkpripwrrr llvrllfasv liavcsvaat awlavtttts aleeeqgqdl aadnkilaql
       61 sgyaadhpdw sgvghtvral aaktgrrial ttadrtliad saphdtplpp rpaaavdplh
      121 tdtytesgaq lsgidpravg pfrltavere kldlvatkek vcfdhmgvqt tvqrtpsgrp
      181 yvvvddardt plqlkarcgt vygepavets dpldfpttte tkaldaladl arpclqakgm
      241 dlggplslty dptgrdpvsg gflvtergek retdqakscv tdarrtqlep yvapaaelfl
      301 gigdqsaprf dmstankari vgaaglvlav tvavtavval rlvrplralt aavrqppelh
      361 vrapvrtrde tgllaeafnd lterrerlee qrkamvsdia helrspltni rgwlevtrdg
      421 lvdpdpalla slheealvlq riiddlqdla aadagtlrvh repvraadla eqvaaayrva
      481 adtagvtllt dadgtppdsv vqapggaplp cgrrvrwavr rkrsepaarv arl
//
LOCUS       WP_181808741             404 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Streptomyces shenzhenensis].
ACCESSION   WP_181808741
VERSION     WP_181808741.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..404
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42976
     Region          150..393
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mqrrppvpei aavaqslrpr laelveraar rirdeidvyg psgtvpegel raslrrnids
       61 mlaqfargsg pdltepggtg rlravqggpl pdvlrayrig faevwtvvae eaarlrvdpa
      121 vmvaatadaw qladeysdal tssyrqatae lvrarerers alteallsgr indpgalwev
      181 aqtlglprkg pfvavaaevt mlgheplgev earlsahgip sawalrpdlh igitsllrpd
      241 aldltmtvlr rgatarvgms pafasldctg qalrharlam ksrpagtaav vrfqddpltl
      301 vmaatpeaaa dlarrvmgpv lalgkdasav lldtfqcwid aagnavatar alhchpntvr
      361 yrlrkleglt grslqapgda aelvaalrav rvlpdtaadg narp
//
LOCUS       WP_181808766             121 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [Streptomyces].
ACCESSION   WP_181808766
VERSION     WP_181808766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
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="Streptomyces"
                     /db_xref="taxon:1883"
     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=13029
     Region          4..91
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mqvplyqaka dffrmlghpv rirvlellqh gpvpvrdlla dieiepssls qqlavlrrsg
       61 ivvsiregst vsyalaggdv adllraarri ltellsgqnv llaelrqada sasplsvnhr
      121 g
//
LOCUS       WP_181808833             396 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181808833
VERSION     WP_181808833.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..396
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41829
     Region          53..374
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mpslgtrehp cerggsrels vprlrvetpe ragldptqlr hlvrevrdlt tgerpwaaga
       61 vvvagrgpvi avqeaagwav rysaydpatd tgvelppaaq vpmtvdtpfd lasltklcta
      121 vaavqqlerg tlgidarvga ylpdfrgaaa hgitvrqllt htsglrpelp lydcpddaar
      181 ldllraetps sapgayrysd lnmlllqhvl eritgrpldv lvrdgitrpl gmtatdfgpc
      241 pgaaatedqr rpwakadrgm lrgvvhdeta walggvagha glfstardla vfsrallsgg
      301 aygtarilgp dfvdlllgpp glgflvdqpw fmgelsghga aghtgftgts lvldratdtf
      361 lvllantvhp rrrpgdsapr aaaatrlara vhtiag
//
LOCUS       WP_181808893             465 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase, partial [Streptomyces shenzhenensis].
ACCESSION   WP_181808893
VERSION     WP_181808893.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 465)
  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 465)
  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 465)
  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 465)
  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 10172632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         <1..465
                     /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          <1..282
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(39..40,42,63..66,91..94,118..120,141..142,164..165,
                     179,206..207)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(142,166,179,183)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          301..385
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 lalregvlrv arlarvtaag tpghrpldpe gtvlitggtg tlgailarhl vtrhgvrhll
       61 ltgrrgadap naaaivaelt eagatvtaaa cdvadpeala rllariperh pltgvfhlag
      121 vladgalgsl tpdhvdtvlr tkadaawqlh gltrdadlaa fvlyssmagt fggagqanyg
      181 aanafldala rhrrslglpg lsvswglwqd rsemgagltd qdlarrmars gtrgltaeqg
      241 talldaalds pdahlvaarf dfptlraqag dgplpallrg lvragrrsag aaaqtglrer
      301 laaqgpaera aglldavrst valvlghgsa dqvddgrafr elgldsltav dlrnrlsals
      361 glklpatlaf dhptpraiae fldekmfgtp vevtppvltd ldrlelallg adtsdpalra
      421 kvtmrlhslv arwsdgetpa aadglgleda svdqlldfid dmgtf
//
LOCUS       WP_181808912             407 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Streptomyces shenzhenensis].
ACCESSION   WP_181808912
VERSION     WP_181808912.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 407)
  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..407
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..407
                     /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=45261
     Region          18..401
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(55,62,92..93,100,104,111,236..237,240,244..245,248,
                     281,286..287,290..291,293,316,343..345,348..349,351..353,
                     357)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(62,86,88,91,93..94,175..176,185,235..236,239..240,
                     244,287,290..292,392)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mqesqvteel dvsfvqtphe vlkrlreagp avkvmlpngs lvwivtryee vrqalsetkl
       61 skdfkglnel marhtkegha pkqydealvg hmlasdppdh trmrrlvnka ftprrvegmr
      121 pmlreltarl ldemdkhdei dllealaypv pmevlctllg vpeaerlafg ryaavvlsdl
      181 apegyeeatr amreylvkli qvkrenpgdd llsaliaard eddkltegel latiylmfsa
      241 gtetavnlig ngvlallthp geleklradr sllpqaveef lrfdgpvnla tfrytiapvs
      301 lgdvtipvge vvmvslmaan rdpdrfdnpe lfditrpigg qmtfghgihy cmgaplarle
      361 aeialgmlld rfpelslacd pnelqwrlst vthgleklpv rphgtdg
//
LOCUS       WP_181808920             290 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181808920
VERSION     WP_181808920.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         <1..290
                     /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          1..263
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 aishhydlsn dfyallldet mayscgywaa ddpgftpada qraklelicr klalkpgarl
       61 ldigcgwgsl tlhaaerhga lvtavtlare qaayvrervr erglaervev vcrdyrdieg
      121 ggfdavctie mgehvgdaey pafaaalhrf lrpcgrllvq qmsrgrtapg ggpfieayia
      181 pdmhmrplge tvalleeagl evrhteslre hyvrtvaawh rtledrwdsf vrlageetsr
      241 vwrlylaggt lafeegrmgv dqilgvrpgp ggdsgmptat hqwyegleqp
//
LOCUS       WP_181809323             388 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            shenzhenensis].
ACCESSION   WP_181809323
VERSION     WP_181809323.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..388
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41404
     Region          35..382
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 matfflksal alsvaalvla aapaalarpp spelagscgp hdgvrralte lttadhltga
       61 svltdgpcgr wtavagtadl gtgrpmngtd rlrvgsvtkt ftatvvlqla aehrlsldaa
      121 vgrylpglid ahgydgrrit vrqllrhtsg lpdyldapew ehpersryrq ftpgeligra
      181 lqlprprqrw hyattnylvl gllvqkvtgh rpedeisrrv irplglrdty wpgdgtrirg
      241 pyshsyftsd dgrrvdgtdw nmsfggvgga lvstqgdltr fatallggrl lpaaeltemk
      301 rtvaadpdrl wpgaryglgl issplscggv wwghagtvpg ghralvavgp ggrsvavaln
      361 qvpdslqael dfqnlvdtsl caterssa
//
LOCUS       WP_181809332             670 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein, partial [Streptomyces shenzhenensis].
ACCESSION   WP_181809332
VERSION     WP_181809332.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         <1..>670
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          <1..670
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 aaaaagqede larllpelge atsgrhdeqg marlfeltar llervaaert vvvaledlhw
       61 adastrhlla yllrtlrtgr lvvlatyrsd dihrrhplrp llaeldrlrt vrrlelarft
      121 reevgrqiag ilatepdpaq vdeifersdg naffveelav aategccagl tdslrdlllv
      181 rvealpesaq rvarivaegg stveyrllaa vaqlaeddli ealraavgan lliatpagdg
      241 yrfrhslvre avaddllpge rsrlnrryae alesdptlva adahvtrlas ywyqahdpak
      301 alpavldasv marrrhayse qlrllerame lwdtvpeevr aalrpvdftd vypppplper
      361 rggtpsgcdp attplryldl maeaavagrf cgereralki tkkalrilqd ehdpqraawf
      421 waqrsrlvqg largdgwqel anaqelvrgl ppsqvhadvl anaatwsmlh qpgpeafaaa
      481 eraveyarmv gareielnar vtlgclmvds gdvdnglael yrvkdavlqd gvahvvgray
      541 vnlpselesv grsreavpil reglaftrry glldseawiw gnlseslyal grwdeaaeaa
      601 tgalgsaasa kprgvgalrl ahialargda eeaarrlaia hahygthdpm pqvllpvari
      661 aigvaaeegr
//
LOCUS       WP_181809410             555 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 27 protein [Streptomyces shenzhenensis].
ACCESSION   WP_181809410
VERSION     WP_181809410.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 555)
  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 555)
  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 555)
  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 555)
  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..555
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..555
                     /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=57053
     Region          64..326
                     /region_name="GH27"
                     /note="glycosyl hydrolase family 27 (GH27); cd14792"
                     /db_xref="CDD:269893"
     Site            order(71,106..107,148,182,184,216,235,239)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Region          338..413
                     /region_name="Melibiase_C"
                     /note="Alpha galactosidase C-terminal beta sandwich
                     domain; pfam17801"
                     /db_xref="CDD:465512"
     Region          428..553
                     /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(439..442,452,454,457,461..462)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(448,484..487,497,499,502,504,506..507)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
     Site            order(467,471,473,480,484..486,497,499,502,506)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467297"
     Site            order(527..531,540,542,549..550)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467297"
ORIGIN      
        1 mptttaragr prtrrlrlps lpapvrrtla lafsavllva aapllalgaa qpaaalgngl
       61 altpqmgfnd wnaygcnvse slikstaqam htngmqaagy syvniddcwm thsrdsgghl
      121 vpdpakfpdg ikgtadyvhs lglklgiyed agtatcagyp gslghettda qsfaswgvdy
      181 lkydncnstg tpaqtrytam rdalaatgrp ilfslcnwgq envwtwgagv gnswrttgdi
      241 nasfssmlsi fhsnvglasy agpghwndpd mlevgngsmt atesrsefsl waemaaplia
      301 gtnipsasad tlatltnsrv iavdqdslgr qgtmvsssgg ldvlakplag gdvsvalfne
      361 tgstatittt aaaigktgas syaltdlwsg assttsgtis asvpahgtvm yrvaggtssg
      421 ggtsvtgelh avgagkcldv pnstttagtq vqiwtcnggt nqtwthstsn qltvysgsgq
      481 mcldaynnqt tagtkveiws cngqanqqwt lnsdgtitgv qsglcldvtg gstadgalae
      541 lwtcngsgnq qwtlg
//
LOCUS       WP_181809463             136 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            shenzhenensis].
ACCESSION   WP_181809463
VERSION     WP_181809463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..136
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15181
     Region          14..120
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mpqtktrdrg gvdtvddivv eacpvrevld rvagkwsili ivaaargpvr ftelersidg
       61 isrrmltltl rnlerdglls rtvfatvppr veyeltdiar elhqsllslt dwaerhrati
      121 saarvaydae rlteeg
//
LOCUS       WP_181809516             504 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181809516
VERSION     WP_181809516.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 504)
  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 504)
  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 504)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>504
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
     Region          70..>265
                     /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 mtsatdpvph tpvspdwgpp taspaassaa pptatppdta prwslpalia ililaavlys
       61 wnlsgssmnt fysgavwaat kswkawffgs ldpgnfltvd kpplatmvmg lssrifgfgt
      121 wqmmapmivl alatiyilhs tvkrvwghga atvaalvlal tpitvainrd nnpdtllvfl
      181 mvsgsalafr atrdekllpl lgaaacfgla fntkllagwi alpavfalyl yaskatwakr
      241 avnlalaavv lavssfwwav avslvpasdr pyiggstdgs awdlimgydg lgrvfggegn
      301 gggggggggg fsgsaglgrm fndilggqis wllpfsaial vgglvlcgra prtdlrrmal
      361 vlwggwtllh yvifataqgt mhpyyttala pgiavlcggg gamlvrafrt dkrwiwvlpl
      421 afgvtgiwai vllrrasgwn twlwptigvl tvagivgmlv frsgakvrll taslavavva
      481 alagptayam avpfgstggg mggt
//
LOCUS       WP_181809518             298 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase, partial [Streptomyces shenzhenensis].
ACCESSION   WP_181809518
VERSION     WP_181809518.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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..298
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         <1..298
                     /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          29..262
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 vrldhtptgv aevddlartl qtvlarydqq aarttealat arsfaatash elrnplmsvg
       61 tnleiltghp dlppaeraev lddlrrehgr vlgllvmlra laegdlveae afgpvdladv
      121 vhqgagdlrr rhpgadvvvr agsglvvqgw eqglrsvvdn llanalvhgh eagspaqvev
      181 svhsardedg pvavltvgdr gpgippaara avferfhrrp dspgsglglt lvaqqtalhg
      241 gritvqdrpd gpgtrfevrl plaaagdpaa aaatlpqlrr dwltadfgrs qtfhkdrs
//
LOCUS       WP_181809546             423 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein, partial [Streptomyces shenzhenensis].
ACCESSION   WP_181809546
VERSION     WP_181809546.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>423
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
     Region          <6..>405
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mieqnrpqda aagmwrtarg tharqlvgrq remdvlrsav gncrdgvstv ieitgdpglg
       61 ktrllselad laaaeglavl ygrasefepq rsfgvfvdpv rrcfgrraaa ahgpldedma
      121 qlldlvapgg agadpgrpry peveryrlhh avgrlladag gergvllcld dlhwadagsl
      181 ellhhllrqp prtplilacg hrprqaaakl laafqhtpad ygierlplap ldqrecrall
      241 gsahpprrrd rlcevsggnp lylevltelt tdgtdaaeel tglphtlraa larevalltg
      301 eelatlraaa vlgdpfdpll lgpvaglatg palealdvlv gmdlvrsgts nglaqdeprq
      361 llhfrhpllr evvsrdtppg wwlaanarad ealsrsgasp verapylars artgdleavr
      421 vlt
//
LOCUS       WP_181809631             394 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181809631
VERSION     WP_181809631.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 394)
  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 394)
  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 394)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>394
                     /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]"
     Region          22..394
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(59,66,89..90,97,101,108,235..236,239,243..244,247,
                     280,285..286,289..290,292,315,342..344,347..348,350..352,
                     356)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(66,83,85,88,90..91,173..174,184,234..235,238..239,
                     243,286,289..291,391)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mdarttppvp atvdpaella dpytgyarlr eagpvhrvag tdglpawlvt ryedvrqala
       61 dprlsldkan agpggyrgla lppaldanll nmdppdhtrv rrlvsraftp rrvallrepv
      121 rrtadallda maplgrtdli aayaaplpia vicellgvpa edrpdlrawt dalvvpdpar
      181 perakeavga llaffsllla rkraepaddl lsamiavrde edrlsedelm slaflilfag
      241 yentvhlign atlallrnpg qlaalradpe rlgpaveela rydgpaplai rrfptedvti
      301 ggvtvpaget vllslaaahr dprrfpdpdr ldigrdatgh lalghgihyc lgaplarlet
      361 eialgaller fprlgldvpv drlvwrpsmr trgl
//
LOCUS       WP_181809614              75 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181809614
VERSION     WP_181809614.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 75)
  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 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   3  (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   4  (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 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         <1..75
                     /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          12..69
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 ppveapaald aldglaamer qvaalvmega tnreiaarlf vsvktveatl trvyrklgir
       61 srvdivrlaa grrak
//
LOCUS       WP_181808693             984 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181808693
VERSION     WP_181808693.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 984)
  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 984)
  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 984)
  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 984)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>984
                     /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]"
     Region          2..>971
                     /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 miplsfaqrr lwflgqiegp saaynipvvl rlsgtldrta lgaalkdvig rhevlrtvyp
       61 aadgqprqrv mqvgetgfel pvtevpparl aeeirratry afdfateipv rawllaeapd
      121 ehvlvlvvhh iaadgwsmgp llrdvsvaya arlegrepgw eplpvqyady alwqrevlgd
      181 eddpdsvlse qvaywrrtla gapeelalpt dlprpamsth rahtaelnis adahrrllal
      241 arergatlfm avhaglamll srlgagedip igtltagrtd eglndlvgcf vnnlvirvdl
      301 sgdpafadvl arvreaalda ftnqdvpfek lveelapsrs larhplfqtm aavqsadlls
      361 grrggsalel pglrvgtlag eqtmrdldld lvvgetfden gspaglhgnl igaadlfgaa
      421 sveriadmma rlletvaaep atrlgtlqvv seperrrmlr qwndtaaplp dglvpdlfaa
      481 qaartpeata lvsggtelsy retdqrsnrl arrlvaagig pesvvallmd rsadalvail
      541 avlkaggayl pidpgqpgpr iaatladaap alvlaetgta paqdvvgavp vllldtsalh
      601 eelaghadta vtdadrrapl lpahpayviy tsgstgrpkg vvvshegfan lsgshdrfga
      661 gpgsrvaqfa sigfdmfcee wllalltgaa lvvvppqqrl geefaefltq hgvthatlpp
      721 avvatlpega lredfvldvg geacppevit rwsdgrvmfn sygptetsvn tavwrcrpdl
      781 apgtaapigr pivntrvyvl ddtlqpvpvg vtgelyvtgt glargylgrp gltgerfvac
      841 qfeagqrmyr tgdrvrwdae gqlvfagrad dqikirgfrv epgeieavla ahpavdlavv
      901 iaredtpgdm rlaayvvpat dgvdtapdgl attlrehaaq hlpsymvpaa vvvlaelplt
      961 vnakldrkal pvtrsrcagc sgcs
//
LOCUS       WP_181809635             110 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Streptomyces shenzhenensis].
ACCESSION   WP_181809635
VERSION     WP_181809635.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     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          <1..95
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 dagwasfism lsykaerygr tlikigrftp tsrtcstcga vdgpkplnvr ewtctacgtv
       61 hdrdtnaain vkqaaglavs acgapvrpga ipaqreeags rgfptepraa
//
LOCUS       WP_181809656             285 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Streptomyces shenzhenensis].
ACCESSION   WP_181809656
VERSION     WP_181809656.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  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 285)
  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 285)
  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 285)
  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 285)
  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..285
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..285
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31159
     Region          10..269
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mftsvddvsa rlaetgylas pavattvfla drlgkpllve gpagvgktel akavaqvaga
       61 rlvrlqcyeg vdesralyew nhakqllris agrdetwdea rtdifseefl lprplltair
      121 gddpkvllid etdkadveve glllevlsdf qvtvpelgtv tatrrpfvvl tsnasrelse
      181 alrrrclflh igfpdeeler rivrlkvpgl tealaesvvr vvgalramdl rkvpsvaeti
      241 dwartllalg adtldeqvvr dslgvilkhq ddiqkaaakl dldal
//
LOCUS       WP_181809967             710 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Helicobacter pullorum].
ACCESSION   WP_181809967
VERSION     WP_181809967.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pullorum
  ORGANISM  Helicobacter pullorum
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
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="Helicobacter pullorum"
                     /db_xref="taxon:35818"
     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=77594
     Region          2..708
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mevaklnisg mhcsacssti eknlekiegi knikinavsg rakisyegsc iseqkiieli
       61 tsygfpafrd nakeleiiyl eglkkrllvg iplfvvifal hmggfhgiws siiqlvlati
      121 vqvycaypfy rgaksvfktk sadmnvlial gtsvaylysl ylfiigdsng yyfegssavi
      181 cfvllgeflk skakkkagde lesltkilpp karilkgenq ewisidnikk gdqclvvgge
      241 kipldgkiik gnaevssahi ngeelpkilg vgsevvggsl vlngeivves lkdsneffvy
      301 emldllelsq tkkppigkma dkiasifvps ivvlsvvaff fwwmmgegfa fslsiaaail
      361 vvscpcalgl avplaivcas mrakkseili ktpevyerar eiktivfdkt gtltkgeisi
      421 knvefishds nlivslcyam qennphpiak afveylkakk erivleekey iiakgvraky
      481 asdeyflgsl ewietiidkk itqnrenvia fsnkseilal fylqdsikeg aremveslqn
      541 igiesvilsg dnvesvkkva qnigiteyya gvspmqkaei ikqlqakggv cfvgdginda
      601 lalkeasfgi sfanatdlak evgdilllrd dlslvykvfe isfatlknik enlffayvyn
      661 vvlipiaagv lypafgivlq pafaggamaf ssvsvvanal risrlklkge
//
LOCUS       WP_181809649             418 aa            linear   BCT 28-DEC-2024
DEFINITION  adenosine deaminase family protein, partial [Streptomyces
            shenzhenensis].
ACCESSION   WP_181809649
VERSION     WP_181809649.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 418)
  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: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         <1..>418
                     /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]"
     Region          19..411
                     /region_name="Add"
                     /note="Adenosine deaminase [Nucleotide transport and
                     metabolism]; COG1816"
                     /db_xref="CDD:441421"
ORIGIN      
        1 rtaaphdpra lrgfflklpk ggdlhnhlfg avrteylial aagdglcvdt atltavvppc
       61 gpgtrpaada rtdpgfreai lrawsmdrfp adrsghdhff atfdkfglvp alhpgrvlae
      121 vadsvaaqhq fyletmvnpa sdragqlade vgwdpdlaal harlvaggrl devvaaarga
      181 tddadsgfra aarcgtdhpr pgcrltvrfv yqafrgesre rvftelalgm rlaerdprfl
      241 avdlvqpedg ptaladytlq mrmvrflhtv ypkahvtlha gelrpglvpp edlrfhvrqa
      301 vdiagaervg hgvdlrhedd wqrtartmaa rriavevpft snaqilgvrg aahpfatyra
      361 ygvpvvlatd dpgvsrtdis heyqyaaety gltypelkdl arasvqyafl pgrslwrg
//
LOCUS       WP_181810124             309 aa            linear   BCT 28-DEC-2024
DEFINITION  chemotaxis protein CheV [Helicobacter cinaedi].
ACCESSION   WP_181810124
VERSION     WP_181810124.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter cinaedi
  ORGANISM  Helicobacter cinaedi
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11122260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Helicobacter cinaedi"
                     /db_xref="taxon:213"
     Protein         1..309
                     /product="chemotaxis protein CheV"
                     /calculated_mol_wt=34919
     Region          25..153
                     /region_name="CheW"
                     /note="CheW-like domain; pfam01584"
                     /db_xref="CDD:460257"
     Region          183..294
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Site            order(287..290,292)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381085"
ORIGIN      
        1 mriasnemel vdfrlfedkn getyegvygi nvakvsgiva ypeeifetpg spdymlgmfd
       61 lrgdilplid ltkwmnikpk edavrdkkvi vtefnnkqlg fvvhatrrlr rvswadiesa
      121 mfslsnddqr gkitgttrie dgrtllildl egiiddldfq mpnggdrvdi eqfkpknkfe
      181 gsvlilddss iarkllcntl seigfdvvda idgeaglerl eqlyerwged iakhlkliis
      241 dvempkmdgf hfaaqvknda rfnkiplifn ssisdkfsas kgkeigaeay lvkfdaklfy
      301 deitrilsk
//
LOCUS       WP_181810087             255 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA 2-thiocytidine biosynthesis TtcA family protein [Helicobacter
            cinaedi].
ACCESSION   WP_181810087
VERSION     WP_181810087.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter cinaedi
  ORGANISM  Helicobacter cinaedi
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 255)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Helicobacter cinaedi"
                     /db_xref="taxon:213"
     Protein         1..255
                     /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]"
                     /calculated_mol_wt=29130
     Region          21..201
                     /region_name="TtcA-like"
                     /note="tRNA-cytidine(32) 2-sulfurtransferase and similar
                     proteins; cd24138"
                     /db_xref="CDD:467514"
ORIGIN      
        1 mketpkiskk ilsvvgktna qyglikegdk vllglsggkd sillatilay mqrhapfkfe
       61 fkaltvdygr ggeyeyifey cqklgipyel yrtdiyeile qnkregtiyc sfcsrmrrga
      121 lyskaleygy nklalahhld daaesffmnl tyngamrsmp piyraengle virplifvre
      181 rqiidfiasn giyiapdcnc pinwldsdkk pyareatkqf lknmesenpn ffkslknafs
      241 nihagsfcdt nylni
//
LOCUS       WP_181810179             708 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Streptomyces ipomoeae].
ACCESSION   WP_181810179
VERSION     WP_181810179.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 708)
  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 708)
  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 708)
  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 708)
  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 11461572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..708
                     /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=77163
     Region          50..637
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          643..696
                     /region_name="DUF4982"
                     /note="Domain of unknown function (DUF4982); pfam16355"
                     /db_xref="CDD:465102"
ORIGIN      
        1 mtgfptrrqv lsgtaggvla slagipkaga asaattytap nprvwthind gwrfirqdvt
       61 gaqapgfdds gwtsvntpht wnavdgadgg nnyyrgvgwy rrhytvpstm agkrlylqfa
      121 gvnqvadvwv ngtylgqhkg gyarfrfdvt gvlvpggdnv iavkvtnard tgiapvsady
      181 tfeggiyrnv slwaidnlhv rmtdyagpgv ylrqsnvtta satvtvttkl wndnstarsv
      241 vvrtviadss gnvvadtstt arslaaatga disqtvtvns prlwngpadp ylynasveih
      301 dvtagadria dvvterlglr siavdadtgf qlngshlhlh gvnlhqerav kgwaisdadh
      361 tqdfdlirel gantirmahy qhdqkdynla derglivwae iplvnsvtds aaftantqnq
      421 mrelirqnyn hpsivfwgig neqtdyngta tntllqslad ivasedpdrl styavrsedp
      481 dnaqaglhtq ttgfnkylgw yygskdgelg awadnlhtts psrkiaisey gaganttqha
      541 lnppkpapgg swhpeeyqsl fheaawkqla erpyiwgtfv wamfdfasdg rgegsqpgin
      601 dkglvtrdrq irkdafywyk anwattptly itsrrwtqrt dattelkvys nasqvtatln
      661 gtslgtlsss dhifrwtnvt lkpgqntvtv tatingstyt dsvdwtlg
//
LOCUS       WP_181810232             777 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Streptomyces ipomoeae].
ACCESSION   WP_181810232
VERSION     WP_181810232.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 777)
  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..777
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..777
                     /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=79751
     Region          55..493
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mnggaggges egrgqgrsqg reqdrgqgpg irgirqgqgt girvrplgad dpeaigpyrl
       61 lgrlgsggmg rvhvarspgg rlvavktlla egvvsesdrr rfarevrlar rvggvctanv
      121 vdadpdaerp wlatefipap alddlvrgcg plppdavpwv aagaaealva lheagvvhrd
      181 vkpgnillpp dgprlidfgi shavditrtt ltlgtiayts peqargeett agsdvfslga
      241 tlfhlatgrp pyrdtgdtlr llaqvsrgdr dlsglppelg plvmrclhdt pdrrptpsql
      301 ldelaplvaa gptsageghw lppkwlrlie syeaegrall dgrarleghr psgpdprraf
      361 srgegdgsaa pggsgvedar asedvlgpda tptqdlrtrp vpepnptrpy tqvrpagssa
      421 sagssvrsga srseagassa gagassakag dsrsgagass akagdsrsga gasssvsgss
      481 tagartgssa sgastagpga gssasgasta ksgaararag ararqrtrsw aeanpgagrd
      541 ggrvrssgrv rsapapapaa pkpappakks sggwlmavfi vllvvwfanl ssqdddssga
      601 gsypttapit ptplnspspd pteeafaavr agdclnaygt gylgqwstev pervdcdaad
      661 afvrvtsteg savdcpdstg rsywsyygrt agyqvlcler qfrvgqcvpa eaadnggvra
      721 nllrvwncga dtvpaghkyi lqitniykgs dgqcpvstry wtwsvyggka ylcmvtv
//
LOCUS       WP_181810269            1057 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Streptomyces ipomoeae].
ACCESSION   WP_181810269
VERSION     WP_181810269.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1057)
  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 1057)
  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 1057)
  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 1057)
  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..1057
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..1057
                     /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=113324
     Region          1..243
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          202..1057
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          924..950
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(926..927,930..931,933,964,967..968,971..972,
                     974..975,998,1007..1008,1011..1012,1015)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          960..992
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          997..1031
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrfavlgslt tvdddgvtvv vggpkprall avlllepnrt vpldtvraal wgedppptat
       61 aslhnhvarl rrslrdadgt rlrtmthglq lrvdegeldr dvfegqvrra qearnrgdwe
      121 aaerdadaal alwrgapfad vpalaghpvv tllqeqrlqa lecrfeallh ldrldglaae
      181 lgslvkehpf retlhrqlml vlgrtdrqae alalfrslrr tlveelgvep gpavqeahre
      241 vlrsaavrhr epptpaapfa dpaadpwtlr agapprpaqr lsagrpprsa qhpsaatppr
      301 paqhpsaatp prpaqhpsag tparpaqhps sgtpprparh lsaetpprla qlpappggfv
      361 graehiaeir celesdrsrt alavisgmpg vgktglalhi aeqlrhafpd gqlylnlhga
      421 tpgvaplapa dalavllhgl gvdarripsd vaagsallrs tlaptrtllv lddaasvsqv
      481 rpllpagagc avlltsrqpl atlgasthvr ldplspqdsa lllerasgrs waatdaeava
      541 rlvalcghlp lalrvcaarl rsrrtlpvek laerlarqed rldhleledl svrrslmaah
      601 eallgsgdpr dgdaatalvl igaldlpeyg aplmatamds tersaeqald rlvevallqe
      661 agwgryvphd lvrdfarela arpgaqpena daverslrwy qrrlarcaat lrphpgrvpe
      721 qpgggtdfvd aaaalawgdt eaanllflag sgghgrlgpt rtldlintlf pylhdrgrvr
      781 dlerltrhai tlarssgnta aegralghla sahysvgrvr qalllldeav elsehlsddv
      841 armrhlgnra allrelgrdt darttlarcl alrpdtlapg eeaillghqg yvaeltdpra
      901 alsfhlrsre larqagsavi eqvalcntgr thlalgepaq alrrfdealr vmasgaahwn
      961 aeretrlgra qalrelgrla pareacgell eettargdsy grglaeheyg hvlralgneq
     1021 ealtrwnsal saldgtdaqv ltdlrtltat atttadg
//
LOCUS       WP_181810083             327 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Helicobacter cinaedi].
ACCESSION   WP_181810083
VERSION     WP_181810083.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter cinaedi
  ORGANISM  Helicobacter cinaedi
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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..327
                     /organism="Helicobacter cinaedi"
                     /db_xref="taxon:213"
     Protein         1..327
                     /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=36576
     Region          2..303
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mefknllmla plagytdlpf rsvvkgfgvd itvsemissh alvysnkrtl kmaekspqeq
       61 pysvqisgsk eevikqavei lntqegidii dlncgcpapk vanhgngsgl lkdlnllvki
      121 anlikenakt pytslkvrlg fdkkipneia qalkdvksdf vvvhgrtrad gykkekidyd
      181 aiahikqnvp mpliangeid svekaqkvle htgangvmig raaitspwif wqirnnthei
      241 ppivkkelvl ehfnkmiefy gergaimfrk nlhaytkghe gasefrnlin slsdveqitq
      301 hienffshnq mvthnfpqlv hlnkrts
//
LOCUS       WP_181810271             228 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces ipomoeae].
ACCESSION   WP_181810271
VERSION     WP_181810271.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     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=24178
     Region          35..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 msplgtgtss dggpvapdgs pvglyrsfpp grepalihga vppgaavlel gcgagritha
       61 lvdlghpvva vdqsadmlac vqgatrvhad ieeldlaref pavvlasfli ntivpgqrea
      121 flatcarhva ddgvvlvqrt spdwaaslrp grehrsgefl ititearleg gvlhaaqecr
      181 rgetvwthsw tdvvhsdedm eklaasaglp ldrwldeere wallrpar
//
LOCUS       WP_181810329             957 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces ipomoeae].
ACCESSION   WP_181810329
VERSION     WP_181810329.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 957)
  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 957)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 957)
  AUTHORS   Rosinski,J.A. 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 957)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..957
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..957
                     /product="helix-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=100581
     Region          <2..888
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          887..943
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 maplvsrege larldevldr lgegsrgpvv vdvtgaagig ksrlvsefcg rarergmtvl
       61 rgrateyerh lpyqplvdal adldldagse wpspfadghp tdrfafqrrv tdhlvgiaaa
      121 ggglvvaldd vhwadpasle lldhlvrhpp rrapvvivva rrerqtsapl aaalfrgvea
      181 gtvlrlelgp lderaclaal apgvpsglaa elyaagegnp lyflallqar rpaglsslll
      241 deltpltdaq rrtaqaiavl gdhaapalva avtgrhesel dadfgelaar dlarpgpdgr
      301 walrhpvlra lvhdttdptl rtrmhhlaaa elarigapvt erahhversl tgwdppavav
      361 lteaaeqaaa tapassahwl gvalahlpdr paygalrrdl mlrraealgv cgglresrdl
      421 lhevislspp gtgdgvrvsa vtlcavmerh lgryaeaval lrrelargsg lstaetvelg
      481 lelgssapha ssypdvrddv artlelarsl gdevaeagal aitalgesye gntavaaeav
      541 draaalidsl tdrdlaglce plarlgwaea fldryadaer haerglaiar rggrlyvmph
      601 lllckshvqv qtlrlpsave laeeaetiar gigsdellaf vlaaktqali palppgdgga
      661 laaaeeavar agagtrwwas iawcmlgyaa ihagdperar aavlragged lgglqpcmrp
      721 lfleilvtaa vavgdhdear lwaerarkea ehlgipaqra salrsrahip lgegdvaaaa
      781 elfeqaaeet vragttmwea htlllgaplt aaagraerar amwersrrls aeggahllag
      841 ladalrpavv peaatpsgsa gapaavdgge gdsdhagahp esaplelssl sprereiaal
      901 vaegltspai aerlflsprt vethlsriyr ktgitsraal talqvrdelg vsggrae
//
LOCUS       WP_181810341             441 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Streptomyces ipomoeae].
ACCESSION   WP_181810341
VERSION     WP_181810341.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     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=46290
     Region          22..409
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mssagissss saslpgdppg grralavwsi gvavyfvavi frtslgvagl daadrfhvsa
       61 salstfsilq llvyagmqip vgllvdrlgt kkvltlgall ftagqlgfal spsygtalas
      121 rallgcgdam tfisvlrlgt rwfparrgpl iaqfaglagm agnlvstlvl arllhgvgwt
      181 aafagssaag lvvlvlvllf lkdhpegyep epsphqgaay vrrqiatswr epgtrlglwv
      241 hfttqfpamv flllwglpfl veaqglsrat agdlltlvvl snmvvglvyg qvvarhhaar
      301 lplalgtvla tatvwaatll ypgehapmwl lvvlctvlga cgpasmlgfd farpanpper
      361 qgtasgitnm ggfvasmttl lavgvlldmt nddyrvafsa vfvlqalgls qilrlrgraa
      421 rrererlvas rvetvhvpas r
//
LOCUS       WP_181810344             544 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces ipomoeae].
ACCESSION   WP_181810344
VERSION     WP_181810344.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..544
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..544
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=55057
     Region          17..148
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          <459..544
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtepavpptp pvslsallar edlglrqiag pvddgtvihw ahtsemsdpy pyllggelll
       61 tagvhipeaa gsdggapgra ksrpgdyfdd yvsriiaagg aalgfglapv hdtvpralve
      121 acdgyglpli evpprttfsg varavwqlma rarhaelrrv teahqslaaa ashadpvrav
      181 lrrlarrvgg ravlygpdga elaaagpapt ptaladlaav vrpgglpgpg gvpgsgtalg
      241 ptptpasatd tvggthlaay algagqgfal avatprrdpg dhtiasvaav llslltgeqr
      301 sgtgaartsa lvrlllgaap eevapllgdd idvrpggead gargekgare gsdgptasga
      361 rwlvvhalpa gdgpppdavs aaalgaslgs sladahgdvv rvlvpagrev taqpgwtcgv
      421 sapaapdawa sadaqaaral araratrtal vrhggrtafa dlipaddata hartllapla
      481 aspalietlr twlslhggwd rtavalsvhr ntvrqhvarc aallntdldd pdvrmelwfa
      541 lrah
//
LOCUS       WP_181810421             195 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Streptomyces ipomoeae].
ACCESSION   WP_181810421
VERSION     WP_181810421.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 195)
  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..195
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..195
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=20557
     Region          66..136
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mtasgeliad vnddghpdrv sdpsrigtrf nitfgvgsad eatvgarala dytggrqeyv
       61 igaaadfnrd gwtdlvivag deqaddspiy prtaelrlgp fsntgrgqri lplglgatse
      121 msvvdynhdr ypdlavyghv gdgermasar lcagatalsa tgsydrgtef esparlpnsg
      181 lgrfyrrcsa sgmte
//
LOCUS       WP_181810428             233 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces ipomoeae].
ACCESSION   WP_181810428
VERSION     WP_181810428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 233)
  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..233
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..233
                     /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=25175
     Region          23..219
                     /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 masssmasas eggpgvsgil lrshsgnvyr fdpgalclel lvtggpgala rfevlntpdd
       61 lvkwvaesrl tptpesfdvt dddvaytrrl rdaltrtfvs rvhgdglpel gipaadpadl
      121 rvineaaarp plapalredg trgwaagaat gaqlmstvar davelltgph aarvrmcage
      181 rcyllyvdts rpgrrrwcsm ehcgnrnkvr ahrarraeee paehrksrpr nre
//
LOCUS       WP_181810463             435 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces ipomoeae].
ACCESSION   WP_181810463
VERSION     WP_181810463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 435)
  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 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
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Rosinski,J.A. 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 435)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..435
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..435
                     /product="helix-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=46682
     Region          <3..>304
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          369..422
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdlverdkef silknaitdc lggrnrprlv ivsgppasgk tklleacrty aaaqgsllla
       61 atasrsgdrs plsmmirlfr saglptglrd dddvdsklsr klrsdlielg rvrpvlicvd
      121 naqysdtasl allssisrhp lparilivla egpdlqqpmt pcvaqshnph vqhisldlls
      181 pagvaqmlgn ainaepsqet vsawhtvsgg npllvqalid dwsgsreedh gdmrkltpva
      241 gdgfrkavmt iinncgrytr tvaevlavlr afdsaecvrg lldrapetvl scvralenag
      301 lltegrfrer aaeaavlsaa aakhteldav vaahlvtekv drhrgsqpsp gdrkvpdrst
      361 tdggdfgkpl sraergvaml vgmgytnrei srelhitvst vgqhltriyr klgirtrael
      421 aatsvhledv ltgss
//
LOCUS       WP_181810472             229 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces ipomoeae].
ACCESSION   WP_181810472
VERSION     WP_181810472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 229)
  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 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   3  (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   4  (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 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     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=24089
     Region          36..215
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          158..213
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mqcpvpapat rppaplvvav igghvpayer lrrtgdlvlr hirppytvvg gggcdvvllc
       61 tpdpapdllr rlgervppil mvspatgarr ittalrlgvk sclvdgdydd rtlanalrst
      121 aagitvlspa avkalsgdlg rpqagparpe shglrirpsl spreqqlmdl vasgltvaei
      181 skrmtlavkt vrnylsaiyt klgvssrtea avlwlgatar prrtaehga
//
LOCUS       WP_181810487             373 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Streptomyces ipomoeae].
ACCESSION   WP_181810487
VERSION     WP_181810487.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..373
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..373
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40583
     Region          88..349
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mlqelqdvin gisaevgvpt sltdtrlnsl vfgphddagi dsvrrqalll rstpewvrew
       61 fgrygidtat apvripadpe helasrvvvp arwgsttcgy iclldvrhel detrmgavmd
      121 aarevgrvly ldqqarhsda dllgdlvrgs aavrgkaadr laeqgrfpvg wpvavlflrl
      181 ldgasdteal ehwlwrdhga lprgalrcld aegavilaav ppsadpghme riadqllaga
      241 hdvprfivgi gdaqsdlhda hlsyehaqla araamvwpet gpvcswdrlg alrvligtpd
      301 hllrdlmdpr vsllkeaqls hanlidtlei yldsgcdnqa taarlhvhrg pvgsggrrpy
      361 lrcgeprhre aav
//
LOCUS       WP_181810532             290 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Streptomyces ipomoeae].
ACCESSION   WP_181810532
VERSION     WP_181810532.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            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..290
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..290
                     /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=30009
     Region          8..284
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 msepdvgsyr rpdnlselli lldrrpasvl aggtdlvvmr adgtvdrahd ivdikgvsel
       61 rgislntdgt ltigaatslr elarttvvpp naitdgaalv ggwqtrargt iggnicrasp
      121 agdtlpgvla adaqlelast tgtrlvpghd fftgpgrtvr epnelltrii vpashgasay
      181 lrftyrlamd lavvgvaahl eiengrcvaa rvalsaaaat pvpapdaada lvgteldeps
      241 ieaaaqlvln tatpiddgrg srahrrtvlp vlakraigia lerargghqr
//
LOCUS       WP_181810506            1017 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces ipomoeae].
ACCESSION   WP_181810506
VERSION     WP_181810506.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1017)
  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 1017)
  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 1017)
  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 1017)
  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..1017
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..1017
                     /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=108826
     Region          291..972
                     /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 msprpssapt lsptprtakp lpgvllpggp sperggaslr aqlvlallca ayavgaafgw
       61 gneqvalvmg dfglsaaaat aavscfryar srrsrfrpaw llfalssama algngvwgwy
      121 evvlerpvpn psyadlfflc fappaivgll vlakrpvtqa gwvclaldaw liggslvtls
      181 wslalaqtaq lddsdtahta lslayplldi alvsmvlalh frrssmhrsa vntaigalal
      241 tvmcdalfas pllhnsyrsg qlldagwfag slllayapwa gqrhgqpeee qharvvhehi
      301 pgqrhdadgh rhdadghrhd gphgghvhvp lqggghsryp vtrpiagsla altpylaaav
      361 ctlgilynvl ngrsvdrvvl itactvvlal vvrqgimlld nitltqelaq kenhfrslvq
      421 gssdvimiaa psgilryvsp aaagvygrpa eelvgkelas iihpedlgcv vhevrrflaa
      481 spaeepttri ecrfksgdgg wlnvestvnr hhgglilnsr dvtervrlqa qlqhnaehdp
      541 ltdlpnralf tkrvqqalsg rrssdrgial rntavlfidl dgfkavndti ghqagdellv
      601 qaarrlqesv rqgdtaarlg gdefaalivg dgsrdraare qhifeladrl rvtlsqpyti
      661 dgndvrvaas igvafaeagl gagellrnad lamyrakasg kgrvelyqpq mqqdvvrkae
      721 latrlraalh dgeflllhqp vveletgris svatearwrs sqgvlftpae flrvsedndk
      781 taelgrwmle qavehaserl vnglhvpvsv rmsarrlldr slppgsletl ltrhglpsgs
      841 lvielsdtev kgslddlerr lsqlrrlgvr valdglgsgq aaitalrrlp vdvlkldrsl
      901 vegvvestrl hkitsgllri agdlglesva egvdlpeqvv alramgcthg qgaafsgpld
      961 eyrlrralst gnypvprgpa epafagggag vytsgvpavy gggsalrshn etpvppt
//
LOCUS       WP_181810558             309 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces ipomoeae].
ACCESSION   WP_181810558
VERSION     WP_181810558.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..309
                     /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=33792
     Region          49..297
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mmaknrhdsa reipevafaa pagtpagvev mslaelgqrv ceqtlarpqr pdfhhllalt
       61 agslwhvvdf dgyalrpgsw lwvrpgqvhq wgdltkaegt lilfrqdmld patataarvd
      121 dphapviitp vsddaeavtm aaehlsrefr slghlpldvh iaalrhllav lllrlahlav
      181 pvgspapepd etylrfrdav erhftstrrv edyarmlgys grtlaraala gaglsakefi
      241 drrvvleakr llahgdetaa qisdrlgfvt psqfskyfmq rtgrspidfr ngvrgraedp
      301 gpsadlgrg
//
LOCUS       WP_181810570             344 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            ipomoeae].
ACCESSION   WP_181810570
VERSION     WP_181810570.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     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=36534
     Region          64..313
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnprqplptn pdvspqltpe plqprqppsp ditsaptrls fgygtngltd lrlddalall
       61 adlgydgvgl tldhmhldpl apdlaartrr larrldalgl tvtvetgary ildprrkhgp
      121 tlldadpddr arrtdllira vqvaadlgah avhcfsgitp pgtdedtawk rlpdaltpvl
      181 daataagipl avepepghll aaladfhrlr ealdspaalg ltldighcqc leplppadcv
      241 raaapwlrhv qiedmrrgvh ehlplgagei dfppvleala avghqaltvv elprhshagp
      301 hfaeqslsfl qtltrdltaa gptktratpd tsgltppspn gsts
//
LOCUS       WP_181810789             283 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces ipomoeae].
ACCESSION   WP_181810789
VERSION     WP_181810789.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 283)
  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..283
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..283
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31792
     Region          12..75
                     /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..278
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 magsptpirr rrlaallvef reragrspee aaerigchrs kinrienarl gislgelrdl
       61 lkfygiedpa dvdhmvslar rmrepawiqr aglarptypd fieyertadr irsyqsnlia
      121 gllqtpeyar evisaapsfl khedvealie armkrqeild rpdaprlcvi eseaalriev
      181 ggrgvmrrql ehletmaghp svevqvipne agahigltgs fvllafpspw fpdvvcleqr
      241 tgtvflehpd daaeyahife slrstalspk dsldmiarvr qel
//
LOCUS       WP_181810820             339 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            ipomoeae].
ACCESSION   WP_181810820
VERSION     WP_181810820.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     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=36552
     Region          2..305
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mvigatgqig rvavgalard gwevtavsrg gdrdknwpeg vrvaradrad daalsaaigd
       61 gcdvlvdmva ygpeharqlt glaervgsav vissisvyed dkgrnfdtqa epdgfpeypv
      121 pltesqrtvr pgeasystrk aglerellaa gerlpttlvr agaihgphcr tprelyfvkr
      181 nldgrrrrvi ayggesrfhp asvhniaeli rlaaarpgtr alnavdpdap kvteiaaaid
      241 avmgvrtenv lvdgpppvpa vgdtpwsvpa pvvcdmsaae relgyrpvva wyaetlpetv
      301 awierqlagg rdwreaypkm fqtygdlfdy aaedawlks
//
LOCUS       WP_181811075            1017 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces ipomoeae].
ACCESSION   WP_181811075
VERSION     WP_181811075.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1017)
  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 1017)
  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 1017)
  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 1017)
  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..1017
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..1017
                     /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=108788
     Region          291..972
                     /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 msprpssapt lsptprtakp lpgvllpggp sperggaslr aqlvlallca ayavgaafgw
       61 gneqvalvmg dfglsaaaat aavscfryar srrsrfrpaw llfalssama algngvwgwy
      121 evvlerpvpn psyadlfflc fappaivgll vlakrpvtqa gwvclaldaw liggslvtls
      181 wslalaqtaq lddsdtahta lslayplldi alvsmvlalh frrssmhrsa vntaigalal
      241 tvmcdalfas pllhnsyrsg qlldagwfag slllayapwa gqrhgqpeee qharvvhehi
      301 pgqrhdadgh rhdadghrhd gphgghvhvp lqggghsryp vtrpiagsla altpylaaav
      361 ctlgilynvl ngrsvdrvvl itactvvlal vvrqgimlld nitltqelaq kenhfrslvq
      421 gssdvimiaa psgilryvsp aaagvygrpa eelvgkelas iihpedlgcv vhevrrflaa
      481 spaeepttri ecrfksgdgg wlnvestvnr hhgglifnsr dvtervrlqa qlqhnaehdp
      541 ltdlpnralf tkrvqqalsg rrssdrgial rntavlfidl dgfkavndti ghqagdellv
      601 qaarrlqesv rqgdtaarlg gdefaalivg dgsrdraare qhifeladrl rvtlsqpyti
      661 dgndvrvaas igvafaeagl gagellrnad lamyrakasg kgrvelyqpq mqqdvvrkae
      721 latrlraalh dggflllhqp vveletgris svatearwrs sqgvlftpae flrvsedndk
      781 taelgrwmle qavehaserl vnglhvpvsv rmsarrlldr slppgsletl ltrhglpsgs
      841 lvielsdtev kgslddlerr lsqlrrlgvr valdglgsgq aaitalrrlp vdvlkldrsl
      901 vegvvestrl hkitsgllri agdlglesva egvdlpeqvv alramgcthg qgaafsgpld
      961 eyrlrralst gnypvprgpa epafagggag vytsgvpavy gggsalrshn etpvppt
//
LOCUS       WP_181811054             355 aa            linear   BCT 28-DEC-2024
DEFINITION  oligopeptide/dipeptide ABC transporter ATP-binding protein
            [Streptomyces ipomoeae].
ACCESSION   WP_181811054
VERSION     WP_181811054.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            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  :: HMM
            Evidence Accession :: TIGR01727.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..355
                     /product="oligopeptide/dipeptide ABC transporter
                     ATP-binding protein"
                     /GO_component="GO:0009898 - cytoplasmic side of plasma
                     membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015440 - ABC-type peptide transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38216
     Region          14..315
                     /region_name="AppF"
                     /note="ABC-type oligopeptide transport system, ATPase
                     component [Amino acid transport and metabolism]; COG4608"
                     /db_xref="CDD:443658"
ORIGIN      
        1 mevsdahvvh rartgglftr drvyaltgad lfiapgetvg vvgesgcgks tlakvlvgve
       61 rptagtvsfr grdlwsmspa errvtvgsgt gmifqdpsta lnrrlsirri lrdpldvhrr
      121 gtsaeredrv relmslvglp pvlaealpgq lsggqrqrva iaralaldpd lvvadeptsa
      181 ldvsvraqil nllldlrerl glalvfvshd iqtvrrmsdr vitmylgriv eespadsvtd
      241 rarhpytral fsatpglldp iepiplvgpv psatrppsgc pfrtrcwkad gvcaekmpdf
      301 saasapghrf rchhpvqete strdlvaeaa tasasvspat amavedrtdr avrdt
//
LOCUS       WP_181811072             432 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Streptomyces ipomoeae].
ACCESSION   WP_181811072
VERSION     WP_181811072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces ipomoeae
  ORGANISM  Streptomyces ipomoeae
            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..432
                     /organism="Streptomyces ipomoeae"
                     /db_xref="taxon:103232"
     Protein         1..432
                     /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=47174
     Region          5..431
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 msdfdvivvg ggfagvttar dlsqaglsvl vleardrlgg rtfyreftgr dkklefggtw
       61 isaqhqkfvg aeldrygipt fqspvperfg wgvngevahk pfpipaeewv dferalahii
      121 aqasrlrfge eplgqdgled ldvpfqqfvd amnlppttrd filawpafyf gaypdqlsal
      181 hvlswvtgfg nsavawftml tdkiadgtkn lvdriigdcd aevrlstpve svteesdgvr
      241 vvtrtgealt araiviatpi ntwgsmtftp alegshlrma qekqagqsvk iwaltrgvda
      301 nffgvgwhtt ikwlateytt degaylvgfa saaadldphd qaavtravqe flpeaevlav
      361 dahdwnadef sqgtwmayrp gqviahskal qeprgrmyfa nsdlasgwag widgaiesgg
      421 raadavlkll rq
//
LOCUS       WP_181811392             607 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF885 domain-containing protein [Shewanella putrefaciens].
ACCESSION   WP_181811392
VERSION     WP_181811392.1
KEYWORDS    RefSeq.
SOURCE      Shewanella putrefaciens
  ORGANISM  Shewanella putrefaciens
            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..607
                     /organism="Shewanella putrefaciens"
                     /db_xref="taxon:24"
     Protein         1..607
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=68559
     Region          35..602
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mktvlkrigl gslilvlllv glaahewyak kpfffrafld rsvvkmafes petltslgfl
       61 esfgvtghna llddgspeal dkvftkvrel retllsyqdd dlddnqrisk dialyladfa
      121 lasepyryhn yplnqlfgvq ngypsfmqaq hqvnsvgdge nylsrlqqvk tkfsqtlegl
      181 kirenkgivp pkfviervlt emnafvrapv senilyssfk tklaetdiaa geqerllaga
      241 etnikefvyp ayqlfidyft elqtkagtnd gywalpdgdv ayeqllkfft ttnysadeih
      301 akglaevsri qseimtilad egydveqgfs vaiealaadp kfyyedsdag raqilvdyqs
      361 ildeinagld gafrirpeag mevvripefk ektapgayyq qpaidgsrpg rfyanlydik
      421 atpkygmrtl ayhegipghh fqiavamele gvplirkmap ftayiegwal yserlawelg
      481 fqkdpfdnig rlqaelfrav rlvvdtgihh srwtreqaid ymkkntgmsd rdvtaeiery
      541 ivmpgqatay kvgmmkilel rekaklalgd kfdlrdfhdv vlkngavpld ildklvnryi
      601 aeiqskk
//
LOCUS       WP_181808892             441 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase, partial [Streptomyces shenzhenensis].
ACCESSION   WP_181808892
VERSION     WP_181808892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 441)
  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 441)
  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 441)
  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 441)
  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..441
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     Protein         1..>441
                     /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          1..29
                     /region_name="Docking"
                     /note="Erythronolide synthase docking domain; pfam08990"
                     /db_xref="CDD:462650"
     Region          31..>441
                     /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 medtriieyl krvtadlhra rarllelesg rqepvaivsg acrfpggids pedlwravve
       61 erdlisampa drgwdvdely dpdpdavghi yvkeggflrd aagfdaalfg ipprealsmd
      121 pqqrlllett wetferagld plglagsrtg vfigilshdh gtrltpapeg fegmigagta
      181 gsiasgrlsy vfglegpalt idtacssslv alhlavqslr ggecdlavag gatvmstves
      241 fvefsrqrgl apdarikafd daadgsswse gvgtllverl sdarrnghpv lavirgtavn
      301 qdgasnglta pngrsqarll rtaldnahlt padvdvveah gtgtrlgdpi eaqallttyg
      361 qnrtsplhlg svktnightq aaagvagvlk miwamregll prslhlsrpt sqvdwsegdi
      421 rlldralpwp etdrprragv s
//
LOCUS       WP_181811536             279 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Yersinia pseudotuberculosis].
ACCESSION   WP_181811536
VERSION     WP_181811536.1
KEYWORDS    RefSeq.
SOURCE      Yersinia pseudotuberculosis
  ORGANISM  Yersinia pseudotuberculosis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
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="Yersinia pseudotuberculosis"
                     /db_xref="taxon:633"
     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=31458
     Region          1..278
                     /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 mdiqvffvsy lifgamvgtf lnvliyrlpi mltnlssrse shgeeikmrs hlrninlfqp
       61 gsfchhcnes ipikynipil gwiflrgasr ccnkkistry lfievlaviq tllvlmifke
      121 dllictslvl iwsltalafi dfdtyllpdc mtipllwlgl linidtvfap ltsavlgavs
      181 gylflwlsyw lfkivrgidg mgygdfklma algawfgvsa vpflilfssf fglvayaify
      241 ffdkkdngke inyiafgpyi slagvlylfl gshvtnlfs
//
LOCUS       WP_181812646             284 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Lactiplantibacillus
            plantarum].
ACCESSION   WP_181812646
VERSION     WP_181812646.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..284
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         <1..284
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          28..267
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 lkeadlfcpn svrinftiyl mptaesqrdr llnllltehq ggtfadqfae qhvqlptamv
       61 lircepladq apmilqqrlq ylmmprfkqv lvstyqqqcm alipislvay nqnqfkltlk
      121 qitkqadcrl ivsqhyvnpe dtfaaytvce rtaqlkagrg rvifcedqfy nlalarvnhl
      181 eilpffinpa lclllaydqq nhtelvptld vylratcnlt rtakqlyvhp ntlrnrlhhi
      241 ttltgcdlrd aetcfklaas fklrqfltqh qyqyrpdipi ptqd
//
LOCUS       WP_181811661             384 aa            linear   BCT 28-DEC-2024
DEFINITION  CMD domain-containing protein [Escherichia fergusonii].
ACCESSION   WP_181811661
VERSION     WP_181811661.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            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 10008969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..384
                     /product="CMD domain-containing protein"
                     /calculated_mol_wt=42928
     Region          <67..197
                     /region_name="YciW1"
                     /note="N-terminal domain of uncharacterized protein YciW
                     (function unknown) [Function unknown]; COG4950"
                     /db_xref="CDD:443977"
     Region          214..382
                     /region_name="ahpD_dom"
                     /note="alkylhydroperoxidase AhpD family core domain;
                     cl00460"
                     /db_xref="CDD:469777"
ORIGIN      
        1 meqrritgks hwyhetqsst sphdplplvp eaanctdkfl ldlalseneq mpfqawlsps
       61 rqlanqlfpq aitlsklhsf slyermstal tvaqvcgvqr mcnhyaarla plpgpdssre
      121 snhrlaqitq yarqlasspa vintrsrqql ndvglsekdm liinliigfv gfqarviaaf
      181 qaylsqparw lpgqdtqqfa dtslfqqqht rwrsafplvd esnasqqqld slascadipe
      241 lrhlapvlar epelltlsrq ivnalallfp aspladftal lvsringsvd cfnsritlse
      301 lsefrsvlra dekeikhwin grlelrnglq aiqlltiapd rfstdqfell chqelssana
      361 ihvlaccgly gwinrlkigl gety
//
LOCUS       WP_181811538             472 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Yersinia pseudotuberculosis].
ACCESSION   WP_181811538
VERSION     WP_181811538.1
KEYWORDS    RefSeq.
SOURCE      Yersinia pseudotuberculosis
  ORGANISM  Yersinia pseudotuberculosis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 472)
  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 472)
  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 10106964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Yersinia pseudotuberculosis"
                     /db_xref="taxon:633"
     Protein         1..472
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=51764
     Region          96..266
                     /region_name="vWA_subgroup"
                     /note="VWA subgroup: 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...; cd01465"
                     /db_xref="CDD:238742"
     Site            order(103,105,107,175,201)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238742"
ORIGIN      
        1 mllkpailik tdmlikpdil ikpatlikqt arikqmtlll llflfslfgv akaatqvvnv
       61 kselaapvml ansedknylk isltgfnlds trrspinlal vidrstsmsg eriekareaa
      121 ilavnmlnit dtlsvvaydn haeviipatk vtdkpalias iqqhihprgm talfagvsmg
      181 igqvdkhlnr eqvnriilis dgqantgpts iselsdlarm aakkgiaitt iglgqdyned
      241 lmtaiagysd gnhtfvansa dlekaftkef qdvmsvvaqd ivvqiktgdk vkpvrllgrd
      301 gdilgntvnv klnqlysnqe kyillevipe kgtdkqqkdl advsisylnl sskkqdqine
      361 rvtvsysqsv ekvndavqee vlaeseiqkt alandeaikl idagrkdeak kvlesnaskl
      421 dsmsfsspva ekkvrestnk qrkladdids kdaatyrkel keqnynvkqq qk
//
LOCUS       WP_181812632             290 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Lactiplantibacillus
            plantarum].
ACCESSION   WP_181812632
VERSION     WP_181812632.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 290)
  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..290
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..290
                     /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=32446
     Region          12..262
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mrgrielrpl qviqisdlhl tprgqvpahg qqydpwgkla niiddirrlp tmpdlivftg
       61 dlihdgsadd yqrlhaivht meaefdchvr vilgnhdrra afyegylpad pgpyyasrmr
      121 ignndfyfld skvsgyeagw lapqqlqwlg khlrqaptkr aflflhhpld gpamtnmhya
      181 ilqntpalls vlrghnlggv fsghvhfvss yligdnilnv vagsaayaid chdphhhyvh
      241 egssyqiiti drgqvgvttr qllhgkavid eltipdtkfv grapqgyesr
//
LOCUS       WP_181812865             385 aa            linear   BCT 28-DEC-2024
DEFINITION  CMD domain-containing protein [Klebsiella pneumoniae].
ACCESSION   WP_181812865
VERSION     WP_181812865.1
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 11471826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..385
                     /product="CMD domain-containing protein"
                     /calculated_mol_wt=42902
     Region          31..196
                     /region_name="YciW1"
                     /note="N-terminal domain of uncharacterized protein YciW
                     (function unknown) [Function unknown]; COG4950"
                     /db_xref="CDD:443977"
     Region          251..379
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 meprrvngkn hwyhetqsti cpvdvlplvp eaahvedrfl ldltlpaawl rahadwlhpa
       61 rqlaellfpd qvavsrlqtf taydrlstal tvaqvygvqr lcnhyaarla plpgpdssre
      121 snrrlaqitq farqlagsps vindlsrsql devgltsrdi ilfnqiigfv gfqaraiavl
      181 qaaqgfpvrw ipgmpqqeea paelfapppg awqadiadpd lqyadderqr riagwqslpg
      241 lgelapllac dpqlfaplet lirqlstddt fgpqvallta rtngsptcfd awlphwqgee
      301 efashlregd qalhhwlqqh pqarslvtav qlltrspdrf saaqltplae yrlseqqaid
      361 lliwsglcgw mnrlkialgn vrqqt
//
LOCUS       WP_181813020             456 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Klebsiella pneumoniae].
ACCESSION   WP_181813020
VERSION     WP_181813020.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..456
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..456
                     /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=48660
     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..158,161,265,268..269,272..274,277,304,308,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mnhtnvvdvk awidarpvsr fqwnvlllcf iiimldgyda avmgfvapal iedwgisrae
       61 mgpilgaamf gvaigalvag plsdrygrkr illwsvalfa lfslagavaq spsqlalmrf
      121 ltglglgavm pncvtlvaey mperrkgvmi tlmysgfnvg sglggfiaag llshyswhsa
      181 lvfggvlplm vlpfmivmlp esamnmvarr lpgeqiaral nrlggqftae tvfqlnappi
      241 trsskvaqlf rhgyargtia lwltyfmglf viyllngwlp tilrsgglsl qqaammtglf
      301 qlggplggil vgmlmdrasa kaviaatyfl gclcllsqgv mdfgsaalsv lifisgmcin
      361 gaqnglqays payyqteira tgvswmhgig rtgailsstl ggmlmlavpg hssiflvlal
      421 paclagicil lhrmnhakpr lteaeldals splehr
//
LOCUS       WP_181812756             392 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Escherichia fergusonii].
ACCESSION   WP_181812756
VERSION     WP_181812756.1
KEYWORDS    RefSeq.
SOURCE      Escherichia fergusonii
  ORGANISM  Escherichia fergusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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 392)
  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..392
                     /organism="Escherichia fergusonii"
                     /db_xref="taxon:564"
     Protein         1..392
                     /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=45647
     Region          5..383
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maisdtklrt iygkpysgpq evadadglsv rispkgviqf qyryrwhgkp nrlglgryps
       61 lslkdarqit adlrklyfsg tdprtyfeek vensmtvaqc ldywfdnyvs ttlrektqal
      121 yrstvmkrmh dafpnrpass itvkqwvdll teeerdnprr arqvlsqlrs aiswcmrrql
      181 idscaimsiq prdfgsraev gdrvlsyhel akiwlaiers rastsnkllh qmlmlwgarl
      241 selrlakkte fdllenvwtv pkehskmgnv irrpifeqik pflekamtty ndvlfpgedi
      301 nkpisiaaan rfvnrirggm dlgywrthdf rrtlvtrlse mnvephvter mlghelggim
      361 siynkhdwie aqrkayelha dklfwhirsi sd
//
LOCUS       WP_181813033             249 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Klebsiella
            pneumoniae].
ACCESSION   WP_181813033
VERSION     WP_181813033.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae 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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=27190
     Region          24..248
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 markiivvta aygndhvksl ggqaavmpfi anagadgvei rrelcsaeel nalpslaati
       61 erhgllacys apqalftdng elnpdlptll aeaqtlnalw lklslghflh nqqldelrdi
      121 lsdsgmalvv endqtdcgql apmqrfkatc rvhqlpitlt fdmgnwlwvg dspeeaarhl
      181 apavsyihvk aaephhekfr avppdqaaer wlalldnlpa daprgiefpl tghdltavtr
      241 ryvnllred
//
LOCUS       WP_181813193             551 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Klebsiella pneumoniae].
ACCESSION   WP_181813193
VERSION     WP_181813193.1
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=58060
     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 mlspalaagt llaftlaiee fgvpaalgsr agvvmltvgi ekkladwpvd
      241 lpgaallsll lmavalfaww lqrrlvgeke vtsvtgkpge nhgaslgwmm 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 iwpqfeqgsv gqgmamaslt lltglvlmlt
      541 alalmqrrtc g
//
LOCUS       WP_181813262             459 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein [Gaiella
            occulta].
ACCESSION   WP_181813262
VERSION     WP_181813262.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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..459
                     /organism="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..459
                     /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=49118
     Region          12..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 mtlrldvpre laleraaeiv aeawrsfdqa rpteppider lralldaalp eapssalevl
       61 edarrtldet iaqtrprffa fvassgleig vlgdllascf danlavwaaa aseveeqavr
      121 wvaefvgfpa gagaftsggt isnmtalaaa reraipgars rglggveaal ycsqeahysi
      181 ersaellgig aanvralpid eqrrlipeav aeaiaadraa grlpvavvat agttltgavd
      241 pigaladvca eqgvwlhvdg ayglpaattp saghlfqgld radsvtldah kwlylpkacg
      301 vllvrrrgdl aqafsheeay iphersghmv ditleysrpf ralklwlafr ahgaqafrda
      361 veenlrqarl lyelveahea lepmcgpppl sivpfrhvaa agdlnehnaa lvralqddgr
      421 vwvapatvds kvclrpcfvn frtsdddvra lvdlavelg
//
LOCUS       WP_181813305             301 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Gaiella occulta].
ACCESSION   WP_181813305
VERSION     WP_181813305.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..301
                     /organism="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..301
                     /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=30169
     Region          24..283
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 msvrsfttaa tlddalaama agarpvaggt dlvvgarqgk aplpesivai hrlaelhgie
       61 eagaglrlga lvrhaeivss glvrerfsal adasaivgsh atraqgtigg nlmnaspame
      121 tggplmcfga tatlrsaage rivpveqlfa gpgrtiaeag ellvavavpa qpagtgscyv
      181 rleyrrqmei avvgatavva ldggrvthar iaitalapti rrvpdaeaal agsdggraaa
      241 eaaaqaaaqa aspisdvras eryrramaav itrrailaav arargehvpv pasptlhggl
      301 s
//
LOCUS       WP_181813350             347 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Gaiella occulta].
ACCESSION   WP_181813350
VERSION     WP_181813350.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Gaiella occulta"
                     /db_xref="taxon:1002870"
     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=36560
     Region          1..342
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 midlrsdtvt rptdamraai aaaavgdeqq redptvnllq eraatllghe ralflptatm
       61 anqialrlhg rpgdvlvaee lshvlvyefg gaalhaglvt vglrgsygri rgeqvrsvaa
      121 rsaydvdqrp avlaledthn saggtvwpld elddvvaaar eagmavhldg arllnaavaq
      181 glapseiarr cdtvtlclsk glgcplgavl agsealiera wrekhlfgga mrqagivaaa
      241 glhaldhhvd rladdnarar rlaeawhaag vpidlesvqt nfvqidlapl glgrdealer
      301 vraagvalsa tihetrvrav thldvddddv eraiacvpaa lgarasr
//
LOCUS       WP_181813377              98 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Gaiella occulta].
ACCESSION   WP_181813377
VERSION     WP_181813377.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
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="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..98
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11153
     Region          12..73
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     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 makrraysnd glgptierlm aetgltyral aektklsagy lnhivhgnrp vpsnevleri
       61 akafdvkaeh freyrirait dkleqmpeli drlykrlg
//
LOCUS       WP_181813469             325 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Gaiella occulta].
ACCESSION   WP_181813469
VERSION     WP_181813469.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
REFERENCE   1  (residues 1 to 325)
  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..325
                     /organism="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..325
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34472
     Region          3..297
                     /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 mlaaaqplag tlvaeltryl pgayagrela rlgarvvrme apdgdpmrrs apawdralrr
       61 gkesvvcdlk tdaafaralc aradvvlegf rpgvaarlgv gpedvparvv ycsitgfgst
      121 gphaaraghd lnylgwagal edtapasppl qiadlaagal gavteilaal vrrartgega
      181 rieismthra hdlvehrlgg dpvprmltgg lacyrvyeaa dgrhltvaal epkffirlce
      241 lagrpelagr qfdddqerla gelaalfasr plaewlalfd redvcagpvw traeaadvfg
      301 srdaadedva lgahteawrg eldlp
//
LOCUS       WP_181813472             304 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Gaiella occulta].
ACCESSION   WP_181813472
VERSION     WP_181813472.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Gaiella occulta"
                     /db_xref="taxon:1002870"
     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=31377
     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 mtssvflvnp asanggtgrr wpqiahaaaa aglegdalfs erpghlgela rsaalagadl
       61 lvvvggdgsv nevanglvgl ahapelavvp rgtgwdfvrt fgiprdveqa vavalhgavr
      121 tidlgrvsyr awdghdaeav fanvasagms gavaqranda tkalggkasy lwatfavfag
      181 wsavetrvsv dgatragrmf dvvvangkyf gggmkmcpea epddglldvv aigdvtkrdl
      241 vltmpkiyrg thlphpkaea lrgrvvtvet depvpveldg eqpgttparf eallgalrlr
      301 vpaa
//
LOCUS       WP_181813445             258 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Gaiella occulta].
ACCESSION   WP_181813445
VERSION     WP_181813445.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
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="Gaiella occulta"
                     /db_xref="taxon:1002870"
     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=27114
     Region          1..249
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mqrvavvtga ssgigeatar alaaqgwlcv lvarreerlr alageiggev elcdvaerpd
       61 veataarvle rhpaihllvn nagmpargtf lqvdpdlver vmhvnylggv wcarafmpgl
      121 eaaarqggah vvnlvsvagt vsfapagaya askhaqlafs rslaaalrgs ginvhavlpg
      181 fvetegfpqk nvlasrllra fviepddvar aivravarnr getvvpwfpy rligiaqalv
      241 pgivarfvgm sgyrkgsi
//
LOCUS       WP_181813473             352 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Gaiella occulta].
ACCESSION   WP_181813473
VERSION     WP_181813473.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
REFERENCE   1  (residues 1 to 352)
  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 352)
  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..352
                     /organism="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..352
                     /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=37388
     Region          12..314
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mhvdlreswa igpvevptrl vlapmagvsv qafrrqgrrf gaglvcsemv scagiehrne
       61 ktlgylrvaa dehplaiqif gsdpaamgea armveaagad ivdinfgcpv rkvtktgaga
      121 tllddpelac rivaavadav eipvsvkmrr glrdgswdcl svgprlveag arsltlhprs
      181 aqqmytgsad hrltaelvdl vdvpviasgd itsrakaqav lattgaaavm vgrgaqgnpw
      241 alreivdgdg geptreevva elvlfiretv relgerrasg flkkfygwyl grgrfprpfk
      301 qelvvldatg everrllaaa pgalalidel eaglphgdei tlelpisiyg gg
//
LOCUS       WP_181813499             358 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Gaiella occulta].
ACCESSION   WP_181813499
VERSION     WP_181813499.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
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="Gaiella occulta"
                     /db_xref="taxon:1002870"
     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=39829
     Region          60..345
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mrrkacivrr gsswavkqpl phgryrwqtv gsrkrdaell rdeinrrial gaayparaqt
       61 fgeftatwle ryaqrvrpat laschgslkh lsvfdgwqle tiraadvedh vfavargapr
      121 saelmldtlk milraakerg qvideaalrv rpprrersem rflgwpqvdd lasetvepfg
      181 nlirfacltg lrqgelfalr ertidlaagr llveagareg kivptktsag rrnvhfsara
      241 llvlrkqlea rtnnelglvf ptpggavwrk dnfmarifrp avaraglapl rfhdlrhtya
      301 almvaagahp kllqaqlght sinvtlntyg hlfpdafadv gdaldrlvrg qanratgt
//
LOCUS       WP_181813517             356 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Gaiella occulta].
ACCESSION   WP_181813517
VERSION     WP_181813517.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
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="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..356
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39095
     Region          6..194
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 maptstplvs vlvtardner hvgaaltsvl rqtltslell vvddgsadat paiveslrde
       61 rlrfvrfpes rgisarrnel lerargryva pldaddvwlp drlerhvrll esrpdlvavg
      121 sdvlvvddgv gvgryfrlpr sdaairwncl ftsplihsas tirasafhdg vrydpaypla
      181 qdydlwtkll rrgrsenlav pltlyrvhsa qasqrracer raeqeriglr aiedpagghg
      241 ptgdrarlaw clgaamavad eeledaiday relfariesa yrgtsglrea rriaattllr
      301 raglaadaaa walrraalai drrvtvsava vraaniaagr ryrrpaarll adlaea
//
LOCUS       WP_181813505             388 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Gaiella occulta].
ACCESSION   WP_181813505
VERSION     WP_181813505.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
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   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 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   4  (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   5  (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   6  (residues 1 to 388)
  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 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 11447491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Gaiella occulta"
                     /db_xref="taxon:1002870"
     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=42810
     Region          18..376
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 mvernpftfg slacgdafvd redelralts dlrggrdvll laprrygkss lalravqeaa
       61 regilvatcd ltrtptkerf aaalaktidd dlasppgqpr draaglfrgl pvrptieldp
      121 ddgalsfsfr ashadgaidg tierllelpg riaaererqv ailfdefqei valdprlpdl
      181 mrsvfqaqpd vahvyvgsrr harhaifddr dgalwrgarr melgrlphdt laghlrsrfa
      241 atardaddea vsrileitdg hpyatqelaf ftwahvprgh aaraadveag lvdvlraehn
      301 nlarlwdaat rnerlvllal ragaqslyae etreraglpa ptfvqravts lvredviekg
      361 pdgryrlaep flaewlerka strlegda
//
LOCUS       WP_181813628             377 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Gaiella occulta].
ACCESSION   WP_181813628
VERSION     WP_181813628.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Gaiella occulta"
                     /db_xref="taxon:1002870"
     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=39930
     Region          34..371
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mipywlseah epppavaldg ppdvvvvgag vtgcaaalrl ahagmrvrlc darevaggas
       61 grnggfalrg apapfdvtaa svgeesarai wawseraidr ieelagdafr rvgslrlavd
      121 eeerdelrse ydalvgagfa aewlddlapp lagrftaair hvpdgvlqpa rwvrrlarla
      181 aeagveireh arvtsldele gatvvvcsdg ypsgllgpie gliiptrgqv iatepiperl
      241 fqvphygrhg fdywhqaedg rvvaggfrdv slfseftade httdvvqdal ssfvnglvgr
      301 elrvdyrwag ifglvmdflp vvgavpgldr vwvaggysgh gnvlglacge lvaravaged
      361 dpllplfdpg rllgaga
//
LOCUS       WP_181813600             530 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Gaiella occulta].
ACCESSION   WP_181813600
VERSION     WP_181813600.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
REFERENCE   1  (residues 1 to 530)
  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 530)
  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 530)
  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 530)
  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..530
                     /organism="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..530
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=57096
     Region          1..470
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 msatplfaag elvsvdpatl revgrvvate peaigeivae armaqerwar epfeqrsrvl
       61 rgvarallda geeiaetiva etgkpiveay tselfvcldn liwlashlgr vlrpervpmp
      121 qlhvrhksas lryepagvig iisawnfplg vpltqaatav aagnaavvkp seltpltgaw
      181 veelfrraga paglvrivqg pgetagdaiv rqrgihrvvf tgssdagrav arraaerlcp
      241 vtlelggkdp mlvlddadle ravegalwas fsncgqvcsg veriyvdasl yepfvarlge
      301 raralrigrg sdprtdlgpl vtemqrarve elvadaverg aavvsgggrp plglpgwfle
      361 ptvlaevpad arvhaeeifg pvvivasmen esdgirrana srfglgasvw trdrqrgrrv
      421 aeqleagsvw mndhaysyga cqapwggrke sgygrthskh glyemsqvky tdadrgrltp
      481 pwwypyseev vdgfrgalga lygdgvrgra aalvahrhgl valgrralrr
//
LOCUS       WP_181813689             250 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Gaiella occulta].
ACCESSION   WP_181813689
VERSION     WP_181813689.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
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="Gaiella occulta"
                     /db_xref="taxon:1002870"
     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=25428
     Region          14..247
                     /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 mnvalaalvl ppalafgsfa nvvaarvplr rsvskprssc tacgtpivar dnipivsyll
       61 lrgrcrscha risplypave altaglvaag vlvygptaya alasfflvvl vtlsaadlry
      121 rlvpnrivip aaaialvaht aidpsvewla aalgasgfll vaalvhpqgl gmgdvklall
      181 lgamlgrnvt valmagflaa lvpslvllar hgsgarrmai plvpflalga vaalfwgdal
      241 ldaylglggg
//
LOCUS       WP_181813734             234 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Gaiella occulta].
ACCESSION   WP_181813734
VERSION     WP_181813734.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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..234
                     /organism="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..234
                     /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=25745
     Region          8..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 malydpiaai ydpwsrsvte digfyvdeav asggpvvela vgtgriavpv aeagvrvigi
       61 dqsggmlela rtyarergve alldlrlgdl reppvdervp lvvcpfrsll hmrdeteklr
      121 alsaarallr pggrlvfdvf spspadiaet dglwlereeg iferadwdeg srtltlsvrg
      181 geaaatmtlh wlsalewrrl ldeagfdvvg lygwfdrrph dggedsiwvc rrrg
//
LOCUS       WP_181813796             393 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Gordonibacter pamelaeae].
ACCESSION   WP_181813796
VERSION     WP_181813796.1
KEYWORDS    RefSeq.
SOURCE      Gordonibacter pamelaeae
  ORGANISM  Gordonibacter pamelaeae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Gordonibacter.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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..393
                     /organism="Gordonibacter pamelaeae"
                     /db_xref="taxon:471189"
     Protein         1..393
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44941
     Region          21..197
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msilwdisra clyekrgaiv pkvsviipcy nqekyletcl nsvlsqslsd ievlcvddgs
       61 tdgtgdilaq yaarddrlhl lsqknkgasf crnraidqar geylifcdsd diypdtaiie
      121 rlycagvehd akavagsysi fdetdnevry dfdgllwgqs fkregfvsfl dyqfdygftr
      181 fmfrsreikn sgirfapysr fedppflval lgylemfyai pdvvyqarvg ykqvvwdssa
      241 qvdllkglsd nlrysrihrl knlheltvrr ieeeyagvfy wslidemvfs aivrangevs
      301 pellsssfqg rvvdgflllk pmeqqvanaq kwnkdiqdlh gavlaeradk enawerlkda
      361 grelaavyds ttwrigsvft avprwfrdfg rkv
//
LOCUS       WP_181813821             338 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Gordonibacter
            pamelaeae].
ACCESSION   WP_181813821
VERSION     WP_181813821.1
KEYWORDS    RefSeq.
SOURCE      Gordonibacter pamelaeae
  ORGANISM  Gordonibacter pamelaeae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Gordonibacter.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Rosinski,J.A. 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 338)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..338
                     /organism="Gordonibacter pamelaeae"
                     /db_xref="taxon:471189"
     Protein         1..338
                     /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=36804
     Region          85..336
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mrnpsenfkn raetareadt gidtlfepqi rqlggvlida aahgrqgllw lidpavgkgs
       61 fwyfpigdrl avgafdfalr eeggffcdaa dcfyfgsysh emlpylgiep tlpgrtvlgh
      121 awkhapyhqr vqggarlset fvallpealr dvslrlhcdp vvlssaiaal dgtscpaglp
      181 sllddmrrar psavvaeafy eskvveacal ivdwrlaygr apvalsaddv aavaaaqrli
      241 qqdlahpvtt eelcravcvg tsklielfrl scgmtpqeya rdvrmhhace llettdlsla
      301 aiaacvgysr qgsfseafra rcglsprewr anaralhr
//
LOCUS       WP_181813826             408 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Gordonibacter pamelaeae].
ACCESSION   WP_181813826
VERSION     WP_181813826.1
KEYWORDS    RefSeq.
SOURCE      Gordonibacter pamelaeae
  ORGANISM  Gordonibacter pamelaeae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Gordonibacter.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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 408)
  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 408)
  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..408
                     /organism="Gordonibacter pamelaeae"
                     /db_xref="taxon:471189"
     Protein         1..408
                     /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=45340
     Region          <12..401
                     /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 mrssaaaara avcvdidnfk lindvdgyer gdevlrelaa ilcdeagrdg iaarlsadnf
       61 llllpyarce ealdacrrva erargivgng kplslhiglc csedapdard vnelmdrari
      121 aqnesrkrgi tpcayskpmr dallrradle rsmegalaqg effhlvqpky dvagtcvlgg
      181 ealvrwrrpd egivgpdefi plfeqngfil rldefvfesv crdlrarlda glpvvpisvn
      241 vsrlhlhrpd flptyvrikd eygipdglce leltesivie dlhgvfgime gmrragfrca
      301 iddfgsgqss lnvlkdlpad vlkldrefll esslpgteet vvrfvitmar elrmetvmeg
      361 vetpkqlafl rttecdmvqg fvfsrpvppe efyrlletga pdegafrd
//
LOCUS       WP_181813930             436 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Photobacterium damselae].
ACCESSION   WP_181813930
VERSION     WP_181813930.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium damselae
  ORGANISM  Photobacterium damselae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
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="Photobacterium damselae"
                     /db_xref="taxon:38293"
     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=48609
     Region          <206..434
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mffaktdnla ssstykvlly fiacvamifm lfihqvfvss eafyhkqler eltseastfs
       61 llvsvgdink iyrlieersr asktffyriq krsgsktsin ypvlltsady yhegnkrtev
      121 vvrlsstekl iiginpnllr syrdtvtpil lsgiaipvil mlagatlfsl silkklarvn
      181 qgmsrvisge kgvklpessn ddefnlltkk lnflieqvek nesslkdlsv gmahdlrtpi
      241 ariklrlekv laanpqpytn eleachddle tllnmfngll eisrlnsgkq dvhkeiahld
      301 viaqdavefl tplaeekqqe lifrvdssfe lsgepsllfr avynlvenai kytpkkgtit
      361 vvvdpfglvv vdtgmgvssk dklrikepmf radasrtkqg yglglslvda vvqshggelv
      421 fsdnkpglra rilfss
//
LOCUS       WP_181814009             115 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Stutzerimonas
            nitrititolerans].
ACCESSION   WP_181814009
VERSION     WP_181814009.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas nitrititolerans
  ORGANISM  Stutzerimonas nitrititolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..115
                     /organism="Stutzerimonas nitrititolerans"
                     /db_xref="taxon:2482751"
     Protein         1..115
                     /product="helix-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=12686
     Region          43..93
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mphsshrsar plppgsvpph rrlgsppspk aaedadgasr shylnndeaa dflrlsprtl
       61 ekqrvigggp rfrkfgrrvm yaladlqawa darcfettfd paylerhpgg arddr
//
LOCUS       WP_181814239             232 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Helicobacter canis].
ACCESSION   WP_181814239
VERSION     WP_181814239.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter canis
  ORGANISM  Helicobacter canis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..232
                     /organism="Helicobacter canis"
                     /db_xref="taxon:29419"
     Protein         1..232
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=26696
     Region          2..229
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mklynadsyt liaqmrenkl rvhhiitdpp yniskpnnfp smrqrrqgvd fgvwdkgfdl
       61 vswipqyvei ldkngsmivf csyrfislia qalessnmlv kdiliwqksn pmprnitrry
      121 vqdlefavwa vksgakwvfn kpsdmpylrs ifthslvsgk eklghptqks lklmkdliqi
      181 htnpneivld pfmgsgstga aclelgrefi giekdkkfft maqkrlesyn kd
//
LOCUS       WP_181814474            3757 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein [Leclercia adecarboxylata].
ACCESSION   WP_181814474
VERSION     WP_181814474.1
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 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3757
                     /organism="Leclercia adecarboxylata"
                     /db_xref="taxon:83655"
     Protein         1..3757
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=378763
     Region          257..1966
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          1978..3646
                     /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 mkprqytlnt gktritlqag qtnihkaapg etyrvlkrqg endqekladd vvasrhgqdl
       61 qldyadgtsl tlqdwftqsd tsvtlpadgt stqvmtpast egaaladgsh vfyahgspda
      121 lasmtsghpg ldhilsglqn gtagsghpmt ylpqshsyag ylagalglgg vvgvavasgh
      181 sggdnggkhd ngggepaven avqlnfvggp alssndlnve iyqadgktli gtgtlgpngs
      241 vtvsagsysg vvivklvnsg gaadyldeat gagkdlsaql wsmgvisgdn stlvlninvl
      301 ttlaytkaqe amggtpdspa tlnatqvadt saaisnllgv ddilnttvva tnggsydatd
      361 glsagekygl llaafsgaea nagastqtil dtvtagitlg sssslsdgvq sllikgaaaa
      421 tdtssglsli idthapvfss sstasvdeni gagqvvwtav atdpspftys lsttgdsalf
      481 sinaatgavt lsgnpdfesk asysftvvat daagnassqa vtlavnnlde vapvitsgtt
      541 ataidensga gqviytatat dtadisggvt fslkagsdtg ltidpvtgav tlsgnpdfer
      601 qasysftvva tdaagnhssq avtlginnld evapvitsgt iatainensg agqivytata
      661 tdtadisggv tfslqpgsda gltinpvtga vtltgnpdfe nkasysftvv atdaagnhss
      721 qavtlavnnl devapvitsg ttatainens gagqviytat atdtadisgg vtfslqpgsd
      781 agltinpitg avtltgnpdf eskasysftv vatdaagnhs sqavtlginn ldevaptits
      841 gttatainen sgagqviyta tatdnadisg gvtfslkags dagltidpvt gavtltgnpd
      901 fenkasysft vvatdaagnh ssqtvtlgin nldevaptit sgttataine nsgagqviyt
      961 atatdtadis ggvtfslkag sdagltidpv tgavtltgnp dfenkasysf tvvatdaagn
     1021 hssqvvtlav nnldevapti tsgttatain ensgagqviy tatatdnadi sggvtfslka
     1081 gsdagltidp vtgavtltgn pdfeskasys ftvvatdaag nhssqvvtla vnnldevapt
     1141 itsgttatai nensgagqvi ytatvtdnad isggvtfslq agsdagltin pvtgavtlsg
     1201 npdfeskasy sftvvatdaa gnhssqvvtl avnnldevap titsgttata idensgagqv
     1261 iytatatdta disggvtfsl kagsdaglti dpvtgavtls gnpdfeskas ysftvvatda
     1321 agnhssqvvt lginnldeva ptitsgitat aidensgagq viytatatdt adisggvtfs
     1381 lkagsdaglt idpvtgavil tgnpdfenka sysftvvatd aagnhssqav tlavnnldev
     1441 aptitssnia tainensgag qviytatatd nadisggvtf slkagsdagl tidpisgavt
     1501 ltgnpdfenk asysftvvat daagnhssqa vtlginnlde vaptitsgtt atainensga
     1561 gqviytatat dtadisggvt fslkagsdag ltidpvtgav tltgnpdfes kasysftvva
     1621 tdaagnhssq avtlginnld evapvitsgt iataidensg agqviytata tdtadisggv
     1681 tfslqpgsda gltidpvtga vtlsgnpdfe skvsysftvv atdaagnhss qtvtlavnnl
     1741 devaptitsg tiataidens gagqviytat atdnadisgg vtfslqpgsd agltidpitg
     1801 avtltgnpdf eskasysftv vatdaagnhs sqavtltvnn ldevaptits gttatainen
     1861 sgagqivyta tatdtadisg gvtfslqpgs dagltinpvt gavtltgnpd feskasysft
     1921 vvatdaagnh ssqavtlgin nfdevapsft tgnssdsyas atvnvaenta astaiytaqa
     1981 ndndaadgge hvtysladen gaadaqyfsi davtgavtfk snpdyegaha paytfavvat
     2041 daaghttrqt vtvnvtdvde iaptvtldgs stgpvmlnpa slntylngyd ttalgdgtfl
     2101 vtwasnnngn lgiyaqrlsa qgvamgdpvq lasgatytvm sssdsilsvt alndagayav
     2161 awigkdgtss yssiftqsfn adgtplsaaa qldgaasahd lapqiatlad ggyivswsis
     2221 sggiyvqrfd dtgvavgntv plavsgssgn aspqvsvldn gsyvvtwqgy ttgdyhiyvq
     2281 qfdatgngtt pvmldattgn snnyesqpqi taltnggyvv twsgynysgs nynsstyvqq
     2341 fdatgtrvgs iveldgssna nnggnytypy vaaladggya itwmeydnsn gyydykvyvq
     2401 qfsaggskvg davqldaphn stsndrdqfp ritalgdggy avtwmsigss nwdiyaqkfn
     2461 asgvavgdiv rleasggand lypqvtavga dgeymvtwyg yspgsgvsgy hlyvqkfnad
     2521 gstydnlvvl nhdgqatvqs tetgtvylvn dnvvvsqlsd itgaasdqwa staviantsa
     2581 sisaanladg tyhawavdaa gnlsvisgrs vvvdntvpvf tsattaadit dstvagdtvy
     2641 taaatdahgi tyslndtqhf rinastgvvt lisspgqssg aqfivtaida agnqttqtvt
     2701 ynvvdttppg vmlvsdadgv ensgemvivq sseagtvylv sdsvtvtdln sltnaadnlv
     2761 nsvavaanvg tvlalnglae gtyhayavda sgnvsaisgs svtvdntapv isggatangt
     2821 sltsgaaagt qvydanasda haitysldqd slawfdinaa tgvvtlnsaa vagsynlvvt
     2881 atdaagnhss qtvtvevapg nnldgipmvs gsttdtstem tvnvglekls ngytvveymr
     2941 qtggdnltgd ptgalydgvv rvldagnnvv ktldisipag ytlvdtqika langgfvvaw
     3001 sqvdalswtd fsvhyaiydn sgnlqssdtl aspgsgvtia aqssanggdf aiayqtmgpg
     3061 tdqqeaisvf hyngsgsnft pgtqtliggn dasqnfggva spavqlmkfq ltpgvltals
     3121 dgsyvlasev ydwigtpgqs atttpigafi fkldasgtlt sfdsgttwqr vnwndeqgsp
     3181 tnviafdggf avfsqeyrta twevtlynnn gtlittniqs ntvhnmgtqs yhavdvgamd
     3241 kethsglawy ingylaasat aydngtdlvf vfpdgsggls qvtiskttge ltsdvtdsgi
     3301 tvpqggqlyn privpdgagg yditysvlfd snpvdddrig yvvgdiyqig lnagpapvlp
     3361 tvtdahiait stpggadgmt ykvgdtvtav wdnsasgdan tsavtsvtmd fsqfggstsa
     3421 tayddgthgd aiagdgkfta qytvtagald hvagrnvavt vtaanhtstt tadstgltvd
     3481 stapvltsst pqdnggsiat ganltltfse dvlagsghit lvnesdssqn kviditdssq
     3541 vsisgntvti dpttdlaaga nyhvqidsta lhdtagndya gisssaglnf ttvsastvdp
     3601 sivvfdlttg qssdhngrvf dantaytiyi qvnssynstl agldsnemws gaqnlgaddk
     3661 ivlvgtgsdv qgrygdpvmt mrhggnsvnw lagfsisfss ynvagvdasg kfsrdgnnvd
     3721 lwngtwtvnp nedngfaqay lkempagvlt sqglamp
//
LOCUS       WP_181814562             228 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Kluyvera ascorbata].
ACCESSION   WP_181814562
VERSION     WP_181814562.1
KEYWORDS    RefSeq.
SOURCE      Kluyvera ascorbata
  ORGANISM  Kluyvera ascorbata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Kluyvera.
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="Kluyvera ascorbata"
                     /db_xref="taxon:51288"
     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=25666
     Region          13..>215
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mfnapelphd rlavrlsvii trlvagdlln lrsladefgv sertlqrdfh qrlghldivh
       61 enghyrlege lqadnspatl sfiqntgiah iipdkehall mlltrdcpns pcliwhpplk
      121 phaglsefft rlaeaiteqt qisvlvkgqr hdalepyrli hfgeewylvv cqcgelrvft
      181 lstitavtlc gkrftrnedi syltagegfi aalphfplis diintfrk
//
LOCUS       WP_181814509             675 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Clostridium perfringens].
ACCESSION   WP_181814509
VERSION     WP_181814509.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 675)
  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 675)
  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 675)
  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 675)
  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..675
                     /organism="Clostridium perfringens"
                     /db_xref="taxon:1502"
     Protein         1..675
                     /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=77784
     Region          1..486
                     /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 mnivgirikn yksfldsgki pvdkklfsli gqnntgksai mdavqcvfps skksvsvldf
       61 hkgtddeisi eiwfdgvnet yleekiygdk ilkqlekvrn iqaglgenpt qskikkldae
      121 kekiekirse nydeytakyn ikdekfyvrl vskkgknlyk kfyidneiei tegdlkallp
      181 qlkvipaird pknestagsn sylkeliqml ddeiqtsiki egnnitykel nkviaeetka
      241 rcksigesvt qfynqaigte eyiviidsdv niskgttytt kirdintgie sdilncgtgy
      301 qsmiilsile tyvkisqkns dyillieepe vylhpklqrk midtlvtisn knqiiftshs
      361 pitvsklskd qirlvkkvng vakveniipk ivinelgiks ddiltnkgii fvegkddkni
      421 ielllnkiey gisdkiniid agncenlkfy anaeilinnn fdiptliird tdtkepskrk
      481 eelikeitsh rnnglpseve rkinksivil eryslegyfi dekllsildi epsdikiaiq
      541 cyecqynyys krvyeneldg kilsswyqpk yflekfidkf kssqleliee hnfryenqwk
      601 kfekcksckh skidtcinvr akindeiksl klakkdfiie sikdknidei ketklkiive
      661 iledfityin kqynl
//
LOCUS       WP_181814653             669 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Sphingomonas aracearum].
ACCESSION   WP_181814653
VERSION     WP_181814653.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas aracearum
  ORGANISM  Sphingomonas aracearum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 669)
  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 669)
  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 669)
  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 669)
  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..669
                     /organism="Sphingomonas aracearum"
                     /db_xref="taxon:2283317"
     Protein         1..669
                     /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=71016
     Region          16..669
                     /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 mgdgtirrkr rslpvaqapl yvlsfhqrde lamlaaedgw qviaarravg aeqrfassga
       61 avavvdarga lgdgvgatga lgavaaeqga allvlvapsd lgalprffea gathflcspf
      121 grteflqalr fagryaerla gswgaatart lgwrfdpsng kvhltaelsr llafeeavst
      181 rtllrqlpqd eraavvsrlr gltaarrrav fahdlpglgr fvqhvqldpq sgrveaiaep
      241 lgtvpdagel lrdamvgisd iggarrwlgr eleegrrtdl qvmlvslnrf emvntsygrr
      301 agdallraal gridlvarqe tphgaflart agseylialh ataaqvadla rsvaaalarp
      361 fvagdsiivl gsrigvamaq qddtastllr rasealaear dadgvtmrva gtipdlpldr
      421 laadlrqaig ggeiqvlfqp qvtiatrait gvealarwsh pefgtigaea lfaaaqradi
      481 evplsdhiqr ivleqaaawp rllaglrlsl nltagdiarp gfadlfldrv dasgfprnrl
      541 tleitesgli ddlgvaagll ntlrqagcrv aiddfgtgys slaylkslpl dylkidkkla
      601 qdiggtardr vvvrgviema rslglaviae gvetdeqldl lakegcqlfq gflcagplav
      661 aelvelmge
//
LOCUS       WP_181814769             198 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Sphingomonas aracearum].
ACCESSION   WP_181814769
VERSION     WP_181814769.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas aracearum
  ORGANISM  Sphingomonas aracearum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..198
                     /organism="Sphingomonas aracearum"
                     /db_xref="taxon:2283317"
     Protein         1..198
                     /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=21279
     Region          86..197
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mfrpapvglp glaalalgff lfllalfaar rralggptam earrsnrswa gialqamaig
       61 tvaigpvrvg ldplsgpsll ragtvlllml gatglfhaas ramgrnwsiv artrtdhqlv
      121 qcgpfahvrh piyvalflll pafalayghe ralaigvply cigtllrvrh eerllraqfg
      181 gaydlyagrv krfvpgwf
//
LOCUS       WP_181814810             278 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Sphingomonas
            aracearum].
ACCESSION   WP_181814810
VERSION     WP_181814810.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas aracearum
  ORGANISM  Sphingomonas aracearum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Sphingomonas aracearum"
                     /db_xref="taxon:2283317"
     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=28497
     Region          1..278
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtikphrsal flpasnrrai ekaqglpcdv vildledava peakgearaq avdavrgggf
       61 garqvvvrin alttpegaad aralgearpd avllpkvsrp adithaqall rdlpiwamie
      121 tpaavlalpa iaavaglecl vagtndlakd lrctpgedrm pllphlaaiv vaarahglta
      181 ldgvsnvlae tealvaecdq garlgfdgkt lihpaqiaaa nrafapteaq iaearaivaa
      241 faapeaagkg airvdgrmve rlhlvaserv lalaaasa
//
LOCUS       WP_181813415             446 aa            linear   BCT 28-DEC-2024
DEFINITION  MBL fold metallo-hydrolase [Gaiella occulta].
ACCESSION   WP_181813415
VERSION     WP_181813415.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
REFERENCE   1  (residues 1 to 446)
  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 446)
  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 446)
  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 446)
  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..446
                     /organism="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..446
                     /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=46907
     Region          2..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(56,60,112,137,140,144..146,182)
                     /site_type="active"
                     /db_xref="CDD:293810"
     Region          258..>284
                     /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          338..434
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mifhqfldgd lgcacylvgd edagvavvvd ppyavepvla eaerrglrlv rvieththad
       61 hvsghgrlal ehgipisiha dagveyshdp mrdgdeievg avalrvihtp ghrpehccls
      121 vidrsragep wlvltgdslf vgdaarpdla vgavegaegl fsslgrlmel adgvevfpgh
      181 vagslcgkam sskpsttigf errfnpalqf tevdafiada aaivapkppn larivelnrg
      241 pflgaqpaae elaappagtq lldvrpvasy laghrpgavn vpvagtsfat kagfvldggr
      301 pvtvlaaard eaeeavrglr svafldvegy vlgageerve avavdeleel maagaevidv
      361 rekderdtgy ipgsrnvpyr lmktccpdmp tdrpvvtice sgaraaiaas ilrgrgydar
      421 pvveggmaaw rarggdtief rrcgsg
//
LOCUS       WP_181815007             340 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Corynebacterium striatum].
ACCESSION   WP_181815007
VERSION     WP_181815007.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium striatum
  ORGANISM  Corynebacterium striatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
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 11427881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Corynebacterium striatum"
                     /db_xref="taxon:43770"
     Protein         1..340
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37077
     Region          58..331
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mtalssglka rvltvvmtva valglvvatg tqeaeaanrd wlradatgsc ewdrvgwwvq
       61 rcdvwsqamg rnipvqiqpa knggnaglyl ldglratdst nawvndvnaa rtyephnitl
      121 vmpvggagsf yadwngpaty dlvaptnyqw etfltselpg ylernfgvar nnnsiaglsm
      181 gataditlag khpdqfrqvl sfsgyltttl pgaqtfmrla lldaggfnin amygslfnpr
      241 rfendpfyqt drlrntdvyi saatgipgag dagylpqhql sgavlemfsr attrmweaka
      301 ratglrvttn ypmqglhnwa qfgyqleqsk pqvlnvmnaw
//
LOCUS       WP_181815058             374 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA desaturase [Vibrio vulnificus].
ACCESSION   WP_181815058
VERSION     WP_181815058.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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..374
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..374
                     /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=43910
     Region          4..283
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mqqqkppfiw lnivifvtsl vlalvvtpwy gikegfgfeh liwllvtfsf tnlsitagyh
       61 rlwshktyea hpllrivfai ggafslqnsa lhwssdhrmh hkfvdhhdkd pysasrgfwf
      121 shigwmlrdy nqstyndytn crdlqkdpvi mwqhkyyvpl aiatnlgipl llgwyyqdii
      181 gmllvvgalr ltlshhstff inslahiwgk qtftdknsar dngflavltf gegyhnfhhi
      241 fendyrngiy wwqydptkwl ikscswlglt rnlrlnpqmk idkaraatrl knalyqlaqr
      301 geqeslkqql qlefdglvat mkdyydakkq lleckkqtal kkyevalvki ryqqakedll
      361 srykrwhalt ahya
//
LOCUS       WP_181815186             493 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Klebsiella pneumoniae].
ACCESSION   WP_181815186
VERSION     WP_181815186.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=53942
     Region          20..489
                     /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 mtamstlnpi lagsvqsvea yqqvieqtsq avvqwlkqpe myqgksvdel rerislefne
       61 qglgnqaaid raieyflkds lsvhhpqcva hlhcpslvis qaaevlinat nqsmdswdqs
      121 psatiiemkl iewlrarvgf pagdagvfts ggtqsnlmgl mlardaffar qghsiqqdgl
      181 pgdirkykvl csenahfsvq knmalmglgy rsvtlvktde farmdvsdlq akiaqaqang
      241 eqimaivata gttdagaidp lrdiagiaae hqiwlhvdaa wggalllseq yrdyldglel
      301 vdsvtldfhk qffqtiscga fllkdarhye lmryqaayln sefdeehgvp nlvskslqtt
      361 rrfdalklwm glealgqkqy aaiidhgvtm aknvaeyvks qptlelvmqp qlasvlfrsr
      421 paqmagsdaa aiallnqrvg dallasgran vgvtehngvt clkltllnpv vtlddvkvll
      481 nlvertaqel laq
//
LOCUS       WP_181815190             459 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Klebsiella pneumoniae].
ACCESSION   WP_181815190
VERSION     WP_181815190.1
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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..459
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49947
     Region          3..452
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mserrsidyi peserhghpf sqftlwfggn lqitaivtga lavvlggdvv wslvgllvgq
       61 mlgaavmslh alqgprlglp qmilsraqfg vfgavvplvl vcvmyigfsa sgtvlagqam
      121 akllnishva gmlifsaiii viavlgykvi hklgklasiv gilafvymfi tlllsadlsa
      181 lahnnhfslp tfllavslss swqiafcpyv sdysrylprd vsatktwcsv ffgtvlgtqt
      241 smtlgiltaa iagsafpghe vsylvglgks qamamviyfa icfgkitftt lnaygsfmsl
      301 ttivsafrrq tvlsqkcria fvvlmvtasc iiallsepaf lkhfthfllf llaffvpwsa
      361 icltdyylis kgaidipals dpqqrygfwn lyaitlyivg vliqlpfien plfhgsltwi
      421 fagndvswii gwfgtgvlyy alrrfdrrsl paqslfpst
//
LOCUS       WP_181815322             230 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Corynebacterium minutissimum].
ACCESSION   WP_181815322
VERSION     WP_181815322.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium minutissimum
  ORGANISM  Corynebacterium minutissimum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 230)
  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 230)
  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 230)
  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..230
                     /organism="Corynebacterium minutissimum"
                     /db_xref="taxon:38301"
     Protein         1..230
                     /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=24643
     Region          <20..>158
                     /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 manlfsalrr eknsinippv vviglgrfga slakelmehg vevlgidade kfvrehaayl
       61 tevvtadstd sealrqlgvd evervvlgig tdleasilta snlvelgikd iwakadsdah
      121 ariltqigvq hvirperdtg rrvahllggr fedfaeiavd ygvtvmsppa sasagpvdlq
      181 kvweehhvql isrcagpgqw rpladatqlt prdliavags padleafsqs
//
LOCUS       WP_181815328             419 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Corynebacterium minutissimum].
ACCESSION   WP_181815328
VERSION     WP_181815328.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium minutissimum
  ORGANISM  Corynebacterium minutissimum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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..419
                     /organism="Corynebacterium minutissimum"
                     /db_xref="taxon:38301"
     Protein         1..419
                     /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=45589
     Region          16..378
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 melvfaflag vaacglaipv lrrirerles rrardadsnq vtsvsqvlhl avggspsgmt
       61 vlsrskevif snpaahemsm vhdravnpdi wsvaqevfed ketrtldlsi pkrrtgnrvt
      121 qvravvkplt lnddrfiivy gtdesesvrm esarrdfvan vshelktpvg giallaeall
      181 qdtgdpehve yfgskvqkea armadmvnel islsklqgae alpemepvdl deivdeamtr
      241 nqlaadahnn qltrgesvgv rvmgdksllv taisnlisna ihyspdempv svtqkvvsgn
      301 vvlvrvtdrg igiapedqer vferffrvdk arsrqtggtg lglaivkhvv anhggniklw
      361 srpgtgstft ielpiyteek padtvdnkdn kedgavssaa pglqravarv aarrkdksq
//
LOCUS       WP_181815389             137 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181815389
VERSION     WP_181815389.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 137)
  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 137)
  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 137)
  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..137
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..137
                     /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..127
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 iedlkvsnms ksaagtvsqp grnvraksgl nrsildqgwy emhrqleykq lwrggqvlav
       61 ppaytsqrca ycghtakenr lsqskfrcqv cgytanadvn garnilaagh avlacgemvq
      121 sgrplkqept emiqatv
//
LOCUS       WP_181815786             272 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Alteripontixanthobacter
            maritimus].
ACCESSION   WP_181815786
VERSION     WP_181815786.1
KEYWORDS    RefSeq.
SOURCE      Alteripontixanthobacter maritimus
  ORGANISM  Alteripontixanthobacter maritimus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Alteripontixanthobacter.
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="Alteripontixanthobacter maritimus"
                     /db_xref="taxon:2161824"
     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=29519
     Region          59..176
                     /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 mtdktldcpa cgmhasavdd rdfphcnkcg hrwmpttlqe qseveqsvyg hsyagyredp
       61 vldnnfdrli aehiqptvqs gdrvldvgcg agaflraaqr asmdaqglev sddaaaicrd
      121 agckaeagdf lqygqpdsfa vitmwdvleh lrdplafvqr vrlllgrdgi yvsktptfga
      181 lsvrlsdrme rlrgpllgap ghvqyftpss latllkrggf dlqksipmpg gmrsrpsegs
      241 lkrkfgrkar gligsvsgds nmlyvaspti ak
//
LOCUS       WP_181815814             267 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Moraxella ovis].
ACCESSION   WP_181815814
VERSION     WP_181815814.1
KEYWORDS    RefSeq.
SOURCE      Moraxella ovis
  ORGANISM  Moraxella ovis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
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="Moraxella ovis"
                     /db_xref="taxon:29433"
     Protein         1..267
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29987
     Region          1..167
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mpelsidvit pcynaadtie ravmsvliqs nlgriylidd gsvdeiwqvi trlqknypnl
       61 ihierlpink gvatarnwga mlaksnfiaf ldaddsyqsq vlpacamvfs qfdvgmirlp
      121 mtpinlpkef adhpefdiaw rtfemtagsn mvfyrpyfla lggfdddeif krfggedgal
      181 glatidtsmi atlfdnpdye vgvdyhchqn mfanhlfhal lfgentrsvt qddlhkanqs
      241 tqnainrikk lrkiintktg kmpivls
//
LOCUS       WP_181815898             493 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Klebsiella pneumoniae].
ACCESSION   WP_181815898
VERSION     WP_181815898.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=53957
     Region          20..489
                     /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 mtamstlnpi lagsaqsvea yqqvieqtsq avvqwlkqpe myqgksvdel rerislefne
       61 qglgnqaain raieyflkds lsvhhpqcva hlhcpslvis qaaevlinat nqsmdswdqs
      121 psatiiemkl iewlrarvgf pagdagvfts ggtqsnlmgl mlardaffar qghsiqqdgl
      181 pgdirkykvl csenahfsvq knmalmglgy rsvtlvktde farmdvsdlq akiaqaqang
      241 eqimaivata gttdagaidp lrdiagiaae hqiwlhvdaa wggalllseq yrdyldglel
      301 vdsvtldfhk qffqtiscga fllkdarhye lmryqaayln sefdeehgvp nlvskslqtt
      361 rrfdalklwm alealgqkqy aaiidhgvtm aknvaeyvks qptlelvmqp qlasvlfrsr
      421 paqmagsdaa aiallnqrvg dallasgran vgvtehngvt clkltllnpv vmlddvkvll
      481 nlvertaqel laq
//
LOCUS       WP_181815896             446 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Klebsiella pneumoniae].
ACCESSION   WP_181815896
VERSION     WP_181815896.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 446)
  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 446)
  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 446)
  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 446)
  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 446)
  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 446)
  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..446
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..446
                     /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=47836
     Region          <1..131
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
     Region          217..408
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mmkmqwlsal vlgalscaaf aeeapadsnl ikqgeylara gdcvachtng kagkpfaggl
       61 pmetpigtiy stnitpdkeh giggytfeef ddavrkgvrk dgstlypamp ypsfarisea
      121 dmramyayfm hgvepvnvan kdtdipwpls mrwplafwrg ifaptpsdfv anpqvdpvle
      181 rgrylveglg hcgachtprs ltmqekalse segddylags napidgwvas slrgenrdgl
      241 gtwseaelae flktgrndks vvfggmsdvv ehslqylsdd ditaiarylk slpprggkqt
      301 papvedsvak dlwkgndskt gaalyvdnca achrtdgagy krafpslkgn pvvqtedats
      361 lihivltgst tpavkdavsn ltmpsfgwrl ddqqvadvvn firtswgnna pavsasdvak
      421 vrketaayde kalgnadisk lpgagq
//
LOCUS       WP_181815917             265 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Eggerthella lenta].
ACCESSION   WP_181815917
VERSION     WP_181815917.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella lenta
  ORGANISM  Eggerthella lenta
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Eggerthella.
REFERENCE   1  (residues 1 to 265)
  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 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   3  (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   4  (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 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Eggerthella lenta"
                     /db_xref="taxon:84112"
     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]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29438
     Region          206..260
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mmyinyasvl gglvsalalv aiwrfrtiry sinhlfrvmf pflvvvlcal pfigmdslvv
       61 taaaiyitys fmglslqvlc lqtahdygvn pvfcisfqig vslctqglgy llgnavniav
      121 lssipplasi alisvamlal vmyltrglsi sqeeegrdie flslsrkahr tgegddgeta
      181 vpwdddvkya drlsircdli gkkyylsqre ievmhlfarg ytmaaiaqel fisentvkth
      241 mrrlyakvgv hkkqqllsml nnyve
//
LOCUS       WP_181815943             674 aa            linear   BCT 28-DEC-2024
DEFINITION  cation:proton antiporter [Eggerthella lenta].
ACCESSION   WP_181815943
VERSION     WP_181815943.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella lenta
  ORGANISM  Eggerthella lenta
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Eggerthella.
REFERENCE   1  (residues 1 to 674)
  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 674)
  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 674)
  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 674)
  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 674)
  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..674
                     /organism="Eggerthella lenta"
                     /db_xref="taxon:84112"
     Protein         1..674
                     /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=74052
     Region          56..504
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 meeplealml allllaavlv ssvidqlvpk isspliqill glgiallass qikielddkl
       61 flvlfiapll ydeaknidka slwrnrkpvl slaiglvlat alvvgfavhw lvpsislfaa
      121 falgaalgpt davavaslsk etsissrsks ilegeslind asgivafqfa iaaavtgtfs
      181 lvdatadflf sffggilmgi algylgnflv rkvrswglen ttfhvlfevf tpfivylvan
      241 alhtsgilav vaaglvnvis prvigpsisr mnivstsvwr vlsfalngvv fvllgtqlpl
      301 afqgtwesta vsndkliayv lglafivifa rfvwvmamew vhsraeradr pfglenvrta
      361 avmtlggpkg aitlavafti syavpqrdlm ifmacgvivv tlllatfvvp llapkkpptd
      421 edlrcdetev sieilrtvie dlaarqtaen raatqmvirs yndriariks rndiedepnt
      481 alrlqavrwe qeltlklidd eeihpiigyq ylsrlarien mlkhhrgrws aqnfmlrlra
      541 iarsgwhriv aglpginvte rvqairdlqm qcaehvverl qqklaspesd epaedvstll
      601 leyqrsital rnanpsital tntaskaqdi eryglrlele qiqaryedgd lcrssykrlr
      661 envalmqvdl ednv
//
LOCUS       WP_181816003             748 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Dermatophilus congolensis].
ACCESSION   WP_181816003
VERSION     WP_181816003.1
KEYWORDS    RefSeq.
SOURCE      Dermatophilus congolensis
  ORGANISM  Dermatophilus congolensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Dermatophilus.
REFERENCE   1  (residues 1 to 748)
  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 748)
  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 748)
  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 748)
  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..748
                     /organism="Dermatophilus congolensis"
                     /db_xref="taxon:1863"
     Protein         1..748
                     /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=81182
     Region          <290..744
                     /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 mktptpphts pthrplaiai algattlitl tylrhptfmt tplsiaqcat ltittlsplr
       61 rkphppthwa tfiagtitli latifntttp ntphpltetl hltgyllitl ffftnhtrnn
      121 phphpiinld taaaaiatll ilwsiplalp hcppaintlq wtihptldal lcayfathan
      181 hpnqhtptah wltatfgill asdtikastq ltnqpiptws naatfiattt lalafthpdi
      241 ltithphttn thrtlnrgin aafylsaipg vaslaihsnn tpdqilrtcl vtallillfi
      301 rflramtkls ateadsrhra thdpltglln rsgllhactn alrrnringh htlmlfidcd
      361 hfkyvndtwg hsagdvvltt iahrlrtthp nditarnggd efilitpiph pehaktiaht
      421 tlhsfdtpie iapgvfhnit psigvatatp tenitpeelt aradialysa kqrgraryai
      481 fdddlgatar trsltlaalr qavttnaitv hfqplmtgpn fttilgweal arwndptlgp
      541 iapdvfipla eeiglieplg ahvlrtacre lhtlrtlpgy ehtivsvnvs viqlrrpdfv
      601 ekvlttlhet nlpptaltle vtesiplieg siahktlvql raagvavsid dfgtgyssvt
      661 allqtpadtv kidrsltarl dttddgiaqv saaievvtsl gipsvtaegv etaeqahilt
      721 slgchhaqgw yfgraeppsn liarhtha
//
LOCUS       WP_181815958             596 aa            linear   BCT 28-DEC-2024
DEFINITION  PHA/PHB synthase family protein [Legionella pneumophila].
ACCESSION   WP_181815958
VERSION     WP_181815958.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 596)
  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 596)
  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 596)
  AUTHORS   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 596)
  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..596
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..596
                     /product="PHA/PHB synthase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67533
     Region          56..595
                     /region_name="PhaC"
                     /note="Poly-beta-hydroxybutyrate synthase [Lipid transport
                     and metabolism]; COG3243"
                     /db_xref="CDD:442475"
ORIGIN      
        1 mnglekqccp kevlltqree lsvgtdsccv ptdastsdnf fpffnqliqa nlakwtmgis
       61 paaigssyst wlwqliqspg nlwelafypi fhandcinni vcvdraaggk dvrfkkdswq
      121 pmpwrlfseg flqvedwwrr attnvpglpr pvertvsfwa rqwldalsps nfvwsnpdlf
      181 neairtggln liqgsqiald dwlekltgtp ptgsehfipg qqvaitpgrv vfqnhlieli
      241 qyesqtktvy kepililpaw imkyyildls phnslvkwlv kqghtvfiis wrnpdkedrd
      301 lgmddyyrlg amaaidavst ilpeakinlm gyclggtlal itasvmgrdk derlnsltll
      361 aaqgdfteag elmlfvtesq vdflksmmre qgyldtkqma gsfqmlrayd liwskmiqdy
      421 mhgmrrgmid ltawnadatr mpykmhseyl eklflkndfa egrytvegkp vaaeniqlpv
      481 favstekdhv apwqsvykih lmtdsdvtfv ltggghnagi vsepghpgrs yrihehkege
      541 aylnpanwlt vaekregsww rgwhewlvlq stkkripppv idtslpaapg tyvhqk
//
LOCUS       WP_181816070             479 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Dermatophilus congolensis].
ACCESSION   WP_181816070
VERSION     WP_181816070.1
KEYWORDS    RefSeq.
SOURCE      Dermatophilus congolensis
  ORGANISM  Dermatophilus congolensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Dermatophilus.
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="Dermatophilus congolensis"
                     /db_xref="taxon:1863"
     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=51259
     Region          188..448
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mrgedideas gllasgefnt srplsvtwfs ylvaaggaca vvftvagglv slplhemgle
       61 naflcvvaav afvafissgp rifrpaawaf pffvaafvfw spyalartpd vrageleltr
      121 lftafvmala vyactqatsv gmtsmrlgwf fglvlsvvva gweiftrqhl wisarnpfif
      181 pepvvvgtyi npnnfatalv amivgaiala aqsrsrlfsv vvlgvvaagc vavvvtqsrs
      241 gvlalvvvla levrrrmltr rgerslvwrq rcadvsgrsr vlvrvacgvi ccgvvaaftv
      301 palvarnpvm qmlvaqagae trrsdtlrlq llktawrylr dsgwlgsgag sfeyllwhdp
      361 apatlkltnl hnafmelltq ygvpiavcyg mfvvgvlvtl agsvrvpdtr varyeaigyl
      421 ialsalgvaa ssalhvstww vmhaaagaca wrvaththrl plwgqegags vdpggkdic
//
LOCUS       WP_181816077             520 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Dermatophilus congolensis].
ACCESSION   WP_181816077
VERSION     WP_181816077.1
KEYWORDS    RefSeq.
SOURCE      Dermatophilus congolensis
  ORGANISM  Dermatophilus congolensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Dermatophilus.
REFERENCE   1  (residues 1 to 520)
  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 520)
  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..520
                     /organism="Dermatophilus congolensis"
                     /db_xref="taxon:1863"
     Protein         1..520
                     /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=56900
     Region          3..467
                     /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 mkrglarsre vgeilarngl raladsagls rhpsdpprsd asiraventr pevlvstlte
       61 lgtawiklgq tlatrrdlip aeycdaleal tdhtapapfa diratiatsl gadpsalfrh
      121 idpvplgsas vgqvhpatts dgrevvvkvr kpgvlenvhi dlelmerlvk amcrarpqle
      181 elgvietmqt faatlraeld frteasncee mrsrfasdea iaipavyrdl ttadvltqer
      241 ivggirlddl esmraagidp dragrryvda lmrmlltfgr fhadphpgnv yvhldghltf
      301 idwgmvghvd tatrrallrl iagfaipheg llisalldla tprrhldrpk lrrdvgelvh
      361 ilrsttlsel saaevgglit rivrahrlrl dpsipvalra msvaeglvrr lsphlslpdl
      421 aavqareafg admrpeqlrq iatdllgdam vfahdlparv srvldviesg esevtvagds
      481 lqkmrrqrdr dtrrlvggml assgiiagsi vwsawyrark
//
LOCUS       WP_181816078             766 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Dermatophilus congolensis].
ACCESSION   WP_181816078
VERSION     WP_181816078.1
KEYWORDS    RefSeq.
SOURCE      Dermatophilus congolensis
  ORGANISM  Dermatophilus congolensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Dermatophilus.
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="Dermatophilus congolensis"
                     /db_xref="taxon:1863"
     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=83346
     Region          105..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 msiveeaera ghkppllrra thrqralill fvflipyiiw lgdranatql iatnalmlvl
       61 astvaatpll aayrprrlwv ffsltwlcpv gatlvrnypg spdphiania lfdilslasy
      121 viagiwvlya twhltglrgl tyaifdtsaa tigiviatwa isqqihptgr tadlawaiyp
      181 ivdlailgfa gqvlfrikgt tpglnwfltg vlimlavhgv vtyyalnyds wppswimgfn
      241 lfswasfiag ithphikdwg khvvkpvdad nmtlrnvyvi vavtatsfgl ltpmlstfdy
      301 rirsllvval llllisrlia atrhlalser dssyrathdq ltgllnrfal hndlnrrllr
      361 qrsnspaial iyldcdafkd vndtwghdvg dkvlqhlaag mreatgpedt varhggdefa
      421 lvtevtdeae alalaaklqa lfsapvaiga rrghtvtasm gialacpheq htaaellsna
      481 dlalhrakat grgtctlyds vlkeqavkra vmsealreal srnalsvafq pifrgnnyse
      541 lagwealarw qhptlgpipp nefiplaeel glicdlgdli lrksaaefsd lisalgledv
      601 slsvnvsvaq llqanfvdtv letldqvrls pcrivleite smlvdddspa ldtlhrlrqa
      661 glalslddfg tgyasittll nlpidgvkld rslvkrlddd paaparvkav ldlvasvgin
      721 rvtaegietp eqsqalaqlg cprvqgffyg rpvpsaqilt apvetg
//
LOCUS       WP_181816086             336 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Dermatophilus
            congolensis].
ACCESSION   WP_181816086
VERSION     WP_181816086.1
KEYWORDS    RefSeq.
SOURCE      Dermatophilus congolensis
  ORGANISM  Dermatophilus congolensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Dermatophilus.
REFERENCE   1  (residues 1 to 336)
  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 336)
  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 336)
  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 336)
  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 336)
  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..336
                     /organism="Dermatophilus congolensis"
                     /db_xref="taxon:1863"
     Protein         1..336
                     /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=36595
     Region          2..267
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mktavlggkg lfghrlcesl vaaghevvsv rprrqgsvas pyrgvtysav dvtddeavit
       61 qvlhgvdalv ygvgvsdvgp veggdavewv rdvvgrtfra aaaagveqvv vigsylaawe
      121 ranpglgiad rhpyvraria eadfaievgt elgmrvcvle ipyvfgagsg erhhwreill
      181 drlrgpvvlf ptggtsvitt qqlvdavmsa lqrgehaary pltdmdltwr emisvvmdal
      241 gqrspimgvp rwvaqpicvr virrlqrhgq lrglsaehvl ddflcshiyv datwsrellr
      301 yrpggvpqai rdesldaygl piesprpvpq fagrrr
//
LOCUS       WP_181816108             459 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Dermatophilus congolensis].
ACCESSION   WP_181816108
VERSION     WP_181816108.1
KEYWORDS    RefSeq.
SOURCE      Dermatophilus congolensis
  ORGANISM  Dermatophilus congolensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Dermatophilus.
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 11472026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Dermatophilus congolensis"
                     /db_xref="taxon:1863"
     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=49190
     Region          128..459
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrflvfvgr rpgtwslrrq vvvlsgiflt vllgiglvlf vialravlvq sasdatlnqt
       61 yqlaqavrsg dttpvhavqr aapgstmlqa lsrdgrvlaa sgnafvtval vdpipvvgna
      121 vtqqhegfld lagdsdayva saqtvvtpgg eqvtlvvaqp leveshtiei avmllavasv
      181 vlvgvvlvlv drvlrralep vrritehaah itrartserv vvpptgddia vlamtvneml
      241 drlaraeett qrfvsdashe lrsplaavrt hveiaergag ldlplvrsev mrvqalvedl
      301 ltlaksddeg lrlvrepldl deivsaearh lrvvtdarve vvlaaaevwg dgarlgqvlr
      361 nltenarrht sgvirlvmev dgqvvrvhvd nsgapvpekd rliifdrfar ldaarerdlg
      421 gsglglaiar tvaelhggsl vagvapegwc rfsltlplv
//
LOCUS       WP_181816180             454 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Mobiluncus mulieris].
ACCESSION   WP_181816180
VERSION     WP_181816180.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 454)
  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 454)
  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 454)
  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 454)
  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 454)
  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 454)
  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 454)
  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..454
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..454
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51203
     Region          3..446
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mkllrfkvrn frsireaqsi dflrdtppan qapdwaslar pvtvflgpna sgksnvllam
       61 ryaftviars fawqqgdsly kplevypfsl ddhslqepsy fefdffqagt ryvyafeygl
      121 sgvtseslyy vpkrrltpcf trtntgdgve iefnqsigls addekllrrv aspqglvlsa
      181 alrlrlpflg kvgkalaneh fnfislsdqh ldarfawvay mimtniadld eigvlmriad
      241 tgitearldf kaldqavlkk lekrniistk qydegssqfs isigdadfep deaaeilqsf
      301 rfshrgehgs felrtvdesy gtltwlsvap ailralrqgs vliadeidas lhqnllefii
      361 ksfsssfsnp hgaqliissh ntnllehiks ldlepnsfwf tekryhgetq vytlddfekh
      421 pnanyerryl sgkygalpsl spamlralvs peee
//
LOCUS       WP_181816196             476 aa            linear   BCT 28-DEC-2024
DEFINITION  rhamnulokinase [Mobiluncus mulieris].
ACCESSION   WP_181816196
VERSION     WP_181816196.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 476)
  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 476)
  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 476)
  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..476
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..476
                     /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=51216
     Region          8..452
                     /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 melvvvdvla idmgssaira flghwntaen elslqeiyrq pievqvdadn hltwpvaqfa
       61 eiakkcaava aqtlghapds vgvdgwgvdf vkisasgece pqavayrdtc ghigqaaldt
      121 kitrrhqyrf tgvmpqdins vnrltganav gkapyagilf lqdmitrvla tadipgwdap
      181 vacapwasqg vastsammdv nrfewnteil kaagidpkil ppihgepsll vkrgrtnvvl
      241 sgshdtacaa yciapnvgdi fvscgswavi gaitpkpltt deayekgvtn eaatggsnra
      301 elnqtglwll qecrrqwske gkdvsfsqld kqcweakslg vfinpsdael ispgempsrl
      361 raklesefgi lecsdgqllr tikeslahsi vagindlrhl vksegvvhit gggtydtflm
      421 qeianllgep vrlakceasi ignmlaqlhv lgvpkgatqk wfdtsdytev lqpitl
//
LOCUS       WP_181816243             173 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Mobiluncus mulieris].
ACCESSION   WP_181816243
VERSION     WP_181816243.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
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   Wintjens,R. and Rooman,M.
  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 173)
  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..173
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..173
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=18989
     Region          <30..69
                     /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(31..32,43,46,50..51)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mptkprlqgg klnqavtaii tgildikqvs rrelaarldt shtylnnrln gsvdftvtdv
       61 dviatalgvr tffifvaaew aingqrpale gddvdwkqiy dlaatvnpel rlppeleqvf
      121 dkkttskpql aphepqkieh lfaptpaapk ptplfsdrrd dgdpgnealp rma
//
LOCUS       WP_181816297             290 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Flavobacteriales].
ACCESSION   WP_181816297
VERSION     WP_181816297.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriales
  ORGANISM  Flavobacteriales
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia.
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="Flavobacteriales"
                     /db_xref="taxon:200644"
     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=34430
     Region          <86..286
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mktlkfhkte cgvdfllnvl pstevrdsyl kgevyntdff eivffkkgng hiilnhqkkv
       61 iednsivfis afqkrqwqln pdnldftvla fqedflndff sdklftyrll yfyqleyplc
      121 mqvqqdittf ycvllsemkt ellktkadsv hiirsliyyl lqklnreyae khqlplekng
      181 nnyafqfkkl teihikekqr indyteilnv srislnkavk eyfnvtatym lkqrllieik
      241 dylihseltv aeiayelnfs epnhlmrffk nqtgmtttef ladyqngihs
//
LOCUS       WP_181816479             359 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Bacillus velezensis].
ACCESSION   WP_181816479
VERSION     WP_181816479.1
KEYWORDS    RefSeq.
SOURCE      Bacillus velezensis
  ORGANISM  Bacillus velezensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus amyloliquefaciens group.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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..359
                     /organism="Bacillus velezensis"
                     /db_xref="taxon:492670"
     Protein         1..359
                     /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=39984
     Region          79..353
                     /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 mlkelflnlt ilitfnylft llfkeslsyk edrlmfqllk gtvcgllgvf liafgfsysd
       61 siidlrnipi iiaalyggwv staaafaiiv agrilinfna saifsiaavg viailsaavl
      121 rgkkpdhkma fvmmlfsnvi ftltllflmp eqpagalvyy wlisvlggml slyiikhead
      181 arllfkqykf qanydfltgi fnkrkfeevs rvlydrasqs pssqlaliyl didhfkqind
      241 qyghyegdqv lkelgarlrf llsssdpsar iggeefavlm pnctytkglh laeeirhtid
      301 anpilltsgd tipvtvslgi ahyptntsdp qtlpliadrm lykaktsgrn qvcstekke
//
LOCUS       WP_181816481             960 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Bacillus velezensis].
ACCESSION   WP_181816481
VERSION     WP_181816481.1
KEYWORDS    RefSeq.
SOURCE      Bacillus velezensis
  ORGANISM  Bacillus velezensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus amyloliquefaciens group.
REFERENCE   1  (residues 1 to 960)
  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 960)
  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 960)
  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 960)
  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 960)
  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 960)
  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 960)
  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..960
                     /organism="Bacillus velezensis"
                     /db_xref="taxon:492670"
     Protein         1..960
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=109691
     Region          1..955
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1..197
                     /region_name="AAA_27"
                     /note="AAA domain; pfam13514"
                     /db_xref="CDD:433272"
ORIGIN      
        1 mkitamhiyq ygkfsdrsfq lsdssvqviy glneagkttl msfiksvlfg fpkskkyepk
       61 nggvyggtve lkhvdhgavk iertkgaaek vrvymasgei kdgewlkqll sdtdralyea
      121 iysfdvfglq eiqafnrdki gefllysslf gseaaakldg rlakeldrmy kpngrnprln
      181 qeldtlkrfs aqlkqaeaae agyhslleek ksaggrlqda earlkditee iktvksaiea
      241 kpladkktal eselssypea lkqfpkdgmh qlekyeshlh pkaarleglr akadelrrqa
      301 ellapnedll qkerqlqels geqhmyesrg eqlaaiqsqi rqtsarvssg lqqlgrheed
      361 gilslntdye yewrlqeavq sagqarerka qldamfeqar leleeaerkh avtaenildp
      421 avrkekeaal qsykqtadte gnewqahvqq lekqrarqkk lflgggilfi aifamlkewl
      481 paalftgall lymlsgmqkp lpserggpgh kkkkpaiske aadllqeelw rdgrhrqqli
      541 adqavleqke aayervirqy eeweaemaps ekqaelfmke lgfsgshshl ldayhvmkdv
      601 kkeilnkhel tieagrlqkl qrafedrvkk lspsdgrels vkerlhvlla qaerareeak
      661 rkqaletdll haqeqmreln eevhyyeqqv kqlfmaagak nrehfcelar lnesrreter
      721 qlreikthls giggkqlepy msrtvseleh tvvqketekk tleeknaqlr eqtalltvkq
      781 eqlessglvs dlkqqtemqk ervkktakew aalqtvrhii rekmerhkkv tlprlletag
      841 alygpltdgr yhklyfsead dsimvmrkdg tvfsagelsq aaceqlyaai rfalaseres
      901 avslpflldd sfvhfdrqrl qrlfdvlnql seggrqilyf tchehvsrsf hsgqvmrlls
//
LOCUS       WP_181816600             297 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Bacillus velezensis].
ACCESSION   WP_181816600
VERSION     WP_181816600.1
KEYWORDS    RefSeq.
SOURCE      Bacillus velezensis
  ORGANISM  Bacillus velezensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus amyloliquefaciens group.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..297
                     /organism="Bacillus velezensis"
                     /db_xref="taxon:492670"
     Protein         1..297
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34766
     Region          69..287
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mnpllaiypr avlsdtccta edvfcfydek rrvyvaipke ditpkeklll esfltpaeek
       61 gdffpetaaa krwrrfllee gpvpdvkepr vrfihydllg erdwgaytea lrhfwpvsyt
      121 vvrtgrdhgv iveeekleap dsddiasfvk ilegdfyfsv rffigryyck gerlrlhyqr
      181 eqqycqigrr hlpqlstlta etvfpamlte esreklsall heeaallfqk epelkhtiqt
      241 fiehnsnmsl tskklhlhrn slqyridkfa ersgidikty rgallayfic lqyeksh
//
LOCUS       WP_181816747             190 aa            linear   BCT 28-DEC-2024
DEFINITION  YceD family protein [Myroides odoratus].
ACCESSION   WP_181816747
VERSION     WP_181816747.1
KEYWORDS    RefSeq.
SOURCE      Myroides odoratus
  ORGANISM  Myroides odoratus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 190)
  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..190
                     /organism="Myroides odoratus"
                     /db_xref="taxon:256"
     Protein         1..190
                     /product="YceD family protein"
                     /calculated_mol_wt=22184
     Region          1..190
                     /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 mntektysis figlkngeht feyqigsdff knydyddfnr ieanisvlln kkatllevnf
       61 kakgvvnvpc dvtnedfdlp ienefnlvvk fgeefnddhd eililpmney einlsqyiye
      121 llvlsipvkr vspeaaeded fdeeefdflf rdededneme esqeeettsd sdqadidprw
      181 eklkklltdk
//
LOCUS       WP_181816760             131 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Myroides odoratus].
ACCESSION   WP_181816760
VERSION     WP_181816760.1
KEYWORDS    RefSeq.
SOURCE      Myroides odoratus
  ORGANISM  Myroides odoratus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..131
                     /organism="Myroides odoratus"
                     /db_xref="taxon:256"
     Protein         1..131
                     /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=14715
     Region          6..130
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD/TolR; pfam02472"
                     /db_xref="CDD:426791"
ORIGIN      
        1 maikrnkrfk aeiatsslsd imfflllffl ilstlanpnv ikmmlpkaas nektnkqhlt
       61 isvtedkrff inktevsyea leqtllaelg gntdqsvvir ipfnsqiqel vdvlqigvkn
      121 nikfviatqk q
//
LOCUS       WP_181816294             194 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TlpA family protein disulfide reductase
            [Empedobacter].
ACCESSION   WP_181816294
VERSION     WP_181816294.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter
  ORGANISM  Empedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
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="Empedobacter"
                     /db_xref="taxon:59734"
     Protein         1..194
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22381
     Region          52..191
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mktkllllsm fftffscnks eqkieesaei ekidsvakke speseipkel ikapdfslad
       61 ingkrfdlsd fkgkyvymdi watwcgpckv qipfmkelek qfhnapihfv svsldkledk
      121 piwekmvren qmsgvqlfag rednfgfdyk ieyiptfiil dkegnimidr apapmdyqtg
      181 ginqqlvdil kmmk
//
LOCUS       WP_181816791             119 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Eggerthellaceae].
ACCESSION   WP_181816791
VERSION     WP_181816791.1
KEYWORDS    RefSeq.
SOURCE      Eggerthellaceae
  ORGANISM  Eggerthellaceae
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales.
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 10611674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Eggerthellaceae"
                     /db_xref="taxon:1643826"
     Protein         1..119
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13354
     Region          10..64
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(16,20,45)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(19,44)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(26..27,38,41,45..46)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mrsrvpekse laaqlkryry daglkgdeag avigkkattv ykyeagtlwv spadlrslln
       61 eygvnmvtaf teigdpragg rkkdesalrw rkmrtyydmm npakqrtlld varamaedf
//
LOCUS       WP_181816802             379 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Eggerthella].
ACCESSION   WP_181816802
VERSION     WP_181816802.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 379)
  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 379)
  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..379
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..379
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44049
     Region          4..>181
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mvakvsiivp vcnsekylke cldsilsqsi rgievvcvnd gstdnsanil dryacedsrm
       61 vvisqknsgy gkamnvgisa argewigfve sddyilpsmy sdlvsiaern rldfvksslc
      121 rffgegekrt fqrepitknq dllatvvnps kdprlldalm nnvtgvyrke fldnnqirfn
      181 etpgasfqdn gfwfqtfmka ekamlvdeay ymvrrdnpns svksaekvyc mreeyqfifs
      241 llesdeelfn rfiyqwckkl fsncvatlnr idrsfrrdfl ctmsqdyrlf kekgwidfal
      301 ynqrerrmlt limddperyc vqyvedkvsd mqkivrenec rieqktkkln slkhsqslki
      361 ghlilhvpqk lhlvvkdqa
//
LOCUS       WP_181816803             378 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Eggerthella].
ACCESSION   WP_181816803
VERSION     WP_181816803.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 378)
  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 378)
  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..378
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..378
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43332
     Region          2..220
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mrpdvsvvip vynskafldc linsvlgqtl tnieiicvdd gstdgsgdil ryfadsdhri
       61 qiiekengge gsarnaglrh aageyvcffd sddfvdrnml eemvscaran tsdlvicaid
      121 ayyeesdiyk pnewavsrea vpvgvafdpl kiedlfrhiv gyaanklyrt sfvldndllf
      181 qeirthgdls fsyaglaaak rvvyidtpfy hhrirkgsls dttqeshwhc lfealdnlrs
      241 elyrldiwse cerdfanyvl qmakwkfsrv ggqvrvdlde glrsewfphl gvltypkdff
      301 ynkdclafle dtmslpymdr qekelerlrl liadqdvila nldyecdqit msasykigha
      361 llrpfwllkr afsvhrgr
//
LOCUS       WP_181817322             218 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paracoccus
            pantotrophus].
ACCESSION   WP_181817322
VERSION     WP_181817322.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus pantotrophus
  ORGANISM  Paracoccus pantotrophus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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   Wintjens,R. and Rooman,M.
  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 218)
  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..218
                     /organism="Paracoccus pantotrophus"
                     /db_xref="taxon:82367"
     Protein         1..218
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24330
     Region          41..86
                     /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(42,46,71)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(45,70)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(52..53,64,67,71..72)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mrrqdlsdld ielgpdpfrv devweedvti rraglniaqg lkacrkklgl tqselanvln
       61 ctersvadye agrrsmpaek lgrllerttv glhepfcvlp dqptvedraa iidlafdlvg
      121 eilgvypead rkdveaivkg eilsfpdpqm vsaaerrhsv qmcvqmlvar ygdecredfs
      181 nrpctaelvv qrrpaqpasa frlkpsppar rgrprkvp
//
LOCUS       WP_181817677             491 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Psychromonas sp. B3M02].
ACCESSION   WP_181817677
VERSION     WP_181817677.1
KEYWORDS    RefSeq.
SOURCE      Psychromonas sp. B3M02
  ORGANISM  Psychromonas sp. B3M02
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Psychromonadaceae; Psychromonas.
REFERENCE   1  (residues 1 to 491)
  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 491)
  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..491
                     /organism="Psychromonas sp. B3M02"
                     /db_xref="taxon:2267226"
     Protein         1..491
                     /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=53955
     Region          19..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 mtasnnwsay faqlgenqaf eqataqtkaa idglfqhatk pysglepall kqqlngvdfs
       61 qpaplaevie ttneliakns llvqhphtia hlhtpplias ivaehfiaal nqsmdswdqa
      121 paatfveqqm vdwlcatyql geradgvfts ggtqsnlmgl llardwyayq qsqhdiqqdg
      181 lphyaqkmri icsdkshftv qksaslmglg ersvvlvktn vqgqidvdel qltidalkaq
      241 dllpfavvam agttdhgaid dleavvniar nagcwshvdg aygaalqlse qhkgrlkgie
      301 ladsvsvdfh klfyqtiscg allikdkanf ntllhhadyl nregdelpnl vdksiattkr
      361 fdalkmfmtl kavgekqfge fydhllsltq evadkinqnp hfelcctpll stvlfrlssk
      421 iqgelndvef nqlhqtlrlq lltsgeavia etkvdgqlvl kftllnpcln sadfdsliak
      481 iettalqlin q
//
LOCUS       WP_181817567             379 aa            linear   BCT 28-DEC-2024
DEFINITION  xanthine dehydrogenase family Fe-S subunit [Serratia fonticola].
ACCESSION   WP_181817567
VERSION     WP_181817567.1
KEYWORDS    RefSeq.
SOURCE      Serratia fonticola
  ORGANISM  Serratia fonticola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 379)
  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
REFERENCE   2  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449882
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Serratia fonticola"
                     /db_xref="taxon:47917"
     Protein         1..379
                     /product="xanthine dehydrogenase family Fe-S subunit"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40800
     Region          8..159
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
     Region          207..350
                     /region_name="CoxG"
                     /note="Carbon monoxide dehydrogenase subunit CoxG [Energy
                     production and conversion]; COG3427"
                     /db_xref="CDD:442653"
ORIGIN      
        1 mqtnklnqvs levngkllsv fvedrtslad llrdeldltg thlgcehgvc gactleingh
       61 psrscitlak ncnkasirti edfnddpvms alreafsenh alqcgfctsg mlssardivl
      121 rgveneeeti rtamsgnlcr ctgymgiiks vrsvlaires liditsigsq kiaparnytg
      181 dlpaferkig kidqlqpsip dgdegnqite sinlnqsied vwhlmrnveq vvncvpgarl
      241 leqtgddlki mmeasfgais asfkgdgrft fndndhtgrf egqgkdarsg sgasgalsfr
      301 lepkgsgcnl nlvasyevtg alaqfsrggl vksfakaits ifgenlaksl kgetvdsssg
      361 aklnvfklil mvikgffkr
//
LOCUS       WP_181818220             131 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181818220
VERSION     WP_181818220.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 131)
  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 131)
  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 131)
  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..131
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..131
                     /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          <16..110
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 snmsksaagt vsqpgrnvra ksglnrsild qgwyemrrql eykqlwsggq vlavppayts
       61 qrcaccghta kenrlsqsqf rcqvcgytan advngarnil aaghavlacg emvqsgrslk
      121 qeptemiqat a
//
LOCUS       WP_181818223             135 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181818223
VERSION     WP_181818223.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 135)
  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 135)
  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 135)
  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..135
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..135
                     /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..125
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 dlkvsnmsks aagtvsqpgr nvraksglnr sildqgwyem hrqleykqlw rggqvlavpp
       61 aytsqrcacc ghtakenrls qskfrcqvcg ytanadvnga rnilaaghav lacgemvqsg
      121 rplkqeptem iqata
//
LOCUS       WP_181818941            1307 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein [Rhodococcus sp. AG1013].
ACCESSION   WP_181818941
VERSION     WP_181818941.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. AG1013
  ORGANISM  Rhodococcus sp. AG1013
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1307
                     /organism="Rhodococcus sp. AG1013"
                     /db_xref="taxon:2183996"
     Protein         1..1307
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=126657
     Region          <133..1245
                     /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 mgaagaapas vgwsdgnskf trtvsnstps vgetvtvstk fertggtvew lqavkdlhpt
       61 cmtyvsgnts gpeiaadyvr vtgnwpvypn ispksqtfef nylvgancar atplmttmhy
      121 sgglgdgtyt dkgptitvak dattttlaav pnpivtgqav tlsatltgva qgstiefydg
      181 atklgdgqsn aagvatyawt pttagarslt akfpgtaiaa ssqsaaqnvq vnapvatsaa
      241 lsvpgtavtg tpvtlsvamt psnasgtvqf kdngsnigsp vtvsggqasl qhtftatgah
      301 sitadfvags gsvnssaaaq tvtvadpdva tsltvaapas aetgasvdls atvspsnaqg
      361 svqfsvngsp agaavpvsgg satlphtfga agsysvtaef tgaagftgst aaaqsitvtd
      421 pdvatsltva apasaetgas vdlsatvsps naqgsvqfkd ngsnigspvt vsggtatlph
      481 tfttagshsi tadfiagsgs gfvnssasaq svtvtdpdve taltvgvpas aetgssvdlt
      541 atvspsdaqg svqfkvdgvn vgaavpvagg satmpytfna aetyavtaef tgaagftnst
      601 ataqsvtvtd pdqqtslsla vpgsaqtgse vdltatvsps daqgsvqfkd ngtnigspvs
      661 vsggsatlph tfttagshsi tadfiagpgf vnssasaqsv tvtdpdvtts ltvgvpasae
      721 tgaqvdlaat vtpsdaagtv qfsvdgtavg gpvtvsggta tyaytfnaae tyavtaeftg
      781 aagftnstat aqnitvtdpd qetslslavp gsaqtgsevd ltatvspsda agtvqfkdng
      841 tnigspvavv ngaatlphtf ttsgahsita dfaagpgfvn ssaaaqsvtv tdpdqktslt
      901 vaapgsaetg asvnlsatvs psnaqgsvqf kvdgapvgta qavsggsatl pytfgaagsf
      961 qvsaeftgaa gftnstaapq giavtnpvvp dtqtvtavtl patgetgqqv tlsaavspap
     1021 tggtvqfkva gadagapvtv dasghagmpy tfnsagsfav savysgapgf egstaatqsi
     1081 tvsdpapidv etvtvvgspe tattgietvl satvqaqsgt avptgtvqfr dggieigspv
     1141 tvsngaatld htfttvgthq itavfapgag faaststphp vevsapnptd vpstvviasg
     1201 qsatagtaft ltaqvggapt lpgtvqffdg gveigqpvsv vngvaelvht ftqsgphqiy
     1261 avysggpgvq gstspvqtld vaqsgggdgg ngslgslgsl sgllfgs
//
LOCUS       WP_181819223             562 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Curtobacterium sp. AG1037].
ACCESSION   WP_181819223
VERSION     WP_181819223.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. AG1037
  ORGANISM  Curtobacterium sp. AG1037
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 562)
  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 562)
  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..562
                     /organism="Curtobacterium sp. AG1037"
                     /db_xref="taxon:2183990"
     Protein         1..562
                     /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=61437
     Region          19..473
                     /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 gqqdvdagsl rsrgrrfael laiarrhrll pfrrldfsha petadlrrdq
       61 aehlrralee agggfvkmgq llstrddllp eewteglahl qrsvtpadag avaalleeel
      121 gapvdqvfas fdpepvaaas iaqvhratlq dgtvvavkvq rpgidaavrr dvdialrvvr
      181 flartstear qvgvadvaqq yaddlvrqvd fssemrnlaa lraaqarsar pdavafpepy
      241 rdlssrrvmv meflegetls alraarstrd ldepmravld aflrqvvfdg iyhadlhpgn
      301 vvllpdgrpa lidfgsvgrl dpglretvqd llagyiqddt ariadgvlrm apvrndedea
      361 dfrrdiaafv adelgpgari gvetvddava vfgryrlkpp pdfvaaaral aifegtlrtl
      421 apsfdllees rdlargqird qlrpravrdl airelfgvvs tvrrlprrvd rigealengk
      481 lavnirlfsd rrdrevvsgl irrvllvllg agagvlsivy lamparptav lsngaagglm
      541 ggaavvlllw aavdawrarr rr
//
LOCUS       WP_181819168             710 aa            linear   BCT 28-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Curtobacterium sp. AG1037].
ACCESSION   WP_181819168
VERSION     WP_181819168.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. AG1037
  ORGANISM  Curtobacterium sp. AG1037
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 710)
  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 710)
  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 710)
  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 710)
  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 710)
  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..710
                     /organism="Curtobacterium sp. AG1037"
                     /db_xref="taxon:2183990"
     Protein         1..710
                     /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=75391
     Region          31..567
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mdtttaqpsa aiaaeaqeal aaltgrpdav fhpgqleais alvehrqral vvqrtgwgks
       61 avyflatlll rrrgggptvl vspllalmrd qvaaaaragv ravsinsana hewadtqaal
      121 ardevdvllv sperlnnprf rdeqlptlva rmgmlvvdea hcisdwghdf rpdyrrlael
      181 irslphgvpv lattataner vvedvaeqlt agpadpvfti rgslaraslr lgvltlpdar
      241 qrlgwllahl aelpgsgivy tltvsgaedi arllrengya vraytgrtdn eereqleqql
      301 kanelkalva tsalgmgfdk pdlgfvvhvg apsspvayyq qigragratd nadvlllpgr
      361 edqeiwqyfa sasmptesra aavlgalstd tamstvaleg lvdikrstle lllkvldvdg
      421 avrrvaggwv stgqpwqyda pryervaaar aaeassmlay esttacrmql lqqdlddpsa
      481 epcgrcdnca gvwyptavsd sdtsgaaaal drvgvevapr aqwpsgmsal gvpvkgripa
      541 gelvepgrai arltdlgwgg plrtlfapst pdgpvskalv dgcvralkdw pwaerptgvv
      601 amssrsrpel vaslaqaltt igrlrflgtl grsggeprgd gatnsayrla gvwdtfvvdp
      661 glaaalqahe gpvllvddlv dsrwtvtvag relrragada vlpfalatva
//
LOCUS       WP_181819228             642 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Curtobacterium sp. AG1037].
ACCESSION   WP_181819228
VERSION     WP_181819228.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. AG1037
  ORGANISM  Curtobacterium sp. AG1037
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 642)
  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..642
                     /organism="Curtobacterium sp. AG1037"
                     /db_xref="taxon:2183990"
     Protein         1..642
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=65430
     Region          19..>151
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
     Region          <460..>555
                     /region_name="PLN03223"
                     /note="Polycystin cation channel protein; Provisional"
                     /db_xref="CDD:215637"
ORIGIN      
        1 malvavglvv gpvlvpetaa datepvdlag ayvvddagal ssgqrtqver aiqdlydktr
       61 tqlyvvyvpt ftdptdhtaw gdaviqrnqi gsdsivlsva vddriadiqq ttegelsstd
      121 vedayqqdav pqlrdgnwsg aavaladglv asqappdltw lwvalavvvv gllvlllvvr
      181 arnkrrtaaa araqqeslag leraaggalv tiddelktae qevgfaaaqf gddaakpfae
      241 avdaakrsvr qafayqqqld devpdtpqqr aewanqiiai ceqahaaidh qteafdrlra
      301 ledgvedaar aldsavaaap adlaaartal drvrgayagr tlasvsdnvd qaqqvldyat
      361 ersraataai aagdkgeavi avrdaqhala qvqqltgsat aaettfaeaa araqamradl
      421 egdvaaaram rsgdpalaaa atqadavlrq gvdprdpiaa vdaltkanta idaalatars
      481 qqeqraraqr alddalrdar trisqardfi svrrgavgtt artrlseaer alddavdlat
      541 sdparavqaa rsaeqyaaaa mdaanddmgg wpgqggggng aqlgglvtgl vlggllggrg
      601 gsfgggsfgg ggfggggfgg ggggfggggg gggggfsggg rf
//
LOCUS       WP_181818985             406 aa            linear   BCT 28-DEC-2024
DEFINITION  NACHT domain-containing protein, partial [Escherichia coli].
ACCESSION   WP_181818985
VERSION     WP_181818985.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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 amino end.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..406
                     /product="NACHT domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          <54..>233
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 dvynifidkl nisdkicilh slskndrfss sdasfkvlad llcdkeeleg ticnpilvtl
       61 lyycypymnd ipnniiefyr slfdtlyarh dkikvytrek ksniigekak lcfsaicyna
      121 lieekfefwg eellryaeda ietegylked asnfiddlie itcliqpegn nryvflhksv
      181 qefyaafava nlpieykkdi yenlmvaikc seqldnfmlf lhsldskafi deitikasrd
      241 mgvvdvanmt rervenvfds alsrvfikgn stsndsvisl hydfvlgsll gidilpimsg
      301 kervpmteid lifddlfsct mdkgelnlyk fevkkqknni dtdvqtddyl fplvdylkvr
      361 gfyglmldty hqtikdfydr yyqpaydsnl rrtlamgrnf klkknn
//
LOCUS       WP_181819328             486 aa            linear   BCT 28-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein [Curtobacterium sp.
            AG1037].
ACCESSION   WP_181819328
VERSION     WP_181819328.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. AG1037
  ORGANISM  Curtobacterium sp. AG1037
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 486)
  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 486)
  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 486)
  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..486
                     /organism="Curtobacterium sp. AG1037"
                     /db_xref="taxon:2183990"
     Protein         1..486
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=53631
     Region          12..226
                     /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 mtdtttptvt dqfvmldptt vvvesnvrte dktyltkefv dsiraegvlt pvlcrraedg
       61 tvyvragqrr tlaareagvm lparivtade ntadrivqqi iendqreals nadraaawqq
      121 lsldgmaptk iakrtgrkas evkaglqvae savavetvtk hditldqaai liefeddadl
      181 hatlveaaef dpaqfehevq rardertera qiaalteewa akgytvites vysgsewyra
      241 aslrkdgqpi dqdaplpesi gedrgvrvek yfyqdeptvt lyvrneaqhg ydarpvyqqp
      301 tsqsgpmnde qkaerkrlva nnkawasaet vrrewiakfl trktlpkdvt afiatavtqy
      361 rtsvadhmgr gnslaatllg aedhgardgv sayltshpar aayvtlavvl ggvegstske
      421 twryeterkr fagyftqlqt wgyvlsdver ivldglpdid apepeqatea eseqgadiap
      481 dgdeve
//
LOCUS       WP_181819298             407 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Curtobacterium sp. AG1037].
ACCESSION   WP_181819298
VERSION     WP_181819298.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. AG1037
  ORGANISM  Curtobacterium sp. AG1037
            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 sp. AG1037"
                     /db_xref="taxon:2183990"
     Protein         1..407
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43951
     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 aavttavvgg 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 lklprsvrkv
      301 aqrllrtpvl hhvagldhpv dlreldmvar adeltvpili lhsdddgfvp ssashdlara
      361 rpdivrlevq ttarhtklwn hdadwfdari lawltevvqp tdatsar
//
LOCUS       WP_181820386             277 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: segregation and condensation protein A [Paracoccus].
ACCESSION   WP_181820386
VERSION     WP_181820386.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 277)
  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 277)
  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..277
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..277
                     /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=30671
     Region          35..277
                     /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 mtkvpyltpv pdpapdpaph lpglgpqava erraeevlvv dvsgfegpld llltlsrtqk
       61 vdlmqvsvle ladqylafvd earalriela adylvmaawl aylksrlllp pdpeaegpsa
      121 eemaahlafq lerlnamrea aarlmardrl gqdrfargap etvarqrqva wqaglidlmr
      181 ayarlrtrde frpyafdrrd vltmeqaldr vrgligyagd wtalsaflpe gweadpqrrr
      241 sataatfaat lelarqgave isqagtfapi tirrrpe
//
LOCUS       WP_181820635             738 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Paracoccus versutus].
ACCESSION   WP_181820635
VERSION     WP_181820635.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus versutus
  ORGANISM  Paracoccus versutus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 738)
  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 738)
  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..738
                     /organism="Paracoccus versutus"
                     /db_xref="taxon:34007"
     Protein         1..738
                     /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=79031
     Region          47..538
                     /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 mtgkanpdli dsldriareg tgllgaagva ragalpawfl gpkaeneavl relvgmaisg
       61 hvaarrdyap qdprlgpdrv fesdayratv ermraclaem igklagstpl ssyrnqshmy
      121 wditlpgvag yiaallfnqn nvaaeaspvt tlleitvgre lcrmagfdda qrppwghvtc
      181 dgsvanaeai waarnlkylp favaealrev palaaargle vrtgqgqarl ldldawglmn
      241 lpvrtvldlt gdlarsagve peaavaalag rtvqdlglae mhrrhapdlp vplvlapata
      301 hyswpkgaal lglgraalrs vpvddngrme igalermlae cldqrrpvml avavlgttee
      361 gavdpldriv slreafggrg lgfalhadaa wggyfmsmlr qpplgssdpn hmldidddda
      421 ppgmhlnprv earleaarhc etltvdphka gfipypagal cyrdgamrdl vsfaapvvfh
      481 dgvvptvgiy giegskpgaa aasvwlshrv ippdqsgygr llakcifasr rfyaalragf
      541 padgpvavtp fqrlpaerrg ldpqavaeqe rrlhdeiacl dndalvdrll sdptlmalfr
      601 sigsdtsivp yafnfrserg lntdlglmnr lndaifrals leeapvsgpp pkpmfvtase
      661 fdpavygegf varfarragv epqpgmgvrf listqqnpfl tatedgdfip rliailreta
      721 teaageicra aglrlkkg
//
LOCUS       WP_181820789             133 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Rhodobacterales].
ACCESSION   WP_181820789
VERSION     WP_181820789.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacterales
  ORGANISM  Rhodobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
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   Wintjens,R. and Rooman,M.
  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 133)
  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..133
                     /organism="Rhodobacterales"
                     /db_xref="taxon:204455"
     Protein         1..133
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14558
     Region          33..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(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 mgankelllg sqtpdqeeif aieelvfsvq islqramnrn gvsskelaer lgmtparvsq
       61 ifsskgsnlt iktiakvina lgeefefspk vkkrstqate qvakfaplil qfpstiweer
      121 pandvprkak iaa
//
LOCUS       WP_181820807             108 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HesB/IscA family protein [Rhodobacterales].
ACCESSION   WP_181820807
VERSION     WP_181820807.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacterales
  ORGANISM  Rhodobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
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="Rhodobacterales"
                     /db_xref="taxon:204455"
     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=11167
     Region          7..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 mltippkvtp raferlaeig aaaqgkalri avegggcsgf qyeidlddvk dddlalsdqg
       61 etvvidavsl pfladatidf seeligarfv innpnaassc gcgtsfsm
//
LOCUS       WP_181820883             352 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Rhodobacterales].
ACCESSION   WP_181820883
VERSION     WP_181820883.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacterales
  ORGANISM  Rhodobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
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="Rhodobacterales"
                     /db_xref="taxon:204455"
     Protein         1..352
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37908
     Region          13..328
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkdtvprka tldlqplaka fdqsfaqsgl vsagfgfqqs ddapqiyvgg tqsttdatpv
       61 svgaawhigs itktftavla fmlsqdglid ldapvkdylp eyaadmdpsw reitltqvls
      121 hraglrsnpd rasmralydg aldqyqflsa cwraplpqnp gtflysnigy ifaahvmetv
      181 sgqswedllr driiaplgla sfgigppadi cghrsvlglf krplapdarm adnpalfspa
      241 grmhlsipdm liwgrfllta hrgetallqa ssvqrmmdtg dgdygaglmr fqipgtdqia
      301 wghdgsnrlw ygllalvpek davafvisge grinkvaklg valldtalav ka
//
LOCUS       WP_181821065             372 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Kocuria rosea].
ACCESSION   WP_181821065
VERSION     WP_181821065.1
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..372
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     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=39864
     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 mrqfahldam raaavmlvvl ahaglevvpg gsgvtiffvi sgfiithlvl kehrrtggfd
       61 iagfyrrral klappllval vlptalyawl vrpvslgdfl gqvffffnwr ytdsqvdvlp
      121 gsivvwslsi eeqfyvafal iwlllvgrrr patalavlag taalasagar valhlggasa
      181 driyfgtdtr leaiaigvla avwyaratge rasgeraaga pawwgrdrvl vlavllylas
      241 llirdelfre tvrytaqava aclvvlwglh gptgrigtrv lagmrwkpiq llglasysiy
      301 llhlgaghal savfgelpgp agvalrvlvg taagiacwwc veepvarwhh rrraarrpaa
      361 aaapvpagqt sg
//
LOCUS       WP_181820910             133 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MerR family transcriptional regulator
            [Rhodobacterales].
ACCESSION   WP_181820910
VERSION     WP_181820910.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacterales
  ORGANISM  Rhodobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
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="Rhodobacterales"
                     /db_xref="taxon:204455"
     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=15461
     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 mttemmnire mcdafdvtpr tlrfyeskel lfptregqkr lfskrdrarl klilrgkrfg
       61 fsleeirqll dlyhmddgqe aqlsktyvta erhladmeaq raeldeaise lkeqmawgaa
      121 klaelghrkh daa
//
LOCUS       WP_181821061             478 aa            linear   BCT 28-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Kocuria rosea].
ACCESSION   WP_181821061
VERSION     WP_181821061.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 478)
  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 478)
  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 478)
  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 478)
  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..478
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..478
                     /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=52616
     Region          11..478
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mdapespdrg tttivwfrdd lrvtdhpald aacrrgavva lcvldqeseg vrplgaaakw
       61 wldgslrslr eslrelgipl vlrrgpagtv vpevlertga ggitwnrryg gpelavdagv
      121 kqwcaehgve ahsfqaallh epwtlrtgag gpykvftpfw kalraleirq plpvpgpgrg
      181 aaaevaaaag tedqvdwdlv psperaagla avwtpgeaaa werlddfldr vedyaeghdr
      241 pdrdgtsrls phlrwgeisp favrdaavrh rseqgsspgl ekflaelgwr efnwhllhqv
      301 pdlhvrhvrp afdafpwrda aeaagdvraw qegrtgfplv dagmrqlrat gwmhnrvrmv
      361 agslltknll vdwrvgeqwf wetlvdaepa sgpgnwqwva gsgadaspff rifnpltqgr
      421 kfdpearyir rwipelagde gvdphepgll gpsvgypepv vdlpasrgra ldayasir
//
LOCUS       WP_181821124             294 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Kocuria rosea].
ACCESSION   WP_181821124
VERSION     WP_181821124.1
KEYWORDS    RefSeq.
SOURCE      Kocuria rosea
  ORGANISM  Kocuria rosea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 294)
  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..294
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     Protein         1..294
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30694
     Region          23..>207
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mdrralaata lalaaltgcs ggaadpvevp arpagsnvld sagvltdaqe qqldamiedr
       61 gagtdaarva vltveeatgs iedyarevat awevgdagad ngvlvvaatg drelrietad
      121 gvrerfsdde aervvedvla pafaderyaq glgeaveqih vyaqggeppr epfdwallgw
      181 vaggfglvgv lvawwiaadl rrrrriadee lraarqrdpe lrlteeqhaa yrtyryhhrk
      241 pdavtnpavw lplylanpgl ysggsgggts gdgqggssfg ggggftggga sgsy
//
LOCUS       WP_181821184             357 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Kocuria rosea].
ACCESSION   WP_181821184
VERSION     WP_181821184.1
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..357
                     /organism="Kocuria rosea"
                     /db_xref="taxon:1275"
     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=38474
     Region          1..334
                     /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 msdrhnrlna lrlvlaslvi vghawpltga dgptlvflsd vavngffvls gyliaesrvr
       61 ttlvpylwrr flriypaflv sllvvaavfa plaaalegrp ldlasaagfv lsnadlkmsq
      121 wgidgtltav papdswngsl wtlfheavay vliglvlsla vtarharwvl pgmfllmlvl
      181 rpllegplev ttsiylsgar lvgyflagaa vwawagtwrp twvhvagagv vyavltdqgw
      241 adlygqlpla vlllglgaap srnwttrtdl sygvyiyayp vqqllvllgt aswgvavnsv
      301 lvlvltlpla llswrlvekp alrakawldp rdrpdrrvps pgaadphaaa vtgrhpd
//
LOCUS       WP_181821713             556 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase, partial [Thermoactinomyces
            intermedius].
ACCESSION   WP_181821713
VERSION     WP_181821713.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 556)
  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 556)
  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 556)
  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 556)
  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: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         <1..>556
                     /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]"
     Region          <1..554
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 ltqnkmmvth iwadqvlfqv tgngydpegd illektkvnv qkwdslkrlm eiaalcnnaa
       61 fiqkskkgll nkknqweldg dptegallvv akkagldrnh ldktwervke ypfdserkmm
      121 svwvkqagkh flfskgapdv llnkcthllv dgkvvpltet krkkimqmne qlaakalrnl
      181 afayreikpk pvntdlkdwq meqrlifvgl tgmmdpprpg vkeaiqqsrq agiktvmitg
      241 dhqataeaia telkikrpgg ltltgqdlyn mkdeefiriv ndvdvyarvs pehklrivka
      301 lqkkghvvam tgdgvndapa ikaadigiam ggmgtdvske assliladdn fativaavee
      361 grniyenirk fisyllasnv geilimflam laslplplvp iqilwvnlvt dglpamalgv
      421 dpaeenamqr pprdsresif argvgwkivt rglfigvcsl aafwisyiet penlvraqtv
      481 afatlvlsql iyvfdcrsqg tifqrtpldn pmlvlavlss vvlllgviyy pplgpvfhtv
      541 plglrewilv tvtstm
//
LOCUS       WP_181821895             692 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Citrobacter].
ACCESSION   WP_181821895
VERSION     WP_181821895.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=75749
     Region          139..679
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mshtlarhsv kkrdavflwv llswlafall pswsldygll estrdeivda ygwsqvnvsw
       61 lwyllpglll irpfqeatre qrnrhyldag wslfcmafvv isatvegrgl gyatlvlfva
      121 lgaimtlalt rlewlggdrf vigslvaiva ligvfivwps iaifipmftg dtgefaplaf
      181 mtvlsqahii qviinsials iavgvgctff glvlaiyttr iarrsaiigr ifsilpivtp
      241 pfvvglgvtl mmgrsgyvte wmvdwfgltn tnwlygftgi wlaqvlaftp mafmildgai
      301 ktihpsleea sytlrasrwq tfngvfvpll kpalanafli vivqsladfs nplvlggnfd
      361 vlatqiyfyi tgsqldyqaa stlgaflllf sllvfcvqym wigkrsyvtv sgksyrgdvq
      421 plpvtlvwsv vvilavwvaf nallygsify gsftvnwgvd ytltldnfik lfgqgmsdga
      481 wpslldtlly agiaapitaa fglliawivv rqqfkgkkti efttmlcfav pgtvagvsyi
      541 lafnsapvyl tgtaaiviis mvmrnvpvgi ragiaglgqi dksldeasls lragslrtit
      601 hillpllrpa ilsaliysfv raittvsaiv flvtpdtrva tayilnrved geygvaiayg
      661 silivvmlai ififdwlige arisrskakn qa
//
LOCUS       WP_181821640              69 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein, partial [Thermoactinomyces
            intermedius].
ACCESSION   WP_181821640
VERSION     WP_181821640.1
KEYWORDS    RefSeq.
SOURCE      Thermoactinomyces intermedius
  ORGANISM  Thermoactinomyces intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Thermoactinomyces.
REFERENCE   1  (residues 1 to 69)
  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 69)
  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 69)
  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 69)
  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..69
                     /organism="Thermoactinomyces intermedius"
                     /db_xref="taxon:2024"
     Protein         <1..69
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
     Region          <1..69
                     /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 apelekvdee mgdqlkiakv nvdnspetag kfgvmsvptl mvfkdgemvs kmvgaqpkeq
       61 lvawlkeyv
//
LOCUS       WP_181822095             414 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase
            [Enterobacteriaceae].
ACCESSION   WP_181822095
VERSION     WP_181822095.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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="Enterobacteriaceae"
                     /db_xref="taxon:543"
     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=47448
     Region          2..406
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maltdikvrt akptdkqykl tdgngmhllv hpngskywrl qyrfggkqkm lalgvypavs
       61 ladararrde arkllansid pgdkkkndkv eqeeartfeq laiewhatnk kwseehsrrv
      121 lkslednlfp aigkrniadl ktrdllvpik avelsgrlev asrlqqrtta imryavqsgl
      181 ldynpaqemv gavassnrqh rpalelkrtp ellqridsyt grpltrlave ltllvfirss
      241 elrfarwsei dfetsmwtip aereaiegvk hsqrgskmrt phlvplsrqa lailkqvhkl
      301 sgerdfvfig dhdhrkpmse ntvnkalrvm gydtkvevcg hgfrtmacss liesglwsrd
      361 averqmshme rnsvraayih kaehlderrl mlqwwadfld anrekevspy dfgk
//
LOCUS       WP_181822569             230 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Citrobacter].
ACCESSION   WP_181822569
VERSION     WP_181822569.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 230)
  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 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   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
REFERENCE   4  (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 13591165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     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=27038
     Region          30..152
                     /region_name="Autoind_bind"
                     /note="Autoinducer binding domain; pfam03472"
                     /db_xref="CDD:427319"
     Region          168..221
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mkdtyyndtr inaliqneln kffedyngii yayaimnkkd psqmriinnn ptwfdiyler
       61 kyqfidpvii ralrcvedff wenkvilsgg ynltrifnes sehniyqgqt fplhdylnnl
      121 vvlsiisqed sgvdmeknrs hfmhfliqlh qktlnlyskv dqkknvflsp rerqilkwvs
      181 agktyaevsv ilsitertvk fhmsnamkkl gvnnarhavk lgmelrlldn
//
LOCUS       WP_181822452             158 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: prepilin peptidase [Citrobacter].
ACCESSION   WP_181822452
VERSION     WP_181822452.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..158
                     /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=17017
     Region          <4..146
                     /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 mitalpfllc yvsstlylal ydlrtgllpd rvtcpllwig lvfhqcffpa rladalwgav
       61 agymgfagly wtyrfirgqe glgygdvkfl aalgawhgwp slpllvlcas llaslcvave
      121 tlicgkralr nplpfgpfla aagfitgchq lmtggisl
//
LOCUS       WP_181822356             249 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Citrobacter].
ACCESSION   WP_181822356
VERSION     WP_181822356.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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"
                     /db_xref="taxon:544"
     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=27141
     Region          4..248
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mqrkimvvta aygydtvrda ggqiamlpvi anagadgvei rremftdael ntlpalasai
       61 esvglqacys vpqplfvtda slnpqlpall qeaqtlralw lkvslghfqh tdsfdtlrdw
      121 ltssgmalvv endqtacgrl esmrrfnaac qqqalavqlt fdmgnwlwvg dspeeaanal
      181 assvgyvhvk aatrhhdsyr aippdradpr wlallsalpa hvprgiefpl egadltavtr
      241 ryvdvlrke
//
LOCUS       WP_181823138             203 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: lysophospholipid acyltransferase family protein
            [Citrobacter].
ACCESSION   WP_181823138
VERSION     WP_181823138.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 203)
  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 203)
  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..203
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..203
                     /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=22897
     Region          1..203
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mtrllrtlft lcvvwpviwl wlglrvrhre rlpthgpaii vanhnshmdv fallslfslr
       61 rqgqvhpvaa adyflrnkwm awfalnilni ipvmrkggda nplarceqal regktlilfp
      121 egtrgepgkl aplksglwhl sqrfpevpii pvwltgterv makgnriplp lfidvtigga
      181 myadpdkraf mdnlraqlla lsq
//
LOCUS       WP_181822285             249 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 4'-phosphopantetheinyl transferase family protein
            [Citrobacter].
ACCESSION   WP_181822285
VERSION     WP_181822285.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 249)
  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..249
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..249
                     /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=27457
     Region          1..156
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mgihfargil teghlisvrl ptschldarn lpahrqtrfl asrgllaelm fmlygtlelp
       61 eiiikakgkp afreqnlpsf siayagnvvg valategecg ldmelqratr sfvpphcspp
      121 pvfssnerlw iskqndpnea raqmitlrqs ilkltgdvrn ddprelqllp gagrlkcahv
      181 apleaicdae dllvwsvavt pgidklqvwe fdgkqgwknl pdiqtranae tgrlmrfaql
      241 saaksythn
//
LOCUS       WP_181823351             146 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181823351
VERSION     WP_181823351.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 146)
  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 146)
  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 146)
  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..146
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..146
                     /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..136
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 vsknhamivi edlkvsnmsk saagtvsqpg rnvraksgln rsildqgwye mrrqleykql
       61 wrggqvlavs paytsqrctc cghtakenrl sqskfrcqvc gytanadvng arnilaagha
      121 vlacggmvqs grplkqepte miqata
//
LOCUS       WP_181823323             184 aa            linear   BCT 28-DEC-2024
DEFINITION  ParB/RepB/Spo0J family partition protein, partial [Escherichia
            coli].
ACCESSION   WP_181823323
VERSION     WP_181823323.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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 184)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>184
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          31..>184
                     /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 msvteskakt erkssrkpak tqetvlsall aqteevsvpl asliksplnv rtvpysvesv
       61 selaesikgv gllqnlvvht lpgdrygvaa ggrrlaalnm laernilpad wpvrvkvilq
      121 elataasmte nghrrdmhpa eqiagframa qegktpaqtg dllgysprhv qrmlkladla
      181 pvil
//
LOCUS       WP_181824114             313 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein [Blautia obeum].
ACCESSION   WP_181824114
VERSION     WP_181824114.1
KEYWORDS    RefSeq.
SOURCE      Blautia obeum
  ORGANISM  Blautia obeum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
REFERENCE   1  (residues 1 to 313)
  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..313
                     /organism="Blautia obeum"
                     /db_xref="taxon:40520"
     Protein         1..313
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34333
     Region          1..238
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 mkkwigrmav llafvltlsg stlaafgkip satkefyvnd yagvfsdtwk eelckageql
       61 yedttaqlvv ltvdttdged isdyavetgr kwgigskkkn ngvlivlsvs drkvwvsvgy
      121 glegklpdsk igrlldeyav psykdnqfek gtvelyyall neireeygle kitapryenv
      181 qqdvdddede gtvweialgl vmivllmvga yllcvmlpvf livtmvlilk glimklsgkd
      241 tadywkknfs rmsvlhrlfn slfplswilg rggkssggss gndddrdddy dsydsgssgd
      301 ggsfggggag rdf
//
LOCUS       WP_181824079             310 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Blautia obeum].
ACCESSION   WP_181824079
VERSION     WP_181824079.1
KEYWORDS    RefSeq.
SOURCE      Blautia obeum
  ORGANISM  Blautia obeum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
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="Blautia obeum"
                     /db_xref="taxon:40520"
     Protein         1..310
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35052
     Region          31..290
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mnkdqnline faiktlkenl nvmyaqiwre gqltaeykrm pvktrlntws ackgvvscaa
       61 gialdeglir ldekivdifp eyapenpegy lgdvtlenml tmttglessl ffcdwperyt
      121 tpdwiryffe nakvikkpgt ewlysnfnty miscaiekra gvnlleylrn rffeplgign
      181 pdwtlcpkgh vhaanglyvn ideftrygqm ilhkgnyngk qlvpesymkm atsnlvdnsa
      241 agspgnlysg fgygyqfvmn peagsyrsdg nygqfclafp dkdavvtvms legdfqkign
      301 hlwttvipel
//
LOCUS       WP_181824124             354 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Blautia obeum].
ACCESSION   WP_181824124
VERSION     WP_181824124.1
KEYWORDS    RefSeq.
SOURCE      Blautia obeum
  ORGANISM  Blautia obeum
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Blautia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..354
                     /organism="Blautia obeum"
                     /db_xref="taxon:40520"
     Protein         1..354
                     /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=40847
     Region          13..333
                     /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 mnkekcktnr qirhynsidg lralsclgii vmhieantky qlggsavfdq fipsftwlvy
       61 lflmisgfgm cagyldkfhn nvidmeafyk krymkilpff glllvvafvm ehsvssvyei
      121 sieilllhgl lpnnavsvig vcwtlgvifl fyllfpafsv lmkskkrawi slvislwivf
      181 vcnqyffsdy fvtesftprh nflyclpmfi ggglvylyre eikticekyr giflvgcmaa
      241 sifwykiped skslfyigtl mlyclwlsya igsnskflss kpmkflssis memylaqmii
      301 frivekmhll yvfgdkgisg wisflvafvl tvlglicfie cyklilrflk kgke
//
LOCUS       WP_181824549             145 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Falsiruegeria litorea].
ACCESSION   WP_181824549
VERSION     WP_181824549.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria litorea
  ORGANISM  Falsiruegeria litorea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Falsiruegeria litorea"
                     /db_xref="taxon:1280831"
     Protein         1..145
                     /product="YybH family protein"
                     /calculated_mol_wt=16287
     Region          2..124
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 makeeiadli etyllawnar dfekmaslfs epatyivpsg nlhipdkdal vsklrqqffa
       61 leaegfdhte ieevvvtmcn dyaalaelrn lrrlksdgse iaaidalyic vleegrwrls
      121 vamagdcgwn rdieqsqiae iaref
//
LOCUS       WP_181824629             344 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Phaeobacter gallaeciensis].
ACCESSION   WP_181824629
VERSION     WP_181824629.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter gallaeciensis
  ORGANISM  Phaeobacter gallaeciensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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..344
                     /organism="Phaeobacter gallaeciensis"
                     /db_xref="taxon:60890"
     Protein         1..344
                     /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=38770
     Region          56..344
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 masiyksrdk wtaqvnldgk rrsrtfdrkr daerwarqee aqqdatgtvq tviadltfnd
       61 viaayldefg eqasrsklgt irhiseligr tplpdltsar irefakmrka egagpatigq
      121 dltyihtilk mggavadvdt daalgaytka railnasgtv grptertrrp tdaelvalre
      181 qwakrrrvvp mwdltqfaia tamrlseicr irwadldveg rmiwirdrkh prskkgndqn
      241 vpllcgpvvi dgvtvdpmel vmrqhrtdpe ifphdpktvs ttftrgvasc gisdlrfhdl
      301 rhdgvsrlfe agyqieqvsl vsghqdwgml rrytqikpes lhra
//
LOCUS       WP_181824639             249 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Phaeobacter gallaeciensis].
ACCESSION   WP_181824639
VERSION     WP_181824639.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter gallaeciensis
  ORGANISM  Phaeobacter gallaeciensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 249)
  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..249
                     /organism="Phaeobacter gallaeciensis"
                     /db_xref="taxon:60890"
     Protein         1..249
                     /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=26244
     Region          36..234
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mtfkeklsnp tirltahvct ipsaavtqam aaarsdavii dmehgaidya tahamiaata
       61 gtscaplvrv tendsaqvkr vldlgaegiv fplirtaeda eqavaslryp pngtrgfgpf
      121 lahsrwgtsl meyresvdgh lvcfllvetr davenieaic avpgidaiip aqfdlstdlg
      181 vsgqfdhpdf laavakveda assagiplgn vglakpqadg llakgyriia gfdilwlkam
      241 aaetqswir
//
LOCUS       WP_181824684             381 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: aromatic ring-hydroxylating oxygenase subunit alpha
            [Roseobacteraceae].
ACCESSION   WP_181824684
VERSION     WP_181824684.1
KEYWORDS    RefSeq.
SOURCE      Roseobacteraceae
  ORGANISM  Roseobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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 381)
  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 381)
  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 381)
  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..381
                     /organism="Roseobacteraceae"
                     /db_xref="taxon:2854170"
     Protein         1..381
                     /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=43782
     Region          24..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 mqtmtveklr qeltnlkald reqartmpts fytsenflel ekehifhrew vclghvgeip
       61 nagdfyttel vdeqllvsrg hdgevyvlsn vcrhrgnmve tnergnrrsf vcqyhawtyd
      121 tdgrlktapl mkkaknfdlk gcrlpqfkte lwnnfifvnl dgqaaplteq lgglqdilqn
      181 yhhedrnllf sdtavwgtnw knltenfmeg yhlfsthpqt lqpmtptqlc kkvpgqdrwt
      241 ayrayyhsdf pprgpfhpdm tdeeknnsvl fntfpsfvca vasnytlflc lrpagadkva
      301 irwgvcglkt dpadpevvdy vnlcksfnae dkekletlqi aqntryyssg plapddlegt
      361 iwdflgymek mlgaekelte v
//
LOCUS       WP_181824687             947 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Phaeobacter
            gallaeciensis].
ACCESSION   WP_181824687
VERSION     WP_181824687.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter gallaeciensis
  ORGANISM  Phaeobacter gallaeciensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..947
                     /organism="Phaeobacter gallaeciensis"
                     /db_xref="taxon:60890"
     Protein         1..>947
                     /product="beta strand repeat-containing protein"
     Region          <5..919
                     /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 matftvsntn dsgagslrqa iisangaagd diidfsiatg stinltsgel vissgitfda
       61 didnnsatrd vtvnaggasr vfsfvsgtss idnllitggn lagdggnltn sgvangkgen
      121 tqgagifnag sltltnstit ansaggggag assngggggf ggftgstggd ggvggyggtg
      181 gvggvnsggv ggtndngasp gnggggatna gggvgglgen ggnnggtggt agsagggggg
      241 gaagysqsgg hgghatggiy nsgalvitds titsnlgagg ggggagggsa vagnggdgvg
      301 aitnsggtlt isqstidtfs gnvggggggg sggggtagts annidgaytv sgtettfvvn
      361 ttldtgadat vtgdlaaeta dgdglslrea vllanpgdti tfdgsldaat iklvsgtlei
      421 itgenliidg dldndnsadv tisgdannsg tvnagdvrvf tvqsgaslql dgvvvsggyd
      481 tgangsngtn gadqipgsss eggngtdgtd ggyaaggiln agaltllnst vsnstaiggt
      541 ggaggdggtg gvslpngngy sggaagegga gghaaggiln lgtgtltltd asiigitsts
      601 gvggvggagg dggpaqgsqt dggparggga ggdggvaaai vnfalnlvng vptvstntln
      661 agaggtggtg gtggagqtgt ggtggiggss dtagssgnng sggalggtsg eisevgdsga
      721 rgdgsgggag ggggytglta pevvnvfapv irnldgdsnt fteggsaval dtntaaavsd
      781 eddtefnggs ltvslsangt ssdqlsilat gdntgeidvd ganvefggsv igtvaggtng
      841 tdlvvtfttg sarenavesl isalrfnntg sppntstrti dvtlndgdlp satsqvtvtv
      901 daaninpsvt llpgdlsfte dtagnvalga avfadpdsdp vtvtlav
//
LOCUS       WP_181824666             268 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: trypsin-like serine peptidase [Roseobacteraceae].
ACCESSION   WP_181824666
VERSION     WP_181824666.1
KEYWORDS    RefSeq.
SOURCE      Roseobacteraceae
  ORGANISM  Roseobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 268)
  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 268)
  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..268
                     /organism="Roseobacteraceae"
                     /db_xref="taxon:2854170"
     Protein         1..268
                     /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=28241
     Region          36..237
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mirlaailws vlcafavqad gvrrlsdrgd llgweavgrl diqgagyctg tliapdlvlt
       61 aahcafdstt grpypsdkim fraglrdgvs iadrgvaqva vppefepkga vsrgrirvdv
      121 almrlaepis vaqanpfalh sgdisnaevs vssfgrgrse aisrerscqi lwqdaelfaf
      181 dcdvtfgssg salmarvgdr grilavvsav gtvdgrdvgy gmalpnvvaq lkqqlrrdaq
      241 apkatirrlr vgsglsesga kfvrpggs
//
LOCUS       WP_181824848             412 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Aeromonas sp.
            ARM81].
ACCESSION   WP_181824848
VERSION     WP_181824848.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas sp. ARM81
  ORGANISM  Aeromonas sp. ARM81
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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 412)
  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..412
                     /organism="Aeromonas sp. ARM81"
                     /db_xref="taxon:1747384"
     Protein         1..412
                     /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=45962
     Region          1..400
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mlrgvqcrly ptaeqreffa rsfgcvrfvy nealaycqae reaqrkhpna idlqkrlvsl
       61 kgqypwladv dsqalkescr dldkafaaff rrvkagqtpg yprfksrndr ansytatqrl
      121 hadfcdrrik lpkcgwvkcr glrkfdgkik sitvrqsasg rytasllied ghaeplptal
      181 pagvavtgid mgcktegdrq qlatlstgqv immpaylkga lkrlaraqrk larktkgsnn
      241 rrkqrqlvar lhervanqrr dflhqtthrl trenqalave dlnvkgmmas prpkqdeqgg
      301 ylpngraakr glarsltnvg lgefarqlry kalwrgvall ecgrfepssk tcsgcghrla
      361 elplavrawv cpecgaehdr dvnaainirn faimavgags pelklpergt aa
//
LOCUS       WP_181824740             574 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: metallophosphoesterase family protein
            [Roseobacteraceae].
ACCESSION   WP_181824740
VERSION     WP_181824740.1
KEYWORDS    RefSeq.
SOURCE      Roseobacteraceae
  ORGANISM  Roseobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 574)
  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..574
                     /organism="Roseobacteraceae"
                     /db_xref="taxon:2854170"
     Protein         1..574
                     /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=64123
     Region          6..234
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mseplftlav iadthmrapd gdlsspysvn akandraava vdlihaqnpv ltihlgdmvh
       61 alphmeeyda aceeaqrils glhptlhfvp gnhdigdkpl easpanvvtq qtaarysdhf
      121 gaqwhhvdhg dcrfvminas ivnsglpaee eqfawlekiv qteqrvflft hyppfidtpd
      181 edehydnyge pgrsrvieia rkykieavls ghvhqfffnr vedtkyyclp stsfvrqdys
      241 elynvapdtd fgrndlgkfg vtlidvyedg hklrflptgg aessavvdls lrkpaaktel
      301 tpfmrhawyq srdlpysgak eefgrkrarn dypllrlwqm gietvrtplv dlahaesrrr
      361 vqdfastgir fhmfttsmps aavlqliadn aqvlsalevv qvdedltrvk aiakaflkvt
      421 dvpiyvsrpg ssadevivgr mfshnvwtgy ryanraevld aladtslplr pifavawrad
      481 wvgkiggmqa efakrgiqga aavqlmtgnp etanfdeeyi eegvlelmrn rdafplvslm
      541 ldtfetfdrg fnpraglidr vgnltaagra ltkl
//
LOCUS       WP_181824894             278 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Enterococcus
            durans].
ACCESSION   WP_181824894
VERSION     WP_181824894.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus durans
  ORGANISM  Enterococcus durans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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="Enterococcus durans"
                     /db_xref="taxon:53345"
     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=31021
     Region          44..274
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mfplnlgira hdltittken lvqklqelrl shiqfapqka fskeltlgnm tlgtashfgt
       61 yfqkndiels ilgcyvniss edshirkqal atfkhqislc saygakmiat etgsvetgyt
      121 prnfteeayq iardsviemv keaekfgvtv aieaginhpl ysyqlakrli hdvaspnlkl
      181 ildcanlicp qnhgeqkaii qnaleelgph laalhlkdyi iknktiqmvp vgqgcldfrp
      241 llhfakydrp llyttleatp eksvvqavth lerlydic
//
LOCUS       WP_181824900             241 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Enterococcus durans].
ACCESSION   WP_181824900
VERSION     WP_181824900.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus durans
  ORGANISM  Enterococcus durans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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 241)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..241
                     /organism="Enterococcus durans"
                     /db_xref="taxon:53345"
     Protein         1..241
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27407
     Region          2..241
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mvitgtyasv vlrrpnhyta vlpnklnaat kaifllhgfg fdeqswlhnt plvqysekyn
       61 vaffspdagi sfytdhidgq nygeaigkef yeemqrvfnl dmtrentaia gfsmggygsv
      121 llglrfsqfy gwiggfspaf vfykkernea hfnhvfskgd ygsendvlvr yqellesdss
      181 ipsiiftcgv edplcqqten iiqqlkeidp kariefktqs gfhdfslwkn dlsmflekfa
      241 k
//
LOCUS       WP_181824909             406 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Enterococcus durans].
ACCESSION   WP_181824909
VERSION     WP_181824909.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus durans
  ORGANISM  Enterococcus durans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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 406)
  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 406)
  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 406)
  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 406)
  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 406)
  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..406
                     /organism="Enterococcus durans"
                     /db_xref="taxon:53345"
     Protein         1..406
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46445
     Region          36..391
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mnpkilsivv egvktyknnv fsldfmteqr vfqhekddkv vtsvskhgnl nniialagvn
       61 asgktsslll inyvlhlvfl gsnanfkkqi idlfdekiki httficdnfv ykttselekk
      121 kyddsirief cneiicrkki nkntskkdlk fnneqeepnl eiverkkldg tilkflkned
      181 siipsqlsnl pknyvidtfs qtdmnflsgg tgfpsemimy ldqtieeisl qlpkdlkked
      241 ltidklmfnl kfeneprktv sivdlnmyls sgtikglgll nriiralkvg gyllvdelei
      301 hfnksiveni idlfqsdvne kgatiifsth yselldsltr rdsirvvrki enkieiesln
      361 nlankedknr sdiknsdlfl sglfgtapsf drywklnrfi kglieg
//
LOCUS       WP_181825231             438 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase
            [Enterobacteriaceae].
ACCESSION   WP_181825231
VERSION     WP_181825231.1
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=50387
     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 lekecytvis retkakdvtp lqiktilsgi iqrdavvhan
      181 rirsylmaaf nyglkadndp mntnvgitfg levnpvsaip kqssaekvgd twltleelrf
      241 vmeqfaeatn vgplmqhlir fcvyaggqrp femiasqwsa idwqqktllv iadvsknkre
      301 hlipltesal qelasvkelt kesnspyifp lstngerpvr tdslarsimy frafnpefkv
      361 ftardlrrtc ktlmgeagis keirdriqnh alndvsskhy drydyltekr raleiwedrv
      421 nnyqrqqenn vvnlfgrr
//
LOCUS       WP_181825189              97 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Citrobacter].
ACCESSION   WP_181825189
VERSION     WP_181825189.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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   Wintjens,R. and Rooman,M.
  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 97)
  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..97
                     /organism="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..97
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10454
     Region          5..50
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mklsekvkal reaeglsqak fsqiidlsls tlkkyetgnf epsgtallki ttnpqfqkyt
       61 lwlmtdktap eagqispvva hsgpdettss psdrkig
//
LOCUS       WP_181825200             249 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 4'-phosphopantetheinyl transferase family protein
            [unclassified Citrobacter].
ACCESSION   WP_181825200
VERSION     WP_181825200.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 249)
  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..249
                     /organism="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..249
                     /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=27679
     Region          20..156
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mathfargil teghlismrl psschhearr lpthrqtrfl asrgllaelm fmlygtldlp
       61 eivykakgkp vfrdknlpsf siayagnmvg valttegecg ldmelqrapr gfisphtadv
      121 ptfssneslw iskqndpdea raqmitlrqs vlkltgdvrn ndphelqllp vsgrlkcarv
      181 aqieaicdae dllvwsvavt paidklqlwe fdvkqgwksl pdiqtranap mgrlmrfaql
      241 saatsythn
//
LOCUS       WP_181825332             250 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LexA family protein [unclassified Citrobacter].
ACCESSION   WP_181825332
VERSION     WP_181825332.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
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   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..250
                     /organism="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..250
                     /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=27830
     Region          32..242
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mlnttqatfs nlriyhfaks gnnagmenke irkanlesly ekrqnesgmt kaqfaeliet
       61 spaalsqllg pnpnrnigdr markiettln lpfgwmdvlh tsektsnvsf reindakgsy
      121 pviswvsagq wmeavepyhr rsidrwydtt vecsedsfwl dvkgdsmtsp vglsipegaa
      181 ilvdplvepr ngklvvakle sdneatfkkl vidagrrflk plnpqypmle vngnckiigv
      241 vvdakilnip
//
LOCUS       WP_181825321             376 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-methyltransferase [unclassified Citrobacter].
ACCESSION   WP_181825321
VERSION     WP_181825321.1
KEYWORDS    RefSeq.
SOURCE      unclassified Citrobacter
  ORGANISM  unclassified Citrobacter
            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 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="unclassified Citrobacter"
                     /db_xref="taxon:2644389"
     Protein         1..376
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=40599
     Region          4..366
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mtyqlhvgrc edalktlpdn svdaivtdpp yglsfmnhkw dydvptveqw qeclrvlkpg
       61 ghllafggsr tyhrlvvnve dagfeirdqi lwiygsgfpk shnldgdfdg wgtalkpahe
      121 pivmarkpfk qtvsanmneh gtgainidac riptdealng gsggllshqr dgtkpvadye
      181 qapegrwpan iihdgsdvvv safpdakgqq galtgnepss kmgaancygq mdrrhestpr
      241 idssksaarf fycakvkpke rdeglerfia tsasdmtggr kegsvgindp ragagrtsga
      301 knnhptvkpi almsylcrli tppggtvldp wmgsgstgrs aieegfnfig idlnpdyvti
      361 asariaysfk ktteaa
//
LOCUS       WP_181826021             709 aa            linear   BCT 28-DEC-2024
DEFINITION  GumC family protein [Citrobacter freundii].
ACCESSION   WP_181826021
VERSION     WP_181826021.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            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 freundii"
                     /db_xref="taxon:546"
     Protein         1..709
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=78087
     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 kairdmklde npeftgekag
      121 argadsnesr qlrmeqalkt laknlnvigi rttnlasity estspqvaad iangvaqafi
      181 nytveqkrlk vekarelnfe kmeeiqtsia kqkdemdnyl knaglltfrg idgfeteqls
      241 ivtnrladat qrrvaaesvy nevngggksi esvislpsvs nhaqiqdlri aliqaqrtls
      301 eqrkvygpkn pailkaeadv qsiqnqtgrv lgelkvglrq qylaaladek nyqqqvteqk
      361 eifqkmaskr dawnsqklsl dkmedlyksl yqrtqelsls gvnadavlyd pavpalkpak
      421 pnksllllmv vmlvvvfsim yfivkaamdn sigtlsrmkk rlnvaplgei rrfsgtsgra
      481 qvrdmimknp lnadivhgir trimldnrpl qtlavasteh gdgrsllanl lansfsfdqk
      541 tllidadffn tdglsselas vtsaglaell rgevqlekar vtlsdhldfi phgkttissl
      601 lmlssghvep lmrelkshyq riiidvaavn qsqdvqlikr avdgvifivk agtgsagqia
      661 naldkleenn gvvigavlna veekdletqe glrslnfstd qlmttpgrv
//
LOCUS       WP_181826182             653 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidase U32 family protein [Citrobacter freundii].
ACCESSION   WP_181826182
VERSION     WP_181826182.1
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..653
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..653
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=72871
     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 dlarssvgrt 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 gdevltlkfd crpcemhvig kmkhhilkmp lpgsvvasvs peelmktlpk rkg
//
LOCUS       WP_181826176             704 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Citrobacter freundii].
ACCESSION   WP_181826176
VERSION     WP_181826176.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 704)
  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 704)
  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 704)
  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 704)
  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..704
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     Protein         1..704
                     /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=77887
     Region          10..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 mlhvswdpvl igisfivafi asfialdsag kvaissrres tfwrlsggat lgmgiwsmhf
       61 igmlamkmsm pinyhlslta fsffialisa tvainiaisg ntlstkrlli atsilsagvv
      121 tmhyvgmyav iehvaitwdr slillsviia vaasgvglwl afhlrqnsrr alinrliaaf
      181 imalaiasmh ytgmgaatft hfghtahdgl stlelsiwvc avtlvilgim lvvsmvdsql
      241 rtsrladnlh qlncqlehqv hfdaltglan rtqidtclla clrhsklhqq hfalvfidld
      301 rfkvvndtwg hhigdqllia stqriftcld dsmtlarlgg defillvpdc nqqdisallt
      361 riadvigepf tlfghtirvs lsagssiype hgstlhelkv kadmamyhvk qagrngwaiy
      421 hpemeaiadt pptflqelsq alernqfelw yqpkytagdh sltgfeallr whhpergmll
      481 paeflsaled tgliipvgkw viqqaclqlh qwtlqgntew tlavnlspaq feqhdiidvv
      541 cnalaqyqls pacltlelte stalknlkrs vevlnafsal gitvsiddfg tgysnilmlk
      601 slparelkid rifvkdisen skntkivsti idiahsmnmr vvaegietqe qeilltqmgc
      661 smlqgflfak plpahkihel iqqensikqk pvvhplshrq sitl
//
LOCUS       WP_181828202             134 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator, partial [Klebsiella
            pneumoniae].
ACCESSION   WP_181828202
VERSION     WP_181828202.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 134)
  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 134)
  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..134
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         <1..>134
                     /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..>123
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 ldkygarfvh srgagyrlqv dnaalfsalq hqerrkhatp rsaqervhyl lvrfltsafs
       61 lkledladew fvsrgtlqnd maevrerlah yqltietkpr ygmklfgaem airacltdll
      121 fqlhladaen plln
//
LOCUS       WP_181828321             328 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CobW family GTP-binding protein [Pectobacterium].
ACCESSION   WP_181828321
VERSION     WP_181828321.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..328
                     /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=36057
     Region          1..324
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mltkvnlitg flgsgkttti rhllsqkped evwavlvnef gevgidgall adsgavlkei
       61 pggcmccvng lpmqvglnml lqqkkphrll ieptglghpk qilslltsdi yqpwltlqst
      121 lclldarqls dtrytgnenf rdqlaaadii iankrdtyna ddlaalqqwq qasgdgrqii
      181 easegkidrq lldqsrhnlr elpdgahhhs hkptnglaal qlpggqswrr slnqgqgyha
      241 cgwifapeta fdtaalldwv rlspvnrvkg vmrikegtlv vnrqghdlhi etrsaapmds
      301 rieiinetpa ewntlqasll karlanvd
//
LOCUS       WP_181828539             498 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent decarboxylase family
            protein [Pectobacterium].
ACCESSION   WP_181828539
VERSION     WP_181828539.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 498)
  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 498)
  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..498
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..498
                     /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=54454
     Region          25..493
                     /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 mttmsqlvet avnpilassa qsieayqeai tqssqavmqw lqqpemyqgk tvaelrerit
       61 ldfnpqglgn qaaieraiey flkdslsvhh pqcvahlhcp slvvsqaaev linatnqsmd
      121 swdqspsati iemkliewlr tqvgyqsgda gvftsggtqs nlmglmlard affarqghsi
      181 qqdglvgnlk kikvfcsena hfsvqknmal lglgyqcvtl vktdrfarmd lndlaekvaq
      241 aeangeqila ivatagttda gaidplraia tlaaehqiwv hvdaawggal llsekyrdyl
      301 dgielvdsit ldfhkqffqt iscgafllke arhyelmryq aaylnsefde aqgvpnlvsk
      361 slqttrrfda lklwmgleal gqqqyaaiid hgvtlaqqva qyvaehasle lvmqpqlasv
      421 lfrfrpqqla tandatiall nqrigdalle sgranvgvte fngvtclklt llnptvtldd
      481 vkvllalves taqpllta
//
LOCUS       WP_181828557             409 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SAM-dependent methyltransferase [Pectobacterium].
ACCESSION   WP_181828557
VERSION     WP_181828557.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..409
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..409
                     /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=47427
     Region          132..404
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 msstqtqvvr hpsnitrytr arkvlfllls rieggglrlr epeghetlfg drhaplqgei
       61 tihhhrvyrr vllggsiaag esyidgdwss tnltpvlqll aqnqalvdtl etrfgwliap
      121 lhrfihwcrr nrpqqaqkni aahydlgnhf yrsfldsemh yssawyqhpd mtleeaqqak
      181 lrrlceqlal retdhlleig tgwgglaela areygchvtt ttlsqqqydy averiqqagl
      241 shkvtvllqd yrtltgqydk lvsvemieav gkaylptffk rcqqllrpqg rmvlqaitia
      301 dqrysrycrn vdfiqryifp ggflpsitam tttmtrhtdf itrdlfdigq dyartlsewr
      361 qrfyqqwhtl naqgfdepfq rlwafylcyc eagfrartis tvqltaerp
//
LOCUS       WP_181828533             394 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent aminotransferase
            [Pectobacterium].
ACCESSION   WP_181828533
VERSION     WP_181828533.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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
REFERENCE   2  (residues 1 to 394)
  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 394)
  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..394
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..394
                     /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=42676
     Region          55..388
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mnflinesdv lnpkrrallk lsgallgtaa vttglssrvf aetqpesaaf tapsadnpir
       61 infnenplgm spkaqaaard avvkanryak deilmlgnkl aahhqveass vlltagsseg
      121 iraaieayas ldaqlvipel tygdgehfak iagikvtkvk mldnwafdie glkaavagys
      181 gpsivylvnp nnptgtitpa dliepwiask pantmfivde ayaefvndpr frsispmitq
      241 gaeniillkt fskihamagm rvgyavahpk vialmgryva gekinfsgvd aalaslddsa
      301 fityskksnd vsrqillkal ddlklpylps egnfvfhqlv vplkdyqkhm adagvligra
      361 fppadnwcri slgtpqemqw vadtmrefrn knwi
//
LOCUS       WP_181828576             411 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Pectobacterium].
ACCESSION   WP_181828576
VERSION     WP_181828576.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 411)
  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 411)
  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 411)
  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 411)
  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 411)
  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 411)
  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..411
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..411
                     /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=46455
     Region          99..407
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mksiyqqvtl ktrimvsfvl lmvavmafvv vadqldydel rayvisenlr nevqprlead
       61 itkgitpimp egnllydaqs apdvlrqyal gyhrmekpag whllvfelnd rryyllqdgk
      121 dyeyleymid gfaplvillc ilcafwigrl tsarvtvpit rladvvqrkq kpfpfqdssd
      181 eigvlarafa qhsdelerfl qrercfvsda shelrtplai iggaaetivh qlptgshlmp
      241 saerivrttq emqrqltcll llsrdpqtlp ladvplrplf eecitrcqpw lakkpvaltl
      301 dvpqnvhvht naelarsvvw nllrnacqyt degevrialh gttliisdtg pglppsidpq
      361 qfqrflpssr esgeglglsi vqrivehlgw nmtvessekg crftlemrca a
//
LOCUS       WP_181828654             342 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NAD-dependent epimerase/dehydratase family protein
            [Pectobacterium].
ACCESSION   WP_181828654
VERSION     WP_181828654.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=38072
     Region          4..302
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkntilvaga ggyigiplch llinqgyrvv afdrfyfgqp vsempqspkf htlrgdirhi
       61 tpdilhnvea vidlaglsnd paaqisstlt hainydgach lantakkagv qryiymssas
      121 vygrsgaesa deemeckpqs lyaelklnve rkllqlrdtt fhpvilrnat vfglaprmry
      181 dlsvnimtrm avrekfitid gdglqhrpfi hvqdvaravl lalqldlpls vppvfniggd
      241 slnhtinsia aiiteeipev kivhhplsld trdyqlcfsh arttlgflpt rsirdgvrei
      301 vhvlttdqla gtqptcftaq wytdliewek rlqplqldgh lf
//
LOCUS       WP_181828820             648 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: relaxase/mobilization nuclease domain-containing
            protein [Pectobacterium].
ACCESSION   WP_181828820
VERSION     WP_181828820.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..648
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..648
                     /product="relaxase/mobilization nuclease domain-containing
                     protein"
                     /calculated_mol_wt=71740
     Region          3..635
                     /region_name="VirD2"
                     /note="Type IV secretory pathway, VirD2 component
                     (relaxase) [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3843"
                     /db_xref="CDD:443053"
ORIGIN      
        1 msrndddrfr irpgaprqrg dafinqvlrq tskagakvak agsrpgsrlg rghvvarftg
       61 vsltassrrv tiktrlvnla kagarststh lryieregvg rdgepgkayg pmtdeadlaa
      121 feergredrh qfrfivsped aeqlddlrty trhlmarmea dlgtrlewva vdhwntdnph
      181 thvvlrgkdd tgkdliisrd yisqgmrera selatewlgp rteleiqrgm qreveqerwt
      241 gldrtlqhea vdglvrterl eaeprlrrqr llligrlqrl qrmglatemq tgvwavhaea
      301 estlramger gdiirtmqra msgqqcelav fqpgedarti vgrvagkgla delydkgylv
      361 vdgidgkahy valppktele qyptgavvev kssadvraad kniaelasdg lyladhhlai
      421 eqgrakpgrd pqevvaahvr rlealrragi vervaeglwk vpidlaergr qydvqrlggv
      481 avelkshlpi erqarvigat wldqqliggg rglgdlgfgg dakqalqqrv dfleeqglae
      541 rrgqrvilar nllgtlrnre laqaakgiaa dtglehrpva dgqrvagiyr rsvmlasgry
      601 amlddgmgfs lvpwrpvieq rlgqqiaatv cgsgvsldis rkrgpqig
//
LOCUS       WP_181828842             399 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Pectobacterium].
ACCESSION   WP_181828842
VERSION     WP_181828842.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=44598
     Region          5..378
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makikltksa vdaaqaqaqp ielrdtlvpg flckitpagr kvfmlqyrtn agerrkpalg
       61 lygeltveqa rslaqewlaq vrrggdpaae kaaarqaptv relcikfmed yssqrnkpst
      121 qegyqsvidr niipmlgrmk vqdvkrpdva smmkkmahkp adanrtfsvm rkmfnlaevw
      181 gyrpdgtnpc rhvpmypngk sthlisdeem gklfryldql eaeglehavi plairlqfef
      241 aarrseiisl qwdwvdlenr rvvwpdsktg gmskpmseea yrllstaarg attpyvlpsp
      301 chpdrhltdg eyyngwtrtl kaagvthvgt hgirhrsatd iansgipvkv gmaltahktv
      361 amfmryvhte dkpvreaael vanrrkaitg aqrdegvma
//
LOCUS       WP_181828859             507 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PepSY-associated TM helix domain-containing protein
            [Pectobacterium].
ACCESSION   WP_181828859
VERSION     WP_181828859.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 507)
  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..507
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..507
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=55317
     Region          36..458
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mshpnqasat aaasgtrsag etapvqhavd nvspraaiva lfirlhfyig ifvgpfifva
       61 altgtlyvlt pqienrlysh qlftqsqgtp hsladqiraa qaglvhhqda kllairpapa
      121 agettrvmfa lpelgpsesr avfidpvsle nrgseivygt sgilpfrtwl dylhrglllg
      181 digrnysela aswlwvaalg giviwwstrh vssaakrrkl knsqttaakt qrlrhwhatm
      241 glslvlgllf fsatgltwsq wagsnisvar talgwqtpsv ktqlpapmsh hdmmhghdma
      301 matdehaehh asmpmgdagt ssptlfdevl aaarhagida nkieirpatq phrawtvsei
      361 drawptqvda vsinpdtldv vdktdfntfp laakltrwgv dahmgvlfgl pnqlilaafg
      421 lglcamivwg yrmwwirrpk srhsvnpvnt ltaawlavpv fqrvlialit lllavslpvm
      481 gislliflli dtvrwymgnp kqaiaks
//
LOCUS       WP_181828883             385 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DegT/DnrJ/EryC1/StrS family aminotransferase
            [Pectobacterium].
ACCESSION   WP_181828883
VERSION     WP_181828883.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=42710
     Region          4..367
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mknpiyvtsp llppleeftp yleeiwqnkw ltnggpfhqr leqaladylg vryislfsng
       61 tlalltalqt lritgevitt pysfvatshs llwnglkpvf vdidpvtcgl dpekvemait
      121 pstsailpvh cygipadven iqriadnygl kviydaahaf gvkqdgasvl hqgdlsilsf
      181 hatkvfntie ggaiicqdak tkkridylkn fgfsdevtvv apgingkmne vqaafgllql
      241 qhidgalskr qkiyqhyhns lnnipgvrll kvpdnitwny aycpifidas fpcsrdelys
      301 lmkdkgiltr ryfyplissf pmyrgfdsan panlplaqsi aeavlclpih pdlqedeqnl
      361 vidillaqar rsllltaden vgdvv
//
LOCUS       WP_181829027             345 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pectobacterium aroidearum].
ACCESSION   WP_181829027
VERSION     WP_181829027.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=37005
     Region          24..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 msyrtyritl ltvvvftlli avcslgigrf slspwrivqi lieplsgndl lfgkklqlgd
       61 ieqqvvwsvr lprvllawca gaalalsgat lqgvfrnplv dphiigvsag aafggtlail
      121 lswtplflll saftfgmlal llifmmaaaf gkqnvlilil agvilsgffg alvslmqyla
      181 dteeklpsiv fwllgsfata hwnslvatav plglagglll rlrwhinvls mgeqdaralg
      241 iavqplrwli lslcaaivaa qvavsgsigw iglviphvar mlvgadhrrl lpvslwlggg
      301 fmvlvddlar mlseaeiplg iltallgapl favllyktqr qergr
//
LOCUS       WP_181829054             525 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Pectobacterium].
ACCESSION   WP_181829054
VERSION     WP_181829054.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 525)
  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 525)
  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 525)
  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 525)
  AUTHORS   ter Beek,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 525)
  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 525)
  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..525
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..525
                     /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=56682
     Region          38..521
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mtnvsysett aftapssplc kpvalltlia lilsllgfvp lgfvigvsid tgwetarall
       61 frprvgellt ntvllvaltl pictvlgvll awlterttlp arrlwslllt aplaipafvq
      121 syawistapg lhglpagvfl svvaylpfly lpcaatlrrl npaledvaat lgvppvtvff
      181 rvvlpqlkla iggglllial hllaeyglfa mirfdtftta ifdqfqstfn gpaanmlagv
      241 lallclfllc adarvrgvtr yahvgsgapq aitpkhlspf plllalllla tlvlftlgvp
      301 fitlsrwlwf ggwdvwlrre lldafrqtmt lalsgavltt laaipmawlt irhpnrlyrf
      361 legcnyitss lpgivvalal vtttihlirp lyqteftvll ayllmfmpra lvnlragiaq
      421 apveleqvaa slgrsplqtl mtvtirlaap gvatgatlvf laivneltat lllapngtrt
      481 latgfwalts eidypaaapy alilvllslp wtwflytqsq kmagl
//
LOCUS       WP_181829248             377 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: fatty acid desaturase family protein
            [Pectobacterium].
ACCESSION   WP_181829248
VERSION     WP_181829248.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 377)
  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..377
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..377
                     /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=43284
     Region          46..322
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mlnqdrvfdv mvvlialslf frlaiklyyr dgerilpkfk lspgnrdeis yykrfdtlfa
       61 plpfiycwle ifaavlffrw tdynvlsgvl lavvtsgrmr alqelghnal hlalcpskrl
      121 qwflsntffq fptlkrdmds rfithviehh pnadvpgkdp nlrrviaagm vpgisrgqfi
      181 kalfypvslk glannikgnf rdvfrentsk qtallravvt isvvalylwv ggiaalivgw
      241 vipifsiypl fswwsllskh rwhtpytptr yrlahdyehg ratdfsgvfg aiqrylifpm
      301 sdayhlahhi yptvryqymp avdwalkvne prytqyiakg mifgsggqpa alselyhrlv
      361 ntavqspvnr ergtind
//
LOCUS       WP_181829314             397 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Pectobacterium].
ACCESSION   WP_181829314
VERSION     WP_181829314.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..397
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42707
     Region          19..395
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mitpvfpldt dapsthfsar iqsavqqald drrlvgavvl varngelihq qaagwadren
       61 arpmaldaif rfasvskpiv svaamvlvaq grldldedit rwiptfqtrl ldgspsritv
      121 rqllshtagl gyrffephad gpyaqagvsd gmdasdisln enlsriasvp lqyvpgtawg
      181 yslatdvlga liervqgspl deavrqlvte plgmhdtgft vrdplrltta yvndtpqphr
      241 ltegetvspf egaigiaysp aricnaqafp sggagmagta wdllrlleal rkgggvllpd
      301 alieemgrdq tqglelpnap gcgfglgfsv lrdpqlaesp essgtwrwgg ayghswfvdr
      361 qqglsvvaft ntmyegmsgr fvtdlrdavy ssleair
//
LOCUS       WP_181829329             601 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AMP-dependent synthetase/ligase [Pectobacterium].
ACCESSION   WP_181829329
VERSION     WP_181829329.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=68706
     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 mtnhlqpyhv vhrvqdrinh cagrialrew tpageqqltw tqagqrirri asallalrvd
       61 vqervaifsh nsmnwsladl allhlraisv piyatntaaq aafiindadi rtifvggqdq
      121 ldallslres cpqlrniivm degvnlrgsd ivqslhefea qavdefwrde wqtridsrdl
      181 ndlftliyts gttgepkgvm ldytnmamql klhddrldms endvslcflp lshvferaws
      241 fvimhrgaqn vylrdtnlvr aamqavkptv mcavprfyek vysaihekva qapwyrqrlf
      301 nwavtqgqyv flasqtakka glfrrimhry adrlvlgklr qllggeirfm paagarlddn
      361 iilffssigi ritygygmte tcatvscwee nrfrlgsigt plpgievrig eekeiqvrga
      421 timrgyfhrp qetaeafted gwlktgdage ldangnlfit erlkdlmkts ggkyiapqhl
      481 egtlgqdrfi eqvaiiadtr kyvsalivpc fealeeyahs inlkyhdrle llrhshiiel
      541 feqrlremqk elsrveqvkk ftllpvpfsm aegeltptlk lrrkiinqry qleidamyae
      601 s
//
LOCUS       WP_181829387             551 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Pectobacterium].
ACCESSION   WP_181829387
VERSION     WP_181829387.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=58304
     Region          5..545
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mnkftllpll tvavlftlvg ipvlfvalqa ifpnlgsgsf anpfsafadv faqarlfall
       61 kntlllglgv alccaviaip lgalrglfal plarfwdllf lipflippyi aglswmlalq
      121 prgyaeqllp iqlgealfsl pgmigvmtln ifpvvyfavs rsmaasgnrl advarvhgas
      181 gwqaflrvtl plslpataas lllaftlaie eygipaalgs ragiqvlttn ieqrladwpi
      241 dlsgsavlsl llvaialcaf tlqralvags nvetttgkpa aivtrplgiw rwpvlvlfsv
      301 vgllavgipl asmlitafsa tisstiswqn ltwqhftmlv ddenealpal ttslglavgs
      361 alltgtvgfl aawfvvakri rgaavldgls mlpaalpgiv vgvglilawn qsfwpvtpyn
      421 twvilllsys clllpypvry ssaalaqigs nlesaarvhg anamaalrli vfplvfpsll
      481 aammlvfava srelvtslll spagvqtvsi fvwrqfeqgs vgdgmamasv avlislsvml
      541 lalrfhslkt k
//
LOCUS       WP_181829390             319 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YbgA family protein [Pectobacterium].
ACCESSION   WP_181829390
VERSION     WP_181829390.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36708
     Region          71..316
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mtlklipvgi sacllgnpvr fdgghkrlef aveqlapyfr fepvcpemai glpvprpalr
       61 lvregeshit lrasngspld vtqqmavfsa dkvsqlqhlc gyivcaksps cgmervkiyd
      121 eaqknarksg iglftqelmr qmpwlpveed grlhdpglre nfiarvyalh elnqlwqdgl
      181 srgaliafhs rykllllahs qpeyrelgpf vagiykwdsl kdyvveyrkr lmkllstpat
      241 rrnhtnvlmh vqgyfrrqln sqqrqelsql idryrqgfqp llapitllkh ymaeypdayl
      301 aqqryfepyp ealrlrygh
//
LOCUS       WP_181829461             349 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DNA-methyltransferase [Pectobacterium].
ACCESSION   WP_181829461
VERSION     WP_181829461.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..349
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..349
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=38262
     Region          7..324
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mndilthgdc ldvlrsmpdn svnsivtdpp ygikfmgktw dydvpsqviw eeclrvlkpg
       61 ghllsfagsr tqhrmaarie dagfeirdmi vflyetsnaa rvlieslssd qlklldatfg
      121 rdgmlgwvyg sgfpkshhtl kpalepitla rkpfkasias nvriygtgal nvkecripla
      181 egespydypn gpggsdpnhm wrgrnkgdgg iarqgnpdgr wpanlihdgs davlarfwdn
      241 plqaeissas rffycakask kdrdegnnhm cvkptelmry lcrlvtppgg tvldpfmgsg
      301 stgkaaameg fcfigidree dyvkiarrri aaarsttahs gdagrhidd
//
LOCUS       WP_181829507             317 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecR family protein [Pectobacterium].
ACCESSION   WP_181829507
VERSION     WP_181829507.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..317
                     /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=35003
     Region          10..52
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          57..317
                     /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 mndyppeiqq qaarwairla eaplddeqel afqhwlvqdp rhrhaleqag mlwhglgsls
       61 aeqrqvlqpq ppatflirrv nratqwkiaa llllgfsigt twisdgilml rsdyhavhqv
      121 khvtlpdgse vdmdagsais laytpqerrv tllqgsawft vsptttqekr pflvdaasgt
      181 tqalgtqfiv qnasqtttvg vvehsvqvta ngqslqldeq qaaryteqgm trlpgwnsre
      241 rgdwrrglli fdqqplavvi arinqyragt iviptsalrq rqvsgifsln eldgalqtia
      301 telgaktvsl pgvtvly
//
LOCUS       WP_181829525             322 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pectobacterium].
ACCESSION   WP_181829525
VERSION     WP_181829525.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (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   2  (residues 1 to 322)
  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 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
REFERENCE   4  (residues 1 to 322)
  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..322
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..322
                     /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=35074
     Region          <145..319
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          236..318
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mnasplkats epevtisnli aelhvvrpdt gadcsllrat lqegldilvw rgqfrqpttm
       61 hlhddwgrin fscslqgdsq falkgdrgre hllkqgsgci sytpdcqgts syagqfesvt
      121 vslspellan wvpdlagnlq qqldsgrlct hcdcnaemra taqvlshals glthpqqvge
      181 srhaplwllg qsmimvslav aghadtapqq dtlsladrhk llrakdllla dlsqaptiam
      241 lsretglsvl klkrgfrqlf nnsiyglfqa ermhearrrl fatgapvmvv atdlgyanas
      301 hfsaafqkqf gvtpsafkrl ni
//
LOCUS       WP_181829582             343 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease
            [Pectobacterium].
ACCESSION   WP_181829582
VERSION     WP_181829582.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=35648
     Region          5..342
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mgkvwtvrvg kvsrqidrrt savalslllv llaviflsls lgevlmspaq vtsallgkad
       61 sgvhfivndl rlprallall vggalaisgl ilqsivrnpl aspdilgits gasaaavffl
      121 sflataisqr wlplaamgga witaiaiyll awkqgasplr lvlvgvglsa imgaavtmml
      181 vfspigttlt ayvwltgsiy gaqwqhvsel agwlligapf lvglarhvnv helddalacg
      241 vgqsvgrirl alltlsvala gaaiayagam afvgllaphi akklasrsfp glalvsaltg
      301 gllvmvadli grmaflpldl pagifisvlg tpffiylllr qry
//
LOCUS       WP_181829639             499 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Pectobacterium].
ACCESSION   WP_181829639
VERSION     WP_181829639.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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   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 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   4  (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   5  (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   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 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..499
                     /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=56674
     Region          174..489
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mlaatlnkik ikklgqrwqv kikhwqllga sqypgflcts nfrqaitivf lfllmmlmci
       61 vgfsslsetl irthvrevil gniydysmqs rltsadslit qlrqdnrakg delplflvmd
      121 kqgdilyhnh llrthplssd sfnthrlemr qrtdcrmdvs clkaeisspd dpnliglsvm
      181 lddggvlfta ynirpmlerv rtiplvagag lfivllfclf vsrhfslrsl rsvekiraal
      241 hryssgeqqv rmplspyddd fdslsadinq nlerierlme qvrntsshva helrtplthl
      301 qnrlfnlter agldndvrde lnlavdevhk ilglfrtvmr igeiesgrcv hqfeniearq
      361 lleeiaeyyq plaeergcrl kieikagiql fgdrallfqa lanlvenalk yaaqgkyitl
      421 svtlyrgwia lsvadrgpgi ppalhtkalq rfqrldtwfq sgyglglslv qaitdlhggk
      481 lyldssepgl nvylclnrc
//
LOCUS       WP_181829641             130 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YybH family protein [Pectobacterium].
ACCESSION   WP_181829641
VERSION     WP_181829641.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..130
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..130
                     /product="YybH family protein"
                     /calculated_mol_wt=14520
     Region          6..126
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mkphpireii eacdkaiser dfdalmryya edaalvikpg mvargkddir kafiaiadyf
       61 knqlvveqgn mqviegggda lvimetvlhy pdeqgsivtt trratyvfrk dadgnwlytv
      121 dnsygttlld
//
LOCUS       WP_181829643             395 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [Pectobacterium].
ACCESSION   WP_181829643
VERSION     WP_181829643.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=44823
     Region          1..395
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 miysygfkny fgfkegaeis felnsrvpkg isngrdvati lgvkgangag ktnllkalyf
       61 istfstesfk snaddeinad syfeskepsa fyidfrsadi rytyelavth kevvyerlyr
      121 knysadslgk ktrkvlvfer dgnkivkrle eissidvial ksnaslista yhykfespll
      181 mlndvydffn gfmsnvgytg lhdislster ihkttlsyfn nkeafdfvks liissdlgis
      241 dikildrvdd sgkkiyfpvf ehivdgkaht ltiydqssgt kslyvklhly wltlvlggvl
      301 ildefdlnfh plmlpklldl feskvtnpln sqfiftshit evleklskfr tylvnkddne
      361 cycyrldeig gdllrhgrpi apiynegklg gvpkl
//
LOCUS       WP_181829894             274 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Pectobacterium].
ACCESSION   WP_181829894
VERSION     WP_181829894.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=31306
     Region          35..118
                     /region_name="DUF6597"
                     /note="Domain of unknown function (DUF6597); pfam20240"
                     /db_xref="CDD:466391"
     Region          <89..264
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mhpdsasfrv rplqpwfvin aaedylkksv sqspiahfys ftvdraepmt lavpdgsvdl
       61 llhccseaps grvcgstasa qitrlmpger yfgvrfmpgi mpafldlspg elagqeipfd
      121 evapdtprll rrlvnthdfn eqvslflhyf sywttrsapp lllqiidlim ahdgkirvde
      181 lerktlysar yihrlfhdnc gmspktfcrt irfqralall nqgnidsltm laqhleyadq
      241 shffrefkaf ascspqhyla rlqavryqyr irqc
//
LOCUS       WP_181829823             347 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [Pectobacterium].
ACCESSION   WP_181829823
VERSION     WP_181829823.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..347
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37295
     Region          7..346
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mtwritiglv tnlllsfavl anagigfqhi tladegnnrp ldvavfypvs sssqtttige
       61 navfpgitvs knaapesggh plivvshgyg gnwlnqlwla qalvkqgyiv aapnhpgttt
      121 kdmrtekaqe lwqrphdisr vvtallaape ktgrvdekri aavghslggw tvlelaggrf
      181 steqfekdcl thaglasckv yekmqvakna asraqldkpl vdprisavis ldmglargit
      241 aeslaainip vlimaagypn eelpaelesh dlarklppah saykeiadat hfsfmqrckp
      301 gaveiinaen pgdgmicldg gersreqihq evakdvsefl qaawrkp
//
LOCUS       WP_181829900             569 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: dipeptide ABC transporter ATP-binding protein
            [Pectobacterium].
ACCESSION   WP_181829900
VERSION     WP_181829900.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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..569
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..569
                     /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=61276
     Region          20..567
                     /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 mslnplphps htasdtsakt pllrvdglsv tfpspfgpir svknlsfqvn ageilalvge
       61 sgsgksvtar tlvglagenv dvkanaielt rhdgglcdlr yltdrdwrai rgreigfvlq
      121 dalvsldplr kigqevaepi lthrllprqq vpahvaellt kagipdpehr aaqyphelsg
      181 glrqralias alaagpqlli adepttalda tvqkqvlkvf talaqaghgv llithdlavv
      241 aevadrvivm qqgslvegge arqilsapth pytrkllaai ptastrgkwl agtdplqngi
      301 apssaslaad hastddtial tadriavsfk rpdgsrmqav nqvslqikrg etlgivgesg
      361 sgkttlgkvi lalqkpdsge vrladnawst ltererrplr ariqtitqdp lssfdpqftv
      421 aqilnqplrl rrdlsddekq rriltlleyv gltpdllsrr pralsggqrq rvsiaqalas
      481 epeilicdep vsaldvttqa qvldllvalq rqlgltmlfi shdlgvvqhm shriavmkdg
      541 divetgpveq ifnqpqhpyt rlllstvae
//
LOCUS       WP_181829925             107 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Pectobacterium].
ACCESSION   WP_181829925
VERSION     WP_181829925.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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 11459264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..107
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11497
     Region          43..102
                     /region_name="YiaG"
                     /note="DNA-binding transcriptional regulator YiaG,
                     XRE-type HTH domain [Transcription]; COG2944"
                     /db_xref="CDD:442187"
ORIGIN      
        1 mtaksksksp afkaihsaas glfsvdaipq etmrnfdkac lssvddlqpl eikalrekln
       61 vsqpvfasyl ntsvstvqkw esgvkrpsgl slklltvvqk hglkvlv
//
LOCUS       WP_181830093             631 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: bifunctional metallophosphatase/5'-nucleotidase
            [Pectobacterium].
ACCESSION   WP_181830093
VERSION     WP_181830093.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 631)
  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 631)
  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..631
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..631
                     /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=69808
     Region          21..530
                     /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 mkktllslll clstsamaaq epinitilgt sdlhgtfvpw dyatdtanma gslsqiatqv
       61 hkvraqqpnv ilvdagdtiq gnfvetfknd ktspmilgfn alnydvwvmg nhefdfglnv
      121 lntsldqfkg talagnifwe sgkpylpayk iverqgvkig iigmdtpmta efakgtdrvk
      181 glnftdpvga vktviqqihd kvdaivlvah mgidnenqrp gtgvgdiara npelaaivag
      241 hmhvkvdkev ingvivtepd kygralsrid lqfeqqngky vlinkdsyty sikdvdsdrk
      301 mediyepyhn tlrananrpi aqllghdlvp qdavkgipqv hvqdtgisal fqeasrhyap
      361 kaqvialqid ndrpklnvgt isakdiafny qyaggeitvy qltgkelkky mewsagyfnq
      421 lqdgdvtysf npqrraskys tndffdgvty tidltkpagq ritdlkmnng tpvtddmpir
      481 lgmnsyrmgh ltqkggvleg rqfpvlsdtk aeygeeagti rnltirylte vkkgqyegtv
      541 pqrwklaglq gyererhive sllnsgkisv ptsddgrysn vqsinvksll lpdtaqrekr
      601 vaeltqqrds atnaltkqrl ndqltiiaai n
//
LOCUS       WP_181830127             379 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: fatty acid desaturase family protein
            [Pectobacterium].
ACCESSION   WP_181830127
VERSION     WP_181830127.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 379)
  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..379
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..379
                     /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=43621
     Region          6..360
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mandlparpy paqgeqafhr alqretsayl ranhdhrfad sgqfvkagll flgciacysl
       61 sliqqtawaf flsyfsfiml smvlniivnh dashntffrn rtlnrivgri vtlplgidpd
      121 ywrlrhvdfh hiypnvehyd ldteengifr qtpfqrhray mryqhlywpl vaslslpyia
      181 wvfdwadrlg ktpvnarsmq sgyrgwmifi gskvghivll lvipivvgaa qgispgvvll
      241 syllgqmlas llvvflllgs hwaetefyav tdtevmplgw yqhnfvtacd wlptprwlah
      301 wtgglhlhlt hhlfpgwhhr hypalaailr rlaaehgmdy rcityrella sqrrflksmg
      361 egrdqrtaqr aaeegreeg
//
LOCUS       WP_181830446             149 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Pectobacterium].
ACCESSION   WP_181830446
VERSION     WP_181830446.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 149)
  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 149)
  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..149
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..149
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16481
     Region          19..122
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msqsktpidl lppllptgdv faekcpsrqi lnhvtsrwgv liliallddt hrfsqlrrri
       61 ggvsermlaq tlqwlesdgf vlrtaypvvp phveysltpl gkevgvrvke laiwvegnld
      121 eimaaqqsse qpsgeqrsdk qpsgklras
//
LOCUS       WP_181830551             731 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor [Pectobacterium].
ACCESSION   WP_181830551
VERSION     WP_181830551.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 731)
  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 731)
  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 731)
  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 731)
  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..731
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..731
                     /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=78110
     Region          80..731
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mnarknftpp tgktrfpips alavavtaam avlsgiaipa laetgerdds tivveakdae
       61 avqglvaggm sarssstgll gkkdvmdtpf nvsnvtsafi enkqaqtlgq vvahdasvrv
      121 sssqggllds yyirgfplne gnlsdiamng vygvapnyql mtdyiervev lkgpsallyg
      181 lspnssvggv inavtkrptt vgnltrltts wqsdsqltqh adisrvyale nnnllgvrfn
      241 gnygygdtvw ngsdkrtqvg algldfsser fratldlitq hlktrapsrp ysfaagvtvp
      301 dapdgntnis qpwgfwhskd qsvllhteyd ladnvtwftd lggssahvsr lseqvpqvin
      361 nngdirsgvg nyrfttsryn fatgvradve tgsvthklsa qtsyyrdrqa sasragtaid
      421 sniynpvsap aqdiaapssi ykrsstalsg ialadtlgfw ndalqvtggl ryqqinsdnf
      481 aapdggarss ydksaitpml gvivkpwqhv slyanyiegl skgdvaptta snagqvlspy
      541 kskqyeagvk vdalgtistl svfqitkpsg alvngtfvda neqrnrgiel dvvgspledl
      601 rltggvmlld aeltksvtpg aqgkrapgts rfqanagvey dlpflrdltl sanvthngkq
      661 nvntintqsi pswttvdfga ryktriynap ttfradvlna fdrnywsgvt sfstvsqgtp
      721 rtlmlsvavd f
//
LOCUS       WP_181830606             561 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Pectobacterium].
ACCESSION   WP_181830606
VERSION     WP_181830606.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 561)
  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 561)
  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 561)
  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 561)
  AUTHORS   ter Beek,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 561)
  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 561)
  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..561
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..561
                     /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=61455
     Region          44..557
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mtppsgsvin nsdliqysfd smisgvwrvs swllagllll platvfyqaf fadgmgfaql
       61 wqiglptyli hsvvivigtl lfsllfglps awfiamyrfp ghrvlqwalc lpiampafll
      121 aylytdalrh lspllreggl qivssweefh vaglsvslgc vslvlalvly pyiyllvrea
      181 lvkqpaslih sarllnqtrs qvlrrlclpi alpaiacgga lvvvetlgdy gaasyldipt
      241 mttqvldiwq kqgdlgaaar lgvlilpaif llmflvnlwr rkqkiyqaqa nasqvvppvl
      301 sgwrskvvrg ycwgivclsf lfpvlyllfl alrhmmsvwd maflhaimns llasatatai
      361 itlmalsfif ytrmagifan qtpvrlvsls falpgavlav glftllslvd nginlfahaa
      421 glptvdalla gslfililay svkfgrlmld slersmdaip rsldsaslvl gasplsrwsr
      481 vhipllrrsl figallifte smkelnvsll lrpfgidtla tyvfrftase qvasfafpal
      541 vlvavglipv fwlnralnik g
//
LOCUS       WP_181830552             633 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: IucA/IucC family protein [Pectobacterium].
ACCESSION   WP_181830552
VERSION     WP_181830552.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 633)
  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..633
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..633
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72597
     Region          23..622
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnikseevkh rdihqdtddf lsdysnknal rrlircffae gilnkndlsf iednsrgaml
       61 alqdgkavlk fddispapan tyinngniyl insdgtsfpv tgheqlidvl rdsfdfhpee
      121 sgilglkkdv gnsirndtha rryrrqwrae vadamqrdgq nhftlwlrrq lsirdaamll
      181 dqwgsleghp yyptwksrpg lsdedvqqls pefnarvplr italrrdmay vecmphvdnf
      241 hqwfaqafpa lwqdwkqrln qqgldetqwl plpihswhle nwvkshyade iaegilltdg
      301 pdlitlpgms frtvlpvepp sspfiklpva iwmtsemrsl qaksihmgpr istiieaila
      361 qeggfeqrle ffreeaafhy khavhqddap gkhlsvvfrd ahayeradga lpvtvatlft
      421 alphrdqplf telvalsglg peawfrqyvr avtrpviaiy llygigleah qqnsqilfsp
      481 egvaqgllir dfgdgrtyap llrqrgyhlq pyvwpgilpt vfegdiepvr mfvvdacfvs
      541 hlhelalals aeygfadarl wqvmkeetaa afdavksrvd gelwqterdm fltqpwytrs
      601 llrmhiqeyr dyriqhglsn pflvegedtr irs
//
LOCUS       WP_181830792            1090 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            ochracea].
ACCESSION   WP_181830792
VERSION     WP_181830792.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1090)
  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 1090)
  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 1090)
  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 1090)
  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..1090
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..1090
                     /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=121706
     Region          24..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkylfsvf fllffttigw sqeimvkgtv ssdemplpga avvvkgtthg tqtdfegnyt
       61 ltakegdilv fsfvgyttqe rrvtgggnvt lniklkeesn tldevvvtgy gvqtrktlat
      121 svsklntkvl esaprsnaat alqgsiaglr vtqvtgkpgt tpeiqlrggt gfdgsgsplv
      181 lidgvpgsfy alnsddiesm evlkdaasta iygaraangv ilittkkgka grsnitvrtk
      241 ytmnqkralp dyleardfiy wnrraiknvq dygvhnfdqf ltgthamatg nnttdspytt
      301 meltnanryl lnnpewqtmt dpldptktli fqnnnvgeli yqysdakdys vsfeggndkg
      361 tyylglgyld dtglvlgsnf krysgtfngs ykitddfkvs snvlyaqsnk vgsfrdalst
      421 yaneddyfif qrfagqapts riyntnpdgs sskdynpgsn ssfgnpayyk dkflmdnieh
      481 ritasvqfdw kllknlslma rgshfavhnt ddrfykaymn sgalvssrqa ktaydrtmnn
      541 qgtltlnykn tftekhnlsv llggeyfkqq qfasnaateg sptdlirtln agakasgipy
      601 sykrdysivs afgqlnydyd dryllgltfr ydgtsklrdn kfgffpgasi gwnahneeff
      661 kegkisqvis rlkprvsygv ngnidaltis ndyywllgky svqspyngkk gyvntsvply
      721 ylkwekattl nfgldlglfn nrvnflvdyf irdiydklad qripistgfs svkinngtlq
      781 nrgieieanf kvintddikw niganftrir sfvkklphng ndknriggqe iwdpsnptkt
      841 myvggrqege rvgddlvvgy qdegvyhnqa eleadkdrqi dfyagtipat nrkpmvgdtr
      901 wkdvngdgii nsrdrvvlgr ttpdfiggft tdftykninl fvktdyavgh lvhngvrsrg
      961 isqvqgnmnw tseikdtwtp enpnadipry dftdprgnhk aetkageeqf tassrywekg
     1021 dylalreitl synlpgslvn nafkdirlfv sgtnlayftk ysgyspekgg wdngrfplpr
     1081 sftfginatf
//
LOCUS       WP_181830814             219 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Capnocytophaga ochracea].
ACCESSION   WP_181830814
VERSION     WP_181830814.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     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=25013
     Region          49..155
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mnppvtdmql lgqllrcpsg iyakevgeya ffsnrtmifn tidylsllpn snvleigfgn
       61 ashlrylfek eptihytgve tsgemiaeat vnnpelvaqq svsflqvqpd erlefnilfd
      121 vcfsvntlyf lksptryyrn iyqllkpmgk vvitfidksv gekapfaqvg fkfytvpevr
      181 killhigfkn ikeytfeetl vsksgkkirr pycimmgek
//
LOCUS       WP_181830882             732 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Capnocytophaga ochracea].
ACCESSION   WP_181830882
VERSION     WP_181830882.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 732)
  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 732)
  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 732)
  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 732)
  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 732)
  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..732
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..732
                     /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=83684
     Region          8..732
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 metnidleee nkaiareyke llrisyqtls dedkklirla fdtavdahkd qrrksgepyi
       61 fhpiavakiv asqigldaia iasallhdvv edtdytiedm erlfgntvah ivegltkiss
      121 msrendislq aenfrklllt mnddvrvili kiadrlhnmq tmdsmaeykq akiasetlyi
      181 yapiahrigl ynikteledl alkytdpery nsilnkmees keeqqeyiea ftkivetslt
      241 qqkidysikg rpksiysiyr kmesqgvsfe evydkfairi iyksepaeek flawkiysiv
      301 tdhfrpnptr lrdwisspks tgyealhitv mgpkgkwvev qirsermhei aekgyaahfk
      361 ykhgdqkeeg iemwlnrlqe ifenseanav dfvedfklnl yskeifvftp ngeikslpkg
      421 atpldfafyi htgvglktrg akvnnklvpl nyvlksgetv eiitaenvkp tknwlnyatt
      481 akarskikna lkeetktvaa egkeilvrkl kqlkiilnee vmnemvsyfk tktsldiyyq
      541 agtgeisnqm lkdfvshrts ffglfknkav kkptdepiys pnvhydsivf gkeeesldyt
      601 fskccnpipg dpifgfvtin egmkvhkktc pnaismqsny ayriiqakwv ksderdfkvs
      661 lkisgidrdg lisdiskvil dskfvkltnv nidtegnvfs gkvsisinnn atlkklmqdi
      721 knikgvdkvn rl
//
LOCUS       WP_181830841             385 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Capnocytophaga ochracea].
ACCESSION   WP_181830841
VERSION     WP_181830841.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   ter Beek,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 385)
  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 385)
  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..385
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..385
                     /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=43320
     Region          1..220
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          125..383
                     /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 maiaaiavgm vmmliaiatg iglqrkirek lvvfhghiqi fdysnntsqv ttkpiaikqd
       61 fyptfsavpe vthiqavatk ggiirtetty esilakgvgk dynwslirdf itegrtpnva
      121 seevtdevlm ssylanrlhl klgdrcqaif lkdeaaqapn qrsfkivgly nsgfqefdas
      181 yvftdirhiq kinkwqpdqi gnfelfikdf drieevgkqv ygkvgsflds qtiiqkfpfi
      241 fewlgmfdfn iyliigimiv vggfnmitai lvlilektpm igtlkslgas drsirkifly
      301 natyiiglgl lwgnvlgfll lwlqqrysli kldpatyyvt evpiaftplw vlllnigvll
      361 lcllmllipt yvitkisptk smkfa
//
LOCUS       WP_181830947             455 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Capnocytophaga ochracea].
ACCESSION   WP_181830947
VERSION     WP_181830947.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 455)
  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 455)
  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..455
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..455
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51382
     Region          318..455
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mmmkklfils laaigfvacs kradyivlsg kvegtngipl elkiiggevd qplhikpdgt
       61 fqdtlrvpsn yytifnpqgi eiplyleqgd elgvnidltk mpleikfsgk dtlanaylhk
      121 ksdltmeiqk sggmqqllvk apaefktavn eyskkytdll kntkklskdf vkkeeksiny
      181 emlylksiyq nahqkltqee valpkefade lakidydiae dyntyrayke lvtnklfdkf
      241 qdnendenpw gkliahvkgl ksknikadlt ryfisgvsva ntpeenaeli ksikenvkdt
      301 aalkeldrri avlerlkpgt dfpsftaedl ngkpvsyesl kdkllyidvw atwckpcike
      361 ipsmkalqea ykgkpvtfvs isvdqdkeaw kaavqrekls giqlytnlsm nrdfidnydl
      421 sgiprfmlvk ngkiisisap kpsdakvkel inanl
//
LOCUS       WP_181830956             109 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [Capnocytophaga].
ACCESSION   WP_181830956
VERSION     WP_181830956.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
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="Capnocytophaga"
                     /db_xref="taxon:1016"
     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=11515
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mhylyltlai vlevlatall gksegftkwl favgsllsyg vcfyflslal kniplgvaya
       61 iwsgvgivlt aivsilvfks kvdlpfvlga vliiagvvvi nlfskangh
//
LOCUS       WP_181831190             989 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            ochracea].
ACCESSION   WP_181831190
VERSION     WP_181831190.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 989)
  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 989)
  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 989)
  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 989)
  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..989
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..989
                     /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=109332
     Region          29..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvlkehlml mmvllvgfvg faqaqysrvt gtvtddkgtp lpgvsvvikg ttkgvatdfd
       61 gkytltevar gavlefssvg hktldlkvtg eqlnvklsev aqdldevvvv gygtqkrgdv
      121 ttaitsvktq dldqrpvtsa aqaiqgraag iqvvqpsgap gaglavrirg ntsisasndp
      181 lyvvdgipvq disgiaptdi esmqvlkdas saaiygsraa ngvvlittkh gkrnepkvsv
      241 ntyvgisqva krieslntaq ykelmdetga vtlpsgltdk tdwfdetfrk siirntqlsf
      301 snatentkyy isagnskdeg virssffery nvrlnletkm rkwltfetnl sysdyssngi
      361 itgtgsnrag vvlsvintpk yapiwsdkpg eegwyyynfy ganlthpven isrnadntsk
      421 snrlvgsvsa ivtffpslkf kstvgidrlg rtqthwtdpk lteygrkifg taddirtnnt
      481 vmtydnlltf dksfgkhnls alagtsgtvs kwnesylyas hfltpdiktl naankieqgs
      541 gssaaewaim sylgrisyny dskylltanf radgssklap gkrwgyfpsv svgwrlsqen
      601 flknvewlse lklrggwgqt gnqagisdyg ylqrfsitrq nwweagkgda mvtlrpnsfs
      661 npnltwettt qsnigldial fknrislavd aylkkttdll mdvplpatsp vpsiyrnege
      721 mtnkglefsv dsrnltgnfe wntnfnisfn rneltkltlq kvyyyastse aiteqvvrit
      781 egqplgkfwg fisegvdpqt gnikykdlng dgkisvsdkt yigdpnpdft fgltndfsyk
      841 nftlsvflqg sygndiynas rietegmydg knqstavlnr wrkpgditdi pravrsadni
      901 kassrwvedg sylrlktltl aynlsneell rygirkiqpy ftaqnlwtlt nykgfdpevn
      961 qglsgptmgi dwgtypqtkt fifglnidf
//
LOCUS       WP_181831156             246 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Capnocytophaga
            ochracea].
ACCESSION   WP_181831156
VERSION     WP_181831156.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
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="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     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=28878
     Region          42..243
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mkllkytfwl lwkswfyllv lilillwlpl lfiltaraew yrsfywvarn lwatpilygi
       61 gflpkihrey tvpndrhsym lvanhysmmd imlmfycskn pfvfvgkkel sktllfgyfy
      121 krvaimvdrk spksrkevya qamerikagl sicifpeggv pddesivlds fkdgafriai
      181 ecqipivpmv fydtkkrfpf rffagsmgtm rvdilrsipt qgktlddkda lreevrslil
      241 qrltva
//
LOCUS       WP_181830971             975 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Capnocytophaga ochracea].
ACCESSION   WP_181830971
VERSION     WP_181830971.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 975)
  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..975
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..975
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=110072
     Region          34..496
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          536..953
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mlkrnlflwl ftvaitfgas aqnyewkeaq gggytykyvt hdptnarfyt lkngltvils
       61 ptnkepriqc yvavkagskt dpatntglah ylehllfkgt dkygsldwak ekveldkida
      121 lyeeynhtkd pakrkaiykl idsvsgvask yaianeydkm mtamgaqgtn aftsfektvy
      181 tddvpanain kyitvqaerf rnpvlrifht eleavyeekn rsldsdnsev fetlfselfk
      241 khnyglqtti gtvehlknps lkeirkyfht yyvpnnmavi lagdfnpdtv iaqidkafsy
      301 mqpkavpqyt fekeapitap iikkvvgpda esvsmafrlp gnqdkdalla dlvgeiltng
      361 kaglidlnlv kkqkllgasa faytlidygv lylsgkplqg qsleqvkdlm lgeienlkkg
      421 nfdddlipsi innlkkqtiq gtesygnran mlmsaftdnl dwkdqvayvn nlskltkadi
      481 vafankylgn nyvavykekg trpnvekiek paitpvetna dkqsafvkmv nempstpvkp
      541 vfldynkdlq kgklgkaeil yvqnkdnely rltfrykvgt lndlklamaa nysqflgtdk
      601 ksaeqltkef ykiassfris sggeyttvni eglqenfeta vklyedfitn ikvdeealka
      661 lkarvvksri dakanrnaim qaltnyamyg aknqsnytfs daeieaitgk elvdklknln
      721 nveqtviyyg patlseltnk lktlhkvpak ftkvapkkef kqveqtknqv lfadyemvqa
      781 etrwirntvp fnpaestvis tfnnyfgggm gslvfqtire skalaystyg fyasprkkad
      841 kyymlayvgs qadkfkeave amnellntmp elpanlqlak lqikqeiete ritqdgiiys
      901 ylaaqelglk ddirkqvyqn vmgitmkdik afhdkylskk pytyvilase kklskddlqk
      961 igdfkklsle elfgy
//
LOCUS       WP_181830885             515 aa            linear   BCT 28-DEC-2024
DEFINITION  sialidase family protein [Capnocytophaga ochracea].
ACCESSION   WP_181830885
VERSION     WP_181830885.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 515)
  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 515)
  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 515)
  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 515)
  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 515)
  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 515)
  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 515)
  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..515
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..515
                     /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=57710
     Region          151..515
                     /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 mkqlftilal cflsfgyaqk gmtftqaqmp latdkdnpvt sfvlpvkqgt evkelslqfk
       61 skklnlsels vyvganakre qatlfaktsn lscntklqgn fkatndtlfv wvsarttqkp
      121 dllqklylsk iklitnetki tlnnakkegq rfaialrqrk qdgiecyrip glvttnkgtl
      181 iavydnrynn ckdlqedidv gmsrstdggq twepmkkvid mgewggkpnr lngvgdpavl
      241 vdeqnntiwv mglwqhgldp qtmswwgsks gmtpeetgqi vvvkseddgk twsepinits
      301 qiknpewrlf fqgpgrgism sngtlvfagq fkdkdqvphs tiiyskdhgk twhvgtgaks
      361 htteaqvvel sdgalmlnmr ddrnrsnyel sdnyhgrsva vtadmgktwi ehntsrtalt
      421 epncmasiis ykdkkgklyl ffsnpndakn rvnmtikvsd degntwdklp svllyeqaam
      481 gyscltvidn kyigilyegd gdlyfqkvpi kefik
//
LOCUS       WP_181831192             501 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 30 protein [Capnocytophaga ochracea].
ACCESSION   WP_181831192
VERSION     WP_181831192.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 501)
  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 501)
  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 501)
  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 501)
  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 501)
  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..501
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..501
                     /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=56308
     Region          38..500
                     /region_name="XynC"
                     /note="O-Glycosyl hydrolase [Cell wall/membrane/envelope
                     biogenesis]; COG5520"
                     /db_xref="CDD:444271"
ORIGIN      
        1 mklfpsfllv ilwsiascsc qkksntgees tpppvvepsv gkvnvlltta nrqkelykeq
       61 tdlkliknpn asysitlkpa ekfqsiygfg aaitgstcyn lmqmspadrk afltetfset
      121 egfgqnfvri sigcsdfsls eytlcdtkgi ehfaltqeet kyvipilkei lainpkvqii
      181 gspwtpprwm kvnnltdlqp hnhwtsgqln pahyqdyaly fakwlqamkd nglnvkaiti
      241 qneplnrgns asmymgwdeq lafiknalgk tlrnkgfaev kiylfdhnyn ydnkpsqqqy
      301 plhiykdada sqyvagaayh nyggnpnels nihnqypnke liftessigt wnngrnlerr
      361 ltedmqelgi ktlnnhckav ivwnlmldeh gapnreggck tcfgavdiqt sdyktmqrns
      421 hyyvishlsa vikqgatcis vekttddnvq ctafenpdgs lacvllnkkk eatyltlstg
      481 kyyfsyevpa nsvvsflipk i
//
LOCUS       WP_181831223             824 aa            linear   BCT 28-DEC-2024
DEFINITION  polysaccharide biosynthesis/export family protein [Capnocytophaga
            ochracea].
ACCESSION   WP_181831223
VERSION     WP_181831223.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..824
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..824
                     /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=91833
     Region          155..331
                     /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          <500..584
                     /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          <581..719
                     /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          <717..796
                     /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 mlkiklliiy lllvisqava qvtspnatyn nvdittvnvd nlsdaqikny wdraqaqgys
       61 ldqfvalars rgmqemqvmk lkqrimqlst ssdiknklke ntktgrrpae gddifgytgk
      121 enkdsittkq kkdsifgmsf fknpkisftp nlnmatpdny qvgpgdellv evwgategsf
      181 kqkvdaegni flngigrihv gglsfsevka kinsqlkriy sgisapegsy akiytgvtis
      241 qvrtvkvnii gevavpgtys lsslstvlna lyacggpses gsfreinifr ggkkvatfdv
      301 ynflingsek gniglkdqdv iivppyknrv wvdgkvkrrg fyetldnetl anlitffggf
      361 tsdaftntlv lerikdakre vkeipfadis kvkmqngdrl nvhaitdeyh nrlsiggavy
      421 qpgvyefreg mtaydllnra ngvrkdasln rglifrtenr vdyqtlsfsv kdliekkndi
      481 plkdndsihi fyrdslqykr fvkvegavnk pkelpfmenm tvedvislag glangadpsm
      541 ievfretndg nfqklsqafk vssnhqlepq gerltlqpnd vvsvryikgf tpmqtvtvmg
      601 evlypgvysi qskdervsdl lervggftpf aykegltlvr kktdegdiqq edflkeliei
      661 endtssstsn ktlrrvakks neyrigldvk kilnrkhsky dlllndgdml lvpsekqtve
      721 irgevlapsl vryekgasih qyvssaggfa srakrsaiyv myangdikat rtslffknyp
      781 kiepgaiiiv pskpekqrlt tgetvgiisa ittmgvliys afkk
//
LOCUS       WP_181831403             260 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Capnocytophaga ochracea].
ACCESSION   WP_181831403
VERSION     WP_181831403.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
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 19271407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..260
                     /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=30670
     Region          23..>72
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          52..246
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mdrkeriiln dilngdkify rnisvdnvif gyhkrelkvl lfknaaqerw llpggyvkkd
       61 etlekaahrv vryrtnlkkl hlhqfftfgn pdrnknthft sellstitgq evtkdhwlld
      121 sfisvafftl vdyyqvkptg sfyieecqww disnlpemaf dhreiidqal lslrffshvs
      181 pigkemlpek ftipelqsly etilgkkldn rnfvkkmtni gliekldekr nigkhrspfl
      241 yrfnqaryda lakgdefivf
//
LOCUS       WP_181831439             458 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Capnocytophaga ochracea].
ACCESSION   WP_181831439
VERSION     WP_181831439.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 458)
  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 458)
  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..458
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..458
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=51334
     Region          160..>201
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
     Region          <255..431
                     /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 mknisyflll clalligacg nrnaykpvdr gssiteyrde nsatdyrees sgelaeiavv
       61 gygekstkrk hskktgdvsr sdestmsakm svakdvatsk pakrtepkhr khrpesdpqp
      121 qsglvtagew ndlnswdfyq ktlnknefas fpehwqmytn hriavlvtan gkpavnatvs
      181 lyrnntllwt aktdntgkae lwvsafqkek elntehlrlk vndqwvstek aitentlnri
      241 vlknevkkas nevqiafivd atgsmsdele flkmdlknvi tkveegnknl kistatvfyr
      301 degdeyvvkh sdftkdinkt iqfinsqkad gggdfpeavh talnqlnklq wdgeartria
      361 flvldapphh edkilksvqa svktaaekgi klipivasgi dkpteflmrf maiytngtyv
      421 fitddsgign ahlepsvgey qveklsdlmi rlikkyte
//
LOCUS       WP_181831454             453 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Capnocytophaga ochracea].
ACCESSION   WP_181831454
VERSION     WP_181831454.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 453)
  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..453
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..453
                     /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=52152
     Region          241..447
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mkflslsinl ffiifagvyf vlpidfnipa vdglldffyh iglvisllva svdvylkrkq
       61 lfknidyyrl fitflanfta ciyiynsktp lglsilllgl cliyglvkkt yysphpimvv
      121 lflfsslkim sclwssdirq gwahidyyta fvflpiiscf yrveakeqka fiypifsfft
      181 nlltltfiay iltvkqlnqs fwsfltlnke ylgynietgi ynyyqsigws ktfhpskiaw
      241 ifltvlavsy wlwqegkkki ittfqlsfya llllivslvl qarvailgff ilvslfiwvg
      301 lmryvksrks iffytllaif vaisgvilsi tqttffsdps rlkmstlvfk sffeypflgg
      361 gafhealllh qanidlvslh nefltalsdq gilglllfla fhilviyygl knkyflgiyv
      421 llafaifnat egvmgypici pfflfclipp kqt
//
LOCUS       WP_181831480            1312 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Capnocytophaga ochracea].
ACCESSION   WP_181831480
VERSION     WP_181831480.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1312)
  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 1312)
  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..1312
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..1312
                     /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=150558
     Region          316..>374
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            338..344
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          389..1200
                     /region_name="DNA2"
                     /note="Superfamily I DNA and/or RNA helicase [Replication,
                     recombination and repair]; COG1112"
                     /db_xref="CDD:440729"
ORIGIN      
        1 mnqevftalq nklkvgnrrg vhlnalpgas rykfdiarls aifkslperf ildlltlrnl
       61 nfsfsihdte stdidhrgag srtpeegqav kvnekeegks vkekgtreva leklvdsien
      121 lmfqsevits ekgvntlgfg fpillrrdmg dgqltaapil iwsvkikpat qmntwvisrs
      181 eedpiylnev ltnhlqndsg vslkpipdem ledgkidkpe lhslcsdiln qlkvtqnldf
      241 llnnyteilp lktkaayedl lpnkgdafie kcgilslfev qkqniindye slkkefvplq
      301 ttaneqfqsl saietdpsqq sileslksqq kiliqgppgt gksqtltail inalenkqkt
      361 lvvcekqtal evlynalqnk glgryctmik daiadrrfiv davrnhidna efkketpafl
      421 enllaeqvqa mrkittdina ihhklnqpll nqlswtdvma elmhyetdre eldlsafsfq
      481 ftdeefaslt plwqqgealy qryapyaqnh lfnpkkltat nlfntqqqla eafkqyaqqw
      541 eviqqqiavy kayylhkrke efiqqldtla qyrneyelit atlpptspvy qpevtkgffy
      601 klsalfsaek kqvlktqkrl qelctaikal slhrnfssia isdnlllnkt viaeytpait
      661 qaqtdfdskv nadfaaldll nyyersfvna dldklisevk slknrieads wldavnfgnt
      721 faefkafitr slatynsyqa dpaqplvaqy ewfaffqsln dfqerivlsl tkvthweasf
      781 lyayytlllq rnaddtlnfn erdyadfkkk vhyfastqkd fiegywntqq rkavktfeet
      841 nkeltvanly nkrksekhnr ltlrqiamkd tdlftsffpi ilttpdaccn lfegknfyfd
      901 nvvfdeasql klednlpaml kgktiiiagd ehqmppsnyf skvfdgtaed dddneeedev
      961 ltyknamlni eslldyaley qfsknhldfh yrskhpylid fsnhafynar lrplpstesr
     1021 tpihftqvng tfdehinree aaevlrilsq iepradgsyp svgiatfnit qrnyirkqil
     1081 qkqndptqta frekinaleq aglfiknlen iqgderdiii lsvtygkkkg gkfvqsfgpl
     1141 nftkgyklln viitrakeqi yvcnsipeel latykealaq egannrravl yaylayarav
     1201 sdgndalrre ilseldlygh khtdidqqsk safkeqtyrq lkekypdqri tmdyefggyt
     1261 idillapkeg kpiaveclsk plynndlayl edlhkekill nagfdykrkw ak
//
LOCUS       WP_181831541             384 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Capnocytophaga
            ochracea].
ACCESSION   WP_181831541
VERSION     WP_181831541.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
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="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..384
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43492
     Region          82..375
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkflinfvv vlllligtly vagygyilka vvvvygtght ttflddytyf dnrtiakspt
       61 pqpwplsady nkipetpelq nahkkygtva fliikgdsiw heqyfegynt esksnsfsma
      121 ksyvsallgk aiadgyiksl dqkvsdffpe ykkgfgaqlt vgdlssmasg ldwdeayynp
      181 fsittrayfd khfrekmlql rivsppgkay kylsgntfll gmvlekatkk tltqyltesl
      241 wqpmgcesda lwqldseesg lekayccias nardfarlgk lyrdngkwng kqlldstfva
      301 tsvqprfaes peygygwwll dykdthffmm rghlgqyviv nptdkviivr lghrtadtsp
      361 egskftqdiy dyideaykvl gvrg
//
LOCUS       WP_181831659             166 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Capnocytophaga ochracea].
ACCESSION   WP_181831659
VERSION     WP_181831659.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 166)
  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 166)
  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 166)
  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 166)
  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 166)
  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 166)
  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..166
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..166
                     /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=18325
     Region          <39..166
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkkhfltfat malltacggg tnnnntttds ttqeatttap apsnsasepd fpdwqnnkgi
       61 gpvktitppl adtpdaamva kgeetfntyc tvchrpkkrl tgpamiglld rrtpewvmnm
      121 ilnpdvmekq dpiakklvee yntlmlnqrl neqqarelle yirtik
//
LOCUS       WP_181831606             484 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Capnocytophaga ochracea].
ACCESSION   WP_181831606
VERSION     WP_181831606.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 484)
  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 484)
  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 484)
  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 484)
  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 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   6  (residues 1 to 484)
  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..484
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..484
                     /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=54869
     Region          7..478
                     /region_name="PRK09835"
                     /note="Cu(+)/Ag(+) sensor histidine kinase"
                     /db_xref="CDD:182101"
     Region          <260..478
                     /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 mfkkntlrfq iflsmtllvl vafailafvm igqykkqale yhderlidke nqikmqiqyv
       61 fsqttfpvet pyiplifred iysianiqnl nfalydldgv llksskasls pdqdaffipp
      121 dvlhqlsatl nkrlvehhef agrgyqtsys yitdlqfkpi ailnipyfen dtfneralkg
      181 slynlamvyf sllvvaltva yfiskyitks lktiegrlek trllsqneki llksapteit
      241 elvnayngmi deienskall aqsereqawr dmakqvahei knpltpmrls vqsyqrkalr
      301 epqtaeqtne fcesliqqid ilsnistafs altnmpaknd eefdfvsvik rtldifdsde
      361 ihfthshdei isvfdkdqlg rvvtnlvkna lqatenepfp sievslnksd tditlkvkdn
      421 gtgipdadke kifepkfttk tsgsglglam vknivlsygg sihftsevgk gseftvvlvh
      481 flnk
//
LOCUS       WP_181831770             177 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Capnocytophaga ochracea].
ACCESSION   WP_181831770
VERSION     WP_181831770.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 177)
  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 177)
  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 177)
  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 177)
  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 177)
  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 177)
  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..177
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..177
                     /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=20443
     Region          <83..173
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkhfnnyiky lllillvvgc rnkqernief mpdmyespay ktyevaplsp pehtvkrgel
       61 pyrypntieg yeqakaqlsn platdtlqqt qnltdgkkly giycalchge kgdgkgilvq
      121 rekilgvpny ksreltegsi yhvlyygrnt mpafanqlse kerwqvamyv eqlrdkr
//
LOCUS       WP_181831810             296 aa            linear   BCT 28-DEC-2024
DEFINITION  flavodoxin family protein [Capnocytophaga ochracea].
ACCESSION   WP_181831810
VERSION     WP_181831810.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..296
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..296
                     /product="flavodoxin family protein"
                     /calculated_mol_wt=33963
     Region          4..147
                     /region_name="FldA"
                     /note="Flavodoxin [Energy production and conversion];
                     COG0716"
                     /db_xref="CDD:440480"
ORIGIN      
        1 mkrilvvyyt qsgqlkeiid svlspltevt idflpidtte pfpfpwtdea ffgafpesyl
       61 qipqplkpfq lahtdydlvi lgyqvwylsp sipfnsflqs eagkrllqgk pvitisgtrn
      121 mwvmahqkvk klltecgahl vgniaftdrh hnhisvitiv qwlfsgdknk cylgvfpkag
      181 vadkdiqgas vygtliaphl qtgdytglqq eivahggvhy krfllsaekk gnrlfgiwak
      241 miygskkrkf llkcfriyly iaiwvlmpiv wvlywltypl ffwkverevk qliien
//
LOCUS       WP_181831954             246 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Capnocytophaga
            ochracea].
ACCESSION   WP_181831954
VERSION     WP_181831954.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 246)
  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 246)
  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 246)
  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 246)
  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 246)
  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 246)
  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..246
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..246
                     /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=27482
     Region          2..239
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mnifiiggts giglalasyy ylqgnrvgvc grdlqklade srfekyqadv tnivqlqnvi
       61 qqfvgertls llincagsya edvaddisye eavamlqtni mgavnclevg rkamchtggq
      121 ivllasisgi ldypesslyt ktkrsviqia dayrralrly giaittiapg yvdtqklrnl
      181 nhndlskkpf lvtktqavre itqaitekka lllfpkqmkw lmrflsymps fllskimykk
      241 ahymkk
//
LOCUS       WP_181832032             730 aa            linear   BCT 28-DEC-2024
DEFINITION  FUSC family protein [Capnocytophaga ochracea].
ACCESSION   WP_181832032
VERSION     WP_181832032.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..730
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..730
                     /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=83071
     Region          22..721
                     /region_name="YCCS_YHJK"
                     /note="integral membrane protein, YccS/YhfK family;
                     TIGR01667"
                     /db_xref="CDD:130728"
     Region          370..630
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mytsiisffk sfsffkgclk tiavliplgl gycfdlmdig ipialsviai spsdipgnqk
       61 hlygglliat llatisstlv nltapyeyll lptiflltfg nayislyghr atmvafaglf
      121 eiastlahlq tgwgivlysg cvllgglwys vlvyiflkir prlyseqllg kcfaltaeff
      181 svradlliak drseglkkli nlqtslneky eklreavlds rsksgktdyl qrqflmfiel
      241 vdifelalan pvqyekvdka faehreylqt yvdflkelsr qlqqmseyig srkkiqldnc
      301 lkdllaqtke knealkalse vseedkertl llrnfyiyie sqyhsienir hifenyysnd
      361 agvrdestyr kfvsyqnysw rrlkdhislk stffrhamrl sivvflgyli gdifpinnay
      421 wiiltifiim rpgfgitqer slsrvygtmi ggvasfaviy llpypslyly vailcmpiaf
      481 gliqenymya sifitisaif ifalitpnvy sliydrlldt vigvglsfag nylilptweh
      541 ntyreavtks vkanigylqq vkeifntgeg ittaykvsrk eavlalsnln ttfqrmlqep
      601 kfmqyknpsv ygiiviqqtf lasvasfgir lnskkvtfpk svfneaiesl iaalqhcltl
      661 lveptataqt dyktpieqfn qsireiidtp qntdssspis mretqfygeq fnylfglakn
      721 leqairsint
//
LOCUS       WP_181832122             804 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Capnocytophaga ochracea].
ACCESSION   WP_181832122
VERSION     WP_181832122.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 804)
  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 804)
  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 804)
  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 804)
  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..804
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..804
                     /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=90811
     Region          8..759
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mfrwikasfw gtiaglilrn riafllliaa itgglatqwk nvrftftean mlpddhpvnm
       61 eykhfldkfg eegnlilmal ddkkiytpev lnkwialsne lkkfkqidav isidnlpilv
      121 kdtaqqcfvt hkfiegkvkn qteadslkkv lseklpfyeg liynkktntl qtavymnkki
      181 vntqarkdfi lndfipivek feaqtglkvh tsgmpyirtl saqnimdeig lfilaallst
      241 saifffffrs framfismgv vsiavmwvfg flglfgyeit iltglipplv ivigipncvf
      301 linkyqqeis khgnqaksli rvirnvgnvt lltnlttaig fatfiftess llkqfgvias
      361 invvsiffis lllipiiysy mhipqekhlr hlhrnwiggl ikfientvkh hriavfttai
      421 allilsiigi ykikisgsli edmpksadff dditffekny ggimpleiti ntkqkngvtr
      481 lanlkridel cthieeipei skplslvnlv kyakqayyng npkyyslptt qeqnfilsyv
      541 knskgnanml sayvdslgqt arittfmkdi gtekmqqied niytkaqklf psnryevkit
      601 gkaylftkgt nylatnliws lalaillial imaymfrsfk mivvslipnl lpllitaglm
      661 gyfgiplkps tilvfsiafg isvddtihfl akyrlelvar nwkisksvya alretgvsmf
      721 ytsivllcgf svfllssfgg tkalgglisa tllfammtnl lllpslllfl erslsnketi
      781 kepkieifpk deeeenteke nktl
//
LOCUS       WP_181831983             279 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Capnocytophaga
            ochracea].
ACCESSION   WP_181831983
VERSION     WP_181831983.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..279
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..279
                     /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=32227
     Region          <67..263
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdiavkhial qqfstpvrve nycvfifrge gtiavdtvpy syegntllfl spyqyfqwve
       61 gtandnllle fhgdfyciey hkkevacngl lfnaiflhph ikitdkrfae iitlferied
      121 esktpslyse pvlksylqli lalaskeksl llehtslkte hhlandfqkl ledhfitern
      181 vsfyasalcl tpdsfskkik tllgktpnkl iqervvleak kllhltyksi kevafelnfe
      241 defyfsrffk knvglspkhf rkkvgisiva qpkteksmk
//
LOCUS       WP_181832042             574 aa            linear   BCT 28-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Capnocytophaga ochracea].
ACCESSION   WP_181832042
VERSION     WP_181832042.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 574)
  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..574
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..574
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=66785
     Region          47..574
                     /region_name="DltB"
                     /note="D-alanyl-lipoteichoic acid acyltransferase DltB,
                     MBOAT superfamily [Cell wall/membrane/envelope
                     biogenesis]; COG1696"
                     /db_xref="CDD:441302"
ORIGIN      
        1 msidallqwf idtfttenis kwfvdnfsft teqvrqwfiy dpnhpllfns slflglflvf
       61 ylvyiitkkh ahfrtvyvtl fslffyykag gnffvlliis sllnyffagq iyrrqnaslr
      121 kfflavsmva dlgilayfky tnflidslnt llqsnfalqd iilpigisfy tfqtmsytid
      181 vyrreiepak sfldftffvc ffpqlvagpi vrakdfipqi ykkisltkee tsfalfliig
      241 glikkavisd yislnfvdrv fdapnsytaf enlmavygys lqiycdfsgy sdmaiglall
      301 mgftlpinfr tpyqsknite fwrrwhisls twlkdylyfs vggnrkgtfw gyffptvffa
      361 stllwafhmq ektmlplyit lgaivvfvla ilisknrqks vrshfnqmtt mllgglwhga
      421 nlrfiiwgal hglalavhkt fteffpnknp ekrtffkgia niifvvitfh fvafcwiffr
      481 akdfdialsv iyniqsityd lhqfqviaeg yqnvfllmai gfvwhffpas lnewlkkvfg
      541 ampilfkaii laltfwmvya tassgaqpfi yfqf
//
LOCUS       WP_181832534             328 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Allobosea caraganae].
ACCESSION   WP_181832534
VERSION     WP_181832534.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
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="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     Protein         1..328
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34113
     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 mrsdrrslli yacqigllag lpgraqaasw pakpvtivvp ygagggadil grilaeelsi
       61 dlkerflven kagmsgslgv gyaaksapdg ytfvlctvga qitnpflykk lpydpmadlv
      121 pvvhlttppn ilvahaslgv stvkelialg ktraepllfa ttgtgsssnl saelfksmag
      181 ikitpvayqs saqaaldltt grvhatidsl tsminyteag gqlkllavat rdrlanyekv
      241 ptigetlpgf daspllyisa ptgtppdiva tlntainkii srpaiaakll glgypvgggt
      301 aqdlaaiiee erkkwraviv saglmate
//
LOCUS       WP_181832557             644 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Allobosea caraganae].
ACCESSION   WP_181832557
VERSION     WP_181832557.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
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="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     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=71244
     Region          1..599
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrnarergqr tafrhkdlgi wqswtwaeta eqirayargl qdlglkrgdk vaiigynrpr
       61 lywsmcaaqw lgavpvpvya dsvaeemayv ldhaeavfac vqdqeqvdkv lsiadrlprl
      121 rqmlydeprg lrdydhgklh digdviasga kalkdgaage aidremeqga gsdlaiilyt
      181 sgttgrpkgv mlshfnvita aeigcqfdgl neqdeviayl piawvgdhvf syaqaivagf
      241 cvncpegpet viedrrevgt tyafapprvf enmltitmvr medagplmrr mfhyflgvak
      301 qhgekilnge pvplgallly klgdmliyap lrnrfgltki kvgytageai gpelfkfyrs
      361 igvnlkqlyg qteagiyitm qpngeiradt vgrpapmvei rldengevly rspsifggyf
      421 kdpektaetm tadgyvrsgd agffdetghl kiidrakdvg klnsgelfpp kyienklkfy
      481 pnikeavafg qgrgyatvav nidltavgnw aernnvvyas yqelaghdlv ydmvarhide
      541 vnrslaaepm mggaqikrfl ilhkeldadd geltrtqkvr rgfiaeryap lvaalydgse
      601 aadistevtf edgrkgvisa rvkvrdakty pvtaperpaa araa
//
LOCUS       WP_181831720            1014 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            ochracea].
ACCESSION   WP_181831720
VERSION     WP_181831720.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga ochracea
  ORGANISM  Capnocytophaga ochracea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1014)
  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 1014)
  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 1014)
  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 1014)
  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..1014
                     /organism="Capnocytophaga ochracea"
                     /db_xref="taxon:1018"
     Protein         1..1014
                     /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=113337
     Region          23..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnlflsvl lfllvswsya qqrtirgtvs dattkeplms asvvikgtsk gvstdmsgky
       61 tievsvgqtl evsfmgyvtq nvkvtantps plnialaeeq rkldevvvvg ygvtkvrdla
      121 gaitsiktnd vkagvvadms qmlkgrasgv qvrqnslepg gnvsirvrga ssvsadnepl
      181 yvidgfqtdn msqisiddie sieilkdast taiygargan gvilittkkg kegsfnveys
      241 nqtsyknmyn pwnlldaget ialtrrlyeq tqdaaygkwt aqqatyrgkg tdwlketthd
      301 aftvlhqlsv sggtdrlsaf msgnyltepg illntdynry ggrinlqyki spkvraganm
      361 sfskskkkfl dmgtvssdkn imyrifnlep wknkegfdvf gtkdrrpavf eemsgaqlyr
      421 hfntmyatay adidllpslt ingrytyayd hlktekyydr stsigqsykg qaflsheenv
      481 khqiegvaty hpkmegkhdv kvtagtsyiy qrgkgdevqa ygfasdvfsf knigaaqhld
      541 wigsgessik kasvfgraey ifnnryiina svradgssvf gadyrwgifp agsiawhlge
      601 eefmefvkpl fsriklrtsy glsgndgirf glsqyqysvr dvyigndvns kgmypsnpyn
      661 pklrwettaq wnagidlvvg rveasfdyyi krthdllnpd pihpsggfpn yvndgrrfey
      721 tammvndgei enrgfevaik stninkndfv wttafnfshn rsevlklndg kprfqyirph
      781 gsydekeymm lkegeplsai ygyefdgilq egesyapqpn sapgdpkfkd lngdgkidek
      841 drtvlgtgip ktiiglnnsf tykgfdfsff feaslgakml nltriyledn nrlsdsadrw
      901 tkahasnsvp rngyqktakl qygsyvnsrf vedadfvklr nvelgytftg sqwnmktlkt
      961 mrvfvggqnl ltftkyqgfd pdistngssa iaqgldlnsy payrtinfgv kltf
//
LOCUS       WP_181832627             490 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Allobosea caraganae].
ACCESSION   WP_181832627
VERSION     WP_181832627.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     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=52486
     Region          8..490
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mrsghsdqhy dvivvgagma glsaaallar hnykvlvaeg hdrpggcmts wvrkprdrnr
       61 varrfvfdag vqdisglspq apvrhllsqi geqdsldwlp vqhryvvngt tldlprnwdg
      121 lervlcaafa edaagisall reirlvydel yagmaaadyr pvtasaqmqs gqrfehaara
      181 agqsyvalle rhignptlis ifkilseyvt ddpaclsltd mvplfgyyig ggfypaggaq
      241 klpdllcrsi qrhhgeirlk srvnafilrd griagielas gqaayapavi snadigashg
      301 allgpydlpp ryrqrlkqlk rgpsailinf gldaipdlpa rvfveqdgli fglgnpsaid
      361 stlapaghaa lsllhllpea eahswfalsp aqdedarkly aqkliaaagr vipgledhiv
      421 hyevaapptf rhyiqsengs iygaargqwc ppvaspvpgl flagagtatg pgveaavlsg
      481 lhaahavmdr
//
LOCUS       WP_181832676             273 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Allobosea caraganae].
ACCESSION   WP_181832676
VERSION     WP_181832676.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
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="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     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=30203
     Region          39..160
                     /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 mslviatter raapvsagsa qasgslgnff qglrpdwhar wawenyepti lnlsrqfglr
       61 rvceigggrd plftaeqaar hgvdlivndi dagelaltpa gletarfdia gdlsepdvrr
      121 gaydlmvsrm vfehvhdveq awrnihella pggvalaffp tlwapvftln hilpekasra
      181 ivhalyparr dgggdpkfpa fydwcrgnpa llgpmlnrag fsdvhvqpfw gheyfkrmpg
      241 ireadhafna lsakigwhfv tthayvvvrk grd
//
LOCUS       WP_181832618             181 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Allobosea caraganae].
ACCESSION   WP_181832618
VERSION     WP_181832618.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 181)
  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 181)
  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 181)
  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 181)
  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 181)
  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 181)
  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..181
                     /organism="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     Protein         1..181
                     /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=19109
     Region          <51..149
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mggsvesrqv rveqplllgg ilafaalvcl iaagglvlaq rgrverasfi eplsherlea
       61 gfalyrqhca schgaflaga pgwqadaslp palnetghaf nhsdldlfqr vaagarapgg
      121 rismpafrgv lgddeivtvl syiaawwpeq erlrrsgpdw vfpatcspga apetpdragr
      181 s
//
LOCUS       WP_181832689             325 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Allobosea caraganae].
ACCESSION   WP_181832689
VERSION     WP_181832689.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
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="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     Protein         1..325
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34678
     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 miplskslaa vlacviglst asaamaadty psrpvtmivp fgagggtdvi artvsdelsr
       61 algqsivvea rpgangaigs avvaravpdg ytllftaqst yslnpnlmkd plfdqlkdlv
      121 pvasigrspw liavpmesef ksladvvayg kanpgklvfp fwqssvlvtg etfgrmadir
      181 mrkvpykgqv eantdflggr lplmvtdiag grapveagkm rllasttakr saafpdvptm
      241 reqgldvvtd smlavfapag tpqpildrln qevsrivlgs ekvrdrlrql gleptvmtqn
      301 eadafvrsem trweemirra glqke
//
LOCUS       WP_181832736             263 aa            linear   BCT 28-DEC-2024
DEFINITION  inositol monophosphatase family protein [Allobosea caraganae].
ACCESSION   WP_181832736
VERSION     WP_181832736.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 263)
  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..263
                     /organism="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     Protein         1..263
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27684
     Region          9..262
                     /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 mserqfsvll geadalarda aellvrmqge qpvvtrkdlr dvvtaadlas eklvieglrk
       61 ltpeaailse eagfsgstag prwiidpldg tvnyasglpw fsvtmayqeq grtvlgltha
      121 plagivarys adgiatindr paavsgterl sdavvsvvlt shyttdeiar ttnvirrlae
      181 ltrgvrivvs gglemslvaa grldsfvglk adivshaaal plvraaggrv tmvdgrdsgd
      241 ddlekvasng lihdelleai rsa
//
LOCUS       WP_181832860              55 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Allobosea
            caraganae].
ACCESSION   WP_181832860
VERSION     WP_181832860.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 55)
  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..55
                     /organism="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     Protein         1..55
                     /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=5885
     Region          1..>55
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mvtelallrl ergsgpafea afarvasllt gadgylrhrl vptlddadly llqve
//
LOCUS       WP_181832827             327 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Allobosea caraganae].
ACCESSION   WP_181832827
VERSION     WP_181832827.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
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="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34463
     Region          8..323
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mlwksvgltl avvtsvltgs ayaqgtdypt qnvriivpft pgggtdltar ivadalgkaw
       61 gqsvivenrp gaasqigidy vakakpdgyt llwssadgis vlpavkpkmp ykipdsfefv
      121 stfssfplil gvysklpitn mkefidyaka npgkmhysss gagggghlqp aymakelgld
      181 vkhvpydsaa patvavaggh aeftdvapst vapyikdgtv raiatsgrnr tilfpdvptv
      241 selgypdlte dffygmyapa gtpadivakl rdgvqavlks pgmaerlral gleplgltge
      301 efkafavadl nrwtkiakai dfqlsgq
//
LOCUS       WP_181833033             219 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Bacillus taeanensis].
ACCESSION   WP_181833033
VERSION     WP_181833033.1
KEYWORDS    RefSeq.
SOURCE      Bacillus taeanensis
  ORGANISM  Bacillus taeanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
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="Bacillus taeanensis"
                     /db_xref="taxon:273032"
     Protein         1..219
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25055
     Region          1..200
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mikaigfdmd gvlvdtmknh arawqqtfle hkykieeqli fqlegmngpk tidwlndhys
       61 fslsteakql iynrkrllfk einvlsffed tidtiryiqk qglktalitg snrefaeevl
      121 ksknltfdav itgsdvkngk phpepyqram ealmidpkew livenaplgi taakkagakv
      181 lavetslpkq ylthadhiip fpallkeeii nwinererl
//
LOCUS       WP_181833634             342 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Klebsiella pneumoniae].
ACCESSION   WP_181833634
VERSION     WP_181833634.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=36422
     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 mmddyrrivr rrlllillla llivasllld fmlgpsglpl qslwqtltdp asadpgtrai
       61 vwdirlpyav maiivglalg lagaemqtil nnplaspftl gvssaaafga alaivlgigl
      121 pgipgqwfis anafifalla allldgitrw tqeatsgvil fgialvftfn alvsmlqfia
      181 nedtlqglvf wtmgsidras wskvaillva lalvmplslr sawkltalrl gedraisfgi
      241 nvrrlrlttl lrisilsals vafvgpigfi glvaphiarm lfgedhrfyl pasaligalv
      301 lslasiaskn lipgaiipvg ivtslvgvpf flsiilrhrg qv
//
LOCUS       WP_181833647             266 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Klebsiella pneumoniae].
ACCESSION   WP_181833647
VERSION     WP_181833647.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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 14398448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=29583
     Region          30..125
                     /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          189..264
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mimagaksem pgsidkaprh dettgwssta isyqrgeadp phhhvegqll fatrgvmlvq
       61 tesdrwvipp qralwlpplh ihsyhllsqt hlraiyfsss liaectsftk sqqvhvitat
      121 plvkeliagl fsedyarpsq rkiallllei lseappltma lpmpnderlf saarsllvnq
      181 rweaslsela fmsamsertf srlfmkdtgf sfrtwkqrar icasldllan gvpikqvayq
      241 lgfscpaaft aafrcilgat prdfvp
//
LOCUS       WP_181833749             423 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Acidipropionibacterium
            virtanenii].
ACCESSION   WP_181833749
VERSION     WP_181833749.1
KEYWORDS    RefSeq.
SOURCE      Acidipropionibacterium virtanenii
  ORGANISM  Acidipropionibacterium virtanenii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Acidipropionibacterium.
REFERENCE   1  (residues 1 to 423)
  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..423
                     /organism="Acidipropionibacterium virtanenii"
                     /db_xref="taxon:2057246"
     Protein         1..423
                     /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=45544
     Region          178..411
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 marwreglpv aglsalmvve tffdlrrsla pspwlwnsyl ivylvaalac lvlaamirga
       61 gghpvafsra gwavvvaaaa lmayclvssc ltprprvsyv tvpraylvvp tltamatlll
      121 avtavralpd rpvhrllwwp aavtlvcsfv qwprsalvhg sprlatgmgg savvhvplll
      181 atgvvlaafl agwhrwwsla ltvmgaaavv ltgsrsgvvc lvlagavvcl qwlrsrrawl
      241 vagivavvag avvvavpmlh rllnptdelr aknletaitf wtatpkhvll gvgsgrlwpw
      301 yafdshllrt pwrglvgtqw gpalnsshst flqvlvelgl agmllllpvv tvpvlilvrr
      361 lwpglrgvar pvpdvvtlva laatipaffl dtyllknyga slwwwlvilc clraghqwps
      421 gra
//
LOCUS       WP_181833895             378 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Acidipropionibacterium
            virtanenii].
ACCESSION   WP_181833895
VERSION     WP_181833895.1
KEYWORDS    RefSeq.
SOURCE      Acidipropionibacterium virtanenii
  ORGANISM  Acidipropionibacterium virtanenii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Acidipropionibacterium.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..378
                     /organism="Acidipropionibacterium virtanenii"
                     /db_xref="taxon:2057246"
     Protein         1..378
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=40590
     Region          139..377
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 makrlaarts amttatlaqm tqrhswfral saddrswisi varngidgfv rwfaddeaep
       61 ysptdvfdva prsmtrkisl hqtvdlvrtt ievveeqiee kmprgdrsvl snaiahysre
      121 vafaaaevya raaeqrgtwd erlealvvda ivrddvddeq ltsrastlgw kpgsklcvvv
      181 gavgssralh glrraaehah lsvlaavqsd rmvavisgaa lsddasavga aeplaehfge
      241 gpvvvgpvvg dltgapgsar salsaaraav awpegprlia sadvipervl agdrqavewl
      301 vaevftplne atgdlmdtcv sfldhggsve gtgramyihp ntvryrlkki qdvtgysptd
      361 preayllrla vtlgrlrg
//
LOCUS       WP_181833897             238 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Acidipropionibacterium virtanenii].
ACCESSION   WP_181833897
VERSION     WP_181833897.1
KEYWORDS    RefSeq.
SOURCE      Acidipropionibacterium virtanenii
  ORGANISM  Acidipropionibacterium virtanenii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Acidipropionibacterium.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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..238
                     /organism="Acidipropionibacterium virtanenii"
                     /db_xref="taxon:2057246"
     Protein         1..238
                     /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=26234
     Region          18..>76
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          48..219
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mrapfrdqrg vakyrhevla vvlrageasr lqvlarrrdh epfagrlalp sgpvevsesm
       61 eeamdrhlad qlglaglahr eqlatysdpg rdpfertiat aylglvpcdr qedlaigavw
      121 vdavdlpela fdhhlvveta lerlrgkisy tniafalapa eftmatlrai ygavlghdvd
      181 vtnlsrvlrr rrqiervgil aepgarggrp pstwrfteds yrvtdpfaal gpgrghev
//
LOCUS       WP_181832824             280 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Allobosea caraganae].
ACCESSION   WP_181832824
VERSION     WP_181832824.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 280)
  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..280
                     /organism="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     Protein         1..280
                     /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=30244
     Region          49..>238
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mqskvaswss vkriidksyv agrnirfpfs erslyrswqk ngriflisrn slkqaivetr
       61 rikgvhftyp alaameilaa ggldyiyidg ehgaftisdv eaccivadrl gvtpvarvpd
      121 gtapvitqfl drgvrgiivp hveteeqari aaeatyfapl gqrsfgggrp yahvgnkdip
      181 sllkqanagv slslmietak gldniaaiaa vpgvdylsfg mfdlcqslgh pgdpkhpevt
      241 aaveaaaakv ralgkpired fitfawindl vvegarrllp
//
LOCUS       WP_181834209             297 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Aquitalea
            aquatica].
ACCESSION   WP_181834209
VERSION     WP_181834209.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 297)
  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 297)
  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 297)
  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 297)
  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 297)
  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..297
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..297
                     /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=32235
     Region          3..250
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mklsifqesr iggrsynqdr lviahsreav mlvvadgmgg hlqgevaaqi tidlmselfy
       61 qqatptlshp nrflvnaiss thqaildyaa dqrlpeipst tvvaaiiqqg mlywchvgds
      121 rlylldnkqg mrlrsrdhsq vqrlidqgkl teegarthpe rnkiynclga tsdpdidige
      181 kqflqagasi vlcsdglwsq isdsemekvf igravgqvmp almnvaerra gsagdnlsav
      241 avtllddsad iagkadaldt lltpprhagr vildpnlelm hkeilasrva apsgkqs
//
LOCUS       WP_181834256             289 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Aquitalea aquatica].
ACCESSION   WP_181834256
VERSION     WP_181834256.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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..289
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..289
                     /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=31344
     Region          28..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 mtemasvfag nagllvvvvl lfgllvgsfl nvvihrlpkm melgwqqecd aylgreptaq
       61 pkynllvpas hcpvcrqevr pwqnipllsy allrgrchgc staislrypa velltavlfa
      121 llawhygwsv qlpaylalta vlvaltfida dtqllpdslt lpllwagllf nlltgtvals
      181 davlgamagy lslwlvywlf klatgkegmg ygdfkllaaf gawlgwsmlp liillsslvg
      241 avvgivlill armgrgqalp fgpylaaagw iallwgqdiv swylgiyah
//
LOCUS       WP_181834369             676 aa            linear   BCT 28-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein [Aquitalea aquatica].
ACCESSION   WP_181834369
VERSION     WP_181834369.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 676)
  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 676)
  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 676)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..676
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..676
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75467
     Region          54..370
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 mpaliapafp eagylptrld evianrsqqq qqvdaahcqa rqegqpspcv qvlnislffd
       61 gtnnhgdsdd kanpvnssnv rrlfnasigy ldgrdwgyys yymqgvgtvf keigegkpsg
      121 sglsfaagge drilwgltrl idalrraysa qnekldaeda yalvkamqys yvesehgvkq
      181 qrsttrqerr eliqqqlapl ltkrqngykp eilsiklyvy gfsrgaaear afiwrlreql
      241 ddgceslcgi plsveflglf dtvaavglte lapgaeghmg wadgtmklpp eahlprrcah
      301 lvsaheqrlc faldsiaian rsypactlge wvypgmhsdv gggyppgdqg karegqgmll
      361 sqlpllhmyr lafdagaplq vnkellhgsa eriaqlqqre qwrfmkests qlytyselli
      421 trfeawrqqa sasssledil qfqtaqitaw riaryagglh ekggpgyena pfyqhsrdtp
      481 swqaeaekda wkkqskqgks qavtleapvk ngkptdgnkt ytpninkeye atqdktqlke
      541 gakdfaddyv grttlsfnvi gglatfftgi srvfsddcge elvmlredge glynavtqnp
      601 elmalydehv hdsrawfmha alakrephgt ylryrtvfft dgnsnkqlic rsprvtdikr
      661 keleqsaqqr isrssh
//
LOCUS       WP_181834329             196 aa            linear   BCT 28-DEC-2024
DEFINITION  IMPACT family protein [Aquitalea aquatica].
ACCESSION   WP_181834329
VERSION     WP_181834329.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 196)
  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 196)
  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..196
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..196
                     /product="IMPACT family protein"
                     /calculated_mol_wt=21343
     Region          1..189
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mfqlaapvva eieikksrfi aalypvqsrd eamlqlaalr rewpdarhyc avllvsgdsm
       61 ldddgepsgt aarpmynvlm hkqlhnvlav vvryfggikl gagglvrayt qavntalqta
      121 qlqpvvlmqs clarvgfase srlrhccael aisvgaaeyg ehvvlalmmp qaqcqalqtr
      181 lydllagevy fmtdes
//
LOCUS       WP_181834400             111 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Aquitalea
            aquatica].
ACCESSION   WP_181834400
VERSION     WP_181834400.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 111)
  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..111
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..111
                     /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=12234
     Region          10..87
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mplklpsppy wavifssqrs aadqgyanma ermlrlaevq pgylgaesar dsagfgitvs
       61 ywdsveaiaa wrqhaehlva qklgrevwyr dfslkvarve rahasgqgrd a
//
LOCUS       WP_181834768             298 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aquitalea aquatica].
ACCESSION   WP_181834768
VERSION     WP_181834768.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 298)
  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..298
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..298
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=34138
     Region          69..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 mpssrifkll sgkrqcfgvl rvlicllasl paqaadnvir yypsgsiyty rwallklald
       61 hvekvdhrry elvplddkvt qwraeqllst gkvdvlafap naqrerllqp vrmdilkgil
      121 gyrvffvrke dvaifrgmnp qqfragvrlg lnsqwadypi mknngyevla sigyeslfem
      181 lvagrfdafp rglnevgsem rellprypal tlektkaiyf pfpvyfwvgk entplakril
      241 qglkmaerdg sfkalflrhh aeairllgen gwqttqiant elpagnakpd tswwwtrr
//
LOCUS       WP_181834681             242 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aquitalea aquatica].
ACCESSION   WP_181834681
VERSION     WP_181834681.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 242)
  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..242
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..242
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27098
     Region          24..241
                     /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 mriqlylasl lllcsqlvqa applrvlted yppfnmmgqg ghisglstdi vqelfrragv
       61 sydisllpwi rafnltvlea ntclysttrt dsrehqfkwi gplvenpwvl yaradsrhai
      121 lsleearsfk iggysgdais qylidrgfdv dlantdqlnv kkllvgridf watgkylgas
      181 llarekvsql kpvltfnttl lylacnpama dsqvqqlnel lrgmqrdgtl arinakylnq
      241 kd
//
LOCUS       WP_181834562             402 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Aquitalea aquatica].
ACCESSION   WP_181834562
VERSION     WP_181834562.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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=45507
     Region          135..395
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 msithtldkl ppslppsarl llsrlqrlqs gglrlltpag halwfgqpqh svnaelhihd
       61 wagcrkllta gdigfaeayr dglldspelt allrlalrne havppalsgs lparwwyrlk
      121 hllrrnsrrg srrnihahyd lgndfyrlwl dpswtyssaw fngdytqslq qaqqakyqri
      181 cdtlglqpgm rvleigcgwg gfaehasrag iavhgitisp aqlelarqrl agqplaqlel
      241 rdyrdldgqy davvsiemfe avgeaywpqy frtvrrllhp ggqaliqsit iadayferyr
      301 aksdfiqqfi fpggmlpspa rfsqtasaag lhtsqrldfg pdyaetlrrw rqafentlds
      361 vrqqgfdeaf irlwrlylcy ceagfdegri gvsqfllqdr pa
//
LOCUS       WP_181834942             444 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Aquitalea
            aquatica].
ACCESSION   WP_181834942
VERSION     WP_181834942.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (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   2  (residues 1 to 444)
  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..444
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..444
                     /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=48730
     Region          4..434
                     /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 msplsneasl dtisrmldel sepriviteh feilhanqay raaygaealg rhcyevshgy
       61 qrpcdeeges cplrmtlasg qpervlhihr tahgdehvdv elmpladisg hrhlfiekmk
      121 plqlassqaa adkmvgrsav frrmlllaqr aapsraavll igesgtgkeg laraihdsgg
      181 aaqrpfiavd caslsetlle selfgyekga ftganqrkqg lveaahggtl fldeigdlpl
      241 sqqvkllrll esgsfrrvgg insipasfrl iaathrnlaa mveagsfrad lyyrlavfpi
      301 rlpplrerre dipllaasll ervapgrrlq leaaalqwll qqpfngnire lrnllerasl
      361 lsdgdvitld nlcadewcst papaaamphf hcgllpleql esqylqwave qsglsrqqla
      421 salqltertl yrrlagrqkk apaa
//
LOCUS       WP_181835137             386 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Aquitalea aquatica].
ACCESSION   WP_181835137
VERSION     WP_181835137.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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..386
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..386
                     /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=41678
     Region          23..377
                     /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 mkdqemleaa feqfntvssq lidayrqlev qvnvlnaqld eannqlrkqr denaelaerl
       61 gmllealpag vvqlaadgvv vaenpaaqll lqgkhgglaw davmsgwtrs eldgtytlpq
      121 qeaarrlalq yqdlpasggr ivllhdvsrl hhltvelahq qklaamggma aslahqlrtp
      181 latamlytan lkqeglrped rakfvdksla rmkalegliq nmlgfvrgqt salewldvaa
      241 lvedvaavli pqchergmiw dcnnllpsai tvmgdrkalq galvnllena mhfspeggri
      301 gltvclqdeq vcfrveddgv glrgadparl fepffttrpg gtglglsivk kvaeelagtv
      361 vggdraqgga yfeltlpcrg mgaidv
//
LOCUS       WP_181835209             109 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Aquitalea aquatica].
ACCESSION   WP_181835209
VERSION     WP_181835209.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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=12378
     Region          9..99
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpdeqghper deielgkvlm aladptrrrv vkalledvef aerhctsfgl qlskatrshh
       61 frilreagli rqvdrgnsrm aqlrrqdieq rfpgllglil qeadkdiap
//
LOCUS       WP_181835241              98 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Aquitalea
            aquatica].
ACCESSION   WP_181835241
VERSION     WP_181835241.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 98)
  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..98
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..98
                     /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=11265
     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 mileaamlqv kagmqqefea afaqaqliia smpgyhwhql qrclevegky lllvgwdsva
       61 aheqgfrqsa gyqewkrllh hfyqpfpvve hfeqilpv
//
LOCUS       WP_181835353             505 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Aquitalea
            aquatica].
ACCESSION   WP_181835353
VERSION     WP_181835353.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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=54222
     Region          25..378
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mrsdattpat qdfvrkladq afarsagapl iagnsvqlly dssdnfpawk qaiaaaedsv
       61 fiemyivand hfgreirqll mdkaaagikv cllydwmgcw kpslggffrp llaagaevra
      121 ynpptltggl tllgrnhrkl ivvdrqtafi sglcissswe gqpdagiapw rdtglalrgp
      181 lvaealaafa dswascgtal adtwqqppgp qpeagtiaar liattpstah mmrldmlias
      241 farrtlwltd ayfmgtstyl salkqaaldg vdvrllvprs sdirwiatvs rtmyrplles
      301 gvrvfewngs mihaktavad srwarigstn lnisswlanr eidvaiedet vagelaarfl
      361 qdlqqstevv lsghkrtpvl thprqrqsps flfpaashaa rssasaaarq aarigdalga
      421 vvrgtrsidt seaaafltig lallalallv vlfpwlvagp laflllvsgg aivlkalgly
      481 rrrnekkqql aatknnlkpp appag
//
LOCUS       WP_181835360             375 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Aquitalea aquatica].
ACCESSION   WP_181835360
VERSION     WP_181835360.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..375
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..375
                     /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=42651
     Region          1..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 mktnyyqldg lrgiailmti fthasfgmmg vlsitplfqq skneiilpdy irhigdqsgh
       61 gvqlffiisa islvfslssn tsfhlkhylt krffriapaf yigiiyylai lgfksrqfap
      121 ngisasdilv tlsffhiwss kaynavvpgg wsisnevmfy vllptmlcii kksrisfill
      181 tivsyayaql nyiwisnnaq wsafqyfnft nqlpvfmtgl llghtlfnln itkfkspfil
      241 ikyskslsii filfailalp qfnidrtlqs hlaftiiacl siyfifinps ilftnkilvh
      301 igkvsfsiyl ahfslmrich qlasilihth gitfllayfl llftlsylia ivtyriielp
      361 fikfsqkits staaq
//
LOCUS       WP_181835436             517 aa            linear   BCT 28-DEC-2024
DEFINITION  two-component system sensor histidine kinase NtrB [Aquitalea
            aquatica].
ACCESSION   WP_181835436
VERSION     WP_181835436.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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   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 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   4  (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   5  (residues 1 to 517)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
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 11467505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..517
                     /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=56826
     Region          191..511
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
ORIGIN      
        1 mperslpltp rkalafvngf ralmllvllf msmlqgtegq plvdggarfy lwsavyggli
       61 lcwfalrtgk iahtlqlsla iaadilmivl lmglnggvks gygmlllpyl avagllssgr
      121 yalfyasiat aslfgyvgye hyrhevlfgs tadlfqtgll slagfvtsmv tyqlarvare
      181 seelasrrgg eianlnrlne lvlqsqrdav ivldetgtvr qfnaqavryf pgmqrgillp
      241 elapiverwr lnshspmpvf vernvrgrql agrmvpilag dlrgvvmflr dmadmaeeak
      301 riklaalgrl taniaheirn plaaishagd llaegaedaa tqrltrivrd narringlve
      361 evlmlgrrdr vktetiklsq fladfleqfg maqpeaagri lttfhssssv yfdrghlgqi
      421 lsnlvanawr hssrvhgavq ieisqlesqv lirviddgpg mnedaqshlf epffttessg
      481 tglglyiare laeandarld yippggvfrl schhaye
//
LOCUS       WP_181835462             366 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Aquitalea
            aquatica].
ACCESSION   WP_181835462
VERSION     WP_181835462.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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
REFERENCE   2  (residues 1 to 366)
  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 366)
  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..366
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..366
                     /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=39748
     Region          37..362
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mtrfarhleh htivnpfpgi vkletalghr iktrigsnes lpdpvsplag elgkalaema
       61 rlypdpyaha lreraaklng vspteilfdt gadslillal rltcnpgdav vttagtyptf
      121 ryfaegvgar vlevpycqrg qhmqpdlarl aevaraehas vlylanpdnp tghywqaedi
      181 rtlraalpph tlllldeayv dfctdaadap ptgilphtlr lrtlskayal aglrvgyaia
      241 sadiiakadq irpqyalssi aqaaaqivld dpdysrklva qtitlrhhls halydqgltp
      301 lpshtnfvcv aypdalqaea iqrhllqcgi aihrpqhpav rhmlritahp qatsarvlaa
      361 lagqld
//
LOCUS       WP_181835346             381 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Aquitalea aquatica].
ACCESSION   WP_181835346
VERSION     WP_181835346.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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=40721
     Region          1..380
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mkfatktihs ghdssqhsra vmppiyqtsv fefaeigeql pfayartgtp traalescla
       61 slenaqhgla fasgmaaida vlratlkpgd eviavadlyg gayrlltkvm epagitvtfa
      121 dltdtanlaa iisprtkllw lesptnplln lvdisalsai ahqhgtkvav dstfatpylq
      181 npldlgadiv vhsatkylgg hsdvllglva vndqqlftdi kfiqnsaggv pgpqdcfltl
      241 rgiktlhlrm drhcdnaeqv aaflqghpkv ekvffpgfad hpgheiakqq mrrfggiiti
      301 wlkedsraea srvasklqlf alaeslggve slvnhsytms hggmppeqka algiregglr
      361 lsigvedied iladlaqala d
//
LOCUS       WP_181835544             244 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Aquitalea aquatica].
ACCESSION   WP_181835544
VERSION     WP_181835544.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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   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 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
REFERENCE   4  (residues 1 to 244)
  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..244
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..244
                     /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=26806
     Region          7..240
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          157..240
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhttdtllle lrsyqqesqq hqhdyhqlvl pargrlelev dgrgghveag qlaviaagsd
       61 hgfaapgdnv fvvanvptal apqlaqlpaf lpldagllay vaflreelqr pqagengrrq
      121 mlllltqlla eragaglqld rrvaaarall darfaeeisl vqlaaaahls vrqlselfrr
      181 qlgmspgqyq leqrmqhgwl lleqgslpvq qvaehcgyas lsafsdrfrr hfgiapshfr
      241 hpak
//
LOCUS       WP_181835602             722 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Aquitalea aquatica].
ACCESSION   WP_181835602
VERSION     WP_181835602.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 722)
  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 722)
  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 722)
  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 722)
  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..722
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..722
                     /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=79266
     Region          67..722
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkqslqqsah lqqrklparm avgmlavals pslalaaetg qtletvtveg eapvrdtykt
       61 vtsnigktkq qlrdipqsit vvnqqlmqdq gaatlkdalr nvpgitfaag eggrtgdqvv
      121 irgfsaatdt yrdgmrdigq ynrdafnddk vevlkgassm lfgrgstggv vnqvskspyl
      181 gsklegdlti gtndfqrvta dinqttgdhs avrlslmdth dgsdrgaakn erwgiapsva
      241 fglgepttvv lsymhqeenn vpdygvpynt atrqplnvdr skfygldgdf ekttadivta
      301 kithdfgdgm elsnqlrynr fwrdvsptap rlastdtsds aimrrskplr dgvdqswnnq
      361 tdltsrfatg dirhtlltgm elsyelsdts ryallnsvps ttvgnpnsad avnlaryrts
      421 ntqfqasnig lyamdtieln rqwkavlgtr fdrfegdynv raynangsln ssnsydlsrt
      481 dnvwswrggl iwqpdlaqsy yfsygtsfnp sgetysldka takvdpeknr nielgakwdl
      541 ldgdaslraa lfriektner ntdpldtsvv vlsgkrhtng vevegsgrlt erwevfagvt
      601 lmdskidkaa paaqgqtgte gmmprytpra taniwttykf tdlitggiga tyvgkryate
      661 tnvnylpdyt ignamlsyet khyrvqlnln nltnkkyfdg aygghatlgt preaqltvgl
      721 ky
//
LOCUS       WP_181835671             535 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Aquitalea aquatica].
ACCESSION   WP_181835671
VERSION     WP_181835671.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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=57094
     Region          50..511
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mssspssasa taaadafnpa vtpdlqlpgr rlplwlsgss llisllallp vafiivisvq
       61 tgwetvarlv frprvgellf ntsllvvltl plcvalgial awltersnlp arrmwsalai
      121 aplavpafvh syawisllpa fnglaaavll sviayfpfiy lpaaaalrrm dpaledsaaa
      181 lglapwaifr rvtlpqlrla iwgggllvsl hllaeyglya mirfdtftta ifdqfqssfn
      241 gpaanmlagv lalcclllls veaatrgnar yarvgsgsar qtvptrlgwr wgvpalllcl
      301 ttaaltlgvp lltlghwlwe ggpaawqnda lwpalrqtll ygavgalltv laavplawls
      361 vrapsrlqrl qegcnyitsa lpgivtalal vtitinfarp lyqtvitill ayllmflpra
      421 lislragiaq apaelehaar slgctpgkal wrvtlrlaap gaaagmamvf laisneltat
      481 lllapngtrt latgfwamts eidyimaapy allmvllslp ltwllhhhsk rtagr
//
LOCUS       WP_181835750             140 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Aquitalea aquatica].
ACCESSION   WP_181835750
VERSION     WP_181835750.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 140)
  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..140
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..140
                     /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=15871
     Region          10..140
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 meksypiidr qtitmrwgdm davghlnnty yfryleqirl nwlealghgi dpqstgpvla
       61 stsctfrkql typavveiti eleklgrssl qlrhhfyrlg dpdtvyayad vtlvwvdyqa
      121 gvpvaipddi rqaieraiaa
//
LOCUS       WP_181836158             260 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Aquitalea aquatica].
ACCESSION   WP_181836158
VERSION     WP_181836158.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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..260
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..260
                     /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=28495
     Region          1..256
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          16..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"
ORIGIN      
        1 mrdaelellg dvprdvvvie rafaagshyp ahrhqrgqla farqgsisvm trfghwlvpp
       61 gravwvpagi ehemqmlgpv vmlntfvsvd aadrvglath cqvcavspll yqlllqavel
      121 plvypmdgrs hhlmglllte ismatvlplh aplpmnegla alcrsllaap tllmdtdama
      181 armamsrstf trffrketgi symqwrqqac llaairrlee gqsvtsvale lgygspstft
      241 alfrktlgms pqayvriqan
//
LOCUS       WP_181836167             238 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Aquitalea aquatica].
ACCESSION   WP_181836167
VERSION     WP_181836167.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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=26907
     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 msrterlftl lqalrhhrfp vtgasladel gvslrtlyrd iatlqaqgan iegepglgyi
       61 lrpgfmlppl mftaeeieal vlgskwvakr tdthlgsaak nalakissvl pqelrhnlds
      121 sslmvgtasq aetdvvdlsi irrairseyk lridycdvqg nvtqrtiwpl algyfdhvrm
      181 lagwcevrqd frhfrtdris tllitqdhyp rrkqdllkew rtcdayqqas nnkigknn
//
LOCUS       WP_181836412             346 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Aquitalea aquatica].
ACCESSION   WP_181836412
VERSION     WP_181836412.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 346)
  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..346
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..346
                     /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=36674
     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 mqtrltetfg vrlplacpgm syiatpelva atanagglgi latgplkpeq traairrire
       61 ltdrpfgigc tlmmpgaren cevalqeqvp vinfslgkgd wivkaahsyg gkviatvvte
      121 khaisaekag vdgllvtghe aaahggevts lvlipairkv calpiiaagg fgsgagllaa
      181 lalgadavam gsrlamtqes pvherskemi rqrsvadtly srnfdglwcr mmdtptaraa
      241 trkpmnllaa awkasaiark mgmpvwkval ggmlqkpqel rqlalfgaat esirlaieeg
      301 nhqhgvqlig qvqgliddvp tvqqlferim qeaghnlsrl qqlnqa
//
LOCUS       WP_181836442             401 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Aquitalea aquatica].
ACCESSION   WP_181836442
VERSION     WP_181836442.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 401)
  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 401)
  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..401
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..401
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=46442
     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 mlidfftalr daglpvslke fltllealkq qvafgsldaf yylarttlik dekhydrfdq
       61 vfghyfqgke lllddlqtei pedwlrkqve kflseeekqq lqalgwdklm dtlrqrleeq
      121 kerhqggnkw igtggtspfg aygynpegir igqdgsrhrr avkvwdqref rnfdnaaelg
      181 srniklalrr lrefaregae evldldgtia atarnaglle lkmlrelrnt vkvlvlfdvg
      241 gsmddhikav eelfsavkse fkhleyyyfh ncvyetvwkd nrrrqgssls thelihtfgs
      301 dyklifvgda tmspyeisyp ggsvehmnpe sgevwmrrll qqfrhavwln pvaepywdyt
      361 qslqmmrrll qermypltle gvdqamralk ksmpasalpp v
//
LOCUS       WP_181836539             417 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Aquitalea aquatica].
ACCESSION   WP_181836539
VERSION     WP_181836539.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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 417)
  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 417)
  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 417)
  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 417)
  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 417)
  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..417
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..417
                     /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=45193
     Region          7..410
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 masprfkqya vlasstlaft icfmiwmmfa vlgipikqhl glnetefgil aatpvlsgsl
       61 vrvplgiwtd rfggrivmfv lmlvcvpfiy lmqyataywq flaigllvgl aggafsvgtp
      121 yvarwfkpeq qgmamgvfga gnagssltkl vapgiiaaag wqmvptvyai imlvtailfw
      181 lfsyqdsahl vsskvslrqq lalmkdpavl rycqyysvvf ggyvglalwm tkyyvgeygf
      241 dikhaaflaa cfslpggvlr amggwlsdrf gphrvtwgvm wvcwvaffil sypqtdfvia
      301 tthgvqsfhl glnvtlftlv lfavgiamai gkasvfkfia nefpdnigav sgvvglaggm
      361 ggfllpilfg vllditgvrs safmllygtv cvslvwmhfs fkakvgneaa amarqar
//
LOCUS       WP_181836674             421 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Aquitalea
            aquatica].
ACCESSION   WP_181836674
VERSION     WP_181836674.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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 421)
  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 421)
  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 421)
  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..421
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..421
                     /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=47370
     Region          24..410
                     /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          178..414
                     /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(196..197,201,204..205,208,210..211,215,338..339,
                     376..378,380..384,395..398,403,406,410)
                     /site_type="other"
                     /note="putative alpha subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:176893"
     Site            order(205..206,208..209,211..212,216,308..309,311,319,321,
                     328,330,360,363..364,370..371,374)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176893"
     Site            order(205..206,208..209,211..212,216,308..309,311,319,321,
                     328,330,360,363..364,370..371)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176893"
     Site            order(211,216,374)
                     /site_type="other"
                     /note="Fe binding site [ion binding]"
                     /db_xref="CDD:176893"
ORIGIN      
        1 mqqsaitfqp vhklrelvar rqpghsleap fynsqevfea dlkyifqrhw iyvavaaeip
       61 epgdyvtvei gkepililrd ddmqikafhn vcrhrgsrlc adekgsvgnl vcpyhqwtyn
      121 lagklifadh mpegfdlthh slkpvhlknl egllfvclad eppadidqml eqmgpyiaph
      181 qientkvaaq idiieagnwk ltmennrecy hctgnhpelt islyaysygf apkaelaagl
      241 anyenivkds harweacglp saeieklsdv sgfrtmrmpl drkgqsqtmd tgaackkllg
      301 dikdadsggl sfwtqpnswh hfmadhivtf tvlplspdtt lvrtkwlvhk davegvdydv
      361 anltrvwnat ngqdrhlvee sqvgvnssay rpgpyspyte elvekftswy igrmeagleq
      421 g
//
LOCUS       WP_181836748             273 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Aquitalea aquatica].
ACCESSION   WP_181836748
VERSION     WP_181836748.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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 10616068
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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: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=30858
     Region          34..175
                     /region_name="Methyltransf_32"
                     /note="Methyltransferase domain; pfam13679"
                     /db_xref="CDD:379330"
ORIGIN      
        1 mslipeikpq qslellkelh iltrdgkinq dtrrklkqvy hlyqfiepll qdvldskgsv
       61 tladhgagks ylgfilydlf lkdkavgevf gietrpelvq ssqelaarlg fermgflnlt
      121 veqsitsdal paqvdiital hacntatdda irfalakdak yivlvpccqa evaavlrqkk
      181 netfgktpls elwrhpihtr efgsqltnvl rclqleargy qltvtelvgw ehsmknelii
      241 akktgkgkqs arerqeailr elnledlrer fvy
//
LOCUS       WP_181836202             400 aa            linear   BCT 28-DEC-2024
DEFINITION  nitrate/nitrite transporter [Aquitalea aquatica].
ACCESSION   WP_181836202
VERSION     WP_181836202.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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   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 400)
  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 400)
  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 400)
  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 400)
  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 400)
  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..400
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..400
                     /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=41531
     Region          14..383
                     /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..227,230,258,262,317,321,
                     336,339..340,343..344,347)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 mdrtfwqagh kptlfsafly fdlsfmvwyl lgplqvpiat alhlstqqrg lmvatpilag
       61 ailrllmgvl vdrigarrag iigqliviaa llgawqigia slggalllgl flgvagasfa
      121 vslplasrwy ppqhqgtamg iagagnsgtv laalfapala lafgwqnvfg laciplvaal
      181 fifvvcakda pnappakkla dylavlkekd awwfmffysm tfggfsgfas alpgyfhdqf
      241 afdaktagmy taacvfagsv mrplggmlad rlggtrslla vylccallig aagfnvggps
      301 valllfilam lclgagngav fqlvpqrfgk eigvmtglvg maggvggfal aaslgaikqa
      361 tggyaaglwl faclcclawl slagvkqrwr sgwtvaaarv
//
LOCUS       WP_181836446             255 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aquitalea aquatica].
ACCESSION   WP_181836446
VERSION     WP_181836446.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..255
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27932
     Region          23..241
                     /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 mrillllill svvlpasals ifteewppit fqrngvadgm avevvreiqa rihdntaiev
       61 vpwargyrel estpnvllft vgrsdareki mtllgpvavs qtvllsrkge asnllalgag
      121 lysrpvgayr gsifadaaas agfvevdlap tpqvsaqkll ggrydlwveg sfvvasvlks
      181 ihqpadavev vrvleslely lafsrgtssr tirrwyegma amkkdgsfrr iynkwlprdn
      241 aplemrqlgl tpqqp
//
LOCUS       WP_181836833             198 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Aquitalea aquatica].
ACCESSION   WP_181836833
VERSION     WP_181836833.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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=21494
     Region          6..198
                     /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 mtpsdtriyl asgsprrrel leqlgvhler ihadidesvq pgeaavayte rlarekaaag
       61 wavvqncglp srpllsadtt vvldgeiygk padaadaarm lrafsgrshq vvtsvavrqd
      121 erielrssit evyfralsed diqryidsge pfdkagaygi qglaavfiqr iegsytgvmg
      181 lpvfetatll slfghqfp
//
LOCUS       WP_181836870             701 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Aquitalea aquatica].
ACCESSION   WP_181836870
VERSION     WP_181836870.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 701)
  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 701)
  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..701
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..701
                     /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=77234
     Region          158..>374
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          292..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 mryaaialat fgaimlylla vatgnaskla eyywwvfgln sllllgllgv vgrqllrlrq
       61 rvkgrvfgak ltqrlvmmfa vvalvpgllv ftisaqfltr sieswfdvrv esaldrglel
      121 gkgalnyvle dvarksrvvl ddidglpgsm lpsrlerlre qlglrelaif nksgqllnfa
      181 snnahqlpqq pardilrglk lrqgsksien eagglalkvl lpyrtldgdw rvlqvvqtap
      241 qaiahdaeqi etaraeyhql llsrdglktf ymltlalacl laltsalafa lflserlsap
      301 lselaagtra vaqgdfskrh pvyrrdelgm lttlfnrmtq qleearqtan qnqralesgk
      361 lylesilanl sagvialdeg wqlraantsa grilgvdfae lvaypvkqws tqvpaliplv
      421 dtmlqhgenk leeewqtqld yvtgqgarsl lvrgarlper sgsgyvvvfd ditelgraqr
      481 daawgevakr laheirnplt piqlsaerla mkltakleaa dadmlkrstd tiikqvaalk
      541 nmvdafrdya rapriklsel dlnqvvreva tlyesnpavk ieledrplmi mgdaallrqv
      601 lhnlmqnaqd avldvdipmi hissrqegrn atvcvqdngs gfpaellpra fepyvtskpk
      661 gtglglavvk kiaeehhgqv ilgngeqqga rilltlplle a
//
LOCUS       WP_181836872             135 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Aquitalea aquatica].
ACCESSION   WP_181836872
VERSION     WP_181836872.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 135)
  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..135
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..135
                     /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=15118
     Region          1..135
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mshetrikvr gyhldlyghv nnarylefle earwsffedr gdlpwflqsg lalvvvnini
       61 dyrypatmgd elalatsvks igsrsavmhq rvtlagsdkv vaeadvtfvv fdakqnkavt
      121 ldgqlkellq smldq
//
LOCUS       WP_181836997             127 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Aquitalea aquatica].
ACCESSION   WP_181836997
VERSION     WP_181836997.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 127)
  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 127)
  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 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   4  (residues 1 to 127)
  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..127
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..127
                     /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=14819
     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 maehtfsise larefdvttr tirfyedqgl lepqragqrr iysrrdrvrl mlilrgkrig
       61 lslleirelf dlydaasnde pqlrefiril srkeqqlqeq lddirvvlge igqirsqcek
      121 algkqas
//
LOCUS       WP_181837043             117 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Aquitalea aquatica].
ACCESSION   WP_181837043
VERSION     WP_181837043.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 117)
  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 117)
  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 117)
  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 117)
  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..117
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..117
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12861
     Region          9..103
                     /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 mpasvplwlt ldefdfhhrl palpgntlvl fgqpgcaacr swrqalsqwq paalqqlayv
       61 dvqqcmalah qydifhlptl llfvdghyhg qlhsplqaqa idrtlaalla tpaaeep
//
LOCUS       WP_181836949             373 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Aquitalea aquatica].
ACCESSION   WP_181836949
VERSION     WP_181836949.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..373
                     /organism="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..373
                     /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=42004
     Region          3..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 mssskqhirf dfadglrgva ilcvilfhft qtfwqhreri sdilnmeple gyanasfvlp
       61 fnlgavgvgl fllisgllip lsltrmgglr favsrvfriy ptywaglavt lvalwiaawl
      121 adndfditrl dvighvsiaf qdmlggrnid pvmwtlkvel wfyallgtaf altgrrikwa
      181 iwlllplvam lcrgpsaqgl hgqlahfway dqyflasvvc yfplmfagcw cyfyltgqag
      241 kletvlhfvg llamfvwvtn wpslelygsy ligislfvlg vlrpalwssr wlariaavsy
      301 awyvchsnag yvlmevlamy nlpwwllvaa atvmtwtlal ainrwvelpt qklgkrvada
      361 lkdkpasdnl arq
//
LOCUS       WP_181837276             142 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Aquitalea aquatica].
ACCESSION   WP_181837276
VERSION     WP_181837276.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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=14928
     Region          <38..131
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mtsaiarlas hllylitynf ktaamttlsr qsthdatpsp aqlpaersgl fclpmpdqal
       61 agagieagcl levdgqgspv qgclvvaavd gellvrrlqr sgsrlqllaa hpdyplieps
      121 yeqdfaiwgv vaepaalatr qa
//
LOCUS       WP_181837559             551 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Aquitalea aquatica].
ACCESSION   WP_181837559
VERSION     WP_181837559.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     Protein         1..551
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61620
     Region          17..>256
                     /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 mltyspqnat vpvptekpwv llllcfvwlw pgiighdpwk pdepyvmavv egmlrsgnwl
       61 lptlqgvpyl espplyywva agfaklfspw llpahdaarl atplfmalgl tlagmtgrdl
      121 igrrygrsvv miligclgli vtghqmtpmv asftgfaaaf yalsltlrsp glagailgaa
      181 svtlflsasl levmlvwavv iflpaftawr nkryaitvfm allvalpval iwplqlersy
      241 palfrlwwer halgpldgfg kvslfhgfgy ytfntiwfaw pawplaawtl frnrkyelpm
      301 lqlplmffgv vlimltlser ksmdyampll lplsllaave ldnlrrgaaa flnwfglmtf
      361 gvfglliwag waamnygwpe rlagraqyfs pyyvphvsvl aavfavlati twiwavtrsh
      421 lrgrqaitnw aagltlcwgl alslwlpwld aaksyrpvve smvrampaag ldkaqciate
      481 nqnmvarisw hyyagidlla ypagesspcd yqllvrsrnd glaepgwtll wqgarprekf
      541 elfglfrran n
//
LOCUS       WP_181837548             486 aa            linear   BCT 28-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Aquitalea aquatica].
ACCESSION   WP_181837548
VERSION     WP_181837548.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea aquatica
  ORGANISM  Aquitalea aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
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="Aquitalea aquatica"
                     /db_xref="taxon:3044273"
     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=53954
     Region          3..486
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mspfssltfg qrllelppvf yrhiqpqpls epylvagnaq lcatlgitag elalpaslal
       61 lsgkqfvpdv salaalyagh qfgvyvpqlg dgralslgdt vdteghrwew qlkgagltpf
      121 srmgdgravl rstireylcs eamhglgipt tralamtgsp dpvyrerpet aavltrlaes
      181 firfgsfevf yhrgqhdeir qladfvirhh yphcaqtdqp yaalfadiva rtaqliahwq
      241 avgfchgvmn tdnmsilglt ldygpfgfmd gfnaahvcnh sdhagryayn qqpqvglwnl
      301 hclasaflpl vseeqlveal sgyreqysqy wlmlmrnklg lvveqegdea liealllamh
      361 ahhtdytvff rrladfdmag enhalrdmfl drslfdgwat ryaarlqlet rsaaerklam
      421 laanpkyilr nylaeqaiqa aqqgdfslia slhdclshpf deqpqyqafa geppgwaqei
      481 svscss
//
LOCUS       WP_181838085             281 aa            linear   BCT 28-DEC-2024
DEFINITION  PAS domain S-box protein, partial [Pseudomonas savastanoi].
ACCESSION   WP_181838085
VERSION     WP_181838085.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            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 :: TIGR00229.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..>281
                     /product="PAS domain S-box protein"
     Region          13..>259
                     /region_name="KinE"
                     /note="Sporulation sensor histidine kinase E [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5809"
                     /db_xref="CDD:444511"
ORIGIN      
        1 midtsdreas clsegkfasv faqcpdamii asladghimd anaafvertg ltldevigkt
       61 ptqldlwavp gigpkvlqql qtgnihnlei pfrrkngetf sglmsaqpfd qsstqavlvi
      121 vrditqrkqa qqqlqlseek fakafhaspd glaitrqqdg mllevnegfc ritgyseayc
      181 lehstfdlgv wvdlgdrsrl ieqlkrhgsv rdfrarlrnv dgsirlcels shpiviagdd
      241 clltiardit esrqmqeklh laatvfesta egvligsisf f
//
LOCUS       WP_181838189             419 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Pectobacterium].
ACCESSION   WP_181838189
VERSION     WP_181838189.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=47634
     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 maltdikvrs akpeekeysl tdgdgmfllv hpngskywrl rfrfggkqhl malgvypevs
       61 lsearqkrde arkqvaagid prehkkaika kqeedektfe vvarawhadn kkwseshger
      121 ilkslsdnif paignthiad lktrdllapi ksversgrle vakrlkqrvt aimtyavqng
      181 lidynpaqdm agaimpgkve hrpalalerl pellgridgy kgreftkwvi nlsllifirs
      241 selrfarwpe idferalwti pperepipgv kfsergskmh tphlvplsrq aleilkkire
      301 vsghcelvfi gdhssrkpvs egtvnkalqt mgydtktevc ghgfrtmacs sliesglwsr
      361 daverqmshq erngvraayi hkaehlderr lmlqwwadfl danrergvsp fdfgkltag
//
LOCUS       WP_181838346             358 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Pectobacterium aroidearum].
ACCESSION   WP_181838346
VERSION     WP_181838346.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..358
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..358
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=40624
     Region          12..341
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mqntvkinsa elvnadslqy iktlpdnyid aiitdppyyk vksndwdnqw sspvdflawl
       61 deflaefwrv lkpngslylf cgpklsadte ilmrdrfnvl nhivwakpsg rwngankesf
      121 rqffpasehi lfaehygsdg fakgntgyas kcrelksqvf aplieyfqsa rqrlgisake
      181 insatgtqmc shwfsnsqwq lpnaeqyaal qllfnrravg agragldsdh aslmreysgl
      241 saeysglvrq yddlrrefen lrrpfsvtks vphtnvwtyp pvqyypgkhp cekplsmmld
      301 iinastrpgd liadffvgsg avlkaaemlg rpsigvelee erflqtvhem rnlnpspr
//
LOCUS       WP_181838445             315 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nocardia africana].
ACCESSION   WP_181838445
VERSION     WP_181838445.1
KEYWORDS    RefSeq.
SOURCE      Nocardia africana
  ORGANISM  Nocardia africana
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..315
                     /organism="Nocardia africana"
                     /db_xref="taxon:134964"
     Protein         1..315
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32510
     Region          5..311
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpdgtpppdg wpliswahgt tgvadicaps rdtgpdypah dytaqvrevq qrwlaagyav
       61 aqtdyqglgt pgphgyliga tearavadma laareldasi gtrwaaighs qggqaaiftd
      121 aqarawapgl dlrgvvalap asqvefgiga qrlastvgag aaltgalgns naflpllirg
      181 aqtagnidps rfltpralsl lpeadtgclg alrapdswgg lpadaafspl gdatpllrvl
      241 tdndpstlri dvpllvaqgs ddttvpprat damvarlrla dqqvtyrtyp gadhrgilqa
      301 slpdalawid arfas
//
LOCUS       WP_181838530             256 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Thalassospira].
ACCESSION   WP_181838530
VERSION     WP_181838530.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
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="Thalassospira"
                     /db_xref="taxon:168934"
     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=29124
     Region          89..187
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mrlvvlwvvr llswlyriip gkvrggivfg llmmesriga paqslprlya ikdnlerlls
       61 eramayegge hpkhrlmmyh dffiknispn svvvdigcgy gavarsvaan vpgcrvigve
      121 mdearyeqav asrnpdnlhf vfgdafevlp eetadtvils nvlehiedrq gflrrivevl
      181 spsqilirvp aferewhvpm rkelgityfn drthfiehtv hefekemsda dieiaslgtt
      241 wgeiwavclp mvrkeh
//
LOCUS       WP_181838597             491 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat-containing sulfotransferase
            family protein [Thalassospira].
ACCESSION   WP_181838597
VERSION     WP_181838597.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 491)
  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 491)
  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 491)
  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 491)
  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 18649763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..491
                     /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=54660
     Region          <2..191
                     /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          239..424
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 metairrrlg tepgngilay mladaifqde likspgvcva prlaeaidal vlipaqsaqy
       61 ddaqillari hlhqeqhaqa fdvlekfvir ypdnlavqmm laasyaaane askavstcla
      121 iisvnpfysa qpyliisfmr pksmpegavg yldsmldkqd lanaerykaa fararieetk
      181 gnmkqafdfy klghaanrae rpfdivherk elarlrdmag etpvwdhaga gdengpqpif
      241 vvgmprsgtt lterilgahp dvyaageigd fakavidvvg vgpvseklar idrkaaarir
      301 kqyldalkay apekrfvtnk tpanfmriem irrvfpdapi ihthrhplat clsiyttpfs
      361 vpmrysddlg eladyyrgyv almkasfead drgqmydlsy edlvsdpetv aqdylahcgl
      421 dwhpgclefy rsdkaaatas miqvrrpinq dsvqkwqrfe pfigplvala ddaefrqwqa
      481 pvkssrrvva a
//
LOCUS       WP_181838782             286 aa            linear   BCT 28-DEC-2024
DEFINITION  glycerophosphodiester phosphodiesterase [Emticicia sp. BO119].
ACCESSION   WP_181838782
VERSION     WP_181838782.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 286)
  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..286
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..286
                     /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=32123
     Region          47..282
                     /region_name="UgpQ"
                     /note="Glycerophosphoryl diester phosphodiesterase [Lipid
                     transport and metabolism]; COG0584"
                     /db_xref="CDD:440349"
ORIGIN      
        1 mksltfllli sitiyasafi pnhtlnkskq tgadslkslk ekynlsisah rgssiiapen
       61 tlatfktvla mgvdyieidv rttkdgqlai lhdgslnrtt ngegpmknft laelkelsag
      121 kghhekfiae riptlqettr lvaewnkthk hqtnlyvdck dvapeplvre lkadkllkna
      181 vfygsdnfll alkkvypkak lmpslnkpqe iedkverlkp yafdvrwtil nkelvteihk
      241 hnikvfsdvl glldmpanyk kaaemgvdli qtdhvrkvyq tllegn
//
LOCUS       WP_181837835             400 aa            linear   BCT 28-DEC-2024
DEFINITION  alanyl-tRNA editing protein [Bacillus cereus].
ACCESSION   WP_181837835
VERSION     WP_181837835.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            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 cereus"
                     /db_xref="taxon:1396"
     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=44956
     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 mehklyytda ykqdfttkii kqdydkngnl yvvlnetafy ptgggqpydt gtlndinvin
       61 veeingeirh yiaeqlhted vegkinwerr fdhmqqhaaq hilsaafwdh fniptigfhl
      121 gketvtidle tenlhtetve kavqiankiv fenhpiriew mnleeaktlp lrkepnmten
      181 irvviienyd yngcggthpk rtgevgliqv lgwernkggi rltfiagwrt lklmgqqqqi
      241 mkdvskqlns setdipakva qlltsqkene ktiqtmnekl lfaeanellq qpteihagll
      301 iskaftdrsm qeiaklsaii teqqehaity fvienddklq cilacgktvt ldmnallkda
      361 lpaiegkggg nkkxargggk avmhgdefln qlvsslqsav
//
LOCUS       WP_181839219             104 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Emticicia sp.
            BO119].
ACCESSION   WP_181839219
VERSION     WP_181839219.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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   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 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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..104
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11622
     Region          4..101
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mttkkieent etcpaqtllk llsgkwkpei frlavvgplr fssllrqleg snkqtlaial
       61 keleeaglle kvtiklkplh ieyyltekgk tmipvfltle alvd
//
LOCUS       WP_181839362             372 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181839362
VERSION     WP_181839362.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..372
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41790
     Region          31..371
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msancqkydn sksinkdass vglslnidsg rvdkyilarm aqskipaisi givykgdliy
       61 anaygkanle hnialkpesp fklasltkpf tafailqlfe kgkikldeka sfylknlpik
      121 wetitvrqll shtsgladyf qspdwswqns wrldlshkef iamnekspii fspgermqyc
      181 ntnyyllgmi ievitgksyn qylkeeifep lgmshtqidk semlisdrvn gytlsdkkll
      241 naeytsntwa ysegglistv edlakfdkal yseallrket ikemwspskl kngkegvigd
      301 ngagnpnhyg lgwflsdykg hkltlaggnk pgftctyfhf edkslsiiil snlsssplyp
      361 mageiaemyl nw
//
LOCUS       WP_181839464             578 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Emticicia sp. BO119].
ACCESSION   WP_181839464
VERSION     WP_181839464.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 578)
  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 578)
  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..578
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..578
                     /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=65456
     Region          7..>215
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          146..574
                     /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 mkirtkltlg vgllfmlitl ltyvgaksin alkndtdnil vanyntleys rnilmaldel
       61 vtdksamnki eenllkqesn iteigereat qqlrqhftil kinnfdrtth fiirkdiaei
      121 mrlnmesiqr ksnvakqtaa satiwialsg tlcfviaftl linlpgnias pirkltesik
      181 riaandysqr vyfqdhsefg elarsfnrma ekleeynnsn lsqllfekrr ietlinnmhd
      241 pvigldenkk iifvnnqalk viglkpeqli nqqaqnvsli ndlirslvkd limpesivie
      301 dkkkpvkifa dnkesyfekd iidiafvptg ekelqhighv iilknitpfk eldfartnfi
      361 atishelktp issikmsiql lekqqtgtin eeqkqlidsi kedsqrllki tsellnlsqv
      421 etgniqlniq kstpyqilkf ateavkvqae qkqikilsei denlplvkad tektawvlin
      481 fltnainysp eqskiniris lqdqlvnfsv sdqgkgiekr ykdkifdkyf qvpgsvktgt
      541 glglaiskef ieaqngtigv eseigmgstf yfklgivs
//
LOCUS       WP_181839412             469 aa            linear   BCT 28-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Emticicia sp. BO119].
ACCESSION   WP_181839412
VERSION     WP_181839412.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..469
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55242
     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 mlfnslqfif ffivvtlayf slphrgriwl lllascyfya vfkpiyilil fvtivvdyfa
       61 giliadatgk krkwllilsl itnigflayf kyynflntnl aiilskfdtp tpfafldfal
      121 piglsfhtfq amsytievyr rnqkaekdfi iyalyvmfyp qlvagpierp qnllwqfhsy
      181 fkydfgnlke gliriawgmf kkvviadrla lmvdycydnp qdhngltlli gtifftfqiy
      241 cdfsgysdia igtarvmgfk lmenfdtpyf stsisefwrr whislsgwfr dylyipmggn
      301 rvgekrmyfn rffvfmmsgl whgaawtfvi wgalhglyli laqirdkyfk lktsilprfl
      361 skpinliftf ilvmltwvff rakgltnaki ilqkifsfgn ygntihspln nvemifcwll
      421 iaglllkekf ykiidttntp rfyllfivlm ivcyffgvfe snqfiyfqf
//
LOCUS       WP_181839505             163 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Emticicia sp. BO119].
ACCESSION   WP_181839505
VERSION     WP_181839505.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..163
                     /product="YybH family protein"
                     /calculated_mol_wt=18839
     Region          35..149
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mktllcailt csffitlaqs dnieteinnq vwlpfiktyn nfdaigfmnl hsrdlvrvpv
       61 dakkiytfee ysinnqqsne mslrnkrkqa iefsfedrih netsafetgy ykvtssdnqg
      121 ktrtfygkft vvlrkfgdrw kivldsdtgk nitesnflsg kkl
//
LOCUS       WP_181839233             512 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfatase family protein [Emticicia sp. BO119].
ACCESSION   WP_181839233
VERSION     WP_181839233.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 512)
  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..512
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..512
                     /product="sulfatase family protein"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56990
     Region          28..480
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16143"
                     /db_xref="CDD:293762"
     Site            order(36..37,75..76,129,131,273,325..326)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293762"
     Site            order(36..37,76,129,131,273,326)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293762"
ORIGIN      
        1 mkfkllills flflngsfik keplpqkpni iiiyaddlgy gdvsayekgi lqtpnmdkma
       61 kngirftngh atsatctpsr yglltgiypw rkegarvlpg dapllidtsl vtipkmlkka
      121 gyqtgivgkw hlgigkgeid wnkdlllnpn dvgfdysyim aattdrvptv fienrrvvgl
      181 eindpllvny nknfegepta lsnpelmtkq kwdhghnmsm hngiprigfq kggksalwhd
      241 edmadiflkq sldfihihkn kpfflyyglh qphvprsphp rfagksglgv rgdvileadw
      301 cvgeimkkle etgldkntlv ilssdngpvl ndgyidgave mngqhtpsgg lrggkyslye
      361 agtrvpfias wkgvirpqvs dalvcqidfl asfaqltgqk npsadsqnll nvflgkskkg
      421 rknlvleasn rlafkkgdwv lipphkgssi akevnielgn slqyqlfnlk sdnaeqnnla
      481 kvnprkleem keamkqivdn rynfdakele lk
//
LOCUS       WP_181839513             201 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Emticicia sp. BO119].
ACCESSION   WP_181839513
VERSION     WP_181839513.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..201
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..201
                     /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=22366
     Region          1..>87
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 maapkparks psmdmtamcd vafllltffi mttqfksqes vtvdtpssvs eikvedkdma
       61 titidkdgky yfgvtnpldr ysliqkmndk ygaglsdaeq knftklaetg vsitslkqyl
      121 alpeaqrgqv riqgipndst kselvdwvkt yltdinkkak lavrgdvqtq ypaikklfae
      181 lgkndinkfq litdsenked k
//
LOCUS       WP_181839514             183 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Emticicia sp. BO119].
ACCESSION   WP_181839514
VERSION     WP_181839514.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..183
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..183
                     /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=20240
     Region          19..170
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 maeiqesggg gkkgggkvrs kkaggkpdmt pmvdlgflli tffmytttfg kpnmmklnmp
       61 dkpnpddppp pevkvtntit vlmgkddrif wyqkplpelt ladlnetdys pegirksvlv
      121 kkanaldink ftviikpsde anwkntvdil demaitksdr yaivdlapke kelldqklae
      181 pkk
//
LOCUS       WP_181839517             575 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Emticicia sp. BO119].
ACCESSION   WP_181839517
VERSION     WP_181839517.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 575)
  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 575)
  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 18646610
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..575
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=63248
     Region          <126..333
                     /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          128..161
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          166..>545
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          169..197
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(170,173..174,177..178,180,204,207..208,211..212,
                     214..215,238,241..242,245..246,249)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          202..232
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          271..295
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnkilrslsv savavlaltf htlaqtvqdg lrnldaeryn aagtifnqlv tsapteenyf
       61 yqgyyylnlp epdlakanea ftkgttlskr pdplnrvgla avkllsgdka gakvdfddir
      121 kdtknknpev lfrigeayai senpklndpa eavmniqagl dvlkvknnpd yyialakayl
      181 lkndggsamt alenalnmgq ktavirtlmg rvwfqgksyp kaqqdlnesi kadpehapay
      241 yylsgifqvf gkfdlaakna klylekseat deaklryvkl aftskdydga tevlnsifdk
      301 iqdpvkyrlr gytqiekgec aegvknvqef lkkapedrhl asdygtigrg yicinddvnk
      361 avndsigity mekavslgdt ttdyttdivn vykaakrwdk lattyeqsia kegakadgad
      421 yynladayir skdyikadsa lsttivlykd twltpyilka rvkqyadpnd stfsaapiye
      481 kyislvpead kakdltkkyl aeaygylgik allldkdtak akeymnlvlt ydpnnqqatk
      541 vlesingtst tttpngsgtp pannnpsgss ggpkg
//
LOCUS       WP_181839702             161 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Emticicia sp. BO119].
ACCESSION   WP_181839702
VERSION     WP_181839702.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..161
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..161
                     /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=18481
     Region          7..135
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 maeittnsrv arvdmtpmvd lgfllitffm fttvfskpfi mklnmpdkng kppimkesnt
       61 ltlilgkddk ifwhqknada lnisllsein yglelrklif qkrkeakiie nftviikpsd
      121 dsnyknmvda ldemkitnqd iymladitpk ekqvyeakik p
//
LOCUS       WP_181839824             142 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Emticicia sp. BO119].
ACCESSION   WP_181839824
VERSION     WP_181839824.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 142)
  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 142)
  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 142)
  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 19109204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..142
                     /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=16819
     Region          3..>104
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd18882"
                     /db_xref="CDD:467593"
ORIGIN      
        1 mffvatgllf dknnrlliyl rddkptisfp nhwdlfggii eegespeyal vrevkeeigi
       61 dlisyykfre yysdsedrpn wkyvffakid ylpeelilne gqrltsinlk erfnykfani
      121 lgriiddfan selycnyilk ka
//
LOCUS       WP_181839866             269 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Emticicia sp. BO119].
ACCESSION   WP_181839866
VERSION     WP_181839866.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=30980
     Region          37..250
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mqrrdflknv slatilladg siipalsaes fakrnrlrfv vasdghygqd ktafqqyfdt
       61 avnqinlqhk kgkldlcifn gdvihdnpsf lraskqaldk lempyyvtqg nhdrvtpeiw
      121 eqtwkmpldy dvvmkdnafl fgttsnikge ylcpnvswfr nkleehknkk nvfifvhitp
      181 vkwtengvdc vefqelmkqy knvrgvfngh dhdqegvkik dgipylfdsh iggswgtayr
      241 gfrivelkrn ndiltylmnp iekineati
//
LOCUS       WP_181839880             320 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181839880
VERSION     WP_181839880.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 320)
  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 320)
  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..320
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..320
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=36095
     Region          <46..276
                     /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 mnwikpltiv eyvfigifll vyiiyfvrty iiakrlgtta rsvvikffir taylglfiig
       61 llgpsfgvse ieaqasgkdi yfafdvsrsm daidieptrl ekvkfeiikn lnvlksdrvg
      121 ivvfssnayv hipltydkda lklfvqklss dlfiesgtdl nsalkliqtk fnsanvpnrk
      181 vkviimvsdg edfgqlepev iqdlrinrvn flalgvgtpt ggkiregssf kqdkdgveii
      241 skldadylkq lskvlngkyl qlsnqindvs amlkevsqle nnwidtrkmt vannkyfyfv
      301 flgfilmiid vlitirtikl
//
LOCUS       WP_181839927             417 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Emticicia sp. BO119].
ACCESSION   WP_181839927
VERSION     WP_181839927.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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..417
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..417
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45921
     Region          2..405
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mknwkiklsl ylnyfvfail lnsvgiliqk sinsyhvdei aassleafkd lsiafvsffv
       61 gsflprlgyk kgmlialgtv figcvvmyfg nsftavrilf acvgisfavi kvsvyslvgl
      121 lasndkehks ilssiesffm vgiavafvsf plfysdidpn awlrvylvva llvlisfvfl
      181 lfsdfdaldy evpgsnigdd fkqmisllkr plvlvfaiaa fmyvmteqgi mswlptfnek
      241 vlhlpertsv fmavilmlsi aggrfvssil ikkiywltil lvcligaalm vilvlpqtng
      301 levkeinslg dlpiiayvfp ligfflaply plvnsivlsa tekifhspma slltffsaig
      361 gtlgsrlvgy lfkniggdka fyfslipmgi liiclfllns iqkksgknie fntsggh
//
LOCUS       WP_181839931             405 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181839931
VERSION     WP_181839931.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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..405
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..405
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46067
     Region          117..403
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkyliltfif lvkiqvnaqk kaieqyfpty newqqkkpfd lglngtkiee aisfaianes
       61 rnprnmevsh yqsfgkepfg igigpfterg eptgliiykg yiiaqwgepe rcdmthsvtk
      121 sflssvvgia ldrgliksvn dtvanyvppi elhgepvnrs addfgkpell qlfntphnkt
      181 itwdallrqt sdwegtlwgk pdwadrpdkd asqwlnrprh kqgevyeynd vrvnvlslaa
      241 lsvwrkplpq vlrenlmdki gasntwrwtg yrnswivldg qaiqsvsggg hwgggmfina
      301 ydmarfgllt lnrgkwkeeq ilsedwirka ltptssepty gymnwflntd kklfpsanvs
      361 afchigngtn mvfvdpdhdl vivsrwinnn ntdglvkkvf eafnk
//
LOCUS       WP_181839841             426 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydroorotase [Emticicia sp. BO119].
ACCESSION   WP_181839841
VERSION     WP_181839841.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 426)
  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 426)
  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..426
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..426
                     /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=47063
     Region          4..426
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
ORIGIN      
        1 mktllksvki idrksdfngq ikdiliiegk iskiadkied egvkviegan lhvstgwidm
       61 rvspkdpgye skedltslcr aaaaggftki vtlpntrptv qtkesiayyk gfsktqvvdi
      121 lpaaaitknc egkdftemld lhnagaiaft dgehplwnad illktlqyly pingflmnrp
      181 eettltlfgq mhegiestll gmkgipstae elivmrdlkl leyafsqvse tgknavlhfs
      241 tistkravel ireakvrglp vscdiaahql aftdadlkef dtnlkvnppf reindiealq
      301 egladgtidv ivsdhnpqde esknlefdma dfgiiglets fgvantyskl svealvdklt
      361 inpakllrls eetikegeia nitifnpdle wtfmekdirs kakntpfvgr klrgkvigii
      421 nknqfa
//
LOCUS       WP_181840202             320 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181840202
VERSION     WP_181840202.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..320
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..320
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=36094
     Region          38..>218
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 meiteekmas nsnqgifkvs fgvligilal lgylfmgarn dtfelqkslt ekveqlsstq
       61 ikldsiskvl dekiakinrl ggnivelkri kaqlendkkl lksdlnfslq kyntkirdye
      121 nfltvkdkef nllkeentel kartelleqe kqevlnents lktdketlsq tvaeysaeny
      181 nlqrqvtmas smkainvqva alsangkare gntfkasrin rlkisfimps npiavknkkd
      241 iylrildang giitdnvnsg vleyegneig fstrqgvlfe nndqkvdiiy vqdapytpgk
      301 yeieiycegf kigkgrfevk
//
LOCUS       WP_181840032             503 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfatase family protein [Emticicia sp. BO119].
ACCESSION   WP_181840032
VERSION     WP_181840032.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..503
                     /product="sulfatase family protein"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55863
     Region          24..458
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16143"
                     /db_xref="CDD:293762"
     Site            order(32..33,72..73,127,129,245,297..298)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293762"
     Site            order(32..33,73,127,129,245,298)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293762"
ORIGIN      
        1 mkkkyilsil iccnilsvgf aqkpnivyil addlgigdvs synpngkiqt enidklaqng
       61 vrftdahtts avctptrysi mtgrynwrtt mkkgvlhgyd tplidakret vgsflqkqgy
      121 ktgvvgkwhl gwtwnnieag ekkvdfskkv adnpnsrgfd ysfcipasld mppyayveng
      181 fctsvpkdtc egrkgielfr agisapdfkp edvigkftek alsfinqnan kdkpfflyfp
      241 laaphtpvlp igdfvgkskv spygdfvlmv ddvvkqvvat lkkngiydnt iiiftsdngf
      301 ansanlqaql akghnpsidy rglktdifeg ghrvpfivhw gnvikkgkvs eqlvcssdlf
      361 rtvaelnkar lgdnvaedsy sflseitdkk sgyeqrasii hhssngyfai rkgpwklimc
      421 shsggnskpk edseeakklp piqlynlktd ldetnnvyaq ypeivkelta lltkhvqdgr
      481 stkgqnqtnd gpthwsqlnw lgk
//
LOCUS       WP_181840174             267 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Emticicia sp. BO119].
ACCESSION   WP_181840174
VERSION     WP_181840174.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=29592
     Region          1..238
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mrpnrlkqlw kedktvvnaw vtipsswtae vvahsgfdam tidaqhglas dhmtiltmlq
       61 aisttdtvpl vrvqwnepat hmkmldmgay giicpmintr eesesfvgac ryipdgyrsf
      121 gpvrasvygg dgyfekstee ivtmsmieta eglknvedia ktstmtglyv gpwdlsismr
      181 rprqgdfddt ellkafdkvl nacarnnlia giqcpspeia irmsemgfrf vtaandttll
      241 kqgavdtikr fyhkstgetr nvsnpya
//
LOCUS       WP_181840208             242 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181840208
VERSION     WP_181840208.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=28261
     Region          4..237
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkdkltcyii ddeplaqeil eeyiskvsfl elkgsfmspl eaagslekdq pdilfldinm
       61 pdldglsfmq mlnrkpmiil ttaydqyalk afeldvkdyl lkpfsferfy kgvlrlyqeq
      121 nsrqqpekna tipevkteqe yiflkvghri rkvairdilf aegmkdylri htteekimtl
      181 lsfakleell pstdfarvhr sfliaidkid hieknriwlg dqiipisdty sesffkmlrg
      241 iq
//
LOCUS       WP_181840251             103 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Emticicia sp. BO119].
ACCESSION   WP_181840251
VERSION     WP_181840251.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=11817
     Region          4..84
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mrrdvfqaia dptrrniigl ianqsmnlna vaeqfdisrp aiskhikilt ecglivirqe
       61 greryceakl dklnevsawa dqyrkfwtsk ldaldnflkn qhs
//
LOCUS       WP_181840264             382 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181840264
VERSION     WP_181840264.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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..382
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..382
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43192
     Region          72..355
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mfkklvialt aitfllfgll flppfehirn ylswgkhsif dfrthptrlv engnapqfwp
       61 idsaynkrqi pdallaqids nnthafliiq ngrllyeqyw dgytkdsisg sfsaaksiis
      121 mligiglgeg kiksldepvg nyvthfkegd lskvrikdll tmssgsnyke sdqsylglsa
      181 kmyyaddeay vvnlmrkkev pginweyrsg dtqvlglile kafgknisal tseyfmkpmg
      241 aekdalwlld gekkhekafc cfngvardya rfgelmltdg kwkneqivpe tfmkaaltpa
      301 sylkdptegg kpvdyygyqf wivnhkgmai psmnglfgqy vfaikeknai ivrlgetkvv
      361 kpihhfqpen ytyidaalsi le
//
LOCUS       WP_181840390             104 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181840390
VERSION     WP_181840390.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 104)
  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 104)
  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 104)
  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 104)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 104)
  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 104)
  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 104)
  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..104
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..104
                     /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=12306
     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 meflyitkkv qvlidniryl qadinyttiy tcqeesiist ttikrlndki esgnfirinr
       61 kiivnkefik aynywsnkvi ldngetfiis rrknralrnv lelq
//
LOCUS       WP_181839130             110 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181839130
VERSION     WP_181839130.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 110)
  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 110)
  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 110)
  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 110)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 110)
  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 110)
  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 110)
  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..110
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..110
                     /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=12628
     Region          <18..106
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkknllnpiv flnqktavni nevlflegnv nytiihlegk hpitiastlk kiesklkgyn
       61 flrihkrfll nmtfadrsll snnrllikkn iaitvsrrkr selkdwltaa
//
LOCUS       WP_181840406            1028 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            BO119].
ACCESSION   WP_181840406
VERSION     WP_181840406.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1028)
  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 1028)
  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 1028)
  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 1028)
  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..1028
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..1028
                     /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=113161
     Region          39..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkiyhysk llllvavfis aysqnghaqn sdsrqpvsit gkvtdtkske givgatvaik
       61 gtttgvltdv ngnfdfktsq kppftvvvsy lgyrrqevev feiepltfal seikglklde
      121 vvvigystqe rknlvgsvtk idpgdvknip vasvdaqlqg kaagvqinan tgipgeaisv
      181 rvrgttsing snaplyivdg vfinatslqt inmggtstsp ladinpsdie sievlkdana
      241 taiygsrgan gvviittkrg eyntkakinl nvtqgfseiq ksrlwklvtg pesaafvnea
      301 winagidnpa lkqtfanrpy rpkseggrgl peeqgtfdrl sdvfrvaslk eydlslqggt
      361 kttkyyiggn ytkqeatvrp vyferssfkl nldqqvndqi tigtsnsisr syrnqlisgs
      421 tprgifqsal ltatnlpkyn ddgtpalwgg fdnvdvlvnn nfintvslry ignlyadidl
      481 lpnlkfrtsw svdynnyden eywtdetvvg aaptngrars sltqnsawvn eqtlsyrkkf
      541 dkhsfsalvg ntlqsnilkn taaegsnfpn nsyqiissas ifnasqswtk gslasffsrv
      601 dynynskylf eftfradgss rfggnnkwgy fpsvggawrv keedflknvs fisdlklras
      661 vgvtgnqsgi gdfaslglwn ggpgypdnes sgvrpgtspq qlanpdlvwe ktrqanigle
      721 agfldnrinv elnfydkytt dvllqlplpg tsgftsyasn vgkisnkgfe lsintfniqr
      781 drfkwqtnln vatnvnkive lpnpinsgfi tleqgypmfs fqvykqlyvd aqtgnavyed
      841 vnkdgqitva drqilgtftp kffggltnal sykdfdlnvl ftfqqgnylf nenrnygesg
      901 gtradrsyhl tqanrwqkpg ditdipritt vgtnynlspn sryledasfi rlknlslgyt
      961 ipvqttsklk iskarlfvng snlwlltkyt gpdpeayvps sgnqnavgrd fcippqpqsv
     1021 qfginltf
//
LOCUS       WP_181840510             325 aa            linear   BCT 28-DEC-2024
DEFINITION  COX15/CtaA family protein [Emticicia sp. BO119].
ACCESSION   WP_181840510
VERSION     WP_181840510.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..325
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..325
                     /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=36450
     Region          4..312
                     /region_name="CtaA"
                     /note="Heme A synthase [Coenzyme transport and
                     metabolism]; COG1612"
                     /db_xref="CDD:441220"
ORIGIN      
        1 mvvfrklgvw tigavyvlil vggivratgs gmgcpdwpkc fgswvpptdi sqlpinykei
       61 fgaklkgeve fnaiktwtey inrlvgvlig ffvfatfits irsfwnkdrt ivwlsflafi
      121 lvgfegwlgs kvvsselhpv mitlhmllsv iivfillyav arsytrviev edikesssis
      181 flltalilvt lgqvllgtqv remvdhvanm lgeqaraewa inlggkfemh rwfsfivlgl
      241 hilflyrilk snsqkgliyq fsigliilia iemvtglilg ylglpayaqp ihltiailml
      301 gvqfilylll nkervfrgvp eftlk
//
LOCUS       WP_181840506             204 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Emticicia sp. BO119].
ACCESSION   WP_181840506
VERSION     WP_181840506.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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 204)
  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 204)
  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 204)
  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 204)
  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..204
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..204
                     /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=22663
     Region          32..201
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkfsvrnitl avavatfsav vlsschdnns tgwefapnmy nsrayepltq wrentinpdg
       61 knmrqpvpgt iartnyhtsf lqddstvind lmvynlpads iavaeatlkn pipwsdaaet
      121 egqalyernc ahchgekgag dgpvgkvykg vpnyaseayk nmndghifhv itygkgrmwp
      181 hasqvnpeer wkivhyvhrl qlgn
//
LOCUS       WP_181840588             666 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Emticicia sp.
            BO119].
ACCESSION   WP_181840588
VERSION     WP_181840588.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 666)
  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 666)
  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..666
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..666
                     /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=74472
     Region          412..665
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkklslsiaf cltfifatqa qkwepissat gklpltwktt qqtaslvvdi dndgieeiil
       61 gcrekgpali yfkyessigw rvftiekefl tieaggafyd idgdgdkdiv fggdwqsnkl
      121 wwwenpypfy npnvqwkrhe ikadgatqhh dqafgdfkqt graqlafwnq gaktlyiadv
      181 peeafrggkw dytpvfvage kekkawyaeg ctaadvdgdg ftdliagnhw fkyvdgkfka
      241 iqfgeeggrv vaakfrpgkk rqivvspgdg tgrllyyect gsaevtanwk akdligreli
      301 hghtleaadi dddgnldifc aemakwsekk tepdnpnaea filygdgkgg frkttfqkgv
      361 dfhegrvyda dgdgdidivs kpynwnaprl dmwlqngtgk klpnisrald gkiglelysl
      421 rdyfktdvvg tldyvkslgi kevevagtys mkpedfrkel dnrgitpyst lldfglfrds
      481 lskviaiakg lgvtyvgtaw iphkpnqfsk tdadkaiaif nkagaelaka glhffyhchg
      541 yefkpseegt lfdyivqktd aqnvsfecdv ywafhggqdp alllkkhkgr fiaihikdmk
      601 pgqetgefsg gtpltsdvav gtgqlnfpei lraaiqsgvk yyyiedenae vkqhlpfslr
      661 ylknlk
//
LOCUS       WP_181840670             245 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Emticicia sp. BO119].
ACCESSION   WP_181840670
VERSION     WP_181840670.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=26703
     Region          1..244
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mniygligyp lghsfskkyf tekfgqmgia dtnayelfel pdiqalpqli esqpnlkgln
       61 vtiphkqavm pfldgldasa ekvgavnvik igeggkligy nsdyygfkts leefipanss
      121 lkalvlgngg aakavvaaln dlaiafkivs riksegtlgy edlaieigny qliinsspvg
      181 typksdvcpd ipyeqltpdh ylydlvynpv qtlflqkgde qgakthnglk mlhlqaekaw
      241 eiwns
//
LOCUS       WP_181840672             105 aa            linear   BCT 28-DEC-2024
DEFINITION  (2Fe-2S) ferredoxin domain-containing protein [Emticicia sp.
            BO119].
ACCESSION   WP_181840672
VERSION     WP_181840672.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 105)
  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 105)
  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..105
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..105
                     /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=11594
     Region          1..102
                     /region_name="COG3411"
                     /note="2Fe-2S ferredoxin [Energy production and
                     conversion]"
                     /db_xref="CDD:442637"
ORIGIN      
        1 mkfkkhvfic tndkeapkks cgsvhgmelv eafkasikek glqldiraqk sgcldicafg
       61 psmvvypegv wygnvqlsdv eeiveshlvn nepvdrltlk fparv
//
LOCUS       WP_181840764             354 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181840764
VERSION     WP_181840764.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..354
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40391
     Region          89..315
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkqtkvmil iallasaaai vscspkfwns anktyqplpa ithpenpeki yqayqflkdk
       61 teydafiavk ndsllaswgd ihlpimthsa rksimsvlyg iaidkgliql nqtlaelkid
      121 dikapltaie ktctvrdllm srsgiyieaa getkemkaar pqrgmhkpge ffyynnwgfn
      181 vlgtifeqqt hlsigeaiee wlakplgmkk fkadyviyrq pdysehkqyi ifmtaedlar
      241 igilmlndgk wkgktivsak wvadstypys edrnnepfdh yaylwlndtd egtfwasgwg
      301 gqfmivdrkn rlvvvsrndt grallqqglf mwrgkqasrq hhqdlhhlmi eacl
//
LOCUS       WP_181840731             184 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Emticicia sp. BO119].
ACCESSION   WP_181840731
VERSION     WP_181840731.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 184)
  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 184)
  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 184)
  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 184)
  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 184)
  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..184
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..184
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21055
     Region          1..160
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mkkifllial ltgtfttfaq qanssaqtke iqwislqeay artqkeprkt ivdvytawcg
       61 wckvmdkqty tnpdvidyln knyymvklda etrqeivvgg vkymfdeknn tnqaaiallq
      121 gklsypttvf ldaqynmiqp lpgyldakaf hqvitfiggd nykkesfdqy kegtyketfk
      181 gtkl
//
LOCUS       WP_181840827             330 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Emticicia sp. BO119].
ACCESSION   WP_181840827
VERSION     WP_181840827.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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 330)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..330
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36490
     Region          47..>167
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
     Region          66..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 mnqtlsiisa tlltffilsc ekelsinddg nlvpktvdqd aslpsitvnn tqlhaetfgn
       61 panrmlvilh ggpgsdyryl lnckafanqg yyvvfydqrg sglskrhpks iysiqimldd
      121 lsaviahykt sasqrvfllg hswgamlata yinaypksis gailaepggf iwqdvldyvg
      181 rsrsfrltse tlndatyldq fitgkqneqa ildykfslma sadesaessl gndgplpfwr
      241 sgaviqealf evgnkekpdw ttnlnlytnk ilfiysernk syglahaqkv ssaypniqle
      301 kiigaghdmi sfptgwstfy pkalnylnal
//
LOCUS       WP_181840920             387 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Emticicia sp. BO119].
ACCESSION   WP_181840920
VERSION     WP_181840920.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 387)
  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 387)
  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 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   4  (residues 1 to 387)
  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..387
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..387
                     /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=43201
     Region          1..382
                     /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 makllivdde ksirdalrdi leyeeyevde akdgeeglem vlkthydval cdikmpkldg
       61 lemllkakee gvmtqfvmis afgnvenave atkrgafdfi tkppdlnrll vtvrnaieks
      121 kdveviktlk rriykineiv gesdlikkvk dtidrvapte arvlitgpng sgkemvakqi
      181 heksnrcnqp svevncaaip selieselfg hekgaftsai kqrigkfeqa dggtlfldei
      241 gdmslsaqak vlralqeski trvggdkeik vnvrviaatn kdlkkeiaeg nfredlyhrl
      301 nvipihvpal tdrktdipll adkflhdvad eygdavkefe pdameymksl pwtgnvrelr
      361 nvverlvimc gptitlddvk lyagigf
//
LOCUS       WP_181840937             290 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Emticicia sp. BO119].
ACCESSION   WP_181840937
VERSION     WP_181840937.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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..290
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..290
                     /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=32674
     Region          14..>130
                     /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          <86..>240
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
ORIGIN      
        1 mkriltflyl llpfisvaqg gteiylfdlk fsnnqfslsn pvnitmhkgy dsqpffhpqy
       61 pivyyasand sgrtdikayd yskyftrqit ntsereyspt vtpdgynlsc iiqrdngqqd
      121 lgqymitggn spakvlidnl kvgyhtwida nslllfvlad stnnlheynl atsettiiar
      181 kpgrslhkip nqqafsfidk ssadqwvikq fdpatkaisp iintfgksed icwttngyil
      241 tsdgeklyac kpqsgkawqq vdtkdlpmlk kitrmavnke tnrlavvvse
//
LOCUS       WP_181840967             349 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Emticicia sp.
            BO119].
ACCESSION   WP_181840967
VERSION     WP_181840967.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 349)
  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 349)
  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..349
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..349
                     /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=38316
     Region          145..348
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 meksnnpsvs rrqflgtaat lvsgsvlasn avfgapayik nlfgpnslin gvqigaitys
       61 frempdqsae avlqyvlesg isaiellgdh aeiyagkpks yvdmrsvfpl mrkrnekqel
      121 teeekkkled aeaqmkaynt evakwregas mgkfeelgka ykkagisiya fkpnafgrnn
      181 sdaeiiygmk aakalganqv tvehpsndeh tlklgtmaqk mgikmgyhgh eqqtftlwdt
      241 alaqspansl nldlghfvaa gnanpldiik qkhdrivsmh ikdrqtpahg kgnvvwgqgd
      301 tpirealnlm kdnkykfpat ieleykipeg snsvaevkkc lefcknsls
//
LOCUS       WP_181840965             269 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181840965
VERSION     WP_181840965.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=31024
     Region          <183..265
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkyletgqfh gqtnriigle gitltdteyt ldkvdwhyhe nayftfilqg rviegnkkev
       61 yncgagsllf hnwqephyni kppgytrgfh ielnhewlet tgteidkltg sicisnpelk
      121 lllyrifres ktndmttgla vqslllqlls qmerdsqkei nknpawvqhl kellhdsftd
      181 hwslselsae lgihpvhlsr dfsryfhcni geyirrlkie kslsllaqkn ksladiafec
      241 gfadqshfar cfkalngina sehrkivmn
//
LOCUS       WP_181840981             232 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181840981
VERSION     WP_181840981.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=26841
     Region          2..226
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkfsclivdd eplavalmen hvrqvpflil agkcfnamea iafleknevd lifldiempy
       61 ltgmqlksfl pekqkviftt aysefaiesy eknafdyllk pitferflks vkrlqgsesv
      121 kpvmsnstda hifvksgrei ikleyddilf ieglkdyvsl vtetdkvity klmreleesl
      181 panfarvhls yiincnkirk isdnqviiqe ksipisekyr erflqkvsdr ml
//
LOCUS       WP_181841007             439 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Emticicia sp. BO119].
ACCESSION   WP_181841007
VERSION     WP_181841007.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 439)
  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 439)
  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..439
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..439
                     /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=50475
     Region          23..426
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mikklylllt illisvlsls aqiqsgpmlg ysemrevmlw vqtkkeasvk fvywdkekpt
       61 ikystnevkt nktdafvarl vadevlpgkk ygyevwvdkk kvaisyplef qtqtlwqwrt
      121 dppafkfavg scayinedgf drpgtpygse yeiftsiyqs kpdfmlwggd nlylrevdwn
      181 tktgilkryt htrslpemqp llgsvhnyai wddhdfgpnd adrgfvskkq tldafklfwg
      241 nlnytfndeg vtgsfqwadc qfflmddrww rtpndritga reyfgqkqiq wlidalkfsn
      301 apfkfvvvgg qvgnpakife nfanyeeern qlfdliarek ipgvifisgd rhwtslckie
      361 rpgtyplydl tvsaltsgas kpvkeeadtp yvegtsvtrh nfglleisgp rtnrvlkini
      421 ldkdgkelwt keikaselk
//
LOCUS       WP_181841053             122 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181841053
VERSION     WP_181841053.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 122)
  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 122)
  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 122)
  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 122)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 122)
  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 122)
  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 122)
  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..122
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..122
                     /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=14353
     Region          <8..113
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mktktdvtpe psvlwfnhkk kcvrtddvvy lksfdnytrf ylsngrqfls shtmkiyeqq
       61 lqskgdftrv hrgtllnlky ltkfeknteg nwaclstgek ifvsrrkikk feehtssnfs
      121 en
//
LOCUS       WP_181841021             352 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Emticicia sp. BO119].
ACCESSION   WP_181841021
VERSION     WP_181841021.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..352
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..352
                     /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=40834
     Region          2..327
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mqqfdyiivg qgiagsllgy qllkadrrvl ilndesipts savaggifnp itgknldktw
       61 ladsifpyfk dfylslenet hchfyhetnl yrpyaneqqr rhflqltdey dldtyirlvk
      121 pdaykevenh lgglfttsag wvdvplmigv lrklfiqsna yhnerfdyqa leiseekviy
      181 knfqaskiif cegyyasqnp yfnwlpfnpa kgetliatmq tysikeivnq gawiiplgnq
      241 qyrfgstyvw nqldwqttke sketitskid kflktpyqit eqqagirptt kdrrpfmgnh
      301 paypnvyvfn glgtkgvsla pyfaehmlyf lekekdlmpe sniqrfysly sl
//
LOCUS       WP_181841088             350 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Emticicia sp.
            BO119].
ACCESSION   WP_181841088
VERSION     WP_181841088.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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..350
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..350
                     /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=38970
     Region          8..323
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mktikgpaif laqfmgdeap fnsldtiady maglgykgiq lptwdgrvid lqkaaeskty
       61 adelkgklad kglaitelst hlqgqliash paynamydaf apasvhgnek arrkwaeqql
      121 iwaakasqnl gltshvgfsg alawpflypw pqrpagliet afkelarrwk pilnvfdehg
      181 vdycyelhpg edlfdgstfe mfvdylkghk rvcinydpsh fvlqqldyla fidlyhdrik
      241 afhvkdaefn psgrqgvysg yagwadragr frslgdgqvd fsgifsklsq ynydswavle
      301 wecciksseq gaaegapfie shiiqvatra fddfaatgad ekvnrkalgi
//
LOCUS       WP_181841104             263 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181841104
VERSION     WP_181841104.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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]"
                     /calculated_mol_wt=30617
     Region          <178..258
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqatkisscy lgpqispeef vtehfflylv kgrmngydgn kyatleagec clvrknhlar
       61 ynkqkqdnaf ekvvvifded flkrcqekyq faiiksdkgd aflrlkddal ipnflqslap
      121 yyngngqidp lfadikreel llillktnpe lytilfdfte pskinleefm nrnfrfnvsl
      181 erfaymtgrs lstfkrdfek ifsdtpshwl mqkrlheayf llektgkkvs dtylevgfed
      241 lshfsfvfkk qfgvapsevl gkv
//
LOCUS       WP_181841092             240 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181841092
VERSION     WP_181841092.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=27669
     Region          2..235
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mkirclvidd eymarlllen yiqklpqlel vslcenaiea msmlqkekie vifldiqmsh
       61 ltgleflhtl qqkpvviftt ayseyalegf rldavdyllk pfsferfvqa vnkaahylsf
      121 qannkesast piesnetrql fvksdgklvk vrfdeilyie glkeyvsiyt phnriitlqs
      181 lrnletllpr stflrvhksy iialdkiqai vgnqveihkk lipigatyke ilmnalqlee
//
LOCUS       WP_181841219             457 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Emticicia sp. BO119].
ACCESSION   WP_181841219
VERSION     WP_181841219.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=51507
     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 mlliidddia vrtslsllmk kegfdfvavg sqqealaflq levpdlvild mnfsndtsgd
       61 dglnllekik kvnnsipvil itgwatidla vkgmklgasd finkpwqnah lmqsirtild
      121 lsekktltlt rkrldaqynf sqligedaef lriletigrv astdasvlim gesgtgkeli
      181 aeaihqnsqr nrkpfvkvnl ggistslfes emfghvrgaf tdarydrvgr femankgtif
      241 ldeigdldls sqvkllrvlq drtyevlgss rtktldvrvv catnknlees vqknafredl
      301 lyrinlitin lpplrkrpnd ipllvnffvq nlreiysrpn lrvtqeamkw lkqlplpgni
      361 rqlknlvert ilvsshdtle vadfqaqwqp tarkpssval pevgsmtlee mevqmikral
      421 efhkgkvmtv akalgltrsa lyrrlekyni phdedpd
//
LOCUS       WP_181841242             350 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181841242
VERSION     WP_181841242.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 350)
  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 350)
  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..350
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..350
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39985
     Region          43..346
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mknlllslcm mvftncqaqq vdnllikelk dkiadktypk idaivvkqgd eiiveeyfng
       61 frkdtphdtr ssfksitsil agiaidkklm svddkigrff pelkneakrn isiqnllemr
      121 sglnceefyd igpecedkms etddwiaycl gvdlirtpgv nwsynsnepm lvgeiiaras
      181 gmtvvefarq nlfeplgikd ykwtlspkgq aqtagsfymk padmlkiiel vkkkghwqgk
      241 qvvsadwiek stnchipidf sfvryskmpe akyesarygf fwykekltyk diktevlfas
      301 gnggqyimyl pdynltavft gsnygnwrgk lpfeillkyi ipavekgkdk
//
LOCUS       WP_181841286             367 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Emticicia sp. BO119].
ACCESSION   WP_181841286
VERSION     WP_181841286.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 367)
  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 367)
  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..367
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..367
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42513
     Region          230..344
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mrarlktfil lsililpyql laqkkfavki sfppkanigs isirydngrd annelanvik
       61 anqcviagef fsryatiiis feadslfyys rfwvtektat irfvnrgekk ltdaidlktv
      121 eaekftayvs veqkdlddfy eenfkkiadn dslrylysqk idqlqqkqla fvkannkdyy
      181 slwlyrdliy tdnsldslna iyrafpdslk ntyegktier vlysrtiksg vkapdfitrd
      241 ikgralslad fkgkylllnf waswcepcia elpaiklihd tyasnqleil avtqdtkyka
      301 fetavkkynm nwlhvfrdme lfksygdmsl pkvflidptg tiiyvrdeqn didlslltkl
      361 mseelkk
//
LOCUS       WP_181841221             607 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Emticicia sp. BO119].
ACCESSION   WP_181841221
VERSION     WP_181841221.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 607)
  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..607
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..607
                     /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=67037
     Region          1..>268
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 migqkiqnyn veellgeggm gtvyratdtl lqrsvavkil hphlvrdttf ferfrneail
       61 saklnhsnva vlynflrdrn dnfmvmefvd gmnlekllkq ngalplesvl kilmqtldgl
      121 hhahekgilh rdikpanlml trdgtvklmd fgiarmvgsq rltradrivg tleymapell
      181 dgsepsvqsd lyaigvlmye llsgkmpfea stdstlitqi ltkkpiplrt rignlpkkve
      241 eildtllqkk perrfesaad lrhilstivt pgkvvpqslq pkkveinvnp tvaytkantn
      301 ptrladyhqk qqqgtgfkpt vvqtvksrml stegmilgga vlaavmivig gvffmspkkp
      361 dnkqeqsftp ttqvvipqtv sdtdsqkvsn nsvgfqqpld kvinptekke irpkdippvd
      421 nkekskekdk tkqpvekkee ekkkedpkpt psepivkqpv ndpvkdpvkd pesvkeepkv
      481 rasrnvtirg lsvavaldet issndpgikg ksinlrvltd irvdgivvia agaratakvt
      541 sarssdagks flefrpervq avngdwvplk spelgksgst tepvvftrgm rilpdpktan
      601 ailtitl
//
LOCUS       WP_181841260             247 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181841260
VERSION     WP_181841260.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 247)
  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 247)
  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 247)
  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 247)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 247)
  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 247)
  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 247)
  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..247
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..247
                     /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=27987
     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 mltailidde kgcldtleie lqtycadvkv lakfqsaeka levletirpd mifldismpq
       61 mngfdfllki pkinfevifc taydayalta fefcaidyll kpiskdklir avdkvrqkqs
      121 kqvdiqnlel llanmrggih hkpnvavptp eglefisind iiyaeadgny srimmankek
      181 vlisrtlkdl etllsnhpfv rihqsylvnl thikkyikge ggyvvmnngt slqvsranrm
      241 klmdlvr
//
LOCUS       WP_181841501             651 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Emticicia sp. BO119].
ACCESSION   WP_181841501
VERSION     WP_181841501.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 651)
  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 651)
  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..651
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..651
                     /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=74704
     Region          416..647
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mnfrniiifm liamiglitf qwywienais vrqeqfdrnv ndalqetvkk iekqeiifla
       61 nqkmkieeqk kllaitqkkq ekkklpkppk aeqledfgaa ftpeaplspv fpqefnsykg
      121 yntyyapqgs eplakvrqra grgsntvavt dvfgttrlle ipvrqmdlik emleeqnmal
      181 edlnqplrnn vmrqktaddl ikefnrqvli lnknsnenhq ilsiggiedq ssgfsfgyti
      241 stpvidssht vyvkpkkhkv vekpkiktee ptvtvaqedi ertknkaelv kdvltdvihg
      301 srdiherldr isldtllkke lksrgitipy qyivknssnl ifasfaenti pnfirdsyra
      361 qlfpsdlqpq nhflyvhfpd tqgfilrnmw tvfassvfli lmiggifyts vntmlkqkkl
      421 atikndfinn mthefktpis tislavevmk dndvkkdnnk mnrylniiqd enrrlgtqve
      481 kvlqmalldk gdvklklepv nihetieqvl hnlsvqieqk ngtvnlelda enpeieaddv
      541 hvtniiynll dnankyspet peitiktene egflkitiad kgigmtkeql nriferfyrv
      601 ptgnlhdvkg fglglsyvrk mveshqgviq veskigegsr fevylplnrr v
//
LOCUS       WP_181841502             281 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Emticicia sp. BO119].
ACCESSION   WP_181841502
VERSION     WP_181841502.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 281)
  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 281)
  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..281
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..281
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=32265
     Region          48..277
                     /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 mfwplvtgfl iilvilyiwl wqkitrdkpr nyptlqnrqk lnsskkilvc fgdsnthgnv
       61 synwvsdiet afqnlqvlna gvnsdltysl lqriddviac qpdfitilvg tndvsatisq
      121 elansfkqin ripqemmpdy gsfksnyqei idrlkketha kiavmslpli sedltheani
      181 kadiyseyik amaqtqhlsy lplreklkdy lqanpqplkh tfdetlklli fsiinhyilg
      241 kdwdytsrkh gyqltpdnih lnsvsggiir dlvkefisvt q
//
LOCUS       WP_181841564             302 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Emticicia sp. BO119].
ACCESSION   WP_181841564
VERSION     WP_181841564.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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..302
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..302
                     /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=34016
     Region          26..177
                     /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          148..299
                     /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 mkfllyifpv avfaqtpqnv estletinik sgkrtiilke krhfeapnws rdgkyfiina
       61 kgllekistt geklgtintd fankcnndhg isfdgkmivi shnddrmkgt pggssriftl
      121 pieggtpkli tekapsywhg ispdgqtlvy casrngefdv ysipvtggee krltnaqsld
      181 dgpeyspdgk yiyfnshrtg kmhlyrmkpd gseqeqltnd eysnwfahps pdgkwivfit
      241 yiedqkashp fgkdvklrlm dlktrkikdl tdvffggqgt invpswspds kqlafvtyri
      301 dk
//
LOCUS       WP_181841532             425 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Emticicia sp. BO119].
ACCESSION   WP_181841532
VERSION     WP_181841532.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..425
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..425
                     /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=46043
     Region          12..422
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mnyiepapik dtenplesmm srfdaavkil giseemyyil kvparqvtvg lpvtmdngqv
       61 kvfegyrvih stilgpskgg irfdpavnid evralaawmt wkcavvdipy ggakggiacn
      121 premsageme rlmraytlam ldifgpdkdi papdmgtgpr emawlmdeys kakgmtvnav
      181 vtgkplvlgg slgrteatgr gvmvsalsgm eklrlnpyrt taavqgfgnv gshaaqllqe
      241 kgvsicgisd isgayynskg idiekaiayr nankgtlegf reaelisned llalnvdvlv
      301 paakedvith enaahiqakl ivegangpts asaddiinek gimvvpdila naggvtvsyf
      361 ewvqnrigyk waldrinrrc drmmkdafdk vfetsqkhkv smrlaayiva idkvastykf
      421 rggyg
//
LOCUS       WP_181841548             495 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181841548
VERSION     WP_181841548.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 495)
  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 495)
  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..495
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..495
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55235
     Region          36..347
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mknflgikyg lhkgiiifil lsnstlifgq slsdidkkki knlliqqvdh nnvasisiav
       61 inkgkvilee sygyankerk ivatihtpyy lasvtksita tailqlaekg kislhdpvnk
      121 ylthykvtsk fwnidsvtir ktlghtagft thdrdcypdk mtcpitmatt fsryanviwk
      181 pgskfdysni gyqvlgeiik eqskmslaky fekeifsplk mknsflaeta ipantalryr
      241 ggppfsaael kisntpasss ayssvndltk fallhlgyid reilslktik lketslnndf
      301 gwsvnqdyfg fksfyaqggt tdaqasirli ptegiavivl ansghadcnt itnkilsvln
      361 knfeenfekq tkttsstlnn pgelfsedlk gewggeietf ngnvpvklci qcnsenkiei
      421 dndikvtsin ykngvvsfnl ihkipidedm gnepyslrfy lsqkentlyg vvstmnidyn
      481 naprlsyivk lkkae
//
LOCUS       WP_181841580             306 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Emticicia sp.
            BO119].
ACCESSION   WP_181841580
VERSION     WP_181841580.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=35131
     Region          2..305
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mlklgfvsai ladfgfehvv dfaskngfsc iemmcwpkdn gdarryagvt hinvdnlddk
       61 hikyikdyth ersitisglg yypnpldpdi kksefyiehi kkviracnkl gvpvmntfig
      121 rdpqknmkdn leifkklwkp iietaeqegi kigiencpmf ftndewpggk nlaispavwd
      181 imfetfptpl fglnydpshm ifqmmdeikp iyqyknrlhh ihikdvkvyr dkldrvgima
      241 npleyhspkl pglgdvnwrg ffaaltdvry rgpvvieved kayegsiddv taailtarny
      301 ikqflc
//
LOCUS       WP_181841376             302 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Emticicia sp. BO119].
ACCESSION   WP_181841376
VERSION     WP_181841376.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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..302
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..302
                     /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=33357
     Region          3..298
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mkkilitgsn gllgqklvel ltktnnceii atargenrlp fkdgyiytam ditdkaqvqe
       61 vidrtqpavi intaamtnvd mcetakddcw kqnvnaveyl aeaaernncf llhistdfif
      121 dgkngpyked aeanplsfyg wskyaaekiv insnvrwaia rtvlvygiah dmsrtniilw
      181 vkksledgkn ikvvtdqwrt ptlaedlakg caliadqeae gifnisgkdf ltpyemaimt
      241 adyfgldkal isqadsttft qpakrpartg fdltksreil gyepvsfteg igilaeqisv
      301 sa
//
LOCUS       WP_181841633             248 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Emticicia sp.
            BO119].
ACCESSION   WP_181841633
VERSION     WP_181841633.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=27732
     Region          46..244
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mkkildyils viyllyfgll lvvfhvvqvi afnifgkkah kksvdifnla lntsyyvtgt
       61 svhfrqleey ptdrpiifia nhqstfdipg iiwylrkhqp ifvskqelah gipaisynlr
      121 ksgaalidrk dgkqavseil klskyihenn fsavifpegt rskteemkpf aeggisallk
      181 rapnalivpi aiqgtrkfnp tngmfpltsf sklswtalkg iepkgkttke vadeakaaiq
      241 evlnlrka
//
LOCUS       WP_181841649             296 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Emticicia sp.
            BO119].
ACCESSION   WP_181841649
VERSION     WP_181841649.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 296)
  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 296)
  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..296
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..296
                     /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=32632
     Region          32..291
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mnrrdflaqa slltasslis feslaaakvk hkmaysaitw ngndlvaikd iaalgfkgiq
       61 lrantyapfk dkpqdlkdil dqngltlamf ssgnvgisdd iskdlethln harfikalgg
      121 kslqitnnsr pkdrmpttee lkkyaknmse iskqiigetg vqpawhnhmh qlgetpeeve
      181 ivatsmdtny ikleldvahy tqgggnaada vikykdilya thikdtkpae sksgyqfvel
      241 gqgrvdfpai fkalekikfk gwnvieldsv pvkgrtales gqtskkyles inikfs
//
LOCUS       WP_181841654             516 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Emticicia sp. BO119].
ACCESSION   WP_181841654
VERSION     WP_181841654.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (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   2  (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 10149267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..516
                     /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=56971
     Region          4..514
                     /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(174,177..182,184..185)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(177,296..297,318..323,401,413,416,427,507)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(177,217..218,265,267..268,271,296..297,318..323,401,
                     413,416,424..427,488)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(217,267..268,271,296,424..426,482,488)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 mfnlstileh harnspakea lifadkritf gqldavanqi anglkalgig hgdkvaltcp
       61 nlpyfpmiyf gilktgatvv plsvllkrne iafhlqdsda kayfcfvgtp empmgqegla
      121 gfemidtckn ffmitpaftd atpiegtktl gmlmtgqspv fqshftspdd taviiytsgt
      181 tgrpkgaelt hsnlflnacl skdlqdlsyd dksmlvlplf hifgqtvcml asiykgatsv
      241 lvprfdaemv ltlmqkekit hfagvptmyw glltyadtdk fdmgaiknnl klcmsggaal
      301 pvqvlrdfeq kfdvailegy gmsegspvvt fnqkdrgrkp gsvgtpvwgv evcimdengn
      361 elgnnekgei cyrghnvmkg yykrpdatae tiingwlhsg digirdddgf yfivdrtkdm
      421 iirggynvyp reveelmmqh pavsmvavig ipseeygeei kacvvlkpnt tikdkelinw
      481 tkeqiasyky prviefmssl pmgasgkilk relrlk
//
LOCUS       WP_181841733             275 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Emticicia sp. BO119].
ACCESSION   WP_181841733
VERSION     WP_181841733.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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 11459274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..275
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31003
     Region          <32..181
                     /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 mkktllllfi ilkflnstaq dlynydnskk faeylsksgq yelatreyer lifmlpqnds
       61 lktsllsmyr rsgkldeall rgrqlypdit vmtspsavey srslllktdy ktarefwssn
      121 tklsqpdkii lsatseilqd dytaaneils vlkdedhkla adykalasqa vkikrkspal
      181 agimstivpg tgrfytkdwk dgivsmffvg tmafqsirgf nksgvnstrg wifgavgfgf
      241 ylgnihgsvv sakgynkksh qsirnridnl fnsyf
//
LOCUS       WP_181841683             982 aa            linear   BCT 28-DEC-2024
DEFINITION  S9 family peptidase [Emticicia sp. BO119].
ACCESSION   WP_181841683
VERSION     WP_181841683.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..982
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..982
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=110301
     Region          459..>581
                     /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          701..952
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkkyfitcll lcsvvvwaqe kpkppltwkd vaswkaipaf ggtqlssdga wfayvlnpne
       61 gdaelilrkt gdttrvkypv gsstsfsmsf sddakwlafk vypkdkdkka aakpggkpvp
      121 dkvflinlsn kkktefervk sfafngekss vlalqltpan asgsqnadap kgsdlllydl
      181 tlgktqnign iseysfnkqg dwlaltvdaa ekagnglwlr nmntnvvmil dndkatyksl
      241 nwtekgdgla llkgikdekf ktelnsvvgv knfstmpels myepkkdtla fpkgmtisan
      301 rtpywsedlg rlffgitkte lvkketpkad vktdstkket daeklakika dtsiktiddl
      361 akaiakiktd stkkiataqg adkekpdmti whwqdkrlqs rqqvqetqdk nfsfianydv
      421 stkkflrlad sslknlsiap kqlygigqdi snyeldnnld gqnysdiyiv dlktgnrkkv
      481 iekhyipdfy anpsaspdgt kflywkdgnw ivfdlnnqtl rnisdkagts fidveddhnv
      541 rkppypvigw tsdnhfvlvs dgwdiwqlsv dgtpspqnlt kngktgqiry qnryvldpee
      601 kgidlakiqy fkmygewtkk sgfvalengq iksllwedts vgnlnkakka nafvytrqtf
      661 ktspeyylta stnlengqki tqntpsfeky awspsvrlid yksdkgdklq galflpagye
      721 agkkyptiiy yyeklsqtlh nfanpaysgt gwnpsvytsn gyavfipdiv yklndpgmsa
      781 vwcvlpgvka aiktgiidet kigihghswg gyqtsflitq tnmfkaaaag apltdmismy
      841 nliyknsgss ngaifeasqg rllppwenwe aynrnsplyh vkkvntpllm lhndadgavd
      901 ftqgieyyna lrrlkkpvvl iqykgenhgl akltnrkdya vrmmeffdyh lkgkpapdwl
      961 ekgvdrltld ehldkramev ek
//
LOCUS       WP_181841777             132 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Emticicia sp. BO119].
ACCESSION   WP_181841777
VERSION     WP_181841777.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 132)
  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 132)
  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 132)
  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..132
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..132
                     /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=15217
     Region          4..125
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04690"
                     /db_xref="CDD:467572"
ORIGIN      
        1 mrwidkiawl yirdrkvlst rsrgkdtlyf pggkreages deeallreik eeltvdlipe
       61 slqflgkfea qahghpkgim vimtcyqany rgelktdsei eelawltyad kdkssavdql
      121 ifdhlknhnf id
//
LOCUS       WP_181841790             307 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181841790
VERSION     WP_181841790.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..307
                     /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=35066
     Region          <143..301
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 medynkiies lgvkfakarh irilqtvkik nvydventil ilydgdvkla gndervqpgd
       61 llfipggkaa titygagepk nisfeefmtr resywetmtd ssnvgrvpns fgliafeakv
      121 fdsvnfftsl dippffikqh sklgllihdi lkedfsdevg rgrvirnkte eivieivrhi
      181 lkhrmfveql atnstyfkdp rlidiftyik nslagdlsnk qlanvanvse dyvgqyfkml
      241 tginpqdyie yqrmeaavtl lrtskksira ighevgykdt ayfcrrfkmm fgipagkmrr
      301 reslmig
//
LOCUS       WP_181841958             426 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Emticicia sp. BO119].
ACCESSION   WP_181841958
VERSION     WP_181841958.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=45496
     Region          21..>84
                     /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          64..406
                     /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 mkksyllall lgvssttfaq rtlihcgtli dgisntpksq vtivveknri adiqngytaa
       61 qatdkvvdmk trtvmpgwid mhvhiesets kdqylkrmss nmadvafesq kyaattlmag
      121 fttvrdlggs gvnisirnai nkglvigpri ftagrtiatt gghgdptngi sntysvpdyv
      181 tngvvdspeg grqavrqryk dgsdcikita tggvlsiakn gkgpqftede isaivstakd
      241 ygfhvaahah gaegmkrair agvttiehgt fmddeaielf kkhgayyvpt iiagktvgds
      301 vkvpgyyhpl vvpkaietak qiaetfakay kagvkvafgt dagvfphgyn akefqymveg
      361 gmpmmeaiks ativnaeilg mkselgsvek gkladivave gdplkdakvm mnvalvmkeg
      421 kiykek
//
LOCUS       WP_181842002             411 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Emticicia sp. BO119].
ACCESSION   WP_181842002
VERSION     WP_181842002.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 411)
  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..411
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..411
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46691
     Region          1..408
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 misyehftlq nglevyvhed httpmaavni lynvgsrded ekktgfahlf ehlmfggskn
       61 ipsydeplqk vggennafts pditnyyitl paknietafw lesdrmmsls fddkvlevqr
      121 kvvieefkqr ylnqpygdvw lklrplvydk hpyqwatigk eishieeatm ddvkgfffky
      181 ylpnnailvv agdvtvaqvk ylcekwfepi pagekyvrnl pqetiqteak fmetsakvpl
      241 ngiykayhmp grfdpefyna dllsdllgrg kssrlytrlv kekqlfnnis ayitasldpg
      301 llmvqgnlne gvaleeadaa ieeiiaelvn dkveetelqk vknqsestla faevellnra
      361 mnlafaanag naewcnqdae kiaavtpesl qimakhilrk ensstmyyra n
//
LOCUS       WP_181842351             461 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Emticicia sp. BO119].
ACCESSION   WP_181842351
VERSION     WP_181842351.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=51806
     Region          72..456
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkiqtkiaiq fsiivaslls lfswiiyqqs amyreeefme rlknkaltta sffikvdeid
       61 nallkiidkn tltalhdekv lifsdknell yssideivin ydaalldrvr eakylefpsg
      121 eneslglvyn ldhqnfvvla safdkfgksk lknlrktlil glivgiliti llgvffagga
      181 lkpvnlfisk istitannlr qriegheskn eigllaaafn kmlarleqsf elqksfvsha
      241 shelrtplaa lkseveisle enlsieqhkg ilqnirqdin rlinlsndll qivrpfkspl
      301 infgevridd iifqaqdelg lskpeyrvtv kyaqepedes siivfgneal lkttfinlid
      361 nackyspmqq aeviidfnkt ytivtikdeg igipkddlat ifepffrskn alnisgfgig
      421 lsvcnkiiel hkgkisiqse lskgtkvtvq lpnadndqtn f
//
LOCUS       WP_181842120             144 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Emticicia sp. BO119].
ACCESSION   WP_181842120
VERSION     WP_181842120.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 144)
  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..144
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..144
                     /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=16084
     Region          1..144
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 miskkakyal kalkllsery eskqpvliae iaekenipkk fleaillelr nngilhsqkg
       61 kgggyqlrlp peqvtiakiv rivdgpiapm lcvslhfygk cddcadevtc rirpimekvr
      121 danlavyeht tlrdlieetp vmav
//
LOCUS       WP_181842388             209 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Emticicia sp. BO119].
ACCESSION   WP_181842388
VERSION     WP_181842388.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 209)
  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 209)
  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..209
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..209
                     /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=23671
     Region          45..201
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mnfadfiskl shrlanyplp gheeivkkms pnrmrlkgep nestrrsgvl llfypkgevi
       61 ylplilrpqy dgvhggqmaf pggraelkdk niqatalrea qeeigikasd vkiignltel
      121 yinpsnllcq pvmgyinykp dfypdereve dilevplsdf inpdtvqnrf veargykfet
      181 pgfiiqeqiv wgatammiae lieimkdik
//
LOCUS       WP_181842398             229 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181842398
VERSION     WP_181842398.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=26001
     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 mltaiaidde pralevvevh asrvpfldlk atftdafeai pylqqnkvdl lfldikmpdi
       61 sgiefinilq kapmvvftta yseyavkgfe ldaidyllkp fslarftkac nkalelsqlg
      121 kentsdfifl ktgyeeekvl fddilyieae gnymsfilkn kkllsrqnis etlsslpanq
      181 fvrihrsyvv ainkiqkitr qavwiagnei svgasyedkl meireklkk
//
LOCUS       WP_181842452             327 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Emticicia sp. BO119].
ACCESSION   WP_181842452
VERSION     WP_181842452.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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 327)
  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 327)
  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 327)
  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..327
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..327
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36979
     Region          23..314
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 meneeeifkn ridlelvtka vsdikhelnq ivfgqdevid liligilsdg hiliegvpgv
       61 aktmlskllg kvldisfkri qftpdlmpsd vlgtsvfnpk tldfeykrgp vfgnivlide
      121 inrapaktqa alfelmeerq itidgntylm dmpfivlatq npieqegtyr lpeaqldrfl
      181 fkvnigypsa ddevlmlkrf nyetykdvve nlqpvlsirl lkelrqivrq viiedhilky
      241 itlliqatrn ykllelgasp rasialmlas kakaalsgrd fvtpedvksm akptlrhrii
      301 ltpdaemegv nedevldnlf skveipr
//
LOCUS       WP_181842528             301 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Emticicia sp.
            BO119].
ACCESSION   WP_181842528
VERSION     WP_181842528.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 301)
  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 301)
  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..301
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..301
                     /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=33767
     Region          34..292
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mkrrdflqkg amalaastal shdlfaakkk gelvgvqlys vradmqkdpm gtlkkvaemg
       61 yknvehanyv nrkfygysat efkkilddlg lkmpsghtvm gkqhwdeakg dftdlwkqtv
      121 edaaicgqqy vispwldvsl rkdmdslkrf mdvfnksgel cqksgmkygy hnhdfefslk
      181 lnaipvydli lqntdpklvi qqldignmyg gggraadllk rypgrfesmh vkdeiavtga
      241 nekyesavlg tgiinvkeii dmgrksggtt hfiieqesyq gkapldsike dlviinkwgy
      301 k
//
LOCUS       WP_181842598             301 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181842598
VERSION     WP_181842598.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=35055
     Region          89..294
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkqvfnfnti neynafnnhe alhplvsvld fskanqrtgs rmnfgiycii lkdvdcgdlk
       61 ygrnyydyqe gtlvfispgq vvdvenkayy qptghglafh pdllhgmpla ksiheysffs
      121 yqtneslhls krerqlvldc flkiefelqq sidkhskkli asnielflny cdrfydrqff
      181 trdktnkgil ekfeellnsy ftsekpqtig lpsvaycade lhlsanyfgd likketgksp
      241 qeyiqnkild iaknkifdnd ktvneisyel gfkypqhfsr ffkqhvgmap keyrisneli
      301 l
//
LOCUS       WP_181842738             427 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Emticicia sp. BO119].
ACCESSION   WP_181842738
VERSION     WP_181842738.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 427)
  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..427
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..427
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48106
     Region          9..427
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mildrtiapp sqtieqvsip kaekvlldnq vpvymvkage qpvvrlelif eagsryenht
       61 geayfaskml segtsshtat eiseyfdqyg afleinhsve rlaitvhglt khlpkllpll
      121 qemiadsvip enelqvqkni ssqnlkinle kgsyiagqvf reqiyglnhp ygksltleai
      181 daitrkavnd fyqkqvrgks frifiagkfg neevmalnqh lgqtpvespd hnaiidnise
      241 ikhpesvlve rldnlqssir lgkrmfgrth pdffkfivtn tifggyfgsr lmkniredkg
      301 ftygissglv pqryggylvm gtdvkkeytq qtldeiakei sriqntpvde deidtaknym
      361 igslvgslnt pfevadrqki illdelpedf ydnyiqkira vtpldviema ntyfkqedlc
      421 evvvggk
//
LOCUS       WP_181842893             331 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Emticicia sp. BO119].
ACCESSION   WP_181842893
VERSION     WP_181842893.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..331
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..331
                     /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=38396
     Region          1..309
                     /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 mkkyeyidya rgfsiftivi ydflftyplp tylnyaksfg aagihlfffv sgfgltlsky
       61 tdyqtfikrr likvlvpyyi titliflinl vtkvygidfl aflghillfk mfnsdyttsy
      121 gaqfwfisti vqfylifpll lwilksekyk lfilltvvis vgyslflsfv ipeggdaykr
      181 fffqylwefa lgmvvartgk ldklisapii yffiiaiism aatailaikg gdigknlndi
      241 faffaytslt iilfrimpli nkfflwiskf sfslylthmi lwdyieakfn ssfftpltls
      301 alliitliys yyydillnki taritsasiq k
//
LOCUS       WP_181843011             313 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Emticicia sp. BO119].
ACCESSION   WP_181843011
VERSION     WP_181843011.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=36374
     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 mnrfdritai liqlqskkiv kaqdiadrfn islrtvyrdv rsleeagvpi vgeagigysi
       61 megyrlppvm ftreeartfi taeklmetft dlstkasyks amykvkavlr saekdmlnsi
      121 eenievrqrt tpfnksinnt leiilnsise kkiakmeyas fnsseplqrk iepvgiyhef
      181 nywytiafch lrndyrhfrt driskialtd esfkkehysl keylermpen enlitvviqv
      241 nkpamrflle qkyfngfvse tdkgetmemt flsasldvfa rwyitfadqa eiltpkslkd
      301 klktmlanis skf
//
LOCUS       WP_181843065             204 aa            linear   BCT 28-DEC-2024
DEFINITION  IMPACT family protein [Emticicia sp. BO119].
ACCESSION   WP_181843065
VERSION     WP_181843065.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 204)
  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 204)
  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..204
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..204
                     /product="IMPACT family protein"
                     /calculated_mol_wt=22953
     Region          5..197
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mlfddtytti kqatealfkd rgskflafty pitneqevkk yldtlrglhp kanhhcyayr
       61 lgidrsqfrv nddgepsgsa grpilnvlls kdvtnilvvv vryfggtllg vpglinayks
      121 atiealtgae liqktlndly eisfdfeamn dvmrvvkefg lkisnqtydn rctltievrk
      181 ailnqvltkm ekidsintky lltn
//
LOCUS       WP_181843072             248 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Emticicia sp. BO119].
ACCESSION   WP_181843072
VERSION     WP_181843072.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=27886
     Region          1..248
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mfskqqqkyv qslqikkyrq ehhsflvega ksvielidsd fgielvlcts kffeenekki
       61 kkisveqisq telekistlk sndsavaivk mkpniylktt enefvlvldd irdpgnlgti
      121 lriadwygik kvvcsdttvd lynpkviaas mgsftriqaf ytnlqayfeq isthmpaiig
      181 tflnhtnlhk fsfpnagyii lgnesngige avekfvtdkv tiprfghaes lnvgiataiv
      241 ldnlmrrk
//
LOCUS       WP_181843076             436 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Emticicia sp.
            BO119].
ACCESSION   WP_181843076
VERSION     WP_181843076.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 436)
  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 436)
  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..436
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..436
                     /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=48620
     Region          <5..434
                     /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 mtnnaeiqsv knrfgvigna palnyalsia vqvaptdltv litgesgsgk esfskiihal
       61 ssrkhgpfia incgaipegt idselfghvk gsftgaiddr kgyfettntg tifldeiael
      121 pigtqarllr vlengefipv gsskvkktdv rvvaatnvkl leavergkfr edlyyrlntv
      181 piyvpplrer gydidllfrk fsydfaeknh iqpveltesa tqllmsfrfp gnirqlknia
      241 eqitiletdr lvsaevlaky lpreqvsglp allkgmnggn dggiserdll ykvlfdmrkd
      301 mtdlkklvls lmqggqinpe tmkqhselfn gihtdesvsl vpqtmygpva spfqsyqpvd
      361 eggfikiddi qddrnnvedi shetqedsfs lekqekemii kalkkngfkr kyaasdlgis
      421 ertlyrkikq ydiede
//
LOCUS       WP_181843089             465 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Emticicia sp. BO119].
ACCESSION   WP_181843089
VERSION     WP_181843089.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 465)
  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 465)
  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..465
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..465
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53774
     Region          322..463
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mirifalllf itantfaqgp frisaevqdp tekrailvlh rdwvsaeeey eltlnndnrf
       61 sfittlkdla yidfyygdqs lhfwivepnd eitlkfnpkn fwktlqvtgq gsekgkyyte
      121 hqnkfeivnd welqvetwrr lplkayfekl deeqakqidf lenyqnlsqn fkdtrkadit
      181 gtiqnykvet lssekyasws qdsirnnlkm geippvaqaa sleygntyln lidlfiakea
      241 vrkkknltea deynfiksly skkqisqela ervlgfklqn aieangaigk iltpaydyla
      301 fvqnkaykny inqlinlqrt lakgspakdf slkdidgkei slkdykgkvi yldfwaswcg
      361 pcifdmkfae kikehfknkd vvfiqisidn etewkeavkl yelkginvrt ddnsaivkny
      421 avsgvpsyfl idkngnfavs kvvdpsdeeg ktliqqieev larne
//
LOCUS       WP_181843107             404 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Emticicia sp. BO119].
ACCESSION   WP_181843107
VERSION     WP_181843107.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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..404
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..404
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47006
     Region          <200..370
                     /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 mklkyswlil llvvqvaeaq fswfggstkk khhevllanr aiqiettqai nnmynfnyde
       61 aerdfkwliv kypehpigyf liglnewwki lpdskneqyd dacfynmdka idladdmldd
      121 dnedkeaaff maaayavkgr lhserenwik aawaskqamk ylekcrgfgd fspelaigdg
      181 lynyyskwip enypslkpml vffrkgvkne gikqleyvaq nafytrmeak yflmqiysme
      241 nqhqkayyta sqmhsmypnn sffhryaart afvlgkadea etlsqellnn vnsgkpgyea
      301 tsgryaayil ayinmnyrhd makakeyyqk tidfaiqskv kdsgyflgan ialgkmaase
      361 kdytraiqyf sivvdnaekk sdnykeakkq ideirklmkt lkkk
//
LOCUS       WP_181843099             244 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181843099
VERSION     WP_181843099.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=28672
     Region          9..238
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mlnqpsnekv rciavedepf alqiiaddir kipflelvkv fsnaidaqnf lnentidlif
       61 ldiqmptltg iqflkkleyv pmvifttaye qyalegydls ildyllkpip ferflkaank
      121 ayelhllklr eikpveneer lfffihseyk qikifydeil yieglkdyvk iftktyakpi
      181 ltrlnlktie nklandqfcr vhqsyivsld kivsfqktkl miaqqeipig rsfidtfrtk
      241 yqds
//
LOCUS       WP_181843112             343 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Emticicia sp. BO119].
ACCESSION   WP_181843112
VERSION     WP_181843112.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=40014
     Region          6..336
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mpanrnalvr yktidaclrn rqrkwtlddl vekvsdtlye yegidkgisi rtiqadiqmm
       61 rsdklgyfap iividkkyyt yedpkysitn ipisnadlgr mneavellkq fkgfshfnql
      121 neivqkledh vyaaahkkqs vinfeknenl kglsyldlly hsivqkkave ltyqsfkaqe
      181 antfifhvww lkefknrwfa vgvrgvkkii mhlaldriqy lcpdektdyi endlydsetf
      241 yqdvigvtvs tglkaeeitl fvanedapfv etkplhhsqk ilnknkdgit vqikvqinfe
      301 lereilgfgd rmqiispaaf kkrihdrlhr svknyetknf iqs
//
LOCUS       WP_181842062            1058 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            BO119].
ACCESSION   WP_181842062
VERSION     WP_181842062.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=115884
     Region          29..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkenyfvpir gtlicgilwl msivafaqks vsgkvsdpkg eaipgasisl kgtttgtitd
       61 aegnykisvp nsggilvvss igyknqeiav gnqstlnvil esdeaaldev vvtgygtqsk
      121 rditgavttv nakdlqsvpa ttfaqqlqgr asglsivnda tpggnatvri rgfgtignnd
      181 plfiidgvpt enqgnlnpnd ietiqilkda sassiygsra angvviittr kgkigpakis
      241 fsayygvqkv sedvqslnak elgeylylad kyagktpshg qytfgsngev sipdyvfpsa
      301 gkegaantnp alysltpdni ypitksadty wwgevthsap iqnyqltasg gsensryals
      361 vgyfsqdgvv kfigydrytl rsntefsain kklrvgenft vsfdnrkggf gnndeqnavs
      421 gsykhhpllp iydingffag srganlgnns npyatlarqa dnrryrlrgf gniygeydil
      481 pfltfktslg idittengky igranpeyie gsfnngsesn tsydyqwvwq ntlsfskvfn
      541 nvhkvdayig teaikqfgey fgatrngyaf etlpiisyld lgdptrvgny grvgndytlf
      601 sefgkfnyay ndkylvqaiv rndassrfls asrnalfpaf slgwrlseek fistnlpfvs
      661 dlklrfgwgk tgnqkignyn ayttyrsdiy hagypidgsq gtptigydtq afgnpnakwe
      721 attstnfgid aslfkgklgf eidfwkrvts dmlfttpltf tvgdanapaf nvgqmtnkgl
      781 dvginyksni nnfrysiaan lstyknnvdr ldaspntryf gygsrvpavt ltqaglpiss
      841 fygyqvvgif qsqseadawp kyedynkpgk fkiadingdg kitdadrtii gnphpdfvyg
      901 lnlnfgykaf dltifangtq gndvfnytry fsdfntfqgn rskralydaw qpthtsgtvp
      961 imdandqvss rpssyfiedg syfriknvql tynlpaklas ktaldhaqiy lqvqnlatft
     1021 kytglnpeiq tgtdntlgfd ggympvsrtf ilgvnlgf
//
LOCUS       WP_181843177             344 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Emticicia sp. BO119].
ACCESSION   WP_181843177
VERSION     WP_181843177.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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..344
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..344
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=39486
     Region          30..58
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(31,34..35,38..39,41,65,68..69,72..73,75..76,99,
                     102..103,106..107,110)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          33..293
                     /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          63..93
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          98..122
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(140..141,143,167,170..171,174..175,177..178,201,
                     204..205,208..209,212)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          165..195
                     /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          234..261
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          266..296
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          301..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnytyntfik fitfiiflll vsckrekkds elffvqgnva ykkgdyekav qyfseaiqkt
       61 psfadaynnr gsarlalgdt dkaiedfeka vsldndfvla kynlgdalsi tsrldeslhl
      121 lksiekkyqd ssfyfvtlsn iylqknnfse anqvlqksls lnqrndkalt nlgflqyqlk
      181 eyqqakvnfe kaisinpkqh falnnlslvy ayggnfqkai elvdraielh knlvyennkg
      241 fyllntgnlt egkklinktl eennsnawai rnlgvyemlk knpkqaiill ekadklnpdv
      301 ellnyylgea yfstgnklka chyweigsql keensikklr evck
//
LOCUS       WP_181843145             436 aa            linear   BCT 28-DEC-2024
DEFINITION  cryptochrome/photolyase family protein [Emticicia sp. BO119].
ACCESSION   WP_181843145
VERSION     WP_181843145.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=51424
     Region          3..432
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
ORIGIN      
        1 mnqkvsifwf rrdlrlddna glfyalksty pilplfifds eildklenky darvefihks
       61 ildlheqlke ldssilikyg kplevwkdli etctiaevyt nhdyeqyang rdlrvgelln
      121 skgigfytyk dqvifeknei ltggntpyti ftpysrkwre klnefyvksy pteayfknfl
      181 kfenkvipgl temgffktnt rfpekeidtn liekyndlrd ipsilgtsrl svhlrfgtis
      241 irklvqkali lsqtwlneli wrdfymnily hfphiskges fkkeydgivw rnnenefqaw
      301 cmgltgypiv dagmrelnet gfmhnrvrmi tasflvkhll idwrwgeayf aeklldydfa
      361 annggwqwaa gsgcdaapyf rifnpttqtq kfdpelkyik kwvpdvsnfd ypepivehtf
      421 arervldayk kalnkn
//
LOCUS       WP_181843232             741 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Emticicia
            sp. BO119].
ACCESSION   WP_181843232
VERSION     WP_181843232.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 741)
  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 741)
  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 741)
  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 741)
  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..741
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..741
                     /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=83706
     Region          23..>110
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
     Region          98..689
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 msanfknifi gffilisyss fsqtlkgivl ekkadgkvep vigavvrwkn sklgtsadie
       61 gkfnlsktvd nrhliissvg fktdtlivqs eefltihlqp esstlqevtv kseatvidrl
      121 npiqteiitt kalakaaccn lsesfetnas vsvsysdavt gskqiqllgl sgnyvqtnse
      181 nipnirglnt tfglnyipgt wissidvgkg agsvvsgyes mtgqinielq kpeladklyl
      241 ntylnsfgrg evnlnlakki nkklsvglls hvstlqnrid rngdnfldip lynqynvinr
      301 wkyqtdnymv qfgikglyed rlggqnnfqp eqrgsslvyg fgsqtkrief fsktarfyqs
      361 kpykglglil ngavhdnqsf fglrnytgvq ktlyanliyq nifgntnhqy kaglsylldd
      421 ynetlsginp rnrqesvpga ffeytytlpe kltivaggrv dihnlygtrf tprlhakydi
      481 skdihlrvsa gkgwrvanpl aenygllvss rfvefentlr peeswnygis lsnefhvfgn
      541 ktsliidayr tdfqnqvivd mesagllrfy nlqgrsysns fqaelnyvpa krfdlkiayr
      601 lfdvkndflq tdrslllksk qflnrdrvlf nigyalpydk wkfdltwqwn garripampq
      661 hiesyfkasa tapgysnina qitrtflkwd vylggenlnn ftqanpiias ddpfgrhfda
      721 gmtwgpvigr mvyigmryki k
//
LOCUS       WP_181843316             406 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Emticicia sp. BO119].
ACCESSION   WP_181843316
VERSION     WP_181843316.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 406)
  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 406)
  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..406
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..406
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=45299
     Region          45..>113
                     /region_name="PLN03088"
                     /note="SGT1, suppressor of G2 allele of SKP1; Provisional"
                     /db_xref="CDD:215568"
     Region          60..88
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          97..122
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          98..335
                     /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(98..99,102..103,105,129,132..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"
     Region          196..223
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(231,234..235,238..239,241,265,268..269,272..273,
                     275..276,299,302..303,306..307,310)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          231..258
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          263..293
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          298..326
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mqksvniyfl lsitvllaac gqgnrdrski ppspfqvesv mntaavdalt dairsnpsva
       61 enyfkrasvf lkignteral edinradqlk qntgkylfik alilrkmkky neafsfaqsa
      121 eilnvdtpel ytllgdlsqq kndnasaeky lakslqiapy dgethfyrgt laarkgdtlk
      181 aislinkaie lkpsfregys kltevlqnyr mydsalvvnk saliqfpdnt dllverglvf
      241 fksgrldsal vnyekaaiid skrtdvllys aaiyyrwkny tkalenyekv ldinedtpkv
      301 nyligltqeq lgnideaena lkeaveknpn deqaiialnr vsgrvnaglg nysppvnvrk
      361 pvaaapkpvv veepkklldt srlrintikp kakvnvktds tkrigf
//
LOCUS       WP_181843492             305 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181843492
VERSION     WP_181843492.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..305
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..305
                     /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=35623
     Region          80..304
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mktpdfevfi gitklmqalg lpdphspdfq lyrfeesmrt rpaispvyrs dsyifalvts
       61 gklafkvgis dflmqegtly flspwhlhqy hrledltgyi cffnesffas tpeglltire
      121 lpmfqlegra vfdlsaeqqq pfkdlfelml kevncsspsr weimrhllhi ffikaqetyh
      181 thtritpeha rnvrlsrafe rlleqhflll skgrtgkvft vnefaeqlnv hpnhlsntlr
      241 kelgksakql iherlifeak sllhttelsv teiayrlrfd eptnftkffk kstgilprey
      301 rtqai
//
LOCUS       WP_181843529            1004 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            BO119].
ACCESSION   WP_181843529
VERSION     WP_181843529.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1004)
  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 1004)
  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 1004)
  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 1004)
  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..1004
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..1004
                     /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=108533
     Region          43..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmnsyqvgrs ierllacvkn svftlavlll tsftfavmaq dvtvsgtvkg adgtglpgvt
       61 vqekgtskgt qtnvdgtykl sgvsknatlv fsfvgmltqe vavgnktvvd vtllddtkal
      121 eevvvvgygt qkrkeisgtv tslgsrdfnp gvvtnplaaa qgkvaglvit qssgdpnarp
      181 tvrlrgtgsl sagseplyvi dgvigapien vapediltmd vlrdassaai ygsrgsngvi
      241 lintkrgkag attvdyngyv gqekisqrpd llnaaefrqa aqkynqtfdd ggadtdwlkv
      301 itrtalsqnh nigvsggsen fsyrasvgyl dqigtligss karlngrlnm dakglngkll
      361 mkfnmsasqa dasfaperai gfamnmrptd pvyssngnyf qlpgtfgnfn plavlesisq
      421 kerlqdflfn aqagytiidg lffnvsgtlr tqnknssfya kstvdnllrt vggnsasrgl
      481 davvdkqlet tlnytkaits nsnlsvlagy tyqdvvsdgf gasnnnfltd vfgpnnlgag
      541 lgirsnpnll gsykneyklv sflgrvqysl mnkyfatvnm rrdgstkfgd nnkwgffpsv
      601 svgwtlseep flkgnpaidl lklrvswgrt gnsegiaplr srgfygtsgt yydatlndfl
      661 psyaiqgnpn pnlkwevnen ygagidfalw ksrltgsidw ytrqtkdlly vvnapqekgy
      721 vfptilanvg smqnrgveis ltyqwvdkkd ftfsstfags fnknkvisls ndlfqaqnqi
      781 flttnlgsal rgtsavnfsv lqagqpvgvf ygavvdrien gkyvfkdlng dgkieqqagd
      841 rtylgdpnpf fvggltnsfk yksfdfqfql tsnmgakimn tnqlllgrqd griaesnalk
      901 saltspindn qtipmdyyve sgnyvrvnna slgytlpanl gvlrrariyi agnnlllftk
      961 ysgvdpeisq alkvdgdnqr apgidvrety yktrgltagi nlsf
//
LOCUS       WP_181843563             424 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Emticicia sp. BO119].
ACCESSION   WP_181843563
VERSION     WP_181843563.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=49736
     Region          28..423
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mpknklhlls alqierlshs dndqmfndgg glylfvrhyg ekewifryts pitkqrrkqs
       61 lgsfkdtnlk qarvlasqkr tllesgldpl ieadkqlqke tkelaerkrq qshtvrnvfe
      121 swkqnelqnr kdkgceinra fekdvfplig ntpinevtrq eirsilerlt nrkaksmanr
      181 llanlkqffa yaedeelinl dptrrltkdr vggkeksrkr yleeqelvll kdllpqsglr
      241 teyealiwfl lstgcrvnev lrakwehfdi srrmfvipse hakntfkhev ylsrfalkql
      301 imlkktrttq ylvpnrksdg pitrqvltkq vtdrqqessk knrvhnpqal vlpkgrwvih
      361 dlrrtagtim qelgimphii kkclnqkied kiietyqras liheqkeafe klgqyllaig
      421 qkkk
//
LOCUS       WP_181843093             107 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Emticicia sp. BO119].
ACCESSION   WP_181843093
VERSION     WP_181843093.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 107)
  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 107)
  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..107
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..107
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=12809
     Region          1..100
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 mkiyipaflh kyrfyvlttf glliwiaffd gsnfiaqfrl wqkyrelene keyyvdalkk
       61 vkqeekevmg nadamekfar ekylmkktge tvfvivdenn qsvekee
//
LOCUS       WP_181843656            1042 aa            linear   BCT 28-DEC-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            BO119].
ACCESSION   WP_181843656
VERSION     WP_181843656.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     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=112597
     Region          16..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlgiiftawq aaaqertvsg kvtasedgsp lpgvsvtvkg tkqgtqsdas giykvnvsgn
       61 atlifsfigt vtqevavgtr tivdvqlvsd nkqlsevvvv gygtqkrtef tgaastvkat
      121 qiaerpvqsf sqgltgqaag vnitqpngll nnppvirvrg lsslslssfp lvvidgipit
      181 tgdvsgnast nnplgdinpa diesidvlkd aasaaiygsr aaagvllitt krgksgsakv
      241 sidswagvsn avrlpdvlna qqymdhknma ignalsinpn aiatsqrndk nqsflpnyds
      301 ngnlidtdwy kevyrtgfsq nhnltiqggt ektsyyfstg fsdqdgflka nsfqrrsgrl
      361 nldhqatkwl klsaninftn smnkspnsgs ytggafatsg lgriavaqvp nlppynedgs
      421 ynienntvgr knnllpaqfp naavlrdldk stsetnriis nlgaevklye gltfkttysw
      481 dlrntenirf wnpyngdgws aqgdaynqts radnwnwint lqylktigek hnlsfvlgsd
      541 vqkrrttswg aqrqtladff ftdfqgnfgt nlaagngisq vayeaylgsi synfagkyfl
      601 sgnyrrdgns alsaenrwgd fggvsagwti seeeffknma lgnkisslrl kaswgkvgng
      661 nlnnaygsfs tfssglygss ptlsfnqagn kdlkwetseq tnigmdisfl ndritleanw
      721 ynkninnlvl dvpqapskgi pgnsilanvg smynrgwefa ltavpvnkgg fvwstnlnfs
      781 tnknmvtalv ddntpiltnt sgleatsitk vgysaaqvyg vithgvnpan grrifvtrdg
      841 kevqylhlgg pnawtfldgt qtvspssqqq ilggtlptwy ggfnntfkyk gfdlalnftf
      901 sggnyiyngs kaglrdqrvw nnsvdvlrsw kqagdvtdvp ravygdnvsn gssflisenl
      961 ekgdflrlqt atlgyripst fgktgisslr vyvqvnnafl itkytgvdpe istngdsnla
     1021 sgierntipq grqftaglnl sf
//
LOCUS       WP_181843444             184 aa            linear   BCT 28-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Emticicia sp. BO119].
ACCESSION   WP_181843444
VERSION     WP_181843444.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 184)
  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..184
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..184
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=21781
     Region          5..184
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 mkarffphqs dfrkwleeny aiekelvvgf ykvnsgkpsl twsesvdqal cfgwidgirk
       61 sidnesycir ftprkptsiw stvninkmee mipkglvqea gllayekrkd dksriytyeq
      121 veielssiie ekfkddqtaw effqkqppyy rklmtgwivr akqektrfsr leklinasrd
      181 gkrl
//
LOCUS       WP_181843711             110 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor [Emticicia
            sp. BO119].
ACCESSION   WP_181843711
VERSION     WP_181843711.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 110)
  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 110)
  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 110)
  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 110)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 110)
  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 110)
  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 110)
  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..110
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..110
                     /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=12504
     Region          <10..104
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 metkirkphr nhnkllfras dnivrleani nyttfilngg tqkvmsytlk vygtilpqsf
       61 vrvnrscivn trfiadlnfd hktvvlkdgt kigisrrrle tvrqnmgava
//
LOCUS       WP_181843658             476 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181843658
VERSION     WP_181843658.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 476)
  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 476)
  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..476
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..476
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53833
     Region          21..357
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 miqrlkltlf tcftiasvsi qanaqadaql klidqfiqkn mannhipgls iaianknqli
       61 fsksygkdgn gkniisstpf aiaslskaft smavmqlvea gkinldspvk tyipsfsmad
      121 pladkitvrq flnqtsglsd vvypelsfkq qpastantid nlkdvkldtk pgekfhyhnp
      181 nyhilarlve vvshekfidy lqkhifaplq mthtasyhtt lefqkhlaqg nifvfgqpvk
      241 inepnwfieg sagivsttsd larwlrlyln kgayqeqrll sekgietmft ppanssyglg
      301 wfvdaqknvs hsgvlwtyqa eqmiltkegy aivilfnsgi nafqdyhtfm qgvsniltnq
      361 epelplmnds iyelimatfi llillltfmr frnmrtwiak hrlkpswivn skiiirllpl
      421 vfllltptll tllshrvlsw eriflmapsv iiwlgiaalc nllivivrvv nlrkrw
//
LOCUS       WP_181843727             143 aa            linear   BCT 28-DEC-2024
DEFINITION  SRPBCC family protein [Emticicia sp. BO119].
ACCESSION   WP_181843727
VERSION     WP_181843727.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..143
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=16972
     Region          10..130
                     /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(17..19,21..22,27,37,45,47,49,54,56..57,59,62,68,
                     70..71,83..84,86,88,98,100,102,104,110..118,120..122,125)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176856"
ORIGIN      
        1 manifhyfpi naspekvfet istpeginnw wsiesrgttg lgevyefvfg eeyhwagvvs
       61 kynpctefel tfnksdddwd gskvgfwlid kntytqvefy htgwpeaneh yrisnycwam
      121 ylrllkrfie ynefvpyelr lev
//
LOCUS       WP_181843830             419 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Emticicia sp. BO119].
ACCESSION   WP_181843830
VERSION     WP_181843830.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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..419
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..419
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46465
     Region          24..415
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkylcsiifi lfthhfsfsq tlvaatpesq gmstqrlqri dkvvneyvek sytagavvlv
       61 vrngkivynk glgyddlstr klmqkdaifr iasqskaias vavmmlyeeg kfllddpisk
      121 yipsfknptv ldkynekdtt yttvparrei tirdllthts gisyagigtk eavaiyaknk
      181 ipsgigtpdy tledainrla kmplvhhpge kwtyglntdv lgyfveimsg msfdsflher
      241 vfkpigmndt yfylpeskfs rlaalntedk dkmvmkvtgn qgnyptqkgt yfsggaglvs
      301 tatdyamflq mllnggkyng qrllspitvn mmihnqignl svgnnkfglg fgltttaeaa
      361 rippsegtfd wggyygttyw adpkegiigl imtqkvpnsy gdlgekfkvl vyqaitkln
//
LOCUS       WP_181843844             174 aa            linear   BCT 28-DEC-2024
DEFINITION  D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
            [Emticicia sp. BO119].
ACCESSION   WP_181843844
VERSION     WP_181843844.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
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 11415520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..174
                     /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=19438
     Region          1..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 mqkcifldrd gvlnedrvdy vykiedyvip egvvdglnll kkagyllivv tnqagiakgi
       61 ytredvlncy dflqsqcggv iddiylckhh pqyssesllr kpdslmleka iakydidtth
      121 symigdaerd vkagmkagvk tihiatgkeh teladyrfgs lleaskfiid npvq
//
LOCUS       WP_181843875             330 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Emticicia sp. BO119].
ACCESSION   WP_181843875
VERSION     WP_181843875.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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..330
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..330
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38191
     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 mpvvsvlmpv ynaerylkea insilnqtfk dfelvilnda sgdsskdiil sfkdtrikyi
       61 eneqnkglsf srnrllsear adyiawldad diayptrlee ehrflkehts famvaswarl
      121 idaedrptgn fiksyipney lsalllfvny fvqssvllkk sclpevhyrp efpptedydl
      181 wvriaanypv ailsktlvdy rihtanissv qqqksekavk lnhqiqlenl gilpsdeevn
      241 lhyniafrka eslvflqqta nwlqrisnqn kiskrfdtka lhyilahrwi kvctsnkslg
      301 ikalgiyfks kfaeinfrnv fliikylvnk
//
LOCUS       WP_181843897             510 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Emticicia sp.
            BO119].
ACCESSION   WP_181843897
VERSION     WP_181843897.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 510)
  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 510)
  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..510
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..510
                     /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=56903
     Region          28..509
                     /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 mkklllllsi tlllaacrta kvgkpsqdev avtflhlndv yeispldngk iggmarvatv
       61 rqqllkenpn titvlsgdfl spsvtgtlry egkgikgrqm vdvmnavgid wvcfgnhefd
      121 ldekdlqeri neskfewlnt namekingnl vpfgkivngt kvpfpkiqif sfktpkgeev
      181 kigmfgivlp snpkeyvwyd dffesakkay etlkpqcdfv vglthinkvd ditlagmlpe
      241 vklimgghdh enmkekignv imakadanak tayihrivyn kanskities elrkidntip
      301 dnteaalvvk kwediadasf kaigidknev itdlkepldg heatvrnqqc amgnmiakam
      361 tlatpdatdc affnggsiri ddivsgkmtq ldvlrvlpfg gklievkmrg rlleriletg
      421 fqnkgsggyl qwdkisyeat kkewringkq ldvnqeynvv tsdflltgke rnldffvktn
      481 pdiisvtdsf pesdvrndir kaviaylkkn
//
LOCUS       WP_181843911             410 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Emticicia sp. BO119].
ACCESSION   WP_181843911
VERSION     WP_181843911.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. BO119
  ORGANISM  Emticicia sp. BO119
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 410)
  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..410
                     /organism="Emticicia sp. BO119"
                     /db_xref="taxon:2757768"
     Protein         1..410
                     /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=47220
     Region          171..398
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mlrisfkkns lilsmliisg gigtylfpin ilggnlfafr iivviifini mlkhinmifg
       61 lfnslslfif kmlifiwffi plitlflvsn skialinyfn ivfglitfiv ilfylknfkn
      121 slsilvksis ficiinlvin yielitfkhl dytfvdslpd yakeipiayg ffgnpnnnay
      181 flclslpily ldfnnnkkkv ilislltfis ilfsssrlsf igllifwsfm ffanfnknkk
      241 tfisifitll gflvfyikdi itllelnali issdnyntss sevrlqhfhn mfyylketyg
      301 fglgpggyes lgnnmrghpe sisphnffve vftdygilig vllsisltir iflerkstnk
      361 rinflltlfg ilflilspqn sgylknqitw mflaivfsnf ndnefntdel
//
LOCUS       WP_181843950             646 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [Streptomyces].
ACCESSION   WP_181843950
VERSION     WP_181843950.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 646)
  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 646)
  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 646)
  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 646)
  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..646
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..646
                     /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=68663
     Region          59..646
                     /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 msgttegpsa atgqapaapq ehrlhetrpq erpphdappy epsvpapagc earppvpgar
       61 ahspsdvrad afrrapmama vldragrvve andafaallg tgpgagslsr vaaellgrpg
      121 deavravleg rraglrrtrr vrgaegrarw llvavdppra dgpgdallsv tdisarrele
      181 arvrdlrmhd pvtrlpnral fferlasvtg ptgpegateh gehpedrwpp eagqartgri
      241 gvcyldldgf kavndtfghr tgdllltava erlirvaaag arggrtplva rlggdefall
      301 vpdssgaeql tslasaalva leepfdagge rlsvsasvgv verpaaatsa telmqdadtt
      361 lywakadggg rwtlfdpern ahrmtrqvla aelrpaigrg efvldyqplv eladgttsgv
      421 ealvrwrhpq fgtlppsrfi gqaeedgsvv qlgrwvlrta caqarawqva rpgrraifvs
      481 vnvavrqvwd sdlvadvaaa leatglppel lqleltesal mgsagrplrv lqalsamgvr
      541 iaiddfgtgy snlsylsrlp vsvlkldgsf vrsfrddvpp gaadevvvea mvslahrlgl
      601 tvtaecveta qqarrllgig cdtgqgwlws rpvgperiag llrrqg
//
LOCUS       WP_181844317             328 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Pectobacterium aroidearum].
ACCESSION   WP_181844317
VERSION     WP_181844317.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..328
                     /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=36057
     Region          1..324
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mltkvnlitg flgsgkttti rhllsqkped evwavlvnef gevgidgall adsgavlkei
       61 pggcmccvng lpmqvglnml lqqkkphrll ieptglghpk qilslltsdi yqpwltlqst
      121 lclldarqls dtrytgnenf rdqlaaadii iankrdtyna ddlaalqqwq qasgdgrqii
      181 easegkidrk lldqsrhnlr elpdgahhhs hkptnglaal qlpggqswrr slnqgqgyha
      241 cgwifapeta fdtaalldwv rlspvnrvkg vmrikegtlv vnrqghdlhi etrsaapmds
      301 rieiinetpa ewntlqasll karlanvd
//
LOCUS       WP_181844361             329 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pectobacterium aroidearum].
ACCESSION   WP_181844361
VERSION     WP_181844361.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=34258
     Region          21..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 mrqsivtaag iallllsmva slmlgqttis fgavynalfh ynpeqidqil vlttrlsrtv
       61 ialvvgasla vagalmqalt rnplaspgif ginagamfai vllsslftfs sqtalawtay
      121 lgaavsgvmv yvlgtlgnar sshlrivlag aaisalfisf tqallvinqd gldsmmfwla
      181 gsvsgrslsm llpllpyfvi alfltlllar hlnilvagde iakglgqrta lvralsglcv
      241 iglaggavai agnigfvgli vphivrrvls adhrwllpgc aifgatllll adiasrlliv
      301 pqevpvgamt allgapffiy larkgmrhg
//
LOCUS       WP_181844384             423 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pectobacterium aroidearum].
ACCESSION   WP_181844384
VERSION     WP_181844384.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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 423)
  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..423
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..423
                     /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=48705
     Region          3..405
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mslndtkirn lkppvtpikl sdshglylhv kptgsrlwyf ryyffgketr ialgayplis
       61 lsearqkrde lrkllaqnin ptqqraaeka arspaksfkt valswhksnr twsenhavrl
      121 lasmnnhifp iighlpvtel ktrhfidllk giekkgllev aartrqhmcn imrhavhqel
      181 iehnpaanld giiappvkrh ypalplerlp elltriedyk qgreltrlav sltlhlfirs
      241 selrfarwse idfrnkiwti patreaitgv rysgrgakmr tphivplsrq sitilkqire
      301 isghqelifp gdhnrykpmc entvnkalrv mgydtkdeic ghgframacs almesglwpq
      361 daverqmshq ernsvraayi hkaeyldark ammqwwsdyl dtnreeyvap yiyaqqhkta
      421 gaa
//
LOCUS       WP_181844517             319 aa            linear   BCT 28-DEC-2024
DEFINITION  YbgA family protein [Pectobacterium aroidearum].
ACCESSION   WP_181844517
VERSION     WP_181844517.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..319
                     /product="YbgA family protein"
                     /calculated_mol_wt=36646
     Region          71..316
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mtlklipvgi sacllgnpvr fdgghkrlef aveqlapyfr fepvcpemai glpvprpalr
       61 lvregeshit lrasngspld vtqqmavfsa dkvsqlqhlc gyivcaksps cgmervkiyd
      121 eaqknarksg vglftqelmr qmpwlpveed grlhdpglre nfiarvyalh elnqlwqdgl
      181 srgaliafhs rykllllahs qpeyrelgpf vagidkwdsl edyvveyrkr lmkllstpat
      241 rrnhtnvlmh vqgyfrrqln sqqrqelsql idryrqgfqp llapitllkh ymaeypdayl
      301 aqqryfepyp ealrlrygh
//
LOCUS       WP_181844518             551 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Pectobacterium aroidearum].
ACCESSION   WP_181844518
VERSION     WP_181844518.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=58322
     Region          5..545
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mnkftllpll tvavlftlvg ipvlfvalqa ifpnlgsgsf anpfsafadv faqarlfall
       61 kntlllglgv alccaviaip lgalrglfal plarfwdllf lipflippyi aglswmlalq
      121 prgyaeqllp iqlgealfsl pgmigvmtln ifpvvyfavs rsmaasgnrl advarvhgas
      181 gwqaflrvtl plslpataas lllaftlaie eygipaalgs ragiqvlttn ieqrladwpi
      241 dlsgsavlsl llvaialcaf tlqramvags nvetttgkpa aivtrplgiw rwpvlvlfsv
      301 vgllavgipl asmlitafsa tisstiswqn ltwqhftmlv ddenealpal ttslglavgs
      361 alltgtvgfl aawfvvakri rgaavldgls mlpaalpgiv vgvglilawn qsfwpvtpyn
      421 twvilllsys clllpypvry ssaalaqigs nlesaarvhg anamaalrli vfplvfpsll
      481 aammlvfava srelvtslll spagvqtvsi fvwrqfeqgs vgdgmamasv avlislsvml
      541 lalrfhslkt k
//
LOCUS       WP_181844757             334 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pectobacterium aroidearum].
ACCESSION   WP_181844757
VERSION     WP_181844757.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=35584
     Region          25..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 mtsrfhprtw liallllmva lmvgaanmga lslslrmlwq tplddpiwhi wlnirvprvl
       61 lailvggala csgaimqglf rnpladpgll gissgaalcv altivlplgl ppllalyspm
      121 faafagslai taiifilsrs eqggltrlll agialnalcl aligvltyis tdqqlrqfsl
      181 wgmgslgqaq wpmllvastl vipaviatly yarrlnilql gdeeahylgv nvkrtkytll
      241 llssllvgva vavsgvigfi gliiphlmrm hlgadhrwll pgsilggacl llfadtlart
      301 llapaempvg llssliggpy flwlivqhkg rgnd
//
LOCUS       WP_181845055             569 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181845055
VERSION     WP_181845055.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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..569
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..569
                     /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=61348
     Region          20..567
                     /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 mslnplphps hiasdtsakt pllrvdglsv tfpspfgpir svknlsfqvn ageilalvge
       61 sgsgksvtar tlvglagenv dvqanaielt rhdgslcdlr yltdrdwrai rgreigfvlq
      121 dalvsldplr kigqevaepi lthrllprqq vparvaellt kagipdpehr aaqyphelsg
      181 glrqralias alaagpqlli adepttalda tvqkqvlkvf talaqaghgv llithdlavv
      241 aevadrvivm qqgslvegge arqilsapth pytrkllaai ptastrgkwl agtdplqngi
      301 apspaslaad hastddtial tadriavsfk rpdgsrmqav nqvslqikrg etlgivgesg
      361 sgkttlgkvi lalqkpdsge vrladnawst ltererrplr ariqtitqdp lssfdpqftv
      421 aqilnqplrl rrdlsddekq rriltlleyv gltpdllsrr pralsggqrq rvsiaqalas
      481 epeilicdep vsaldvttqa qvldllvalq rqlgltmlfi shdlgvvqhm shriavmkdg
      541 divetgpveq ifnqpqhpyt rlllstvae
//
LOCUS       WP_181844887             447 aa            linear   BCT 28-DEC-2024
DEFINITION  acid phosphatase [Pectobacterium aroidearum].
ACCESSION   WP_181844887
VERSION     WP_181844887.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 447)
  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 447)
  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..447
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..447
                     /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=48742
     Region          96..331
                     /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(213,220,253..255,288,294,298)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mryrsmllpa tktlpalnil safkrlpvag lflfplygva apaqpdnasi saivdtttqa
       61 snrphviele qsiqatlrka iqgeapqltr aqleqaretp qmadidwlnn sgydfavkan
      121 qqagialles fshlstdvlq qntaivtrin reattgqreq alvdaegqgy lyyladalgp
      181 rlgkvfinay nhgeirkaav llklsavsts aakqhfnypr pflqpnntih lvpdtavigd
      241 nkpytasgga fpsghtntgy tdalllaemi perfvplidr garygysriv lgvhypldvi
      301 gsrmlaernv ahylndpqyr qlfeqaktel rsalekacgt tlsacaksap qddpyaapem
      361 ktfyrytmty glpaqpgkgs pisvpegaev lldpvlphls aaerknlmvk taladgypls
      421 gapgdkgtqn fwqrlnlhda vqsaqrr
//
LOCUS       WP_181845471             347 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Pectobacterium aroidearum].
ACCESSION   WP_181845471
VERSION     WP_181845471.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..347
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37367
     Region          7..346
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mtwritiglv tnlllsfavl anagigfqhi tladegnnrp ldvavfypvs sssqtttige
       61 navfpgitvs knaapesgeh plivvshgyg gnwlnqlwla qalvkqgyiv aapnhpgttt
      121 kdmrtekaqe lwqrphdisr vvtallaape ktgrvdekri aavghslggw tvlelaggrf
      181 steqfekdcl thaglasckv yekmqvakna asraqldkpl vdprisavis ldmglargit
      241 aeslaainip vlimaagypn eelpaelesh dlarklppah saykeiadat hfsfmqrckp
      301 gaveiinaen pgdgmicldg gersreqihq evakdvsefl qaawrkp
//
LOCUS       WP_181845362             345 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pectobacterium aroidearum].
ACCESSION   WP_181845362
VERSION     WP_181845362.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=36989
     Region          24..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 msyrtyritl ltvvvftlli avcslgigrf slspwrivqi lieplsgndl lfgkklqlgd
       61 ieqqvvwsvr lprvllawca gaalalsgat lqgvfrnplv dphiigvsag aafggtlail
      121 lswtplflll saftfgmlal llifmmaaaf gkqnvlilil agvilsgffg alvslmqyla
      181 dteeklpsiv fwllgsfata hwnslvatav plalagglll rlrwhinvls mgeqdaralg
      241 iavqplrwli lslcaaivaa qvavsgsigw iglviphvar mlvgadhrrl lpvslwlggg
      301 fmvlvddlar tlseaeiplg iltallgapl favllyktqr qergr
//
LOCUS       WP_181845330             722 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Pectobacterium aroidearum].
ACCESSION   WP_181845330
VERSION     WP_181845330.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 722)
  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 722)
  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 722)
  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 722)
  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..722
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..722
                     /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=79617
     Region          11..681
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mnkktsrwal fmlpaiysga inaatndsst nhsttnsdei tvisagrteq nlwespvtmq
       61 vidneklgky tgdsiaealr dipgvditdt alagrkqiri rgeeasrvlv lidgqevtyq
      121 ragpnyslgl lidpsyieri evvkgphsvl ygsqaiggvi nfitrkggdk plsgkikavy
      181 dsatagwqes glaygsignf dyrlsgsysd qgnrstpdgr lpdthfrnsg qsawlgyrlg
      241 dhkfglslds fklstqtytd steydsfsvr ipelerkkvg lfydwqigge vlknlhlday
      301 qqnikrefrn nlsqsgnplr ynsmalyqgk mamstgtddk qtsrgltlqa ditpftdhtl
      361 iaggqwlsdv vkqnafsdvr vtgslspmgt pslsvnpssv snnhwrqnsw alfaqdewki
      421 tpdwtwtlga rqywveslsy ggqktgtvrm ngmvmpnnst saaakendst lvtasslrys
      481 gfdniqlras faqgyvyptl thkfydtaag gsttygnanl kaeksdnyev gmrykddswl
      541 ldsavyhsra rdyittlnca gnaacsgstd sssryyanan rattygmemy aeylgwtlsp
      601 yvngniirre lelptrstyr tgeptftgrv gvknitlfer melesdlylr aasrakdeta
      661 dtalqhsgwa tanleftstf gsenqyqvtl alnnlldkry ttahesipas gfstaigaaf
      721 sf
//
LOCUS       WP_181845576             561 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Pectobacterium aroidearum].
ACCESSION   WP_181845576
VERSION     WP_181845576.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 561)
  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 561)
  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 561)
  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 561)
  AUTHORS   ter Beek,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 561)
  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 561)
  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..561
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..561
                     /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=61385
     Region          44..557
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mtppsgsvin nsdliqysfd smisgvwrvs swllagllll platvfyqaf fadgvgfaql
       61 wqiglptyli hsvvivigtl lfsllfglps awfiamyrfp ghrvlqwalc lpiampafll
      121 aylytdalrh lspllreggl qivssweefh vaglsvslgc vslvlalvly pyiyllvrea
      181 lvkqpaslih sarllnqtrs qvlrrlclpi alpaiacgga lvvvetlgdy gaasylnipt
      241 mttqvldiwq kqgdlgaaar lgvlilpaif llmflvnlwr rkqkiyqaqa nasqvappvl
      301 sgwrskvvrg ycwgivclsf lfpvlyllfl alrhmmsvwd maflhaimns llasatatai
      361 itlmalsfif ytrmagifan qtpvrlvsls falpgavlav glftllslvd nginlfaraa
      421 glptadalla gslfililay svkfgrlmld slersmdaip rsldsaslvl gasplsrwsr
      481 vhipllrrsl figallifte smkelnvsll lrpfgidtla tyvfrftase qvasfafpal
      541 vlvavglipv fwlnralnik g
//
LOCUS       WP_181845266             633 aa            linear   BCT 28-DEC-2024
DEFINITION  IucA/IucC family protein [Pectobacterium aroidearum].
ACCESSION   WP_181845266
VERSION     WP_181845266.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 633)
  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..633
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..633
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=72533
     Region          23..622
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mnikseevky rdihqdtddf lsdysnknal rrlircffae gilnkndlnf iednsrgatl
       61 alqggkavlk fddispapan tyinngniyl insdgtsfpv tgheqlidvl rdsfdfhpee
      121 sgilglkkdv gnsirndtha rryrrqwrae vadamqrdgq nhftlwlrrq lsirdaamll
      181 dqwgsleghp yyptwksrpg lsdedvqqls pefnarvplr italrrdmay vecmphvdnf
      241 hqwfaqafpa lwqdwkqrln qqgldetqwl plpihswhle nwvkshyade iaegilltdg
      301 pdlitlpgms frtvlpvepp sspfiklpva iwmtsemrsl qaksihmgpr istiieaila
      361 qeggfeqrle ffreeaafhy khavhqddap gkhlsvvfrd ahayeradga lpvtvatlft
      421 alphrdqplf telvalsglg peawfrqyvr avtrpviaiy llygigleah qqnsqilfsp
      481 egvaqgllir dfgdgrtyap llrqrgyhlq pyvwpgilpt vfegdiepvr mfvadacfvs
      541 hlhelalals aeygfadarl wqvmkeetaa afdavksrvd gelwqterdm fltqpwytrs
      601 llrmhiqeyr dyriqhglsn pflvegedtr irs
//
LOCUS       WP_181845632              71 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181845632
VERSION     WP_181845632.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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 10616232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..71
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7618
     Region          5..67
                     /region_name="HTH_35"
                     /note="Winged helix-turn-helix DNA-binding; pfam13693"
                     /db_xref="CDD:433408"
ORIGIN      
        1 mnhtdwhpan iiaglrkkgt tlaavsraag lasstlanal trhwpkgerl iaeamgkrpe
       61 eiwpsrysgv k
//
LOCUS       WP_181845864             397 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181845864
VERSION     WP_181845864.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..397
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42767
     Region          19..395
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mitpvfpldt dapsthfsar iqsavqqald errlvgavvl varngelihq qaagwadren
       61 arpmaldaif rfasvskpiv svaamvlvaq grldldedit rwiptfqtrl ldgspanitv
      121 rqllshtagl gyrffeahad gpyaragvsd gmdasdisln enlsriasvp lqyvpgtawg
      181 yslatdvlga liervqgspl deavrqlvte plgmhdtgft vrdplrltta yvndtpqphr
      241 ltegemvspf egaigiaysp aricnaqafp sggagmagta wdllrlleal rkgegvllpd
      301 alieemgrdq tqglelpnap gcgfglgfsv lrdpqlaesp essgtwrwgg ayghswfvdr
      361 qqglsvvaft ntmyegmsgr fvtdlrdavy ssleair
//
LOCUS       WP_181845773              95 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Pectobacterium
            aroidearum].
ACCESSION   WP_181845773
VERSION     WP_181845773.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 95)
  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 95)
  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..95
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..95
                     /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=10941
     Region          2..82
                     /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 mtyklkfvps amkewkklgh pvreqfkkkl verlenprvp saqlhgrkdq ykiklksagy
       61 rlvylvqdet itvmimgvgk regsqvyfdt kgrsa
//
LOCUS       WP_181845949             607 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Pectobacterium aroidearum].
ACCESSION   WP_181845949
VERSION     WP_181845949.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 607)
  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..607
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..607
                     /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=67596
     Region          38..421
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mtsltrrtfv klgagsaitl aggffhanae ssvpasplri aiisdvhihn iygnydfdgl
       61 pdaqtgkklt irtlkdsvns trifnepyfa llaaldelak qqvkyvvlsg dysddgqqpt
      121 vegiaailtq yeqrhgmrff atpgnhdvnr pqgddswqrm lnadgsstml sskpgvklgd
      181 aqslivtakm qalgyerglp lmkpfgffkr dnflhwetpf gdsdelskrq ylarspdgsk
      241 qwnivdasyl vepepglwll sidanvyqvk dgpekregie gystssntgw nalltekpfm
      301 lpwvksvvqr aktqnkkllv fshyplvdfl dgtvedekql fgsnsfikrt prpdvaeqal
      361 aagirlhfsg hlhvndtgvy rgsqgtlvnv avpslaaypp amklatlhsd rvdidtlvlr
      421 nvpqfnhlfp fyqkelertg eplgdilksr dyydflhhhl allvrqrflv kdwpedlspl
      481 intlncadll wiaqqkepln akalpdatar kpnavagteg lqdislltlv tdwyclrngs
      541 dlawqdipaa rvkqyralla vytptaalpp dslqyrfglm lkilagyind epatrfvvdm
      601 qgnfitv
//
LOCUS       WP_181845977             140 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Pectobacterium aroidearum].
ACCESSION   WP_181845977
VERSION     WP_181845977.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 140)
  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..140
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..140
                     /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=16174
     Region          5..117
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mlndsrlshe veltvsfhdc dpmgvvwhgn yfrffevare allskfnygy remqasgyvw
       61 pvvdtrvkyr aaltyeqrir iratieeven rlriayqifd aesgqrtttg ytiqvavqeg
      121 crelsfvspp ilfqrlgvtp
//
LOCUS       WP_181846022              75 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181846022
VERSION     WP_181846022.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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 10616232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..75
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8460
     Region          5..74
                     /region_name="HTH_35"
                     /note="Winged helix-turn-helix DNA-binding; pfam13693"
                     /db_xref="CDD:433408"
ORIGIN      
        1 menndwypad iiaslrkkgt tlasvsrksg lalstlanal trhwlkgerl iaealnkrse
       61 eiwpsryqsd rnefn
//
LOCUS       WP_181846023              87 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181846023
VERSION     WP_181846023.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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   Wintjens,R. and Rooman,M.
  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 87)
  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..87
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..87
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9996
     Region          5..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(7,11,40)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(10,39)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(17..18,33,36,40..41)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mlpirlksar lnvdltqekl gtlagieeet arsrvsqyen gihrptfemm cafakvlnvp
       61 egyfytvddk faemlldlfr qyksrsf
//
LOCUS       WP_181845880             395 aa            linear   BCT 28-DEC-2024
DEFINITION  sialidase family protein [Pectobacterium aroidearum].
ACCESSION   WP_181845880
VERSION     WP_181845880.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 395)
  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 395)
  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 395)
  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 395)
  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 395)
  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 395)
  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 395)
  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..395
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..395
                     /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=43874
     Region          27..394
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
ORIGIN      
        1 msseiitver sgkvhhaegd aarldayips ecpqnhaanl lhlpsgdvlc vwfggtqegi
       61 adisiymsrl vkgsdnwsra vklsedatrs eqnpvlflap dnvlwllyta qksgnqdtai
      121 vryrqstdfg ttwgeigtll dqpgtfirqp itvlangdwl lpvfycrvqp gekwvgnndd
      181 savkissdrg ktwreypvpn stgcvhmnit plqdgtllal yrsrwadfiy qsrstdggkt
      241 wsdpvptdlp nnnssiqvtt lenghlalvf nhmsaadate rrlslydeie deedkasnak
      301 mpevqagsrs afwgaprapm tlaisedggk swpwqrniev gdgycmtnns teklnrefsy
      361 psvkqaqdgk lhvaftyfrq aikhvvvsee wvkan
//
LOCUS       WP_181846273             137 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [Thalassospira].
ACCESSION   WP_181846273
VERSION     WP_181846273.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 137)
  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 137)
  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 137)
  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 137)
  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 137)
  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 137)
  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..137
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..137
                     /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=14392
     Region          1..137
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mtasiaaiah egasgviekr mdgmkaigqq vkimvpmmkg alpydpakva esagiiesha
       61 genftslfpe gsnekpseal gdiwtdwskf tdlaaelqts analktvaag ngsedefkga
      121 lgtmlrtcks chtdfre
//
LOCUS       WP_181846288             280 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein
            [Thalassospira].
ACCESSION   WP_181846288
VERSION     WP_181846288.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 280)
  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..280
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..280
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31587
     Region          50..279
                     /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 mdlgccyhrl cgakpartgi cvlllammvi llsgrplsaq dritvslyse dsnvpyafld
       61 gdepdgiytr ilkeavarlp kydleivnvp frrgmdllrn gtvmgffppy qrlerdwier
      121 ysipilretv vaicssdyan rrelnhfpad yagarfanna gyklagdaff kmvdqgeivl
      181 eeanttasnl rfmmagrvdc yvnerlaild gmreldvdrn itrlfdetai igqeygflay
      241 gpdpenqwpw rntfadaldt vlakmrdsgv idqlvsdyfa
//
LOCUS       WP_181846329             366 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecR family protein [Thalassospira].
ACCESSION   WP_181846329
VERSION     WP_181846329.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..366
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..366
                     /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=39793
     Region          36..76
                     /region_name="DUF4880"
                     /note="Domain of unknown function (DUF4880); pfam16220"
                     /db_xref="CDD:435227"
     Region          115..363
                     /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 msdkpqhwdr gpvsdnlsdq devtdalmsd dlmdlaiawh arkgvddpns diyaefrewc
       61 qrspdhqiaa dkvnafmadd gfnnllagle aelqtqpgsp nkqarkpasr nfepaasrtr
      121 rlvrrmglfa giaatlsvaa vialsslnia gggdrdqrlv aeryaihqtl sdgsritlap
      181 gavvswamts eqrhlhleeg aitieaspdk nrpmvvstay sdvtvvgtqf ivisdphgde
      241 igvaegivrv rerqsgefge vtltagqgii ldqtgklirr eitaaqiekv segwrlfask
      301 plvdvaaair rqsgiklvid pgvadrlvrg rlnvadgekt igllvkslkv nrydlpfgyv
      361 lltdri
//
LOCUS       WP_181846402             269 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein
            [Thalassospira].
ACCESSION   WP_181846402
VERSION     WP_181846402.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 269)
  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..269
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..269
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29476
     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 mifvkrhsrr ycmammlgla gavfggyada ysapaqtaac etitvsshsn yppysfledg
       61 vlkgaaidli rvigkdigvn idiqnigpwm ralttlrkgg idmlttvylv perlgdlayt
      121 rpyiedpivv ftvgddapdl hehtdlinld glttrgesrg eefdrfmass lnimtvnsie
      181 qiihmldqgr adyglqglys lkkaerhtsi tkkiwitdvp inaakmcfaf artspctgwi
      241 painaeiekr iadgtvtdlm akyaalagy
//
LOCUS       WP_181846491             765 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GumC family protein [Thalassospira].
ACCESSION   WP_181846491
VERSION     WP_181846491.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 765)
  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 765)
  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 765)
  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..765
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..765
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=84041
     Region          31..740
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mnnttkvsgv adngaldvkt srlknltdri sqsangdeid lqellrtlwr rkslifsvva
       61 iltalttlvv fqvtpkytat tnviidgrkn nvvdiesvms gmsaemgall sqvevirsts
      121 lirrvvekln lendpefnaa iakkswlasl ldpktfvpdd vllalgltdn eiilsqdela
      181 eqttnrvvnt vqesmevavv grsqviainf tsvsarksal iantiadqyi vdqleakfea
      241 trratswlnd rlgdlrqrve vseqaveayr etisaqsgqs ssmteqqise lnsqlilaqa
      301 nraeaqarln qvqrllnsss dissaaevln sqliqrlrsq eaevirkvse lesrygdrhp
      361 qmikaraelt dlrasiegev rkiaqslrne mgvadarvat lrqslnqlev knssqnqaav
      421 rlrelerean anrllyenfl srfketnnqe dlqeadarii sraevpvdps apkkkliiav
      481 alvgslflgv vlvfvleqld ntfrgaeqie qmtgipaigm vplltgtllg rtdvgrypsq
      541 kpgsattesv rslrtslmls nvdappkvvg itstvpsegk stlaawlaqv aatsgqrvll
      601 vdcdlrrptv hrtfsvdneh sivellagec qldqaikkde etgiyllpak ntqanaldll
      661 ssahmadnvk alrehfdfiv ldappvlavs dakviglmad kmlyvvkwdg tprglvqagl
      721 ketvesgidl agtvlsqvnv kkhskygygd ygyyygrykd yyssk
//
LOCUS       WP_181846788              66 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pectobacterium
            aroidearum].
ACCESSION   WP_181846788
VERSION     WP_181846788.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=7647
     Region          5..61
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mknvqliplk mvleiypvsr atlyrqikag ffpepvqiga rrvawrmdei qeridnlqkv
       61 alsdrh
//
LOCUS       WP_181846782             393 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pectobacterium aroidearum].
ACCESSION   WP_181846782
VERSION     WP_181846782.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=44834
     Region          1..388
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mltdtqcrta kpkeklyrln dfnglylevk pngkkawryr fklngkssmf algeypavkl
       61 aearekceqa rkqvadgvsp tqarqldkir kvndasntfe liakewlqmk dwaditktrr
      121 ldmlervvfp aigklpirei tphhilkilq etakrgaptv aaearrtiss vfelavatlr
      181 adsdpvwpvr kalpanktqh kqalnpqqig kllscfdnsr gsyqvnycmw lmwwtlarpa
      241 evteaewaef dldnalwtip atrmkarreh viplpsqavs mlrtlqgitg nrqhlfpgrd
      301 nprgpmtshs lrqllkslgw sgtysphatr ttgstrlnem gyrpdaieaq lahadtnnvr
      361 rtynhatyld erkvmmqdwa dkldgwvqvt vev
//
LOCUS       WP_181846952             137 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pectobacterium].
ACCESSION   WP_181846952
VERSION     WP_181846952.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
REFERENCE   1  (residues 1 to 137)
  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 137)
  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 137)
  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 137)
  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..137
                     /organism="Pectobacterium"
                     /db_xref="taxon:122277"
     Protein         1..137
                     /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=15862
     Region          58..135
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mnlnitntpd sdeeefvias lwkhneqfda vdisplflnf kddenniiag lisrtwwgal
       61 evqylwvsek hrksglgrql mqaaekealn rgchlayvdt fefqakgfye klgyreygnl
      121 pgyahkhtrh ylaklir
//
LOCUS       WP_181846877             342 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181846877
VERSION     WP_181846877.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=38034
     Region          4..302
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkntilvaga ggyigiplch llinqgyrvv afdrfyfgqp vsempqspef htlrgdiryi
       61 apdilhnvea vidlaglsnd paaqisstlt hainydgach lantakkagv qryiymssas
      121 vygrsgaesa deemeckpqs lyaelklnve relirlsdtt fqpiilrnat vfglaprmry
      181 dlsvnimtrm avrekfitid gdglqhrpfi hvqdvaravl lalqldlpls vppvfniggd
      241 slnhtinsia aiiteeipev kivhhplsld trdyqlcfsh arttlgflpt rsirdgvrei
      301 vhvlttdqla gtqptcftaq wytdliewek rlqplqldgh lf
//
LOCUS       WP_181846971             456 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pectobacterium aroidearum].
ACCESSION   WP_181846971
VERSION     WP_181846971.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 456)
  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 456)
  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 456)
  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 456)
  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 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   6  (residues 1 to 456)
  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..456
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..456
                     /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=51030
     Region          136..453
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mmirgrlfwk illgfwltfl vmsqllwlaf sfygerhkpl eeivvsriat mqtemvaaal
       61 qhgglgelnd vmsllpqeeq kyisvtespl plseqelisa pqtarmpgdd fvpdkrkaqr
      121 dshiikqvng pggkwyqiry daellrsefr pprpveflnv pvpfviiagf ggllfssvla
      181 wslarplsqi ragfdqvaqg dlnvrllpvm qrrhdeisdv ardfdsmver ldslasareq
      241 llhdvshelr splarlqlai glirqnpdnv enslqriere sllmdkmige lltlsrtehs
      301 gieeayfdll glvtavvnda ryeaqvtgve illaadeded ytikgnaelm rravdnvmrn
      361 alrfsapeqq vsvsligneh ewtiqvadqg pgveksklss ifdpfirvds plsgkgyglg
      421 laitrkvvla hgghieadng eprglvirlc vprwna
//
LOCUS       WP_181847016             130 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Pectobacterium aroidearum].
ACCESSION   WP_181847016
VERSION     WP_181847016.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..130
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..130
                     /product="YybH family protein"
                     /calculated_mol_wt=14445
     Region          6..126
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mkphpireii eacdkaiser dfdalmryya edaalvikpg mvargkddir kafvaiadyf
       61 knqlvveqgn mqviegggda lvimetvlhy pdeqgsivtt trratyvfrk dadgnwlctv
      121 dnsygttlld
//
LOCUS       WP_181846962             220 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181846962
VERSION     WP_181846962.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 220)
  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 220)
  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..220
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..220
                     /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=24906
     Region          7..206
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mpshppldft qqakthlsai narwaslieq vgdcrhqtap hrepyealmr avayqqlttr
       61 agdamvakll rvhddtfpsp eqmlacstdt lrqcgfsark adtlhgiaqg alsglvpslk
      121 raaemdddtl iqqltslkgi grwtvemfli yslertdimp lddlgirqgl ryvydlqdmp
      181 kprdlqalsl qcqpyrtvas wylwrslelp ayqhfklthr
//
LOCUS       WP_181847097             569 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181847097
VERSION     WP_181847097.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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..569
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..569
                     /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=61250
     Region          20..567
                     /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 mslnplthps htasdasakt pllrvdglsv tfpspfgpir svknlsfqvn ageilalvge
       61 sgsgksvtar tlvglagenv dvkanaielt rhdgglcdlr yltdrdwrai rgreigfvlq
      121 dalvsldplr kigqevaepi lthrllprqq vpahvaellt kagipdpehr aaqyphelsg
      181 glrqralias alaagpqlli adepttalda tvqkqvlkvf talaqaghgv llithdlavv
      241 aevadrvivm qqgslvegge arqilsapth pytrkllaai ptastrgkwl agtdplqngi
      301 apssaslaad hastddtial tadriavsfk rpdgsrmqav nqvslqikrg etlgivgesg
      361 sgkttlgkvi lalqkpdsge vrladnawst ltererrplr ariqtitqdp lssfdpqftv
      421 aqilnqplrl rrdlsddekq rriltlleyv gltpdllsrr pralsggqrq rvsiaqalas
      481 epeilicdep vsaldvttqa qvldllvalq rqlgltmlfi shdlgvvqhm shriavmkdg
      541 divetgpveq ifnqpqhpyt rlllstvae
//
LOCUS       WP_181847289             149 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Pectobacterium
            aroidearum].
ACCESSION   WP_181847289
VERSION     WP_181847289.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 149)
  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 149)
  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..149
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..149
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16471
     Region          19..122
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msqsktpidl lppllptgdv faekcpsrqi lnhvtsrwgv liliallddt hrfsqlrrri
       61 ggvsermlaq tlqwlesdgf vlrtaypvvp phveysltpl gkevgvrvke laiwvegnld
      121 eimaaqqsse qpsgeqrsdk qssgklras
//
LOCUS       WP_181847290             403 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyltransferase family protein [Pectobacterium].
ACCESSION   WP_181847290
VERSION     WP_181847290.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=45090
     Region          32..384
                     /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 mnnnlivkdd ssnyyqsnlv ikrtekgylp nlpslngtri iaallvylfh tsignmlnlf
       61 sdesigeays fvlskagwvs vsfffilsgf vmnwsspsir splqfykkrf akiypvsmli
      121 iillvftgii svgrvdvwlp nllliqtwip qgdiyiggnv pswflsvivs lyivypfllk
      181 vvkkiptesl wvsvllcyaa ligvygaiyt llptvplieg wpfevgeiqw wfaytfpptr
      241 vfeftigmll sriiqegkwi svsvttsvil taltycidlf mpfllsfnlv tliplvllig
      301 slaasdlqgk rsflhakpmq wlgsisfcfy lihflvlrll newtdgnqyg vadaalliia
      361 agavsliagw llyqfieqpv gnlltakkkq svsnqvqest pts
//
LOCUS       WP_181847308             279 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Thalassospira
            profundimaris].
ACCESSION   WP_181847308
VERSION     WP_181847308.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
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="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..279
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31380
     Region          47..260
                     /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 maalakqlcf ialltgltva vlyvpvyaet ngppfglkhn itidlqttew ppyssehlpg
       61 qglasiivra afarenisvh iefmpwqrsl qnfntentpg tghrpdaifp iydnpqrqkg
      121 fflsrtivrs pvgfvyyhgs afdwqtlddl tnltigvvrg ysngsdfdqy vqdgklhive
      181 thddttllrl laagrvdvvv mdqlvmrhil dtnpdfdqtr rwfyfhpnil enkslhvgfh
      241 htpegkalrn afdrglsalq cpdnncparh vpptkfptn
//
LOCUS       WP_181847310             462 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Thalassospira profundimaris].
ACCESSION   WP_181847310
VERSION     WP_181847310.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 462)
  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..462
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..462
                     /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=50668
     Region          189..450
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 marllrrivf fgllalvala plpygsnlpw awsllslwvg ilvvvdaiac lmsppegerq
       61 ffkrikipmv lffivvawiv vqatpgivpa iahpiwaeas aqlgirlapr vtiapdltwd
      121 almvllayag vfwlsarygr krenaslmlk ffvlvstaya vyglvvyfgg wetvlwyhkt
      181 ayrgdltstf inrnsyatya aiglvaslvy lvkilardfr dggtarqitr kmldgtlvsa
      241 wlplvgvltt gtalmlthsr agfvsgmigv fvallcfrfs ravssrfgnv miagavllai
      301 ggfaisgagl ekrfeylega qkqrmhlyda vsaagtqals tgygygsfes gfrpfkdvkl
      361 spytwslahn sylefyfgtg lyglvtvlaa fllvfyqitk gvfsarkdtf yliigtsamv
      421 ivgahaltdf slqmpamgig fvfvvamafs rnvieqnrrq qv
//
LOCUS       WP_181847446             298 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Thalassospira
            profundimaris].
ACCESSION   WP_181847446
VERSION     WP_181847446.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..298
                     /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=33563
     Region          73..297
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mkedtassta ytvlqglvyv arrtqhsylv pdnvrrlgec vlsaseegra rlaeldkplv
       61 glkvgirefi flpgitlhyi lrkrciedka raaiaggvtq vvslgagyds lifrlscefp
      121 dvnfieidhp atqkfkadaf dktpesqagl arvnylsvdf thqniedrlr gfdhfdpfrp
      181 tlfisegvtv ylteeevthm fasirnlsga gtqflftvve phgsprsntr kalawylnfi
      241 geplkwtmea pnmeaylkkq gcelhsldat dqfrekymdp grrarlhhge yvvlaefv
//
LOCUS       WP_181847525            1330 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Thalassospira
            profundimaris].
ACCESSION   WP_181847525
VERSION     WP_181847525.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1330
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         <1..1330
                     /product="beta strand repeat-containing protein"
     Region          2..1325
                     /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 itaqggdvva ndfiktsdat ieitgdnnvs ftnglsdvms sgtgavtiia tkgditqadg
       61 stidggsdkv tltagngltl dqvqtsgadi aitaengsvt akdfittsga kigiraaqnv
      121 afdndeadvt stgsgeveii atagnitqad gstidggsdk vtltagdsqt ldqvkttgad
      181 iaitaqngsv takdfittsg akigikaaqn vgfdneeadv vstgsgevev iatagnitqa
      241 dgstidggsd kitltagagq tldqvktaga divitaqngs vtakdfitts ganigitaaq
      301 nvtlfngead vtstgsgdvt itatagdlyq endstidggt gkvtltagkk vtldqvqtst
      361 saiaitaqgg divandfikt sdatieitgd ndvsftngls dvtstdtgai tiiatngnit
      421 qadgstidgg sdkvtltagd sltldqvtts gadiaitaqn gsvtakdfit tssgnigita
      481 aqnvtlfnge advtstgsgd vtitatagdl sqadestidg gtgkvtltag nkvtldqvqt
      541 ttsaiaitaq ggdvvandfi ktsdatiait gdndvsftnl lsdvtssgtg avtiiatkgd
      601 itqadgstid ggsdkvtlta gdsltldqvk ttgadiaita qngsvtakdf ittsngnigi
      661 taaqnvtlfn geadvtstgs gdvtitatag dlyqedgsti dagtgnvilk agnditldqv
      721 rtnianitvt adqgsiland firtkdgsit llahkdvtln npesdvisea sgsiditatt
      781 gkivqkdgse idggdgrvsl asaqdmriat lrtgagtsgt sydgvtrmig islrsvsgti
      841 slgeisatnh idivagnsiv esnafvdhgs gsvqlstavl kgdtvamiae ggtigtsssd
      901 rfevqttaqd gseiavardq faskrryttl qardgiymae tsgdlsvdrv iagtakggsn
      961 dnagivlair ngssdigtis apekidmras gqdiqienlk srnadlyveg sdgrldiekg
     1021 slgdstvmea qhisltrlen yvdsaqllmk vtglngslsq tvnanitapk kvqfdllrtn
     1081 kavfdinttk ttivtgqitg dmivqlplgk almdnvtqki rlgyqlqlfd ndtwfnelwf
     1141 dktdfnlpvd trivtmqdnt fhgplviddp edrigritat tptetprpst ntptpqpqsa
     1201 nnsatgtpan qvgsgtvtlg aanvvtldrp tgtggngvit gqggfaangg gfentvfqps
     1261 lsvgnpgpat pasatgtsat gasptpttna pvtpagaatn sgpatetgqt gvngdtgngt
     1321 nnngsdeqdq
//
LOCUS       WP_181847593             278 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Thalassospira
            profundimaris].
ACCESSION   WP_181847593
VERSION     WP_181847593.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
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="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..278
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30883
     Region          40..255
                     /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 mlkvglrqlc fgflvlaiag lplarsqaat eavrlcftrw epyayddgnd tgpaglaidi
       61 akrafdlagr avtfvqmphs rchigirmgh ydgilfeslk ekpveklvts rfalvnrvlv
      121 avvresypka gydglstfqg anwlrvvgdd ypekiiddpd mypvdvgena hgllmlrrny
      181 vdvvfrdlas lhfgsdavkg tpglktllpa vdvepfymrl eerlapvmkg yddaiakmls
      241 dgsidhlfyr hlgfsqiafn hyfsgdetpv lpqdrlmp
//
LOCUS       WP_181847706             330 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Thalassospira
            profundimaris].
ACCESSION   WP_181847706
VERSION     WP_181847706.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
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   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 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
REFERENCE   4  (residues 1 to 330)
  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..330
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..330
                     /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=37766
     Region          1..283
                     /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 mriiqeritn pegyswgyfh yvwddfrcnw hqhpeyeltl tlnakgsrli gdhrqsfdgv
       61 dfamvgpnlp hlwecqrlst dkqievyvlw lsqewvenlt rdfvefadly alfeqarrgq
      121 sftpeavqkv laiapeldda aprkrfmlii eileillngi dgplasasfg ndtagnsdsl
      181 rvdraiafih ahhaeplrvs tlanvagvse ssfyrlfkry tgrsvveyln eyrisracvq
      241 lsrtdwpiyr iaefngfsnl snfnrrfrqy rgksardyrd nirihgqfpd yppmpdarig
      301 avparplpse tdgvsfgrcv glkgvpaevv
//
LOCUS       WP_181847875              90 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181847875
VERSION     WP_181847875.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..90
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10128
     Region          11..80
                     /region_name="HTH_35"
                     /note="Winged helix-turn-helix DNA-binding; pfam13693"
                     /db_xref="CDD:433408"
ORIGIN      
        1 mnieqqeqrm dwhpadiiaa lrkrkttlaa vsreaglsss tlanalnrpw pkgerliada
       61 lgipasdiwp nryfdsqgqr ipreirhknn
//
LOCUS       WP_181847736             416 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pectobacterium aroidearum].
ACCESSION   WP_181847736
VERSION     WP_181847736.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=46986
     Region          2..405
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 malteakvrn akpaeksvkl tdgngmhllv qsngskywrl qyrfagkqkm lalgvypavs
       61 ltearrrrde arqqiannid pgekrkaekv eekglltfet varswhasnk twseghrtli
      121 insltthvfp iigqkniatl ktrdllipak naektghlel asrlqqrita imryavhndl
      181 idvnpaydla gaiataksvh rpalplehit elmtrieayk gkgitqlavq lclltfirss
      241 elrfarwsef dfknalwtip akreplknvk fsnrgskmkt phlvplskqa lvilkelhti
      301 sgehklvfig fshadkpise ntinkalrvm gydtktevcg hgfrtmacsa liesglwsrd
      361 averqmshqe rnsvraayih kaehlderkl mlqwwadfld anrdgvvspf efaqkg
//
LOCUS       WP_181847879             419 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pectobacterium aroidearum].
ACCESSION   WP_181847879
VERSION     WP_181847879.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=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 maltdikvrs akpeekeysl tdgdgmfllv hpngskywrl rfrfggkqhl lalgvypevs
       61 lsgarqkrde arkqvaagid prehkkavka kqeedektfe vvarawhadn kkwseshger
      121 ilkslsdnif paigsthitd lktrdllapi ksversgrle vakrlkqrvt aimtyavqng
      181 lidynpaqdm agaimpgkve hrpalalerl pellgridgy kgreftkwvi nlsllifirs
      241 selrfarwpe idferalwti pperepipgv kfsergskmh tphlvplsrq aleilkkire
      301 vsghcelvfi gdhssrkpvs egtvnkalqt mgydtktevc ghgfrtmacs sliesglwsr
      361 daverqmshq erngvraayi hkaehlderk lmlqwwadfl danreravsp fdfgkltag
//
LOCUS       WP_181848007             415 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Pectobacterium aroidearum].
ACCESSION   WP_181848007
VERSION     WP_181848007.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 415)
  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..415
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..415
                     /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=45745
     Region          151..395
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mklnflpafl tdadkrnfpt itafvlglsl plsnqllkva lilalicvlk yrdmkylrkl
       61 ivhpmvilpa lmtgllalsl lthyhetgpe mvekykklly vlplalffvl rpaqgssfvs
      121 gfllgnvlal vasmtvgllh lfpthidpas ptvfklhith nffmalavll wlerartsqg
      181 yiratylllv avavynilfm vpgrtgyval vagigvwvll slkprqslla isagvialcl
      241 lfavpnratd rlmlgvneie nclqqesgta ysscnssmgq rtafvlqavq likqapvlgn
      301 gagsfwyhnp etgysinnph nqylletiqn gavglvifll wmtyfavaaw rqpphlrnvl
      361 iavlasymac hlfnsfllds teghlfvilt alllakhipl vqrdknealq hgtps
//
LOCUS       WP_181848204             453 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Pectobacterium aroidearum].
ACCESSION   WP_181848204
VERSION     WP_181848204.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 453)
  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 453)
  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 453)
  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 453)
  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 453)
  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 453)
  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 453)
  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..453
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..453
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51773
     Region          1..418
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mflsvsvenf rsiknkntis ffasgakdhh pghiydseks ghailksagf yganasgksn
       61 fllafeairy iavrsgnlke gdripcyepy klsketvghp tifeidflsk dniryiykvs
      121 fneqeiiees ldfypnkvks nifhrvpndt wetikfggny kggtrkvaff knnsylakag
      181 dnastpqmir dvynflrldc iclgtretfk lrstdvkdmn vimdkiskvl cyvdtgiksi
      241 amtevdveip dfineslpde irsriiadsk dkfifthige dgtkanfeee desdgtrkif
      301 smmhpimeaf kdrtifvfde ldnglhphia dlvvrlfndk tinkvgsqli fsthnmqims
      361 pekmrrdqiw fveknegnsr fyslddfdkk kvkpttpyhv wyddgrfggv ptvnytkiks
      421 lilelngekd vdvdlfgsvd evelfdsfni kgv
//
LOCUS       WP_181848329             516 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator [Pectobacterium
            aroidearum].
ACCESSION   WP_181848329
VERSION     WP_181848329.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 516)
  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 516)
  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..516
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..516
                     /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=59283
     Region          12..>505
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mmqpltsrqn rllkyllqhq gyvtvkdiah yldvsektvy rdmqfveafl svwniypdkk
       61 vgagimlttd ddrhltlleq qivvddgetd alinnarrvk iasqllsdtp hetsisklse
      121 ryfissasiv ndlkiieswl hplglalvrs qsgthiegse nqvrqamasl indvmhhkep
      181 gplnhsrldp gsykalinyf geedvsfves llqdmerqls yplgepyyin ifthtlimmh
      241 riaqgkalmm aeesvhqqvd nrifsiaqnm vsqieqrves tlpsdevwfi yqyiissgiv
      301 meeradnqll ryqfsngesr rithaltqif sdlinidlrt dkllheglli hikpllnrlk
      361 yqihirnpll ddiksefidi ydmtqqamde vcqrfqlkpv aedeigylti hfqaalerqi
      421 ahkrilvvcs sgvgtshllk nrilrafpdw iivgvvsasn mqmfcqqeei eliistihle
      481 eqhipvvyvs affndddikr vtekvianql hqavph
//
LOCUS       WP_181848261             304 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181848261
VERSION     WP_181848261.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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 304)
  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 304)
  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 304)
  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..304
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..304
                     /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=34455
     Region          3..301
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mkkvlitgit gfigshvaea likegfcvig ykrstsdlwr lqeiksevif ydidrvslds
       61 afsqhkidyv ihlatlyrkf dneddfidqm nsnvtfptal lglcekyrvk gfintgtffe
      121 ldcsqqpvsa nasekafnfy aktklafqhm lktyqnsvps itfrlfspyg ekdnaklipt
      181 viqkslrgek iflsdglqki dpiyvndivs aylagiksfe lidskyrvyn lgsgkaisir
      241 eivsvieqhl cktidkewge psqadipiay adisfllsdl dwypkytihq glcktvnyyk
      301 gmgk
//
LOCUS       WP_181848406             512 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Pectobacterium
            aroidearum].
ACCESSION   WP_181848406
VERSION     WP_181848406.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (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   2  (residues 1 to 512)
  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..512
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..512
                     /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=57726
     Region          <173..509
                     /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 mqhalelala ltrqhdeagl cdwlletmqa awqpqgmllg mvdvsgrqlt cqgrvhdmpv
       61 elnlgvddfs hplayalhkn qartwdslyg gariehrdfr qmlisvgtnc glhaqpllsd
      121 sgkplavlal ldtptrlqtl hqrgecerla qvfcrqlill relahtrreq valrdslrqi
      181 kdegqsrreq ekrvettlvg qstvikalhq qiyqaakhrl svliqgetgs gkdvvarllh
      241 qcseraskpf iaincaaipe nlieselfgy qkgafsgaqs nkiglveqan ggtlfldevg
      301 dmpqsmqakl lrvlethsfr plgaekevhs dfrliaathq pleqhvsdgv frqdlyhrlc
      361 qcllqvaplr erpddirllc ehfinqfadk qqkhvgplnr aflrqlvgyd fpgnvrelrn
      421 llevacahtp dgealslasl ppelrerlts staeeqdryq hihdlriatq ryeaaviear
      481 lrqfqgnrll vadslnipkr tldhkcqkle vn
//
LOCUS       WP_181848696             369 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DegT/DnrJ/EryC1/StrS family aminotransferase
            [Pectobacterium].
ACCESSION   WP_181848696
VERSION     WP_181848696.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=41364
     Region          4..369
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mkkpiyvtsp llppleeftp yleeiwqnkw ltnggpfhqk leqeladylg vnyislfsng
       61 tlalltalqa lritgevitt pysfvatsht llwnglkpvf vdidpvtcnl denkieeait
      121 patsailpvh cygipanvdk iqsiadnygl riiydaahaf gvkkddmsil nhgdlsilsf
      181 hatkvfntie ggaiicpdek akkridylkn fgfadeltvv apgingkmne vqaafgllql
      241 nyidgalhcr kklyqtycer lggisgirli svphnvtwny aycpifvdsn fpvdreilye
      301 nlkkkniytr ryfyplissf pmyrgldsam gnnlsianni semvlclpiy adltdeeqde
      361 vineilsfl
//
LOCUS       WP_181848738             527 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pectobacterium
            aroidearum].
ACCESSION   WP_181848738
VERSION     WP_181848738.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
REFERENCE   1  (residues 1 to 527)
  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 527)
  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 527)
  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 527)
  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..527
                     /organism="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     Protein         1..527
                     /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=58911
     Region          <192..516
                     /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 mshpvrkqpq vllswismnh ggapivtalq psswpfaqcf dgvylcwrnv pdddsgkeal
       61 ertrndiekv fhknlkikdi qwdtqasptd hyaiygfaqk alwqvrkehp eamitlhlsp
      121 gtpashavwl alvstgaveg pmqliqtrre dqvqkheslv qvttfkldtl lqrfrqtqpg
      181 hvgsedtghn ieplqaqspa lcetmkllkh waplrvpvll lgergtgktt fanllralsp
      241 fqkddikdwp svvcgqfrvn pqlaqaklfg hekgaftgad klhrglleqa dgdslffdei
      301 adldrdtqrm lmaalegrgf qriggtqtqh stfrlicatn cslsrlqdel ldpdffdrig
      361 tfilrvpplr ecvediphfw aktlessvkl agisvegwrh ysdhpalllq lqkhplpgnf
      421 rdlqrvayhl laalaagcdq deilsqassa lpvqnalgeg eidlasltaq lpvdvrarle
      481 vqemawyqaa lqralnnkte aakllnlprk tfdnrlgnls dqakski
//
LOCUS       WP_181848786             402 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pectobacterium aroidearum].
ACCESSION   WP_181848786
VERSION     WP_181848786.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium aroidearum
  ORGANISM  Pectobacterium aroidearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
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="Pectobacterium aroidearum"
                     /db_xref="taxon:1201031"
     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=46122
     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 mpltdvkvrs akpedkaykl tdgegmhlmv hpngskywrl qyrfdgkqkt lalgvypeit
       61 lsearqrrde akrqiatgtd pceqkkvdkq lrqtlvdntf kaialewhey krpnwskgya
      121 edlmeafend ifpdigkrpv aeikplemlt slrklekrgv ldklrkirqa cnqvfryaiv
      181 tgraennpas elasalpppk athyphllpd elptflrals tysgskvtql atrilmltgv
      241 rtielrqaew kefdfekglw evpkermkmr rphlvplsdq vigalqqlya vtgrynlvfp
      301 grnditkpms easinqvlkr igyhgkatgh gfrhtmstil heqgyntawi elqlahvdkn
      361 tirgtynhaq yleqrrsmlq wygnyidgla argiavnirk ka
//
LOCUS       WP_181849156             285 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces parvulus].
ACCESSION   WP_181849156
VERSION     WP_181849156.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 285)
  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 15241384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32406
     Region          15..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(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 massvnptvr rrrlgqelrr lrelkgmtae evaerllvsq skisrlengr rsisqrdvrd
       61 lcgvyevedq rivdslmqma kdsrqqgwwh afgdipysvy igletdaesl rtyepqiitg
      121 llqtrayaea liqgalpets vadiekrvqv rirrqerisa dnnplrlwvv ldeaslrrvv
      181 ggkqvmreql ehvaemsqlp hitvqvlpfd vgahpgingq ysilefadaa dssvvyiegv
      241 tsdlylekal dvqkytvmye hlraqalnve qsrqliedva keyar
//
LOCUS       WP_181849092             158 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            parvulus].
ACCESSION   WP_181849092
VERSION     WP_181849092.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            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..158
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..158
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16409
     Region          89..147
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 maepvdaags vhrtateryg mrvltqalvg itaavgitag glatggaava aggyptcnty
       61 knvnghkvpa ygqptpsltc nlvlntsrsn eavkvlqtsl nnchnfslav dgyygektfl
      121 avrsiqaayl geshadgyyg pqtrdvmkhw glsgcsri
//
LOCUS       WP_181849314             134 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            parvulus].
ACCESSION   WP_181849314
VERSION     WP_181849314.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..134
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15114
     Region          16..119
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msstqertve repaydvfsr gcpsrgtleh vtgrwgaltl galfegsfrf nelrrrvdgv
       61 sekmlaqtlh alerdglvhr eaqhtnpprv dyelttagre vaqrlialiq clegrmddvl
      121 asrerydtqr mpta
//
LOCUS       WP_181849318            1022 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces parvulus].
ACCESSION   WP_181849318
VERSION     WP_181849318.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1022)
  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 1022)
  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 1022)
  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 1022)
  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..1022
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..1022
                     /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=107912
     Region          277..955
                     /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 mspppaptld galraqpapg pllprpssaa ggsafvrqll lalvcagygv gsalgwgsey
       61 aakvmgdfgl saaagaaavs cflyargrrv rfrpawllfa lssamaslgn lvwgwyevvl
      121 rvpvpspsya dlfflcfapp aivgllvlak rpvtkagwic lgldawligg slltlawsla
      181 laqaakaegg ssvahsalsv ayplldialv smvmalhfrr spvcrsavnt aigalaltvm
      241 cdalftspll hnnyrsgqll dagwfagsll layapwaasr rgrtpdedgt gghtrvvreh
      301 lpgqrgaghp qvpppvpaag gergrypaar piagslaalt pylaaavctl gilynvlngr
      361 svdrvvlltg gtvvlalvvr qgimlldniv ltqelaqken hfrslvqgss dvimiaaptg
      421 ilryvspaaa gvygrpaeel vgselaglih pedlgcvmhe vrrflaaspv eeptariecr
      481 frsgdggwln vestvnrhhg glifnsrdvt ervrlqaqlq hnaehdpltd lpnralftrr
      541 vqqalsgrra mdrgaalrgt avlfidldgf kgvndtighq agdellvqaa rrlheavrkg
      601 dtaarlggde faalivgdga rdraareghi leladrlrst lsqpylidgn dvrinasigv
      661 afaepglgag ellrnadlam yrakaggkgr velyrpqmqq dvvrkaelat rlrvalhdge
      721 fallhqpvvs ltdgritsvc aqarwrssqg vlftpaeflr vaedgdktae ldrwvlqeav
      781 eqaaeraatg lpvtvairig arrlldrsmp lgsveaqltr hglppgslli elsdidprvg
      841 ldeldrrlna lrrvgvrial dgfgsgyaai talrrlpvdv lkldrglidg vvesarlhki
      901 tsgllriatd lglksvadgv dlpeqivalr amgcthgqgm afsgpldeyr lrralgtghy
      961 pvphgpaepa faggakaryg kgvgsavaag gqvgggvpqg lpavlgggta lrshnetpvp
     1021 pt
//
LOCUS       WP_181849319            1028 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces parvulus].
ACCESSION   WP_181849319
VERSION     WP_181849319.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1028)
  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 1028)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 1028)
  AUTHORS   Rosinski,J.A. 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 1028)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1028
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..1028
                     /product="helix-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=110266
     Region          <8..975
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          957..1020
                     /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 mlgsvetrsv spvfvgrage ldtlkdalgr adaaepqall lggeagvgkt rlveefagea
       61 trrgavvalg gcveigadgl pfapfstalr alrrhlpael aaaaagqeee larllpelge
      121 atpgsgggrh deesmarlfe ltarllerva arhtvllvle dlhwadastr hliayllrtl
      181 rtgrlvvlat yrsddihrrh plrpllaeld rlrtvrrlel srftrdevgr qiagilaaep
      241 dplqvdaife rsdgnaffve elavaahegs ctgltdslrd lllvrvealp esaqrvariv
      301 aeggstveyr llaavarlte ddliealrsa vnanillpap dgdgyrfrhs lvreavgddl
      361 lpgersrlnr ryaealeaep alvpaservm rlasywyhah dpakalpavl dasaearrrh
      421 ayaeqlrlle ramelwdsap devratlrpv dyteiyppcg cdpatkplry ldlmaeaava
      481 grlcgerera mkitkralry leepdagaga gtgsrdpqra awfwtqrsll vqaqgrgdgw
      541 relgiaqelv rglppsqvha evlamaanwq mlhspgpgav taaeraveya rmvgaadiel
      601 narltlgglm vdagqidagl aemfqvrdrv vaqgrspava rshvnlpsal egvgrseeai
      661 gvlregidlt rrmglldsea wvwgnlaesl islgrwdeam raadmaaapg rgpaprggaa
      721 lkravislar gecaeaarlh aearaaygsh dpmpqhhlpl aslavglaaa dgrlqdarae
      781 lgsaldtgfp pgtqrygwpl llsaaeaead artlpaaaeg raealeriaa aakslatgap
      841 vweahalwvr aellrardld tphtwseavt afeclerpyd larvrhrlag allatggede
      901 raratdllrl agtvaghlga rpladavall aqrarltlgh paapapgpad pvealgltgr
      961 erdvlrlvad grtnrqiaee lfispktasv hvsnilaklg vsgrgeaaal ahrlelfpae
     1021 rptsrstr
//
LOCUS       WP_181849468             356 aa            linear   BCT 28-DEC-2024
DEFINITION  ferritin-like domain-containing protein [Streptomyces parvulus].
ACCESSION   WP_181849468
VERSION     WP_181849468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 356)
  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 356)
  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 356)
  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 10583968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..356
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37063
     Region          53..247
                     /region_name="Ferritin-like"
                     /note="pfam12902"
                     /db_xref="CDD:403953"
ORIGIN      
        1 masaaltaaa pmaaaapara adgpagpagc rsvaallavp dasrdlawlr eslqvavale
       61 latlppylcg wwsvedrssq aarlirrila demyhmgvvc nllvavggrp rvadvapvyp
      121 gplpggvrse vtvylsgltr pfvhdvmmai eapdaplarn adaspgigdf ydalldvfta
      181 tapelsaqgq lserigtdvl epvtdldgva raigiikeqg egtasspada fgddhpahyy
      241 afgeiyhgrq lretedgwqf tgapvpfpaa rpmarvpagg wsgvsepvqg lldrfdtaya
      301 kvlttleaaw adgdartlrs avramgalea palrlmetel pggggtygpq frppga
//
LOCUS       WP_181849490             222 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces parvulus].
ACCESSION   WP_181849490
VERSION     WP_181849490.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23617
     Region          13..178
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mgaqelraga tgrlivldfd gvlldtervg idvwrdlldd gprpardals vradgtldrd
       61 alrrgltatl grrraralws eferrnrvra drldarpgvr pflahcrerg hrlavasgng
      121 rdwveghlqr lgirsafhsv hcagpgvrtk papdtylral hacapagpas gllavedsya
      181 glaaagaagl pavwltdapg salspgpvar rvraldelig tl
//
LOCUS       WP_181849627             465 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Streptomyces parvulus].
ACCESSION   WP_181849627
VERSION     WP_181849627.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 465)
  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 465)
  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..465
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..465
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49084
     Region          84..392
                     /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          87..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(88..89,92..93,95,127,130..131,134..135,137..138,161,
                     164..165,168..169,172)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          125..155
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          160..188
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          234..259
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(235..236,239..240,242,266,269..270,273..274,
                     276..277,300,303,306..307,310)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          264..294
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          299..322
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 meiqhgwrsr rgrrvliasa agavvlggvl vvlpgegdda pppapgpaav argavttgvp
       61 aalgdlavli gdreshlrah pldgaswavl gsayveqgrr tadtanwaka ekalntslkv
      121 gaernpqale glaalavarr dfpaakkwge saaraapkrw tahavlieay tglgdhkgvg
      181 raldkllelr agtpaakara aavyrdrgwr edaaaqisda aaaaaapaer aayleqagrl
      241 afergdprea lrffqeslrt dpdqraaqag qgralaalgr ttdaltayqa alakrpspey
      301 alelgelyes lglgqaarvq ydllrarvrd aaaagadeel vlgrfeadhg dpaaavrrlr
      361 aewgrqpgta vadalgwalh rdgadeeale fatiatdgeq gggvrsalha fhrgviekel
      421 erygparrhl realminphf splrapeaer alkelgepse egppd
//
LOCUS       WP_181849632             182 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            parvulus].
ACCESSION   WP_181849632
VERSION     WP_181849632.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 182)
  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 182)
  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..182
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..182
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=20035
     Region          5..105
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 malgkdyaaq ecsiaralei vgerwtllvi rdalygvrry ndflvhlgip ravlagrlqa
       61 ltdegilekr ryqdapprde yvvtdrgial wpalralgiw grehlggqpm rtfwhascgt
      121 elspydtcpa cgtlvavrdi emkpgpgldp dptdpvsral ltprrllqpi eteqqpavad
      181 pa
//
LOCUS       WP_181849797             300 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Pseudomonas aeruginosa].
ACCESSION   WP_181849797
VERSION     WP_181849797.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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 10002921
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..300
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=33439
     Region          27..288
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 mpkpkadaps gveriqrpel ltlrgstlfe gdaltvlrrl psgsvrcvvt sppywglrdy
       61 gieeqigleg tmpqflhrlv aifaevrrvl tddgtlwlni gdgytsgnrg yrapdkknpa
      121 ramdvrpdtp eglkpkdlig ipwrlafalq adgwylrsdi vwnkpnampe svkdrparsh
      181 eflfmltkse kyyydwqavr epadggglrn rrsvwhvntk pfagahfatf ppdlirpciq
      241 astepgdyvl dpffgsgtvg lvcqdenrqy vgielnpeyv alaadrlqgq dsnviriaaa
//
LOCUS       WP_181849885             276 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Thalassospira xiamenensis].
ACCESSION   WP_181849885
VERSION     WP_181849885.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 276)
  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 276)
  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 276)
  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 276)
  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 276)
  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 276)
  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..276
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..276
                     /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=30110
     Region          188..270
                     /region_name="Cytochrom_C"
                     /note="Cytochrome c; pfam00034"
                     /db_xref="CDD:459641"
ORIGIN      
        1 mksygkhalw aqfclflpmt aqaaelqlts psgifsvyqa dellshpqar divvandggy
       61 gqdmtyravp lvsligdans vddqtglevi aldgfvanip vpliiregde haqawlaiep
      121 edapwpnlpg kdvsagpfsv vwvnaaashi rseqwpyqvs kigyaefppa rwpqlaladg
      181 apdnakqgqt ifidqcfach rmngagitel gpnlnlpmnp vdyfkpealv mlirdpasvr
      241 hwpdmqmhgf ttdqlsdaei rdviaylqam agrkae
//
LOCUS       WP_181849928             257 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Thalassospira xiamenensis].
ACCESSION   WP_181849928
VERSION     WP_181849928.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 257)
  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..257
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..257
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28414
     Region          32..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 mtfparlfal lilvvgmafa vlmsatqsha etiyvdeanp pfmyragdea agiypalvra
       61 ifrhaginvd vvavpwkrai enldankggv agiyknlerq kkyvfsepih veqlmlyqrq
      121 stfdnptdid dlrgqtvgvi rgwsygdqid darkrgvfsa seatgdeqnf qmlalgrvdt
      181 viaigeagdv wvkrlglsdk vvrsetpire nptyivfnra sstistvtmi nrsieelren
      241 gtlqriaqev lqgasny
//
LOCUS       WP_181849942             211 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Thalassospira
            xiamenensis].
ACCESSION   WP_181849942
VERSION     WP_181849942.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
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="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     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=23355
     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 mqnateraen pvefwedhyr tkktdysgnp gellvryvad ltpgraleig cshgddalwl
       61 agrgwdvtga disqtaiera qkrlvgsdfs grvlfvacdl ereipdgeyd lvtasyfqsp
      121 valaradilr ramaklvpgg yflciahasa ppwrkgngeh qfptlqeeld gldlrpdewi
      181 lhkagyatrn vtgpegekae vrdivlflqr g
//
LOCUS       WP_181850161             739 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Thalassospira profundimaris].
ACCESSION   WP_181850161
VERSION     WP_181850161.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
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="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     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=79018
     Region          84..739
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mrftgqklss tlllgtaial vfaapnfara qstndttsse tentgstetp aivieadska
       61 epgdptppvy aggqvatggr agvlgnkdvm dtpfsttsyt selitnqqaq dvadvllndp
      121 svvnstgygn fadrfnirgy dlqsddisld gvsgtaprqk aiietyerve llkgasafln
      181 gmppgssgig gtvnlvpkra tanpvtsltg stengktfgs hvdigrrfgs adqfgarana
      241 vyrdgetsid deevtarlas laldfngena rvtvdgiinq hyisqarpsv nigsaltsip
      301 napsashnya sawtysdled yigqvrgeyd ltdstmayvv lggrnseeeg gyatptlnss
      361 dgtasfgssv infqntdlss magirqkfet gpvnhevnlg isgiwqknyq ayefyssqtg
      421 siygsgadsh sstvtftggn lndlplsskn tfvsyyiadt mgflndriel tagirhqevn
      481 tkgynlgtga qnsyydsrad spmfaivgkv tnewsvyany ieglskgktv tdtgaanfgs
      541 vlapyvskqf etgvkadfgt fgggialfqi ekpsvykdst tniedtngeq qnrgieftaf
      601 gepvegfrll ggltyidsel qdtdnrtndg krakgvaeyq atfsveydlp flrgatltsr
      661 vihsgpqfvd dentlqldew trldvggryn ttlygypvtf rgnienltnn nywasastds
      721 eyitmgaplt aklaltanf
//
LOCUS       WP_181850182             291 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein
            [Thalassospira].
ACCESSION   WP_181850182
VERSION     WP_181850182.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
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="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..291
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=32636
     Region          49..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 mpsslvltta trfltraiga avagifaglf fagptdahep sfnrtdngll iaafsvwepf
       61 viededgsrh gidvalltei arrlgleldl hpcpwrrclk tledgqidvl tsfaftkera
      121 efahyvtppy sqvtpvfyyn renpvsitdy gdlrnltiga vvdsryfepf dsdtsldkfe
      181 agseiillrm lnakrldaiv gsdsnadfei rrdhledtiv kapfrsghhn dihmavsrks
      241 plmarteqis qimqdlldeg fidrlheqyw pdkgpsqhsr ddnpdatqpi q
//
LOCUS       WP_181850183             262 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Thalassospira
            profundimaris].
ACCESSION   WP_181850183
VERSION     WP_181850183.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
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="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..262
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28953
     Region          30..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 mpgiamlfvl lfggmqtsfa episdctrpl virasetysp fsikdangma agidnqfiar
       61 vmratgcefq fvfmpwkral yaiehgdidi lpsasfteer aryglfsvpy rndifgfvvr
      121 kgdarrikls sledvvrqql vigyvrgayr geafktfsen penapyiadv smaphgtqll
      181 makridlllg lpaaylaqae algfsggvee hpfilakepv rlmfssktis pqlarrlsna
      241 itretftdsy hslfgnqsvs tn
//
LOCUS       WP_181850352             383 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Thalassospira profundimaris].
ACCESSION   WP_181850352
VERSION     WP_181850352.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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 383)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..383
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..383
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42965
     Region          83..284
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mllavvipaa aiascafppd nelyqqspdi ppykqdsfke yvtqtrdwva ehrvfitqdr
       61 dtelarnipf ekgptspddr tpkrgvlfvh glgaspwyfh diatrmakng wlarsmllpg
      121 hgtrpadlgi pdyadwteav ahqvallegk vdevwlggfs tggnlvtsya aehseiagll
      181 lfspgiypdn gflfltpvik ylwdwidvds evnainyqsl ssraselyyr svldaqehla
      241 aepfdrpvvl vmsaddsvla pietlrtfek rfthpksrfv wyddtpaptr dkrvetlnsk
      301 lpdqqistfs hlsvlfapsn pyygvkgsfi fvengqenia lpedlstiwr sswgytepgk
      361 yhgrltwnpy fdaligtidd vtn
//
LOCUS       WP_181850385             501 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181850385
VERSION     WP_181850385.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 501)
  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..501
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..501
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=53265
     Region          1..375
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 maarplllsl hggagalfgv llfvvlfsga wslghddlre wlrapaqagg etlalerlle
       61 rageegvdir datlllpapg haafsvcdar ldcrldldpa sgrvlppmpa ldlllnlhks
      121 lfvgfpgrvl vslfgvslll lclagvllhs rrwrdlrrwr rdrglrlalf dlhgligiwg
      181 lpwlllfgft galsglgalg tlllapvayp qepnrvfvel mgppppaaeg rplasridld
      241 rllagdavra pgfvaqrlsl shagdvagsv eiagirrglp stanferhry rladgtllge
      301 rssaqrgfwl rafiavqplh faqyqwlgpg wsaalrglhl amglgacllc asglylwlqr
      361 rasapdarvr llqrlsqgfc aglvaaaall llglqlapse llagpwpgrl flvlwaaagl
      421 aalllpgdwp largllgvag laclaaavah lapwlmrgrl palgpdltli lcgallirha
      481 gmqaraaapp ahprvtgdhh a
//
LOCUS       WP_181850530             765 aa            linear   BCT 28-DEC-2024
DEFINITION  GumC family protein [Thalassospira xiamenensis].
ACCESSION   WP_181850530
VERSION     WP_181850530.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 765)
  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 765)
  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 765)
  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..765
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..765
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=84640
     Region          31..740
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mnsttkvssv mdnsarehnk srlksltdri sqqsnsdeid lqellrtlwr rksiifsvfv
       61 tmtvlvtliv fqiaprytaa tnviidgrks nvvdiesvmt gmsaeisall sevevihsss
      121 lirrvveklk leqdpefnve iakkswmasl ldpenyvprd vlvslglten etllsedelt
      181 eqttnrvvka vqaqlevgiv grsqviainf tstnarkasl iantiadqyi vdqleakfea
      241 trratswlnd rlgdlrerve tteravedyr etiaassgqs ssmtqqqise lnsqlilaqa
      301 draeaqarln qvqrllssss dlasaaevln sqliqrlrdq eaevlrkvse lesrygdrhp
      361 qmikaraelt dlrasierev rkiaqslrne mgvadarvat lrqslgqlet knssqnqaev
      421 rlrelerean anrllyenfl nrfketnnqe dlqqadarii araevpvdps apkkkliiav
      481 alvgsmflgv vlvfvleqld ntfrgaeqie qmtgipaigm vplltgtllg rtdvgryptq
      541 kpgsattesv rslrtslmls nvdappkvvg itstvpsegk stlaawlaqv aatsgqrvll
      601 vdcdlrrptv hrtfgvsnen sivellanec sldqaikkdp esgiyvlpak ntqanaldll
      661 ssshmaenlk alrahfdfiv ldappilavs dakviglmad kmlyvvkwdg tpralvqsgl
      721 ketveagidl agtvlsqvnv kkhskygygd ygyyygrykd yyssk
//
LOCUS       WP_181850824             471 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181850824
VERSION     WP_181850824.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..471
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=51968
     Region          9..415
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mqpnekngrd fyalawrwhf yaglfvapfm illaltgivy lfkpqldall ypqllrveag
       61 aqvrsadqll agvrqahpqa avsqylppse agrsaqfvig eegrqwnlfv dpysgrelgr
      121 qdaqlnlqav aralhgelma gtvgdrliel aagwgivlvv sglylwwprg raasalfwpr
      181 lhlrgrplwr dlhvvagfwg sllllfmlls gmtwtgywgk qfadvwnrfp aamwndvpts
      241 dmqagslnsa srqqvpwple ntplprsqpp aadahaghrg hsaqaghemp mdmpmpagip
      301 lqrvvdiare rgvaagygia lpsgmegvyt isvfpddprh datlhidqys gkvladvrwq
      361 dynavarsvq mgvvlhegkl fglgnqllml avclaillss asglwiwwkr kpagrlgvpp
      421 lrhelprwks giaimlalgv afplvgasil lvwaldwlvl srlpavrrvl a
//
LOCUS       WP_181850942             300 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181850942
VERSION     WP_181850942.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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..300
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..300
                     /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=32968
     Region          13..286
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msnaaqalat pvrldiqpva grigaeirgv tlsgeldaat veaiqaalvr hkviffrgqs
       61 qlddqtqeaf ahllgepvah ptvpsregtr flleldgaeg rranswhtdv tfveaypkas
      121 ilrsvvapes ggdtvwanta sayadlpael reladrlwav hsneydyagv kpsasveqle
      181 nyrkvftstv yetehpvvrv hpqsgertll lghfvkrlkg lsqhdsahlf avlqghvtrl
      241 entvrwcwqa gdvaiwdnra tqhyaiddyg dqprvvrrvt lggdvpvgid gqrsrtirka
//
LOCUS       WP_181850962             320 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose 4-epimerase family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181850962
VERSION     WP_181850962.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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   2  (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   3  (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   4  (residues 1 to 320)
  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 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 10142572
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..320
                     /product="UDP-glucose 4-epimerase family protein"
                     /EC_number="5.1.-.-"
                     /GO_function="GO:0016854 - racemase and epimerase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34471
     Region          5..312
                     /region_name="UDP_G4E_4_SDR_e"
                     /note="UDP-glucose 4 epimerase, subgroup 4, extended (e)
                     SDRs; cd05232"
                     /db_xref="CDD:187543"
     Site            order(10,12..15,35..37,72..74,93,116..118,144,148,
                     171..174)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187543"
     Site            order(94,118,144,148)
                     /site_type="active"
                     /db_xref="CDD:187543"
     Site            order(118,144,173,186,196,205)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187543"
ORIGIN      
        1 mtrhnvlvtg atgfigaalv nslcfsgqyk vwagcrrrgg awprgvtpll lgelgssvvw
       61 daeaaidtvv hcaarvhvms etasdplaef rkanvqgtld lareavsrgv rrfifissik
      121 vngegtepgr pytadsppnp vdpygvskre aeqallelae etglevviir pvlvygpgvk
      181 anvqtmmrwl krgvplplga mhnrrslvsl dnlvdliitc iehpaavgqv flvsdgedls
      241 ttellrrmgr algaparllp vpaswigaaa kvlnrqafar rlcgslqvdi mktrqvlgwt
      301 ppvgvdqale ktarsfldrq
//
LOCUS       WP_181850623             311 aa            linear   BCT 28-DEC-2024
DEFINITION  EamA family transporter [Thalassospira xiamenensis].
ACCESSION   WP_181850623
VERSION     WP_181850623.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
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="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     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=32557
     Region          12..310
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 msistalpaa vpahfprqia vlilvvvacs fagnhvaarl afengtglll ailcrsgval
       61 ailitlviwq rqtirlpvgt rrwqlllgll vtiqslclys avaripvala lltansfpii
      121 lalltwalgg arptlksaal mlfilsglvl aldvpgvlam egdvganwwq gigfalgaat
      181 sfavalwvtd hklsalrgsv rsmftmvivf asmiiagfae lvpggmalps atpgwfglga
      241 lvllyggafs vlfisvprln marnapvmnm epiatllfgw vvleqmispa qmlgglvvit
      301 giviltvrks a
//
LOCUS       WP_181850986             192 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181850986
VERSION     WP_181850986.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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 aeruginosa"
                     /db_xref="taxon:287"
     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=21074
     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 mpdlilasss pyrrelltrl rlpfesaspd ideshrpees aeelvrrlsa skaealagry
       61 pqhlvigsdq vavldgdilg kphtperaiq qlrnasgkrv tfltglalln sasrriqvac
      121 vpftvhfrhl desrirryve aerpldcags fkaeglgvsl frategedat slvglplirl
      181 vdmlleegve ip
//
LOCUS       WP_181851003             223 aa            linear   BCT 28-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181851003
VERSION     WP_181851003.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..223
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=25075
     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 mqsylqsgrf vdsdhpvvve faeksrgnsa kprdqavaly yavrdgvryn pyvfsrdpqt
       61 lkashalqqg esycvpkail laacarhcri parigladvr nhlatprlle alrsevfamh
      121 gytelylagr wvkatpafnr alcrafdvas lefdgvadsv fhpfnrqger ymeyladhgq
      181 fadlpeelff shlqqhyphl fsgrplaldg dfqaeagqde grr
//
LOCUS       WP_181851124             635 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas aeruginosa].
ACCESSION   WP_181851124
VERSION     WP_181851124.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 635)
  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 635)
  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..635
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..635
                     /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=69457
     Region          145..>366
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          305..633
                     /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 mvkakiyagi aiivvfgvms mlyvyrglde vvghltrler igapfsiaal emeknvgeya
       61 fgvqqyivrp dpeiraetan dstdfsryha symqlsrtrr enelghhlas dfgklsriga
      121 tlmdkrdrld vgfahvtgll eqvvtitgqs lplaaaqrep arsrslaala nlkaraaqae
      181 lrlsafrrrp talamrqaqe elaeleeals gyrrlslgne arrledelva lsiplrsgve
      241 awlsgegalq alagefarlq ehiddvcdke ieplaakglt tpqeqadria vrvldmlrya
      301 iplyllvalg vgaslvlaiv rplrtlasgt raigagdldy rilernrdef ddlarqfnrm
      361 varlqestvs rglledserr lrltvaelre eiaererser ereklqaelr rseamaamgr
      421 lvagvahevr nplfgisstl daleasanvg kggerhrevl rgevgrlnkl mtdlleygrp
      481 pgetfssgrl gqviveavri cgpaaeaagv givyqvdgcd gtlpmnhgrl lqvfvnlien
      541 avqhapagsq vtvaaktlev ngqrsvecrv edsgagfape dlpfifdpff trrrkgtglg
      601 laivqrivee hkgsieagga aqggavmrlr lpipd
//
LOCUS       WP_181851125             452 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pseudomonas
            aeruginosa].
ACCESSION   WP_181851125
VERSION     WP_181851125.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=50314
     Region          2..443
                     /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 martrilivd dedsirfgmr gflesrgygv vdadscqrar elfqasppdv avidyrlhdg
       61 saldllrdfr rlepdvpviv ltaygsidla vqaikegaeq fltkpiempa lhailkrlld
      121 nrrlqrqqri vvtreqreri dplfgespai ralaeqvdkv mgsdspilil getgtgksll
      181 akwlhlhgpr adepfvdlnc aglspdflet elfghekgaf tganaskpgi leiadggtvf
      241 ldeigdvdpr vqpkllkvle eqrfrrlgav rerevdirli aathqdlagk vkertfrsdl
      301 yfrissipls mpalrerked ipalartlla rladapgrsv rlgedaeqal cgyawpgnir
      361 elrnvlerav llrngdtiar rdlrfestpl qdvqvgdtgl tlqqverqhi ervlrevggk
      421 veqaalrlgi prstlyqkik vhgivaaqnd pg
//
LOCUS       WP_181851164             222 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Pseudomonas aeruginosa].
ACCESSION   WP_181851164
VERSION     WP_181851164.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23909
     Region          1..194
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mdgvlissre aiaaawsrva geqgvalgpd clrdhvhgrp ggytldylfg hlpterrril
       61 kqrvdeleeg adcpllpgva avirqlgwld vplalvtssw paridhvlrq hdlqaafrtl
      121 vsrddvvhgk papdgyrlaa arlgvapsrc lvfedslsgv qaacaagatc vaigeesgll
      181 aagarwsvrd frelrivred drlycqhrhp attgsersvg vp
//
LOCUS       WP_181851192             319 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181851192
VERSION     WP_181851192.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  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..319
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..319
                     /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=35885
     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 dahhhfwdpq anyhpwlaed anipfrygdy saikrrylpa dyfgdvgahr
       61 vvetvyvete wdprdplget rfvhrlaerh gaphavvaqa wldapdaaev laaqagfarv
      121 rsvrhkpggp qrpqqvgelr slmsderwrr gyaelarhgl hfdlqtpwwn laeaaclard
      181 fpdtlivlnh aglpsdrsae glaawqrama rfaecpnval kisgigqagr rwsvednawi
      241 vresialfgv eramfasnfp vdslcgsfdd iyggfkriva dlpyanqerl fhgnarriyr
      301 tvpdtvrlqq aspdprtsp
//
LOCUS       WP_181851197             688 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Pseudomonas aeruginosa].
ACCESSION   WP_181851197
VERSION     WP_181851197.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=75040
     Region          1..478
                     /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 mflsalkien frqfgnggha lniqfnkgvt alvgendagk tavidairyv lqtrdaeyir
       61 lqiedfhiak dgtqaetitl rctleglsla elgafaeyvt ykdgvgrlyv hwsarrvvas
      121 astrkwvdis vrsgengdgp sldigvrqll ataylkplrd aeremspgrn srlsqvlssf
      181 pnidagssfn pallpadlas aealsiagmg dflrhlvnsh saivsaqkei ndtylrplsl
      241 agqpltsrig fgeagtdpak lkqilerlel glldhatgea rgayglgsnn vlfmacelll
      301 lgkepdglpl llieepeahl hpqrqlqlme flegaaqpsa dlrpvqiilt thspnlsski
      361 plqnmvlmqr qqafslaenk tclaaddyrf lsrfldvtka glfyakgllv vegdaeaill
      421 pslarrlgld ltkhgvsiin vggvglrrys kilqrkdsse geitvptaci tdmdvmpdca
      481 peilslkgvk gavwpdkadr rwrtvkdfga tspdierglk ehrdkraesd gqcvrtfvad
      541 hwtleydvaf kglskevhha aylainedki degketkasv lkkaqtafek iqtahateea
      601 rcsaiyklfk raskaiaaqh lidlidqrfd drsldattlr gllpayivna ieyatrgatm
      661 tntnpahptm vpaapnpgsa dsveevak
//
LOCUS       WP_409929163              38 aa            linear   BCT 28-DEC-2024
DEFINITION  hypothetical protein [Salmonella enterica].
ACCESSION   WP_409929163
VERSION     WP_409929163.1
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.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..38
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..38
                     /product="hypothetical protein"
                     /calculated_mol_wt=3990
ORIGIN      
        1 miisamcikf ltflnsqdln slfsilsrir gggsngsk
//
LOCUS       WP_181851246             885 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas aeruginosa].
ACCESSION   WP_181851246
VERSION     WP_181851246.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 885)
  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 885)
  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..885
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..885
                     /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=96861
     Region          8..885
                     /region_name="PRK10490"
                     /note="sensor protein KdpD; Provisional"
                     /db_xref="CDD:236701"
ORIGIN      
        1 mtdtaradal ladlpadgrg rlkvflgaap gvgktfamlq aaqaqlrqgv klragvveth
       61 sraeteslla gvpqqplrsl eyrgmklqem dldglladpp alalvdelah snvpgsrhak
      121 rwqdiqella agidvyttvn vqhleslndq vrditgvqvr etvpdwvlqe ayeivlidlp
      181 prellerlre gkvyvpeqar aaidaffsqt nltalrelam qtaaarvdad lnhryrqrge
      241 eapalrgrll vgidgdeqae rlvrhacrva errhlpwsvv hvdtgglrge qarmrlqgaq
      301 qlaerlggei vvlragevar tllqharerr aslvlvgqsr rrwyrrafgg glagrllrdg
      361 qgleisalds eadlrpaepr prypvvwndy llallatala sglawgvahl lelpnislvf
      421 lmavllvavr sslmpallca vasflaydfl fipphfsfai hrhedllsla fflfmagltg
      481 nlaarqrrql ealrdtqeet slllelsrkl taatdrqavl aaaaqqfddw kdvevcllgq
      541 vngkwkteag vqrqlvdqer vaadwawahd qpaglgtgtl pggrwwwwpl saeegplall
      601 gvapldgqpl spqrrrllaa lgqplaqala rarlaedlea arlhgeteql rsallasvsh
      661 dlrtpltamr gsidsllals evippadrre llestrdeae rldryiqnll dmtrlghggl
      721 klardwvapg divgsalnrl ravlapyrvq aivandlpll yvhaalieqa linvlenaar
      781 fspshgrlri evgqdaaelr favsdegpgi peaerekifd mfytaargdr ggqgtglgla
      841 icqgmigahg grisvgegld grgttlvlhl plhpqpdlgq legde
//
LOCUS       WP_181851307             249 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF899 domain-containing protein [Pseudomonas aeruginosa].
ACCESSION   WP_181851307
VERSION     WP_181851307.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 249)
  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 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   3  (residues 1 to 249)
  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 249)
  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 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
REFERENCE   6  (residues 1 to 249)
  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..249
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..249
                     /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=28501
     Region          8..237
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mnpslqehpv ssreqwldar rrllarekql trlrdqvaae rrelpwvrvd kdyrfqgerg
       61 erslaelfgg nsqlivyhfm fapgwsegcv gcsfladhid ganrhlahhd vslvavsrap
      121 leefqafrrr mgwrfdwyss ygsdfnrdfg vsfdkaqlaa gsvdynyrpt pdageempga
      181 svflrnpage vfhtysayar gldillttyn fldltprgsn edvimdwlrh hdrydeapks
      241 acchaqash
//
LOCUS       WP_181851319             391 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181851319
VERSION     WP_181851319.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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..391
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..391
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42161
     Region          14..389
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 msgfergpgr slaenvdqvi eaaftdqrlv gavvlvahrg rwlyrraagl adreagrimg
       61 edslfrlasv skpivsvaal slvdegwlal depiadwlpa frprladgre aritprqlls
      121 hsaglgyrfl eadadgpyar agisdgmdlp gfdlaenlrr lasvpllyep grawgyslat
      181 dvlgalverv dgrplavalr qrvgipagmr dsgflcadaq rlaavyvsdr pcprrmaere
      241 tvapfedcvg irfeprrafe psayasggag migsagdvlr lleilrqgga plltsglvee
      301 lgrdqvpgse lpanpgfgfg lgfsvlrdpa iaqspeapgt wrwggayghs wfvdrtrels
      361 vvaltntlfe gmsgrfvndl rdavyrsael r
//
LOCUS       WP_181851538             418 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181851538
VERSION     WP_181851538.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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 418)
  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..418
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..418
                     /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=46347
     Region          16..397
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(53,60,88..89,96,100,107,232..233,236,240..241,244,
                     277,282..283,286..287,289,312,339..341,344..345,347..349,
                     353)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(60,82,84,87,89..90,172..173,181,231..232,235..236,
                     240,283,286..288,388)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mpdrklrlge elisplhaly dglqvdgapr pahraaehpv wvvtryrdar kvlnhpgvrr
       61 darqaaelya krtgspragi geglshhmln ldppdhtrlr slvgraftpr qverlqphie
      121 riteelldam agreqadlma dfaipltiav ifellgipea ereharqswe rqaellspee
      181 aqaladaqvd ylrvlleakr rqpaddvysg lvqaadesgq lseaelvsma hllmmsgfet
      241 tmnmignalv tllvnpeqla llraqpellp nameelvrhd spvrasmlrf tvedveldgi
      301 tipageyilv snltanhdae rfddpdrldl trntdghlgy gfgvhycvga slarlegria
      361 iqrllarfpd lqlavphael qwlpitflra lisvpvrtgc sapantasha npierivq
//
LOCUS       WP_181851579             393 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181851579
VERSION     WP_181851579.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 393)
  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..393
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..393
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41999
     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 mkgplsslkv ldfstllpgp fasllladmg advlrvespg rmdlvrvlpp hvdgtsasha
       61 ylnrnkrsig ldlkrqgare vvlelvreyd ivleqfrpgv mdklgvgyea lkaanprliy
      121 vaitgygqtg pyreraghdi nylalagvas ytgrrergpl plgvqladla ggslhgvmgl
      181 laavihrqqt gegqfvdism tdcafslngm agagylaagv epemealaln ggsfydyyrt
      241 rdgrwfsvgs lepqfmqqfc aaigrpelas rglspkpeeq ralkreieme fekrdfaewq
      301 avfaaldacv epllplseal ehpqlqargl vgrvpladgg sqaqmacpik fsaglpaprh
      361 igaalgadtv avleglgysa eriaelkaag aia
//
LOCUS       WP_181851609             107 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Pseudomonas aeruginosa].
ACCESSION   WP_181851609
VERSION     WP_181851609.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=11235
     Region          2..105
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawiylllag vfeivwatam kesagltrlw pslvtllfmv fsfgllavsm ktlplgtayt
       61 iwvgigavga falgillfge spsplrllav glivagivil klatrqg
//
LOCUS       WP_181851715             248 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudomonas aeruginosa].
ACCESSION   WP_181851715
VERSION     WP_181851715.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..248
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27462
     Region          29..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 msifrlalgc vgslallcas alaraetlvl ltenlvpfnm avnggnyakd dgisgistdt
       61 vraaceraqi ecqlilrfpw drvyqqalse pgygvfstar tperedrfkw vgplavndwv
      121 lmargdssih lnsledaary riggykndai sqhlvdrglq vqlalrdnen vdklasgqid
      181 lwvtadpsgr yvaqreglke vkvvqrfhta elflalnkdt pdelvqklqt avdalrsegl
      241 lkqirery
//
LOCUS       WP_181851539            2352 aa            linear   BCT 28-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181851539
VERSION     WP_181851539.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 2352)
  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..2352
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..2352
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=259328
     Region          4..>2072
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2077..2341
                     /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 drdpeaavrs wlrdafrhay pldgrslvdl
      121 allhsdqaly vyvrthhivs dawglqlfls rvragylgel gepqaqmpta sllaqletdn
      181 ysgseqyrgd rayfaealeg lepalftrrr paglrrtarh rltlertlld airdrgespf
      241 lflsaavaly larihqnddv vlgvpvlnra draakqvvgh fantlplrir tapeqtvdef
      301 laqlreatrt llrhqkmplg dllrgasplf dttlsymrwp aaqtipnasv etvaqthahd
      361 pdalaiwvse fdghsdaqvd feyacdvfda dfpmdaaalh ietflralve ggerrlgeld
      421 plsaaereel ihtrnatdqa fpeqatlptl faeqvartpq rtalleadgg tlsyaeldak
      481 vqavadalra agvsaderva llvargphll pailgvqrag gayvpinpdh plervrllle
      541 dcgarvvlvd eraatlgesl getrvlhler lpqstgdlpa anvapgdlay viytsgstgm
      601 pkgvmvehrs vvnrlnwmqr rypigerdvl lqktpvtfdv svwelfwwsf tgarlsllpp
      661 gaekdpreml rsiqrdavtv ihfvpsmltp fldlldgdpt artaasslrl vfcsgealap
      721 lqvarfrrlf gdavrlvnly gpteatvdvs dhecasdnpt rvpigrpidn lrlyvldral
      781 rpqplgavge lyiggvgvar gylnrpelna erfladpfva ggrlyrtgdl arwladgnle
      841 ylgraddqvk irgnrvepde vrdrlaalpg vrdaavvard savrgthlvg yyvaaaeldp
      901 gqlraglsat lpdfmlpaff vridslplsa ngkldrrqlp appeqvaava prtateaela
      961 avwadvlgva evgvhddfya lggdsilmlr iraaaqrrgl gfeladlmrn ptvaglaerl
     1021 vrplaersyq pfelvsevdk prlegledaf ptsrlslgll fhsrqrpdss vyhdvfhyrf
     1081 dlawdeaafr haldrvvaay palrssfdls gaseplqlvh tqarseplil dlrgnpeagt
     1141 vldehirqrr fhryslqqpg lflfaafvre dgldlvfsfh haildgwsva nlivalvaay
     1201 rgeplpgpap alachvreel aalaspaavg ywtgllegar mtrldgfgah epqaaqgpas
     1261 hretlpdgll erlkataaqr glplksllla ahcltlhlfs rsdsvvtgai sngrpelpda
     1321 drmvglflnt vpvrseiagh swievadalf rqerdghahr ryplsaiqqi vgdelssafn
     1381 yvnlhvlepl wqlrdfrvwe etnfallvnv iatpsdgmyl ridsdgrgis rsqaaligat
     1441 fvellwrlae hpdeaadfaf laprrdaasq peplvdvvsl ferqvealpg saalafeeqr
     1501 wtyrdldhva rcvatrlvra garrgdaigv alnrspemia tiwgilragl vcvpldvsyp
     1561 aqrlalilet aqpfrvvahp ehahvaaaer vlpveelvad iepetfaapq ldelamllft
     1621 sgstgrpkgv elshrmwany thwqlrvasg vpglrtlqfa plsfdmafqe ifstlcggge
     1681 lqlisnrerm dpsallhvle rrqvqrvllp fvalqrlaea sntlgvrpgs lrvvvssgeq
     1741 lritedvraf caampgllle nqygptethq vtyhslsgdp ahypdlppig rpldgvevqv
     1801 ldaalrpvpv gvtgelyfgg dclargyhra peltaerfve hpwrpgarly rtgdlgrilg
     1861 ngeivwlgra dtqvkvrgfr iepaevelai mrqaerqpgl rgaavvarer qgndaflaaf
     1921 llgepeavdl aelkqalrse lpehmvpahf awvdgfaltp sgkrddaalr alplehgtni
     1981 eylaprddye rtlagllgel ldrprvgird sffdlggtsl samrfmllie krygvdlpma
     2041 alietptveg laerlrersa vrafdplvpi raggsrpplf lvhplgghvl cylplvralp
     2101 pdqpvyalqa agtgqgstpl avlediaasy laairrvqpe gpyylggwsf ggfvayemar
     2161 qlraldpqav aqlivldsit vdrnhagsas dealllffyw elvwfersde eveplpegas
     2221 leqkldhive raieagvlpa gtpratvqrl yelfraswqa lidyrpevsd qdmtllradg
     2281 plplalkpmh daagthygdp kngwqhwtsg rldvidvpgd hlvlmkepyv etvaaeiaal
     2341 lepstssert rp
//
LOCUS       WP_181851807             391 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181851807
VERSION     WP_181851807.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 391)
  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 391)
  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..391
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..391
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42040
     Region          1..389
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mssferepgc glaehvdqvi eaafadqrlv gavvlvahrg qwlyrraagl adreagrimg
       61 edslfrlasv skpivsvaal slvdegrlal depiadwlpa frprladgre aritprqlls
      121 hsaglgyrfl eadadgpyar agisdgmdlp gfdlaenlrr lasvpllyep grawgyslat
      181 dvlgalverv dgrplaevlr qrvgipagmr dsgflcadac rlaavyvsdr prprrmagre
      241 tvapfedsvg irfepsrafe psayasggag migsagdvlr lleilrqgga plltpglaee
      301 mgrdqvpgle lpanpgfgfg lgfsvlrdpa iaqspeapgt wrwggayghs wfvdrarels
      361 vvaltntlfe gmsgrfvndl rdavyrsael r
//
LOCUS       WP_181851956             231 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Klebsiella pneumoniae].
ACCESSION   WP_181851956
VERSION     WP_181851956.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 231)
  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..231
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=26678
     Region          <165..217
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mfdiayvsll nflmtcevii mrgcnceikc iacglncrie aknkiertlc gekkfsvwpd
       61 rnyffkravn dlvfreltcf vpegivvvdf slgnilyfln ecwtrklrds glkiiliadk
      121 nmlpmanfwr lrsgfswavv evnsdlsnli nkikrvmlgr nllcrrtpsl tehemktlcl
      181 laeghssqdi arimacdtrs vyrfqyslck kfgglnrlrn lhfrhtipal d
//
LOCUS       WP_181851896             270 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Klebsiella pneumoniae].
ACCESSION   WP_181851896
VERSION     WP_181851896.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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..270
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..270
                     /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=28930
     Region          54..270
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mrrdvllllc sfyllplgah addsglsakd iktlffghdd rkavnrpees pwdaigqlet
       61 asgnlctatl isphlaltag hclltpprgk pdkavalhfi srkgnwvyei hgidgrvdps
      121 lgrrlkadgd gwivpsaaap sdfglivlry apsgitpipl fpgskadlta alkaadrkvt
      181 qsgypedhld nlyshqdciv tgwaqtsvls hqcdtlpgds gsplllkted gwqviavqss
      241 apgpqdrwra dnraiavtgf rdklealage
//
LOCUS       WP_181851921             524 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Klebsiella pneumoniae].
ACCESSION   WP_181851921
VERSION     WP_181851921.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae 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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=56254
     Region          41..520
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 msvlslslgk ktgrlperrr pafpmvalal lfsllallpl gfvvavgfdt gwptikalvf
       61 rprvgellsn tlwltvvavp isivlgvtla wltertalag rqlwsalava plaipafvqs
      121 yawvsavpsl hglsagvfls vlayypfiym pvvavlrrld ptledvaasl gtppwkvffr
      181 vvlpqlrlai cggallvalh llaeyglyvm irfdtfttai ydqfqstfsg paanmlagvl
      241 alcclailll esasrgkary arigagaare qkrlvlgkga afgaqlllll lvmlamgvpl
      301 lvlcrwlwlg gidnwlhadl whslrqtlll gaggallttv calpiawlgv ryprplfrll
      361 egcnyitssl pgivtalalv tvtihyarpv yqtevtlfla yllmfmpral inlragiaqa
      421 pvelenvars lgrsparalw sitmrlaapg aaagaalvfl gvsneltatl llsplgtrtl
      481 stgfwaltse idyvaaapya llmivislpl tavlymqskk magl
//
LOCUS       WP_181851902             342 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Klebsiella pneumoniae].
ACCESSION   WP_181851902
VERSION     WP_181851902.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=36357
     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 mmndyrrivr rrlllillla llivasllld fmlgpsglpl qslwqtltdp asadpgtrai
       61 vwdirlpyav maiivglalg lagaemqtil nnplaspltl gvssaaafga alaivlgigl
      121 pgipgqwfis anafifalla allldgitrw tqvatsgvil fgialvftfn alvsmlqfia
      181 nedtlqglvf wtmgsidras wskvaillva lalvmplslr sawkltalrl gedraisfgi
      241 nvrrlrlttl lrisilsals vafvgpigfi glvaphiarm lfgedhrfyl pasaligalv
      301 lslasiaskn lipgaiipvg ivtslvgvpf flsiilrhrg qv
//
LOCUS       WP_181852259             414 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181852259
VERSION     WP_181852259.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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..414
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..414
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45754
     Region          92..413
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrscisvfrp allalfvsas gsagadaave nprigraadl yelipeyqpd tyrnmdkvyp
       61 trvihkgtkv rplpagvaia pryriggeey gvddfmrrnr vggvlvlkdg kvaleryglg
      121 ndertrwtsf svvksisstl vgaavqqgll aldqpvdkyl pslagsayqg vtveqvlqms
      181 sgvrwnetyr dpksdrrqmf daqlaerpgg ilrllaslpr qypsgthfty stgeshlqse
      241 llhaatripv sdylseriwa rmgmesdgfw qlespagqei gssglsatlr dygrfgqfvl
      301 edgvidgeri lpegwvdras rveasshlap gklydgeyal gygyqwwtfp vgakalpeyd
      361 ggafeaqgif gqylyinrke kivavvwsaw pkpemddree etyaflgaav kalr
//
LOCUS       WP_181852344             760 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudomonas aeruginosa].
ACCESSION   WP_181852344
VERSION     WP_181852344.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 760)
  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 760)
  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 760)
  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 760)
  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..760
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..760
                     /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=86256
     Region          86..749
                     /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 msprlsalrl slaylaiaia waflsdhllq nqvqdhdqlv fwmtakrlff faatglllyl
       61 ylvrqfrrka qaydelhgse qrlnraleav rdglwdwdlv tdrmfvspgy aaliglapee
      121 lgdpietwkk rlhpeeyatv leahrnhlqg ltdnldhiyr lrhkdgdyrw ihsrgrvlrd
      181 algkplhytg varditlqrl kedhlrqaaa vfdstregvl vtdaqavivh vnpsferitg
      241 yrsedvlgkt pailrsgrqd qafyqrlwla lreqdvwsge iwnrrksgei ypqwlhirvv
      301 rndqgqlthy vgvfsdlssi krseneldfl ahhdsltglp nrvllrerie qalengkdrt
      361 vagalllidl dlfkhindsl ghttgdmllk evskrlqhql dercllsrlg gdefailven
      421 ddpeavarls qrildgfnap fdihcqpiyi saslgvslyp edasdvdhlm qhadaalfqa
      481 kdsgrnayaf ytrvltarar ahvqvesalr haldhdelrv hyqpvhdlas grivgveslv
      541 rwqhperglv ppgefvpvae ecgliaaldn wvlkracrqm rewqqrgvel efvavnvssr
      601 lfnrggleer ianaleesgl eprylelevt esavmedfeq slnllcrlri lgvnlaiddf
      661 gtgysslmrl krlpvhklki dqgfvaglpg avddaaiara ivalaqsmgl rvvaegiehq
      721 dqalflrehg cdfgqgywyg rpqpaealrf dlppvslped
//
LOCUS       WP_181852417             144 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            globisporus].
ACCESSION   WP_181852417
VERSION     WP_181852417.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 144)
  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..144
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..144
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=15153
     Region          38..>77
                     /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 mtiratnqad viplrplpta adpapqdlpr eplwrdlvge vlrrerraqg rtlkdvseas
       61 rismaylsev ergrkeasse vlaaaaqalg lsladvlala gerlvsltaa rtrtrsrslg
      121 ttgghrpvrt tgpagpmggv llaa
//
LOCUS       WP_181852458             569 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces globisporus].
ACCESSION   WP_181852458
VERSION     WP_181852458.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 569)
  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 569)
  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..569
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..569
                     /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=58386
     Region          191..525
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkamkavqvl rrpwtlrtrl vvsavsliav vaavigsvta iafhsymygk lddqlhsvve
       61 raqrlpgplp lpdslreagp lgfvggggqp lgtfgalvdg dgdvtaskvv edgglraqes
      121 akpltgeqrt alenaapgag dgtrsvdlpg lggyrveatt taegdtvlvg ipsaevsgal
      181 ttlivvevcv taagliaasi agtvlvgvam rplrrvaata trvselplhr gevallervp
      241 daeadprtev gqvgaalnrm lghvgsalva rqesetrvrq fvadashelr tplasirgya
      301 eltrraaggt agpepdpvtr halgriesea drmtglvedl lllarldagr plsygttdll
      361 plvvdavsda raadgtgaeg pdtgpgdarh hwrlelpeaa epvtvradpd rlqqvlvnll
      421 anarthtppg ttvtvsvqps vraggpvtle vrddgpgipa ellphvferf argdasrarg
      481 adgggatgst glglaivqav vsahggrvrv esapgrtvfa velpadavpm davpmdgvst
      541 davstngvpa ghgmirvdsq agdrlttpv
//
LOCUS       WP_181852481             288 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase/citrate lyase family protein [Streptomyces
            globisporus].
ACCESSION   WP_181852481
VERSION     WP_181852481.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces globisporus
  ORGANISM  Streptomyces globisporus
            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..288
                     /organism="Streptomyces globisporus"
                     /db_xref="taxon:1908"
     Protein         1..288
                     /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=29930
     Region          19..288
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
ORIGIN      
        1 mtgcdapfpp lpedpqdapg rppltwlyvp gdrpevvaka lgsgadvviv dledavaper
       61 keyarsatae llgdqvtaap davpvhvrvh geddiralag lpglaafrlp kithavsvhh
      121 vaavapgvpl ypllesalai ehaysiasah havrgialge adlradlgvr edagldwprs
      181 rvvvaaraaa lpppvqsvfp dvrdldglwa scvrgrglgl lgraaihprq levierafrp
      241 taeeieaaeq ivaasaveag alalpdgrfv daavvasarr tialagra
//
LOCUS       WP_181852181             774 aa            linear   BCT 28-DEC-2024
DEFINITION  LTA synthase family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181852181
VERSION     WP_181852181.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 774)
  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 774)
  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..774
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..774
                     /product="LTA synthase family protein"
                     /EC_number="2.7.8.-"
                     /GO_process="GO:0070395 - lipoteichoic acid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=85788
     Region          56..525
                     /region_name="MdoB"
                     /note="Phosphoglycerol transferase MdoB/OpgB, AlkP
                     superfamily [Cell wall/membrane/envelope biogenesis];
                     COG1368"
                     /db_xref="CDD:440979"
ORIGIN      
        1 mrplsrwlss cgsllalaal flvvplagry wlgwstpfgy lsdlalgsll vlllhrrslw
       61 falpvmllwc lflignaelv gavgrmpeps dlkylldpqf vssstqgggl ahlplalglg
      121 gatllcvllw rrrgprlpry ayalpaafla ahvglqylrp sdadqwqqyn lphkllasal
      181 ssgqlavedw laddrpdtpp dvaglnqldl sgtpllaggg rarnvlivam egipgayiaa
      241 nraainssyh eapmprlsgw aeramttpdy vlhshqtirg lyamlcgdys kldsgtpkgv
      301 ellnnparar eclpaqlrqh gfsthflqga glrfmakdkv mpqmgfdktl grdwfrntsy
      361 lefpwgmddk affegaatyv kqlrqqkkpw mltlltvgth qpysapadyl arypsakqaa
      421 vaylddaida fladlekqgv lrdtlvvlts deshgvdqvr lasawgfnlv lapeqaalpp
      481 iksgvyghvd laasvldyfg yrvpagisgr slfrdyasgr emmsytngml rhhdgkdtfv
      541 ecdfqqicrr yrsegfiade aeflgrfsgr qarlvsqraa vldhsvqqag qlgqefqfat
      601 herirlkpet hndwtdnlig aqylempkns rttvtlkira lqmdrngarv tlktkeferd
      661 vpipvpdipr llkgkpldms ftfdnpeark afsfhllaeg rgiieisdfh vvtaanpepv
      721 esrsqvaeaa keqpllrtlk slfanrpete eaeradapre rtvipeqkal ilsh
//
LOCUS       WP_181852658             480 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181852658
VERSION     WP_181852658.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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..480
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..480
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51301
     Region          2..462
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mtqgsdskpl ierrsidyip anerhgrlys qftlwlganl qitaivtgal avvlggdvfw
       61 slvglligql lggavmalha aqgprlglpq missrvqfgv ygacipialv clmylgftat
      121 gtvlsgqaig qltglsdsag ififaafivl vtvlgyrvih iigrivsvlg iiafaylfsr
      181 lmllsdigdl lairhfswas fllavslaas wqiafgpyva dysrylpast sswktflavg
      241 lgsvlgaqas mvlgvfsaal angqfagrev ayivglgssg tvaallyfsi afgkvtistl
      301 nsygsfmcia tiissvrgql eitrvqrlff vlaivgastl iallgqhsfl aafksfilfl
      361 ltfftpwsav nlvdyyfitr erydvpalad pdgrygrwnl pgiavytlgv lvqmpflatt
      421 lytgpmvehl ggvdiswiig llvpavlyyl varrkatrqa parmilpadp gafehpahga
//
LOCUS       WP_181852843            1217 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Nostoc sp. ATCC 53789].
ACCESSION   WP_181852843
VERSION     WP_181852843.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. ATCC 53789
  ORGANISM  Nostoc sp. ATCC 53789
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 1217)
  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 1217)
  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 10353476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1217
                     /organism="Nostoc sp. ATCC 53789"
                     /db_xref="taxon:76335"
     Protein         1..1217
                     /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=139754
     Region          114..>213
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
     Region          <776..973
                     /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"
     Region          1033..1142
                     /region_name="Methyltransf_24"
                     /note="Methyltransferase domain; pfam13578"
                     /db_xref="CDD:433324"
ORIGIN      
        1 mnnasienql nqanqyfnnq qfseaiklyk aifrdnpqla kqglsislah clllsvnwqe
       61 isanlipgtn yleisgwlns lsqgkpvnaq nlpipwytyp aiefledkik rdfsvfefgg
      121 gqstlwwadk vqqvisiesd egwfnqiyqq mplnvqlkle ldeqkyadfi lqypdkyfdv
      181 ivvdginrng clensldklk qngllifdnt ddhrydsslr llsslgykki dfwgfipgyv
      241 yknctslffk steiletnsl psekksvlgk scmqitspka temsnyeyed nwqlttpvaf
      301 lifnrpettt rvfeairqak ppkllvvadg aradklaeae kcaatraiin qvdwecevlt
      361 nysdvnlgcr krissgldwi feqveeaiil eddclphptf frycqellek yrdderimmi
      421 sgdnfqfgsn rteysyyfsr yghcwgwasw rrawtkydds mqlwtelrdn nwlnevlqne
      481 qavsywskif qgvydgfntw dyiwqytlwi nnaltilpni nlvsnigfgs gthtttdnnk
      541 lgnmtveavk fplkhplfmi rntqadnfte etifssaank mklkpeyyis leeiitkvnn
      601 nqnkvvldsi yssireynai nyvkavalar qgkitealat letllnhapa htkgiilrke
      661 lrknldsdtt avhpiiekan nlleenqiag cfeilndska lkqpimgldf lrakcflqmr
      721 qpaasiqslr eelryfpenn qaenflnqll nqypefvssn iqdsefqely rliqpytmls
      781 earlyslftl ikriclenip gnfvecgvag ggstalaaav ikrhtrqprw vyafdsfdgm
      841 paptekdksn gilaevtgwg tgtcaapets vkeicnklgv gdivqlvkgy fedtlpkmrd
      901 rvgmiaflhm dgdwyestkt iinnfydris ndgfvqvddy gfwegcrqal hefeaerqlk
      961 felhqidstg vwfncphkfs inpvfeksli eefdqddpvk ygiqsqmskn erfqlyyavr
     1021 kllptnsspc rfveigsfag sslflnqkal vrehndlegw aidpglhpql klvldnllsk
     1081 ithlrmfshd alaqlqtife rdhnyppyif vdgdhsyegv krdianyypl lapgglmifh
     1141 dylppldeqn sssilfhhgg nepgirqacq elmentyhce iielpllypd dptqtqaylp
     1201 iipgvlsslk iyrkpsn
//
LOCUS       WP_181852987             702 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181852987
VERSION     WP_181852987.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 702)
  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 702)
  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 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
REFERENCE   4  (residues 1 to 702)
  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..702
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..702
                     /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=78767
     Region          9..638
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mpiasrapvs ltllallfgs klaaadlfnd psgvpevlta trlkqspaev pgsisvldre
       61 livasgardi pelmrlvpgm mvgylsgnqp tvnyhgtsms garrlqvlid grsvyrpgla
      121 svdwsdlpla ledverievf rgpntvsyga nalmgvinii trapgespgt rlkytagqrg
      181 irdwyasqsi aledsdfrls lsgqeddgfd hdhdghalrd grrlsrfnln ashslapnqs
      241 lewqlaakeg snqhpyayrs pfpqvpddvd nsdtlahdya gslrwnvdld prhsfyiqgy
      301 aqhwerrqew naceagiafs pqlaqlweln pdylrrfadd ptrlppgsaq elqlatqvld
      361 qlrngglrpv cgrvdrnire srydlemqdt lslgdnlrll nglsyrydqa nsetfyggrv
      421 ssqiwrlfsq lewhagehwl lqgggmledv egsgssfspr lavnylfnpq hslravysea
      481 vrspgmyend vdwryrvrhl tpapygqsea yyfasahgpg dlgkehtrsr eigyngffre
      541 tglamdvrlf heeitglisd plsvvdfspd ngdrirfsga egqldwrlgl rdrlratyay
      601 ldydatsryd rrltarhggs agwmhdwgqg wssalfyygd dslnghrfer vdlrlakrip
      661 lgkaalelag vlqqrlddqp ltfpdnryds rhllyfgaev tf
//
LOCUS       WP_181853055             345 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Klebsiella pneumoniae].
ACCESSION   WP_181853055
VERSION     WP_181853055.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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..345
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..345
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39943
     Region          3..215
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mstplvsvil pafnaemflr esissilnqs lknielviin dgstdstedi iksfsdnriv
       61 ylkntinlgi iktlnkgidn akgkyiarmd addismpnrl krqievlend esidivnika
      121 yilndsgtfy tknkgsveas sntmrylqyl rnmimhpgvm vkkdimqhfk yrdseevlhi
      181 edydlwlrlf kagykcftid dellyyrfnp nsisrtkqne qhnrvialsa knikndfsfe
      241 fsvdslkynw gefdsfkyfs ldryhkelra ffdkinqdgs lgpsdmavfe rfisfkmlav
      301 lisfiklggi rgkviaasfl lrnmniiprf flltnifskk kkfin
//
LOCUS       WP_181853322             283 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudomonas aeruginosa].
ACCESSION   WP_181853322
VERSION     WP_181853322.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..283
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..283
                     /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=31212
     Region          49..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 mrsdlheanr lswnaatrah nshkadqaaf frnggstlyp eelqllghld glrllhlqcn
       61 agqdslslar lgarvtgvdi adsaidfarq lsrdsgiaad fqrddilrwl pvaatrgerf
      121 ervfasygtl vwlsdlkrwa dgiaqvlfpg grfvlvefhp falyfdphwq paydyfsrep
      181 iaesgvsdyv aesgaslaps gyragvenfs nphpsyefqw gladvigall gaglqlerle
      241 eypyangwag fdgmrdgggg rmlppadrpr lplmyglsar kpr
//
LOCUS       WP_181853545             446 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Pseudomonas aeruginosa].
ACCESSION   WP_181853545
VERSION     WP_181853545.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=46648
     Region          23..430
                     /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..155,158,260,263..264,267..269,272,299,303,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mnrqsaaavi daarfnrthw lilgwgcfim lfdgydmviy gsvvprlmqe wqlspvqagt
       61 lgscalfgml fggtllapla drfgrrrlvi attllaslaa fltghardpl elgagrfftg
      121 lalgalvpsa inlisefapa grrstlvtvm safysvgavl sallaiamip awgwqsvfyv
      181 avlpvlavpl mlrwlpesaa flelkgrrae ldallrkvdp dyrpgaeran avaaeapsgr
      241 vaqlfegrqa vgtlllwvaf amcmlmsygl ntwlpklmag ggyalgssla flvtlnvgat
      301 lgalfggwla drlgagrtlv lffalaaasl aalglgpgpw llngllvvag attigtlavi
      361 hayaaqfypa wvrstgvgwa agvgrlgaia gpmlggslla lelpfeqnfl afaapgviga
      421 laiacihlrp rvpaeasvda takkpl
//
LOCUS       WP_181853422             119 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family transcriptional regulator, partial [Klebsiella
            pneumoniae].
ACCESSION   WP_181853422
VERSION     WP_181853422.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 119)
  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 119)
  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 119)
  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 119)
  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 119)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (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   7  (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
REFERENCE   8  (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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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 both ends.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         <1..>119
                     /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          44..103
                     /region_name="MarR_2"
                     /note="MarR family; pfam12802"
                     /db_xref="CDD:432797"
ORIGIN      
        1 akeskknktl visetkenrf ksisegveyv hlfpknlkvl ikkyglntne llvlteimes
       61 mlshgnllin fsqktlcelt einkstmskt fkslkqkqcl ieknghiyln svifmkglp
//
LOCUS       WP_181853797             244 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CobW family GTP-binding protein, partial
            [Klebsiella].
ACCESSION   WP_181853797
VERSION     WP_181853797.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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 the amino end.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         <1..244
                     /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          <3..221
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 gtrgveslla eqimfcnkll ltkndrlpfy vvtevaraih plnpqvaima vpwgnlqlde
       61 llsmpdydfh rvallidelq daidavlsde pdkkydiswr vieddrpfhp qrlwdtchrf
      121 mgagvyrskg ffwlpgrddl allwnqaags inlefisywk agvlthtdns ltkeeraair
      181 qqlakmpgrf gdrrcrltvi gesgeiddfa lalrqcllte eeilwwqqgg ifhdpwptkv
      241 arla
//
LOCUS       WP_181853956             401 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pseudomonas aeruginosa].
ACCESSION   WP_181853956
VERSION     WP_181853956.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=45308
     Region          3..401
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mgkltsktve siakaatpgk tndgdglyfq vsksggtswi frykldgrsr emglgpfpai
       61 tlsqarqlaa dqrkllasgs dplatrdaak eakreaerqa aarrttfedi areyqqahgg
      121 swsekwrkgw lrklelyafp tmgklsadii stehvlaalq piwitktrta devrgqieqi
      181 ldaakarrlr egdnparwrg hldnllskae kkkarqrqhf palqwkdtpk listlanidt
      241 rdaiatrlli ltgaryhmiq haqwpefdle agtwalpaer mkmrkpfvip lppqvvemlk
      301 dinkthsayl fpgqgksgvm hgnavrnllh klghaditrh gfrstfrdwa nectnyprev
      361 celalahder dqteaaysrs dllekrrslm aewaefctsq k
//
LOCUS       WP_181853812             493 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Klebsiella pneumoniae].
ACCESSION   WP_181853812
VERSION     WP_181853812.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=53941
     Region          20..489
                     /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 mtamsklnpi lagsaqsvea yqqvieqtsq avvqwlkqpe myqgksvdel rerislefne
       61 qglgnqaaid raieyflkds lsvhhpqcva hlhcpslvis qaaevlinat nqsmdswdqs
      121 psatiiemkl iewlrarvgf pagdagvfts ggtqsnlmgl mlardaffar qghsiqqdgl
      181 pgdirkykvl csenahfsvq knmalmglgy rsvtlvktde farmdvsdlq akiaqaqang
      241 eqimaivata gttdagaidp lrdiagiaae hqiwlhvdaa wggalllseq yrdyldglel
      301 vdsvtldfhk qffqtiscga fllkdarhye lmryqaayln sefdeehgvp nlvskslqtt
      361 rrfdalklwm glealgqkqy aaiidhgvtm aknvaeyvks qptlelvmqp qlasvlfrsr
      421 paqmagsdaa aiallnqrvg dallasgran vgvtehngvt clkltllnpv vtlddvkvll
      481 nlvertaqel laq
//
LOCUS       WP_181853961             424 aa            linear   BCT 28-DEC-2024
DEFINITION  CynX/NimT family MFS transporter [Pseudomonas aeruginosa].
ACCESSION   WP_181853961
VERSION     WP_181853961.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (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   2  (residues 1 to 424)
  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 424)
  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 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   5  (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 13023805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..424
                     /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=44352
     Region          54..413
                     /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(54,57..58,61,93,142..143,145..147,150,169,172..173,
                     176,244,247..248,251..253,256,283,287,336..337,341,345,
                     362,365..366,369..370,373)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340897"
ORIGIN      
        1 mthalnarpg ahpghppeel lidaevddep appapplrpw llllglvlva lnlrpalssl
       61 apllnqvrdd tglsaaaagl lttapvlclg lfaplaprla rrigaersvl lilfclaggi
      121 vlrslfpvfg lfagsvlaga sigiigvllp givkrdfprq agvmtgvytm alclgaalaa
      181 gatapleklf gnwemalafw slpailaaaf wlpqtrqgqh ahrqafrvvg lwrdplawqv
      241 tlymglqssl ayivfgwlps illdrgmtav eaglvlsgsv mlqlitalla pwlaarardq
      301 rlavvlvmat tlagllgfly aplptiwgwa vllglgqggt fsialalivl rsrdahvash
      361 lsgmaqgvgy tlaamgpfmv gvvhdltggw navgyifigv aiaatlfglg agrsqyvgar
      421 sehl
//
LOCUS       WP_181853987             402 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Pseudomonas
            aeruginosa].
ACCESSION   WP_181853987
VERSION     WP_181853987.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 402)
  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 402)
  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 402)
  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 402)
  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 402)
  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..402
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..402
                     /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=45056
     Region          13..>218
                     /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          183..>363
                     /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(186,188,190,197..199,201..202,230,240,242,244,246,
                     295,297,299,301,303,312..313,315,317,323,325,327,329,
                     341..345,356..357,360..362)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176888"
ORIGIN      
        1 mseyietdda syfrvrrqay vsaelhrrel heifddswly aahlselrep gdfitrdvgg
       61 rnliiqrrvd gepavylnac ahrgakvcae rqgnsqrftc pyhgwtydsh gsliglpdka
      121 ayqhagqchp elsltrvkha vyrnflfihy garqaslety lgqakdyidl icdqseaele
      181 iipggfehsi kanwkllaen gvdayhlpfa hkryleylns lgtdpeshkr hgrgealgng
      241 haliisgpps tgrpiaywsp lfpealkpsi aakferlver fgqaraedia htnkslfifp
      301 nlvindilgl nirsffptaa devsvtvwga gfadetreer aaringlisf igpggfgtpd
      361 dvecsaarns saccainptr lvfqwwkrnf riarrvppgy pn
//
LOCUS       WP_181854123             405 aa            linear   BCT 28-DEC-2024
DEFINITION  ANL family adenylate-forming protein [Pseudomonas aeruginosa].
ACCESSION   WP_181854123
VERSION     WP_181854123.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 405)
  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 405)
  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..405
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..405
                     /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=44579
     Region          56..392
                     /region_name="AFD_class_I"
                     /note="Adenylate forming domain, Class I, also known as
                     the ANL superfamily; cd04433"
                     /db_xref="CDD:341228"
     Site            order(60,63..68,70..71)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(63,181..182,203..208,286,298,301,312,390)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(63,103..104,154,156..157,160,181..182,203..208,286,
                     298,301,309..312,370)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(103,156..157,160,181,309..311,364,370)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
ORIGIN      
        1 mlidpewgea akqaivdemr lealasehpl egalaglrla ldfersatrr ldraahshmi
       61 lftsgttgqp kgielsqqam lhayrigrdc lgigehtrsg cfyrisglgi lginflfpll
      121 yggsavllpl hcwadsegfw eyverfgisf lylvppvvnh mvkegspppr rlplqrllcv
      181 agsarldadl qaafqrdyaa laniyglsec gfaflfgkrr gdafdnsvgp avglelkltd
      241 pdgrplegsg ergrlwvrtp slfsgyvnrp dltaqvledg wlntqdlayf dedrcvhvlg
      301 rcdgtinkgg nlfhlnecer alngldevid vcclkvdcpl ygedyvavih tapqvefafl
      361 pwlqqqlgtl rapqrvvlsh qalplngagk hdrralatll qreas
//
LOCUS       WP_181854177              91 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181854177
VERSION     WP_181854177.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 91)
  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..91
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..91
                     /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=10238
     Region          3..>86
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mlsckelvar ssdfldgqld frgqlavrsh llmcrhcrrf irqmrltqat vrhlpegqgp
       61 eldrlaahls elrkcsavrn laricainda p
//
LOCUS       WP_181854308            2352 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: amino acid adenylation domain-containing protein
            [Pseudomonas].
ACCESSION   WP_181854308
VERSION     WP_181854308.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 2352)
  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..2352
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..2352
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=259388
     Region          4..>2072
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2077..2341
                     /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 pyqwldtdae fearhvdlra drdpeaavrs wlrdafrhay pldgrslvdl
      121 allhsdqaly vyvrthhivs dawglqlfls rvragylgel gepqaqmpta sllaqletdd
      181 ysgseqyrgd rayfaealeg lepalftrrr paglrrtarh rltlertlld airdrgespf
      241 lflsaavaly larihqnddv vlgvpvlnra draakqvvgh fantlplrir tapeqtvdef
      301 laqlreatrt llrhqkmplg dllrgasplf dttlsymrwp aaqaipsasv etvaqthahd
      361 pdalaiwvse fdghsdaqvd feyacdvfda dfpmdaaarh ietflralve ggerrlgeld
      421 plsaaereel ihtrnatdqa fpeqatlptl faeqvartpq rtalleadgg tlsyaeldak
      481 vqavadalra agvrtderva llvargphll pailgvqrag gayvpinpdh plervrllle
      541 dcgarvvlvd eraatlgesl getrvlhler lpqstgdlpa anvapgdlay viytsgstgm
      601 pkgvmvehrs vvnrlnwmqr rypigerdvl lqktpvtfdv svwelfwwsf tgarlsllpp
      661 gaekdpreml rsiqrdavtv ihfvpsmltp fldlldgdpt artaasslrl vfcsgealap
      721 lqvarfrrlf gdavrlvnly gpteatvdvs dhecasdnpt rvpigrpidn lrlyvldral
      781 rpqplgavge lyiggvgvar gylnrpelna erflvdpfva ggrlyrtgdl arwladgnle
      841 ylgraddqvk irgnrvepde vrdrlaalpg vrdaavvard savrgthlvg yyvaaaeldp
      901 gqlraglsat lpdfmlpaff vridslplsa ngkldrrqlp appeqvaava prtateaela
      961 avwadvlgva evgvhddfya lggdsilmlr iraaaqrrgl gfeladlmrn ptvaglaerl
     1021 vrplaersyq pfelvsevdk prlegledaf ptsrlslgll fhsrqrpdss vyhdvfhyrf
     1081 dlawdeaafr haldrvvaay palrssfdls gaseplqlvh tqarseplil dlrgnpeagt
     1141 vldehirqrr fhryslqqpg lflfaafvre dgldlvfsfh haildgwsva nlivalvaay
     1201 rgeplpgpap alachvreel aalaspaavg ywtgllegar mtrldgfgah epqaaqgpas
     1261 hrealpdgll erlkataaqr glplksllla ahcltlhlfs rsdsvvtgai sngrpelpda
     1321 drmvglflnt vpvrseiagh swievadalf rqerdghahr ryplsaiqqi vgdelssafn
     1381 yvnlhvlepl wqlrdfhvwe etnfallvnv iatpsdgmyl ridsdgrgis rsqaaligat
     1441 fvellwrlae hpdeaadfaf laprrdaasq peplvdvvsl ferqvealpg saalafeeqr
     1501 wtyrdldhva rcvatrlvra garrgdaigv alnrspemia tiwgilragl vcvpldvsyp
     1561 aqrlalilet aqpfrvvahp ehahvaaaew vlpveelvad iepetfaapq ldelamllft
     1621 sgstgrpkgv elshrmwany tqwqlrvasg vpglrtlqfa plsfdmafqe ifstlcggge
     1681 lqlisnrerm dpsallhvle rrqvqrvllp fvalqrlaea snalgvrpga lrvvvssgeq
     1741 lritedvraf caampgllle nqygptethq vtyhslsgdp ahypdlppig rpldgvevqv
     1801 ldaalrpvpv gvtgelyfgg dclargyhra peltaerfve hpwrpgarly rtgdlgrilg
     1861 ngeivwlgra dtqikvrgfr iepaevelai mrqaerqpgl rgaavvarer qgndaflaaf
     1921 llgepeavdl aelkqalrse lpehmvpahf awvdgfaltp sgkrddaalr alplehgtni
     1981 eylaprddye rtlaglfgel ldrprvgird sffdlggtsl samrfmllie krygvdlpma
     2041 alietptveg laerlrersa vrafdplvpi raggsrpplf lvhplgghvl cylplvralp
     2101 pdqpvyalqa agtgqgstpl avlediaasy laairrvqpe gpyylggwsf ggfvayemar
     2161 qlraldpqav aqlivldsit vdrnhagsas dealllffyw elvwfersde eveplpegas
     2221 leqkldhive raieagvlpa gtpratvqrl yelfraswqa ligyrpevsd qdmtllradg
     2281 plplalkpmh daagthygdp kngwqhwtsg rldvidvpgd hlvlmkepyv etvaaeiaal
     2341 lepstssert rp
//
LOCUS       WP_181854690             459 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Klebsiella pneumoniae].
ACCESSION   WP_181854690
VERSION     WP_181854690.1
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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..459
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49891
     Region          3..452
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mserrsidyi peserhghpf sqftlwfggn lqitaivtga lavvlggdvv wslvgllvgq
       61 mlgaavmslh alqgprlglp qmilsraqfg gfgavvplvl vcvmyigfsa sgtvlagqam
      121 akllnishva gmlifsaiii viavlgykvi hklgklasiv gilafvymfi tlllsadlsa
      181 lahnnhfslp tfllavslss swqiafcpyv sdysrylprd vsatktwcsv ffgtvlgtqt
      241 smtlgvltaa iagsafpghe vsylvglgks qamamviyfa icfgkitftt lnaygsfmsl
      301 ttivsafrrq tvlsqkcria fvvlmvtasc iiallsepaf lkhfthfllf llaffvpwsa
      361 icltdyylis kgaidipals dpqqrygfwn lyaitlyivg vliqlpfien plfhgsltwi
      421 fagndvswii gwfgtgvlyy alrrfdrrsl paqslfpst
//
LOCUS       WP_181854768             393 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudomonas aeruginosa].
ACCESSION   WP_181854768
VERSION     WP_181854768.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 393)
  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 393)
  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..393
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..393
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45421
     Region          1..392
                     /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 mllnlfnemr aakvpvsvre lldlidalkh rvvfadmdef yylartimvk derhfdkfdr
       61 afgayfkgle klddhlksli peewlrkefe rlltdeekaq iqslggldkl ieefkkrlee
      121 qkerhaggnk wigtggtspf gsggfnpegi rvgdagkrqg kaakvwdqre yknlddqvel
      181 gtrnikialr rlrkfarega aeeldidgti dhtakdagll niqmrperrn tvkllllldi
      241 ggsmdahvkv ceelfsackt efkhleyfyf hnfiyesvwk nnlrrssert atfdllhkyg
      301 pdykvvfvgd aamapyeitq aggsvehwne eagyvwmqrf mekdkkliwi npypkdtwny
      361 tastglvrel vkeqmypltl sgleegmrfl srg
//
LOCUS       WP_181854145             515 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 1 protein [Pseudomonas aeruginosa].
ACCESSION   WP_181854145
VERSION     WP_181854145.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 515)
  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 515)
  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..515
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..515
                     /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=58435
     Region          48..498
                     /region_name="BglB"
                     /note="Beta-glucosidase/6-phospho-beta-glucosidase/beta-
                     galactosidase [Carbohydrate transport and metabolism];
                     COG2723"
                     /db_xref="CDD:442035"
ORIGIN      
        1 mkirrsllqf knfrktlkkn iknrlallsl allydtslat akpqencnfl wgtasaayqv
       61 eggwnldgkg psnwddfthr gitkyliges htgdvatnqi srdvylkdid lmrklgvnsy
      121 rfsiswarvl pdgqtinpkg leyykiliqd lkeagitpiv tlyhwdmpla lykkggwyss
      181 kspdwfagya klifsnfgee vpyfitfnep egniftltpl venfltetps pyekvlsves
      241 raaqaeamhn lllanslavt sykeagykgr igialnlspc vdnenpnsaa krncnsvhna
      301 wvldalykgn ypkdiktlyq kyapafqpsq ddmkkimqgr pdfigvnfys ptlvkddpsq
      361 pfgianrpnp dqypsyngpv spshlvellm qidkeydhpt liitengagf gvddeklten
      421 rvldplraky lsdhidavls arhagvkveg ylfwslldnf ewlfgyrnrf gmigvdfesp
      481 qlartpkssy ykyqekirdy kernkclpqq srhsg
//
LOCUS       WP_181855222             171 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Winogradskyella sp.
            KYW1333].
ACCESSION   WP_181855222
VERSION     WP_181855222.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella sp. KYW1333
  ORGANISM  Winogradskyella sp. KYW1333
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Winogradskyella sp. KYW1333"
                     /db_xref="taxon:2282123"
     Protein         1..171
                     /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=20032
     Region          <77..168
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 meilfsiiys lipfslvyli glngfyqfei fsgissnyfi dnfnknmfvq skkqskndfe
       61 qfkqtiiier lyakknltly dlsialkmkk rvisilindn tdttfyhfin qlrikefkkh
      121 liedehqkft lfglaqevgf sskstfytsf ksiegmtpkq yqsklkksvs t
//
LOCUS       WP_181855295             245 aa            linear   BCT 28-DEC-2024
DEFINITION  glycine-rich domain-containing protein, partial [Pseudomonas
            aeruginosa].
ACCESSION   WP_181855295
VERSION     WP_181855295.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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 10008452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..>245
                     /product="glycine-rich domain-containing protein"
     Region          31..160
                     /region_name="COG4278"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443419"
ORIGIN      
        1 mallgitlla gaafvggyly rrgldrrryr fiqqfrlppr vtqavreryp qlseeqvqrv
       61 lgglreylll craagkrmva mpsqvvdvaw helilhtrly qhvcrkglgr flhhtpaqam
      121 rsprqaqegi qrawklacrr egidplnptr lpllfaldte laiadgfrya lncaqrqdgg
      181 aavycashig cssgcasdsg stfgsdgqds rhgcggdsgg dggsgcgggg svrarrhppp
      241 gtasr
//
LOCUS       WP_181855318             249 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Klebsiella pneumoniae].
ACCESSION   WP_181855318
VERSION     WP_181855318.1
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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..249
                     /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=27295
     Region          12..142
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 midiprifti sesehrihnp ftpekyatlg ralrmapgtt ildlgsgsge mlcswardhq
       61 ivgtgvdmsl lfsqqaaara eelgvsdrvt fvhqdasgyv asqscditac vgatwigggv
      121 agtiellkqs ltpggmllig epwwrkrpat aeeaiacgaq spddfltlpa lvahfgelgy
      181 dvvemvladq egwdryeaak wltmrrwlea nphddfapev rqqlttaplh hvtwtreylg
      241 wgvfvlmar
//
LOCUS       WP_181855579             610 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181855579
VERSION     WP_181855579.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 610)
  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 610)
  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..610
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..610
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=67320
     Region          40..379
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mframhlsll gcllgtsgch glppappaps aavgnygevi dylqrhirre merqdvpgla
       61 lalvddqqlv wargfgyadr qhrinaseht afhagdlskl liasatlqla ergqlsldap
      121 lqdtlrefyv rsrfhadqse adraitfrrl lshqsglpge hlpplfgerp nslgqlpakv
      181 sgvwlsnppg tqvahsnlgy elvgaaiern tgkhfeqhmr ehlldplqmt rssfarnalp
      241 qaqrahgysg ggrpgsasdl pvndlwsspv dlsrfvrmlf angrhkerql lrkhsveemf
      301 rqqnagnald fdcqvglawf lspcgsaple ggirhyeyas atpgfsahlv llpeqrlaai
      361 vmsnaddrgs ltaslarqaa slmlqvrqga rrpavqptpa rapalkvpsp edrrqlygry
      421 atrqgqvrly errgrlyadf geqrvellrd tsgwlqmrkr llgfwpvgvd sagqlqldvv
      481 sygqrrilvs rrhdqtaylg erikptslpq awteavgtyr vastgrhsyl nglsiriedg
      541 fllvrgqagg trsgefilqp idsahavlag sgqglgdtfs rdfdglnalg yrfaqqgtka
      601 rpwlqrkesp
//
LOCUS       WP_181855568             320 aa            linear   BCT 28-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Pseudomonas
            aeruginosa].
ACCESSION   WP_181855568
VERSION     WP_181855568.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=35863
     Region          1..316
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mdrlsiidia plygadrgaw ndvarridqa crewgffyia ghplpaarfe allaaareff
       61 alpveeklki ditrsrnhrg ygaiateqld palpsdfket fdmalhlpae hpdvragksf
      121 ygpnrhpdlp gwealleghy admlalartv lralaialgi eedffdrrfe qpvsvfrlih
      181 yppasarqsa dqpgagahtd ygcvtllyqd aagglqvqnr qgewidappi dgtfvvnigd
      241 mmarwsndry rstphrvisp rgvhrysmpf faephmdtei rclpgcfdad nppkyppttc
      301 gdwltsrfaq tyayrrgeta
//
LOCUS       WP_181855611             254 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Pseudomonas aeruginosa].
ACCESSION   WP_181855611
VERSION     WP_181855611.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=27797
     Region          10..101
                     /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          170..245
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mlpeplpvpl falridraas rtashrhacg qlyclergll vvedehgrqa lpprqiawip
       61 pghphsahsh gslagwsayl aaehcrdlpr hpgvlacsaf valiveratr wptgsawste
      121 renllrvlld elrhavpqrt rlpypgdsrl rriaealltn pcdprpaaew arwaglssrs
      181 lsrlfgaetg msfaqwrqla rlhaaverla agqavgevaw slgyespssf asafrtvfge
      241 tpsgyssran eala
//
LOCUS       WP_181855670             282 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudomonas aeruginosa].
ACCESSION   WP_181855670
VERSION     WP_181855670.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 282)
  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 282)
  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..282
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..282
                     /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=31648
     Region          36..141
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mnaiieqars ldgyqdssel lqrrdqdwvl dragieprsl ldlgcgigsl llggarrwpg
       61 lqrlwgiers plrleqaraq lrgagvearl legdlldlpp laerfelism tavlhwlypd
      121 eerlfrwvar hleaqgiflf tshhpfaedg lggeddlvaq alvemglaas ervaalyaea
      181 gllpmgtrtr grealrerve rhfrvdsivs rpavlrvads aeyqrfhaat fgtyfaplvp
      241 atrleeffvr lgriaerrmq adgqvseipv svwrcrareg ea
//
LOCUS       WP_181855707             569 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181855707
VERSION     WP_181855707.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 569)
  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 569)
  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 569)
  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 569)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..569
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..569
                     /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=63118
     Region          <192..278
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msseplepnq dviiprsrds lgrpvykaql trtdnqsekl alirqtaplp vifipgimgt
       61 nlrnkadkse vwrppnglwp mddlfasiga lwtwawrgpk arqellkaeq vevddqgtid
      121 vgqsglseea arlrgwgkvm rsaynpvmgl merrldnivs rrelqawwnd ealsppgdqg
      181 eeqgkvgpid eeellrasry qfdvwcagyn wlqsnrqsal dvrdyientv lpfyqkecgl
      241 dpeqvrrmkv ilvthsmggl varaltqlhg yecvlgvvhg vqpatgssti yhhmrcgykg
      301 iaqvvlgrna gevtaivans agalelapsa eyregrpwlf lcdaqgqvlk didgkprayp
      361 qnqdpyeeiy knttwyglvp eqnsqyldms dkkeglrvgp rdnfedlids ianfhgelsa
      421 agyhsetyah ygaddsrhsw rdliwkgdpt pletpgatln ddengtynsw frrglptivq
      481 gpletgnpld asgsggdetv ptdsgqapal agvkasfrhg skgkgqantk rgyehqesyn
      541 daraqwaaly gvikitqlad whpndkggt
//
LOCUS       WP_181856078             436 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Pseudomonas aeruginosa].
ACCESSION   WP_181856078
VERSION     WP_181856078.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=47230
     Region          25..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(134,136,262,264,299..301,350)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mndsikacla aaclalplla qgaetltiat vnnndmirmq rlskvfeesh pdislkwvvl
       61 eenvlrqrlt tdiatqggqf dlltigmyea alwgakgwle pmsglpadya lhdllpsvrd
      121 glsvkgtlya lpfyaeasit yyrkdlfqqa glrmpeqptw tqlgefaarl nrpdqgqygi
      181 clrgkagwge nmaligtlan afgarwfder wqpefsggew kkaldfyvst lkrygppgas
      241 sngfnenlal fnsgkcaiwv dasvagsfvt dksqskvada tgfafaprev tdkgaswlys
      301 walaipassr akdaakafat watsqaygkl vanregvanv ppgtrastys eaylaaapfa
      361 rvtleslkrv dpnhptlkpv pyvgiqlvti pefqaigtqv gklfsaaltg qmssdqalaa
      421 aqqstaremk ragypk
//
LOCUS       WP_181856230             103 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Streptomyces
            reniochalinae].
ACCESSION   WP_181856230
VERSION     WP_181856230.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces reniochalinae
  ORGANISM  Streptomyces reniochalinae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces reniochalinae"
                     /db_xref="taxon:2250578"
     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=11389
     Region          9..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 mpkervgtfr vlltvqvkpg meagfeqvwr qgsaqvtaqp anlghtlars aheesvyyvv
       61 sdwtdkdsfl afesspehva hreqlhpyrt ggslatmhlv evv
//
LOCUS       WP_181856322             341 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Streptomyces reniochalinae].
ACCESSION   WP_181856322
VERSION     WP_181856322.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces reniochalinae
  ORGANISM  Streptomyces reniochalinae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces reniochalinae"
                     /db_xref="taxon:2250578"
     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=34595
     Region          32..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 mgtgrpsrqt gtvltaglla lvavlatvaw lslavgsgpa gagdawrtvf dadpadkaql
       61 lirevrvprt aagllagval glagtliqgl trnpladpgl lglnsgasaa vvfaigvlgl
      121 taseqyiwfg flgallatml vygvgslgre gatpvklala gaatsallla vttaqlltds
      181 rtfdqyrfwq vgslaerepa vlwqaspfia vgallalclg pllnvlslgd dlarslgqrv
      241 gharllcggv vvllcgaatv vagplafvgl vvphaarlvt gpdyrwtlly savlapllvl
      301 asdivgrlva rpgevqvgvl talvgavpfv vlvrrrdvag l
//
LOCUS       WP_181856284             414 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Streptomyces reniochalinae].
ACCESSION   WP_181856284
VERSION     WP_181856284.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces reniochalinae
  ORGANISM  Streptomyces reniochalinae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces reniochalinae"
                     /db_xref="taxon:2250578"
     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=45664
     Region          13..410
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(50,57,87..88,95,99,106,239..240,243,247..248,251,
                     289,294..295,298..299,301,324,351..353,356..357,359..361,
                     365)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(57,81,83,86,88..89,171..172,182,238..239,242..243,
                     247,295,298..300,400)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mpplfdwrfa adpypayawl rehapvrktr vpsgveawlv tryadarqal adprlsksph
       61 hhgeqgahgk gkvgipgers anlmthllni dppdhtrlrr lvstaftprr vaafaprvre
      121 ladtlidgfa grgeadlihe yafplpiyai cdmlgvprqd qedfrswagm mihqpgsprg
      181 gvgravkrmr gylaelihrk raeldrrgeg addlisglir asdhgehlte neaaamafil
      241 lfagfettvn ligngtyall rhpgqravlq ravadgdtgl lataveellr ydgpvelatw
      301 rfatreltlg gqrvregdpv livlaaadrd pdkfdapdtl dltrsdnqhl gyghgihycl
      361 gaplarlegr talaallhrl pdlrlaaqpe elrwrgglim rglrtlpvef targ
//
LOCUS       WP_181855415             732 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Pseudomonas aeruginosa].
ACCESSION   WP_181855415
VERSION     WP_181855415.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=80675
     Region          65..732
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mdrrnepspl ptkrplaplm llmaacsspa laedaarkdd plelgadtvt geqassrver
       61 sasakyavpl ldtpqtvtvv pqkviqeqna lslrqvlsnv sgitfnageg gggsgdsini
      121 rgfsananmq vdglrdsaqt srsdlfnlea vevikgpnsv fggagtsggs inmvskqpka
      181 eafthlgagl gtdryrrltl dtnqpleglg estafrlnlm ahhndvagre qidkqrwgia
      241 pslafgldtp trltlsyfhq rddnlpdygv palngrkldg vsrhdyfgwr nldeeridnd
      301 vatlklehdf sddfqlqnli ryshlhrdtv isashvnqkg lppgrylpag pqaygrdskt
      361 rmwinqtnlt grfdtfglah tliggfelsr etydrttysy nlgkfypang fdlhnppgyw
      421 ngptdkrdsa rnrtelevka lyafdtiald erwdlslglr ydwidgtsrs tpsgkptvra
      481 dssdgklstr aglvfkplen grvyfsygts fnpsaehlvt tgsgvteatg glapeknsty
      541 elgtkweflg rrleldaalf qvkkedarer ladgsyvlag eqrvrglels asgklnehwd
      601 lfatytylds etlkssnpqr egqalgntpp rslslwstye lpegvtlgyg aryvsqrnvt
      661 svdngklday wvhnmmlgyq atrdlklqln ldnlfdkayv ervrqvygnq srssaieygd
      721 grtailsaiy af
//
LOCUS       WP_181856575             670 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces reniochalinae].
ACCESSION   WP_181856575
VERSION     WP_181856575.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces reniochalinae
  ORGANISM  Streptomyces reniochalinae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 670)
  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 670)
  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..670
                     /organism="Streptomyces reniochalinae"
                     /db_xref="taxon:2250578"
     Protein         1..670
                     /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=68752
     Region          177..371
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mgdaavrrrl vrlavlpagl valtgaavvv cvlrgrgsap lgapvwgvla agaliccvvp
       61 gaaaylaaae argtaercaa lrratargqa elksmlwalr hgerpvprtr apqgepvgdg
      121 ldllvhqaal aqcgaeaava eavalmgrar gegeekmevf vnlarrlqsl vhreirfidd
      181 lehevedpdl lkgvfhvdhl atrirrhsen lavlggavah rqwtrpvsls evlrssvaev
      241 ehytrvqlvp piegavrgha vadvvhllae lienatvfsa petrvlvrte pvtaglavev
      301 edrglgmnpe eqdqlnavla dpegidvpal vrdgriglyv vaalahrhgv vvqlqnniyg
      361 gvqgvavlpr sllgepaghg kaalpnggrs ggagagpaap pggaaaatgf aevgseprsg
      421 ahhpalppeq trtvgeeraa gdadasavsp adprprarar ggqrgpatpa plgasgqtes
      481 tgspeggard rdrrapgppg paararraeg rgrhvpgtss gpgqaaastr gqgqeqqrqg
      541 qaaptawgqd vapaqgrdag aaqgreaapa qgpkaapagg rgaaspqgrg avggeplvdr
      601 pplprrrrqt hlapelrepl ppvgsardeg ghdpglmaaf rrgstlahgi dhpvggpppp
      661 hpgeerdhge
//
LOCUS       WP_181856764              88 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Klebsiella pneumoniae].
ACCESSION   WP_181856764
VERSION     WP_181856764.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=9615
     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 dtvherfirl pevmhlcgls rstiydlisr eafpqqislg
       61 gknvawaqse itgwmadria ernrgyda
//
LOCUS       WP_181856774             104 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein, partial
            [Pseudomonas aeruginosa].
ACCESSION   WP_181856774
VERSION     WP_181856774.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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 11465558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..>104
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          2..65
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mtlrygdrsq evlqlqrrln twaganlyed ghfgaateda vrafqrshgl vadgiagpkt
       61 laalggadcs hllqnadlva agarlglpla tiyavnqves ngqg
//
LOCUS       WP_181856810             319 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Nocardia farcinica].
ACCESSION   WP_181856810
VERSION     WP_181856810.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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="Nocardia farcinica"
                     /db_xref="taxon:37329"
     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=34700
     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 madvtrrlla llaalqtgra fagdelaarl avsprtlrrd verlreygyp vrtqpgpggy
       61 yrlaagttvp pllfeddeal atllglalls atgnagagsl ddaatraygk vdqflpkrlr
      121 praaalragl etgalaapga daatlgalad aihqhrvvtf eytgaegass arrvephrqi
      181 hlrlrwylla wdtdrrdwrv frtdritgmr vgervftprp lpadtgidyl ragfdkhrqr
      241 vvltvdapva avagaltgqd meltalpdgr travlmldtw qwlvlalafl daevtveepa
      301 efraalhrfg drlrggtph
//
LOCUS       WP_181856885             474 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Nocardia farcinica].
ACCESSION   WP_181856885
VERSION     WP_181856885.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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   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 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   4  (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   5  (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   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 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..474
                     /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=48595
     Region          143..471
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrrrllvalt vfaaiavlaf avplsltyat srtqqlvlgr sgdadrfasl adavataegd
       61 taalaeevtg yhalygenvl vvdargattv nagidtadpd vaaavaaarr nqqpqpavrl
      121 lpwsaatmli arpvgtgvqv ngavviqast taaraditra wtvivlgavl amlvfmllav
      181 tlsrwvlrpl aalsdavael tatlptpppg tpdpaaptsl trrhggppem ravaqsfdam
      241 aravadsaha qrqlvadtah amrnplaalt irldslepav pesaaptfrk asaeverltt
      301 lldglltlav aetpaafpae adrdrcdavq vvadrmdawh safraaeqtl vaadamgste
      361 vavpadtlaq ildvllsnan ryagagtrtv iavtpepdgv tvtvrddgag vpapeldrlt
      421 trfyrgstap aggsglglpi aaalaqargg rltvaaadph glavsvhlpa avpa
//
LOCUS       WP_181856922             151 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Nocardia farcinica].
ACCESSION   WP_181856922
VERSION     WP_181856922.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..151
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..151
                     /product="YybH family protein"
                     /calculated_mol_wt=16374
     Region          9..135
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mnhahptehs aaahaelrrr ideavdalrt kdlaalerly tpdvvsfdie pplqhvgvaa
       61 klanwarvfe vfdtvtyevr dltftagadv afghafarlg gtradgtats giwvrvsngl
      121 rridgawlia hdqvsvpldi rtgrgvvdle p
//
LOCUS       WP_181856841             193 aa            linear   BCT 28-DEC-2024
DEFINITION  NADPH-dependent FMN reductase [Nocardia farcinica].
ACCESSION   WP_181856841
VERSION     WP_181856841.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 193)
  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..193
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..193
                     /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=20425
     Region          9..158
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mptphptplt lavivastra grfgptvadw fldhvrtrpe lapvvvvdva aadlphtfga
       61 papaladiga tlaaadafvv vtpeynhsyp gglknlidlh saqwrakpvg fvsyggrsgg
      121 lravehlrav faelhtvtvr dtvsfhdpwt arddtgalqa gegaelaakt lldqlvwwae
      181 alraaratrp yva
//
LOCUS       WP_181856973             247 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Nocardia farcinica].
ACCESSION   WP_181856973
VERSION     WP_181856973.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 247)
  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 247)
  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 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   4  (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   5  (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   6  (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 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     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:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25435
     Region          5..233
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtgtrsalvt ggsrgigaei aarlaaegyq ltlaartadt leqtaqrlra eygvrvqpvv
       61 armnepeqvr alaaahdaaf ggmnvlvlsa gtgtagavad mpaktyerml dvnfrgpitl
      121 iqaalpllrk saaedvarga kivalasitg vageaglaay gatkaalisl cetvsleesa
      181 ggvsataisp gyvdtdmtaw krdeldravm lttgdvaemv laltrlsrna vvpnivlsra
      241 geqiwra
//
LOCUS       WP_181857021             487 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Nocardia farcinica].
ACCESSION   WP_181857021
VERSION     WP_181857021.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Nocardia farcinica"
                     /db_xref="taxon:37329"
     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=50632
     Region          1..470
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 madvavvgsg pnglaaavvl asaglsvevf eaaatagggc staeltlpgf hhdvcagahp
       61 masaspffra fdlaahgvel lappasyahp ldggragvaw rdldrtvadl gpdgpawrsf
      121 feplvrdwpg vvgvamsdlr hlppdlptav rfglrlleqg splwnlrfrg dvapalltgv
      181 athaitspra lpavgagvll gtlahaagwv iprggsqaia daliaelerl ggsvhtghrv
      241 dsldefggar aivldtspae llrlaqdrlp agyarrlrrf ryggaackvd falsgpvpwa
      301 apdcaqagtl hlvgsraeam aaegavasgr haerpyvlai qpgvvddsra pagrytfyty
      361 ahvphgsdld vtdaviaqve rfapgfrdli lahntrtaae lpthnanyvg gdisagamil
      421 pqvlfrpapr wnpyatplpg vylcssatpp gpgvhgmngl naarhvlrre fdittdplel
      481 lgtavrt
//
LOCUS       WP_181857005             579 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Nocardia farcinica].
ACCESSION   WP_181857005
VERSION     WP_181857005.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 579)
  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..579
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..579
                     /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=63745
     Region          1..579
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mydtiikggr wfdgtgaasa irhlgirdgr vvtvsaapld eqgcarvida tdrwvlpgmi
       61 dihthydvev lgspqlsesl rhgittvllg scsistvhvg petagdlfgr veaiprrhvi
      121 davargksws saheyaqale elplgpnvaa fighsdmraa amgldratra gvrpdgaeld
      181 tmarwlteal dagfvgmssq qlrfdkldgq ycrsrtlpst fatarerrrl gdilrargrv
      241 lqggpdasrp htvvtmaaat lglfraplkv sllsaadlka lpavihlfsl lartlnllgg
      301 nfrwqhlpvp fevyadgidl vifeefgaga aamhladqve rrrdmladpd yrrrfrrdyd
      361 rrfgprvwhr dffdaeivdc pdprvigktf gqvgldrggl hpvdafldlv vehgdkvrwr
      421 ttisnhrphv ldrlaahpgv hlgfsdagah lrnmafynfg lrflrrvhea eragrpflsl
      481 eravhrmtge ladwygldag hlrqgdradv vvidpahlda eldryaeapv aqydnlsrmv
      541 nrndaavsav lvggefvfge gragdsvgvt rtgrflrar
//
LOCUS       WP_181857064             403 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Nocardia farcinica].
ACCESSION   WP_181857064
VERSION     WP_181857064.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..403
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..403
                     /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=42345
     Region          5..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 msairsalvv gggiagpvva talleagiea qvheaypgps dgigsglala pngvaaldll
       61 gagdrvraia tpvtgmilsv ggrhhrlptv adepplqvvd raelhrvlhe havaagvpfh
      121 ygkrlvgaes datgvtarfa dgstatadvl igadgvrstv rgiidpdapg pqytgllgfg
      181 atiecaidtp adamvfaygk rayylywsdg dgrvgwganl phkqylslte aravpaerwl
      241 ailretydad tpggelarrt rpdqlevvgg lhimppvprw yrdrmvlvgd avhapsnssg
      301 qgaslavesa vqlarclrdl pdpgaafaay erlrrtrveg iaaraarinr skapgpvgra
      361 mmnllmpllv rtvmkpdekv agersyriew dapvpgepes gra
//
LOCUS       WP_181857149             341 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nocardia farcinica].
ACCESSION   WP_181857149
VERSION     WP_181857149.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 341)
  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 341)
  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 341)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..341
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..341
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36298
     Region          43..339
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mdprrnrala caatvlalac tpltgavata tpdapavtat padarlvdla vyspatqrsi
       61 avkvlrpadt trpaptlyll ngagggedaa nwfgqtdavd ffadkhvnvv ipmegafsyy
      121 tdweradegl aetlgnngrn mwttflteel ppvidatfga tganalagis magssvldlt
      181 iqaptryrsv aaysgcamts dplgrmfvtv vislgggdpe nmwgptggdg wrehdpylqa
      241 hrlppipmyi ssgsglpgph dtlanprlhn ddrqllnqtl vggaiesvtn lcttrlaqrt
      301 aelgrtdity nirrpgthsw gywqddlrds wpmiarsiga e
//
LOCUS       WP_181857169             210 aa            linear   BCT 28-DEC-2024
DEFINITION  cysteine dioxygenase [Nocardia farcinica].
ACCESSION   WP_181857169
VERSION     WP_181857169.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 210)
  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 210)
  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 210)
  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 210)
  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..210
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..210
                     /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=22701
     Region          85..181
                     /region_name="cupin_CDO"
                     /note="cysteine dioxygenase, cupin domain; cd10548"
                     /db_xref="CDD:380416"
ORIGIN      
        1 mrssvlslag ipatttapra arrrpvltpd darleravap alptrlrpad llrltdegae
       61 dvldgrydhl lpaggawpte erwatrlrad devdvwlisw tpakttelhd hagslgaltv
      121 lsgalselrw tgtelrartl sagdqaafpi gwvhevmrap aaiepvtaep tlsvhayspp
      181 ltamsyyeit gqgtlrrtrt vltdepegdi
//
LOCUS       WP_181857258             343 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Nocardia farcinica].
ACCESSION   WP_181857258
VERSION     WP_181857258.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..343
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..343
                     /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=34443
     Region          24..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 mirvrtsitl gvlsvavcaa mvfatglgae tlpvgsvwhv lrdrmtgtap adlgldtivw
       61 qlrvprtvla aivgaglala gaamqtlvrn pladpfllgv ssgagvgaaa vitsgffaga
      121 gvwalsggal agaflaatlv fliasaqggl tplrlvltgt vlgsafaafs sflvfrsadp
      181 aaaqsvlfwl lgslagadwt rialpltvvv lagvallaaa gwldallvga dtaasvgvpv
      241 rqlrialfvl lavlvgvlva vsggigfvgl vvphaarllv gprhrdllpv calcgalflv
      301 vadaatrilv rpteipvgvl tgligapafl lllgrrtyrf ges
//
LOCUS       WP_181857317             470 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Nocardia farcinica].
ACCESSION   WP_181857317
VERSION     WP_181857317.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..470
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..470
                     /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=49225
     Region          1..470
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mstavvvgsg pnglagaivl araglsvtvl eaaprlggga rsreaivpgl lhdecsaihp
       61 mavgspflrd leldryglrw awpeldcvhp lddgsagvlh rdvaataagl gtdgrawral
      121 fgapaagfeh tvtdvmgpll rlpdhpirla rfgipalapa dllakvfrtp qaralfggva
      181 ahafhplhrp lsasiglgil taghaygwav aeggsqsive amaslldklg gtvetgtpvr
      241 saadlppadi vlwdlaptav adimgerlph riatayrrfr ygpgafkvdf avaegipwta
      301 paarragtvh lggdyaeiaa geravhagrm pdrpfvlvgq qyladphrsv gdihpiwaya
      361 hvphgytgda taaviaqier fapgfreril gsetrtttgf adynpnyvgg nimtgakdir
      421 qlvfgprptl hpydlgipgh ylcsaatppg pgahgmcgan aaeralrrlr
//
LOCUS       WP_181857455             309 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Nocardia farcinica].
ACCESSION   WP_181857455
VERSION     WP_181857455.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (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   2  (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
REFERENCE   3  (residues 1 to 309)
  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..309
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..309
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33577
     Region          23..86
                     /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"
     Region          110..295
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mkparaagta taagagpava rrqlgrylrd wrtqagltia eaarlmewga stlqrlekgq
       61 adrirsldiq elcriygipd dlraaltgla qqspgsswwh ahgevipedf dvypgieaia
      121 aelscyqpel vppllqtpdy arallrlarp saddveldhr vqvrvqrqav ltrksparlt
      181 avvheavlrr ivgcpkvmaa qlrqladtst rpnvtvlvlp faaglpvgeq tgaftvlrfg
      241 agagrivepp lvhvagftgd lylerpqdva rfeaahdclr hyaldaqasr rmlrqaakey
      301 aaqaghigr
//
LOCUS       WP_181857252             293 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Nocardia farcinica].
ACCESSION   WP_181857252
VERSION     WP_181857252.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 293)
  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 293)
  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 293)
  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 293)
  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..293
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..293
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32695
     Region          14..272
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mskpddpayh wngaeldlda ylarigfage raptlatlre lvyrhttaip fenleavlgr
       61 pvrldlaslq dklvhsrrgg ycyenaglfa aalerlgfgv tghtgrvtmg agglrpatha
      121 llrvttaddd rvwmcdvgfg rgplrpyelr pqpdeftlgd wrfrlerrtg elgtdlwvlh
      181 qfgrdgwvdr ytfttapqyr idfevgnhfv stsprspftt rpflqrfhpd rhhvldgltl
      241 tterpdgsad iraltpgelp evmnelfdie lpgpdldalt tgswlervaa gtp
//
LOCUS       WP_181857460             577 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Nocardia farcinica].
ACCESSION   WP_181857460
VERSION     WP_181857460.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 577)
  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 577)
  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 577)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..577
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..577
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=62985
     Region          28..570
                     /region_name="COG4425"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:443540"
ORIGIN      
        1 mlekadtltr lrargvvvvr rtedvidlny vglvvatvff alsvtpslvp rdwlfqglis
       61 ginaalgygl gcllewlfrl wvrprlkvpp aptwvryavk tavlltaalt aalmlvqsar
      121 wqreitalmg megtttpayl rtgllslgvg vlvvagyrtv reiilflarq lnrwvrvpre
      181 lapavgalvl vvaavtifng vasraffava nsafsvrndh tspnavqpqq persgspesl
      241 aawdtlgfeg rwfvshgpta sriaavtgrp arepirayvg lesaedgedq aelavreler
      301 tgafdrqviv vvtttgtgwv nslaagaiey mfggdtaiva sqysylpsvl sfladrgkaa
      361 aagerlfdav hehwsqrppd qrpklfvyge slgsqgseaa fdgladlrak vdgalwvgpp
      421 nsnrlweqfv arrdpgspev lpvyadglvv rfaanppdla vpgpewrspr iaylqhasdp
      481 ivwwstdlif srpdwlsepr gsdvssqmrw apfvtfwqvt adltnaqgva dghghrygsl
      541 vldawaaiaq ppgwtpelae qvrfqleaae efervvk
//
LOCUS       WP_181857518             382 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Nocardia
            farcinica].
ACCESSION   WP_181857518
VERSION     WP_181857518.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 382)
  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 382)
  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 382)
  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 382)
  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 382)
  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..382
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..382
                     /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=42257
     Region          176..>297
                     /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 mhtaylgevf gavfladllr tgahaanrdd lrwlylleet trrrlathld vaalaaqvde
       61 hehychefat vvagqtwqef mrdtirlare alpdfellpv lasaearrdm aavldhelsl
      121 lafatralag rptdrplrer tpreipgpvr nregvtmtet ttgtdtervt aslvagwqlp
      181 adlyydpavh rqkqrrifdk awsyvcrerd laepgayvtt rvgdlpvvvv rdrdgvlhgh
      241 vnvcrhrlhp vaegagcrqv fqcryhgwty ghdgslraap glrdedtfdr qtmglrrgav
      301 pqgrlmtnce stiamfqrrt waalndggta ptgpaaappr papgratcvs pprprgssrs
      361 nsrhptarrs pdgnpaptst ca
//
LOCUS       WP_181857528             303 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Nocardia farcinica].
ACCESSION   WP_181857528
VERSION     WP_181857528.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 303)
  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..303
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..303
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33316
     Region          6..281
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 mvatdvaevl gllevehedr hcfignhpes sgprvfggql vaqairaagh tqsvdrtphs
       61 ahayflrpgs paeplryrvt plrdgatfsv rrvvatqshg dvlemlvsst svpgedrfgr
      121 ampevpapdq lppvyrqlqp yadeldgwwv rprpvelryv gqppraaldn pgpdrtapen
      181 rvwmraegpi pddpilarcl laylsdmtll dpllrrhgrt srgpgavgsl dhaiwfhddp
      241 dltdwilydq ravggstrrg lcegylhqsd grllctvsqe gflspvaptt drrtpahtle
      301 sta
//
LOCUS       WP_181857577             183 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Nocardia farcinica].
ACCESSION   WP_181857577
VERSION     WP_181857577.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 183)
  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 183)
  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..183
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..183
                     /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=20523
     Region          <1..167
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mvifaactas rigevsgcrv rdidtqtwtw rvrrqtmssp ggmedkgtkg nrvryvplie
       61 eirqlvldrl qavgrddpda rlfrgprggr iatgvlrdat hwdevvaklg yehlrrhdlr
      121 htgltrfada evslhvlqkt vghadsrtte rylhpdrrei tgagdkltkh lrsrsgpalr
      181 vvg
//
LOCUS       WP_181857742             409 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Nocardia farcinica].
ACCESSION   WP_181857742
VERSION     WP_181857742.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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 409)
  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..409
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..409
                     /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=44782
     Region          19..406
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(54,61,90..91,98,102,109,239..240,243,247..248,251,
                     284,289..290,293..294,296,319,347..349,352..353,355..357,
                     361)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(61,84,86,89,91..92,177..178,187,238..239,242..243,
                     247,290,293..295,396)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mestqmplvl dpigadiqge serlrargpv tsvempggvr awsvtdpall kqllvdprvs
       61 kdprqhwpaf ingeisqdwp lflwvavtnm ftaygadhrr lrklvapaft arrteamrgq
      121 veritkelld tlaqtpagea vdlreafayp lpiqviselm gvpedlnpgl racvdgifdt
      181 sltaeqaqan ygemyrilge liayrranpg edmtsllitq rddegssltd qelldtlllv
      241 isaghettvn lldqavfall thpeqraala egratwtdvv eeslrfeapi ahlplryavd
      301 dldvggvhia kgepilasya aanrdpkvfg dnadqfdlsr ttkdhlafgy gahhclgapl
      361 arleasialp alfdrfpnlr laaapdelgt vqsfisnghr hlpvyltae
//
LOCUS       WP_181857769             552 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Nocardia farcinica].
ACCESSION   WP_181857769
VERSION     WP_181857769.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 552)
  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 552)
  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..552
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..552
                     /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=61074
     Region          4..478
                     /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 mnstpspeiv dvigvgagft gmylshrltt agwtfagfea gpsvggtwfw ntypgarcdv
       61 esiyysysfd eelqqewtws qrfapqaeil syiehvadrf dlrkhftfnt rvvastwnaa
      121 drvwevrldn geirrsryli sgagglstpk dfdvpglsnf aglkvltsrw nislddlrgk
      181 rvavigtgss gvqaipliae vaehltvfqr tpnyvmparn avltpdqvaa vkenypaire
      241 ecrhspggip drpvtdrafd vsdeerkrry eaayersgfq gvggefadll fdmeanrtas
      301 efihdkirei vkdpvtaerl vpkyhplgak rsvfgtdyye tynrsnvslv slreeaietm
      361 tenaiitsng ayevdaivla igfdaftgpl yglgltgasg rrlqdawsdg irsylgfmaa
      421 dfpnffmvgg plspalasnv vvtieqavdw iadliehard tgatqieatp eaqqewvdit
      481 ewtvsqtlya ttdswyrgsn vegkpntfmg ylggvgkyrr mcteiakrgy pgvaidgraq
      541 srtlgpihee is
//
LOCUS       WP_181857808             385 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Nocardia farcinica].
ACCESSION   WP_181857808
VERSION     WP_181857808.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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 385)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..385
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..385
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40224
     Region          36..371
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mielrrlvaa alavavlplg aataapvaaa pvsapelpmp tgvfavgrdt whvvddsrrd
       61 pwvpseprel mvglfypalp gdgavapyat paearllvtr agarssdage avratgthsv
      121 tdatpqpgsf plvvlspgfg mprytltsla eelasrgyvv aavdhaneam giefpdgrms
      181 tcracetled qgafallvet rardvsvlld rlaaadapsv arsvdftrig maghsiggas
      241 aaaamardgr vragvnmdga ffslppgddp agraflllgt ddevhrpggs dptwtltwpa
      301 lgmwkrwvtf agadhysftd ipvlaeqldg selglppggt lsgqravalt rayvgaffdq
      361 rlrgipqpll dgptpgrpea rfhml
//
LOCUS       WP_181857814             341 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Nocardia farcinica].
ACCESSION   WP_181857814
VERSION     WP_181857814.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 341)
  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 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 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..341
                     /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=37389
     Region          2..318
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mseripvliv agflgagktt mlnhllrdds gtrigvvvnd fgavnidaml vagqvdamvs
       61 lgngcvccai dvseldemfe rltqpqalid vivveasgla epgnlirmvl gsenpriryg
      121 glievvdaeq fpdsrarhpe laghlrmadl vvlnkadrve pgvldrlrae iaerargvpv
      181 yatahgridp allfdppare rtpvaeqlsf delwrehdhg dpghrhlhdd ytsvsftsdr
      241 dlhprrligv ledpppglfr akgvlafagd hrkftlhvvg rhirlepqsw rrdearassl
      301 vligaglpad talarlrdtv haepeppdeq amlgvwryvp h
//
LOCUS       WP_181857939             707 aa            linear   BCT 28-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Nocardia farcinica].
ACCESSION   WP_181857939
VERSION     WP_181857939.1
KEYWORDS    RefSeq.
SOURCE      Nocardia farcinica
  ORGANISM  Nocardia farcinica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 707)
  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 707)
  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 707)
  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 707)
  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 707)
  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..707
                     /organism="Nocardia farcinica"
                     /db_xref="taxon:37329"
     Protein         1..707
                     /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=75958
     Region          20..571
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mgrvttasgp aaidltapdl reraeellre laggharlre dqwtaiealv vrrqralvvq
       61 rtgwgksavy fiaakllrra grgptvivsp llalmrnqva aaeragvvaa tinsgnvtew
      121 deihdrvaag eidvllvspe rlnnpdfrdq vlpklaadag lvvvdeahcv sdwghdfrpd
      181 yrrirtliad lgsdvpvlat tatandrvvt dvatqigtdt lvlrgsldre slhlsvvafd
      241 davertawla arlrelpgsg iiytltvaaa hdladvlath ghqvaaytgq tdpaereale
      301 nallrnevka lvatsalgmg fdkpdlgfvv hvgapsspia yyqqvgragr gteraevvll
      361 pgpedtriwa yfasvafpre hivrgvldal dadrplstaa lepmvelnrs rldmvlkvld
      421 vdgavrrvrg gwvgtgqpwe ydteryerla aareveqqam leyqrttdcr mnflrrqldd
      481 pslgadapgc grcdnctgar pdrsvdaeav aatrarldrp gidlaprkqw ptgmaklgvp
      541 lsgkitagae tgrvvgrltd lgwgqrlral ldgpdgpvpd avfdaciavl rkwdwaarpt
      601 svlalesarh pvltaslaar laevgrlrdl gtlatrpdrp pvsaansahr vaglhdswli
      661 pdltgvdgpi llvdaltdtg wtftvaahal rmagaaavlp falasvt
//
LOCUS       WP_181858173             418 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydroorotase [Polaribacter sp. WD7].
ACCESSION   WP_181858173
VERSION     WP_181858173.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. WD7
  ORGANISM  Polaribacter sp. WD7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 418)
  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 418)
  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..418
                     /organism="Polaribacter sp. WD7"
                     /db_xref="taxon:2269061"
     Protein         1..418
                     /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=45357
     Region          4..415
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
ORIGIN      
        1 mttliksaki vdassphhlk rkdilivdgm itkiedtiiq qdativtfnn lhvslgwfdt
       61 svslgepgfe eretidkglr vaaksgftsi avnantnpvi dtkssveflk nkakghatnl
      121 ypiaaltqks egiemaelyd myqsgalafa dykrpiandn lmkiallyaq nfgglvmsfp
      181 knkaiagegi aneginstkl glkgipdlae hlqiardlfl leytggklhi ptistaksvs
      241 likeakkkgl qvtcsvsinn lflsddnlhg fdsnfklnpp lrtkgdvksl qkavksgvid
      301 iitsdhnpid iehkkvefsq akdgaigles afsvlnsife ieefiaqitt npkeifglen
      361 tsisegniad vslfttdgey eftlenilst sknsaflgkt lkgkaygifa nnqlvlnq
//
LOCUS       WP_181858167             102 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Polaribacter sp. WD7].
ACCESSION   WP_181858167
VERSION     WP_181858167.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. WD7
  ORGANISM  Polaribacter sp. WD7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
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 10650117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Polaribacter sp. WD7"
                     /db_xref="taxon:2269061"
     Protein         1..102
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11568
     Region          <1..50
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mnqrqfseli gvsqqlisav vnytkkpnet ilfaiidnip didpmwlltg rgkynnnyap
       61 lsevrspief qiksivkkqf eelssnilqr isnieesvnq sn
//
LOCUS       WP_181858183             240 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Polaribacter sp. WD7].
ACCESSION   WP_181858183
VERSION     WP_181858183.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. WD7
  ORGANISM  Polaribacter sp. WD7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
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="Polaribacter sp. WD7"
                     /db_xref="taxon:2269061"
     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=28107
     Region          64..233
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mlytagfgli tficssfffl lfpilfqsff ddenwtvakn ifflfllvff isvgnyyyns
       61 lvqntqnidl lslkdflgft ftiaifpiii ftyvsekmyr yhrektakki mniklskkvd
      121 skdidtneii ifgennkeni sfnvndliyi tsqgnyacfy lktekqtker iirntlfniq
      181 kclnnysnfv rchksyiint kfinsvsgna rgyylksdsi nkkipvsrnf kkdeltnlis
//
LOCUS       WP_181858576             277 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Marinomonas foliarum].
ACCESSION   WP_181858576
VERSION     WP_181858576.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas foliarum
  ORGANISM  Marinomonas foliarum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
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="Marinomonas foliarum"
                     /db_xref="taxon:491950"
     Protein         1..277
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31271
     Region          39..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 mlvivykwtl aviflisasv ptwaesssae ldslsgatvr vcgnnayppv twinknqqid
       61 ginvavirrl feplgvtvdt fqdsnwrrci kevelgnvdi lsgfktdvrq qfmtyldapi
      121 iresiylyyp iehplmfegw ealaglrvgv lmgdsfgnkv daalhkypsl efvstqdqnl
      181 lkladnrldv vpmgglsgql dlrrlglegk igytktdvsd fwylaiskks sliqwlplln
      241 qrlnqllkdp eivsklvtky hqvysedldl srrraeq
//
LOCUS       WP_181858232             150 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Klebsiella pneumoniae].
ACCESSION   WP_181858232
VERSION     WP_181858232.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 150)
  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 150)
  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 150)
  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 150)
  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 150)
  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 150)
  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 150)
  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..150
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..150
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16994
     Region          <7..144
                     /region_name="COG1106"
                     /note="ATPase/GTPase, AAA15 family [General function
                     prediction only]"
                     /db_xref="CDD:440723"
ORIGIN      
        1 mkktasgeis vpidfesegt kkivyllgpi ynamingnll lvdefdskfh tllskflfri
       61 fhaqseglsq iiaavqdvnl mntdcfrrdq iwfvdkdiks gsshlyslve ykekqrtlks
      121 syghdylsga fdaiplfdnl defeklmpeg
//
LOCUS       WP_181858501             246 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Marinomonas foliarum].
ACCESSION   WP_181858501
VERSION     WP_181858501.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas foliarum
  ORGANISM  Marinomonas foliarum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
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="Marinomonas foliarum"
                     /db_xref="taxon:491950"
     Protein         1..246
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27396
     Region          35..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 mstapiygee ivlhtihlpp hiidpniipp pegldedavy gfdvdilraa yatqgvlvrv
       61 eltpwkrimr dveeglilga vscrrlpvre tfalfsapls dsanafvtrr aflddevptl
      121 sllnqysvaa vngwsqtdil kganipyysa sgldqginlv lrrnhdifmt erdsaifaar
      181 rmgvidqlsf ydvsglgldh yagcfskkyp naeqwrdlln kglkelnesg erdaiferyg
      241 lpflsh
//
LOCUS       WP_181858673             141 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181858673
VERSION     WP_181858673.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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 aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..141
                     /product="YybH family protein"
                     /calculated_mol_wt=15745
     Region          1..126
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mssevsairq liedwraavr asdvprivsy yaedivafda ilqlqfkgrd ayqkhwqact
       61 emckgpmtfn iaelqihadp qvafahylch cggtgpdgqp hsswmrvsag yrkhgdgwkv
      121 ihehfsapfd mdgkalidlq p
//
LOCUS       WP_181858728             384 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pseudomonas aeruginosa].
ACCESSION   WP_181858728
VERSION     WP_181858728.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     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=43301
     Region          2..317
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mfvrflfese vvieevcdda lvsfsdwlik rkkssgnhin rillrvisfl ewyqtllvgk
       61 rlvgslgqga qvtislrslk skqgvvrvri qhhamvpasv prtvrpissn tvsalldsce
      121 wtaktnfrrs rdrcmlvlla dtgirreelt wirvsdivga sadrklpvrt skrkgnpyrl
      181 ipisdetfrm lleyvdvtrs iqvrrlnrrk igfkdqgwlf ctregfkmap stvsqlfsdl
      241 raeagltdri sahmlrhryi tlqvmarlrs lssrgsigve alttvlskva slsghsslds
      301 mwryvdwaye eleaeykdsa nvaaeamsvi etlmgeakss enrvlaesll ivrealsqlr
      361 tksyelpsvv ahslrgsatq srhg
//
LOCUS       WP_181858780            1267 aa            linear   BCT 28-DEC-2024
DEFINITION  type VI secretion system protein [Pseudomonas aeruginosa].
ACCESSION   WP_181858780
VERSION     WP_181858780.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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 10626802
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1267
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..1267
                     /product="type VI secretion system protein"
                     /calculated_mol_wt=140731
     Region          130..344
                     /region_name="IcmF-related_N"
                     /note="IcmF-related N-terminal domain; pfam14331"
                     /db_xref="CDD:433873"
ORIGIN      
        1 msgatlfmlv lllvllgalg wwwrtrggte irsfyaavrq mereqgwqgr yeapwllmlg
       61 netegeqlcs twrllpvvrp awfgrwwsdg egaillvpes vflpdeglrr qsgawlrllr
      121 lflrlrggra ldgvvwnipl arlqdgeqaa nlglaarrry veltqrlgls lpvyvvitgl
      181 edlpgfqell aalpeearer algwsspfaa eaawqsrwce qaleeitatl tesivelgtl
      241 rgqvdnelyc lpprleslrg slqallepvf qgnargeapr frglylsgse aagaaadevl
      301 pavdaprrrs sfasqlwarr ilaeeglaqa vprilqlrqr wqrgiglaal clcllwgglm
      361 twvwrdalrd agelsqllhg aseryqplde dtrraaqvrq nvqawwqlvs qaprwrftsl
      421 afpsswfssl daridnayrr vserllvrpl rsllegeasd lrairsdgqp glkegddpsq
      481 wkdylaakdl varattlerh nrlfaqaidn rrtplddllq lsndalgssy nagslarlay
      541 ynrtlfaerp adlaaldlgr vaataadnfh dlmarwlnay fltdslertg naltqelaql
      601 gqerdataaq llgigelinh lqqqvnrinl iwgngvgqdl vpgyqnllks aqqssllgnr
      661 veelqnltvq lqqqfrsewi appeaagdgl lvkqgatlkl addllglkra iddlktkdfv
      721 svaladktla dhsllsiddi gvtqalsffn dftgyyestl pslnpryrys vlhaaasaat
      781 eamwqslgpr srslasrnas rfdvqvkqvq vlqaallelq dlqagarlll slnalavadi
      841 gqalrdideq avlrepvdfs rwsgapnfgl qmfraqdsae lkqslnsqfn amaavaerha
      901 palewlqaqq sslatadyna fvrfsalnae lqkfkadnpa staaqlaklv gndfnqmdig
      961 scadilngvl lpssrsdlat rlvdlrqgal grcqslqqqq aaqawkdlad yfnqylagrf
     1021 pfaysleaad aepgrvrhll klmetrlpqv reglaqvrsp dlpaaedfvr rleqaqrwlg
     1081 plferdksgl lgvaldidwr sdrslergad qviawslysg dqesrfpgaq dkgltwnvgd
     1141 plkimlrwak ngsqrpaddp rqaslavadl eagwsyqgsw allrmmrahf srqrppnvdy
     1201 tefplvlqlp vyapyspene armflrlslm slggktplsi qplpvrapqs pfatllpatv
     1261 astggtp
//
LOCUS       WP_181858957             605 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: polysaccharide biosynthesis protein [Bacillus
            amyloliquefaciens group].
ACCESSION   WP_181858957
VERSION     WP_181858957.1
KEYWORDS    RefSeq.
SOURCE      Bacillus amyloliquefaciens group
  ORGANISM  Bacillus amyloliquefaciens group
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
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="Bacillus amyloliquefaciens group"
                     /db_xref="taxon:1938374"
     Protein         1..605
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=66932
     Region          119..234
                     /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 mtyrrrlsmi faldtylvll svvigyqffe dsyhfydsga llltavsmli shhvcafmfh
       61 qykqvwtytg igellalmkg itlsaavtaa vqygvfhtil frllavswmv qllfiggsrm
      121 isrvlketig rkqndssral ivgagaggtl lvrqltqknd lgimpvafid ddqtkhklei
      181 mglpviggke simpavqrlr ihhiiiaips lcthelqtly kecvqtgahi kimpqfdeil
      241 lgtqaaghir dvkaedllgr kpvtldtski sdsikgktil vtgaggsigs eicrqisafl
      301 preivllghg ensihsvhte lsarfgkevl fhaeiadiqd rdkifalmkk yephvvyhaa
      361 ahkhvplmeh npeeavknni igtknvaeaa dmcgtetfvl issdkavnpa nvmgatkrfa
      421 emvimnlgkv srtkfaavrf gnvlgsrgsv ipifkkqiek ggpvtvthpa mtryfmtipe
      481 asrlviqaga lakgrqifvl dmgepvkivd laknlihlsg ytteqipief sgirpgekmy
      541 eellnhnevh teqifpkihi gkavdgnwav lirfmeefsr lpeeelrkrl feaiesvhee
      601 aaagv
//
LOCUS       WP_181858989             409 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Pseudomonas aeruginosa].
ACCESSION   WP_181858989
VERSION     WP_181858989.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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 409)
  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 409)
  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..409
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..409
                     /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=43826
     Region          18..399
                     /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(28..29,32..33,36,69,119..120,122..124,127,148,
                     151..152,155,230,233..234,237..239,242,271,275,326..327,
                     331,335,351,354..355,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 msdntfsvqr fralpteihv mlvgtlltrg ayfmvwpfla lllwrefrls asaiglllal
       61 atvcgalsgi ytgwlsdrfg rkrliffgts lsglsfvllg fsgqplsygl aisgvsigca
      121 llessckali gdrvedrrsr elalycryfl inlgaalgpl igltlgvaaq agtflvtalv
      181 yfcyglllwr llhhlelkrr slaprsstgf leaclsmarh raftllllcn mlaaliyatf
      241 dstlvqyltr sglpdvvnsi allvtinalt ivvaqfpllr llentgtggr lmlgillmll
      301 aqlgfawtpv tlfaglalat vvlslgeliv fptfsvevdq ltpddlrgsy fgaanlyslg
      361 talaplyggi mldhagsqal ylglaalcgv imllqvgavg lrqaeragg
//
LOCUS       WP_181859209             617 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pseudomonas aeruginosa].
ACCESSION   WP_181859209
VERSION     WP_181859209.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 617)
  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 617)
  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 617)
  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..617
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..617
                     /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=69596
     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 malsdlavrq akatgkaytl pdldglslav taaggrtwhf ryywagkqkr mslgtypevt
       61 lrearslrde arallakgtn prvhrkqkrt avrladentf eavyrkwlkh rglslkegrq
      121 ttlsilprif dkdvlpalgk rsvyeikrpd lleviakiek rralsvaekv rtwfnqlfry
      181 alvivpgleq npasdldvva lplppvnhnp flrmaelpkl lqrlrsyrgr rqtqlglrll
      241 lltgvrtgel rqampdqfdl drglwiippd vvkqlqldmr kkrrqpkdip pyivplsiqa
      301 meivrhllde fkpaqrylfr hdsdlkkris entlngalkr mgyqerltgh girgtmstal
      361 neigypkvwv daqlshvdpn kvsatynhae yveqrrrmmq dwadrldlfe qnqveaasmp
      421 ltvhlegvpa fpneqtasap stpvaaspil lvtkpgdamp lvsaaahrlp avppprsaap
      481 lvpsdiqrer melfdvfeap hnlpvaafak magksrrwis yeikagnlla lnvgnrgqrv
      541 pdwhldplkh eliqsvlklt rgadpwqiyh allqprsmlr grsalegvta gnldklviav
      601 stavkesewt pprvgva
//
LOCUS       WP_181859281             483 aa            linear   BCT 28-DEC-2024
DEFINITION  T6SS phospholipase effector Tle1-like catalytic domain-containing
            protein, partial [Pseudomonas aeruginosa].
ACCESSION   WP_181859281
VERSION     WP_181859281.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 483)
  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 483)
  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 483)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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 the carboxy end.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..>483
                     /product="T6SS phospholipase effector Tle1-like catalytic
                     domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <228..411
                     /region_name="DUF2235"
                     /note="Uncharacterized alpha/beta hydrolase domain
                     (DUF2235); pfam09994"
                     /db_xref="CDD:462937"
ORIGIN      
        1 mpnfgfhiap thpvagrliy dskklsenil kqqsdervfs rvqeqkrlse gdvvggapcc
       61 kaihitlgfd gtnnndkadd ssvspscsnv arlihasigs gddinsrgif kyycpgvgtv
      121 fpdikeftps smgligaegg enrinwglvq lvdalfytll ksrlklnevq glveemstnw
      181 tvstltggll engekkrraa lepklkelee klrqrqnsgq kphilamrly vygfsrgaae
      241 arafanwlqe ltrvsdadgr veyrfaglpi sieflglfdt vaavgladsa pfavghmdwa
      301 ddtmrlpdea lsqclptilp edcsflkrcv hlvscheqra sfpldsirrr dmdangrrtg
      361 pscyrkwtve yaypgvhsdv gggygvgnqg kavggsefll sqialqhmya eafeagaplq
      421 vpapavhpdf hedwrvmvpk ieaefsvsee latrfnawqa qakagpleev irretalita
      481 wri
//
LOCUS       WP_181859600             938 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Vibrio harveyi].
ACCESSION   WP_181859600
VERSION     WP_181859600.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
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="Vibrio harveyi"
                     /db_xref="taxon:669"
     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=106151
     Region          46..472
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          523..938
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkinkllilt sgvflsacqv lapnktvess ldltqpltfd rradvgqlen glsyyiaent
       61 npesrvyvrl vvnagsmnee ddqrgvahiv ehmafngtkh ypenevikvl eeagmkfgvd
      121 inaftdfent vytlnlpnnn petlelvmdv vsdwasnvtm lkgdldaerg ivleewrarl
      181 gpmlrlgdkk saiemagsry vtrdpigdpy tiqhvskyrv adfynkwyrp dnmsivivgd
      241 vnteqmkqli srklghdrtp dtslekvdys iplidgwrse tvseegyssp svevsffsef
      301 kpdlsyaryq ddlahqiatr llnvrlqrwe qdednvvnaa nfyssnvgre ttqavfslql
      361 vdgeyeqatq glfkfvsqla qhgfseqein geisrlkgvi ergkdkkdys idlagdlmvs
      421 aasgqtlidk eqayqlnkyf leritpqqvn dafkriiapk srlilltqps dkrkpkldek
      481 wvegvwqttm qeqqppwfid esqavlpvvd pkvgsvkqer kwaehqitey rlsngsklvy
      541 rysdsnpgqv hfkaltaggt rsipqqdyha lktavslvdd tgvgvvpqad iqtifhgnpv
      601 vmstlvdeyq qgfsgwakte sfekmlklfh lklaaspise kslkeyqvem aqklngarfd
      661 gadrfvrkvs elrfpdiptv ysdngehaas ytaqglsevy qkyvagktdy tyfvvgdisa
      721 tqieslaary lasikvkevs reyyevkass pkvrystpds kepraeveiy ltqdsqwrpd
      781 nayylelsge lvqeqlrlkl reqasgvygv aswfwqdvhs pqaegrilft capervdeli
      841 slthsvlssv aetgadeqvl enkllqrddq idrylrsdlg mlnameqsyl ltdsprliqa
      901 qrranseask qkvdaimrqf lnqatrfeav llpentak
//
LOCUS       WP_181859808             885 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudomonas aeruginosa].
ACCESSION   WP_181859808
VERSION     WP_181859808.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 885)
  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 885)
  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..885
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..885
                     /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=96928
     Region          8..885
                     /region_name="PRK10490"
                     /note="sensor protein KdpD; Provisional"
                     /db_xref="CDD:236701"
ORIGIN      
        1 mtdtaradal ladlpadgrg rlkvflgaap gvgktfamlq aaqaqlrqgv klragvveth
       61 sraeteslla gvpqqplrsl eyrgmklqem dldglltdpp alalvdelah snvpgsrhak
      121 rwqdiqella agidvyttvn vqhleslndq vrditgvqvr etvpdwvlqe ayeivlidlp
      181 prellerlre gkvyvpeqar aaidaffsqt nltalrelam qtaaarvdad lnhryrqrge
      241 eapalrgrll vgidgdeqae rlvrhacrva errhlpwsvv hvdtgglrge harmrlqgaq
      301 qlaerlggei vvlragevar tllqharerr aslvlvgqsr rrwyrrafgg glagrllrdg
      361 qgleisalds eadlrpaepr prypvvwndy llallatala sglawivahl lelpnislvf
      421 lmavllvavr sslmpallca vasflaydfl fipphfsfai hrhedllsla fflfmagltg
      481 nlaarqrrql ealrdtqeet slllelsrkl taatdrqavl aaaaqqfddw kdvevcllgq
      541 vngewkteag vqrqladqer vaadwawahd qpaglgtgtl pggrwwwwpl saeegplall
      601 gvapldgqpl spqrrrllaa lgqplaqala rarlaedlea arlhgeteql rsallasvsh
      661 dlrtpltamr gsidsllalg eaippadrre llestrdeae rldryiqnll dmtrlghggl
      721 klardwvapg divgsalnrl ravlapyrvq aivandlpll yvhaalieqa linvlenaar
      781 fspnhgrlri evsqdaaelr favsdegpgi peaerekifd mfytaargdr ggqgtglgla
      841 icqgmigahg grisvgegld grgttlvlhl plhpqpdlgq legde
//
LOCUS       WP_181859895             672 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Pseudomonas aeruginosa].
ACCESSION   WP_181859895
VERSION     WP_181859895.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            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..672
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..672
                     /product="PhoX family protein"
                     /calculated_mol_wt=73722
     Region          58..667
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mslekkdail fgdgdelpsn hsnnphmndl iaglgrrqvl aggaalgala flgvalpasa
       61 apaeaqvpaa eglrglpfkr rnrlpfeaia sgradtirvp agykatplip wgtpisgsyp
      121 gflddasnsa qdqaeqigmh hdgmhffpid aqfgfggghi snhgllvlnh eyidapllht
      181 ngptvvdgkr tvadevrkei nahgvsvvei rrnvrgewnv vpsqrnrrit aatpmriagp
      241 arghellrtr hspdgtrtrg thnncsngft pwgtyltcee nwvgyfstqd selpreltry
      301 girntsrfgw etlagdefer fdatrkgkqa qddyrnepnn fgwiveidpf dpqsvpvkrt
      361 algrfahegl vfapvkpgrq vvcysgddsq neyiykyvsr dkfrpgrsnt rlldegtlyv
      421 arfnadgsgq wlpldiadgn fraacrkagv sfadqgevli ntrlaadvlg atkmdrpewg
      481 avnpdngdvy ftltnntsrt vadaanprvk nayghiirwr ersrdyagqr ftwdlfmlag
      541 pgedsrgpdg kplnqdnila spdglwfdpe grlwiqtdms gsqlssgpfg nnqmlvadpr
      601 tgelkrfltg plgcevtgia atpdfrtlfi niqhpgegst adnllstwpd gpgrrprsat
      661 vvitredgrr ll
//
LOCUS       WP_181859954            2352 aa            linear   BCT 28-DEC-2024
DEFINITION  amino acid adenylation domain-containing protein [Pseudomonas
            aeruginosa].
ACCESSION   WP_181859954
VERSION     WP_181859954.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 2352)
  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..2352
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..2352
                     /product="amino acid adenylation domain-containing
                     protein"
                     /calculated_mol_wt=259144
     Region          4..>2072
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2077..2341
                     /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 pyqwldtdae feachvdlra drdpeaavrs wlrdafrhay pldgrslvdl
      121 allhsdqaly vyvrthhivs dawglqlfls rvragylgel gepqaqmpta sllaqletdd
      181 ysgseqyrgd rayfaealeg lepalftrrr paglrrtarh rltleralld airdrgespf
      241 lflsaavaly larihqnddv vlgvpvlnra draakqvvgh fantlplrir tvpeqtvdef
      301 laqlreatrt llrhqkmplg dllrgasplf dttlsymrwp aaqaipnasv etvaqthahd
      361 pdalaiwvse fdghsdaqvd feyacdvfda dfpmdaaarh ietflralve ggerrlgeld
      421 plsaaereel ihtrnatdqa fpeqatlptl faeqvartpq rtalleadgg tlsyaeldak
      481 vqavadalra agvstderva llvargphll pailgvqrag gayvpinpdh plervrllle
      541 dcgarvvlvd eraatlgesl getrvlhler lpqstgdlpa anvapgdlay viytsgstgm
      601 pkgvmvehrs vvnrlnwmqr rypigerdvl lqktpvtfdv svwelfwwsf tgarlsllpp
      661 gaekdpreml rsiqrdavtv ihfvpsmltp fldlldgdpt arvaasslrl vfcsgealap
      721 lqvarfrrlf gdavrlvnly gpteatvdvs dhecasdnpt rvpigrpidn lrlyvldral
      781 rpqplgavge lyiggvgvar gylnrpelna erfladpfva ggrlyrtgdl arwladgnle
      841 ylgraddqvk irgnrvepde vrdrlaalpg vrdaavvard savrgthlvg yyvaaaeldp
      901 gqlraglsat lpdfmlpaff vridslplsa ngkldrrqlp appeqvaava prtateaela
      961 avwadvlgva evgvhddfya lggdsilmlr iraaaqrrgl gfeladlmrn ptvaglaerl
     1021 vrplaersyq pfelvsevdk prlegledaf ptsrlslgll fhsrqrpdss vyhdvfhyrf
     1081 dlawdeaafr haldrvvaay palrssfdls gaseplqlvh aqarseplil dlrgnpeagt
     1141 vldehirqrr fhryslqqpg lflfaafvre dgldlvfsfh haildgwsva nlivalvaay
     1201 rgeplpgpap alachvreel aalaspaavg ywtgllegar mtrldgfgah elqaaqgpas
     1261 hrealpdgll erlkataaqr glplksllla ahcltlhlfs rsdsvvtgai sngrpelpda
     1321 drmvglflnt vpvrseiagh swievadalf rqerdghahr ryplsaiqqi vgdelssafn
     1381 yvnlhvlepl wqlrdfrvwe etnfallvnv iatpsdgmyl ridsdgrgis rsqaaligat
     1441 fvellwrlae hpdeaadfaf laprrdaasq peplvdvvsl ferqvealpg saalafeeqr
     1501 wtyrdldhva rcvatrlvra garrgdaigv alnrspemia tiwgilragl vcvpldvsyp
     1561 aqrlalilet aqpfrvvahp ehahvaaaer vlpveelvad iepetfaapq ldelamllft
     1621 sgstgrpkgv elshrmwany tqwqlrvasg vpglrtlqfa plsfdmafqe ifstlcggge
     1681 lqlisnrerm apsallhvle rrqvqrvllp fvalqrlaea snalgvrpga lrvvvssgeq
     1741 lritedvraf caampgllle nqygptethq vtyhslsgdp ahypdlppig rpldgvevqv
     1801 ldaalrpvpv gvtgelyfgg dclargyhra peltaerfve hpwrpgarly rtgdlgrilg
     1861 ngeivwlgra dtqvkvrgfr iepaevelai mrqaerqpgl rgaavvarer qgndaflaaf
     1921 llgepeavdl aelkqalrse lpehmvpahf awvdgfaltp sgkrddaalr alplehgtni
     1981 eylaprddye rtlagllgel ldrprvgird sffdlggtsl samrfmllie krygvdlpma
     2041 alietptveg laerlrersa vrafdplvpi raggsrpplf lvhplgghvl cylplvralp
     2101 pdqpvyalqa agtgqgstpl avlediaasy laairrvqpe gpyylggwsf ggfvayemar
     2161 qlraldpqav aqlivldsit vdrnhagsas dealllffyw elvwfersde eveplpegas
     2221 leqkldhive raieagvlpa gtpratvqrl yelfraswqa ligyrpevsd qdmtllradg
     2281 plplalkpmh daagthygdp kngwqhwtsg rldvidvpgd hlvlmkepyv etvaaeiaal
     2341 lepstssert rp
//
LOCUS       WP_181859665              80 aa            linear   BCT 28-DEC-2024
DEFINITION  glutaredoxin family protein [Vibrio harveyi].
ACCESSION   WP_181859665
VERSION     WP_181859665.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 80)
  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 80)
  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 80)
  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 80)
  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 80)
  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..80
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..80
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9093
     Region          2..73
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 mkiemyskeq csqcetaamw lqnqgfnvat lkldvefdre tlfelfptar sypqfmldgk
       61 pigdfsrlks alafeqnaaf
//
LOCUS       WP_181859769             319 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Pseudomonas aeruginosa].
ACCESSION   WP_181859769
VERSION     WP_181859769.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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..319
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..319
                     /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=35144
     Region          3..311
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mqialapmeg lvdeilrdvl trvggidwcv tefiritdrl lpatafhkla pelrdgsrtr
       61 agtpmrvqll gsdpacladn aafacelgap vidlnfgcpa ktvnrsrgga vllkepklmh
      121 divaavrrav pseiavtskm rlgydspdga ldcaraladg gsahvvvhar tkvdgyrppa
      181 hwewvarvae avrvpvfang evwtlddylc crevsgvedi mlgrglvsrp glarqiaawr
      241 dggeirempw sellpllrdf wlqarrklap ryapgrlkqw lgmltrtype avelfarirr
      301 esdcetidrl lqvsfsqaa
//
LOCUS       WP_181860188              40 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial [Enterococcus
            faecium].
ACCESSION   WP_181860188
VERSION     WP_181860188.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 40)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 40)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 40)
  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 carboxy end.
FEATURES             Location/Qualifiers
     source          1..40
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     Protein         1..>40
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          2..>40
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 maiivnldvv laqkkmsvte lsekvgitma nisilkngka
//
LOCUS       WP_181860124             515 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator [Pseudomonas aeruginosa].
ACCESSION   WP_181860124
VERSION     WP_181860124.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 515)
  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..515
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..515
                     /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=56905
     Region          8..124
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          245..490
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mpqsirhlia lpelrsrlls gaggldrpvr wahvcelddp tewlgegdll mttglgipsd
       61 aerqrryvrr laeaglagmm igenmeapsd ldalretaea lgfplilthy gvpfaavtrg
      121 ivdagqkdey errnalariy esarlsmqgl glpallqrlg kdvrsslyli vpdtlaawqp
      181 glpglpaela dalrnrrreq aepqpmvlrh plaegealsi gipsdrncll ialgerlpdy
      241 sllhhltavl gieierlrve serhlrlgse llddllqrrl yreqaeerle ellpgldldd
      301 avvsvasseg latdpiglfr ghdsrllvra qgqeiillhq aglastlqea ldsslgvsap
      361 lrraercaea lrearlalah shsrqplcry aelddeapwl prslaeaera frlvlgalhd
      421 ydaangsall ytlqvfleen rswlnaaqrl hihkqslvyr irrieeisgr sldstadvat
      481 lwfalqatrl speargrtak gslleqsahh ggdmd
//
LOCUS       WP_181860324             414 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Candidatus Similichlamydia laticola].
ACCESSION   WP_181860324
VERSION     WP_181860324.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Similichlamydia laticola
  ORGANISM  Candidatus Similichlamydia laticola
            Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia;
            Parachlamydiales; Candidatus Parilichlamydiaceae; Candidatus
            Similichlamydia.
REFERENCE   1  (residues 1 to 414)
  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 414)
  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 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 11414248
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Candidatus Similichlamydia laticola"
                     /db_xref="taxon:2170265"
     Protein         1..414
                     /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=47095
     Region          135..369
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 msdispfegk ilqaqlllre afldgwllcs ykdqnaflaq llspefrlqt efpvflwips
       61 hgpgvfclhe rdqachslpg evrtyhswke rakllaklle qavriasefs fksfvpeisf
      121 ldagtytlik sfgvdlvsse dlvselfltw dqeelnrhlf aasvleqlcs hlprkiresl
      181 cseqlldels lknyilavle ssdcfteipp kvlvnersar pwaltiesna iswgdyvlvd
      241 lacrkneega pyatlsrcff lgdspdafly dtfflarraq qaalhfmeer rrdahsflgw
      301 evdriardfi hlaglessfr cplghslgkh syrvgpsldd lyvhdtrmiv prtcfclgpf
      361 lsvegrfgid vktsvyfssd gtfflttgeq aelytftesr earipmqssk ivsy
//
LOCUS       WP_181860418             269 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_181860418
VERSION     WP_181860418.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 269)
  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 269)
  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 269)
  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..269
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>269
                     /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..>269
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 agkekllalg vypevtlada rakreeakrg iaggidpmea kreeknaret qlnntfkdia
       61 lewhssklkk wsagyasdil eafnkdvfpy igkkpiaeik plellnvlrr iegrgateka
      121 kkvrqrcgev fryaivtgra eynpapdlts amqghesnhy pfltakelpd ffkalssysg
      181 salvvmaarl liitglrtge lrgalwdeid lnkaiweipa srmkmrrphv vplskqalsl
      241 igqikeltgn yplmfpgrnd prktmseas
//
LOCUS       WP_181860541             927 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_181860541
VERSION     WP_181860541.1
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=104128
     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 ndeqsfveqa
      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 qritystind niwaslqnaq iqalktldqr paekfaqqmy
      661 etryaddrtk llqenqivqf taadalaadr qlfsspadit fvivgnvsed klvalitryl
      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_181860703             252 aa            linear   BCT 28-DEC-2024
DEFINITION  S1 family peptidase [Streptomyces diacarni].
ACCESSION   WP_181860703
VERSION     WP_181860703.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces diacarni
  ORGANISM  Streptomyces diacarni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 252)
  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 252)
  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 252)
  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 252)
  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..252
                     /organism="Streptomyces diacarni"
                     /db_xref="taxon:2800381"
     Protein         1..252
                     /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=25642
     Region          35..252
                     /region_name="COG5640"
                     /note="Secreted trypsin-like serine protease
                     [Posttranslational modification, protein turnover,
                     chaperones]"
                     /db_xref="CDD:444365"
ORIGIN      
        1 mritrllptl iaallaaltl qtaaaaedrs adegaraava tkahdlqdgq qpiigggyaq
       61 sgpwaarlfs ggrqtcssti iaptwiltak hcvsggalsf rvgsldqtsg gttangtqvs
      121 thpsadlalv rldrsvstty atlgdpgtvs vgqtvqvygw gatsrcgqei ncqsrylkva
      181 nvvvtggcrd ayngsaicar rgdgitaggd sggpmmagga qvgvastsdr qtttaytnvt
      241 qyrswirsva gv
//
LOCUS       WP_181860970             357 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Streptomyces
            diacarni].
ACCESSION   WP_181860970
VERSION     WP_181860970.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces diacarni
  ORGANISM  Streptomyces diacarni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 357)
  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 357)
  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 357)
  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 357)
  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 357)
  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..357
                     /organism="Streptomyces diacarni"
                     /db_xref="taxon:2800381"
     Protein         1..357
                     /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=38490
     Region          24..348
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mgthntdlsa aetahdpsea aadvlvtgas gfigghltrr lvarghrvrv lvrsgsdrsg
       61 fadvaeeiet eigdledpds lcraakgvtt vyncagvsad wgpwedfhri nvegakrvve
      121 aahqagtvsr vlhvsttdvy gypkqpcdes aggkdiglpy nrsklmgera vrkaagetgm
      181 rvtivrpvsv ygprskdfvi eignlllqkq mlyirggnvp agllyvdnav damiaaatsg
      241 etvgkvynlr dperttwrqy vealadglgv kppwlnlpap vatgaallse klygalrits
      301 rpvltrhtvh lfdrdqsygi kqaqrdfgfe spvgfaegmr rtlawldsae grehvar
//
LOCUS       WP_181860971             450 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Streptomyces
            diacarni].
ACCESSION   WP_181860971
VERSION     WP_181860971.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces diacarni
  ORGANISM  Streptomyces diacarni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 450)
  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 450)
  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 450)
  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 450)
  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 450)
  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..450
                     /organism="Streptomyces diacarni"
                     /db_xref="taxon:2800381"
     Protein         1..450
                     /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=50899
     Region          6..315
                     /region_name="PobA"
                     /note="Chlorophyllide a oxygenase/letal leaf spot protein
                     [Coenzyme transport and metabolism]; COG5749"
                     /db_xref="CDD:444459"
     Region          <375..>442
                     /region_name="dermokine"
                     /note="cl42387"
                     /db_xref="CDD:455732"
ORIGIN      
        1 mipdlwypva isgdvtdkkp kgirrlgeei vlwrdidgkv vcqgarcphk gawlgdgrmk
       61 gnaiecpyhg flfnpegkct ltpamgrdar ipgslkvpvy pvrekhgliw vwwgddrpes
      121 elpeiiapre ikendrvydt iswnkpvhyt ryiesvqefy hvtyvhrdhw lnwldfmfly
      181 gtkkkfgldg kenylkatmi hnhhvetddd gmtfrysfdh geednpersi hyvitfsfpc
      241 mvhveteafa ttswfspide entehifrvy efpqlkpilr heklrramst lqcylekfvq
      301 dpqdfkimaq qeprisgggv nkfipvdemn akfiktrarl lrearerreg tpaavdtsdg
      361 mvgeldmatd earigqpsta aetkgrtsar sngrtrngas sgrnggsprt ggaqgnghva
      421 gngngsdsgp aapeseevrn wsedraaars
//
LOCUS       WP_181861126             926 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces diacarni].
ACCESSION   WP_181861126
VERSION     WP_181861126.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces diacarni
  ORGANISM  Streptomyces diacarni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 926)
  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 926)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 926)
  AUTHORS   Rosinski,J.A. 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 926)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..926
                     /organism="Streptomyces diacarni"
                     /db_xref="taxon:2800381"
     Protein         1..926
                     /product="helix-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=101301
     Region          <5..876
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Site            order(711,714..715,717,746,749..750,753..754,756..757,782,
                     785..786,789..790,793)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          711..734
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          744..777
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          781..807
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          852..902
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 miaertrefe lldedlvess sgrgrvvlls gtvasgkttl lrafcdrhad gvwplfatap
       61 paahgepfgv lrqlfeetpw prdrlqgllg tgqmadcahc aaaallelae dtplvvvvdd
      121 vhyadkpsir cllkvahrnr ssrlmlvlae stcdwsvrsv yrmelvrqsh frrvplahls
      181 vagvrevlae hlgtsiaqqv aeevhdttgg nqllvralae dyvdsleyad rdgwavgesy
      241 rqavltclyr sghevlevar alavldiags aqqiahmlek qprpvrralq rierlglttg
      301 grfrhpaara avyddvdpgv ladlhfraal llyrgrpcgr aadhlvasrs adkswavael
      361 rraaeealak dddetairyl efalhgraep reraglsmll vvakrrsdpa aavhhwaalm
      421 rahrqgllsv pqvadllrfa lwhgftqdae elvdwlgray hasdgppdgv llttgrllrh
      481 typsflppgr qegsycpkdc vplpsgfpvq aaemlstllr egvdtdgscs rmaeqilhni
      541 plsdeffeav msvlqtlvfs gqlpqaarwc ddllaeaarr gvprwqaqlm acraeidlrk
      601 galpdatrna egaltllgpd gwgvgigapi gilvsaatar gdvtaarghl rrrvpeamfq
      661 trfglqylqa rgqyylavgq phaaladfry cgrlmaswdi dapaflpwrs qlaevllqlg
      721 dteaarsyak qqiararsht tpaygmalrl laqtadrrer prllkeaaev lhacgarlpl
      781 vqtltdlgya yeaggnpqka rmllrragrl aeviglpdvp tqaaaskqdq qtrgsqghsg
      841 graerspaes pprtltvaer kvaalaglgy snreiaqkly vtvstveqhl tkafrklnvk
      901 srdalpldle ldielpspsa sahvdp
//
LOCUS       WP_181861154             369 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Streptomyces diacarni].
ACCESSION   WP_181861154
VERSION     WP_181861154.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces diacarni
  ORGANISM  Streptomyces diacarni
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Streptomyces diacarni"
                     /db_xref="taxon:2800381"
     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=40277
     Region          32..368
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 madaphlnrp drspaqpatd arrrhdpqvr gfasdnyagv hpeilaalal angghqsayg
       61 addytahlqd vvrshfgrra eafpvfngtg anvvalqalt drwgavicad tahihvdecg
      121 apervgglkl ltvptpdgkl tpelidreaf gwddehramp qvvslaqnte lgtlytveei
      181 ralcdhaher gmlvhldgar ianaaaaldv pmraftnaag vdilscggtk ngmlfgeavv
      241 vlnpdavrhm khlrklsmql askmrfisvq leallagdlw lrnarhsnam aqrlaegvrg
      301 vagveilypv qanavfarlp hdvserlqkr yrfyfwdepa gdvrwmcsfd tseqdvdgfv
      361 aalreemgr
//
LOCUS       WP_181861132             234 aa            linear   BCT 28-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Streptomyces
            diacarni].
ACCESSION   WP_181861132
VERSION     WP_181861132.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces diacarni
  ORGANISM  Streptomyces diacarni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 234)
  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 234)
  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..234
                     /organism="Streptomyces diacarni"
                     /db_xref="taxon:2800381"
     Protein         1..234
                     /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=22779
     Region          <99..227
                     /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 marttthgdr asggaqaaaa rggrlrrava gaaagfalll aapglpaagp sgasavlaga
       61 gaprkaeppp pdassaggas gqgagagaae aggsagtvrw vrpiavegvr vsqaygvkgd
      121 waaghhtgid lavpegtgvr svgpgtvvfa gwsgdygkav tvrmtdggyt lfahlsrlsv
      181 tagdtvhpgt plgrsgntgr stgphlhfev raergygsdi dpvrylaghg vrlv
//
LOCUS       WP_181861195              94 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181861195
VERSION     WP_181861195.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 94)
  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 94)
  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 94)
  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..94
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>94
                     /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..94
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 hamiviedlk vsnmsksaag tvsqpgrnvr aksglnrsil dqgwyemrrq leykqlwrgg
       61 qvlavppayt sqrcaccght akenrlsqsk frcq
//
LOCUS       WP_181861525             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Brachybacterium alimentarium].
ACCESSION   WP_181861525
VERSION     WP_181861525.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     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=32661
     Region          8..292
                     /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(34,240,243)
                     /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 msrpavhvig ealidvvvra dgvervrpgg spanvavgla rlgvltdllc rigadaygdl
       61 lrahleqagv glpdggspap artstavatl gadgsasyrf gidwdpgtia vptarilhtg
      121 slatvlepga tavanalsaa dpatlvsvdp nvrptvgvpq vevrsrterl agrahllkms
      181 dedldwlypg aapeevaarm helgvrlfvv tlgaqgcfls tsewscripa eaatlvdtig
      241 agdafmsgll yaviaddgdq tvrtgvlqre qvenwahtaq rsaaltlgrd gaeppllael
      301 harelvsqsa gepvsr
//
LOCUS       WP_181861835             345 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Slackia].
ACCESSION   WP_181861835
VERSION     WP_181861835.1
KEYWORDS    RefSeq.
SOURCE      Slackia
  ORGANISM  Slackia
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 345)
  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 345)
  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..345
                     /organism="Slackia"
                     /db_xref="taxon:84108"
     Protein         1..345
                     /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=37558
     Region          1..342
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mrrlqsfyai latifavaas iltfflvcif gipdiglllw flfagtafaf tlslvighyl
       61 aepltdlhvr aqailhgdar vdikpegkly eadelaedfv alsaktkaqm sdlsvqenrq
      121 trfisdvahe lrtpltairg naetlmdpdm ppalrerfcq tiineserlt rlsndlltlq
      181 hieegtdqvi mkrvnlhdva ervadamnpi feengaelki egeapdvlgn pdrlqqviyn
      241 lvanasrfvg kgghvtirla gladksvisv iddgpgfgdi dpkllftrfy rgdnsrarnt
      301 ggtglglsiv kgiveghdgt ieafnaaggg acfvvslpsv hehih
//
LOCUS       WP_181861870             540 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Slackia
            isoflavoniconvertens].
ACCESSION   WP_181861870
VERSION     WP_181861870.1
KEYWORDS    RefSeq.
SOURCE      Slackia isoflavoniconvertens
  ORGANISM  Slackia isoflavoniconvertens
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 540)
  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 540)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 540)
  AUTHORS   Rosinski,J.A. 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 540)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..540
                     /organism="Slackia isoflavoniconvertens"
                     /db_xref="taxon:572010"
     Protein         1..540
                     /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=58012
     Region          482..539
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msvaqargiv kglkwhhlgf cffwavtfva lmapadefaf astgfsvgkq lstivavvaa
       61 atlsvrrgsk afspesayia gialsagsll yylaffladf svasvaiasv lvgasqgaff
      121 vmwqsfyase gtsrttvyip lsalcsvvlc iaigflptew lvvcgvivlp algawtlrks
      181 laevvpyeae pltrerrrml lrdmarpvfc vcaigfvwkm igyvvpqgnl gsfegimlgm
      241 scatlvvaai elftergfdm lrvyqvlfpl itgvfllptf fgiewlgavs vftmfgfevv
      301 nllllitcaa yasrkaidss lvyalcvapt laslllgdsv gqvaaahtvl dftlvvdvlf
      361 vcvyvltaal flaslgrnrs dvrrsitaap qsgsgerdsg esiaenvarm kseefpvqga
      421 svveggqcaq kepsskeasr dvqqceekps aalrrsngaa pmtptdespt sleerlssld
      481 ladplsarec evadlmrhgn tvaviarrly isentvrght ksiyrklgih skqelidlln
//
LOCUS       WP_181862088             485 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181862088
VERSION     WP_181862088.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=51028
     Region          <75..483
                     /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 mnktirrasv fslllvlall vratwvqfye gqaladnknn rrnaieqyay plgdiivage
       61 aitgserttg sdlaykrtyk dgtlyaavtg yssqvygatq legiyedlld gtdtrlknpv
      121 dtvtgkradp gdvvttidpd vqkaaydalg gkkgaavaid pstgkilglv stpsydpsei
      181 sgttdsaawk altqdsdkpm tnralrqplp pgstfklvva aaaledglys svdtrtdspn
      241 pytlpgtttv lsnenaaapc enatirtalq yscnnvfakm avdlgqdkvk amaekfgfnd
      301 aeldvpvray esvypsdmdk aqtglsgigq fdvtatplqm amvsaaiang gelvsphmvs
      361 qisdsdgnvl rdyddstdtk rivssstaeq lqsamvtvve egtgtnaqia gatvggktgt
      421 aqhgennskt pyawftsyak ddssgkevav avvveqsdaa rsevsgngla apiakammra
      481 alqqn
//
LOCUS       WP_181862248             195 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces himalayensis].
ACCESSION   WP_181862248
VERSION     WP_181862248.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11467951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=21840
     Region          1..99
                     /region_name="COG4189"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:443343"
ORIGIN      
        1 maskenrrit dvgtlkalah plrmklyrgl ivarvatasq laeqvdeavs lvsyhlrkla
       61 ehglieeaep qsedgrerww qpasegvsir dedfrdapek aaahtaasrl fsdqrtemyr
      121 rylderahwg pewnhaaess esvlrltage lsdlvtamqa llkeytergr aadeagdteg
      181 renvavhtna fpfrv
//
LOCUS       WP_181862287             501 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Streptomyces himalayensis].
ACCESSION   WP_181862287
VERSION     WP_181862287.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..501
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=52611
     Region          19..493
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mariavigag mgamaaaarl avgghrvvvy eragtyggal grverdgfaf dtgpgllqlp
       61 avfrdlflkt gkeplercve lsqvepavrh vfadgtevsl pnasragvge aldaalggga
      121 garwaafmnr areawdrsrr plleeplwpn wqvlaerepy paavqrrllr rdrvattlte
      181 vaelelggep rlrallehya laygldprtt ppsaavlpym eqtfgawsvr gglraladav
      241 yerclargve frfgaevtri vekdgraagv elsdrsaeda afvvagvapg vldgllpgpp
      301 vratgevpsq aqgglpsrlt vllalrggrp edtpyrtvvh agdrqdeldr lfgprpavav
      361 spsvtvlrpg dpelvpdaeh eavtltvtvp ahaevseaev ervltvaera vpglrdrllw
      421 hevrtpadva aatgadggsv papalasagg rllhpsnstr ipglfavggw ahpggglpha
      481 gmsgalvagl ivegpdfrgs q
//
LOCUS       WP_181862367             460 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-amylase [Streptomyces himalayensis].
ACCESSION   WP_181862367
VERSION     WP_181862367.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 460)
  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 460)
  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 460)
  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 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..460
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49305
     Region          35..376
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(79..80,83..84,119,122,171..174,204,206..207,
                     209..210,233,235,240,296..297,302)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(121,176)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(206,233,297)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          382..456
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 masrtlsgal alvaaatvav avpgataqas ppgtkdvtav lfewdfdsva kectnrlgpa
       61 gyglvqvspp aehiqgsqww tsyqpvsyki agrlgdttdf rdmvatchna gvkvvvdtvi
      121 nhmsagsgtg tggssytkyn ypglysapdf ddctaqisny qdrynvqhce lvgladldtg
      181 eeyvrsaiag ymntllgygv dgfridaakh mpaadlanik srlsnpsvyw kqevihgsge
      241 avqpteytgn gdvqefryay dlkrvfnsen layvknygeg wgymssgvsg vfvdnhdter
      301 ngstlsykdn anytlanvfm lawpygapdv nsgyewsstd agppndgtvn acwqdgwkcq
      361 hawpeiesmv afrnatrgas vtnwwdngnd aiafgrgskg fvainhesss ltrtyqtslp
      421 agtycdvqsr stvtvngsgq ftatlgsnta lalysgkstc
//
LOCUS       WP_181862382             459 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            himalayensis].
ACCESSION   WP_181862382
VERSION     WP_181862382.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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 459)
  AUTHORS   ter Beek,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..459
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..459
                     /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=49446
     Region          48..449
                     /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(160,162,288,290,323..325,366)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mhnqsrpspr srsrarslit aaaagallls gcagagaggg gsddgdsidv lmvnnpqmve
       61 lqkltaanft ektgikvnft vlpendvrdk isqdfanqag qydvatlsny eipiyakngw
      121 lhaldayvak deafdqddvl ppmrqsltga dgklygepfy gessflmyrk difekhglam
      181 pqkptwqqva dlaakvdaee qdmkgiclrg lpgwgealap lttvvntmgg twfdkdwtar
      241 ldspefkkat kfyvdlvreh geagaaqsgy aeclnnvtqs ktamwydsta atgsleasgs
      301 pvkgkmgyvp apvdktassg wlytwawgvq kaskspdaaw kfvswasske yealvgkelg
      361 wanvpagkra styerpqyrk eaaafadvtr taiesarpnd pgvqprpapg iqfvgipeft
      421 dlgtkvsqei saaiagrqsv daalaksqkl aekvseqyk
//
LOCUS       WP_181862236             259 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Streptomyces himalayensis].
ACCESSION   WP_181862236
VERSION     WP_181862236.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 259)
  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 259)
  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 259)
  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 259)
  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 259)
  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..259
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..259
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27778
     Region          91..257
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msdknregkr tareriaver erqkarerrr rtlivgasvv cvlalaavig viaantgedk
       61 pdtsgpvaap tgasgqdslv ipvgqdtars tltvwedfrc packnfedty rstiheltea
      121 gklrveyrla tlidknmggs gslraanaaa caqdagkfta yhdvlfanqp vetddafadn
      181 sklielarkv dglvtpafek clndgthnsw vaksneafea ggfggtptil lngknvyadq
      241 qnpltpdrlk qmveeaaka
//
LOCUS       WP_181862393             226 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces
            himalayensis].
ACCESSION   WP_181862393
VERSION     WP_181862393.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=24254
     Region          33..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 mregyegtgp gaitpdgcav elyarlpvgd epdiiagavp agahilelgs gvgrvthpll
       61 ergftvtavd esaemlervr gartictpie rldlgetfdv vmlasflvha gdaevrrgll
      121 ntcrrhvadd gcvliqrege dyhtnlprer vdpsgftvrm vsaepvgdgv nsvraeyvfp
      181 daawtqtfla rpltreafeg alaeagltvd ryltddgtwv ralpvp
//
LOCUS       WP_181862411             254 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181862411
VERSION     WP_181862411.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=27116
     Region          11..212
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 mkfsiggplk lafrpwvegl envpsqgpai lasnhlsfsd slflpavldr kitfiaksey
       61 fttpgikgrl taaffkgvgq lpvdrsgarg ageaaiksgi gviergelfg iypegtrspd
      121 grlyrgkpgg larvalatga pvipvamidt ekiqppgkvv pklmrpgiri gkpldfsrys
      181 gmehdrfvlr avtdevmyei mklsgqeyvd iyataakrqi aeaakaerea akaearavkd
      241 agdkggteqe rsgs
//
LOCUS       WP_181862536             269 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Streptomyces himalayensis].
ACCESSION   WP_181862536
VERSION     WP_181862536.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   ter Beek,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 269)
  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 269)
  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 269)
  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..269
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..269
                     /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=28514
     Region          1..269
                     /region_name="COG4587"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443644"
ORIGIN      
        1 mgqgrlyaav avsgfrrhat yrvataagvf tntvfgfvla ytyialwder pglggydqaq
       61 altyvwlcqg lhatvaamgr gmeveligri rtgdiavdly rpadlqtwwl agdvgravfh
      121 llgrgfvpma fgallfdlav psdpltwlaf lvavalgvvv sfairylval safwlmdgag
      181 aaqmaaltgi ffsglllpln vfpgalgeia ralpwsallq mpadvflger tgvglletya
      241 fqgawavall aagrlvqsaa trrvvvqgg
//
LOCUS       WP_181862495             217 aa            linear   BCT 28-DEC-2024
DEFINITION  CGNR zinc finger domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181862495
VERSION     WP_181862495.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 217)
  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..217
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..217
                     /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=23359
     Region          32..201
                     /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 masgatsaaa atrtspalah tspaqaaapp pheprfdagr icldllatah peerlgsver
       61 lrtwcadagl vppdtplsaa epswlaafre lrlrvdelvr geldgryagd alervnalar
      121 wspptpravr addgtlvral hddpgctall aavardavel ltdpvararl rqcegdncpl
      181 iyldtsrgrr rrwcsseacg nrervarhrr raalara
//
LOCUS       WP_181862548             716 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181862548
VERSION     WP_181862548.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 716)
  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..716
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..716
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=77649
     Region          8..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(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 mekgeefgpw larqlklagk tqaelaeelg ltraavsawi tgrstprptv mvdiakalgt
       61 dvgtvhtrtt dtqaglpvtw yhrpgyldgg rdlgnaaafa fdadvqvlar etcqnslder
      121 rqngrpvrvc ytlheltgea ledfrdailw ndlfphysav senagnqkvg rvvdagvrdm
      181 yekgrlillr vddynasglt gddytdgkfa avvrrqlesl ksgsgaggsy glgkatlwat
      241 salglvlins tlseshegrt errmigrlel pwrevdgkpy agpawfgrpd pdspgaevar
      301 swwadeetaa rlhltresde pgtsflivga hdvaildeks sdaddesvdv dvegsedthd
      361 irrmhrrlvk algrdfwaam tggggrlpll easvrtmrng dvvvpdeqvd psaeqpartr
      421 alrayyegtt vervteagqv aarsvplrlp laggargtlg thqatllvte atgdadapkn
      481 qvhslrgnrm tvrkagvanv pfgsnpfqav llvgeaagds apfakeaedf lraaeppehd
      541 rwgqteeltl rwspsayrri naltyevnsa irelvarpkr ssreggealr kaltvkkars
      601 kvkaptgpvv pvlteldati gddgewriaa evsiprgdei tpmvpvaqle vrsggrpkld
      661 waelvavegc dvedgilrft pgarrakfrg stdvtshtvr taltrlvlel rtgkge
//
LOCUS       WP_181862497             783 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Streptomyces himalayensis].
ACCESSION   WP_181862497
VERSION     WP_181862497.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 783)
  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 783)
  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 783)
  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..783
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..783
                     /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=85403
     Region          17..768
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 maaqeavdsa adtavdsvrd reisveqehl drvyqrleek iheaeflmhd aakrghvgtp
       61 galaerdaqv fragihlnrl nnefedflfg ridlltgkdg kkgpdgayta vepaegavrt
      121 dntadiaetl higrigvlda dysplvidwr apaaapfyrs tpvdpgrvvr rrvirskgrk
      181 ilgveddlmr peltayldgq alpvvgdgal maalgqarth tmrdivasiq aeqdlvirap
      241 aasvtyvegg pgtgktaval hraayllyqd rrryaggili vsptpllvay tegvlpslge
      301 egqvairavg slvdgaeatv ydspsvarvk gssrmlrvlr kaargalelg paghtpaqtr
      361 grptapaapp nrlrvvafgr rlelegealq rirrtalggt apvnllrpra rkllldalwe
      421 qsgagsrhtd pelaaelrss fdeditsedd fiafldawwp eltprgvlsa mgdekllgrw
      481 arrelnpgev rrvarslrrd glsvhdvaml delqailgtp frprkkreld pleqltglee
      541 lmpvreessr eraerlaqer teyahvivde aqdltpmqwr migrrgrhat wtivgdpaqs
      601 swsdpdeaae ardealgtrp rrrftltvny rnpseiaela arvlalampg spspsavrst
      661 gvqprfavvh gegmaqtvre earrlleqvd gtvgvvvamn rreeaarwla glgervvalg
      721 sleakgleyd atvvvspaei adespaglrv lyvaltratq qltivsaerd epdaagmpdl
      781 lrd
//
LOCUS       WP_181862579             505 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces himalayensis].
ACCESSION   WP_181862579
VERSION     WP_181862579.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 505)
  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 505)
  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..505
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..505
                     /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=54066
     Region          137..352
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 maalavvsia vvvivllmqe gtadaatwgv lsaaavlgcs cvagavvaan aeargasrry
       61 aalqrlaagg qadvqemlhr largerieqp pfarpgplea gpldrlahei allrshataa
      121 liqvaqpavp asegegrera evfanlarrl qslvhraige iddleheved pellkrlfqv
      181 dhlltrnrry aenlavlgga vsrrqwsspv slmevlrssi aeveqysrvk lvpeiegtlh
      241 ghavadvihl laelvenatv fskphtnvll ssqrvaagla vevedrglgm ppedqgrina
      301 llanpndvdv sklladgrig ifvvaelarr hgiavqlrrn iyggvqavvv iphrllgded
      361 epvaprpatv dmprhttavp tqrsavqaap aaqplaappa vaqplpevrr vtmsphvpqh
      421 qprtaeaapp rdydsahhvd aqdgrpelpr rnaqqhlvpq lmdtpgtrtp egeddvepsm
      481 rnwtaftggf nraegadesp sdgsr
//
LOCUS       WP_181862636             266 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181862636
VERSION     WP_181862636.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=28418
     Region          1..262
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mklafstlgv pglpiadvvr laaehgyhgv elraheeepv hpgigltera dvaaefksag
       61 iqilgiagya rvaapgadep vlteirglle lardlgapfi rvfpgggtkq taeeadataa
      121 rrlgtaveya gdlgvrille thdshrtgaa atrvlgqvgh rrlgalwdvm htwlggeqps
      181 etyaalspyl gyvqvkdias aedttplplg sgvlpltecv evlmrngwdg wlcweyekrw
      241 yeaaaplpgl lrpgrehlar llnesa
//
LOCUS       WP_181862616             299 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces himalayensis].
ACCESSION   WP_181862616
VERSION     WP_181862616.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 299)
  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..299
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..299
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32908
     Region          15..296
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msqalqslld lldlerieen ifrgqsrsav vprvfggqva aqalvaagrt vpedrlphsl
       61 hayflrigdp gapivytvdr mndgrsftar rvvavqhgqp ifalsasfqk yeegldhqap
      121 mppapdpatl ptaeerlply gnldpevver llearaavdl ryvddppygr ygepraprsq
      181 vwfrtngkld ddpplnsvwg dpllhiclat yvsdmtllds vllahgrggw avgdvvgasl
      241 dhamwfhrpf radewllydq esptssggrg lgqariytqd grlaisviqe gvmrvprps
//
LOCUS       WP_181862694             235 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces himalayensis].
ACCESSION   WP_181862694
VERSION     WP_181862694.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..235
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24786
     Region          12..>174
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mskagraatt svifdldgtl vdsepnyfea grhvlaqhgi tgftwedhqq yvgigtqetl
       61 alwkerfglg apldellaek nrrylelarv stpvypemrk fverlhdagv qmavasgssr
      121 eaieailssa glatllpvvv sadevahgkp apdvfleaar rigaepadcv vvedaapgaa
      181 aahaagmrci aipyvagqad dprfatagll frggqgefta qaafewlala pttps
//
LOCUS       WP_181862761             641 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181862761
VERSION     WP_181862761.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (residues 1 to 641)
  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..641
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..641
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=68336
     Region          75..254
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          331..635
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 msrdqlhsag sttagaeapf lellargasa dayeqpvlla radgqpseri taleqaklla
       61 lrvrseiegr rrreaelsal fetahdlagl rdldavlqai vhrarsllgt dvaylslndp
      121 argdtymrvt egsvaarfqq lrlgmgeglg glvaqtarpy vtddyfkddr fqhtgaidag
      181 vreeglvail gvplmlgahv igvlfaadrr arvfereqia llgsfaalaa aaidtanllt
      241 etrealghle raneiirdrs gvierasevh drlaelvlrg ggvhdvaaav srvldgtvef
      301 adagtapaea letsraegha vrhggdwiaa vtagdellga lvlrghpgld pvdqrtlera
      361 amvtsllmla rrsaseaeqr vrgellddll dsrdrdprvl reravrlrad ldathvvlaa
      421 rleapaadae egaagrrrlw aaashlaatr hglaaardgg tvlllplhkg dtaatvarrt
      481 akhigtavhe avtvgasapv gdlaaypdtv vaayaeaqrc vdalrllgrs gegaaaedfg
      541 flglllsdsr diagfvdrti gevvaydarr gtdlvrtlda yfasgmspar tkdelhvhvn
      601 tvaqrleria rllgpewqnp araleiqlal rlhrlsaavi p
//
LOCUS       WP_181862852             413 aa            linear   BCT 28-DEC-2024
DEFINITION  FUSC family protein [Streptomyces himalayensis].
ACCESSION   WP_181862852
VERSION     WP_181862852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 413)
  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..413
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..413
                     /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=45098
     Region          18..213
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mpevrgaava apvaefvkrs repvvvqtlr staaatiayv valqlssepa pltapltall
       61 vvqvtlyatl ttgirrvnsv vvgvliaigf salvgltwws lgliilaslt vghfvrvsef
      121 vpevaisaml vvgvtrvadt awdrvletli gaavglafnf llappvwvge agasiedlar
      181 rmrrlmlrsc eqltsptppd eaadqlhear rldhdiadvd aalrqaedsl rlnprvkegl
      241 lhrvvlrtgl dtleictvvl rvlartltdl akirrtdepl lrrdigvalq ellghvadav
      301 vsfavlvttq vsenaeaaea rlagelaaan asrdklalvl legvqqdprn whlhgallte
      361 vnrildeldm ehrskrlfee ldrnareqre rhpwlarirh rlgsdrpsqe dtp
//
LOCUS       WP_181862799             542 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Streptomyces himalayensis].
ACCESSION   WP_181862799
VERSION     WP_181862799.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 542)
  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 542)
  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 542)
  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..542
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..542
                     /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=57977
     Region          8..358
                     /region_name="FAD_binding_3"
                     /note="FAD binding domain; pfam01494"
                     /db_xref="CDD:396193"
ORIGIN      
        1 mneevdhrvp vlivggslvg lsaslflgrl giehmvvekh satsmhprgr gnnvrtmelf
       61 rvagaeqrir eaasiladnh gilqtpslae egewlfkemd pggglarfsp sgwclcsqnd
      121 lepvllqcar elggdirfst emlsfeqdad gvtavvknrd tgehttvyae ylvaadgprs
      181 pvrerlgigq tgpgelfhnv sitfnskmla dvvgdrrfia cylttpeadg allpvdnvek
      241 wvfhapwqpg rgetledftd ercidqirka vgvpdidvei tgrapwhaae rvaesyasgr
      301 vflagdsahe msptgafgsn tgiqdahnla wklaavlngw agpgllatye terlpvaqvt
      361 sarasarsve hshpgfappp gtgggqqggv lkvalgyryp rgavigadpa qpvvpdtmql
      421 tgqpgsraph mwllrsgvrt stldlyersc vllcgaastw hmaakrvaer lsvpldsyri
      481 gsgpdadlap ekggdwaalh gtteqgavlv rpdgyvawrs egavadpeat lyeimaslld
      541 la
//
LOCUS       WP_181862880             211 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Streptomyces
            himalayensis].
ACCESSION   WP_181862880
VERSION     WP_181862880.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=22977
     Region          1..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 mtddsfsaee ywdgryaesd rmwsgkpnpv lvreaaglqp graldlgcge gadaiwlagq
       61 gwqvtavdis rlaldraaah aaaegvadri dwqqhdlaas fpdgafdlvs aqflhspvem
      121 prekilrnaa tavapggvll ieghggfpaw ehnhhpdlhf ptpdeviddl glrdgqwevl
      181 lseeheriqn dpdgrpttri dntvkarrlp a
//
LOCUS       WP_181862901             104 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces himalayensis].
ACCESSION   WP_181862901
VERSION     WP_181862901.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=11272
     Region          7..88
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mltsvdtelm rvladplrlk ivsllaretl ctthlveetg arqtnlsnhl rvlreagvve
       61 tepcgrftyy rlkpevvasv adsfaelaes arataesgak racp
//
LOCUS       WP_181862973             484 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181862973
VERSION     WP_181862973.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 484)
  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 484)
  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 484)
  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 484)
  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..484
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..484
                     /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=50962
     Region          6..478
                     /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 mtedrrtydv ivlgagptge nvaertsaag lstviverel lggecsywac epskallrpv
       61 laradarrvp glrqavggpl dvpavlahrd eivfhwkdds qvgwlesvsv dlirgharld
      121 gprkvavqtp dggtvlltar havavctgtg aavpeipgld svrpwtsrea tsagrvpgrl
      181 avvgggvvav ematawqalg sqvtmlvrgd agllarmepf agqlvadglr eagvdvrlga
      241 svaslaredg evritladgg elaadeilfa tgrasrtadl gletigltpg dwltaddtcr
      301 vtavadgwly avgdvnhrvl lthqgkyqar iagaaigara kgeradetrw gahaatadvv
      361 avpqvvftdp evaavglttr eaeragrrve vvdydiagva gahqyadgyr grarllvdme
      421 rgtvvgvtfv gpgvgellys atvavvsevp lerlwhavpa fptisevwlr lletyrdrqq
      481 psps
//
LOCUS       WP_181863021             331 aa            linear   BCT 28-DEC-2024
DEFINITION  GDP-L-fucose synthase family protein [Streptomyces himalayensis].
ACCESSION   WP_181863021
VERSION     WP_181863021.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (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   2  (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   3  (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   4  (residues 1 to 331)
  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 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 10142801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..331
                     /product="GDP-L-fucose synthase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36043
     Region          21..319
                     /region_name="GDP_FS_SDR_e"
                     /note="GDP-fucose synthetase, extended (e) SDRs; cd05239"
                     /db_xref="CDD:187550"
     Site            order(25,27..30,51,54..57,77..79,81,101,120..122,151,155,
                     178..179,181)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187550"
     Site            order(98,122,151,155)
                     /site_type="active"
                     /db_xref="CDD:187550"
     Site            order(122,151,180,199,216,224)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187550"
ORIGIN      
        1 mtaastvptv thhtldrsap vfvagrnglv gsavwrhlta egftallgpg saeldlrdrr
       61 avfdwfaenq pqavilaaar vggikanatr ptefisdnlr iqvnvldaal khrvqrllfl
      121 gssciyprda aqpiresall tgpleetnda yaiakiagil qvqavrrqyg lpwisamptn
      181 lygpgdnfha enshvlpsli rrfdqahvek aakvvnwgtg tprreflhvd dlaraclvll
      241 erydsdspin vgtgedltir elaemvasvv gyegalewdp tqpdgtprkv ldisrisalg
      301 wtpeiglydg iastyawyms rgfaglrtms c
//
LOCUS       WP_181863136             365 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Streptomyces himalayensis].
ACCESSION   WP_181863136
VERSION     WP_181863136.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=39458
     Region          53..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 mklpgqdaia rqadehlvth rvklprrvve rplrqvakrl amalavlvgt afivyadsgg
       61 yndnsdgrvd lldafyyatv tlsttgygdi tpvsdaarft nifvitplrv lfliilvgtt
      121 levltertre ewrlnrwrsn lrehtvvigf gtkgrsaiht vcatglkkeq vvvvdpsera
      181 iesatasgyt givgdatrse vllraetqka rqiiiatqrd dtavlvtlta rqlnraakiv
      241 aavreeenap llrqsgadvv itsasaagrl lglsvlspsa gmvledliqq gsgldiverp
      301 vikaevgrgp reiedlvvsv vrghrvlgfd dpsvgalkpt drvitivrat pgtrvtpdtr
      361 plpqd
//
LOCUS       WP_181863161             957 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181863161
VERSION     WP_181863161.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 957)
  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 957)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 957)
  AUTHORS   Rosinski,J.A. 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 957)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..957
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..957
                     /product="helix-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=102801
     Region          <4..891
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          464..494
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          500..531
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          888..945
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mslglpthlv greaelavlr daiaqlrtgt ggvvlvegep gigksslvaa aaaagqesgc
       61 tvlhgiadqa ahplplrllc dcleitqran darraemlrf araerpdllv ssavhaamie
      121 mlltlveedc ataptmmvld dvqwaddasl dvcrrlasta ahlplllvls frpvprgsgm
      181 rqlratlrgh atttislgpl gpdairdlls dvagappgpa lvelaaqasg nplyvrelve
      241 slvreggvtv geradlrets lctvrrslaa aldsrlsfvr adaldmlrva allgrefavg
      301 evaavlgrst idisddlqea vaagilvdag qrmafrhpli rqalydgmpt alrvalhqda
      361 araldgiggv epqrvaqqll esgrvgdrwa rrwlartapv lavraprlaa elldrelehg
      421 vadqrdraaf saalaqilvg agehekaagr arqalavsge padrgrmywv laralfsggd
      481 ndaavatleq aleedlpddw rarllgslam fqragsgale aadatarram eigesagdtf
      541 aiayaltdlw lthsvqrqhl saldcvdral etlnatddhv dlrcyalhar iftlqnlsrw
      601 sdaeaalrea rqflldddrt ddarfsvtaa vltywlgqwd dtlaelesvd qsvsamtyrg
      661 lrergpmwlw hglaaliavr rddraaaegh lraglrqppv tvadrentdf llfaralsae
      721 qkgdphlals hlggvlsrep gemtlihqwl ptvvrlalav dddsaaaaal aacraeaate
      781 qvparataaa dwctglyerd paplrsameh yravgvpvel agtledlavv lveqgntges
      841 krligealdl yggfgavwdi rraearlrry girsgvrgar tkrpahgwda ltptehkial
      901 lvaagsstsd iaqsmfltrr ttqthishil aklglrsrve iareafsrdp aaiptdl
//
LOCUS       WP_181863165             411 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces himalayensis].
ACCESSION   WP_181863165
VERSION     WP_181863165.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 411)
  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 411)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 411)
  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..411
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..411
                     /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=42931
     Region          149..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mivrcsswsr vlawtislav plgtlglldh rwgafsvtgf gappleaall avlvallaph
       61 lkanvlpvaa maaalaslgv asavhamdss dgdrftgldg yafaeavalv vvlgfvtwra
      121 tpvavtvtap allaavvlrp laggvrdtvv avslflalia favvgaglaa rlvaadrlrr
      181 etalqlrqrt efardlhdfv ahhvtgivvl aqgagavaak kpellppale rieqagteal
      241 esmhrmvgml repddrvgpr pvadlggavr rlverfelpg artelveege pgplpaevat
      301 tahhvvmeal tnvrkharhc tsvevsltht edtvrirvsn dggrhrstgg rfglrgleer
      361 vamiggtlrs gpaaqegwlv eavlptgtap tnasgpaapg qghdrtqret v
//
LOCUS       WP_181863247             545 aa            linear   BCT 28-DEC-2024
DEFINITION  N-acyl-D-amino-acid deacylase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181863247
VERSION     WP_181863247.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 545)
  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..545
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..545
                     /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=58378
     Region          1..545
                     /region_name="COG3653"
                     /note="N-acyl-D-aspartate/D-glutamate deacylase [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442870"
ORIGIN      
        1 mdlvirgvrv ldgtgdpsyr adiridggri aeirresdga prlaaggghr tleadglala
       61 pgfidmhahs dlallrdpdh sakaaqgvtl evigqdglsy apvddrtlae vrtaitgwng
      121 ggpgdesidf swrsvgeyld rldhgfdgeg iavnaaylip qgtvrmlavg wddreatpae
      181 ldhmrrlvae gmeqgavgms sgltytpgmy akdselaelc rvvaahggyy cphhrsygag
      241 aleayaemve ltrtagcplh lahatmnfgv nkgrapella lldealdaga disldtypyt
      301 pgcttlvaml pswaseggpe ailarlrdde taerirhhme vvgadgchgv piewdtieis
      361 gvsqpglgsh vgrtiqqsad ergeepwvta rrllledrlg stilqhvghe envqtimrhr
      421 vhtggsdgil qgdkphpray gtfpqylgry vrelgvlsle ecvahlsghp aarlrladrg
      481 lvregyradl vlfdpetvaa gstfeapral ptgiphvlid grfviedgrr tgvlagrair
      541 gagar
//
LOCUS       WP_181863303             308 aa            linear   BCT 28-DEC-2024
DEFINITION  aldehyde dehydrogenase family protein [Streptomyces himalayensis].
ACCESSION   WP_181863303
VERSION     WP_181863303.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 308)
  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 308)
  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 308)
  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 308)
  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..308
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..308
                     /product="aldehyde dehydrogenase family protein"
                     /EC_number="1.2.1.-"
                     /GO_function="GO:0004030 - aldehyde dehydrogenase
                     [NAD(P)+] activity [Evidence IEA]"
                     /calculated_mol_wt=32304
     Region          19..>264
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
ORIGIN      
        1 msehvsisgs aarrlsvfkt yklyvggkfp rsesgrvyev tdskgnwlan aplssrkdar
       61 davvaarkaf ggwagktayl rgqilyrvae mlegrrdqfv revaeaegls kskaaaqvda
      121 aidrwvwyag wtdkisqvvg ggnpvagpff nlstpeptgv vavvapqess flglvsaiap
      181 viatgntavv iageksplpa lslgevlats dlpggvvnil sgrtaeiatp laahqdvnai
      241 dltgadevla keleiaaadn lkrvlrpqpv dnavdwpadp gthrltafle tktvwhptgs
      301 lgasgssy
//
LOCUS       WP_181863297             590 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Streptomyces himalayensis].
ACCESSION   WP_181863297
VERSION     WP_181863297.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 himalayensis"
                     /db_xref="taxon:2820085"
     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=62241
     Region          1..456
                     /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 yadpdrdavh vraadeafal ggdtpassyl
       61 diakvlqaak dsgadaihpg ygflsenaef aqavldadli wigpppqair dlgdkvaarh
      121 iaqragaplv agtpdpvsga devvafaeeh glpiaikaaf ggggrglkva rtleevpely
      181 dsavreavaa fgrgecfver yldkprhvet qcladqhgnv vvvstrdcsl qrrhqklvee
      241 apapflseeq nrqlysaska ilkeagyvga gtveflvgnd gtisflevnt rlqvehpvte
      301 evtgidlvre qfriadgekl gyddpavrgh sfefringed pgrnflpapg tvttftpptg
      361 pgvrldagve sgsvigpawd sllaklivtg atrqqalqra aralaefqve gmataipfhr
      421 avvtdpafap eltgstdpft ihtrwietef vneikpfaap adadaedesg retvvvevgg
      481 krlevslpas lgmslartgl aagakpkrra akksgpvasg dtlaspmqgt ivkvaveegq
      541 evkegdlvvv leamkmeqpl nahrtgtikg laaevgasit sgaviceikd
//
LOCUS       WP_181863288            1114 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Streptomyces himalayensis].
ACCESSION   WP_181863288
VERSION     WP_181863288.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1114)
  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 1114)
  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..1114
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..1114
                     /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=115778
     Region          128..595
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mkracattva aaaavalaag mtnpasange nsstsraaga elgpkhritl itgdrvlvda
       61 kgrvaglera kgrehipvqk rtanghtyvv pfdaqrliaa gkldqrlfdv telnkaahrk
      121 aqkkglkliv gykgasaaaa kaevrgagdt qvrrtlktln adavttpkdd aselwdavtr
      181 eqgngsvttt agvgtiwldg vrkasldksv pqigapkawa agydgkgvki avldtgidat
      241 hpdlkdqvia eknfstsada qdrfghgthv asiaagtgaa spagdggtyk gvapgaklln
      301 gkvlgddgsg edsgilagme waaeqgaqvv nlslggpdtp aidpleaein klsaekgilf
      361 avaagnsgpn slgspgsada altvgavddg deladfsstg prvgdgaikp dvtapgvdit
      421 aaaapgsvid qevgqkpdgy ltisgtsmat phvagaaail kqqhpdwtya elkgalaast
      481 kggkytpfqq gsgriqldka itqsviadpv svsfgvqewp htddtpvtkq vtyrnlgtkd
      541 vtldltatat npkgaaapag fftlgakqvt vpaggkasvd ltvnsklggt tdgtysayvv
      601 atgggqsvrt aaavereves ydvtlshigr dgkpsewyst dltgvsgnvn etwfspyead
      661 gtvtvrvpkg gyvlnsgilv dpdeykgadw laqpklsvtk dttitldart akpvditvpd
      721 aaaesvfasp dytvetdegs ytfgwwldsy anfgtrglgp qvtdgslyqq wdghwtkgat
      781 aeydtkagar vkqlatgytk hykaselatv kvglgasakg kegavtawgy lpesssgsai
      841 sfpqqlpstr tlylstankv kwtfdveqyg gtdedgwpit eagytlgtpq tfkagttytk
      901 tfntgvfgpr lsasygvfrd gntiagylpm yadgknhagy sqylsvkttl yrngtkiaet
      961 edpldgsgef kvpsadaayk lttsikrsvk vgtastrvdt swsfrskktt dmkqlplsta
     1021 rfgpalglds tapagktqsv pvtvqgaakg snlkslsvyv sydygktwkk lsvkngkvsv
     1081 knpakgkgis fhakitdkkg nkstvsiyna yygk
//
LOCUS       WP_181863426             347 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181863426
VERSION     WP_181863426.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..347
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36461
     Region          21..340
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mplprtplav llaavllgla pgsapasatp padaalpllv trgrapaaal ltreengsrf
       61 artgpairra dhfragsvtk tfiatvvlql aaeqrlslsd tvdrhlpgli rghgndgrkl
      121 tlrtllthts glydftadtq gtvplsplqa vrtalahpps erggfaysnt nyvllgmvik
      181 qvtgrsyaae aerriitplh ltgtsfpgah tslpsphgrs ytadgtdvta ldprvagaag
      241 elvstladlg rfyaallggr llppaelhem lntrathgry gmglyplrlp cgttvwghng
      301 riagsyvrta atadgrrvli lrvntdgiae pklepallaa efcprap
//
LOCUS       WP_181863622            1255 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Streptomyces himalayensis].
ACCESSION   WP_181863622
VERSION     WP_181863622.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 1255)
  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 1255)
  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 17582184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1255
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..1255
                     /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=132121
     Region          131..581
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
     Region          799..>862
                     /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"
ORIGIN      
        1 mratprtavt aaitavlavt avapsgaqpr dgaadgtspl vgspaaaqgd gtrqatvtlv
       61 tgdrvvvrtd kdgrstatvl phedgtqplv qtrqsgkdly vypesaipai tsgkadeqlf
      121 nvtglvrqgy ddahtdqlpl iatydtsvdv aesapaaprg serkrvldav dgvalkadkk
      181 kaadfwadvt nsrsraagdl kklwldakve atldrstkqv gapeawaagy dgtgttvavl
      241 dtgadadhpd lkdriaesrn ftdsdtaddr dghgthtist vggsgaasdg kkkgvapgtr
      301 llagkvlndy gygetswiia gmqwavdqka dvvsmslgsp eptdctdpms iaaeelagts
      361 dtlfvvaagn sgpalnrvss pgctpgvltv gavdrndsma tfsspgpapy thtlkpeiaa
      421 pgvgisaaaa ggrgvyayqs msgtsmatph vagaaailkq rhpawsarql kaalvssahs
      481 gipgdvretg ggrldvkaai gqtvlgspav qggtfdwpqt ssdrttvevp ytntsdnpvt
      541 ldlsvtgvtg ndetkvhatv aklgqrsvtv pagetvkvpl tldpsahler sqygdvtgrv
      601 iaegdgvtvs tpfslyvqpe tvtlrvklvd rlgepasgls sldvigtdda sgerrfnega
      661 adqtyelrpg syflsafvat pdnggdlvns laylarpefe ltkdttvvld areahrltve
      721 tdrptedrnt tlafarswdd twlhggsmsg nrqvkgyyas vegrahdgdf efgsywrrya
      781 pqiesfaieg gpqlhpvtas tgsdnldgsg saevvdagsg tvaelaaanv kdkialvkva
      841 ddetylyqqa qdaknagava vvahhasadr wypsvgwtng plpvlalpad eagelldrla
      901 sgpvtvkwqa taaspyvynl afpedapfas draykvrdtk lgrnettyha mgvaadylda
      961 vtayrpnadv yltgffdlva apgkrseyyt agdtsfsqwv sssfpygesm lnaqhayeag
     1021 ekrteswygg vlaptapldd ageqelaaer qgdligiapa fwgdsehagl qgsfgdigsi
     1081 qlridgeeqe sspvpwgvwk vpaedaayel tlttmkfgip grvwkrstmt qttwefrskl
     1141 desvysqglp ilfpqyrlpe dgmktlaaed dqkltlgvtg hagytpgale saqlsysydd
     1201 gqtwteakta vedgtwtatv hhagasgkpv tlkaeltdan gnsvtqivtr aydvr
//
LOCUS       WP_181863472             284 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181863472
VERSION     WP_181863472.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 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 16009431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..284
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31933
     Region          13..70
                     /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          100..276
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 maqsdmptmr srrlgnelrr lrieaglkvt daakalecgq pkvsqiengk rgirpldltv
       61 lfnlygvede ayqaslrrla reihkvdwws sqghllhdsl kdyltleads davrtyepsv
      121 lpgllqteay mraifeagqr penvdalvet rmkrkellap tgdfrlrtvi dapvlhring
      181 srqvvreqle yllkaaqnps vtlqvlpvsa avptwqyvpv hiftlrgepp advawlehmt
      241 ggtlleqrrd vqvyvqgwnd ltaaalspse srryirglle esgs
//
LOCUS       WP_181863698             148 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Streptomyces himalayensis].
ACCESSION   WP_181863698
VERSION     WP_181863698.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=16771
     Region          1..134
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 marhiyscpl rwsdmdafgh vnnvvflryl eearidfmfr lapgdgspsf sggsvvarhe
       61 idyvrplvhr hepvtveswv tkinaaslti ayeikdpdqv yvrastvvvp ynleaqrprr
      121 itaeektylq qylegeksed dksealaa
//
LOCUS       WP_181863774             629 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces himalayensis].
ACCESSION   WP_181863774
VERSION     WP_181863774.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=67792
     Region          1..626
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 msdtqtlien rppsvatlfl ervaatpdae ayrypvpsss gegpdewksl swaqaaervy
       61 aiaaglielg vqpeervala sstrvewils dlgilcagaa tttvypqtna eesafilsds
      121 dsrvliaeda aqlakarekr aelpglthvv vidpkgveaa adepegwvlt laelevrgaa
      181 yleknpdlik kkvsaitadq latliytsgt tgrpkgvrlp qdnwsymaka iaatglvaad
      241 dvqylwlpla hvfgkvltsg qievghvtav dgridkiien lpvvqptyma avprifekvy
      301 ngvaakarag gpakykifqw asevareyak vtqdnfrrtg tasapfglta khkiadalvy
      361 sklreafggr lracvsgsva lapeigyffs gagihilegy gltessaasf vnpgeayrtg
      421 tvgkplpgce vriaedgeil lrgpgimegy hglpektaev lepdgwfhtg digelspdgy
      481 lkitdrkkdl fktsggkyia pteiegqfka vcpytsnivv lgadrnfcsa lialdeaail
      541 gwaaenglgg ksyaevvaap etvelidgyv qkmneglqrw qtikkfkllp rdldvehgel
      601 tpslklkrpv vereyqhlie emyagarea
//
LOCUS       WP_181863906             326 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Streptomyces himalayensis].
ACCESSION   WP_181863906
VERSION     WP_181863906.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..326
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..326
                     /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=34965
     Region          1..320
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 mhpfsytrvs dtrealaags rggryiaggt tlvdlmretv erpealvdis glplrevsat
       61 ergglrigal vtmsqaaadr kvrtlypvvs ealelsasaq lrnmatiggn imqrtrctyf
      121 rdvtadcnkr dpgsgcaard gfnrmhailg tsdscvathp sdvavafaal eaqvhllgpd
      181 gertlpfadf llrpgntpnr eqairqgeli taveipalpr plrsgylkvr drqsyefalt
      241 saavalhisg gvireakvaa ggvgtvpwkl paveqhlige rpseslwaaa aakaadgarp
      301 lqhnrfkpql lnrtverqlr ivgens
//
LOCUS       WP_181864045             274 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Streptomyces himalayensis].
ACCESSION   WP_181864045
VERSION     WP_181864045.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 274)
  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 274)
  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 274)
  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 274)
  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..274
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..274
                     /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=29746
     Region          196..>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 mtttlrpiep lqhdaggars rryqvcvnsr pagaihlgth pvfgpaaaqi relhiderdr
       61 rrgrgtvaal aaeevargwg crrmevsvpa daeaalrlvt algyvqrnrg mekplgttpp
      121 alpegslgrp mteaeygpwl ahgkehyaqs wikrgvseae araksekdha tllpdgpatp
      181 dmllsvlehq gdaigtlwvg lrdddafvfd veaderyrgr ghgrslmlla eaqaiaagrp
      241 riglnvfagn tpaerlyesl gyaptvyamy kdll
//
LOCUS       WP_181864364             287 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Streptomyces himalayensis].
ACCESSION   WP_181864364
VERSION     WP_181864364.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 287)
  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 287)
  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 287)
  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 287)
  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 287)
  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..287
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..287
                     /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=30018
     Region          8..275
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mpapelispr sprisaarrl arrnfrgker rflaegpqav reavryrtde gpalvelfat
       61 peaaeryadi vadaraagar vhlaadevig eisttvtpqg lvgvcrfldt dfddilaarp
      121 rlvavlahvr dpgnagtvlr cadaagadav vltdasvdly npkavrasvg slfhlpvavg
      181 vpveravqgl kdagvrilaa dgagehdldt eldhgtmggp tawvfgneaw glpeetrdla
      241 davvrvpihg kaeslnlata aavclyasar aqraaggcra tasgqnr
//
LOCUS       WP_181863857             241 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Streptomyces
            himalayensis].
ACCESSION   WP_181863857
VERSION     WP_181863857.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=25728
     Region          6..237
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mdkplvails gagistdsgi pdyrgpkglw rrdpeaeklv tyehymadpe irrrswqmrr
       61 knrtlqaqpn aahlavvdle rsgvpvrvit qnvdglhqla glpdrkvlel hgtarsvmct
      121 gcgarssmed alarvaagee dpscldcggi lksatvmfge rldpevlgqa vaitkacqvf
      181 iavgttlqvq paaglaglaa dhgarliivn aeptpyddqa devvrepigt alpellrsla
      241 h
//
LOCUS       WP_181864391             317 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181864391
VERSION     WP_181864391.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=34945
     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 maiskaerlm nlalcllgtr rplskrelrg sieayleags ddsfnrmfer dkddlrelgl
       61 vietvenldg evgylarrds nrlppvtlda eeaaalglaa kvwqqarlag aasgalqklr
      121 aaglpedvdp ygahgaleph ipvheaafep lmlacrdrrp vafeyrkata arpelrqvep
      181 walecwrghw ylagwdrerg aervfrlsri tgkvrnrpgk ftaavpdvvt vretvaswag
      241 etadrsalir lragagyplr akavsvrelg dgwdeleipy ghgldawlve fgpdvvvlep
      301 aelradvvdr lravakg
//
LOCUS       WP_181864197             426 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase 5 family protein [Streptomyces himalayensis].
ACCESSION   WP_181864197
VERSION     WP_181864197.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 426)
  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 426)
  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 426)
  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 426)
  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..426
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..426
                     /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=46334
     Region          26..355
                     /region_name="COG3934"
                     /note="Endo-1,4-beta-mannosidase [Carbohydrate transport
                     and metabolism]"
                     /db_xref="CDD:443135"
ORIGIN      
        1 mstphastas tasttsttvp pspplrfgvn ytprrgwfhs whdfdpahar edlaqiaalg
       61 ldhvrvfhlw pllqpnrtli rttavdqlvh lvdlaaeagl dvlvdgvqgh lssfdfypew
      121 trswhhrnvf tdpeaieaqt dllralgral dgrpnliglq lgnelnnlve hnpvtagevd
      181 hyldtllaaa reglggdhlv thsafdaawy gddhpftpea sarkgdlttv hpwvfsgdca
      241 rrygprspqv lhlaeygvel akayardpar avwvqetgap ephipaadap efaratllna
      301 agcaglwgvt wwcshdvdrs ladypeleyt lglfdstgra kpiadalaat vaelrakprs
      361 tpprstalvl ectpatrsvs gpgggffeaw mrlrtegirp avvlaeraed tayltargva
      421 dvlrms
//
LOCUS       WP_181864408             223 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181864408
VERSION     WP_181864408.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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..223
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..223
                     /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=24218
     Region          3..216
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msrfalikav lgpimrlmfr pqvegaehip gtgpvilagn hltfidsivl plvcdrqvvf
       61 igkdeyvtgk glkgrlmawf ftgvgmipvd rdganggvaa lmtgrrmlee grifgiypeg
      121 trspdgrlyr grtgiarltl mtgapvvpfa migtdklqpg gagmprpgrv tvrfgeamef
      181 sryegmdrdr yvlravtdsv maevmrlsgq eyvdmyatka kaa
//
LOCUS       WP_181864298             298 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Streptomyces himalayensis].
ACCESSION   WP_181864298
VERSION     WP_181864298.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 298)
  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 298)
  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..298
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..298
                     /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=33583
     Region          64..241
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mrllpklnqa fasatgyqvr rvvsapttpa kkapaksapp kkrpdvpfrc pddpevdrll
       61 rqpvfimspv rsgstllrml lnahprlhap helhirrlev gfgsklsqka msaldlergd
      121 lehllwdrvl hreltrsgkd fivektpsna faykriaacw pdakfvfllr hpvsiarswh
      181 eadpekrtyd eaaadalrym kavenarkgl tgghtiryeq ltedpegqlr slctflgidf
      241 dasmlayger qdgdlvkglg dwrdkirtgr vqagrelpke deipevlrpm cvswgyas
//
LOCUS       WP_181864579             241 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Streptomyces
            himalayensis].
ACCESSION   WP_181864579
VERSION     WP_181864579.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 241)
  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..241
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..241
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=25900
     Region          2..102
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msprrsydqy cpaaraldvv gdrwtllivr ellagprryt dlhadlpgvs tdvlasrlrd
       61 merdglttrr rlappgaayv yeltwrgrel lpvlqalgew gapaleerrs tdavrahwfa
      121 lpllrrleal ggdpgvvevr ieegefhvrv gaseslsgtg krrsgsadsg sadsgsadsg
      181 stdsppygeg papqtpdarl rldaetciav segtlalsdg vregrvevlg dsalakwlre
      241 g
//
LOCUS       WP_181864124             483 aa            linear   BCT 28-DEC-2024
DEFINITION  rhamnulokinase [Streptomyces himalayensis].
ACCESSION   WP_181864124
VERSION     WP_181864124.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 10167330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..483
                     /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=50810
     Region          9..458
                     /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 msagtagsfa avdlgassgr vmvgrvgpgt ldltevhrfp nrpvrlaegl rwdiltlysg
       61 vldglraagq vdsvgvdswa vdyglldadg allgnpvhyr dartegvaek vwatvpaeel
      121 yaatglqyap fntlyqlvaa hdtaqltaae rlllipdlis ywltgeagte ltnasttqli
      181 dprtrdwsyd taarlgidls lfaplrnpgd paghllphvl eetgltgpvp vtavgshdta
      241 savaavpatt erfayictgt wslaglelda pvlseasrta nftnelgldg tvrylrnimg
      301 lwllqeclrs wggpdlpall qdaaqveplr avvdagdaaf lapgrmperi adacratgqp
      361 vpgspaettr cildslalah rraiteaqql adrsvdvvhi vgggahnell cqltadacgl
      421 pvvagpaeaa algnvlvqar arglvghras mrellartqp lrryepagdt aawraaeari
      481 tap
//
LOCUS       WP_181864615             403 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181864615
VERSION     WP_181864615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..403
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43677
     Region          1..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 mgndafdgvr vvelaqwvfv pvagalladw gadvirverp egdpyrglst qgigsdstgi
       61 nlsvalanrg krsvaldlrs degprlldrl ldtadvflts lrpaalrrlg ldaeelarrf
      121 prlvyarghg fgvrgpgadr agydssafwa qggmahvltp perdhpisqr gamgdrngam
      181 alafgissal lrrertglgs vvdvsllata mwtlssdvla alaggkprgv sgrggavnpv
      241 vgayrtkdgr hiqlvflesd rywpefcrli grddligdpr fadlrargen reacvaelea
      301 efalrtfdew kdllsridap wapvqaveel lsdpqvlang yvgeveledg ssyrlptvpv
      361 qfderppalr rapehgehte avllelgftw eriaelkdag vip
//
LOCUS       WP_181864705             462 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181864705
VERSION     WP_181864705.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 462)
  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 462)
  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..462
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..462
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49446
     Region          9..324
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mtplhgellp atrrallhri ataqaegrtp slvtavvrgd elvwsgarsc vdghapddnv
       61 qyrigsitkt ftavlvmrlr degvldlgdp lekhlpgtga gevtirella htgglaaetp
      121 gpwwertpgs lrpeladvlg dqpfrhpsgr rhhysnpgyt llgslveevr gapweevlrr
      181 evleplglhr tsgqpaapha ggwavhpwad vmmpepaedl grmapagqlw sttgdlarfa
      241 vflakgderv lsadsvlemr tptappdtae vaegrayglg mqiqyrdgrt lvghsgslpg
      301 flagltisvd ddlaaivlan atsgplvtmv asdlvwivae aepripepwr plaevdtall
      361 elagpwywgt qagvlrlasg gdlelgplsg pgrrsrfran ddgtwtgldg yyagevlrav
      421 rrpdgsvshl dlgsfvftre pyeegasvpg gvdpegwral pq
//
LOCUS       WP_181864814             850 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces himalayensis].
ACCESSION   WP_181864814
VERSION     WP_181864814.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 850)
  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 850)
  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..850
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..850
                     /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=91010
     Region          3..832
                     /region_name="PRK10490"
                     /note="sensor protein KdpD; Provisional"
                     /db_xref="CDD:236701"
ORIGIN      
        1 margklriyl gaapgvgkty amlseahrrv ergtdcvvaf vehharprte vmlhgleqip
       61 rkelayrett ftemdvdavl arrpqvalvd elahtnipgs rndkrwqdve elleagidvi
      121 stvniqhles lgdvvesitg vrqketlpde vvrradqvel vdmspealrr rmahgniykp
      181 dkvdaalsny frpgnltalr elallwvadr vdeylteyrs ehhvsaiwgs rerivvgltg
      241 gpegrtlirr aarlaekgag gevlavyiar sdglssaspk elavqrtlve dlggtfhhvv
      301 gddipaalld fargvnatqi vlgvsrrksw qyvfgpgvga tvaresgpdl dvhlithdea
      361 gkgrglpvar garlgrarmi wgwlvglggp alltlllsta aldvglandv llfltvtvaa
      421 allggllpal asaavgslll nwfftppvht wtiadpkniv aiavffgvav svasvvdlaa
      481 rrthqaarlr aeseilsfla gsvlrgetsl dallervret famesaalle rendtapwtc
      541 agnvgrgpvv erpedadvdv pvgdhmalal sgrvlpaedr rvlaafaaqa avvldrqrlq
      601 seadqakela egnrirtall aavshdlrtp lagikasvss lrsddvewse edraelleai
      661 eegadrldhl vgnlldmsrl qtgtvaplir evdldevvpm alvgipdhds avvldvpetl
      721 pmvavdkgll eravanvven avkysrvgep vavsasalae rvevrvvdrg pgvpdeakdr
      781 ifepfqrygd aprgagvglg lavargfaea mggtltaedt pgggltmvlt lpaarshasv
      841 paelpatars
//
LOCUS       WP_181864774             273 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            himalayensis].
ACCESSION   WP_181864774
VERSION     WP_181864774.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 273)
  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 273)
  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..273
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..273
                     /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=27676
     Region          18..273
                     /region_name="FabG"
                     /note="NAD(P)-dependent dehydrogenase, short-chain alcohol
                     dehydrogenase family [Lipid transport and metabolism];
                     COG1028"
                     /db_xref="CDD:440651"
ORIGIN      
        1 mqvsvpdvss rslaelisls grravvtgag rglgraiaer vveagadvlv adiehglaat
       61 vaedltarrt gcavaahvdv tdagsvaaaa dlavrelggv diwvnnagif psvpalemse
      121 ktwdevfavn trgvflgsre aarrmreags ggvivnvvst agfrgtapgl aayvgskhaa
      181 rgitrqlale fapfgirvlg vaptfvpteg nmaaaaeagl pldaeslmsv mkpgplgrlg
      241 vpddiarvvl fcasdlsafm tgstlladag eti
//
LOCUS       WP_181864939             369 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Streptomyces
            himalayensis].
ACCESSION   WP_181864939
VERSION     WP_181864939.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 369)
  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..369
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..369
                     /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=39028
     Region          9..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 metelskklg iehaifgftp fpavaaaisr aggfgvlgav rytapdelkr dldwieahve
       61 gkpygldvvm pakkvegvte adveamipeg hrqfvkdtla kygvpqlaeg easgwritgw
      121 meqvartqld vafdypirll analgsppad vikrahdqgv lvaalagsar harkhadagi
      181 divvaqgyea gghtgeiasm vltpeaveav aplpvlaagg igsgeqvaaa ltlgaqgvwl
      241 gslwltttea elhsraltrk llaagsgdtv rsraltgkpa rqlrtewtda wddpagpgpl
      301 pmplqgllva eavsriqkye vepllgtpvg qivgrmnser svqavfddlt rgferavdrl
      361 nriagrglr
//
LOCUS       WP_181863914             344 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Streptomyces himalayensis].
ACCESSION   WP_181863914
VERSION     WP_181863914.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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 344)
  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 344)
  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 344)
  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..344
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..344
                     /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=35758
     Region          15..342
                     /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 mteqirrvlv rslyditleq vpapvpgdde llirttvvgv cgsdthaaag hhpfvdlpyr
       61 pgheavgiva aagngaedfv pgdrviiepn lycgrcpqcr sgrynicqel kvfgcqtpga
      121 mtdlftipad rvhrvpdgmt dieaalvepl atpvhavaka gdltgrtvvv lgagpigllv
      181 laaarhagaa kiavtdllpg krdralrlga dralpadatd ladqahaalg gpadvvfdcv
      241 areqsiaqat dlvtkggtii vvgvgaagtt pvrldlvqdr eiriegtlmy tgddyrtams
      301 lissgaidta eivtatyple daakafaasv dpeqvkvlvt vdgp
//
LOCUS       WP_181865005             608 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Streptomyces himalayensis].
ACCESSION   WP_181865005
VERSION     WP_181865005.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 himalayensis"
                     /db_xref="taxon:2820085"
     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=66371
     Region          18..608
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mrefttppla lpppvgglad avfdhavedp lrialgrkgd dgqwhdvtsg efrdevlala
       61 kgllaqgvrf gdrvaimsrt ryewtlfdfa lwtigaqvvp vyptssaeqv fwmmhdaqvt
      121 aamvehedha mtigsvidrl prlhrlwqld edavqelyea gahidddvvh rhrravtpes
      181 vatviytsgt tgrpkgcvit hgnfmfeadt vierwepvfh skrgdeaatl lflplahvfg
      241 rmvevaairg rvklghqpql naaallpdla afrptfilav pyifekvfna arrkaekdgk
      301 agafakavdv avryadavea kafgtgpgps aalrmqhqlf dklvyskvrd amggrvrham
      361 sggsamdrkl glffagagvl vyegygltes taaatanppe rtrygtvglp ipgatvhiad
      421 dgevwlhggh vfqgylndpk atdatlhdgw latgdlgsld edgyltisgr kkeilvtssg
      481 ksvspavlee rvrdhplvaq civvgndrpy iaalvtldae avehwlqmrg kptpkpadlv
      541 hdtdletevr ravvaantlv sqaesirtfr ilahqfteeh glltpslklk rkaieqayat
      601 evealyra
//
LOCUS       WP_181865008             312 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Streptomyces himalayensis].
ACCESSION   WP_181865008
VERSION     WP_181865008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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..312
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..312
                     /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=35211
     Region          67..243
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mqdprwdavr kglrrrgrll gealkppapk psaaaqerpl dgipaqrapr pegpavepar
       61 rlvespvfll spvrsgstll rvllnshsri raphemhlrt lhvredrdft vtamralgln
      121 reelehmlwd rvlshelers gkdlivdktp antlmwprlr rawpearyif lirhpaavve
      181 sltarrqdpd ldeihaevqr yaerleqaqe aldgvtvaye dltadperet rrictylgie
      241 weeamldygs qdhgkfrphi gdwsekirsg riqpartatd csglperlve iaegwgygvs
      301 gaqgvdsgmp pa
//
LOCUS       WP_181865101             408 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181865101
VERSION     WP_181865101.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 408)
  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 408)
  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..408
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..408
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43908
     Region          11..408
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 maqlrqevdp aeagldaeal erldrhfarl vdegrlpgyl vvlarhgkva hvtaygcrnr
       61 eaalpvetdt lwrmysmtkp vtsvaalmlc eegliglddp larylpafad pqvydggegn
      121 diktrpaegp irirhlltht agltfgfyys hpvdglyraa glessvpsga dlaetcdvya
      181 slplqfepgt qwnysvatnv lgrvievasg rpldeffaer ifgplgmpda gfcvaedqae
      241 rlgelygena dgsisaiagl plhgrprfls gsggmvasal dyhrfmeflr rrgeldgtrl
      301 lspstvdamv snqlpggadl rtfgspahae pgnsgigfgf gvsvvvdpdi tqapshlgty
      361 gwsgvatttf wvdpqkdltv qfltqvrptt shtlyadlkr lvdeaivg
//
LOCUS       WP_181865019             257 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            himalayensis].
ACCESSION   WP_181865019
VERSION     WP_181865019.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=26961
     Region          8..252
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mpnsqpdiai vtgaasgigr aaalrladsg wsvaavdisd tglaslaehs pnirpfvcdi
       61 tdppavaeav krisdeigsp rrlihsagia kvgqlldqdp adtlrlmnvi yggtlhliha
      121 vvpamvsrgg gqivllgsia gwvpvpeggg ygaakaavhl laetlsvecr eqgiqvlcvc
      181 ppavetpmld rmrrdapamf gprpglttda vldsmdrala rgrlwafpgr gthamwtarr
      241 maprlvsrii artivrq
//
LOCUS       WP_181865105             420 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181865105
VERSION     WP_181865105.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..420
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43153
     Region          26..411
                     /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 msskdvppdd gsgavggagr galaglriad fsrvlagpya tmlladlgad vvkverpgtg
       61 detrewrppa dengtstyfl gvnrnkrsva ldltnetgre raraliaesd vlvenfrpgt
      121 mdrlglgyad lrarhprlvy csvsgfgadg gaaipgydll vqavgglmsv tgeadgepvk
      181 tgvalvdvit glhatlgima alrhrdatge gqrvevsllg sllsamvnqa sgyalagvvp
      241 grlgnahpsi apyetfptad rplalavgnd gqfvalaavl gcpgladddr frtnpgrvah
      301 raelrkllge rlltagadhw satllaagvp agpvntldea fafahrlglp givsvpvpvp
      361 vdgsadgstd gsapapvsrq vahpialses paqyrlpppg lgehtaevfr rtagdtpeta
//
LOCUS       WP_181865131             403 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181865131
VERSION     WP_181865131.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..403
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43205
     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 mpstalagir vldlsrilaa platqmladl gaevikierp gtgddsrayg ppfadgpege
       61 rtdtaafyls cnrnkqsvtv nhataegqal iralaarsdv lvenfragtl akygldhesl
      121 revnprlvyl svtgfgqsgp yaqrpgydgi fqamsgmmsv sghpdepmkv gvsmvdiltg
      181 lyaatavlaa lrhrdatgeg qfidlslldc glaslshfam nylvsgevpr rrgnggyggi
      241 psqafmckdr plflvagndk qfaafcaaad rtdllqdprf attsarithr eeilpvlegi
      301 mrtrtrdewl aildehdvpa gpfnempevf adpqiqhrgm lvevedpvsg rlpllanpir
      361 faatpvegya appalgehta dvlgrlagvt erqlaelrar gvv
//
LOCUS       WP_181865195             100 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces himalayensis].
ACCESSION   WP_181865195
VERSION     WP_181865195.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=11076
     Region          2..85
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 maddlfkala dptrrtilde laeksgqtlf eicsrlsmkh qlgisrqgvs qhlavleaag
       61 lvetrregry kfhdlntapl rqiaerwlvp dtsgpeests
//
LOCUS       WP_181865082             567 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Streptomyces himalayensis].
ACCESSION   WP_181865082
VERSION     WP_181865082.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=61462
     Region          35..>420
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mssaiwtgve wtnlsdqlcs gakvvsvwdl apsdprlvgp yrtravlgeg gmgrvllatd
       61 aggelaavkl vqgafaaydd sfrqrlhlea laaqrvesph tarvikadan agvpwlayef
      121 hhgptlrqal naagplnedt alhlaagltt alrdihahny ihrdlspsnv llttdgpvvi
      181 dfgvvrpthh sddtshhtra ititrtgtvi gnpgfmspeq amgvshltpa sdlfalgtvl
      241 vmattghnpf qgatseqtrl nimtrepdlh qvpprlrrii epcfarnhtd rpnatdilqs
      301 igalprthrp wpqpihqlie dqktevqrya hidptailpg preldptkif tssrepgsts
      361 gagsrakrsr qrliavvaat vvvvagvlwt vvssgrsgad dapgagtsqd pspkvdhafa
      421 nttqgdcfrn agdmqipdfr aadcdgdvfe avrifknttd lsvcnyvdrv ewrysarnpd
      481 vtvclvyqhs ggtaynadqg dcvygesedt vwsleecrsg nftvvarfeg rsstqdceev
      541 pdhqqsryft vsgmpelnvr lclalqp
//
LOCUS       WP_181865311             419 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181865311
VERSION     WP_181865311.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=44301
     Region          10..>83
                     /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          51..399
                     /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(69,71,243,263,331)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 marprtpqpp vllraarlld vdkgeyvqpg elliegeriv evaptsvpkd avvldlgdlt
       61 llpglmdmev nlllggpdhr splnpvqddp avrtlravan arrtlrsgft tvrnlglfvq
      121 tggllldval kkaidlgwid gprvvpagha itptgghldp tmfqafaphi melsveegia
      181 ngvsevrkav ryqikhgaev ikvcasngvm shtgpagaqq ysdeelraiv deahragrkv
      241 aahcmgdtai raaldagidc iehgslasde tldlmvergt flvattylte gmdvshaape
      301 lqakaadvfp rsratigkai ergvriacgt dapavphgrg akelialvdr gmaplqaira
      361 attvaaelid addrgrleag lladviavpg dpltdigvte nvrfvmkggq vyrheeptg
//
LOCUS       WP_181865331             359 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces himalayensis].
ACCESSION   WP_181865331
VERSION     WP_181865331.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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 359)
  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..359
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..359
                     /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=38815
     Region          54..356
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mhrrpglsar lkltlsyagf lavagallla vvwvfllryv pdnpqgllgi apnryllvrt
       61 fapaaavamv fllvfglvgg wilagrmlap ltqitaaarm agngslshri rmdgrqdefr
      121 eladafdtml eqleshvaeq qrfaanashe lrtplaisrt lldvarkdpt rdhdelferl
      181 qavntraidl teallllsrs drgnftresv dlslvaeeaa etllplaeqr ritldvtgga
      241 trtsgsaell lrmvtnlvqn aivhnlpagg tvtvhtesqh dasvlrvent ghplpselvp
      301 tltepfqrgt ervrtdehag vglglaivhs ivrahdgtld lvprpaggll itvrlpgtp
//
LOCUS       WP_181865519             434 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Streptomyces himalayensis].
ACCESSION   WP_181865519
VERSION     WP_181865519.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  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 434)
  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 434)
  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 434)
  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..434
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..434
                     /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=45730
     Region          136..392
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mrqrvlrval vavlvalvvl avplaaamra yffaderdel erdaltaavr vgpdftsgdp
       61 velpagggdv rlgvydmrmr lragegpara dpdtrradtg tvvrgraggd lvvavpvsqn
      121 eqvigvvras spawgvwlri llawlallga algalavavl varrqarvlt aplealsrqs
      181 ravtegdlta raapsaiaei dqvarthnam verlahllqr ernftantsh qlrtplaglq
      241 lgleaaladp rtdprtalee alesthhlhh tidevlrlag perspmpepa aaqllgeald
      301 saeqrwhglf adagrrfiva aepgtrempv pgrtvgqild vlldnarghg rgtaevtars
      361 lgetvaldvr degilridpa vlfdrghttg pgagiglala adlaeaaggr lvlagtdptt
      421 ftlllppgpa etnd
//
LOCUS       WP_181865624             274 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181865624
VERSION     WP_181865624.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=30830
     Region          12..265
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 maepvvripd akvalstasv ypestatafe iaarlgydgl eimvwndpvs qdiaalrrls
       61 dyhripilav hapcllitqr vwstdpwvkl qraksaaeql gastvvvhpp frwqrqyard
      121 fvrgiwrmad etdvrfaven mypwryrdre mlayapewdv tkddyrhyti dlshtatart
      181 dalqmidrms drlghvhlad gtgsgkdehl vpgrgtqpca evlerlalng fdghvvlevn
      241 trramssaer eadlaealaf trlhlasavr vprs
//
LOCUS       WP_181865742             402 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181865742
VERSION     WP_181865742.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=44612
     Region          1..394
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mmraykfllr ptvrqeqala emlrdhcsly ngalqerrda yrhssktsik ygdqsaqlkd
       61 irrfdpqrqg rwsfssqqat lrrldkafka ffrrvkagqt pgyprfkgvg hfdtvifpkd
      121 gdgcrwdstp hdrqtrvrlq gvghvrvhqh rpahghvkti sikregrrwy vvlacddvpa
      181 eplpptgaiv gidmgithfl ttsdgknvan pkllnaaaee laaaqrhlat fpkrtrqrtk
      241 khraaarkva klhakvrrqr ldfhhktaha lirdhdtiah erlntagmtk apapkpdpen
      301 dgaflsncaa akaglnrsil dagwgqflti lankaesagr lviavdarnt srtclecghv
      361 saenrvtqak fkctacgfta nadhvgatnv lnraglalcd aa
//
LOCUS       WP_181865672             711 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Streptomyces himalayensis].
ACCESSION   WP_181865672
VERSION     WP_181865672.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 711)
  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 711)
  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 711)
  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 711)
  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..711
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..711
                     /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=77419
     Region          33..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 mtgtpdgped rlrrfatiws raifpvtats ltrpefeqql lplarrlrda lrartfdaaa
       61 gkavgaglvd thctepeals rtldvvdayl vlycgtegaq eeqrvrsarl qhaaaagfaq
      121 alrertlteq eaiyraalda raavaaalhn searfravfq eaavgvgiad ldgsilevnd
      181 alirmfgisg qtmrgynvmd whhpedapqv wrlydelvrg erdhyrvekp fsrpdgtvlw
      241 tnltvsllrd aegrpeyqla lmedtterrl lnlrlryeat hdaltglpnr tlfferleka
      301 lsagegqrfg lcyldldgfk tindslghaa gdrllvevad rlgscatapg emvarlggde
      361 fvalttgpdt qaeveelaar imnalaapir vdgreltvrg smgvvegpag ergsaevlrs
      421 aditmyraka aggnryetad aeaealaitr hglttalpsa ldrgeffiey qplvhlgdgs
      481 vrgaealvrw lhpqhgvlgp drfiplaeht glivplgrwv leqsvkqarr wqerhadagp
      541 lrinvnlspc qlthpglvsd tvailqaagl aanalclevt esaligaddd llkplrrlae
      601 mgvdialddf gtgysnlanl rrlpvsvlkl drsftqsmqr fpadpvdlki vegivalahs
      661 lnltvtvegv etgaqaeqlr ilgcdtaqgw yyarpgppdr lhelalvdaa s
//
LOCUS       WP_181865755             106 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces himalayensis].
ACCESSION   WP_181865755
VERSION     WP_181865755.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=11488
     Region          14..104
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mtttpppstt padepirale aasdllkala spvrlgivre lseggkyvhe lvaalgvsqp
       61 lvsqhlrvlr nsrivttrrq areiqygltd ehiahivlda irhaqe
//
LOCUS       WP_181865576             130 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system VapC family toxin [Streptomyces
            himalayensis].
ACCESSION   WP_181865576
VERSION     WP_181865576.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..130
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=13618
     Region          12..128
                     /region_name="VapC"
                     /note="Ribonuclease/mRNA interferase VapC, contains PIN
                     domain [Defense mechanisms]; COG1487"
                     /db_xref="CDD:441096"
ORIGIN      
        1 msgtlvldce glsklvrrtp eltewlaaae aedirvvass vtlveardpk tnqarfdyav
       61 srvniippte aiarhaskil aaaglhghky aldaivaata laspapvtil tsdpedllil
      121 cgpgirvlkv
//
LOCUS       WP_181866065             304 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Streptomyces himalayensis].
ACCESSION   WP_181866065
VERSION     WP_181866065.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..304
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32905
     Region          7..296
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 melvidahga elpatltlpd gpargglipl hgshcgnrdf vlyehlaevl pahgiavlry
       61 drrpsrlgvd vpfvdqaada raaisllrrh igdaaiglwg fsqggwvapl aaatwpdeva
      121 fltlvspsgv spgaqmrygl aqqlrnngfa dcldeltrfq damaaylrgq sdaetmreef
      181 akaasqpwwp llgydfsddv fnappgelwv dmdadltssy eavrcpvltf hgetdqwlsi
      241 desigiwrea saksgrpape virlpgcdhv ptirtgdttg isptyekall dwlnrhavsp
      301 kaav
//
LOCUS       WP_181866018             237 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 12 protein [Streptomyces himalayensis].
ACCESSION   WP_181866018
VERSION     WP_181866018.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  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 237)
  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 237)
  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 237)
  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 237)
  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 10012694
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..237
                     /product="glycoside hydrolase family 12 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0008810 - cellulase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000272 - polysaccharide catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25145
     Region          1..237
                     /region_name="PRK06215"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:235746"
ORIGIN      
        1 marrtlsrlt kallapalal gatiglaaap aqaavwnscd qwgnttlngy tlynniwgsg
       61 agsqciwans gtnwgvwanh pntggiksyp nakkvinksi tslgslsssy nvtvpssgay
      121 ntsydiwdtd ydyeimlwvn yngavgplgt sqgnvtlggh twtvykgnng anevfsflrt
      181 sdsnsgtvni lpilkwikdt kgwmgnetig dvqfgyeits ssggldfqtn tltvsss
//
LOCUS       WP_181866140             333 aa            linear   BCT 28-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Streptomyces
            himalayensis].
ACCESSION   WP_181866140
VERSION     WP_181866140.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=36328
     Region          16..331
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mtealteqsa grqpkpript idlrpwltgd pearaeiart vdealqtagf llvtghgvdp
       61 slrariraaa reffalpasa kepysakvgg rgwlgpgaea ngysegtetp pdlkesltfa
      121 thepfedpei naewyapnvw paevpelqml ceeylarmge lenqllsllg ealglesgff
      181 trhmdhptyg fninwypgte vvgapqegqf rigphtdfgt vtildrqagk gglqvftdeg
      241 gwedapydpe aftinigdlm arwtgdrwrs grhrvlpppa dapaeelmsl vyfgectpgt
      301 lvesvpapvg rvayepvdsh vylraqldai tvg
//
LOCUS       WP_181866246             226 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Streptomyces
            himalayensis].
ACCESSION   WP_181866246
VERSION     WP_181866246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=23282
     Region          1..219
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mstiaiigag pgmglaiart fgsrgfdval iartkdrldg lveqlgtegi taagfaadvl
       61 drpsltaale aararfgsid vleyspaphs pvpgftqavp seatvenlqp qieytfygav
      121 eaaravlpam reagagtllf ttgggsidpv pmlgnvnaag galrnwvlnl nkelagsgvy
      181 aghvainvwi gqggpegfpt atpeqiaply welheardra eavfna
//
LOCUS       WP_181866273             326 aa            linear   BCT 28-DEC-2024
DEFINITION  phosphotransferase family protein [Streptomyces himalayensis].
ACCESSION   WP_181866273
VERSION     WP_181866273.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  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 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..326
                     /product="phosphotransferase 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=36161
     Region          1..259
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mtrdqlaeaa raalgggrrl dalerlaggs rkgvyrltmd dattaiaylw eesenywpaa
       61 egdddltdpf spgvgldlfe aaharldslg lrvpevhlvd rdrshypadl aivedfpged
      121 lldllnrdpr aaeptmarla daltamrshr aptfgkvali dagrtsrats ceqaaldfal
      181 rclaeaasrd rriadahdrl eerlrefaaa vrpraeysvv hgelgldhvl vdrdgnpvli
      241 diedllyfdi ewehvflqlr hpgshyqwla vegldedrla lytltqrlsl tagplrlleg
      301 dfpdrefmqg iaehhlneal alvsvv
//
LOCUS       WP_181866085             459 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Streptomyces himalayensis].
ACCESSION   WP_181866085
VERSION     WP_181866085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=49388
     Region          34..450
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mtsrsskata rtssearava rtqtllkgkd gigtvrrttl pgglrvvtet lpsvrsatfg
       61 iwahvgsrde tptlngathy lehllfkgth rrsaldisaa idavggemna ftakeytcyy
      121 arvldtdlpl aidvvcdmlt gslieqedvd aergvileei amteddpgdc vhdlfahtml
      181 gdtplgrpvl gtvdtvnalt adrirrfykr hydpthlvvt aagnvdhakv vrqvrnafek
      241 agalsgtaae plgpregrra iraagrvdll drkteqahvv lgmpglartd errwamgvln
      301 talgggmssr lfqevrekrg laysvysyts gfadcglfgv yagcrpgqvh dvlkicrdel
      361 ehvaahglsd deigravgql sgstvlgled tgalmnrigk selcwgeqms vddmlaniaa
      421 vtpddvreva rdilgqrpsl svigplkdkq aarlqeavs
//
LOCUS       WP_181866335             115 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Streptomyces himalayensis].
ACCESSION   WP_181866335
VERSION     WP_181866335.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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 11448415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=12228
     Region          7..107
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mskasapsgd ellkvlsalg nphrmriiaa lsegrnyvsa lareigmgrp llhmhlqrle
       61 aaglvtgsle lsesgkamky feltpfsyvl tpdavaeaar tltedekttv kesas
//
LOCUS       WP_181866352             145 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system VapC family toxin [Streptomyces
            himalayensis].
ACCESSION   WP_181866352
VERSION     WP_181866352.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 10006427
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..145
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=15670
     Region          3..144
                     /region_name="COG2402"
                     /note="Predicted nucleic acid-binding protein, contains
                     PIN domain [General function prediction only]"
                     /db_xref="CDD:441958"
ORIGIN      
        1 miavadtsgl ltlfnrsdpd hhtarkaadq cgflvatpla ltevhqvats ragraaadgi
       61 lrsltvrvrq mrlvlasmtp eildaalsvr aryasldldl vdavnvalaa eydtdavltr
      121 dirdfrtvrp lggrhthfri lpddl
//
LOCUS       WP_181865468              55 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Streptomyces
            himalayensis].
ACCESSION   WP_181865468
VERSION     WP_181865468.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 55)
  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 55)
  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..55
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..55
                     /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=6013
     Region          <2..52
                     /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 myeavdalae dprpanstpy gsayrrlrvg pyralyvidd qvirilvthi gpvps
//
LOCUS       WP_181866375             277 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces himalayensis].
ACCESSION   WP_181866375
VERSION     WP_181866375.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..277
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..277
                     /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=29314
     Region          <51..168
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mdisevsdsl fgafagihal alprtvvspp fdgllgvfyt klvsmspqdp awfvahadsa
       61 pgdvldlccg ggrtavafaa aghrvtgvdl spvqisaaek raaehgvads ttwltadvvg
      121 lrlgrtfdtv vigglsltlf dgprrtalle vvrrhlapgg rvlldhtpaq edepateqni
      181 tlplalgarr gfvllgarrq pthgvqltnm yaeiidadgr terhltgfrf rvdssdglvr
      241 elaghglvvr erhrdlqape saaptpfpar elvvasa
//
LOCUS       WP_181866377             222 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Streptomyces himalayensis].
ACCESSION   WP_181866377
VERSION     WP_181866377.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..222
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23718
     Region          12..204
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtsdfaqprs gkyvlfdvdg tlidavdnqr rvwrtwagry gldadavyqv alrtrpmetf
       61 aavvpdrdpg eclsalhele dedvrsgvya afdgasells alpsgcwglv tsnyehrvrg
      121 rfartglpvp svlvdaaave egkpspvpyl laaerlgaep edclviedap sgvesglrag
      181 mtvwgvnapv avdgahrhfg slreavpdil vfatgahres av
//
LOCUS       WP_181866454             285 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181866454
VERSION     WP_181866454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 285)
  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..285
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..285
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32418
     Region          13..70
                     /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 masnvnptvr rrrlgqelrr lreqkgmtae evaerllvsq skisrlengr rsisqrdvrd
       61 lcgvyevedh rivdslmqma kdsrqqgwwh sfgdipysvy igletdaasl rvydpqvvpg
      121 llqtrpyaes liagalpeta ptdidkrvqv rmrrqerisa hsnplrlwtv ldeaalrrvv
      181 gsrnvmrdql ehlveqsqlp hvtvqvipfd mgahpglngq yailefpdaa dssvvyiegv
      241 tsdlylekan dvhkysvmye hlraqalnve qsrnfiadia keyar
//
LOCUS       WP_181866493             397 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Streptomyces himalayensis].
ACCESSION   WP_181866493
VERSION     WP_181866493.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 397)
  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 397)
  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..397
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..397
                     /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=42420
     Region          36..388
                     /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 mndsttparp svphhedrpv yvigggpggl aaafalrsrg vravvlerte hvgaswrrhy
       61 drlhlhttrr lsalpglamp rsfgrwvsrg nvvrylekya qhheleivtg vevsrvepsp
      121 dgsgwllhat ggreltgsai vvatghnhtp rlpdwpgrgs yagellhasd yrnaapyagr
      181 dvlvvgvgnt gaeiavdlve ggasrvrlsv rtaphivrrs tagwaaqftg ilvrrlpvav
      241 vdrlvrtlak vsvpdltehg lprpdtglys rvnegsipvq dvglidairk grvepvaave
      301 sfedgkvvla dgsrigpeav iaatgytrgl qelvghldvl dgrgrpvvhg artpenapgl
      361 yftgftnpis gmfrelaida ekiakaiagr asvqtrs
//
LOCUS       WP_181866663             327 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Streptomyces himalayensis].
ACCESSION   WP_181866663
VERSION     WP_181866663.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..327
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34007
     Region          1..327
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mrlrtplall gaavlvlagp pllttgsgae tgtqipglrf mvpntpgggy ditartaakn
       61 aedaglthni evfnlpgagg tvgltrlvge hgngklamsm glgvvgavrs nhapttlaet
      121 tpiarlteeq dvvvvakdsp yqtidqliea wkkdpgklpv gggsspggpd hlapmlmara
      181 agiapkdvny ipfdgggell asilgnkvaf gvsgvgeyld qiksgelrll avtgpervdg
      241 ldaptlkesg ydvdftnwrg ivappglsda erdkltslit klhdsdewqe slekngwdda
      301 fltgdkfgaf ldaqdkrvvs vlkelgl
//
LOCUS       WP_181866772             252 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181866772
VERSION     WP_181866772.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=27331
     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 mfyyvlkyvl lgpllrllfr prieglehvp esgaaiiagn hlsfsdhflm pailrrritf
       61 lakaeyftgp gikgrltaaf frsagqipvd rsgkeagqaa ireglgvlsk gellgiypeg
      121 trshdgrlyk gkvgvaamal karvpvipca migtfeaqpp gqvvpslrpv tirfgeplef
      181 srysgmedek avlravtdei myailglsgq eyvdkyaavv kaeeaekakq aadgpegqkg
      241 pegrkfprmp ls
//
LOCUS       WP_181866852             485 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Streptomyces himalayensis].
ACCESSION   WP_181866852
VERSION     WP_181866852.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 485)
  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 485)
  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 485)
  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 485)
  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 485)
  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 485)
  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 485)
  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..485
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..485
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53635
     Region          1..331
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 mfdrdfewse lvrfvtypgp eatlgvvsgr rrqgktflld giaratdgff faaseateae
       61 slrqygvama rfegrtvpyr fthwdeavea tmhlatartg pltvvidefp flakaspelp
      121 sllqralgpq grreggpvrl llcgsalsfm gnllsgtapl rgrasleliv ptldfrlaad
      181 fwgitdprla mlvnsvvggt paygreftlg dvpadlddfg pwilrnilnp grplfrearf
      241 llaeepdlrd talyhgvlaa iaqgnhtrgg iasflerkst dlghaltvle dtgmisrepd
      301 afhgkrsayr inepiltfyy almrpewsdl erpgqaesvw qrshptfrsk vigphfeqlc
      361 rtwtrwyasp dtlggqrtrv esgtvadtaa rashevdvaa fgrdedgret llaigeakwn
      421 etmgfghvqr lehirdlira rgtvnapatr llcfsgagft ddlharaahd pniqlvdler
      481 lykga
//
LOCUS       WP_181866983             249 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Streptomyces himalayensis].
ACCESSION   WP_181866983
VERSION     WP_181866983.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..249
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..249
                     /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=26478
     Region          7..142
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 mdrqtisala hgdhpiaapl sdasvarlle ralpraagrl ldlgcgsgew llraldgrpg
       61 lradgvdlaa aslesaraaa erdgtgdrlt lhhqdatkft ashaydlvls vgaahafggl
      121 lptlraargh lapggsvlvg dgfwerepdr atldagfaad efadlattvd rvvadgwlpv
      181 yghvstleew ddyewswtgt ltrwaldhpd dpghddalka anahreawlr gyrgtlgfvt
      241 lvlrraada
//
LOCUS       WP_181867003             322 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867003
VERSION     WP_181867003.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..322
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=34273
     Region          1..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 mrallvvnpa atttsartrd vlihalasem kleavtteyr ghardvgrqa aestdvdlvv
       61 alggdgtvne vvngllhhgp dpdrlprlav vpggstnvfa ralglpndav eatgalldal
      121 regsertvgl glaagtpgta deavpgrwft fcaglgfdas vigrveqqre rgrrsthaly
      181 lrqvvrqfld ephrrhgait lerpgedpva dlvlsivcnt spwtylgnrp vyasprasfd
      241 tgldvlglsk lstgavarya tqlltssper gpkgkhavsl hdltdftlhs kvplplqmdg
      301 dhlglrtsvt ftgvrralrv iv
//
LOCUS       WP_181867074             157 aa            linear   BCT 28-DEC-2024
DEFINITION  Fur family transcriptional regulator [Streptomyces himalayensis].
ACCESSION   WP_181867074
VERSION     WP_181867074.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 157)
  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 157)
  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..157
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..157
                     /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=17260
     Region          4..136
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mvstdwksdl rqrgyrltpq rqlvleavdt lehatpddil sevrktasgv nistvyrtle
       61 lleelglvsh ahlghgapty hladrhhhih lvcrdctnvi eadvaiaaef taklrdtfgf
      121 dtdmkhfaif grcrdcgaag ragsseaqnq aenpgek
//
LOCUS       WP_181867096             194 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan-binding domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867096
VERSION     WP_181867096.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..194
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..194
                     /product="peptidoglycan-binding domain-containing protein"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20803
     Region          <96..128
                     /region_name="PGRP"
                     /note="Peptidoglycan-binding (PGRP) domain of
                     peptidoglycan hydrolases [Cell wall/membrane/envelope
                     biogenesis]; COG3409"
                     /db_xref="CDD:442635"
ORIGIN      
        1 mstlkhalrr sltaaalavv taatcttpas atpsqgyisg sgtvtddwyn egtlsmynyr
       61 ttyavglwhr ilyaegayyp vggagsivtp lqkqwidcdf gsgtriatqd lqnrwglead
      121 gyvgpltlgr adnnlvligd yntatqvvey rgrahtvqfl rvksngayqf rrvasdgvtd
      181 ggwntasynt pgpc
//
LOCUS       WP_181867109             132 aa            linear   BCT 28-DEC-2024
DEFINITION  6-pyruvoyl trahydropterin synthase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867109
VERSION     WP_181867109.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 himalayensis"
                     /db_xref="taxon:2820085"
     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=14383
     Region          1..132
                     /region_name="QueD"
                     /note="6-pyruvoyl-tetrahydropterin synthase [Coenzyme
                     transport and metabolism]; COG0720"
                     /db_xref="CDD:440484"
ORIGIN      
        1 mfsitvrdhl miahsfrgev fgpaqrlhga tylvdatfrr veldadnivv diglatqelk
       61 evvgeftyrn lddepdfagi ntsteflakv iadrlaarvq agklgegarg lagitvtlhe
      121 shiawasyer al
//
LOCUS       WP_181867204             347 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Streptomyces himalayensis].
ACCESSION   WP_181867204
VERSION     WP_181867204.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=35428
     Region          42..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 mlvdsppeqr aetapappnr ramrgagllv slgvllavav asiaigakhl pvdqvwhglf
       61 qdsgtysdvv vrerlsrtvl gllvgaalgl agavlqaltr npladpgllg invgasaavv
      121 taitffgvts ltgyvwfafa gaaivgvlvy slggsrsatp vrlalagtal taalsgylqa
      181 vmimdnaalg kmrfwtvgsl gsatnatimq vlpflavgtv lalglarpls avamgddtar
      241 algahltrtr alsmiaatll cgaataacgp iafvglmvph avrsftgpdl rwilpyaavl
      301 spvlllgadv mgriiarpae lqvgivtavi ggpvfiylvr rrrtaql
//
LOCUS       WP_181867219             237 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Streptomyces himalayensis].
ACCESSION   WP_181867219
VERSION     WP_181867219.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 237)
  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 237)
  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 237)
  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..237
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..237
                     /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=25514
     Region          14..>72
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     Region          45..222
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 mrgydkyafe pfavtvdlav ftvragelqv llvergqapy agrwalpggf vlphesaeta
       61 arrelaeetg ivdvsglhle qlrtysepgr dprmrvvsva ftalvpdlpe prgggdaaqa
      121 rwlpcggaga lafdhdrila darervgakl eytclatsfc ppeftlgelq qiyetvwgta
      181 ldrpnfrrkv latpgfvepv pgaarltggr gkpaalyrag pattlhppll rpegrps
//
LOCUS       WP_181867239             343 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Streptomyces himalayensis].
ACCESSION   WP_181867239
VERSION     WP_181867239.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=35535
     Region          2..341
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mriravrsrg lsvrldiral tvvvllivaa lvasvvligt gdfpipaadv irtlmgngda
       61 gqefivnelr lprvlvgllv gaalglggal fqsisrnplg spdvlglgqg stagalimiv
      121 lfkgsafqva ggslvggllt glaiyvlawk rgvhgyrlvl vgigvsavvm avngylltka
      181 dlvdaaravv wmtgslngrg weqvwplltl cavlvplvla narplrmlem gddvayalgv
      241 rvertrmllm lsavlltasa taaagpvsfv altapqlsrr ltrspgpnlv pamcmgaall
      301 ivadwasqra fgadqlpvgv vtgvvggvyl lwllvterka gri
//
LOCUS       WP_181867264             343 aa            linear   BCT 28-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Streptomyces
            himalayensis].
ACCESSION   WP_181867264
VERSION     WP_181867264.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 11466022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..343
                     /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=37856
     Region          4..317
                     /region_name="PcbC"
                     /note="Isopenicillin N synthase and related dioxygenases
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3491"
                     /db_xref="CDD:442714"
ORIGIN      
        1 mtaskdftel pvvdasellh ggpeaqreva eqlgraarev gfmyvsghgi apelfdglld
       61 aarrffalph eekmrswigr srnhrgfvpe geevfaqgta drkevfglal dlplddpdvr
      121 agtpllgpnv wpeldgfrea ttayyeavla fgqllfrafa valgeepdtf sryatkapsg
      181 lrlihypyda daldrpgiga htdyecftll rptgpglevl ngagewidvp plgdafvvni
      241 gdmlelwtng efvstthrvr rvseerysfp lffnvdyhtr veplprfvtp drparpglva
      301 gehlwsqvlq vygylkdrra ageltlpena lalsagfgre lgd
//
LOCUS       WP_181867282             419 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867282
VERSION     WP_181867282.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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 419)
  AUTHORS   ter Beek,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..419
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..419
                     /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=45135
     Region          74..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(153,155,271,273,305..307,349)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mtahsqaapp pprrrsrral apltvvsalv ataaltgcgq qrddnvytll nsstdesyhr
       61 wdgdtlarcs kqlgvtieqq svpapqvmtk alrmassksl pdivqfdgse mptfaetggl
      121 mdleklgvst edipqgiley gsydgtyyga artvntlalf ynkdildkag levpttwdem
      181 retakkltqg sqygialsag gaedgvyqft pfmwsnggde tdldspevvq aldywkalig
      241 dgslskstvn wtqadvndqf magnaammin gpwqvetlnt kkdlnwgiaq ipvpqkgdds
      301 vgplgggmlt ipdigdtere kmsariitcm tseqeeitya lnswmipanq kaadtwrekv
      361 pelssladqv atarsrtakl gagwssvsla lqsafqaalt gqdseavlkk aqqrlesgn
//
LOCUS       WP_181867335             276 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867335
VERSION     WP_181867335.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 276)
  AUTHORS   Rosinski,J.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 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..276
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30934
     Region          7..>60
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          95..270
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mstdfqqarv slgarlrelr agitgrdlaa rlgwpqskvs kletgrqtat aadltawaea
       61 tghpeaaeel tarlqgmesh vrswrrqlra ghrpvqdalt veyerstvlr awegsmvvgm
      121 lqtpdyarhi ftryaelhgt krdiddavra rvrrqdllyq pgrtfhivmw eaalhagvcp
      181 pnvlaaqldr lggvigldtv klgivpfgap vnippangfw lyderlaive dwhaelwldd
      241 tdslrvyrrv wdtlnqsavy gshahrliar arahld
//
LOCUS       WP_181867454             132 aa            linear   BCT 28-DEC-2024
DEFINITION  YybH family protein [Streptomyces himalayensis].
ACCESSION   WP_181867454
VERSION     WP_181867454.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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 10008488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..132
                     /product="YybH family protein"
                     /calculated_mol_wt=14440
     Region          1..129
                     /region_name="YybH"
                     /note="Ketosteroid isomerase homolog YybH [General
                     function prediction only]; COG4319"
                     /db_xref="CDD:443460"
ORIGIN      
        1 mtnndstada vgmvdaygqa lqtgdkdtil rlyadeseii peaapslrgt daidsfytdt
       61 faaigfegdl qvvsaevyde ialvrseqpi vvvavadgtr tetyyrelfv lrhtpdgwri
      121 hkymfsqnpa qa
//
LOCUS       WP_181867128             321 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867128
VERSION     WP_181867128.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  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 321)
  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..321
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..321
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=31891
     Region          120..262
                     /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 mpdilalvaa dtglwaggpd glafvpypaa aevpapeaga pavsplspqt reaapamtss
       61 atvpadapvt alfltdrvlf vggigtiarr asdpaserpa dtcrvpggfg pvadfgtdgs
      121 gtlfaatled gvlrstdggr twvrsgyglp gpevmslvta adgavfagtp dgvfraragg
      181 rawqvcpgte gapvasmvll pqdgtvvaat edgtvlrsad dgvtwatada pknptalaps
      241 pggglvlata gegvhhspda gatwlrdspd pavrtvhcla atdravhagt sdgvavspgp
      301 glpwrplvpa tprpeqskeh a
//
LOCUS       WP_181867503             440 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867503
VERSION     WP_181867503.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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 440)
  AUTHORS   ter Beek,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..440
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..440
                     /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=47784
     Region          1..321
                     /region_name="UgpB"
                     /note="ABC-type glycerol-3-phosphate transport system,
                     periplasmic component [Carbohydrate transport and
                     metabolism]; COG1653"
                     /db_xref="CDD:441259"
ORIGIN      
        1 matagacsss esgdaaggkv titvtdmppt tqeasrkeft drvaaferan pdidikpsea
       61 vwdpktftar laggqletaf ivpltepqgl ikrgqiadit ddvkalpnad qfdrralaps
      121 tdadgriygl ptsefalsli ynrelfdkag ldpdnppktw devreaakki seetglpgya
      181 hpatnntggw tltamtytyg graekeeggk qvaafndapm rdalqwlkdv rwkdnsigtq
      241 hlrdaaeiyk sfsagrigmt matpsvfdeh itkyngdpki fgvtalpsat rsatllggkm
      301 avinpkasda erkaavkwid yyylrykydp keaearaktk avdgvpvgtp yvpfyqpavd
      361 ravqeatnkh atvplrnfep ylqgvqeqef vtepsvaaqd lyaaldsava avltresadp
      421 qaeldkaekk vvpaleraqr
//
LOCUS       WP_181866445             289 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181866445
VERSION     WP_181866445.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=31664
     Region          21..283
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mahttapvts svpapspses prldldayla rigwsgrrea saetlrsvhr ahiqgipfen
       61 vqpvlgsaps lalddlqakl vrsrrggycf ehntlfaavl ealgfgvtrl aarvrvgaqg
      121 avrprthmll lvdvpgesrq yladvgfgsi gglleaiplt agsevhhggr thrlvrephq
      181 gledlwvlqa fqegawsdqy aftrepfepa dyevinwhva tnprspfqht lyaqrttpea
      241 hlalaghvlv itradgtrek reltdpaelr rvldsdfgie lpesarlef
//
LOCUS       WP_181867544             527 aa            linear   BCT 28-DEC-2024
DEFINITION  purple acid phosphatase family protein [Streptomyces himalayensis].
ACCESSION   WP_181867544
VERSION     WP_181867544.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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 11244734
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..527
                     /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=56904
     Region          81..186
                     /region_name="Pur_ac_phosph_N"
                     /note="Purple acid Phosphatase, N-terminal domain;
                     pfam16656"
                     /db_xref="CDD:465220"
     Region          190..451
                     /region_name="MPP_superfamily"
                     /note="metallophosphatase superfamily, metallophosphatase
                     domain; cl13995"
                     /db_xref="CDD:472684"
     Site            order(201,203,228,271..272,363,398)
                     /site_type="active"
                     /db_xref="CDD:277249"
     Site            order(201,203,228,271,363,398)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277249"
ORIGIN      
        1 mdtpnvgipe qlarrmsmpe qheylrarlt rrrvltgtag aagglgllag ssgaaygsra
       61 asaaplarsa tvtvdgslva pfgrhlafga dpktqmrisw qvpfavrnpy vrvglkpwel
      121 gqkieaevrd lhtpalsakl pavdqyylhv alnglkpgat yyygvghdgf dpasaerlat
      181 lgsfrtapat petfvftafg dqgvsydala ndqlilgqnp sfhlhagdic yadstghged
      241 sdtydarvwd qflaqtesva ksvpwmvttg nhdmeawysp ngyggqsarw slpengfdpk
      301 sapgvysfvy gnvgivalda ndvsyeipan kgytegrqta wldrrlgelr asasvdfivv
      361 ffhhcmysts thasdggvrd awlplftkhq vdlvinghnh vyertdairn gevgrpvpvg
      421 astdptrdgi vyvtaggagk dlygfpagve dsyegavkdr dsvltfhwtk srlpdpdtve
      481 wsrvrytgfs flaveavaga darlkvsalt esgkridyfe vlrspgg
//
LOCUS       WP_181867463             366 aa            linear   BCT 28-DEC-2024
DEFINITION  Leu/Phe/Val dehydrogenase [Streptomyces himalayensis].
ACCESSION   WP_181867463
VERSION     WP_181867463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 366)
  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 366)
  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 366)
  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 366)
  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..366
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..366
                     /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=38448
     Region          23..140
                     /region_name="ELFV_dehydrog_N"
                     /note="Glu/Leu/Phe/Val dehydrogenase, dimerization domain;
                     pfam02812"
                     /db_xref="CDD:460706"
     Region          157..361
                     /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(191,193..195,214..215,219,253..254,275,277)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133444"
     Site            307
                     /site_type="active"
                     /note="Phe binding site [active]"
                     /db_xref="CDD:133444"
ORIGIN      
        1 mtdvtgapad vlhtlfrtdq ggheqvvlcq drasglkavi aihstalgpa lggtrfypya
       61 seeeavadal nlsrgmsykn amagldhggg kaviigdpqq ikteqlllay grfvaslggr
      121 yvtacdvgty vqdmdvvare cpwttgrspe kggagdssvl taygvfqgmr asaqhlwgdp
      181 tlrgrkigia gvgkvghhlv ehlledgaev vitdvreesv rrvldkhpgg rvtavadtda
      241 lirtagldiy apcalggaln desvpvltar ivcgaannql ahpgvekdla drgilyapdy
      301 vvnaggviqv adelhgfdfd rcrakaakif dttlaifara ktdgippaaa adriaeqrma
      361 eartar
//
LOCUS       WP_181867615              71 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Streptomyces himalayensis].
ACCESSION   WP_181867615
VERSION     WP_181867615.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 71)
  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 71)
  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..71
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..71
                     /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=7908
     Region          4..>69
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 msvdltdrqv rilrcirewi aehgegpsir eigkhvglss sssvayqlgk leqqgmvsrs
       61 grrwrscklg r
//
LOCUS       WP_181867589             888 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Streptomyces himalayensis].
ACCESSION   WP_181867589
VERSION     WP_181867589.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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..888
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..888
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=95324
     Region          <3..888
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Site            order(606,609..610,613..614,616,647,650..651,654..655,
                     657..658,688,691..692,695..696,699)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          606..633
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          645..675
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          687..712
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtqgrsgrfv paplwerdse iaeaaqtvda lhsgatsgsl lvysgeagig ktalltevgr
       61 iaegrctvws arggetvtsv pfyvlrqllq palvalsega areylgdwyd iagpalgiaq
      121 ptgrqadpqg vlnglvavar rfarlhwplv lliddahwad qetlqwlaaf aerlddlpvl
      181 vvvahrqrdt adenarqler igaaarprtt lraltpdatt gltratlgeh adapfcrevw
      241 avtggnpyet vellakvqds elepveasaa elrtlnrsar grglidrlea lgtdvtrfar
      301 aaailgtris lelaaslagm khdearrcae vlrtariltg gededgsell efvhpliatt
      361 vyrsippatr talhghaawa vtqsgrgaaa aarhllevhp dddpelveqm reaarehlav
      421 gapdaarrcl eralrepplp dvharvlyel gcatfltspa ttighlreal avpgleghlr
      481 vdavcrlsqa lvhndqleea vrivddeaar lepgparmrl lamhylwegi hageqdspgr
      541 srslaelagp ltgrdnsera llilrafdam argenaeevv efcdrslvng slapglgwtd
      601 tewgfelllm lgisylfadr vdrahslfte glrayetagw sgghlafaha svgyvhrirg
      661 klteaeaylr eslrladrvg rglpmhwdaa cmlidtllar ghvdqaqeia drygfappyp
      721 stivvpdahs vrgrlliasg rikegvtele aaenaaaarg gynpimapwa gdlvralaad
      781 dpgraagiaa aarrqaerfg tdtaigealr caaalergpr svtlyakaaa hleaspcaye
      841 havarveygi aarsvaeltr gltlarscga dglaaraqev ldtgrglh
//
LOCUS       WP_181867469             116 aa            linear   BCT 28-DEC-2024
DEFINITION  histone-like nucleoid-structuring protein Lsr2 [Streptomyces
            himalayensis].
ACCESSION   WP_181867469
VERSION     WP_181867469.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 116)
  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 116)
  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 116)
  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..116
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..116
                     /product="histone-like nucleoid-structuring protein Lsr2"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12180
     Region          1..115
                     /region_name="Lsr2"
                     /note="pfam11774"
                     /db_xref="CDD:432065"
ORIGIN      
        1 maqrvvvtly ddidggeaae tiafgldgrs yeidlnpana rklrkalapy mqagrkrtaa
       61 gkstggtagk taadythtav aaspaavraw arsnkmdvpp rgripkkvye afdaan
//
LOCUS       WP_181867874             503 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867874
VERSION     WP_181867874.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 503)
  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..503
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..503
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=53994
     Region          27..73
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     Site            order(27,31,56)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(30,55)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(37..38,49,52,56..57)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
ORIGIN      
        1 mtdfeaidtl lagakqqial ppaqerralr eklnlsrmqv aqalgvspst vggwesgrdp
       61 sgevrekyay flqgaqakle arppagqaed vsdvlsdgaa aedaaaedgt agtvaadsgs
      121 devqslttpq pcvlcggpar hqvagfpqhl daaecgtaaa aparaakpvq vrpvgrrmqt
      181 asetsdpiga avaaalathe gdveaaiaal vkraipdama lldatrtggr ydivahpwmp
      241 dilrkqsarg sdqiwearpk warpelppga hevtaldvng aylsalkthl pigqlehstg
      301 fdhdrrragv hlitppaweh ddvlpnpvga rdepgplwvt eptlrlllrl sgpkyglcdp
      361 peihesftsg atenllekfr ivlkdardra iaqddevtle yvkamyskfv stlgesnynr
      421 eiyrtdwmhl irsqafanlw mkaykaydeg lmvvramgtd elhvvgdwra vfpegrgvse
      481 vkvkdtysvg tdpetaaage agd
//
LOCUS       WP_181867139             179 aa            linear   BCT 28-DEC-2024
DEFINITION  DoxX family protein [Streptomyces himalayensis].
ACCESSION   WP_181867139
VERSION     WP_181867139.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..179
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18156
     Region          37..154
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mttstttrft pttrhtpslh aydvgllllr lavgltmaah gtqklfgwfg ggglegtgqf
       61 ftmsgypsgr tmaavaglte tlgglglalg lltplagaav fgtminalav kwgggffapd
      121 gveyelvltv aaaslaltgp gryavdrllp glrahrlgyg iaavvlgavv agvilllrk
//
LOCUS       WP_181867876             109 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867876
VERSION     WP_181867876.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 109)
  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..109
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..109
                     /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=12024
     Region          3..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 msvvkinvlt vpaeqretle krfasrahav ensdgfewfe llrpaegtdn ylvytrwrde
       61 esfqawmegp mkaahqggsg eggerpkpaa sgstlwsfev iqqagpkna
//
LOCUS       WP_181867939             440 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein [Streptomyces
            himalayensis].
ACCESSION   WP_181867939
VERSION     WP_181867939.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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 440)
  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..440
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..440
                     /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=49172
     Region          14..424
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mtselglekr qfghrarlal spaeirlidd qahaartmwn clhawwtmlp kakrtlaaad
       61 aairqarkei dwlgalpaqa aqavlktyfq awkncwegra eepnfkarfr samsvdvpqg
      121 rdlqvtrvhr rwgmvnipkv grvrfrwtrd lpvgktanad nritgarlik dalgwhvafr
      181 ittleakpep hqgpqagida gvtiplalsd dnhqdhgrpa rlpngtsdrd kwlkadekak
      241 llrlerqaar lkqhrkpgqr ssnrlravyd qigklrakak rratdwqhqt ttylartysv
      301 lvvehldipn mtksargtie epgknvkqka glnrsisqea wgrtvtmlty ktaryggtlh
      361 kvpapgtsqr csacgfttpg sresqavfvc knpgcgwsgn adhnaarnvl hlyrmglalv
      421 paagravvrr prrvkpatar
//
LOCUS       WP_181868151             532 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA carboxylase subunit beta [Streptomyces himalayensis].
ACCESSION   WP_181868151
VERSION     WP_181868151.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 532)
  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..532
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..532
                     /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=56630
     Region          21..530
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtvlesaldt aapdhaahre amlgklaeld aeharalagg gekyvarhra rgkllareri
       61 ellldpdapf lelsplaawg sdyavgaslv tgigvvegve clitandptv rggasnpwsl
      121 kkalraneia yanrlpcisl vesggadlps qkeifipgga ifrdltrlsa agiptvavvf
      181 gnstaggayi pgmsdhvimv kerakvflgg pplvkmatge esddeslgga emharvsgla
      241 dyyaldeqda lrqarrvvar lnhrkahpdp gpaeppkyde dellgivpgd lkipfdprev
      301 iarivdasdf defkplygts lctgwatlhg ypigilanaq gvlfseesqk aaqfiqlanq
      361 rdipllflhn ttgymvgkey eqggiikhga mminavsnsr vphlsvlmga sygaghygmc
      421 graydprflf awpgaksavm gpqqlagvls ivarqsaaak gqpydedada alramveqqi
      481 eseslpmfls grlyddgvid prdtrtvlgl clsaihtapv egarggfgvf rm
//
LOCUS       WP_181868246             460 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Streptomyces himalayensis].
ACCESSION   WP_181868246
VERSION     WP_181868246.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..460
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..460
                     /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=47933
     Region          27..427
                     /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..41,44,78,128..129,131..133,136,156,
                     159..160,163,272,275..276,279..281,284,311,315,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340923"
ORIGIN      
        1 mtpetvqpav rperaarrrr peflvtglcf avivfdgydl ivygatvpal lqydswnltp
       61 amagaigsya ligmligali agavtdtvgr rrvlltgvaw fsatmigcal apdatwfgif
      121 rllggiglgg vmptavalta eyadpkrrsl nnammfsgya vggiiaavla mtlmpalgfr
      181 fmyamgaapl llvpllaryi peslafltak grheeaarta aklgmevpap gpasddrpap
      241 dgealgqrkr aglmqlagre ylgpallfaa vsffglllvy glntwlpqim raagyplsgs
      301 llfllvmnlg avvgsllisp lgdrfgmkpv tmavflaaav sitllafata aplmyalvav
      361 agfgtigaqi mvlgyvaqhf pvevratalg ctlglgrlga itgplfggfl ldagvstawn
      421 fyafavpaal atalvlllpg ralverglpg qernlsatnh
//
LOCUS       WP_181868342             309 aa            linear   BCT 28-DEC-2024
DEFINITION  AurF N-oxygenase family protein [Streptomyces himalayensis].
ACCESSION   WP_181868342
VERSION     WP_181868342.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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 309)
  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 309)
  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..309
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..309
                     /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=35356
     Region          19..292
                     /region_name="AurF"
                     /note="P-aminobenzoate N-oxygenase AurF; pfam11583"
                     /db_xref="CDD:431946"
ORIGIN      
        1 mttateadal rdalgvlkdr eqvakrlles sakhsfdpdk eldwdapfee gkwfwppelv
       61 slydtplwkr mseeqrills qheaaalasl giwfeiilmq llvrhiydka atsahvryal
      121 teiedecrhs kmfarlisrg gtphypvsrv hnnlgrvfkt isttpgsfta tllgeeildw
      181 mqrltfpder iqplirgvtr ihvveearhv ryareelrrq mmtargwske ftrltsgefa
      241 rvfsvafinp evytnvgldk rqavaqvras ghrrevmqtg arrltdfldd igvlrgvgrq
      301 lwkssglla
//
LOCUS       WP_181868424             259 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Streptomyces himalayensis].
ACCESSION   WP_181868424
VERSION     WP_181868424.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=26846
     Region          2..235
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mkqaalggrn pilyhqslps fsmpewaaaa gyngvvldlq hgelgleaac rilrsiprdn
       61 ayayarvgsl dpapilrlld sgargivapt vesrsqteal vaatkyppvg nrslgpsrpa
      121 lypgdpgdsy teagnravsa iaqietkagv draeeivstp gldsvyigpa dlavsyglpg
      181 rgdwedgpvr eaiaylrevt tahgvtlgiy sgkpdyaagl ladglvdyvg lgidlvllnr
      241 afgdtiaale aarstgsts
//
LOCUS       WP_181868175             148 aa            linear   BCT 28-DEC-2024
DEFINITION  MarR family winged helix-turn-helix transcriptional regulator
            [Streptomyces himalayensis].
ACCESSION   WP_181868175
VERSION     WP_181868175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     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=16966
     Region          5..128
                     /region_name="MarR"
                     /note="DNA-binding transcriptional regulator, MarR family
                     [Transcription]; COG1846"
                     /db_xref="CDD:441451"
ORIGIN      
        1 mtalsrqrdg dtelwwqlfr lssyvshvlq rklmrrhgig ltdfialdvm rqaeskamqm
       61 relaqatgik katlsrvaer lerrglakrw tsegdrrvtf inltdtgrke vdlfaatfad
      121 elrtafrraa gspsmapflk rirsepwp
//
LOCUS       WP_181868440             277 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181868440
VERSION     WP_181868440.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15193332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..277
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30693
     Region          13..>66
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          87..264
                     /region_name="DUF5753"
                     /note="Domain of unknown function (DUF5753); pfam19054"
                     /db_xref="CDD:465962"
ORIGIN      
        1 mangsrqaaw effgaelkrr redtgftqve lgsrvfvsga yigqfeqair kpqldvahri
       61 devlqtggff ermcrklind rryadyfapv aelealakei cefaptvvpg llqtaeyare
      121 vtlasnplat deyveekvra ridraqilkd atrpvywail hetalrisvg gpaamarqld
      181 hiatmvrerk tlvqvlpyat gayaqmgkpl klmefedapp tayteavysg nllddpavvk
      241 raqatydllr aaalspeasl aliesaaedf rrcastt
//
LOCUS       WP_181868515             112 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptomyces
            himalayensis].
ACCESSION   WP_181868515
VERSION     WP_181868515.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
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   Wintjens,R. and Rooman,M.
  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 112)
  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..112
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..112
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11884
     Region          1..71
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mkwnlrmvaa qrdlwrptel leafktvgft pslsrvaamw sgtpvtvrld dldkicavln
       61 ctvgdllqae pleaaagese alpkavgses snggpvrptp grqgsrrslp pn
//
LOCUS       WP_181868715             167 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein, partial [Streptomyces
            himalayensis].
ACCESSION   WP_181868715
VERSION     WP_181868715.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         <1..167
                     /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]"
     Region          <1..164
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 sdvavpltal daiihiqgtd dsrsiplpqf ylppgdtphi envlqhgeli taveipllpe
       61 garshylkvr drvsyefalt sagvalvied glirqarval ggvgtipwra wnaedvlrga
      121 ragadsfrta aeaalegarp lpgtafkvel akrtlvrtle tvagvls
//
LOCUS       WP_181868637             353 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Streptomyces himalayensis].
ACCESSION   WP_181868637
VERSION     WP_181868637.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 353)
  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 353)
  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 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   5  (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   6  (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   7  (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 10008345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..353
                     /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=38445
     Region          33..351
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 msltagsrpe gtrrtrppaa veeptaavat agaktraprt rskagkvpwr vrlrrdrtli
       61 vmtlpvivll lifnyvpllg nvvafqeydp yaagngitai fhspwvgveq fsrmlqdplf
      121 wsatqntivl fvlqlvlffp vpialalvin svirprvrav aqaimylphf fswvlvvtvf
      181 qqilggagii aqtlekhgws gfdlmtdadl fkylvtaqav wkdagwgiiv flaalsavst
      241 dlyeaaaidg agrwrrmwhv tlpalrpvia lllvlrvgda lsvgfeqfll qryavgagas
      301 evldtyvwnm giqngdfsya aavglakgvi gvclvlgank fahllgeqgv ykk
//
LOCUS       WP_181868723             123 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein, partial [Streptomyces
            himalayensis].
ACCESSION   WP_181868723
VERSION     WP_181868723.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            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: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         <1..>123
                     /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]"
     Region          1..>75
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 dgvlnperli ditrlplggi thtdssirvg alttmeelaa dpvvrerlpf vrealllgas
       61 tqlrnmatig gnllqrarcr yfrdptvaac nkrnpgsgca aitgiqrmha ilgtsdhcia
      121 lha
//
LOCUS       WP_181868821             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Brachybacterium alimentarium].
ACCESSION   WP_181868821
VERSION     WP_181868821.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     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=32673
     Region          8..292
                     /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(34,240,243)
                     /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 msrpavhvig ealidvvvra dgvervrpgg spanvavgla rlgvpadllc rigadaygdl
       61 lrahleqagv glpdggspap artstavatl gadgsasyrf didwdpgtia vptarilhtg
      121 slatvlepga tavanalsaa dpatlvsvdp nvrptvgvpq vevrsrterl agrahllkms
      181 dedldwlypg aapeevaarm helgvrlfvv tlgaqgcfls tsewscripa eaatlvdtig
      241 agdafmsgll yaviaddgdq tvrtgvlqre qvenwahtaq rsaaltlgrd gaeppllael
      301 harelvsqsa gepvsr
//
LOCUS       WP_181868833             324 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Brachybacterium alimentarium].
ACCESSION   WP_181868833
VERSION     WP_181868833.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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 324)
  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 324)
  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 324)
  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..324
                     /organism="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     Protein         1..324
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35159
     Region          14..305
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msmtceqarw fsetfaqlvr nvgqavlgkd evvrlvltam lapghvlled apgtgktsla
       61 rataatvqgs striqftpdl lpsdvtgvti yeqstrtfef hqgpvfaniv ladeinrasp
      121 ktqsamlevm eegrvtvdgi shevadpfmv iatqnpleha gtyrlpeaql drflmklslg
      181 fpdhassmqi lagaalrdrs srlgprialh avsdmtrlae tvhvdpavla yvsrlmeetr
      241 lapevragvs irgalglvra vkvwaaangr hfvtpddvkh laghvwlhrf vleseaefdg
      301 vtaqaimtri lrevaapqar qqva
//
LOCUS       WP_181868857              70 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein, partial
            [Brachybacterium alimentarium].
ACCESSION   WP_181868857
VERSION     WP_181868857.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 70)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     Protein         <1..70
                     /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]"
     Region          <8..68
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 rrldiarpgf isvtllasad ktrvlnvaqw esaddvkatq sdpeaaeyak ktagiakasp
       61 glyqvvgeyk
//
LOCUS       WP_181868870            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181868870
VERSION     WP_181868870.1
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=166344
     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 eqfryplwqa kpfepqqgvk
      181 legassnfis pqpgniyipl gqqepglylv eamvggyrat tvvfvsdtva lskvsgkell
      241 vwtagkkqge akpgseilwt dglgvmtrgv tddsgtlqlq hispersyil gkdaeggvfv
      301 senffyesei yntrlyiftv rplyragdrv dvkvigrefh dplhsspivs apaklsvlda
      361 ngsllqtvnv tldarnggqg sfrlpenava ggyelrlayr nqvysssfrv anyikphfei
      421 glaldkkefk tgeavsgklq llypdgepvk narvqlslra qqlsmvgndl ryagrfpvsl
      481 egsetvsdas ghvtlnlpaa dkpsrylltv sasdgaayrv tttkeilier glahyslsta
      541 aqysnsgesv vfryaaless kqvpvtyewl rledrtshsg elpsggksft vnfakpgnyn
      601 ltlrdkdgli laglshavsg kgstahtgtv divadktlyq pgetakmlit fpepideall
      661 tlerdrveqq sllshpanwl tlqrlndtqy earirvsnsf 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 miqdnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqaigvt qqpeywqhml dsyaeqadnv
     1141 pllhralvla waqemnlpck tllkgldeai arrgtktedf seedpsdind slifdtpesp
     1201 ladavanvlt mtllkkaqlk stvmpqvqqy ardkaansnq plahtvvlln sggdatqtaa
     1261 ilsgltaeqs tieralamnw lakymatmpp vvlpapagaw akhkltggge ywrwvgqgvp
     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_181868453             264 aa            linear   BCT 28-DEC-2024
DEFINITION  DedA family protein [Streptomyces himalayensis].
ACCESSION   WP_181868453
VERSION     WP_181868453.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces himalayensis
  ORGANISM  Streptomyces himalayensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 264)
  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 264)
  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..264
                     /organism="Streptomyces himalayensis"
                     /db_xref="taxon:2820085"
     Protein         1..264
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=25957
     Region          29..>169
                     /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 mdiarlmswv ditsglsthl agtacwayai laittlppll pnavllvtgg mlaargemsi
       61 tlvllsvvgs allgdvmihr fgwsaggrvr rriagrgrqg elfewaaarv qrggipfvvg
      121 vrflpsgrll gglaagaary pagrfaigaa laetvwaays vgvgyfggav sddpvysvai
      181 glalsvavag vaavaqrrta rsavavsaat sgadlsaaas gadvsaatse aaastatsga
      241 asaatcgaaa cagvraraak sgae
//
LOCUS       WP_181868958             312 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Yoonia sediminilitoris].
ACCESSION   WP_181868958
VERSION     WP_181868958.1
KEYWORDS    RefSeq.
SOURCE      Yoonia sediminilitoris
  ORGANISM  Yoonia sediminilitoris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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..312
                     /organism="Yoonia sediminilitoris"
                     /db_xref="taxon:1286148"
     Protein         1..312
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=32293
     Region          35..311
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mamglgtlaf adghqilddi hflipggagg gwdgtargvg ealtesglig sasfenmsgg
       61 gggtaigyll enadslegtl mvnstpivir sltgvfphnf rdltlvagti gdyaaivvpa
      121 gsdistmddf lavydadpag tpigggsvpg gmdhlvaamv measgrdalg vnyipydagg
      181 tamaallsge ikalstgfse avdlanqgev kiigitadar vdaapeamtm meqgidttfv
      241 nwrgffgapr msdeklaqyq aaiaamydte eweavrarng wvnihnpgdd frvfleeqet
      301 vigdlmtklg fl
//
LOCUS       WP_181869385             701 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Escherichia coli].
ACCESSION   WP_181869385
VERSION     WP_181869385.1
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 both ends.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>701
                     /product="beta strand repeat-containing protein"
     Region          <27..701
                     /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 svadgstanm lrvrvtdafg nalagqtvsv magngatvsp tvttepdgtv eisvtsqtag
       61 tsavtatins ssqsrdvtfi advrtaqias levtqdnsva dgamantlrv kvtdafgnal
      121 agqtvsvtvg ngatvaptai tgpdgtveis vtsqtagtsa vtatinsssq srnvtfiadv
      181 xtaqiaslev tqdnavadgs tantlrarvt dafgntlagq tvsvladnga ttaptvttqp
      241 dgtveiivts qtagvssvta sinnstlsrn vtfvadvrta kiadlvvikd gsvadgatan
      301 tlqvkvtdan gntlagqtvs vtadnsamva ltvitepdgt veisvtsqta gtstvtasin
      361 ssslsrnvtf vadvstakia dlvviqdnsv adgamantlr mrvtdafgnt lggqtvsvta
      421 dnsamvapta itgpdgtvei svtsqtagis tvtasinnss lsrdvtfvad vrtaqiadlv
      481 vikdgseadg stantlrarv tdafgnalag qtvsvladng attaptvite pdgtveisvt
      541 sqtagvstvt asinssslsr nvtfvadvrt aqiavlevtq dyavadgsta ntlrarvtda
      601 fgntlagqtv svtagngatv aptaitgpdg tveisvtsqt agistvtati nsssqsrdvt
      661 fiadastaqi adlvvikdgs eadgstentl rvrvtdafgn t
//
LOCUS       WP_181869487             271 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Vibrio].
ACCESSION   WP_181869487
VERSION     WP_181869487.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 271)
  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 271)
  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 271)
  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 271)
  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 271)
  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 271)
  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 271)
  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..271
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..271
                     /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=30813
     Region          27..121
                     /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          183..264
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mltrqidsks gvmtsnemma anphspvlvk tidmpkgyid alhqhtwhqi ifpikgllqt
       61 qtehyqhlvp htsalfvpag vqhesialsn tifvgiylnp afgatyepqv rtialtpfln
      121 ellqeirrqc egetsheevl hllavlhdqi lksnvqtfql llpqdrrlkl ifeqltdepa
      181 lscslkewge kigasertls rlfakefnts fllwrqqirl iyslslldes lpiqaiadlv
      241 gyqndssyik afkayfdmtp qqfrvngasr r
//
LOCUS       WP_181869739             309 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: shikimate dehydrogenase family protein
            [Adlercreutzia].
ACCESSION   WP_181869739
VERSION     WP_181869739.1
KEYWORDS    RefSeq.
SOURCE      Adlercreutzia
  ORGANISM  Adlercreutzia
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 309)
  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 309)
  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 309)
  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..309
                     /organism="Adlercreutzia"
                     /db_xref="taxon:447020"
     Protein         1..309
                     /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=32399
     Region          1..274
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 mseklyvlgh pvshskspvm ynavyekagl pwhyglmdvp tvpeaetfla ardflsinit
       61 tpykpeafaa advraasatl ahganvlvnk dgaliayntd gqgcvayler agvdfrgasv
      121 vvcgtgptsl silhavaqag paevvligrd kekarnvmrt yadelgamig rvvdmpafke
      181 ghlsfsevyk qvgfkfgsya tsrqaiagad iiidatplgm kagdpapfdt allsagqtvf
      241 dvvyghgeta laraaraagc tfldgagmlv gqavvtvgil rdiageeald ipedelfrlm
      301 aqaaefela
//
LOCUS       WP_181869785             316 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Brachybacterium alimentarium].
ACCESSION   WP_181869785
VERSION     WP_181869785.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     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=32629
     Region          8..292
                     /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(34,240,243)
                     /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 msrpavhvig ealidvvvra dgvervrpgg spanvavgla rlgvpadllc rigadaygdl
       61 lrahleqagv glpdggspap artstavatl gadgsasyrf didwdpgtla vptarilhtg
      121 slatvlepga tavaaalsaa gpatlvsvdp nvrptvgvpq gevrsrterl agrahllkms
      181 dedldwlypg aapeevaarm helgvrlfvv tlgaqgcfls tsewscripa eaatlvdtig
      241 agdafmsgll yaviaddgdq tvrtgvlqre qvenwahtaq rsaaltlgrd gaeppllael
      301 harelvsqsa repvsr
//
LOCUS       WP_181869820             324 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Brachybacterium alimentarium].
ACCESSION   WP_181869820
VERSION     WP_181869820.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 324)
  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 324)
  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 324)
  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 324)
  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 324)
  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..324
                     /organism="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     Protein         1..324
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35076
     Region          14..305
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msmtceqarc fsetfaqlvr nvgqavlgkd evvrlvltam lapghvlled apgtgktsla
       61 rataatvqgs striqftpdl lpsdvtgvti yeqstrtfef hqgpvfaniv ladeinrasp
      121 ktqsamlevm eegrvtvdgi shevadpfmv iatqnpleha gtyrlpeaql drflmklslg
      181 fpdhassmqi lagaalrdrs srlgprialh avsdmtrlae tvhvdpavla yvsrlmeetr
      241 lapevragvs irgalglvra vkvwaaangr hfvtpddvkh laghvwlhrf vleseaefdg
      301 vtaqaimtri lrevaapqar qqva
//
LOCUS       WP_181869951             129 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF4870 family protein [Halomonas sp. DQ26W].
ACCESSION   WP_181869951
VERSION     WP_181869951.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. DQ26W
  ORGANISM  Halomonas sp. DQ26W
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..129
                     /organism="Halomonas sp. DQ26W"
                     /db_xref="taxon:2282311"
     Protein         1..129
                     /product="DUF4870 family protein"
                     /calculated_mol_wt=14564
     Region          9..123
                     /region_name="COG3671"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:442888"
ORIGIN      
        1 mtdnlhpddd rdhravtdpg spdttipivi yalflagivs ggltqvigvv iayvyrgkgp
       61 hwldehyryq irtfwmsmly favsglltli migfvtwlla viwlvircvk glkslqekra
      121 pdnvdtwlf
//
LOCUS       WP_181869498             136 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar 3,4-ketoisomerase [unclassified Vibrio].
ACCESSION   WP_181869498
VERSION     WP_181869498.1
KEYWORDS    RefSeq.
SOURCE      unclassified Vibrio
  ORGANISM  unclassified Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Thoden,J.B., Vinogradov,E., Gilbert,M., Salinger,A.J. and
            Holden,H.M.
  TITLE     Bacterial Sugar 3,4-Ketoisomerases: Structural Insight into Product
            Stereochemistry
  JOURNAL   Biochemistry 54 (29), 4495-4506 (2015)
   PUBMED   26125548
REFERENCE   2  (residues 1 to 136)
  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 136)
  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 136)
  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 14448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="unclassified Vibrio"
                     /db_xref="taxon:2614977"
     Protein         1..136
                     /product="sugar 3,4-ketoisomerase"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=15487
     Region          6..122
                     /region_name="cupin_QdtA-like"
                     /note="sugar 3,4-ketoisomerase QdtA and related proteins,
                     cupin domain; cd20292"
                     /db_xref="CDD:380426"
     Site            order(11,14,17..23,32..42,46..47,60,62,106,108,114..115)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380426"
     Site            order(34,36,47..48,50,115,120,122)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380426"
ORIGIN      
        1 msliklinfn vigdargslv aleqnndipf dikrvyylyg mqssvprgfh ahkdtvqvav
       61 clngsceilm ddgitkeiit lnspsqglli dvmqwhemyn fsencilmvm anevykesdy
      121 irnydeflke iqnvnn
//
LOCUS       WP_181869989             432 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Halomonas sp. DQ26W].
ACCESSION   WP_181869989
VERSION     WP_181869989.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. DQ26W
  ORGANISM  Halomonas sp. DQ26W
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..432
                     /organism="Halomonas sp. DQ26W"
                     /db_xref="taxon:2282311"
     Protein         1..432
                     /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=47808
     Region          9..426
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 msrqmdhanl fadarsrldd vfnaldvhdd viqrlmqpsl slkvsvpvrm ddgrlrvfpg
       61 wrvqydttlg pakggirfhp dvdqlevttl sfwmavkcav vdlpygggkg gvkvdpkqls
      121 rlelerlarg yiraiadvmg prrdipapdv ntnatvmgwm adeynhivrg kepaaitgkp
      181 pslggshgrv aatgrgalhv ldqwakrgqr kpedttlaiq gfgnaayhfa rlayergyri
      241 valsdsggai ysnegldpep imqqktqnqr lhdlvycdds vciaedvehl drddlltldv
      301 dvlvlaaled qvhsdnveqv kakalleian gpvtskaeaa lierdvpvlp dvlvntggvi
      361 vsyyewvqnr tgerwteetv nqrlaeqies qgrlvlerae kegisyrqaa yrqgieriah
      421 gilqrgncqy ge
//
LOCUS       WP_181870022             418 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Halomonas sp. DQ26W].
ACCESSION   WP_181870022
VERSION     WP_181870022.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. DQ26W
  ORGANISM  Halomonas sp. DQ26W
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Halomonas sp. DQ26W"
                     /db_xref="taxon:2282311"
     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=45056
     Region          6..407
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mhvqpqhadv aiigagivgl stawalieeg revvlidpgp pggeassgna atlanyavep
       61 larpsllptl psllfspasp fhlrwrhlpr ltpwllrfvg aarrsrteha trtlchllap
      121 slddwlalhs siqtdseaaa lhqrgalyff rrtrnwqlar sdfearqrlg vaqlylnaqe
      181 taalepaldg iaqgailfpe achfgdplrl anglakqler rgatfipara vslerhahgv
      241 siltdagdwh aeqvvvaaga wsqplarsag dripleverg yhlefsgaet llsrpccpae
      301 nafymtpleg rlriagtvel ghpadpanha rlaylrrhae amfgplgaas hewlglrpsl
      361 pdslpvigpa aipnvtyafg hghlgltlap ttgrlvaasl agkaphwlrh chasrfar
//
LOCUS       WP_181869886             278 aa            linear   BCT 28-DEC-2024
DEFINITION  RHS repeat-associated core domain-containing protein, partial
            [Escherichia coli].
ACCESSION   WP_181869886
VERSION     WP_181869886.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Tucker,R.P. and Chiquet-Ehrismann,R.
  TITLE     Teneurins: a conserved family of transmembrane proteins involved in
            intercellular signaling during development
  JOURNAL   Dev Biol 290 (2), 237-245 (2006)
   PUBMED   16406038
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Joo Lee,P., Ahn,J.Y., Kim,Y.H., Wook Kim,S., Kim,J.Y., Park,J.S.
            and Lee,J.
  TITLE     Cloning and heterologous expression of a novel insecticidal gene
            (tccC1) from Xenorhabdus nematophilus strain
  JOURNAL   Biochem Biophys Res Commun 319 (4), 1110-1116 (2004)
   PUBMED   15194482
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR03696.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..278
                     /product="RHS repeat-associated core domain-containing
                     protein"
     Region          <35..217
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          180..271
                     /region_name="AHH"
                     /note="A nuclease family of the HNH/ENDO VII superfamily
                     with conserved AHH; pfam14412"
                     /db_xref="CDD:464166"
ORIGIN      
        1 lvfngfelis qqfsrvrqph psvapqwvtr tnhavsdltg rplmlfnseg ktvwrpgqts
       61 lwglalslpa dtgypdprge ldpeaapgll yagqwqdves glcynrfryy epetgmylvs
      121 dplglqggeq tyryvpnplg widqyglagc pralaramkr anrnlaksag ymnrawykfk
      181 gsaahhivaw ddpralgark ilekygihid saengiflkh vdpnslqpgs yhrvihtnky
      241 yadvearlad aakangkqgv ldeldairdd llfnrliy
//
LOCUS       WP_181870046             125 aa            linear   BCT 28-DEC-2024
DEFINITION  group I truncated hemoglobin [Halomonas sp. DQ26W].
ACCESSION   WP_181870046
VERSION     WP_181870046.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. DQ26W
  ORGANISM  Halomonas sp. DQ26W
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 125)
  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 125)
  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 125)
  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 125)
  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 125)
  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..125
                     /organism="Halomonas sp. DQ26W"
                     /db_xref="taxon:2282311"
     Protein         1..125
                     /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=13886
     Region          8..123
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(10,15..16,19..20,23,58..59,62,91,94,98,101,112,115)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(24,33,36..37,45,49..50,53..54,56..58,60,68,70..73,
                     76..77,80,82,86..87,90,115,118,122)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(26,29..30,93,96,100..102)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 mtsislyerl ggergiaalv ediveshmqn pniqarflpy aedphhleev kghlrnflsa
       61 ggggpheyhg rsmpeahrgm niseaeymaa iddilavldk heidpqtrqe mlgiayslkd
      121 eimhv
//
LOCUS       WP_181870243             254 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Paracoccus
            lutimaris].
ACCESSION   WP_181870243
VERSION     WP_181870243.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus lutimaris
  ORGANISM  Paracoccus lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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 254)
  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 254)
  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 254)
  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..254
                     /organism="Paracoccus lutimaris"
                     /db_xref="taxon:1490030"
     Protein         1..254
                     /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=26673
     Region          11..249
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mteseiafdh dfaalsdrgr vrqqnedsvg afpefgvwvv adgmgghaag dvasriivee
       61 lgstgvaisa qdqrarvler lsrahlriln hsrdsglgga gstvaalllh gselacvwag
      121 dsriylmreg rltpltrdhs evallvaaga ltedqartap rrnvitraig igptvepdia
      181 sgvikdgdrl llcsdglteh lsdaeiaafa grslsaegva qalinetlqr gardnvsvil
      241 vdclarpapv edae
//
LOCUS       WP_181869772             254 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Brachybacterium alimentarium].
ACCESSION   WP_181869772
VERSION     WP_181869772.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 254)
  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 254)
  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 254)
  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 254)
  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..254
                     /organism="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     Protein         1..254
                     /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=26220
     Region          159..251
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtthisdaaa sagstaasst tpaaasaitv rpareadvdv ivdlvqvayr geggwtteah
       61 lvsgsrthaa evremladpa vtllaaeidt vdgldgldgl dtladasgpd sveaaddapt
      121 tspghaehag qpghaadspa psgprvvgcc ytrqepaddd gmtraelglf avhpglqsrg
      181 lggrlleaqa ehlreagiei lmirvlqsrp elhawyerhg fvrtgasvpf agnpdwlqve
      241 glgmdvmerp lqag
//
LOCUS       WP_181870323             551 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Paracoccus lutimaris].
ACCESSION   WP_181870323
VERSION     WP_181870323.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus lutimaris
  ORGANISM  Paracoccus lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus lutimaris"
                     /db_xref="taxon:1490030"
     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=57899
     Region          6..551
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 malarmtqgr marngigwqa aalavaalvl mpvlalavfa aqgspglwah lvqnvlpsaa
       61 sqtvillagv gvivasigti sawlvaacdf pgrrifgwal llplavptyi vayayldllh
      121 pvgpvqsllr dilgydsprd lrlpdirsmp gcilllglvl ypyvylpvra lfamqagnlm
      181 daarmlgagp vatfwrvvlp larpavavgt alalmeslnd igaaeflgvr tmtvsvystw
      241 inrsdlpgaa qislvmlaiv talillerrg rkrqryaaga qrsqpikrvr lrgwraalat
      301 lacalpvafg faapaaylai eaweryvfag lsprivaeag ntamfaaiat liavglglvv
      361 tgaarlrpgr ftqalarvst lgyavpgtil aigllpvitl adrqidavaq aiwgsgpgll
      421 llgsgaaliy aytarflaia tggiesglsr vppsldhvar tlgrtpagvf revhvpisrp
      481 alaaagllif vdcvkelpat lllrplnfet lathlygeaa rgtyedaaia aliivaigil
      541 pvivlartir r
//
LOCUS       WP_181870380             193 aa            linear   BCT 28-DEC-2024
DEFINITION  Maf family protein [Paracoccus lutimaris].
ACCESSION   WP_181870380
VERSION     WP_181870380.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus lutimaris
  ORGANISM  Paracoccus lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus lutimaris"
                     /db_xref="taxon:1490030"
     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=20521
     Region          4..189
                     /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 maappltlgs asprrlella qigispqqiv paeidetplr nelprryvqr marektqala
       61 gmgsgavlca dttvvagrri lgkpadarea aeflrllsgr rhlvltaial ghagrlqerl
      121 vetvirfrpl tameiddyla cgewqgkaga yavqgragaf vlwmrgsysg vvglplaeta
      181 tllagigirg kae
//
LOCUS       WP_181870356             333 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paracoccus lutimaris].
ACCESSION   WP_181870356
VERSION     WP_181870356.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus lutimaris
  ORGANISM  Paracoccus lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus lutimaris"
                     /db_xref="taxon:1490030"
     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=37527
     Region          12..323
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mtdaryaqye sllrllimle grsdgigiad ieqvagiqrr aaermrdvll ralpqleevr
       61 egaskrwrle apvlnrslap tledlaalnr avavlrasgd agtadclstl sdrlraaler
      121 rarpsfeidl ealleadgvv hrpgpreald aevvgrlrea ilcgcwveld lqtadsgrms
      181 wrnrvgpiaf llgegrqylv gfsdyrqqvq lfrlarlrgv rvlseayerp egfdlsrwla
      241 rsfgtwrdep hqiewrfash vaaevrqfrf hpdqrltdea dgsvtvrfta cgldemcwhl
      301 frwgdtvrvv apkalrerye dmlaaagaal dds
//
LOCUS       WP_181870378             291 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paracoccus lutimaris].
ACCESSION   WP_181870378
VERSION     WP_181870378.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus lutimaris
  ORGANISM  Paracoccus lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 291)
  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..291
                     /organism="Paracoccus lutimaris"
                     /db_xref="taxon:1490030"
     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=32131
     Region          57..244
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mlhaiatila trtvegvwqf yvsqmaewgf phaayhgvrl lsaaneqvad dsiflssysp
       61 rllhdlvsqn lfssvpmyrw itqhkgsesw gwlqarrlag rltaselrai dlftryghvs
      121 gyavsladsv hrvragvims gavgqrqdkl deywhlyqpq iealtglvhl rlaslpytpp
      181 devltarqre vlecisight tqeiaevldv tpstvekhlr larkalgart taqavllaas
      241 rrqmfvdpge actvasnqaa tgspatapqq pwgfasivet sdymrehipe t
//
LOCUS       WP_181870475             214 aa            linear   BCT 28-DEC-2024
DEFINITION  IbrB-like domain-containing protein [Hafnia paralvei].
ACCESSION   WP_181870475
VERSION     WP_181870475.1
KEYWORDS    RefSeq.
SOURCE      Hafnia paralvei
  ORGANISM  Hafnia paralvei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Hafnia.
REFERENCE   1  (residues 1 to 214)
  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: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Hafnia paralvei"
                     /db_xref="taxon:546367"
     Protein         1..214
                     /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]"
                     /calculated_mol_wt=23788
     Region          49..150
                     /region_name="IbrB_like"
                     /note="immunoglobulin-binding regulator IbrB activates eib
                     genes; cd16397"
                     /db_xref="CDD:319255"
ORIGIN      
        1 mgadmndtme eslqcleaal gemdeatrtl alntirrrlh tlspfrsepv dcvlwlpagk
       61 vrandynpnv mapveqrllh tslltegytq pvvvaqsgqg ysvvdgyhrm qlgkhkrrlr
      121 erlkgylpvv lvhqesggda erraatvrhn rargqhavta msdlvrdlar lgwedgriak
      181 elgmdagevl rlkqisglae lfgdetfsqa wtve
//
LOCUS       WP_181870494             170 aa            linear   BCT 28-DEC-2024
DEFINITION  YagU family protein [Hafnia paralvei].
ACCESSION   WP_181870494
VERSION     WP_181870494.1
KEYWORDS    RefSeq.
SOURCE      Hafnia paralvei
  ORGANISM  Hafnia paralvei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Hafnia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..170
                     /organism="Hafnia paralvei"
                     /db_xref="taxon:546367"
     Protein         1..170
                     /product="YagU family protein"
                     /calculated_mol_wt=18941
     Region          5..168
                     /region_name="YagU"
                     /note="Uncharacterized membrane protein YagU, involved in
                     acid resistance, DUF1440 family [Function unknown];
                     COG3477"
                     /db_xref="CDD:442700"
ORIGIN      
        1 msikllettp kqnrhyfiaf vigvitgiis afvksgtedi lpprtperia ppvqmltdmg
       61 idwhslvysy sdqlvywggn fvhivfsiva tvfycvvaei fpritmlqgi vfgilfavvc
      121 hgvmlpilgl spavihlpvd eiiseilgtc lwiwsvellr ialrekmtqi
//
LOCUS       WP_181870684             599 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Vreelandella rituensis].
ACCESSION   WP_181870684
VERSION     WP_181870684.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella rituensis
  ORGANISM  Vreelandella rituensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 599)
  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 599)
  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 599)
  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 599)
  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..599
                     /organism="Vreelandella rituensis"
                     /db_xref="taxon:2282306"
     Protein         1..599
                     /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=66038
     Region          9..592
                     /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 mfcincekgd vqmledtteq kyadtrlrdv eaalqaatew aqvtlnsigd avvttdlecr
       61 vtylnrvaet ltgwssidal gkplaqvftl idsqtlqaat npaqrameen rtvglamdcv
      121 lirqdgsqle iedsaapihd rdgcikgavi vfhdachspt hssklayqaq hdaltdlpnr
      181 vllserlsra iglakrhqhq vallyldlda fkavndslgh avgdfllqsv agrlsecird
      241 tdticrqggd efvvllseie npqdavriae kilgslaepy ricnhelrit tsigislypd
      301 hgtddhtlln nadtamyhak ksgpnhyqlf eaemhalkmq hshlksqlqp alkadalfld
      361 fqpridiatg ypvsaealvr wrnptlgliq psvflpvaea cglivpighw vlseacrrlq
      421 kwraegveiv piavnmsaie lcdktlpari adiltktgle ahflelevte sclmqlytdt
      481 sistlvelsr mgvriaiddf gagsvslkhl kcfpinmlni apcfvhdmld drenvsfika
      541 linfgqdlsl rviakgvetq aqfdhlklqg cdgaqgflfs kslsakdfrg lldpdwprl
//
LOCUS       WP_181870857             312 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Escherichia coli].
ACCESSION   WP_181870857
VERSION     WP_181870857.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 312)
  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..312
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>312
                     /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..>311
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mlilkaykfr leptpeqsqr lrqlcgcarf vwnlglaetk rildsgeklp safelnrmit
       61 vwkkmpeyif lqdaytdnlq qklkdlhtaw krcfdkklaa kapvwkrkne grdsirfvnf
      121 ekycclenrr vklpsglgwv kfrqsqrvng kiknatisql agqwyisfqv eietaepnht
      181 sttivgldag vaklatlsdg tvfepvnsfq knqkklarlq rqlsrkvkfs nnwqkqkrki
      241 qclhsriani rrdylhkvtt tvsknhamiv iedlkvsnms ksaagtvsqp grnvraksgl
      301 nrsildqgwy em
//
LOCUS       WP_181871009             843 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Sphaerisporangium album].
ACCESSION   WP_181871009
VERSION     WP_181871009.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
REFERENCE   1  (residues 1 to 843)
  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..843
                     /organism="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     Protein         1..843
                     /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=84224
     Region          101..538
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     Region          <506..762
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mqpllpgdpq qvgdytllgr lgdgprgtay laehtrpasa pqspaspgss issvpettpa
       61 psgtgsepsa aepsetgars setagtvaep ssprasgepa aegsgdeprf vvkllprwpe
      121 addqarsrvl ddlsaaqrvs sayavraida gwvddrayvv reyvegrslr qaveaggplt
      181 gdaleriavg tltaltavhl agiahrglta dnvflgpdgp rvadfglget dyrspeqvrg
      241 epagpaadvf awartmayaa tggepftggp qaiatawpdl galptplrdv agaclaktpa
      301 qrptaqgaml wllgeekaap paraipaapv pgavlppaag sapgmvisge lvsgpessgd
      361 tvavtpggsg vvipgpavsg pvisgdprpe agvvepgsvv tprtagqepv wevpaqappt
      421 qqvwsapalp teespehpar psangeggsa aasprkkaga hfpvglaagv givvglaglg
      481 lwgagkyasp qeigrvaaeg qvtgaaesag tqaqgsdvgg ttaprpqvtv pwatspapqd
      541 qgvypmritt atpsigiptp sqwpqftppp iptqttspaq spspqptvtv tatptvspsa
      601 eptpspsgps etpvpsgtps psptgsptas ptgsptgspt gsptgspvps ttasptaspt
      661 lsprptasgp atprptatrt vtprptvtrp rptvtkpfvp vpvatgsvap rptggtvvpr
      721 atqptrtqap asnpytpaqv cesagrgtay yvqrssafsg gvtyqlfsnq sgascvvtmk
      781 tdhigvaspv satlevqgsa pltdggseky yagpvimqsk gkcvrfrgtt gsgstsapfg
      841 ncr
//
LOCUS       WP_181870918             407 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: O-antigen ligase family protein [Eggerthella].
ACCESSION   WP_181870918
VERSION     WP_181870918.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 407)
  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..407
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..407
                     /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=45509
     Region          160..384
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 maegdlqaar psvfyllavf sflffapleg lyaqysvlra lswlclfasv flllcfyivh
       61 sargegkrld vvfflvalic lifgsftlvn egslfqymkk vafilgpwly ltvfgrygfk
      121 pvlkamligs liiiganfit mlimyphggf rpeygdtwlf gqrtymrnfi flalclclfy
      181 drvrhrrfsv ltlavvvvsl atlilgdamt slvvmvflla vlvlsgcglk csiilrpivv
      241 vsvaldvllv hlrqialfgd fivgvldrnl tlsyrtqawd vameeigtnp lvgtgfrdle
      301 esgitvgfgr qlsnahnevl dvcykggllg alsffalvav cclpllrksg ywaafilgaf
      361 lggffiealv sdiwypqfff llyfaaylkh waplleetkr qtpqrea
//
LOCUS       WP_181871011            1001 aa            linear   BCT 28-DEC-2024
DEFINITION  AfsR/SARP family transcriptional regulator [Sphaerisporangium
            album].
ACCESSION   WP_181871011
VERSION     WP_181871011.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
REFERENCE   1  (residues 1 to 1001)
  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 1001)
  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 1001)
  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 1001)
  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..1001
                     /organism="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     Protein         1..1001
                     /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=108412
     Region          1..228
                     /region_name="DnrI"
                     /note="DNA-binding transcriptional regulator
                     DnrI/AfsR/EmbR, SARP family, contains BTAD domain
                     [Transcription]; COG3629"
                     /db_xref="CDD:442847"
     Region          94..997
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          675..703
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(676,679..680,683..684,686,710,719..720,723..724,
                     726..727,756,759..760,763..764,767)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          708..744
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          755..783
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(803..804,806,830,839..840,843..844,846..847,876,
                     879..880,883..884,887)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          828..870
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          875..903
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          915..943
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mefrllgwvg ledggreidt ghsrqrcvla allidarepv mtaelvsrvw gsdppdsaln
       61 vlygyvtrlr kvlapsgirl lrrgggylid vepalvdalr fkrlqatdpa aaleawrgkp
      121 lpgiegewad qvraglialh lsaqlrlaee etaqgrhtaa vdrlsgvlae hpleervvav
      181 lmtalfragn tpqaldcyla frrrlsdelg igpgarlrll hqrilegdsa ldrqeaapvp
      241 aglpydvpgf vgratelaam nrvlrsrtpl visaiegmag vgksalavrw ahrvrerfpd
      301 gslyadlggh aptgpadpar vlgdflaalg taparipggl darsalfral ldqrrmliil
      361 dnarseqqvr pllptadsca tvitsrvplh glvvreraqr ivigtltpae sesllrtfvp
      421 ygdaaslrel arlcahlpva lcvageraar gdrplpdlva elrsasnrld llevagdpls
      481 svravfswsy rtlpepvasm frrlgahpgp diepgaaavl tgcspgeaad llgalaearl
      541 iepyqpgrwr mhdllraysv ecggeqdeav arlldhyldr lssaislalp gevvirpdae
      601 pfpdpaqaqa wmeaersnlv aaadmaltrs palgrdlgrm lvrhldmagq qeearrlyrs
      661 aaraahatgd lmgqasalta lgvalirnge leeahesfrr avelwetldd prsqggalgn
      721 iamiqvfrgq yaaaladler aaalfersgh lsgqanvlnh igeihwrtga yriavplher
      781 ameiaaeigd ragvavsrgd ignalfrlge ygealehlea srdlarsisy vyaeltsmvn
      841 igrvhaatgd lqaaydlyqe vlaalreted rdmeaetldc lgeiylawge heraldhhrr
      901 alelfrasgs rtfeasalng lgeveralgh pkeagarhqe aleltkamgd rfqqaralvg
      961 larlradqgl paeewgealr lmddmevpea aqlrgelnap l
//
LOCUS       WP_181871058             407 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Sphaerisporangium album].
ACCESSION   WP_181871058
VERSION     WP_181871058.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
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="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     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=43315
     Region          6..405
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mrapvrvalg ngipvwvlnr pgatattvsl wlltgsryep eavaggthll ehilmqaplp
       61 gggrpidlle glggegnait srdhlvlyar vpspeapaal eilaramaep dlgeeilese
      121 rkvvqeelrl aagdpfdivh dvfydvafag hplarpvggt aesvgrvnld dlrafhsrwv
      181 rassaavivc gdltpeavlk vlesgpltal ppgggepdhg lpsvsggrrn hplnndsagv
      241 vlggpavpyg hrllpawqvl mdliggassa llfeeirnrr glaydmwaft nayrdtgvwr
      301 afiatapehv gevvetatal lteraergwt aaevelatrr tagllqlete qsfeeallyg
      361 ryglipghdn wtlagqiesi ravtaedvll slrtaldpmv itvagid
//
LOCUS       WP_181871191             292 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Sphaerisporangium album].
ACCESSION   WP_181871191
VERSION     WP_181871191.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
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="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     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=33049
     Region          4..245
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mlsfvigtgr cgstlvhevl arhpevgfvs nlddryarcp gwvrrnsgai yrrvpprlta
       61 kgrlryapse aysalarevs pllvdpfrdl lasdvtpwla rrtraffesr aeaegapayl
      121 hkftgwprtg flreifpgtr fvhivrdgra vanslvqmpw wrghlgpegw sfgplperya
      181 rewdaegrpl vhlaglawkh lidaygaare alpedawlev ryedivadpr khlevilefl
      241 glswthgfer gfarysfsas radafrrdlt paqvglldrs lgghlerfgy ql
//
LOCUS       WP_181871196             352 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator
            [Sphaerisporangium album].
ACCESSION   WP_181871196
VERSION     WP_181871196.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
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   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 352)
  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..352
                     /organism="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     Protein         1..352
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=38844
     Region          55..152
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
     Region          218..307
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mnekeipagv gtgrpaagra tngvdaidas pggallgvap gqpggpgepa aglsgigral
       61 ailgdrwvll ilqrafllhv rtfagwrdql gisesvlasr lkelvrygif eqkayrdgrt
      121 rleyrlteag lklwsflvav hswerdwadr pdlltlmhdr crhdarpyla cgacrkpmta
      181 rdthtvrgpl atfsrvglpr qhrrttargd vrtdyvgycp lsmeilgdrw stsvlagafl
      241 gvrrfvdfqs elgiapsvlt drlkrfvelg vlqadagrhy rltdrglayf evfaflvhwg
      301 qrelpgppgs dldithkpcg splspvllcr hchevlerre vrfdlsayph la
//
LOCUS       WP_181871222             322 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Sphaerisporangium album].
ACCESSION   WP_181871222
VERSION     WP_181871222.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
REFERENCE   1  (residues 1 to 322)
  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 322)
  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 322)
  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 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   5  (residues 1 to 322)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..322
                     /organism="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     Protein         1..322
                     /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=34966
     Region          3..222
                     /region_name="DUF5937"
                     /note="Family of unknown function (DUF5937); pfam19361"
                     /db_xref="CDD:466054"
     Region          <256..314
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mitvkfnisg lartriapsp afeitswlrl aaanrrhpil gmagsaarya lrdpdvalva
       61 avmppgaqgy vldmltprpd agpwhrvlag qldavsetpi ekiaeqllee rfpdgdmpdg
      121 vrraledggf arraadglrr fwltaladqr kgleerlsad laarahlmat ygvghvlesl
      181 hpdldwapee mrivkpydga gdlsdselvl spsllgwpnl hvqvcdplda fmaypvsatg
      241 papkadtgls gligtsraai lrdlavsrst telsrrhrla pstvsyhlsv lleadlvsrt
      301 rqgpvvryqr traanallrd rr
//
LOCUS       WP_181871352             335 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Sphaerisporangium album].
ACCESSION   WP_181871352
VERSION     WP_181871352.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
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 11454343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     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=36069
     Region          117..334
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mspaerwavp lwavfaigns almwvvpgae tipfhlvwis lalvygvrpw pvpatlavcl
       61 gvavatgapl wqhahskvia feetaeiplm cllflvmvwh vrrrtaavae arlaasrerv
      121 ahemterfvr iathelrtpi tvargyaeml qldssdpgqa sdvsvvvdel gklsritgrl
      181 aalawahqda rdgalvldlg alvqrvarrw apvvdgtirv esaptpvagd eermetaldc
      241 lvenairhgr apialrvrqd asaavveved hgpgiapara rellrgsdsp ysprsglglm
      301 iaqgiveahs grialtraps gglkatihlp rlrpe
//
LOCUS       WP_181871378             178 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Sphaerisporangium
            album].
ACCESSION   WP_181871378
VERSION     WP_181871378.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 178)
  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..178
                     /organism="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     Protein         1..178
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=19427
     Region          34..78
                     /region_name="HTH_26"
                     /note="Cro/C1-type HTH DNA-binding domain; pfam13443"
                     /db_xref="CDD:433211"
ORIGIN      
        1 madkryrrpl aeqldhlfrt vrqpdgttys yeqaareitr rgtpvshttl wklrtgrtdd
       61 lsvshlvaia dffgvepayf fddayaeqan vrlellpamr dagvrriamr aaglshssie
      121 niaamiahlr tleglppdsp ggttpskdvl dpppasspdp vrgavskapr taepearp
//
LOCUS       WP_181871450             341 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Sphaerisporangium album].
ACCESSION   WP_181871450
VERSION     WP_181871450.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
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="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     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=34626
     Region          27..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 mtragglrpv lllaslaavl lvlcllsial gargvpldqv lralsghads rlvenivwtv
       61 rvprtalgla agaalglaga lmqaltrnpl adpgvlgvsa gaafaivfsv avlglgslyg
      121 yvwfafagal aagvlvfflg rlgrsgltpv klalagiavt slltsltsav vltnpdalnr
      181 yrfwnagsla dqtgatvlrv lpfvaagall alacapalns lalgddvaas lgrrlglvrl
      241 qgvaavtllt gatvsvigpv vflglvipha arvlaqragv gpdhrwllpl sallapclll
      301 aadivgrvvv rpveiqagvl iafiggpffi amvrrrrlae v
//
LOCUS       WP_181871605             195 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Sphaerisporangium album].
ACCESSION   WP_181871605
VERSION     WP_181871605.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
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="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     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=20806
     Region          18..>89
                     /region_name="COG1777"
                     /note="Predicted transcriptional regulator, ArsR family
                     [Transcription]"
                     /db_xref="CDD:441383"
ORIGIN      
        1 mqdiaviedp aaaevsldpi rarllaelse pgsatmlaak vglprqkvny hlktleahgl
       61 vemieerrkg nvnerimrat aasyvispta lasvepdpar spdqlsaswl lavaarlvrd
      121 vgalitgaar arkrlatfai dgevrfasaa draafaqela qtvaalvsky hdesaeqgrd
      181 hrivvavhps mkeap
//
LOCUS       WP_181871625             640 aa            linear   BCT 28-DEC-2024
DEFINITION  dipeptide ABC transporter ATP-binding protein [Sphaerisporangium
            album].
ACCESSION   WP_181871625
VERSION     WP_181871625.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
COMMENT     REFSEQ: This record represents a single, non-redundant, 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..640
                     /organism="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     Protein         1..640
                     /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=66725
     Region          23..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 mtestrthap eashpdvpea ahapplveia glsvdfatrh gvvravrdvd ltlragqcla
       61 lvgesgsgks vtartligla gegatvragt lafegrdllr lggrewrrlr grrigyvlqd
      121 algsldplrr vgdevaeple vhglatrddl edrvigllad agipdpeerl lqyphelsgg
      181 lrqraliasa iaarpsllia depttaldvt vqaqvldllr qmkdagtall lishdlavva
      241 rmadhiavmr agqvveqgpa thvltqpehp htaallaavp sldagprtat tlaapvarag
      301 tvlaeaagsg tgpllvdpav sktgprspga aaggavdvvq vravtktfrs ldgrrrtavd
      361 dvsftlaage alglvgesgs gksttarlvl aefepdagsv lldgepwsgp rerdrrarrs
      421 riqlvdqdpl gsfdprftve qviaealgpg apvngseggr peapgsgvrg grpfgsgaga
      481 rrervvella avgldagflv rgparlsggq rqrvaiaral apgpevlvcd epvsaldvtv
      541 qaqilallar lrreaglsll fishdlgvvr qvcdrvavmk dgaiveigev davfraprhp
      601 ytaallaavp rldtawhdta rplngpatep atdrdtkgir
//
LOCUS       WP_181871205             212 aa            linear   BCT 28-DEC-2024
DEFINITION  GOLPH3/VPS74 family protein [Sphaerisporangium album].
ACCESSION   WP_181871205
VERSION     WP_181871205.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
REFERENCE   1  (residues 1 to 212)
  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 212)
  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..212
                     /organism="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     Protein         1..212
                     /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=23165
     Region          8..>149
                     /region_name="GPP34"
                     /note="Golgi phosphoprotein 3 (GPP34); pfam05719"
                     /db_xref="CDD:428605"
ORIGIN      
        1 mvdvpdtlpe rlylltydve kkrmtyrsel gylmragila elllaghiad atggpvarak
       61 tladplldet lqmvaesrrr twqhwvnkgs gaaarqvrdr lesggwirve rrhvlgfipl
      121 tkvtvrdtrv vkrlagtvas alrgahpasr ldrrdaalaa laaavrlrtv mpradwrarr
      181 vrgeelaevv apvpwalrka iqaaqaaags gg
//
LOCUS       WP_181871716             265 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Brevibacterium aurantiacum].
ACCESSION   WP_181871716
VERSION     WP_181871716.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium aurantiacum
  ORGANISM  Brevibacterium aurantiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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..265
                     /organism="Brevibacterium aurantiacum"
                     /db_xref="taxon:273384"
     Protein         1..265
                     /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=28896
     Region          <14..253
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mwrlaafapd attrniilvm astglrfgev aalrvedfdp dtgeivvnka laldhgkvye
       61 trtkshedrs vyiddwvral iaeavegrgd rdriftteqg rdlnrdnwad rkfgkaasra
      121 csaiadlqse lgvserkkgv affgpktaka lkegsqsqsl qdvlrtpgew iepqfdhavk
      181 viatsdgggf qvlkpddvdf kkptphdmrh taashlirqg tdvktvqsql ghadagttln
      241 tyagvwddak veagrvlasa larpe
//
LOCUS       WP_181871739             111 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Brevibacterium aurantiacum].
ACCESSION   WP_181871739
VERSION     WP_181871739.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium aurantiacum
  ORGANISM  Brevibacterium aurantiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
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="Brevibacterium aurantiacum"
                     /db_xref="taxon:273384"
     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=12100
     Region          25..103
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mpkyaipdsp lppgaggaar mlginhvrmv ilrslqdype gattgmlaqd ldlpyqtvvr
       61 hvraleddgl vssdtedrag rrvnytvdrt kvasllgdlw qyllparpqd d
//
LOCUS       WP_181871901             365 aa            linear   BCT 28-DEC-2024
DEFINITION  EamA family transporter [Brachybacterium alimentarium].
ACCESSION   WP_181871901
VERSION     WP_181871901.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 365)
  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 365)
  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..365
                     /organism="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     Protein         1..365
                     /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=36943
     Region          26..309
                     /region_name="RhtA"
                     /note="Threonine/homoserine efflux transporter RhtA [Amino
                     acid transport and metabolism]; COG5006"
                     /db_xref="CDD:444030"
ORIGIN      
        1 mttsassapt aqapvavasr ggsgvpltpv lfilgscisl qfgaalatql fpalgswgtt
       61 alrlgiaaiv llvivrpklh rftrqqwiav llfggaigam ngsfyaaiar iplgtavaie
      121 flgplavsal lstrrsdllw vvlalggvgl fgvesftgaa aldglgvlfa lvaavfwgty
      181 iltsarvgkl vpgqdglava mavgallvlp fgasgavtgv ldlhllalav gtallasvlp
      241 ytlelaalrr lprhvfgill slepvialla gvlligqeat alrvaaavlv vgasvgitlt
      301 arstapgepq pvdeapgwel ptpthatltg empmlteedl iaenliaedl dadgqpaedg
      361 praae
//
LOCUS       WP_181871923             482 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Brachybacterium alimentarium].
ACCESSION   WP_181871923
VERSION     WP_181871923.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..482
                     /organism="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     Protein         1..482
                     /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=50476
     Region          64..406
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mhttasipaa rrpdgvtait atatvtradl adladpacas atdsgteras tdpaaasaaa
       61 grrdpaidlv ralcvlavvv lhgiqvgvtv tgtapvleyt tvyapwyppl twilqvmpif
      121 fviggfagal alrrllargg tstdfvvgrv hrlllpaivt vlavgmvlaw lgilgvpael
      181 lglagvrygq plwflgvfla cqallpallr ahdraavrtl vmlviaavtv dalrgltsid
      241 algytniafv wlalqqlgff lvdgpldals pavrrsagaa avavliggvv agiwtpdlia
      301 hlnpptiall lvgaaqtaal sllrpalael sahpwieaft rfvtartmti ylwnlpvlla
      361 magvsavlal rdgmplpeps glmwwttrpw wlvlsivltf alaavlgsie rrrparptrl
      421 srralqavll gligvlilll agttvltaga avglflaals rirarvpred saspprvrtv
      481 gr
//
LOCUS       WP_181871943             431 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Brachybacterium alimentarium].
ACCESSION   WP_181871943
VERSION     WP_181871943.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium alimentarium
  ORGANISM  Brachybacterium alimentarium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
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="Brachybacterium alimentarium"
                     /db_xref="taxon:47845"
     Protein         1..431
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46019
     Region          <222..431
                     /region_name="Fes"
                     /note="Enterochelin esterase or related enzyme [Inorganic
                     ion transport and metabolism]; COG2382"
                     /db_xref="CDD:441948"
ORIGIN      
        1 mplpasddll fpaalwqprp rsggpeeplp itrrdelgie taaasadgsp lgagpafgeg
       61 prvisrggdt alvhfrhaar aatavalqan gwwrpeprea cdlrptgngw wegtfevpad
      121 wratygyveh eedgdppwwe sglkdpgapv vsdlsnprrh raarggaqra vicvpddgpf
      181 tpglvrdgep spllhtlatr egepvtrwwa srpgdpgced ldpsaplpll ivtdglqhvd
      241 qlgtpsrlrr gvaagilppl aavfvesgps rnevlgvpgg harwiaeqla prlreeglrd
      301 stgdvpltdq asrtivtgss fggltalfav arapqligta iaqsvslwry eegalveplr
      361 raarqhplrl rlhagrfegt mparaaalld gltagagtdd rldatlavhs gghdwawwqp
      421 mmlqelaall r
//
LOCUS       WP_181872289             520 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Eggerthella].
ACCESSION   WP_181872289
VERSION     WP_181872289.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 520)
  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 520)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 520)
  AUTHORS   Rosinski,J.A. 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 520)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..520
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..520
                     /product="helix-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=55813
     Region          338..507
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          448..501
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msetrcerel gkkpwtqmll rldddmpllk yfgfacwvaw fsvaysssvw vegaeetasv
       61 vsdmflystl shatallaca cfsqavskva drpwfppsag alaalgcvcv vqagsllvss
      121 talfvagscl tgigtaalsi naglllcavr prqalrvily cellaallqf mvlglpdpfd
      181 lalfvalpll saacfvvgsa qrakpvvqes qrlkpskafg lfllvvcvls aaanfgkgmh
      241 ravvspgqla edgsittllt vvclvalllf islrrrelnf ehllypmalv tilslsvtff
      301 fpgsavvgvv lvgvafqlfd vvtwymfsyi vyqskasavq vvalgraiia lgvtmgdalg
      361 arcagmgied aplatavfvl lfaaviavff vfperqvdkl llpipdedde gvasadasev
      421 savegedata aehrgrwkql cmqlgderql terekevlvm largygsqsi sdaltislyt
      481 trahtrniya kldvhsrqel adcvrayvea fdrdvasgra
//
LOCUS       WP_181872009             665 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Bergeyella
            zoohelcum].
ACCESSION   WP_181872009
VERSION     WP_181872009.1
KEYWORDS    RefSeq.
SOURCE      Bergeyella zoohelcum
  ORGANISM  Bergeyella zoohelcum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Bergeyella.
REFERENCE   1  (residues 1 to 665)
  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 665)
  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 665)
  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 665)
  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..665
                     /organism="Bergeyella zoohelcum"
                     /db_xref="taxon:1015"
     Protein         1..665
                     /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=74681
     Region          2..581
                     /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 mifiarlayl qlftdryvln aantsiktey iipqrgaifd rngqilvsnq psyelsftkn
       61 llkkedfnva efcqligist eeyeqkmkvi deeiaakkhs kltpipflkn isredvariq
      121 eiifkypafs ivqrpqrkye vntsgiilgy tnevnnqeia kdslyyirgd ligkrgveks
      181 yekvlrgekg vryiqkdikl rdigsyknga ldkeevsgkd itltldyelq rmaeemlvnk
      241 kgaivaldpn ngeilvmatg pdidpnlfsg pektknlyql qvdtiydwkp tfdrsvqaay
      301 ppgstfkmlt alaamqmgvm dentifpcgg gfryrglgik ghggadplip airvssncyf
      361 syafiammnk ypgdpgrgvd ewkaimesfg lgrymnndla sgvtgfipdg efyrkrsggk
      421 kdwspqytmn gsiyngmgqg avsltplqma nftaaiandg wyytphivka idgkpnpdpr
      481 fkkknytlvq nkkyyefvkk gmeqvvlggt arglksseft qmaktgtaqv pqgkdnsifv
      541 liapadkpki vvaavmehag fgatwagpac tviaekyitg dlkrehlykk mitssflpey
      601 krqwvtdlkr kglykepskd svallkieal lednppkdqk qklirqkdsi ierirktvpl
      661 ksikk
//
LOCUS       WP_181872382             100 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Phyllobacterium
            bourgognense].
ACCESSION   WP_181872382
VERSION     WP_181872382.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium bourgognense
  ORGANISM  Phyllobacterium bourgognense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
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="Phyllobacterium bourgognense"
                     /db_xref="taxon:314236"
     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=11392
     Region          1..100
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mfvyvhdeql dlifktlgda trrrildllq erserslfei casfaaadgk slsrqtisqh
       61 ldmleragli itswkgrtkt hslnvapmqv atnqwlkkyl
//
LOCUS       WP_181872424             373 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Phyllobacterium bourgognense].
ACCESSION   WP_181872424
VERSION     WP_181872424.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium bourgognense
  ORGANISM  Phyllobacterium bourgognense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..373
                     /organism="Phyllobacterium bourgognense"
                     /db_xref="taxon:314236"
     Protein         1..373
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39080
     Region          117..360
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mnkyifvsgl llaltalsgc nnsnphssst tpdqsattas tfatsvatpa gtpevttget
       61 tsiddtlgkd rtakdddptq appnsppqli vndetpppsk plppftvkee ittflvngqk
      121 vvgtlavpeg tgpapvilvf hgytgsrdan lvagtggesl fsraarlwat egyaslridf
      181 rnsgesdgiw adttfdgqid daiaavaflq idkrvdgkri aavgwsqggl vasalaaktp
      241 alravglwna vtvppltysl ilgpqalkdg paaanklvgr tglkgsffqg iytidpvaei
      301 arydgplfva agtndsvvap qpqmgnlflk yhegieelwv rdmdhgfdkd rsaavvdema
      361 katltllrkg ldk
//
LOCUS       WP_181871644             245 aa            linear   BCT 28-DEC-2024
DEFINITION  adenylate kinase family protein [Sphaerisporangium album].
ACCESSION   WP_181871644
VERSION     WP_181871644.1
KEYWORDS    RefSeq.
SOURCE      Sphaerisporangium album
  ORGANISM  Sphaerisporangium album
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Sphaerisporangium.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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 245)
  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..245
                     /organism="Sphaerisporangium album"
                     /db_xref="taxon:509200"
     Protein         1..245
                     /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=26045
     Region          18..188
                     /region_name="Adk"
                     /note="Adenylate kinase or related kinase [Nucleotide
                     transport and metabolism]; COG0563"
                     /db_xref="CDD:440329"
ORIGIN      
        1 mllaqqsarq gpvavsvlgp paagksslta tlasrhrgli frlreyarhr aahdeglaqt
       61 mrtstdplgw vpdpvalsli dhalhgpfrp spgilllleg fpgnpvqavh tagvldrmgv
      121 elhvvellvd qesarrraqt rrvcpacesg sadephrpat agpdggcarc ggplrarrdd
      181 tadllaartg rfrqhhprir refqtrgvpw htidtrcspa avvaaaeaal gicpslhpdp
      241 galip
//
LOCUS       WP_181872701             850 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Billgrantia montanilacus].
ACCESSION   WP_181872701
VERSION     WP_181872701.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia montanilacus
  ORGANISM  Billgrantia montanilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 850)
  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 850)
  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 850)
  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 850)
  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..850
                     /organism="Billgrantia montanilacus"
                     /db_xref="taxon:2282305"
     Protein         1..850
                     /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=94075
     Region          182..848
                     /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 mesagkvkhm tapsmqiihv dwnalrlisl erfmaetpdt nalftdlaea lamafsmvcv
       61 avivkdgnsp gyltgdsdaa qllltldgvq atladgnprt evpppgtala naafiaiepl
      121 slphqqeqtt viafagknli dservvalmh slatetanel mvlrqapfla aafaeiecgv
      181 tiadptladt pliyanaafe rmtgypraei lgrncrflqg dlqdqpgrri lrnaltrgtd
      241 ctvivtnfrr ngesfenrlk lrtirtpdgt ishiigiqld vtkersales larqkrryes
      301 lieaqtgfiw lmnaegelme vpekwlemag lslsrvpadl aairgalspe aaeafcdgwv
      361 ealrnvtpfe viyhlpaqsr sprwfldrvt pvldeehkll ewiaasqeit elkraekeie
      421 raayedrltg llspegfaqr lderlkrmdl hpaspvvvvd ikalreinnt qgydvgdevl
      481 revarrltae vgesgliart ggdeftvlap lenqrtprql skcmaavfdv pfeirgfsfh
      541 veasfgyari rssagdarkl mtdaalamhr sqhnpaltwt qytkaldhqt retvnlttkl
      601 rhalqadqle lyyqpqvdla sgrivsaeal lrwnhpqagf ippgkfipla eqsqligpig
      661 dwvlrracrd lrawrdagll vtpvsinlsl iqfqlgsvpd kvrqaltdyn iapeeltlei
      721 tesvfehqgq alkqdlealt amgvrlsldd fgtgysslah lndyffdeik idksfvsqld
      781 kgpyaqsivk avvviaaaig advvaegiew sshittvlhl gctkgqgyhf srpvpeprwr
      841 qllfdqkalp
//
LOCUS       WP_181872678             271 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Eggerthella].
ACCESSION   WP_181872678
VERSION     WP_181872678.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella
  ORGANISM  Eggerthella
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae.
REFERENCE   1  (residues 1 to 271)
  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 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The 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 271)
  AUTHORS   Rosinski,J.A. 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 271)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..271
                     /organism="Eggerthella"
                     /db_xref="taxon:84111"
     Protein         1..271
                     /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=30831
     Region          206..270
                     /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 mrksgatekt germvelsdt rwraiddlll alygasdlad lrrrvmrgfk dlvpydkgff
       61 dlcdcsesgr fvffdpvsvd mtdeellsyy qkyepsdytt wlfsvndpvv yrdstfvtde
      121 mrkrselyre wmipmdthfs mgstqvgngm iygsitlfrn rasgdfteee eeclavlnrh
      181 lstclavahp rglrrdegkp vvgrtsltar eqeiaaliae glsnqqiglr lfisentvkk
      241 hvkgifqkmg vsnrhqlmae lyrtaaivvd a
//
LOCUS       WP_181872762             298 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Billgrantia
            montanilacus].
ACCESSION   WP_181872762
VERSION     WP_181872762.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia montanilacus
  ORGANISM  Billgrantia montanilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
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   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 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   4  (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 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Billgrantia montanilacus"
                     /db_xref="taxon:2282305"
     Protein         1..298
                     /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=33061
     Region          57..294
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          214..294
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mavgvnhcst hgsrslgclp ltqthceldd glavnllrhh saferieksc dpygrpmlal
       61 tfglqgesqf rqndgarltf ragyttiagf tasrgerclp agqsilqlri llderrlrqy
      121 angeqvakwl gndsvnrlaf aattgvchah vralacqmqq dcsrldmqvh alsalahalr
      181 vllldsrenn rlsharierl erarslller ldcppaladl saavglneca lkqgfrhrfg
      241 ttprrllhea rmceahtfle sgcqvaqaay rvgyahpgnf svaflryygy ypkavfdk
//
LOCUS       WP_181872810             427 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Billgrantia montanilacus].
ACCESSION   WP_181872810
VERSION     WP_181872810.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia montanilacus
  ORGANISM  Billgrantia montanilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 427)
  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 427)
  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 427)
  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 427)
  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 427)
  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 427)
  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..427
                     /organism="Billgrantia montanilacus"
                     /db_xref="taxon:2282305"
     Protein         1..427
                     /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=48475
     Region          112..412
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mllvigysll sayyftrgmd nimmanmsqa aqsfiervpa tqhdvrnefs gftitrdwlq
       61 mpeeirqafd qpprepnvly krvegarlgp pdalniaihl qpddfplyva mrmthemapd
      121 hevasldaih rllaliaigl aivllltasl wwlwrhvsgp vnalgqwart ldaaklaelp
      181 pdfvypelne mahlvrssls saqeslareq rflafashel rtpisvvrsn lelmrkmqqc
      241 epeestfrqe qvlarmeras ltmkhltetl lwlsrdqhep lpsheldldk likevieelr
      301 ylleekcvev tvdterfatl lpeapariil gnlirnaflh twegqiairq egcqvwiene
      361 qsalardsdt gpshtdqgfg lglklteqla dklgwpytnq pgpmghriyi elrcsamgfv
      421 daisrap
//
LOCUS       WP_181872874             625 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Billgrantia montanilacus].
ACCESSION   WP_181872874
VERSION     WP_181872874.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia montanilacus
  ORGANISM  Billgrantia montanilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 625)
  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 625)
  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 625)
  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 625)
  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..625
                     /organism="Billgrantia montanilacus"
                     /db_xref="taxon:2282305"
     Protein         1..625
                     /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=69436
     Region          17..499
                     /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 mplqnetepa gtlgermkla lfkvtryrnv wdsgwvdvnd vtafvgqnes gksnlfealy
       61 rinpfsaddi ydidedwpvd dwgnkdpstl vceahfalaa ediedlyeva gllasdeged
      121 sqltaeateg eevahvapei paelvlvgsr sydsgpmfav agdqaadldp ksvdawakry
      181 vpkfvliqdy glsgtqieln qladrykklh whgltneeqt vkivldlaki diddflakgg
      241 taegrtvrsf dkraassyls kqfrdlwtqk kvnfhieidg ttlnifaede avgmpvrlhr
      301 rssgfrwhvs fawkfthask ghykdcilll eepgvhlhys gqrdllevfq rlsesntily
      361 tthlasmvdp aypervrive tqannhttvk kgvvssqrap mavvelslgl tgdmsgllgt
      421 rqtliveggd dalilhklsg ilrsegkphl sdriylwpar gapktpmyaa favgqgwdag
      481 vlldtdhegq takkkidelv lkdlageqka rfrvlmlgta agikktdaai edlfedqfyi
      541 dcvntafgla ikpgdlpedg sdmitkrver vlieryghkt idkrrimsei msrfdgwekv
      601 sdlpkgtptr aeklftainn afsaa
//
LOCUS       WP_181872879            1067 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Billgrantia montanilacus].
ACCESSION   WP_181872879
VERSION     WP_181872879.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia montanilacus
  ORGANISM  Billgrantia montanilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1067
                     /organism="Billgrantia montanilacus"
                     /db_xref="taxon:2282305"
     Protein         1..1067
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=117562
     Region          6..1067
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          734..762
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(735,738..739,742..743,745,775,778..779,782..783,
                     785..786,809,818..819,822..823,826)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          773..803
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          808..842
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 miipqdgrlr ldrerlkqhr krlglsqeal aeycfdrrlc vsiasikrae sgkavlyrta
       61 rhlaeiygve vealsaeaee aavvasdike mesarvliql havaadqsal ascvqhfggs
      121 laeggtalfg lprayrsdaq rgllcaatlv eqgvassvhl qaghwpsaep pviakdssgv
      181 wvergvavql aerfvfddeg gewlryrhpr geahearfdl vgrrvelgql qailestray
      241 qaghlvyirg vagigktrls aefaemaaah adhhqaevld fgtradegpl mqltrsllqt
      301 ageaqgemkg dakgemkgeg qgevlaeaql larlsalrlp tdhamllrpl lglaqpeeaq
      361 slyaamtpat rsqrlvqalr dvllarcihr pqllvvedlh wadeallatl tgllqetqda
      421 pviwlftsrl eqdpletrlr pqlpelpltl ielpplraqe aealvasfgt vpaehaarcv
      481 tqaqgnplfl tqlllfhphr slpaslanlv qtkldqltdl drramciaav mgqrfslasl
      541 qevlgqadyq pelpqryslv rpleegsyrf vhdlilqgiy egipkiqrdr lhlrlaelyg
      601 eaepglrarh lhrarsleap saflqavaae maryrheeal allkqcrsid yapkdeyrlm
      661 llqgqvamat gqiqaarehf eaarafaqee gqrisadlwl arvlnmldal eaeeaildgl
      721 lplaealedp lplaealylk gnlyfprgdf atsrayhtra leqarrggdv rteiqalsgl
      781 gdahyaegqm rstlelfdhc vtlcrthgha dleasnlfml gtariyanet eaaladcfda
      841 aelgkrvgnr raevvarlta gwilisqgdp qaadeqieqa lavarglgsg rfeafllesr
      901 arvelitgrl dearasiera wqlveqhalk afigpwvlgt ralleddlet rlatlqqgea
      961 ildagcvghn gyrflvtaae vslldqrpda arhyaqrltq lmgaepcawg ehhralieah
     1021 adwlenghvq ekesddestl ealracwhrg eaaglamtlp rlaasrr
//
LOCUS       WP_181872970             258 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Eggerthella lenta].
ACCESSION   WP_181872970
VERSION     WP_181872970.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella lenta
  ORGANISM  Eggerthella lenta
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Eggerthella.
REFERENCE   1  (residues 1 to 258)
  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 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   3  (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   4  (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 18824274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Eggerthella lenta"
                     /db_xref="taxon:84112"
     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]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29342
     Region          193..257
                     /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 mvelsdtrwr aiddlllaly gasdladlrr rvmrgfkdlv pydkgffdlc dcsesgrfvf
       61 fdpvsvdmtd eellsyyqky epsdyttwlf svndpvvyrd stfvtdemrk rselyrewmi
      121 pmdthfsmgs tqvgngmiyg sitlfrnras gdfteeeeec lavlnrhlst clagghprgl
      181 rrdegkpvvg rtsltareqe iaaliaegls nqqiglrlfi sentvkkhvk gifqkmgvsn
      241 rhqlmaelyr taaivvda
//
LOCUS       WP_181872972             191 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Eggerthella lenta].
ACCESSION   WP_181872972
VERSION     WP_181872972.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella lenta
  ORGANISM  Eggerthella lenta
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Eggerthella.
REFERENCE   1  (residues 1 to 191)
  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 191)
  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..191
                     /organism="Eggerthella lenta"
                     /db_xref="taxon:84112"
     Protein         1..191
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20856
     Region          35..>145
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mqdaiwrqiv nsrqqykial slneetdlhd nlnglvsivv pvynvenyie rcvqsimtqt
       61 ysmievilvd dgstdssadl cealadkddr ikvihkengg lssarnaalp lvegeyltfv
      121 dgddvirsqh veilaralhg dnrgissvsa isipnqdslp nlswskvdcl elsqkealsq
      181 mllgkglsvs a
//
LOCUS       WP_181873101             286 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Fontibacillus phaseoli].
ACCESSION   WP_181873101
VERSION     WP_181873101.1
KEYWORDS    RefSeq.
SOURCE      Fontibacillus phaseoli
  ORGANISM  Fontibacillus phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Fontibacillus.
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="Fontibacillus phaseoli"
                     /db_xref="taxon:1416533"
     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=30887
     Region          23..281
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 misteialll dkyrhkikav gmhhekiael rrmlnhgtad qsglrfaaeg mwsqqkllma
       61 glpisafyfc pecaysreaf hlaqsmihaa gevcliskkv lgklvdrdkp dgflsvaelp
      121 mipeheleli lpdnalvmvl dglespgnig tilrscdgag vdallicnpk vrlthpklik
      181 asmgaafvip mvcfaaaehc vdwlvsrgye iyladssaee cykaarrggn talvagsery
      241 glseawhggg dairkvsipm hgicdslnvg iaasiliyei sttpld
//
LOCUS       WP_181873115             416 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Fontibacillus phaseoli].
ACCESSION   WP_181873115
VERSION     WP_181873115.1
KEYWORDS    RefSeq.
SOURCE      Fontibacillus phaseoli
  ORGANISM  Fontibacillus phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Fontibacillus.
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="Fontibacillus phaseoli"
                     /db_xref="taxon:1416533"
     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=45592
     Region          10..409
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 meksdlslrr ltngltviam pqadvetvsv glltgagarl eepgelgssr ileywiwdgl
       61 saeladlgih kksapniewt rywatalapy faqmlrtllq avsapglqer sfaafrslaa
      121 hqaaarenep qactadllrq amggtqpiar saygrsdgyg tldpqivrnv yerlyqpanc
      181 vlaivgnyde aqldellydc qekwkdrfsv tgfpsalapl wtpgivarer eanqayltlg
      241 ipgvpydddd ffplavlvqi igggdgsrly eeirqrrglv yqirssltsf rdaglmtiql
      301 gsrkesalea leqiilelrr lerdgvtese vqsakgqlik qmvmrsestv armntlltsg
      361 wypkyprtld amrrsieevs aaavseaifr hpltgslgia sigplaasdl kagaih
//
LOCUS       WP_181873166             136 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Fontibacillus
            phaseoli].
ACCESSION   WP_181873166
VERSION     WP_181873166.1
KEYWORDS    RefSeq.
SOURCE      Fontibacillus phaseoli
  ORGANISM  Fontibacillus phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Fontibacillus.
REFERENCE   1  (residues 1 to 136)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..136
                     /organism="Fontibacillus phaseoli"
                     /db_xref="taxon:1416533"
     Protein         1..136
                     /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=15484
     Region          <14..113
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mnensavfhl hpeeacvrml tgevdlerlg tasdeeavqs llsikgigrw taemflifal
       61 grehvvslrd iglqraakwv ydmeeridwk ylqqvehlwa pygsiaslyl weainaghvd
      121 sgetleqrft klhetl
//
LOCUS       WP_181873222             373 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Fontibacillus phaseoli].
ACCESSION   WP_181873222
VERSION     WP_181873222.1
KEYWORDS    RefSeq.
SOURCE      Fontibacillus phaseoli
  ORGANISM  Fontibacillus phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Fontibacillus.
REFERENCE   1  (residues 1 to 373)
  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 373)
  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..373
                     /organism="Fontibacillus phaseoli"
                     /db_xref="taxon:1416533"
     Protein         1..373
                     /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=44051
     Region          218..326
                     /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 mdnlekeqys evsvtvevpv eliftdvdvr tanrehlipd ftemwfahhl sfsdisiarl
       61 ephrmlfryl mgvpaaspep yldwyvkiht lrgqspeldn nellmqrqme finmrdylqt
      121 gstffsdypi evsyrtpgrf nihdghhras flycsglrrl pvrmtkpdye rwlndhalle
      181 teatitgqhr klfytpilhp hfynvrcerd evyktrldyi leyigllnlr dknvldigcn
      241 igyysrhftr egakvtgiep dsyhfellkk lnllertpfe litepmersq lnkeyeigll
      301 ltvfyhlmrd pmkrepflav vnrsvrsmlf wesgdnieee ksmllngtsf ksylkladtf
      361 gtgkyrelgv flk
//
LOCUS       WP_181873285             450 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Fontibacillus phaseoli].
ACCESSION   WP_181873285
VERSION     WP_181873285.1
KEYWORDS    RefSeq.
SOURCE      Fontibacillus phaseoli
  ORGANISM  Fontibacillus phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Fontibacillus.
REFERENCE   1  (residues 1 to 450)
  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 450)
  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 450)
  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..450
                     /organism="Fontibacillus phaseoli"
                     /db_xref="taxon:1416533"
     Protein         1..450
                     /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=50701
     Region          163..>281
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mfnsalwkkq adiiakvlek apkfdkeyrl pseefadrqq kvweavkaag fdcgivysde
       61 hycgdvpylg gdnniivepi agvitesgfh fiaglesgiv aeqmyrrsga kmnrvdilki
      121 depnypaklv rpeqiieaac grkpkkigll ttryvfpvsl ynilrnyvge eniediseky
      181 yeikyeksdl emrlieegsk icdammegml rilrpgmyet qvaqwgyaia helgveemgf
      241 kvmvtagdsn ktmvgrasnn vikegdivhi gvspkrdglc aaerasvvcv kdpslvppny
      301 kvwfdflega fhegvtqfrk iaeqnlpgnt heqamidyyk skaeemsrkt givfkdfael
      361 kgyvtthnsg ytecqefyga lsldfnkpla nrmvmmmdag ikgygenwsd svikdidylv
      421 iektlgkygr evrilndlpv nlqhlvgeaf
//
LOCUS       WP_181873267             416 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Fontibacillus phaseoli].
ACCESSION   WP_181873267
VERSION     WP_181873267.1
KEYWORDS    RefSeq.
SOURCE      Fontibacillus phaseoli
  ORGANISM  Fontibacillus phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Fontibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..416
                     /organism="Fontibacillus phaseoli"
                     /db_xref="taxon:1416533"
     Protein         1..416
                     /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=47547
     Region          3..394
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mikdekigiv gagisgvtla yelakkgyrh vtimekgdrv ggkchsieyk gktyemgali
       61 glpsykstme lmeefdlkes gpllersffn regtrisqvp keqmadfake fkrlpalfgr
      121 yesikapgle dipsdlckpf aswcdenglf vlkqvfmhyf safgygside vpaayvmkll
      181 nfdnlmsfie ithmiswpkg vtelikrmgd rasdlrltce vnriaqeepg kvrvetnqge
      241 lyfdkviyta slhdlpdktn ldaedrklme kivferfrvy ayrvdnipkl sgyipgnmgp
      301 drrgrmmawy yrwadlaesd litvyvaqnd smsdsemres ieatlaslgg enirlymmks
      361 wnhfphvdta alqrgfytql eraqgkygiy fageimnfpt lenciiyaka lveryf
//
LOCUS       WP_181873771             361 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Tsukamurella tyrosinosolvens].
ACCESSION   WP_181873771
VERSION     WP_181873771.1
KEYWORDS    RefSeq.
SOURCE      Tsukamurella tyrosinosolvens
  ORGANISM  Tsukamurella tyrosinosolvens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Tsukamurellaceae; Tsukamurella.
REFERENCE   1  (residues 1 to 361)
  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 361)
  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..361
                     /organism="Tsukamurella tyrosinosolvens"
                     /db_xref="taxon:57704"
     Protein         1..361
                     /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=37333
     Region          3..334
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 mssravpvvv vagylgagks tllnhllsga gdarigvvvn dfgavnidam lvsgasgsga
       61 vrtvslsngc vcctvdddel edvlgalaar dldlvvveas glaepaamvr rvvlardpri
      121 dygglvyvad aahlagtmer hpslrhhlal adlvvlnkid lagdpgaara lvrehapsap
      181 vvgtvdavvp vellidaevl arraaqrrds prqltldeal rehdhdhahg hatgeahghl
      241 hdeyvavtve tgrldarata dlladpprgv frtkgfvtaa dgtrlevhav grhvrtaper
      301 ggrggaasvl vflgigldee avntrvqgcl aapdapadpq avlsllrysa aaqsdsaile
      361 d
//
LOCUS       WP_181873859             278 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Tsukamurella
            tyrosinosolvens].
ACCESSION   WP_181873859
VERSION     WP_181873859.1
KEYWORDS    RefSeq.
SOURCE      Tsukamurella tyrosinosolvens
  ORGANISM  Tsukamurella tyrosinosolvens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Tsukamurellaceae; Tsukamurella.
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="Tsukamurella tyrosinosolvens"
                     /db_xref="taxon:57704"
     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=29901
     Region          10..266
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 mnddgawgap aldlpryler vglsdppapd laglsalvra hattlpwenf davrgvpgel
       61 tvdalqrrmi dgrrgygctg hvpllaavlq rtgfrfgaas grvlvdgrps asthallvve
      121 vdgaphlaev gfgavplapl rlesgleqda ggwryrltae tvglgeewrl dfldpssgqw
      181 rpqyrfaltd rtwsdlrmtn fyvatsphsp frgrlmavvn rpgerhvltr davittrpdg
      241 vkesapyaat drrailaetf aidlpedeaa alaavsgs
//
LOCUS       WP_181873885             140 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein, partial [Tsukamurella
            tyrosinosolvens].
ACCESSION   WP_181873885
VERSION     WP_181873885.1
KEYWORDS    RefSeq.
SOURCE      Tsukamurella tyrosinosolvens
  ORGANISM  Tsukamurella tyrosinosolvens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Tsukamurellaceae; Tsukamurella.
REFERENCE   1  (residues 1 to 140)
  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 140)
  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..140
                     /organism="Tsukamurella tyrosinosolvens"
                     /db_xref="taxon:57704"
     Protein         1..>140
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          2..>120
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mlselierev aegplpgava afddpegvei aaggerapga pmtrdtvfri aslskpilaa
       61 aalvhvergt vglddpvtrw lpelaeprvl rdpsgplddt vpavrpitvr hllsftgglg
      121 mvsdfsaplm ealfgtlhqg
//
LOCUS       WP_181873969             273 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Tsukamurella tyrosinosolvens].
ACCESSION   WP_181873969
VERSION     WP_181873969.1
KEYWORDS    RefSeq.
SOURCE      Tsukamurella tyrosinosolvens
  ORGANISM  Tsukamurella tyrosinosolvens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Tsukamurellaceae; Tsukamurella.
REFERENCE   1  (residues 1 to 273)
  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 273)
  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 273)
  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 273)
  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..273
                     /organism="Tsukamurella tyrosinosolvens"
                     /db_xref="taxon:57704"
     Protein         1..273
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29629
     Region          12..232
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 msptapdeap vrrvaaffdl dktiiakssa lafsrpffde gllnrravlk ssyaqflmml
       61 taadhdqmer mrdhltqmce gwnveqvsti vrealhdvvn plvfaeasdl iaghharghd
      121 vvivsasgee mvrpiaemlg adysvaskmk vedgkyagev efycygenkv vamealaaeh
      181 gydleqcfay sdsitdvpml aavghptavn pdrglrkeaa ergwpvvsfs nptplrdrip
      241 tpsrnsvlas aglgvvaaga gvatylvlhr kkh
//
LOCUS       WP_181873127             275 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Fontibacillus phaseoli].
ACCESSION   WP_181873127
VERSION     WP_181873127.1
KEYWORDS    RefSeq.
SOURCE      Fontibacillus phaseoli
  ORGANISM  Fontibacillus phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Fontibacillus.
REFERENCE   1  (residues 1 to 275)
  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 275)
  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 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   4  (residues 1 to 275)
  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 10248791
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Fontibacillus phaseoli"
                     /db_xref="taxon:1416533"
     Protein         1..275
                     /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=32195
     Region          2..110
                     /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(3..5,19,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133389"
     Region          121..265
                     /region_name="BltR2"
                     /note="GyrI-like small molecule binding domain [Signal
                     transduction mechanisms]; COG4978"
                     /db_xref="CDD:444003"
ORIGIN      
        1 mlrisdfsil sqlstkmlrh yadidllppg fidestgyry yyvhqlavan kinmlktmgl
       61 slhlikkily eydediylmk flnrqaaqlq eeikekqdki llinsmikhl naqkdsskyt
      121 vtakkipkrr viylraqikq yqdetllwrr lsrivhgqni rlsyphfntt vfyeedvqnq
      181 ridievqksv sgdyenlqga nikiekeqtv asfiyegnyn elsevnetva hwildndyel
      241 ngsqfniyhi speeaneaan llteicfpik kktns
//
LOCUS       WP_181873900             588 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Tsukamurella tyrosinosolvens].
ACCESSION   WP_181873900
VERSION     WP_181873900.1
KEYWORDS    RefSeq.
SOURCE      Tsukamurella tyrosinosolvens
  ORGANISM  Tsukamurella tyrosinosolvens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Tsukamurellaceae; Tsukamurella.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 588)
  AUTHORS   ter Beek,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 588)
  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 588)
  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..588
                     /organism="Tsukamurella tyrosinosolvens"
                     /db_xref="taxon:57704"
     Protein         1..588
                     /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=62546
     Region          17..588
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 mtttplaggv lsargragrt rgagiaadvl vvlgaaaliw lvirvgqgmn apvdlshaqa
       61 gidtdpaqlp yyaarsllrm flalaaslvf tfvyatlaar srraravlmp lldvlqsvpi
      121 lgflsvtvtl fialfpgstl glecaaifai ftsqawnmtf afyqslisqp relgeaaenl
      181 glsrwqrfwr ldvpggmipl vwnammsfgg gwffltasea vsvagkeyal pgigayvasa
      241 sadgdlgrvg wavlamivvi vavnllfwsp ltawaerfrl edsatgrepk savltllrrs
      301 hvcavvgrtl aplvavcdrv fgplggragt atvvaparrr lgdllfaavv lallgyglyr
      361 cvevilrdag laevghvlll glatlsrvav vmlvatvvwv pigviiglnp alsralqpfi
      421 qifasfpanf lfpvvtavfv awniplnvgg ivlmalgtqw yilfnviaaa saipgdllea
      481 addmrlprlm twryvllpgv fagyvtggit aaggawnasi vaevvsydgr eyhayglgdy
      541 iarataatgv ehtahlllgi vvmclfvvgt naalwrrlyr laerrysl
//
LOCUS       WP_181871840             440 aa            linear   BCT 28-DEC-2024
DEFINITION  J domain-containing protein [Brevibacterium aurantiacum].
ACCESSION   WP_181871840
VERSION     WP_181871840.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium aurantiacum
  ORGANISM  Brevibacterium aurantiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 440)
  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 440)
  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 440)
  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 440)
  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 440)
  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 440)
  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 440)
  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 440)
  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..440
                     /organism="Brevibacterium aurantiacum"
                     /db_xref="taxon:273384"
     Protein         1..440
                     /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=47923
     Region          10..132
                     /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          270..373
                     /region_name="NERD"
                     /note="Nuclease-related domain; pfam08378"
                     /db_xref="CDD:462454"
ORIGIN      
        1 maqtagitly etlgveptas qdeirrayrk llrtahpdsg gtvgmfrsiq hayevlsdpt
       61 qrsqydagpp hppfsdpgpp aghstsdges snskessnqe psadseqsta sdssarhgrn
      121 dapspmddip appdpgfpep tfippehppe rntkaptwtk iwawvlggig vllaafqlvg
      181 mfatisfrns aggdsstvig dfmprivgtv iffliiallp yvifkfvrsr aprvplasdf
      241 iqsqylrnqe fgipgeglsi arfgkraqlg rtgeertarv lrevalsiap sarvihglrw
      301 pgkdhadidh ailvganlml vdskymqdgn ywfdnvdlyr dgvqmdpfkl gfavtavrnr
      361 fpnlnvsgvv lihsptgnla rppvelanvp arrlddpnyv avlamnaksf tqhlhrfvig
      421 sntntvdtkl ladvlnlkql
//
LOCUS       WP_181874113             486 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Eggerthella lenta].
ACCESSION   WP_181874113
VERSION     WP_181874113.1
KEYWORDS    RefSeq.
SOURCE      Eggerthella lenta
  ORGANISM  Eggerthella lenta
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Eggerthella.
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 10648172
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Eggerthella lenta"
                     /db_xref="taxon:84112"
     Protein         1..486
                     /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=52310
     Region          420..475
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mghriimyfg lalallvglf tlwgglslgg ltrlgipeil kywsipllia lgltffsvla
       61 krkpptkrcs saaavaagvf vlggyavlfi ettgvlrlat vsasailvgv gygllslvwq
      121 hrlsslafdd vvktllfalv iqsagylllc allqdctwvv fpflvalava fclialrhpe
      181 pnedrrthsk rrkgalksav aelsdpllcv caiafavalt raitldgier tdainliasg
      241 ciivvalaly giwfvlgddr apfkklsilg lyraffpiiv tallalsivg nslalsvatl
      301 vyvlftfvsv fimstsisva rahsvpatsv ygafagatyf vfaaatalga wvyyprnfga
      361 atlsvivlfv fyilamsyaa iqarkkrrge dattrnpvea katvvdgvse rcavlsqqhg
      421 ltarendtll llakgrdvps iakqlfisen tvrshsksiy kkldihskqe lldlletiel
      481 gyengr
//
LOCUS       WP_181874643             493 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Klebsiella pneumoniae].
ACCESSION   WP_181874643
VERSION     WP_181874643.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=53929
     Region          20..489
                     /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 mtamstlnpi lagsaqsvea yqqvieqtsq avvqwlkqpe myqgksvdel rerislefne
       61 qglgnqaaid raieyflkds lsvhhpqcva hlhcpslvis qaaevlinat nqsmdswdqs
      121 psatiiemkl iewlrarvgf pagdagvfts ggtqsnlmgl mlardaffar lghsiqqdgl
      181 pgdirkykvl csenahfsvq knmalmglgy rsvtlvktde farmdvsdlq akiaqaqang
      241 eqimaivata gttdagaidp lrdiagiaae hqiwlhvdaa wggalllseq yrdyldglel
      301 vdsvtldfhk qffqtiscga fllkdarhye lmryqaayln sefdeehgvp nlvskslqtt
      361 rrfdalklwm glealgqkqy taiidhgvtm aknvaeyvks qptlelvmqp qlasvlfrsr
      421 paqmagsdaa aiallnqrvg dallasgran vgvtehngvt clkltllnpv vtlddvkvll
      481 nlvertaqel laq
//
LOCUS       WP_181874702             181 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein, partial
            [Marinitenerispora sediminis].
ACCESSION   WP_181874702
VERSION     WP_181874702.1
KEYWORDS    RefSeq.
SOURCE      Marinitenerispora sediminis
  ORGANISM  Marinitenerispora sediminis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Marinitenerispora.
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   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 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 18527459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Marinitenerispora sediminis"
                     /db_xref="taxon:1931232"
     Protein         1..>181
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          11..74
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          96..>180
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 msvgsgahtg rgdlsrrvah rraelglsrq evaeragmat gyvayleehq pqltrwaltr
       61 laaalrttpg allgvgadlp pgsgregvpa pvlywlgaee cmelvapggi griafctega
      121 sgpavlpvty tvvdgnivfr tapegtiaeh segyvsfevd qldgvmsegw svlirgrarp
      181 a
//
LOCUS       WP_181874942             420 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Legionella feeleii].
ACCESSION   WP_181874942
VERSION     WP_181874942.1
KEYWORDS    RefSeq.
SOURCE      Legionella feeleii
  ORGANISM  Legionella feeleii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 420)
  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..420
                     /organism="Legionella feeleii"
                     /db_xref="taxon:453"
     Protein         1..420
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47353
     Region          33..404
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mkltiprgii yhslsqdlws fvsalfvrld nkplinkfeq qfasyigckh gvafpyaria
       61 lyftlklkqf prgseiimpp itikaildvv lelglkpvfv didpdtlgfd lnnlkksitt
      121 ntkailityl ygmvpdmgsm lticndynlf iiedfsqcln geyknkkvgs lghvgiysas
      181 siktldtygg gllvtndtal ydqlrdcqst lekpsrkfli qkiftnivrn fatkriifht
      241 lvfpllkaih llkpdiyikn tgernknplk nlpsawftsy tsfqahigqk lllnvekedr
      301 qrilnaevir tnksvhfpqg ahntknvywq tiayfsepla alkllqnngi dsattsleki
      361 stlsnypiqg ntpnadtiys calfiptypg lktkdlthim ntlnlislns rvgealqwtr
//
LOCUS       WP_181874958             128 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Legionella feeleii].
ACCESSION   WP_181874958
VERSION     WP_181874958.1
KEYWORDS    RefSeq.
SOURCE      Legionella feeleii
  ORGANISM  Legionella feeleii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 128)
  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 128)
  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 128)
  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 128)
  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 128)
  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 128)
  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..128
                     /organism="Legionella feeleii"
                     /db_xref="taxon:453"
     Protein         1..128
                     /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=14108
     Region          <34..109
                     /region_name="CytC5"
                     /note="Cytochrome c5 [Energy production and conversion];
                     COG3245"
                     /db_xref="CDD:442476"
ORIGIN      
        1 mivlcgwftt tfscaeshhp qaflnsikgs knegeqiveh fcsnchavkp liplgapgmk
       61 qkadwearik gglkqlveht engfnamppr ggcfectdkq ltlailamlp delakeilid
      121 rkvykknk
//
LOCUS       WP_181875224             328 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Staphylococcus aureus].
ACCESSION   WP_181875224
VERSION     WP_181875224.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..328
                     /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=37670
     Region          8..314
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mkenfwselp rpffilapme dvtdivfrhv vseaarpdvf fteftntesf chpegihsvr
       61 grltfsedeq pmvahiwgdk peqfretsiq lakmgfkgid lnmgcpvanv akkgkgsgli
      121 lrpdvaaeii qatkagglpv svktrlgyye idewkdwlkh vfeqdianls ihlrtrkems
      181 kvdahwelie aiknlrdeia pntlltingd ipdrktglef aekygidgvm igrgifhnpf
      241 afekepreht skelldllrl hlslfnkyek deirqfkslr rffkiyvrgi rgaselrhql
      301 mntqsiaear alldefeaqm dedvklel
//
LOCUS       WP_181875255             148 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Escherichia coli].
ACCESSION   WP_181875255
VERSION     WP_181875255.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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   Wintjens,R. and Rooman,M.
  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 148)
  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..148
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..148
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16406
     Region          15..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(19,23,47)
                     /site_type="other"
                     /note="non-specific DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238045"
     Site            order(22,46)
                     /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"
ORIGIN      
        1 mgnnehevma dkqraerikk aildhstyee laektgisvs tlvriasgkt epkfsdiiqi
       61 akitgadlnt laygyaldvk eeaterklit sadgytdeet tnahnfivwn irtlekqdil
      121 alarqvsals sytystkmfm kkalsgee
//
LOCUS       WP_181875489             364 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Escherichia
            coli].
ACCESSION   WP_181875489
VERSION     WP_181875489.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 10169520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..364
                     /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=39231
     Region          15..362
                     /region_name="THR_DH_like"
                     /note="L-threonine dehydrogenase (TDH)-like; cd08239"
                     /db_xref="CDD:176201"
     Site            order(51..53,56,169,173,193..198,217..218,222,238,
                     261..262,264,284..285,308..310)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176201"
     Site            order(51,53,81,169)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176201"
ORIGIN      
        1 mkinrivneg fmktmlaayl pgnstvdlre vavptpginq vlikmkssgi cgsdvhyiyh
       61 qhrataaapd kplyqgfing hepcgqivam gqgcrhfkeg drvlvyhisg cgfcpncrrg
      121 fpisctgkgk aaygwqrdgg haeyllaeek dlillpdals yedgafiscg vgtayegilr
      181 gevsgsdnvl vvglgpvgmm ammlakgrga kriigvdmlp erlamakqlg vidhgylatt
      241 eglpqiiael thggadvald csgnaagrll alrstadwgr vvyigetgkv efevsadlmh
      301 hqrriigswv tslfhmekca hdltdwklwp rnaithrfsl eqagdayalm asgkcgkvvi
      361 nfpd
//
LOCUS       WP_181875717             927 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_181875717
VERSION     WP_181875717.1
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=104096
     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 ankklaayvf pgrnlsltvd adpqaeissk etlaenltsl tlsngarvil aksageeqkl
      541 qiiavsnkgd lsfpaqqksl ialankavsg sgvgelssss lkrwsaensv tmsskvsgmn
      601 tllsisartn 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_181875721            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181875721
VERSION     WP_181875721.1
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=166341
     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 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 tfrhflrfsq kgqfvlppar yvrsyapaqq svaagsewtg
     1501 mqvk
//
LOCUS       WP_181875744             328 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Staphylococcus aureus].
ACCESSION   WP_181875744
VERSION     WP_181875744.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..328
                     /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=37682
     Region          8..314
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mkenfwselp rpffilapme dvtdivfrhv vseaarpdvf fteftntesf chpegihsvr
       61 grltfsedeq pmvahiwgdk peqfretsiq lakmgfkgid lnmgcpvanv akkgkgsgli
      121 lrpdvaaeii qatkagglpv svktrlgyye idewkdwlkh vfeqdianls ihlrtrkems
      181 kvdahwelie aiknlrdeia pntlltingd ipdrktglel aekygidgvm igrgifhnpf
      241 tfekepreht ckelldllrl hlslfnkyek deirqfkslr rffkiyvrgi rgaselrhql
      301 mntqsiaear alldefeaqm dedvklel
//
LOCUS       WP_181875897             262 aa            linear   BCT 28-DEC-2024
DEFINITION  trypsin-like serine peptidase [Staphylococcus aureus].
ACCESSION   WP_181875897
VERSION     WP_181875897.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 262)
  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 262)
  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..262
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..262
                     /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=28602
     Region          65..260
                     /region_name="eMpr"
                     /note="V8-like Glu-specific endopeptidase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3591"
                     /db_xref="CDD:442810"
ORIGIN      
        1 mskntiiksl valtvmttla tttngitdlk qshlvaqaee tnvvppkrev vknslhspyn
       61 ivtkiqgpgf sasgfvsgkt tvmtnkhvld silkegtlkt dvilakndan egdkkdlgtf
      121 kikdytlapd nmdvvvlemn pnekgqhigd vvqpakikna deinqtwidn nkdkkfftag
      181 ypgdkdlnkm whseghllff vgrtdpydfh akmpgapgvs gspvfndkne vvgifyggwe
      241 agngidglmf reklydfvva ns
//
LOCUS       WP_181875931             229 aa            linear   BCT 28-DEC-2024
DEFINITION  CDP-alcohol phosphatidyltransferase family protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_181875931
VERSION     WP_181875931.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..229
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..229
                     /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=25897
     Region          4..222
                     /region_name="PssA"
                     /note="Phosphatidylserine synthase [Lipid transport and
                     metabolism]; COG1183"
                     /db_xref="CDD:440796"
ORIGIN      
        1 mkkyipntlt clnlfsgcag vlfalkgefq ytfycvlfsg icdffdgmaa ralhvkstig
       61 keldsladmi sfgflpgavi yfllkeinte mswlpylafv mtvfsglrla kfnvderqst
      121 dfiglntpmn tfyiislpfi aqiypeiimn nvfllvtvvl ssallvselr lfsmklssls
      181 wkanqfkylf lilsivllgl lkflaipfil layivfsiih frtlrqdkd
//
LOCUS       WP_181876306             447 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Staphylococcus
            epidermidis].
ACCESSION   WP_181876306
VERSION     WP_181876306.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus epidermidis
  ORGANISM  Staphylococcus epidermidis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 447)
  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 447)
  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 447)
  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 447)
  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..447
                     /organism="Staphylococcus epidermidis"
                     /db_xref="taxon:1282"
     Protein         1..447
                     /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=49656
     Region          1..438
                     /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 mkqydvvflg sghaawhaal tlkqsgkqva ivekdtiagt ctnygcnaki llegpyevle
       61 eakqypniid shnlevnwkn lmhykeqvin pmsetltsmf eqqgidvimg kgklvdahti
      121 evnnttlqsd yiviatgqhs hqldiegkey thdsreflsm qslpdsitfi gagiisiefa
      181 simiksgvev nvihhtnqal egfneshvnk liqklkdkgv kfyfsentks vkpnaqrfiv
      241 etesgkmiet dyvldatgrk pnvqqiglek vgiqfsdrgi evddylrtnv kniyasgdvi
      301 nkmipkltpt atfesnyiaa hilglntdai qyppipsvly slprlsqigv tvseakkddt
      361 ymikdipfgr qmvfeyqnet eaemsivlds hkrlvgaeiy gndagdlvnl lvfiinqklt
      421 aqdlnkiifa fpgassgvid llklamm
//
LOCUS       WP_181876445             196 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Yersinia
            pseudotuberculosis].
ACCESSION   WP_181876445
VERSION     WP_181876445.1
KEYWORDS    RefSeq.
SOURCE      Yersinia pseudotuberculosis
  ORGANISM  Yersinia pseudotuberculosis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
REFERENCE   1  (residues 1 to 196)
  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 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   3  (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   4  (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 11970391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Yersinia pseudotuberculosis"
                     /db_xref="taxon:633"
     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]"
                     /calculated_mol_wt=22452
     Region          <39..191
                     /region_name="PRK15201"
                     /note="fimbriae biosynthesis transcriptional regulator
                     FimW"
                     /db_xref="CDD:185123"
     Region          139..193
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mivdndkyqt lgmvsivkki ftslgfkkei kfyrkafysa dvifigvdef sffealkrld
       61 ktpaeadvfl icdarlnsfl qgiprfsdvt mifredslet vsnkiatvfk rkfrgfkdnl
      121 ierktakllh lvsserqylt pnenivlklf negfsggdia rilkksektv sgqkrsamkk
      181 lgartdveli kmfmfk
//
LOCUS       WP_181876475             279 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Yersinia pseudotuberculosis].
ACCESSION   WP_181876475
VERSION     WP_181876475.1
KEYWORDS    RefSeq.
SOURCE      Yersinia pseudotuberculosis
  ORGANISM  Yersinia pseudotuberculosis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
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="Yersinia pseudotuberculosis"
                     /db_xref="taxon:633"
     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=31478
     Region          1..278
                     /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 mdmqfffvgy lilgaivgsf lnvliyrlpi mlanlssrce sqgekikiys hlrninlfqp
       61 ssfchhcnes ipikynipil gwiflrgasr ccnkkistry lfievlaviq tllvlmifke
      121 dllictslvl iwsltalafi dfdtyllpdc mtipllwlgl linidtvftp lpsavmgavs
      181 gylflwlsyw lfkivrgvdg mgygdfklma algawfgmsa vpflilfssf fglvayavfy
      241 fldrkengkk inyiafgpyi slagvlylfl gshvtnlfs
//
LOCUS       WP_181876890             493 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Klebsiella pneumoniae].
ACCESSION   WP_181876890
VERSION     WP_181876890.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=53905
     Region          20..489
                     /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 mtamstlnpi lagsaqsvea yqqvieqtsq avvqwlkqpe myqgksvdel rerislefne
       61 qglgnqaaid raieyflkds lsvhhpqcva hlhcpslvis qaaevlinat nqsmdswdqs
      121 psatiiemkl iewlrarvgf pagdagvfts ggtqsnlmgl mlardaffar qghsiqqdgl
      181 pgdlrkykvl csenahfsvq knmalmglgy rsvtlvktde farmdvsdlq akiaqaqang
      241 eqimaivata gttdagaidp lrdiagiaae hqiwlhvdaa wggalllseq yrdyldglel
      301 vdsvtldfhk qffqtiscga fllkdarhye lmryqaayln sefdeengvp nlvskslqtt
      361 rrfdalklwm glealgqkqy aaiidhgvtm aknvaeyvks qptlelvmqp qlasvlfrsr
      421 paqmagsdaa aiallnqrvg dallasgran vgvtehngit clkltllnpv vtlddvkvll
      481 nlvertaqel laq
//
LOCUS       WP_181876762             789 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Staphylococcus aureus].
ACCESSION   WP_181876762
VERSION     WP_181876762.1
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 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..789
                     /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=88100
     Region          <51..180
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <324..788
                     /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 maqakkksta kkkttskkrt nsrkkkndnp iryviailvv vlmvlgvfql giigrlidsf
       61 fnylfgysry ltyilvllet gfityskrip ktrrtagsiv lqiallfvsq lvfhfnsgik
      121 aerepvlsyv yqsyqhshfp nfgggvlgfy llelsvplis lfgvciitil llcssvillt
      181 nhqhrevakv alenikawfg sfnekmsern qekqlkreek arlkeeqkar qneqpqikdv
      241 sdftevpqer dipiyghten esksqsqpsr kkrvfdaens snnivnhhqa dqqeqlteqt
      301 hnsvesenti eeagevtnvs yvvppltlln qpakqkatsk aevqrkgqvl entlkdfgvn
      361 akvtqikigp avtqyeiqpa qgvkvskivn lhndialala akdvrieapi pgrsavgiev
      421 pnekislvsl kevldekfps nnklevglgr disgdpitvp lnemphllva gstgsgksvc
      481 ingiitsill nakphevklm lidpkmveln vyngiphlli pvvtnphkaa qalekivaem
      541 errydlfqhs strnikgyne lirkqnqeld ekqpelpyiv vivdeladlm mvagkevena
      601 iqritqmara agihlivatq rpsvdvitgi iknnipsria favssqtdsr tiigtggaek
      661 llgkgdmlyv gngdssqtri qgaflsdqev qdvvnyvveq qqanyvkeme pdapvdksem
      721 ksedalydea ylfvveqqka stsllqrqfr igynrasrlm ddlernqvig pqkgskprqv
      781 lidlnndev
//
LOCUS       WP_181876901             459 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Klebsiella pneumoniae].
ACCESSION   WP_181876901
VERSION     WP_181876901.1
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 10003700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..459
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49947
     Region          3..452
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mserrsidyi peserhghpf sqftlwfggn lqitaivtga lavvlggdvv wslvgllvgq
       61 mlgaavmslh alqgprlglp qmilsraqfg vfgavvplvl vcvmyigfsa sgtvlagqam
      121 akllnishva gmlifsaiii viavlgykvi hklgklasiv gilafvymfi tlllsadlsa
      181 lahnnhfslp tfllavslss swqiafcpyv sdysrylprd isatktwcsv ffgtvlgtqt
      241 smtlgvltaa iagsafpghe vsylvglgks qamamviyfa icfgkitftt lnaygsfmsl
      301 ttivsafrrq tvlsqkcria fvvlmvtasc iiallsepaf lkhfthfllf llaffvpwsa
      361 icltdyylis kgaidipals dpqqrygfwn lyaitlyivg vliqlpfien plfhgsltwi
      421 fagndvswii gwfgtgvlyy alrrfdrrsl paqslfpst
//
LOCUS       WP_181877033             467 aa            linear   BCT 28-DEC-2024
DEFINITION  rhamnulokinase [Streptococcus pneumoniae].
ACCESSION   WP_181877033
VERSION     WP_181877033.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pneumoniae
  ORGANISM  Streptococcus pneumoniae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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 10167330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Streptococcus pneumoniae"
                     /db_xref="taxon:1313"
     Protein         1..467
                     /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=52725
     Region          3..454
                     /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 meavlaidlg atsgraivgy lsenklvmee inrfsnlpir vkghlswdvd fllakilesi
       61 rlantsykil sigidtwgvd fglidnegkl lsqpvhyrde rtkgvlkeis emteleklys
      121 etgnqimein tlfqlfkarq espdsfyktn killmpdlfn ylltgkfate ksiasttqlf
      181 dprsqnwnqn ilklfeldss llpeivsegn vlgrikeeyg lgdipvvnvc shdtasaivs
      241 vpktegslfi ssgtwslvgv eltspiltte sfsygftnev gkdgeitflk nctglwiiee
      301 lrrsferrgk aysfddirtm vekekenlpl idtestefat esdmhktlte ylayhhetre
      361 wtdgqlfkiv yeslaetyrk aielleelth kvykriyvig ggarasyfnq miadrtgkev
      421 ltgsteatav gnivvqliam gqlkgmeeah hvieeflqle syysqkn
//
LOCUS       WP_181876395             364 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase family protein [Escherichia
            coli].
ACCESSION   WP_181876395
VERSION     WP_181876395.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 364)
  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 10169520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..364
                     /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=39204
     Region          15..362
                     /region_name="THR_DH_like"
                     /note="L-threonine dehydrogenase (TDH)-like; cd08239"
                     /db_xref="CDD:176201"
     Site            order(51..53,56,169,173,193..198,217..218,222,238,
                     261..262,264,284..285,308..310)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176201"
     Site            order(51,53,81,169)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176201"
ORIGIN      
        1 mkinrivneg fmktvlaayl pgnstvdlre vavptpginq vlikmkssgi cgsdvhyiyh
       61 qhrataaapd kplyqgfing hepcgqivam gqgcrhfkeg drvlvyhisg cgfcpncrrg
      121 fpisctgegk aaygwqrdgg haeyllaeek dlillpdals yedgafiscg vgtayegilr
      181 gevsgsdnvl vvglgpvgmm ammlakgrga kriigvdmlp erlamakqlg vmdhgylatt
      241 eglpqiiael thggadvald csgnaagrll alqstadwgr vvyigetgkv efevsadlmh
      301 hqrriigswv tslfhmekca hdltdwklwp rnaithrftl eqagdayalm asgkcgkvvi
      361 nfpd
//
LOCUS       WP_181877449            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181877449
VERSION     WP_181877449.1
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=166351
     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 slpssnyvpp aggtffllad ssfssseeak vrleapgrdy rryqmeeygg
       61 vdvrlyripd pmaflrqqkn lhrivvqpqy lgdglnntlt wlwdnwygks rrvmqrtfss
      121 qsrqnvtqal pelqlgnaii kpsryvqnsq fsplkkyplv eqfryplwqa tsvepqqglk
      181 legassnfis pqpgniyipl gkqepglylv eamvggyrat tvvfvsdtva lskvsgnell
      241 vwtagkkqge akpgseilwt dglgvmtrgv tddsgtlqlq hispersyil gkdaeggvfv
      301 senffyesei yntrlyiftd rplyragdrv dvkvmgrefh dplhsspivs apaklsvlda
      361 ngsllqtvnv tldarnggqg sfrlpenava ggyelrlayr kqvysssfrv anyikphfei
      421 glaldkkefk tgeavsgklq llypdgepvk darvqlslra qqlsmvgndl ryagrfpvsl
      481 egsetvsddn ghvalnlpaa dkpsrylltv sasdgaayrv tttkeilier glahyslsta
      541 aqysnsgelv vfryaaless kqvpvtyewl rledrtshsg elpsggksft vnfdkpgnyn
      601 ltlrdkdgli laglshavsg kgstshtgtv 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 sekslymkws
      901 mptvyrmgdk paaglfifsq qdnepvalvt kfagaemrqt ltlhkganyi slmqniqqsg
      961 llsaelqqng qvqdsistkl sfvdnswpve qqknvmlggg dnalmlpeqa snirlqsset
     1021 pqeifrnnld alvdepwggv intgsrlipl slawrsladh qsaaandirq riqdnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqalgvt qqpeywqhml dsyaeqadnm
     1141 pllhralvla waqemnlpck tllkgldeai arrgtktedf seadtsdind slildtpesp
     1201 ladavanvlt mtllkkaqlk stvmpqvqqy awdkaansnq plahtvvvln sggdatqaaa
     1261 ilsgltaeqs tieralamnw lakymatmpp vvlpapagaw akhkltggge ywrwvgqgvp
     1321 dilsfgdels pqnvqvrwre paktaqqsni pvtverqlyr lipgeedmnf tlqpvnsnei
     1381 dsdalyldei tltseqdaal rygqvevplp pgadverttw gisvnkpnaa kqqgqlleka
     1441 rnemgelaym vpvkeltgtv tfrhllrfsq kgqfvlppar yvrsyapaqq svaagsewtg
     1501 mqvk
//
LOCUS       WP_181877566             789 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Staphylococcus aureus].
ACCESSION   WP_181877566
VERSION     WP_181877566.1
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 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..789
                     /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=88005
     Region          <51..180
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <324..788
                     /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 maqakkksta kkkttskkrt nsrkkkndnp iryviailvv vlmvlgvfql giigrlidsf
       61 fnylfgysry ltyilvllat gfityskrip ktrrtagsiv lqiallfvsq lvfhfnsgik
      121 aerepvlsyv yqsyqhshfp nfgggvlgfy llelsvplis lfgvciitil llcssvillt
      181 nhqhrdvakv alenikawfg sfnekmsern qekqlkreek arlkeeqkar qneqpqikdv
      241 sdftevpqer dipiyghten esksqsqpsr kkrvfdaens snnivnhhqa dqqeqlteqt
      301 nnsvesenti eeagevtnvs yvvppltlln qpakqkatsk aevqrkgqvl entlkdfgvn
      361 akvtqikigp avtqyeiqpa qgvkvskivn lhndialala akdvrieapi pgrsavgiev
      421 pnekislvsl kevldekfps nnklevglgr disgdpitvp lnemphllva gstgsgksvc
      481 ingiitsill nakphevklm lidpkmveln vyngiphlli pvvtnphkaa qalekivaem
      541 errydlfqhs strnikgyne lirkqnqeld ekqpelpyiv vivdeladlm mvagkevena
      601 iqritqmara agihlivatq rpsvdvitgi iknnipsria favssqtdsr tiigtggaek
      661 llgkgdmlyv gngdssqtri qgaflsdqev qdvvnyvveq qqanyvkeme pdapvdksem
      721 ksedalydea ylfvveqqka stsllqrqfr igynrasrlm ddlernqvig pqkgskprqv
      781 lidlnndev
//
LOCUS       WP_181877611             302 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Streptococcus milleri].
ACCESSION   WP_181877611
VERSION     WP_181877611.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus milleri
  ORGANISM  Streptococcus milleri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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="Streptococcus milleri"
                     /db_xref="taxon:33040"
     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=35592
     Region          6..297
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mlfsfrliel hdrlskggll nkakilvefg idsktfqrdi dklrlyysek glgdikydrk
       61 nncyrlesrp hqlskkeifa lckiliesra fnkqefidii dkllklyqke eakevyrain
      121 nekvnyiepq hgkdliseiw elrqtiteqq vtqidykrad nkvkqhkvkp vgiifsefyf
      181 yllafqmdek ikyptifrid riqkiditnt rfsvpysqrf seaefkkriq fmysgelktv
      241 rfeftgvlea lldklptaqi ekeieggviv kaevfgngid mwlrsqgsrv kilgeesstv
      301 wk
//
LOCUS       WP_181877634             380 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Streptococcus dysgalactiae].
ACCESSION   WP_181877634
VERSION     WP_181877634.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus dysgalactiae
  ORGANISM  Streptococcus dysgalactiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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="Streptococcus dysgalactiae"
                     /db_xref="taxon:1334"
     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=44785
     Region          64..375
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mwieeqsngk lryverykeh ytgkykraye lierdtlqgr kkaatalrlk ieklvhirpk
       61 kekvtfgevy qnfysswslg vkqstiystk nidriilkki pndyliskid rrflqkifdd
      121 llsegrshny vkkvkwklnr ifkyalrmdy idvnemihve lpkeiltteq akkkkdkfld
      181 qkefklfaqn lreevyrdyr vkkylriaiv lyltgmryge laglniskdi dfkkktihiq
      241 htfnfrtkqr ttpktkgsdr iievsdtvlk niqeqlaeni ragfetdylf intlgypttp
      301 ervigafkrh gqkagiekni tthifrhshi sllaeigipl paimervghs dskttlevys
      361 hvtlqmttnl akklnevklf
//
LOCUS       WP_181877715             927 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_181877715
VERSION     WP_181877715.1
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=104109
     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 ewgnaatfdk levdaergvi teewrahqda kwrtsqarrp
      181 fllantrnle repiglmdtv atvtpaqlrq fyqrwyqpnn mtfivvgdid skealalikd
      241 nlsklpanka aenrvwptka enhlrfniin dkenrvngia lyyrlpmvqv sdeqsfieqa
      301 ewsmlvqlfn qrlqeriqsg elktisggta rsvkiapdyq slffrvnard dnmqdaanal
      361 maelatidqh gfsaeelddv kstrltwlkn avdqqaerdl rmltsrlass slnntpflsp
      421 eetyqlskrl wqqitvqrla ekwqqlrknq dafweqmvnn evaakkalsp aailalekey
      481 ankklaayif pgrnlsltvd adpqaeissk etlaenltsl tlsngarvil aksageeqkl
      541 qitavsnkgd lsfpaqqksl ialankavsg sgvgelssss lkrwsaensv tmsskvsgmn
      601 tllsvstrtn npepgfqlin qrithstind niwaslqnaq iqalktldqr paekfaqqmy
      661 etryaddrtk llqenqiaqf taadalaadr klfsspadit fvivgnvaed klvalitryl
      721 gsikhsdspl aagkpltrat dnasvtvkeq nepvaqvsqw krydsrtpvn latrmaldaf
      781 nvalakdlri nireqasgay svssrlsvdp qakdishsla ftcqperhde lltlanevmv
      841 krlakgiseq elneyqqnvq rsldiqqrsv qqlantivns liqyddpaaw teqeqllkqm
      901 tvenvnttvk qylshpvnty tgvllpk
//
LOCUS       WP_181877659             548 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator [Streptococcus
            dysgalactiae].
ACCESSION   WP_181877659
VERSION     WP_181877659.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus dysgalactiae
  ORGANISM  Streptococcus dysgalactiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 548)
  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 548)
  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..548
                     /organism="Streptococcus dysgalactiae"
                     /db_xref="taxon:1334"
     Protein         1..548
                     /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=63624
     Region          11..>505
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mmildkksyd llsyllklea petvmaisha lnqsrrkvyy qldkinealp reveqiisyp
       61 rvgilltdeq kaacrlllee vtdynyvmks derrrlssvy iavstervti dklmqindvs
      121 rntilndlte lreeledkqy kiqlhatkar gyyfdchpma liqylykllv dvyqggnssf
      181 idmfnrklse tqglsvyfsk dilayfheyl llsqaslgkt intqdsqfml qilpfmflsy
      241 rnmqlnsdik salkkdfnli wkrkeyqiaq elagelyqnf klhlddievg mvamlmlsfr
      301 kdqdhhvesq dydemratis hfidqlenry qlhfthkqdl lkqltthcka lvyrkaygif
      361 svnpltdhik ekyeelfama qscstilekd wdisltdddv ayltihlgge lrnntadqdk
      421 tklvivsddg igiqklllkq cqrylangqi eavftteqyq svydllsvdm ivattdalet
      481 kvpmlivnpi lsdddiikli rfskqgrlte hsrfstelak aieavvkges dryaltskie
      541 klihrell
//
LOCUS       WP_181878017             195 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Janthinobacterium lividum].
ACCESSION   WP_181878017
VERSION     WP_181878017.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium lividum
  ORGANISM  Janthinobacterium lividum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..195
                     /organism="Janthinobacterium lividum"
                     /db_xref="taxon:29581"
     Protein         1..195
                     /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=22233
     Region          3..>181
                     /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 mydwlfapga agvdlffiis gfimvyttrd ndgsfqyfys ymvkrisriv pvymvltliy
       61 wtamliasdv vgsefgyglk dviksllfyp lnvvsgeppn lgaavlypgw tlnyemyfyl
      121 vfgasllfrk mrwlaltgwi vftlivlpll kggvpvldan lsygwgsyln lltspmiwef
      181 lrvysldlfi fqdlk
//
LOCUS       WP_181878515             604 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Enterococcus faecalis].
ACCESSION   WP_181878515
VERSION     WP_181878515.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecalis
  ORGANISM  Enterococcus faecalis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 604)
  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 604)
  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 604)
  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 604)
  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 604)
  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..604
                     /organism="Enterococcus faecalis"
                     /db_xref="taxon:1351"
     Protein         1..604
                     /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=69419
     Region          19..337
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mkaftrkggn vdrfeikeef llngqpfkil sgaihyfrvd psdwyhslyn lkalgfntve
       61 tyvpwnlhep qkgtfhfegi ldlerflkla qelglyaivr pspyicaewe fggfpawlln
      121 epgrmrsnnp tylkhvaeyy dvlmekivph qlanggnilm iqieneygsf geekaylrai
      181 rdlmiargvt apfftsdgpw ratlragsmi eddilvtgnf gskakenfgm mqaffeehgk
      241 kwplmcmefw dgwfnrwkep iikrdpqela esvrealalg sinlymfhgg tnfgfmngcs
      301 argtidlpqi tsydydapld eqgnptekyf alqkmlheey palpqaeplv kesfaqtaip
      361 ltnkvslfat letisqpvvs vypqtmeqlg qntgyllyrt siekdaaeek lrvidgrdrl
      421 qlfvnqvhqa tqyqtkiged iyvtlpqenn qidilmenmg rvnyghklfa dtqkkgirtg
      481 vmadlhfmtq wqqyclpmts ceqvdysrew qpdqpsfyqy hvelaevkdt fidvskfgkg
      541 ivfvnqtnlg rfwnvgptls lyipkgllke gqneivifet egtyqpeiql vkeplykemk
      601 eglq
//
LOCUS       WP_181878662             847 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Corynebacterium renale].
ACCESSION   WP_181878662
VERSION     WP_181878662.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium renale
  ORGANISM  Corynebacterium renale
            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 renale"
                     /db_xref="taxon:1724"
     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=95034
     Region          19..840
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mfltemlpdl aevpeslvde sifegfrvwn sqrglsfypa qeeailglla gdnvilatpt
       61 gsgkslvaaa ahfiamargq rsfytapika lvsekffalc eifgaenvgm mtgdatvngq
      121 apiicataei vanialrdgk qaridqvvmd efhyysdper gwawqvplle lpqaqfllms
      181 atlgdttfle kdltrrtgrd tnlvagaerp vplsfeyvyt pvhetvekll ergeapiyvv
      241 hftqreater aqaltslqll saeekekiae eigtfrfttt fgkqlsrlvr kgigvhhagm
      301 lpkyrrlver lsqtgllkvi cgtdtlgvgi nvpirtvlmt glakydgtrq riiksrefhq
      361 iagragragy dthgtvevqa peheienarl reragqdpkk lkkqrlkhar egevtwskkt
      421 fdrlitsepe pmssqfrvsn smvinllgrt gdtydhfkhl lrtnhdtrsk qnsdilttve
      481 lvrglvnaei vekvdpthpd ptgrtyalak emqrdfalnq plapfalaal elldpesdtf
      541 dldvisvfes ildnprviln aqqkqargee iaalkadgvd ytermalved vtwpqplaee
      601 leaayetlta gapwarefdi tpksivrdmi ehamtfsdfv atyqlarseg vvlryltdcw
      661 rtlkhtvpda yiseeldeii ewlgemirqv dsslvdewam ladpdtplsq dvveherafg
      721 vtdpdaltan kraftrmvrn lmfrvvelfa lereeqleem fdylddapdf gdamdayfde
      781 yddvdfspaa rgpeyfrlnd dgrawevrqv lkdpddeggf aftamvdlda sdahgevrls
      841 slrfdas
//
LOCUS       WP_181878789             716 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Enterococcus durans].
ACCESSION   WP_181878789
VERSION     WP_181878789.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus durans
  ORGANISM  Enterococcus durans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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="Enterococcus durans"
                     /db_xref="taxon:53345"
     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=83067
     Region          53..713
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mekqrmleeh hlsfvhqklv trkntlrsfl dksygshlkd lqtmgtdirl nfdnlsdsle
       61 tyaaiesknr eidqmnlslh taekelatie rllkspyfgk ivvdfldges aesfyiging
      121 fadeeshnli ydwrspiael fynntlgdss yqvnghmiav sienrrqliv aydklirffd
      181 tsiaiqddvl ldalekndgk kmrditasiq keqnsvirdq ssqtllvngv agsgktsvim
      241 qrvayllyqy rsqitsdnvl ilspnqkfih yisevlpslg eknplnqtir qfcsfllqea
      301 ktvpleneea yfsrlqepvt fqtetirsne fvaflkeaas ktaliepsfh silrkgkvvi
      361 skekiqsiyq stpqlpmier lqatkkrlis ewesrlirns kkqelqdqvl tlseqqqqry
      421 fghlieddsp tsiqkytmql lrmryhvvdd qlkdnswide drfldhyyta ftqrpylkqs
      481 titldeavir lfnrhlfvek lavpslsfll ideiqdytpa qcallltlfp raaftmvgde
      541 nqaifnsaip fseiqkifet nnrtvkrydl rtsyrssgei tklfaklvnd etlsivpvrp
      601 agesprfirf enerkwlaai tpfmknenhy tiltnsqtea afleeyfkgq anqrsfsiys
      661 idiakgrefd hvilydiske kfhtaqdkri lytmlsrgme sifvtykkel sdffqi
//
LOCUS       WP_181878753             153 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Moraxella catarrhalis].
ACCESSION   WP_181878753
VERSION     WP_181878753.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 153)
  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 153)
  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..153
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     Protein         1..153
                     /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=17459
     Region          32..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 mldfyqthak dffnqtinvd mhnvyqpfle nlpsgkqiis digcgsgrds vffakqgfqv
       61 maidgsqnli klakqnhpti dwqclafnei knqnwhnkfi giwacasllh vpfdelpnil
      121 ndllemlkpn gilyasfkyg dserekdgrf fvi
//
LOCUS       WP_181878851             228 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Legionella pneumophila].
ACCESSION   WP_181878851
VERSION     WP_181878851.1
KEYWORDS    RefSeq.
SOURCE      Legionella pneumophila
  ORGANISM  Legionella pneumophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 228)
  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 228)
  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..228
                     /organism="Legionella pneumophila"
                     /db_xref="taxon:446"
     Protein         1..228
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=26282
     Region          81..215
                     /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          97..125
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(98,101..102,105..106,108,132,135..136,139..140,
                     142..143,169,172..173,176..177,180)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          130..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..196
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnewwlvill vvlavfactl ityplrrnrl vslllapiif imvftgyyfw gdfarwqeyl
       61 hrneaqelaq smlksikspq elidklkakl daqpesakgw yllgrlyssq kdnqnaslaf
      121 akahqlkped eqfavnyahs lwqlsnqqfn pdileifhtl lknnprqpda lamlamhayl
      181 shdyeaainy wqrllqlapa qseealairk aiakaekhin rggkksdr
//
LOCUS       WP_181878945             252 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Micrococcus
            luteus].
ACCESSION   WP_181878945
VERSION     WP_181878945.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
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="Micrococcus luteus"
                     /db_xref="taxon:1270"
     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=26793
     Region          19..236
                     /region_name="PlsC"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     [Lipid transport and metabolism]; COG0204"
                     /db_xref="CDD:439974"
ORIGIN      
        1 msgvdaqspa aaggrptraa rapyvipgai vrpamralvr qvwegtehlp etgailavnh
       61 isevdplsva hmvynqgllp tflakaelwk vpvlkqvlea trmipvertr dggrslaaar
      121 eavatgraii vypegtvtrd pdgwpmaarn gavrlalqtg aplipvgqwg iqgllpyggr
      181 slrvlprkta rirvgapvdl adlrdrplta atlregtdrm maaitdlvae lrgepapegr
      241 wdpttgrrvt ga
//
LOCUS       WP_181879096             471 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Streptococcus
            pyogenes].
ACCESSION   WP_181879096
VERSION     WP_181879096.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus pyogenes
  ORGANISM  Streptococcus pyogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
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 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Streptococcus pyogenes"
                     /db_xref="taxon:1314"
     Protein         1..471
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=54944
     Region          6..>54
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mkffdenysq eiptrikclr kkynlkqsdl gnagqvsqve kgkrqvtasi llylntqtds
       61 dykeiifgdi akfvenmfyh cfssilfrdl etvdkrmysf sdddlisiqs sclrlsktfa
      121 nfniqrkifl asdetemdtf hkkddidvwv ggksynpars frnnpinelt vidfeemadi
      181 lllmlrdnli rsfeinvcnt lfeldkngep ttfnldkids iinkwwsenv steiipnlik
      241 klrenplfni gfmvndiler mykedipksy ltsvplvisk karttfayrm tdgqqrdeak
      301 leqihndyiq llhqgkdvae lnqkyskeel erngfsvhks ediklteert fdeiiswvsn
      361 pyatspiqer htiqleptrf sqedkkkiek tasqgindid lvdlielydi nldntnvsrh
      421 iegvltnntq vtyyfqeqln eellsmasal drvqqafikl lskeeirkfa l
//
LOCUS       WP_181879276            2380 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein [Levilactobacillus brevis].
ACCESSION   WP_181879276
VERSION     WP_181879276.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus brevis
  ORGANISM  Levilactobacillus brevis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Levilactobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..2380
                     /organism="Levilactobacillus brevis"
                     /db_xref="taxon:1580"
     Protein         1..2380
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=234433
     Region          22..1422
                     /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 mrhkafkddp kirykmfkag ktwvftaias fsllgaggis aradtstqad ntskvdatsa
       61 aseveakatd dtpvvadvsk denenaitnn ssasegvtpd qavssesaas saansfggqs
      121 sqnvssssvs satsasdnls ekvqassaas kvktdvtltt dvtstvaava ttrqqvvtvs
      181 gtassasgsl adstaaetat saasaaassa qlagsyatlv pidstesays aatsfagqts
      241 taadlavhyn slatmylnaa nvagvdaadm alkyanamsv assyattans tanlassaaa
      301 aaelaaaqni kdlvsstnsa tssaasaaqa aanaallaas saynatqyvq snaaavaays
      361 eanssaheaa naaslaksla kaaqaeygva ssaaisgdfs aassayaaaq siesqsqdty
      421 laastatsma essalratel avttiassaa adasaaatna sqaaslaada tqykgnqsia
      481 yassassfat qaassatlas saaaaaatat saavatslar lassaaadaa taysgassta
      541 slaaaydtda antqtstdsd tnaagattnt iaststavti gdaftlsstl algsydpgll
      601 ygsqnykltg tttytwyvst daknwtavtg natytptisa agtyyfqlvv agskkaswnl
      661 gassktstfs aasnvitvvv sdpngnyatq assaaaaans aaalatsqak aassayaqli
      721 sssdlsdita ssyatqaqks tstamsnats asaaasaats saslaasyea aknyssaavy
      781 aanaismqsd assyaavast atstaadfid ltyntianqs saaaylassy aelaasyane
      841 aktqaekana dtananaaya sapdlnsgat davaaaalan saaannaqla ssiavvaasy
      901 asagnwsgas saannastym vlateaatda asyasqatkt iveaqsshas siaavtsvei
      961 naaastatia tsvanslatt mktntslgss yvadatsyaq daqlaaataa asndfatsym
     1021 tqassavaag nftaassyad eakaslktag vlasqatdaa saasaaasna vvysnnlgss
     1081 qkkptgdawt llgltisggy tqqpttltst vsgktvvlts taktglgavn lshdstwyvq
     1141 vngkwqklgt vgsgvlqqnt rtgtitasdg ttiakytiqn ttsllsslat ssssltlemd
     1201 enytgslifq svdsftgtst ltgdfasdla evdvydsevp atgisitgdd yilnnsdtsn
     1261 tgtytavtnp gnatgdvtws isdptiatis sagvvtptsa tasgqvtita tiknsdgtsy
     1321 satktitign gledktvntg dslewkpaat smgsgsstsv tyqwyystta gslgtkidga
     1381 tsstlslsdi sagkagyytl rvtsssttvs lgqakltvna tisegasssa smaasaavda
     1441 agyasaassy anvasqyagk gstassyadq aaaaavtass aaaeasmaas qaaaassaas
     1501 saeaasdnsa assyaaeaek aassaqvake kassaandaq syadlainaa eeadsdsdsd
     1561 sdsdsdsdsd sdsdsdsdsd snsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd
     1621 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd
     1681 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdse sdsdsdsdsd
     1741 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd
     1801 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd
     1861 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdse
     1921 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd
     1981 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd
     2041 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsesdsd
     2101 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd
     2161 sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd sdsdsdsdsd snsgpdgdsg
     2221 sgsgsgggse ngndndsgsa gdtgsngdst ggsnnsgggt nngsttttvt gtsdgaaitp
     2281 laansstapt pltdlattsg nadgtsndkk atdksqsast dksssadtvn dgtngadaas
     2341 tqkdnnsgsi wgaiaaaiaa vtggswwffa gkrrknkddd
//
LOCUS       WP_181879392             338 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Legionella donaldsonii].
ACCESSION   WP_181879392
VERSION     WP_181879392.1
KEYWORDS    RefSeq.
SOURCE      Legionella donaldsonii
  ORGANISM  Legionella donaldsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
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="Legionella donaldsonii"
                     /db_xref="taxon:45060"
     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=39109
     Region          32..337
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnlldeqnsk nrkfvidkif hpldghfdtn slsawlsyyy svhvkgapek teqakmkdla
       61 kfinffqmev ghdlvdswtp avskhfqkhl cktisektgk pykatsinrt matirhvgrw
      121 lhqqrpllag dplaqvkdlq tdapdwnglt skqlmrlksa ceqrlkgctr knqnplmeta
      181 lfyvllgtgl resevvslnv gqyrqeglcd vsrhksnris qkiplpkesr myleeylekr
      241 gaqddeplfi trygtrlqtl dvyricqrvl kqalaflpeq ekfdftphkl rhtflkkvtd
      301 khgvhfaqel sgnvsikeif ryakpsqdei qltieelf
//
LOCUS       WP_181879605             256 aa            linear   BCT 28-DEC-2024
DEFINITION  LysM peptidoglycan-binding domain-containing M23 family
            metallopeptidase [Moraxella bovis].
ACCESSION   WP_181879605
VERSION     WP_181879605.1
KEYWORDS    RefSeq.
SOURCE      Moraxella bovis
  ORGANISM  Moraxella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..256
                     /organism="Moraxella bovis"
                     /db_xref="taxon:476"
     Protein         1..256
                     /product="LysM peptidoglycan-binding domain-containing M23
                     family metallopeptidase"
                     /calculated_mol_wt=27689
     Region          <12..116
                     /region_name="PRK06347"
                     /note="1,4-beta-N-acetylmuramoylhydrolase"
                     /db_xref="CDD:180536"
     Region          42..86
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          <133..256
                     /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 mgvailtali lsacankpty qpnnntrttp aggnhakqgv pqryqvqrgd tvskiaaryg
       61 lnwrevsrin rldsnhtirv gqwltlwgts npaqagtsts itqspmhsnt ntnttkvitv
      121 knpmvgsvgv mqfeypvskd skvvrhfgei sningintka egmwfigknn dpiraarsgt
      181 vvhadnastg giitishpdg fvssylhvkd vsvrkgqkig vgdpiakmkq qqnratllef
      241 riakngvyid pvtvlk
//
LOCUS       WP_181879626              95 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Salmonella enterica].
ACCESSION   WP_181879626
VERSION     WP_181879626.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 95)
  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..95
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     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=10708
     Region          <20..82
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mspqmiqklp aitllegmfp elstnqlkvc ifyamgvpyd aiaqncrlsp etvrtylkrs
       61 lknlnlegyd alrsavlmrt fvfmisntak enekm
//
LOCUS       WP_181879694             215 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Moraxella
            lacunata].
ACCESSION   WP_181879694
VERSION     WP_181879694.1
KEYWORDS    RefSeq.
SOURCE      Moraxella lacunata
  ORGANISM  Moraxella lacunata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 215)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..215
                     /organism="Moraxella lacunata"
                     /db_xref="taxon:477"
     Protein         1..215
                     /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=23985
     Region          7..195
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mqtfqydnsh tdylasrcpk mamainkigh idrpvnpdif seliraiigq qisssaaqtv
       61 wqrltnltdi tptalanlsa delqgigisy rkvgyiqgia cdildnqldl dslhtmsdde
      121 ikqvlvafkg vgewtaqmlm ifslnrmdvl sqhdlaivrg lrmlyrhrei tpklfakyqr
      181 rfapynsvas lylwaiagga ldltdpkpav kkaks
//
LOCUS       WP_181880087             468 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Enterococcus
            mundtii].
ACCESSION   WP_181880087
VERSION     WP_181880087.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus mundtii
  ORGANISM  Enterococcus mundtii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 468)
  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 468)
  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..468
                     /organism="Enterococcus mundtii"
                     /db_xref="taxon:53346"
     Protein         1..468
                     /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=53202
     Region          3..455
                     /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 meeivllhtn dlhshlenwp rirrfleqkk renekknntt tltvdlgdfv drwhplseat
       61 nghanvelmn qigydaatig nnegvgnskn elnhlydhan fdvllsnlfd kntlqppvwt
      121 kpykiietkq rtkvgliaft apfpltynpn gwdirqpydl lpelveqlrp qvdvlilmsh
      181 lgiqddlqia keipaidvil gshthhlfid gkvvnevqla aagkfgqyvg evhlslenkk
      241 ivghyakaip tdtmtafved ekeiagyleq ghrllaqkkv adlpfdlsld lfdehsfiqi
      301 aleavkergn teasflnsgl flnsvpkglv dqdqlhsalp hpmhlinvtl kgsdmirlvl
      361 eieksrlflr nfpikgmgfr gqifgeifys gitydavnre vlwqkqpiee eknytvttvd
      421 hlmfvpffpt ieivgqvdfl fpefirtvvg dylnahyptn ekegiiek
//
LOCUS       WP_181880169             927 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Escherichia coli].
ACCESSION   WP_181880169
VERSION     WP_181880169.1
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=104059
     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 sdeqsfieqa
      301 ewsmlvqlfn qrlqeriqsg elktisggta rsvriapdyq slffrvnard dnmqdaanal
      361 maelatidqh gfsaeelddv kstrltwlkn avdqqaerdl rmltsrlass slnntpflsp
      421 eetyqlskrl wqqitvqsla ekwqqlrknq dafweqmvnn evaakkalsp aailalekey
      481 ankklaayif pgrnlsltvd adpqaeissk etlaenltsl tlsngarvil aksageeqkl
      541 qitavsnkgd lsfpaqqksl ialankavsg sgvgelssss lkrwsaensv tmsskvsgmn
      601 tllsvsartn npepgfqlin qrithstind niwaslqnaq iqalktldqr paekfaqqmy
      661 etryadnrtk lpqenqiaqf taadalaadr qlfsspadit fvivgnvaed klvalitryl
      721 gsikhsdspl aagkpltrat dnasvtvkeq nepvaqvsqw krydsrtpvn latrmaldaf
      781 nvalakdlrv nireqasgay svssrlsvdp qakdishlla ftcqperhde lltlanevmv
      841 krlakgiseq elneyqqnvq rsldiqqrsv qqlantivns liqyddpaaw teqeqllkqm
      901 tvenvntavk qylsypvnty tgvllpk
//
LOCUS       WP_181880291              60 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Escherichia
            coli].
ACCESSION   WP_181880291
VERSION     WP_181880291.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..60
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>60
                     /product="helix-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          6..60
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mitpvslmdd qmvdmafitq ltgltdkwfd klikdggfpa pikmgrssrw lkseveawlq
//
LOCUS       WP_181880245             721 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Escherichia coli].
ACCESSION   WP_181880245
VERSION     WP_181880245.1
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 both ends.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>721
                     /product="beta strand repeat-containing protein"
     Region          <44..721
                     /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 advstakiad lvvikdgsea dgstantlqv kvtdafgnal agqtvsvmag ngatvaptvi
       61 tepdgtveis vtsqtagtst vtasinnssq srdvtfiadv rtaqiaslev tqdnavadga
      121 mantlrarvt dafgnalagq tvsvmagnga ttaptvttqp dgtveisvts qtagistvta
      181 tinsssqsrd vtfiadasta qiadlvvikd gseadgsten tlrvrvtdaf gntlggqtvs
      241 vtadnsatvt ptvitepdgt veisvtsqta gvstvtasin sssqsrnvtf vadvrtakia
      301 dlvvikdgse adgstantlr arvtdafgnt lggqtvsvla dngatvaptv ttqpdgtvei
      361 svtsqtagts tvtasinnss lsqnvtfvad vrtakiadlv vikdgsvadg atantlqvkv
      421 tdafgnalng qtvsvmagng atvtptvitg pdgtveisat sqtagistvt vtinnsslsr
      481 nvmfvadvrt aqiadlvvik dgavadgama nmlqvkvtda fgnalagqtv svlagngatt
      541 astvttqpdg tveisvtsqt agtsvvtasi nnssqsrnvt fiadvrtaki adlevikdgs
      601 eadgstantl rarvtdafgn alagqtvsvl adngatvalt ettkpdgtae isvtsqtagv
      661 savtvsinns sqsrnvtfia dvrtaqiael vvikdgsead gstantlrvr vtdafgnala
      721 g
//
LOCUS       WP_181879532             363 aa            linear   BCT 28-DEC-2024
DEFINITION  SPOR and LysM peptidoglycan-binding domain-containing protein
            [Moraxella bovis].
ACCESSION   WP_181879532
VERSION     WP_181879532.1
KEYWORDS    RefSeq.
SOURCE      Moraxella bovis
  ORGANISM  Moraxella bovis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain
            That Targets Proteins to the Site of Cell Division
  JOURNAL   J Bacteriol 199 (14), e00118-17 (2017)
   PUBMED   28396350
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Yahashiri,A., Jorgenson,M.A. and Weiss,D.S.
  TITLE     Bacterial SPOR domains are recruited to septal peptidoglycan by
            binding to glycan strands that lack stem peptides
  JOURNAL   Proc Natl Acad Sci U S A 112 (36), 11347-11352 (2015)
   PUBMED   26305949
REFERENCE   3  (residues 1 to 363)
  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   4  (residues 1 to 363)
  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 18526854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Moraxella bovis"
                     /db_xref="taxon:476"
     Protein         1..363
                     /product="SPOR and LysM peptidoglycan-binding
                     domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=39651
     Region          91..247
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          286..361
                     /region_name="SPOR"
                     /note="SPOR domain; pfam05036"
                     /db_xref="CDD:461531"
ORIGIN      
        1 milyavnqgq sdtaqnvqta ktipqtdnva ttaddgvvrp tvepltvdma teskllsakq
       61 eareartlaq ekeamaliea qekaqqlald kataeqkata tpadtltvet rpeaiavaka
      121 qakrellekl akekelkakk eqeqrekddk ekakkeqdek akadklkaqk sqdkkdkaek
      181 ekkeqakkar deapqnanng qhkvvrgdgl iklsrqygvp vsalaeannm grhdplplgk
      241 tikipskaqv trlereaker eaqkaaaasa dkrlkearqk gsdgdsnary gvqvsladnq
      301 akadelakry rnagykvsts qtsrgvrvlv gseknqdaat alrdkiknds rvdgsgawvk
      361 rvq
//
LOCUS       WP_181880561             309 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Pseudomonas].
ACCESSION   WP_181880561
VERSION     WP_181880561.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (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   2  (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
REFERENCE   3  (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
REFERENCE   4  (residues 1 to 309)
  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..309
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..309
                     /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=33864
     Region          72..300
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          220..300
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mayasvelcr vapdaplqrl ravpasapqt laieddllll rldashsgtg vqrtcellgg
       61 pllcltfleq ghvqyadrkg rcwrfeagqs itqllhappq asrfqfgrga cglhllvgeh
      121 tlrrylgeqq awrllhcqge apllqhatsr dacshvqala trlaqghcap ldthlhvlnl
      181 lshplrqlav ssqatlllpa aqvkrleqar qllhdeldqp ltvallcrrv glsaaklkqg
      241 fhalfdttpy rmllalrmqr ayillqegcq vaqvayrvgy shpsnfsaaf sgyfgfapke
      301 vgkrgavpt
//
LOCUS       WP_181880662             288 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Ectopseudomonas mendocina].
ACCESSION   WP_181880662
VERSION     WP_181880662.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas mendocina
  ORGANISM  Ectopseudomonas mendocina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
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="Ectopseudomonas mendocina"
                     /db_xref="taxon:300"
     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=31705
     Region          13..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 maldfmadnl safvfvcvvf glligsflnv vvyrlplmlq rdwqsqarev lelpaaptaq
       61 tfnlilpnss cpncgheirp wenipvisyl flrgkcsnck tpiskrypiv elacgllsgy
      121 vawhfgftwq agamlvlawg llamslidad hqilpdvlvl pllwlglivn yyglftsled
      181 alwgaiagyl slwsvywlfk litgkegmgy gdfkllamlg awggwqilpl tillsslvga
      241 vlgvimlrmr gsdsstpipf gpylaiagwi allwgdvits nylkfagf
//
LOCUS       WP_181880786             223 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Edwardsiella tarda].
ACCESSION   WP_181880786
VERSION     WP_181880786.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella tarda
  ORGANISM  Edwardsiella tarda
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Edwardsiella.
REFERENCE   1  (residues 1 to 223)
  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 223)
  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..223
                     /organism="Edwardsiella tarda"
                     /db_xref="taxon:636"
     Protein         1..223
                     /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=24441
     Region          4..219
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mktemkdrir srriqlnitq qalakrlgvs rvsvtkweng ttkpdgenlh qlaatlqvap
       61 ewllygsssa spdeikddtr vipylkppva vpiisavqag twtetyassk hsdviswtqt
      121 tanvsdevfg lvvrgesmtn pnglpsipeg sivivephyd qiddlygkiv vavldgssea
      181 tvkklvwdsp ytylmplnpl fkpiqitgnc rivgkvvqit qni
//
LOCUS       WP_181880825             192 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_181880825
VERSION     WP_181880825.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 192)
  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 192)
  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..192
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..192
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          <5..161
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 fympdqrhhm lfatlwntgm rigearmltp esfdldgvrp fvrilsekvr arrgrppkde
       61 vrlvpltdis yvrqmeswmi ttrprrrepl wavtdetmrn wlkqavrrae adgvhfsipv
      121 tphtfrhsyi mhmlyhrqpr kviqalaghr dprsmevytr vfaldmaatl avpftgdgrd
      181 aaeilrtlpp lr
//
LOCUS       WP_181880876             611 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Crenobacter cavernae].
ACCESSION   WP_181880876
VERSION     WP_181880876.1
KEYWORDS    RefSeq.
SOURCE      Crenobacter cavernae
  ORGANISM  Crenobacter cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Crenobacter.
REFERENCE   1  (residues 1 to 611)
  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 611)
  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 611)
  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 611)
  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 611)
  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 611)
  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..611
                     /organism="Crenobacter cavernae"
                     /db_xref="taxon:2290923"
     Protein         1..611
                     /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=67657
     Region          336..607
                     /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 mstsadaase tplvrqvvgr vllclsllsi avvgwqtwrg yhteiehags ierlirdqym
       61 pilaqnvwdv dlpsaektlq aiathpgvay aelttdsdqr lsssrlpmtv kptrvvevpl
      121 mlghrppvkl gtlrvmlsya tlyahirdea lqnalvqllq lalvalllal alnhyftapl
      181 ntltehlrry rlgaavlpdt rrcheldalv dafgdlqdrl adknaeglra ceelaahrdr
      241 laelvairta eldhlnrfqq lvselstrfi nvtedaldat laealarigg flgvqrcylf
      301 ildsrlavqe thewhaaqsr svnelltlys adaspwlvpq larhsvvild ahtpdshglg
      361 qeqltlsllg iatlvlvkvr vshvplgffg cdtatprvwg eqevallrli gemlanvmar
      421 rhqlralqaa rqdledsnar lhrqarrdal tglanrlhfd eikrplfdsa llnrtplslv
      481 lcdvdhfkly ndryghprgd tclarvseal ravfrrsndl variggeefi vilpgadthl
      541 aqelaeemre avaeldieha aspvapcvtv svgvatldaa rhhniealin dvdtalyrak
      601 qqgrnrvisa e
//
LOCUS       WP_181880976             374 aa            linear   BCT 28-DEC-2024
DEFINITION  N5-glutamine methyltransferase family protein [Crenobacter
            cavernae].
ACCESSION   WP_181880976
VERSION     WP_181880976.1
KEYWORDS    RefSeq.
SOURCE      Crenobacter cavernae
  ORGANISM  Crenobacter cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Crenobacter.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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 374)
  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..374
                     /organism="Crenobacter cavernae"
                     /db_xref="taxon:2290923"
     Protein         1..374
                     /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=40642
     Region          112..>259
                     /region_name="ABBA-PTs"
                     /note="ABBA-type aromatic prenyltransferases (PTases);
                     cl19121"
                     /db_xref="CDD:473141"
     Region          <200..341
                     /region_name="PrmA"
                     /note="Ribosomal protein L11 methylase PrmA [Translation,
                     ribosomal structure and biogenesis]; COG2264"
                     /db_xref="CDD:441865"
ORIGIN      
        1 msefpliswt eagqthtarw rsesdapppk kvmiaddtls adkayklvce gtallwrgdy
       61 hnarqllsal arragrkprk passpteafn fhrqtqaqra rllgmlllpf nadysiplrr
      121 apdvrqacee aygpagvafv aslrelqglv gshewrkkgv eitalggehi hphygvyspi
      181 rgeyldlvae aplpsttlaf digtgtgvla avlarrgver vigtdqdpra lacarenldr
      241 lglsgkvdvv eadlfpegra plivcnppwl pakptspien avydpdsrml kgfldglaah
      301 lepggegwli lsdlaehlgl rsrdallalf daaglkvvdr ldirprhpka gdasdplhqa
      361 raaevtslwr laar
//
LOCUS       WP_181881014             314 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Crenobacter cavernae].
ACCESSION   WP_181881014
VERSION     WP_181881014.1
KEYWORDS    RefSeq.
SOURCE      Crenobacter cavernae
  ORGANISM  Crenobacter cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Crenobacter.
REFERENCE   1  (residues 1 to 314)
  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 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 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Crenobacter cavernae"
                     /db_xref="taxon:2290923"
     Protein         1..314
                     /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=33978
     Region          4..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 mpsmkktivn lfsgflgvgk ttalkaliar rpaherwavi vnefgevgid gaalsqdglp
       61 vaeiaggclc cvagpqmtat vatllrrerp drllieasgl ahaagvidel nekplgdalt
      121 igavvtvvdp rqfvnpdyar qplyrdqvai advlvankae madevsltaf reqaaalfpp
      181 kaliaevsqg eidpawldlp faeksryrpa vakdaasawq segftfdaer nfcgekltrf
      241 fdelpklqpg larakgvfrv ldsfvwlnwa egqwgasqva wrrdsrfeli atepidaaai
      301 estlasclek egkr
//
LOCUS       WP_181881323             191 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class I SAM-dependent DNA methyltransferase [Vibrio].
ACCESSION   WP_181881323
VERSION     WP_181881323.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 191)
  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 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   3  (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 11471966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..191
                     /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=20918
     Region          1..166
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 maqdwdglak nwesnpateq faqsvfeqlq qltqldgikv ldfgcgtgql sqrlspmvkd
       61 ivaldaseam ieeldkkelv nvepvvdals rglvaqhpaf rgqfdlvvas svlafvedld
      121 asltishsll nhggyfvhfd wiaeceqdgf tltkseralk eagftevesq hvfditsdgk
      181 tmsvlmglgr r
//
LOCUS       WP_181881422             159 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Shewanella algae].
ACCESSION   WP_181881422
VERSION     WP_181881422.1
KEYWORDS    RefSeq.
SOURCE      Shewanella algae
  ORGANISM  Shewanella algae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
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="Shewanella algae"
                     /db_xref="taxon:38313"
     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=17363
     Region          77..>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 mghvlnqtsr fevmeyclat hellllrdra glpvhgldds clpakpllsl cirersggen
       61 lqqgqlvala lvrsgsvaep sqeqehyllq dflvlpefrh lglgsfllea vierlsllga
      121 pkrqlmlevl pgdevlaqrl gfkpgghsvp gnlwlrsvg
//
LOCUS       WP_181881571             816 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Escherichia coli].
ACCESSION   WP_181881571
VERSION     WP_181881571.1
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 both ends.
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>816
                     /product="beta strand repeat-containing protein"
     Region          <42..816
                     /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 vstakiadlv vikdgseadg stantlqvkv tdafgnalag qtvsvmagng atvaptvite
       61 pdgtveisvt sqtagtstvt asinnssqsr dvtfiadvrt aqiaslevtq dnavadgama
      121 ntlrarvtda fgnalagqtv svmagngatt aptvttqpdg tveisvtsqt agistvtati
      181 nsssqsrdvt fiadastaqi adlvvikdgs eadgstentl rvrvtdafgn tlggqtvsvt
      241 adnsatvtpt vitepdgtve isvtsqtagv stvtasinss sqsrnvtfva dvrtakiadl
      301 vvikdgsead gstantlrar vtdafgntlg gqtvsvladn gatvaptvtt qpdgtveisv
      361 tsqtagtstv tasinnssls qnvtfvadvr takiadlvvi kdgsvadgat antlqvkvtd
      421 afgnalngqt vsvmagngat vtptvitgpd gtveisatsq tagistvtvt innsslsrnv
      481 mfvadvrtaq iadlvvikdg avadgamanm lqvkvtdafg nalagqtvsv lagngattas
      541 tvttqpdgtv eisvtsqtag tsvvtasinn ssqsrnvtfi advrtakiad levikdgsea
      601 dgstantlra rvtdafgnal agqtvsvlad ngatvaltet tkpdgtaeis vtsqtagvsa
      661 vtvsinnssq srnvtfiadv rtaqiaelvv ikdgseadgs tantlrvrvt dafgnalagq
      721 tvsvladnga tvaptvttqp dgtveisvts qtagtstvta sinsssqsrn vtfiadvsta
      781 qiaslevtqd navadgatan tlrvrvtdaf gnalag
//
LOCUS       WP_181881658             106 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: thioredoxin family protein [Helicobacter].
ACCESSION   WP_181881658
VERSION     WP_181881658.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter
  ORGANISM  Helicobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae.
REFERENCE   1  (residues 1 to 106)
  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 106)
  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 106)
  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 106)
  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..106
                     /organism="Helicobacter"
                     /db_xref="taxon:209"
     Protein         1..106
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11628
     Region          1..104
                     /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 mlekltkatf enavkegvcl vaigapwcpd crkiepiigm lmqeygaqvk ffaimadeee
       61 alkdslnvrr iptlifykng aevgerlvep nskslieeai ksaina
//
LOCUS       WP_181880889             686 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Crenobacter cavernae].
ACCESSION   WP_181880889
VERSION     WP_181880889.1
KEYWORDS    RefSeq.
SOURCE      Crenobacter cavernae
  ORGANISM  Crenobacter cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Crenobacter.
REFERENCE   1  (residues 1 to 686)
  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 686)
  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 686)
  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 686)
  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..686
                     /organism="Crenobacter cavernae"
                     /db_xref="taxon:2290923"
     Protein         1..686
                     /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=75439
     Region          40..686
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mglalmplyv haeeaelpei qvvgqaagsy kapvsraatr ipmelkdvpq tvnvvnqali
       61 rdqnatsfqd alanvvgigq svgdgqrdqi tirgfsaitd qfvdgvrdds lyfrdlsnve
      121 hievlkgpas vlygrgsagg linrvtkkpt ldpvqtlgfq fdefgqkrae idlgvagesa
      181 qfrvtgayed segfrkqsfi dreavapslm lnlsertkll lqadylhdrr ladqgvpryl
      241 gapvdvpiet yygsangkde tyvdtdvksq tatlehefsa dtrfkqlvrh yefdlarnyt
      301 tnvvnepakk vtvrhtrrlr desgwfsqte lthgfnalga rhellaglev gkqdkaeiqw
      361 rraassltty dlfnprlvsl gappsganpd innankvdia alylqdlisa grwkflaglr
      421 fdrirqkrdd ltsanvdldr tdnvwsprag vvyevtpsts lyasasrsfq pladsftfkr
      481 nsddlkpeqt dgfevgaksd lldgkasatl alfqiekknm lsgdptdptn rfvpigrqqs
      541 rgvelslagq vlpgleasag yayldavike ardsdgksld gkrpslaprh tanvwlkqsl
      601 gndfygtagv ryvderfass tsnivrlpay tvgdigliyq gkrfeanlml knvadvkyyv
      661 sahgaaddyn mpgaprtlsl strfhf
//
LOCUS       WP_181881785             167 aa            linear   BCT 28-DEC-2024
DEFINITION  NuoB/complex I 20 kDa subunit family protein [Helicobacter sp. MIT
            14-3879].
ACCESSION   WP_181881785
VERSION     WP_181881785.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter sp. MIT 14-3879
  ORGANISM  Helicobacter sp. MIT 14-3879
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 167)
  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 167)
  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 167)
  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 167)
  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 167)
  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..167
                     /organism="Helicobacter sp. MIT 14-3879"
                     /db_xref="taxon:2040649"
     Protein         1..167
                     /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=18769
     Region          4..157
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 mgeyemnytn sipvkltrld kilnwatsns lwpmtyglac caiemmasgg srydfdrfgt
       61 ifrasprqsd vmivagtvtk khaefvrrly dqmpepkwvi smgscantgg mfntystvqg
      121 vdriipvdiy lpgcaprpet lqyavmvlqq kirsqkaiks htkkrli
//
LOCUS       WP_181882172             407 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: cytochrome b [Helicobacter].
ACCESSION   WP_181882172
VERSION     WP_181882172.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter
  ORGANISM  Helicobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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..407
                     /organism="Helicobacter"
                     /db_xref="taxon:209"
     Protein         1..407
                     /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=46842
     Region          1..407
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 mmevkkangv idwldqriai kkvievlatk ywvpkninfl wamgvilltl ftllvvsgff
       61 llmyykpdtk lafdsvndti mrevafgwlw rhihavaasm vfliiyihmf vavyygsykr
      121 greviwiggm llfvvfsaea fsgymlpwgq msfwaaavit nlpsaipgig pdlvewvrgn
      181 fviadstltr ffmlhvcllp ivilmlialh fytlrvphvn nengeeidfe aeakkyeegk
      241 kkeakvisfw pdflskdifv vsvfmmlffy lvcyhfnfam dpinfepann mktpahiype
      301 wyflwsyevl rgfffsadvg liafgiaqvv flflpwldrs pivapahkrp lfmiwfwvli
      361 ldlvvltifg klppeginnq iglvaavgfl vwvfvalpvv timerkk
//
LOCUS       WP_181882176             384 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: trans-sulfuration enzyme family protein
            [Helicobacter].
ACCESSION   WP_181882176
VERSION     WP_181882176.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter
  ORGANISM  Helicobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae.
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="Helicobacter"
                     /db_xref="taxon:209"
     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=41942
     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 mtqnsldtll ihgglttdsk tgavntpiyq tstyaqtalg knlgyeysrt knptrdgies
       61 liaeleggkf gfafasgmaa igtilslfks gdkilissnv yggtfrildk vfcnfniiye
      121 ivdmrdyall esvitpevka lfietpanpl msvvslqklv qiakaknllt ivdntfmtpy
      181 lqrplefgvd ivlhsatkyl gghsdvvagl avvrdeslaq kigflqnsig gvlapfdsfl
      241 lirgiktlgl rmqrhcenal qiaeflrahn gvkkvyypgl kddegysihn eqarggggmi
      301 sfelqetydy kkffestkfi vlaeslggve sllchpasmt hasipaeira kvgitdnlir
      361 lsvgieyvnd liddlthaie qakr
//
LOCUS       WP_181882555             110 aa            linear   BCT 28-DEC-2024
DEFINITION  TPM domain-containing protein, partial [Escherichia marmotae].
ACCESSION   WP_181882555
VERSION     WP_181882555.1
KEYWORDS    RefSeq.
SOURCE      Escherichia marmotae
  ORGANISM  Escherichia marmotae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 110)
  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: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Escherichia marmotae"
                     /db_xref="taxon:1499973"
     Protein         <1..>110
                     /product="TPM domain-containing protein"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
     Region          1..>106
                     /region_name="YgcG"
                     /note="Uncharacterized membrane protein YgcG, contains a
                     TPM-fold domain [Function unknown]; COG1512"
                     /db_xref="CDD:441121"
ORIGIN      
        1 dltsslnsqe kkelthkles ifnntqvqia vliipttkde tieqyatrvf nnwrlgdakr
       61 ndgiliivaw sdrtvriqvg ygleekvtda lagdiirsnm ipafkqqkla
//
LOCUS       WP_181882633             247 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 16S rRNA (uracil(1498)-N(3))-methyltransferase
            [unclassified Helicobacter].
ACCESSION   WP_181882633
VERSION     WP_181882633.1
KEYWORDS    RefSeq.
SOURCE      unclassified Helicobacter
  ORGANISM  unclassified Helicobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013870
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="unclassified Helicobacter"
                     /db_xref="taxon:2593540"
     Protein         1..247
                     /product="16S rRNA (uracil(1498)-N(3))-methyltransferase"
                     /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=27383
     Region          4..242
                     /region_name="PRK11713"
                     /note="16S ribosomal RNA methyltransferase RsmE;
                     Provisional"
                     /db_xref="CDD:236959"
ORIGIN      
        1 mydecagkne lalegesyay ifksrrwqke knlilsnltd gklyeykita lsrnkarlel
       61 vdsiieqtng asdgvnaiks ansgasespn arvhiiwaiv dskvvektlp flnelgigkl
      121 sffyadfsqk nivlnearlr kilvhsceqc grnelleief lpnlqavlqk ykniialdfp
      181 aptldcvlks intrpsvlig aegglsener allqsfstpc aqikhaytlr sesaciftas
      241 ilgfvef
//
LOCUS       WP_181882697             422 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Pantoea agglomerans].
ACCESSION   WP_181882697
VERSION     WP_181882697.1
KEYWORDS    RefSeq.
SOURCE      Pantoea agglomerans
  ORGANISM  Pantoea agglomerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea; Pantoea agglomerans group.
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="Pantoea agglomerans"
                     /db_xref="taxon:549"
     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=46557
     Region          174..409
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mtnkisrngl tlvvnfsvva lclalslnmf vtglpqkify lvsylsiasv lyglvrrrve
       61 fkengfyial favliifali rlfwaihvkg ietapstdai tnmgnyllga krllmgafvl
      121 lslavygdrv slttlrvgkg lillgllitl gfgihehlyt enirikltte aasmssymil
      181 fiycawlwls ryethaywkv adiavlavtf allylcgtrv tlialiavgl lflvqtyrls
      241 lltnwrisal lvgvmavlil mtsnrwvegv qdienfgsns stslgarvai wggavnfieh
      301 hggfatpdar ttearqfita hyplnvegft nvkynmhnef levtslqgwl gtaslallyl
      361 tvlagwlkkc dlrgvalpmv alfttgltds vlpynqtati fimalalcci rrplpvtrvt
      421 ta
//
LOCUS       WP_181882958            1123 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Escherichia coli].
ACCESSION   WP_181882958
VERSION     WP_181882958.1
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 both ends.
FEATURES             Location/Qualifiers
     source          1..1123
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>1123
                     /product="beta strand repeat-containing protein"
     Region          <15..1121
                     /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 vstakiadlv vikdgseadg stantlqvkv tdafgnalag qtvsvmagng atvaptvite
       61 pdgtveisvt sqtagtstvt asinnssqsr dvtfiadvrt aqiaslevtq dnavadgama
      121 ntlrarvtda fgnalagqtv svmagngatt aptvttqpdg tveisvtsqt agistvtati
      181 nsssqsrdvt fiadastaqi adlvvikdgs eadgstentl rvrvtdafgn tlggqtvsvt
      241 adnsatvtpt vitepdgtve isvtsqtagv stvtasinss sqsrnvtfva dvrtakiadl
      301 vvikdgsead gstantlrar vtdafgntlg gqtvsvladn gatvaptvtt qpdgtveisv
      361 tsqtagtstv tasinnssls qnvtfvadvr takiadlvvi kdgsvadgat antlqvkvtd
      421 afgnalngqt vsvmagngat vtptvitgpd gtveisatsq tagistvtvt innsslsrnv
      481 mfvadvrtaq iadlvvikdg avadgamanm lqvkvtdafg nalagqtvsv lagngattas
      541 tvttqpdgtv eisvtsqtag tsvvtasinn ssqsrnvtfi advrtakiad lvvikdgsea
      601 dgstantlra rvtdafgnal agqtvsvlad ngatvaltet tkpdgtaeis vtsqtagvsa
      661 vtvsinnssq srnvtfiadv rtaqiadlvv ikdgseadgs tantlrvrvt dafgnalagq
      721 tvsvladnga tvaptvttqp dgtveisvts qtagtstvta sinsssqsrn vtfiadvsta
      781 qiaslevtqd navadgatan tlrvrvtdaf gnalagqtvs vlagngatta ptvttqpdgt
      841 veisvtsqta gisavtasin nssqsrnvtf iadvrtakia dlvvtrdnsv adgamantlr
      901 vrvtdafgnt lagqtvsvma dnsatvsltv ttepdgtvei svtsqtagvs avtasinnss
      961 lsqsvkfiad vrtaqiadlv vikdgseadg stantlqvrv tdafgnalag qtvsvtadns
     1021 amvastvitg pdgtveisvs sqtagisavt atinnstasq nvmfiadvrt akiadlvvtr
     1081 dnsvadgama ntlqvkvtda ngntlagqtv svladngatt apk
//
LOCUS       WP_181883100            1504 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Escherichia coli].
ACCESSION   WP_181883100
VERSION     WP_181883100.1
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=166400
     Region          116..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 pelqlgnaiv kpsryvqnsq fsplkkyplv eqfryplwqa kpvepqqgvk
      181 legasnnfis pqpgniyipl gkqepglylv eamiggyrat tvvfvsdtva lskvsgnell
      241 vwtagkiqge akpgseilwt dglgvmtrgv tddsgtlqlq hispersyil gkdaeggvfv
      301 senffyesei yntrlyiftd rplyragdrv dvkvmgrefh dplhsspivs apaklsvlda
      361 ngsllqtinv tldarnggqg sfrlpenava ggyelrlayr nqvysssfrv anyikphfei
      421 glaldkkefk tgeavsgklq llypdgepvk darvqlslra qqlsmvgndl ryagrfpvsl
      481 egsetvsdds 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 qdnepvvlvt kfagaemrqt ltlhkganyi sltqniqqsg
      961 llsaelqqng qvqdsistkl sfvdnswpve qqknvmlggg enalmlpeqa snirlqsset
     1021 pqeifrnnld alvdepwggv intgsrlipl slawrsladh qsaaandirq miqdnrlrlm
     1081 qlagpgarft wwgedgngda fltawawyad wqasqalgvt qqpeywqhml dsyaeqadnm
     1141 pllhralvla waqemnlpck tllkgldeai arrgtktedf seedtrdind slildtpesp
     1201 ladavanvlt mtllkkaqlk stvmpqvqqy awdkaansnq plahtvvlln sggdatqaaa
     1261 ilsgltdeqs tieralamnw lakymatmpp vvlpapagaw akhkltggge ywrwvgqgvp
     1321 dilsfgdels pqnvqvrwre paktaqqsni pvtverqlyr lipgeeemsf tlqpvtsnei
     1381 dsdalyldei tltseqdavl rygqvevplp pgadverttw gisvnkpnag kqqgqlleka
     1441 rnemgelaym vpvkeltgtv tfrhllrfsq kgqfvlppar yvrsyapaqq svaagsewtg
     1501 mqvk
//
LOCUS       WP_181883264             580 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Pseudomonas
            fluorescens].
ACCESSION   WP_181883264
VERSION     WP_181883264.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
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="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     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=63104
     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 rfrvvlglla lmvgaiawri idlqvvdrdf ligqgdarsl rhipipahrg
       61 litdrngepl avstpvttlw anakelqvak dkwtelahal gqdpkalker leaqankefi
      121 ylvrgltpeq gqgvldlkip gvygieefrr fypagettah mvgftdiddh gregvelayd
      181 ewlagvpgkr qvikdrrgrl ikdvqvtkna kagkplalsi dlrlqylanr elrnaiieng
      241 akagslvimd vktgeilamv nqptynpnnr rnlqpammrn ramidvfepg stmkaismsa
      301 alesgrwkpt dkvevypgtl qlgkytirdv srsegpvldl tgilinssnv gmskvafdig
      361 geaiyhlaqk iglgqptgld fpgervgnlp nyrewrkaet atlsygygls vtaiqlahaf
      421 svlanngrmv plslihvdea pkaeqvipen vaktmqtmlq qvieaprgvf raqvpayhva
      481 gksgtarkts vgtkgyaens yrslfagfgp msdpryaivv videpskagy fgglvsapvf
      541 skvmsgtlrl mnitpdnlpp tqqanagppa avvkanggrg
//
LOCUS       WP_181882628             134 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: type II toxin-antitoxin system tRNA(fMet)-specific
            endonuclease VapC [unclassified Helicobacter].
ACCESSION   WP_181882628
VERSION     WP_181882628.1
KEYWORDS    RefSeq.
SOURCE      unclassified Helicobacter
  ORGANISM  unclassified Helicobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 134)
  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..134
                     /organism="unclassified Helicobacter"
                     /db_xref="taxon:2593540"
     gene            1..134
                     /gene="vapC"
     Protein         1..134
                     /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=14893
     Region          5..131
                     /region_name="PIN_VapC4-5_FitB-like"
                     /note="VapC-like PIN domain of Mycobacterium tuberculosis
                     VapC4 and VapC5, and Neisseria gonorrhoeae FitB and
                     related proteins; cd09881"
                     /db_xref="CDD:350229"
     Site            order(6..16,24..27,34..35,38..39,41..43,45..47,49,56..60,
                     62..64,66,69..70,72..74,78..79,81..83,85..86,89,95..102,
                     110..111,116..117)
                     /site_type="other"
                     /note="oligomeric interface [polypeptide binding]"
                     /db_xref="CDD:350229"
     Site            order(6..16,24..27,34..35,43,45..47,56..60,62..64,66,
                     69..70,72,74,85,95..102,110..111,116..117)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:350229"
     Site            order(38..39,41..43,45..46,49,58,62,72..74,78..79,81..83,
                     85..86,89,97..98,101)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:350229"
ORIGIN      
        1 mvkylldtnt iiyainkthk svleriakcd iceiatcsiv aselcfgvak styktqneia
       61 ldkmlnnlvi ldfglkeaka ygairakqeq nrqlignmdm liaavaiand lilvtnnekd
      121 fsriaelkle nwil
//
LOCUS       WP_181883392            1036 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Escherichia coli].
ACCESSION   WP_181883392
VERSION     WP_181883392.1
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 both ends.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>1036
                     /product="beta strand repeat-containing protein"
     Region          <51..987
                     /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 savtasinns sqsrnvtfva dvrtaqiadl vvikddsvad gstantlrar vtdafgnala
       61 gqtvsvlagn gattaptvtt qpdgtveisv tsqtagisav tasinsssqs qnvtfvadvr
      121 takiadlvvi kdgseadgst antlrarvtd afgnalagqt vsvladngat taptvitepd
      181 gtvdisvtsq tagistvtat insssqsqnv tfiadirtaq iaslevtqdn avadgamant
      241 lqvkitdafg ntlggqtvsv ladngatvap vvttqpdgtv eisvtsqtag vsavtatins
      301 stqsqnvtfi advrtakiad lvvikdgsea dgstantlra rvtdafgnal ggqtvsvmad
      361 ngattaptvi tepdgtveis vtsrtagisa vtatinnssl srnvtfvadv rtakiadlvv
      421 tqdgsvadgs tantlrarvt dafgnalggq tvsvmadnga ttaptvitep dgtveisvts
      481 rtagistvta tinssslsrn vtfvadvrta qiadlvvikd gseadgatan tlrarvtdaf
      541 gnalagqtvs vmadngatta ptvitepdgt veisvtsrta gistvtatin sssqsqnvtf
      601 iadirtaqia slevtqdnsv adgtmantlr vkitdafgnt lggqtvsvla dngattaptv
      661 ttqpddtvei svtsqtagts avtasinsst asrnvtfvad vrtakiadlv vikdgseadg
      721 atantlrarv tdafgnalag qtvsvsagns atvapavite pdgtvdisvt sqtagistvt
      781 atinnhslsq svmfiadvrt aqiadlvvik dgseadgata ntlrarvtda fgnalagqtv
      841 svsagnsatt aptvitepdg tveisvtsrt agistvtati nsssqsqnvt fiadirtaqi
      901 adlvvikdgs eadgstantl rarvtdafgn alagqmvsvl agngattapt vttqpdgtve
      961 isvtsqtagi savtasinns sqsrnvtfia dvstaqiasl evtqdnavad gatantlrar
     1021 vtdafgnala gqtvsv
//
LOCUS       WP_181882586             326 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tRNA dihydrouridine synthase [unclassified
            Helicobacter].
ACCESSION   WP_181882586
VERSION     WP_181882586.1
KEYWORDS    RefSeq.
SOURCE      unclassified Helicobacter
  ORGANISM  unclassified Helicobacter
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 326)
  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 326)
  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..326
                     /organism="unclassified Helicobacter"
                     /db_xref="taxon:2593540"
     Protein         1..326
                     /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=36232
     Region          7..303
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mnfenllmla pmagytdlpf ramvkkfgvd isvsemissh alvfnnqktl kmiekdsies
       61 pfsvqisgsk qevlqravei lnekngidii dlncgcpapk vanhgngsgl lkdlnllvkc
      121 anlikqtsnk pytslklrlg fdkkiplela saindtnvdf vvvhgrtrad gykkeridyd
      181 sialikkhik ipliangeia saqvarnvre rtgangvmig raaikapwvf wqiknntdsl
      241 pslvlknlvl ehfdkmisfy gergvvmfrk nlhayskgln gahefrnvvn smtesaqara
      301 kieefftqdv qlsefpqlvt lnkrts
//
LOCUS       WP_181883595             713 aa            linear   BCT 28-DEC-2024
DEFINITION  GumC family protein [Sphingorhabdus pulchriflava].
ACCESSION   WP_181883595
VERSION     WP_181883595.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus pulchriflava
  ORGANISM  Sphingorhabdus pulchriflava
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 713)
  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 713)
  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 713)
  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..713
                     /organism="Sphingorhabdus pulchriflava"
                     /db_xref="taxon:2292257"
     Protein         1..713
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=77409
     Region          27..711
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mtesnqlvpv tpasagppst rhetflpata drldltesva ffrrrftlil gvlalcliag
       61 layamlapki ytakatvmlt dnaaekiraa drpesrqvls nelvdtqvei itsrtmaerv
      121 agalgmgrgl nsdalrnvid elerevsaer tgnsyalais ysateaeasa tianefarqf
      181 agwelrsnke nhaesltlvq qrlgelraqa qadttalqqy riannllsts gaslteqeis
      241 nynqevagar aaaaedearl qtalaqlrsg ssgddvgeal gstvisslra qeaeaageva
      301 nlgskyganh pqliqaqsrl vevraqiqae igrvisnlra krdvsqqrma slsgslasar
      361 gqltqnnsam vglsdleraa gasqgiyeay lnrykellaa egserpnaki ltlasvpawp
      421 espnipmtii lslvvglglg viaayiaeai fhgvstpdel erasggnylt sipllksvep
      481 kirhavtamq hspnsgfaes fraldtaisq athgrnqvia itsalpdegk tvvscclsyv
      541 laqsgkktil idcdlrragm srlldmrehd hglieyldgk tdinfddlsd qrifcvlplr
      601 psneqpdhll tgdafirlld elrtrfdhii ldlppvlpia stpilasrad atvmttrwrk
      661 tsrfalraal krlpadqvnl vglalnqvdm rrrayfergd psfyykqyrd yys
//
LOCUS       WP_181883544             250 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Sphingorhabdus pulchriflava].
ACCESSION   WP_181883544
VERSION     WP_181883544.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus pulchriflava
  ORGANISM  Sphingorhabdus pulchriflava
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
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="Sphingorhabdus pulchriflava"
                     /db_xref="taxon:2292257"
     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=26757
     Region          12..235
                     /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 mqllaslgsp tlamlaavvg aiigsyigvl vlrwpagept vsgrsrcdtc qrqlawfdlv
       61 plfsflilrg rcryckavid pvqafaewag ailcglafhl lpiesaavca llflmllpla
      121 lldarhfwlp drlvialall glllggipsg gveltmrlla aalafvales lrrlfrnvrg
      181 regmgagdpk lfaalalwls pydmpllili astlgialal ftvarrrsmq qmpfgsllaa
      241 avvvlvlvrl
//
LOCUS       WP_181883700             335 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Sphingorhabdus
            pulchriflava].
ACCESSION   WP_181883700
VERSION     WP_181883700.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus pulchriflava
  ORGANISM  Sphingorhabdus pulchriflava
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 335)
  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 335)
  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..335
                     /organism="Sphingorhabdus pulchriflava"
                     /db_xref="taxon:2292257"
     Protein         1..335
                     /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=37403
     Region          136..234
                     /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 mtefiytrpe tctacgaglh lwrqnvrdgv ygvdgiwnlh rcnnsecaas yldarlsasq
       61 lagfyetyst hhdpvfaang tklifrqale wlfhrrlgyr rpktstllat larffelvpl
      121 lremalsrvf wlpyvaggkl veigfgnaqt llqmrelgwe vegvefdemc irkaralgfn
      181 vkqgdfesqd ypdgsmnavv gshviehvpd pgklmatiyn klqpggrmvl vtpngaswgc
      241 rlmgaywrgl evprhltiqt psslirharr agfkkielsg tplgggilqq slrlrlgkpi
      301 ngsgrlpqlf waslasmihl lrpqasdeiv micek
//
LOCUS       WP_181883677             376 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Sphingorhabdus
            pulchriflava].
ACCESSION   WP_181883677
VERSION     WP_181883677.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus pulchriflava
  ORGANISM  Sphingorhabdus pulchriflava
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
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="Sphingorhabdus pulchriflava"
                     /db_xref="taxon:2292257"
     Protein         1..376
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40090
     Region          42..356
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mivakaaial aiaalafapi assaepvlpr pavvridfds skilasradg eagvrgravs
       61 andpvrvasi sklvtaiavm rlvdqgridl drdiseylgf qirnpafpdq ditlrhlmth
      121 tsgvrdkidy lipldgqvea vmtnaaawds khrpgiyfsy anlnspiiaa tieaatgerf
      181 dklvaktvla plkidacfnw gagcspgrra qavtllrtng dlardaaikg sdpcpvlaaa
      241 dgscdlrryp lgrngssfsp qgglrisadd lakvgqlmln ggrpllsska faemtrlqwr
      301 fngvngdddr gyfkayglgv hihedsagal wighvgeaya lraglwvnpe trkgfaqyvt
      361 mvpaetpigh cletcp
//
LOCUS       WP_181883775             379 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Alteriqipengyuania
            lutimaris].
ACCESSION   WP_181883775
VERSION     WP_181883775.1
KEYWORDS    RefSeq.
SOURCE      Alteriqipengyuania lutimaris
  ORGANISM  Alteriqipengyuania lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Alteriqipengyuania.
REFERENCE   1  (residues 1 to 379)
  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..379
                     /organism="Alteriqipengyuania lutimaris"
                     /db_xref="taxon:1538146"
     Protein         1..379
                     /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=41680
     Region          24..338
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mtmhqtidpa qpqperqiap vratrlqfmv eddkamlraa rdltkdlgta kpavywadml
       61 lsaglgyaai atailagnla iqilaglvga lafyraemfi helthihkka lrgfrtgwnl
      121 lvgiplltps fmyegvhtih hkrtqygtve dpeylplalm kpwslplfvl vallapvall
      181 frfavlvplg avipavrrft wqrlsslsin pefrrkapeg afakrvrwqe agacvwaial
      241 lasplafgwr pllialails ltallnqlrt lvahlweneg eamtvtaqfl dsvnvpppgi
      301 vaevwapvgl ryhalhhlmp smpyhdlpea hrrlarelgm gstydganhp gllvlvgria
      361 rstmlkrtnv epsegnsag
//
LOCUS       WP_181883863             322 aa            linear   BCT 28-DEC-2024
DEFINITION  prolyl hydroxylase family protein [Alteriqipengyuania lutimaris].
ACCESSION   WP_181883863
VERSION     WP_181883863.1
KEYWORDS    RefSeq.
SOURCE      Alteriqipengyuania lutimaris
  ORGANISM  Alteriqipengyuania lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Alteriqipengyuania.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10653727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Alteriqipengyuania lutimaris"
                     /db_xref="taxon:1538146"
     Protein         1..322
                     /product="prolyl hydroxylase family protein"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=35729
     Region          <28..92
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          49..78
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          143..308
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
ORIGIN      
        1 maedvrhltd seqldravta lrsqlaegng eaafilaywr vegisirrdl deatalfrra
       61 velgyeaarg plaamlahgy gqsrrdwqga lqqlasyrep tatrharlid amqldpegnp
      121 grsfspeilc rdplvlvfre fltrrecksl velaspalrr sqvvhpqtgq lvddpirnss
      181 saaftlteet pflhainrri aaasrsrpeq geptqvlsye agqeyklhhd alpgeqnqri
      241 qtfliylned yeggeihfpt pnlrfrgntg dalcfsnvsa nmqparnaah aglpvvagrk
      301 iilskwirrs pldltgpagl py
//
LOCUS       WP_181883782             174 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Alteriqipengyuania
            lutimaris].
ACCESSION   WP_181883782
VERSION     WP_181883782.1
KEYWORDS    RefSeq.
SOURCE      Alteriqipengyuania lutimaris
  ORGANISM  Alteriqipengyuania lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Alteriqipengyuania.
REFERENCE   1  (residues 1 to 174)
  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 174)
  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 174)
  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..174
                     /organism="Alteriqipengyuania lutimaris"
                     /db_xref="taxon:1538146"
     Protein         1..174
                     /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=19103
     Region          5..151
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mddpdpwdfe nsayerdkra atiaalqgar fpnaleigca tgflsrdlaa hcdallaldv
       61 seqalaiars ksvtndtvly rraeaprdwp egsfdlivls evlyflstee iaivsrrahe
      121 tlvanglcll vnwtgpndla vggeeaarlf agsarwrgek priepsyrid rllk
//
LOCUS       WP_181882837             385 aa            linear   BCT 28-DEC-2024
DEFINITION  pseudouridine synthase family protein [Helicobacter sp. MIT
            01-3238].
ACCESSION   WP_181882837
VERSION     WP_181882837.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter sp. MIT 01-3238
  ORGANISM  Helicobacter sp. MIT 01-3238
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 385)
  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 385)
  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 385)
  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..385
                     /organism="Helicobacter sp. MIT 01-3238"
                     /db_xref="taxon:398627"
     Protein         1..385
                     /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=43428
     Region          85..282
                     /region_name="PseudoU_synth_RluA_like"
                     /note="Pseudouridine synthase, RluA family; cd02869"
                     /db_xref="CDD:211346"
     Site            order(123..126,265)
                     /site_type="active"
                     /db_xref="CDD:211346"
ORIGIN      
        1 mpfirsqyfv dsptkatkfl tqtlgftpsl aqktidkarl rigidarqia qksdilqgiv
       61 wlthfsphyy easelvkpif ctqdfalfdk ppkllthpkg nflhksllds irffcgyeaq
      121 sihrldfets gailiakhkk aqialktalm nrkihkcyla kvrgeiknec linapiitpt
      181 rtqksqnlsi rskidyaale snatepstle sstlessale sntlqsttke kssksaitrv
      241 vpiyfdgkht fikafpltgr thqirlhlah ighaiendfl ygvsdevser yldelrvira
      301 estthanidt ksttmpneks nakskvrvds kkifhtnddl sensnenfgd fadkvlalhs
      361 fgvdfcyegv ryvlstkvps wwqar
//
LOCUS       WP_181883900             261 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Alteriqipengyuania lutimaris].
ACCESSION   WP_181883900
VERSION     WP_181883900.1
KEYWORDS    RefSeq.
SOURCE      Alteriqipengyuania lutimaris
  ORGANISM  Alteriqipengyuania lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Alteriqipengyuania.
REFERENCE   1  (residues 1 to 261)
  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 261)
  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 261)
  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..261
                     /organism="Alteriqipengyuania lutimaris"
                     /db_xref="taxon:1538146"
     Protein         1..261
                     /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=28316
     Region          15..206
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
ORIGIN      
        1 maegqaqdtr dvgipaatvv ifrnapdgga philmqvrsr alafaggmav fpggrvdaad
       61 halaqttgtp dpdeaahria airetleetg lalglrgaid atrakearal llkegtlaav
      121 ldrfdwslap edlvpfarwy pknerlprlf dtrfyladlg tgavdievda qentclfwts
      181 ardalanadr geievifptr rnlerlaqfe tfadarahae ttpvrtivpw ieerlegrsl
      241 cipddcgypv tsvplddakr g
//
LOCUS       WP_181884197             141 aa            linear   BCT 28-DEC-2024
DEFINITION  YdeI/OmpD-associated family protein [Bacteroides fragilis].
ACCESSION   WP_181884197
VERSION     WP_181884197.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 141)
  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..141
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..141
                     /product="YdeI/OmpD-associated family protein"
                     /calculated_mol_wt=16754
     Region          4..>111
                     /region_name="YdeI"
                     /note="Uncharacterized conserved protein YdeI,
                     YjbR/CyaY-like superfamily, DUF1801 family [Function
                     unknown]; COG4430"
                     /db_xref="CDD:443542"
ORIGIN      
        1 meiinlldft drnelrnwlk anhnqakscw vitsrskqpt ykcipyievv eealcfgwid
       61 stikklpdgr laqrlsprrk rshwtelnke rcmnledrgl mtdagrqafe rtysyeivrk
      121 dslieeiikk hnqelrpdly k
//
LOCUS       WP_181884295             427 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Aeromonas veronii].
ACCESSION   WP_181884295
VERSION     WP_181884295.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
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   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..427
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     Protein         1..427
                     /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=49094
     Region          37..408
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mplfdsliyl eagnpqvnqy lanlslndvp daglvyelav dwlleqrnse nnyktyrsel
       61 ttflhwcfre aaispkdltr rimiryldyc qsppdeliay rnvaqfildk ewgerlpnpq
      121 wrpflgkrel grtlpyrlse qamktklail saffqfliqe eymdrnpall lqrvkrpqqq
      181 eaddqvhafs elqwsyvmqa adtlandhpe qhersrflti lmyacylris evaarpgftp
      241 vmgqfrrdrk tgvwgyfipq skggkrrtva vsqallaale ryrrflglsp lptpdeqtpl
      301 fvrhkaaahg reqgelnanl girqlrdlim viigkgaela eqdgfvqdaa emrqlsphai
      361 rhtgithdin lhgrplshvq adaghdsidt tskylhtsns erhesaqqkp ldrlsnevrd
      421 ditkdsr
//
LOCUS       WP_181884542             201 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Neobacillus
            piezotolerans].
ACCESSION   WP_181884542
VERSION     WP_181884542.1
KEYWORDS    RefSeq.
SOURCE      Neobacillus piezotolerans
  ORGANISM  Neobacillus piezotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Neobacillus.
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="Neobacillus piezotolerans"
                     /db_xref="taxon:2259171"
     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=22468
     Region          17..176
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mkrfakqfrv pggflgkiag kimyfenkki nkwtidnlsl tngqtvleig fgpgyaigli
       61 aercpdctie gidlstkmke etankhehll nagklklwrg diadfnfpse kydrifsvnn
      121 fplwknpqet larfpyalkn ggkvaitvqp reegdtnhta relgeqlehg lkeaglenic
      181 isfkndhpvl avcataekph r
//
LOCUS       WP_181884651             250 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Neobacillus piezotolerans].
ACCESSION   WP_181884651
VERSION     WP_181884651.1
KEYWORDS    RefSeq.
SOURCE      Neobacillus piezotolerans
  ORGANISM  Neobacillus piezotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Neobacillus.
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="Neobacillus piezotolerans"
                     /db_xref="taxon:2259171"
     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=27633
     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 mvlitcllfl ygitlgsffn vvglrvpegq sivkprsacp ncrqhlrard lvpvfsyvil
       61 rgkcrgcgtr ispvypitel ltgvlfalap ivlgwswelv vtwtlislfm iifvsdihym
      121 iipdkvllvf agiflferll wpltpwwdsl lgaavgfvll llialvskgg mgggdiklfa
      181 vigfavgtkl vllsflfatl cgavfgvigl mlrlvkrrqp ipfgpfiglg slvayfygpk
      241 iidwyftffy
//
LOCUS       WP_181884758             922 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Arthrobacter sp. RT-1].
ACCESSION   WP_181884758
VERSION     WP_181884758.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. RT-1
  ORGANISM  Arthrobacter sp. RT-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 922)
  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..922
                     /organism="Arthrobacter sp. RT-1"
                     /db_xref="taxon:2292263"
     Protein         1..922
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=99951
     Region          55..899
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Region          725..751
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(727..728,731..732,734,764,767..768,771..772,
                     774..775,804,807..808,811..812,815)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          762..798
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          803..829
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrslleparp kgsasqrlas rpggyllavv ddeldllqfr rqvaagarav qagnlaggar
       61 hlrqavelfn gpafpdladi elmaadldgl eesrldayqd lfdielalgr haaligelqr
      121 lvpqhpfrer lwaslvlaly rsdrqadala acrearetft telgidlgvr lreletlvlr
      181 qdpslntpav qgqrrsrqrl dnlpaaltpl vgrenelgev cslyrsedcr lvtvtgaggt
      241 gktrlalaaa arlrermadg vgwvnlaplt qvqqvpgaia stlgleagag ddplkiasrf
      301 lhrrrlllvl dnfehledaw pvvldmltaa pelrilttsr rrlglrpeye felaplelps
      361 lepplpprql revpavkllv nrgrsvrphf dvndgntvvv trlchrldgl plaielaaaq
      421 lrrlderall aelevslaam paafrdlpdr qrtltatmew syqllpdaer llfdrigvfa
      481 gdptvtaiga vcgqtsakpl svddvlsala ahslvrrysd yagrqrvsvl hsirefarnr
      541 llllndaadv rrrhaehyls laealgpqlw grdqveafrt lhsdapdlra allwaagpdg
      601 stelalrlvg qlwhyweitg dvaeqqgiav alveaapdap pelrgpalsg aatlcwalgr
      661 ydqaanlhgl alqafretsn spaaawtmmc lavqaaysgk tskarqlsad vlaapdaslr
      721 trisvlvlls rlaffegdhq qaldlsrrcv evgrpigdrs llgvvltnla ecaeqscdyd
      781 aaerllheav daslelsaqs nlvavlesla gvyaaqnrld pairllaaan ayrlehgrpl
      841 dgeeakrvea itararaeag pirfglawag graltvtqaa nelvqggrgr ggintapaes
      901 tepipashtq saaddpadpa pw
//
LOCUS       WP_181884667             755 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-glucosidase [Neobacillus piezotolerans].
ACCESSION   WP_181884667
VERSION     WP_181884667.1
KEYWORDS    RefSeq.
SOURCE      Neobacillus piezotolerans
  ORGANISM  Neobacillus piezotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Neobacillus.
REFERENCE   1  (residues 1 to 755)
  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 755)
  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 755)
  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 755)
  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 755)
  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..755
                     /organism="Neobacillus piezotolerans"
                     /db_xref="taxon:2259171"
     Protein         1..755
                     /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=82678
     Region          18..>385
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          106..698
                     /region_name="PRK15098"
                     /note="beta-glucosidase BglX"
                     /db_xref="CDD:185053"
ORIGIN      
        1 mntklsaekr tellldamti eqkmqqivis rfnenntget vvinrrgssk ymngvfepqg
       61 tlpgcewqdt grqirgidel giptirmtng gtgvkggsch ndplatglps tlamaatfnr
      121 klnneagril gqetrafahh vmlgpgmnlv rhpyngrnye yfsedpyltg tlatqqvkgi
      181 qgqgvqvqlk hlagneqete rwtmgvqvps ramnelymlp femaakdanp asvmcsfpdv
      241 ngtfacdsse llqdalrkkw gfkgyvmsdr raihntvsai kagtnveldw apqyytqaki
      301 kkaldsgqit endidnllrp ryikmiefgh mdkpfskflp eivdakvnga sarkmaeega
      361 vllknengfl pldgkpksia ligvdwfagi akmsprsirv nnenvvtpyt vtpkqglenv
      421 ikelgyntkv tyndgrdpqa aaklasqsdi vllmvgdtpg etidrqtlgf painqvkqep
      481 lidavlkana kntavilkts gtvlmpwlnq vpavleawyp gmedgnavan llygkvnpsg
      541 klpmtfgaka reaafatekq ypgtrqdtgk pggpgpygng sqqliaqyte glkmgyrwye
      601 annvkpvfpf gyglsyttfk ydglkvkrvr gnkgslsgid vsftvtntgk vagkeaaqvy
      661 ltlpneagep skrlvnfekv dlkpgerktv tlrineadsn hpfsyfipke pdnlanwadg
      721 vwatadgkyr vhvggssadt plakdiplnf klgkk
//
LOCUS       WP_181884894             655 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Arthrobacter sp. RT-1].
ACCESSION   WP_181884894
VERSION     WP_181884894.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. RT-1
  ORGANISM  Arthrobacter sp. RT-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 655)
  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..655
                     /organism="Arthrobacter sp. RT-1"
                     /db_xref="taxon:2292263"
     Protein         1..655
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=69811
     Region          74..252
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
     Region          368..646
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mraddssaih agggpsagar sagrlmamld sgisaaelet tlsawlddga idqstaaaar
       61 rlnarlweas rregllrvly dtatdltrir dveavlkaiv rrtrsligsd iaylslndyd
      121 sgesyvrvtd gattalfrni rmplgegvlg avatgeapaq sadylldetk shlessdrav
      181 aaegvraimg vplraegkvi gallvadrhp hqfssddval mesigthaav alenaryfse
      241 mahalarldq aqqqnlahvr dleelssldr rlmetlastg slphllslla eslgapvflv
      301 spmgeplagi aadsdftslp alsaaeesva tssavqfevt grkytamsav agdqhlatli
      361 vaeqlstarl avlersalvl svsllfertf qdaqyrlqle liddllsprs ehaealsrra
      421 gqfglanhlq lvvrvvgvad dqrqralsvl rlraegtpgi ialheshlci iepfdrrtar
      481 adgtggagdn grsiieelkr rritasvgts epvtgfagls aahteahtvl ralqalsrdg
      541 eaadraalgt agmllgamds pfagqlltaq lgpllgyder rgtqlvltaw mfqekggamq
      601 etadalhihp ntlrqrldri daligatwrr gsrsldvqva lrlwrmktsg vtsga
//
LOCUS       WP_181884936             380 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Bacteroides ovatus].
ACCESSION   WP_181884936
VERSION     WP_181884936.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 380)
  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 380)
  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 380)
  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 380)
  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 380)
  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 380)
  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 380)
  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..380
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..380
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43866
     Region          17..380
                     /region_name="COG1672"
                     /note="Predicted ATPase, archaeal AAA+ ATPase superfamily
                     [General function prediction only]"
                     /db_xref="CDD:441278"
ORIGIN      
        1 mnmetpflyg riaenenftn rrneteflkk nfkglintvi isprrwgkts lvhkvaklis
       61 eeeknviicq vdifncrtee efytvfansl lkstttvwee fvggvkkylg rlapivsisd
      121 atqtyelsfg idfkdsrlsy deildlpqvi andtkkrivv cidefqnine yeeplafqrk
      181 lrshwqkhts vcyclygskr hmllnifnny smpfykfgdi lflskiehae wvtfiserfa
      241 dtgkqistel agliadkmkn hpyytqqlsq qvwfrtpdsg ctkeiveeaf ssliaqlsll
      301 fanvvdsltp kqinfllava dsvsnfsske vltkyklgts aniknlrkat lekdlidvlp
      361 gniieiqdpa feywvkyvyr
//
LOCUS       WP_181885030             243 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Pontibacter diazotrophicus].
ACCESSION   WP_181885030
VERSION     WP_181885030.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter diazotrophicus
  ORGANISM  Pontibacter diazotrophicus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   ter Beek,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 243)
  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 243)
  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..243
                     /organism="Pontibacter diazotrophicus"
                     /db_xref="taxon:1400979"
     Protein         1..243
                     /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=25811
     Region          1..243
                     /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 mlqhfgkyll fmssllfrge sprilfnrtm deailigins ifivaivstf igavtsvqis
       61 ynldnafipr stigfmvrem tllelaptit sivlagkvgs siagglgtmq iteqvdalev
      121 mginstsylv lpkviaailv fpmlvilamf lsigggfiag vlsgeitqqe yisgirsdfi
      181 pynilfalik svvfaflvss issfkgyyts ggalevgkas tgavtnsvia iliadfvlan
      241 lll
//
LOCUS       WP_181885199             158 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Pontibacter
            diazotrophicus].
ACCESSION   WP_181885199
VERSION     WP_181885199.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter diazotrophicus
  ORGANISM  Pontibacter diazotrophicus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Pontibacter diazotrophicus"
                     /db_xref="taxon:1400979"
     Protein         1..158
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18147
     Region          27..158
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkqllfvvsl alsfsahcqd slvgisdapl vtlegdtltr dhltgkvlvl nfwfiacgpc
       61 rqeipaldkl rtkyidnkdv tfiaissmde fdkiryfvsr rpfgyehatk nrewlnfykv
      121 vvfptnivid ktgkmtfrqk gympdiftel dreiqksl
//
LOCUS       WP_181885240             126 aa            linear   BCT 28-DEC-2024
DEFINITION  group I truncated hemoglobin [Pontibacter diazotrophicus].
ACCESSION   WP_181885240
VERSION     WP_181885240.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter diazotrophicus
  ORGANISM  Pontibacter diazotrophicus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 126)
  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 126)
  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 126)
  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 126)
  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 126)
  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..126
                     /organism="Pontibacter diazotrophicus"
                     /db_xref="taxon:1400979"
     Protein         1..126
                     /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=14097
     Region          14..124
                     /region_name="TrHb1_N"
                     /note="truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 1 (N); cd00454"
                     /db_xref="CDD:381253"
     Site            order(16,21..22,25..26,29,59..60,63,92,95,99,102,113,116)
                     /site_type="other"
                     /note="apolar tunnel"
                     /db_xref="CDD:381253"
     Site            order(30,39,42..43,46,50..51,54..55,57..59,61,69,71..74,
                     77..78,81,83,87..88,91,116,119,123)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381253"
     Site            order(32,35..36,94,97,101..103)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381253"
ORIGIN      
        1 metvkepqti tlyerlggae giasiandsv dqhlknpvvs trykysdiak vksmafefma
       61 mgtggpqtyt grnmldthrg mniseqefme vvddilvald mnhidqkekd evlailyslr
      121 keivrv
//
LOCUS       WP_181885320             328 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Trinickia dinghuensis].
ACCESSION   WP_181885320
VERSION     WP_181885320.1
KEYWORDS    RefSeq.
SOURCE      Trinickia dinghuensis
  ORGANISM  Trinickia dinghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 328)
  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..328
                     /organism="Trinickia dinghuensis"
                     /db_xref="taxon:2291023"
     Protein         1..328
                     /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=35596
     Region          43..324
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mvnrrqmlim tgaalgaslt gfqdvmakel ghmspigfkv pigvvdshch ifnpekfpys
       61 pkrkytppsa tvqdlqrfha aihvhrtvfv qpsvygtdna clldalrqvg snargiavid
      121 rtfssqqldd lagagvvgvr inlevgkdrn ldlavtrleq tvetlrgkpf iiqiyaalpi
      181 ldelapriqv qphrvvidhf glakaaagpe qpgmsalval maskkafvkl sgpyqisakk
      241 pgyadtipig ralveaspdq viwgsdwpht ggssrpanak ptdiepfrde degrnftlvk
      301 dwapqeaqrh kllvdnatrl fgfskaaa
//
LOCUS       WP_181885321             295 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Trinickia dinghuensis].
ACCESSION   WP_181885321
VERSION     WP_181885321.1
KEYWORDS    RefSeq.
SOURCE      Trinickia dinghuensis
  ORGANISM  Trinickia dinghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
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="Trinickia dinghuensis"
                     /db_xref="taxon:2291023"
     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=32246
     Region          8..292
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mhlklppgsc dchvhlfdpe rfpyapkrsy tpgtvrvadl lafeerlgid rivlvqpsvy
       61 gtdnaamlag lrelgpdrar gvavidpkaa tigdlramhd qgvrgirlnl aanldrdhsa
      121 aleqlrhaad vvgqlgwaiq iyadvdvvas margieqlsv pvvldhfaga raanqpgqhd
      181 afdavialvr sgrtyvklsa pyraskqapd yadldpiavr liearpdrmv wasdwphtgs
      241 aaqrsgdlsq vepfrnidaa caldrlqtwt kdeplrrril venpmnlygf aaptr
//
LOCUS       WP_181885387             265 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF899 domain-containing protein [Trinickia dinghuensis].
ACCESSION   WP_181885387
VERSION     WP_181885387.1
KEYWORDS    RefSeq.
SOURCE      Trinickia dinghuensis
  ORGANISM  Trinickia dinghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 265)
  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 265)
  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 265)
  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 265)
  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 265)
  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 265)
  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..265
                     /organism="Trinickia dinghuensis"
                     /db_xref="taxon:2291023"
     Protein         1..265
                     /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=30140
     Region          17..235
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mttssgnerk dgqqptmrtp pvvspqawet arqqllvkek aqtrardala aerrrmpwma
       61 vesayvfegp sgktslldlf egrrqlivyr afyepgvfgw pdhgcrgcsm vadqvahvah
      121 lnardttlvf vsrapqadia rlkarmgwdi pwftltdnfd adfgvgewhg tnvfyrdgdr
      181 vfrtyfinnr gdeqmggtwn ylditplgrq evwedspegy pqtptykwwn whdsyvadap
      241 pdkkwvevsd ageaafrkqa tngqp
//
LOCUS       WP_181885689             298 aa            linear   BCT 28-DEC-2024
DEFINITION  cell division protein FtsX [Marnyiella aurantia].
ACCESSION   WP_181885689
VERSION     WP_181885689.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,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 298)
  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 298)
  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..298
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..298
                     /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=33555
     Region          9..289
                     /region_name="FtsX"
                     /note="Cell division protein FtsX [Cell cycle control,
                     cell division, chromosome partitioning]; COG2177"
                     /db_xref="CDD:441780"
ORIGIN      
        1 martvedfnk rrlrssnitv vvsialvlfl vglsglilin aqkysdylke qlvvnayfdq
       61 dydakdslkl asqeleavek ikalapvkka tyisrmqasr earvslgidt eklfdahifp
      121 ssveialkpe yvdpakvnda ikqistvpgi vdvknnsesq qiyenlnkil kwilafsilf
      181 lilaivlinn sirlkifskr fiiktmqlvg akrrfilmpf vkeaillgvl gavlgimalf
      241 gvwyyftsti qtpfvqdtnq fvllvglial igifitvlst ifatwrflrs niddlyyt
//
LOCUS       WP_181885725             244 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Marnyiella aurantia].
ACCESSION   WP_181885725
VERSION     WP_181885725.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 244)
  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 244)
  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..244
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..244
                     /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=27239
     Region          8..241
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mndtindlhs kienlkneis fknglisils hdsrsmfgnf lwltaaleqe titkedffkm
       61 lpqvksdaqk nlqtvqdsta wlktqygdfk ikpekiavig lfqhleekya gglkeknlsf
      121 rfqgdtsafi etdriliefv ldkilnnavk ysmpgqdiyl nviteeaqvi lsvtdsgtgm
      181 dekflaniyt ydnpvfqgta getgvglslk ivknfislmq gsieiissad kgttvslflp
      241 kmne
//
LOCUS       WP_181885757             634 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Marnyiella
            aurantia].
ACCESSION   WP_181885757
VERSION     WP_181885757.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 634)
  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 634)
  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 634)
  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 634)
  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..634
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..634
                     /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=70351
     Region          4..602
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkkrvifvga llvvsshams qqqdvtqide vtvaskvpqq lyktgknvkl ltqedlekfq
       61 gqnvaevlqq vagiqvsgsa nnaqepkfsk irggklgnil vlldgvplkd vtgndysatd
      121 lrllalenve sievlsgass vlygsnaaga vinirtqkns kktvegevsa rggsygtfaq
      181 naavrgnisg fnyqlsgfne ksdgfssaeg pgfdkdgfek qnasatvgyr gsrvsanmqa
      241 gwnhhifeyd agafadgmsr gddnqkfvga nadfkydkgq lvanlrytnt drtiqgyand
      301 ayrdeyfygg nnlfaelfnn ytisdrfsit agvqherqql gssslpwgss emqedlikad
      361 telyntdifa kasvnymdfh vdagsrmtnn skfgnhfvys vnpyylkesg smyyklgysf
      421 atafiaptly qtygtlpytt anfdlkpern sthevdlsvg nkdrsmvfna taflteekdv
      481 fayvtnpdft gnfvnvdenl ikgfelgfdy ritdqvklgg nysfvekeke atrlrvpknr
      541 vnsyidiapl agtrialthq fvskrtdyyf nenfervdvn ldayhllnln lnqklgksfe
      601 vfgnignlfn tsytdvvgft tkrrnytagf syrf
//
LOCUS       WP_181885860             207 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Marnyiella aurantia].
ACCESSION   WP_181885860
VERSION     WP_181885860.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     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: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=23699
     Region          47..146
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 menfdrkkhw eniyqtkelk dvswfqpkpd tsldffkqyn vpqtakvidi gggdsllpdh
       61 lltlgyedit vldiseaavy rakqrlgeqa dkvkwlvadv sdfnptvkyd fwhdraafhf
      121 ltdqdeinky vktaheninp ggimvigtfs elgpkkcsgi eirqytaesl sevfhdgfek
      181 iscftadhtt pfdtvqnfvf csfrkti
//
LOCUS       WP_181885880             409 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Marnyiella aurantia].
ACCESSION   WP_181885880
VERSION     WP_181885880.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   ter Beek,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 409)
  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 409)
  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..409
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..409
                     /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=45497
     Region          31..239
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          150..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 mkfplyfskk iafskdnknn lsriiifigr lsvalgiivs litvsvgfgs keaiklrmad
       61 fsghiniksk rsnssydssv ldrtgldlkk iranpdvata qnyvsvsgil rnehnfagvv
      121 mkgigkdfdh erfkkfivkg ntpkvtedgy nngvviseki asdlhlgvkd sivaifskqn
      181 qqplyrnfev igiyktdikm iddqfilgdi nharkildme kndvggidif lkdvndieke
      241 tpeidrsvgl knytekatek ypqivdwini fdnniaviiv imlsvviini vmvlliliie
      301 rtnsigllkt lgasngqirt lfiyytllim vpglifgnli gftllglqki fsiiklnpen
      361 yyistvpvdl nplipvvisa gillvsafam ifpsyliski spvksikyt
//
LOCUS       WP_181886039             734 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Marnyiella aurantia].
ACCESSION   WP_181886039
VERSION     WP_181886039.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 734)
  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 734)
  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 734)
  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 734)
  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 734)
  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..734
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..734
                     /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=84786
     Region          6..734
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mvydleqekq eilarykdli sntyrtldee qnklirkafd ialdahkdqr rksgepyiyh
       61 pievakivan eiglgatsia callhdvied seythedlek lfgekiakiv ngltkisimn
      121 hqnisiqsen yrkllltlse dfrvilikia drlhnmrtle smrpdkqkki asetvyiyap
      181 lahrlglyni kseledlslk ynnpevyaei dhklelaneq rhkyvdeftn evserlkeen
      241 lsftikgrak aissiyrkmv kqsvlfeevy dnyairiiyk sdarnekfla wkiysivtdl
      301 yhsnpqrmrd witqprstgy eslhltvlgp dkkwievqir sermddiaek gvaahykyke
      361 gyrpnsdekn fekwvttire vletqqhltt telldnikln lyskevfvft pqgeikilpv
      421 gstaldfafs vhsdlgtrcl gakvngklvp ishvlqngdq vdilssqnqk pksdwldfvv
      481 tskakskiks ylnstknhlv segkeilqrk lrhakiafnd eeinrmqkff nlktsqelfl
      541 ffqdgtldtg dlrkyiesks vfnnllnrfr kspvknlafe epaqtnldmi vfgkdeekln
      601 ytfakccnvi pgdkifgfit isegikihsd ncpnainlra qydyrvmeak wvnaesfknr
      661 ikieiegldr mgminditqv isnsmsidmk smtiasndgi ftgsinlevk nrsqleetfk
      721 qlknisgisk vqri
//
LOCUS       WP_181886164             462 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Marnyiella aurantia].
ACCESSION   WP_181886164
VERSION     WP_181886164.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 462)
  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 462)
  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..462
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..462
                     /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=53898
     Region          14..365
                     /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 mdnkenlqnk rigiigagps glaqirafea lkergenipe ivcfekqsnw ggmwnyswrt
       61 gvgkygepih gsmykylwsn gpkeclefsd ysfddhfeka issypprpvl fdyiegrikk
      121 snareyirfd ttvrwvsyde dtrkftivld dlkinktyse efdylvvasg hfstpnmpyf
      181 kgietfsgnv mhahdfrgad qfkdrnilli gssysaedig iqcykhgaas vtlsyrsnpi
      241 ghdwpqgike vplvthfdgd taffkdgtse dydavimctg yqhkfpflpd elrlktknnl
      301 ypdnlykgif ynnlpqliyl gmqdqyytfn mfdtqawlar dfmmerlelp segerrvdid
      361 twldrnsklq ssfddvdfqt yyikdllsft dyphfnldki aamfkewlqd keeniltyrd
      421 ktyqsvvtgt maeahhtdwm delddskery lygaeeeeli pe
//
LOCUS       WP_181885844             173 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Marnyiella aurantia].
ACCESSION   WP_181885844
VERSION     WP_181885844.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 173)
  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 173)
  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..173
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..173
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=18154
     Region          38..153
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mkiltaffil ffscsfaqrs aetqpspqar lvksvdhltl eaalelakns tekaaqlnkq
       61 vslavldtag nvillmrgdg vgihnteaar rkaytavstk tatltllrna ranpdtnnln
      121 tlpellllsg gvpiwyrgnv igslgvaggg spenddaiar aaaipekgil tsk
//
LOCUS       WP_181886655             247 aa            linear   BCT 28-DEC-2024
DEFINITION  shikimate dehydrogenase family protein [Marnyiella aurantia].
ACCESSION   WP_181886655
VERSION     WP_181886655.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 247)
  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 247)
  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 247)
  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..247
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..247
                     /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=27192
     Region          5..240
                     /region_name="AroE"
                     /note="Shikimate 5-dehydrogenase [Amino acid transport and
                     metabolism]; COG0169"
                     /db_xref="CDD:439939"
ORIGIN      
        1 msaekkygli grnisysfsk kyftekfrll qldnhsydiy elgeiseiee lcranglsgf
       61 nvtipykeei ipylnslsee avqigavntv vvcggktkgy ntdaagfekt llklkqenhq
      121 salilgngga akavkyvlrs hgipyetvyr kgnlnfdtlt aenvskhsii iqttpvgtfp
      181 nvndsvafpf ealspehlvi dliynppqta flseaaargs visngqlmle qqaekaweiw
      241 sstsdel
//
LOCUS       WP_181886703             195 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Marnyiella aurantia].
ACCESSION   WP_181886703
VERSION     WP_181886703.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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..195
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..195
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22884
     Region          33..190
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mlykillvlf gfcftpcfsq vekcnlesty fedlkrvdad avkclaknse kpntlffvfa
       61 rwcepcmwhl ptfmsiekey dvnlyvilid lensqmtela kdyvweryps akivvlkdfp
      121 krgkgkkykd finsitpprf ekiddmskyf vldnegdvvl vtswkdskgd pdwkddrpmv
      181 krlvlpllqk kmesl
//
LOCUS       WP_181885103             403 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Pontibacter diazotrophicus].
ACCESSION   WP_181885103
VERSION     WP_181885103.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter diazotrophicus
  ORGANISM  Pontibacter diazotrophicus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 403)
  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 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   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,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 403)
  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 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 11454872
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Pontibacter diazotrophicus"
                     /db_xref="taxon:1400979"
     Protein         1..403
                     /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=44567
     Region          11..388
                     /region_name="NarK"
                     /note="Nitrate/nitrite transporter NarK [Inorganic ion
                     transport and metabolism]; COG2223"
                     /db_xref="CDD:441825"
ORIGIN      
        1 mrtyylflke nagpvffgwl ltffssfgqt ffislfvpfi ldqfhfsksv fggyyavati
       61 iasffllqfg hrvdsrplrp ltiqtillll assimlglai hpamvfialv glrlggqgfm
      121 shislsvmsr yfsadrgkal sisamgypaa emvfplvagl llsywnwhva liitasflll
      181 ifipirklnl ealdvheeke evsgkakway fkqlvtekpf wvlippvfay sfvvtgifff
      241 qyvlanekgw plewyamcfs gyavvrllfl lyggiltdkl sasklfpyyl mpfvlgllal
      301 aiipgkiaal vfllftgvsa gtssivtsav iaelygtdrv gqvrslfsmi mvlstalapv
      361 vigflldqgt tvsqigfgca aalglvtins frirllkrqq vpv
//
LOCUS       WP_181886709             437 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Marnyiella aurantia].
ACCESSION   WP_181886709
VERSION     WP_181886709.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
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="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     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=49669
     Region          20..437
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkrrilsaaa vafvsmmlna qqikfeeykl pngmhvilhq dntapvvttg vmyhvgakde
       61 dpgrsgfahf fehllfegta nikrgdwfkv vssnggtnna ntsndrtyyy etfpsnneql
      121 glwmeaerlr sgvinqigvd tqrevvkeek rlrmdnqpyg nimtalqtnl fskhpyrwtt
      181 igsmedlnaa kleefqnfyk kyyvpnnavl vvagdinpeq tkkwiqeyyg sipkgtvypk
      241 nyakedpitt qkevtvtdkn iqlpayvfay rtpgakerda yilnmvsayl sagkssvlyk
      301 klvdeekkal qvqafsqgle dygifgffai pmgatskevl qkdidaeikk mqtsmiseed
      361 yqklqnqfen nfvnsnssiq giahslvhny mlmgdtnlin keidiyrgit rqdimnaakk
      421 ylspnqrvvl nyvpeak
//
LOCUS       WP_181886710             677 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Marnyiella aurantia].
ACCESSION   WP_181886710
VERSION     WP_181886710.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 677)
  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..677
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..677
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=73375
     Region          28..446
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkfnfkyiav aflisgmvsa qkidinkmpv agptpvinia qpktftlkng ltvmvvennk
       61 lprvsatism drppyyegni vgvsqimadq igegtakmsk dafnkrvdyl gaslnfssgg
      121 afanslskyf pevlgmmsda iinpkfsaee vekskermie glkteeksad aiasrvsnav
      181 iygkntsrge feteasikav tladvqntfk khyapdnayl vivgdvkfdd vkklveknfs
      241 gwkksntkya alepasnvat tqidivdvpt avqsvisvnn lhdlkmndsr yfagaianyi
      301 lggggearlf mnlreknaft ygaysslsts kyspmfsass svrnevtdka vkefmnelng
      361 iskvtpeela nakaklkgdf irslerpeti arfavstrtq nlpadfytny lksidkvtaa
      421 dvsnavkati lpnrsrifia gkaadisegl eklgypvkyy dnqanpvakp vakavdasit
      481 paavadkyia aigglanvqk vnfittnata kvqgmdlalk liqgkgaktf mdvqmmgntv
      541 qkivfdgksg ymeaqgqkmp lpaetaaema mdtelfpelt fakssdfava gieknngeda
      601 yvvkgknaty yystktglkt gevktqsgqt ipitwgdyke vagvkmpyaf tqniggmdve
      661 fkvnsyqinq ataadfk
//
LOCUS       WP_181886658             201 aa            linear   BCT 28-DEC-2024
DEFINITION  IMPACT family protein [Marnyiella aurantia].
ACCESSION   WP_181886658
VERSION     WP_181886658.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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..201
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..201
                     /product="IMPACT family protein"
                     /calculated_mol_wt=22572
     Region          2..200
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 msnsyntiek pvlniilkek gsrfigfawq vnseeeirkr leelkaehpk athhcyayrl
       61 gingekyran ddgepsgsag lpiynqllah gvtnillvav ryyggtklgv sglvraykdc
      121 akmtlaesti tvreleftie iefnfsqqnt vftvlnrygt kildfqsgds ctitaslklg
      181 hkksiseqls emqhiqftfr d
//
LOCUS       WP_181886766             726 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Marnyiella
            aurantia].
ACCESSION   WP_181886766
VERSION     WP_181886766.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 726)
  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 726)
  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 726)
  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 726)
  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..726
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..726
                     /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=83749
     Region          12..651
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mfysqkedtl rtqtieevvf qrkgnvtqdv tnvsinarqa gqiasvsggi egliktlpsv
       61 nsntelssqy mvrggnyden liyindieiy rpflirnsmq egmsiinpdm vstvnfsagg
      121 feakygdkms salniyyrep ekfeisgeas miggrlstgf atgnkkltal vsgryrntnl
      181 ilntlneetd fnprymdfqs flnyhispkf smsfigyysq ndyemipkak evefgsvnqp
      241 ikvsvfydgr eddryknmmg tfslnyrpne kwrilldnfa yqnrereyys iasayvlesf
      301 dpvtgdpvts ydvggqidha rndlmvrtyg tqlrtrfspn insnlevgfk fekenlrdlt
      361 newrlvdslg ysvprdqvlp gvldpssmel yyhiagdnav eptrmsayaq ysnkfywgrs
      421 rayfnagarv anwsfnketi fspraqfaik pdwesdmlfr vaggiyyqqp fykeikdldg
      481 sfnsdiksqr smqlilgndy efsmydrpfk lttelyykkm ddlipyfmdn vrirysgknn
      541 adgyaygidt rlfgefvpgi dswlsasyar tfenidgrgd iaratdqrfr faifyqdymp
      601 kfpkmrvnlt giyamglptg apimfdnngl psletrydyq ktlpsykrvd iglsyvfidp
      661 keknkswgfw enfeeltlgv qvfnafniyn tvanqwvtdv snnyiypvpv nltgrffnak
      721 lefrik
//
LOCUS       WP_181886814              94 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix domain-containing protein [Marnyiella
            aurantia].
ACCESSION   WP_181886814
VERSION     WP_181886814.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
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 10612879
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..94
                     /product="winged helix-turn-helix domain-containing
                     protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10562
     Region          13..92
                     /region_name="HTH_34"
                     /note="Winged helix DNA-binding domain; pfam13601"
                     /db_xref="CDD:463932"
ORIGIN      
        1 misklnkefe srvrlgimsv lmvndwvdft emknlleitd gnlashstal ekseyievkk
       61 efvgkkpkts yratetgkka fgehlsalek llgr
//
LOCUS       WP_181887018             250 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Marnyiella aurantia].
ACCESSION   WP_181887018
VERSION     WP_181887018.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
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="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     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=27071
     Region          1..249
                     /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 mikkfltafg eyflllgkai rtpqkmsvfi klffreindl gvnsfglvvf tsvfvgavta
       61 iqmfnnfsss sipiptpfig yatkavlvle fsptiislil agkvgsyias sigtmrvteq
      121 idaldimgvn spnflilpki lacviynpll iglsmavgim ggfaageltg nwtisdfttg
      181 vqmympmlfy yyafiktivf afiiasvpsf fgynvsggsl evgrsstqav vwtmvfiiis
      241 eliltqiilg
//
LOCUS       WP_181887036             421 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Marnyiella aurantia].
ACCESSION   WP_181887036
VERSION     WP_181887036.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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..421
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..421
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47399
     Region          56..387
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mrkgfwlglm clmllgsckk eleifqkepe thlpnfgnvk lnevfsrkds kqangdsida
       61 viqnyyntvw eggdlwggfl iakgddilfe gyrgfaqdnk qepitqstpl hvasisktit
      121 amavmklvea gklklddeit kyfpdlpypg vtvqslltqr sglpkyeyfi ekiepkpael
      181 skkyltnqdi lnlmirhkpe aarspntgfm ycntnfavla llvekvtatp fpaameqmvf
      241 kplkmknsfi fqekdtltas ksfynrgpkv ypydrldliy gdknvyttpr dllnfsramy
      301 aenflrkdlk dmvfepysne raginnygig frmkvydngn kltfhtgwwh gtnsvfahll
      361 gsnvtivaig nkfsrqpyta lslaalfdqy pievdrlknt lkkgsaassg seedsaging
      421 g
//
LOCUS       WP_181887093             682 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Marnyiella
            aurantia].
ACCESSION   WP_181887093
VERSION     WP_181887093.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 682)
  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 682)
  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 682)
  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 682)
  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..682
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..682
                     /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=76647
     Region          8..599
                     /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 mkpqflkils vliliaaifv arlsylqlft dryalnaant sikieyiipq rgvvfdrngk
       61 ilvgnqpaye isytqalmrp dfdtisfcal lgiskhefek kietlkkeky ysklvpmtfm
      121 knlsreevar iqeiifkypa fsivsrpqrq yevstsgnll gytnevgerd lkkdslyyrp
      181 gdfigksgve kayevqlrge kgmryiqkdi klrdigsyrd geldkeevtg kditltidyd
      241 lqrmaeemlv dkhgaivald psngeilvma tgpdidpnlf tgpqksrnly rmqmdtvynn
      301 rptfdrsiqa ayppgstfkl ltaaaamqmg vmdentifpc gggfnykglr ikghggadpl
      361 ipaiqvssnc hfsyaylaii nkypgdpsrg vdewkkimss fglgeflnnd lavgskgrip
      421 sgefyenrme ainkaigrgr vknwdplatg avfngmgqgd vlltplqman svvaivnrgw
      481 yytphivksi dgkpnpdprf rkkhqtlvnp khfdpiikgm eavvlngtar glkstdftql
      541 aktgtaqvpq gkdnsiyvma apadkprivv vavmehagfg stwagpastv iaekyltgdl
      601 krehlykkmv nasfmpeyrr qwisdlkrkg lyresdkdsi fmhqledsik tvkdsnrrae
      661 liykrdsika rmniakpknr tk
//
LOCUS       WP_181887109             232 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Marnyiella aurantia].
ACCESSION   WP_181887109
VERSION     WP_181887109.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 232)
  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 232)
  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 232)
  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 232)
  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 232)
  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 232)
  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..232
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..232
                     /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=24252
     Region          38..209
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mrnmkqkifk itaalaittv mlnscgpkdn pplvyfpdmy fpvaydplmk aedaysdhen
       61 eipafvkngg atgmipvdgt vmqnkdgvae ansasamtpd qynagyaesk gltasplnaa
      121 gqkknlergk ilydrtcaac hgtsgdgqgp ivqsgaysgv pkyadrdisv gsvhyvimhg
      181 rnamgsyagq lnagdrwrva myvmnafkgg mtpassgaaa gtaastdsta tq
//
LOCUS       WP_181887283             316 aa            linear   BCT 28-DEC-2024
DEFINITION  isopenicillin N synthase family dioxygenase [Marnyiella aurantia].
ACCESSION   WP_181887283
VERSION     WP_181887283.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..316
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..316
                     /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=35847
     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 mkqipsvdlr dflsgdperk qkfvneigka yeeigfvalk ghflddklvk dlysevknff
       61 empvekkqky eipgiggqrg yvgfgketak gfkkgdlkef whfgqyledg skyssvypdn
      121 vqvtevpefn evgkqaykml ektgiyvlra lalhlgldef yfdkfvkegn silrpihypp
      181 iteepdnavr aaahgdinli tllmgaqgkg lqvmnhdgew vdaiaepdel minvgdmlsr
      241 htnnklksti hqvvnpprel wgtsrysipf fmhpvsempl nalentvden hpklyedtta
      301 geflherlve lgliki
//
LOCUS       WP_181887345             145 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Marnyiella aurantia].
ACCESSION   WP_181887345
VERSION     WP_181887345.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
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="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     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=16811
     Region          14..122
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mkerntpsda ivnrqtvrvr fnecdplgiv whghyivyfe dgreafgreh gisyldvqhn
       61 gfatpivrtv cehflplkyg eiitvettfv nlptakmmfr yrifneenkl vcsgetvqvf
      121 idingnlqly npsfyqewkd kmgls
//
LOCUS       WP_181887361             160 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Marnyiella aurantia].
ACCESSION   WP_181887361
VERSION     WP_181887361.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 160)
  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..160
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..160
                     /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=18882
     Region          1..140
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mnkeistlvk vrfsdcdpig hlnnvkyley mmnaredhve tyygftyeey srrtgctwit
       61 vqneiaylre vrfnskvqis sktievrdri skveilmkse dgktvnavlw itviyfnmkt
      121 rksevhppet rglfeeflte vpektfaerv ayfrkqnkls
//
LOCUS       WP_181887478             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Marnyiella aurantia].
ACCESSION   WP_181887478
VERSION     WP_181887478.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
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="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     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=38563
     Region          6..331
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 masnknalir yktldrclrn tyrkytledl meecsealfe yegkesfvsr rtvqldlqnm
       61 rssrfgyeap ievfdrkyyr ysdpdysihk ievnssdlla mnnaiqilkq fkdfsmfkdm
      121 dgviqkleds vhsagqksvi hldkneqltg lefidplyqa iingqalril yqsfkardat
      181 yltvhpqllk eynnrwflic whknrmfnla ldrikevetd lkteyeykdf dadsyfadvv
      241 gvtvlesqrp qevvfkvdhs napyiktkpi hhsqqilsed ndgitfsirv qlnpelervi
      301 lgmgssltvi spaslrtril enlktavgny ge
//
LOCUS       WP_181887501             327 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Marnyiella aurantia].
ACCESSION   WP_181887501
VERSION     WP_181887501.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 327)
  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..327
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..327
                     /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=35399
     Region          25..322
                     /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 msnfidfgva ekmyresqnr isrlfnikyp ivqggmiwhs gwklasavsn cgglgligag
       61 smypdvlrdh irkcktatdr pfgvnvpmly pnldevidii leegveiift sagnprtyte
      121 tlkkeglkva hvvsstkfal kcqeagvdav vaegfeaggh ngrdetttlc lipnvrkhid
      181 ipliaaggia lgsqlkaami lgadgvqigs rfaatveasg heawkekitg lnegdtqltl
      241 kelapvrlvk nkffrdierl yetgrdteal tatlgrarak rgmfegdlee geleigqvsa
      301 videvlpvet vfahllkefe aagnptl
//
LOCUS       WP_181887508             209 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Marnyiella aurantia].
ACCESSION   WP_181887508
VERSION     WP_181887508.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 209)
  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 209)
  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..209
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..209
                     /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=23867
     Region          45..202
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mglyardlit riqqaelege nahavysppy rplfsyeeim nrapkfaavn ivlylkdnqw
       61 ffplivrstn erdrhsgqis lpggkkeesd rdfehtakre tseemgieqh ylrtiremsp
      121 iyippsnfyv rpfvsytrkn ptfilqetea veliefpvss llnlaeqptm avlpgsngve
      181 vpvisfngym iwgatsmils efstllkkl
//
LOCUS       WP_181887526             644 aa            linear   BCT 28-DEC-2024
DEFINITION  polysaccharide biosynthesis protein [Marnyiella aurantia].
ACCESSION   WP_181887526
VERSION     WP_181887526.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 644)
  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 644)
  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 644)
  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 644)
  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 644)
  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..644
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..644
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=73468
     Region          145..267
                     /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          309..594
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(313,315..318,338..339,365..367,388..390,392,407,430,
                     446,471..474,477..478)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(339,341,345,349,363..366,369,372,390..393,396,400,
                     403,406,478..479,484)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(392,432..434,442,472..473,479..481,484..485,
                     496..498,502,504,539,566,569)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(408,432,442,446)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 mklrrfgnki yggdtlinlt dirylprwvv lildlcfvaa avyfscyvie kltysvqsvf
       61 ygrnymyfli lgisvffmfi frtftgiirh stfidlfklf matfcttfsv gvgsflfylv
      121 tnerliymsi pfsaifftts fiflfifrla vkeffyyare yrrsaqrtri wvlgideqav
      181 avaravldnp nlpyhiagfl tqrndsaras llgkpiyskd kientskedl mldgilvvke
      241 mmskeelnqw vafflekdlq vykaptlqql rnndpdasik slqiedllnr kaikiendei
      301 ksrhfgkiil vtggagsigs eivrqvaqye palivvldqa etplyetele lrtnfpkvnf
      361 kfvladisnr hrleplfqky hfamvyhaaa ykhvplieen phesilvnvl gsknlaflss
      421 ryevnrfvmi stdkavnptn vmgaskrtae lyvqalqevd nnktkfittr fgnvlgsngs
      481 viphfkkqie kggpitithp divryfmtip eacelvmeag tmgnggeifv fdmgepvkil
      541 dlaermikls glepdldiki vftglrpgek lyeelltdgt ktlqthheki liskdaclpf
      601 dqidgltnlv ikaalrrdkv dvvrnlkniv pefisnnsvy eald
//
LOCUS       WP_181887553             374 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Marnyiella aurantia].
ACCESSION   WP_181887553
VERSION     WP_181887553.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 374)
  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..374
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..374
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41401
     Region          3..374
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mykiplfdln fdekeeqaal etiqskwist gpktaafeak fagmlsvkha ialsnctvsl
       61 hlalklvgve agdevicpsl tfvatvnair yvnavpvfgd vvsyenptis aedirkkitp
      121 ktkaiivmhy ggfacdmdti maiakehdlk viedachgpl aeykrrklgt igdvgcfsff
      181 snknistgeg gmlitnnddy aartkllrsh gmtsmsyera kghstaydvv elgynyrmdd
      241 ihssigivql dkiqadlekr aevrtaylna lndvsgiiip fadytdfnsn yifpivltdg
      301 daerrdaira qlaeagiqts mhypavhhfs iyqefaselp vtdflvdhli tlpmyskltv
      361 eqvnyisetl kkli
//
LOCUS       WP_181887707             143 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Marnyiella aurantia].
ACCESSION   WP_181887707
VERSION     WP_181887707.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 143)
  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..143
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..143
                     /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=15976
     Region          1..138
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mfskaceyai kaaiyvakqs lhkelvnvkq vaasvdapva ftakilqrmn rehilessrg
       61 kmggfvfdee kqksttiydi vilfdgpgvf tecglglrrc savnpcpvhe dfkvvrdklq
      121 vmtqkfsfyd lavrtengla wlr
//
LOCUS       WP_181887286             704 aa            linear   BCT 28-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Marnyiella
            aurantia].
ACCESSION   WP_181887286
VERSION     WP_181887286.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 704)
  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 704)
  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 704)
  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 704)
  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 704)
  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..704
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..704
                     /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=78938
     Region          28..698
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mkfrtimqsa avvflascan qkmnsshkyp etkkvshtdt yfgaqvadpy rwleddraed
       61 tndwvqrefk ftqdylskig freqirtqlk dlwnyekisa pfkegdftyf ykndglqaqs
      121 vlyrtdrsgk tevfldpnkf sekgttslag vsfnkkgnlv aysiseggsd wnkiiimnal
      181 tkeiidetiv dvkfsgaswl gdegffyssy dkpkgselsa qtdthkvyfh klgtkqsadk
      241 miiggesfkr rymgvgvsdd grfqilsase atngnelyik dpkkhkdfva vqkgydyntd
      301 fidskgdwiy altdrnapnm rlvkfhidrp dvwtdvipet envlsvstga gyifarymkd
      361 avtsvqqldy dgklirtvel pgigtaagfg gkddaaevyy sftnyitpgt iykfnpktgv
      421 sevyqkpkvk fdpanyvseq vfytskdgtk ipmminyrkg tkldgknpti lysyggfnis
      481 lqpafsvvna vwmdnggiya vpnirgggey gkkwhdagtk fqkknvfddf iaageylqqk
      541 gytspeymal sgrsnggllv gavmtmrpdl akvtfpgvgv ldmlrynkft agagwsydyg
      601 taedskemfe ylksyspvhn vrkgvcypst miitsdhddr vvpahsfkfg aelqekqscs
      661 npvlvrievn aghgagrstd qviaentdll sfalyemgir nikk
//
LOCUS       WP_181887819             301 aa            linear   BCT 28-DEC-2024
DEFINITION  transcription antitermination protein NusB [Marnyiella aurantia].
ACCESSION   WP_181887819
VERSION     WP_181887819.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002503
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..301
                     /product="transcription antitermination protein NusB"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_process="GO:0006353 - DNA-templated transcription
                     termination [Evidence IEA]"
                     /GO_process="GO:0031564 - transcription antitermination
                     [Evidence IEA]"
                     /calculated_mol_wt=36268
     Region          <204..300
                     /region_name="NusB"
                     /note="Transcription antitermination protein NusB
                     [Transcription]; COG0781"
                     /db_xref="CDD:440544"
ORIGIN      
        1 mlgrrqirek vvetlysyyq npikfdvlek nmlteiekiy hlyiyqlnfm valkelaemq
       61 ieigrkkylr tdaelhpnqr fvenlvlrki ednterrsft skhaelnwdm hddllvktfq
      121 riisgkryqd ymkeeeqsfe qdqkfvgklf lryiaenedf hehleekems wgddfhisns
      181 miqktigffk kdeeshtlir mikdhqdedf arrllkesln hweesekkle aklenwdldr
      241 valmdkiilv aaiteldrfp ltparviine yieiskvyat drsnifvngi ldkytkelnr
      301 i
//
LOCUS       WP_181887315             143 aa            linear   BCT 28-DEC-2024
DEFINITION  deoxycytidylate deaminase [Marnyiella aurantia].
ACCESSION   WP_181887315
VERSION     WP_181887315.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 143)
  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..143
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..143
                     /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=15774
     Region          5..138
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
ORIGIN      
        1 mtlnkfdiay lrmarewarl sychrkqvga livkdrmiis dgyngtpsgf dntcedgegk
       61 thwyvlhaea nailklaast nsakgatlyl tlspckecsk lvlqagisrl vyiseysdge
      121 giaflqnhgi eimqiaeeql dln
//
LOCUS       WP_181887823             557 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Marnyiella aurantia].
ACCESSION   WP_181887823
VERSION     WP_181887823.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 557)
  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 557)
  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..557
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..557
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=61633
     Region          29..298
                     /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          58..88
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          93..123
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          128..159
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(129,132..133,136..137,142,169,172..173,176..177,
                     179..180,208,211..212,215..216,219)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          167..202
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          207..235
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          214..542
                     /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          241..264
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          275..301
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          432..462
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          467..495
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          505..540
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mknnmklpqk avfavaaaff anftfgqtlq dgitsidshk yaqakqnfeq mvskspsaen
       61 yfylgntylt qnepdwatae qnfrkglaed sksylnrigl atiklgkgdk savaeiqniv
      121 kdsrekdaev lfragqaltl feknnnpela iqyldkaver amkggvpapy yytlgdayrl
      181 qltnspqvag kamsayekal plaknkasvy trmgtlwmqa nqwkmakeri tqaistdpty
      241 apayralagy emkfqqpqaa tqalvnyaky adedpgtqle isklyftnqd yansravldk
      301 vfnvvedpik yklrayldya dgkytqaqtd lntfintvtd ksriypadrg leglilagla
      361 kdekdaakks smmiesqqki aiaknakdet lnwdnellki qgggastaaa nagptnpaie
      421 alkkqtaanp ndadalvklg sayqeaqnwn gailtwdkmi alsptwaysy yakgaayqql
      481 gneamaessy qkfidtvltq kpeeqaaqke tlsyayylva yfnqtkdvak ardyaakavq
      541 lnpgyedavn lnanlnk
//
LOCUS       WP_181887711             234 aa            linear   BCT 28-DEC-2024
DEFINITION  RsmE family RNA methyltransferase [Marnyiella aurantia].
ACCESSION   WP_181887711
VERSION     WP_181887711.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 234)
  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..234
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..234
                     /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=26088
     Region          1..226
                     /region_name="RsmE"
                     /note="16S rRNA U1498 N3-methylase RsmE [Translation,
                     ribosomal structure and biogenesis]; COG1385"
                     /db_xref="CDD:440995"
ORIGIN      
        1 mklffgeifp evridedeqq hilkvlrmra gdeitltdgk gngacgrlil egkkvtlgnv
       61 kilsaappfs pllhiaiapt knidrteffv ekatemgise itfiltekse rrnlnfdkiq
      121 kqitaaskqs lrfhfpkvnn ltklsdfvqk qysehtfvah cdpafertel nqipslekit
      181 fmigpegdfs paeikmlaea gikavslggq rlrtetagtf vaawnygkmi legf
//
LOCUS       WP_181887827             201 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Marnyiella aurantia].
ACCESSION   WP_181887827
VERSION     WP_181887827.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..201
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..201
                     /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=22505
     Region          1..>72
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 marvkpkrhn irvdmtamtd vsfllltffi ltaqfakpdv etittpssis ekllpdaslm
       61 tilstpdgkf yftpvengse rmqlldnmge kygmkftdpe kaafsqvqai gvpmnqlkgf
      121 lnlpdedrka yksptgipmd sanaqlidwv qqslavnpdy klaikgdtqt kypkvkalfe
      181 glrdidflkf wlitsqetaq e
//
LOCUS       WP_181885943             852 aa            linear   BCT 28-DEC-2024
DEFINITION  copper-transporting P-type ATPase [Marnyiella aurantia].
ACCESSION   WP_181885943
VERSION     WP_181885943.1
KEYWORDS    RefSeq.
SOURCE      Marnyiella aurantia
  ORGANISM  Marnyiella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Marnyiella.
REFERENCE   1  (residues 1 to 852)
  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 852)
  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 852)
  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 852)
  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 852)
  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 852)
  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..852
                     /organism="Marnyiella aurantia"
                     /db_xref="taxon:2758037"
     Protein         1..852
                     /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=91849
     Region          22..52
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          145..172
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          191..843
                     /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(488,490,799)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(532..534,600,616..618,648,688..690,710,713,716,735,
                     738)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(800,828,832)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 menqhkkqnh ihpserisps svyycpmece gekvyfspgk rcpvcnmflv pieeradyrd
       61 kpqtfsktnl pesfsekvge yfcpmfcetd ktygsdvgcp vchmhlekit adllqnaags
      121 iidhnsantd hraestvpna gnagkyycpm fcegdklyds nvgcpvcgmd lvqipgaavg
      181 gedktyetlk kkfitslvft vpvfilsmgg mlisfpfshr vqailelllt lpvlfysgwf
      241 lmkrgwvsfk twnlnmfsli algiaaaflf slvalatpgi fphemthsgs iplyfeavcv
      301 iltlvilgql leagahkktg saikelmnls pdqatlmlng qetnvsladv kigdllkvkp
      361 gekipvdgkv tegassides misgepipve knegdrvnsg tingngvfim eaekvgdetl
      421 laqiikmvhd asrsrapiqk lvdkvsrvfv ptviaisvlt ficwliwgge nritmaflns
      481 vavlivacpc alglatpmsl mvgigkgakn gilirnaeal eqmqkvevli tdktgtlteg
      541 kpsvdgifav nkysreeilk faaalnsnse hplaaavlra hkdgqaaele atsvqhfeni
      601 agkglkaein sevvllgnaa llqqfgvtlp kqasdyaaeh qrqaktvsfl akgievlgvl
      661 sfsdrikpas pdavnylqqh gikvimltgd nehtaqavan elgiaehhga qlpgdklnyi
      721 kklqesgkvv amtgdginda palaqsdvgi amgtgtdvai esaeitllkg dilgvakari
      781 lseqllknir qnlffafvyn ifgipiaagl lypffgills pmiaaaamsl ssvsvilnsl
      841 rlnsvdinik ks
//
LOCUS       WP_181888039             574 aa            linear   BCT 28-DEC-2024
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Corynebacterium haematomassiliense].
ACCESSION   WP_181888039
VERSION     WP_181888039.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium haematomassiliense
  ORGANISM  Corynebacterium haematomassiliense
            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 haematomassiliense"
                     /db_xref="taxon:2754726"
     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=61297
     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 llpgktsaet
       61 ymnipaliev ahragadclh pgygflsena dfartveqag lkwigpspea iellgdklsa
      121 ralavevdap lapgtgepls tweeardfad ahgmpiaika afggggrglk vvfdeadiee
      181 gfasagreak eafgrgecyv ekflthprhv eaqvladahg nvavlgtrdc stqrrfqkli
      241 eeapapfltd eqrtaieega reiirtanyq sagtveyivs edgtvsflev ntrvqvehpv
      301 teaitgvdii aeqfriadgl plsfgdadpq ihghafefri naedvtngfa pspgtvtrfd
      361 vptgpgvrid tgvrtggqip pyydslmgkl vvwgpdrdta lkraqqalse fviegvrtvl
      421 pfhrdmvdap eitgdsldvy tdwvdhnysp sqkhsdvdie hiyderrdvv ieidgrlhti
      481 gfpvallggg aapaaadaaa psgdeagavt skyeativew lvadgdvvak gdaiatveam
      541 kmesqlkapr dgqislaaqq gervkanati atis
//
LOCUS       WP_181888142             361 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Corynebacterium
            haematomassiliense].
ACCESSION   WP_181888142
VERSION     WP_181888142.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium haematomassiliense
  ORGANISM  Corynebacterium haematomassiliense
            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 haematomassiliense"
                     /db_xref="taxon:2754726"
     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=37528
     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 mitrvsakpd vaedarrsai dsylkrgrrk sfaiagllva vvasfmfavv vgpidiavad
       61 vfhavfnper vdeqtlvvir tlrlpaavma vlcgaalgla ggqmqtildn plaepftlgi
      121 saaaafgaal sivmgwslva npqfnlaata alaaliavai vagasvwrga taesmillgi
      181 alsfffqall sllqyganve alqqivfwtm gsmqranwta niilavvlaa aipfcvanaw
      241 rltalrlgdd raaalgidvk rlrlatllva sflaaasvaf tgiigfiglv gphvarmlvg
      301 edqkfflpaa aaagamllsl ayavslsiip glaipigiit slvgvpffvf liftrarrkg
      361 a
//
LOCUS       WP_181888313             729 aa            linear   BCT 28-DEC-2024
DEFINITION  YhgE/Pip family protein [Corynebacterium haematomassiliense].
ACCESSION   WP_181888313
VERSION     WP_181888313.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium haematomassiliense
  ORGANISM  Corynebacterium haematomassiliense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Geller,B.L., Ivey,R.G., Trempy,J.E. and Hettinger-Smith,B.
  TITLE     Cloning of a chromosomal gene required for phage infection of
            Lactococcus lactis subsp. lactis C2
  JOURNAL   J Bacteriol 175 (17), 5510-5519 (1993)
   PUBMED   8366036
COMMENT     REFSEQ: This record represents a single, non-redundant, 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 :: TIGR03062.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Corynebacterium haematomassiliense"
                     /db_xref="taxon:2754726"
     Protein         1..729
                     /product="YhgE/Pip family protein"
                     /calculated_mol_wt=77656
     Region          11..>173
                     /region_name="YhgE"
                     /note="Uncharacterized membrane protein YhgE, phage
                     infection protein (PIP) family [Function unknown];
                     COG1511"
                     /db_xref="CDD:441120"
     Region          <281..>473
                     /region_name="PRK02224"
                     /note="DNA double-strand break repair Rad50 ATPase"
                     /db_xref="CDD:179385"
     Region          500..712
                     /region_name="ABC2_membrane"
                     /note="ABC-2 type transporter; cl21474"
                     /db_xref="CDD:473876"
ORIGIN      
        1 mrtvfsiayn dlrrlytnvm agivmvglia ipclfawfnv laawdpfgnt drlevavant
       61 drghtsdltp lavnvgdmvl sqlyrddsmd wvitdvddai egaksgeyya aivlpptlsd
      121 dmftfyadda epsridlyin ekknpispll issgtqgvsa qisasftral sevsfgliet
      181 tsdyfneaet kqaldsiatr tanardqlls santvdalas ltessvplvd saerisgalg
      241 dslgqvhpvd lgvtgaslgg dgaalaaalg atsvsfaavs ervdqllads satsqataas
      301 ltdiaaridv qvkqytalrd tingqvapal ppdaqpgvra vvghlndaia rqtavrdrln
      361 daaahltagq ggrdgknadr qeiedsiara reamdsakns ydtgirprle alsgsldnvr
      421 anvdkarsdm dgvssalanr pgslrdtlaa sgadlrdtae slranaarmq eakqsiaqar
      481 ssgdltklad lvsshpevla dalvdpvkve rkevfprvsf gagmaplytv lalwvgallt
      541 svavrtddrs ieqnvvdpdr ltagqkyfgr yltfvttgla qstllmagli vyvgiepahp
      601 fllymagwvs slvfhlicyt lvlslsnagk avgvlilvlq vsaaggaypl qllpgwtqai
      661 spwlpatysi ramraavfgt ygwdfwralg clvlfvlpfl flglwlrhrl hhaigrmdea
      721 vaqtkvmmt
//
LOCUS       WP_181888814             265 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: serine hydrolase domain-containing protein
            [Corynebacterium].
ACCESSION   WP_181888814
VERSION     WP_181888814.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
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"
                     /db_xref="taxon:1716"
     Protein         1..265
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28257
     Region          3..264
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 melekffsnw pvdnvaaalv gdteatfgdq dkvfelasvt kllsayavll aveegafeld
       61 daagppnsti rhllahaagv gfdsrepqke sgerriyssa gyeiladhve ettgiafady
      121 aregvfeplg mdsteiygsa ghggrstvgd lsafasells prlldpstlg eafsnqfgdl
      181 rgvvpgygmq kpcqwglgfe ikgekaphwt gdgmpadtvg hfgmagtylw vaggqacvvl
      241 tdrefgdwak plwqetntal wealg
//
LOCUS       WP_181888847             443 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Corynebacterium
            haematomassiliense].
ACCESSION   WP_181888847
VERSION     WP_181888847.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium haematomassiliense
  ORGANISM  Corynebacterium haematomassiliense
            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 haematomassiliense"
                     /db_xref="taxon:2754726"
     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=47702
     Region          1..441
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mqmtvigtgy lgathaacma elghevlgvd vdeskiealk nskvpfyepg lpevlernie
       61 agrlgfttdy aeaatfanvh figvgtpqqr gsyaadtryv eavidnlvpq legehlilgk
      121 stvpvgtaaa lqqradelaa ehgnkasvei awnpeflreg yavkdtiepd rivlghraen
      181 sraeeigrev yatplendtp fivtdlqtae lvkvsanafl atkisfinav sevcenvgad
      241 vtqladaigy ddrigrkflg aglgfgggcl pkdirafmar agevgadqal tflrevdain
      301 mrrrqrvidl areelgsvig rnitvlgaaf kpnsddvrds palavagqls lagasvrvyd
      361 pqgmdnarkv nptldyavsl edalrgtelv ilatewqefk emdpvwaael vdkqllidgr
      421 nvlpvtdwqs agwkltalgr aak
//
LOCUS       WP_181889597             846 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Corynebacterium].
ACCESSION   WP_181889597
VERSION     WP_181889597.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 846)
  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 846)
  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..846
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..846
                     /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=94587
     Region          19..839
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mltdlledia qapeslfeda vwdsfnswtt srgislypaq eeaslallag dnvilatptg
       61 sgksmvanaa hfiamargqr tfytapikal vsekffalce ifgaenvgmm tgdasvnsna
      121 piiaataeiv anialregkd aridqvvmde fhyyseperg wawqvpllel pkaqfllmsa
      181 tlgdtawlek dltertgrkt tyvggaerpv pldfhyvfsp vhetieglle dnkapiyvvh
      241 fsqreatera qaltsmniit peekqriade igdfrftttf gktlsklvrr gigvhhagml
      301 pkyrrlverl sqtgllkvic gtdtlgvgin vpirtvlitg lakfdgtrqr ilksrefhqi
      361 agragragyd tegtvvveap eheienvklr rkagddpkkl kkirkkaard gevswsentf
      421 erlkvaepee ltsqfkvsns mllnvvarpg dgyehmrhll rtnhdprakq nrdiiqavnl
      481 frglinagvv ertpdspayr pytltqeldr dfalnqplsp falafltlld pesetytldv
      541 isafeaildd prqllqaqqt aargeeiaal kaegvdyter maiiedvtyp kpladeldea
      601 fdtftqgnpw akefelspks vvrdmieham tfsdliatyg larsegvvlr yltdawrtls
      661 ysipdaymne eledivvwlg elirqvdssl idewahmtgd dqpvsqdtid relafgvedp
      721 taltanrraf timvrnyffr lvelfayeke dqlaemldyl epdarvdwpa amddyfdeya
      781 dvdlgpdarg peffrladtt grfwevsqii kdpegdnafq lhgtvdldas deagevrlsa
      841 lvvkgg
//
LOCUS       WP_181889656             428 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Corynebacterium
            haematomassiliense].
ACCESSION   WP_181889656
VERSION     WP_181889656.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium haematomassiliense
  ORGANISM  Corynebacterium haematomassiliense
            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 haematomassiliense"
                     /db_xref="taxon:2754726"
     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=48051
     Region          136..403
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mtvadivdtl fpsgtpfkwe afdgsstgpa dakhtvkvns pgglsyivth pgdvglaraw
       61 vtdgltvega hlahpydvfd dmrtlynnyk rpnprelvri arslrsmgal qiqpipeaeq
      121 aswlertirq glaphskerd aqvisshydv gndfyelflg dsmaytcayy ptpdatldea
      181 qenkfrlvfe kmnlkpgdkh ldvgcgwgsm vryaarqgvk slgvtlskeq aewaqakike
      241 egledlaevr fldyrdvtet gfdaissigl lehigvknfa syfefladkl rpggvmvnhc
      301 itypdnhkts qgdfinryif pdgeltgsgt iiyemqdhgf evfheenirf dymrtlhdwc
      361 enlkanwdea valvgentak lwgmymagse wgfehdvvel hqvvgiklas dgsragtper
      421 rwwndsvf
//
LOCUS       WP_181889968             358 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: potassium channel family protein [Corynebacterium].
ACCESSION   WP_181889968
VERSION     WP_181889968.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 358)
  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 358)
  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 358)
  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..358
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..358
                     /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=38270
     Region          50..346
                     /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 mklrsllslr adatnlteip vhslldvvni ptaaratpws liarrffyal llivavafva
       61 yldrdgysep ltfidalyys avtlsttgyg ditpvtqsar liniflitpa rvaflmllvg
      121 ttlsvlteds rktlqiqqwr nsvrnhtivi gygtkgrsai daliaggasp ssivvidpdp
      181 aaltvaekrg litvhgngtk sdvlrvaais rarsvivaps sddtavlitl svremapsam
      241 ivasvregen qhllmqsgad svivssetag rllgiatvtp pvvemmedll spdegfavae
      301 rpiaddevga nprhladivl gvvrsgelyr idspeaetve pgdrllyvrm ngaitnrd
//
LOCUS       WP_181890077             372 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Corynebacterium].
ACCESSION   WP_181890077
VERSION     WP_181890077.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
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"
                     /db_xref="taxon:1716"
     Protein         1..372
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39538
     Region          65..362
                     /region_name="FrmB"
                     /note="S-formylglutathione hydrolase FrmB [Defense
                     mechanisms]; COG0627"
                     /db_xref="CDD:440392"
ORIGIN      
        1 mkkikaaala altavslacs gapavsaqpa gqegivkawd artnpplitr tgqaqewvnq
       61 vdhktvlsyn vyspsmrrdi pvavvpatda agnrvrnapt lyllngagga eqnqdwlkly
      121 pvkdyfagkg vnvvvpqaga fsyytdwvkd dvasdyvngp qkwetfltke lpgpiervvg
      181 angrravtgv smsatsallf aqhnpgmyqa aaafsgcast ssphgynfar ltvnragtpn
      241 fqtvtpemmw gpmngpynry ndallgaekl rgtrlyissg sglaghpdqv syllgkgapm
      301 paaqagaavl qveggvieaa vnkcthdlka kldglgipah felrnvgths wpywtedmdr
      361 awhttikpal gv
//
LOCUS       WP_181890147             109 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: antibiotic biosynthesis monooxygenase family protein
            [Corynebacterium].
ACCESSION   WP_181890147
VERSION     WP_181890147.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 109)
  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..109
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..109
                     /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=12098
     Region          3..105
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 msivkinait vpegageele rrfaarkhsi dghpgfqgfq llrpvkgedr yfvvtrwade
       61 esynawwega graghgeskd adsdkprkpv sqsadllefe vvldsleqd
//
LOCUS       WP_181890355             416 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FUSC family protein [Streptomyces].
ACCESSION   WP_181890355
VERSION     WP_181890355.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 416)
  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..416
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..416
                     /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=45961
     Region          21..211
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mrearegrws rerlakvlrd pvvvqtlrsa aaatiayvia lrlspeaapl tapltallvv
       61 qvtfyatltn girrvnsvva gvlvaiafsl lvgltwwslg llivaalgvg hlvrvheyvp
      121 evaisamlvl gvtsvgdvaw arvletliga vvglgfnlll appvwvdeag eslgdlarrl
      181 rqlmlrigee aagrqpyeqa aarlhearrl dhdiievdaa lrqaedslrl nprvregllh
      241 rvvlrtgldt leictvvlrv larsltdlak drepdslfek etgavldqll seiadavvsf
      301 svlvtthvss nadaaesrls telrtaagtr drlapllhee aqrrpehwql ygavltevnr
      361 iidemntehr srrlleeldr vsqeqrarmp rltrirermg iqeklwsrtg vsgrsr
//
LOCUS       WP_181890428             555 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Streptomyces].
ACCESSION   WP_181890428
VERSION     WP_181890428.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 555)
  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 555)
  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 555)
  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 555)
  AUTHORS   ter Beek,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 555)
  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 555)
  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..555
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..555
                     /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=59470
     Region          12..547
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mdlarpevvg rrtrsaaarl glvavpvaff avffaypvaa ivarglhvdg vwrfgrlwdv
       61 lgqsdirhvl wfttwqalas taltllialp gayvfarfdf pgkqvlravv tvpfvlptvv
      121 vgtaflalvg rgglldelwg arldttvwai llahvffnya vvvrtvgglw aqldprqeea
      181 armlgasrwt awrtvtlpal gpavaaaalm vflftftsfg vvqilggpaf stleveiyrq
      241 tseifdlsta avltivqfva vgailavhaw tvrrrestlr lvdaaltarr prgagqwall
      301 agvlavivvl lllplavlvq rsldapdlgy yralteadgg vflvapieai gnsleyavva
      361 tliavlvggl aaaaltrrda grfvrgfdal lmlplgvsav tvgfgflisl deppldlrss
      421 wilvplaqal vgvpfvvrtm lpvlravddr lreaaavlga spwrvwreid lamvrralli
      481 aagfafavsl gefgatvfia rpdnptlpva varllgragd lnygqamals tvlmvvcava
      541 llvlerlrtd rtgef
//
LOCUS       WP_181890978              48 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein, partial [Citrobacter
            portucalensis].
ACCESSION   WP_181890978
VERSION     WP_181890978.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 48)
  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 48)
  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 carboxy end.
FEATURES             Location/Qualifiers
     source          1..48
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..>48
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
     Region          7..>48
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mmniqnkvsv iipvynaeky ltsciesile qtyhnyevii indgstdn
//
LOCUS       WP_181891011             231 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Citrobacter portucalensis].
ACCESSION   WP_181891011
VERSION     WP_181891011.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
REFERENCE   1  (residues 1 to 231)
  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 231)
  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..231
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     Protein         1..231
                     /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=25706
     Region          21..225
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mddvstkrnn ggmnmkwnel arvrmkelgi tqemlaeelg mtqggvghwl rgsrhpslde
       61 igvifqylgi snvsfnhdgt fsitgevsna pvkkqynypv fshvqagmfs pefrtfterd
      121 aerwvsttkk asdnafwlev eghsmtapag skpsfpegml ilvdpeepvd pgdfciarlg
      181 gdeftfkkli kdsgqiflqp lnpqfpmmpc nehcrvvgkv vasqwpeetf g
//
LOCUS       WP_181891091             468 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Bacillus
            altitudinis].
ACCESSION   WP_181891091
VERSION     WP_181891091.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
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 altitudinis"
                     /db_xref="taxon:293387"
     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=53729
     Region          51..433
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mlqflfflif lyvvyvflta fvlfylpfqk tckehciyka ssisgddqgi nqvmlldngf
       61 esgqvrvqmi reakknirls yysiqkgkta ewvlgaliea adrgvkvqll ldgichslrg
      121 plkhlryava nhpnmairfy epfrlfkpwt whnrlhdkll ladgrvavmg grnigdkyfa
      181 dqppkdfayd rdvllynakk gkvldemeqy fvylwnhdft krtkdvfska kakkgkklrk
      241 qllrsyqeai rtkepfvtst ydwakdaira kqiafftnpv erlnkrplvl kklndlaqrs
      301 krsvliqtpy viptrpmkdg ltplpsdiqt tvvtnsltat pnplafagyl stkkelmktg
      361 vhlyeyqgpy sihaksmvid dnlsiigtyn ldarssflnt esilvidsap falslteaie
      421 rkiaysvlva kdrteykasd ygqkkkpfmk rllltglsti tvlwrrli
//
LOCUS       WP_181891230             289 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Bacillus
            altitudinis].
ACCESSION   WP_181891230
VERSION     WP_181891230.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 289)
  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 289)
  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..289
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..289
                     /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=33391
     Region          41..284
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mwekhllvep pyhfdqvlrr lssdplkavd ldkreikvpm rlnhkpyvav vqatgtkeap
       61 sfrvqangpe eailsevkri fgmehqlhav hdhfaqtnla piferhigtp lmldfhlyhc
      121 lmkciihqql nlafayelmk rfvhtygeqi dgvwfdplpe tiasletddl rklqfsqrka
      181 eyvidvskri vsgsldleel hdlpdieiee rllpirgigp wtvqnvlmng lgrpnlfpma
      241 digiqnaikr hfdlpekptk eemavlskew apylsyasly lwrsietdk
//
LOCUS       WP_181891391             552 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Bacillus altitudinis].
ACCESSION   WP_181891391
VERSION     WP_181891391.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 552)
  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 552)
  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..552
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..552
                     /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=61768
     Region          21..542
                     /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 mtvrvqnlvq nwfpsedgna eerkeliklm eqiisgvddl kdpnrahlkg eknreedfyk
       61 kltetsqipm ngqqaelvne ellkllhnhp yhtkyfftni lpmastpgil gmltamlvng
      121 nnlwdvygpa gaeaevrvvs mmskligydp nvsggyttwg gqgaifsglr laiakvapes
      181 lrkgvpqnly afcsdaahys lfksmeatgi gtdnlirikt nkdhsmdmed lrcqmervaq
      241 nggipvyiva ttgttdaiai ddvkgvreta eaiaekyglk vphihadsal ggffaffney
      301 dvsenplqfs dgvlrmlkei kakfqhlsla dtmcfdfqkl gqtpytsslf lvknaadlkr
      361 ldleeqetpy vghrgygeyh tgytlecsrm gssismlsvl ltfgiegyqr llgqflevnl
      421 afrealrqei pqaevvnddn vgmatlfriy ldgsprfkee isgeatamei ernndlnkml
      481 feklgekrde mffgdttkfl qvnakegqef ylsvskffvi spytlpehip hivsylkdvi
      541 asvcgqfesv ea
//
LOCUS       WP_181891404             413 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Bacillus altitudinis].
ACCESSION   WP_181891404
VERSION     WP_181891404.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
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: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     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]"
                     /calculated_mol_wt=48158
     Region          99..390
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mknktqqttk ypgvyvddkg nffyqsefgi dritgkrirk kgrkdingkp fssafeanke
       61 ltrlkreyhk vnsysnykmt yeqfmnsvyi pyyqtnvees tfsvrkrile kirdrfasip
      121 lrsisvedvq hfrtwlltsk enggagysqs yaslvfgtfr ksldkavemq ylemniskkv
      181 raipkgkaiv sywtkedfek vinqiyiedf yehlnfvmlw vyymtgirvn egtalrwndv
      241 dlknkrlrvh hmlimktrse wkrnsytkte dgkriialdd dtiniltiwr nrqleiglgn
      301 sndfifsydg lpmikstigr iirrysqfag vtriqakglr hshasyline fnvsvlvlsq
      361 rmghsspeit lkhyahmwsg adtalaeima gnieiktaee tnvkfngnqa lkk
//
LOCUS       WP_181891322             279 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Bacillus altitudinis].
ACCESSION   WP_181891322
VERSION     WP_181891322.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
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="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..279
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32298
     Region          3..194
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mrqpkvsiim gvyncqetve esiesilrqt yenweliicd dastdgtyek vlhytmrdpd
       61 rirlirnehn qrlaaslnrc lteangelia rqdgddisvs trlekqvhfl eahpeydvvg
      121 tamtvfdesg akgvralvse pdrrvlargt pfchgtimmr asaykalngy rsvkttrrme
      181 didlwirffa agrkgfnlqe plylvredea afqrrkfrys mdnawlvlka ckqlklspfd
      241 ylfalkpvir acmspkimrf yhqrklggsm vkrrtirde
//
LOCUS       WP_181890528             707 aa            linear   BCT 28-DEC-2024
DEFINITION  FG-GAP repeat domain-containing protein [Streptomyces sp. M7].
ACCESSION   WP_181890528
VERSION     WP_181890528.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. M7
  ORGANISM  Streptomyces sp. M7
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 707)
  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..707
                     /organism="Streptomyces sp. M7"
                     /db_xref="taxon:255705"
     Protein         1..707
                     /product="FG-GAP repeat domain-containing protein"
                     /calculated_mol_wt=74865
     Region          559..621
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          610..672
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Region          661..>703
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
ORIGIN      
        1 mtrrarittt laclaalgag tlttagtata dttptpirtd gvwgidyagg flttventps
       61 gsqwvigrdi sadgstvleq tsrgyadaya dgsqiqrvpc eagprgcvpm rstgngwvgy
      121 flenaagqqv aqlrltensl sgtdepkvtg grfvdatgry yvynasstgk qyvdavnayr
      181 thdvrrtrav taasvwgsil wtpgtgdgav tgydlearkt vqtlatgapc tvkelqvvgr
      241 wvywncgptg aagvydrtak kavkvpsgpa lvgdgylvrh drtagklmlt dfhtgtaape
      301 ravadlpagt tadqrrlswt vdkfggdiay vgqdkairiv psdvpaqpla kiesdvdsdv
      361 vdpseragvp ywdsfwqlnr pahwtftvkd dqgrvertik gsgasvevew dlrsdtgafl
      421 sngrktwtlt atpeeggagy gtsgtlgytg glqghhdqgg yrygelvtln ssggltlqyt
      481 egkgtfdfkr sasgwpsgtv avpfgdmgkd rcaemlvrmp ngelrryagk cgasytpsss
      541 htslgtgwna ydvltapgdl tgdgrvdlla rkastkdvyv fandgagklk agvrirtawt
      601 gytkivgagd ltgdghgdvl ardkagtlwr ydglgdgrlk drvkvfsdwg gsynaivgvg
      661 ditgdgrddl vsrdtagnly rntgngegsf gsrvkiasgw qgykglf
//
LOCUS       WP_181891405             506 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-dependent nuclease [Bacillus altitudinis].
ACCESSION   WP_181891405
VERSION     WP_181891405.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 506)
  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 506)
  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 506)
  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 506)
  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..506
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..506
                     /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=58757
     Region          8..383
                     /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 mteilnlsme itniksikta nfeiplengv haivggngag kstlllalaq tissfylttl
       61 kpydckqdsr lvfklgelqh ewfydmvtkr wepkrsksek gsqritfpgl yegslfygkr
      121 fndsrivdkl iedgkistdy ivdadeyike nlsfilhgdh lhyknlkrmr nkfiaksfkl
      181 antpyfmeid nhlisqykms sgecllisll hfiynsivrr sipidqikli lideielalh
      241 pvavsrlidf ldeitqqydk tsiiltthaa evirkinpnn iynienynge lnfinpcyps
      301 yairniytad rydyillved vlaetiieki indknlresk liqivpvggw envlklqidl
      361 lsknlfglgt elisildgdv keqvskldky kdlkklflpi ksvekylyei litnpnyklk
      421 kvlndkyfti rsidnilmdf nkkypkhveq ldkklyfalr kdlinrkide rtfvtnlcnd
      481 ilenvdfskf vdqlstkviq kslvkr
//
LOCUS       WP_181891430             300 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Bacillus altitudinis].
ACCESSION   WP_181891430
VERSION     WP_181891430.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..300
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34137
     Region          49..300
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mekkskreql lsllgemper hrveaytlki eeresylvet lilsihgvee vpayfvkpkd
       61 tvkkrpvvlf qhshggnyvd gkeellkgah ylqapsyake ftskgysvla idhagfgerr
      121 grteseifke mlltgkvmwg mmlyesmcai dyllsrsdvl perlavfgms mggllswwta
      181 aldervsvcv dlcaqvdhht lietnhldrh gfyyyvpsla khftaadiqe mifprphlsi
      241 vgkhdqltpa egvgriqqtl sqayqaaslk eryqliglha ghfetaamrh eatrflkkwl
//
LOCUS       WP_181891436             113 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Bacillus
            altitudinis].
ACCESSION   WP_181891436
VERSION     WP_181891436.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 113)
  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..113
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..113
                     /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=12871
     Region          11..97
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mlftqtpapp yyaviftskr tnveqkeyaa aaqkmeqlak eldgflgies ardehgvgit
       61 vsywdslaai kewkahtahq rvqkkgkkdw yesyttrick vehaytkeds lle
//
LOCUS       WP_181891550             708 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: peptidoglycan D,D-transpeptidase FtsI family protein
            [Bacillus].
ACCESSION   WP_181891550
VERSION     WP_181891550.1
KEYWORDS    RefSeq.
SOURCE      Bacillus
  ORGANISM  Bacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
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"
                     /db_xref="taxon:1386"
     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=79659
     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 gkmydargrv vvdnesvpai vytsesgvka edkikvarkl atyikmdtdf
      121 lrerdirdfw lashpkeadk liskaeqknl kskdvyplqv ervpkkeika 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_181891652             690 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Bacillus
            altitudinis].
ACCESSION   WP_181891652
VERSION     WP_181891652.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 690)
  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 690)
  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..690
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..690
                     /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=77391
     Region          3..>57
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
     Region          107..341
                     /region_name="PAS"
                     /note="PAS domain [Signal transduction mechanisms];
                     COG2202"
                     /db_xref="CDD:441804"
     Region          226..684
                     /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 mqrvlivgag qggsalletl lktntvqiia iadldleaqg mdeakkngie tttdwkeyik
       61 ddidiiiett gssavlkeli eqkpehaviv pssmayvmse lmtekqqliq ilkeqtykhd
      121 rifnatndgm ifinmdeevv lfnrsaakmv gcsqkdaigr hirevipntk lpdilrsrep
      181 efnqkqflnq qiqivttrlp iiddagrmlg alsifkditd avelaeevtn lkevrtmlea
      241 iiqssdeais vvdeqgkgil inraytkmtg ltdkevvgkp agadiseges mhlkvletrr
      301 pvrgvrmkvg pnkkdvivnv apvivdgilk gsvgvihdvs eiqsltneln karqlirtle
      361 akytfediig eseqmlvale qaklgaktpa tillrgesgt gkelfahaih nesdrkynrf
      421 vrvncaalse tlleselfgy eegafsgarr ggkkglfeea nqgsifldei gemtpstqak
      481 llrvmqekei vrvggtkaip vdvrvitatn vniekamaeg kfredlyyrm nrypisippl
      541 rqrlediesl skrliqkinl dygrnvsglt dralhrlrsy swpgnvrele nvlgramifl
      601 npqeewidea hiafmesdeh eekerqelav sqfegetlsd aveafeaqli kqtlekhqfn
      661 rtktaktlgi sirnlyykmd kyqlakdsmq
//
LOCUS       WP_181891752             505 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Bacillus altitudinis].
ACCESSION   WP_181891752
VERSION     WP_181891752.1
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 11440907
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..505
                     /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=57250
     Region          19..492
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mkiivigagp gglaaammlk skghdvhiye kqsfvggrns kfqlgdftfd tgptflsmih
       61 iaeelftfag knlydyidvi elkemyrlif qdekldmird rdemykrlea fapgegegyv
      121 rfmndtkrkm drltpilqsk mdrfhhylrp kvikalpqls lnkslydvls dyfsnesvky
      181 aftfqskylg mspwecpgaf silsfmehdt gvyhpkggvn qlseamakaa vesgatlhls
      241 tgvekllteg rkvkgirlet geeiqadevv vngdfahvmt klvepgllkk ysekklkkkk
      301 fscstfmlyl gldtiydeph htivfsddya kfvkeitktf elpddpsiyi qnasvtddsl
      361 apkgksalyv lapvannqsg idweahqeef relvldtler ktgfknirqh ievermitpk
      421 hweeelyvye gatfnlghql tqmmvlrphn efdelkhcwl vgggthpgsg lptilesari
      481 ttnailakek hthkrvphqe kgsas
//
LOCUS       WP_181891728             457 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Bacillus
            altitudinis].
ACCESSION   WP_181891728
VERSION     WP_181891728.1
KEYWORDS    RefSeq.
SOURCE      Bacillus altitudinis
  ORGANISM  Bacillus altitudinis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 457)
  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 457)
  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..457
                     /organism="Bacillus altitudinis"
                     /db_xref="taxon:293387"
     Protein         1..457
                     /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=52150
     Region          7..455
                     /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 mlqklwlyht ndlhshfenw pkiaayieek rqvhdqmllf digdhmdrvn lvseadygkv
       61 nvkllnqlgy dgvtignneg itlpherldq lykdaqfpvi lsnlfekgkr pswakpyevi
      121 tlnnglkiav lgvtiaytpv yeklgwditd pfesiremlq evkgqadviv llshlgiihd
      181 revahdfpei diilgshthh lleqgemdng vllacaekyg hyigcvelti dtasseliek
      241 katvqsvdql isesdeaitt lqkaerraks lmqekvssik skletkwfdd sqlpqlltda
      301 ikewceadig mmnagmvlds leagivtred ihricphpin pirvtltgkq lietvsrgce
      361 ekmeqlrikg fgfrgelmgk mlysgltysl eegeakrvke vyvndqlvke ddsytvgtvd
      421 mytlgslfph irdheyieyf mpeflrdvls wrlrdek
//
LOCUS       WP_181891962             319 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Campylobacter upsaliensis].
ACCESSION   WP_181891962
VERSION     WP_181891962.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter upsaliensis
  ORGANISM  Campylobacter upsaliensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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..319
                     /organism="Campylobacter upsaliensis"
                     /db_xref="taxon:28080"
     Protein         1..319
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37983
     Region          58..>156
                     /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..96
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(72..73,76..77,79,106,109..110,113..114,116..117,140,
                     143..144,147..148,151)
                     /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"
ORIGIN      
        1 mdfffveyrd pivglifltl lilvvalahy awrifadkde eqklekfikk felenshkel
       61 lrsenlsfsn lsflaeiftk sgefekasgi ylialektkd kneqeeafla lakvyfkagf
      121 lekctevlln alkirprnqe alkllkisyl klkkyqenle lleclfelge dikeeaefik
      181 alsfqnqena kekilkldes salkrylfek ygifkkqnlv qicdllyksk epinlddeey
      241 yeffymlglv ekkegfsfkn shfkmyhilk qnhfkarlef symcleckni mplffyhcpv
      301 cyefnrckil yevkndetr
//
LOCUS       WP_181892480             816 aa            linear   BCT 28-DEC-2024
DEFINITION  efflux RND transporter permease subunit [Campylobacter
            upsaliensis].
ACCESSION   WP_181892480
VERSION     WP_181892480.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter upsaliensis
  ORGANISM  Campylobacter upsaliensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 816)
  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 816)
  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 816)
  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 816)
  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..816
                     /organism="Campylobacter upsaliensis"
                     /db_xref="taxon:28080"
     Protein         1..816
                     /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=92665
     Region          1..811
                     /region_name="MMPL"
                     /note="Predicted exporter protein, RND superfamily
                     [General function prediction only]; COG1033"
                     /db_xref="CDD:440656"
ORIGIN      
        1 mmafflkfli nhpkstfllt llfcvflsff afklhidasa esllleddkd lktfrelskh
       61 yksdnflmla fkpsdenpfs qeslkklenl hqelegvegv ervfsvinap lllssenkdl
      121 kelmqnipni tskdinqsra kdeiltspfy qnniiakdgk ttaliiylkp dltyidliea
      181 rdgakdenek erlrtqikth qetqnafnka lltqirtims gyekdgarly lggvnmisdd
      241 misyikddlk lygislvfll gfalwyffrs fslmilslfi cfislsaasg lfalldfpit
      301 vissnyaplm liitlsvvvh lithfieisr lypnttqkrl vlqtllakak psffaifttm
      361 igffslifsh iepiiklgim mslgiglgli lsylflsstl mllkkqnftq kefklslllw
      421 canvsikhkk fiyalalitl ilafigipkl kvensfvnyf kdgsaikegl lvidkdlggt
      481 lpldiiirfk eqqksqmkeg enldsfedef eslalkdtyw fdskktriak kvhhflenke
      541 fvgsvlslns llslgksinn gkdlddfala flnenlppnf kqdllspfvn ikqnelkfsi
      601 rvidsnpnlk rdtflknlkn elnellkneg vevqitgiml lynnmlqslf ssqfdtlafv
      661 vlaiftlfvl ifrsfkiati aiicnlipls lvfafmgfld ipldlmsiti aaiaigigvd
      721 dilhyiyrfk eelkhnsvkk aivnshlfig talyytsisi vlgfsvmmss nfiptiyfgi
      781 lttlvmilll fgslfllpsl lisfyakrnn kpkvlk
//
LOCUS       WP_181892482             319 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Campylobacter upsaliensis].
ACCESSION   WP_181892482
VERSION     WP_181892482.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter upsaliensis
  ORGANISM  Campylobacter upsaliensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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..319
                     /organism="Campylobacter upsaliensis"
                     /db_xref="taxon:28080"
     Protein         1..319
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=38022
     Region          71..96
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(72..73,76..77,79,106,109..110,113..114,116..117,140,
                     143..144,147..148,151)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          74..>156
                     /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          104..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdfffveyrd pivglifltl lilvvalahy awrifadkde eqklekfikk felenshkdf
       61 lrsealsfsn lsflaeiftk sgefekasgi ylialektkd kneqeeafla lakvyfkagf
      121 lekctevlln alkirprnqe alkllkisyl klkkyqenle lleclfelge dikeeaefik
      181 alsfqnqena kekilklden salkrylfek ygifkkqnlv qicdllyksk epinlddeey
      241 yeffymldlv ekkegfsfkn shfkmyhilk qnnfkarlef symcleckni mplffyhcpv
      301 cyefnrckil yevkndetr
//
LOCUS       WP_181892197             157 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
            [Helicobacter pylori].
ACCESSION   WP_181892197
VERSION     WP_181892197.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Deutsch,C., El Yacoubi,B., de Crecy-Lagard,V. and Iwata-Reuyl,D.
  TITLE     Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA
            nucleoside
  JOURNAL   J Biol Chem 287 (17), 13666-13673 (2012)
   PUBMED   22378793
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     Protein         1..157
                     /product="tRNA threonylcarbamoyladenosine biosynthesis
                     protein TsaB"
                     /EC_number="2.3.1.234"
                     /GO_process="GO:0002949 - tRNA threonylcarbamoyladenosine
                     modification [Evidence IEA]"
                     /calculated_mol_wt=17696
     Region          35..>91
                     /region_name="Carbam_trans_N"
                     /note="Carbamoyltransferase N-terminus; cl22532"
                     /db_xref="CDD:451406"
ORIGIN      
        1 meldlvlisl gdgvllgvyq nnflctsyts klktsealve vfsqlfkdfk nptlpaikgv
       61 yyakgpgsft slklthvflh tlalihdfel ysttgfdfnd ntpilayank yfvskeresl
      121 sdfkdlkiap kdfmlpsfle kdkftqlntp fyilppi
//
LOCUS       WP_181892652             480 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Pectobacterium
            parvum].
ACCESSION   WP_181892652
VERSION     WP_181892652.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium parvum
  ORGANISM  Pectobacterium parvum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..480
                     /organism="Pectobacterium parvum"
                     /db_xref="taxon:2778550"
     Protein         <1..480
                     /product="beta strand repeat-containing protein"
     Region          <14..>467
                     /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 atvkdssghl apntdisftt tdgtlsqtta itnasgeatv sltsatigdi tvtakvnnna
       61 adtgksatva ftsnvvvfsm mpntataqad nmtpvtftat vkdssghlap ntdisftttd
      121 gtlsqttait nasgeatvsl tsatigditv takvnnnaad tgksatvafi nanvvsltpd
      181 vttaiadnft pitftatvrd tlgnlvpnad vgftnssgtl sqpiaitnan geatvsltnt
      241 tigdtlvtak vnnnaadagk satvaftadv ttaivtsltp dittaqadnm tpvtftatvk
      301 dssghlvpnt disftttdgt lsqttaitna ngeatvslts atigditvta kvnnnaadtg
      361 ksatvaftad vtavivtdie pefptaaigf nfisitatvk dssghfvena nvrfdtthgn
      421 ispqqivttd vngqatvnls gstpgnaivt akvdsnpndi grsttvtfvp eivrtipnpe
//
LOCUS       WP_181892718             287 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sugar phosphate isomerase/epimerase family protein
            [Pectobacterium].
ACCESSION   WP_181892718
VERSION     WP_181892718.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium
  ORGANISM  Pectobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae.
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="Pectobacterium"
                     /db_xref="taxon:122277"
     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=31957
     Region          34..277
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mpcmtllrra faiplllivs sglafaerpa enqkialqmy tlrslntlde qfsmardagf
       61 kavelvgthg isasemkgll gkyqlkaiaa hvqfgelksn maevvafnka ignsmiivpw
      121 lniedrpdsa egwkrfglem ndlgrelnkq gmklayhnhn femkkyrgkt aleimmdaae
      181 penlmlemdv awvsrggqdp vrllrqykgr iysihakdnt sigirddemn fappgegila
      241 weeilpaask agaqwfvaeh dlpkdpqaiv saayqslyek lskiksk
//
LOCUS       WP_181892093             327 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Helicobacter cinaedi].
ACCESSION   WP_181892093
VERSION     WP_181892093.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter cinaedi
  ORGANISM  Helicobacter cinaedi
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 327)
  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 327)
  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..327
                     /organism="Helicobacter cinaedi"
                     /db_xref="taxon:213"
     Protein         1..327
                     /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=36567
     Region          2..303
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mefknllmla plagytdlpf rsvvkgfgvd itvsemissh alvysnkrtl kmaekspqeq
       61 pysvqisgsk eevikkavei lntqegidii dlncgcpapk vanhgngsgl lkdlnllvki
      121 anlikenakt pytslkvrlg fdkkipheia qalkdvksdf vvvhgrtrad gykkekidyd
      181 aiahikqnvp mpliangeid svekaqkvle htgangvmig raaitspwif wqirnnthei
      241 ppivkkelvl ehfnkmiefy gergaimfrk nlhaytkghe gasefrnlin slsdveqitq
      301 hienffshnq ivthnfpqlv hlnkrss
//
LOCUS       WP_181892940             508 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Falsiruegeria
            mediterranea].
ACCESSION   WP_181892940
VERSION     WP_181892940.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
REFERENCE   1  (residues 1 to 508)
  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 508)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 508)
  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..508
                     /organism="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     Protein         1..508
                     /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=56279
     Region          58..472
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 maqksgsnrs vvigavlffl qactgapldq dtpvtqarla pqstlvtaar elshgqagfv
       61 plsdgdqalg arlrliegaq dtldlqyflm kpdlggalia dallraadrg vrvrfllddf
      121 fttvddgsla lvdahdniqv riynpaarpw pkpvgmalef srvnrrmhnk sftadqafai
      181 iggrniadey fqlntssefa dfdllvvgpp vkeigqafdr ywndgwavpl sslsepataq
      241 elrearvelt aelqparqvy ddavenryir qigtsavply rgraelvvdp pkklkqpvrg
      301 gprplaetll armrdaerev illtpyfvpe dyggrllsdl vqrgvrvriv tnslaatnhp
      361 yvhagyrrhr adllkagvel yelradslqe lglvpaesei gvvmhtklav idntvfvgsl
      421 nldprsikqn telglfmasq gfardilidl eqglvdytyr islddnerlq wryeqpdlit
      481 vkqqepgatf wkqllvgita llpveqql
//
LOCUS       WP_181892037             169 aa            linear   BCT 28-DEC-2024
DEFINITION  NuoB/complex I 20 kDa subunit family protein [Helicobacter
            cinaedi].
ACCESSION   WP_181892037
VERSION     WP_181892037.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter cinaedi
  ORGANISM  Helicobacter cinaedi
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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 169)
  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 169)
  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 169)
  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..169
                     /organism="Helicobacter cinaedi"
                     /db_xref="taxon:213"
     Protein         1..169
                     /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=18754
     Region          1..159
                     /region_name="PRK06411"
                     /note="NADH-quinone oxidoreductase subunit NuoB"
                     /db_xref="CDD:235797"
ORIGIN      
        1 maehqvnytq saglpialss vdrllnwsrs nslwgltygl accaiemmat ggsrfdldrf
       61 gtifrasprq adlmivsgtv tkkhaefvrr lydqmpepkw vismgscant ggmfntystv
      121 qgvdriipvd iylpgcaprp etlqyavmvl qqkirkqkai pqikpkrlv
//
LOCUS       WP_181893042             382 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Falsiruegeria mediterranea].
ACCESSION   WP_181893042
VERSION     WP_181893042.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
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   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 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 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     Protein         1..382
                     /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=42547
     Region          45..382
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makkmklsar nlaalehgql awdtevkgfg arkakddavt lflnyqvret gkyrrvtiar
       61 lgectvdaar tiaarmrlei ragvdvaqqa etptarvasg etlghhiqrw ldaphsawgk
      121 strttyrrlm ardvlgteva gkritdvsrg dlmqlvdtaa rrtesgaill akvlrsflsw
      181 adargltevt lasnkridls ieprtrvmtd aeivalwcta pklgerwgta grlvllsgqr
      241 sgmitrmesd wvrqdgihfp tepnrksaat wvpltpwalt hlrpimgggg rlfsrsetfd
      301 sdalkkwrti aevdarlrlh dvrrslrtwa arqgygydas eaalghtvqr taldkayqqh
      361 syaeeaaevl rgwqrhiegl vs
//
LOCUS       WP_181893121             439 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Falsiruegeria mediterranea].
ACCESSION   WP_181893121
VERSION     WP_181893121.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
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="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     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=48882
     Region          11..382
                     /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 msetraayal igagpmglam akvlkeqgip flgfelhsdv gglwdidgpk stmyetahli
       61 ssknmteftd fpmdegvaey pshhdlrnyf rdfadhfglr dhytfnaevl eteplggpgd
      121 gwrvtwrdvd gdhtaefagv miangtlsep nipefpgqfg gelihssqyr hpsqfdgkrv
      181 livgagnsgc diavdaihha nlcdlsmrrg yyfvpkyvfg kpadtmggli klpmwlkrri
      241 dgmilkwfvg dpqkygfpkp dyqlyeshpv vnslvlyhag hgdlriradi ermagktvhf
      301 rdgtsddydm ilaatgyklh ypfidrdlln wqgdaphlyl namhperddl fvlgmveasg
      361 lgwqgrheqa emivryikgl qagcpvaasl kseksngfer atggmnylql armayyvdka
      421 tyrnavtgwi aklskgaqa
//
LOCUS       WP_181892827             762 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase NtrY-like [Falsiruegeria mediterranea].
ACCESSION   WP_181892827
VERSION     WP_181892827.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
REFERENCE   1  (residues 1 to 762)
  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 762)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 762)
  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 762)
  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..762
                     /organism="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     Protein         1..762
                     /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=84069
     Region          71..300
                     /region_name="NtrY_N"
                     /note="NtrY N-terminal region; pfam19312"
                     /db_xref="CDD:437144"
     Region          295..736
                     /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 masrsqngpi ltisrwrrtr karnigtlgl vvlgpvltla tylaigpfdq gasslslrli
       61 lladfvyilv laalvlgqva rliaarraks agsrlhlrli gvfsllalip avtvaifagl
      121 tlnvglegwf sdrvravvgs sltaaeayes eqrldlseda malaqfldqs rgvnffindg
      181 efrqllargq sqiqrglrea yvidgtgeil frgdrsylfd ferpsneqis eaqergllii
      241 qdwdnnefra lvplnaylnr ylyvsrevdg hllnlldetk etakfyqqle sergrvlfqf
      301 gllylgfavi lllaavwlgl wfaerlsrpv grlttaaqrv gggdlavqvv edggddeiam
      361 lgryfnqmtr qlkgqrdall entrqieqrr rlfdsvlssv tsgvvgldpd grvtfvnrsa
      421 erlldwsgge qslalgiavp eflplfetmq stgsetaqge ikvsrmgqqe nllvrmstrr
      481 gedgglegyv vafddvtdlv saqrmaawgd varriaheik npltpiqlsa erikrkftga
      541 lpeedaekle amtdvivrqt ndlrrivdef skfarmpepd rrnedltqlv rdavllqqtg
      601 qpdlrivadl pddpittdvd gtmlsqaltn liknageaie tlkekgapdn lepqihvslt
      661 dsgagviiti adngvglped rarlfepyvt trdegtglgl pivkkiieeh ggtltledap
      721 vfdgqdhfga mavirllrdd phkpkapieq aaktlvkagq ye
//
LOCUS       WP_181893171             385 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Falsiruegeria mediterranea].
ACCESSION   WP_181893171
VERSION     WP_181893171.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..385
                     /organism="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     Protein         1..385
                     /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=43195
     Region          117..380
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mfyvskrvkh nfldacsqiq tgrvtihtpe gsvhqfgsgg vesemvirdw svisalaarg
       61 dvglgeayvd glwetpsied vatvalgnad hfadyvepsa fnrlkfravd rllranskrg
      121 ssrnirahyd vgnefyqlwl drsmtyssal fsegdmdler gqqrkydrvl dklsagertl
      181 eigcgwggfa eraaergrhv tgltisrsqk gyadarldgr adialrdyra etgkydnivs
      241 iemieavgek ywpqyfaqlk sclaedgrav vqaitvpdsn fdmyrrrsdy irqytfpggm
      301 llsdavishh arevgldvrd sysfgadyaa tcriwaerln dqiarikalg fsdrfvrswr
      361 yyleicaasf atkgtdvvqv elsha
//
LOCUS       WP_181893251             282 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Falsiruegeria mediterranea].
ACCESSION   WP_181893251
VERSION     WP_181893251.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     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=31985
     Region          10..281
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 mvapisnayt siiakpfapn lgaeiygvdl srpvpddqfa eicdafhtyq vlffkeqkei
       61 ppaqhiefgk rfgplhahpa aptmegypei feihatknsk vangefwhsd vscdetpplg
      121 tmlqihiapp cggdtmfsdm yaayddlsdp ikemlnglsa lhssehiykg rysdrgqkdr
      181 didcpeavhp ivrthpdtgr kslfvnrtft trilglsdte sdailnmlfe haeqinyqir
      241 frwslndmaf wdnrccmhra iwdywpaerk grrvtvkgdr pv
//
LOCUS       WP_181892924             505 aa            linear   BCT 28-DEC-2024
DEFINITION  malonate--CoA ligase [Falsiruegeria mediterranea].
ACCESSION   WP_181892924
VERSION     WP_181892924.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
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="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     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=55053
     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 manplydtlf gqhlgkttpf leladgaiis hsdyleraaq yahvftqlgl kpgdrvavqi
       61 gkspqalavy aacvqsglvf lplntaytpd evsyfvensg arvilcdakr seelepiaea
      121 tgavletmnn dgsgsfalqa evmpstfstv drseddlaaf lytsgttgrs kgamltqgnl
      181 lsncqaltre wqftsddill halpifhthg lfvatnisll agskiifmpk fdldviidrm
      241 psattmmgvp tfytrlleda rftkelakgm rlfvsgsapl laethvqfed rtghrilery
      301 gmtetnmnts npyvgerrag tvgfplpgie ikitdsdsga tlpqgeigei evrgpnvfkg
      361 ywqmpektae elredgffit gdlgqidddg ylhivgrnkd liisggyniy pkeielildd
      421 eegvlesavi gvphpdfget vvgvlvaeag aeldleaikk svgtslarfk qpqklvvlpe
      481 lprntmgkvq knelrddykd lfapa
//
LOCUS       WP_181893288             430 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Falsiruegeria mediterranea].
ACCESSION   WP_181893288
VERSION     WP_181893288.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     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=46619
     Region          31..401
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mirnenpvia nslwsataky tdtypalsge qqadvaiiga gftglsaalh laeagasvtl
       61 idsqhpgwga sgrnggqinv glkdgptgir akfgdhwger mirmagdagd lvfdlierhq
      121 incdakrpgw lraahtpktl qqlhelaedw drhgggmkkl dqaemqrltg teaynggvld
      181 rrggvlhpln yalgladaah rngvaiyggt panhiqaegg ryrvktpnga imtdkvlmct
      241 naysgdldpk vaksvlpvrs vqvatpplsd nirrsilpeg nalsdarrll lyfrqdaegr
      301 flmggrgtyn dgstrrqier lkrvsvelyp qlsdvkwdya wggfvaltrd hyphlhelap
      361 giyaglgyng rgvaiatamg rvlarwaage ptedldfpvt plkplllsfa retlveaeil
      421 rlklldklgl
//
LOCUS       WP_181893409            1053 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Falsiruegeria mediterranea].
ACCESSION   WP_181893409
VERSION     WP_181893409.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1053
                     /organism="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     Protein         1..1053
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=115948
     Region          5..1052
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mthvgerrqv svlfadmvgf taaverlged gtlpftqviy nlmsdtvveh ggtvssfggd
       61 svmalfglpe aledgalrsc raalaiqsaf aeaadeierr fglrprmrvg vssgvalmas
      121 iegqdapata vgntvnlasr iqnlaaagnc licdttrrlv egqvelnfdd eydikgvskr
      181 rklwnllair kaatrfdasv arglshfvgr ekelaalsdt fsvaggdfkv vdlvgeaglg
      241 ktrlvfeflq qinpkesrly rghcaadrtq vpfypflevv neafqirsed etaeislklk
      301 tgltglgldn penlglllnl lgkeppagsl dgldgvligh rtrnllraml raecarsivi
      361 fliedihwid sasaeflgki vgdgepnnlf vlhtrrpeya pgwsdnwrvt eialmplssn
      421 eighlvqtrl qvdnlplslv eqvskraggn plfgeeilsf liskgalsvd venanfdidl
      481 assglpesmr slftvrmdrl epsdkallqa asvigrrfdp glltsvlqtd gsvgetlrrl
      541 qtldlihrdd rssdyefkhv llrdtvyqsl lseqaaelhl aiataleqrn enrfgevaga
      601 lahhylrter rdlafkynal agarslgvys lgdanryfes alglyqsdpg candrefaaf
      661 lvdystcsni slkitefiel aphvrpilgr lgdtyqhvvf lhhyiaclvy ngryvdafat
      721 qqdltamaer ldtpeaaaya lvselsvscy fgqlsneafe akrreaevam ksvqdaylqn
      781 fflailawne tsrgrfahay ettrrmvdlg kakndprslg yatalnalia mlsddhakal
      841 eiaeqalkvs haeferasae aartaalvpl erpealgevn rfiskceqdg wglflsgpdm
      901 mlgvaltmng rideglrhme daigrrereg ydlaadwyrl flaelylgil sgegeaslgl
      961 lfrnvrslsw vfmfgagrii klidqacenp lfdrngyyva rgqmilglly klkkkkglav
     1021 ehlrdarria dqigpspflt ridvaladle aat
//
LOCUS       WP_181893353             252 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Falsiruegeria
            mediterranea].
ACCESSION   WP_181893353
VERSION     WP_181893353.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
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="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     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=28455
     Region          31..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 maptkfqaki lnkgqerytr yqvqhrkyfg vpqtgrvldf gcgaggfvlg alqdgldawg
       61 ievdeererq fdniternfp qwrdrfylyp grlmpypsnh fdgiyswfvf ehvpdpqtsl
      121 reiarvlkpg gtlhihaedv rnlweghala pwpaympref aaayleglgk pehadfvtnl
      181 vvyisapiiq eilttlglev vyasaapvrp aipeglyvtn dqearalgmk mrniaisgpq
      241 enltiiarkp kt
//
LOCUS       WP_181893775             290 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Actinobacillus ureae].
ACCESSION   WP_181893775
VERSION     WP_181893775.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus ureae
  ORGANISM  Actinobacillus ureae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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 290)
  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 290)
  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 290)
  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 290)
  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 290)
  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 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Actinobacillus ureae"
                     /db_xref="taxon:723"
     Protein         1..290
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32447
     Region          111..>281
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 msegsassra lasiflglmr gnnsnsedfa lttwqadksk mllpwlanlt hprlmdenar
       61 nmginyltpa tlvsgkemai qlslprrsts tvsvvetesf grriqsvngv ieasdstvkl
      121 gkirhlwqkt aqdvaldlqq laghifvtgs tgsgksntiy qllnelnrnd ikfmviepak
      181 geyknvfghr ddvkvfgtnp kktkllrinp fkfpedvhvl ehidrlveif nvcwpmyaam
      241 pavlkeamld ayqesgwdlt tsenkypklf ptfadlfqql etvldrstfs
//
LOCUS       WP_181894917             618 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Bifidobacterium longum].
ACCESSION   WP_181894917
VERSION     WP_181894917.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
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="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     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=67415
     Region          25..613
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mteniadkai ndtrivkqft npvkepidsd inlfdlldnr akrdpegami eykgddgtwq
       61 pysaqvfrdm vidlakglig lgvnkgdsva ivshtrwewt aldmaimsig altvpvyetn
      121 sasqvswifn dskvtlaiae ddgqrdkies vrdevptlrn vfvieaggln aiktygesvt
      181 daefweykea shgddrativ ytsgstgtpk gvelthrnfa flvlsalqym pragawpnrr
      241 lllflplshv farfleffsf ggtislalss nmktmvkdfe tfgptlllav prvyekvyna
      301 asqragtgfa gkmfmraaen arewskaeqk geqlpitgri ahafyeqvvy kkirtifgpn
      361 adfaitggap mdselshffn gigmpvlegy gmtetcgpvc vslpednrig tigmpmcgit
      421 agiaedgelv vkgplvckgy hnnpgvtaqq itdgwlhtgd lgdisedgfi sitgrkkdli
      481 itaggknvsp glleasvmts pvvnqclvig dkkpfvaalv tldladannw lesqgakpep
      541 dlaslaknai vhaeveravn aanegvsrae sirkfeilpd efteangmlt pslktrraqi
      601 vehyrelidd viyvplkk
//
LOCUS       WP_181894978             292 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Bifidobacterium breve].
ACCESSION   WP_181894978
VERSION     WP_181894978.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 292)
  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 292)
  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 292)
  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..292
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..292
                     /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=31776
     Region          9..280
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 mpitpkildn pksdrvrrit dlarakgrer sgrfliegpq svreavtwrp dvvqdlyvev
       61 aqaldhpriv sstlerivea sqdatiyvhq ctgdvirris adaqgvlavg naqvmqsdvd
      121 dlaldtadya priaafwqvr dpgnagtvir aadaagcdav ifvddcvdvl npkvirstag
      181 slfhlpvltm rtdeffdwts dhhvdvwaad vygtekrkpe slpavladka avsmsqavlf
      241 gnearglepe ilercgriis iplygkaesl nlgtsaavml mslamsghie rm
//
LOCUS       WP_181895337             280 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: segregation and condensation protein A
            [Corynebacterium].
ACCESSION   WP_181895337
VERSION     WP_181895337.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 280)
  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 280)
  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..280
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..280
                     /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=30748
     Region          23..266
                     /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 mtspdsytpe psssegvqee itgfrvalan fsgpfdlllq lisskkmdvt evalaavtde
       61 fiaytrslda vsdldeitef lvvaatlldl ktarllprgd vdseedlell eardllfarl
      121 lqyqaygkva dqfeewqkta prrypravgp dkqfeellpp vrlgmtlgef aefaavvmrp
      181 kppeevgvgh ihgvpvsvpe qagkildslr lagegtwltf tqltsecrvs mevvgrflal
      241 lelyrakaig veqeealeei hvawtgldvd pavvaaanwe
//
LOCUS       WP_181895302             425 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase, partial [Staphylococcus felis].
ACCESSION   WP_181895302
VERSION     WP_181895302.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus felis
  ORGANISM  Staphylococcus felis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 425)
  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 425)
  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 10165685
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Staphylococcus felis"
                     /db_xref="taxon:46127"
     Protein         1..>425
                     /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]"
     Region          114..411
                     /region_name="Peptidases_S8_Lantibiotic_specific_protease"
                     /note="Peptidase S8 family domain in Lantiobiotic
                     (lanthionine-containing antibiotics) specific proteases;
                     cd07482"
                     /db_xref="CDD:173808"
     Site            order(121,168,172,225..227,266,268..269,378)
                     /site_type="active"
                     /db_xref="CDD:173808"
     Site            order(121,168,378)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173808"
ORIGIN      
        1 mtrkeyeiif kqetrihkvi eisqiinahn kiltikvcya ylsiktvkwl ksldcvirvn
       61 dttfitqedf frnqsdydsi pmtkekrnir nkqwdiiklt nnrksyrlhn isrkikiali
      121 dsgidkdhid lkhsilrdsk nlvpkggfnn teiyedgnis nfddvlghgt svagqitang
      181 vlqgiapgig invyrvfgsk vaktswiiqa iieavddgnh vinlsvgsyl lkngsyingk
      241 ndyegflvfq raieyahskn viivstlgnd alnlkshtet ndfiqkknsk kissigqiid
      301 apsnfkgvik sysidrdnki ssysnwgydn laistyggki ssyclnnynd fiqknlyetd
      361 wilsthlqns ynffygnsma tpkisatial iidkfnifey pqlairhlfn nsyyangnfk
      421 idtyr
//
LOCUS       WP_181895424             625 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Corynebacterium amycolatum].
ACCESSION   WP_181895424
VERSION     WP_181895424.1
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=67223
     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 yrisvpkghn
      241 aivtskvlan idaegkgqqd vrtevdeiin etggkcqddg rmgsltgaea sadswtptsa
      301 dasilewdsd riesscdqtk wlvannvwvy dgesvadyrd epvkvevsvq fepvlkkqda
      361 dklnegrsss tgdkaykkat fgeakpvngg nnaaqapevk sgdtisdtiv pgeqkyykip
      421 vewgqrpmva artgnserdn adsmgvalln pfevsvadgt mhfyrdseal nlatdrpiey
      481 nnrsanvggr pvanagyyya tvrmanyrpd eevsgidqpf qlaflldnkp tkgpdwrptd
      541 kngptpsdkp ilakgesekd sskessedas kesdspdtds qasasssdme degmsplvig
      601 tvvavvavfi givgaivyqn kkrqe
//
LOCUS       WP_181895718             322 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Clostridium
            perfringens].
ACCESSION   WP_181895718
VERSION     WP_181895718.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
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="Clostridium perfringens"
                     /db_xref="taxon:1502"
     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=37857
     Region          8..322
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkelkdpkvn rvltifeklk egegintkks aedfcvnekt iqrdindira yiannnknls
       61 ivykrskkay flvedenlgl hkedilamck illesrafcn eemnhiinsi lqnvsyedkk
      121 fikelignel fkfmplkhee klldkiwdls eavhhrevle lqykktngei vkrtvrpvsi
      181 ifseyyfyli vyfnnskmdm pivyrvdkil kyknlkekfr ineanrfqeg efrkriqfmy
      241 sgelmrikfe ftgpsleavl driptsriie shegkhilea evfgkgikmw llsqgsgikv
      301 lspesfakem aleakkicel yn
//
LOCUS       WP_181895736             189 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Staphylococcus felis].
ACCESSION   WP_181895736
VERSION     WP_181895736.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus felis
  ORGANISM  Staphylococcus felis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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 189)
  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 189)
  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 189)
  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 189)
  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..189
                     /organism="Staphylococcus felis"
                     /db_xref="taxon:46127"
     Protein         1..189
                     /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=22031
     Region          <1..183
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mshdintplt alrlelfhla heyhikaedi nvsyerieyi sklirnisid qkekiqyfyt
       61 fnnevdiqsl casiiskwqy lfkrqgievt ykvlneqviw lgealwyerl feniisniyk
      121 hssaknvclt lsssqisfsd dgvgfnprey qesnglniir niaerfhlnv efqsnhhgtt
      181 vvlkanqsk
//
LOCUS       WP_181895973             386 aa            linear   BCT 28-DEC-2024
DEFINITION  CdaR family transcriptional regulator [Bifidobacterium breve].
ACCESSION   WP_181895973
VERSION     WP_181895973.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     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..386
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..386
                     /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=43078
     Region          3..127
                     /region_name="Diacid_rec"
                     /note="Putative sugar diacid recognition; pfam05651"
                     /db_xref="CDD:461704"
     Region          74..378
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mdidpriaqt ivenikgiir ydinffdahg kmiastdatr igtfhdaarl aaerkrtvav
       61 dgdnqfigar nginapvmfg dsvvavigit gqrhevepfg imitkmteil irenveqitr
      121 fdqrmmmtnl inllvsqhnd edlvsylsst ldvdlsiprc ivlgrctnad adhtkrnall
      181 naldkrfpsg sesifrtsar gfcilfaitd qvgsmgqlde hhmgvlsdlq keishvlgrp
      241 isigigsmem sanqywrsyr qataavewlr fthgarveey sniglgmllp amqqsiseqf
      301 vqnifagldd qridafqtaf naytryngsv sraadslfih kntlqnhlna iaeqtgynpr
      361 klddhtvlel aflirnyrsf tgedps
//
LOCUS       WP_181895034             431 aa            linear   BCT 28-DEC-2024
DEFINITION  integrase catalytic domain-containing protein [Bifidobacterium
            breve].
ACCESSION   WP_181895034
VERSION     WP_181895034.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium breve
  ORGANISM  Bifidobacterium breve
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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 431)
  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..431
                     /organism="Bifidobacterium breve"
                     /db_xref="taxon:1685"
     Protein         1..431
                     /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=49295
     Region          171..262
                     /region_name="rve"
                     /note="Integrase core domain; pfam00665"
                     /db_xref="CDD:459897"
ORIGIN      
        1 maakrqvtlr frdeymrask kqkgvildrm ceslgigrst arrllaqagr rthneavpae
       61 rprrysdrsr ellrevwvmm dmpcgkylkt mlpqwlpmlr acgeldaydg stfdelmtms
      121 aatvdrylrp vrdaarpkgi attrpagell rnsitirkag deldglpgnv eadtvahcgp
      181 sargefcrtl tvvdfatgwt enasarnnay rnlsraeami eerlpfairs ydndngsefi
      241 naefiahlqa ldveqtrsrp yrkndqatve srnnhivrrh afyyrytvee ldllnelwel
      301 vrikanlftp skkpvgrsst rdgrprrvyd rpmtpwerlk rfdredrgng gsgfilpgrr
      361 eqieetiaat npaelvrrih diqdrleama aprtrrlekr lgpdmayldr tlaritgvtp
      421 enhnetpadt d
//
LOCUS       WP_181895799             191 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase [Bifidobacterium longum].
ACCESSION   WP_181895799
VERSION     WP_181895799.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 191)
  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..191
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..191
                     /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=20918
     Region          30..166
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mkflsrnkgm ragknldlrl sqyihcagsv vlgdncrlyc wdashgkpfd repeiriger
       61 vhvtrnltlq ctseiiiedd tllasdivmi dynhgmsplp dsyldndlel tsgihigrga
      121 wignnviilg gvkigeksii gagsvvtksi ppysiavgnp ahvikqynps tnlwesirtn
      181 devdraaskt m
//
LOCUS       WP_181896187             408 aa            linear   BCT 28-DEC-2024
DEFINITION  MFS transporter [Bifidobacterium longum].
ACCESSION   WP_181896187
VERSION     WP_181896187.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
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="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     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=43398
     Region          4..407
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 maslllaviy vafislglpd sllgsawptm sqdlnvpvaw aggisavism ftivsallsd
       61 rmtlkfgagk vtavsvalta aalagfsvap nywvllaiai pyglgaggvd aalnnyvaih
      121 yesrhmswlh cmwgvgasvg pyimgyalsq gqgwpwgyry iailqvmltv ilvlslplwk
      181 krgvtavges tdgtvssdgn aerfgtaegv svaerkplgv agvlairgak eilvmffcyc
      241 avestaglwa ssymvmhsgi dkitaaswas lfyvgitvgr alsgfltmrf kdpvmirlgq
      301 vlvfagiltm fvplphhlgv vvglvvigfg capiypcvih stpayfgedk sqaivgvqma
      361 cayvgsllmp plfgiiaqyv tislypwyll vllvlmvvmh erlrklrg
//
LOCUS       WP_181896417             232 aa            linear   BCT 28-DEC-2024
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Seonamhaeicola
            aphaedonensis].
ACCESSION   WP_181896417
VERSION     WP_181896417.1
KEYWORDS    RefSeq.
SOURCE      Seonamhaeicola aphaedonensis
  ORGANISM  Seonamhaeicola aphaedonensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
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 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Seonamhaeicola aphaedonensis"
                     /db_xref="taxon:1461338"
     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=27105
     Region          92..186
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mnlfnpnfel vwslssiiay flvfhffwkp kpdystilei kglnldlipy lilvvigygf
       61 vgqpfwdcnr lieyyqnsni epytgglrkl nlqyayslir alviapilee vffrkflflk
      121 llekyklfva iiissicfsa ihfetpnnli pslifgvisc liffktknis ysillhflnn
      181 lcitlfnmfg esyfnwldnl kfnfvywtlf vlgiltiilg mkkitttnkv kk
//
LOCUS       WP_181896691             380 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [Bifidobacterium].
ACCESSION   WP_181896691
VERSION     WP_181896691.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 380)
  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 380)
  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..380
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     Protein         1..380
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=39364
     Region          <205..376
                     /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 msslrrraav vaaavcagal altgctafnn sddgtadgng tsattqtfqp sggkptatls
       61 iasgsenkev avaiqkaadq snvavtmhym gsleimnalk aggqdhdavw passmwismg
      121 dtkhivkdaa ststtpivfg iakskavklg waddtgatkp vstadilaav sdgkltfsmt
      181 satvidsaln vyqtalrkps wtiwvvdysg smsgegkngv vkglnaaldp dqakksyiep
      241 asgdvnilip feteahrpvk atgtstsdll headatdasg gtdiyeglls aldelpsese
      301 asqyttaivl mtdglsnsdh qdefesayks rgrdlpifsi mfgdadpsql kslatlsnak
      361 vfdgrsgdla avfrqakgfn
//
LOCUS       WP_181896702             347 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Bifidobacterium longum].
ACCESSION   WP_181896702
VERSION     WP_181896702.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..347
                     /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=40469
     Region          1..308
                     /region_name="WecH"
                     /note="Surface polysaccharide O-acyltransferase WecH [Cell
                     wall/membrane/envelope biogenesis]; COG3274"
                     /db_xref="CDD:442505"
ORIGIN      
        1 mpqkpaarnv siellrivam fliltchfvi hfdwdhhqlr vvlpqepgww salrfvivqy
       61 gqvgvsiffi isgyflveks fkwnrlvktw lqmfcysvaf liivlllgaf hhypmavepi
      121 mhgvdlyrsi laslfpffyn sywfigayll mllvapylnt lfntlpkrsm emlivllgff
      181 siqilifera snwnnlvyam lgyliggwlr kyyqdyedrf rtlpmigiiv altllmvafn
      241 hyiseqswlv dfmgwknrih dgivlfpiii gmlvfimvsr vdmnqspevv qraictiapt
      301 tfgiylihen wfgfrivwdc vskmsyppsl pilrpmagvc iipefnl
//
LOCUS       WP_181896743              87 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase, partial [Bifidobacterium longum].
ACCESSION   WP_181896743
VERSION     WP_181896743.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 87)
  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 amino end.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         <1..87
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
     Region          <1..87
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 lalgcdqvmm epvlrragls istpgisyas idhsmwwyqd idinewhlyv qdtpiaahgr
       61 glgiakvyaq ngdlvaaiaq eamvrvp
//
LOCUS       WP_181896744             190 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase, partial [Bifidobacterium longum].
ACCESSION   WP_181896744
VERSION     WP_181896744.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 190)
  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..190
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..>190
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
     Region          9..>186
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 maqattvtpl dhlvkvlklg epsayrnhty ingesmyfpt grvyggqvia qsviaasktv
       61 gpsrlphsvh gyfiaagdir qdllfdvenl rdgrsfsarr vnvtqaegsi ltaiasfqet
      121 gqegvefadp mpenlpdpet ltsakelmqp faekspfany yaekspfdir hvtptvmlra
      181 dkdsaehdsg
//
LOCUS       WP_181896990              75 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Corynebacterium
            senegalense].
ACCESSION   WP_181896990
VERSION     WP_181896990.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium senegalense
  ORGANISM  Corynebacterium senegalense
            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="Corynebacterium senegalense"
                     /db_xref="taxon:2080750"
     Protein         1..75
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7986
     Region          1..68
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mvchldelie argitgaala eqvgitpvnl svlrnnraka vrfttltalc raldcqpgdl
       61 ftvepgepde ltehd
//
LOCUS       WP_181896797            1227 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Bifidobacterium longum].
ACCESSION   WP_181896797
VERSION     WP_181896797.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 1227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1227)
  AUTHORS   ter Beek,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 1227)
  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 1227)
  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 1227)
  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 19952326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1227
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..1227
                     /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=132144
     Region          <262..640
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          968..1225
                     /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 mkrrnlddsg grgagvsavf akdtlrcwlr swkrfvsiav itllgvavlt giyagcrdaf
       61 laagrfydqq glhdlqvlst ygltdddata lrridgvqtv qpersqtvtt lvdgtkktvt
      121 mqeigtegld qpyirqgklp nkagevavtq qflndsglki ggtitvtpqd tsssvisvaa
      181 tetddsnnad tvgvaanasa sdaksaantd adaeqspqfp tkltitgvvl dprdlnnpdg
      241 ysgmtsfrst ssedytffap sdgvtgniyt aisvavtgas dfdtfsdayd eavktvadri
      301 ehqiqttrqk arrqqivssa qrklddakde aneqldeaqk qiddnwaele ankttlqdsr
      361 telennrtti tdgerqladg raqiasarqq iaqgrqqiae artqlesgka qltsarkqld
      421 aaqteltanr tkieqgitqi dqgvaqidqm lsmiqqadnl laqldpnidf nsptwqaikq
      481 llarlgitlp evpsiselrq qlaakqtelq tqrdsltqqk adlqrtlnet iapaqstldq
      541 qnaqltakeq eaaageaqln tksaeleana atletrsaql eaqaaqlasg kqqleegerq
      601 leegeqqlad gkaklddaqs aldamrseae sefakqqrri ddvanarwyv qtrasidgfs
      661 slksdvssie sigrafpivf llvavlmslt tmtrmveedr gligtylglg ygglavssry
      721 llfallaclv gggigllvgf lgipafllvv ieglyilpgv rleydwlygs agivlfvvgv
      781 gvvtalacre eirhtpaalm rpkapktgar illerirpvw srlnflgkvt arnifrfksr
      841 limtvggvag ctaliicgfa indtvdtigv kqyeqiyqyd lmvvanddna aamrkqvaed
      901 gqatetlnlr vdsgemsnaa qesetvqlmt vpndslniln dmvtleqagd dewfglpnif
      961 gkagggtval ddsgvivsqs aanslnihag dtvtlgnggs srakvqvtav trnlvgsdvy
     1021 iserlydqkf aadgvtssas gdgtastltw namlaklkgs eteqaeyadr lgeessvlka
     1081 vscahlaatf kfdlmgavva livglaggla lvvlftlant nvserirema tlkvlgfydr
     1141 evhnyvnrem miltgmgvvv glplgrwigg lltaalnmps lyfevevhwy syaiavvatl
     1201 afallvqlft npvldrvdpv sslksve
//
LOCUS       WP_181897120             404 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein, partial [Bifidobacterium
            longum].
ACCESSION   WP_181897120
VERSION     WP_181897120.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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 404)
  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 404)
  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 404)
  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 12807984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         <1..>404
                     /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]"
     Region          <1..296
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          257..>404
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
ORIGIN      
        1 taeevsstgv hwtfspvlci ardtrwgrvd etfgedpmli gemasamvkg yqggaqaget
       61 lpkdailaca khfagysetq ggrdaseadl shrkleswfl ppferiakeg cgtfmlgyes
      121 iegvpvtfnk wlladklrga wkyngtlitd wdnvgrsvwe qkvkpdyvha aadavkagnd
      181 lvmttpgfyd gaieavhtgl ldeslideav arilalkfrl glfedprlpd ekrikavigs
      241 edhrrvnlel areavallrn dgglpfdaap aeaipgsgda parkriavvg pladdaqnql
      301 gdwagssgqv gwmpdghprg mittvldgfr alagdgcevt yarganvidl vpdpegefyp
      361 dgqprpkigv sapvdralld eavaaaread livavvgdvv qlvg
//
LOCUS       WP_181896273            1231 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Bifidobacterium longum].
ACCESSION   WP_181896273
VERSION     WP_181896273.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   ter Beek,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 1231)
  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 1231)
  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 1231)
  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 19952326
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..1231
                     /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=132191
     Region          <266..644
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          972..1229
                     /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 mkrrnlddsg grgagvsavf ardtlrcwlr swkrfvsiav itllgvavlt giyagcrdaf
       61 laagrfydqq glhdlqvlst ygltdddaaa lrridgvqtv qpersqtvtt lvdgtkktvt
      121 mqeigtegld qpylqqgklp nkagevavtq qflndsglki ggtitvtpqd asssvisvaa
      181 tetddannds nnadtvgvaa nasasdaksd antdaaaeqs pqfptkltit gvvldprdls
      241 npdgysgmts frstssedyt ffapsdgvtg niytaisiav tgasdfdtfs daydeavktv
      301 adriehqiqt trqkarrqqi vssaqrkldd akdeaneqld eaqkqiddnw aeleanettl
      361 qdsrtelenn rttitdgerq ladgraqias arqqiaqgrq qiaeartqle sgktqltsar
      421 kqldaaqtel tanrtkieqg itqidqgvaq idqmlpliqq annllaqldp nidfnsptgq
      481 aikqllarlg itvpevpsis dlrqqltakq telqtqrdsl aqqkadlqrt lnetiapaqs
      541 tldqqnaqlt akeqeaaage aqlntksael eanaatletq saqleaqaaq laggkqqlee
      601 gerqlkegeq qladgkakld daqsaldakr seaesefakq qrriddvana rwyvqtrasi
      661 dgfsalksdv ssiesigraf pivfllvavl mslttmtrmv eedrgligty lglgygglav
      721 ssryllfall aclvgggigl lvgflgipaf llvvieglyi lpgvrleydw lygsagivlf
      781 vvgvgvvtal acreeirhtp aalmrpkapk agarilleri rpvwsrlnfl gkvtarnifr
      841 fksrlimtvg gvagctalii cgfaindtvd ttgvkqygqi yqydlmvvan dddaaamrkq
      901 vakdgqatet lnlrvdsgem snaaqesetv qlmtvpndsl nilndmvtle qtgddewfgl
      961 pnifgkaggg tvalddsgvi vsqsaansln ihagdtvtlg nggssrakvq vaavtrnlig
     1021 sdvyiserly dqkfaadgvt ssasgdgtas tltwnamlak lkgseteqae yadrlgeess
     1081 vlkavscahl aatfkfdlmg avvalivgla gglalvvlft lantnvseri rematlkvlg
     1141 fydrevhnyv nremmiltgm gvvvglplgr wigglltaal nmpslyfeve vrwysyaiav
     1201 vatlafallv qlftnpvldr vdpvsslksv e
//
LOCUS       WP_181897262             367 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Streptococcus sp. NM].
ACCESSION   WP_181897262
VERSION     WP_181897262.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. NM
  ORGANISM  Streptococcus sp. NM
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Streptococcus sp. NM"
                     /db_xref="taxon:2292266"
     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=40301
     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 mkkvaiigag ivgataayyl skeadlevtv fdhgqgqatk aaagiispwf skrrnkawyk
       61 marlgadfyv dlladleksg qeidfyqrsg vfllkkdesk leelyqlalq rreesplidq
      121 laildpasan elfpglqgfd hllyasggar vdgqllvtrl leasqvklvk ekvtltplas
      181 gyqigeevfd qvilatgawl ghlleplgye vdvrpqkgql rdyqlaqdme aypvvmpege
      241 wdlipfaggk lslgathend mgfdltvdki llkqmeeaal phypvlarat sraervgira
      301 ytsdfspffg qvpelsgvya asglgssglt tgpiigyhla qliqdkemtl dplnypieny
      361 vkrvkse
//
LOCUS       WP_181897336             357 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Bifidobacterium longum].
ACCESSION   WP_181897336
VERSION     WP_181897336.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 357)
  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 357)
  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..357
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..357
                     /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=39109
     Region          21..353
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 maskkqqqsr ldamkprvkp vdlfsslkle lsvliviata iafamcwfll kfgwsgwiam
       61 pltlvvalgi tyffsrgita plrqmrdvae amadgdytvr vdidqdrhde vgqlarsfne
      121 magelehadk mrrdmianvs helrtpvsal qamvenmadg vteptsanle siltqtqrls
      181 dliaflldls rmeagaasln iekfnfadfl detiepleia dgghahdirv tvpadismeg
      241 dqdrlrqlft niianalkhs adgttvlvda hedenqgtiv tnvvnfgsqi apsdrldifr
      301 rfvkgktgpg tesggtglgl siarwaaqlh ggtvkvvddt rgadfeiilp kyhvaer
//
LOCUS       WP_181897422             321 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein, partial [Bifidobacterium longum].
ACCESSION   WP_181897422
VERSION     WP_181897422.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 321)
  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..321
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         <1..321
                     /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          61..285
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 afcinpslvn awpatsfwtq nlgtgqwatv lhgkglwlys yleihatrnc gfytepgvyq
       61 ivlnaalfvl lfwkkklyfg nekqyrtatv ivlltlitcq sttgylsmmv illcfffmrv
      121 gerdirmlkq kiavlvvait avlitdywlr geesllyvqv lnklfggdig aginledstg
      181 qyrwitvmas lkalsmdpfg igydafyair dsfdpaavaa siatyaavyg vifwlammim
      241 ifypmirrep kkiliavfaf mfinstvset ylfypglmmf piylssyfth kqssvvghai
      301 athnprrslm vsnlmnakev m
//
LOCUS       WP_181897435             495 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein, partial [Staphylococcus felis].
ACCESSION   WP_181897435
VERSION     WP_181897435.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus felis
  ORGANISM  Staphylococcus felis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
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   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 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 10787203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Staphylococcus felis"
                     /db_xref="taxon:46127"
     Protein         <1..495
                     /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]"
     Region          105..271
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 eeetttedne ateeetaten neateeetat egneateeet vtegneatat edneateeet
       61 ttennkmsee vkkedkeaka epktgeksll hdekptvpkg nqghpkptky ptilvhgfag
      121 fpdekkpfff psywggnkvd ldkelkkqgy dvreagmsaf gsdydravel yyyikggrvd
      181 ygayhaqkyg herygetfkg iypewepgkk vhlighslgg qtiqvledml rngvqeeidy
      241 qkqhggtiap lfqgnfdnmv asvtsvatph ngtyisdklg nrpivrklft divkyasnkh
      301 asidygygiw glkqrddety lqylrrvrds kvwqtedsgf ydgslegskr indrltlsdd
      361 vaytsitgrd thstlsgnqr pnlhmfapfk ilsnlnghqq pdswkindgp vplgsglypy
      421 nkphydttfd gtpklgqwgv mptlnnwdhm dfvgwdvldt rikpdmvlhf yedimnylss
      481 veqvqeqkek akasa
//
LOCUS       WP_181897506             269 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Grimontia hollisae].
ACCESSION   WP_181897506
VERSION     WP_181897506.1
KEYWORDS    RefSeq.
SOURCE      Grimontia hollisae
  ORGANISM  Grimontia hollisae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Grimontia.
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 14398448
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Grimontia hollisae"
                     /db_xref="taxon:673"
     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=30570
     Region          41..120
                     /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          189..264
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mvrriqnenc dysewregad liarkwslec ddrvhlsqrp yamhkhhrgq llcidegliq
       61 vnteegtwll ppyragwipp eamhsvsfhg slkgwsllfs psschqlpss pcviemndvl
      121 nvlsnrvvsw sktndlspeq srilgvilde igrapqenly fplpkdprlq kiaqsmldep
      181 gntksvehwa svgaissrtl rrlvrsefmm sfsmwrqqil lihalemlar gisvgdvsfa
      241 lgystpsnfi amfrkvyges paryfskrg
//
LOCUS       WP_181897672             141 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Winogradskyella
            eximia].
ACCESSION   WP_181897672
VERSION     WP_181897672.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella eximia
  ORGANISM  Winogradskyella eximia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
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="Winogradskyella eximia"
                     /db_xref="taxon:262006"
     Protein         1..141
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=16338
     Region          7..105
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkqierrsdc pislsldifg dkwtllilrd fiffdnrhfn elvtiekist niladrlnrl
       61 lendivkkev drnnkssyly sltekgidli pivieiykwg annidgnnan sefknevnsn
      121 fnkvtseivd riktthnngy k
//
LOCUS       WP_181897595             366 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Winogradskyella
            eximia].
ACCESSION   WP_181897595
VERSION     WP_181897595.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella eximia
  ORGANISM  Winogradskyella eximia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
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="Winogradskyella eximia"
                     /db_xref="taxon:262006"
     Protein         1..366
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41636
     Region          23..365
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkakflllyl fvstisfgqi hpkinsliea einankvpal avavidsgkv ihisakghrd
       61 vklkkkatin tpfhiasvsk tvtnmvvfkl ielgkidlka dinnylpfkv enpffpdeki
      121 tvelllkhrs gikddvkfyg phwsnpkgdp klsleylkdy lvsggslyke shydskpnhk
      181 lnfkysntgi allayiveqv sgmsyedfcq knifkpmkmn ntswflknld sslvaktyvk
      241 nktkefifkg hngypdypgg qlrtsitdyt tliagflnad dnnfilnnet kkmiipsvst
      301 phlgyytwfi kainnnlyye hgggdtgvrt isiiepdkkr aiiifanypy nfdelyksie
      361 remwee
//
LOCUS       WP_181897973             237 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Staphylococcus
            felis].
ACCESSION   WP_181897973
VERSION     WP_181897973.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus felis
  ORGANISM  Staphylococcus felis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 237)
  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 237)
  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..237
                     /organism="Staphylococcus felis"
                     /db_xref="taxon:46127"
     Protein         <1..237
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
     Region          <1..229
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 avydrliyfn pcdgielkhk dlsepqkaqy lpkeqikpfl emvkkrdihq yymfrtmiet
       61 girvgeanal qwsdynnkdk tlsitksydq khdrwnttkn kehrtiyitd dlakeltklk
      121 ylqnanrivn ediyneshdf ifcnafgdpl psstthntmm hvtskllgke nklsihklrh
      181 thatlllesd vpmkviqerl ghktmaiteq vyshvtekmn qkakdnfeky ineknif
//
LOCUS       WP_181897385             510 aa            linear   BCT 28-DEC-2024
DEFINITION  acid phosphatase [Bifidobacterium longum].
ACCESSION   WP_181897385
VERSION     WP_181897385.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium longum
  ORGANISM  Bifidobacterium longum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 510)
  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 510)
  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..510
                     /organism="Bifidobacterium longum"
                     /db_xref="taxon:216816"
     Protein         1..510
                     /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=53997
     Region          27..286
                     /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(153,160,209..211,244,250,254)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mkmfrhlssv faiatiapla laatlavtpa iaqadqlpnp dwvallsdye knywqaptda
       61 ehggkvldad tmkldedlav ainhkaaenl dkdglnaqrk ralvdsdlqa eeampdalgp
      121 vlgkymsegl ksgklnavad ifsfnvvsty askraamhpr pylnraessy ggtndlaglp
      181 atldikqsps wlehvpgysn lqknssypsg httgayswgi alagmipela pqimartsea
      241 gnnrivlgvh ypldimggri gasaqngqyw hnefassivp asrqlrdylv srcaadghgt
      301 tlaaciantk asgsggytnd fldpvatepv adqasavrvy tarltytfpq dtaqsgadfv
      361 aprgaadvlr laypelhadq rnailkatal dsgyplwqss dgwqrinwak alcarvtldk
      421 hgdvakveta dqvaltgpsv vnaqytdagn hpasdssage nsaiaagpdl atlhaaqrpa
      481 lisvaigtav iaivggirtv rrksknqlqq
//
LOCUS       WP_181897987             233 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tRNA1(Val) (adenine(37)-N6)-methyltransferase
            [Chryseobacterium].
ACCESSION   WP_181897987
VERSION     WP_181897987.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
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 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..233
                     /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=26484
     Region          2..226
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mkpftfkqfe iqqsknvfrv gtdgvllgsm atvnnalnvl eigtgtglis lmlaqrnsna
       61 qflgidinek aadlttfnfe nspfrprlkn ihcdfknfdm dknfdlivsn ppyfeasese
      121 kdkiarqtve lnfkqlisks sellsengif sviipveagn dfieiakenq lflikkinik
      181 giensktkrl ilefslteka pkesefiiek sprqysdqyl eltkefhifk srn
//
LOCUS       WP_181898045             573 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Chryseobacterium].
ACCESSION   WP_181898045
VERSION     WP_181898045.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Rosinski,J.A. 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 573)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..573
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..573
                     /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=67422
     Region          <468..560
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mikklyflvf vvifrllscq evysdyyklr lryenleenn skalpliqpy inkakkekny
       61 ekllqgykdg vfysssneek lkyadsavwa aklsknkdli ssayiekgvv yyyhykkyqp
      121 alneyltaye yskntdnkfl kfqnlyhigv vksylgyyae asdlfkqcid yygqksksnl
      181 hpneifnnkk gylnslhqli icyrnlgktr eadsaiktgl sevrnnpdya qekgyfllak
      241 gisdfkkety plaldnlnqs lspikkagdf awlsvdyfyi gksylhsknt kesivyfkkv
      301 dsifqkhqfi lpelrenyei linhykkekd qgqqlyytgq llkadsiisk dftylapkih
      361 keydtktlle eknklekans wgnfiiigli ifalgliill ikrykiqkni qqkyilleek
      421 filqqnpsek pistteekrt sldegkveel lrklkifedk keftqkglti nklasqfgtn
      481 snylsqvine ykevnfnkyl selrinyitn llfenkeylk ygietlakec giasrqnfsd
      541 lfyeingirp tdfirkrkqe ldnkrnfstl kpi
//
LOCUS       WP_181898000             274 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: amidohydrolase family protein [Chryseobacterium].
ACCESSION   WP_181898000
VERSION     WP_181898000.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 274)
  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..274
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..274
                     /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=31448
     Region          2..274
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 miidshvhfw nfdpvrdawi tenmavirkd flpedfslyl nennvegcia vqadqskeet
       61 sflvnlaken pfikgvvgwi dltsenleal lqnyqsekli kgfrhiaege eigfllqkni
      121 lngiaalhqy gytfdillrq dqlsdavkll eklsnqpfil dhcgkpdlkt ndlkdwklni
      181 aelaqnpnvy ckisglltqg nwnnidekvi fetldfifsq fgikravfgs dwpvmllggn
      241 yalwlelisk yvgqfskeeq qlffsknavr fykl
//
LOCUS       WP_181898315             593 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Alteromonas
            aestuariivivens].
ACCESSION   WP_181898315
VERSION     WP_181898315.1
KEYWORDS    RefSeq.
SOURCE      Alteromonas aestuariivivens
  ORGANISM  Alteromonas aestuariivivens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alteromonas/Salinimonas group;
            Alteromonas.
REFERENCE   1  (residues 1 to 593)
  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 593)
  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 593)
  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 593)
  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..593
                     /organism="Alteromonas aestuariivivens"
                     /db_xref="taxon:1938339"
     Protein         1..593
                     /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=64960
     Region          47..572
                     /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 mttltmkpny nkskrgakqn vkpslvhwrf vvvlvvvvmv fvvlavraay iqviapdnli
       61 eqgdsrtlrt rnmpsyrgli tdrngvelav svpvraiyad pkiihqkdgl sltrrwqala
      121 evlgqdadkl rsmvtnpkrr fvylqrqvsp amaeyveqld ipgiylrnes rryyptgeva
      181 aqvigitdvd dngiegmerl yndwltgtpg srvirrdakg rqveiletkd geaagnlqlt
      241 idqriqalay reikeamlyy katsasalvv dvksgdilam vnapsfnpnd rddvsphrmr
      301 nrvftdafep gsslkplavl aalefgnvkv gdvidtspgr mrlggslvkd ernygpltle
      361 eiiqhssnmg tsklalgvpk nflldtyynm glmtdtgsni pgessgifhe rsrwsdfela
      421 tlsfgygisv ttaqlarmya tianggvrrp lkivqqpqss gwqpqqeqvv saknanavmt
      481 mmesvtqedg takkaqvpgy rvagktgtsr kaiaggygee yvnifagiap isdprlvtvv
      541 linepggdly hagdtaaptf skimggalql lniapddrqv tstlwmkgaq ngs
//
LOCUS       WP_181898429             635 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Alteromonas aestuariivivens].
ACCESSION   WP_181898429
VERSION     WP_181898429.1
KEYWORDS    RefSeq.
SOURCE      Alteromonas aestuariivivens
  ORGANISM  Alteromonas aestuariivivens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alteromonas/Salinimonas group;
            Alteromonas.
REFERENCE   1  (residues 1 to 635)
  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 635)
  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 635)
  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 635)
  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..635
                     /organism="Alteromonas aestuariivivens"
                     /db_xref="taxon:1938339"
     Protein         1..635
                     /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=71751
     Region          <140..622
                     /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 mpskleiikn dtqlrkrllv gcialslvvi avffmvglnl vidvekrlse eaytdqltvl
       61 rtkiqqhlad dpnhiqdikn elpaylkpls kdivyising empiyssemk hdyewmskpf
      121 pgslapgffy cehatfyynh iavddsgnki yaiwhpssli laskiainrl sitailtfwl
      181 avwaalvmsa litkrfekan lelenlalvd sltklknhna lytervlsgq sgalffldid
      241 hfkdvnsalg hetgdrllva faqrlvrlig ekgtvyryrs defiiwapst gheniqtmaf
      301 qilyecrapl nvddngfels csigaaeypa qgklleilvk naehamyrak rlrlgvqvyh
      361 hqlasnqtve vtlrsqlrsa lmhkqfvlyy qpkvamatet ltgfeaivrw hhpdegilpp
      421 gqfidlieqs givhvftryt ieqaveqilr wqkmgylvpv svnlsaynlm dnafvpfiqg
      481 llqrtgvspn mlefeltesa tmvdikvskk mieafnnlgi rtsiddfgtg mssfaylrel
      541 dihtvkldra firqvhtnsk dqkivegivs lcrnlnveiv aegvevkaqa evlqrldchl
      601 gqgflfgkpa paekverlln refaaqqdfd avank
//
LOCUS       WP_181898499             199 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Halobacillus trueperi].
ACCESSION   WP_181898499
VERSION     WP_181898499.1
KEYWORDS    RefSeq.
SOURCE      Halobacillus trueperi
  ORGANISM  Halobacillus trueperi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
REFERENCE   1  (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   2  (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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Halobacillus trueperi"
                     /db_xref="taxon:156205"
     Protein         1..199
                     /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=22424
     Region          <38..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 mskefwnesf sketyvygkq antfvvemte qlkearyvgc faegegrnav hlakqghqvt
       61 vfdqsdeglt kaeqlaeeeg vhidtvqadl tkkemeaaqf daavmvfghv pkesqsflie
      121 qmirsvkpgg vvlfevysed qlaygtggpk dkrmlysped vlhwiseykc lhfyygeadr
      181 tegerhtgvg hviqafirv
//
LOCUS       WP_181898563             351 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Halobacillus trueperi].
ACCESSION   WP_181898563
VERSION     WP_181898563.1
KEYWORDS    RefSeq.
SOURCE      Halobacillus trueperi
  ORGANISM  Halobacillus trueperi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Halobacillus trueperi"
                     /db_xref="taxon:156205"
     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=40017
     Region          4..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 mkqsnsgkle iiqisralai lfvlighann nfyqeigydw fnvaqwertg gvdfffivtg
       61 fmiyylynky agnkekatqf likrilrifp lywifttlal ivplafpmlq egysmeiilk
      121 sfllltndpi lssawslthi vffyllffay mykpvimkpf igllvgltll gemnifsflp
      181 ssifsisive ifcgalvayl sihfknkyag lcivlgvagy flvwvhnvys ltfiplslay
      241 gfcsmlimfg iaemdktkrn vprflsylgg asysiyiahg pfikgylmif vklnffniis
      301 pffgliiiil lvtasccivy nvvekplvet lrrkvlnkkk vtqpvphlla k
//
LOCUS       WP_181898618             315 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Halobacillus trueperi].
ACCESSION   WP_181898618
VERSION     WP_181898618.1
KEYWORDS    RefSeq.
SOURCE      Halobacillus trueperi
  ORGANISM  Halobacillus trueperi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
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="Halobacillus trueperi"
                     /db_xref="taxon:156205"
     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=35151
     Region          1..293
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msiekirkak etigrvilgk devvellfvs iiadghalle svpgsgktkl aksfakvmdg
       61 hfsriqftpd vlpsdvtgiq ffnpktqefe lregpvmtnv lladeinrat pktqssllev
      121 meekqttvdg etlkiapplf viatqnpveg nhgtfplpea qldrflfkid mgypteqeek
      181 nilrtyqkne pfetltpqil leeilhireq skdiaiaddt mnylldlvrl tresedielg
      241 vstrgalafm rasqaralll gndfvrpedv kflapyvleh rivlsmegai rktksqviqe
      301 viqevpvpve agsvq
//
LOCUS       WP_181898692             319 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein, partial [Halobacillus
            trueperi].
ACCESSION   WP_181898692
VERSION     WP_181898692.1
KEYWORDS    RefSeq.
SOURCE      Halobacillus trueperi
  ORGANISM  Halobacillus trueperi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
REFERENCE   1  (residues 1 to 319)
  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 319)
  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 319)
  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 319)
  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: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Halobacillus trueperi"
                     /db_xref="taxon:156205"
     Protein         <1..>319
                     /product="dihydrolipoyl dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          <1..317
                     /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 dliqeyginl ikgeayfrds htisvagkel taesfliatg aspfipdipg lketsfltst
       61 saldlkevpk hlviigsgyi alelgqmyrh lgaevtlmqr sssllrrhds eisetvedvl
      121 keegitllkg vhyrkveekn gqklvhieve gtlkiiqgdq llvaagrkpn ieklqgenig
      181 lelgeygevl tndyletnls hiyaagdvtl spqfvyvaah qggivgrnvs kqtkktqnle
      241 hvpavtftsp siasiglten qakqagydvk tsvlplesvp raivnhqtkg vfklimdakn
      301 nqiigahvva enagdviya
//
LOCUS       WP_181898391             658 aa            linear   BCT 28-DEC-2024
DEFINITION  BCCT family transporter [Alteromonas aestuariivivens].
ACCESSION   WP_181898391
VERSION     WP_181898391.1
KEYWORDS    RefSeq.
SOURCE      Alteromonas aestuariivivens
  ORGANISM  Alteromonas aestuariivivens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alteromonas/Salinimonas group;
            Alteromonas.
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="Alteromonas aestuariivivens"
                     /db_xref="taxon:1938339"
     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=73212
     Region          3..508
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mvnskaksqs lnkvvfatss vlivvlmlfa vtapelaesl fqqiqdsiid nggwfyvltv
       61 alilfavvfl gvsrygdirl gpeharpefs mpswismlfa agmgiglmff gvaepimhfv
      121 apptaspqtv eavreamatt ffhwgvhawa iyaivalila yfsfryqlpl tlrsalypmi
      181 gerihgwpgh vvdifavtst ifgvstslgf gasqinagln ylmgvpsttg vqivimavvv
      241 glaiisvvtg ldkgirrlse tnmvlaiall vfiialgptv flvqaylqnt gaylseivrk
      301 tlylfayert ewiggwtify wgwwlawapf vglfiarisy grtirefvvg vlciptaftl
      361 lwmtvfgnsa idmvfnqgft elatmveqdt svalfvflqh fpfssvlivl allmvmvffv
      421 tscdsgamvv dmlcshgnnn tpvwqriywa lgvgivasvl lyagglqalq tmtiaaalpf
      481 giillismyg lfkalkvety kreslqttiv plpasrhked wqerlhailh rphkpavsnh
      541 lentikpalk evtkefenqn fdtvideshq hielkvilgv elnfvygvyl tesshpeilp
      601 teqetvdsse nqtyyraevh lseggqnydi mgwsrlgiin dvieqfykhq hflhllte
//
LOCUS       WP_181898855             362 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Chryseobacterium
            indoltheticum].
ACCESSION   WP_181898855
VERSION     WP_181898855.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indoltheticum
  ORGANISM  Chryseobacterium indoltheticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
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="Chryseobacterium indoltheticum"
                     /db_xref="taxon:254"
     Protein         1..362
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41901
     Region          229..359
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkkittivll llsiaqlcaq ipdlekakrk yfqanvisyk ttayypnpet davsvfnvly
       61 tvykpqnkdf efysknetse efyknnsyhe vnhaektvye yekkenqnaa ilssrlrqfg
      121 pttllkqkws fidetqidgk ihshysnies inhyegkeik vefhiyisrn ftiskferks
      181 fvdgklgqtv tylfsnyiff dkttnfkvil ptqyalkyfe rqeslqplak nteapsfeai
      241 dingqefsfi pkeekqtlll fsstncgysk iisdyilssg fnlnpkieli nifgsdskvn
      301 vkkyfvnkev kfpiitdrkd lekqfgingy pilylvneng iitetldgss qvlpflksls
      361 ik
//
LOCUS       WP_181898759             459 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Halobacillus
            trueperi].
ACCESSION   WP_181898759
VERSION     WP_181898759.1
KEYWORDS    RefSeq.
SOURCE      Halobacillus trueperi
  ORGANISM  Halobacillus trueperi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
REFERENCE   1  (residues 1 to 459)
  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 459)
  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..459
                     /organism="Halobacillus trueperi"
                     /db_xref="taxon:156205"
     Protein         1..459
                     /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=52252
     Region          4..459
                     /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 mkeklyfyyt sdlhshfenw pqivgyfnek kkkhekkgee ywlfdngdhv drfhpiaegl
       61 mgkgnvelln eagydvatig nnegitlase dlhslydhat frvvcanldc ksssspawlk
      121 pyhileskyg tkigvlglta pfqafyqqlg wdvlspfdil dgiieelrnq tdiiillshl
      181 ginedeeiar rysdidiiig ghthhlfkng eyidgallta agkhgthlge vavewnidtr
      241 hlekkeayai pteqlkkddg vtkkvkeirs kavhelgtpv aylreplhia wfhdtplmnr
      301 lteqlrlwts adiamlnagv lldhlsagei tyedihricp hpmnpclvel rgdelmevir
      361 aahtkeltei rlkgfgfrge vigkmvfagi diemdddgee hvkrvtfage pidydrtyrf
      421 atadtftfgr ffpeiayskt kkyfmpellr dllsealks
//
LOCUS       WP_181899014             337 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paraperlucidibaca
            baekdonensis].
ACCESSION   WP_181899014
VERSION     WP_181899014.1
KEYWORDS    RefSeq.
SOURCE      Paraperlucidibaca baekdonensis
  ORGANISM  Paraperlucidibaca baekdonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Paraperlucidibaca.
REFERENCE   1  (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   2  (residues 1 to 337)
  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 337)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 337)
  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..337
                     /organism="Paraperlucidibaca baekdonensis"
                     /db_xref="taxon:748120"
     Protein         1..337
                     /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=37515
     Region          93..337
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          254..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mssfteshpg lpaayvllll dvvkrwhvne sellapagld reqltaptlr lpldvvngiy
       61 tralelteep glpfyigmqm klsshgfigf aamtadtvaq aielaerfis lrlmgfalrl
      121 ethndearly lscdlnlqpl rdtavaalmv glgqmaqvlt getlygiadi dipenprfae
      181 fshilpaqiq ygqpenvirf akayldapll madasssqla ieqcerelva ightnrfvrq
      241 vrelihddae gfrsveavas ilcmsertlk rqlaqdgtsf sdiledlrrq ravlllrhes
      301 qsieriaeql gysdvanftr afkrwtgttp sqyrrga
//
LOCUS       WP_181899069             221 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [Citrobacter].
ACCESSION   WP_181899069
VERSION     WP_181899069.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..221
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23955
     Region          5..209
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mmkskavifd mdgviidseg lwrqaqkdal aswgvtvnde ecetltkgkr ldeiarvwce
       61 ycplqtdpgv lesairkrit gliategeam dgvyavlhhf rhrgyriala tssshqviea
      121 vlsklnlrgh fdvicsadde rygkphpavy lsalkklglp aadclvieds lsgfraaqaa
      181 gidtivvsdg cqhpcfseai grytsmpqll etlappvraa g
//
LOCUS       WP_181899235             307 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Lachnotalea glycerini].
ACCESSION   WP_181899235
VERSION     WP_181899235.1
KEYWORDS    RefSeq.
SOURCE      Lachnotalea glycerini
  ORGANISM  Lachnotalea glycerini
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnotalea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Lachnotalea glycerini"
                     /db_xref="taxon:1763509"
     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=34104
     Region          2..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 mlyfivnlhs ksgyarviwk qvkgllqnqn vkyevyftey kghatklvkr itegneklrl
       61 vvlggdgtmn evvngithld nviigyiptg ssndlarslk lpskpreail nilkpkyfqk
      121 ldlgevtass ntrrfvvsmg igfdasiche aldsklkavl nkiklgklty vgialkqlak
      181 fktegatiim dgklsrnyke iyfisshihk yeggglklcp qadyqdgmld icvvnklski
      241 kfllllptaf tgkhirhkav diircrelsi ktsnmlpvha dgeslgkqny vtvksipekl
      301 tiiagni
//
LOCUS       WP_181899181             361 aa            linear   BCT 28-DEC-2024
DEFINITION  CdaR family transcriptional regulator [Lachnotalea glycerini].
ACCESSION   WP_181899181
VERSION     WP_181899181.1
KEYWORDS    RefSeq.
SOURCE      Lachnotalea glycerini
  ORGANISM  Lachnotalea glycerini
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Lachnotalea.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..361
                     /organism="Lachnotalea glycerini"
                     /db_xref="taxon:1763509"
     Protein         1..361
                     /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=41628
     Region          5..130
                     /region_name="Diacid_rec"
                     /note="Putative sugar diacid recognition; pfam05651"
                     /db_xref="CDD:461704"
     Region          76..361
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mitkinesla qqivdtvkdv cgqdinfide egtifastnt nrigdfheig fqvaqtheti
       61 evkkesrfyg tqqgvnvpif hngsflavig isgepelvrk faylairitk lfireqelea
      121 snrtqqeqmn yiihaltkge itnreylyec lqerkldkkq kirvvifklk vdynianrss
      181 feqklfqmfd tlklplytyh ypndyvamin ekelsfslqi lksfaqdnnq ilevgigssh
      241 ellqlkhsye sakialksle rtgqniasfd qldidivlgs ldskimehyl ektvaslcee
      301 dkelltiyya edmslqktae rlylhkntlq ykldriarls gynprtfkea vvlyigiims
      361 k
//
LOCUS       WP_181898880             791 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Chryseobacterium
            indoltheticum].
ACCESSION   WP_181898880
VERSION     WP_181898880.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indoltheticum
  ORGANISM  Chryseobacterium indoltheticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 791)
  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 791)
  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   3  (residues 1 to 791)
  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   4  (residues 1 to 791)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 791)
  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 12114434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Chryseobacterium indoltheticum"
                     /db_xref="taxon:254"
     Protein         1..791
                     /product="heavy metal 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:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter 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:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89595
     Region          4..76
                     /region_name="ATPase-cat_bd"
                     /note="Putative metal-binding domain of cation transport
                     ATPase; pfam12156"
                     /db_xref="CDD:463475"
     Region          85..776
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 msencfhcgq giekerisfd ekifcctgck svyeilntnn lsnfyelnkk agirpeenss
       61 qfdyldtkei fdritdfseg ntslvtfrip vihcssciwl leslhtlhkd ihysqvnftr
      121 kilqisfnhn elklsdlakf ltnlgykpai nletvdkned nldksllikl aiagfafgng
      181 mflafpeyig gedywmehyk glfrilmfll avpvvfysas dyyksawygl knkivnidvp
      241 ivlgifvlfg rsiyeiatdy gpgyfdtlcg llffmllgki fqkrtyssls ydrdyksfyp
      301 iavtkvdfng kqenillsei kigdrilvrn heiipvdail isgngnidns fitgesesis
      361 knpgdkifag gkqigsslel eviknvdqsy ltqlwnkeaf kkhetgldtl inkiskyftf
      421 iilgialvag iywyfidlet mfqvisavli iacpcalals spftfghimr ilgrnkfyvk
      481 dtitiekiak vnalvfdktg tithrkksni ryegseiqef dllnikslvk nsnhplsksl
      541 yeflevqddy fpvdnfeeis gkgyeasvrg niykigsaky nnqesknlet avyisknnef
      601 igkfifkney renlrnlftk ltnykifils gdnaseenql keiipnyssm afnqnpedkl
      661 nyikelqdkg lkvimlgdgl ndagalkqsn vgiaisddsn sftpssdvim ngekvsqldh
      721 ylnvckgsit ivkltflisf lynvvgltfa vtgnmsplfa alimpassit visfttistw
      781 ilgrkyfkkq p
//
LOCUS       WP_181899473             362 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Flagellimonas
            nanhaiensis].
ACCESSION   WP_181899473
VERSION     WP_181899473.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas nanhaiensis
  ORGANISM  Flagellimonas nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 362)
  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 362)
  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..362
                     /organism="Flagellimonas nanhaiensis"
                     /db_xref="taxon:2292706"
     Protein         1..362
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40408
     Region          32..347
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkktllciaf silgvysygq rrplhkavpf kdanaakayl qnqadslkfs gnvlvmqngk
       61 dlikesygla skeknipini dtkinlgsin kaftavcvlq lieagkinfe dkitkyipel
      121 kanmaneisi rnllemksgl gsywdspifl dnyknlrnle dyvpiiaays lsskpgterq
      181 ysnssyellg ilvqrvsgqn yydyvrenvy kkagmvntda ferdksvqnl aqgyskfkvg
      241 edfetqlppe rqyafnynvn drspvkgtaa gggfstvddm kqfvytltsn qllsktstdl
      301 linhfrdspd rnpvynirgg stginsvvfy naskdlliiv lcnydppvgs evarrliatf
      361 ns
//
LOCUS       WP_181899493             284 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Flagellimonas
            nanhaiensis].
ACCESSION   WP_181899493
VERSION     WP_181899493.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas nanhaiensis
  ORGANISM  Flagellimonas nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..284
                     /organism="Flagellimonas nanhaiensis"
                     /db_xref="taxon:2292706"
     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]"
                     /calculated_mol_wt=33093
     Region          <101..282
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mkkhlflinh gnlfamgpll yvfllsinak rnkirihllh lvpfvlfkla vvivdlasvp
       61 vsvqfgkwis yimalyclgy sfgslfylir ksklfskidv rylytligif llgwlfsiva
      121 rivessdygi gqiiwqityi iaglfiyfis wsmikntkil vprtyvydkn pdfeqrlkql
      181 fdedkmylnp tltrqdiakr lnlsnheisy hlsqhlktsf tdfvngyrie efkrkleknd
      241 npnytflgma ldcgfgskas fqrafkkktg ktpseykkev qkii
//
LOCUS       WP_181899676             141 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Citrobacter].
ACCESSION   WP_181899676
VERSION     WP_181899676.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 141)
  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 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   3  (residues 1 to 141)
  AUTHORS   Rosinski,J.A. 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 141)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..141
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     Protein         1..141
                     /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=15853
     Region          61..116
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdkkhiparg eipscigniv fiplnasvsk iskvikqhwf slqqaktpha vhhcgycphk
       61 tltgqqnqla aflyagmtsk qiaykmaigq ktvlahrnal mtkfrlrtdr elllflnavk
      121 eknrhrngmc escndedgwl v
//
LOCUS       WP_181899961             131 aa            linear   BCT 28-DEC-2024
DEFINITION  pentapeptide repeat-containing protein, partial [Mycobacterium
            tuberculosis].
ACCESSION   WP_181899961
VERSION     WP_181899961.1
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 10477883
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..>131
                     /product="pentapeptide repeat-containing protein"
     Region          12..50
                     /region_name="Pentapeptide_2"
                     /note="Pentapeptide repeats (8 copies); pfam01469"
                     /db_xref="CDD:279771"
ORIGIN      
        1 syntgsfnag qantggfnpg svntgwlntg dintgvansg dvntgafisg nysngafwtg
       61 dyqglldfsf pvgplipqth lvhlretvnl gpihidpihv hipplldidq tidlgsftva
      121 pitvapiald y
//
LOCUS       WP_181900614             402 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Paracoccus thiocyanatus].
ACCESSION   WP_181900614
VERSION     WP_181900614.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus thiocyanatus
  ORGANISM  Paracoccus thiocyanatus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus thiocyanatus"
                     /db_xref="taxon:34006"
     Protein         1..402
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43886
     Region          1..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 mqdalkgirv vdfghvlagp yctmqlaslg aevikvetra rpdeqrahrg dgthanlean
       61 snffecnlgk lscsinlttd egralakrlv asadivlenm rpgvmtklgl dydelvkvkp
      121 dlimlslsgf gatgpwrrya aynpcftsvg gvshltgyae kkpntmtnsg gdaragtaav
      181 faamvalrfr qqtgrgqyid ssscevinsm igdqmmdyam nrrsprrhgn sdaamaphnv
      241 yrcagadewi siavgsdaew qglvralgsp dwaqapeyat aegrwihrer ldqsiaawsa
      301 eksyydamrl lqaegvpatp sfkaedlfnd phvlargavq evdhpvlgrr ktitppyrls
      361 rtparirrta pqlgadndhv fktllgmgda eiarledakv iy
//
LOCUS       WP_181900187             903 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Alcaligenes faecalis].
ACCESSION   WP_181900187
VERSION     WP_181900187.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes faecalis
  ORGANISM  Alcaligenes faecalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Alcaligenes.
REFERENCE   1  (residues 1 to 903)
  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..903
                     /organism="Alcaligenes faecalis"
                     /db_xref="taxon:511"
     Protein         1..903
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=99490
     Region          14..867
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 msngthpapq khsrsaqard ddmlafgryq lfpglrlllr dgvrlevger aldvliylve
       61 aagkvvskds llsqiwskdv veenslqaqi sslrktlgdd rdlistefgr gyrftgavqp
      121 hqaaspiiah qtrsklprpr spligrveel lelnrllasq clitlagpag vgktrlaiel
      181 aseasplfpd gvyfadlsql gspasvlpsi ssalaglvgt dtqaashpnr alllvdnceh
      241 vasacahvie qlleadpkls illtsqtplg legeqvfrit plcvpanpik lenaraysai
      301 elfvrrviaa dyhfkltedn ldqitalcra ldgvplalei aaarvpslgl aavaedlais
      361 sgllaarktp ssgrhqtlge amqwsyhlln sreqnafqel aifpgdftls aaeqivsarp
      421 kdstrlpdii yglveksllt lqagtrtiry rylsmlraya leqlgdrqav ladrhahfta
      481 qlasqaqhdw mslptppwrq qyehhiddir taldwafrns qhrslglhil ansapfwiql
      541 slhdegrqri tdalkqstgs sleeqqemmi qaalatsltw srgptpengq awtragelal
      601 qlgdremqlq aeyglwlfhl rsgrytqale hgqnmadlal qfsdraaflt arrligtsyh
      661 flgrhaealf eieamldayv rderhgshfr fgldqrvagw aflsrilwvm gnsnkarhaa
      721 qlaieeaipl dhactlccal aegsctvaal sgdsqevtrm srelnqlagq hglefwaryg
      781 saftlwakva enpaevpfqt lqsaltqlqe hgfdtaysvf lsdfahamie qghspeaval
      841 ikarladeta eeqlwnapel lriqaqammh lpseqpyasa tlqkalslar sqqakawkvr
      901 lka
//
LOCUS       WP_181900619             261 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Paracoccus thiocyanatus].
ACCESSION   WP_181900619
VERSION     WP_181900619.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus thiocyanatus
  ORGANISM  Paracoccus thiocyanatus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus thiocyanatus"
                     /db_xref="taxon:34006"
     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=27885
     Region          7..238
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mnhqdersrf rqrvldgdkl lgafcpapsp elievaaysg fdfvvidaeh gpitisdvvh
       61 mtraahsaga pvivrvpeys gefimrslda gvdgilvpqv eeaaevqrif qamhyppvgv
      121 rglafyarah gftrrtgpea mnsanqhvlt svlvetpkgv enideimavq gldmvlvgtg
      181 dlaanigygp etaakvdaav trvaeagkrh gvttaiagqs addaakfarr gykvmvtgml
      241 phllrfctdf vnasrkgmea d
//
LOCUS       WP_181900616             330 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Paracoccus thiocyanatus].
ACCESSION   WP_181900616
VERSION     WP_181900616.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus thiocyanatus
  ORGANISM  Paracoccus thiocyanatus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus thiocyanatus"
                     /db_xref="taxon:34006"
     Protein         1..330
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34473
     Region          16..329
                     /region_name="TctC"
                     /note="Tripartite-type tricarboxylate transporter,
                     extracytoplasmic receptor component TctC [Energy
                     production and conversion]; COG3181"
                     /db_xref="CDD:442414"
ORIGIN      
        1 mkiqtllsfs stvptaaavi ctiafaggaq aqgdfpsqpi rmivgyapga ivdltarqla
       61 armseelgtp vvvenrpggg gllaneyvsr atndgytvly hdsglvtapa lgrdlnydyk
      121 tdlipvgiav sgvfflygsp gfpadtiqev vaelkenpgk hfygssgngv lnhiafemfl
      181 qatdtkanhv aykgsgpvlv dimadrvels mssapgilpq ykegkvkvfa yggeerspll
      241 pdvptisetv apgftaanwf glavpagtdd aivkrlseal lastsdpafa aamekegaea
      301 vglvgdeaea fiekqavawt evveraglke
//
LOCUS       WP_181901032             251 aa            linear   BCT 28-DEC-2024
DEFINITION  PPE family protein, partial [Mycobacterium tuberculosis].
ACCESSION   WP_181901032
VERSION     WP_181901032.1
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 13657689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..>251
                     /product="PPE family protein"
     Region          <1..186
                     /region_name="PPE"
                     /note="PPE-repeat protein [Function unknown]; COG5651"
                     /db_xref="CDD:444372"
     Region          1..36
                     /region_name="Pentapeptide_2"
                     /note="Pentapeptide repeats (8 copies); pfam01469"
                     /db_xref="CDD:279771"
ORIGIN      
        1 gdfntgssnt gffnpgnlnt gvgntgnvnt ggfnsgnysn gffwrgdyqg ligfsgtlti
       61 paagldlngl gsvgpitips itipeiglgi nssgalvgpi nvppitvpai glginstgal
      121 vgpinippit lnsiglelsa fqvinvgsis ipasplaigl fgvnptvgsi gpgsisiqlg
      181 tpeipaippf fpgfppdyvt vsgqigpitf lsggyslpai plgidvgggl gpftvfpdgy
      241 slpaiplgid v
//
LOCUS       WP_181900643             110 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paracoccus thiocyanatus].
ACCESSION   WP_181900643
VERSION     WP_181900643.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus thiocyanatus
  ORGANISM  Paracoccus thiocyanatus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
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="Paracoccus thiocyanatus"
                     /db_xref="taxon:34006"
     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=12108
     Region          19..106
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 menirpepeq qtdfdalvka ateastflka lghdgrlmil cylmsgpksv telenllssr
       61 qavvsqqlar lrheglvsar rdgqtifysi ldskvvdllt vlkklfgtdc
//
LOCUS       WP_181901102            1633 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Xanthomonas euroxanthea].
ACCESSION   WP_181901102
VERSION     WP_181901102.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas euroxanthea
  ORGANISM  Xanthomonas euroxanthea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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="Xanthomonas euroxanthea"
                     /db_xref="taxon:2259622"
     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=177715
     Region          33..1632
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mrwsgtrrml lwvvllcvai gavackrnes gqlpaasgea ikadkqaitg falaraypdq
       61 tsdglslale fsrplvgtqd fdalvrfeek vgtgdsswtl sddgktlryp yveaakdytv
      121 lvdanllaad gsrlgkplkq kvytgalkpv agfasqgsvl paresrglpv vsvnvpevdv
      181 eflrvreksl paffqqfqrg grrgsweles eyndkqplsr laepvyvnrf ilggkqnerv
      241 ltylptqdik elqepglyfa vmkrsgsfen eqetafftvs diglhtrayk dklfvhtasl
      301 qsgepiknve vrildakgel flkgatdgng nallnytlda ghvlvarskt disvlpfnqp
      361 aldlsefava gresawfdvf awagrdlyrp getmrvsail rdndgkptkp qpvflrlkqp
      421 dgktfretrl qpgeqgyfef tqqipadapt grwqvefrtd paskdavqgm svrveeflpe
      481 rmkldldstq ktlsagqpft llanaaylyg apadgnrfta klavsveqhp laslpgwffg
      541 dptlelprea kdvidttfgs dgvlredial paearpvsti aavvsgsvye tggrtvtrtv
      601 krvlwpakal vgvrplfddk dgtdangtar feltrvdadg kpqpakglka tlvrelrdyh
      661 wnytddhwdy dftrrfenkd trtldiaggn aklefpvewg eyrldvfdpa tglttrypfr
      721 agwswndenr gldarpdkvk laldktgyra gdtltvtltp phagkgvllv esdkllyvqd
      781 idvkpgstfd ipvteawerh dvyvtalvfr ggsapskitp aravgvayvp mdrkarrvav
      841 glaapkqmrp eqalpvtvsv pelagkaahv tisavdvgtl nitrfpvpda naqffaqrrl
      901 gtdaydiygr viesfegasg klkfggdmal ealpqakrpt arvqtvdlfs gsvkldargn
      961 arvqlpvpdf ngtlrvsalv ysetrfgnqs metvvrapil aeasmprvma pgdrstvtld
     1021 vqnftgkpge fnvrvdgigp laiaeaarsv klgvdakqtl sfplsategy svakvrvrvd
     1081 gngfkadrsy dlpvragwpq vlraqtrvld plapisldsg fadglmagsv tarmvvsplp
     1141 pipfasalqg aldypygcae qttskgyaal llddataral gtkgleaakr rermegafgr
     1201 lasmqiasgh fsmwgddgyv npgltpyiae flldakdagf avpdnvlqka lnrlsedlls
     1261 ggnefygqdr rdslkfanqa wsgyvlarvn raplgtlral ydnqrdkalt glslvhlgaa
     1321 lslqgdtkrg qaaikagfak dsserpsyfa dygsairdda lmmallherg lsrpeydtra
     1381 valgraldar ratgwlwlst qeqvalarlg kalmvgqgkq vsgtlsvgge tqqiaparlf
     1441 grsfdsaala rgvqfapqge apmyasleva giprsapepd trtlsversw yttdgkpwtp
     1501 ralkegeali vrvaitansd mpdalltdll pagleienfn lgdakqwadv vvdgigiser
     1561 ssaadvkhee frddryvaal alssgskaql yylvravtpg tytvppslve dmyrpelrgv
     1621 grstpatmtv vqp
//
LOCUS       WP_181901158             328 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Xanthomonas euroxanthea].
ACCESSION   WP_181901158
VERSION     WP_181901158.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas euroxanthea
  ORGANISM  Xanthomonas euroxanthea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..328
                     /organism="Xanthomonas euroxanthea"
                     /db_xref="taxon:2259622"
     Protein         1..328
                     /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=34416
     Region          7..310
                     /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(42,260,263)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(198,231,258,261..262,265)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 msaaknrvvc fgealidmla lpsagpdear tfaqyaggap anvavavarl ggaahfvgml
       61 grdmfgdfll qslqqagvat dgivrtdqak talafvalde agersfsfyr ppaadllfrp
      121 ehfaadaftq aavlhvcsns mtepaiaqct ldgmrrarad gaivsldlnl rpmlwpqdvd
      181 paallweala ladvvklsre eldylagtld gdastvtrkl wqgqaswllv tdgggpvhwq
      241 trtdsgqvpa fdvqvrdsta agdafvggll fqlaarastl eqlcgdavam tavirfaaav
      301 galavtrkga faampsvdev hsliqeqp
//
LOCUS       WP_181901257             279 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Xanthomonas euroxanthea].
ACCESSION   WP_181901257
VERSION     WP_181901257.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas euroxanthea
  ORGANISM  Xanthomonas euroxanthea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Xanthomonas euroxanthea"
                     /db_xref="taxon:2259622"
     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31025
     Region          81..190
                     /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 mragsptlrd rlqqlpeles vdgvfvqrsl addpfeqqyl evrrkegrly tdaqvrslpr
       61 pggklgasle wrvralssal lvrhlraqag egaiaelgcg ngwlsqllaq slqrdvcgid
      121 vnrtelaqaa rvfghdqrls fiaadihtla lprdlfdviv ipaciqyfad paalvirlla
      181 qlrdggelhi ldsplyadah aadasaarsl ryftelgvpa laahyhqhty asfdrfavqr
      241 lfdprgpgar lrrmlklrqp hfpwlclrkq dnldalrpg
//
LOCUS       WP_181901536             327 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Thalassotalea euphylliae].
ACCESSION   WP_181901536
VERSION     WP_181901536.1
KEYWORDS    RefSeq.
SOURCE      Thalassotalea euphylliae
  ORGANISM  Thalassotalea euphylliae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Thalassotalea.
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="Thalassotalea euphylliae"
                     /db_xref="taxon:1655234"
     Protein         1..327
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36912
     Region          5..>122
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mlvepkvsvi ipfyqktkgl lsntiqsiik qtylghiyii vvddgspvti eeelstlstp
       61 dnreliiikq enggagsarn nalnnvpadc qyaafldsdd ewledhlatg ikalelgnda
      121 yfsdhfpalh pdknnfdmig tlivdehlsi dleddihqms isslehivgd gggvigtsnv
      181 vynfrkfptl rfreefyngq dfffwmdlse lkaqwafstk itcrcgrgin iysgsgwgse
      241 kslqrlrnel fiwtsvkkfy pltekleqrn kqtinaiqdn iardilhrii krkaistkil
      301 sdivkmapst lisitlipfk vvlerlk
//
LOCUS       WP_181901586             147 aa            linear   BCT 28-DEC-2024
DEFINITION  TraR/DksA family transcriptional regulator [Thalassotalea
            euphylliae].
ACCESSION   WP_181901586
VERSION     WP_181901586.1
KEYWORDS    RefSeq.
SOURCE      Thalassotalea euphylliae
  ORGANISM  Thalassotalea euphylliae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Thalassotalea.
REFERENCE   1  (residues 1 to 147)
  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 147)
  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 147)
  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 147)
  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 147)
  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 147)
  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 147)
  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..147
                     /organism="Thalassotalea euphylliae"
                     /db_xref="taxon:1655234"
     Protein         1..147
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17096
     Region          25..139
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mqvnqavskl pstqqlleap esnymndeql affkkhlidl hdstrerire akeqmlsppd
       61 lsdisdrasw eeqcailmri vdreqkllpk iqqslerirl geygycletg epigiprlla
      121 rptaeycadv kiyqelkehi yhkqret
//
LOCUS       WP_181901671             294 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Thalassotalea
            euphylliae].
ACCESSION   WP_181901671
VERSION     WP_181901671.1
KEYWORDS    RefSeq.
SOURCE      Thalassotalea euphylliae
  ORGANISM  Thalassotalea euphylliae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Thalassotalea.
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="Thalassotalea euphylliae"
                     /db_xref="taxon:1655234"
     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=31249
     Region          12..261
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mqqaqetaas dsmkdktvli tgasagvgae aarvfaaqga nlvliargqq aldeitqels
       61 aqvkvmsqtl dvndlsqfep llesvmqefg ridvlvnnag yhqrgdaigi apediaqmvd
      121 vnlraplvfs rqvipymkan gggaivnigs lagrmplqgg aaygatkagl rsftyalgde
      181 lkpfnihvgv vspgpidtgf imsnidqved ivfsqemssa rqvadaaltv aqgkerevcl
      241 pasgglltti sylfpwlrtk lrpamyrkga klkakykarn lalkqalkqa nkqa
//
LOCUS       WP_181901743             103 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Thalassotalea euphylliae].
ACCESSION   WP_181901743
VERSION     WP_181901743.1
KEYWORDS    RefSeq.
SOURCE      Thalassotalea euphylliae
  ORGANISM  Thalassotalea euphylliae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Thalassotalea.
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="Thalassotalea euphylliae"
                     /db_xref="taxon:1655234"
     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=11479
     Region          1..98
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnpeqlhqqv tlassylkrl shpvrllvlc tlvegersvs elselselan vsqsalsqhl
       61 avlrehglvs trresqtify sladehciki idvlheifcp tse
//
LOCUS       WP_181901828            1034 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Xanthomonas
            arboricola].
ACCESSION   WP_181901828
VERSION     WP_181901828.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas arboricola
  ORGANISM  Xanthomonas arboricola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1034
                     /organism="Xanthomonas arboricola"
                     /db_xref="taxon:56448"
     Protein         1..>1034
                     /product="beta strand repeat-containing protein"
     Region          <138..1034
                     /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 mstnltasgg vrsllrwmla llllatsqva laaycptpks atvnsggsvs fevgdcdgps
       61 nfgmtdpgvp pahgtyslpg qnpdsteqvt ytnngdgats dsfylldedn nqivfnitvn
      121 psrtasiavs pssrnedsga aftytvtlsq tsssattinl srsgtatsgt dytgapssiv
      181 vpanattatf svtpvadttv eadetvvisv asgsgygigs pssatativn ddfpnasiav
      241 apssvaedga gnliytvtld qaapsavsva fsvggtatsg tdyaavsspl vigagqttgt
      301 itinptadst iepdetvvlt lasgtgynvg spnsatgtil nddqptlsin dvsvnegnag
      361 ttnatftvsl sqpagtggvs fdiatadgta tagvdyvass ltgqtipags ssatftvlvn
      421 gdtlsepnet ffvnvsnvtg asvgdgqgqg tivnddalpa lsiddvsvne gnsgtttatf
      481 tvslsaasgq tvsvnyttad gtatagsdyv arsgtltfap gvtaqgvait vngdtaveps
      541 etfsvglsga snasiaratg tgtivnddvv vtvgpaslpa atagsaysqt lsasggtapy
      601 tftvtagalp aglslsaggv lsgtptasgg fnftatatds ggsptsgara ytltvavatt
      661 tfpatslpag tagqayssal npatggvapy tyavtagalp agitldgssg altgtpgsvg
      721 sfsfsvtatd sttgtpsqat rsytltiaap pivvapstlp aatrgtaysq tlsasggtap
      781 ytyalasgtl pagitlasng tlsgtatveg sfnvtvtatd agsftgnqay tltvagpnlv
      841 lpastlpagt agqayaatia satggtapyt yaltggvlpa gvvvdaatga lsgtptvagt
      901 fnftltasds tpspaaqasr sytltiaapv vvivpttlpa atrgtaysqt lsasggtapy
      961 tyalasgtlp agitlasngt lsgtatvegs fnvtvtatda gsftgnqayt ltvagpnlvl
     1021 pastlpagta gqay
//
LOCUS       WP_181901786             429 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Thalassotalea euphylliae].
ACCESSION   WP_181901786
VERSION     WP_181901786.1
KEYWORDS    RefSeq.
SOURCE      Thalassotalea euphylliae
  ORGANISM  Thalassotalea euphylliae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Thalassotalea.
REFERENCE   1  (residues 1 to 429)
  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 429)
  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..429
                     /organism="Thalassotalea euphylliae"
                     /db_xref="taxon:1655234"
     Protein         1..429
                     /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=47522
     Region          2..428
                     /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 mefkikfalt cfvlafitlv vllttawgws mlatvtsvfl lsyplcwlaw rtwqfwsssi
       61 mrlttytqsl amgesgvsla qrgkstlldd lsdeitqlyq qstvnsgana sltmlfgqlf
      121 edlpiavvif eqdytlsyan raaydiaeis llqgmsakal gfveqnkqln hsalasnwrc
      181 qsslinfqqq pihlftaidi aselkqseqa vqknlvrvls helrntltpm ssmaetllsm
      241 qtldtvqtrk vlervktrss gllnfverfa evakipepnk erfelpalve qtkvlltekd
      301 sltftgqhic yadsqlmaqv lmnlvknave skdtqgvvik vnyyqqdnqq ylsvidngtg
      361 fsnidnaitp lfttkangag iglafvetvl nkhggvvrls nvadsdvkvg nqdnagigak
      421 veliwplqs
//
LOCUS       WP_181902068             712 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Ectopseudomonas oleovorans].
ACCESSION   WP_181902068
VERSION     WP_181902068.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas oleovorans
  ORGANISM  Ectopseudomonas oleovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
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="Ectopseudomonas oleovorans"
                     /db_xref="taxon:301"
     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=80071
     Region          24..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 mecplpqteq gpvllvvddr lenllamqav levgnwrvit aasgeralqy lldetvdlvl
       61 ldvqmpimdg fevarimrsn lrtrftpiif vsaeahsyes vlrgyatgav dyllkpvdpn
      121 ilrhkvrsll dhernrrell qatqqlelak sfsdslldna aegiltvneq grvtfanaai
      181 armlrcsvsd lvhanfldfl eggsglddwq tspfmehydr retyrlhdar lrtnrgdslp
      241 valscaplpr mqramviial dmsrmrelqd qlesqavtda ltgllnrrgf nqtleaalar
      301 sgrngkrmav lyidldgfkr indslgheag drvlcivaeq lkscmrpydi larmggdeft
      361 alldslehpe daarvaekll ellatvhrid gmevslgasi giasypdcgh tvdgllrsad
      421 iamyeakrgg rqqyrffspd mngrarsrlm leesvrnaid nkdfvlayqp qvylrdgrlr
      481 gfeallrweh tvagkvspnv fiplleetrl inrigdwifr egatklqslq eiygdellls
      541 inlspvqfgm pqlaeslrqi iethglrpeq leievtesal mhdidytraq lsqlralgvr
      601 iavddfgtgy sslaylrhfe ldtlkidqlf ianmldssrd aaivstilel grnldlevia
      661 egvetleqrd wliehgceim qgflvsrpls aevtgrfpqq vdwtarrpep tl
//
LOCUS       WP_181902326             231 aa            linear   BCT 28-DEC-2024
DEFINITION  PPE family protein, partial [Mycobacterium tuberculosis].
ACCESSION   WP_181902326
VERSION     WP_181902326.1
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 13657689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..231
                     /product="PPE family protein"
     Region          16..52
                     /region_name="Pentapeptide_2"
                     /note="Pentapeptide repeats (8 copies); pfam01469"
                     /db_xref="CDD:279771"
     Region          <29..213
                     /region_name="PPE"
                     /note="PPE-repeat protein [Function unknown]; COG5651"
                     /db_xref="CDD:444372"
ORIGIN      
        1 dhqmgfggfn sgsgnigfgn sgtgnvglfn sgsgnigign sgslnsgigt sgtinaglgs
       61 agslntsfwn agmqnaalgs aagseaalvs sagyatggms taalssgila salgstgglq
      121 hglanvlnsg ltntpvaapa sapvggldsg npnpgsgsaa agsganpglr spgtsypsfv
      181 nsgsndsglr ntavrepstp gsgipksnfy pspdresaya sprigqpvgs e
//
LOCUS       WP_181902676             440 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Lysobacter soli].
ACCESSION   WP_181902676
VERSION     WP_181902676.1
KEYWORDS    RefSeq.
SOURCE      Lysobacter soli
  ORGANISM  Lysobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Lysobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..440
                     /organism="Lysobacter soli"
                     /db_xref="taxon:453783"
     Protein         1..440
                     /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=46407
     Region          38..>97
                     /region_name="AllB"
                     /note="Dihydroorotase or related cyclic amidohydrolase
                     [Nucleotide transport and metabolism]; COG0044"
                     /db_xref="CDD:439814"
     Region          75..419
                     /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(93,95,261,281,354)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mlkplslall aaiasipvha eaqtaapakd aaqalqcgqv fdarsgkltg pqtllvrngk
       61 ieqviggasa dvagatrvdl sghtcmpgwt dlhvhlgsqs spqsysegfr lddvdyafrs
      121 vdyakktlma gftsvrdlgg evsphlrdai nqglvsgpri waagksiatt gghadptngy
      181 ndalshligp pgptegvins iddarqavrq rykegsdvik itatggvlsy aksgdapqft
      241 veevkaivdt akdygyrvaa hahgeegmkr avlggvtsie hgtymsdevm klmkqhgtwy
      301 vptiyagrfv adkakidgyf pdvvrpkaqr igaliqqtaa naykngvkia fgtdmgvgph
      361 gdnarefiym veagipapva fqaatiraae vlgvddqgvi evgkradiva vpgnplediq
      421 qvmkvdfvmk dgavfrtpea
//
LOCUS       WP_181902732             512 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Lysobacter soli].
ACCESSION   WP_181902732
VERSION     WP_181902732.1
KEYWORDS    RefSeq.
SOURCE      Lysobacter soli
  ORGANISM  Lysobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Lysobacter.
REFERENCE   1  (residues 1 to 512)
  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..512
                     /organism="Lysobacter soli"
                     /db_xref="taxon:453783"
     Protein         1..512
                     /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=55556
     Region          <353..500
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mqrsatdpda rdsfggrgps lagpealgis rtlawialag vafqaffain dlgrhvpnmh
       61 peygtfvall amafagsrpw relaahpavr llgvlavvli vhaayiawll pevrwsnqlt
      121 vvakllrlgf qtcvigwwms vnpraipkll gvlilgllaa vlyhmpwsam paiwsgemrp
      181 wfgisqnlsg miaavggwlt lclligiwrd yprgsrriwl lvlallafag cfcvllfsqs
      241 rgawlsfiva vplaiigyaf trgprrrplp wqpivlallv clilltaahr ifalrfdgan
      301 qlvpawvesl legksasdan avpagpapap apgstidapa sdaiaqapad pralprdidg
      361 ldttipgnka vgirmmlyre gverflerpl fgwgldtipl liqraqlptg geqfvhlhna
      421 yldalvglgv igaallfavf amlmrelwla wrtgivstas fwglagcvgi vliannfdsl
      481 lwrfeyvrap lgllfgccma yglirerrar eg
//
LOCUS       WP_181902782             572 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Lysobacter soli].
ACCESSION   WP_181902782
VERSION     WP_181902782.1
KEYWORDS    RefSeq.
SOURCE      Lysobacter soli
  ORGANISM  Lysobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Lysobacter.
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   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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..572
                     /organism="Lysobacter soli"
                     /db_xref="taxon:453783"
     Protein         1..572
                     /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=61731
     Region          263..411
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mrlaivvlal apvacrspge srphveccsp qlqpatveah edaarawans arrastpaaa
       61 grawllcaah aydalkggaa ssndmanlat rctddflgya ltqnrswskg plrvagtels
      121 vefrqlsryl vppldvtlar evsmelyrgk rfstdgfgvp lallgkrced apecsllppe
      181 gvfrgatawv etdahrrpvl vlsdplrtpq vtigashyll asdtsaawar gaqtsklhrl
      241 gvwglfggre vgrragvfll edydpdkkpl vmihglgssp lmwaglsnei wgdaalrsry
      301 qvwhvvyqtn apllvnrlrv qgyldaawka ldpegddfar snmvlvghsl ggvvarmlcs
      361 dsgdvlwnaa fvtdagrmha aqsdlaivda tfhfkaypgv graiflaaph rgsptatrwf
      421 grvarvlvgr rapeiqslrr vaqanpeavq pelldrylrg wvnsistlqs aqpvraager
      481 lmpregiayh tiagalpryd fesdgvvpva stlldgaqst lvvryghdle espealaeis
      541 rilhedvacg pgwpgdlpss taacatpsfs re
//
LOCUS       WP_181902058             453 aa            linear   BCT 28-DEC-2024
DEFINITION  cation:proton antiporter [Ectopseudomonas oleovorans].
ACCESSION   WP_181902058
VERSION     WP_181902058.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas oleovorans
  ORGANISM  Ectopseudomonas oleovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
REFERENCE   1  (residues 1 to 453)
  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 453)
  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 453)
  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 453)
  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 453)
  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..453
                     /organism="Ectopseudomonas oleovorans"
                     /db_xref="taxon:301"
     Protein         1..453
                     /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=48551
     Region          13..>451
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
ORIGIN      
        1 mtflvwvgvl gsllmilalt saylrwlpvt tsvvclafgm lispiglgla evdfqqsatw
       61 ighltevavl fslfvsglkl rlsfhrsswh gayllagpvm ilsiagvclv ahyllglpwg
      121 valligaila ptdpvlaglv qvnhaqdfdr vrfglsgeag lndgtafpfv llgllllqhg
      181 elqwgwtlew flknvvwgvp aglllgyamg kgvgrlmifl rtrhgdstis pndflalali
      241 alsyvladei gafgflavfa aglglrqaev qtsgnaetps eqlaqpvigh ltgaperatv
      301 anaedieepr maagvmmgdm lafgslvers fevllvtllg vvlithwdsr alllgallfv
      361 virplgvasm lpftridrhq galigwfgir gigslyylcy althqvtadw agtivdltls
      421 vvalsiavhg isiqplldry erltarregs arp
//
LOCUS       WP_181902844             360 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Lysobacter
            soli].
ACCESSION   WP_181902844
VERSION     WP_181902844.1
KEYWORDS    RefSeq.
SOURCE      Lysobacter soli
  ORGANISM  Lysobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Lysobacter.
REFERENCE   1  (residues 1 to 360)
  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..360
                     /organism="Lysobacter soli"
                     /db_xref="taxon:453783"
     Protein         1..360
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=39807
     Region          14..360
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 maattpatka vpkrrlravl swlhlwtglt aglvfalasl agtvlvfhvd llklqhpqla
       61 qhapvadgrv laqlierwgp dgmrsldvpr delpvwqayf edghrqyfap edgalllyrs
      121 qhddvllwlh ewhvdllggk tgrevwgvig cislamilig lylwwpkrgr liaqlkmhag
      181 ppvrrwltwh rstgvillpl lllatvtgvg mvyskafqka ltatlggknv kapelpasea
      241 aidwttaian arvaipdarl arvsvpdase gavsfrlqak dewhpvgrst vvmsrdgrvv
      301 qafdatthkl gmrmsqafyp lhvgavggta mkwitaftgl lpmfllvtgf lfwrrrrgkr
//
LOCUS       WP_181902880             138 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Lysobacter soli].
ACCESSION   WP_181902880
VERSION     WP_181902880.1
KEYWORDS    RefSeq.
SOURCE      Lysobacter soli
  ORGANISM  Lysobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Lysobacter.
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="Lysobacter soli"
                     /db_xref="taxon:453783"
     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=15408
     Region          57..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 mstiadatvv etqricvglq afnraavgei estpihlaak dddgeliggi vgevllgwle
       61 ihvlwlredv rsqghgaall hacerraiei gahsarldtf dwqaeafyrr hgyerfavld
      121 gypdtherif mrkrlstr
//
LOCUS       WP_181902885             386 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Lysobacter soli].
ACCESSION   WP_181902885
VERSION     WP_181902885.1
KEYWORDS    RefSeq.
SOURCE      Lysobacter soli
  ORGANISM  Lysobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Lysobacter.
REFERENCE   1  (residues 1 to 386)
  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 386)
  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..386
                     /organism="Lysobacter soli"
                     /db_xref="taxon:453783"
     Protein         1..386
                     /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=41621
     Region          166..375
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mmhrflianr delaarcrvk vqarsaygvp gaelehgisv fleqviktle leqtadplqs
       61 rrvsgraggg kpalseigdt aarhgkelmq hgftveevvh dygdlcqait dlafeldaqi
      121 eveefrilnr cldnaianav tefgyqrdiv vadqhvhdln arlgflahel rnqlatatla
      181 lsairngsvg vtgatggile rslvnlgnli drslaevrmt aglplqsrlf svheflaelr
      241 lsasleadir gftlkvsnvd pslavdvdrd lllaaagnll qnafkfshph teitvnayav
      301 adrilidved rcgglssgda ekmflpftqq aqdrsglglg lsisrrsiea nagllsvrnv
      361 pgtgcvftid lprhslgdep tvfagq
//
LOCUS       WP_181902941             561 aa            linear   BCT 28-DEC-2024
DEFINITION  pyrroloquinoline quinone-dependent dehydrogenase [Methylovirgula
            ligni].
ACCESSION   WP_181902941
VERSION     WP_181902941.1
KEYWORDS    RefSeq.
SOURCE      Methylovirgula ligni
  ORGANISM  Methylovirgula ligni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Beijerinckiaceae; Methylovirgula.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Methylovirgula ligni"
                     /db_xref="taxon:569860"
     Protein         1..561
                     /product="pyrroloquinoline quinone-dependent
                     dehydrogenase"
                     /calculated_mol_wt=60828
     Region          36..558
                     /region_name="Gcd"
                     /note="Glucose dehydrogenase, PQQ-dependent [Carbohydrate
                     transport and metabolism]; COG4993"
                     /db_xref="CDD:444017"
ORIGIN      
        1 mkrsskhaia falvgaflsl easalradsl avgnadpdnw sqyhrtwnaw rysplaqina
       61 gnvkrlkvaw lhqagditng llstplveng vmyyiapnnn vfaldatngk tiwhyqpkln
      121 pianesfyaf qsrnitlgkd yvyvgtldgr vvavdkktgn evwstqltdl ktcygclfss
      181 tpmlagnvli ggttggdqpi agrifgvdat tgkllwtlrt tkddpkswpg dtwkvggsaa
      241 wnvgtydpet dtayigvgna apdffyndrh gdnlyaatll aldpktgsik whrqeipgdh
      301 ydydstyeav viddgkredi vhlnksgfvf vmnkangklv nvwpmvkhyn faktidpktg
      361 aligqvldyp edkettvcpy llgerswnpg aynpktrlwy nnamevcevl kparqdvski
      421 giaglylgve kleavpppge aasarleard pltgklvwev pyalpglggv lttggdlvfn
      481 gdpeglvhay nagtgkelws fqtgsgirag iisyavngrq yiavpsgwgs lapgfmasvf
      541 pqaakipgga tmvvftldse k
//
LOCUS       WP_181902974             448 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Methylovirgula ligni].
ACCESSION   WP_181902974
VERSION     WP_181902974.1
KEYWORDS    RefSeq.
SOURCE      Methylovirgula ligni
  ORGANISM  Methylovirgula ligni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Beijerinckiaceae; Methylovirgula.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..448
                     /organism="Methylovirgula ligni"
                     /db_xref="taxon:569860"
     Protein         1..448
                     /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=49479
     Region          45..410
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtpdradvpt lrelaggrwr kaignipyww eaappengkd tplpqkvdvv iagsgftgls
       61 aaltlaregr rvvvvdagvp gfgastrngg qvgsgnqkfr vktliamkge rkavellheg
      121 vemldgierl iqrehidcdf trcgrfrgam rpehyeamar dmkdlrryad vesemiprae
      181 qrkeigtdlf yggsllpqda slhpgryhag llarvrdvgg lvranaavkd ivseknrhlv
      241 rfdgfdvear dvivatngyt knvgpffakr ivpvvsaqia tgpippelfd tlfpkrrvfg
      301 nsnrvffyfr papgeyrliw ggrsshiarr gsaaayahla sdllrafpel geiklshawd
      361 gtigytfdef phlgrtvdgi hyamgycgtg vsrathfgrk ialqllgkpe gesafsdlsf
      421 pshplhfaak ravplietwy rlrdtgnf
//
LOCUS       WP_181903123             810 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Marinomonas pollencensis].
ACCESSION   WP_181903123
VERSION     WP_181903123.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas pollencensis
  ORGANISM  Marinomonas pollencensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 810)
  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 810)
  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 810)
  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 810)
  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..810
                     /organism="Marinomonas pollencensis"
                     /db_xref="taxon:491954"
     Protein         1..810
                     /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=91222
     Region          153..794
                     /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 mlalrkrlsy kqakwalglm lllsvvmssf qifsdwreek asihqritaa fnavesatte
       61 aaytlnsrla eqiltgliqs nvfrevtlkd dldnqlayly rpakaspfqw iseflfsdlt
      121 knlefplqyd nqltvgtvig vvdvgavtss fvsrslrlmg tilvmtllfg vammtlfylq
      181 tsrplnrfia klsllsdntl gndtlkfeea srndelgvla rtflalwhqq kyvenkleks
      241 eayfkavlhq ssecmllanl kgrildcnse acyllgydqd alltlniqdi dprhrlpsva
      301 vdfkeaeevq vfeseflrsd ghyipvevrs nvisldgkph flasmrdite rkkdqekvky
      361 layydaltel pnrrffnerl eqavdnathl gviggllfid ldrfknvnds fghhagdtvl
      421 vrtakrvqal lseqdmvari ggdefvallp dlssddekar ekvtrlanei ltalsrpihl
      481 nhteillsas igislfpleq sdamsilqka dtamyqakes grgslyfynd emrnsvaerl
      541 amekalhyal erdefylvyq pqvdgngnil gfeallrwhs kelgqvppsr fipiaeetgf
      601 iaelgqwvld tacqqlkkwq eaglpplfka lainispsqf akdsfvetie qviertcidp
      661 slldleiteg mlvesissva akmrslkkqq vhfsiddfgt gysslrylqh lpldqlkidq
      721 sfvrdishdp nshviintiv smarhmnlsv laegveyvee kniltgigct rfqgyyfsrp
      781 vdvqsatnll anasclplel vpqeaeavad
//
LOCUS       WP_181903368             155 aa            linear   BCT 28-DEC-2024
DEFINITION  PucR family transcriptional regulator, partial [Mycobacterium
            tuberculosis].
ACCESSION   WP_181903368
VERSION     WP_181903368.1
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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..155
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..155
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <1..130
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 dariaigata pgiegfrrsh rdalttarmi irlesphrva fftdvemval ltenaegadd
       61 fiqrtlgnle saspalkttl ltfinqqcna sraarllfth rntlmnrlet aqrllprpla
      121 dttihvaval eaqqwrekqt sdppakkesn gtkmr
//
LOCUS       WP_181903818             126 aa            linear   BCT 28-DEC-2024
DEFINITION  pentapeptide repeat-containing protein, partial [Mycobacterium
            tuberculosis].
ACCESSION   WP_181903818
VERSION     WP_181903818.1
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 10477883
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..>126
                     /product="pentapeptide repeat-containing protein"
     Region          12..50
                     /region_name="Pentapeptide_2"
                     /note="Pentapeptide repeats (8 copies); pfam01469"
                     /db_xref="CDD:279771"
ORIGIN      
        1 syntgsfnag qantggfnpg svntgwlntg dintgvansg dvntgafisg nysngafwtg
       61 dyqglldfsf pvgplipqth lvhlretvnl gpihidpihv hipplldidq tidlgsftva
      121 pitvap
//
LOCUS       WP_181903906             877 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein [Paenirhizobium
            selenitireducens].
ACCESSION   WP_181903906
VERSION     WP_181903906.1
KEYWORDS    RefSeq.
SOURCE      Paenirhizobium selenitireducens
  ORGANISM  Paenirhizobium selenitireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Paenirhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..877
                     /organism="Paenirhizobium selenitireducens"
                     /db_xref="taxon:448181"
     Protein         1..877
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=86773
     Region          <12..871
                     /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 mttqifddil igtgavnitd daqvtanavi gladgvfdlg mtaygsghvi evlgaiygta
       61 gslimgtdas ffsdnqlivg stgtlfttgd gvlilggqss vhndgainge sgiilhadsg
      121 vttstitntg siishsttni gnagiahfgs etlvvvnsgl irglqsfrat sttstdeitn
      181 sglmvgdill gagndlydgr lgrvsgevqg gagddilrgg dggetlyggd gadtlegngg
      241 adtlvggdga dtldggagad tldggsgndt fvvdnagdvv ieadgqgddt vnaaisyalt
      301 dhverltltg aaninatgng ldntltgnag dntldggiga dtldggsgnd tyfvdnagdv
      361 vieadgqgdd mvnaaisyal tdhverltlt gaaninatgn gldntltgna gdntldggig
      421 adtldggsgn dtyvvdnagd vvieaantgt dtvqssisla lganlenlvl lgsatinglg
      481 nslnntlsgn agnntlnggt gadrmeggag ndtyvvdnag dvvveavnag tdtvranrsy
      541 tlganlenlv ltgtanlngs gndlanlltg nsgnnvlngh ggadtmagla gndryivdsl
      601 sdvvvetvgn gtdtvqtavn wtlgdnfenl tllgagnlng tgnglanimt gntgnnilng
      661 rggadtmagl agndtyvvds vadvvteavv qgtdtvqaav nwtlgdnien ltllgagnih
      721 gvgnalnnlm tgnsgnniln ggggndting gaeadrlygn vgndtltggt gtdafvfhst
      781 pnaatnvdti tdfsvaddai wlengvftal gavgalaasa fvrntsglaq dasdriiyes
      841 dtgnlfydsn gnaaggsvli avldpalllt nldftvi
//
LOCUS       WP_181903942             393 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Paenirhizobium selenitireducens].
ACCESSION   WP_181903942
VERSION     WP_181903942.1
KEYWORDS    RefSeq.
SOURCE      Paenirhizobium selenitireducens
  ORGANISM  Paenirhizobium selenitireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Paenirhizobium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Paenirhizobium selenitireducens"
                     /db_xref="taxon:448181"
     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=42447
     Region          1..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 mrflafdglr glfsllvvla hvpaatvlrq sglsatgdtl vdlffvfsgf viaagyekrl
       61 lqgygtgrfl ierlgriypi hfvmlmvfia teiafatllg slgqqgrapf egdksveaif
      121 thltlihawn vhdiptwnyp twslstewaa yivfafallv lrrrfttaav vgigvsivvl
      181 ltvapngmqs yhdygvfrsi lgfsagvlay rtydalnrrq afsalsrpvf taleigglag
      241 lfglqvsfga tdfavalplv ftllmivfay gkghvsalmg srplvylgti slsiyvvhvw
      301 iimragnvaa laerltglnl vtyvaegdsr hlelalppla anllallvva gvvlvshfty
      361 ryvelpgqal frrlakplap avtgpgrava vnp
//
LOCUS       WP_181904567             234 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: esterase/lipase family protein [Microbacterium].
ACCESSION   WP_181904567
VERSION     WP_181904567.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium
  ORGANISM  Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
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"
                     /db_xref="taxon:33882"
     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=24949
     Region          48..149
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mskdavntvr qrirtglrda awwardylya araqvrsarg rdapdvladg egtpivllpg
       61 iyetwrflep laralhargh pvhvvtelgg nrrpiaesae rvaallisrg lddvvilahs
      121 kggligkhvm afspagervr amvavatpfg gsrysrlmpt pslrafasad atiralaasa
      181 aantrivsvf gvfdphipeg selagarnvv lasgghfrvl ddprvvaevi rvae
//
LOCUS       WP_181904662             179 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase [Microbacterium sp. AG157].
ACCESSION   WP_181904662
VERSION     WP_181904662.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. AG157
  ORGANISM  Microbacterium sp. AG157
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
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 10140408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Microbacterium sp. AG157"
                     /db_xref="taxon:2183993"
     Protein         1..179
                     /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=19641
     Region          5..159
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04693"
                     /db_xref="CDD:467575"
ORIGIN      
        1 maddemwdvt diqgtptgtl hrrgdgpvpt gsfhivasvc lvsssgrvlm slraagkdyp
       61 lawefpagsa lrgetsrtga vrelaeetgm vltpddlvlv grvveesalf dlwvariege
      121 pvpvpdpeev qdaewvtldv vhqrwqdgvf atpwnarfdq lwetleqrva emrdrvdga
//
LOCUS       WP_181904676             352 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Microbacterium sp. AG157].
ACCESSION   WP_181904676
VERSION     WP_181904676.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. AG157
  ORGANISM  Microbacterium sp. AG157
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
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
REFERENCE   3  (residues 1 to 352)
  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 352)
  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..352
                     /organism="Microbacterium sp. AG157"
                     /db_xref="taxon:2183993"
     Protein         1..352
                     /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=35800
     Region          20..348
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 migsltapap aalasvvdgr krrrrkwvlv tgiltflvvg afslslmlgq tayspvevwg
       61 vltgqrvpga sftvgelrlp ravtglftgl cfgmggvvfq smlrnalasp dvigintgas
      121 aaavigivvf gmgettvsfl amaaalvaal tiyllayrng gsgarlilvg igvaamcqav
      181 vsyviaraae ydlpaamrwi tgnlndatwd ralpvagavv vlapvllgls grleilrmgd
      241 dtaaavglpv ersrllliva avgllafgta aagpiafvsf lagpiavrll gpvgspilpa
      301 glvgallvlv adfcaqyafg trlpvgvitg vlgapyliyl lvrssrtggt tl
//
LOCUS       WP_181904559             200 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Microbacterium
            sp. AG157].
ACCESSION   WP_181904559
VERSION     WP_181904559.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. AG157
  ORGANISM  Microbacterium sp. AG157
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 200)
  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..200
                     /organism="Microbacterium sp. AG157"
                     /db_xref="taxon:2183993"
     Protein         1..200
                     /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=21717
     Region          <19..129
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mivaqwidrs eygaggrplr raagrallsd tarllglggl rvrrrpgqrp eaetpgvwfs
       61 mshtgdltvc avatsnvaid ieqqnarrer rmvsgppvrf ftaaerelia rdpsrllpvf
      121 takeawakyl glglalgfgs fdeasviard pgveftrvfi dgtvgtavhr ageglvirrr
      181 slrpeqlaag adidraerar
//
LOCUS       WP_181903724             399 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Priestia
            megaterium].
ACCESSION   WP_181903724
VERSION     WP_181903724.1
KEYWORDS    RefSeq.
SOURCE      Priestia megaterium (Bacillus megaterium)
  ORGANISM  Priestia megaterium
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Priestia.
REFERENCE   1  (residues 1 to 399)
  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 399)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 399)
  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..399
                     /organism="Priestia megaterium"
                     /db_xref="taxon:1404"
     Protein         1..399
                     /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=46513
     Region          38..399
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mvkrmlfilv cglclclffq wdvkkgynay vrvhplietp vyqgeialya qgsslypalf
       61 edikkakkyv yiqffiirad nismklfkll kekaaegvkv klsvdrfggn dlsrtliddl
      121 kkngveftfs rkaskqhffy sinhrnhrkf vlidgqeayl ggfnigeeyl gkhkklgywr
      181 dyhlrikgeg ifeiekqflk dweedtgqhi spqrvpiars nganyqllfs tgeeleqkmi
      241 dlinrakvkl tiatpyfips ehlmnalisa kekgvlidii lpdntdawft kppsypktek
      301 llnkgirifl ykkgffhgkv mvidhtiani stanwdprsf ylndeascli ydremiahie
      361 reinedktns rrltktvige ipkwerslkk tpewiyyyf
//
LOCUS       WP_181904918             619 aa            linear   BCT 28-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase, partial
            [Mycobacterium tuberculosis].
ACCESSION   WP_181904918
VERSION     WP_181904918.1
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 619)
  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 619)
  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 619)
  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 619)
  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 619)
  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: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..>619
                     /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]"
     Region          10..619
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mtfepapdga dpylwledvt gaealdwvra rnkpttaafc daefermrve alevldtdar
       61 ipyvnrrgny lynfwrdaan prglwrrttl dsyrtdspgw dvlidvdelg raddqkwvwg
      121 gagviepdyt raliglspgg sdasivrefd mltrefvedg fqlppaksqi twedpdtvll
      181 gtdfggdslt tsgyprvikr wrrgkplada etifegagtd vrvnasadrt pgfertllgr
      241 aldfwneevy elrgseliri eaptdasvsi hrdwllielr tdwtvattry tagsllaaey
      301 deflagsael qvvfepdeht alyqyawtrd rllivtladv asrveiatpg swrreplsgi
      361 paatntvivs adshgdeffl dssgfdtpsr lmrgtddgrl aeiksapaff daenmavtqy
      421 fatsddgtsi pyfvvrrtda dnpgptllng yggfetsrtp tydgvlgrlw larggtyala
      481 nirgggeygp gwhtqamreg rdkvaqdfaa vatdlvtrgi ttaeqlgarg gsnggllmgi
      541 mltgypekfg alvcdvplld mkryhlllag aswmaeygdp dnpddwkfis eyspyqnisa
      601 nrkyppvlmt tstrddrvh
//
LOCUS       WP_181905127             247 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aestuariispira insulae].
ACCESSION   WP_181905127
VERSION     WP_181905127.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
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="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..247
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27849
     Region          25..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 mktfllflav wigcmspvsa rlllvtldyp pyeymedgea rglavnvvre vfrrldedie
       61 iqsfpwarsl kmvelgnada iftayrtser eafldyssev lmpqevslfv rntskietya
      121 tladladqqf aarhgvsygq afdravtdgt ianihrvsdg dtvirllmng radvvvfnrl
      181 ggiyrfrslg vsdqvrelqp plqsvpsyia fskknrlanl rdrvdatlra mkedgtyqal
      241 tvyqliq
//
LOCUS       WP_181904982             443 aa            linear   BCT 28-DEC-2024
DEFINITION  purple acid phosphatase family protein, partial [Mycobacterium
            tuberculosis].
ACCESSION   WP_181904982
VERSION     WP_181904982.1
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 443)
  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 443)
  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 443)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..443
                     /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]"
     Region          <2..64
                     /region_name="Pur_ac_phosph_N"
                     /note="Purple acid Phosphatase, N-terminal domain;
                     pfam16656"
                     /db_xref="CDD:465220"
     Region          127..439
                     /region_name="MPP_superfamily"
                     /note="metallophosphatase superfamily, metallophosphatase
                     domain; cl13995"
                     /db_xref="CDD:472684"
ORIGIN      
        1 tdtvgnprvm lgtptsgfgs vvvaetrsyr daksntevrv nhahltnltp dtdyvyaavh
       61 dgttpelgta rtapsgrkpl rftsfgdqst palgrladgr yvsdnigspf agditiaier
      121 iaplfnling dlcyanlaqd rirtwsdwfd nntrsaryrp wmpaagnhen evgngpigyd
      181 ayqtyfavpd sgsspqlrgl wysftagsvr vislhnddvc yqdggnsyvr gysggeqrrw
      241 lqaelanarr dseidwvvvc mhqtaistad dnngadlgir qewlplfdqy qvdlvvcghe
      301 hhyershplr galgtdtrtp ipvdtrsdli dstrgtvhlv iggggtskpt nallfpqprc
      361 qvitgvgdfd pairrkpsif vledapwsaf rdrdnpygfv afdvdpgqpg gttsikatyy
      421 avtgpfgglt vidqftltkp rgg
//
LOCUS       WP_181905119             171 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Aestuariispira insulae].
ACCESSION   WP_181905119
VERSION     WP_181905119.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
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="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     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=19416
     Region          76..162
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 maividhlic tdgmreelta ltaravksty yrddltqaqr danqriidia ydsclaanrn
       61 dqqavlgawv edelsgfvis tihgeenrel dwlmvdpvhh gqgvadtlmr aglewldpmt
      121 diwlntirfn sraihfyqry gfaidetaqs hhvvpnvimr rpprplsneg r
//
LOCUS       WP_181905174             474 aa            linear   BCT 28-DEC-2024
DEFINITION  S8 family peptidase [Aestuariispira insulae].
ACCESSION   WP_181905174
VERSION     WP_181905174.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
REFERENCE   1  (residues 1 to 474)
  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 474)
  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..474
                     /organism="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..474
                     /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=49467
     Region          62..>406
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 marylsngls ggingivmll igsmanlpsv haddfaqlte raaesgrvtv lagewqpitg
       61 eirpedlesa itgtadreke iasllshvek fggdaralrq yrylpvaays vdakglaalr
      121 dysenmrvws dvpmgvsltd svpmisapaf washgeghgq tiavldagvd aghrffggrv
      181 ireacftrka cpnggdsmyg agaaqtdnkh gthvagiaag sepglrgvap kasiialkvl
      241 kedgmghasd ilagldylmh lvlnegvsla avnlslgase gsnslcadnp feafarlfra
      301 kgiilvsasg nagkenflsl pacapsivsv gavddhyava efsnwspyld ffapgvqims
      361 sadmrgywyl sgtsmaaphv sgaialirgr spemtvdqll aslrsnrlvg ntgipmvelp
      421 gpgqkpstse ksppvldpii tpkpkpvpkk tetgtmpvdg glssdqdgvt aiiq
//
LOCUS       WP_181905176             229 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aestuariispira insulae].
ACCESSION   WP_181905176
VERSION     WP_181905176.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
REFERENCE   1  (residues 1 to 229)
  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..229
                     /organism="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..229
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=25942
     Region          5..219
                     /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 mnllteeyap fnyledgrlt gigadmvram semlgipfka rilpwkrayq qaltdpdtal
       61 fsttrlptre edfqwvgplf evqdylfgnd qfameinnld eardvgsilv qngggshvyl
      121 kslgfqnlqp ytvtdkqlvm ltmgrvdliy lsdlsayyql ringmasdki kpvfrlkkae
      181 lylvfaktad pqivaswqda feqvratgrr eqiirrylpr asadasgsy
//
LOCUS       WP_181905227             259 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aestuariispira insulae].
ACCESSION   WP_181905227
VERSION     WP_181905227.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..259
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29398
     Region          21..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 mpvfiahaee rdgksleirl vtqsfaplqy pqdgrargyv vetlhqmari leqdspirfl
       61 pveflpwkra meiaktkpnv lffsvsrtae reswfhwige vspygqfffk lkshpaitvs
      121 rlsdlrnghh riglqsgssl qrlmesldla stnnivtytd yhqgvkmlfa rrldmipltg
      181 fiarssvcsm gldgdqlepv lpitelarpl wlvmslptpa etaqhvsnal srlnrdgvre
      241 qivtkylenw nkrpckaap
//
LOCUS       WP_181905242             251 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aestuariispira insulae].
ACCESSION   WP_181905242
VERSION     WP_181905242.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
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="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..251
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28531
     Region          31..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 mnwlylltgl iclapwsvra sdlppilmna geappytsed lpgggigpal ireifkrvgy
       61 daeirirpwk ralqegktgs vdgvffsipg qgrekdflfs dsvaeksryf yhlkskpfnw
      121 sqledlrgkt igidatfiyp eeflrlgeen hyylasgrgl gvnvrllleg kidlyprirg
      181 eveyalkkrf skqvrdlity hpaplekqsf hvifsrhaek peillkafnk glaevkadgt
      241 yqhmveqahq y
//
LOCUS       WP_181905271             454 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin monoamine oxidase family protein [Aestuariispira insulae].
ACCESSION   WP_181905271
VERSION     WP_181905271.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..454
                     /organism="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..454
                     /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=50139
     Region          33..453
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 mhvfspisrr tflggfsawa fspayvsasg lsdcvivgag iagisaaqal rranrsviil
       61 eardriggra ytesktfgvp ydhgcawlhs adqnpltkmi eeqpgftivd egsrdlwlyl
      121 dgreaseddy svleeahenl lrridravdr aetisdfedr sirdlsppkg ridriahtlv
      181 gpleageetk risaldvyrq igtgvewmvp qgmaagilqa lgpvaaqlnt ivrridwqrp
      241 eilvetnmgr lrtrsvivtv ptsllaeeti efiphlpdwk rqaaenlpmg lldkitlqfk
      301 pafrslaeea ettglliqen nnsqtwshil rpfghdmtig flggdtarsl sgepdadrit
      361 ielalenlts lfgsdirtlf vkghytnwlq dpwargaysn appgqanark mmarpvaerl
      421 ffageatvtd wstqapgayl sgrraarevi emln
//
LOCUS       WP_181905333             268 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aestuariispira insulae].
ACCESSION   WP_181905333
VERSION     WP_181905333.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
REFERENCE   1  (residues 1 to 268)
  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..268
                     /organism="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..268
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31256
     Region          44..260
                     /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 mgqslairqk lmicfsflal sfflipppaa fgdslpikvl gyhfppyldq knnqgithdf
       61 leflnenqen fqfkleftts krryraleqr rgdmfffemp ewgwegsgva yqstrpilrg
      121 geyyialakp drdqsyflpl rerkiaailg fhygfanfna dqkwlkahfn iilsnsqkkn
      181 ldllrkhrve vavmpisfla helrqqpelh dlflvseqpd qfyhlgtiih pdapiataem
      241 eamlqqlkks gqlqrffery nlgnqliy
//
LOCUS       WP_181905371             249 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Aestuariispira insulae].
ACCESSION   WP_181905371
VERSION     WP_181905371.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
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="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..249
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27953
     Region          24..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 mmiavamvvp sqggawgqtv flvtgneyap ftdetlpegg lftkivrmiy drngeavefa
       61 frpwkrgyle tlegrfeatf pyiltderae afyfsapvlf vlvqlytksd sdffadeynd
      121 ltgrqtclpn gyanttrier lveqgrlkrv tatsmasclr rlaqgrvdfv elnnfvaptv
      181 iretglvpgv frvlelttdk vghyvlypks gpdagnkrdr fdaaleevrk tgeldrliet
      241 ylqglnpns
//
LOCUS       WP_181905384             723 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Aestuariispira insulae].
ACCESSION   WP_181905384
VERSION     WP_181905384.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
REFERENCE   1  (residues 1 to 723)
  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 723)
  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 723)
  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 723)
  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..723
                     /organism="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..723
                     /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=81786
     Region          41..720
                     /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 mgctplsena dltsatasga tdaadrdwkt arrkpaaisc lefldsmrqa alqvtedgdv
       61 vaanrhaarm tgrhidalrn kpldlilpwl npentarwll elaqhdiple teilqfngtr
      121 mpvflqvrkp dilaadhyll slqerpqqeq mpedlllseq rlrqaveifd lchfdweldn
      181 gratydgewp rltgltpeth dpldihwlld llhaedhgmv fmeltalrqg rkrrfdcevr
      241 leadkgeedr wyrmraqair gengkpervi galqdistyk steqqaaliv qqdaltglpn
      301 rqhllnqihr vmdtgdagak tpfalimidv drfryvnesl ghelgdsilr ilatriqkhl
      361 rqedlvarls gdqfavlaqg vspgravqar iirirrkiae tlhvtdeipv nldinvgiry
      421 wngkerlsae eilrdasval hhaketgttr vveyfpelqr rmmetvrfen direairndg
      481 vevhyqpiie ahtgrpigfe alvrmrhper glippadfig iaeetgligd lsrivlkkat
      541 rqlaawkref pslngltvai nlspsqfddp aiidqiakal eksglsgddi kievtesmlm
      601 entsqtvtim edmkdrgiri ciddfgtgys sfshlrnhaf dtlkidrsfi mritedkrda
      661 elvrtilqlg qnigmniive gvetkdqrtl lsdlgahhmq gflfgkplpa kaisdwlsdw
      721 vpg
//
LOCUS       WP_181905401             387 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Aestuariispira insulae].
ACCESSION   WP_181905401
VERSION     WP_181905401.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
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   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 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   4  (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   5  (residues 1 to 387)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
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 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     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=42926
     Region          <19..379
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mlnsaqtsge gavgepegne aqhrricvli idddhldrlv ikkalidsgr rveileadrl
       61 etaeeileqr spdcifldyl mpdgsslsfl etlqadfknr ylgvilitgq gdeevattam
      121 rlgaidylpk drmtpdkima avrqaladlk lkrevdaqrh vienfaalla hdlrdplsat
      181 lgflnlales drlegedrtn vtralegary avglvnelvq yarngsrefa ikavsleevl
      241 lyardvvlqs qavaegveie lhgpfpwveg nfealtllfq nlfqnsvkyr kpdeiahvsv
      301 rfrevgdkse irvrdngrgi apeerdrifr pltrgsqvge qrgyglglat cvrvvglfdg
      361 dirvesalge gaefivtlpt lfkadpe
//
LOCUS       WP_181905444             382 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Aestuariispira
            insulae].
ACCESSION   WP_181905444
VERSION     WP_181905444.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
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="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     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=40868
     Region          12..373
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 masetlknss kpvpllepdi gpaerarvdq cladnwvssa gpyvsafekr vaglanrrhg
       61 iatasgtaal hlallslgig rddfvlvpdw tfsasanavi hagavpvfid idpeswdlda
      121 ssleqalsgl drkpaammvv dppsllgdlp rweamarghg ipliedaaga lgsrresrpa
      181 ghfgtlstfs fngnkilttg gggmmvtddd alaekarhfs aqartgqvyr ydaagynfrm
      241 pslnaalgla qcdrldamls rkreiaaryr affdgnnhls fmplnnlqds nawmsccvtd
      301 ttdaaedlvr hldvagimar pfwcglsdqp pyqaypayls ggsarlsgrv vslpssstlt
      361 dqdldrvlaa lqewphqqgl ps
//
LOCUS       WP_181905457             260 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Aestuariispira
            insulae].
ACCESSION   WP_181905457
VERSION     WP_181905457.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
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="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     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=27756
     Region          7..248
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtgpafptvw itgassgigq tlarlladeg sqvcltarps erleaavagh phfhgqpadv
       61 sdveslraay drimenhglp dlvifnaaiy qpgptseinp edaakqiatn ltgvvngvgs
      121 ilpamlergr griaivgsva gyrglpnagi ygatkaalis yaeslhgecr drgvqiqiin
      181 pgfvetpmta kndfpmpfli tadqaaqtir hglnskrfei afpakfvwil kalailpygl
      241 ffpltrrltg tpehhdneqp
//
LOCUS       WP_181905649             420 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Bordetella
            parapertussis].
ACCESSION   WP_181905649
VERSION     WP_181905649.1
KEYWORDS    RefSeq.
SOURCE      Bordetella parapertussis
  ORGANISM  Bordetella parapertussis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
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="Bordetella parapertussis"
                     /db_xref="taxon:519"
     Protein         1..420
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45377
     Region          12..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 mfthlvdfms isshrllegi rvldmtvala gpyasmllgg lgtevirvea pggsdlgrsn
       61 ppfvgpggvn fgqqgsddvs ltllnrarnk ksitlnvkdp egralfarll resdvfienl
      121 segaserlgv dyarvreind riiyasikaf gepskyqnlk gmdilvqals glmavtgeas
      181 gppmrcgvpv adllaplymv ngilaaliyr grtgkgqkiq vsmldclssw vaeehfdvla
      241 qagfrmrtgn nherlvpfgt yecvdghiai aavhpdwfas lldamgradl qrdprfvdrg
      301 trmrhaadla alvsewtrdk tvafveqalv qergvpaarv rtplemlddp dlhrsgaitd
      361 lqtpdggtvr gmglpigfse chaqfdvpaq algqanasvy adilglsdae irrleekgvi
//
LOCUS       WP_181905389             341 aa            linear   BCT 28-DEC-2024
DEFINITION  MraY family glycosyltransferase [Aestuariispira insulae].
ACCESSION   WP_181905389
VERSION     WP_181905389.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
REFERENCE   1  (residues 1 to 341)
  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 341)
  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..341
                     /organism="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     Protein         1..341
                     /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=37019
     Region          31..287
                     /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            211..214
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133464"
     Site            order(258,269..272)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:133464"
ORIGIN      
        1 mfenitlfli lsassvavtg mvllflrkra ildhpnhrss hkvptprggg iavtsiilav
       61 wlwqlgpdga lldylplgvg fllagmswld diydlsakir flaqlvltgm slpwvfqhgi
      121 pleaylpvwl iailiilawt afinffnfmd gidgisgvea igiglgftli tlssaqsasn
      181 pfptfelapg lliaaatagf liwnwhpaki flgdvgsipl gyflgglllv laargewaaa
      241 iilpgyyltd agltllkrii rrekiweahr dhyyqravrs ghsharvslm ialtncglii
      301 lagwsvaapy yalaaaaali gllifwmnsr haeksrgalh d
//
LOCUS       WP_181905671             291 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-methyltransferase [Microbacterium bovistercoris].
ACCESSION   WP_181905671
VERSION     WP_181905671.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium bovistercoris
  ORGANISM  Microbacterium bovistercoris
            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..291
                     /organism="Microbacterium bovistercoris"
                     /db_xref="taxon:2293570"
     Protein         1..291
                     /product="DNA-methyltransferase"
                     /calculated_mol_wt=32350
     Region          2..278
                     /region_name="YhdJ"
                     /note="DNA modification methylase [Replication,
                     recombination and repair]; COG0863"
                     /db_xref="CDD:440623"
ORIGIN      
        1 miegdnlgva eslasgsftl iyldppfntg raqtrervva traedddead aasapraevs
       61 rgfhghryek vrsmlhaydd rfddygdflm prlqeawrll addgtlylhl dyreahyakv
      121 mldavfgrda flneliwayd ygaksrrrwp tkhdtilvya ktpgghffds davdrepyma
      181 pglvtpekaa rgklptdvww htivpttgre ktgyptqkpe gvlrrivqas srpgdrvldl
      241 fagsgttgav asalgrsavl vdsnpeairv mrermphavv rtgtqnpgsr n
//
LOCUS       WP_181905674             186 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsB family cell division protein [Microbacterium bovistercoris].
ACCESSION   WP_181905674
VERSION     WP_181905674.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium bovistercoris
  ORGANISM  Microbacterium bovistercoris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
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="Microbacterium bovistercoris"
                     /db_xref="taxon:2293570"
     Protein         1..186
                     /product="FtsB family cell division protein"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=20066
     Region          52..143
                     /region_name="FtsB"
                     /note="Cell division protein FtsB [Cell cycle control,
                     cell division, chromosome partitioning]; COG2919"
                     /db_xref="CDD:442163"
ORIGIN      
        1 marrpaplsp spkpsagsas kagaakpaas arsareprar rrvdvgewts girlsafsai
       61 mlslvvlgaw vlvpslgtyl dqrqkiaave asvqvteeei aalelererw ndpayistqa
      121 rerlyyvkpg evpylvdndl dpaalpkeqv pvsdelverk adwmpqllrs iagsglakna
      181 veaplr
//
LOCUS       WP_181905517             423 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-ketoacyl-[acyl-carrier-protein] synthase family protein
            [Aestuariispira insulae].
ACCESSION   WP_181905517
VERSION     WP_181905517.1
KEYWORDS    RefSeq.
SOURCE      Aestuariispira insulae
  ORGANISM  Aestuariispira insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Aestuariispira.
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="Aestuariispira insulae"
                     /db_xref="taxon:1461337"
     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=45275
     Region          6..417
                     /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 mvwfagmsal splgrsgpei meaalagrsa vtcwkgyhpa piyskiggdl fgfdvkealk
       61 tevptlpeem arrlkylalr lprqvqlslw lalkawqdla srmpppdipp erigvimcgh
      121 nlnthyihre tktyleepdf ldglfasssl dsihaaavse llgargpcyt vgaacasgih
      181 alraasrell sgeadlvyvv ggvtesapae ldnmvamqav agepldgdpa aacrpfdqrr
      241 fgfvpaqggg clilggerfr easygrlvsi avcndaqhlp vtsqegqera mkqalskagl
      301 smgdiaavna hatstiqgdl teinairalc egagrkpvpv yapkshlghc lwsaalieta
      361 lallqiqvgr ipgtrnlekp aedwisafst krpqrlsgrh ilknafgfgg yngsmilaqe
      421 nwk
//
LOCUS       WP_181906055             239 aa            linear   BCT 28-DEC-2024
DEFINITION  PPE family protein, partial [Mycobacterium tuberculosis].
ACCESSION   WP_181906055
VERSION     WP_181906055.1
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 13657689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..239
                     /product="PPE family protein"
     Region          24..60
                     /region_name="Pentapeptide_2"
                     /note="Pentapeptide repeats (8 copies); pfam01469"
                     /db_xref="CDD:279771"
     Region          <37..221
                     /region_name="PPE"
                     /note="PPE-repeat protein [Function unknown]; COG5651"
                     /db_xref="CDD:444372"
ORIGIN      
        1 nigfgitgdh qmgfggfnsg sgnigfgnsg tgnvglfnsg sgnigignsg slnsgigtsg
       61 tinaglgsag slntsfwnag mqnaalgsaa gseaalvssa gyatggmsta alssgilasa
      121 lgstgglqhg lanvlnsglt ntpvaapasa pvggldsgnp npgsgsaaag sganpglrsp
      181 gtsypsfvns gsndsglrnt avrepstpgs gipksnfyps pdresayasp rigqpvgse
//
LOCUS       WP_181906357             234 aa            linear   BCT 28-DEC-2024
DEFINITION  DsbA family protein [Microbacterium sp. 1154].
ACCESSION   WP_181906357
VERSION     WP_181906357.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. 1154
  ORGANISM  Microbacterium sp. 1154
            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. 1154"
                     /db_xref="taxon:2817733"
     Protein         1..234
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24111
     Region          66..220
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mmmaaarktt nwfaigvtaa alvvvlivgg vvwfansqat spgtlpqasa idtetgaisv
       61 gtgektvdty idfmcpvcns feqaygptlq qlvddstitl kihpiaildr lsqgtqystr
      121 aanaaycvav dnaanipafv kalyaqqpke ntaglddatl asiatsagas davsscitsg
      181 tytkfvtamt qktplqpnat svatptiavn gtvlqnqtdl sgdpqkdiva rlng
//
LOCUS       WP_181907202             185 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Cohnella lupini].
ACCESSION   WP_181907202
VERSION     WP_181907202.1
KEYWORDS    RefSeq.
SOURCE      Cohnella lupini
  ORGANISM  Cohnella lupini
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
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 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Cohnella lupini"
                     /db_xref="taxon:1294267"
     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=21550
     Region          58..147
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mdyrstdqwn eslwsraekv yddafpehgr ktltiirrmf drgmctldtw seqgevaama
       61 ltsynlqdkm lvidylavgq dwrgkgigml cienirkris aampdcrgiv ieveaerske
      121 neerirfwkk agfhlteyvh syiwvpekyr amflsldgds tladdgkklf etitkyheka
      181 yrgra
//
LOCUS       WP_181907220             284 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Cohnella lupini].
ACCESSION   WP_181907220
VERSION     WP_181907220.1
KEYWORDS    RefSeq.
SOURCE      Cohnella lupini
  ORGANISM  Cohnella lupini
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
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="Cohnella lupini"
                     /db_xref="taxon:1294267"
     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=32238
     Region          64..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 minpfkqdpt seiikqyrkv wqleglrglh hpitltdhne tpftgeravi nsfiksvhtp
       61 vfhehliryd fatrfvsdki vldaacgagf gakmlemaea kavyavdise esllhaqasy
      121 sgnrihysqg dvrnihafkn effdiivsfe tiehissgre wiaeaarllk agglflvstp
      181 nrsitnpgty heehpinpyh hyeysvsefv gellvsfdil elygqtlvrd qinsgfmwdr
      241 qlrgkdpawv ppyspettsh elvpfahikn aqpsyvvavc rkkr
//
LOCUS       WP_181907292             451 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Cohnella lupini].
ACCESSION   WP_181907292
VERSION     WP_181907292.1
KEYWORDS    RefSeq.
SOURCE      Cohnella lupini
  ORGANISM  Cohnella lupini
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
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="Cohnella lupini"
                     /db_xref="taxon:1294267"
     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=49596
     Region          70..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(176,178,301,303,332..334,375)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mvklrfvkal tiiviiamvs viaacsggnd knaaessgtp sasdspkase spketseape
       61 envtvkfgnf sgagdtakyl tqmqeafeke hpnikieiet iaygdyftqm qtrvaagqap
      121 dayelnyenf vsyakkgvll dinpffeatq fdkstlnqqa lnafsadgtq ygmpgsfsnv
      181 lliynkelfa eanaelptnd wtwkefddaa akiraldknt fgvfqpiqfh efyklvqqnd
      241 gsllnadkta ftvnspenve tlqrlvdrvl ksnvmptqaq lsgvgdwdlf kagrlgmivt
      301 gvwafsdfmq nvkfewdvav epgnkkkath ffsnglvink dskvaeaafe wikflssske
      361 aakirvdagw elpavtypdv leaylkttpp anrqavfdsl eflvtppvie qftemadilg
      421 ihltaasega ksaqealdda qkeltdkikl q
//
LOCUS       WP_181907334             290 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Cohnella lupini].
ACCESSION   WP_181907334
VERSION     WP_181907334.1
KEYWORDS    RefSeq.
SOURCE      Cohnella lupini
  ORGANISM  Cohnella lupini
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
REFERENCE   1  (residues 1 to 290)
  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 290)
  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 290)
  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 290)
  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 290)
  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..290
                     /organism="Cohnella lupini"
                     /db_xref="taxon:1294267"
     Protein         1..290
                     /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=32783
     Region          6..274
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mnkryweygi stdkgpykqi nedscflrle svgpkqdcal avvadgmggy gagdqasqla
       61 vdhvkawwae rihevaaldn phpllndeml hvtrkindel cgysrsrsmt pgttlsilii
      121 ihsryylyht gdsriyviag qgspeandes ptrmrqlsmd hswvaeevrq grlhssmmns
      181 hprrnvlthc lgideslelf qatgqvrlnd lfllcsdgfy sifqdeeilr ntklyiqqyg
      241 rlqsvsdrlv qlacelgttd nvsmvlirar aeeqtkakaf irklfkhkgs
//
LOCUS       WP_181907364             276 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Cohnella lupini].
ACCESSION   WP_181907364
VERSION     WP_181907364.1
KEYWORDS    RefSeq.
SOURCE      Cohnella lupini
  ORGANISM  Cohnella lupini
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..276
                     /organism="Cohnella lupini"
                     /db_xref="taxon:1294267"
     Protein         1..276
                     /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=31895
     Region          25..271
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 masikseqai adllhnlqid vtaayrtqct pewrnldhsp dynkfyfile gegwvrveeq
       61 tihprpgqlf fapaytnqgy savndnaflk ywchfttrag afdlfqwigv pycidihdke
      121 rvsrlferlv epqgssalvt lirqksvmle ilatylehvp vqvlqhrsee inrlnvihdy
      181 vdkhlhlsis vdelasllhl hpnyfiayfk krfgvsphky vnrkraekak tllmttalsi
      241 keisaltgfp dtnhftkffr ketgfsptef rgiyas
//
LOCUS       WP_181907527             557 aa            linear   BCT 28-DEC-2024
DEFINITION  PhoX family protein [Cohnella lupini].
ACCESSION   WP_181907527
VERSION     WP_181907527.1
KEYWORDS    RefSeq.
SOURCE      Cohnella lupini
  ORGANISM  Cohnella lupini
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..557
                     /organism="Cohnella lupini"
                     /db_xref="taxon:1294267"
     Protein         1..557
                     /product="PhoX family protein"
                     /calculated_mol_wt=59977
     Region          57..551
                     /region_name="PhoX"
                     /note="Secreted phosphatase, PhoX family [General function
                     prediction only]; COG3211"
                     /db_xref="CDD:442444"
ORIGIN      
        1 mdkqmdrrtf lsylgtgata laaataglgl legkasaask tadhlfgfns nrvsghfdpi
       61 apsnedklvl pkgyrydvva afddvinqag dkfgqgcdyn aflpinganh rgllatnhey
      121 tniflhgplk dgkmnadqik qalyyqgmsv ievfrdtdgs wkmdkssana rringftkfe
      181 ltgpgkgsaa lggntsvtgt fancsggvtl wntvlsceen ftdlaaaasl plthygwvve
      241 idpfdgsflr khtalgrfnh entamglakd grvvvymgdd kkdaciykfv sngkfdkakg
      301 rnnselladg tlyvaslkng swialtydav kktldnpsfk tpaglkgtke dflklfqnqa
      361 dvvtncheaa illggmptdr pedieispfd ntvfichtnn dlhgnihghi trifeqdddl
      421 gaasfdfeif aaggrqsgfs spdnlsfdgn gnlwvvtdis ssslnkgiys tfmnnglfvi
      481 ptsgpsqgda fqfasgpnes emtgpyftpd ektlflsvqh pgenttdlsk ptslwphrsg
      541 dkiarcgvva isgfqlg
//
LOCUS       WP_181907558             256 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Cohnella
            lupini].
ACCESSION   WP_181907558
VERSION     WP_181907558.1
KEYWORDS    RefSeq.
SOURCE      Cohnella lupini
  ORGANISM  Cohnella lupini
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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..256
                     /organism="Cohnella lupini"
                     /db_xref="taxon:1294267"
     Protein         1..256
                     /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=29269
     Region          4..246
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 msqfpiaiqp ytvrdaisqd yvgtleklaa igfqgielgl ppegmtiarq keildrlnlq
       61 vigthasfdn ldvdynrltd ylhqvggkyi tismrfdske dvlrkseqfn rigeicraan
      121 ttflyhnhdw eferfdeeyv ldiilretds rlvkleldty wvrkggldps eylsklkdrc
      181 pllhikdvea geeqffaeig egildfkaia dtaasvgtew liveqdlcrr dpfeslaisy
      241 rnlaamdlik kpanri
//
LOCUS       WP_181907641             282 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Cohnella
            lupini].
ACCESSION   WP_181907641
VERSION     WP_181907641.1
KEYWORDS    RefSeq.
SOURCE      Cohnella lupini
  ORGANISM  Cohnella lupini
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
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="Cohnella lupini"
                     /db_xref="taxon:1294267"
     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=31157
     Region          46..278
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mneipivfsl nsytfasklg pmrtyvwnee fglydmeiep qpetstllgl lvrmgansyr
       61 aievayghlh dtthgalrei rhvaeisrve lasllldfgd lstddpvraa admtmykqwi
      121 diaaeagfsr lrleagearp ddaaaitraa drllelaeya kpaqiwvmte nlgsllstsd
      181 nclkliglcr gnigftadyg nfekdkykql advllyaetv hakaatdeag ridaedyrrc
      241 lsltlesgfe gslsltylgd adpwpklgem rafaeeilkv ta
//
LOCUS       WP_181908980             281 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Paenibacillus sp. VMFN-D1].
ACCESSION   WP_181908980
VERSION     WP_181908980.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. VMFN-D1
  ORGANISM  Paenibacillus sp. VMFN-D1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 281)
  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..281
                     /organism="Paenibacillus sp. VMFN-D1"
                     /db_xref="taxon:2135608"
     Protein         1..281
                     /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=31654
     Region          2..276
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mridahqhyw siarddygwi tpsipvlyrd yqpsdllphl aehhldgtil vqaaptyeet
       61 dyilelaahd drvlgvvgym dladddhkdh ferfaqhpkf vgfrlmiqdm edanaileps
      121 yaaslkhyas lgvpvdllvr sdqldtlvrl ieqipnlhav idhlakpria agemepwags
      181 mkrlasypnl ycklsgmvte adhdgwkpdh lepyvrhvld cfgadrvmfg sdwpvclmas
      241 sydgvvdall ktlpptwgad eslklfggna aafyrlknet r
//
LOCUS       WP_181908983             468 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. VMFN-D1].
ACCESSION   WP_181908983
VERSION     WP_181908983.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. VMFN-D1
  ORGANISM  Paenibacillus sp. VMFN-D1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. VMFN-D1"
                     /db_xref="taxon:2135608"
     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=52697
     Region          121..444
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 manrtrstvw igltillggs asfafamhls iipyipadwl spglsyflyw ltvaamhiyf
       61 yvlpyvycmg glwlnesvtg fvkkvltlal lpgpwllmad hwahepwnqf evarfrwwdg
      121 iyvaagsfgy ilayfkekse aarrrqwrtf vlplamlway tsdyigfehl elgwwsfhle
      181 sngmwesnfi milgtvgfii fyiarsgflg iklriereri dysirtltmg vsilnhsikn
      241 eiqkidylae ksrvllesgq sdkaahtiaq vhgltahllh mvnrikdkae dvvlqegehd
      301 irqlidsvva sagslierhp atitarydae grlycdsvhv aetlsnlirn aldalpasgg
      361 gielhtastr refritvqdn gagiptehla kifepffttk khalnyglgl syctsvmskh
      421 ggrlsvaase pgkgttivlh fpyarfkpls pafkrqadsr tldqvspf
//
LOCUS       WP_181908994             231 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Paenibacillus
            sp. VMFN-D1].
ACCESSION   WP_181908994
VERSION     WP_181908994.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. VMFN-D1
  ORGANISM  Paenibacillus sp. VMFN-D1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 231)
  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..231
                     /organism="Paenibacillus sp. VMFN-D1"
                     /db_xref="taxon:2135608"
     Protein         1..231
                     /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=26222
     Region          1..170
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mirlymlgik nvsaahfdhf mkrvspertr qvrrirnrrd avrslfgevi vrwavsqvkp
       61 aaafskrwtr sefgkpafad epdihfnlsh sgdwvvaalg pselgvdveq vlpvnpgmae
      121 scfspaelgl lqhlseeerl nrfydlwtlk esyikcigrg lsqpldsfti tlrpdgniey
      181 sgpdiearny qfmlipmegp yklavctkak gpieiytpem dqllnmkmfa d
//
LOCUS       WP_181908933             423 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Paenibacillus sp.
            VMFN-D1].
ACCESSION   WP_181908933
VERSION     WP_181908933.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. VMFN-D1
  ORGANISM  Paenibacillus sp. VMFN-D1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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..423
                     /organism="Paenibacillus sp. VMFN-D1"
                     /db_xref="taxon:2135608"
     Protein         1..423
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=46765
     Region          93..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          252..420
                     /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 mkrwkqwtgm gllfclllsa ctsekeepas vpvpdpepae lgqtltvvpt esakaaaedp
       61 sqyqiqtrlt dfqllsgttg iawgltrnel rmyltedngk twvnispasn vqfpdnlkyg
      121 rdlyfkdrmn gwvvrsasgt setivlhtsd gggswkvssi pdknkvtsif fdsnnvgwim
      181 ltaesstgkq dktlyktedg gakwkmvmhn yissnqtstq gaipplgyam gmtftspakg
      241 yamiqelgvp klyrtqdggs ewsegpaffn rdklascsgf ipsspeffdt sntegwipvg
      301 cqvgdsakyn gffttdqgqt wtfapfnlgw nkgvnqslrp sfinstqgwa lvgnlvyhte
      361 dqgktwmplp asrvltsilk eypevgklqf ssqrvgwmlv mkndemrsrl lqtidggitw
      421 kvl
//
LOCUS       WP_181909033             262 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Paenibacillus].
ACCESSION   WP_181909033
VERSION     WP_181909033.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     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=30541
     Region          19..261
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mdrsslytdl vtypsgwkmg thvhphfeic vvtfgrgefy aedqvfsiqe gdvilitpgv
       61 phdyssvtpi rfavlqvdhl shelerlffq mtneeslhlf plahyalerf eklfsvwlhm
      121 tsvrpnqlfn rllktwvelf mlflldrieq qdsritldai aeyirtnldk emrvtdlarm
      181 irmsesglrs cfkktyglsp kqylqqyrms eakmlltfsd ktvqqiasgv gfpnihafsa
      241 wfqkqtgmsp tawrkeqrrr gg
//
LOCUS       WP_181909095             249 aa            linear   BCT 28-DEC-2024
DEFINITION  protein-L-isoaspartate O-methyltransferase family protein
            [Paenibacillus sp. VMFN-D1].
ACCESSION   WP_181909095
VERSION     WP_181909095.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. VMFN-D1
  ORGANISM  Paenibacillus sp. VMFN-D1
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 249)
  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 249)
  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 249)
  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..249
                     /organism="Paenibacillus sp. VMFN-D1"
                     /db_xref="taxon:2135608"
     Protein         1..249
                     /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=27266
     Region          15..170
                     /region_name="Pcm"
                     /note="Protein-L-isoaspartate O-methyltransferase
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2518"
                     /db_xref="CDD:442008"
ORIGIN      
        1 mnpnhlield glhvspsiln afehvdgakf lfhqdgsrvi qstnprfmae mleclqvqkg
       61 qrvleigtgs gfnaalisnl igpegtlhtv evdpsvakra kakldssgir nvkvicgdgf
      121 ygyhqsipyd riiaaakppf lpqpwidqlg iggilvapld lealgdayvv afnkvsehsl
      181 vslslmkgnf mrmapsaeql vlksgkpngv qtdfdidrlq iralrnpnrk ntwtdqvsfd
      241 awdfeyigl
//
LOCUS       WP_181909671             522 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus taihuensis].
ACCESSION   WP_181909671
VERSION     WP_181909671.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus taihuensis
  ORGANISM  Paenibacillus taihuensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 522)
  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 522)
  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 522)
  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 522)
  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 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   6  (residues 1 to 522)
  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..522
                     /organism="Paenibacillus taihuensis"
                     /db_xref="taxon:1156355"
     Protein         1..522
                     /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=58612
     Region          131..494
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 manakalltn icllialayl fdlgyrylfq yasnrakyml ttamfilggw tamafgirtd
       61 glylldlrfv pliiavlvlq epltialigf gigvgrlflg ideaaiaafl nmtivglvsa
      121 wlcsylrwkp wrfeyksiva vlvvnilyal dttltletle lmpvgtywre fgyysfplri
      181 vmsmlliyvi rdfqkeqqrv delrtmnmll rrqtrelrea krdveekare lmvankykse
      241 flanmshelk tplnsiills qllqesdger vsaedvryae lingagndll qlindildls
      301 kveagkmdvy feplstrelv qtlqeqfmpl anrknlafet eiapnvpevm qsdalrvnqi
      361 lrnllvnafk fteqgsvklv vkqeggmple paalkkrrlr swnpaawgrs avritspqrv
      421 sfsiidtgig iehekqklif eafqqedgsi nrnyggtglg lsislqlarl lggtlslvsq
      481 kgegstftly lpvappmtss valgdngqpe ppdkgnrrss ra
//
LOCUS       WP_181909559             455 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus taihuensis].
ACCESSION   WP_181909559
VERSION     WP_181909559.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus taihuensis
  ORGANISM  Paenibacillus taihuensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus taihuensis"
                     /db_xref="taxon:1156355"
     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=49776
     Region          155..445
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mlyvwimlwi asallivanr rnaagrwlsf vsfcggvgal asvlegwivs mlatgdidas
       61 gehvlriiqr ccswtsyygl pygflcfgvs yntdllparl arwvpllgla fplgmlalpi
      121 addypvhynl laiwtipyll lgaallltkk hvhpaerrah aimlvavlpa viaastmnyv
      181 lplfglyrmw rynvypigfa ftifivslfs fgflgvqlli errqlnhslr aitsgtamln
      241 haikndigkm klftdkikre aaaggnaelq adirvissaa qhieamirsv hertqelqlq
      301 lqevslaqlv qeqiaaleqq aaakrvaitt ryddnavaiv daaqtteaih nvlqnaidam
      361 agggqltaav iagkrgstie itdtgigiek sqlrkviepf fttksgktmn fglglaycyq
      421 lmnrqggelr isseagvgtv vrfhfravrk kgaka
//
LOCUS       WP_181909806             450 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Paenibacillus
            taihuensis].
ACCESSION   WP_181909806
VERSION     WP_181909806.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus taihuensis
  ORGANISM  Paenibacillus taihuensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus taihuensis"
                     /db_xref="taxon:1156355"
     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=49032
     Region          59..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(172,174,299,301,329..331,374)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mvkqsgilll iaamavisac gsnngndsng nssstnastn gssdasanes qepakdpvti
       61 kyltytangg qentlksmve afeaknpdvk vdyevvpyad ydtklttlis ggqapdvyel
      121 gyenfrkyag kdllldltpi isadssfdps tykklaydaf nyngkqmgvt esfsdvvlfy
      181 nkdlfdakgv kypdaswtwk eeldaaqkla dpangvwgty spfqfyefyk tiaqngggvf
      241 dasgnptins qanidavqwm idkaekykvs pamnddtfsq pdadlnafms gkiamarfgi
      301 wnfsrfkdak fkwdialepg ntqkahhffa dgivaskdtk qaeavwkfmk yftsdadsvn
      361 kriaagwsvp avaddavlda yykqappesk kvvidaldsl vlppvgpkpe kwgelqaavt
      421 eqldkakfgk isvkealdna qksvadllsk
//
LOCUS       WP_181909825             272 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Paenibacillus taihuensis].
ACCESSION   WP_181909825
VERSION     WP_181909825.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus taihuensis
  ORGANISM  Paenibacillus taihuensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Paenibacillus taihuensis"
                     /db_xref="taxon:1156355"
     Protein         1..272
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29222
     Region          18..272
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msntraseql apqlnaiqip aeagfivari fspggqgpfp tvvlshgfpg vqqnydlaaq
       61 lqhagyqavv fhyrglwgsk gefsvsrale dmktvlaylr heetsakyqi dvqrvavvgh
      121 sfggfvalqt aaadsgiaav aslsganlgl maqllmhpes raqleaafde pasyvtghfs
      181 skmmgdeila hapewnlldr aqiladrpvl lvgaaldavt pvkfnhdplv safqgagaek
      241 mqsliieate hgyegkrqel fevvlrwlne tv
//
LOCUS       WP_181909338             161 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Paenibacillus taihuensis].
ACCESSION   WP_181909338
VERSION     WP_181909338.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus taihuensis
  ORGANISM  Paenibacillus taihuensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 161)
  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..161
                     /organism="Paenibacillus taihuensis"
                     /db_xref="taxon:1156355"
     Protein         1..161
                     /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=17869
     Region          1..>86
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mhnhpeeqls aylddeleev erqqveahle tcescqaivd dllglkhefr ltfaaveapm
       61 nlenrvlltl reeetpqksv rywlaailia mlplaslylf agpialkllh ggyklivtll
      121 ymashfilsv pvlsastiml aiiilvtsgy slkrllqana g
//
LOCUS       WP_181910019             631 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Mycobacterium
            tuberculosis].
ACCESSION   WP_181910019
VERSION     WP_181910019.1
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 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..>631
                     /product="beta strand repeat-containing protein"
     Region          <1..629
                     /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 fgnaggtnvg fgnlgngnvg fgnsglgagl aglgniglgn agssnygfan lgvgnigfgn
       61 tgtnnvgvgl tgnhltgigg lnsgtgnigl fnsgtgnvgf fnsgtgnfgv fnsgnyntgv
      121 gnagtastgl fnagnfntgv vnvgsyntgs fnagdtntgg fnpggvntgw lntgntntgi
      181 ansgnvntga fisgnfnngv lwvgdyqglf gvsagssipa ipiglvlngd igpitiqpip
      241 ilptiplsih qtvnlgplvv pdivipafgg gigipinigp ltitpitlfa qqtfvnqlpf
      301 ptfslgkiti pqiqtfdsng qlvsfigpiv idttipgptn pqidltirwd tppitlfpng
      361 isapdnplgl lvsvsisnpg ftipgfsvpa qplplsidie gqidgfstpp itidripltv
      421 gggvtigpit iqglhipaap gvgntttaps sgffnsgagg vsgfgnvgag ssgwwnqaps
      481 allgagsgvg nvgtlgsgvl nlgsgisgfy ntsvlpfgtp aavsgignlg qqlsgvsaag
      541 ttlrsmlagn lglanvgnfn tgfgnvgdvn lgaanigghn lglgnvgdgn lglgnighgn
      601 lgfanlglta gaagvgnvgf gnaginnygl a
//
LOCUS       WP_181911355             256 aa            linear   BCT 28-DEC-2024
DEFINITION  NUDIX hydrolase, partial [Mycobacterium tuberculosis].
ACCESSION   WP_181911355
VERSION     WP_181911355.1
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 256)
  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 256)
  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 amino end.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..256
                     /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          58..224
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 rgtvalrpda gpswlrplvd nvgqipdayr rrlpadvlam vtaagavsam tssrrdhrea
       61 avlvlfsgpe agpgdggvpd dadllltvra stlrhhagqa afpggvvdpa ddgpvatalr
      121 eaneetgidp srlhplatme rtfiapsrfh vvpvlayspd pgpvavvnea etaivarvpv
      181 rafinpanrl mvyrrphtrr wagpafllnq mlvwgftgqv isavldvagw aqpwdtgdir
      241 eldaamvlid desdpr
//
LOCUS       WP_181912356            1069 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Mycobacterium
            tuberculosis].
ACCESSION   WP_181912356
VERSION     WP_181912356.1
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 11460828
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..>1069
                     /product="beta strand repeat-containing protein"
     Region          <1..1069
                     /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 gnlggqnlgl gnlgdgnvgf gnlghgnvgf gnsglgalpg igniglgnag snnvgfgnmg
       61 lgnigfgntg tnnlgigltg dnqtgfggln sgagnlglfn sgtgnigffn tgtgnwglfn
      121 sgsyntgign sgtgstglfn agsfntglan agsyntgsln agntntggfn pgnvntgwfn
      181 aghtntggfn tgnvntgafn sgsfnngalw tgdhhglvgf sysieitgst lvdinetlnl
      241 gpvhidqidi pgmslfdihe lvnigpfrie pidvpavvld ihetmvippi vflpsmtigg
      301 qtytipldtp papapppfrl pllfvnalgd nwivgasnst gmsggfvtap tqgilihtgp
      361 ssattgslal tlptvtipti ttspiplkid vsgglpaftl fpgglnipqn aipltidasg
      421 vldpitifpg gftidplpls lalnisvpds svpiiivppt pgfgnatatp ssgffnsgag
      481 gvsgfgnfga gssgwwnqah aalagagsgv lnvgtlnsgv lnvgsgisgl yntaivglgt
      541 palvsgagnv gqqlsgvlaa gtaltqspii nlgladvgny nlglgnvgdf nlgaanlgdl
      601 nlglgnigna nvgfgnighg nvgfgnsglg aalgignigl gnagstnvgl anmgvgnigf
      661 antgtnnlgi gltgdnqtgi gglnsgagni glfnsgtgni gffnsgtgnw glfnsgsfnt
      721 gignsgtgst glfnaggftt glanagsynt gsfnvgdtnt ggfnpgsint gwfntgnant
      781 giansgnvdt galmsgnfsn gilwrgnyeg lfsysysldv pritildahf tgafgpvvvp
      841 pipvpainah ltgnaamgaf tipqidipal npnvtgsvgf gpiavpsvti paltaaravl
      901 dmaasvgats eiepfivwts sgaigptwys vgriynagdl fvggniisgi ptlsttgpvh
      961 avfnaasqaf ntpalnihqi plgfqvpgsi daitlfpggl tfpansllnl dvfvgtpgat
     1021 ipaitfpeip anadgelyvi agdiplinip ptpgignttt vpssgffnt
//
LOCUS       WP_181913047              63 aa            linear   BCT 28-DEC-2024
DEFINITION  MOSC domain-containing protein, partial [Salmonella enterica].
ACCESSION   WP_181913047
VERSION     WP_181913047.1
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 10507113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..>63
                     /product="MOSC domain-containing protein"
     Region          1..>61
                     /region_name="MOSC_N"
                     /note="MOSC N-terminal beta barrel domain; pfam03476"
                     /db_xref="CDD:281474"
ORIGIN      
        1 matlsrlfih pvksmrgigl thaladisgl afdrifmvte pdgtfitarq fpqmvrftps
       61 plh
//
LOCUS       WP_181912961             581 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Campylobacter fetus].
ACCESSION   WP_181912961
VERSION     WP_181912961.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter fetus
  ORGANISM  Campylobacter fetus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 581)
  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 581)
  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 581)
  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 581)
  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..581
                     /organism="Campylobacter fetus"
                     /db_xref="taxon:196"
     Protein         1..581
                     /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=66120
     Region          52..580
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkkfvffsiv avvvifande ynatlpptki esksdvdtlk gyvgydraqg srtdlllket
       61 pqtidildis rnksygqndl ssilegtagi dttydmradn ifvrgfnada gdiyrdgvrd
      121 sgqvrrstan ierieilkgp nsvlygrgag ggvinmvskv anfnskslat vgygsydnry
      181 fgldmnhvfn enfaarvvgd lrdsnsyrdy ieekskmisp siiyykdnfs hlleytydya
      241 krvpdrgptk dvyeqmgidy kktfarqgdi vedrlqmyrs klnydfsdkm yiewvlayrk
      301 anqsfdhyfg gkydpktkll sqsyawqntd nstflnsisa nfdfdtfgkr nklllgydfq
      361 iekrepligi krnqnidpfs priswgrint paasisnkhk atnhgvfvqe lfyitdslkf
      421 alggrldeyk fsskdiknks neykgdnfsy nyglvydins qhtayaaynk sfspyggngy
      481 vgistttdpk gfntkpensq qyevgiksdw lnnsisttls tyvlehynir yrpdpindpf
      541 tyairgkeqs kgvefsaigk isdnvyirss vgfmkarvkk r
//
LOCUS       WP_181913464             158 aa            linear   BCT 28-DEC-2024
DEFINITION  pentapeptide repeat-containing protein, partial [Mycobacterium
            tuberculosis].
ACCESSION   WP_181913464
VERSION     WP_181913464.1
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 10477883
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..158
                     /product="pentapeptide repeat-containing protein"
     Region          1..39
                     /region_name="Pentapeptide_2"
                     /note="Pentapeptide repeats (8 copies); pfam01469"
                     /db_xref="CDD:279771"
     Region          <7..>146
                     /region_name="PTZ00395"
                     /note="Sec24-related protein; Provisional"
                     /db_xref="CDD:185594"
ORIGIN      
        1 gntgffnagd sntgfanagn vntgffnggd intggfnggn vntgfgsalt qagansgfgn
       61 lgtgnsgwgn sdpsgtgnsg ffntgngnsg fsnagpamlp gfnsgfanig sfnagiansg
      121 nnlagisnsg ddssgavnsg sqnsgafnag vglsgffr
//
LOCUS       WP_181913451             599 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Haemophilus influenzae].
ACCESSION   WP_181913451
VERSION     WP_181913451.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 599)
  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 599)
  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..599
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..599
                     /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=68509
     Region          6..594
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mnldlhfvhr iqqqaktran mtalrykehg lwrdiswknf qeqlnqlsra llahnidvqd
       61 kiaifahnme rwtiadiatl qiraitvpiy atntaqqaef ilnhadvkil fvgdqeqydq
      121 aleiahhcpk lqkivamkst iqlqqdplsc twesfiktgs naqqdeltqr lnqkqlsdlf
      181 tiiytsgttg epkgvmldya nlahqlethd lslnvtdqdi slsflpfshi ferawaayil
      241 hrgailcyle dtnqvrsalt eirptlmcav prfyekiyaa vldkvqkapk lrqimfhwai
      301 svgqkhfdlr annkaipfll kkqfaladkl vlsklrqllg grikmmpcgg aklepaiglf
      361 fhaiginikl gygmtettat vscwhdfqfn pnsigtlmpk vevkigenne ilvrggmvmk
      421 gyykkpeeta qaftedgflk tgdagefdeq gnlfitdrik elmktsngky iapqyieski
      481 gkdkfieqia iiadakkyvs alivpcfdsl eeyakqlnik yhdrlellkn cdilkmfehr
      541 inavqkelah feqvkkftll sqafsiklge itptlklrrk vileryrkqi eamyhsqea
//
LOCUS       WP_181913678             685 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Haemophilus influenzae].
ACCESSION   WP_181913678
VERSION     WP_181913678.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 685)
  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 685)
  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 685)
  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 685)
  AUTHORS   ter Beek,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 685)
  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 685)
  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..685
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     Protein         1..685
                     /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=75494
     Region          139..672
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mnakklsimh sayfwiilsl lafallpsna ldyglfests deyleamgwa sfnltwawfl
       61 pvivygalpl lrlpqqtqak telfltalsv lfmfisatly kismgysviv llvgytalat
      121 lslaklkvmq gdkfiiasll ciillifffi vyptlaifvs mfydgdtfsp qqvmriltqs
      181 yivrvitnsl flsgfvgivs tvfglafaly ttriarrtaf igkifsilpi vtppfvvglg
      241 vtlmlgrsgy vteflseyfg fsshnwlygf ngiaiaqila ftpisfmild galksvhpsi
      301 eeasytlran ryqtfyqiif pllrpalans flivfiqsla dfsnplvlgg sfdviatqiy
      361 fyiagsqldy asastlgsml lifslaifii qylwignrsy vtvsgksyrg dvqelpnglk
      421 ytiigmlgfw vifnmalygs ifygsftvnw gvdytltlkn yamlfgqgls dgawpslint
      481 liyagiaapl taffglliay ivvrkdfqgk kslefltmlc favpgtvagv syilafnnap
      541 lyitgtgiiv iismvmrdlp igmraaiagl gqldksldea slslkgsswk tlcfivlpll
      601 kpallsalvt sfvramttvs aiiflvtadt rvatayilnr vedgeygiai aygsilivvm
      661 mtiilffdwi vgdtrisrsk akkmn
//
LOCUS       WP_181913708             384 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein, partial [Mycobacterium
            tuberculosis].
ACCESSION   WP_181913708
VERSION     WP_181913708.1
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 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..384
                     /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          6..>50
                     /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          32..358
                     /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(47,49,199,219,286)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 rfqrgpvlvv vedgrisavd fagsacpdmn lvdlgestll pglvdahahl cwdpdgrped
       61 lagdphavlv grarrhaaaa lrsgittird lgdrdyaala lreeyrqktt vgpelvvsgp
      121 pltrsgghcw flggvadsve elvdavqera argadwikvm atggfvttas dpwqpqygsg
      181 qlaavvaaae qvglpvtaha hatagiaaav aagvdgiehc tflsegsaaa spdvveaiva
      241 qgvwcgmtip rvypempenl vavvqdgwrn irrlidagar valstdagva pgrrhdvlpd
      301 dlvylsrhgf tstevltgat aaaaascglg hrkgriapgy dadllavaag vdhdpaglcd
      361 vkavwrsgtq vplqasavgy ntps
//
LOCUS       WP_181913716             269 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein, partial [Mycobacterium
            tuberculosis].
ACCESSION   WP_181913716
VERSION     WP_181913716.1
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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..>269
                     /product="acyltransferase family protein"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
     Region          10..>257
                     /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 mraaeitgei raltglriva avwvvlfhfr pmlgdaspgf rdalapvldc gaqgvdlffi
       61 lsgfvltwny ldrmgrswsv ranlhflwlr larvwpvylv tlhlaavwvi ftlhvghvps
      121 peagqltais yvrqillvql wfqpyfdgss wdgpawsisa ewlayllfgl lilvifrmkh
      181 atrarglmwl afaaslppvv lllasgqfyt pwswlprivt qfaagalaca avrrlrptdr
      241 arriagylsv lvgvaivgil yllhahpla
//
LOCUS       WP_181914251             265 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: energy-coupling factor transporter transmembrane
            component T family protein [Enterococcus].
ACCESSION   WP_181914251
VERSION     WP_181914251.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
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="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..265
                     /product="energy-coupling factor transporter transmembrane
                     component T family protein"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30184
     Region          6..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..37,75,79..80,83..84,113,117,124,
                     127..128,140,156,160..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 mmnklifgry mpgdslihrl dprakllvsf yfigiiflan nwqtyallav ltllavflsk
       61 vdfkffirgi rpliwlilft valqvlftsg gatywswgif nitefgvmng lfifcrfvli
      121 ifmstlltlt tpplelsdai eyllrplkav rfpvheislm lsialrfvpt lmdetekimn
      181 aqrargvdfg egslvqkmka viplliplfv ssfnraedla tameargyqg gegrtkyril
      241 hwhqrdtmvl vvfvlmtial vflrs
//
LOCUS       WP_181914358             165 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Enterococcus].
ACCESSION   WP_181914358
VERSION     WP_181914358.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 165)
  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 165)
  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..165
                     /organism="Enterococcus"
                     /db_xref="taxon:1350"
     Protein         1..165
                     /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=18872
     Region          73..140
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mmknkqsgkt ehseekrivk leqstlpwsl lldadpeeen vqryidqgag fiwkaendiq
       61 gvivfitnkl vfeimnlava pkvqgqeigy allthtlkem kklkttqqqv iirtgstssa
      121 alqlykkigf leisrekdyf vknykqpiye ngqrlrdqvt lakki
//
LOCUS       WP_181914363             367 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: M24 family metallopeptidase [Enterococcus].
ACCESSION   WP_181914363
VERSION     WP_181914363.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus
  ORGANISM  Enterococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae.
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="Enterococcus"
                     /db_xref="taxon:1350"
     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=40566
     Region          7..366
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mnnvkinelr kwmaqnqvdl ayvsdpghia yfsgyeseph ervlalfipl eqdpflftpa
       61 levedaqnsa wsfdvrgyld senpweiigk eirhrygqpg nigieknalt vdrfdaisdv
      121 ltgsdnftdl taiiqrlqli ktleekdqll aagkwadvaf eigfkavkeg vteqaiiaei
      181 eyqlkkqgvs qmsfdtlvla gknaasphga pgstkispne lvlfdlgvvw dgycsdatrt
      241 vaykkptefq ekiyqitlea qlaaqaavrp gvtaaeldqi arnvinsygy geyfnhrlgh
      301 gigttvhefp slvagndlvi eegmcfslep giyipdqvgv riedcvyvtk dgcipftttp
      361 kellvie
//
LOCUS       WP_181914606             106 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Enterococcus hirae].
ACCESSION   WP_181914606
VERSION     WP_181914606.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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="Enterococcus hirae"
                     /db_xref="taxon:1354"
     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=11742
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawfelilag ilevfwstmm kwsdgfskln ysfytvigmi asfyllskai kqlpmslfyp
       61 iwtgigavgs viigvvlfhd kltlatwffv glllislvgi kitsgh
//
LOCUS       WP_181914666             505 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator [Enterococcus hirae].
ACCESSION   WP_181914666
VERSION     WP_181914666.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 505)
  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 505)
  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..505
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..505
                     /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=58384
     Region          <1..502
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mwiegseqnk rhfimdtffg dqaanslkdy lvnshffnef nfeevliiil deireanlkv
       61 sdfimqnlal hlaltikrin egfpiealdf seelvdrrey qvakkivqrm nrvtkvpfpe
      121 aeihyltlhl vaksnpieki ndellyeela rvieqladff gdsliedqql kngllnhltp
      181 mvvrlrqgit lenpltedik kenmvafeqt krifsqmpml rqftinedew ayltlhimaa
      241 lekvrtakki rvliicatgy gsaqllknrv laefgemllv tnvkgyyein emtlmgvdmi
      301 issidlstmi fkipvlhvsv flnpldsqki rqtiadlqpc pskriktict dspkkrqdyh
      361 gqlserwykv yserptketv ildllsllek devkdytlem maqiskrekm gqivfsetva
      421 vphpaipvgv ttkiavavip egmfwddyqq ikfvflvsps fieneeitiv tkaivqlidr
      481 tdlqqqilie ptfenfsnhf devie
//
LOCUS       WP_181914307             348 aa            linear   BCT 28-DEC-2024
DEFINITION  GntR family transcriptional regulator [Enterococcus hirae].
ACCESSION   WP_181914307
VERSION     WP_181914307.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            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 hirae"
                     /db_xref="taxon:1354"
     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=39076
     Region          1..>70
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
     Region          86..346
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mnqplyqqif hdlqqaiadg slpvdsqvpt ekelsakyqv sritskralt eleqlgliyr
       61 vrgkgsfvka ttsdlnrndv iknsrilfll pflsdlsvgd ftkglnpvmq enqlevmmtt
      121 vdflanktak eimqefdgmi yyafatdqhl dllfelslkq fpvvvldkki yelpfptvls
      181 dnfqggslat ahliskghkk iaylfgeqah pqsvrqrylg ylealdkanl pfhttldakg
      241 ttietlltyi neyqvtafvc endlvaiqtm nhlkqqgyri pddfsivgfd diqaaalvdp
      301 plttiaqdfh qlgelagnal itwlktnnip edtsqpvsfi krhstkei
//
LOCUS       WP_181915570             116 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Enterococcus
            hirae].
ACCESSION   WP_181915570
VERSION     WP_181915570.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 116)
  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 116)
  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..116
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..116
                     /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=13963
     Region          1..78
                     /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 mysvefskef sdvfsenqsk kyqeiivykv neylthnfyr ikpvhssaky siyemkihlg
       61 kedfriafri dgkkvqvfyi srtlkkflfd kevnklvnrf nknqwlidee srsavk
//
LOCUS       WP_181914905             464 aa            linear   BCT 28-DEC-2024
DEFINITION  RecQ family ATP-dependent DNA helicase [Enterococcus hirae].
ACCESSION   WP_181914905
VERSION     WP_181914905.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 464)
  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 464)
  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 464)
  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 464)
  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 464)
  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..464
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..464
                     /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=54155
     Region          2..434
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
ORIGIN      
        1 mslkdelqkr fgftsfrsgq eeiiqsllkn dqdvlavlpt gngkslcyql tgylregmvl
       61 ivspllslme dqvmqlqkqg ekrvvafnsl lsrteryyvl nhlsnykflf lspemltqkd
      121 vieqlqkqki glyvideahc vsqwgvdfrp eyqqlgeiaq klgspvtlal tatattavqh
      181 dietvlfqev pvriihsvnr qnialyvkkt sqkeadledl mkqakgsmii ycatkkever
      241 lyqlfrsrft igyyhgglea sqrrqlqqqf sqnklqflia tnafgmgidk pdiryvvhyd
      301 lpdslenyvq eigragrdqq aseaillyke nderihyffn qlsreqrqsf eiylqyhsne
      361 qeqfdeiqqk wleiiaqtsn pqewlnrlkr qekekeyrlq qmlhyvnakt crralileyf
      421 geklikkpek ccdidgavlt sqenrevsps velkqwqdil lnlf
//
LOCUS       WP_181915634             237 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Enterococcus hirae].
ACCESSION   WP_181915634
VERSION     WP_181915634.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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="Enterococcus hirae"
                     /db_xref="taxon:1354"
     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=27962
     Region          1..237
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mlkifvcdde iahrnkltrm itnyllmkdy dvqfqfatdd pmmilsfisk hktegiyfld
       61 idlktdlngi elakkirdyd ptakiifvtt ytdlvyltfl ykvealdyiv kdnmdtfqkr
      121 vtecidvave rylntnletr pqiwikngpv dvklyvdeif yfesnptphk livyldnrri
      181 eyigkikeve smyevfcrch qsyvvnlmnv keinkkervi tmangakclv strhlkk
//
LOCUS       WP_181915822             367 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Enterococcus hirae].
ACCESSION   WP_181915822
VERSION     WP_181915822.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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="Enterococcus hirae"
                     /db_xref="taxon:1354"
     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=40566
     Region          7..366
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mnnvkinelr kwmaqnqvdl ayisdpghia yfsgyeseph ervlalfipl eqdpflftpa
       61 levedaqnsa wsfdvrgyld senpweiigk eirhrygqpg nigieknals vdrfdaisdv
      121 ltgsdnftdl taiiqrlqli ktleekdqll aagkwadvaf eigfkavkeg vteqaiiaei
      181 eyqlkkqgvs qmsfdtlvla gknaasphga pgstkispne lvlfdlgvvw dgycsdatrt
      241 vaykkptefq ekiyqitlea qlaaqaavrp gvtaaeldqi arnvinsygy geyfnhrlgh
      301 gigttvhefp slvagndlvi eegmcfslep giyipdqvgv riedcvyvtk dgcipftttp
      361 kellvie
//
LOCUS       WP_181915910             541 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Enterococcus hirae].
ACCESSION   WP_181915910
VERSION     WP_181915910.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            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 hirae"
                     /db_xref="taxon:1354"
     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=63066
     Region          7..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(21,23,25,29)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200472"
     Site            order(60,63,100,103,144,163,167,199,241,401)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(199,241,316)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          466..536
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mekkwwhqsv vyqvyphsfq dtngdgvgdl qgvitrldyl hylgidtiwl spvyespndd
       61 ngydisdyqa imaefgtmad meeliaeakk reikiimdlv vnhtsdehaw fiearqsken
      121 pyrdyyiwrd pinenepnql rsifsgsawq fdettsqyyl hlyskkqpdl nwenphlrqe
      181 iyqmmnfwid kgiggfrmdv idtigklpdq eitsngpklh dylqemnqat fgnkdlmtvg
      241 etwgattdia klysdpkrne lsmifqfehv gldqqagkdk wdlkplsipe lkqvlskwqt
      301 slgnegwnsl fwnnhdlpri isrwgndqdy reesgkmfai llhmmkgtpy iyqgeeigmt
      361 nypikdisea qdietinmyh erltlgftpe eilcsinakg rdnartpmqw dnsehagftt
      421 gtpwlhvnpn yqtinvktal akkdsifyty kqlielrknn elivwgdyql vtdtpddvfa
      481 yyrtlnneqw lvvcnmsekn qpytladqam tlvisnypqk qiptgklnlr pyeafvlkts
      541 k
//
LOCUS       WP_181915919             659 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator [Enterococcus hirae].
ACCESSION   WP_181915919
VERSION     WP_181915919.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            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 hirae"
                     /db_xref="taxon:1354"
     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=76131
     Region          8..656
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mkqiekallg llinyqkkyi tshelasels lsdrtirkym vdvkekiekn gakiiakqgq
       61 gyqlailkpl afafflkhqn iaadqgmsem effetedrqk yllnkllled eaifmdeles
      121 elfisrssls ndlneikaki epyalkicsk prqgmwiegs eqnkrhfimd tffgdqaans
      181 lkdylvnshf fnefnfeevl iiildeirea nlkvsdfimq nlalhlalti krinegfpie
      241 aldfseelvd rreyqvakki vqrmnrvtkv pfpeaeihyl tlhlvaksnp iekindelly
      301 eelarvieql adffgdslie dqqlknglln hltpmvvrlr qgitlenplt edikkenmva
      361 feqtkrifsq mpmlrqftin edewayltlh imaalekvrt akkirvliic atgygsaqll
      421 knrvlaefge mllvtnvkgy yeinemtlmg vdmiissidl stmifkipvl hvsvflnpld
      481 sqkirqtiad iqpcpskrik tictdspkkr qdyhgqlser wykvyserpt ketvildlls
      541 llekdevkdy tlemmaqisk rekmgqivfs etvavphpai pvgvttkiav avipegmfwd
      601 dyqqikfvfl vspsfienee itivtkaivq lidrtdlqqq ilieptfenf snhfdevie
//
LOCUS       WP_181916014             143 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Enterococcus hirae].
ACCESSION   WP_181916014
VERSION     WP_181916014.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
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 hirae"
                     /db_xref="taxon:1354"
     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=16727
     Region          13..131
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mekftgymre pfyyetdqmg iihhsnyirw meesrvalld hlgfsytkie ktgviipvle
       61 vtcqykemir ygetvrilpk ieqysgtrln fsyeiygldd gklrttgssk hcfllannqk
      121 ltkleqvipa ldrlfheyaq lds
//
LOCUS       WP_181916513            1024 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-mannosidase [Enterococcus hirae].
ACCESSION   WP_181916513
VERSION     WP_181916513.1
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 11417603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..1024
                     /product="alpha-mannosidase"
                     /calculated_mol_wt=118995
     Region          222..1018
                     /region_name="MngB"
                     /note="Alpha-mannosidase [Carbohydrate transport and
                     metabolism]; COG0383"
                     /db_xref="CDD:440152"
ORIGIN      
        1 mkklleferv qriiielkkn miktaipven lvfhsetgtk efergayfge knqyytiage
       61 lclpnefqnq tvdlaifssl tewdsttnpq ikvyfddqli qgldvnhttl rlpkeyasrd
      121 riplqievfs greekkyplt velrlidpls yelyydlfvi ldswrslneh dsnyiyyere
      181 lgqvvdqlnf ykpysseyyq glmkakehle rafyqaglvk napralvvgh thidlawlwt
      241 vmqavekger sfstvlklme eydeltfiqs qpqmyqlikd typqlyekik ekivagkwip
      301 egamwveadc nlasgeslvr qflygkqfir eefgqesqil wlpdvfgysa alpqilkktn
      361 tpyfmttkls wnqfnqipyd sffwqgidgs ralthfitti sdgysptpyy ttynglldpy
      421 tvkgsweryl dkdvndsili aygygdgggg ptrdmletlk rmkkglpsmp qviesaaidf
      481 feelskkmvk hqekewlgel yfeyhrgtyt sigknkrnnr fgetllqtve klysifarek
      541 ypaemleklw kqlllnqfhd ilpgsgikev ydqtdidyhe lftemnqlid tvlpshdagq
      601 flylfnpsgv seqvivplpl esgeclehqg qsivsqktyd gqflgrfdhl palggsyyti
      661 vksdrevttk tettpltkqy etqdfsllfd ehyrmisafd kknqreiagk kavnellvye
      721 dlplnydawd idfyyknkpt iitdiqeali vdqgpirdtl kivrkfydst itqyihlihg
      781 karidfetkv dwqqnhsllr aefpvpvnay qatydiqfgn lqrpahknts wdkakfevcg
      841 hkwvdlsddg ygislltdsk ygfdaqyqhl gvsliksatd pyetadqgnh qftyslycha
      901 qtwkeaktqe earqlnipcl avrqeqktlp egswvncqer nicletlkka etdgsiimra
      961 yefenrqttt vlkfsqpiqh vqicdllenp ietvaldndh evtvvfkpye ihafkiqlke
     1021 qndg
//
LOCUS       WP_181916571             341 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Enterococcus hirae].
ACCESSION   WP_181916571
VERSION     WP_181916571.1
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..341
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..341
                     /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=40306
     Region          9..320
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mkrsrnqkid hlralailci ilahtglqgi lfnlrcfdvp lmafclaisy yyssknlsyi
       61 syvkkrftrl mvptyiflal lftslffiaq itdtpyqfni fyilhaffmd tgygyawimr
      121 tfflvsllmp flyklskkyq hfveilgift lllilqiflv ylipyvpssw qilytqlvpl
      181 afgycpiall gllvfqldrk kllhlsivil cylsisfyly glhgltyfky ppqlpfilyg
      241 cfcgcfcgcf lwymlakyeg nffapisnyl slhsqelyfi hifyiyiyef ylpkegslln
      301 nwffnfiyll smslltlfli nqgkkkvkqi knktrqvecd e
//
LOCUS       WP_181915887             348 aa            linear   BCT 28-DEC-2024
DEFINITION  GntR family transcriptional regulator [Enterococcus hirae].
ACCESSION   WP_181915887
VERSION     WP_181915887.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            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 hirae"
                     /db_xref="taxon:1354"
     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=39094
     Region          1..>70
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
     Region          86..346
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mnqplyqqif hdlqqaiadg slpvdsqvpt ekelsdkyqv sritskralt eleqlgliyr
       61 vrgkgsfvka ttsdlnrndv iknsrilfll pflsdlsvgd ftkglnpvmq enqlevmmtt
      121 vdflanktak eimqefdgmi yyafatdqhl dllfelslkq fpvvvldkki yelpfptvls
      181 dnfqggslat ahliskghkk iaylfgeqah pqsvrqrylg ylealdkanl pfhttldakg
      241 ttietlltyi nehqvtafvc endlvaiqtm nhlkqqgyri pddfsivgfd diqaaalvdp
      301 plttiaqdfh qlgelagnal itwlktnnip edtsqpvsfi krhstkei
//
LOCUS       WP_181916608             647 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator [Enterococcus hirae].
ACCESSION   WP_181916608
VERSION     WP_181916608.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 647)
  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 647)
  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..647
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..647
                     /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=75231
     Region          18..643
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mlskresqli ellleeenfq pasffsekln vsnktiyqdi qklgqflnrf elkiekkpri
       61 giyligtstk kndakifits keamstevky ssnyrrvylf anlifktdkk ryeyfekkff
      121 vsiatlrkdy eeiikycrla giritsnhvi dtqktpeeli qrtfvnyfek nigvgnekyq
      181 yhfvfdqamv qfvddfvknf yqqskqqptn yivhslklsl ltligrvkhg yhsqtnknpl
      241 fveikkmely mvaldfsngv kdelncsfti ndlyficslf mghgvrpfvn lathsqqime
      301 ttkqfiqdms tlvekdlgqd sqllqslfah iepmvyrlqm gitiknplke diirqystmy
      361 tlttycipkl ekamgirvtd deitfltihf qlafekivnt khvflicptg lgtsqllfqr
      421 irhsspstvv yevidvqklq dynldsvdli istvkleney qtpiiyvrpl ptkeeialin
      481 rhlltlnqqd ntflpsiapd ktilkkylkd gwmflnqdfd sresvlsfit ekykeeqlvk
      541 dnflevvlqr eklgatglss gvaiphanpk yvvktkisii tlknkitwgd vdvrvvlfla
      601 iaeedmiqvk nmiallydvf vsperiksia sketrneiin eiigkrk
//
LOCUS       WP_181916634             711 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Enterococcus hirae].
ACCESSION   WP_181916634
VERSION     WP_181916634.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 711)
  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 711)
  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 711)
  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..711
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     Protein         1..711
                     /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=82230
     Region          8..700
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mvntrnleea ylasvyrqll ekqeeyqqll qetsaygrds lqtmsediri nfesyldnld
       61 tysliemknr eidqlnlkiq sanetlkkie rllmspyfgk ieidfleeea qgknsheafy
      121 igtanftnde detlvydwrs piaslfynnd lghssylvnq nqievmiher rqfiikkdql
      181 lhffdtsvai qddvlldale qsetsemkai tatiqseqnt iirdttsqni lvngvagsgk
      241 tstimqriay llyqyrnqls addllilspn hqfidyigkv lpslgeknpl nvtmiqlvdq
      301 lflgnvesek ayfqritqtd vddqtavlrs qafmkqieqa tslfskqadf flaikkkeki
      361 viskevikki ydstpdypnl reklqatkdr llrywekqll kqagsdaikd qllslpeemq
      421 qqyfqqlitd espeklvsyg kqllqrkyrt vtkqikqmaw vdeqflfeei yqsytgnkyq
      481 rttpctldea varlhvrhll iekitqvkkf vlidevqdyt saqlllllni fpnarftlvg
      541 denqgifnst tsfeaiesyf stagrsvtry dllnsyrssg aittlftqys gekekiaivp
      601 vrpygeepef vtaatfdqwl sqvnerqqht geqltvitle eqqaamiqqk vernnqlniq
      661 vrplslskgl efdhvliylt aepntprerr qmytaisram ktvvislvtd q
//
LOCUS       WP_181916810             111 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Paraburkholderia].
ACCESSION   WP_181916810
VERSION     WP_181916810.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paraburkholderia
  ORGANISM  unclassified Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 111)
  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 111)
  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 111)
  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 111)
  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 111)
  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 111)
  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 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="unclassified Paraburkholderia"
                     /db_xref="taxon:2615204"
     Protein         1..111
                     /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=12134
     Region          24..111
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mntpfrscla acavfvlaas tahaepepta lvdqqhcmfc htrdapflap sfeqiaeryr
       61 nvpdaqfmle hklrlggkah wgdmamplpa drggplsaed artlvewvls q
//
LOCUS       WP_181916808             359 aa            linear   BCT 28-DEC-2024
DEFINITION  potassium channel family protein [Paraburkholderia sp. BL27I4N3].
ACCESSION   WP_181916808
VERSION     WP_181916808.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL27I4N3
  ORGANISM  Paraburkholderia sp. BL27I4N3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
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="Paraburkholderia sp. BL27I4N3"
                     /db_xref="taxon:1938805"
     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=39523
     Region          56..352
                     /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 mpespkpepr lprfrlprra rtpwqaprar tlftrpaasp qrmllqrvyl vvglcvlafa
       61 vlyldrdglr danrkvlgiv dlmyftmvtv atvgygdivp vtararlida ffivpirivi
      121 wfvflgtayq fviqrvieef rmkrlqkqlr dhvvicgygl sgsvavrell esgfaaesiv
      181 vidpqqaale aatalgvagl lgdpsredll qqaqvqiara viiavtddat ailltltvrs
      241 vapqtkivvr iqeqtyqrql rqaganvivs stkiggllla davdseyivp fvndllsarg
      301 rvnlverrat aqeigrwsna lpgavvvglv ragrvlsfye depcpieagd llmliqssr
//
LOCUS       WP_181916971             276 aa            linear   BCT 28-DEC-2024
DEFINITION  amidohydrolase family protein [Paraburkholderia sp. BL27I4N3].
ACCESSION   WP_181916971
VERSION     WP_181916971.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL27I4N3
  ORGANISM  Paraburkholderia sp. BL27I4N3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
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="Paraburkholderia sp. BL27I4N3"
                     /db_xref="taxon:1938805"
     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=31048
     Region          3..276
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mlvidsqvhi wenhragrpw pepttprvdw pdgysaesml eemdavgvdr tvivppvwvg
       61 nsnetgleaa ntypgrfavm grfdptlpdv trrlrtwleq phmlgirmsl srpphsklld
      121 ddmldefwaa cerfgipvmi fagrtieklr pvtlrypgln lvidhmgcdl gakgrdafak
      181 mdvvlelakn snvslklsma pnlsrgpfpy tdinpflrrm ydavgprrim wgsdrtnltn
      241 ytdclrhvtd glgflsaddk iwilgktaat vlnwka
//
LOCUS       WP_181917202             363 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Virgibacillus dokdonensis].
ACCESSION   WP_181917202
VERSION     WP_181917202.1
KEYWORDS    RefSeq.
SOURCE      Virgibacillus dokdonensis
  ORGANISM  Virgibacillus dokdonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Virgibacillus.
REFERENCE   1  (residues 1 to 363)
  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 363)
  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..363
                     /organism="Virgibacillus dokdonensis"
                     /db_xref="taxon:302167"
     Protein         1..363
                     /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=41453
     Region          8..361
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mskihrklin lapvsflwrl tflhffvivv alwisgwaly ntacflaagv gnldelrqqq
       61 fnqtllnyvw ifviiaivva silyyylskk llqpihtlme atqllqtgky pdpipvsrnd
      121 eigqlvqqyn qlmeqlnrne tdrkklvsdi shefrtplsn lngylsalks gdiegnqalf
      181 valyqesqrl tsmldqfdql kqwdytnast ynrkemqavk plleqcvsmf hwtlkqtgik
      241 lelqaevadv yvhaegmqqv isnlldnaiq yykgkgsiri tgqkrnngyy iavsgpsepi
      301 psqerelifq rfyrlessrs rdtggaglgl aitkeiidqh dgsiqidtvq drniftvklp
      361 iha
//
LOCUS       WP_181917719             278 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Cohnella
            phaseoli].
ACCESSION   WP_181917719
VERSION     WP_181917719.1
KEYWORDS    RefSeq.
SOURCE      Cohnella phaseoli
  ORGANISM  Cohnella phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
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="Cohnella phaseoli"
                     /db_xref="taxon:456490"
     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=30331
     Region          6..273
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mahfpfrtal nastlfpyel gireqiriaa qagydgieiw mkdlqqhvae ggtadelrre
       61 aeglgieian aisfiawade deavrrsaav qtdeelalls elgcpsfaap pfgsvanasl
      121 ddiadrfaal aeqcrkhgva pvlefwgrsp klnrlseavy iamqsrvada tllldpfhmy
      181 tggsslndld flsadrigiv handypelpp retigdedrl fpgdgiapsg elarrlnklg
      241 yrgflslelf lrdvgdrsal elarhglgkm rsaysvve
//
LOCUS       WP_181917394             377 aa            linear   BCT 28-DEC-2024
DEFINITION  SGNH/GDSL hydrolase family protein [Cohnella phaseoli].
ACCESSION   WP_181917394
VERSION     WP_181917394.1
KEYWORDS    RefSeq.
SOURCE      Cohnella phaseoli
  ORGANISM  Cohnella phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
REFERENCE   1  (residues 1 to 377)
  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 377)
  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..377
                     /organism="Cohnella phaseoli"
                     /db_xref="taxon:456490"
     Protein         1..377
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=42391
     Region          36..241
                     /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 mqtnpveqsn etripqkict fndawtewlq gskfpiaffg dstvdgantt gwvantigvd
       61 gaspnafskk leellrqaan nevlriynsg ftgtnaswav tileeqygvt sayhdtrmig
      121 igfgindrll ypnekayrdg fkgsieqiin wcyskniqpf llttqailep gvkteyaddy
      181 pmrtsehvas ianevkrela ekyglqlvdm nkytesflly ssisvqkiis drlhfgdmgh
      241 ryeaevlfsc lsprtivadg ytkidyssqk ikdsvpddwl tipeaptdsf kvyvehtkad
      301 ttdrnimsaw vfvnarrklt lraykgsspd tyvkingnnr sldgeetiid qldlglyyle
      361 vftgssskvd fkgfild
//
LOCUS       WP_181917935             267 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Cohnella phaseoli].
ACCESSION   WP_181917935
VERSION     WP_181917935.1
KEYWORDS    RefSeq.
SOURCE      Cohnella phaseoli
  ORGANISM  Cohnella phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
REFERENCE   1  (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   2  (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
REFERENCE   3  (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
REFERENCE   4  (residues 1 to 267)
  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..267
                     /organism="Cohnella phaseoli"
                     /db_xref="taxon:456490"
     Protein         1..267
                     /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=30148
     Region          29..267
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          177..260
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msedlrltde sieqtiagsv vyppggtygp lryreiqlvl lhsgsmevev dgaaykvhpg
       61 qlllllpeen vyiafdrsgk srhrwitlsl reyeadlqhq lhamprtipi sepmnrlvdl
      121 svmqrqtdlp eyrsvanalg laairlyaae sarndalian pvigkvksfi hehyaiplsm
      181 keiadhanvs ashlvrlfkq aeqttpiqyl wdyrvehslv llrttglsvg eiaeqcgfks
      241 ryhysrsvkr ytgksaseir alhwqsr
//
LOCUS       WP_181918021             349 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Cohnella phaseoli].
ACCESSION   WP_181918021
VERSION     WP_181918021.1
KEYWORDS    RefSeq.
SOURCE      Cohnella phaseoli
  ORGANISM  Cohnella phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Cohnella phaseoli"
                     /db_xref="taxon:456490"
     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=37362
     Region          8..349
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 mgrndpyidl gtdartapts rmweamqava lnatpfkgqe aveallarac eltgqaaall
       61 lpsctmanli ammahadrgd qvileesshi awsegwgmas iagiypkllk grrgaidlee
      121 ilsaveasvf shrprtkllc lenthnaggg avlpqayaae vcaamkerei yvhldgarif
      181 naavaldlpv rqmtemydsv tinlnkglca legallcgsa amirkasqla ralggdsqhk
      241 aeiiaaagli glnemvddia kdhrraylfa savqripgig velqrvqtni vmvdvsgtgl
      301 aakevlqrlk irgvasylys davlrfvfhr eindedalra srllgeaig
//
LOCUS       WP_181917729             794 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Cohnella phaseoli].
ACCESSION   WP_181917729
VERSION     WP_181917729.1
KEYWORDS    RefSeq.
SOURCE      Cohnella phaseoli
  ORGANISM  Cohnella phaseoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
REFERENCE   1  (residues 1 to 794)
  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 794)
  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 794)
  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 794)
  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..794
                     /organism="Cohnella phaseoli"
                     /db_xref="taxon:456490"
     Protein         1..794
                     /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=90463
     Region          4..673
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          709..793
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; cl38983"
                     /db_xref="CDD:476840"
ORIGIN      
        1 mddqwfiaeh seetngpage wwpavvpgsv htalmnagii pdpyvgknds iaraqsfrtw
       61 wikkefeipa dfaamrivfn gvcdsctvwf nghqiadnqg mftsfefdlt dkvlrkgrst
      121 llvrlesapy ristgepnpy wigmnvgwmd tvifnnvygw hyidvpatgi wrtvvleekp
      181 hveiknpfia tkdymtgtmn lsaeleggvh eregtlriei epdnfegnsf gieyevrpse
      241 nepelhfefq ipehrlwwpn glgdphlyrm tlnfmpkkgi gdrkqvifgi rkvqfgplpg
      301 gpdpeiynwa lqvngralfa kgtnwctida lmrfdkrrya rfmdmarrsh iqlmrawgag
      361 lpetdefydl anrmgimiyq ewptawdshk vqpipilekt vrqnmmrlrn hpsliqwggg
      421 nespdptgva idmmgrlsye ldgtrafrrt qpwggslnny dvywgrqsld rnlqlespfl
      481 gefglasapn lesvkkyipr hewgawpppp fgtfahktpv fnrnedmsrl shyvadfidn
      541 ssmaafvlgt qlaqttglrh tlelartrwp eaagvafykl ndncpsvsws ivdwygapkl
      601 ayyfvqdays plaavvlldg lnpgdspmea pvfilddssc lagqnwevev tafgstlrev
      661 kktsfrgrga ihvrrqvgqf sltkeqmnht plfivselrl egalryrsfy wlnyladrgc
      721 lfrlprttlq serhpgkiti rntgslpavg vnmssphsde ltiednffwm npgetrevdi
      781 sgdrdvslqa wnvd
//
LOCUS       WP_273577780              75 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Xenorhabdus
            aichiensis].
ACCESSION   WP_273577780
VERSION     WP_273577780.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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 10616232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..75
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=8104
     Region          10..75
                     /region_name="HTH_35"
                     /note="Winged helix-turn-helix DNA-binding; pfam13693"
                     /db_xref="CDD:433408"
ORIGIN      
        1 mslisqvgtd whradiraal ekrgtnlrtl siaaglaadt lrnalvrpwp kgekiiaqai
       61 gvepaviwps ryskq
//
LOCUS       WP_273578152             813 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein [Metamycoplasma hyosynoviae].
ACCESSION   WP_273578152
VERSION     WP_273578152.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hyosynoviae (Mycoplasma hyosynoviae)
  ORGANISM  Metamycoplasma hyosynoviae
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..813
                     /organism="Metamycoplasma hyosynoviae"
                     /db_xref="taxon:29559"
     Protein         1..813
                     /product="coiled-coil domain-containing protein"
                     /calculated_mol_wt=93684
     Region          14..>139
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 mikkknllii siplltatpl afsvsckdtk aeqlqkvvsa yqneikvaeq likeledvtk
       61 ypqlqsdltm lkqeveaikk efeksknvaa dvqklitkik tkiqtalekk qaedardktf
      121 dsidasssle iisenatdfy eairqgndfy fdrkayklva vekgkrpnwt eiqkylvnvn
      181 ikdlandlql andaeplygg nkisgkidyq ikdneiifky kvaffnkgnp kvsekiyetn
      241 lgeilsqeql qklaeleeae tktsfeykgq kqleetylse vngedikanv pegfeiakqk
      301 ivknsdvgfy eltilfklki kgtdivskkn kqfiitgwkk tpekiaeeek akkeieeqtk
      361 tikvyvsnek ayqdiivrqk ptqenaqpnf vlngysdlfh atvvevkved eggkkkitvt
      421 yeiwakanqs ikikkqnvnv etnynndttn phnlteeeqk kyledaikdv kiipfyskdk
      481 tyieklrneh ltnksffiqg kkyqnleyqy gnvvkngekf eveatlsysy wpqspkvkvk
      541 keidlsilgv deinktkpdg nkiqdieaps atindffept ldinkfvdsp edeydggpti
      601 kviktntldk ikdlvcwnkt lydqmasgdf gekyllqnlk ydkdtyekkd niyflqrkgs
      661 pkellgnhyv fifskpkydq ntkeltikvs vvsvndlnag nsveqvaskr invkkdifln
      721 endtyktilf sedvyakskf kadewdkknk sadhytvevv knmleqkltg ytvfdvkvdh
      781 sekdqgilky eytvkndkft sypfkitvkn fkk
//
LOCUS       WP_273578440             360 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Xenorhabdus
            aichiensis].
ACCESSION   WP_273578440
VERSION     WP_273578440.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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
REFERENCE   2  (residues 1 to 360)
  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 360)
  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..360
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..360
                     /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=41659
     Region          53..352
                     /region_name="HisC"
                     /note="Histidinol-phosphate/aromatic aminotransferase or
                     cobyric acid decarboxylase [Amino acid transport and
                     metabolism]; COG0079"
                     /db_xref="CDD:439849"
ORIGIN      
        1 mkiiketffy rselyheipe lkvyktkenl slmelpyqtn ldfektsdki khaninryps
       61 ldtnlikekl cesdgiiydd nillgnglle iiqtillsfs tdkttiiipd psffmftrls
      121 kicrvnicki plikkfdidv fgfiqaskky qnpiiiidnp nnptgslfkk qdlkliaenc
      181 ncpiiideay iayskdnssa lsfimnydnv ivlrsfskig faglrfgyli snsdmvsyik
      241 kfslqysltd ikinvlldil nnnkinldhi nsikkqrdii iskishmekv fvsksqanfi
      301 ffrikkyyiy nflndlinhg ikinhfpygy skitnnslrf slgnditnni vislmlknfk
//
LOCUS       WP_273578818             292 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Xenorhabdus aichiensis].
ACCESSION   WP_273578818
VERSION     WP_273578818.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 292)
  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 292)
  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..292
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..292
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32841
     Region          20..115
                     /region_name="ybbN"
                     /note="ybbN protein family; ybbN is a hypothetical protein
                     containing a redox-inactive TRX-like domain. Its gene has
                     been sequenced from several gammaproteobacteria and
                     actinobacteria; cd02956"
                     /db_xref="CDD:239254"
     Region          125..>247
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          125..151
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          156..183
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          203..292
                     /region_name="TPR_20"
                     /note="Tetratricopeptide repeat; pfam14561"
                     /db_xref="CDD:434039"
     Region          223..254
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          259..291
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 mesitntnsh tahiihines niapmiqhsl tqlvvfyfws pqnlhchele etldklahey
       61 agqfalakvd cdqlpniaaq fgvrtaptvi fvqearpvhg fegiqtdetv rkmfsqfltq
      121 qkkslleqan erlaegknqe alsllkeahq aepkeieitl llaqvyialn hledaqnild
      181 tlplekqdqr yndllailes qkqaanspei qqlqqaleiq penaelavql atklhevgrn
      241 eealellfsf lkkdlsaadg avkktlmdii saletgdtla skyrrhvysl ly
//
LOCUS       WP_273578953             214 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Xenorhabdus aichiensis].
ACCESSION   WP_273578953
VERSION     WP_273578953.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 214)
  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 214)
  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 214)
  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 214)
  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..214
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..214
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23284
     Region          6..201
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mdkfnvifdi dgvivdseql hfdvlcelap dhtrdiqpqq liglslaetl seigvplpeq
       61 qgitdkiisv yqeklsahyl rpgvtrliaa lqqndiafgf vstapravcl anlgllglfd
      121 epvlisgddv ertkpfpdpy lamlklkrmd vqqtlviedt dlgiaaakqa gipwvyawph
      181 dlsvaeqygq atciigeltd ipqfsginll sagc
//
LOCUS       WP_273578891             283 aa            linear   BCT 28-DEC-2024
DEFINITION  RHS repeat domain-containing protein [Xenorhabdus aichiensis].
ACCESSION   WP_273578891
VERSION     WP_273578891.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 283)
  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..283
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..283
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30917
     Region          <40..206
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 micrlcsfks slvlgrypen rsdlragelq tqyavcaptg eplalfdpkg hrvwrqpahs
       61 lyglclkalg enaqfdpglk fagqwldees glvynrfryy savagqyltp dpiglaggen
      121 pyayvsnpts widplglaka kgktnaqahe ivkymgegev eavkaaggki vphirgsvar
      181 wvnlpganwn pndevfrvvy titpkgmdil qnakdlegff vgeagykdgv lskntneaga
      241 rgigynlikn pdsafnneii karseqkvkg kwgkpkkcsh kld
//
LOCUS       WP_273579009             333 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Xenorhabdus aichiensis].
ACCESSION   WP_273579009
VERSION     WP_273579009.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     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=35426
     Region          25..327
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msrshspsfg lmalglllfl laissanmga lplsfktlwe sslddpqwqi wlnirlpril
       61 lailvggala vsgavmqglf rnpladpgll gissgaaltv amvivlpftl pasialyghi
      121 iaafvgsllv sflifslnky nhgnlsklll agiainalcm sfigvlsyvs ndqqlrqfsi
      181 wmmgslsqie wptliiaasl iipvcilafs qsrklnllql gdeeahylgi nvqrtkyqll
      241 llsalligca valsgvigfi glviphlvrl rfggdhtwll pisvlggacl llsadtlart
      301 lvspaeipvg litgligapy flwlilkpsg grl
//
LOCUS       WP_273579087             478 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Xenorhabdus aichiensis].
ACCESSION   WP_273579087
VERSION     WP_273579087.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..478
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..478
                     /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=52192
     Region          1..392
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnydvivvgs gaiagsiaye lagrqlkvcr lgrldrsnaa sraagamngc fgevtsglia
       61 sdygklklkm driakdrwst waqrlaassg dtrplftakg thvilntagm evvdsvnyda
      121 iesvlreyne pyevveprsi kgmkpndlar slkglyipee halnshllle mldaallreg
      181 geivdnnvkr vltengiivg vetvdgvrft ankviiaagv qsldilsdqt sivqkipplf
      241 agygvsvllk vknpdelpts virtpnrafa cglhcvprsd gvlyvgatnl lsnqprthat
      301 vatvqfllec aynqlnvdlf eseilaiqvg nrpisadgfp ligpcgidgl wlvtgtyrdg
      361 lhqspllady vanalmglpn leidladftp irrplvglsr dmtiseaakq tvamgyefiw
      421 nlkpgwdeli yesllnsyga qvesiddiyt pppdlvafsc kdeqitkrlr dyyrcwkk
//
LOCUS       WP_273578352             261 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Xenorhabdus aichiensis].
ACCESSION   WP_273578352
VERSION     WP_273578352.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 261)
  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 261)
  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 261)
  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 261)
  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 261)
  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 261)
  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 261)
  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..261
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..261
                     /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=29585
     Region          23..115
                     /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          179..254
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mawlrqsdhf dpdglkysln vpvigiaaem gqhdsgfhqh dmgqllftqq gcikitlanq
       61 lsilpptrva wipprtlhra emrgsvgyrs iyldisgiew isgqseilet tpllrviler
      121 iaispfdtdw rqgkgahlla vffdemseag keptllplps drrlarlpfd qlppplqmla
      181 thigasekti triflretgm nyqqwrqqwr likaiellaq dktlsyvaqe lgfandsafv
      241 tffrknmgrp preymagack r
//
LOCUS       WP_273579120             271 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Xenorhabdus
            aichiensis].
ACCESSION   WP_273579120
VERSION     WP_273579120.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  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 271)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 271)
  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..271
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..271
                     /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=31491
     Region          <99..267
                     /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 mkrttglnqk siythlltip dfntlehkqr glyilldgem iwkdctntyh itsneilfth
       61 pgsyvaktnt encqvlwlpl qmeflrnflk rfgsllskie rrdfparrli pfnqfpllte
      121 sirglanlla hdsppaliql rveellllls lskqgallms vlrqlsnrqv erlqtfmeah
      181 ylkewrlndf arefgmglts fkelfnsvyg tsprawiseq rilyahqlll nsemsiadis
      241 lesgfssqsy ftqsyrrrfg ctpnrarygk d
//
LOCUS       WP_273579271             238 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Xenorhabdus aichiensis].
ACCESSION   WP_273579271
VERSION     WP_273579271.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     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=26424
     Region          3..231
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mkkklateql adakrlkrif vskqkqlgis sqdafadelg mtqsavshyl ngvnalnler
       61 aadfanklgv riadfspsld qqarkllkvi ygddptlaah qhpqkqypll nwanagiwce
      121 epaplypgnd ieqwyetsie csphafwlev kgdsmassne lniqqgmiil vdpdvkptad
      181 nlvvaklege keltfkqlit egydaylkpl npqynmipln dkvhivgvvi eakiaklp
//
LOCUS       WP_273579222             458 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Xenorhabdus
            aichiensis].
ACCESSION   WP_273579222
VERSION     WP_273579222.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 458)
  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..458
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..458
                     /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=48145
     Region          1..446
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 melitqwlna ingivwgipm lvgilgigif mqirlsflpi rklgtgfkll fqkneqrgeg
       61 qispfnalmt alsatigtgn iagvatavvm ggpgalfwmw mtallgmatk yseavlavrf
      121 retdkngnyv ggpmyyikng lgkkwiwlgt lfaffgsiag fgigntvqan svadvlqsnf
      181 giektvtagi lvilvgavli ggikrisdva gklvpvmtvg yfgagiivla lnitaipeaf
      241 vliiksaftp vaaqggfaga avwaairfgv argvfsneag lgsapiahaa aktqnpirqg
      301 liamlgtfid tiivcsvtgl tivitggwlt getgatltas sfsavipggn yivavalaif
      361 afttilgwsf ygekciqyll gpkaivpfri awiialpiga tqslnfvwll adtlnammai
      421 pnlialalls pivyrltkdh irdvnadrie vktaaktd
//
LOCUS       WP_273579247             407 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Xenorhabdus aichiensis].
ACCESSION   WP_273579247
VERSION     WP_273579247.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     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=46783
     Region          7..392
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 maaelnklsd kklkalhgke rnvieffadg aglsakaskv ggiswvftyr ldgkklnrlt
       61 igrypdmplk qaretrdkcr nwlssgkdpk lqfnlamqes lkpvtvkdsi eywiehygrd
      121 hrvnidtlil qlekhiypyi gemalsdcet rywlecfdri kkdapvasgy ifqmckqalk
      181 fcrvrryavs hvlddltisd vgkkqnkgqr dlednelgql wksinsgnyl pyynnllkil
      241 iafgcrtrea rlskcsewnl dsmlwtvpke nsktggkiir pipeymkpfl enlvyqnhkn
      301 dyllgefkst gvvseygaki wkklghtekw tlhdlrrtla tklndmgvtp hvveqllgha
      361 lpgimaiynk sqylpeklda lnkwcerldv lagnyenvii lkagkkc
//
LOCUS       WP_273579337             335 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Xenorhabdus aichiensis].
ACCESSION   WP_273579337
VERSION     WP_273579337.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     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=35142
     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 mnakrrtali lglvlmallt clciaaslsl gskslplsai wqhywlgdqg syydlvinar
       61 eprtliglma gaalalagtv tqgllrnplg dpgllginag aaaavvcfsf ipaldilprf
      121 wtafigasls tllfyllsgg prntnpvrlv ltgasinicl falvqgivli naqamdnyrf
      181 wtigslsams lneasllipy llvavvvtls lsaslnvmvf gegiasslga nvartrilsl
      241 vmvtmlaata tamagpiafi glaaphlmra lvgsdfrwll pyclfagpcl llisdvvarl
      301 liapqeimvg iitagmgapl lylvaknrsq kimae
//
LOCUS       WP_273579284             383 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Xenorhabdus aichiensis].
ACCESSION   WP_273579284
VERSION     WP_273579284.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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..383
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..383
                     /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=44129
     Region          56..361
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msifrrgecw yasysfngkr ikvllgtkdk kqaqelhdkr kaglwrvsvl gempkvtfev
       61 actrwleeka nkksldddkt kiifwldhfe gvylsdides niynavsklt nqkqaenwek
      121 hvsgkkrrqv kkkispvsva tkaaylafik sllrsaerdw kyldkapnik vpkpknnrir
      181 wlepyeakrl idecseplka vvtfalatgl rrsnivnlew sqidmqrkva wihpdqtksg
      241 kalgvalndt achilrqqig nhhkyvfvyt kaknradgtm tptvrkmrvd sntsfrtalk
      301 ragienfrfh dlrhtwaswl iqkgvplsvl qemggwesie mvrryahlap shltehaqqi
      361 dalfhdevsn mshshlsvvg hte
//
LOCUS       WP_273579339             606 aa            linear   BCT 28-DEC-2024
DEFINITION  IucA/IucC family protein [Xenorhabdus aichiensis].
ACCESSION   WP_273579339
VERSION     WP_273579339.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 606)
  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..606
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..606
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70306
     Region          15..593
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 msplytklsp qtshltresw lhankhlvak ilrellhekl ifpvnqseek sysieidkfq
       61 yhfkaqsyql dhldidvasi tkfshnqpqp ldaiqliiel hplldisekm lpiyldeiss
      121 tlygyafkyq nnrltaqdla qadyqaveta mteghpvfia nngrigfdad dylhyapesa
      181 npvtliwiav hrnktvfsal sslsysqlva eelekylpar feqhmqtlgl nlsdyylmpv
      241 hpwqwlhria isfaadianq eivylgeghd rylaqqsirt ffnisqpkkn yvktalsvln
      301 mgfmrgldph smvttpqvne wlnhlvesdv ffqekgftil reraaigyfn hyfeaaikkd
      361 nphkkmlsal wrespmtilk etqrlmtmas llhvdregda vvaalvkdsg lsaeawvtry
      421 ldayfspllh sfftydlvfm phgenlmlvl ennvpvkmlm kdigeeiail ngdiqlpeei
      481 dflhvtikde mkinyifldi fdcffryltp llqkhlalpe arfwelvaec vynyqsqhln
      541 qiekfrkfdl fkhdfvrtcl nrlqmannqq midlddrekn lkfagtlvnp lhalrekyav
      601 tvetdn
//
LOCUS       WP_273579693             245 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent DNA methyltransferase [Xenorhabdus
            aichiensis].
ACCESSION   WP_273579693
VERSION     WP_273579693.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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 245)
  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..245
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..245
                     /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=28294
     Region          6..>141
                     /region_name="COG4976"
                     /note="Predicted methyltransferase, contains TPR repeat
                     [General function prediction only]"
                     /db_xref="CDD:444001"
ORIGIN      
        1 mtdnilynpi ahlyenfsds sphidveirt imhlagevqg ksvldlacgy glfsrkfkkl
       61 gasniigvdi sdkmiqiakn ksrqyqddie fhirnvckme sfgkfdliva awlfchaesf
      121 edlktmfrvv adhlkpsgkl iaytfepdyr lekgnyenyf ikvlseepvk dttllkaefi
      181 ttppspftmy rwsreqyaaa ineaglkhfe whkpmlqerd iekqspgfwd dyqrncldta
      241 lvcql
//
LOCUS       WP_273579751              78 aa            linear   BCT 28-DEC-2024
DEFINITION  transcriptional regulator [Xenorhabdus aichiensis].
ACCESSION   WP_273579751
VERSION     WP_273579751.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..78
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..78
                     /product="transcriptional regulator"
                     /calculated_mol_wt=8468
     Region          6..73
                     /region_name="YdaS"
                     /note="DNA-binding transcriptional regulator YdaS,
                     prophage-encoded, Cro superfamily [Transcription];
                     COG4197"
                     /db_xref="CDD:443351"
ORIGIN      
        1 mintpiekai klwgsqkrfa ehigkaqstv sdwltgkkri spenvviive atngavqahe
       61 lrpdlpkvfp ppeigane
//
LOCUS       WP_273579825             394 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Xenorhabdus aichiensis].
ACCESSION   WP_273579825
VERSION     WP_273579825.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..394
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43489
     Region          1..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 mdflplsgiv vidltrhrag pvtsrllgdw gaeiikieep tdqgdsmggs regfdyqnlh
       61 rnkkslsvnl kteqgqqilq rlvrkadvvl enfrpdvkfr lgvnyeslkk inpriicgsi
      121 sgfgqegpyr srpavdqivq gmsglmsvtg tkesgalrtg aaiadvsagm nlaqavllal
      181 yhrektgegq wvytsllest laimdfqvar wladgktpel mgndhptlmp tgivktkdge
      241 iniaaaeddk fkilchlldi pmiysnpqys dihsrsihrk qlmseieaat ikyeskqliq
      301 mlnaggipsg yvydiaqams dpqmnylnmk cpinhphlgd ltlvgqpmhl safpdfdavr
      361 tpapehgqht gnllknylgf nddeiasfre mqvi
//
LOCUS       WP_273579827             315 aa            linear   BCT 28-DEC-2024
DEFINITION  TauD/TfdA dioxygenase family protein [Xenorhabdus aichiensis].
ACCESSION   WP_273579827
VERSION     WP_273579827.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     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=36774
     Region          8..279
                     /region_name="TauD"
                     /note="Taurine dioxygenase, alpha-ketoglutarate-dependent
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2175"
                     /db_xref="CDD:441778"
ORIGIN      
        1 msdknkytir klspyfcaei rgidlngpld demvkairsd leahevlvfp eqdltsedlm
       61 rlgryfgplt vhpfaensek npelivfdyk dgnppvltdr whsdetyklc ppmatmlysr
      121 ivpeiggdtc fssmttaydf lstktqdfir gleavhdfas ykylfpdtek grqllqrkel
      181 eyppiahpvv rihpstqkkt lfvnphytry iknmdqrdsd allaqlfnat svleyqyrhq
      241 wkpkmlvmwd nrsvqhaavh dyyphhryme ritvggdkpi seaepttveq lrkfkvptyd
      301 hndsrrakrq feies
//
LOCUS       WP_273579966            1089 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Xenorhabdus aichiensis].
ACCESSION   WP_273579966
VERSION     WP_273579966.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 1089)
  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 1089)
  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 1089)
  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 1089)
  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..1089
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..1089
                     /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=122952
     Region          9..>1061
                     /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 mnhpeklkpf alseaqssrw fqyqinpsqr grnngafcar vkglnaqdle dalnhlikrh
       61 pmlracfgly dgelgyriae nseikvqthd arhlsedtlq qlvlddcrhv ldlenplrfy
      121 aswyqcnaqe svmvltfdhl vvdgwsywll leelgmilts qelepisehs yqdyvswqqq
      181 wlnsksakkq qqfwcdnlag dlsalswpmk igsvqngvdn nssspatdki tafgripdal
      241 asklcamape ygnslfaifl aayqillnry taqddivigs mmpgrsqakw gklvgefvnp
      301 valrgqingd itvrehilqt aktirqaien qrypftkvle qfklqrsadt hpifqtlmtf
      361 qkpryvselp tlwmdddsst tvhwggaelr pfphplyadt pvplmvnmme vnqqirchfh
      421 ydpqvfdael inqliknlit lltvmadnqq qsidslplmd eqerrqvlyd fnktdkpfpq
      481 halihqlfeq qvertpdaia licgdnplsy telnqqanrl ahalikagir pdnriaicme
      541 rsldmvigll gilkagaayv pldpeyptdr lghilsdsdp alllihhglq dhlpmtnrpa
      601 wvleseeyqt niasqptdnp vatdlgltsr hlayvlytsg stglpkgvmn ehrgvvnrll
      661 waqdeyqltq hdrvlqktpf sfdvsvweff lpllagaqlv marpgghkea lylleeietr
      721 gittlhfvps mlqsfihltp adrcpslrqi lcsgealsys lqqqclahfa hselhnlygp
      781 teaaidvtsw rcvpnqhagl vpighpidnt qiyildkhdq pvpigvigei yiagagvarg
      841 ylnkpeltae rfvrdpfsqh pdmrmyktgd igrwladgsi dylgrndfqv kirgnrielg
      901 eiearlaqsd gvqdviviar eydagdtrlv aylipkpgvt lsipalreqv gsslpdymip
      961 safvmldafp ltlngkldrk alpapdhsav ltreyaapqg eteeqladiw qkllkidrvg
     1021 rndnffelgg hsllmlqlqs risenfdvel siqqlfahpt icqleehiid aqllqfdaes
     1081 lqdlyktmg
//
LOCUS       WP_273579979              67 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator, partial [Clostridioides
            difficile].
ACCESSION   WP_273579979
VERSION     WP_273579979.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 67)
  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 67)
  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 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   4  (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   5  (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 11457199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     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]"
     Region          1..>67
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkidrlfsiv qmlvnrksvt akeladyfnv svrtiyrdie ilsangipiy atqgkgggis
       61 ilenysi
//
LOCUS       WP_273580174             433 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Xenorhabdus aichiensis].
ACCESSION   WP_273580174
VERSION     WP_273580174.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..433
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..433
                     /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=47927
     Region          29..396
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnnnldslty yaatkkydlr fptltedldv dvviigggfs gvntalelae kgitniaile
       61 grtlgyggtg rnggqvmagi ghdldrikrh vgekgletif risnmgagii rdriakydik
      121 adfckgygyl gynarqektl rgwlkefqaa cpdeeielyt gtdvkkvigs dlytcalkhm
      181 ggghvhslnl llgeakaate qgvrifensq vvnveygprv tvrtamgtvr askilwacna
      241 flngleptiy kktintyafq lmteelsddl iekispirga ysdispviny yrvtkenrvl
      301 fgsatqyley ipsdlkawnr krmldvfpyl kdvkielawg gplscsvnlf pqigslpehn
      361 nvfyvqgysg fgvtpshivc kilaegmseg seryslmssi phlnvvgkdk lrslllsagk
      421 twhqasgywk grr
//
LOCUS       WP_273580102             298 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Xenorhabdus
            aichiensis].
ACCESSION   WP_273580102
VERSION     WP_273580102.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     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=33188
     Region          46..291
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mklssfteii lpdnyhtqdf lafhhrdekg aseivqqsrm kkgiiwhgnp alltvsidkh
       61 raqiqlevdg gdahqsekal stlashmlgl lqpveefesm yqadpvigel vtrqaglriy
      121 qsatpfeals waiigqqisl naaisirrrf iqaigvkhss gllchptheq iiqcsehdlr
      181 qcgfsvskan allnvsqlid sgelklaite geikrltdnl laikgigmwt inyallrgfn
      241 ylngslhgdv avrrnlqyll rqedkvnaeq teawlsgfsp wkalvaahlw rqqsssgy
//
LOCUS       WP_273580231             354 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Xenorhabdus
            aichiensis].
ACCESSION   WP_273580231
VERSION     WP_273580231.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..354
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39168
     Region          8..350
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mavmntvalq raldnwllfs pclgvnvtls dslgnhwhsa sgfeqfenkt emkalqqcyi
       61 ysitktftai rilqlveqek laldsrltei lghcgldpti tirqllnhta gvpnytefdg
      121 ydaatkaspg tpwsydytla lsgekgmkfs pgegwdysnt gymllakvie vvtgesfqkn
      181 indgiilple ltktyvasdi drgtvipgfs rwlnhndvme nitgiyhphw cktelmvstt
      241 keicqvyqal fqgkilspal laemckpisi grsagpfyrk psygmglmid sewghgglfg
      301 hggegpgfnt walylpeyqe ralaicifcn tsmagqpiyl vkdllrvlga sfte
//
LOCUS       WP_273580316              68 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Xenorhabdus
            aichiensis].
ACCESSION   WP_273580316
VERSION     WP_273580316.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     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=7814
     Region          4..67
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mptmttskes lirlpevqrr tgyskawiyr likedkfpkq vkigsrsvaf veseidgwvd
       61 qriaesrt
//
LOCUS       WP_273580407             154 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Xenorhabdus aichiensis].
ACCESSION   WP_273580407
VERSION     WP_273580407.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 154)
  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 154)
  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 154)
  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 154)
  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..154
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..154
                     /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=17399
     Region          75..>146
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mtelremtta efelfrllfi nehaldlast rgypadvslk kasqlidvtq sqatekvink
       61 fwcivksdhe rpvigylwie lqeqaawvcd fhllpewrrk glgkaaldkm ksnlmsmgit
      121 evglrvapnn pvakvlyeks gfhitgfnms ktls
//
LOCUS       WP_273580803              90 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Xenorhabdus
            aichiensis].
ACCESSION   WP_273580803
VERSION     WP_273580803.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..90
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10154
     Region          13..79
                     /region_name="HTH_35"
                     /note="Winged helix-turn-helix DNA-binding; pfam13693"
                     /db_xref="CDD:433408"
ORIGIN      
        1 mfylcvcfrl lywppvdiia alrkqgttla aisrkaglss stlantlirp wpkgewiian
       61 qlemppaqiw psryfdstgh lierkprntp
//
LOCUS       WP_273581140             644 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator [Xenorhabdus aichiensis].
ACCESSION   WP_273581140
VERSION     WP_273581140.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     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=73581
     Region          26..640
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mkgipvalfp yprlahlfev ihterlpqae lakrfgvssr tirtditeln nalrhygaqi
       61 lykrgngysl siedhtlfas lpkqkqmiqt iprtasdrvd alllklllat qpvklddiae
      121 awsisrgtlq hdmgvvreiv skyplqltsi prlgtrltgn eriirscltd tllrrfslev
      181 epslsqfrtd iladidltyi etilqnsltr fgirlnnegr qylifncavs ilritrrhel
      241 tqgvvhewdn aiqnvayeis qslicvlgne isdseadyla gqiaaqripq hdnptphtpk
      301 shqwvdeiln dintsynydl rhdsklrsdl tthltvlisr lqqqistknp lltdikqhyp
      361 fayevtvsal triedqlpfv isedelgyla vhigvglerh yggsthvlvv tdsgnatrrm
      421 ieakiarefp qlkiqrvlpl heynaldyve enfvittlrl seknkpivki apfptayqle
      481 qigrlammeq trpyilerff deryfmvike ditqeilfkt lcrklraggy vredfcpsli
      541 ereaivstll genialphsl gllalktvvv tvlapkgiew sketkeranv ifllaiskqd
      601 yeeamaiydl fvtfvrekat krllrsrnfh dfqiiakdsl grsi
//
LOCUS       WP_273581244             404 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Xenorhabdus aichiensis].
ACCESSION   WP_273581244
VERSION     WP_273581244.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     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=46442
     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 mkltdmaikr akpkeksytl adgnglsllv etngskgwry ryqftgktkm islgiypvvt
       61 ltearakrde arkqvangin psearkaekv asisksentf knialewyeg rkdrwsvgyr
      121 ddmmdafekd vfpyigdrpi adikpmelle vlsvmekrgt teklkkvrqr cgevwkyaii
      181 tgraeynpap dlasafvphk rehyahlsvs elpeflssid kymgsqivrv alrililtgv
      241 rpgelrkaew seinfdtgiw eipaekmkmr rphivplseq viellkqihp isgsyqyifp
      301 srtdyrkhis dmalntmirr mgysgratgh gfrhtmstil heqgyntawi etqlahvdkn
      361 sirgtynhaq yldgrremlq wyadymeale rgenvihgkf gkra
//
LOCUS       WP_273581433             332 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase, partial [Xenorhabdus
            aichiensis].
ACCESSION   WP_273581433
VERSION     WP_273581433.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 332)
  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 332)
  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..332
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         <1..332
                     /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..314
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 neetmgwdal ldeyffsrml rpatewsyrk vvrvfirylg etglpesvth rdvlcwrrhl
       61 lmeknqsgyt wnnkvahlra ifnfgmerkl lshpknpfnd aavkkekkqk ktlskaqitg
      121 iylrmqqyee eerlqtaprg grcalyptgy wltvldtfrl tgmrlnqllh lrlrdinldn
      181 syielrvegs knhsewrvpm ipqlkprlaq lveqakacga kendplfdlt rlrfryhgrh
      241 vshqyhhdre kqhlrsffnr lskecgfavs phrfrhtlat elmkapdrnl qlvrcllghr
      301 svattmeyid idmeiagktl anelafyldl av
//
LOCUS       WP_273580909            1357 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Xenorhabdus aichiensis].
ACCESSION   WP_273580909
VERSION     WP_273580909.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus aichiensis
  ORGANISM  Xenorhabdus aichiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 1357)
  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 1357)
  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 1357)
  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 1357)
  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 1357)
  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 11436933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1357
                     /organism="Xenorhabdus aichiensis"
                     /db_xref="taxon:3025874"
     Protein         1..1357
                     /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=152651
     Region          40..>1088
                     /region_name="EntF"
                     /note="seryl-AMP synthase component of non-ribosomal
                     peptide synthetase [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1020"
                     /db_xref="CDD:440643"
     Region          1099..>1205
                     /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 manikhtelk slkldelkrl vrqkkikdns ipketikknt dpdrkyfpvt saqkniwmln
       61 qylddkkvys lplaitcqlk yeidlrlvkq altylaqkhd ilrttfhltg kelcqyvsdd
      121 avfdfryddi tylperdkkr qveamakaeg nrcfdlaggp laylyivktn sheyvfllsf
      181 hhiiadgwtv glflkefiet ylsllsgeit lkveenlqfs dyalaedqwh aegkyqqgle
      241 ywakklgnvq gilniatdrp rpskmntagr imslffdgdf cqrlqtcavq nnatqfhvil
      301 aayeillhky sgqqeiiigi pfanrnqsvt qnimglfmnt lplcfridpe itlstlvqit
      361 akeceqsmvy qdipfnhild kiayvrnpqv npifqailty qifphyqats lfkyqplkid
      421 ygvakldlnl wvekerdgll ftmnystalf ngdtiqrmla dlrtildafi ghpklavrel
      481 sllshterts ilagchptpd ispaavhqqf eqqaclipna iavrcagrtl sykqlnqqan
      541 rlahyllakg lscgervall maksedcvma llavlkaggc yvpvdinlpq qqvdfiltna
      601 svryilvese elitniscin vnqkfngmpe snprleqsmd drpayiiyts gssgkpkgvq
      661 vnhshlshyc qaitpvldqq pgarygmfss fttdlahtml fpalinqgql evihsqhlsn
      721 pqelfdylat spldcmkvtp thlaallgtp easklipknl lvlggekvpv sliqhirefn
      781 ancrivnhyg ptectvgvtt ynvpaeldrl hsdylpigvp lkdshvlvld tsqklvpakl
      841 pgeiyiggah laagyidgte knrdcfiphp ylagerlyrs gdkgrllpdg nieflgridr
      901 qvkvrgyrve ltviedvlrq fpevtnaavi qcqsptgats lvaylcgvge ryqatvqsel
      961 qkklphymqp eqwiwleslp ltsggkinyt alpllrpdtr qctqepkset ehrlhdiyca
     1021 vlecnkvdtq ksffslggns inalqliiev nhqfgsslsl gqlfensnis qlaalleqta
     1081 psmasplvmf nyglpdnkpt llmihpaggn ilcyhplvre mgadypaygl qvanfsqdap
     1141 ynhdikslae fyltqsgsli qrtrlvlggw slgatiafem aqqlvqktgv aptvlvldqp
     1201 apqvnidnsv qmnkderlvr fvrkvelflg tslniscsvl aemsevqrse lflaefkrvh
     1261 lvpdnisnre fqyflvilra hihatdqyqg kiypgkilvv eaeetlpgri kldesglgwq
     1321 plsydrlkii namgnhvsmm qepyithian qlrevlp
//
LOCUS       WP_273581942             345 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Xenorhabdus sp. PR6a].
ACCESSION   WP_273581942
VERSION     WP_273581942.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=36604
     Region          35..344
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mmtlihspkt ktfkmgnavf iapewqvsri vfsmlllivg lfylslamgr egmdnpfllt
       61 etpyqafilt eirlpralva igagitlals gslfqlttrn algspdiigv nggaavgivm
      121 amvvwpdvlp vpvgalsgai iavlliylgs gagignmqan kiiisgiaia alctavvefa
      181 asnirleqaq qlkallrgsl asqnwqnval isgmvlfipv lfwlgrqlny thlghdiant
      241 lgvpvrliqi vsillavtfa tmsvlvvgpv afialsapqi arrlvrnkgs alfctalvga
      301 llmlvsdlmt lllpttarlp vgvitamvgg vylmyllyae lrrtr
//
LOCUS       WP_273581943             336 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Xenorhabdus sp. PR6a].
ACCESSION   WP_273581943
VERSION     WP_273581943.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=35197
     Region          28..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 mmnpkrrtal ilglvfmvvl tcfcmaasls lgskslplsa vwhhywwges gsyydlvint
       61 reprtliglm agaalalaga vtqgllrnpl gdpgllgvna gaaatvvcfs fipvldgipr
      121 fwtafigagl stllfyllsg gsrhtnpvrl vltgaaintc lfalvqgvil lspqvmdsyr
      181 fwsmgslsam slseasllip ylllavilal slgaslnvmv fgegiagslg anvartrivs
      241 llsatmlaaa atamagpiaf vglaaphlmr alvgndfrwl lpycllagsc lllisdivar
      301 lliapeeimv giitasigap llylvaksrs qkmmae
//
LOCUS       WP_273581800             283 aa            linear   BCT 28-DEC-2024
DEFINITION  N5-glutamine methyltransferase family protein [Xenorhabdus sp.
            PR6a].
ACCESSION   WP_273581800
VERSION     WP_273581800.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (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   2  (residues 1 to 283)
  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 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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..283
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..283
                     /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=32088
     Region          10..264
                     /region_name="HemK"
                     /note="Methylase of polypeptide chain release factors
                     [Translation, ribosomal structure and biogenesis];
                     COG2890"
                     /db_xref="CDD:442135"
ORIGIN      
        1 mnfsheyqif idnarkllse agiwdvesdl eclvdryler rnkeqaynef mlavyercnr
       61 iplghivnsi nfdglplvvg sgvfvprths qlihkwinke snipsgstvl dlcsgcgaig
      121 lsiakrrpdl nvvcveydtv afqylvrnin rlsslsikaq afqtdlrdlq sldkfkesvs
      181 livanppyvp ekysilpewe khhpyvsvys gddgldlirl iiiqskqslk angwlviehq
      241 enqqdvirnl flkegfsqvr tiidnnfsdt tglsvitigi nnf
//
LOCUS       WP_273581945             612 aa            linear   BCT 28-DEC-2024
DEFINITION  IucA/IucC family protein [Xenorhabdus sp. PR6a].
ACCESSION   WP_273581945
VERSION     WP_273581945.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 612)
  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..612
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..612
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70945
     Region          15..593
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mrslntcwgy qtshltkenw lhanrhlvak ilrelchekl itpvhygegq dysveidnfq
       61 yhfqaqayql dhldidaasi skvshgqlqp ldaieliiel hplldisekl lpiyldeiss
      121 tlyghafkyq knrltaqdlt qadyqtvets mneghpvfia nngrigfdad dyldyapesa
      181 hpvtliwiav hrnktvfsal sslsysklva eeldkylpaq ferqmqslgl klsdyylmpl
      241 hpwqwkhria isfaadiakq eivylgeghd rylaqqsirt ffnvsqpkkn yvktalsvln
      301 mgfmrgldph smvttpqine wlgnlveadt ffqekgftil reraamgyfn hyfesaikkd
      361 nphkkmlsal wrespmtilk enqrlmtmas llhidreggs vvaalvqdss lsvedwvsry
      421 ldaylspllr sfftydlvfm phgenlmlvl ennvpvkmlm kdigeeiail ngdlelpeei
      481 sflhvtikde mkinyifldi fdcffrylip llqkhlalpe arfwelvahc vhcyqsqhlh
      541 qiekfrkfdl fkhdfvrtcl nrlqmannqq midlddrekn lkfagtlvnp lhalrekysv
      601 vfeagvmmei sr
//
LOCUS       WP_273582156             449 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Xenorhabdus sp. PR6a].
ACCESSION   WP_273582156
VERSION     WP_273582156.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 449)
  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..449
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..449
                     /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=49342
     Region          1..442
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkvtvfgigy vglvqatvfa evghdvlcvd vdankvenlk ngqipifepg ltplvkknha
       61 egrlnfttda kagiahgklq fiavgtppde dgsadlkyvt avartiaenm dghkvvvdks
      121 tvpvgtadkv ravmqatlae rnialpfdvv snpeflkega avadcmrper iiigcdndnd
      181 nvvdvmrely epfnrnhdrm ivmdirsael tkyaancmla tkisfmneia nlaemlgadi
      241 envrqgigsd srigyhfiyp gcgyggscfp kdvqalirts eqigytpkil qaveqvnnkq
      301 ksklptfvkq hfgddlmgkt faiwglsfkp ntddmreass rvlmetlwkc gakvqaydpe
      361 amqeaqriyg qrddlslmgt keaalkdada liictewqnf rapdfdvvkg slktpvifdg
      421 rnlydperlq argftyygig rgasikpvi
//
LOCUS       WP_273582226             350 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Xenorhabdus sp. PR6a].
ACCESSION   WP_273582226
VERSION     WP_273582226.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..350
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..350
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40314
     Region          91..324
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mvkiarrkyk iqqetirhlf mkkkyrwlkf iplifgflls acdgnnysfk lreddyagah
       61 nkfkthivdd sfvgdgqpam ppkeifslvy ypaedgnmaa fistsptdkt kkypaiiwlt
      121 ggyggigndd ffwsdrpann dqsasafrrd glvlmipsfr genanpgrye mfygelrdie
      181 sarqylaklp yvdsnriyla ghstggtral laseytkgfr aifslggipd lrlrlnyapi
      241 pvavpfdqnd prefelrspr tflksikspt fyfegeyayw eefdevkeit snkgiplyiy
      301 riengdhfni irpltnliae kilndreekv niefnendfl klqynlplpn
//
LOCUS       WP_273582300             107 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Xenorhabdus sp. PR6a].
ACCESSION   WP_273582300
VERSION     WP_273582300.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=12006
     Region          12..90
                     /region_name="sulf_sens_BigR"
                     /note="sulfite-sensing transcriptional repressor BigR;
                     NF040642"
                     /db_xref="CDD:468610"
ORIGIN      
        1 mimkanrpvq qamreaaega advlqalsnd drlllmcqls qgeasvgqle eavgvhqptl
       61 sqqlgvmrrl nlvqtrregk qifyrieder iltllhtlyt lycpkpe
//
LOCUS       WP_273582621             600 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Xenorhabdus sp. PR6a].
ACCESSION   WP_273582621
VERSION     WP_273582621.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 600)
  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 600)
  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..600
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..600
                     /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=68648
     Region          2..600
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mttdslhayh lvnrfqqqfh ehpekiafrq wspseqlemn wrqvgcttqs vakallslgv
       61 evqgkvgifa qncmtwslad lailqlravt vplyatntrd qaafilndae aqvlfvggqe
      121 qydialalie lcpklahliv mdesvdlrgc pqaeylsafi nndysqyqae fdnriagqdl
      181 ndlftliyts gttgepkgvm ldyrniasql ylhdqrltlt nhdvslcflp lshiferaws
      241 yyvmhtgaln vyltdtnlvr eamsdvrptv mcsvprfyek vhsailekvs rapfwrrmif
      301 hwalkqgesr wlrqqknkkg cpftrgsdql adklvlnklr hllggrvrfl pvagarldda
      361 itrfflsigl nikygygmte tcatvscwee knyllgsigt plpgvdvris aegeiqvrgp
      421 ivmkgyfnrp eetvhafted gwlrtgdagg ldddgnlfit erlkdlmkts tgkyiapqmi
      481 egmlgqdrfi ehvaviadar qfvsalivps yealeeyaks inlhyfdrle llrhhqiidl
      541 ferrlkemqk nivnfhqvkr fillpeafsm ekgeltptlk lrrkvisqhy qreiesmyrd
//
LOCUS       WP_273582710             288 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Xenorhabdus sp. PR6a].
ACCESSION   WP_273582710
VERSION     WP_273582710.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 288)
  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..288
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..288
                     /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=33421
     Region          2..247
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mllaisdlhv shatnrtive sfrpatpddw lllagdiaeq esdftwvist lfqrfaqvvw
       61 tpgnhelwct pkdqlklpgv pryehlvnic rqhnvltped efrhyrrgng ttvtiapift
      121 lydysfrnea dytaeqaier arrcgvissd efflktyphr nivdwcreri hytekrlnai
      181 pegedivlis hfplirkple slrnrefsiw cgsekthqwa sktgvrlvvy ghlhlpdldy
      241 ihdvahlevs lgyprewqah grksylvpld gllehtneyh pssmliig
//
LOCUS       WP_273582754             362 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Xenorhabdus sp.
            PR6a].
ACCESSION   WP_273582754
VERSION     WP_273582754.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=40131
     Region          12..358
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mqftdlaaqq lrikykidqn iqkvlthgky ilgpevsele eklveytgak ycitcangtd
       61 alqialmaig ikpgdevitp gftyiataet vallggipvy vdvkpttynl dpaqleaait
      121 pktkaiipvs lygqcadfde inaiaekyni tviedaaqsf gasykgkrsc nlttiactsf
      181 fpskplgcyg dggaiftsde elakiirqia rhgqdrryhh irvgvnsrld tlqaaillpk
      241 leifdeemal rqivaknydk alneigimtt pyiephnisa yaqytirvqn rdelqnklke
      301 kgiptavhyp lplnkqpavs csiilpvgdr isnevislpm hpylrledeq kiteeikksh
      361 ye
//
LOCUS       WP_273582795              80 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Xenorhabdus sp. PR6a].
ACCESSION   WP_273582795
VERSION     WP_273582795.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=9343
     Region          22..75
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mtkqknprmk ntspypeign arkrhtadfl gisdstlhrw ikdkkipqpf eledgffvfd
       61 aaeirqwven kksrresivi
//
LOCUS       WP_273582815             466 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Xenorhabdus sp. PR6a].
ACCESSION   WP_273582815
VERSION     WP_273582815.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..466
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..466
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50577
     Region          1..457
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mstqqkrhrf wkvertgidi vpasertgtp ldlfwvwsaa nigilgivyg aiivsfklsf
       61 lqsvlaalvg lssfalvgyi sfsgklgrtt tltlsrtifg ikgniaptvi fwfismgwes
      121 inivtgtltl salfqacgls esplltvvsm alfaglsigv tllgkemvit mqrwvtkifg
      181 vmtlvvvfyi lfttewqvvl tmpsgswltg flpavsvvaa gsgiawaatg adysryqhen
      241 aakakiftai taggmiplvl llftgillsv qlpdlpnsen piahigsilp dwmvipylmt
      301 aiagivtmav mslysaslnl ltlgikikrv havtidstiv lsvavytlfv tgdfmgpfva
      361 fliffgvfla sweavflldy ivlrrnqgyc pdklfnyvgp nggikwlpil cwllgalagf
      421 svtqndfisg pwavgifans slglflaffv sfvcyglylm lnrykk
//
LOCUS       WP_273583380             433 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Xenorhabdus sp. PR6a].
ACCESSION   WP_273583380
VERSION     WP_273583380.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..433
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..433
                     /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=47938
     Region          29..396
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mnnnldslty yavtkkydlr fpmltedldv dvviigggfs gintalelae kgitniavle
       61 grtlgyggtg rnggqvmtgi ghdldkikrh vgpkgletif kisslgagii rdriakydiq
      121 adfcqgyayl gmnsrhdktl rswlpefraa spdeeielyt gaevkkvigs drytsalkhm
      181 ggghvhslnl llgeakaate ygvkifensq vvdveygprv tvrtatgsvr askmlwacng
      241 fldgleptiy rrtintyafq lmteelsddl ierispirga ygdispvidy yrvtkenrll
      301 yggathfiey ipsdlkawnr nlmlktfpyl kevkielawg gplccsanlf pqigslpnhk
      361 nvfyvqgysg fgvtpshiic kilaegmseg serysllssi phaniigkdr lrnvllsagk
      421 iwhqtsgywk grr
//
LOCUS       WP_273583401             381 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Xenorhabdus sp. PR6a].
ACCESSION   WP_273583401
VERSION     WP_273583401.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=41652
     Region          3..381
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mikniatvli hggkqqdken haifppitta stfvqknlse qgefcysrcs nptrhayetl
       61 laeieggtya tatasgvaaa alvlnllpke shiiamkgvy ggtfrlferv aiennghqfd
      121 yvdlnnltev eakvkentrl iwiesptnpl lelvdikric afaknnnilt cidntfataw
      181 nqkplelgad ivmlstskyi gghsdligga vithrsdlan rldflkttlg aiaspfdayl
      241 alrglktlal rmsaqcanal eiakflqshg kieqvyypgl pthphyaicq aqmraggavv
      301 tiklkgdled tkkflsklry fvlaeslggv esmvnhsatm shgsmtkeer eaigiydtvl
      361 rlsvgiedir dlladleqal e
//
LOCUS       WP_273583448              87 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Xenorhabdus sp. PR6a].
ACCESSION   WP_273583448
VERSION     WP_273583448.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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   Wintjens,R. and Rooman,M.
  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 87)
  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..87
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..87
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9706
     Region          7..76
                     /region_name="HTH_35"
                     /note="Winged helix-turn-helix DNA-binding; pfam13693"
                     /db_xref="CDD:433408"
ORIGIN      
        1 mthtqkdwhp adiiaalrkr gttlaalsre sglssstlan tlsrpwpkge vliatrlgvd
       61 pseiwpsryf dhngqlikrl mrkrise
//
LOCUS       WP_273583668             217 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Xenorhabdus sp. PR6a].
ACCESSION   WP_273583668
VERSION     WP_273583668.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..217
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23642
     Region          6..208
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mnrchvifdi dgvivdseql hfdvlldvlg elgeqapaki sdiqpqqlig lslaetldev
       61 glppsmqqei tekiiaryqe klsahylrpg itgliaalqq nginfgfvst aprdvclanl
      121 glldlhappa lisgddvert kpfpdpylam lklkemdvqq tlviedtdlg iaaakqagip
      181 wvyawphals vaeqygqasr iierltdipq fsginiv
//
LOCUS       WP_273583667             353 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Xenorhabdus sp. PR6a].
ACCESSION   WP_273583667
VERSION     WP_273583667.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 353)
  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 353)
  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 353)
  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 353)
  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 353)
  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..353
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..353
                     /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=38450
     Region          1..323
                     /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 mlalkyhqtw dveiqqvetl sciepddvvv diavcgicgt dvgiitgayp vavpgttlgh
       61 ettgvvsqvg sgmtqfqvgd rvvvnptyfc ghcrmcqtgs pnhcerklgt eagvsydgaf
      121 agqylakenl lirlddhvsm eeasltepls ctltgvdklg ithtniraav agagpmgmly
      181 iwalyergvk afmveknenr iqfarnnlpp ecplysdfde aliqeygnps aridlcvdtt
      241 gqlteyifdh lapggkllnv alkdkhanld imkiadksls vigsidslnn sferayamir
      301 dgvipvkrfi sqifdfkdyq qafltvgcdi asktqvpltt pnckvliris dlk
//
LOCUS       WP_273583827             203 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Xenorhabdus sp. PR6a].
ACCESSION   WP_273583827
VERSION     WP_273583827.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 203)
  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 203)
  AUTHORS   Rosinski,J.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..203
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..203
                     /product="helix-turn-helix domain-containing protein"
                     /calculated_mol_wt=22449
     Region          1..67
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <129..199
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mtladrlkea madkgvtqsa laekagmaqs miwkllsgka aktgklvdla kalgvrpewl
       61 sdgsgnkyqt dnadfavrhd nryvpvkiye geqgthesfm vpvlselqah fdtcrayrit
      121 qntgcaeape gtlivvdkde emanddlvya rignhysvyr ykqggsvgfl svddtripli
      181 tvspdieivg vivylfrdmk rrr
//
LOCUS       WP_273583859             361 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Xenorhabdus sp. PR6a].
ACCESSION   WP_273583859
VERSION     WP_273583859.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=38774
     Region          51..358
                     /region_name="FepD"
                     /note="ABC-type Fe3+-siderophore transport system,
                     permease component [Inorganic ion transport and
                     metabolism]; COG0609"
                     /db_xref="CDD:440374"
ORIGIN      
        1 msvttepmpm vkqqlnecdi kahyrhilrr riawilfivl aistsivldf tlgpsglslq
       61 alwqtlvspe svnaatrviv wdirlpyalm avviglslgl agaemqtiln nplaspftlg
      121 vsnaasfgaa laivagigip gipdqwfisa naflfallaa lmldgitrwt kvstsgvvlf
      181 giamvftfes lismmqfiat edtlqglvfw tmgslgratw eklgimllvf svimpvsmsn
      241 awkltalrlg edraisfgin isrlrlgtll risiltalav afvgpiafig lisphiarmm
      301 fgedhrfflp asaligalvl smasiasknl ipgviipvgi vtslvgvpff lsivlrhrgn
      361 v
//
LOCUS       WP_273584144              87 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Xenorhabdus sp. PR6a].
ACCESSION   WP_273584144
VERSION     WP_273584144.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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   Wintjens,R. and Rooman,M.
  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 87)
  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..87
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..87
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9778
     Region          7..76
                     /region_name="HTH_35"
                     /note="Winged helix-turn-helix DNA-binding; pfam13693"
                     /db_xref="CDD:433408"
ORIGIN      
        1 mnnvrndwhq adiiaalrkr gttlaavsre aglssstlan vlsrpwpkge wivanylevh
       61 pseiwpsryf dmygqlierv arkasik
//
LOCUS       WP_273584148             385 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Xenorhabdus sp. PR6a].
ACCESSION   WP_273584148
VERSION     WP_273584148.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=44099
     Region          57..365
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msifrrgntw ygnyttpsgk rikeslgttd kkqaqelhdr rkaelwrier lgdfpdvtfd
       61 eaclrwieek ankksldddk grmgfwleyf ggvrlkdite asiytavskm knrkakerwe
      121 iqvkaaqkkg keipaykevp vsiatkakhl alikallraa erdwkwleka pvikvpavre
      181 krvrwlephe aqrlvdecpe plqsvvkfal atglrrsnii nlewsqidtq rqvawihpdq
      241 sksaraigva lnetacrvlr aqignhnkwv fvhtkpstnp dgkilpqvrk mrvddntawn
      301 salkragien frfhdlrhtw aswlvqngvp lsilqemggw esiemvrrya hlapnhlteh
      361 arqidalfgg cvpnpsqsgk iaiak
//
LOCUS       WP_273583590             461 aa            linear   BCT 28-DEC-2024
DEFINITION  SLC13 family permease [Xenorhabdus sp. PR6a].
ACCESSION   WP_273583590
VERSION     WP_273583590.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 461)
  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 461)
  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 461)
  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..461
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..461
                     /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=48939
     Region          100..460
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mdasesltpa igstpsnkrg liilaldiil lvvllkflpy gekanaglal mafvgvlwlt
       61 eaihvtital cipilavgmg llntgdalks fanpiiflff ggfalatalh iqgldrlian
      121 rllmlargrl svaillifgv tallsmwisn tataammlpl vlgilanldv rserntfvfv
      181 llgvaysasi gglgtlvgsp pnaiaaaqlg mdfftwmkyg vpmvivlmpv mvgmmylmlr
      241 pnlnhkfdle leylewngkr mitmgifllt vvcwifssfi sdalggvkdl dtiiavsaai
      301 ligitgvstw sqiqnntewg vlmlfggglt lsavlknsga sevmangmaa tfgtspwfvi
      361 iiaiaafiif lteftsntas aallvpifat vaealgmpvm vltmiigiga scafmlpvat
      421 ppnaivygtg yikqsemvrv givlnvvcia iisaiawffw l
//
LOCUS       WP_273584427             404 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Xenorhabdus sp. PR6a].
ACCESSION   WP_273584427
VERSION     WP_273584427.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=45850
     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 mkltarqidt akpkdksykl sdgggmylei fpngskcwrl kyrfagkekr lafgtypivt
       61 laearnkred akkilanddd pglvkrqekr ekalivsnsf ekialewhay kvpnwskgya
      121 edllegftkd ifpfigklai tdikpldmlt vlrkmeqrgv ldklkkirqa cnqvfryaiv
      181 tgraeynpaa elagalatpk akhfphlnvd elpaflqals lysgskitqi atklllltgl
      241 rtielrastw aeinfdkaiw eipqermkmr rphivplseq amallrelea itgrfnfafh
      301 grndaskpms eaainqvlkr igyagratgh gfrhtmstil heqgyntawi etqlahvdkn
      361 sirgtynhaq yldgrremlq wyadymdale qggnvahgkf kkha
//
LOCUS       WP_273584364             271 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Xenorhabdus sp. PR6a].
ACCESSION   WP_273584364
VERSION     WP_273584364.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  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 271)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 271)
  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..271
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..271
                     /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=31311
     Region          16..268
                     /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 mkrttglnqn nicttqlsmp dfniiehkqr glyilldgem vwkdcinsyh iksheilfth
       61 pgsytaktht escqllwlpl hmdflrsflk rfgpllskie rqefpayrli pfrqfpllte
      121 sirglanlla hdsppalvql rveellllls lgqqgallms ilrklsnrqv erlqtfmeah
      181 ylkewklndf arefgmglts fkelfnsvyg tspkawiseq rilyahqlll nsemsiadis
      241 lesgfssqsy ftqsyrrrfg gtpnraracy a
//
LOCUS       WP_273584459             128 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Xenorhabdus sp. PR6a].
ACCESSION   WP_273584459
VERSION     WP_273584459.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
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="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     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=14712
     Region          2..127
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mfskeylvde khldfqgvvd glyypfylew arhafmkeal gldlenefea grmhiileys
       61 lrfrkslqkg nkmevtckva knekrsrinf eqqilvngiv yadatfvatc lvngrpmvpd
      121 ivmnaiad
//
LOCUS       WP_273584857             188 aa            linear   BCT 28-DEC-2024
DEFINITION  coiled-coil domain-containing protein, partial [Clostridioides
            difficile].
ACCESSION   WP_273584857
VERSION     WP_273584857.1
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 both ends.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>188
                     /product="coiled-coil domain-containing protein"
     Region          1..>141
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
ORIGIN      
        1 eksklqrgid leekievlnn sikelkkeid idnkekedle kliinlqnqv dskykkiqdn
       61 nknveslsis tdlkenifet ynkeeelkkl svekeeknkl lkevskriee lkfknidvek
      121 nktsvneklk klldhqetln rscpgdnkiv ssekeylhnl ksrlentkdy ekqinsikdd
      181 lnkneksk
//
LOCUS       WP_273584929             128 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_273584929
VERSION     WP_273584929.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 128)
  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 128)
  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..128
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..128
                     /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          <7..128
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 vaernmvtlh legssvklia vrammldliy nlcengikyn rqggsvtisi yeedqhpvik
       61 vsdtgigips kyqeriferf yridkshskq tggtglglsi vkhvveyqgg yievhstpee
      121 gtaitihl
//
LOCUS       WP_273584944             256 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase, partial [Clostridioides difficile].
ACCESSION   WP_273584944
VERSION     WP_273584944.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
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   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 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   4  (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   5  (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   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 11428264
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..256
                     /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..227
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mefyanishe lktplnniys svqlvenlyk kgkiidfqdi lkehikitkq nmfrllrlid
       61 niinisqvks diykikavnf diiditeriv tsissyaksk gidlifdtde etvmvgldpe
      121 sieriilnil snsikftleg geilvgiykk detveiiikd tgvgiekekl ndifnrfkqi
      181 ensgisnefg sgiglcltks lieiqngkiy idskvgegtn vkiifpikev veevydnsny
      241 ndniekfeie ffdiyk
//
LOCUS       WP_273585344             943 aa            linear   BCT 28-DEC-2024
DEFINITION  cation-translocating P-type ATPase [Columbia Basin potato purple
            top phytoplasma].
ACCESSION   WP_273585344
VERSION     WP_273585344.1
KEYWORDS    RefSeq.
SOURCE      Columbia Basin potato purple top phytoplasma
  ORGANISM  Columbia Basin potato purple top phytoplasma
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Candidatus Phytoplasma; 16SrVI (Clover
            proliferation group).
REFERENCE   1  (residues 1 to 943)
  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 943)
  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 943)
  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 943)
  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..943
                     /organism="Columbia Basin potato purple top phytoplasma"
                     /db_xref="taxon:307134"
     Protein         1..943
                     /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=105373
     Region          9..917
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mnnnnalqdi lkissltsee vlkyfgtspk glnieevkkr hlihglnvmk snknlnvikq
       61 fikqftsmfa illlisgfla fsinetavgi aivtvvivng ffsffqerka skilsslgdm
      121 isnkiqvyrg geakfidtte ltigdvifld mgtnipadar lietnnfyvd nsmltgetih
      181 lnrtcdpnid nikviseipn lvyagttvvq gsakaviysi anntqigevs nlvqnidkgl
      241 stlekeihkv iiiisiiass lalfvflicl wrfgtssdss tssfhifkas itvalgmlva
      301 nipegllpti nlslaigsqr makqkalikk lfsvetlnst tvictdktgt ltenkitcnk
      361 ilfpggfvdi tgnglnkege fknfdkqknd kilikifias ilcseanlid dsvnkkdfqi
      421 igsptegsfl iaakkygldi qnirnnfive kmipfssetk kmsvlvknls qenydlnery
      481 vfikgapsil lkdckfqykn kqvveftqqe keffikrnee lssqgyrlla itykklepnq
      541 eiyeekdivf lgfivnydpp kvevrdaidk lykaglkvtv itgdygptav aigkqvgiik
      601 deqylningl qmdklsqdel qnilkipkpi lfsrttpkhk lriiqayrsn gevvgvigdg
      661 vndilamkaa higiamgksg kdvarntadm illddnfsti pkalleargi ydnikkfity
      721 vfssnipqif pvifmamfgi plyltvmqil aidlitdlip aialgaeeaq sslldkkpit
      781 kndrlldkkl lkrgygflgl iegtlaliff lcyfhyssgq niisfaqnck ftnlidsehf
      841 klastmafga vifaqignvf acrsdkfyfw qtsktknill yfgilcelil fifisqipvl
      901 nkffgtviip fqnyivlssc ifiilffdfi ykfinnkkkl qkn
//
LOCUS       WP_273585359             442 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional folylpolyglutamate synthase/dihydrofolate synthase
            [Columbia Basin potato purple top phytoplasma].
ACCESSION   WP_273585359
VERSION     WP_273585359.1
KEYWORDS    RefSeq.
SOURCE      Columbia Basin potato purple top phytoplasma
  ORGANISM  Columbia Basin potato purple top phytoplasma
            Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales;
            Acholeplasmataceae; Candidatus Phytoplasma; 16SrVI (Clover
            proliferation 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 11416298
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Columbia Basin potato purple top phytoplasma"
                     /db_xref="taxon:307134"
     Protein         1..442
                     /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=51496
     Region          1..437
                     /region_name="FolC"
                     /note="Folylpolyglutamate synthase/Dihydropteroate
                     synthase [Coenzyme transport and metabolism]; COG0285"
                     /db_xref="CDD:440054"
ORIGIN      
        1 mknkknalfw lhnqaknqdk idstffnlye ikallkllnn pekkikvihv agtngkgstv
       61 yylngllqtk fkkvgifvsp hieifneriq insqfisddd lvkiinkirp lisylkqnnl
      121 aggnityfei ltviafeyfy ykktdicvie vglggeldst nvvepiltai ttigrdherf
      181 lghnlkqial kkagiikyki pivtgnisni plsvicakak ekkaihykfk kdfsifyygl
      241 ykwheyfdfr nknfkikklk tpligyyqpe nasmaiqifi lvcelqkinf trfniiqglq
      301 nihlrarmek lqdeplifld gahnvhsikk lvqtmnknfi nykidvlfta lkdknilnml
      361 kqltllektn iylsefehlk slrlnpkynk vnihkifnif cwqnkvkefi iqnspnklll
      421 ivgslyfasq vrhflmnfnk ne
//
LOCUS       WP_273585626             347 aa            linear   BCT 28-DEC-2024
DEFINITION  phage antirepressor [Clostridioides difficile].
ACCESSION   WP_273585626
VERSION     WP_273585626.1
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 11466501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..347
                     /product="phage antirepressor"
                     /calculated_mol_wt=39848
     Region          10..116
                     /region_name="COG3617"
                     /note="Prophage antirepressor [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:442835"
     Region          158..263
                     /region_name="ANT"
                     /note="Phage antirepressor protein KilAC domain;
                     pfam03374"
                     /db_xref="CDD:460903"
ORIGIN      
        1 mdiinkenvk riisfnnelf geirtveidg kmyfvatdia kalgyakpnn aierhcrytl
       61 kqgiphpqsk tktlevniip egdvyrlitn selasaekfe rwvfdevlps irehgaymtn
      121 ealekaindp dwtiklltel kkeratkekl kveqeknkpk lelanaiess sssiliaqls
      181 kilnqngvdi gqnrlfewmr nneylirkkr adhntptqks mdlkvlevse stgvdkdgnt
      241 ivrytpivtg kgqiyflnki lkensqvlkr fminndyikg vmveigktya iydheyygfi
      301 gilksvrnek irveeisdvs ssrdipicmi dyieeasked inkylsk
//
LOCUS       WP_273585725             262 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Klebsiella pneumoniae].
ACCESSION   WP_273585725
VERSION     WP_273585725.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
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="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     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=28011
     Region          1..231
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mtqpshtafi tgassgigai yaerlaargy nlilaarred rlqaladqlq aryaiqasil
       61 kadlseehgi aaveqrlqqd pvidlfinna gtaklagfla stprehqaih tlnttallrl
      121 syaalaaftp rrrgtlinia silalhtlpg savysaskaw vlsftrglqe efadsgvriq
      181 avlpaatatd lwptsgvald alpsgtvmtt edlvdaalrg lemgeqvtlp pvhdlglwet
      241 feqsrlalft sartgqpapr yr
//
LOCUS       WP_273585853             276 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Mycobacterium
            tuberculosis].
ACCESSION   WP_273585853
VERSION     WP_273585853.1
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 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="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     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=29058
     Region          3..265
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mssfegkvav itgagsgigr alalnlsekr aklalsdvdt dglaktvrla qalgaqvksd
       61 rldvaereav lahadavvah fgtvhqvynn agiayngnvd ksefkdieri idvdfwgavn
      121 gtkaflphvi asgdghivni sslfgliavp gqsaynaakf avrgftealr qemlvarhpv
      181 kvtcvhpggi ktavarnatv adgedqqtfa effdrrlalh spemaaktiv ngvakgqarv
      241 vvgleakavd vlarimgssy qrlvaagvak ffpwak
//
LOCUS       WP_273585957             372 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Mycobacterium tuberculosis].
ACCESSION   WP_273585957
VERSION     WP_273585957.1
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 372)
  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 372)
  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 372)
  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..372
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..372
                     /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=38588
     Region          8..372
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mthsqrrdkl kaqiaasgld amlisdlinv rylsgfsgsn gallvfader davlatdgry
       61 rtqaasqapd levaieravg rylagragea gvgklgfesh vvtvdgldal agalegknte
      121 lvrasgtves lrevkdagel allrlaceaa daaltdlvar gglrpgrter qvsrelealm
      181 ldhgadavsf etivaagans aiphhrptda vlqvgdfvki dfgalvagyh sdmtrtfvlg
      241 kaadwqleiy qlvagaqqag rqallpgael rgvdaaarql iadagygehf ghglghgvgl
      301 qiheapgigv tsagtllags vvtvepgvyl pgrggvried tlvvaggtpk mpetagqtpe
      361 lltrfpkela il
//
LOCUS       WP_273585975             158 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Mycobacterium
            tuberculosis].
ACCESSION   WP_273585975
VERSION     WP_273585975.1
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 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   2  (residues 1 to 158)
  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 158)
  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..158
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..158
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=17597
     Region          21..108
                     /region_name="HxlR"
                     /note="HxlR-like helix-turn-helix; pfam01638"
                     /db_xref="CDD:460276"
ORIGIN      
        1 mavsdlshrf egesvgrale lvgerwtlli lreaffgvrr fgqlarnlgi prptlssrlr
       61 mlvevglfdr vpyssdperh eyrlteagrd lfaaivvlmq lgdeylprpe gppiklrhht
      121 cgehadprli cthcgeeita rnvtpepgpg fkaklass
//
LOCUS       WP_273586020             216 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Mycobacterium tuberculosis].
ACCESSION   WP_273586020
VERSION     WP_273586020.1
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=23140
     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 wgaptggvep wagdlpddpr ydpvllrdgd arnvvdayry wtreaiiadi
       61 dtrrhplhva ienfghdani gsvvrtanaf avhtvhivgr rrwnrrgamv tdryqrlchh
      121 dsttgllefa agagltvvav dnvpgaarle qtalprecll lfgqegpgit ddaragaavt
      181 vsiaqfgstr sinagvaagi amhawirqha dlgraw
//
LOCUS       WP_273583457             461 aa            linear   BCT 28-DEC-2024
DEFINITION  nucleobase:cation symporter-2 family protein [Xenorhabdus sp.
            PR6a].
ACCESSION   WP_273583457
VERSION     WP_273583457.1
KEYWORDS    RefSeq.
SOURCE      Xenorhabdus sp. PR6a
  ORGANISM  Xenorhabdus sp. PR6a
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Xenorhabdus.
REFERENCE   1  (residues 1 to 461)
  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 461)
  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..461
                     /organism="Xenorhabdus sp. PR6a"
                     /db_xref="taxon:3025877"
     Protein         1..461
                     /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=48540
     Region          28..456
                     /region_name="ncs2"
                     /note="uracil-xanthine permease; TIGR00801"
                     /db_xref="CDD:273276"
ORIGIN      
        1 mvnlpresns sevphksnne liyhledkpp lphalfaagq hllamfvavi tpamlicqal
       61 glpaqdtqri ismslfasgl asliqmrswg pvgsgllsiq gtsfnfvapl imgglalkng
      121 gadiptmmsa lfgtlmiasm tevllsrvlh laskiitplv sgivvmiigl sliqvgltsi
      181 gggyaamqng tfgapdnlll agvvlavivl lnrqknpylr vaslviamtv gylvawykdm
      241 lpvatpqadt piitvpsply yglsfdwnll iplilifmvt sletigdita tsdvseqpvs
      301 gplymkrikg gvlanglnsv vsavfntfpn scfgqnngvi qltgvasrhv gyliasmlvl
      361 lglfpavagf vqhipepilg gativmfgti aasgvrivsr eplnrrsmmi ialslavglg
      421 vsqqplilqf apdwvknlls sgiaagglta illnlifpqe k
//
LOCUS       WP_273586131             246 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273586131
VERSION     WP_273586131.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 246)
  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..246
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..246
                     /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=26580
     Region          1..>68
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mnindetlsa fldselsehe meqvrkalet ddelvmrlae lsevdmrvke hatsiddapl
       61 sdslaktvak ldtattkntl nsnvvtltpw qrvkhsanks laiaasvavv fgiamtsylq
      121 pnesqnlvas niasaldtql ssgeykqsdg svfsaqlsfk nlqgelcrqy alssnntmqt
      181 siacktqsgw qikaqtaaqq sdngaqyqta snnseldavi dsmisgapld raqeqqaisa
      241 kwqlnq
//
LOCUS       WP_273586170             328 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273586170
VERSION     WP_273586170.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 328)
  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 328)
  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..328
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..328
                     /product="vWA domain-containing protein"
                     /calculated_mol_wt=36084
     Region          85..274
                     /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(94,96,98,171,199)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238744"
ORIGIN      
        1 mfefswpwlf lllplpllll llkpaagnah trlripsfak hnlasqslek sarkltifew
       61 llwlllvtaa anptwlddpi slpnegrdim lavdlsgsmt eqdmayngqy vdrltmvkav
      121 lsdfieqrqg drlglilfgd taflqtpltr dvktvskmls esqiglvgra taigdalgls
      181 vkrfankdks nrivvlltdg qntagnlkpe dalllareeg ikvytigvgs dnprgfslfn
      241 mggmsggsld esllkdiaeq tgglyfrakd vaglqqiyae ldklepisad eqtfrpqssl
      301 fyyplliail lislkvmlst lralkepn
//
LOCUS       WP_273586118             595 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 2OG-Fe(II) oxygenase family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273586118
VERSION     WP_273586118.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   van Staalduinen,L.M. and Jia,Z.
  TITLE     Post-translational hydroxylation by 2OG/Fe(II)-dependent oxygenases
            as a novel regulatory mechanism in bacteria
  JOURNAL   Front Microbiol 5, 798 (2015)
   PUBMED   25642226
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18643154
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..595
                     /product="2OG-Fe(II) oxygenase family protein"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=68014
     Region          1..250
                     /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          30..60
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          65..89
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..401
                     /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(169..170,173..174,176,200,203..204,207..208,
                     210..211,234,237..238,241..242,245)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          169..193
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          198..228
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          233..261
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          300..330
                     /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          369..401
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          493..590
                     /region_name="2OG-FeII_Oxy"
                     /note="2OG-Fe(II) oxygenase superfamily; cl21496"
                     /db_xref="CDD:473886"
ORIGIN      
        1 mqkfkaalta yntknfqksl diidefklsh ldahllkaas ltaldkndka ieiyqcalkn
       61 nptnisllen ytgllcklgd fmgclnllnt tvttvsakls lnklealikl nhlleakrlv
      121 klistptnle frfiwlkiel healgeldii eniinmlpea qqnnfyisyk racnlrsmgr
      181 fnealgllin iekkesttpe ilfligciyk dlnntqqcer ylnkclaiap yyvpahesln
      241 rlyhstknkk lflnsyelvk qkyephpvie hsfisqliks nnygsaldvs tnalklfpnd
      301 haivhahsvv lgklndheka fnllnqlvkk vpqesryrid lahylilngd yieairqles
      361 alkydyfnqe vwaylstawr lsandkyywl tnydqyvkvf elqkpkgyst sgqflenltd
      421 lllnlhahst qlidqsvrsg tqteghllfr snklisdfkh smnncitsyl anlpkdqkhp
      481 lcsrnnnafk vngswsvklg nkgfhanhih pagwlsapsy islpkelnen dtnksgwlkl
      541 getclnlker eeiarsicpk tgqmiifpsy iwhgtyplks tqprltvpcd vmpil
//
LOCUS       WP_273586210             764 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273586210
VERSION     WP_273586210.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 764)
  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 764)
  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 764)
  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 764)
  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..764
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..764
                     /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=85179
     Region          8..709
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mahfklkalv talslcnlav haaqeehttd vkvseelvvy geigyrnrsq elaptleysq
       61 eyfqrfeplt agdalkrvps vtflsdvles dgarmrglsp aytkvlinge evpgagadrs
      121 ffvdripael ierveiirss sanrsadaia gtlnivlrdg ysldggyira gglryddgel
      181 kesfagvygt efaggrlllg anfqgrynpk qkssirygds pennpnyatd dfdnredqsd
      241 trdgddtsln asfekvfdng gkfdisamwv dtdrteders feyddatats nsvveggnll
      301 sdnanvsyid qtnyninsgy elpllggtsk fkvgyasfee svyeqeveld tselpmvfee
      361 aeetveiddk ewslqwqhsl lvgdskevqf gafvqgkerd taifeaeden eqtltgwdqf
      421 sqtpmslaqf nnefeavdgg vntleedrfd lfalikhead lfswemgvrw estdsnitdt
      481 negvtakndy dfflpsahfr ysvsdngrvs asvarslrrp dfdyitpall eeeladndfl
      541 gnpnlkpess wgidlgyeyr lgksgvvgvn vfyrdvsdli eiastgvegs egegtfvlqp
      601 qntgdgtvqg iefdlstpls ainmpntgif lnyswldsev edsfgkrkfn dqsdyvynig
      661 fiqdlpilra sfgatyrnqg daygrfvgee vttsygadle lfvekrwddv tlrlvgsnll
      721 daskdevfnk fdslddqnsr dfdeyelese eagpvvqlml ryaf
//
LOCUS       WP_273586026             673 aa            linear   BCT 28-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Mycobacterium
            tuberculosis].
ACCESSION   WP_273586026
VERSION     WP_273586026.1
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 673)
  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 673)
  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 673)
  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 673)
  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 673)
  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..673
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..673
                     /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=74299
     Region          10..671
                     /region_name="PreP"
                     /note="Prolyl endopeptidase PreP, S9A serine peptidase
                     family [Amino acid transport and metabolism]; COG1505"
                     /db_xref="CDD:441114"
ORIGIN      
        1 mtfepapdga dpylwledvt gaealdwvra rnkpttaafc daefermrve alevldtdar
       61 ipyvnrrgny lynfwrdaan prglwrrttl dsyrtdspgw dvlidvdelg raddqkwvwg
      121 gagviepdyt raliglspgg sdasivrefd mltrefvedg fqlppaksqi twedpdtvll
      181 gtdfggdslt tsgyprvikr wrrgkplada etifegagtd vrvnasadrt pgfertllgr
      241 aldfwneevy elrgseliri eaptdasvsi hrdwllielr tdwtvattry tagsllaaey
      301 deflagsael qvvfepdeht alyqyawtrd rllivtladv asrveiatpg swrreplsgi
      361 paatntvivs adshgdeffl dssgldtpsr lmrgtddgrl aeiksapaff daenmavtqy
      421 fatsddgtsi pyfvvrrtda dnpgptllng yggfetsrtp tydgvlgrlw larggtyala
      481 nirgggeygp gwhtqamreg rdkvaqdfaa vatdlvtrgi ttaeqlgarg gsnggllmgi
      541 mltgypekfg alvcdvplld mkryhlllag aswmaeygdp dnpddwkfis eyspyqnisa
      601 nrkyppvlmt tstrddrvhp gharkmtaal qaaghpvwyy eniegghaga adnaqiafks
      661 alsfaflwrm lag
//
LOCUS       WP_273586327             635 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [unclassified Pseudoalteromonas].
ACCESSION   WP_273586327
VERSION     WP_273586327.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 635)
  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 635)
  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 635)
  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 635)
  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..635
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..635
                     /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=71548
     Region          <184..605
                     /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 mnkfkplggi ffvfilfcfc lnieltnqin rinlfnpdid lrhfdivdtt lemapwynpm
       61 lnghylihqp sadfllvktt dtefiaanat klilmtltsp infilvcmal fvgftiirke
      121 rkkisyqhqi aqlnnnanql lvafnlqpqh dnpsglgnls qsinnlnthv anylkqtqts
      181 icqdkltlli drhayiehid rqinftdeeq lkcallfidl dgfkqvndsf ghsfgdeilv
      241 qvatrlanvl rhhklsnine anqleqnlsr lggdefsifi esvdtdnkvv diakhvlsel
      301 ekdfvlgnki ikisasigia aypesastpq allqladvam yraksdgkgi fkvyspemgn
      361 kmrryhylle elrlavackd fylsfqpivh vedcmidyfe altrwehpie gmispaefip
      421 iaeesnlile lgdwimhesc rqmaawhnag mrkvkisvnv sgvqlkhrsv ydwimknlkn
      481 tglpshslml eitestfika sksmieeler lraegvtiai ddfgtgfssl stladlpidv
      541 ikidrsfisq adkspkyndi lntiselgqk lglkivaegv eeieqfelvk rmgvssvqgy
      601 lvsrpessin vgnkvlrknt anlsaagtsa weies
//
LOCUS       WP_273586345             420 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SAM-dependent methyltransferase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273586345
VERSION     WP_273586345.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..420
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..420
                     /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=47823
     Region          136..393
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mekvssincq eqtgwftnly kklvtkafas ietgqivlve nsrstvfgqq hsnlkttitv
       61 ndtamykafa lsgsvgages yvlgqwscdn ltklieifai nqkqldafek kfsffsglah
      121 rfnhlknsns esgskkniva hydlgndlye sflseemlys cavypskdas ledaqqnklk
      181 qiceqveine gdsvieigtg wgafaiyaat hynchvtttt isdeqyayve nkvkqlglen
      241 nitllkldyr llegqydklv siemieavgh eylpsffkqc nsllkedgam liqaitigdq
      301 ryqhylknsd fiqqyifpgg clpsinemse qiknntdmvi htvsdigahy artladwrtr
      361 fidnwhtlds dkfderfyrl wlfyfayceg afrtratstv hltarkprft sqndeialny
//
LOCUS       WP_273586399             512 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273586399
VERSION     WP_273586399.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     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=56239
     Region          34..504
                     /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 msqlqsaqls pvenkaifeq nglppqfnld qfinyqiasl qglsavqqam akaqkpfsgv
       61 avntlaatvn dvdlakplad fpavlnelks vyldhavyfh hprymahlnc pvtypavvae
      121 hiigaintsv dtwdqsagat lieqklidws cekaklpsta dgvftsggtq snlmamlvar
      181 evavsryapn hevklqglpe vasrfriycs evahfsiqka aallglgyna vvpvatnnkm
      241 qmdmdalnha iadskakgdl piavvitagt tdfgsidpve diatlakkeq lwchvdgayg
      301 ggllvsehhr salngieqvd sitidyhksf mqpvscsafl lsdkrhfshi tlyadylnpl
      361 aeagngtpnl vdkslqttrr fdalklwltl rtmgeaplgr afdkviglar qthivlndhp
      421 dfevinypel salvfrfape elkhnpdlld tlnlhvrqtf lntgeamiar tkinshhylk
      481 ftllnaqcql sdvravleqi stiawqtyke qk
//
LOCUS       WP_273586412             531 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273586412
VERSION     WP_273586412.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..531
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=59646
     Region          4..383
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkdsffrsmt wlhtwvgllt cwiiyviffa gtasffrdei nlwnqpaihn vqaqtdrvaa
       61 qrqqiingfd ylnqhaensp swritlpeer ipylvygyak pkepgqrrsq fvntqlnpnt
      121 mqalppfves kggnffyrlh yqlyyldait grwvvcfasf fmllaiisgv vihkrifkdm
      181 ftfrrnkgtr swldahnlss vlalpfhlmi tytgiitlil mlfpypaltt ydkgmrgffn
      241 dvtpsnnvtn naqgsaellp intildqvyt kwpsaditrv qvskpnmaas tvtvlvspak
      301 alrdqsprll fsgatgelva qtddelsssk alyeslnsmh tgrfatpllr wlyvlggiag
      361 cvmigsgcim wakrirernk gkasfglqlv ealnlatimg lplatcaffi anrllsptva
      421 grgekevtaf flawlvvavm allkrdrlqw rvmaainala clsvpainal ttqgnivsyl
      481 lnkqwalfif davfllfsil flvqteklrt apsaskktan nladnkkrqk a
//
LOCUS       WP_273586492             322 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273586492
VERSION     WP_273586492.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..322
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..322
                     /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=37271
     Region          2..321
                     /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 minsiqylrg laavlvvyyh atiksvqnnl paaevfnfgq agvdlffiis gfiicfstdk
       61 htfsaprflk srvlriiply wfftllallv flvvpnlvns sggetviwks fflvptedky
      121 lvrngwtlsy efyfyfifal favffikrsl vflpllllal igcfnnahfy fdsyliefam
      181 gvisfimykn kvavkynlil lffmffslla mhllevdsvv fyyafimwfi fhgslvleql
      241 ikvsklqsfk nllfklgdss yslylshaft lvvlnkimll impnvgkely lflltfisii
      301 vghlvyvlie lklnsyckkl fn
//
LOCUS       WP_273586515             139 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273586515
VERSION     WP_273586515.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 139)
  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 139)
  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..139
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..139
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16059
     Region          7..35
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(8,11..12,15..16,18,47,50..51,56..57,59..60,85,
                     88..89,92..93,96)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <10..111
                     /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          45..77
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          84..111
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdihdqieqy ceqgndlfde ddflgaiaiw qkaldlivdp nedwnevlwl kvsigdsfym
       61 tdeyekslds lldalnypea nenpfihfri gqcyyqlgdk gssknsllka ymlsgkeife
      121 eheeeglffy gflssvinf
//
LOCUS       WP_273586521             699 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273586521
VERSION     WP_273586521.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 699)
  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 699)
  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..699
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..699
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=81561
     Region          596..>661
                     /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          620..650
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvhwivlgie ptqdkravkl aytqllkktp paefpeefka lrkaydqalk eisksadaen
       61 dnsiilddvl lkddqpqldt dientqaevf felkaspnhd tndepvefsi ihtipqlnla
      121 leqlysdilg rhslekwkml faapifwdvn qsktltenll gffsnhyflp eniwifldns
      181 lkitdglsts sndttrkaai alsryiktlp krindglven isddidfeaf nrhlkirsyi
      241 edkclydtfs aeeiedivqq iepvfktdfp lynyivkylw tingyssikr iltpltipyt
      301 eesllnyqah aeyklknyel alklyiqqer nyrdfctkvm fknigmcylk lnnferayly
      361 ldaetrvaad meievalita rrgyirelra detqnaikia tllyengryq dalsiteqyk
      421 hvfieqanyl qalclcklhr ldeaysefll fidlyierql wlwplivelv rycydlitye
      481 llvetiqeht atfsdfyqta ffsgsleprc yteqemeile ltnerdsvrr slesvwhies
      541 mqifalailc irdtelvdye dhsvvenrkr dalncvkeik qfmlynpsdc lkfleaafdq
      601 qdydtcimla diaikalrta pqayyfkgca llelneygka lesfkqaaye ynthpyavhs
      661 lnsaitcaek lieqglsyqa thnelcmqlq nkkeivdgq
//
LOCUS       WP_273586451             472 aa            linear   BCT 28-DEC-2024
DEFINITION  MBOAT family O-acyltransferase [Clostridioides difficile].
ACCESSION   WP_273586451
VERSION     WP_273586451.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 472)
  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..472
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..472
                     /product="MBOAT family O-acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008374 - O-acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55584
     Region          1..472
                     /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 ggngviwsyy tymflkeywi ffifafifsv
      421 piakkinkfv veqakysmif nvfypisail lffisvtylv tgsynpfiyf nf
//
LOCUS       WP_273586703             636 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273586703
VERSION     WP_273586703.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 636)
  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 636)
  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..636
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..636
                     /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=74049
     Region          397..555
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
ORIGIN      
        1 mkkdllifty adknydffvv pyiyfalnsn pdcfvevave dintfitnns eaieklkgly
       61 ganflirqsn alskypnatp nvirfieepi ntskyvyigd idllifenik svhldyinky
      121 glpfsniird ssvsnprltg lhfcqfdrmy plpdisdldl kllndehvly limkrkgfmv
      181 pdsfrerpec gihlslsrds lgrytgtrds nfkveksakw pvetykerfl ksitdekfke
      241 iyfllpyefr lihmtlesvi tdksrllhrt avshmvdkrl mfdevliakd dlyksranal
      301 qesdtttash itttmnllwp nnidiwykkm wlafstgrqd lalecflhil dlpkgydflk
      361 dskilekkvk fineniilkn klasfeniep qndndivflc ggghsgttlm lavldsnnsi
      421 qsiphetgvf hrnkndkkvi eeiskwkvky nisatvdkyv ektpvhgahi erilklypks
      481 kvifmvrdgr datlsemkrl gnyddaiksw lkintkashf fndsrvlvvk yedlvsdlks
      541 tclkvcdflg vnysesmlty yenqrtwwdk evkkadsske lvgenhkvnr nwqinqpifk
      601 sknnwkesmt eeqkklfktk anhmlislgy aqdelw
//
LOCUS       WP_273586720             134 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273586720
VERSION     WP_273586720.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=15622
     Region          1..134
                     /region_name="FadM"
                     /note="Acyl-CoA thioesterase FadM [Lipid transport and
                     metabolism]; COG0824"
                     /db_xref="CDD:440586"
ORIGIN      
        1 mtfkvdfkvr hyecdlqgiv nnsvyfnyle harheflfan gidfallakq kvnlvvirse
       61 vdykhslvpd defyiavepe risrikfafk qtlvrkhdnk vmlqakvigt svnekgrpfl
      121 ppeidnlfkn ytqd
//
LOCUS       WP_273586810             247 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 4'-phosphopantetheinyl transferase family protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273586810
VERSION     WP_273586810.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 247)
  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..247
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..247
                     /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=28063
     Region          18..199
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtnlffkntl siapsfysdl ppsnntilvf nantlnvehl dltqylspfe lsvinrrkrm
       61 qakqeyvasr illkqlakht qpqyahipln kmsthfneec sklqlhinnt vintcishsh
      121 glvgvalnvt kaefgfdiek inlkrpfekl akhfyhkaei alitaplaik eqahrffriw
      181 tlkeslakat srpiaqllsp nvfdefslln ltassnsitv aneefdisva hkkstdwrcf
      241 ilnnldt
//
LOCUS       WP_273586824             855 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273586824
VERSION     WP_273586824.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 855)
  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 855)
  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 855)
  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 855)
  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..855
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..855
                     /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=92289
     Region          19..804
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mnqslpfrln nlkvstavav gaslslfgaf tahaaqqtpq aqedieqisv igsrrlgrtv
       61 edsavpidii gaealtssgl tetnallsnl lpsfnfpqas ltdgsdhvrp aqlrglapdh
      121 tlvlvngkrr hssallnlng stgrgsssvd lnaipanaie rievlrdgaa aqygsdaiag
      181 vinivlksas sggslaaiyg anvtemdgvp qlesvsegsd gnlafteggd rsltdgqtlt
      241 lqgniglelg dngflniste yrdrhstnra dydqrenynr ledgsldpre ftvnrynhnf
      301 gngdvedlsv fynagyqlan dadlyslgsy skregegagf yrrasdsrni eeiypdgflp
      361 vitsdindys lalgvkgfis dwnydvsavy gedafefgvt nslntsygpt sqtrfdagtl
      421 tydqltlnvd lsrevdvsfl esavsvaiga eyrtegyqie ageeasyaqg sfgpggvvtg
      481 edgpfgaaga qvfpgftpes egdnsrhnvs fyidletylt ddwniavaar yedysdfgdt
      541 lngkiatrys ltedlairas astgfrapsl qqqyftsvat vfvdsvptet gtfapssdva
      601 kalgspglda eeatnygvgf twstdfnfsl svdyyqilid drivlsnnls gaaieellag
      661 tganqgrffl naidsktrgv dvvasynlit dgygdiafnl gynygknevt diidppaelq
      721 gagfdqdnlf sgtelrrfev stprnkynls atwthdalrt tlrttryget qdpsstpeln
      781 evlkpkwitd ldvayaatdn ltlslganni fdvypdptre nveevstfsr lfayssfspy
      841 gfngryvygk iemkf
//
LOCUS       WP_273586878             584 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DUF885 domain-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273586878
VERSION     WP_273586878.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..584
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..584
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=66723
     Region          1..571
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mfkkrilaic laatslpsla dgnsdlktii dnhwqnakae kiffrtdpdg wkpngtlpnw
       61 seqaiakrqa ynnsvlksla sidpktlnnd qlmnyrlfky ereteqqsyl yqdkyfpvnf
      121 lsgwhtyfae apanmaflta ddynaflisl adyprfnqqn idlmkegikt gfthycktfe
      181 nysqsisahi vnnpknsaly epftripntf skaqksnlkq kaqaviknkv ipayqhfydf
      241 fendymphcr aqpgiasvkg gldyykytvn yytttnatpk qihelglkev arikaqmqni
      301 idevgfdgty sefleflatd eqfyakdaqd llektafitq kmygklptyf ghlprntfti
      361 kgsasrgafy mpppdnrspg tyflastpkl qplynleals lheaipghhl qnaiamelnv
      421 pefrrtlshs afgegwalyt erlgkeagfy qspysdfgrl gyemwravrl vvdtgihafg
      481 wsrqkaidyl ashtalpqsa vedqidryis wpgqalsykm geikirelrt kaeeelgaqf
      541 dirsfhdtvi gqgslpmavl edvindwiae qkpvslnntf khdf
//
LOCUS       WP_273586977             315 aa            linear   BCT 28-DEC-2024
DEFINITION  carbohydrate kinase family protein [Pseudoalteromonas sp.
            Angola-18].
ACCESSION   WP_273586977
VERSION     WP_273586977.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..315
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..315
                     /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=33898
     Region          3..304
                     /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(34,252,255)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(190,223,250,253..254,257)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 mtkllclgel lidmlpqdah nsaylpipgg apanvavgya klggeaafcg gkgddhfanq
       61 lsnalaqynv ntdylftiag sqtamvivsl detgersfgf yrhntadvll tqahlaqinw
      121 qsistlhfcs ntltdpaian ttlkalelak thnklvsfdv nlryslwent hdiasnvqac
      181 ytycdivkls rdelnflakh settgedyiq mllntgvklv fltdgpepak vyhsafilne
      241 sapkinavdt tsagdafiag vlyylnnlgs nlmladklnd etsikdalhf alkcgskacl
      301 akgafpalpv ladvi
//
LOCUS       WP_273586888             211 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: methyltransferase family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273586888
VERSION     WP_273586888.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..211
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..211
                     /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=23986
     Region          103..211
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 msyqpfidds aslieftrvy lalfytfvag fytvriiykn rstpagvifp gakfctswwn
       61 hmafkffraa iwfvcvlrvf vpatdnylgm fytlngwpgv mfgnimltag fllsmvvhfh
      121 maslwrsgid pngpqtlktt glysfsrnpm yvgvataqlg fflalpslfs liclavglya
      181 lykqiaveea hlvtrfnndy lkykqtvprw l
//
LOCUS       WP_273586987             784 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273586987
VERSION     WP_273586987.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 784)
  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 784)
  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 784)
  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 784)
  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..784
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..784
                     /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=85646
     Region          61..784
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkhsylalfi aasltpnfya haaqsaantd sierievagq tiksqglsvk datingpfgd
       61 nlalqdiars vtpisselie qlnittlqdv lavspntysa sgfgapslpt irgqlgelfq
      121 dgtrrqagnn gfgvplsfns ieqidvvkga ppvlfgssqr nggfvnlhsk tastdeskgk
      181 vkisagrwdq ysaqvdytap iikdkvglrv syehldegsy ydysgtksds lfaalrilpd
      241 dksswdinfe lyqveftdna ginrptqali ddglyitgqg vqangstvpa egsivsptgq
      301 vkidrstvlt dpdnqneatt ylihsiykre lsanaslkni tyfqhlqree iaqnsfveii
      361 dgadtaqnrt eltyrwnsdq qtifafdvry nkvlgysqft teadlpidlt gplsnrripl
      421 tdaqkarlve lspgvfvspg gqydldndgs gdfnlsdttd srswqtglai qqdsdwgdkl
      481 htsagyrvdf ydveandpia pqgqvaasds inetlhsgqv sfnyklnsdy ttygaasyne
      541 atsnsmaggt slggdntisa qnfatentlv efglkyaptn sdwyadgavf sqrrslrnrd
      601 gsntgirttg fesqvfyday pywlsagysy idarydnsas sqdsaqvida fdnsrpdiia
      661 gtgvgapsft afapsnrqvq gipeqsfsfn gnysinskwq mgfsglytks ypldflatvk
      721 irdqytlnvn tsyaftprtk lrldvnnvtn qknwrpvfeg gyfgatlafp elpinakltl
      781 thnf
//
LOCUS       WP_273587110             529 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [unclassified Pseudoalteromonas].
ACCESSION   WP_273587110
VERSION     WP_273587110.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 529)
  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 529)
  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 529)
  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 529)
  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..529
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..529
                     /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=60055
     Region          <60..525
                     /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 mdnffifili vgallltlsi vptikickkt nrvswillla lifsfivgyw yvlyyfvnnd
       61 iagfiamsvs lilfgggafv ylviqlsyks ilkidrfakr qrtlaendsl tglpnrkkff
      121 qvlnkqvkye psfylmlidl nrfksindsy gnkvgdmlls ifsktlshni vgiaklyrlg
      181 gaefalivdn saneainlci eaikkstkhp fhiyehslrv hvtvgittfa nhsslanell
      241 kqadlalhea kdtqqlyvhy fealstrane lsnmtsrikh aiknhefely lqpifdarad
      301 evhgaealir wpqsdgsfis pevfigiaeq sglilniskw vlletikhlk vlkaagfigs
      361 lhvnlstkdl espefyefve elvkhdptls daiifeitec ammtnleaar tmmqklnsrg
      421 fefsvddfgt gfsslvllre lpisqikidq sfikdmltqi adyaivestl flatrlnckv
      481 vaegiedndl kqtltlmdcd ylqgyyfskp vninefihky aneeeyrii
//
LOCUS       WP_273587069             306 aa            linear   BCT 28-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273587069
VERSION     WP_273587069.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     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=34166
     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 msvlvaitgr dntkliaklk ellpneeimq wpecqklnnv efvlawnapd dlwqqllnlk
       61 avssfgagvd sinmsllpke vdvvrivdte laqdmaeyvl ghvfahklrl keyfvkqsqc
      121 nykpkrayky nhvgilgfge lgkacakklt lngftvsaws kteksdeqvh lysqqqglne
      181 mlptidylvc llpltkdtkg iinadllakl pahacvinva rgehlveqdl inalnsemlr
      241 aatldvftqe plphdhpfwh nakititphc aalsdlnsvt aqiaeninrl ksgltlnnrv
      301 nrtkgy
//
LOCUS       WP_273587176             365 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273587176
VERSION     WP_273587176.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 365)
  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 365)
  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 365)
  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 365)
  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 365)
  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..365
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..365
                     /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=40344
     Region          <51..>149
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Region          126..364
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 msttntlskp snkkfweyap liftgfyllp tlfnlsnlpv ntivmsvafy ivfillyika
       61 mhcetkritt lfvimlvvcf satfyttgts tlfgfiafia gesyakksrl yavfsliftv
      121 alsayladia nikyflagtl lisgallafg iatqkerlhk kreqesanql eqlaaiaere
      181 riardlhdil ghslssialk aelanklnqg eryeqannei aqvadlarql lsdvrnavsd
      241 lkqlnlisqi aqlkqrlieq dfnvnfnvvl ntlppkvegi agliikeavt nllrhssnkn
      301 geinieqtqh qlhisvvdna pcstlnagng lngikeraeq lnghatftcg dkftlnvmlp
      361 isakd
//
LOCUS       WP_273587181             637 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NACHT domain-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273587181
VERSION     WP_273587181.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 637)
  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 637)
  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..637
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..637
                     /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=73209
     Region          8..>447
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
ORIGIN      
        1 mepttiiaks vapailkplt tnvltqlkgw rekiekskel qdirdtihap gdgteqalqv
       61 ienikkrylk frtliaqekq vyldeiyhpl sihyhergln hkvddnqllf nenitilvgi
      121 agqgktttlr kivqrelsde nskiipliit lrdvdwnsns lsvegiisee fsnlgvlvkp
      181 eavpylldkk allicfdgfd evpykfrqka isciskafns srcqtfvttr phteitylsg
      241 nfelasindl eeesitaiis ahplidkeyk elllrailnn knlseilitp ilvdifisvy
      301 gdldiepksp vdfysnlffs lasrhdrfks fsedsgferp skveltikel ykvflrssfn
      361 ilkkfenvsv seqdildvfs nsaakvsssk hndkaheeis drtslilkeg niysyihksv
      421 lefhaavfiq knknidnkkk iyqyladnyd tkyegmlryl yeidtpyfne hfslyqlnks
      481 gilselknvs fsgvfleand ipefyqftia ddtneassvk aisynddsnk meqakrvksl
      541 msilnidfys kgvipqevin lnelyltrdv heflrsdfer erhkapqkvi rfstrpylre
      601 sceiwgeaqt vfenilkvca vtiaqekken elddild
//
LOCUS       WP_273587194             232 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Pseudoalteromonas].
ACCESSION   WP_273587194
VERSION     WP_273587194.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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 10008291
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..232
                     /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=26016
     Region          46..218
                     /region_name="COG4111"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443287"
ORIGIN      
        1 minhyditey knplftvdsv lftvkkgalk vlmvkrasep fagrwglpgg fvdvdiddsv
       61 smtalrklke ktsvapqyle qlqtysginr dprgfsvtlv yfaliaeaqv sthietvdda
      121 kwididevnn lpvafdhkyi ieqakarlkq kalysmapvy clpehftvgq fksvietiig
      181 kpvqrksiir rieasgmfet ldekvksggr laqlykvkag vdivnfernl sv
//
LOCUS       WP_273587215             259 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-18].
ACCESSION   WP_273587215
VERSION     WP_273587215.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..259
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29572
     Region          30..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 mwvkfvrvvl sifvfmlysa mcnaqtitfv aedlppyhfi nennepdgal vdlakatikh
       61 tklsakfeii pmariftmle nnpnaialsl lktpirarqy twlgesyfad aylvslknrt
      121 devthlnhak fyqvatirgy ssatylknag ftedknlvlv syyqqlwqml ykkridfvlt
      181 ntltlnnelk hsglnpnlit krihltdyps klyfsanktl dkhtasaish alntlkenge
      241 yqailtkwql plpttankl
//
LOCUS       WP_273587367             331 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: WD40/YVTN/BNR-like repeat-containing protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273587367
VERSION     WP_273587367.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..331
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=36479
     Region          42..216
                     /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 mkylvyasli isgasiaqda pqyaisaina nktlltditn tgaglvavgk hgtvitskna
       61 eqwqqaqsvp tqvlltavdf snethgwacg hdatiinttd gglnwqlqqa kpeldkpcld
      121 iyfeddsngf avgaygmfyq tsdggkhwrk rfldsllfse dreylndlke ndpqgyeaet
      181 asilphfnri ektdsglmlv gemglmakss dngqtwqrld eiypgsffav asdaqqeiva
      241 glrgnvfakn kneqqwqhfe nvktatvnni inynnehwll lansgvifhl kdglltheqr
      301 pdgkaildgv iinnklvmat edgikvkeln p
//
LOCUS       WP_273587502             300 aa            linear   BCT 28-DEC-2024
DEFINITION  prepilin peptidase [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273587502
VERSION     WP_273587502.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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..300
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..300
                     /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=32897
     Region          16..298
                     /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 menlflditt aiqsqqwfyl ttvglislcv gsflnvviyr lplmmqrewq secrlllede
       61 itnkttqasn sepfnlvkpn stcpkcktai kpwqnipiis wimlkgkcan csnpisaryp
      121 iveaitalls lviaysfgat ehallyifvt wilvaltfid idhmllpdql tlplvwlali
      181 aavmgitisp gdaivgaacg ylslwsvfwl fklltgkegm gygdfkllav fgallgwqsl
      241 ltiillssvv gaiigialls iqgkdkatpi pfgpylaiag witllwgaqi qaayfnligy
//
LOCUS       WP_273587313             385 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: aminotransferase class I/II-fold pyridoxal
            phosphate-dependent enzyme [unclassified Pseudoalteromonas].
ACCESSION   WP_273587313
VERSION     WP_273587313.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 385)
  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 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 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..385
                     /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=42047
     Region          3..385
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mpfeflnthl qqqqqhallr krhvvqrata rtitvnnaty lnfasndylg fgdcsinleq
       61 nnvlgshssp lvtgyqaqqq qleqylcsal gyeagmlfns gfsanssvik alfndkstaq
      121 nsaifqdkln haslidgamh snaalirfnh ndlkhlrsrl ekskahnkli isegvfsmdg
      181 dtapikella lakehnawlm iddahgfgal gktglgscea lldeglvlpd ilvitfgkav
      241 assgacvlan nefinymlqf nrdytystam splmaaltlt rlqaikcadv krqqlssnia
      301 ffkqlckqha iavmesntai qpivlgcaeq tlhaaqrlkq qgiwltairp ptvahntarl
      361 rvtltaahth aditvlvehl kgaia
//
LOCUS       WP_273587811             831 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273587811
VERSION     WP_273587811.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..831
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..831
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=92947
     Region          567..818
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mrisspwttk nkllkqaatf falgslslta iaapldksni efigplgenm qvkpfqtphg
       61 qviinnlleq lqrntqsvsv fgkkhswqpf nkvnaltlgg lqalkfniet trysqgtlti
      121 kgienaqlfi daklqkgdnh tyslsltngs hsvivvaqqv anwnnvsldf epkadtdnit
      181 intsttkrls aeqlfdapti sglslapdak qyvtstrsys nktanqanvv telknsqnqt
      241 lyrfegqqps nmvwspnnqf lvymlgselk qlnrknlsik tlarelegas nfnfynnnsl
      301 ifswsktped nnsltkhykg lqdrwsyarn vsqlymldth sgltkalsqg pishsfedan
      361 tnrgkvlmsr qvmvmqatth petelveldl qsnkitsfgk fktfnhakya nkdvyvvagp
      421 dfkngagral pkgmlannyd gqlyllsdng knvkalskqf dpaigelhvl dngdalikvt
      481 eqdtqplyly dlskqrfkkl ntgldiveqf syshernpqv llsgttastp qqlkrlnisk
      541 nktdliwdsk playantqip tleefnftnk dgveitgrvy iptnldktkk hpalvyyygg
      601 tspvtrgftg rypfnlwaan gyvvyvlqpt gatgfgqtfs aqhvnawgdy tasdimqgth
      661 aflkkydfvd skkvgnlgas yggfmtmlla tktdmfsasi ahagisnlts ywgegwwgyl
      721 ysgeasknsf pwnnaslysd hspvfhadkv ttpllllhgd sdtnvpvges ltmytalkll
      781 nkdvelieyk gadhqifard krfdwwntml ayfdkqlkge pqwwdamysd k
//
LOCUS       WP_273587882             381 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273587882
VERSION     WP_273587882.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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..381
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..381
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=43071
     Region          196..224
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(197,200..201,204..205,207,231,234..235,238..239,
                     241..242,265,268..269,272..273,276)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          202..>380
                     /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          229..259
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          297..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(298,301..302,305..306,308,332,335..336,339..340,
                     342..343,366,369..370,373..374)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          330..360
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkylvftlsl lltacsstpp eapikkvqlt hiinhslfeq vktpsehsif elsepeksaf
       61 ltyahsrlsn vradeiifny lqnqltnfky dgatltaqqa iersegncis lailtqsyaq
      121 llnletsfqe mtsepvyake gnviyvanhf rtkiyapkke tdediiviir agtlidyfpt
      181 rgsfysgsat yndllsnfys nlaatalaen nlnkayslim qanrftpnda elfniagvlh
      241 rragdlksah miyqtaldrn disinlinny rilakelgdk tlekrltsql vdkekdpyel
      301 lviaknnlhq gkvtqakkql elaiakapyi selylelaki ryqqgntaqt qsllekaiqy
      361 ernkerlnvy qaklaslnkh n
//
LOCUS       WP_273587890             323 aa            linear   BCT 28-DEC-2024
DEFINITION  Bug family tripartite tricarboxylate transporter substrate binding
            protein [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273587890
VERSION     WP_273587890.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..323
                     /product="Bug family tripartite tricarboxylate transporter
                     substrate binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /calculated_mol_wt=34508
     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 mklfksvktt llaaslvlss pmaladihfl vpagpgggwd ttargvgegl vkagidnnas
       61 fqnmsggggg raiayliesg tkkgdilmvn stpivlralt gkipysyrdl tpvanmiadf
      121 gafvvrndsp yktwqdvika lkedpssikv aggsargsmd hlvaaqaaka ggidgrriry
      181 ipydgggkak agllsgevnl lstglseale vanggqarvl avtspealad ypkiptlksm
      241 gydmefvnwr gffaapnlpa dklaqytekl rklqstpewe tvrarngwln lfqekdefiq
      301 slekqeaqlk vvmqelgfir kad
//
LOCUS       WP_273587924             230 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273587924
VERSION     WP_273587924.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 230)
  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..230
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..230
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=26403
     Region          24..225
                     /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 mrtlllllaf sfsslllaap nktlrcatth yppftiydde thtftgidid ylafiernln
       61 lnievvhlpw arikkemklg yydcyfalan nteraqylef tteplhttqf glfstekanl
      121 nndlsnsria mlrgvklpnv lakeynikqs nfmhslstka tfdlldkqrv dyaitnyqag
      181 lwyskgykni yakqlegyal pvyiafkhgv vdtalvdeqi krykaqfgvh
//
LOCUS       WP_273587434             119 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glutaredoxin family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273587434
VERSION     WP_273587434.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 119)
  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 119)
  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 119)
  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 119)
  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 119)
  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..119
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..119
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13922
     Region          42..115
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 mkfvrwflgc iilffnfvft prskkrasdv qaqldqqtsq fklyqfkacp fcvkvrraik
       61 reglkietrd akndqqfrqe lleqggkikv pclriekngq vewlyesndi iaylnkvaa
//
LOCUS       WP_273587918             511 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: M17 family metallopeptidase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273587918
VERSION     WP_273587918.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 511)
  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 511)
  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 511)
  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..511
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..511
                     /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=54890
     Region          31..507
                     /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..46,60,66,83,180,182..184,228,234,263,269,274,
                     277,280..281,314,316..319,321,323..327,333,335,339,
                     379..383,385,415..416,418,423,425..426,432,434,449..450,
                     452,496)
                     /site_type="other"
                     /note="interface (dimer of trimers) [polypeptide binding]"
                     /db_xref="CDD:238247"
     Site            order(259,264,271,282,342,344,346,374)
                     /site_type="active"
                     /note="Substrate-binding/catalytic site [active]"
                     /db_xref="CDD:238247"
     Site            order(259,264,282,342,344)
                     /site_type="other"
                     /note="Zn-binding sites [ion binding]"
                     /db_xref="CDD:238247"
ORIGIN      
        1 maypqaiaaq slsasfdsfs hdaliiisdd fsqlannsls daieshakvd srigkqvtfl
       61 vvdnvrvvla ptgplnrdyd dvrryfdavk laineakaag svnpaiylpk lhtdaryqha
      121 levaylgacq alwqpleare yhgesiepit qiglidaneq tvkavnaiaa gqyaardlcg
      181 tepermappr fadycvelfk gskvavdvid dintidknyp mlstvarasy averhhprvv
      241 kleyvpegev trtlmfvgkg lvydtggadl kvggymagms rdkggaasva gfmkavadyq
      301 pkgvkvisyl avvrnsigsd cfvpdeiits regvrvrign tdaegrlamg dllsemkdva
      361 kgevnptlft vatltghaar amgpygayve ngparsants rqiadcgdlw adaaevsrsr
      421 redydfikpr tladdvlssn naasavtarg hqfpmaflav vggldkhgnd seqplpyvhm
      481 diagsgvegg dwqhgkptaa svtslfaryc m
//
LOCUS       WP_273587964             494 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273587964
VERSION     WP_273587964.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 494)
  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 494)
  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..494
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55196
     Region          145..489
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mnlslyqkla vslvvifcfi calvyswskq leltskhhge qnlhlalaeh lvqdnplike
       61 gvydyaalen lfhtlmllgp afefyfvden gkiltysakp gkvkrthinl aplkklinnp
      121 aaapiygddp rnkaqqkifs vapvfnndkl qgylyviigg eaydtslnti knndklwlaa
      181 lwlgaalafl liamlillrf ftnpiqrlar dvsnieaany sltdtklsny stqksnevhs
      241 lgrniqamvt rideqfkale qsdkqrkell thlshdlrtp laslqgflev lnqsrsqlsa
      301 qeqqeylhvs lnncaqlkql ieqifelahl engeisihke tfnlgeliyd ciakfsltae
      361 kkglnltvep aicdfpvvad iaklervlsn lidnairhtp kggsiavnvk ridekqlfvq
      421 vsdtgvgikh delnaifnph yqasnsnneg rqqgglglai ckgllklmds einvqselgk
      481 gtmfsfnlpq kikv
//
LOCUS       WP_273587955             458 aa            linear   BCT 28-DEC-2024
DEFINITION  class II fumarate hydratase [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273587955
VERSION     WP_273587955.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     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=48647
     Region          1..455
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 msnfrtesds mgelqvpsda lyqaqtqrav nnfaisgltm pkqfvtalay ikqaaaqsnf
       61 elnhlskska naieqacqqi idgehyehfp vdifqtgsgt ssnmnanevi atlatrigne
      121 pvhpnddvnm gqssndvvpt aialssainv vyellpslek lsqsleqkka dvgkivktgr
      181 thlmdampvt feqtlsawqs qvnnaasgir hslervcela qggtavgtgi nadgefaskf
      241 tknlsanvgi sfkpssnffy nigsqdaiva lsgqlkvlav aqmkiandlr wmnsgplagl
      301 geielealqp gssimpgkvn pvipeaaamv saqvigndat itvagqagnf elnvmlpvia
      361 hnilqsiell ansaqaladk aiasfkvnqp nidkalaknp ilvtalnpvi gyekaakiak
      421 qaykearpii dvaeqetdlp rseletllnp tkltqggl
//
LOCUS       WP_273588067             439 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Pseudoalteromonas sp. Angola-18].
ACCESSION   WP_273588067
VERSION     WP_273588067.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 439)
  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..439
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..439
                     /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=48787
     Region          90..340
                     /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(144..148,150,160,162,221,240..243,283,287..288,290,
                     301..302)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:270872"
ORIGIN      
        1 maasrsipts rlsrfaklgs laggvatnml idgtksaltg ngwnnkalll qpknieklav
       61 qlahlrgaam klgqllsmda gellspeltq llallradan pmphnqlvkv lksewgedwl
      121 nrfshielrp faaasigqvh layqengekl avkiqypsia qsvhsdvdnv iallniarli
      181 pkeldiqpli neakaqllae adyereahyl nrygellsqh vnfkvpkvyg vhntkrifam
      241 eyvqatpiea lsnlpqgeqn niaarlidlf fkemfefkli qtdpnfanfh yqtqskqivl
      301 fdfgatreis sklskaylsl fiagtennra gvlsaareig yfkdtlldsy kshvidlflm
      361 aceplrttge fdfknsplat niknaglels aqsqqwhtpp vdalfihrkl aglyliaakl
      421 nakidinalf kpyikghfi
//
LOCUS       WP_273588068             472 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Pseudoalteromonas
            sp. Angola-18].
ACCESSION   WP_273588068
VERSION     WP_273588068.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-18
  ORGANISM  Pseudoalteromonas sp. Angola-18
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 472)
  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 472)
  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..472
                     /organism="Pseudoalteromonas sp. Angola-18"
                     /db_xref="taxon:3025338"
     Protein         1..472
                     /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=53067
     Region          1..469
                     /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 mmkqflndpk lllnavgegi ygfdlsgnav fvnpaaermt gwkaqellgk kihqyhhhsh
       61 adgspypade cqiyctmfdg krrevknevf wrkdgtsfav eytstpvyrq geligavavf
      121 rdisaqqqtq nelkqaleqv khlseqlqde nnyliaelne dwqdsglvgq shvfqamlaq
      181 iklvsetdst vlilgengtg kelvarnlhr lskrsnqafi kvncaaftps lleselfghe
      241 rgaftganer rkgrfeladk gtlfldevae lpleaqskll rvlqeqefer vggsttlkvn
      301 irvlaatnrd lwqmvqkgtf ridlyyrlnv fpikvpalke rkedipylct nlitqlnkrl
      361 akqikgvskk aisqlqaydw pgnirelqnv lereailtkh tvlklsqplh gdastavnts
      421 ltlaeaqkqh iiavlelsqw qisgdkgaac klglpestlr skmrklgirk nt
//
LOCUS       WP_273588097             822 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: S8 family peptidase [unclassified Pseudoalteromonas].
ACCESSION   WP_273588097
VERSION     WP_273588097.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 822)
  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 822)
  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..822
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..822
                     /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=87781
     Region          <137..550
                     /region_name="AprE"
                     /note="Serine protease, subtilisin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1404"
                     /db_xref="CDD:441014"
ORIGIN      
        1 mkssiknila glslagfsln aaaaavignq leqklqtmsa tesamvvvsy dqlgalsntq
       61 lqnllslglv egvqfkslpi igllatpsqi sqlvnvpgvr svyanrslty fnkeareltg
      121 vdklqsddfe ahngikftgk gvtvivndsg idatlddley gskvienvqg vthaqaislt
      181 gidgvwiegq pntdlnvghg thcagtvagw gshsdgeykg aapgadligy gsgaglsild
      241 alggydyais hiwdfnspir vmsnswgssg kfdplgpisl asykayklgm isvfaagnsg
      301 sgedthnpya qipwgmsvga stkqaelidf ssrgkngevg dftmpdgsew tyknevsiva
      361 pgvdiistra ktnvvsngga ddidampaeh lpyytmisgt smatphvagv ialmleanpe
      421 ltplevkkii qetatnmpgy eawevgaghi nayaavagal gydnqnsvtv nnlsdfnana
      481 itladadpqp fevlyspvge pevhrfnvna edswinvsse vfatttklkl eapdgtvymg
      541 nltlpvldtt mrvsapaqeg ewklsvygmt slsgvqadpt gltngpgvpe fisgeisilk
      601 sggyeglddi eghpaqnaie favserlvds rnnllyrpda nlkrkelaky lvmgmsvrqh
      661 rdilnnekmp lsdvngqytp fieavtevgs alkdrtqiqa pvmltsegtf spqgnvtkee
      721 layslvqglg leeqvraftg ditieynser ipvldtdqva pefrgyvqaa idmslinvty
      781 qveqgpydss ptvvayfkpq skvkrgdyav iisrlfnnyl rk
//
LOCUS       WP_273588211             251 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588211
VERSION     WP_273588211.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..251
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29164
     Region          26..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 mintlalvsg litispvlaq ptekyvigve nieylpyydg sgtnkrdyfg fskellelfa
       61 kqqnikfefy tlpiprlyke fiehhhvdfk ypdnpnwqvs yknqhqqdin ysvpslvtht
      121 giaslkdnik ledckslakv rgftlqgldk ltsmpglqvl endnviemiy llhkeridci
      181 yishdvlkyn ieeffdtpvp vffqhqlpvd hqafmlssik hpqlvkkfnv flkvnenaie
      241 elkkkhnfiv e
//
LOCUS       WP_273588175             593 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABCB family ABC transporter ATP-binding
            protein/permease [unclassified Pseudoalteromonas].
ACCESSION   WP_273588175
VERSION     WP_273588175.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 593)
  AUTHORS   ter Beek,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..593
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..593
                     /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=65651
     Region          1..593
                     /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 mrskhstikr adamtlkqsi ktlwpyitkf kgrvllalla ligakgatll mpwalkeiid
       61 svdksinpvl vipallllly gglrfasvfl gevrdavfsr vtehamrdig lkvfkhlhsl
      121 elafhldrqt ggisrdierg tsglsflmrf lmfnivptlf eiltvaiifg slfsiwfali
      181 tllavaiyit ftvtvtqwrn rfireanaad nlsntraids llnyetvkyf nneefeakty
      241 dsflanweta rlknrmslla lnsgqaliia saitalmwlg akevvtgalt igelvminay
      301 miqlflplnf lgfvyreirr altdlenmlg llnkkpqvtq rphaqhlcvs kgniafnnvs
      361 fsydasrpil snisfkvkag skvavvgasg agksslarll yrfydisags itidnqaids
      421 vtldslrkai aivpqdtvlf ntsireniay grptasdsei dkaiemahlk dfistlaqgd
      481 ktlvgerglk vsggekqria iarailkqsp ilifdeatsa ldshaeqail kamrdvtqnh
      541 tsiviahrls tivdadnilv fkkgelveqg thsalllqng qyaqmwqlqq qdd
//
LOCUS       WP_273588361             850 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 3 protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588361
VERSION     WP_273588361.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 850)
  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 850)
  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 850)
  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 850)
  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 850)
  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..850
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..850
                     /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=91394
     Region          70..>462
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          436..650
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          683..837
                     /region_name="Exop_C"
                     /note="Galactose-binding domain-like; pfam18559"
                     /db_xref="CDD:436577"
ORIGIN      
        1 mktpfslnki arasliasvg ilaacsndat ttpeannals ktekiwpkln iavkqdpkie
       61 akiadylktm tleqkvaqmi qpeirditve dmrkygfgsy lngggafpng dkhatpmdwv
      121 klaedfyqas vddsidgski ptmwgtdavh ghnnvigatl fphniglgaa nnpalieqia
      181 aitavevmat gidwvfaptv avvrddrwgr tyegysedpr ivrdysaaiv nglqgkaegd
      241 flsdkrvist vkhflgdggt vdgddqgnni dseqdlfdih aqgyvgglsa gsqsvmasfn
      301 swhgvknhgn kylltdvlkt rmgfdgfvvg dwnghgqieg ctnescaqav nagldifmvp
      361 tgawkplyen tiaqvkagei smsriddavs rilrvklrag lfdkpspakr qfsgktelig
      421 aqqhrevarq avreslvllk nknnilplea nqtvliagdg adnigkqsgg wsitwqgtnn
      481 knadfpgats iyaglekqit qaggrailsv dgsyeqrpdv avvvfgeepy aeghgdrdnl
      541 efergnkksl allkslkeqg iavvsvfisg rpmwvnseln asdafvaawl pgtegggiad
      601 vilkakdgsi qhdfsgklsf swpktavqat vnkgdddysp llpygfglty gdknvladnl
      661 dedskldnsa ltsmdilvga pvapwrlllk sgdelldvss sthqlgalky rtedktvqed
      721 arqfnfsgeq kasaeivtsf aedtitylea ngvisfdikl nepltddvnl amtcsgecgg
      781 aialskmvdq sikniwqsvs vdlrcfanqg vdfasltspf slhassktsv svaniqfvpn
      841 kadsaglkcq
//
LOCUS       WP_273588407             859 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273588407
VERSION     WP_273588407.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 859)
  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 859)
  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 859)
  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 859)
  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..859
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..859
                     /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=92915
     Region          15..807
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkiksnalnq aikfalattt taglfisgsa vaaeesetkv nknvekiavv gtrsaprsig
       61 dspvpidiig geeleksgnt dmlellkgsv psfnvhqnpi sdaaslvrpa nlrglpsdst
      121 lillngkrrh rasviaflgg gindgaqgad isvipsialk qvevlrdgaa aqygsdaiag
      181 vmnfqlkdas eggkfevrhg qyyegdgdtt qisgnvglpf tdngfanlsf qyktadatsr
      241 seqrpdaaal saagvpevss laqvwgapev dddisifgnf gleltndsef ymfgnyserd
      301 vrggfyyrnp htrpgvysnd ggetllvadl tedmsgncpt iaiddnvldn pdyisgvann
      361 pdcfafneti pggftpnfgg nitdtsltig tkgmftggfl kdafydlsgt vglnesryfi
      421 ydtvnaslga dsprdfspgk yeqleknfnf dlskgfdfdl aydvniaggl ewheetftvi
      481 sgdeasftag plteqgfgig sngfpgfkps dageytrrny aayvdieapf teeflmglav
      541 rfedydsfgt ttnykvmaqy hvtedlnirg svstgfrapt vgqanvsnvq tnlsdgvlqd
      601 sallpptnpi avqlggtele peesqsytlg avytigdlfv tldyynievd drisqsekiv
      661 lsqddkdtle aagvpnaqsy aqvsfftndf dtttqgidlv anytadmlgg sstfslaynw
      721 netevtkfsd itgefkvkrl eedlpnhrat ltwaqqwesf smftranyyg eyqgvhvdyd
      781 ataktadaav tidaeityfl nesisfsvga qnifdqdaek ldfedrtgip nnnwggqyye
      841 tspyginggf yyakatytf
//
LOCUS       WP_273588489             317 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: YbgA family protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273588489
VERSION     WP_273588489.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..317
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..317
                     /product="YbgA family protein"
                     /calculated_mol_wt=36067
     Region          68..314
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 mqtdtikigi saclagekvr fdtghkksnf cmdelgkhve ytrfcpevav glpiprptir
       61 qvrvgdtikv crpdgtgdvg pklteygkkv ateqaknlsg fvfcakspsc gmerikiyne
      121 agtgntsegv gffaeqimkh npllpceeng rlndmhlren fvmrvyaykq wqllaseplt
      181 vhkltqfhsq ykyllmahny qayrdlgnll gtyngddint ladeyilglm nglkkpasrr
      241 nncntlmhlq gyfkkdlskv ekqelrdaid eyrqglvply vpltllkhhl kvhpneylek
      301 qvffnpypne lklrygi
//
LOCUS       WP_273588492             420 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SAM-dependent methyltransferase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588492
VERSION     WP_273588492.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..420
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..420
                     /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=47824
     Region          136..393
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mekvssincq eqtgwftnly kklvtkafas ietgqivlve nsrstvfgqq hsdlkttitv
       61 ndtamykafa lsgsvgages yilgqwscdn ltklieifai nqkqldafek kfsffsglah
      121 rfnhlknsns esgskkniva hydlgndlye sflseemlys cavypskdas ledaqqnklk
      181 qiceqveine gdsvieigtg wgafaiyaat hynchvtttt isdeqyayve nkvkqlglen
      241 nitllkldyr llegqydklv siemieavgh eylpsffkqc nsllkedgam liqaitigdq
      301 ryqhylknsd fiqqyifpgg clpsinemse qiknnsdmvi htvsdigahy artladwrtr
      361 fidnwhtlds dkfderfyrl wlfyfayceg afrtratstv hltarkprft sqndeialny
//
LOCUS       WP_273588617             424 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: purine-cytosine permease family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588617
VERSION     WP_273588617.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..424
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..424
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44910
     Region          18..420
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mpngndphti nsnelvawpr iaaiaamlsf slptfitgle ihqsssvsnt lwalvigsli
       61 ltliggamgt igvksrlssy llvkiafgna gagivniafa lsligwfgvn idlfsnavvr
      121 llsaefniim pewpidivag camlittlyg fkainvlasi mipilaavta mmlfgaldsm
      181 plvdfinlek saalsledgv aaivggviig aiilpditrf skqkrggvyt sfiaymviel
      241 lvifvavfaa aamqeteils lmlalnlgfs affiviagsw ilnslnlyst alsveatfph
      301 whkkwvivll glvgigaafi nildmfisfl vflsdifvpv agviivdalf ikphaynaaa
      361 lvnnanfslp afsawfvgaa yavcngalfn vsmsgitvid aiiltaviyt lfakaiapkp
      421 viqq
//
LOCUS       WP_273588690             428 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588690
VERSION     WP_273588690.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=48301
     Region          <205..420
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mkirpslrly ffasmvvlss amaigfsfls vnyfidgldk glngvmlkls qttevkpget
       61 kelvgfnias rwedmpasiq qrfkkptevg llhktkdrps mfsmpqnlff vvyypnpege
      121 pryisrimle kdkpqllani epeqrmlwia itgiaaivlf afflfmvmkk iakpveslrg
      181 wakslnqtnl qqtppdftyn elntlatlir ssllsanesv ereqrflsya shelrtpisv
      241 irsnvellnr lsekaplsdk qqltlerier agltmsdltd tllwlsrned qqsspepvnl
      301 sdkittlsne lnyllnakhv evvlntqqes vittdatach ivltnlirna yqhtqfgqvh
      361 itqqgskvti vncskqdeap kasspsakha sigyglglql sekiikrhgw iydvndkpgr
      421 yevvvdfs
//
LOCUS       WP_273588735             959 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: M16 family metallopeptidase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588735
VERSION     WP_273588735.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 959)
  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..959
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..959
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=108076
     Region          45..463
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          489..909
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mkfkllatsl avslaltgca tqqsentqta qqqqttkade rvfsqeylie eldnglrvmv
       61 vktdypdvvs lqipvsvgsr nevkagktgf ahffehmmfk gskkfpqdey taifknagvd
      121 nrayttndyt nyhlnfskqh ldkvleiead ifqnltytee qfrtealtvk geylknnasp
      181 irkllsavre eafdthtykh ttmgffedie ampdqmaygk effdkfykpe yvslvivgdv
      241 dpkatmamvk khwggwkkgd yvadikaepk qqapkyvhek neglpghwll vsykgaawep
      301 akkdraaldl isqlyfsnns dlyqelvvdk qiasqmftyn petkdpgllh vfvkvenedd
      361 lakardainr tyakartelv deqklsdlks nlkysfingl dssqaiastl asymhferdp
      421 evinqlyksa dnitaqdika vankyfvdda rttvtmsald kapgfeqets lnalvakhdk
      481 apeapvfkvl dktnssplid vnflfntgaa adpqgkkgva altaamlaqg gsqstsykdi
      541 qkalyplags fgyqidkeml sfqgrihkdn aatwyalvsd qllnpgfrdd dfkrlkkemi
      601 dgiksglkas ndeelgkevl ystlykghpy esynygdisd lealtlddvk afynteltqs
      661 kltlgligav pkalkaeims dlatlpkgeq srlsipdape lkghhative ksaqstavsf
      721 gfpidtirss edwtalwlvr syfgehrssn sylyerirqt rgmnygdysy ieyfprgmfq
      781 tkpdanlgrs eqifqiwlrp lrsnndahfa trtalfeldk likngltekd featrnflin
      841 yvpqlvasqn rqlgyaldse fyntesfvky vtsklekltl advnrvikdn lqtdnvqyvf
      901 itgdgedmkk rlvseqtspm vyntekpaal vaedkviady klaipannie vmavekvfq
//
LOCUS       WP_273588530             468 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alanine/glycine:cation symporter family protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273588530
VERSION     WP_273588530.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=49825
     Region          1..446
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mfdtvvksvn gllwgegqil iyillfagiw fsvrlkaiqi vkfkhmfsll kgsskckkdd
       61 issfqalctg lcarvgtgnl agvavaislg gsgaifwmwv iailgmatgf aesvlgqvyk
      121 vrdssgefrg gpayyiqqgl gsrafaivfa aclflgygft fsamqtntit dalnyafqvp
      181 tfysglvitv lagsiilggf kaiarfaerv vplmgilfva aaviitimnl pqvpamlkdv
      241 flsafglqea gagamgaaik ngiqrglysn eagagsvpha aasaspmpnh pvtqgyiqml
      301 gvffdtivlc sctavvilla dvdisgemeg irltqsamta hlaqggvyfv aaaitlfaft
      361 svvanyayae snlhlfkldn kvgrtiytll ylsmmlwgas aslkevwdla dialglmtvv
      421 nviaiilltp tilsvncdyn tqrekgiepe fkvkdvkvqg kcesgiwd
//
LOCUS       WP_273588817             189 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Maf family protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273588817
VERSION     WP_273588817.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 189)
  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..189
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..189
                     /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=20512
     Region          5..186
                     /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 mttavylasa sprrkellsq lgiefeqfsv dadetplane qphalverla clkaqtgval
       61 gytdrpvlgs dtvvvidnes lgkprdkndf ittlkrlsgn thqvltavaf atqtdvlscv
      121 vstdvtfktl sdeeinsywe snepqdkagg ygiqglggrf vthiagsyfa vvglplyete
      181 qllqaflrr
//
LOCUS       WP_273588545             512 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent decarboxylase family
            protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273588545
VERSION     WP_273588545.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=56211
     Region          34..504
                     /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 msqlqsaqls pvenkaifeq nglppqfnld qfinyqiasl qglsavqqam akaqkpfsgv
       61 svntlaatvn dvdlakplad fpavlnelks vyldhavyfh hprymahlnc pvtypavvae
      121 hiigaintsv dtwdqsagat lieqklidws cekaklpsta dgvftsggtq snlmamlvar
      181 evavsryapn hevklqglpe vasrfriycs evahfsiqka aallglgyna vvpvatnnkm
      241 qmdmdalnha iadskakgdl piavvitagt tdfgsidpve diaklakkeq lwchvdgayg
      301 ggllvsehhr salngieqvd sitidyhksf mqpvscsafl lsdkrhfshi tlyadylnpl
      361 aeagngtpnl vdkslqttrr fdalklwltl rtmgeaplgr afdkviglar qahivlndhp
      421 dfevinypel salvfrfape dlkhnpdlld tlnlhvrqtf lntgeamiar tkingrhylk
      481 ftllnaqcql tdvravleqi saiawqtyke qk
//
LOCUS       WP_273588833             408 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588833
VERSION     WP_273588833.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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   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..408
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..408
                     /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=46929
     Region          39..380
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maklihsali kikdsetefe dleslptlyt sdarfvhsvn awfydliack rlkdlnsysr
       61 allcywsyle inslnwdefp pikrlkptyk fkyhllsevs crkispstan lylkhvvqfy
      121 iwaieeseid indektapfa iefisikrtd klahlkpkfi vqttdlkirv pkksesgltp
      181 ltsesllafs iklktepvef klmcalalls glrkseacsf tqealnsaip tsnshtrytl
      241 tlgpstgvnt kynkqreiev satlisklrd ysiserrlkk vnklkvrgey eplfisqygn
      301 qtnvgtlsar wsdfrkiinf tynsfhysfh dlrstyatyr lndllnaglg vgealdclmh
      361 wmghdqestt mkyirylqkk talknkfgll dqimhnaies egfinepl
//
LOCUS       WP_273588914             334 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588914
VERSION     WP_273588914.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=35394
     Region          26..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 mditkinqwt ifiaavlial sslfsalsfg aadtplsdvl tgvlsagegs fnariiyelr
       61 lprtllafma gaglaiagli lqtvtrnpla dpylfgissg asfgvvllma vasisagfml
      121 saaallgsfl amglliliag rqkrsqvesm llagvalsfl fsaftsllly wsdpqavagi
      181 lfwtlgsfar aqwatlwlpc vvivvcisfm lsfkrqlnal llgdesaitl gvrvhrfril
      241 mlvlsslita vlvalcggig fvglmvphiv rffisqgsta gllitslvgg tfmvwvdvls
      301 rsllknqelp vgvitaamgs vfflsllffr ktka
//
LOCUS       WP_273588982             635 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588982
VERSION     WP_273588982.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 635)
  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 635)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   3  (residues 1 to 635)
  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 635)
  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 635)
  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..635
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..635
                     /product="vWA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=70038
     Region          <91..266
                     /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          <352..>441
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          369..394
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(370,373..374,377..378,380,399,402..403,406..407,
                     409..410,433,436..437,440..441)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          397..427
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mdftfirpav lwllipalal ffiafikhkk qsadnliaph lapfimnesn tkasqplwlv
       61 avfcclaiif sagpsfeekq vpvfqsksar vivmdmsysm ystdiapnrl mqsrfkaldm
      121 ielfkegdta lvayagsaft ispltndatt ltnlipslsp dimpdkgsnv lagldmakel
      181 ltqagyidgd iilvtdgidq eeqsditslt snssyrlniy gvgteqgapi klpeggflkd
      241 sygqivipti nisrlkslat rsggkfalyq psssdiatfa pgansellkd ekqshalwri
      301 dagiygllil lplglylfrs aafvgaflvl svlptqqasa lelpsflknt dqqaldaykn
      361 kdferaanad ssslkgsaly qqgnfdaale afskdksatg fynyanalak sgqleqaida
      421 ykqaqtlqpn fseaadnqal veqlleqqqq qqqqegdsqd nqqqsdqseq qnnqqsdqsq
      481 qgensdsqse qsqgeqsqeq qgepnhesdt eqgqqsaesg sqsdkqnepe letqpqanqe
      541 qkqpeqtnee qaentqpqta qqqtltdeqk qnaqqqaaqa qtreltneek ekaqqlnqll
      601 rkvpddpail lrnkmqleaq krqyqrrptg veksw
//
LOCUS       WP_273589051             217 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: OmpW/AlkL family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273589051
VERSION     WP_273589051.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..217
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..217
                     /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=23037
     Region          2..217
                     /region_name="OmpW"
                     /note="Outer membrane protein OmpW [Cell
                     wall/membrane/envelope biogenesis]; COG3047"
                     /db_xref="CDD:442281"
ORIGIN      
        1 mktqisiall tsllaitpaa hanlsvnvgt invnpdnsss aineaptlal kgdsdtqlgi
       61 tidyafndkw vleliaatpf shdvngaggl agnkiadikq lppslvaqyh fldtsyalrp
      121 figvglnytt ffdeqpsqal katlgtddve vklddsfgfi aqvganykid qhwglhamvs
      181 mididtdatv yangakalts tveldpvvam fgvrysf
//
LOCUS       WP_273588947             139 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273588947
VERSION     WP_273588947.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 139)
  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 139)
  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 139)
  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 139)
  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..139
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..139
                     /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=16159
     Region          58..133
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mleivatedl kaaaqftfnn mkpyyqmyav dwdvedvyqa tknlknfdil ckeqhigvvr
       61 lsfdegrcql rdiqietayq nkgygahvia kvvdiarqhs vkfidlkvfq lspafklysr
      121 igfavdrkdd rfyymslrv
//
LOCUS       WP_273589137             375 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273589137
VERSION     WP_273589137.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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   Rosinski,J.A. 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 375)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..375
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..375
                     /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=43221
     Region          <284..372
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtesiallvf fthllvavfl lnihsgnqls nrilavflsv tafdisnfif tsfygehlnl
       61 dmfranfsvl tapilyfyvk sivysdlklk akdllhaipf iivclifipr fhlgddiakm
      121 afynnheplf evlfvhvvly lqmfiylali fkklnryklt vlnnysdiei lnkqwlnnfm
      181 mvflidftiv vvrniikfte lqgllnlltt lmmvvtlffv cwilwqalhn psifqgissk
      241 vksfepkkpp qnpsdvvdvn eaqrvlstik chmslnkpyl npslnietla kqlnipalki
      301 sivlnhhlgq hffdfinsyr vneaanilsl ksnkqkaile illevgfnsk ssfntafkkh
      361 favtpsqyrk erlnd
//
LOCUS       WP_273589223             575 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DUF885 domain-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273589223
VERSION     WP_273589223.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..575
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..575
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=65742
     Region          1..571
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mfkkrilaic laatslpsla dsnsdlktii dnhwqnakae kiffrtdpdg wkpngtlpnw
       61 seqaiakrqa ynnsvlksla nidpktlnkd qlmnyrlfky ereteqqsyl yqdkyfpvnf
      121 lsgwhtyfae apanmaflta ddynaflisl adyprfnqqn idlmkegikt gfthycktfe
      181 nysqsisahi vknpensaly epftripntf staqksnlkq kaqavikdkv ipayqhfydf
      241 fendymphcr aqpsiasvkg gldyykytvn yytttnatpk qihqlglkev arikaqmqnn
      301 idevgfdgty sefleflatd eqfyakdaqd llektafitq kmygklptyf ghlprntfti
      361 kgsasrgafy mpppdnrspg tyflastpkl qplynleals lheaipghhl qnaiameldv
      421 pefrrtlshs afgegwalyt erlgkeagfy qspysdfgrl gyemwravrl vvdtgihafg
      481 wsrqkaidyl ashtalpqsa vedqidryis wpgqalsykm geikirelrt kaeeelgaqf
      541 dirsfhdtvi gqgslpmavl edvindwiek qksai
//
LOCUS       WP_273589298             764 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273589298
VERSION     WP_273589298.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 764)
  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 764)
  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 764)
  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 764)
  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..764
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..764
                     /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=85172
     Region          8..709
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mahfklkalv talslcnlav haaqeehttd vkvseelvvy geigyrnrsq elaptleysq
       61 eyfqrfeplt agdalkrvps vtflsdvles dgarmrglsp aytkvlinge evpgagadrs
      121 ffvdripael ierveiirss sanrsadaia gtlnivlrdg ysldggyira gglryddgel
      181 kesfagvygt efaggrlllg anfqgrynpk qkssirygds pennpnyatd dfdnredqsd
      241 trdgddtsln asfekvfdng gkfdisamwv dtdrteders feyddatats nsvveggnll
      301 sdnanvsyid qtnyninsgy elpllggtsk fkvgyasfee svyeqeveld sselpmvfee
      361 aeetvdiddk ewslqwqhsl lvsdskevqf gafvqgkerd taifeaeees eqtltgwdqf
      421 sqtpmslaqf nnefeavdgg vntleedrfd lfalikhead vfswemgvrw estdsnitdt
      481 negvtakndy dfflpsahfr ysvsdngrvs asvarslrrp dfdymtpall eeeladndfl
      541 gnpnlkpess wgidlgyeyr lgksgvvgvn vfyrdvsdli eiastgvegs egegtfvlqp
      601 qntgdgtvqg iefdlstpls ainmpntgif lnyswldsev edsfgkrkfn dqsdyvynig
      661 fiqdlpilra sfgatyrnqg daygrfvgee vttsygadle lfvekrwddv tlrlvgsnll
      721 daskdevfnk fdslddqnsr dfdeyelese eagpvvqlml ryaf
//
LOCUS       WP_273589302             332 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273589302
VERSION     WP_273589302.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..332
                     /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=38358
     Region          110..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnsyvslsdk yltaqglita vvelaqsrgi alhkllrgtg ifeqdllsve hcfsleqqak
       61 llsqfkrlmn tpdsgfllgs qlvndstsaa qsvlysaklg aallqiqrah lqlcplffsq
      121 hyvsnqqfyi flnaatgldd dlhnyileiy saafysllkr lsphypqcef dfsfkrprhi
      181 hqyeqhlglk lrfeqpttrw visktllrqa npyaselrfm qaraqlavks hekytfieav
      241 wrylhtynea sleqtaqyfa mspatfkrkl kchnmrfssl vdeqnkhkai ylltlrakcn
      301 ehvaerlafy dipnfrrafk rwtgltpsql kv
//
LOCUS       WP_273589333             280 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: amidohydrolase family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273589333
VERSION     WP_273589333.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=31663
     Region          4..280
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mslkiidphv hffnlaegqy twlqgenppa wpnlelikqp isekklless dftlagivhi
       61 eagfdnnapi nelnwltahl kklpfkaisy aqldcapvqf akainalahp hligirdite
      121 gadaqrllnp mcfsnlqtlc qqglhyeaqf elentaiaaq laryakalpq lkiiinhggl
      181 pnninnwqqs irmlsahnni aikfsgfell alnlqqqqdc fetmfsyfge qrimfasnfp
      241 vcqinasynd vwhshqalck tnkiwhnlsy anakhfynip
//
LOCUS       WP_273589414             531 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PepSY-associated TM helix domain-containing protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273589414
VERSION     WP_273589414.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..531
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=58382
     Region          5..394
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mksitlkklf llhswvgvvt avllfvvaft galavlarpe lkiwanqslq qtqhipnsei
       61 stlvntyhaq vpkefgenih vfmptghnfh llalvfeshh gdenyqqevl rafefdpasl
      121 alvntyygps kqyyanrktd aasyigefha dlhlgrpigl iltgflgltl lvstvtglfi
      181 hrklikelft frwlkgfdvt isdghkvmgi wgsifnivig fsgaflglat villpaaafv
      241 sfggdqdkli etftaipepi ishvnqptni tailsdaqqr yphavildat vmahndtnaq
      301 vylrllggea vasqllhyng qgeyitsmss fgdiagvsik iieilfplhf gnfaglfvkl
      361 lwvmlglaca lmplsgmmmw lakrtrgstp tlsadayarw nrfiigscgg lvlaccvlfp
      421 vqvllnyava gvehnayfgp vffytwlvwl viaafwqnyk nyfratlllc alflisvlpl
      481 nsvlgvnnvi nanstlvaft disflivgla flwgylktkp daialaevka g
//
LOCUS       WP_273589497             381 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273589497
VERSION     WP_273589497.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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..381
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..381
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=43075
     Region          196..224
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(197,200..201,204..205,207,231,234..235,238..239,
                     241..242,265,268..269,272..273,276)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          202..>380
                     /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          229..259
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          297..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(298,301..302,305..306,308,332,335..336,339..340,
                     342..343,366,369..370,373..374)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          330..360
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkylvftlsl lltacsstpp eapikkvqlt hiinhslfeq vktpsehsif elsepeksaf
       61 ltyahsrlsn vradeiifny lqnqltnfky dgatltaqqa iersegncis lailtqsyaq
      121 llnletsfqe mtsepvyake gnviyvanhf rtkiyapkke tdediiviir agtlidyfpt
      181 rgsfysgsat yndllsnfys nlaatalaen nlnkayslim qanrfttnda elfniagvlh
      241 rragdlksah miyqtaldrn disinlinny rilakelgdk tlekrltsql vdkekdpyel
      301 lviaknnlhq gkvtqakkql elaiakapyi selylelaki ryqqgntaqt qsllekaiqy
      361 ernkerlnvy qaklaslnkh n
//
LOCUS       WP_273589526             592 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alkaline phosphatase D family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273589526
VERSION     WP_273589526.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 592)
  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 592)
  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..592
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..592
                     /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=64795
     Region          3..569
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 maftrrsflk asaagfgaav lslgltgcrf dddddtpvsf dhgvasgdpl sdsliiwtrv
       61 tpldvttksl kvqwqaatdq sftnivhdge thisdttdft lkvdlqglda ntiyyyrfna
      121 hgktspigqg ktlpvgavdq vklavvscan ypagyfhvyg eiakqsdlda vlhlgdyiye
      181 ysntgyated aaqldrllpl dnsseiialt dyrkryanyr ldadlqaahs hcafitvwdd
      241 heitndtwre gaenhnegeg efsqrklnal qayfewmpir nvadkeriyr rfefgnlvsl
      301 ymldtrvlar deqlnysdfd ltslagqsaf aaaigatdra llgseqltwl sdaittsstq
      361 wqvlgqqvlm tkmhlpvevm lllaslqsaq anggdpsell aqanvlfael aqikgrvlag
      421 dpsvteaela rvqttipynl dawdgyayer evllgtaiaa qknlvvlagd thngwagqlk
      481 tdasnpiaas qnagvefata svsspgleey lalntqdaqt vaqieqvial lvddlaynnl
      541 vergyltvtf tpakasakwn yistikarey qvvesrtkel smlagqaqlq na
//
LOCUS       WP_273589636             807 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: beta strand repeat-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273589636
VERSION     WP_273589636.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..807
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..807
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=83448
     Region          <54..>560
                     /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 mrslkrqagy gsllimalvg ilalgstvyy ktrmqqpesv retyestaee lreissalta
       61 yyrdnmawpa tindlaaggy ftgdaarcgg ggafqspfct vifggqtgdd ytltvnllke
      121 svaqavanqi pggtsagttv tatinrpfqs alyddylqrv adpdnpqrtq levdldinnn
      181 dlvnigslnv qratfdnaef tnadidrint eevqlgnnsi tyagnqlnvn agtvrtngsl
      241 smngdivgng nditgidsvs antgqfdyvs adsaainsls gnsldynsgs idsvsgnrlt
      301 fgngsitalg gntftygsgt issvsgnild fnsgnigsls gnslsygsgt vntlsgntlt
      361 ygtvsgtngn fdsvsansgs ignmsvtgta glnrlsssng nvtnldvttg ninsgeansa
      421 sgtsvsssgt stfseldsnr idtnsfkgqt vqassgstsg nasagsvsas nltvnnrlqt
      481 nviesnsssv gnasaskltv lgalsasgin vttanfntgs iasvsgtsan yntvtgnqfn
      541 ggsftsnddf ytsqssvnnn hlliteqrsk ldncvdvtky cipqtpsvnl tcsscnsaaa
      601 rssfsgtatg sisgcrqgcs yswvtsgsgl sfsgcsggti akggsaspsc rvssslgpqe
      661 sasgsiqliv tnshytsrta sdsvnvsytn ttpndpfrsv tagcyvdtaa fdqarpnscm
      721 angwpdktyk ailsvgeylg ienyqfytts dwtiawsgdc tssqwqcvms ftpgtgdqny
      781 sstvsvrhka tgetrnfsvt vrfhtle
//
LOCUS       WP_273589584             461 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273589584
VERSION     WP_273589584.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 461)
  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 461)
  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..461
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..461
                     /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=52980
     Region          84..418
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msviypnivn rtvnlgslpy isdvneqgyr evmfhedrfi erfprvlsln rlqdaleinl
       61 flehrykglf mppkrggnkn plggvslatv qslansmslf lqwveknnvd wqevyavsds
      121 dkakywlpvy ryrkhlieqv iskgierdta nlyinhvrqf yewarkqnri dkvpfkyktk
      181 iikkkrkdgg ldllftdygs dekgftittt dllipkkykq kkpgdaglsp ysqeelklly
      241 asrelakqga klrvdlavqc glraeeiatf sashvvdpal gnkaiyylti igkydkerti
      301 mvskglmtsl wryrngkehq drlakwqleh gncddaplfl nrsgnfmsrk signviskvr
      361 keltpfgktl krdfhdlrst fatnlagfli hknlpigfvq yklmqlmgha dfsttqkyin
      421 farsltfdkq maswvdklfg elveplqeaa fnpgfsgevn a
//
LOCUS       WP_273589726             197 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: Maf family protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273589726
VERSION     WP_273589726.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=21657
     Region          3..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 mkhplilass spfrqsllqk fnlpfrtfsp didetaipne tpeqlvkrls erkaraacdh
       61 fvkglaigsd qvavfdgqil gkphnkenai kqlsmfsgqt vtfltglcvy diandkaktl
      121 iepfevvfrt ltkeqieayc daeqpyncag sfkseglgic lfeklngddp nsliglplik
      181 lsqllaefnl dilaaqp
//
LOCUS       WP_273589760             150 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Pseudoalteromonas].
ACCESSION   WP_273589760
VERSION     WP_273589760.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 150)
  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 150)
  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 150)
  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 150)
  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 150)
  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 150)
  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..150
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..150
                     /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=15911
     Region          3..149
                     /region_name="CytC556"
                     /note="Cytochrome c556 [Energy production and conversion];
                     COG3909"
                     /db_xref="CDD:443115"
ORIGIN      
        1 mklkqflagv alatctlsvs antafkepsd aieyrqaafs misvqisdmg amlkgkipfd
       61 aeqfkmrann aaalskmpwe afyegtdkgd taaladvwsd natfvkkana faanadqlal
      121 aaqsgdkavi gkafgawakg ckdchkqfkd
//
LOCUS       WP_273589766             290 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: diacylglycerol/lipid kinase family protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273589766
VERSION     WP_273589766.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..290
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..290
                     /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=32307
     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 mqlliivkps vksvvldhld wlkktcqkkn ilyitvkttg nfeydlanvk lnaqesqiav
       61 aiggdgtlnl alngvinsac slailpcgtg ndfarrfhct akqwqnaifn apthlidvgk
      121 intryfinva gvgfdahvik qlghlqsmsa wrykwtsfks lftykastln gaflnkqcsy
      181 qnlitvfans qyfgggikia prakiddgll dcyqmqagrl vdhlysfikl ifkrhhtlkk
      241 ltysqlkqar intknlliea dgelvgvtpa viaiheqavn fhipikkrlq
//
LOCUS       WP_273590136             319 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Mycobacterium tuberculosis].
ACCESSION   WP_273590136
VERSION     WP_273590136.1
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 319)
  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 319)
  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..319
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..319
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35951
     Region          16..224
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mvpgdassvv svnpakplis vcipmynnga tierclrsil eqegvefeiv vvdddssddc
       61 aaiaatmlrp gdrllrnepr lglnrnhnkc levarggliq fvhgddrllp galqtlsrrf
      121 edpsvgmafa prrvesddik wqqrygrvht rfrklrdrnh gpslvlqmvl hgakenwige
      181 ptavmfrrql aldaggfrtd iyqlvdvgfw lrlmlrsavc fvphelsvrr htaatettrv
      241 matrrnvldr qriltwlivd plspnrvrsa aalwwipawl amivevavlg pqrrthlkal
      301 apapfrefah arrqlplad
//
LOCUS       WP_273590253             375 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Mycobacterium marinum].
ACCESSION   WP_273590253
VERSION     WP_273590253.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     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=39204
     Region          23..372
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mdsgrfdtav yarrlaaaaa ateqaglagl vitpgydlry ligsradtfe rltalvlpas
       61 gvptivlprl elaslkesaa sdlgvcvrdw vdgddpyqlv aealgvapaa iavtdsmpal
      121 hllpladalg vlpvlatdvl rqlrmvkeaa evdalakaga aidrvharvp eflvpgrtea
      181 qvaadiaeai vaeghsevaf vivgsgphga dphhgysdrk lqvgdivvvd iggtyepgyy
      241 sdstrtysig dpspdvaqqy stlqraqraa vdavrpgvta aqvdaaardv ladaglaeyf
      301 vhrtghgigl cvheepyiva gnelplvagm afsvepgiyf pgrwgaried ivvvtengal
      361 svnnrphelm vvpvs
//
LOCUS       WP_273590440             514 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Mycobacterium marinum].
ACCESSION   WP_273590440
VERSION     WP_273590440.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 514)
  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 514)
  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..514
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     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:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=55351
     Region          141..495
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mtghrntprw lprslrwqll lgvlavvtiv lvavggvsvl slrgyvtamn daevvesmha
       61 fshayaryrn gehtsihtgt ppvsqallef tgqtpgnlia vvrdgvvigs avfsedaprp
      121 appdvihaie tqhwtdepsr vetlgslgsy qvdsraagsd rlivgvslsi adriitrkqi
      181 ttsvlvatal vitaaltvwv vgitlrplrr vaataatvaa mplagddhqi svrvrpedtd
      241 pdnevgivgh tlnrlldnvd salqhrvasd lrmrqfitda shelrtplaa iqgyaeltrq
      301 dssdlpptte yalariesea rrmaslvdel lllsrlgege dletehldlt dlvmnavnda
      361 avaapthrwi kdlpdepvwi ngdharlhql vsnlltnawv htppgvtvkt gitsypddps
      421 gpyteltvsn dgpdidpevl phlferfvrs sksrssapgh glglaivnsi vkahdgsvta
      481 esaagqtvfr irlplidapl nasapgrprq psdy
//
LOCUS       WP_273590509             412 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Mycobacterium marinum].
ACCESSION   WP_273590509
VERSION     WP_273590509.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 412)
  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 412)
  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..412
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..412
                     /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=44895
     Region          72..389
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtraarnnlp pqikrrelps gavryeviad varegtrhqt rkrfarlada kdhlaglqgd
       61 vvrgvhvrrs alsmqqavea wlsgqrlrpk trsayitalr pavdalgakp vqqitksdie
      121 tvvrslvegt setgtwnapt klkgkktrsa waatsinpml arlrsvwqdl vdqgvvsrnv
      181 palvrplptv kpemhtlsvk qvetlfanis gqrlelfvhl allglrrgei aalrwsgidl
      241 dstpptvava anrvavsgga aesdpktdag rrvlpipdel lpilrrarqr sreeqlaags
      301 kwigqghvva defgspyhpd tlykywsrtl kaaglphvrl hdarhscatl mhqrgvplav
      361 iaawlghtda sftlrtyahs spsmlaeaav tlgglvtsrd tsdeqkpdtp tg
//
LOCUS       WP_273590523             384 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Mycobacterium marinum].
ACCESSION   WP_273590523
VERSION     WP_273590523.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     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=42921
     Region          87..364
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 magntprgir krlnaagqpr yqvrylirdp dapsgwvets atfptlreak afksdrdnea
       61 algarrfdpr lgrtplnriw tqfsdskkpa vspktwsgyv qhwdlriapr fghipvdeit
      121 radvqafvdg ltvgpwakvs tlrlmrsild vaqqdgrihr npalgvsagr iperdrhryl
      181 taqevqtltn acgdqgdvvt ilaytglrws elvglrvkdi nlvarrlyvr raapeveghi
      241 vigppktrag irtvplpqvv veifkaritg repdepavts pngamlrsnn wrrhtnwnka
      301 lkktdlaplt ihdlrhtyas larksgadlr yvqktmghst ptvtaniysd lyadeldqva
      361 tnldqlhate ihtpktgqep dken
//
LOCUS       WP_273590330             507 aa            linear   BCT 28-DEC-2024
DEFINITION  nitrate/nitrite transporter [Mycobacterium marinum].
ACCESSION   WP_273590330
VERSION     WP_273590330.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 507)
  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 507)
  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 507)
  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 507)
  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 507)
  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 507)
  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 507)
  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..507
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..507
                     /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=53471
     Region          55..475
                     /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(65..66,69..70,73,106,161..162,164..166,169,188,
                     191..192,195,269,272..273,276..278,281,316,320,382..383,
                     387,391,428,431..432,435..436,439)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340899"
ORIGIN      
        1 meqqmllhre esqsspgrsk avtrrwggsr hishwdaedl vaweagnkri arrnllwsvv
       61 tvhlgysvwt lwpvlvlfmp envygfsagd kflldmvatl vgaglripys vattvfggrn
      121 watfsaavll lpvvgtmvll lhpglplwpy lvcaalsglg ggnfaasmsn anafyphrlk
      181 gsalgiaggi gnlgvpaiql mglliiavag egkpylical ysvflaiaav gvalsmnnva
      241 qhrvkarhmr pivttvlanr dtyllsllyl gtfgsfigfs fafgqvlqtn fmaigehaaq
      301 atlhaaelaf lgpllaavar iyggrladrl ggsritlvvf vamtvvagll isasslegrh
      361 sgpmrgatmt gyfvcfialf vlaglgngsv ykmiptifaa cgrsldhgps vggldhrdrp
      421 rvisgvvigf vsalgalggv ginlalresf vatgtttdaf wlfmvfyaga aaltwkvyvr
      481 rpvvgiqalp paiapqpapa aaellgs
//
LOCUS       WP_273590541             254 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Mycobacterium marinum].
ACCESSION   WP_273590541
VERSION     WP_273590541.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   ter Beek,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 254)
  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 254)
  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..254
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..254
                     /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=26477
     Region          10..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 miqqlavpar avggffemsi dtaraafrrp fqfrefldqt wmvarvslvp tllvsipftv
       61 lvaftlnill reigaadlsg agtafgtitq lgpvvtvlvv agagataica dlgartiree
      121 idamrvlgid piqrlvvprv lastvvalll nglvcaigls ggyafsvflq gvnpgafing
      181 ltvltglrel ilaeikallf gvmaglvgcy rgltvkggpk gvgnavnetv vyaficlfvi
      241 nvimtaigvr isgq
//
LOCUS       WP_273590630             957 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Mycobacterium marinum].
ACCESSION   WP_273590630
VERSION     WP_273590630.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 957)
  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 957)
  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 957)
  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 957)
  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..957
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..957
                     /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=102530
     Region          17..>948
                     /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 mtqptkpvvd iedvmtlspl qlglfalama sgaasddpyt valgidvhgs ldvgllrsca
       61 lamlkrhpnl rarflgrglp hpvqvvpsev qlewarveat aetagaleaq ernrgfdlem
      121 gpairfllie lpgdrwrfli tahhiviggw sialfvdell tlyeadcnid tlpaqprpyr
      181 dyigwlercd veqgqrqwre hlaglaaptl laaplgssgv qpdslpkraq ltldegatts
      241 lvdgarnrgv tvntltqlaw almlstltdr rdvvfgvtvs nrpaelarve smvglfvntv
      301 plrvrldpkt tvaqqcaliq rdaarlreha ylshsqiral agmgelfdtl lvfqnfpslg
      361 ladgkaravg aatfdsltvq spthfpvcit aeltdarlsl siatnanafg ditesalgdr
      421 llavlqrllp mwdrplrdvs mlldghtdgd tavseharld vvgnravlae plvepvsvpg
      481 lfaaqvasra evtalvcgdr sltyreldqa anrlahllvd qgvgpgdvvg lllersveav
      541 iailavlksg aaylaidvnh pdgrigfmie daapvavist aglaqrlady pvavididdp
      601 aiatcypghe lpfpsadnia yliytsgttg kpkgvgithh nitqlftsva atgftpasgq
      661 vwtqwhsyaf dvsvfemwga llhggrlvvv pelitrsaae llallvtegv svlsqtpsaf
      721 yalqaadaaq pqlgrqlcld avvfggease parlgpwlan hgqrprlinm ygttettvha
      781 sfreivrhdl sfavspvgvp lanlaffvld gwlrpvpagv agelyvagag vgcgywrrsg
      841 ltasrfvacp fgaagvrmyr tgdvvrwgpd gqlqyvgrad eqvkirgyri elgevaaals
      901 qldgvdqavv iaredrpgdk rlvgyvvgsv daglpprrga tstaavpprs wwstvcr
//
LOCUS       WP_273589300             305 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273589300
VERSION     WP_273589300.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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 305)
  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 305)
  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 305)
  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 305)
  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..305
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..305
                     /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=34432
     Region          38..296
                     /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 mrfnpfishr lltnsiiama llaiflcayl gelkelqhiq wldiigeggi vimtltwiva
       61 llisrppgkv trylvlglgl fmfsgtldll dewlmqpaqq wlswieslpa pvgmlltslg
      121 lyhwhqeqyv lnkqlrrrea hlrehdkvcp vtgvytaeyl qsvlntqlka pqpvllaaid
      181 irdfasfnne fgfsegdrll reiselilmn crlsdvvcry agdcfmvlmp atskqqgqel
      241 lrqitaalkh cafkvegsgl akfqcvtthi iqaqksdtah ilmqqlhsgl qlqkqqrats
      301 seqlc
//
LOCUS       WP_273590674             296 aa            linear   BCT 28-DEC-2024
DEFINITION  acyl-CoA thioesterase [Mycobacterium marinum].
ACCESSION   WP_273590674
VERSION     WP_273590674.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..296
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31701
     Region          15..283
                     /region_name="TesB"
                     /note="Acyl-CoA thioesterase [Lipid transport and
                     metabolism]; COG1946"
                     /db_xref="CDD:441549"
ORIGIN      
        1 msalttdseq aqwsvdglle lfqvradgvd rftadtgfag lderqvvegt qvvaqaimav
       61 asrfegksvr sahavfcrav ivgpplelvl dvvhegrsta taivaanqng krcltvtvla
      121 diptpdvikh hlprppvvap aganvsqmpm agrqlrlvdv vdvnspdevg ppelyawlhy
      181 epipdrddla kaliayftgh lgisttmrah pgigtsqahl svstapmais vafhepvrwd
      241 gwllyshest qvgagmsyvr gtvhteqgal iasfaqeali rplrtsdtsi darsrf
//
LOCUS       WP_273590532             414 aa            linear   BCT 28-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Mycobacterium marinum].
ACCESSION   WP_273590532
VERSION     WP_273590532.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     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=43032
     Region          16..407
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mlntsrlnlh arverdsrla afrhygarme lpffrtvesa pgpttvvegq prvmfasnns
       61 lglggdprlv eaanratery gpscagappf cgtlqikvel eelladwygt eaalvynsgy
      121 ltnvgaltal lgvtdlafpd seahasiqdg irlsgassrf fahndldale rnlirtadrg
      181 gtklivvdgl ysmqgdiapm agiaalasky nvglfvdaah svgvfgsrrt giaeefgcak
      241 dvdvlmggms kaiastggyi vgsqdlidvl klhsnahift ataapaalaa saaaieiirg
      301 pegaqraaav lanaqalrdg lvahglqvrg givradgsga maphvsvwig resqaiaawn
      361 rafddgvfca lalppavgen ealmrcsvsa ghstaqiera veviaaavlg ardk
//
LOCUS       WP_273590803             438 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Mycobacterium marinum].
ACCESSION   WP_273590803
VERSION     WP_273590803.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 438)
  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..438
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..438
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47650
     Region          1..422
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mpprqaadpa avpalrrttl pgglrvvtey lpavrsasvg vwvgvgsrde gttvagaahf
       61 lehllfkstp trtavdiaqa mdavggelna ftakehtcyy ahvldndlel avelvadvvl
      121 ngrcaaddve lerdvvleei amrdddpeda ladmfltamy gdhpvgrpvi gstqsvsamt
      181 raqlhsfhmr rytpdrmvva vagnvdhnqv vglvrehfgp rlvrgrrpva prkgtgrvng
      241 tpqlvladre aeqthvslgv rtpgrgwehr walsvlhtal ggglssrlfq eiresrglay
      301 svysaldifa dsgalsvyaa clperfaevm rvtrevleav ardgitesec riakgslrgg
      361 lvlgledsss rmsrigrsel nygkhrtieh tlqqidrvtv devnalarrl lvkrygaavl
      421 gphtskrqlp qqlramvn
//
LOCUS       WP_273590836             417 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Mycobacterium marinum].
ACCESSION   WP_273590836
VERSION     WP_273590836.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (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 11445445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..417
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46346
     Region          177..383
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 makpagddaq vspgarqvnp lglgglgsvv tpfvhtgryf aeswrdyldq dsdglpiarp
       61 aialaaqafr deivlmglka rrpvsdphvf eriddevala lqfygdqgwl qrprtffadp
      121 pppsevtvrk vkgrkrsfyr mffdsgytpl pgepggqrwl gytannreya lllrhreprp
      181 wlvcvhgtem grapldlalf rswklhrelg lnivmpvlpm hgprardlpk gavypgedvl
      241 dnvhataqav wdirrliswi rmqepeslig inglslggyi aslvasledd ltcailgvpv
      301 adlvdllgrh sgfgrddprr etvalaepig hmisplaltp lvpragrfiy agvadqlvhp
      361 rrqvarlweh wgkpdivwyp gghtgffrsr pvqqfvedal qqsgllddps eqrdrpa
//
LOCUS       WP_273590898             453 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Mycobacterium
            marinum].
ACCESSION   WP_273590898
VERSION     WP_273590898.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 453)
  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 453)
  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 453)
  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 453)
  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 453)
  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..453
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..453
                     /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=50793
     Region          21..>222
                     /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          189..446
                     /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(191,193,195,202..204,206..207,295,315,317,319,321,
                     337,339,341,343,345,355..356,358,360,368,370,372,374,
                     392..396,400..401,404..406,409)
                     /site_type="active"
                     /note="hydrophobic ligand binding site [active]"
                     /db_xref="CDD:176854"
ORIGIN      
        1 mdaarhddve atltgavtfg vdayicadya raerdklwrk vwqqvgrved lpkvgsylty
       61 dilddsivvv rsaadtfkah hnvcmhrgrr lvdippgakn vcghkksfvc gfhgwtydqd
      121 gncihipekp dwqgaltpen thlaavnvdt wggwiwinmd paaqplrqyl epaatmldpf
      181 rlqdmrckwr kwltfqcnwk vameafnety hvatthpqfn kfgnfrgwaa ahgrhsnigy
      241 dapkdlaqtk skirlgtgad prvstaemqr ytleetnatt trtlvdaalr lveelpedap
      301 agqvldhwlt sarrddaarg vlwptidpeh laqsgtawqi fpnfqigqgl ttalcysarp
      361 hgydpdqcvf eascyelypk geepqtewvy appddpgwrs vlpqdfsnma avqqgmksgg
      421 fggpkpnpym erstanlhrn laeymgtgap rel
//
LOCUS       WP_273591107             621 aa            linear   BCT 28-DEC-2024
DEFINITION  AMP-dependent synthetase/ligase [Mycobacterium marinum].
ACCESSION   WP_273591107
VERSION     WP_273591107.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 621)
  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 621)
  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..621
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..621
                     /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=67178
     Region          18..613
                     /region_name="FAA1"
                     /note="Long-chain acyl-CoA synthetase (AMP-forming) [Lipid
                     transport and metabolism]; COG1022"
                     /db_xref="CDD:440645"
ORIGIN      
        1 mhptlaherp diakidnrpp svarmfldrv aaspsaeafr yphgddwesv tweqvgervg
       61 rlaaglislg iapqdrvala sstryewvlv dfavmcagaa tttvypttia advayivans
      121 gsrvvvaedq tqvdklvehr aelpevarvv vidgqgdgsw vitlaeleql gkqlladspa
      181 avdqrvaaig pdqlasliyt sgttgrpkgv rlthgawtyt asaidalnvl gpadlnflwl
      241 plahafgkvm lslplligfp taidgrvdri vdnlaelhpt vmgaaprife kaharieqmv
      301 aeqgglkkav fdwsigvglk vsasrqagrq pallsrlayq ladrlvfsti rerfggrirf
      361 fvsaaaaldr nvaqwfdaig itvlegyglt etaaasfinr pnayrfgtvg wpfpateaki
      421 atdgeillrg pglmtsyhdl peateealdh dgwfhtgdig eidadgylri tdrkkdmfkt
      481 sqgkyvapaa iqvrfkglcp yagelivvge akpycvalvs ldseaitewa aghglagksf
      541 aeltrdpktr eliagyidtl naelnrweqi kkfavldrel siesgdltps mklrrkvvld
      601 ksadeisaly qqpagqapks g
//
LOCUS       WP_273591112             283 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Mycobacterium marinum].
ACCESSION   WP_273591112
VERSION     WP_273591112.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (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   2  (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]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..283
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..283
                     /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=31070
     Region          <62..164
                     /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 mddvsqrpma aswrslnlan wesrvplhtg pngydldsfd dpdflsaevr ydlprlgrld
       61 gldiahlqch igtdtvslsr lgprstvgld fspaalqaar dlamraradv gfveadvyda
      121 vqalggerfd lvytglgalc wipsisrwad vvasllrpgg rlfmreghpf lwalsdprpd
      181 glvvveypyf etsgipfveh etyagngtva spqiihfnhg lgeiftalta aglmvtglee
      241 hhevpwnplg hamipspdyd gefilaedrd ripmtytvqa ikr
//
LOCUS       WP_273591166             363 aa            linear   BCT 28-DEC-2024
DEFINITION  metal-dependent hydrolase family protein [Mycobacterium marinum].
ACCESSION   WP_273591166
VERSION     WP_273591166.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans 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 10101344
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..363
                     /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=38843
     Region          34..342
                     /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(50,52,184,204,276)
                     /site_type="active"
                     /db_xref="CDD:238624"
ORIGIN      
        1 mrlhvrgrgl pdetavelwi vdghistepv sgadtvfdgg wilpglvdah chvglghqga
       61 ieldqaiaqa eaerdagall lrdcgaptdt rplddredlp riiragrhla rpkryipgfa
      121 aeledeselp aavaaqarrg dgwiklvgdw idrqigdlap lwsdevlkaa idaahangar
      181 vtahvfgeda lpglinagid ciehgtgltd dtislmrdhg talvptlinv enfpgiadsa
      241 vryptyaahm rdlyastypr vaaareagia iyagtdaggt iqhgriadev ealkkigmsa
      301 tealgaacwe arrwlgrptv ehgasadlvc faedprrgaa ilnrpdlvil rgrtyrpnql
      361 ghr
//
LOCUS       WP_273591265             407 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Mycobacterium marinum].
ACCESSION   WP_273591265
VERSION     WP_273591265.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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   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..407
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..407
                     /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=44376
     Region          93..378
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqrrnrragv edrwskavrl pdgttsivps ashgkgmrwr aryvdsdgre iakgfsrkvd
       61 aqkwldsvts tivtgtyiap gagnvtvgam reqwlgtfgh lkattkaare sawithvrdv
      121 wdtkqlcevq tsavrawvnd laaqgtsaat ietalgvlrm ilglavedrr iarnpcdgvk
      181 apprehsrra yltheqvdel aaalardglv vrflaytglr ygemaaltva dfdmlrrrih
      241 vrrsvtevkg klvwstpknh errsvpfprf lgedlarrma gkgredlvfa apgggvlria
      301 tfrtrvfnpa vaklrgigdd gkpttewprp tmhdlrhsaa slaisaganv kavqtmlghk
      361 saaltldtya dlfpddleav adaldaavqa lrkstadglr tdvpags
//
LOCUS       WP_273591075             612 aa            linear   BCT 28-DEC-2024
DEFINITION  PE family protein [Mycobacterium marinum].
ACCESSION   WP_273591075
VERSION     WP_273591075.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 612)
  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 612)
  AUTHORS   Wang,Q., Boshoff,H.I.M., Harrison,J.R., Ray,P.C., Green,S.R.,
            Wyatt,P.G. and Barry,C.E. 3rd.
  TITLE     PE/PPE proteins mediate nutrient transport across the outer
            membrane of Mycobacterium tuberculosis
  JOURNAL   Science 367 (6482), 1147-1151 (2020)
   PUBMED   32139546
REFERENCE   3  (residues 1 to 612)
  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 612)
  AUTHORS   Ates,L.S.
  TITLE     New insights into the mycobacterial PE and PPE proteins provide a
            framework for future research
  JOURNAL   Mol Microbiol 113 (1), 4-21 (2020)
   PUBMED   31661176
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Sampson,S.L.
  TITLE     Mycobacterial PE/PPE proteins at the host-pathogen interface
  JOURNAL   Clin Dev Immunol 2011, 497203 (2011)
   PUBMED   21318182
REFERENCE   6  (residues 1 to 612)
  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   7  (residues 1 to 612)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..612
                     /product="PE family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=63317
     Region          4..94
                     /region_name="PE"
                     /note="PE family; pfam00934"
                     /db_xref="CDD:425952"
     Region          179..398
                     /region_name="PE-PPE"
                     /note="PE-PPE domain; pfam08237"
                     /db_xref="CDD:369775"
     Region          <466..604
                     /region_name="ThrE"
                     /note="Putative threonine/serine exporter; cl46398"
                     /db_xref="CDD:480738"
ORIGIN      
        1 msfvvtapet vvaaasqltg igsaieaana aaaalttrll paaadevsag iaalmsthaq
       61 eyqllggqla tyhdqlvqal drtagwyada etgnaallrn vqqelltglt apgrawsgag
      121 aasagasgvd almssallsg grsvlvvgst gtprpsyrfm revydlfvap hyfgdslfgv
      181 qtpaqfqpft gipnltfdes aatgasylha aitqqladgn rvvvagfsqg asvatpemrh
      241 lqslpidsrp spedlsfvll gnpnnpnggi larfpglyiq svgltfngat pvteypttvy
      301 ttqydgfadf pryplnvvad vnallgisys hslyygltpd qvaagvvlpv sspdvnttyi
      361 lipnehlpll qplrgivpds vldgiepglr dvielgydrt gyadvptpas lfpanvnpnv
      421 vagafvegav rgidnglagm glpplpdlpa apllpeiwsn appipgwpas vpsaiavppq
      481 lggaiagpld hlyrtldsvi ngqinpaits giyqygadls aeaarhgass ellnaiyvgr
      541 qvlpiliegp gviltadtyy sinaikdlaa gnlsgfnqnl qlipatnaml ltfgatipia
      601 agvsayigrd fp
//
LOCUS       WP_273591393             253 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Mycobacterium marinum].
ACCESSION   WP_273591393
VERSION     WP_273591393.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 253)
  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..253
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..253
                     /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=25774
     Region          5..233
                     /region_name="HpcH"
                     /note="2-keto-3-deoxy-L-rhamnonate aldolase RhmA
                     [Carbohydrate transport and metabolism]; COG3836"
                     /db_xref="CDD:443047"
ORIGIN      
        1 mkvvsnlqqr lgrgtplwgg witgptwlgp eefaragydy vgfdtqhgyl ddadvagllr
       61 rlegapiatv vrlpnadpap igrvldagad aviiamiesa eqaaaavaat ryppagvrsy
      121 gplraslgtd paelqsragv yamvetaaal stiddicavd glagiyvgpa dlaislgtgv
      181 vgaldhpavr qavvgihraa saaslhtgih agaakagkam aqlgfeiitl aaesqalrrg
      241 ateylneata gtr
//
LOCUS       WP_273591391             501 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Mycobacterium marinum].
ACCESSION   WP_273591391
VERSION     WP_273591391.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     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=56041
     Region          1..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 mtsplsvgii gagpggmalg illknrgfen ftifdrendv ggtwrintyp glacdvkshl
       61 ysysfdlnpg wsrlwsgqpe ilayfqrcad ryglrphlrl gteirsarwe sqtrqwtlst
      121 adgeqhqfsv vvsavgifsr paypdlveqq rftgtvmhss rwdhsvplag ariavlgtgs
      181 taaqlvpela kvadrvysiq rsptwilpkp drpysrwerw vfahvpfaar lyrtrlwlrs
      241 esntsviehg spktkeftel alrmlentvs dpqlrrqltp dhpmgckrlv fssefltalt
      301 rpnvelvtsp arylrqrslv tadgaeydvd vvvcatgyaa adylgqlevl gedgaglhev
      361 wrdgahaylg mavpgfpnff mlygpntnvg snsvifmlea qaryivaala hlrrksktyi
      421 avrpgvlaef makvdrwmtg tvwttecsny frapngrvvt qwprsarsfw gmtrrfkpad
      481 fsfqpaavfa adggdrnagq r
//
LOCUS       WP_273591426             342 aa            linear   BCT 28-DEC-2024
DEFINITION  zinc-dependent alcohol dehydrogenase [Mycobacterium marinum].
ACCESSION   WP_273591426
VERSION     WP_273591426.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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 11437481
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..342
                     /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=36223
     Region          1..324
                     /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 mrsltfvapg tlrfdevdap tildpgdalv rplaattcdl dhhviadktp fsmaapfalg
       61 hecvgtvvev gsectdfaig dvvgvawhia cgtcaqcrin hparclrygd aqyglpvngl
      121 wggtfselir vpfadynlap lpagvdpvhl asigdnlalg wevvvptvae iadprvavfg
      181 gtgsiglycv daavhcagah tvyydddpvr mavaeqlgae vadingkrek nfdlavdasa
      241 dperlkmalr svvpeghvns vgiyfqdval pmlqlymrgv hfhngkghar psmtptldav
      301 aanvlhpqlv tsgiygwdem pevltskqag hkpifvldas gh
//
LOCUS       WP_273591436             366 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Mycobacterium marinum].
ACCESSION   WP_273591436
VERSION     WP_273591436.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans 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..366
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     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=38357
     Region          16..356
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mrctdvgvvg agivglatay alslggisvt vyergvpghg qsggesrifr hahddarmva
       61 lakrsrliwd ewgrrlgvel lcsdgvvaig pvaerrlgvl eavgdcparr igtdelhrrl
      121 piyadfdgva vlderggair ttraisalta sladrlvtde vllvrttsag tvevrtggav
      181 aehgrlvvca grgtaalarg vglalpvreg ahvrltyrvr geppprlacl qdgatgfget
      241 giyaaaeagn rryavglney vdapggglla paalarlger anayveralp gldpapvdir
      301 hcwvtelpwg sdgvgvwqrd eiffiaghnl fkhapalgse laaaaggdhl fddlrpeaql
      361 gsrspq
//
LOCUS       WP_273591446             300 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Mycobacterium
            marinum].
ACCESSION   WP_273591446
VERSION     WP_273591446.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 300)
  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 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   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..300
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..300
                     /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=32258
     Region          5..293
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mrdskilitg vtgqvaspva ralaganevw giarftdata radleqvgir cqavnlaagd
       61 fteipsdfdy vlnfavaksg nwdkdlaana esvgllmahc raakaflhcs saavydppdn
      121 elrtenaalg dnhkflfpty siskiagevv vrsmarvlel patiarlnvp ygnnggwpff
      181 hmemmlagip ipvprggpar ynpiheddii atipklfaaa svpattvnwa gdqivslqdw
      241 cgylgtligk epvfqesdsa lrpnpvdvtr mheligntav dwhdgmrrlv akfhpeapgl
//
LOCUS       WP_273591380             591 aa            linear   BCT 28-DEC-2024
DEFINITION  type I polyketide synthase [Mycobacterium marinum].
ACCESSION   WP_273591380
VERSION     WP_273591380.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 591)
  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 591)
  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 591)
  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 591)
  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 10172632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..591
                     /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]"
                     /calculated_mol_wt=62733
     Region          <2..229
                     /region_name="KR_3_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 3, complex (x); cd08956"
                     /db_xref="CDD:187659"
     Site            order(14..17,42..45,69..71,92..93,115..116,130,157..158)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187659"
     Site            order(93,117,130,134)
                     /site_type="active"
                     /db_xref="CDD:187659"
     Region          248..333
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
ORIGIN      
        1 miarygarhl llvsrsgpda pgaddlyqrl tqlgaqitit acdasdptal aallgsippq
       61 hplrvvihta avlhdavlte lnpdqldkvl aakadaawhl hqltadadld afvlfssaag
      121 ilgaqgqany aaanafldal ayrrcrdhlp atslawgywq nsgiaahldt ldqarltrnl
      181 ipittehgla lfdaalvsqq phlvpaplnt rtlarharqg slpailsalt ttrrqaatts
      241 iaalatqlag etpqqqlatl ttlvtrvtat alahpdptai dpdlpfkdlg vdslsalelr
      301 ngltreigra lpatlifdhp tpaavayhlq sqligdtaal gpigqllqai cdadlrltli
      361 evvlalsgld ssfisnfgss rnpqattlrs aenvalrlvc isefegqykr fayglpesie
      421 vievlapgfs gtvlptsvqe sgemiidalq rndsygrdav ivghgitcia aihalelmda
      481 slspltksqt alvaispiaa idalsisedp falatfsthl rneqdliafg rylnfglhsn
      541 dkldeersli ltphirghqv gaaesplale patvalriln wltdnnmlds a
//
LOCUS       WP_273591517             414 aa            linear   BCT 28-DEC-2024
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Mycobacterium marinum].
ACCESSION   WP_273591517
VERSION     WP_273591517.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     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=43134
     Region          16..407
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mlntsrlnlh arverdsrla afrhygarme lpffrtvesa pgpttvvegq prvmfasnns
       61 lglggdprlv eaanratery gpscagappf cgtlqikvel eelladwygt eaalvynsgy
      121 ltnvgaltal lgvtdlafpd seahasiqdg irlsgassrf fahndldale rnlirtadrg
      181 gtklivvdgl ysmqgdiapm agiaalasky nvglfvdeah svgvfgsrrt giaeefgcak
      241 dvdvlmggms kaiastggyi vgsqdlidvl kvhsnahift ataapaalaa saaaieiirg
      301 pegaqraaav lanaqalrdg lvahglqvrg givradgsga maphvsvwig resqaiaawn
      361 rafddgvfca lalppavgen ealmrcsvsa dhstaqiera veviaaavlg ardk
//
LOCUS       WP_273591654             224 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Mycobacterium
            marinum].
ACCESSION   WP_273591654
VERSION     WP_273591654.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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   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 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 10004391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..224
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=24866
     Region          1..103
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mstysqfcpv akamellder wtllvvrell lgsthfndlr rgvpkmspal lskrlksltk
       61 agvversdie grtsyslttc grelatvvaa lgewgirwip elgdedldph llmwdirrtv
      121 pidawprart vlafrlagva pkaarwwllv segeadmcdf dpgyqvaatv etslltltql
      181 wrgdqswsra mlnggvridg paqvrrsvpt wlgqsrlaav prpa
//
LOCUS       WP_273591656             374 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Mycobacterium marinum].
ACCESSION   WP_273591656
VERSION     WP_273591656.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans 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..374
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     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=40108
     Region          6..349
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtakqhvcvv gagifgvsta lslardgwrv dlverssdil tgasgcnifr lhrgyhyprs
       61 latavesrds ersfraeynq aiidgthhmy avaaegslvt gaefmahcaa anlpveptsh
      121 pavkqsavql lvsakesrid pnrlaltars kllsagvnvr thtpadpkiq drydfvvlaa
      181 nhgnnsllae fgipvqrrqf evcevavleg vesgdidivv idgpfvslsp ygrntgqfll
      241 ydvehsvrhr tvatvfepps dtsaplatga pvpmpdsavt amldsasrfv rglrharhvg
      301 sllsvrtvlp dvdgtderpt likwhtdttl sifsgkivta vaagqavaes lrsrnkpgll
      361 kgtrrihset gldp
//
LOCUS       WP_273591701             386 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Caballeronia
            novacaledonica].
ACCESSION   WP_273591701
VERSION     WP_273591701.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia novacaledonica
  ORGANISM  Caballeronia novacaledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
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="Caballeronia novacaledonica"
                     /db_xref="taxon:1544861"
     Protein         1..386
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40795
     Region          1..379
                     /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 mgvlsgirvl efeaigpgpf gamlladmga dvlridrpla pqdlgpktng kradvtgrgr
       61 rsvtldlkep raaeaaldlm aradvviegf rpgtmerlgl gpqaalarnp rlvygrmtgw
      121 gktgplaqra ghdlnyials gvlsgigrad gppvpplnlv gdyggggmll algvvaalfn
      181 vqrggegqvv daamiegaaq lgsviwglla sgnwreeres nlldggtpwy dsyrtrdggy
      241 msvgavearf yaeflsklgl adaglpaqhd rsgwpvlrer faaafltrtr dewcavfegs
      301 dacvapvlsf seapahpqhr argsfvevag vvqpapaprf satpstiakp apqrgehgla
      361 alrdwgfdea avermrehgl gykpea
//
LOCUS       WP_273591721             999 aa            linear   BCT 28-DEC-2024
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Caballeronia novacaledonica].
ACCESSION   WP_273591721
VERSION     WP_273591721.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia novacaledonica
  ORGANISM  Caballeronia novacaledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 999)
  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
REFERENCE   2  (residues 1 to 999)
  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 11445956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Caballeronia novacaledonica"
                     /db_xref="taxon:1544861"
     Protein         1..999
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=106345
     Region          10..805
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          834..977
                     /region_name="CoxG"
                     /note="Carbon monoxide dehydrogenase subunit G (CoxG);
                     cd05018"
                     /db_xref="CDD:176853"
     Site            order(836,838,840,849..851,853..854,859,863,869,875,877,
                     879,881,883,888,892,896..898,901,907,909,911,922..924,926,
                     928,937,939,941,943,957..961,963..965,967..969,972)
                     /site_type="other"
                     /note="putative hydrophobic ligand binding site [chemical
                     binding]"
                     /db_xref="CDD:176853"
ORIGIN      
        1 masgrdeaqa strpfvgrpm qrledpailt grgcygddia iktgtlhaav lrspyahaei
       61 rsidvsaala hkgiravltr ddvrawsqpf vvgvkspmeh walamdrary sgepvavvig
      121 etraiaedgl dlvkvdyvpl ppvvsieaav addapvlhek igsnvvsdrs frygepeaaf
      181 dnaphrvsit thyprntcap iecgvviaec lpgnegydvt snfmgpfslh avmsmalkvp
      241 anrlrhkapr dsggsfgvkq avfpyvvlmc lasrkcgapv kwvedrlehl saatsatarl
      301 atleaaverd gritalsydq iedcggylra pepatfyrmh gcltgaydia nllvrnrval
      361 ttktptglvr gfggpqvyfs lerliqriae elkldvldvy rrnfvradaf pyraaagall
      421 dsgnyqealr ralaqgghde lkarreiars egrlygigfa aivepsvsnm gyittvmpae
      481 arrkagpksg aiasatvsvd lmggvivtia stpagqghmt vcaqvvadvl gldpadivvn
      541 vefdtqkdaw svaagnyssr fagavagtvh laatrvkdkl arilakqfsc teqdvcfegg
      601 rvymrqapek alpfaraasn aphwspallp egeepglret vfwnppnmtp pddedrints
      661 acygfafdmc gveidratgr vridryvtah dagtllnpal adgqirgafa qglgaalmee
      721 frygadgsfq sgtladylmp ttcevpdpii vhletpspft plgakglgeg nnmstppcia
      781 navadalgva dlrlpltpak vmamigiddp ppsrpeyrea apakkpvsgg gkaltaqgtv
      841 eleatpeaif avlmnpeala kvvpgchale tigpnqyrad vtvgvgmika rfeakiglsd
      901 idaprslrla gagisplgsa qgeglvrlep takgtllayd yeaqvsgkva avgarmlega
      961 aqvvlrqlfe slgrqasgkd vranaswlgr mlaklrrst
//
LOCUS       WP_273591867             903 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Mycobacterium marinum].
ACCESSION   WP_273591867
VERSION     WP_273591867.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 903)
  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..903
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..903
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=97482
     Region          80..903
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mfeveppsvw hsalvaadlg gppsgivtfl ftdvegstrr wesdpdrmra alaahdaalk
       61 rtiqthrgwl fkhtgdgvca afasprsavd aavdaqrale lpvrmglatg eaephdadyf
      121 gavlnraarv matghggqil ltdstanlis gvdlldlgsr rlrdlpapvr vfqvrapglr
      181 tdfpalrapd ttpgnlrpal tsfvareaei gqvqtalqvh rlvtltgvgg vgktrlalev
      241 atrvadefpd gvwlfelaav sdpaavpdav aavlgitqqa gktvtqsvat alegrvrllv
      301 fdncehvrda aadlieaila gsttvrilat srerlevpde qlwsvpsldv gggvvsaagt
      361 lfveraqsva pgfaptdaqd aaaiaeicrr ldgiplaiel aasrmasmtp ievrdrldhr
      421 frllvgsrrg lgrhqtlrha vawsydhlsd aekvllercs vfaggfdlqs acavagsadt
      481 hddyevldll dalvgkslli vdrlsgrsrf smletirefa eeqlvtrgqa laartaharh
      541 faqrlpdvaa vwdsprqpea ytwltaelan lrlafrwtad nndlddaasi atwvgflgff
      601 vnrfepltwv eeaieravdh pklaflhvla sqcymtgrvq eairyadeaa rllatdryev
      661 pfgiegwpsg aytssghpeq svelcrtqla lghdthtltl gclvlaltik gqcdeaeqla
      721 daliesaeat rnpaalcyal laygftfrdt npasalaamr rglriaqdtg nrnsethlaa
      781 vlcrveakyg dplsaldyft laihnhheag nttlistpla vlaaffdrlg ryeaaatiag
      841 fafhpiteas fpelrttish lrdalgdhay esfsrsgaam ttaamatyay hqidhartel
      901 qar
//
LOCUS       WP_273591986             432 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Mycobacterium marinum].
ACCESSION   WP_273591986
VERSION     WP_273591986.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans 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 12026591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..432
                     /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=45923
     Region          22..329
                     /region_name="Acyl_transf_3"
                     /note="Acyltransferase family; pfam01757"
                     /db_xref="CDD:426413"
ORIGIN      
        1 mtsltgfpsp aelaertpad rdraidviri talvgvvvgh tvmatsvirg gvlrwdnllt
       61 tsttfqaltw ifqimplfff agaaacvpsw rpgtnwggwl mkraarlfrp vfyylsfwav
      121 alvifypllp qhvyepvagv siqllwflga yvlvlaampv lsritstarl aagvtavyam
      181 iaavdavrlh cnaapslgyl nlavwlipam fgvayrrrll traraigtaa illatnvall
      241 cwgpyelslv giegqrlpnm sppslllagh aiilsalavv aapaiarwar rprvwwlaai
      301 gnsgamtlyl whmpallgvh llfdglgapr ypgepgfavi saaqllimcg avaalfgalr
      361 plennplpgw dgapaitsvw rgagvgvllc vagaailasv kwglkddgla ciavtvaalv
      421 aarilavarl pr
//
LOCUS       WP_273592090             489 aa            linear   BCT 28-DEC-2024
DEFINITION  flavin-containing monooxygenase [Mycobacterium marinum].
ACCESSION   WP_273592090
VERSION     WP_273592090.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
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="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     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=54812
     Region          1..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 mtrrdpsvai vgagmagicm aitllnsgit dvtiyekade vggtwrenty pglvcdvpsr
       61 lyqysfaknp dwsnlfspgg eiqsyfcgia dryrlrdrir fgteivsarf eddhwsvvtd
      121 sgeetavdfl ivatgllhhp rvpaiagldd fggsafhsar wdhrvavqgr rvavigsgst
      181 gvqlvsalag vaakvtmfqr tpqwilpwpn rqyskvsrac yrgapwlesl aykiwgrafe
      241 qftaaltrpg whrrvtgmtc raslrlvrdp hlrqaltpdy qpmckrlvms sgfyraiqrd
      301 dvelvttgid rienagivtd dgvlrevdvi vlatgfdsha ffrpmkligr dgveidelwr
      361 ggpyayqtva mpgfpnffmm lgphspvgny pltgiaesqa dhilrwiqrw rssefdtvep
      421 tswatdefna klrsampktv wttgcsswyl nddgvpevwp fapaehraml anpdldqyhl
      481 rrrpevlaw
//
LOCUS       WP_273591692             549 aa            linear   BCT 28-DEC-2024
DEFINITION  PE family protein [Mycobacterium marinum].
ACCESSION   WP_273591692
VERSION     WP_273591692.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 549)
  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 549)
  AUTHORS   Wang,Q., Boshoff,H.I.M., Harrison,J.R., Ray,P.C., Green,S.R.,
            Wyatt,P.G. and Barry,C.E. 3rd.
  TITLE     PE/PPE proteins mediate nutrient transport across the outer
            membrane of Mycobacterium tuberculosis
  JOURNAL   Science 367 (6482), 1147-1151 (2020)
   PUBMED   32139546
REFERENCE   3  (residues 1 to 549)
  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 549)
  AUTHORS   Ates,L.S.
  TITLE     New insights into the mycobacterial PE and PPE proteins provide a
            framework for future research
  JOURNAL   Mol Microbiol 113 (1), 4-21 (2020)
   PUBMED   31661176
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Sampson,S.L.
  TITLE     Mycobacterial PE/PPE proteins at the host-pathogen interface
  JOURNAL   Clin Dev Immunol 2011, 497203 (2011)
   PUBMED   21318182
REFERENCE   6  (residues 1 to 549)
  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   7  (residues 1 to 549)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469623
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..549
                     /product="PE family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=56326
     Region          4..88
                     /region_name="PE"
                     /note="PE family; pfam00934"
                     /db_xref="CDD:425952"
     Region          157..379
                     /region_name="PE-PPE"
                     /note="PE-PPE domain; pfam08237"
                     /db_xref="CDD:369775"
ORIGIN      
        1 maflvaepqv mataagqvee igsaigvane faagsisgva aaagdevsaa iasffaahgq
       61 ayqtmagqva afhtefqqal aqagnayvqa eaagaaalag algvpvtsaa apaatippfp
      121 anlttlvmgg tgipipgpgf inlanelyvr sanallglnt peelypltgt ksltldasvs
      181 egltildnai meqlaipgnt vtvfgvsqsa viaslemqkl aalgpaapta sqlnfvllgn
      241 emnpngglla rfpdlsipsl gltfyggtps dtiyptanyt leydgfadfp ryplnfisdl
      301 navmgivyvh pnyldltqaq vdnaiplats pgysgvtsyy ilptenlpll eplraipvig
      361 nplanliqpd lkvlvnlgyg dpaygystsp adittpfglf pdvpphviad alvagtkqgi
      421 sdfsadiqqm fsqpatlpsp pmlqapdlma alaaaptpve vvntltkivs ddyatllpla
      481 digtafvitm ptydatlfvd qllqgnlina fgypiaadvg ltaisggvva lvaigtlqsn
      541 irdlqslfp
//
LOCUS       WP_273592071             743 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Mycobacterium
            marinum].
ACCESSION   WP_273592071
VERSION     WP_273592071.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans 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 the amino end.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         <1..743
                     /product="beta strand repeat-containing protein"
     Region          15..>731
                     /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 svstvlfgen ntasasaiga gnianvatvl fsdsntstvs sfgveniatv atsygdfnnv
       61 sastpgiggn iatfatafge gntnvhaeag pgganiatla tvfgdgnavs vksigagnta
      121 siatmignnn tadinvfgle nvatvataig dnngltanap glganiatva taigsgnsqv
      181 saeaggaggn iatlssvfgd sntavvtafg agnvptaatv fgsgngvkvn sfgleniatl
      241 gtvfgdnntg vvadaggvgg niatlanvig dgntaaaasa vgtgniatla nvfgdanaat
      301 agsigvgnvp taatvfgsgn gvkvstfgle niatlgtvig dnntgvvada ggvggniatl
      361 anvigndnta aeatasgvgg niatlanvfg dgnavkanvv gfgnvpsaat vigsnntvtt
      421 dvfgveniat lasvygdgns gvlaqsggvg gniatlatvi gsnntateas avgiggniat
      481 lgtalsdgna vsatangfgn tatvatafig ggntatasas gvgniaslat avgadnavsa
      541 tasgaggnia iaataigdgn tevtadaggl ggnigvaata igggntvaas stgltigsva
      601 tavgdgntgi aarghqagnl givstaigfg ntdvaaagfg vanignvatv igsnnqnvfa
      661 ggtglsniat vggdnntala gdqsgglasv nvatvfgsgs gasafngfln laigltdgvm
      721 asagpgnfnv siqpffdvqp lfg
//
LOCUS       WP_273592360             571 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273592360
VERSION     WP_273592360.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 571)
  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 571)
  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 571)
  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..571
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..571
                     /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=66983
     Region          7..475
                     /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(60,63,100,103,144,163,167,199,256,417)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(199,256,332)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          482..>536
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mirkwwkena iyqiyprsfk dsngdgigdf qgiiskldyl qelgigaiwl cpiyespnfd
       61 ngydisdfqa imkdfgtmqd fdefmreahe rgikvvldmv lnhtsdkhdw fvesrssidn
      121 pkrdyyiwrk gknggypnnw esyfsgsvwe ydqeteeyym hlyarqqpdl nwenkevvne
      181 lhdmirwwmd kgvdgfrlda iahivkavgl pdadnpqnlp vvqafqffsn lekvhtllkd
      241 lnqqvfatrd lmtvgetsgl gpeqaleyvg nerheldmvf qfehmhldcv gtgsskwvgr
      301 swnlldikki mshwqtvlhg kgwnanyfsn hdqprhlsrf gntgeyrkqs akmlatlihl
      361 lqgtpyiyqg eeigmtnasf ehiedyrdve tinyynislk egktekeilq nlarrsrdna
      421 rtpmqwddtt hagftdgnpw iqvnsnytdi nveqalndpd sifyyyknli alrkkypvvi
      481 ygdyrllcal hhqvysfirs yegtelmvim nffddeptfe lserisdegw elvlsnydeh
      541 ehhhlhslpl rpyetrvyyk dtpsvlpkaa q
//
LOCUS       WP_273592179             437 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase, partial [Mycobacterium marinum].
ACCESSION   WP_273592179
VERSION     WP_273592179.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 437)
  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 437)
  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 437)
  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 437)
  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 437)
  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 10347224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         <1..>437
                     /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]"
     Region          <7..314
                     /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(19..20,69,71..72,75,89..90,109..114,201,213,216,
                     224..227,288)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(19,71..72,75,89,224..226,282,288)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(89..90,109..114,201,213,216,227,307)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Region          328..400
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
     Region          421..>437
                     /region_name="C_NRPS-like"
                     /note="Condensation domain of nonribosomal peptide
                     synthetases (NRPSs); cl40425"
                     /db_xref="CDD:394795"
ORIGIN      
        1 lltqldldip tggvwsqwhs yafdvsvwei lgallgggrv vvvpehivts pedfhallid
       61 ehvsvlthtp salaqlpdhg leattvitvg escpidlahh watehtllna ygpsettmct
      121 tisnplhpad tvvpigapvs gagvfvldgw lrpvppgtvg elyvagtgvg vgywrrggls
      181 atrfvacpfg atgsrmyrtg dlvcwgpdgq lqylgradeq vkirgyriec gevtaalttl
      241 dgveqavvia redtpgqprl vayyttttgt gldttdiras lsqllppymv paafieidql
      301 pltvngkldr ralpapdytt tsaqtylapq gptektlanl ytqilgvdri satdsffdlg
      361 gdslsamrli aatnttlhtg lrvadvfeap titalahria ttttttqavp aliagerpal
      421 vplsfaqsrl wfleqlq
//
LOCUS       WP_273592413             393 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus sp. PK4536].
ACCESSION   WP_273592413
VERSION     WP_273592413.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 393)
  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 393)
  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..393
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..393
                     /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=44998
     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 mdslqrlitq cieagelita tlsqlrkkdn dsftkviikp velkkqlhyq fayhysnkvt
       61 hdnvlpteai qvlftllqet mrqgllctqe adyqvliskk ykvsiltktp tkmstdlshn
      121 rkkqyiledg epvpflielg imnadgkvla rkydkfrqin rflemvqdvl pslpvnkelt
      181 ivdfgcgksy ltfalyhyln iqqhrplniv gldlkadvie hcsqlaeklh ydqlkflvgd
      241 iadyneleqv dmvvtlhacd tatdaaleka vrwnasvils vpccqhelfn qiqndtmspl
      301 lshgilkerf salatdalra klldllgykt qllefidmeh tpknilirav kaeneqnaem
      361 wqeytafrdm iqakpylena ckdllqsyqk slv
//
LOCUS       WP_273592410             164 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus sp. PK4536].
ACCESSION   WP_273592410
VERSION     WP_273592410.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=18740
     Region          65..151
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 miqkciledd htvqqiwalq hiayrleaql igfkelppll dtvetirrcr etfyayvney
       61 eeiqgvisie reehdtltia rmmvhpsafr qgiasqlieh vfaeypdvpl yivstgqlnq
      121 pavslykkyg fypietfeva agvklttfhr pnpalartge dsid
//
LOCUS       WP_273592433             504 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. PK4536].
ACCESSION   WP_273592433
VERSION     WP_273592433.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 504)
  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 504)
  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..504
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..504
                     /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=56010
     Region          166..504
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mkniysqlvl tfiavvvasf vitllmsdwv fqrqqvnfve driltdaksm aeiqssipkn
       61 miqkyldsqg gqmqivviga dgttyrsigd gpggppglsp ppvpptppds ttdtdtsdhs
      121 skpklklpad plnqwnipet ikqevlngqi yhptaipttn tevpsfnlsl fntkdekepr
      181 yvgvpferdg qnyalfarpa pghfvnqfnr wmilvlsvml vigvvlflfa arliakpiak
      241 lseatrrvak gdyqvrvnlr rkdeigelsr nfnrmigels kieamrqefv snvsheiqtp
      301 ltsirgfaga lrdsaspeqv rhltiieqes erlsklssnl lklasldvvk lhmvpfrlde
      361 qirmsvascv plwteknidl sadldkitfn gdedllsqvw inllsnaikf tpeqgniymt
      421 ltqdqqwikv svqdtgcgit pehlehifdr fykvdtsrts vtggnglgls ivqkiiglhg
      481 griegnsedg qgttmtvflp ltht
//
LOCUS       WP_273592593             226 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp. PK4536].
ACCESSION   WP_273592593
VERSION     WP_273592593.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=25143
     Region          5..89
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 msinpniaev asllaepsra tiltslmdgr fhtaselalm tgitpqtasf hlskliegrl
       61 itfekhgrhr yyqlanqdia silesfltls sppevrslrq ssqvqslrea rtcydhlagk
      121 lgvdltdaml anqyittget efivtakgev ffahfgldly mlkrkrrafs hacldwserr
      181 hhlagalgqg lmhqlfdlgw ivrvpsirav qvteqgaqgf ksvfdl
//
LOCUS       WP_273592606             461 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273592606
VERSION     WP_273592606.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 461)
  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 461)
  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 461)
  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..461
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..461
                     /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=53158
     Region          128..>231
                     /region_name="SIR2_2"
                     /note="SIR2-like domain; pfam13289"
                     /db_xref="CDD:433090"
ORIGIN      
        1 mivivdlfys lelesqedin spnwvglley linlnpekqy pigyytqqyt enlpkvgski
       61 veeyhnyawk nhkndifpkk lfegnyprsi flkyqissyl eqlseafvvk dhykqeelea
      121 lmkitphaii ttnydlllek lfpnhnpiig qqvirsresa nyghllkihg cittpkeiii
      181 ssedydlfme kqkyliakll tyfmeypiif igyalndeni ksiladvsei ivsdddepvs
      241 niwfidwqqd pisetmkpas dklidlnngk sirinyllvn dftnvyeslh qninepvdii
      301 rnlenniyni iksktvtnle anlldfksig dmgqlasklg fesidgsdnt tkinvvgagg
      361 vtdpeqlvll ypyslsdigk lmgykgwhsv kkfmgeiknd tgydiqqdnn lyhldreqgs
      421 greanhrysk lalelfelvr dkskyeirdy sgnvlytgne l
//
LOCUS       WP_273592639             165 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273592639
VERSION     WP_273592639.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 165)
  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 165)
  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 165)
  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 165)
  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..165
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..165
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19743
     Region          51..161
                     /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 mknslliflg iiliislffs vyfynenikl kknmidlkes isntynylds itvtnfekkv
       61 vnkekfivyi grpdcndclf fepmfekfvy andlnnkivy lnirdyraen ekrwnefkrk
      121 ygfqqtpaii yfedgknknv iewsnekglp iddlkkwlkn nklik
//
LOCUS       WP_273592678             317 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            sp. PK4536].
ACCESSION   WP_273592678
VERSION     WP_273592678.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=36196
     Region          23..307
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mltskgeysf stcwnikrhs sgaemiaeiq elgfqqveln ynvttemlkt iepmiergmi
       61 gissvhntfp htpdpdygtd svllgfddev krqkaidllv gsaeyahryg akavvvhpge
      121 ipfannidet lkgiyheqgk dspayqqlws emierresls ehyleriqhs leevcdrvls
      181 kgynvafgie trsrcyqmpt laeakkvrer mkgapvylwy dighgmmmdr mglyqnaeea
      241 namkddiigv hihetlglsd hwcpyihgkd mtffdrfldi idaapvkvye lkaacqpeei
      301 eashqllisk iqerhhk
//
LOCUS       WP_273592769             331 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus sp. PK4536].
ACCESSION   WP_273592769
VERSION     WP_273592769.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 331)
  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 331)
  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 331)
  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 331)
  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 331)
  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 331)
  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..331
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..331
                     /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=39053
     Region          <116..325
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mklflkehll liiiqiiqfs avmgiywldg yrhtgpalys imlglfllsg ylgyqyysrr
       61 qyyrrlqepl lslddsiqrl dqapvaeale qllrqqyryy qqqlatiqqq qqqhltfmnq
      121 wvhqmktpls vieltvqdid epefasiree lermssglnt ilymarlrtf eqdfhirmis
      181 lsevirevvq ehkrlfirnq vypdvqikdg dlwtesdqkw lffmlsqlvi navkysahth
      241 hkvmissyir hqqavievkd qgvgipasdi krvfepfftg engrrfrest gmglyltrea
      301 aqrlnhqlel estvdagttv riifpsyqrk h
//
LOCUS       WP_273592810             295 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273592810
VERSION     WP_273592810.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            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 11446635
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=31719
     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 mkatiiinps sgkeqaleyv kkaedilseq gyhvavneta keldatqfct dackechdlv
       61 vsiggdgtlh etinglmdqe hrpklavipl gtvndfaral qiplnpdqai etlrssnvkt
      121 vdmgqlndql fanviaagsl aealssvpse dksklgafay frdgmkelms nsasplkiey
      181 dgevwegeap lflaaltnsv ggfesmvpda evddgllhcf imtnlnmfnt ltaglslllg
      241 nlkghkdviy ftakhvrvss tepvktnvdg eegpslpvdl riipghirvv vpeea
//
LOCUS       WP_273592791             313 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273592791
VERSION     WP_273592791.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=36067
     Region          1..312
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mkidrllait vlllnrqris akelaarfev stktiyrdid tlsqagipiv ahqgttggfe
       61 imeqytiarq fltlseidam isavkgmttv fndqmfatll dkvqallrpt drmqtpiqha
      121 givfdfnpwg qnpatrdkvn llreaitnty kvhlhylntn gieseravep salilkgyvw
      181 ylhayctlre efrlfrlsri lelectqdsf npraipdwdq yqwnnsntye eqrqnvtllf
      241 gaqvryrlnd mfdpdwislq sdgrievqga fiiddwfynm llsfgdqvri qtpaelipel
      301 igraqkvids ysn
//
LOCUS       WP_273592833             123 aa            linear   BCT 28-DEC-2024
DEFINITION  DMT family transporter [Paenibacillus sp. PK4536].
ACCESSION   WP_273592833
VERSION     WP_273592833.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 123)
  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..123
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..123
                     /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=12916
     Region          2..106
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 maylflaisi igeligtsml kasegftkly ptlltivafv isfyfvsltl ktlplnmtya
       61 iwsgvgavat alisvliwke kintgsmvgi alivvgvvvl nlfgaghgea kestettssi
      121 aqk
//
LOCUS       WP_273593118             330 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Paenibacillus
            sp. PK4536].
ACCESSION   WP_273593118
VERSION     WP_273593118.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=36388
     Region          3..329
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtralitgat gflgghlarr lvalgwdvhg tgrdesrgqa lerigvqmny ydlgdaeqai
       61 eackgqdivf hcaalsspwg kyqqfyqsnv katqhivdgc irhdvqrlih vstpsiyfdg
      121 kahygiresd plprksvnhy aatkllaeqi vlqaykkqgl asimirprai fgpmdqtlfp
      181 rllevnrqsg vpllqggrap idltyvdnvv damllgakap qtalgqayni snsepiafve
      241 llsrlferld iplhtrnvpy svahliaggm eavyrlfpal geppltrysv gsiavphtld
      301 islaqqklgy mprisvdqgl erfadwwcaq
//
LOCUS       WP_273593237             239 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase [Paenibacillus sp. PK4536].
ACCESSION   WP_273593237
VERSION     WP_273593237.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..239
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26637
     Region          18..226
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 mtsehlnhps splwqdppiq afifdmdgvl idsepiyfei ekssfqhlga tveetehhty
       61 vgvtlesmfq qvldkhqldh vlaevlafhk envmkvmqgh eelqafdhve qwiqwlsnsg
      121 iklavasssp rslieliler tglrpfftvm vsgeevahgk papdiflhaa ellqvdpqhc
      181 vviedsrngv qaakdagmrc ighqnpgsgn qdlskadiii hsyaellelr dslhigvrs
//
LOCUS       WP_273593366             305 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Paenibacillus sp. PK4536].
ACCESSION   WP_273593366
VERSION     WP_273593366.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 305)
  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 305)
  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 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   5  (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
REFERENCE   6  (residues 1 to 305)
  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 305)
  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..305
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..305
                     /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=34675
     Region          3..305
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mgkksislmk fikrdkylli mfapvfvyyv ifmyipmpgv liafknftpg hgifggdwvg
       61 lqwfaqfvhs iyfwrllrnt fllaflpllf gfgipilfav civeiknqvf krfaqtityl
      121 phfistvvva gmlinflspa dgivntllar fgmekvnfmm eagwfrtift sseiwqsfgf
      181 ssiiyiaaim sidpemydsg kidgvskfqe lwhltlpsik ptivilllls lggimsvgfe
      241 kvyllyngat yetadvlsty vyrmgiegqn ygfatavglf nsiitfvlvf tvnritrrmt
      301 nmslw
//
LOCUS       WP_273593574             227 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein [Paenibacillus
            sp. PK4536].
ACCESSION   WP_273593574
VERSION     WP_273593574.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=25996
     Region          1..171
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mitvtaihlp dllsledmev lrrnvspark easlkfvrqq daqrgligel lvlhrlrthy
       61 qlqdhqiqfe qnkygkpylh nqpdihfnvs hagewivcad gnvpvgidie qirpidfgia
      121 qrfytepeyq llmnapeseq lttfyalwtl kesyikfvgk glslpldsfs vlqndnheyq
      181 visakpidma sffrhlpids kyqlavcage plsllpliml dwtelip
//
LOCUS       WP_273593086             219 aa            linear   BCT 28-DEC-2024
DEFINITION  endonuclease III domain-containing protein [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273593086
VERSION     WP_273593086.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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   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..219
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..219
                     /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=24872
     Region          34..214
                     /region_name="Nth"
                     /note="Endonuclease III [Replication, recombination and
                     repair]; COG0177"
                     /db_xref="CDD:439947"
ORIGIN      
        1 mnktkivqmy kilshtqptf eetdndwith glnstpfkll vsvaistmth dkrtvkacia
       61 lyekistpqe lieledeela tlikpaahyn rktkslkkmc hqlieqydge vpqtkeelme
      121 lsgigrkcad immhfsvgep siavdthvhr vlnrlgvvnt rsseetadvi ntitpqkykq
      181 hahewlighg meickarapk ckecalrdwc qynqtraig
//
LOCUS       WP_273593677             310 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273593677
VERSION     WP_273593677.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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   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 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
REFERENCE   4  (residues 1 to 310)
  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..310
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..310
                     /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=35786
     Region          40..292
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          207..290
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mikeqlreel kenrihgslm ypvsvypmdd ieeetvlech wheepelilv tkgralfqig
       61 tipyevhage avfvnsgeih tayqmehesc sfvatvfsms llnsagydmi qarfidpllr
      121 kqmvlpvhir gqevweqevl tllnqivdin kqqtvtcelt tkaylylifa qmiehmdtqv
      181 alipapsdkv qrlktvlghi hdnyqqplrl relaeqinms eghfcrffks ltqkspidyi
      241 nryrtqqacr llessdrkiv dislevgfds lsyfisvfkq hrgstpsqyr kqtngvsnsf
      301 itelqknsie
//
LOCUS       WP_273593700             307 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD binding domain-containing protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273593700
VERSION     WP_273593700.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            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 11442470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..307
                     /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=33818
     Region          13..298
                     /region_name="CutB"
                     /note="Aldehyde, CO, or xanthine dehydrogenase,
                     FAD-binding subunit [Energy production and conversion];
                     COG1319"
                     /db_xref="CDD:440930"
ORIGIN      
        1 memnietsri pdpfpcqvwe padmeeammi krqyganaaf vaggtllrtq weggivskhe
       61 hlirldtiad lrgidesdqh irigaltrlr ecgadtyian hgatlyeacr hiaapsirnq
      121 atiggniasa vgdaipallv hnaslhwadi gsevdliqqd ivdwldvvks grrsldailm
      181 givlekqste hqqeitffrk igrreaftps lvtvaframv dplghfsqvr iaagggsgia
      241 mrlsrceqll egnryhaemi tsiallased fvtysdpfas eqyrqqtagk llaaglwesi
      301 hsqierr
//
LOCUS       WP_273593738             417 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Paenibacillus sp. PK4536].
ACCESSION   WP_273593738
VERSION     WP_273593738.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 417)
  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..417
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..417
                     /product="M16 family metallopeptidase"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47163
     Region          1..401
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mervqlhngl rivmekmptf rsvtigiwik tgsryenlvt ngishfiehm lfkgterfda
       61 qkiaevfdgi ggdvnaftak eytcfyakvl dehlsiavdi lsdmffnsll dpeelkkekn
      121 vileeilmye ddpddlvhdl vtmssygdhp laypilgtee rlhpmgseel raymkehyti
      181 entvisvagn iddsviplle khfgafdnhg tkqdltipaf aggqifhkkk teqnhicmnf
      241 pggkiddpry yamvllnntl gggmssrlfq eirekrglay svysyytaha dsglftiyag
      301 tapkqtkdvf elthallhdv kvngiteqel yqgkqqlkgs lvlslestss imnrlgknei
      361 mlgkhntvdq tlqyieevtm edirsviddm faepyalamv ghserslahv rrdelvy
//
LOCUS       WP_273593816             497 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 30 protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273593816
VERSION     WP_273593816.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 497)
  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 497)
  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 497)
  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 497)
  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 497)
  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..497
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..497
                     /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=54685
     Region          30..497
                     /region_name="XynC"
                     /note="O-Glycosyl hydrolase [Cell wall/membrane/envelope
                     biogenesis]; COG5520"
                     /db_xref="CDD:444271"
ORIGIN      
        1 msmfkkslnl vllsslmitp llsvpaqtya anesvevwlt tadpnsepav glspgarltk
       61 kaninfattt gnadytinvn egktyqtmdg fgvsltdsst wlmnyklssg kraevmerlf
      121 gntgigmsml rqtmgasdfa wstytyddta gdtslsqfsi ardqpyiipm tkaalaknpn
      181 lkiiaspwsa pawmkyttnd kngtgklqaq yyptyanyfv kfiqsyqaqg ipiyavtpqn
      241 eplfepgryp gmnmneqdqi gmigdylspa lknaglntkv iaydhnydnw sypntvivgl
      301 knsgkssava gsafhhyggd ytamtsmhna hpdkdiwfte ggfgdwndkv dgstqgfdnm
      361 inefigitrn wsksiilwna aldqkdgpsv igdyntnkgm itiqnsdnsn snpedkvtyn
      421 kqyyllghfs kfvvtgatri dtnssndiqn vafknpdgtk vvvlynsqta tktvkvqwng
      481 qstnytvpgk svvtlkw
//
LOCUS       WP_273593829             327 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Paenibacillus sp. PK4536].
ACCESSION   WP_273593829
VERSION     WP_273593829.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=35754
     Region          56..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 msrstaiptt svtpkhvphy mmmvliigvi lviiecyfsl iinrehmysq tgslfrtlgc
       61 ilvgaclavs gtvmqyisrn tmtspstmgl tqgtalalci iiiflpslsq wmimvwaiag
      121 aaiggfvays ignllpwkvk slrqisggia avflitvism iiyssystid yidhlvnpti
      181 lgdprftiwv llpvtvgaiv icwllslrvp shsattrffs lswatiicml mvilmtgist
      241 mlagplglvg iiipsilrff fhqppirwli lgssiygavl ilgldilsht idpifdiavm
      301 pitviigapf liyqiskeie rnllrys
//
LOCUS       WP_273593211             330 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Paenibacillus sp. PK4536].
ACCESSION   WP_273593211
VERSION     WP_273593211.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 330)
  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 330)
  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..330
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..330
                     /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=37373
     Region          8..314
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 mtdnfwrdlp kpffilapme dvtdvvfrhv vseaarpdvf ftefansesy chpeghhsvr
       61 grlmftedeq pivahiwgdk peffrqmsig maeqgfkgid inmgcpvpnv aengkgsgli
      121 crpelageii qaakagglpv svktrlgfae vdewrdwlth ifkqdivnls ihlrtrdems
      181 kvpahwelip eikklrdaia pntlltingd iadreeglkl veqhgvdgvm igrgifsnpf
      241 afeqesrehs stelldllri hmdlhdkyse ieprsfkplp rffkiyvrgf rgaselrnel
      301 msakntnevr alldefaakq vdsvestvem
//
LOCUS       WP_273593850             278 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            sp. PK4536].
ACCESSION   WP_273593850
VERSION     WP_273593850.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=30591
     Region          1..255
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mikgisqagl ghispeelvr saatygfgav dmstdtlvak yglegtqqll kdhhvvlgsi
       61 glpvewsqte slfreqltrv attayqasll gcescctyil patdelpaay maqsivrlrq
      121 iasildaygi rlglefvgph hlrtawkypf ihsvedtltm idaidqtnvg llvdayhcyt
      181 tgftaddirq lradqivhvh indakdipmd qvldndrlyp aegvidlrsf vqalqdigyt
      241 gvvaqeiltp epptdsitsl wersergfnh vfqalsti
//
LOCUS       WP_273593931             289 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273593931
VERSION     WP_273593931.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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   Rosinski,J.A. 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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..289
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..289
                     /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=33897
     Region          35..289
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mqlsppyevt qmpdktfpin ifhvatphwr wvplhwhehl ewmivykgsf rvqigtehqd
       61 itvgdivfvn trqihaafpl eedteliciv fnealirniq ldhtesryir pllenqlglp
      121 aifpkdhpla kqvtfylqqm iieyeqstsg selliksyll acigwlyriv ahdhielpas
      181 hqpaymqplf qhlshhfres isietaaelc qltptyfcyl fkkttgktfi eyinmlrihe
      241 aeqllrsgdw nisqvayhcg ftslnyfgrv fkqykqmsps rwlkhiaks
//
LOCUS       WP_273593934             633 aa            linear   BCT 28-DEC-2024
DEFINITION  IucA/IucC family protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273593934
VERSION     WP_273593934.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 633)
  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..633
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..633
                     /product="IucA/IucC family protein"
                     /EC_number="6.3.2.-"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73253
     Region          28..627
                     /region_name="IucA"
                     /note="Siderophore synthetase component IucA/IucC/SbnC
                     [Inorganic ion transport and metabolism]; COG4264"
                     /db_xref="CDD:443406"
ORIGIN      
        1 mtftqqlpty salsltqstd pfdmikalhs ehfpaveqri irqlmqaiiy edilpylqte
       61 msqqqirssl sepkayqqft ivgvttdqqk vqymctgkrm vsfgrvrleq vpviriatdg
      121 qqqtahlhef lnevlqqvqq geklqqfrne leqtllkdlq sqayvqqsvf steqsyydql
      181 egqikdghpy hpcyksrigf tlednaqygp efqqslypiw lavakeysls afsttvedhd
      241 sfmqeslgtk qwnqfqqilq qqqlniedyh lipvhpwqwk nkivsafyre lasqqivplg
      301 igndayyaqq sirtlgnrtr peapylkmal sitntstari laghtvlnga mitdwltrli
      361 qhnetarqlg fvvlreragi tfnyeklpey rqsqtygslg tiwreslhty lkegedgvpf
      421 nglchvqpsg vplidpwiqq ygverwtyam ltatvtpiih mlyahgigme shgqniilih
      481 hdglptrial kdfhdgvrfs vthlvepelc pdltpeppsh akinrnsfiq tnnpddvrdf
      541 sydafffiaa temcmfleqh yqlseqsfwk mtadiihqyq hdhpqhqerf dcfdlfaetv
      601 lieeltkrrl fgdgelhfkd gmnplyayrq stc
//
LOCUS       WP_273593949             747 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Paenibacillus sp. PK4536].
ACCESSION   WP_273593949
VERSION     WP_273593949.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 747)
  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 747)
  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 747)
  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 747)
  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..747
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..747
                     /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=84741
     Region          76..733
                     /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 mhtlefqygq mifsflgynl sflamtlliy ffanlsrlli pkyivhllac ipligiplln
       61 gypylfnisi tqseywrvee rtlsfdlmfi iialyslttl itfvvlsyrk mngsllyqre
      121 krmmatiirg sivaaiwlvv tfvytsfcge isffpiaslp ayagmilait lhiamhkynf
      181 laaaerrykl lftlsssgia lmnrdgiave anpafrllta vsesqgeidi lamiqhedkd
      241 nyrdrlkkaf enrtilqnsq vqirnltgms yivevnndfl eidgelycyl lvrditaqql
      301 neaqlielay ndpltglanr fqfnrklwma vdkinqqsnk vvvmqidldh fkwindtmgh
      361 sagdillrhv aqllqqyvpp havvarmggd efsimielap degeeiaigi anqilhafee
      421 qvvivgkyyr vscsigicis pddgedsetl lrhadtamyv akrsgrnqyh lftkqlkrla
      481 ekhlllqqgl enalhrgefs lvyqpqvnsh tqqvfgveal lrwsspdlgi vspvdfipia
      541 eqngairqig ewvmkeaaqq aalwikqght dlqmsvnvsa sqlsdpnfak kvecilketg
      601 lpahllclef teseaireed qilkvckslv dmgialavdd fgtgyssmrt itrfpfqfik
      661 idrslihdig tnprnvavvr svielaqqln mnviaegaev eeqvellsql gcfqiqgyyy
      721 gkpmkakdie rklyrdleen tridqal
//
LOCUS       WP_273593959             686 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273593959
VERSION     WP_273593959.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 686)
  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 686)
  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..686
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..686
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75022
     Region          18..377
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mkkigsllla avltvvpmsq tfaqgstasl sseekakqla ttvvkdygas gvqyaivdhg
       61 kvilsghagi knqaakeqit pdtmfgigsv skmyvtsavm mlvdagkidi dqplttyipd
      121 fkmaderykk itprllmnhs sglygshyhn silfddndtq nydnllkelq terlkadpga
      181 fsvysndsfq llevlvervs gmsysefvkt hisepmnfks thtpldtfdr nqlsktyfpg
      241 iasalpvena nilgtggiys taeelatfgd vlmgnktdll seksaqamqk deyrngiwvp
      301 eernttnygl gwdavnlapf sdygikalsk ggdtimyhad lislpeydms aavvsaggss
      361 iyntqlatql llqelkdqgk ikkilpdqtf kpavqvkmpa elkqysglyg tldntltldi
      421 skgkialpdi lggiipaqty vytgkkqfts kdgsaivsfd kqkngktyik vnanvslpgl
      481 gqtvmvfyey qklsknkvst avqkawkard gkkyyavdek insafyiaps iltktlkvda
      541 tngyvngdri idqnnavnva qipvmtgrdt fdlefvkqnn veylkavkql yipedaiqpl
      601 skqnaskvti asnghvkwfk idkttagksi tvdyannagf vvyddkgmvv qssiinhkks
      661 vvlpqngliv fggeagdvlk vtwgkk
//
LOCUS       WP_273593962             123 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Paenibacillus
            sp. PK4536].
ACCESSION   WP_273593962
VERSION     WP_273593962.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..123
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14150
     Region          22..118
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mrvckdgfqr efiedksdmy tiaftqnils grwkyfilwy lkghtrrysd ikaflgdlsq
       61 gslskqlrel ekdgvikrkv ypvvppkvey sltekgtklm pildamesfg kaygeqpddt
      121 slv
//
LOCUS       WP_273593977             104 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp. PK4536].
ACCESSION   WP_273593977
VERSION     WP_273593977.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=11725
     Region          9..96
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdatafdvkd lkqfdepanl lkalshpirl civrglirkr kcnvsymqec ldipqstisq
       61 hlqklrstgi vttersglev nylladprie qivhilfgee dces
//
LOCUS       WP_273594011             445 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273594011
VERSION     WP_273594011.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=48864
     Region          1..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 msnfdvlfig sgqgawnaam plsmsgqkva iierdkiagv ctnygcnpki ildgpikvme
       61 daqtyhgigm tsemkinwse lmahknkvld alpvmleenf kkagievikg easfvnektv
      121 avngqeytad kiviasgqrp tpldipgkey lktsneflyl edlpdhivfv gagyvsmela
      181 siavkvgatv hviqssdhil nefhqpyaqk lltkmqqdgi qfhfneklsk veqqgeqlqi
      241 ttekgltltt qlvinatgrv pnvenlnlea agveynskgi ivdeylqttq kgiyasgdil
      301 dkkqprltpt avfeakylaa sflgaqtqai eyppiatiaf tvpriaqigv tieeaeatgl
      361 tikpidlgkq wdfagrnete ahlnlvydqe qklvgatays qealeiinsl tpiitlglts
      421 kevdkliyaf psfetmipry mqetk
//
LOCUS       WP_273594012             419 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome P450 family protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273594012
VERSION     WP_273594012.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 419)
  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 419)
  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 419)
  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..419
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..419
                     /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=46512
     Region          25..419
                     /region_name="CYP107-like"
                     /note="cytochrome P450 family 107 and similar cytochrome
                     P450s; cd11029"
                     /db_xref="CDD:410655"
     Site            order(64,72,105..106,113,117,124,253..254,257,261..262,
                     265,298,303..304,307..308,310,333,360..362,365..366,
                     368..370,374)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410655"
     Site            order(72,97,99,104,106..107,189,193,202,252..253,256..257,
                     261,304,307..309,409)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410655"
ORIGIN      
        1 mnsfqnitat sklnpfrsda gegqfsifaq lramgavipi tvpmgntngq qwmitrmeev
       61 sevlknprlf tvdqsliegl tpatpeitpe tdspapttff sgksmisvde pdhrrlrrlv
      121 skaftpryme slrpsvqkia delldqvqaq ghmdivkdya hplpinvicd mlgvpveera
      181 qvhtwstais hglglgvrep eveanlrafg dytaqlvkak rkhpaddlis qlitieeegd
      241 hlsedellsm itllifaghe ttsnllatgt lmlldypeql nklkadpelt ssafeellrf
      301 ngpatmtgpr yatedtilgg qqirkgdvvi pllksanrde llfehseeld ihrkvnrhla
      361 fghgihsclg aplarvegdv afrtllrrmp nlqlavpree vnwhfalssq slmtlpvvf
//
LOCUS       WP_273594259             116 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Paenibacillus sp. PK4536].
ACCESSION   WP_273594259
VERSION     WP_273594259.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=12773
     Region          10..84
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(14..15,19..21,34..36,45..48,50..51,54..55,57..58,
                     64..66,71..73)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mnqniqqfka dffkalahpm riqilealct gdktvnelqt ivgsegsavs qqlsilrskn
       61 vvqsvkegts viyslrdpli qdllavakqi fdnhlvdais llegmrnepe sikhld
//
LOCUS       WP_273594284             250 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273594284
VERSION     WP_273594284.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (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   2  (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   3  (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   4  (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   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
REFERENCE   6  (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 11416738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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:0070401 - NADP+ binding [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27384
     Region          1..>193
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mkytvitgas sgigyesala faakgknlii varrveklee lqakikelyp aldvvvvesd
       61 lsitqqaytl ynslknyeie twinnaglge gsfivdqnls kvemmlkvni esltilstly
      121 vkdyadvega qlinvssalg yaiavgsvay saskyyvsaf teglakelei kgahlkakvl
      181 apaitetdfv knsndieeyd yqanmpkyht akemagfmln lyegtetvgi vdtnyqfnlt
      241 apiypvisef
//
LOCUS       WP_273594285             262 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273594285
VERSION     WP_273594285.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=28569
     Region          1..246
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mkktvlitgv sggigkelad lfardgynlv lvarnevklq emakdykqkh gthsmiiakd
       61 vsvtgvpqav faelqekgii vdylinnagf glygtfletd leqevnmidi nikaltvmtk
      121 lflpdmvkrg hggimnvssl vgffpgplms vyyaskayvl sftealenel rgtgvtvtal
      181 cpgvtatgff nrsgmeeapq meksgsvmts sqvakegyrg flkgdtliip gvrnrllafm
      241 prllprkwtt hlvrstqakn th
//
LOCUS       WP_273594368              71 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273594368
VERSION     WP_273594368.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            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 sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..71
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7928
     Region          4..71
                     /region_name="YozG"
                     /note="DNA-binding transcriptional regulator, XRE family
                     [Transcription]; COG3655"
                     /db_xref="CDD:442872"
ORIGIN      
        1 mkvikirlkq alkdrsltqk qlealsgvsq arisklcrdd rqevnllmls kianamgitd
       61 iselldfvde e
//
LOCUS       WP_273594045             392 aa            linear   BCT 28-DEC-2024
DEFINITION  alanyl-tRNA editing protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273594045
VERSION     WP_273594045.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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 392)
  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..392
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..392
                     /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=44523
     Region          1..226
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
     Region          260..388
                     /region_name="DHHA1"
                     /note="DHHA1 domain; pfam02272"
                     /db_xref="CDD:396724"
ORIGIN      
        1 msailyynds flrewtttiv erkeqdeqyf vrlaetafyp hgggqpcdtg vindiavldv
       61 vkeeeviwhq verlpiedqa dcqlnwerrf dhmqhhtgqh llsatalqlf daptlsfhlg
      121 qdmvtididr ssfsdaemtt leqavnqriy nnlaiksyfv naeqlaqlpi vkmpkvtehi
      181 riveiegvey nacggthvaq tgqisiiklf kaekqkgsir lyfkcgaral qdynnsldil
      241 ntlavkfntg rkdilerfgk weedqqqlkt eleqlrkand iheakqlssq iqnqqlthmf
      301 ehktlpdlqr iaanlmaeqp livllatsse ykvflaqngh pqlecgaffk ehlstfngkg
      361 ggsdlsaqat ftseadliaf ytfaeqqlgi mh
//
LOCUS       WP_273594374             358 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Paenibacillus sp. PK4536].
ACCESSION   WP_273594374
VERSION     WP_273594374.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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..358
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..358
                     /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=39293
     Region          7..356
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 mstqrlnklr qamqeqqlea llitssvnrr yltgftgsag yvlvtaqeay lltdfrymtq
       61 apeqatafsv vehsanvvdt mkellakgni sklgfeqdlv pysryamysk hlgpvelvpv
      121 sgimeeirnf kdaeeiaiie katdiadrtf shilnyikpg vteqeielem esfmrrlgat
      181 gtsfetivas gersalphgv asekvigane fvtldfgaiy qgyvsdltrt vfvgtptdeh
      241 rkiynivlea qlntlkhlkp gmsgrdadal ardviashgy gdafghstgh gigmevheep
      301 rlskmsdtvl spgmvvtvep giyipgfggv rieddvlite dgirvlthst keftilpv
//
LOCUS       WP_273594383             496 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 32 protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273594383
VERSION     WP_273594383.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 496)
  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 496)
  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 496)
  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 496)
  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 496)
  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..496
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..496
                     /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=56741
     Region          28..490
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mkmnrtqlyr klheaetgew ealkqladqs pwrqafhiqp eagllndpng fsffngeyhl
       61 fyqwfplgtq hgikywyhts stdlvhwnnk gigmapdtiy dshgaysgsa iekdnllylm
      121 ytgntrntdw krypfqcmat mdqqgvitkl ppvidkvpag ytdhfrdpkv wqdgeyyycv
      181 igaqridqtg cavlyqspdl qewtfqgeln talpsfgymw ecpdyfeldq qgvflfspqg
      241 laaigdhfqn iyqsgymigt pldlntrqfd hgefyeldhg fdfyapqttl apdgrrllvg
      301 wlgmpeinyp tdtqgwahcl tlprelsied gqlrqrpvae lsqlrgqqsh lhrtvhhhrd
      361 lissiegihy emliqisdiq adkvgievrv gtdektvlyy epalekltld rtlsgqslal
      421 eygttrscsl pleegivtlh lfmdtssiev fvndgrnvft srifpqlnst gfalfaehgs
      481 acfdvtqwdl idkgeq
//
LOCUS       WP_273594561             574 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273594561
VERSION     WP_273594561.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 574)
  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 574)
  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 574)
  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..574
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..574
                     /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=67926
     Region          7..479
                     /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(60,63,100,103,145,164,168,200,256,415)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(200,256,330)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          486..>525
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; pfam16657"
                     /db_xref="CDD:435493"
ORIGIN      
        1 menktaresv iyqiyppsfm dsnndgwgdl ngiatripyl hqlgidtiwl gpvydspmid
       61 ngydirdyyk idpkygtmeq feslleqlhh idmklimdlv inhtsdehpw feqsrsskdn
      121 pyrdyyiwrp aksdgtepnn wrsfqnesaw tydeqtdeyy lhlfdrkqpd lnwehpplrq
      181 eiykmirwwl dkgidgfrld ainmiskhpd lpdaseddph pigqkyykng priheflqel
      241 nretfahyph iltigeapsl tmeqvleytl pdrkelnmvl amdmmrlgkd phdpwrsadw
      301 svsqlkesva kwyehvfarg eygvylsthd hprmipdvvg hhehnmtaak liatflhlip
      361 gvplvyqgee lglpnttydr iedyrdqgtv hyyeeavang qsaeevlsgi hkrsrdgsrs
      421 pmlwdhqhhn fgfspdeqve pwipfpekre lkgysvseqe eqrgsvlsyy rhliamrkqf
      481 pimshgsftm llkdhsevfa firewqsqrw lillnfadie aeidwtqeyr vfptsmvkil
      541 gnyphtahpp hleeeqyied lqylrpyevl iyrm
//
LOCUS       WP_273594605             259 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus sp.
            PK4536].
ACCESSION   WP_273594605
VERSION     WP_273594605.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=28677
     Region          3..256
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mvklankvvl itgassglga gvasllvekg aipiltarse dklqtlsrql kgehqiirmd
       61 vqqdedvkrv vvqvikqygk idillnnagy gqfktiaemp iedyqtmidv nylgivrctq
      121 avlphmlaag tgqivniasl agkfptakst sytatkhavf gftnalrqel retkikissi
      181 npgpiataff dradpsgdyv knvsqfmmtt dkvsrdivkv mekrkeeldl priaipamri
      241 yglfprfidr ltyrlfdrk
//
LOCUS       WP_273594644             406 aa            linear   BCT 28-DEC-2024
DEFINITION  nitrate/nitrite transporter [Paenibacillus sp. PK4536].
ACCESSION   WP_273594644
VERSION     WP_273594644.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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   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 406)
  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 406)
  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 406)
  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 406)
  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 406)
  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..406
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..406
                     /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=43683
     Region          15..377
                     /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(25..26,29..30,33,65,116..117,119..121,124,142,
                     145..146,149,219,222..223,226..228,231,259,263,312..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 mdkksfwqsg hkptllgsfl yfdisfmiwg migplsviia ldypmdpvqk aqlvalpvlg
       61 gsilrlvlgf lsdyigpklt aqigmiltli plllgwqwvq sleqlyvvai llgiagasfa
      121 aalplagqwy pkehqglamg iagagnsgtv iatlfanrla qhfgsweivf giamipiilv
      181 fifftifakn spnrpepkkl sqyatvlkqr dawvfcafyc vtfggfvgla nyltiffntq
      241 ygltavqaad iaticviags ffrpvggfla driggtkmlm ylysgagiml acvsflpplp
      301 vvvsllfvgm mclgagngsv fqlvpqrfgn eiglmtgivg aagglggyal plilgnlyka
      361 tgsytlgfim lsiivlccls llvimqikwr tswldhnvtk tarqvs
//
LOCUS       WP_273594808             260 aa            linear   BCT 28-DEC-2024
DEFINITION  TrmH family RNA methyltransferase [Roseateles koreensis].
ACCESSION   WP_273594808
VERSION     WP_273594808.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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..260
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..260
                     /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=27722
     Region          7..257
                     /region_name="SpoU"
                     /note="tRNA G18 (ribose-2'-O)-methylase SpoU [Translation,
                     ribosomal structure and biogenesis]; COG0566"
                     /db_xref="CDD:440332"
ORIGIN      
        1 msqlqhitsr dnpvlqrlrk lsqdggayrk lgsvwlegdh lvraclqrny pvtlavmtea
       61 aaqdsvlral adaaprqlvv ptalfktisg lespaqigfe vphdaaqrid pavdtvildr
      121 lqdagnvgti lrsagafgfk qilalkgtaa lwspkvlrag mgahfglrli eglgpadldg
      181 lqlpliatss yaekqlhqls lprpcawvmg hegqgvqael mqrcrltvgi pqpggeesln
      241 vgsaaaicly esarqrltva
//
LOCUS       WP_273594938             556 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein [Roseateles
            koreensis].
ACCESSION   WP_273594938
VERSION     WP_273594938.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..556
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=61480
     Region          3..412
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mfssfrlsms wlhtwlglvl gyllivifff gslsvfdref drwalpetrf aaqtmpsyds
       61 mlapifaqmk paadeleaag grvksplpte lkplnwaayt thrdpvvgly aeyavpgnpn
      121 daddhvhghv tvdprngrvl rddqlkigse ffypmhislh igwrnlgywi vglaalvmla
      181 alvsgvvihr rlfrefftfr pkkhvqrstl dlhnltgvva lpfhfffalt gltifagiyl
      241 pvsetllkpq ataaaiaeaq aknlpyaasg vpasiasvda mvieakrrwa shgmagevgy
      301 lyishpgdkn syvtvyrggs drvallgqai hfegatgrvl feepqpstva kinefltglh
      361 lqqfehwalr wfylfggmag cvcivtgflf fvekrkraqp gharcadama vttvtgmlia
      421 vlavlvanql lpqdltlrge wekrafwasw llsfvhaawr skplrpvqps pawfeqccai
      481 avlafaalml nsittgdhll ktvfiehywp vagvdialla vgllatatar rlrlrwpalq
      541 pgasqrsaaa eeghaf
//
LOCUS       WP_273595010             189 aa            linear   BCT 28-DEC-2024
DEFINITION  DNA-3-methyladenine glycosylase family protein [Roseateles
            koreensis].
ACCESSION   WP_273595010
VERSION     WP_273595010.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 189)
  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 189)
  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..189
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..189
                     /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=20740
     Region          <1..182
                     /region_name="AlkA"
                     /note="3-methyladenine DNA glycosylase/8-oxoguanine DNA
                     glycosylase [Replication, recombination and repair];
                     COG0122"
                     /db_xref="CDD:439892"
ORIGIN      
        1 mkklipqfge arlqsradaf ttlarsiigq qisvnsaqna wlkfaalvgg aptkvqpaal
       61 mglgavalrg aglparkvdy lmdlaqhfea gqvhvrqwtq mddeaiidel vairgigrwt
      121 aemflifhlm rpnvlplddp rllkgiseny fsgepvsrae arevgdawsp yrsvatwyiw
      181 rsldpapaa
//
LOCUS       WP_273594531             302 aa            linear   BCT 28-DEC-2024
DEFINITION  FUSC family protein [Paenibacillus sp. PK4536].
ACCESSION   WP_273594531
VERSION     WP_273594531.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     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=34235
     Region          2..193
                     /region_name="YgaE"
                     /note="Uncharacterized membrane protein YgaE,
                     UPF0421/DUF939 family [Function unknown]; COG4129"
                     /db_xref="CDD:443305"
ORIGIN      
        1 mkflvgmrnl ktalavfici iisqllqley pfyaviatii amensvtnsy tvgknrmmgt
       61 lvgaaigfvf awidphsavy saigiviviy icnllkwnks isiasivfla imlnlrpges
      121 pflygmhrva dtligisvav lvnylvfppd hersmeqmrs vlrkhltkla hellreggti
      181 hisplkkdma nlekayetya sefhlkknkq qmlehleqei dvyhntyshm rmirlltdel
      241 pthhhwdlpe qhhshlmaql pldissqqii ynyhvscilq emstlgllip shiaqpfsss
      301 st
//
LOCUS       WP_273595160             515 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Roseateles
            koreensis].
ACCESSION   WP_273595160
VERSION     WP_273595160.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 515)
  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..515
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..515
                     /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=54179
     Region          66..509
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mplqrqlgrs tllfalflsl ltphiahaqv sgggfdqavd qffkhtfgwf vdlifytvpv
       61 gsaqfplivg wlllaalift iyfgfpqftg aklaldlvrg rysdphnkap gevshfqalt
      121 talsgtvglg nmagvgaala iggpgatfwm ilcgllgmaa kftectlgvk yrvvlpsgav
      181 sggpmyylrd glaerglpgl gkvlaagfav mvilgalggg nmfqgnqana mivhtfglpd
      241 gygwvtgvsl aalvfgvmmg gmpqigkvta tmvpwmagvy igmalfviai dfdqipsamr
      301 aiwdgafqae gvagglvgal iqglkratfs neagvgssai ahsavqtkep vteglvalle
      361 pfvdtvmict atalvitiag vnagpfpnps glsgieltsa afrstadwfr yplalvvvvf
      421 avstmiswgy yglkgwtylf gesrladasf kllfctfivv gasisfggvi dfsdaaifam
      481 sifnligvyi lapvvkaeyr qflnkirsga ikryr
//
LOCUS       WP_273595177             161 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Roseateles koreensis].
ACCESSION   WP_273595177
VERSION     WP_273595177.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 161)
  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 161)
  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 161)
  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 161)
  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..161
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..161
                     /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=18019
     Region          61..148
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mreatrgdta elwrvryavr entlpfgrip dielheqiev tgrgwviekp gepasaqapt
       61 lmgfaianar ngniwalfvd pehagqghgr rlhdtmlawm waqglnkvwl tttpgtraea
      121 fyrragwqsm gkthdaeeae lrfemarptd vgqhlarhpa a
//
LOCUS       WP_273594463             167 aa            linear   BCT 28-DEC-2024
DEFINITION  deoxycytidylate deaminase [Paenibacillus sp. PK4536].
ACCESSION   WP_273594463
VERSION     WP_273594463.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. PK4536
  ORGANISM  Paenibacillus sp. PK4536
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 167)
  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..167
                     /organism="Paenibacillus sp. PK4536"
                     /db_xref="taxon:3024576"
     Protein         1..167
                     /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=18846
     Region          1..160
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
ORIGIN      
        1 mvrkdwdtyf mdiahmvstr srcprrhvgs vlvqgkkllg tayngapmgv pdcsedgcmi
       61 seevevvkvd gvetmvkkqr cirtihaeqn lllftdradr egsvvyvtde pcwtcanmla
      121 nsgiieivyy rpypkdtrkv tammkqkgii frqldhynpp pdttvis
//
LOCUS       WP_273595286             245 aa            linear   BCT 28-DEC-2024
DEFINITION  lysophospholipid acyltransferase family protein [Roseateles
            koreensis].
ACCESSION   WP_273595286
VERSION     WP_273595286.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 245)
  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 245)
  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..245
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..245
                     /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=26919
     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 mrsllavvrl lrlighlfyg vglirwrfgs lslarrhvli krwsgkmlri lgvslessgt
       61 prpgaklila nhvswldiaa vhavmpearf vskadvrdwp vvgllvdgvg tlfiertnkr
      121 dalrvvhqma dalkegdtva vfpegttgpg pellpfhgnl lqaaiateap iqpvvlrwfe
      181 pgqrfsttaq figttsliqs lwailrargl gvrvdvltam etahadrral aehvreeisq
      241 rmaqp
//
LOCUS       WP_273595266             229 aa            linear   BCT 28-DEC-2024
DEFINITION  SCO family protein [Roseateles koreensis].
ACCESSION   WP_273595266
VERSION     WP_273595266.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 229)
  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 229)
  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 229)
  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..229
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..229
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25020
     Region          83..220
                     /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 msgsnfsvpp aeplnlsvhs lpdprqmaal qrtrggrlrm llvmavcaap viasyftfyv
       61 lkpsgrayge livptvdlpg eltlhdlsgh avesaslkgq wlltlvqssa cdeacerllf
      121 mqrqlremlg kerdkvdkvl lipddaplrp alqqalttgi pvtilrapaa qlqaflqpaa
      181 ghalsdhlfl idpmgrwmwr spahpdpvqv kndlnrllka nagwdkpgr
//
LOCUS       WP_273595381             247 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Roseateles koreensis].
ACCESSION   WP_273595381
VERSION     WP_273595381.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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: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=27433
     Region          125..215
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mpllrwpvpa llswglawgl flalrtagla awmamalaag lglalaflqa prwrrlmvag
       61 gfplsllvsa hsldlpawaw llplvllala yprrswadap lfptpknalq glgelaplpq
      121 lptqarilda gcglghglre lhraypqarv egiewsllla llarlrcpwa hvsrgdmwaq
      181 dwqpfqmvyv fqrpesmdrv wakarkelap eawlvsldfe ihgqgalasm alprghclwv
      241 yrvprqd
//
LOCUS       WP_273595331             521 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Roseateles
            koreensis].
ACCESSION   WP_273595331
VERSION     WP_273595331.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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=55861
     Region          9..514
                     /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 mspttptfsl lvvddepdlr tlyeltllre gyeldtagtv adalarlqar sysavitdmr
       61 lpdgsgldil qwleqqarre ktlvitaygs aenavealka gaydyltkpv dlrqfrqvva
      121 salgrmpqaa aaspampgrd sagqrmpepl ragvaptagk svaapavpva lsrlagrsaa
      181 mlevhslidk varsmapvlv qgesgtgkel varaihdsgv rarqrfvavn cgaipeqlle
      241 aeffgyrkga ftganedreg ffqtadggtl fldeigdlpl amqskllrai qersvrpvga
      301 vaeapvnvri vsathkdlsa evaggrfrqd lfyrlnviql rvpplrerie dvplisetvl
      361 ariaadagvs ptprltpaal gqlaryafpg nvrelenllh ralamaggew idavdlglpd
      421 svlddsqmgs ldgldslgvr armplgvdst ppqwaglpal aedevpadla ryldeverei
      481 llralarhrf nrtaagaslg lslrqiryrm arlditageg g
//
LOCUS       WP_273595488             575 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Roseateles koreensis].
ACCESSION   WP_273595488
VERSION     WP_273595488.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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=64333
     Region          4..575
                     /region_name="COG4986"
                     /note="ABC-type anion transport system, duplicated
                     permease component [Inorganic ion transport and
                     metabolism]"
                     /db_xref="CDD:444010"
ORIGIN      
        1 midkrffprq vveatgnrwd lvmlpmvlal lsllalagsh matpfqmgev lhisldpwvl
       61 pyyllrttlr mflalgasvv facafaalaa kyraaekvlv plldilqsip ilgflsitvt
      121 gfialfpgsl lgvecaaifa iftsqawnma fslyqsmrtv paelkeaari fhlsgwqrfw
      181 rlelpfampg llwnmmmsms ggwffvvase aisvanqdik lpgvgsyiam aiaardlqai
      241 gyailamlig illydqlffr pllawadkfr feesgnenap tswlltwlrr teliqrvgew
      301 parwlaasfr ytklnydgts irarakpvnp lwergfdail aalvlfavwr lvsfihaevg
      361 wqevahvfkl gfytlarvli liaiasliwv pigvwiglnp riagrvqala qflaafpsnl
      421 vfpvavvliv nwklnpniwl spliilgtqw yllfnvvaga stipselrya aknlglkgwl
      481 lwrryllpai fpsfvtgait asggswnasi vaeyvswgdt tlqadglgsy iqnmtaigdf
      541 prialgigvm cifvmvlnhw vwrrmyrlae qrmhf
//
LOCUS       WP_273595439             316 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA dihydrouridine synthase [Roseateles koreensis].
ACCESSION   WP_273595439
VERSION     WP_273595439.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 316)
  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 316)
  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..316
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..316
                     /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=34362
     Region          2..306
                     /region_name="DusA"
                     /note="tRNA-dihydrouridine synthase [Translation,
                     ribosomal structure and biogenesis]; COG0042"
                     /db_xref="CDD:439812"
ORIGIN      
        1 millapmegl ldhmlrdalt rvggidrcvs efiritdmlm pdrvftrivp elltggmtaa
       61 gvpvraqllg sdpvcmaena aklaalrpeg idlnfgcpak cvnrhrggav lldepeliya
      121 ivaavrramp agmplsakmr lgymddsktl ecaqamvdag aeelvihart kadgykppay
      181 wdriaavraq lavpvvange iwtaadaanc qaqsacpdlm lgrgmvanpg lawairapea
      241 aplpwtqlll vmrdffkavq hhvahrhqag rlkqwlnylr rhypeageay lrlrtvnspe
      301 dlhqqlfgal pdalla
//
LOCUS       WP_273595168             553 aa            linear   BCT 28-DEC-2024
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Roseateles koreensis].
ACCESSION   WP_273595168
VERSION     WP_273595168.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..553
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59678
     Region          30..552
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mlggllapea sraqafsaaa aaaaaatafp evprfailef eidgntvlpv avveqtvtpf
       61 mgddrqmsdv eaardalekr yqqagyltvf vdvpeqrvdg gvvrlhvteg rverlrvtga
      121 ryydqgvire rvsqmapgqv pdfneaarqi seitrderqi qqllkpgltp gtfdvelrva
      181 dklpmsasle innrhtadtd pwraslnvry dnlwqrdhsl sltlttapre vrqssvfvan
      241 ysaplggqds vlgyavlsds lvaplgagtv igkgatyglr wvrtvglade ahsfslgady
      301 kdvrqrqqfg gtdlstpvry lpfqagytgn wfgtsgqtql ttslvfasrs lfaqqidcpg
      361 nvgqvdqfqc srdgadgsfa ywrgdlrgnr svtrllgqds adagswgdlh lhlgwqlstq
      421 plvsgeqmam ggadtvrgyl daeaagdtaw lgslewrsrn llsgwaasga aaagagrpre
      481 lnllgfveag qartlqplpe qqehvslagt glglrfraap ninadldvgw plkttrlspk
      541 geprlhvrls aqi
//
LOCUS       WP_273595522             135 aa            linear   BCT 28-DEC-2024
DEFINITION  GlcG/HbpS family heme-binding protein [Roseateles koreensis].
ACCESSION   WP_273595522
VERSION     WP_273595522.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..135
                     /product="GlcG/HbpS family heme-binding protein"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=13698
     Region          3..133
                     /region_name="GlcG"
                     /note="Heme-binding protein HbpS, GlcG/HbpS family [Signal
                     transduction mechanisms]; COG3193"
                     /db_xref="CDD:442426"
ORIGIN      
        1 mkqkpyltlv dvktiaaaae aealanhwav ciaivddggh llwlqrldga pavsaqiapa
       61 kahtaalgrr eskvyediin qgrtsflsap gisgmleggv pimvegacvg avgvsgvkst
      121 edaqiaragi aalvv
//
LOCUS       WP_273595617             278 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles koreensis].
ACCESSION   WP_273595617
VERSION     WP_273595617.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..278
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30698
     Region          70..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 mdpispyths laraddfhrs carrlvvwic lclgafscfa lglddtplir tsgqsenlik
       61 fdpdnaaapg lsievmraie ridpalkfvg qevlrpvsri dleleagsld vffglvrnqa
      121 rqekyvvlsa plyrqftqla vrgddpieiq tfdeirtlgg agvvgvprgs ayveqlkalg
      181 glvvddgavs ventlkkllk grvrfvyygg tvlrkqlhkd glegriklip trfnredvci
      241 vvsrktepkl atrieqavqr mrgsgelsai qekygvrd
//
LOCUS       WP_273595773             354 aa            linear   BCT 28-DEC-2024
DEFINITION  WD40/YVTN/BNR-like repeat-containing protein [Roseateles
            koreensis].
ACCESSION   WP_273595773
VERSION     WP_273595773.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 354)
  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 354)
  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..354
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..354
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=37530
     Region          58..277
                     /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 mrwtvkrhav cllavlsamt fgaaaqtsag rigsawerpa lqlrdpahav ylaaadaggr
       61 lvavgergvi atrergegaw hqqpsptsvt ltavqfvdar dgvavghagt vlttldggqt
      121 wqlkldgrrl sqialddaka agdparirda erlvadgpdk plldvlawda rhmlvvgayg
      181 lafhtadggr twqswmgrlp nprglhlyaa rrqgnhllla geqglllqse degltfkavs
      241 apykgswfta emrsatewlv aglrgnvwrt adagatwqql snpipaavta skrlpdgavl
      301 lanqagfvlr vgaqslqpln pqplpplagl atdgdqrlwa lgmagpvlip airh
//
LOCUS       WP_273595698             383 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Roseateles koreensis].
ACCESSION   WP_273595698
VERSION     WP_273595698.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..383
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..383
                     /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=41078
     Region          6..377
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkhgqrsadv livgggiiga acarefsrqg lsvaviepgp igggataaam ghllvvdaqg
       61 qaddaefqlt rrgvslwddw laesadhpri aehercgtlw vaedagdmtl aelkyswlnq
      121 rgiaarmvda gplstlepll rpglfgallv pgdariyapk vamrwiqear vthiegrlsh
      181 vdghavhlcd grtlwgamtv lcaglssqaw lpagsliakk gqlaitqryp gllrhqvvel
      241 gylrkahlsd qdsvafnvqp rpggqiligs srqfaaagqt pdpaidlpvl kdmlahacrf
      301 mpklaplnll rtwtglrpas rdgrpligah peharlwlat gheglgltta lstaellvdl
      361 clqrptqmvp epwapcrffn tsa
//
LOCUS       WP_273595776             386 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Roseateles koreensis].
ACCESSION   WP_273595776
VERSION     WP_273595776.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..386
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43151
     Region          133..381
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mfkyfptnyp wnlsvdlaie mgarmgevea mcaplleask apdaagtqaf ratwaamadk
       61 lcalaeedea hgrllsagek ynraatyflt cerlqahgaa grvalyqrfl dvfakgvkls
      121 gencerveip yegklisgly vraegvsgra pilvqvngld stkemkyrvg lpmwlarrgv
      181 sslvidqpgt gealrlhglt arydsehwas rvvdwleqra dvdpkrigme gvslggyycp
      241 ravameprfa cgviwganhd wrdvqkrrle kegnfpvphy wahvrwvwga qdmddfmria
      301 envhldgvve kirvpflvth gekdsqiplk wahrtyeqlv nspkrelkvf tereggvqhs
      361 sfdnsinagh yiadwvaetl ggrtaa
//
LOCUS       WP_273595817             716 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Roseateles koreensis].
ACCESSION   WP_273595817
VERSION     WP_273595817.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 716)
  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 716)
  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 716)
  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 716)
  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..716
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..716
                     /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=79675
     Region          24..694
                     /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 mnvfslqvpt sspechahlq aytallegml eaawlvdgrs rnilavnaaa vqllgyaaea
       61 lvgqivdsla qtpedamfwm eaaadtestl nsdtlmrhad grmlwvtrrv sfvalsgprg
      121 kqdgfwmvvm rdqtrqrqse dereslvael qatlestadg ilvmdlagrm rafnrrfatl
      181 wgipadllre rddeavqlwm rrsvmdngsy aqrlsaiqda plmqssdiik ladgrvlerv
      241 slpqltkgrp igrvysfrdl seklaasqri eelahsdllt glpnrralae rieymkavar
      301 rennvfallv vdldrfqqin etlghtygdr vlkevgerlk dslrevdsva riggdqfsll
      361 ihqadargae naarriqetm srpfnfdtls ftvtcstgia lfpgdgssad elmasaeram
      421 hwvkesgrgt fhfhrprkdv dllsrmrldh amrqalqerq frlqyqpqid lrtgqvigae
      481 alirwrdplr gdispaefip vaeesgfvva igdwvlqqav eqaaiwlrkg rrmpvavnvs
      541 alqfqqdsfa stvasalras glppdllele ltegvllgda eealhrmqal aalgvcmsid
      601 dfgtgyssla ylkrfpiqrl kidrsfikgl pgdasdagiv haivqmgqal rlhviaegve
      661 teaqreflar agcdefqgfl fapslepqvf eervwpasrw vspgrvtlpf vggihr
//
LOCUS       WP_273595892             180 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Roseateles koreensis].
ACCESSION   WP_273595892
VERSION     WP_273595892.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 180)
  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 180)
  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 180)
  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 180)
  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..180
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..180
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18797
     Region          77..155
                     /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 mqkkiacscs tlggerrtaw lgaavlavat wgaqvhpaqa qvsgaaaspk avyneqadar
       61 selnqalaaa naqkknvlvv fganwcsdcr aldrkmnegn laapvsrrwv vvkvdvgrfn
      121 hnvdlaqqmg vslkkgipav avlgrdgdvl katnggelad arnmgddavl rvleglhatq
//
LOCUS       WP_273595903             211 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Roseateles koreensis].
ACCESSION   WP_273595903
VERSION     WP_273595903.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 211)
  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 211)
  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 211)
  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 211)
  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 211)
  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 211)
  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..211
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..211
                     /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=22040
     Region          28..119
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          139..211
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mktaallkpl vfllsgfvlt saamanegaa pakpdlakgq aissqvcaac htadgsrgap
       61 tnpilqgqhp eylakqlnef ksgvrnnaim kgmastlsde diknvtafya tkhakegfak
      121 nkdtvalgek iyrggiadrq ipacaachgp sgaglpvqyp rlagqhadyt eaqlnafrag
      181 trtnnvqmag vaakmndrei kavadyiagl r
//
LOCUS       WP_273596026             260 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles koreensis].
ACCESSION   WP_273596026
VERSION     WP_273596026.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..260
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28645
     Region          34..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 mnrrnlltag lmagltggma iappawpqsa eadiivmled lhpysyrdtq gapagyavei
       61 ahemlrragl ngrfeitsws rvlakgrtvp gvlipaivrl perekefywv gtaarrqaml
      121 yrrrnradis vssmqdihry rtavvigdas ehemlalglt aerhldrsad ygialrrffs
      181 dradllvisk slaptvlkqy gyniadlepv lklresassv alslgteaat rnklqqafda
      241 mhrdgalael aarypaitld
//
LOCUS       WP_273595875             516 aa            linear   BCT 28-DEC-2024
DEFINITION  malonate--CoA ligase [Roseateles koreensis].
ACCESSION   WP_273595875
VERSION     WP_273595875.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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   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 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   4  (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 11482749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..516
                     /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=55878
     Region          2..515
                     /region_name="PRK07514"
                     /note="malonyl-CoA synthase; Validated"
                     /db_xref="CDD:181011"
     Site            order(170,173..178,180..181)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(173,213..214,217..219,259,261,265,287..289,308..313,
                     317,335,394,406,414,417,420,449,485)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(173,287..289,308..313,335,394,406,414,420)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(213..214,217..219,259,261,265,287,309,311..313,317,
                     417..419,449,485)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
ORIGIN      
        1 msnanlfttl raafptdlda iaiecadqhg pdglalsysw rdlergtaml anlfvslelp
       61 agsriaahtd ksvealmlyl avlragyvyl plnnayqaae ldyfiknaep allvcagknf
      121 gwvsklafqa gtayvftlnd drsgtlldra atlsdqhepa hkepnelaai lytsgttgrs
      181 kgamlshgnl rsnaltlkdl wdwkpgdvli halpifhvhg lfvashgall ngskmiwfar
      241 fdphaviarf avasvfmgvp tlyvrmlaea tltpqacanm rlfisgsapl lldtfedwqt
      301 rsghtilery gmsetlmlts npcrgldger iggtvgpalp gvdvrvsrdd gascatgeig
      361 nievrgpnvf sgywrmpekt qeeftadawf ktgdvgrkde ngyftivgra kdliitggyn
      421 vypaeieayl nemdgvlesa vvgvphpdfg eaviasvvar pgatldgdal iatlkrqiag
      481 fkvpkqvfvv adlprnamgk vqknllrqqh qqgfks
//
LOCUS       WP_273596096             276 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Roseateles koreensis].
ACCESSION   WP_273596096
VERSION     WP_273596096.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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=31066
     Region          11..276
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mtthtpptpv raiiadderl mreqlrsrla dvwpeldiva eakngleava lvrehrpdlv
       61 fldirmpglt gvdaarqiaq lpededwlvp eivfitaydq yaveafeqgv adyvlkpaer
      121 erltltvdri kkrlaakqgn dadnlsaspp lqqllhklsa qlnpggkpsy lqwiqatvgq
      181 aiqmipveev lffisdekyt rvqtarveal irkpikelvd eldpalfwqi hrstlvnaha
      241 idgitrdfrg rqlvgvkgha eklevsrsyt hlfkgm
//
LOCUS       WP_273596532             152 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Roseateles koreensis].
ACCESSION   WP_273596532
VERSION     WP_273596532.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 152)
  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 152)
  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 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   4  (residues 1 to 152)
  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..152
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..152
                     /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=17101
     Region          30..148
                     /region_name="HTH_GnyR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     regulatory protein GnyR; cd04776"
                     /db_xref="CDD:133403"
     Site            order(31..33,47,63..65)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133403"
     Site            order(76,79,83..84,93,115,119,125,129,132..133)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133403"
ORIGIN      
        1 msavqtkrqh qtaarnvedl sggapsealf gitelcrdfd lsprairfye dkgllmprrv
       61 ngtrvytqrd rvrltlilra krlgsslaei kqfldlygdh gegrakqlqf lldrtsneia
      121 vleekrahid vtlaelriin asvrqqlagi ek
//
LOCUS       WP_273596458             133 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Roseateles koreensis].
ACCESSION   WP_273596458
VERSION     WP_273596458.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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=14687
     Region          16..87
                     /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"
ORIGIN      
        1 mkdlpaaalv qiagyfqala eptrlqilnl lrqeerrvgd laelcgfsaa nisrhlavlq
       61 qhglveresr gtsayfriad asvyqlcdlv cgniarqsdr mvleraaffp vqpelqspsr
      121 pqaprarksl akr
//
LOCUS       WP_273596334             536 aa            linear   BCT 28-DEC-2024
DEFINITION  formate dehydrogenase beta subunit [Roseateles koreensis].
ACCESSION   WP_273596334
VERSION     WP_273596334.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 536)
  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 536)
  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 536)
  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..536
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..536
                     /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=55701
     Region          7..97
                     /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(8,10,44..46)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239361"
     Region          104..520
                     /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 msataavkly vpcdsaalav gadavaaali dgcrqrgwpv qvvrngsrgl fwieplveve
       61 taagrvaygp vtsadvpsll dagllqgaph vlchgltaqi pflarqhrlt farmgvtdpl
      121 sladyeaheg waglrraasm agaaivqevm dsglrgrgga afptgikwkt vmaataaamt
      181 gpaaaqkyvv cnadegdsgt fsdrmtmegd pymliegmai aglavgatrg yvyiraeyph
      241 avatmneair ragaagwlgd daagsgrafh levrkaagay vcgeetamle siegkrgvvr
      301 akppvpalqg lfgqptvinn vislasvpli largaafyre cgvghsrgtl pfqlagnikq
      361 gglievafgv slrelmfdfg ggsrsgrpik aaqvggplga ylpesqwdlp ldyeayasvg
      421 avlghggivv hddqtdmakm aryamafcal escgkctpcr igstrgvevl drvaqggqrg
      481 qqiellrdlc etmtqgslca mgsmtphpvl salnhfpadf glstaapdtp atgpdi
//
LOCUS       WP_273596725             423 aa            linear   BCT 28-DEC-2024
DEFINITION  Glu/Leu/Phe/Val family dehydrogenase [Roseateles koreensis].
ACCESSION   WP_273596725
VERSION     WP_273596725.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..423
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..423
                     /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=45520
     Region          13..421
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
ORIGIN      
        1 mpnlsfvspt rnspwgtyls qidavepylg klarwvetlr rpkralivdi pieldngsia
       61 hfegyrvqhs ltrgpgkggv ryhpdvtlee vmalsawmti knaavnlpyg gakggirldp
      121 kalslkelek vtrrytseig iiigpqqdip apdvntngqi mawmmdtysm ntgatatgvv
      181 tgkpialggs lgrvqatgrg vfvigreamr rlhidmegar iavqgfgnvg siaaklfaan
      241 gakvvavqdh tgtilnesgf dmqnlldhva atggvggfkg gdaianddfw kvksdvlipa
      301 alegqinker aeglqtrlvl egangpttpd gdavladrgi vvvpdvians ggvtvsyfew
      361 vqdfssffwt edeinvrldk iitgafkhiw dtseihrtsl rtaafvvact rvlearverg
      421 lyp
//
LOCUS       WP_273596933             543 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF1302 domain-containing protein [Roseateles koreensis].
ACCESSION   WP_273596933
VERSION     WP_273596933.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..543
                     /product="DUF1302 domain-containing protein"
                     /calculated_mol_wt=57728
     Region          25..429
                     /region_name="DUF1302"
                     /note="Protein of unknown function (DUF1302); pfam06980"
                     /db_xref="CDD:462059"
ORIGIN      
        1 mkkpnfgagv laaaaataca cahaetfsne yfagsfdstl slgtgirtka psgaliiegn
       61 qggpagqlai tsamgdqgdl nyakndafts ylkgshelll kfpenitama rvswlrdfta
      121 arttgwtsat tppgldgnla ddarsdlkfk arlldlwvsk kfeiddqsvr vrvgnqvisw
      181 geslfvpggi nvtnavdvmr lsqpgtqlke ailpapiisa aaglgnglna eayvqlgwna
      241 nympptgsyw svsnglgagh dayglqegka rnsgqwglsl ryqpqgtqln lgayvinyhd
      301 ksptftfnnp ngamgwvyge drklyglsan fplgdwaigg evsyrpkdav tlnaangcts
      361 qngtcavdta rvqmaltalf slspdasptl lkvlgadsgt llaeavairf pnlksqygdd
      421 liaaggwgwg qeksatgvpl avgsknssgf nfdfswvydg tlipgwqvvp evyyfralsg
      481 rtpngaatfm qgassanyvv sfiqnpakwq fainyarfmg gdsafdqpyr drdfiglnls
      541 rnf
//
LOCUS       WP_273596852             195 aa            linear   BCT 28-DEC-2024
DEFINITION  KdsC family phosphatase [Roseateles koreensis].
ACCESSION   WP_273596852
VERSION     WP_273596852.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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 195)
  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 195)
  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..195
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..195
                     /product="KdsC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=20312
     Region          26..187
                     /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 mhtlqaalrf ppellvkaqg tglglkaaif dvdgvltdgr iyigeqgelf kafstldghg
       61 lklldqagit pivitgrdsp avrrrvadlg lrhavygakd klavalplln slglawgeva
      121 amgddwpdlp lmtragfaca paqahaevka iahyvtqaag ghgaareccd vilqacgryq
      181 tllnghldtl dggva
//
LOCUS       WP_273597090             208 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Roseateles koreensis].
ACCESSION   WP_273597090
VERSION     WP_273597090.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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=22344
     Region          16..123
                     /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 mtthplhptp aaslppavsp wllrwpqtlm pgaraldvac gsgrhvrwla qaglrvtgvd
       61 rdaaataplq plaeiitadl eggpwpladr qfdlvlvtny lwrpllpril aavapggwli
      121 yetfalgqhv igrpsraefl lrpgellqic qglrvvgyed gfepgaelpp gdtkiappvn
      181 gryvqrvaav rappaddgvf lryalpgr
//
LOCUS       WP_273597111             107 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Roseateles koreensis].
ACCESSION   WP_273597111
VERSION     WP_273597111.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..107
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12034
     Region          7..79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
ORIGIN      
        1 mddwwiqrie glkqqaklsd valakrldis pamlahvrvg rralplqarl rlldalgyvi
       61 trdlllrvlp eevraavvdt naamteahyr pketgaddsl elppewr
//
LOCUS       WP_273597115             427 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Roseateles koreensis].
ACCESSION   WP_273597115
VERSION     WP_273597115.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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   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..427
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..427
                     /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=48062
     Region          38..381
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mlttfvaktd sscvidgkvy pdlpllmtnd gilevqsdyl reltvmrgls pasvnemsky
       61 lrthvhimda gglsweqtne valrrwrneq agenpsnarr gylnqqlavi yhfliwaekk
      121 griqgvvgpl spadqstflv pveiarwhsd gtpahfklpl lyrtvgesdr rnatagqvde
      181 lfvalaneqn pylaernsli grfaentlmr rheiaallas qlpslgaaka acssgeelti
      241 slhitkgmka retivdpqlv idtwtfiean raemlqrrsl pdrsdlpifl swrtggkiha
      301 daltnlfssk qkqagvkras lhnlrskgat drveslidmy eqtgaplpde etlllqaqel
      361 lghasiattr tyirrekkrr adrkraehke ltdrserlrq ldreiairqa elarlakese
      421 vrtrvrd
//
LOCUS       WP_273597157             247 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Roseateles koreensis].
ACCESSION   WP_273597157
VERSION     WP_273597157.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 247)
  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..247
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..247
                     /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=26779
     Region          2..235
                     /region_name="YfcE"
                     /note="Predicted phosphodiesterase, calcineurin family
                     [General function prediction only]; COG0622"
                     /db_xref="CDD:440387"
ORIGIN      
        1 mkialisdlh anreaftavl ehaqgqgvgd yallgdfvgy ggdpawvvdr vralvdagai
       61 avmgnhdqaa ikgaaptmhe eareavawth aqlsaeqrdw laqlpmsvir ddrlyvhana
      121 yapsgweyiq grmeamrslq atecrytfcg hmhepmlyhl sgtgkageft papgtpipll
      181 pnrqwlvvpg scgqprdgnp aacyaifdsv sselsfqrvp ydieaaaqri raaglperla
      241 qrlsqgq
//
LOCUS       WP_273597183             285 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Roseateles koreensis].
ACCESSION   WP_273597183
VERSION     WP_273597183.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 285)
  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 285)
  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 285)
  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 285)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 285)
  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 285)
  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 285)
  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..285
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..285
                     /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=31683
     Region          10..285
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mtsfasrpaa liaddepllr eslaralnai wpelqivgqa rngrealemf ealrpdivfl
       61 dvhmpglngv eaarqlarra qivfvtafdq yavqafeqga ldylvkplee krladtvqrl
      121 qerllarsnh spvdkdappa eaargdalet learidmlmk qlsrsaeapp aanggsppwl
      181 qwirasvgat lklipvdeit ylrsdekytl vvwgegeali rtpirelmaq ldpqkfvqvh
      241 rsvvvnlhav shvtrgpnet advhlrgrae vlpvsrsylh lfrqm
//
LOCUS       WP_273597363             408 aa            linear   BCT 28-DEC-2024
DEFINITION  metallophosphoesterase family protein [Roseateles koreensis].
ACCESSION   WP_273597363
VERSION     WP_273597363.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 408)
  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..408
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..408
                     /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=43304
     Region          81..383
                     /region_name="CpdA"
                     /note="3',5'-cyclic AMP phosphodiesterase CpdA [Signal
                     transduction mechanisms]; COG1409"
                     /db_xref="CDD:441019"
ORIGIN      
        1 mshapvfsgq grlraaltla alaaasfags vwaqnttpvv ftfsavgdsr qdpinfdkas
       61 vgstlngqda twlqntkatt rilrtiqsqk asmlffngdm vhgygwagfg ytsnaaqssi
      121 naspvapasv sdvvssdlvk fyqqygfwrg lmapmmetgt yvfpvagnhe vqckacgkks
      181 kvenenawaa nmgdlvldts rftgilgtap qnvnygpavg sspdglstdq sklsysfdyk
      241 gmhfavintd pvgmesrapt qwlsadlaaa kargmkksfv fghkaaytya ylantataag
      301 gldaapgsta erdafwdvie angatyfcgh ehiynisrpr ggayqvivgs ggspfdakst
      361 dvtkspatdr syawatvkvh qdggvdvlgy gfdehfgptq llqqiylp
//
LOCUS       WP_273597421             715 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Roseateles koreensis].
ACCESSION   WP_273597421
VERSION     WP_273597421.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Wintjens,R. and Rooman,M.
  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 715)
  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..715
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..715
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=78845
     Region          16..66
                     /region_name="HTH_XRE"
                     /note="Helix-turn-helix XRE-family like proteins;
                     smart00530"
                     /db_xref="CDD:197775"
     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 matdevlsav elgrhlmqvr ersgikqael akrvslsaav lsriesgdrp vtreevqdil
       61 vqlgtpeaae lakavqrtwk vlprppldhp dqdllwdadl vahelvelre rpdtphafer
      121 rlseyidelg rgatmllkre hqvafigsig vgkstaickm tglevqkddg tmtpvlevgg
      181 ggitvcevhl rtgpefgliv epkgddelrq dvldladsil kgvpapdedg psgqesqgis
      241 kevaralrnm aglavqrpkg adgkrttvdp akqlaqqfpt qrefvvevls rmdlhrrdkr
      301 diwydsasgk apktwlretf aainngrsse ftlprrievv vpekllqvad ltvrfidtkg
      361 idrnaaredi echfddphtl avlcspfnna paaearllle rakdagirtl dtnaallvlp
      421 rptealamkd datsapvesa eegyelkgeq ialaleplgl qtlgvafyna nedpaasaqe
      481 fllerltkar aafrtriaea ttgaqallrn hgeerihavl rdagetlhtw alqnaavqpv
      541 qghvqeslma qiqvayastv raavrregew pqlsyshhig ygarrlavma lekpveqftg
      601 hcrlmaatps yaeaadllvq aervltvsye ellrkvqlmg qtvfkdalka dpmlwqacmd
      661 ewgqgpgyks rvaghnrdwf ndgarrklqd elqaliarew tralanvtal lepqq
//
LOCUS       WP_273597466             348 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Roseateles koreensis].
ACCESSION   WP_273597466
VERSION     WP_273597466.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 348)
  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..348
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..348
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36438
     Region          1..338
                     /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 mkpplhgvri vefeglgpgp lagcmladmg aevtvitrpq kgavlmqlgg ntanpllrgk
       61 tvlaldlkqd agrtealrlv aaadaliegn rpgvmerlgl gpadaaalnp rlvygrmtgw
      121 gqsgpwahta ghdlnyvals gllslsarrg erpmvpptvl gdasgalgla fgiacalfea
      181 rssgqgrvvd gaiidilaml ggiaqlvrag gqldspapsp fhdspfydvy acadgshiti
      241 galepqfyal llnklgltdv dpaqqydtht wpalkarfsd lfasqprahw esllggtdvc
      301 fapvlslgea alhphnaare iyrvdasgmm qahaaprflp lgdpqder
//
LOCUS       WP_273597547             140 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Roseateles koreensis].
ACCESSION   WP_273597547
VERSION     WP_273597547.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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=14725
     Region          <5..131
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mprqasplgl ilqlcllgls gamlaahaqd kplapqtppv ltqaqdtppg parqaqlrri
       61 lsqdcgschg ltlkgglgpd lrvdamralp htaiastiyd grpgtpmppw ksmitraeae
      121 wlasylqqep papspkdvtp
//
LOCUS       WP_273597554             141 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Roseateles koreensis].
ACCESSION   WP_273597554
VERSION     WP_273597554.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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=15750
     Region          50..128
                     /region_name="Cytochrom_C"
                     /note="Cytochrome c; pfam00034"
                     /db_xref="CDD:459641"
ORIGIN      
        1 msrgftsqma rnifyggtlf fvllfaalif nteqripqrs naaaltpavv rgkhiweann
       61 cigchtilge gayfapelgn vytrrgpefi kawikaqptg apgrrqmpnf hlndqqlddl
      121 veflkwtngi ntekwppnve g
//
LOCUS       WP_273597564             806 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Roseateles
            koreensis].
ACCESSION   WP_273597564
VERSION     WP_273597564.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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=85364
     Region          14..759
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mtlkhhkkst vaqaawvlsa llagqawaad aestakidpv tivgsrakvr tvidsdvpvd
       61 vfsrqdiera masgdlgeal qalspainmp kvsasgtsdt vraiqlrgla pdqalvlvng
      121 krrhtnavld qeglfpgtva vdlntippsa ierievlrdg agalygsdav agvvnivlkk
      181 raeggsayvs fggyhtafsp tgktlndgqn lqmgadagfa fgqggsvhvg fdlqhkngsn
      241 ragpagdfsw nstpadtarv gqvlyksgdp dlrntqlfyd aslpvgggle aysfatynhr
      301 eaegaaffrw pgdpgnvpav ypqgfrpett nkindgalvv glrgdvqdwh mdaslrhgen
      361 rfeyglknsi naslgatspt rfhlanfiss qtglnvdlrr sfdnaplpwn lalgaevlhd
      421 hyetqpgdpa syaagalgga pgsqgdpglq pqnavnlgrt aksiyvdvds ditdrlllga
      481 alryadyags gnqttgklsg ryklsenflv rsalsnsfra palaqigfrn stldfnadqt
      541 glvnaallpa tdalakqfga qplkpetstn fslgfaaqla kstsltvday qirikdrisr
      601 ssdlngsava aylssigrsd iesvafltna ldttttgvdv vvshattlqg galnlsaaln
      661 lnqnhldavr nsstalsaid pslslfsdkt lfdlmhqspk nkliltadws ggawslmara
      721 trygefsvms yagpevkyha dwgvdleaql kltqrlswsv ggnnvfnryp dqsgpndnla
      781 gslpynyvap igingayfyt rlslaf
//
LOCUS       WP_273597654             193 aa            linear   BCT 28-DEC-2024
DEFINITION  RBBP9/YdeN family alpha/beta hydrolase [Roseateles koreensis].
ACCESSION   WP_273597654
VERSION     WP_273597654.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 193)
  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 193)
  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 193)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..193
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..193
                     /product="RBBP9/YdeN family alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20829
     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 mktppiyllp gwlnsdpdhw qsrwetalgh srveqsdwew prrgdwmarl devllgdarl
       61 netpavlvah slgcqlvasw aahsqhtarv agallvappd sehpqmppql hnwrpiarqr
      121 lpfpsvavis tddpfcapdr aaemaaawga kllvagplgh lnsasglgdw pegqallael
      181 sqsagpvhra gpa
//
LOCUS       WP_273597626             140 aa            linear   BCT 28-DEC-2024
DEFINITION  MerR family transcriptional regulator [Roseateles koreensis].
ACCESSION   WP_273597626
VERSION     WP_273597626.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 140)
  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 140)
  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 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   4  (residues 1 to 140)
  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..140
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..140
                     /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=15759
     Region          17..134
                     /region_name="HTH_GnyR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     regulatory protein GnyR; cd04776"
                     /db_xref="CDD:133403"
     Site            order(18..20,34,50..52)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133403"
     Site            order(63,66,70..71,80,101,105,111,115,118..119)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133403"
ORIGIN      
        1 mtssastsva eaqgrlftit elaaefditp rairfyedmg lleptragrn riythrdrtr
       61 lkltlrgkrl glslqeikql vdmydsdtdt asqlkaflav lqqhrrqlqq qlddiaitla
      121 eiaqheerce slladaqagr
//
LOCUS       WP_273597696             689 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Roseateles koreensis].
ACCESSION   WP_273597696
VERSION     WP_273597696.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..689
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..689
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=76052
     Region          421..680
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 msacllamgl cmgawaqpvp vataaaapvt lapipveaff qwpkvmqvkl spsgrqlalt
       61 tsrnnnrvgl vvitlggsge aptagyvagf sdadithfdw vgdkrlvfsa idlqagsged
      121 yrlapglyav dadgsqmrql vkrrgrqffv dgnvidrtle wnhillatpk qqpgvasdev
      181 lighmdfidk rvrqitpmwl ntrtgrthsa avfgapsqtv awkfdsrgep rlavtydegr
      241 qrvhwrapge sqwrlisesd lltppfhpvd vddagtlylt ygegargdav lsvfdfekga
      301 pqkpglvstp gfdyrgnlvl drpggralgv tvetdaeqti wfdpemkqlq alvddklpgr
      361 vnrlscrrcg addmvvlvrs fsdrdpgrly lyeaadqrwk fistvlddid prrmatvdlh
      421 ritardgrdl pvwltippgv qpghpapavv lvhggpwari ghwqwqameq flasrgylvi
      481 spefrgstgy gdahyragwk qwgqsmqddv adallwaraq gwadkeraci agasyggyat
      541 lmglvrnpel yrcgvawaav tdpflfiqgs wwvdddisgd grkyylqhmv gdaekdaaml
      601 taaspvaqak riqaplllaf gesdrrvpia hgrrlrealt daghppewvs ypneghgwrl
      661 msnqidwaqr vekflaqhlq adskaevah
//
LOCUS       WP_273597040             394 aa            linear   BCT 28-DEC-2024
DEFINITION  S1C family serine protease [Roseateles koreensis].
ACCESSION   WP_273597040
VERSION     WP_273597040.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 394)
  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 394)
  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 394)
  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 394)
  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 394)
  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..394
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..394
                     /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=41013
     Region          120..390
                     /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 mrrlwlifaq attvtlaivf vlntlkpnwl arprptapat vvlgappsap lsgldaaera
       61 ahpthtgysr aarraapavv svmaskapar naeleararr yhfglpdrsn natqepsqtg
      121 lgsgvivssq gylltnnhvv egaadievll sdgrqtkatl vgtdpetdia vlkieldrlp
      181 viqlghiegl qvgdvvlaig npfnvgqtvt sgivsalgrd qlgintfenf iqtdaainpg
      241 nsggalvdtd gnlvgintai ysrsggslgi gfaipistas qvmeslirdg rvargwigvq
      301 treltpefid afklsvregv lisgvlanap aakagikpgd vitqigpkav htpaqlllav
      361 savppqtatk vsvlrgkqsl eldvtvaqrp vpkp
//
LOCUS       WP_273597731             336 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Roseateles koreensis].
ACCESSION   WP_273597731
VERSION     WP_273597731.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 336)
  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   2  (residues 1 to 336)
  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 11427312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..336
                     /product="ABC transporter permease"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36188
     Region          1..333
                     /region_name="DppB"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0601"
                     /db_xref="CDD:440366"
ORIGIN      
        1 mltfllkkla tliptligit avafglirlv pgdpieimmg erqldpaaha alvhrmgldq
       61 plhqqyfdyl gklahgdlgq slvsrepvar efavlfpatv elascallla vsvglllgmw
      121 aslrrgswvd qgvmglatvg ysmpvfwwgl vlimffsvgl swtpisgris veydptmrtg
      181 fmlvdawnsg eagafksacl hlllpalvlg tgtlavvarm trsamlevlr edyirtarak
      241 glsparvvav halrnalipv ltiigmqtgs llagavltet ifswpgigkw lidaiarrdy
      301 pvvqagilis altfigvnlv vdllygvvnp rirsph
//
LOCUS       WP_273597967              88 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator, partial
            [Clostridioides difficile].
ACCESSION   WP_273597967
VERSION     WP_273597967.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
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   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 88)
  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 amino end.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..88
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          <2..71
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 pselrrqisg isqkmltqel relerdhivn rktynvippk veyslsdygq tlstlldqvc
       61 swgemhvqtl qkngvdvkln stgisgrn
//
LOCUS       WP_273597996             436 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Roseateles koreensis].
ACCESSION   WP_273597996
VERSION     WP_273597996.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     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=47911
     Region          33..403
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mtllsvdhel trdsyylats rretsheplq qtihvdvaiv ggglaglsaa ielaqqgrsv
       61 aileagqvgg gasgrnggql ihglacdqet ieqqlglada rrvwamtlea ldivqerctt
      121 hqidadrqgg flslattpgk aaqlqkwqqr maeiydypmt wipqahmadw iesprfkagl
      181 hdprsghlhp lkyclglaaa akrlgvqiye ntavtrmdeg qvltlhtatg qirasqalla
      241 gnvylperap klahqlsari mpvgtyivcs epieaqrfer lipsrsavcd tnfvldyfrp
      301 tpdrrilygg rvsystrspr svkdsmaerl rlsfpqlsdv gmefawggfv ditmnrapdf
      361 grigqanniy ylqgfsghgl altglagriv aeaiqgdser fdvfsrlkhk pfpggkllrm
      421 palvlgmayy rlkdll
//
LOCUS       WP_273598285             393 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Roseateles koreensis].
ACCESSION   WP_273598285
VERSION     WP_273598285.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 393)
  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 393)
  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..393
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..393
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45413
     Region          1..393
                     /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 mlikffytlr aaklpvsvre flslleglka gvigsdgpps iddfyflara tlvkneahfd
       61 kfdrafsayf kgvelltdfs kevplewlrq hlqleltpeq kaaiekmgwd elmetlkkrf
      121 eeqkerhegg nkwigtggts pfgnsgynpq giriggasrn ksavkvweqr aykdyddnle
      181 lgtrnikval rrlrrfareg seleldldnt ihktaanagm ldirmiperh nkvkvlllmd
      241 vggtmdehih rveelfsaak sefkhmeffy fhncvydfvw knnrrryaek tptwdiirky
      301 nrdyklifvg datmspyeil qaggsveynn eepgaewlqr lanafpkyaw inpepqgvwq
      361 yrqsvaliqq imhqrmfpls laglegamrl lsk
//
LOCUS       WP_273598226             366 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Roseateles koreensis].
ACCESSION   WP_273598226
VERSION     WP_273598226.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 366)
  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 366)
  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 366)
  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 366)
  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 366)
  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 366)
  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..366
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..366
                     /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=39642
     Region          68..350
                     /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 mrytdslars aehlraalpl mtrqraalhp vsyavwyefv sarnlalhqa vlthtrdgat
       61 ldeaqtwaly qdhigsqlts ldaataqkvg dglarvldtm aasaaeagqe tarfdnslnt
      121 wveqllgdpn qqtqadvlqe llsgsreirg avgalqsqls qsqheiealr qevrharnea
      181 lvdaltglsn rrafdqalst clansahkpd dpkaaastap clvlgdidff krindsfghg
      241 fgdqvlrava qtlktvaand iitariggee falllprssl dqaeglaekm rstvakgrir
      301 rgeqaqeqqn vtisfgvtql apgesandfl nradralyas khqgrnrvtv ltsdsndaqe
      361 pvklra
//
LOCUS       WP_273597733             195 aa            linear   BCT 28-DEC-2024
DEFINITION  IMPACT family protein [Roseateles koreensis].
ACCESSION   WP_273597733
VERSION     WP_273597733.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 195)
  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 195)
  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..195
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..195
                     /product="IMPACT family protein"
                     /calculated_mol_wt=20530
     Region          4..193
                     /region_name="YIH1"
                     /note="Putative translation regulator, IMPACT (imprinted
                     ancient) protein family [General function prediction
                     only]; COG1739"
                     /db_xref="CDD:441345"
ORIGIN      
        1 mactlahpvh seliikksrf iacvepmadr alatarvaal raehpgavhv cwallaggqs
       61 aavddgepsg tagrpmlevm rhqdlegala tvvrywggtk lgagglvray tdavaqalqk
      121 aekipllrqq tllctlpyaf egllrreiea agatllaveh gaqvqahfsl petaaatlva
      181 rlneagqgri gwlke
//
LOCUS       WP_273598286             622 aa            linear   BCT 28-DEC-2024
DEFINITION  autotransporter assembly complex protein TamA [Roseateles
            koreensis].
ACCESSION   WP_273598286
VERSION     WP_273598286.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..622
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..622
                     /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=67478
     Region          43..621
                     /region_name="TamA"
                     /note="Outer membrane translocation and assembly module
                     TamA [Cell wall/membrane/envelope biogenesis]; COG0729"
                     /db_xref="CDD:440493"
ORIGIN      
        1 mslsacsgla pfsrqaaapd akvqaataps dsasapqgvr mvaeytlnvq apselrellt
       61 enldlarfrn apadqrlgtq elarlsaaap qqaqsllete gyfnarvtvd rdltqtpivv
      121 tvkvdpgprt tiknvtfsfs gelappesgs aslpapqqaa qqqaeqlrsa lqgswplkng
      181 apfvqgawsn aktallgqar akgypqarle qsavhvdaet nsaeielqld sgplfrlgel
      241 hitglknqpp evierlsgyt pgdpyseqal ldfqerlvkt tlfdnvniti rpepdgpvqt
      301 pvwvevreap rqqlttslgy ssgngprvgl dytnrrpfgl nlrsrfkmnv sqenpsldwe
      361 lsshprtdmq rdlaalyler vvedakvsin lrarlgrlre tgaddriyyl evlrahetdp
      421 qqqinsgavs aniqwtrrrv dstlkpttgy taslllglgr adntiansgt fgrseltlhg
      481 yqllpggwyg sartnwseif srddvglpea lryraggdes vrgynlrdlg pvdsdgnatg
      541 grvmwtgsle lahaltaklp dlqgaafvda gqaamgwstl hptvatglgl ryrsplgtlr
      601 ldfahahatg nwrlhfsvav am
//
LOCUS       WP_273598292             557 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Roseateles koreensis].
ACCESSION   WP_273598292
VERSION     WP_273598292.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 557)
  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 557)
  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 557)
  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 557)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..557
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..557
                     /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=61622
     Region          <201..281
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 msepkepllg dpsrlvktrp mgngqftanw tltpdtitep vvfqintdvl piifvpgimg
       61 snlksvgrts dpvwrldatl gqpggllfdw gtasagqrqa llhpsrcevd dggatpqhlv
      121 gfvhelaqyr qrgwgevaet syhsfllhle atlnterwha lkkwihspgq gdaetlkawr
      181 aektaqvlse aevtetnhwr fpvyacgynw lasneeaakl lserikaviq ennqgqlhrc
      241 aqvilithsm gglvarrcqq lgmaeqiagv ihgvmpaiga pvayrrtkag mgdesmiagw
      301 vigslgsdvt pvfaqapgal qllpnaqypk gwlrllnekg qlidsfpkad pyeeiylnrk
      361 dwwglvkeew lrptggiqwt wkdytdkalk lakdfhtalg tsyhpntyvf cgepddlhek
      421 nsvaavswrm klspyqskki addklaglph saflepggsy vlkqepnpny nsqfggsyrf
      481 vqpwsmvmdl fdaggdgtvp avsgrapltq npqciqqqir lagfghekay qneaaqdwvl
      541 yalakilkka kvpqvkp
//
LOCUS       WP_273598303             278 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles koreensis].
ACCESSION   WP_273598303
VERSION     WP_273598303.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..278
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30052
     Region          39..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 mnaqrrawla raasaallah fagpaeatsl skirergtlr vgiyqdmppf hvaglgvdvd
       61 laqalaqalg vklsllpfna denmlddlrn mvwkghylgy gpadvlmhvp vdrplmdacp
      121 qvqilapyyr ervmiardvh klprleqlsq igtqtiavpg qtlagwlllg adqgayrqql
      181 stqwpdgcac aqalqrgeva aaaglaselq silrdqpqya iealplprlp regwaiglav
      241 kagetelart lqeavstlsq tgslrtlfea hkvgwtpv
//
LOCUS       WP_273598327             180 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Roseateles koreensis].
ACCESSION   WP_273598327
VERSION     WP_273598327.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 180)
  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 180)
  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 180)
  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 180)
  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 180)
  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 180)
  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..180
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..180
                     /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=19006
     Region          <11..143
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mhltqgtisr lvlstfcsll vagamasdka sirrgeylva lggctdchtp ghflghpdlt
       61 rylggsdvgf sipgagvfla rnltpddetg lgkwtreqiv taittgkrpd grqlapvmpy
      121 mafsrltpad aqaiaqylks lppvrnkvpg pfgpneapts fvfavlpadv ynampkppak
//
LOCUS       WP_273598348             699 aa            linear   BCT 28-DEC-2024
DEFINITION  prolyl oligopeptidase family serine peptidase [Roseateles
            koreensis].
ACCESSION   WP_273598348
VERSION     WP_273598348.1
KEYWORDS    RefSeq.
SOURCE      Roseateles koreensis (Kinneretia koreensis)
  ORGANISM  Roseateles koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 699)
  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 699)
  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 699)
  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 699)
  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 699)
  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..699
                     /organism="Roseateles koreensis"
                     /db_xref="taxon:2987526"
     Protein         1..699
                     /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=77950
ORIGIN      
        1 mpmaqdadtt analsdsdpy lwledvqger alnwvrerna astrvlqarp eykglrkdma
       61 evlnakdrip mvrrmgpwly nlwqdeqhkr glwrrtslae yqkpqpewet vldldalgaa
      121 enenwvfgga sclapdyrlc llslsrggad ahvlrefdth tkqfveggft laeaksessw
      181 idadtvyvgs dfgpgsltds gyprvikrwq rgtpisaavt vfegeaqdva vsvqvdhtpg
      241 yartifsral dfynqssfll dtraqsqgqt plvkldlpsd vqpyfwgarl lleprkdwtv
      301 tghtypagsl lmgdaaaflq gerkfqslft ptesrslagy tvtrqhviln iseqvasrle
      361 ewsftgaepq lrkiqapfpg tlsiaslyds elpaddladr yivnyadflt pdtlylaqag
      421 sderqalksr epqfnaggmk aeqffavskd gtrvpyfvvw pmgakadgkn ptllygyggf
      481 evsmqpaysg gigrawvkrg gvyvlanirg ggefgpnwhq aavkenkqrs yddfiavaqd
      541 likrkistpk hlgimggsng gllmgatfvq rpdlfnavvc qvplldmrry hkllagaswm
      601 aeygdpdqat dwafisqysp yqnvkkgvky pkvlfttstr ddrvhpghar kmaalmqaqg
      661 helyyyenie gghggaadnd qratlkamef aylwqqlkr
//
LOCUS       WP_273598490             763 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Roseateles albus].
ACCESSION   WP_273598490
VERSION     WP_273598490.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 763)
  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 763)
  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..763
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..763
                     /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=82301
     Region          117..>398
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          290..726
                     /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 msrrarltwv istvivtgvc gvlaflllig vssqrgffer hyvwlfwlna avasllvlvi
       61 gvaavrlvlr vrsgkfgsrl llklagifal vgvvpgvmiy gvsyqfvnrs ieswfdvrla
      121 galeaglnlg ratldglvsd lsdktlsaag rlsesggmpq plalerlrvq lgarsvdlvn
      181 ghgqilmssg gdtssltaer psegmlrlar vakvasqleg ledetlamqg qariralalm
      241 pnadyrlsss ssgerflmvv qrvpasvvan alavqaasge yqqralerdg lrrmyigtlt
      301 lvlilavfaa lllavtlgnq larpllllad gvrqvaqgdl srkpmlasrd elggltrsfa
      361 dmtaqlsdar amvgrsvael esarthlqti ldnltagviv fdaqarietv npgavrilrl
      421 ppedlrgrkl delpqlqpfa aeimqrfeqd rplrpsvaea slglgtehwq dafelqleag
      481 qdvltllvrg aklpqdarlm vfdditevvs aqrsaawsev arrlaheikn pltpiqlsae
      541 rlqhkleakl egadqamlvr svativnqvq smkqlvnefr dyarlpsaql kvldlnalvs
      601 evltlyaeaq esgllraela pdacaikgda tqlrqvihnl vqnaldavqe rpdgqvlvrt
      661 vqvftesgev rvlrlnitdn gpgfaekvlk rafepyvttk tkgtglglav vkkiadehga
      721 rirlsnlhva gddalavvga qvslsfskfs taavdagpad kpa
//
LOCUS       WP_273598559             986 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein [Roseateles albus].
ACCESSION   WP_273598559
VERSION     WP_273598559.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..986
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..986
                     /product="beta strand repeat-containing protein"
                     /calculated_mol_wt=99753
     Region          <47..869
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          606..622
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          624..641
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          643..661
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          678..697
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          698..717
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          720..738
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          740..757
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          759..777
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
     Region          779..798
                     /region_name="FHA beta-helical repeat"
                     /note="FHA beta-helical repeat [structural motif]"
                     /db_xref="CDD:293785"
ORIGIN      
        1 msvrqnwnpg vtpmgfdhlh fgtstfttvt ydplsnrsyd kisfdvgana ftlqsagnsl
       61 alshgivnns skvqtlvwsa sslfidgdqt wdggtagmni tggigqrndl tlsnkvaykn
      121 lgsaligdsg sgnskvslti nsgssfstaa dltlgsafpt ssgtinvqgv gsslvvgtdl
      181 ilgdvgsstl lidsgasass qrlfigkkgt akltvdgags sfssgdvsfs nselivsggg
      241 kftatinmtd sftpnenasv tvkdtgtlfk vdlgfylgsk gnglmqlskg ataeisslfi
      301 gqqstggfgv leatglgstl ktkvvigrag llnvsngaqv qvsdwmnige agessfaaav
      361 ggggallsva qaltvgsaga grldvlgggv vdvgqlvigd lgvvnlqggt lkmvtgniag
      421 tlnwdsgtln fksnyatgdf lghdmvlsag qilkgdaqir vgsgdsltfa ggalqaidfq
      481 mdanasakvg rasslaanti knygrlmldg gsvngallna gtmtgsgair anlgqggfin
      541 sgrfdqgdyv elvnpgsnin tgvwtlgkgg alqlrssnln nqglmslaga sigafdgtsk
      601 lvneaggmis gngvisasfa nqgslivegg klsvdkrfan sgqilltsai aslsggaidn
      661 sgrieglgqi gnainnqgfv sakggiltla aggisnrgtl svdrdatlrl tqgllpnmgk
      721 iqlaggtfdn ngfamsnevg avingfgsln sglltnkgki llsggnstiy admlstaasq
      781 iilsgnsnst fygnvdvqng aelrvstgsv atffgtvqqr tgakfsgaga krfegtltvg
      841 aspglgsdeg dvefgdssty laeiggitac tlrcgsdeaf knssfdkyiv agnlslngtl
      901 kltswngfva qkgqsfdlld wgtltgtfad idatgfklaa gtqldysqly tsgeirvmaa
      961 pvpepetyal mlaglgllaw rrrkfg
//
LOCUS       WP_273598620             450 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Roseateles albus].
ACCESSION   WP_273598620
VERSION     WP_273598620.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=48628
     Region          1..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 msilildddp dvgiaarlll qrrfgpvrll qrpaelaaal aaepvellll dmnfqpgqtd
       61 gaqgqavlre vlklgpkapp vivmtayaev slavaslkag afdfitkpwd nqkltatvaa
      121 alasrqttap vttsllgesr amrelraliq svapteanvl vlgemgsgke lvareihals
      181 kragqtflav dlgalsettl eselfghkrg sftdarqerp grfqaaeggt lfldevanlp
      241 lagqaklltv lerrevtplg adsaqpvnvr ivsatnldet slfdaqrfrp dllyrlntiv
      301 lrvpplrerr ddvplllkhy ldhyaeqygk paracseaal aacqahdwhg nvralrhace
      361 ravilaqgsq feaadfalqa pgnasieplr plqtmeamep ttpsplllsq lertalvdam
      421 qsvqgnisqa akllglsraa lyrrlekygl
//
LOCUS       WP_273598621             421 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Roseateles albus].
ACCESSION   WP_273598621
VERSION     WP_273598621.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 421)
  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 421)
  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..421
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=45203
     Region          79..421
                     /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 mdsrrafriw plllwatlmc lgaalagwqh daprplvlal llmlvglyga lcqmkrllql
       61 aeaglaeplr aapdsaraae ltqqrmllne allehapval whqsakgqvl plnnaarrlv
      121 apggatdsad lfarlaqpre qsaghslfsf esergsercl lasrdlvlsq sperllalmp
      181 ieseleaetl kawrqlvhvl theimnsltp isslsrtare llaeqgaahq edrqdltlam
      241 dtiarradsl asfvgnyrrv selpepklep vrlnelfarl eklagadwaa rggaavfave
      301 pasltlmada gqleqallnl iknaaqatge qakphlsvra rlvrggrlsi evrdngpgvp
      361 agmetdiflp ffstkplaqp glaaggqgig lavvrnlvhg mgggvryvkp vsggaafvls
      421 f
//
LOCUS       WP_273598625             169 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA recognition motif domain-containing protein [Roseateles albus].
ACCESSION   WP_273598625
VERSION     WP_273598625.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 169)
  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 169)
  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 169)
  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..169
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..169
                     /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=15499
     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 aysvrdetlq eafsqfgqvt sakvmmdrdt grskgfgfve mgsdaeaqta
       61 ingmngqdid graivvnear preerpggfg gggrsggggf gggggrsggg gygggggggg
      121 ygggggyggg agggggrsgg ggyggggggr sgggggyggg ggrsggggy
//
LOCUS       WP_273598739             253 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Roseateles albus].
ACCESSION   WP_273598739
VERSION     WP_273598739.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=27838
     Region          4..251
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mknikaliad deegpreqll aalkrlwpel divaasengv dawddylehe palcfldirm
       61 pglsglevar rmselaappq vvfvsaygdh alsafeagav dyclkpveda rlaqavqrvq
      121 arlsaaapqa gdlqkmlqql lpaakpvsrp iqaslgreik liapeeviyf esdnrytrvv
      181 yqggealirt plkellagld aeafwqlhrs vlvnsrcias avrvdensmh vtlkgreekl
      241 pvsrqfqglf kgq
//
LOCUS       WP_273598734             935 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Roseateles
            albus].
ACCESSION   WP_273598734
VERSION     WP_273598734.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 935)
  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 935)
  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 935)
  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 935)
  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..935
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..935
                     /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=100740
     Region          14..890
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mmflkthkas avrlaviaam gamtvsaqaq naqlerievt gssikrisse galpvqvisa
       61 kdiarsgats vsdvirnlpa mqgfqiadta agtnsggist anihdigssy tlvllngrri
      121 aptgdgstvn lnsipmsaid rievltdgas alygsdaiag vvnfvlkkny qggnvvasgm
      181 vplegggksa yasltygigd idkdrfnvlm syrhdqqqql katdrafgst ayipfeyggk
      241 qyiydrtsps avpanvtvta kngangkplf payafnpyak anggkcadrn fsnltnvvgv
      301 qetcgfdyan tieiypeskr dslfvsgqfk vndklsfysd valarfdlta riaanpvpva
      361 iptstdlfak yvapyltptq ianlsletdk tspnfgkprv tasyraqdfg trdsqtitds
      421 khfvigaeae lagwimnggl twsqnsinek yvggyfkkne fismvqknqf dpfaeagkqt
      481 patlqlmads iyhgtvrnge ttltgadfra srelyklpag dlslglgadi reqqytntpt
      541 adavngviyn yaaantfdvk rksggvfgel lipviknlel taalrydtik ktdnavtgks
      601 vgedlsatty kisgryqvvp qvllrgsygt gfkapdmltl aspllsngvt aasfdcpfpg
      661 tspcqptrrq ysqlaggnel vkpekseqma fgirfepnas fgigadyynv yitdaisgvs
      721 aaqafaepak fanlfttyqq paedkpyyaf ksvstnigrs knsgidwdiv grtnlenlgr
      781 ltlglagtyv iessytlpgt ndqytnslgq yndvsasvtf rnkvlatatl dtgkftnsft
      841 lnwksgykdk ladvrdvatn kltkvavdvp rsstldwqgv yrhnkaatlt vgvknlfnre
      901 pefslrdssg hqvgydpryg dtlqrrvyvt ggydf
//
LOCUS       WP_273598833             417 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Roseateles albus].
ACCESSION   WP_273598833
VERSION     WP_273598833.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..417
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..417
                     /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=47136
     Region          8..380
                     /region_name="WecH"
                     /note="Surface polysaccharide O-acyltransferase WecH [Cell
                     wall/membrane/envelope biogenesis]; COG3274"
                     /db_xref="CDD:442505"
ORIGIN      
        1 mhsqttsstp psrlffldwl rilafsllvf yhvgmyyvsw swhvksatlv taleplmmls
       61 spwrmallff isgaatqall rktqgvgllk qrsarllwpl lfgmfiivpp qsyfevvykl
      121 ayegryldfm qrylaadpnf crieagarrc ltvptwnhlw flpylwiytv lawalvkasg
      181 plldrlsasv arsapatlml glalplmfsr ltlvqfegtn npvwdwysha qylsvfllgl
      241 lcmrgtadda glwgriarlr wpallmalaa wgllqgyfsy yaeieppyll rmatrllwga
      301 mqwwaimaac gfakqwlnfd svwrrrlsaa vfcvyilhqt viillsqalr plglapgiea
      361 pmlialtfai calgyllarr lppalglllg ihekadtqkt retatfgans tacktlq
//
LOCUS       WP_273599052             297 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles albus].
ACCESSION   WP_273599052
VERSION     WP_273599052.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 297)
  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..297
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..297
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=32779
     Region          43..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 msedlpqdct grtrvfrqpr rllcwilagt faqlapalaa pelrflttey ppysspkleg
       61 ggamewvlra aleprgyviq vqpvpwaris reiaqgqvdg vmllwptdvt elgllptqpv
      121 fishlgffvr reqwqgqgis nwqmlkgqtv gvvrgytypd qlhatgavle pslsdlhnlk
      181 klaakrfdya aleratgehq laqdangelv rklvwqapal vsipltfgiv pgrpgaerll
      241 nelelglqql rgqralkaml dkfkvdpaaa lqpeplpalk lrraspanpn arpskpq
//
LOCUS       WP_273599050             938 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Roseateles albus].
ACCESSION   WP_273599050
VERSION     WP_273599050.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=102503
     Region          63..472
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Region          505..938
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mlripfrlsg vllalvlaqv lapnsveaka sqpktsiaaq anatthtank taqqpvfvre
       61 lggiaeyrlp nglqillfpd eaqstttvni tyrvgsrhes qgeygmahll ehlvfkgtpt
      121 hrdipgafaa kgirfngttt ndrtnyfasf nanpdtlnfa laleadrmvn sfiaradldk
      181 emsvvrnefe rgenepmqvl fqrvqavayd whpygnstig arsdienvpi erlqafykrh
      241 yrpdnatilv agrfdpastl akiaehfgpl kkpeqpllqt ytqepaqdge rtvvvrrvgg
      301 qpalvayyhv paiahadsap llvlsllmsm ppsgqlykel vesklalhag lgglggqapg
      361 gitaiaippt qeqadkvekl lldlvegrag kpfteeelqr vrdvalnsyr eqmknpeali
      421 qqisgllgag dwrllfqlme dlprvtladv ervrkaylqp anrtlgryvp advvtrveip
      481 aappldqrla dlkgppkvee gerfdptpak lqertvmktl psgivlqtla kqtrgnnvqm
      541 qmqlrwgere atfarrgtgw vgelmmegsa glskqalqda lirlkagmsi sggdqgatls
      601 itaeqgslie vlqlaarlmq apalpneafd rikqaglagl qssrqelevl rreavrahyn
      661 ralgvqlghp dyqlsldeqi tqlqetqlad vrsfhadyws anearvavvg alpagleaav
      721 eqlfggwkkp aatrfvrhsp ahmaipaarf dvlardkana alrmrldfkl seadadfvpl
      781 nlavqvfgag gmesrlstrv rqqeglsygi gaglnapfwg ndaslsiggs fapqnrdavi
      841 alvqdelrrm netgiseael qrakkdlaea rlqaraseaq lagtlnllad rskdwayvaa
      901 rdaaiqaatl eqvnaawrrh ikaegfvist vgdfkdkp
//
LOCUS       WP_273599017            1047 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Roseateles albus].
ACCESSION   WP_273599017
VERSION     WP_273599017.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1047
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..1047
                     /product="ATP-binding protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=111767
     Region          3..1042
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
ORIGIN      
        1 mfcprcqaas paggrfcaqc gaplpasdav qrssrrqmtv lfcdlvgste laqrcdpddw
       61 laalqqyhdl vrrvsarygg fvarivgdgv dvyfgyplan eddaaralht glnlaaelpr
      121 ievepgvpls lrigiatgmv avsvgqgvav agptpnlaar iqaavppgai gvapstrhia
      181 ggqfefaelg ehalkgfeap vainvvrral sqdsrsawrg rdtrlpmvgr raelnslqai
      241 wqrasagrtc galvlgepgl gksrlvtald lvlpaqghtm lrlqcspfhv nsalqpfvqh
      301 lavaaglsss dsnpvkldkl eaqlaiggie dpsdcaliaa llgvasdgry palampppmq
      361 lqlikealkh yfsglahqrl spaneqtltr yfvghaeerp lllviedmhw vdptslelie
      421 qllasgddas illlmtarhd fssrwqdgen flqlvlqrlp dedafavaaq qlqqadlppq
      481 wlaaiiertd gvplfieemt hmllerraap sgavglghav petlvdllte rldrlpaaak
      541 elaqvaavig refdrellfa aapelegglq aalqamldsg lllsgsadge rllfkhalve
      601 dtaygsvpak rcaeihgrla dvllsqfktr vhhqpelaar hlsragrgle aaawwqaagg
      661 qalsrgapre aaghlragva alggvaasae rdraelglls mlgpttmvll gpgsdefgsv
      721 qqrayelsqt lpgqpllfpt syawclfnwg rarlveagel adglllaaal rageteaala
      781 ahtmagmvqf hrgqpeaara hlsqstalye pqrdaalypv ylmdfgvfgr fylalatqvl
      841 gfadaarria aealllaegl nqphtlgfam lanfntavmr gdaaealpma erciefssqf
      901 gfpefiamar iargwawahg qarwaeglae lqagiagwae tgfenwqtwf avleaemlgq
      961 lgqhgaalal merqlarvaa ngehqfesll lgeraaalaa lpgrsaeaka eaqaeanfes
     1021 aaalareqga aawsqriasr raqvlpq
//
LOCUS       WP_273599059             267 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles albus].
ACCESSION   WP_273599059
VERSION     WP_273599059.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..267
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29315
     Region          28..235
                     /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 mlirssillm cltasvwaen gpgvqavvra cghpaappms wdhegqligv cveaarrafs
       61 avgltlkvep pipwarcqlm vengevdvnl cafandkrre yavmveppig hneavlivrr
      121 dsslvykswa dlkglrigmg rgvsfgsdfd nylaqharld ialsearnlq kltlgrldav
      181 itarlagqql irsmgcegql rllpaqvteg rllmqmskhs khlavlpqlt aflkrpaqve
      241 wlqaqhirfd atyaqlhpaa qtrvcep
//
LOCUS       WP_273599069             447 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Roseateles albus].
ACCESSION   WP_273599069
VERSION     WP_273599069.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 447)
  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 447)
  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 447)
  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..447
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..447
                     /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=47978
     Region          32..374
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 makvkftapk vaafkcsadk aqafmwdsta pglglrvtpa gkpsyvfqgr yeektirvti
       61 gspdawsipe aqaktrelqr qidegrdpre vkaaitaadv akreadrgqg vtvaevwpry
      121 laegkpkrrt awkpgyradl eavasmggvp kkrgqgltkp grlsalmalp lasidqdlir
      181 dwyakeaktg pyqasramam fsgflgwcat kkdyralvdk taaraselgd vlpevnrrtd
      241 cieidqlpaw fsgtdklrsr aaaaylqclv ltgarreema glrwadvdfq wskltiadkv
      301 dntrtiplsp yvasllaglp rtgtlkngka npfvfasals asgritepra pledvlkdag
      361 iphmtihglr rtfsllgeaa gapagaiaqv mghkpsatae gyrprsidal rpylalieaf
      421 ilekagitfd paaagagagg lklvasa
//
LOCUS       WP_273599099             596 aa            linear   BCT 28-DEC-2024
DEFINITION  bifunctional metallophosphatase/5'-nucleotidase [Roseateles albus].
ACCESSION   WP_273599099
VERSION     WP_273599099.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 596)
  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 596)
  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..596
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..596
                     /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=62496
     Region          68..580
                     /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 mpsihstspa hscarasnqg garstlnala alavaamlaa ctgvlprqae pgetraakpa
       61 skldasaspr elsifsindf hghiqpkspt plmprlpdaq tgelkpqaag giaylasams
      121 klrsgrehsv fvaagdliga splysallkd epslaalgel dlvasalgnh eldaglmelk
      181 rkangecpal gcawpeykgp gfpylaanml daqtgkpvlg thiikevagf kvafvgavtr
      241 dtpmvvipks ivglrfadea dtlnallpql raegaqilva vmhegasfng aandpsyecp
      301 glqgrgvdia rrldpayaii isghthqayt ckingrllvq agsyggwvte srltldasgk
      361 vldaqsvnhp vlqsvytpnp afvalvqraa altaavrnkp vadlkqgaqr svqapfgdst
      421 lgnliadsql ayakkrgpad lalmntggir adltvepgrp atmsdlfaiq pfanelvvmt
      481 vsgaqlrell qrqlpkgdgp prllqvsssl ryqyrigadg vaqlgavslg glplddqrky
      541 rlvvnnfmae ggdgqsvlrq gtervsvgvd idamiellte npdavmhiap grirre
//
LOCUS       WP_273599135             255 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase [Roseateles
            albus].
ACCESSION   WP_273599135
VERSION     WP_273599135.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=27610
     Region          10..253
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 mtrtlpgfrl saatgthrgd rqyqqdqvev ilhphnsacl lavvadgmgg ksggrkaadq
       61 vlltsqqlfe rfvpgqesee ellkqilsea hlmikltals aeeephstla afmitadrrc
      121 hwihsgdsri ylfrgpnllk rtldhsfvqg lvdkgeitea easvhpqsnl ltgclgtvqd
      181 pvgssecieg ledgdtlvcc sdglwhfftp selgvvlhtl ppreaaelli skarqrargg
      241 gdnlslaivr vqals
//
LOCUS       WP_273599249             967 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein [Roseateles
            albus].
ACCESSION   WP_273599249
VERSION     WP_273599249.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 967)
  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 967)
  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 967)
  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 967)
  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..967
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..967
                     /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=103514
     Region          9..922
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mfqrkrinva vllalgsals gvamaqeslq rvevtgsrir tidtestspi ivlsaesira
       61 dgirtaegll nnlpqvmadf ggsvsngasg tatvnlrnlg ssrtlvling rrmpagsprn
      121 vaadlnqipv smiqrvevlt ggasavygad avagvvnfil kdnfqgvefd asyqffnhqq
      181 gnsvanivea rgfalpgdks adgkvrefnl tmggnfadnk gnatinftrn qtdallqser
      241 dfsscalnpa gatftcggss tsypgrffln tgsrtvadan gntrpfksat dvfnfgptny
      301 fqrpstrysv tasahydind kvrvytlnsf hddstvaqia psglfgtdfs gvnsikfenp
      361 llsadwkaql hasnqeadtp ttfnkpgdta dlqiarrnve gggrqdhirh tsyrtvtgvk
      421 gdigawsyda faqigkviyq etykndfstv riqramdvva dkngkpvcrs fasgvdpncv
      481 pydiwslgkv dpaavkylat pgfqkgyteq qvlgaslagd lteygiklpt aksgvgvafg
      541 lerrterlql etdaaftsgd lagqggptig tegeysvtdi fgevrvpvfe rmplayalnl
      601 natyrhsnys tgpktntwgs gldwspikdi kvrgsyqvav rapnvvelfs sqagglfnme
      661 sdpcagdkpt ataaqcantg vtaaqygkiv dstagqyngl fggnpllepe tsnsmtfgvi
      721 lnpikdmtfs vdyfdiqiek aigslppdgt vneclntgnp aycklitrds kgtlwllpqa
      781 qvistninva kigtkgvdfg ldygmrmgdm gkldfsvmgt ylleaksetq pgkgafdcag
      841 yfgttcgnpa ptwrhklrgt wtapfglstt ltwryfgsak nqltsddpql hgdvaesqsn
      901 ikavsyldla mgykltknit lsasinnlld kdppvlntga pfgngntypv vydalgrrvt
      961 lgfnakf
//
LOCUS       WP_273599262             779 aa            linear   BCT 28-DEC-2024
DEFINITION  heavy metal translocating P-type ATPase [Roseateles albus].
ACCESSION   WP_273599262
VERSION     WP_273599262.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 779)
  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 779)
  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 779)
  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 779)
  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..779
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..779
                     /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=82192
     Region          60..776
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mmisdskhlh phdaepacaa eriaalddpd llapfthwra aegeaasgqs naaptvaisq
       61 fqlaglhcga cagiierall dlpgvqaarv naasarltlt wlptrtrlsa ilerveragy
      121 gaapdaaapa relrereqrk alwrlfvavf lmmqvmmmaa payfaepgdl spdlerllqw
      181 acwvlslpvl lfsagpffsa awrqirsgrl gmdvpvvlgl lttfvassga lfepggffgd
      241 evyfdsltmf vafllggrfl emrarhraaa qleqssaalp daverlepdg ssarvapsrl
      301 qvgdlvrvfa gqafpadgri esgatsanes lltgeslpva kgvgdevvaa slnmqspvlv
      361 rvqrvgadtr hqaiqrlmre amtqrpatte ladrvagpfl wavlalaigg allwsfidps
      421 ravwvavsvl ivtcpcalsl aapsarlaat galakrgvll vrlelletlc kvdtvvldkt
      481 gtltqedmvl lqqqavggda aallsaaral akhsqhpfsr alvgadssqv sepalpemea
      541 waqvqelpgl glqavdaagq vwrlgspawv reqepsvate pqladaqlaf gsgaqalymr
      601 fgemlradar ealaalhsqg lrslllsgda gervarlaas agvqsaqgda taamklaava
      661 qlqaegrcvl mvgdgindap vlaradvsvv mgqgamlara sadalllsnr lldlamarkl
      721 alrtaqiirq nllwaavyna aciplallgf lppwaaglgm agsslfvvln aqrlarsph
//
LOCUS       WP_273599377             133 aa            linear   BCT 28-DEC-2024
DEFINITION  ExbD/TolR family protein [Roseateles albus].
ACCESSION   WP_273599377
VERSION     WP_273599377.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=14107
     Region          1..130
                     /region_name="ExbD"
                     /note="Biopolymer transport protein ExbD [Intracellular
                     trafficking, secretion, and vesicular transport]; COG0848"
                     /db_xref="CDD:440609"
ORIGIN      
        1 mqvqnevkpi dtinvtpmld layvllvvfi lmttasvqgm sitmpkpsnk pstekhdlki
       61 vqvmegggvl ingvgvtlae leaqlsqaks rdpqmsvaik gdartqyasv vavidlcnkl
      121 qvnmglvtar igt
//
LOCUS       WP_273599382             219 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Roseateles albus].
ACCESSION   WP_273599382
VERSION     WP_273599382.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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 11467871
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=24458
     Region          20..>99
                     /region_name="Tam"
                     /note="Trans-aconitate methyltransferase [Energy
                     production and conversion]; COG4106"
                     /db_xref="CDD:443282"
ORIGIN      
        1 mpgsfvvfds lvekliaaia pqtaldigcg agkygqllsr lapdckrsai eaessyierf
       61 glrelyhelh vgtaadwqhq aldrqydlti lgdciehmpk sagldllnfl ayrsaytlvi
      121 spefvlqgiv dgviseahvs vwserdlgwh dlwawdncrs vsifllrgyl papvslkqlv
      181 eqinagavpi hefhdpqtlv rparlrlvnh wretvyrpa
//
LOCUS       WP_273599408             281 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Roseateles albus].
ACCESSION   WP_273599408
VERSION     WP_273599408.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 281)
  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 281)
  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 281)
  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 281)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 281)
  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 281)
  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 281)
  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..281
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..281
                     /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=30197
     Region          7..275
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 msvpsllkvl lvddeplarl rlrsllegcv dpraevlaea gsasqaqawl rehrcdlvll
       61 dvqmpgpdgl qlagalraqa qlggnspavv fvtahaehal qafeleatdy lskpvrrerl
      121 qaallrvaqr laeraamqaq pegrglplge pdgvinvsdr grllrvplae vlyfkaelky
      181 ltlrtatqsl vmdgslsdle prlgerflrv hrnalvakaa vrelqrhavs hagedeansd
      241 sadsadgadg wavriagvne wlavsrrqva avrealagqg g
//
LOCUS       WP_273599418             378 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Roseateles albus].
ACCESSION   WP_273599418
VERSION     WP_273599418.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..378
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40242
     Region          5..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 msnqaakgpl qglrviemag lgpapfcgrl ladmgadviv ierpaalrgl ntgnainrgk
       61 rsicldlksa lglqaaktli ngasaliegy rpgvmehlcl apaifevsnp qlvfgrvtgw
      121 gqtgplaqap ghdinfvals gvstiasrag aapslpatli gdmaggamfl afgllcaile
      181 aqrsgrgqvv daamidgvsa lsglihsmrg sgmwpatpeq nlflhnspfy dsfecadgry
      241 itlgalepkf yremlrllel sdvdparqyd aaqwpslrar vadriksktr tqwcellegs
      301 dacfapvltl deaaehphnr wrgnfvevmg elqaaaaprf srsqarppqa gplpgqhsre
      361 lllelgfnle qikqmapa
//
LOCUS       WP_273599420             762 aa            linear   BCT 28-DEC-2024
DEFINITION  RelA/SpoT family protein [Roseateles albus].
ACCESSION   WP_273599420
VERSION     WP_273599420.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=84372
     Region          26..762
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mgfrsfaasr lpaaltglpg lrspieptaa eaasfdallh llsylpkadi krvreaykfa
       61 deahlgqfra sgepyithpi avagicaewr ldaqaimaal mhdamedcgv tktelierfe
      121 aptaelvdgl tkldklqfst keesqaesfr kmllamardv rvilikladr lhnmrtmeam
      181 aaikrrriar etldiyapia hrlglnqiyr elqdlsfqhi npwrhaalsk aiskargnrr
      241 dlvsriekdv lkafegaqyk aeidgrekti ysiykkmkdk hlsfaqvsdi fgfrvvvadl
      301 phcylslgvl hqlykpqpgr fkdyiaipkp ngyqslhttl vsplgtpvef qirteamhmv
      361 aekgvaahwl ykdsggahsa qqmgarwlqs lieiqdetrd aneflehvki dlfpdavyvf
      421 tpkskimalp kgatpvdfay aihsdvgdhc vaaqingeav plrtelrsgd vieivtaaga
      481 rpnpawlsfv rtgrarskir hflknleqde srdlgekmls qalraeglal pslhedaeea
      541 agtdsaaqlw qqlarwagnr hvdellveig lgrkiativa kklarmlsaq gqrpdavmls
      601 mgrfaadaep aqgqvtldgs egasvrlatc crpipgdevk gylgrgegll vhtaecqvgr
      661 klfardsehw iavhwadelt rpfeaavsll lnngkgvlaq vaaavsaaea dithilmsde
      721 sqqretaemn lllsvrdrlh ladvlrtlkr spavlrvwrv kp
//
LOCUS       WP_273599427             599 aa            linear   BCT 28-DEC-2024
DEFINITION  GGDEF domain-containing protein [Roseateles albus].
ACCESSION   WP_273599427
VERSION     WP_273599427.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..599
                     /product="GGDEF domain-containing protein"
                     /calculated_mol_wt=65908
     Region          20..255
                     /region_name="EAL"
                     /note="EAL domain. This domain is found in diverse
                     bacterial signaling proteins. It is called EAL after its
                     conserved residues and is also known as domain of unknown
                     function 2 (DUF2). The EAL domain has been shown to
                     stimulate degradation of a second...; cd01948"
                     /db_xref="CDD:238923"
     Region          292..412
                     /region_name="CBS_pair_GGDEF_EAL"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains associated with the GGDEF
                     (DiGuanylate-Cyclase (DGC)) domain; cd04598"
                     /db_xref="CDD:341373"
     Site            order(293,295..297,320..322,391,404,406,408..409,412)
                     /site_type="other"
                     /note="putative ligand binding site II [chemical binding]"
                     /db_xref="CDD:341373"
     Region          293..361
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341373"
     Site            order(320,333,337..338,341,366,391..393,408)
                     /site_type="other"
                     /note="putative ligand binding site I [chemical binding]"
                     /db_xref="CDD:341373"
     Region          366..412
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341373"
     Region          427..590
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(457,501)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(462,465..466,470,474,497,499..502)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(493,522)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mttliypaps rslerpaplr vqtlisedll ttlfqpivql dcgliyghea lvrgpagsal
       61 eypdalfaag rregltvele vrcaaqalkd wsrhklggrl linmsaaalt halhdeqgrg
      121 glfsdeafgv apgsimielt ehervtdies lrraitalrr qgvgialddf gdgrsslrlw
      181 seiqpdivki dkyfshdlpa haeklqtfra llqlaetfga qliaegiesa eelrvlrdlg
      241 vtfgqgwlig rpsregatea lpgartvlas sdiavlpelr rassngvtae rlmmeavtvr
      301 edasheqlfr lfneheqlha iavlnakdep valvdrsqfi nrwakpffnd lygrhactlf
      361 anpsplivda dtgiealttv ltsadqrylr egfiitregr ylglgtgeql vrsvtearie
      421 aarhanpltf lpgnipisqh igrlltsgrg fvaayadlnh fkpfndeygy wrgdemirlv
      481 arvasshcds qrdflghvgg ddfvmlfqsd dwelrceqiv trfndlarnl fdaaalqagg
      541 imaedrhgdm rfhpcttlsi gavqiapgtl qrpeqvasaa atakrhakhe qlsvyvmaa
//
LOCUS       WP_273599490             380 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles albus].
ACCESSION   WP_273599490
VERSION     WP_273599490.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 380)
  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..380
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..380
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=41270
     Region          42..257
                     /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 mrtllhtlgq rpsrnaylcl lllglplpll aqdrasqelp vlqvavsrsl appfviwrdn
       61 qavggidvei aqavaaqlkt qvefialprl rvesalssge admacnlspl hlpkgevlaq
      121 sadlfelqem lagnpgapav dkpeqinpgs vlgtlqaqay palepffaqg rlkrddaldd
      181 erlllkltkd rhpygisnrq vlswfaaqgg enklaswrlp lasrpyrctf sprgrydarq
      241 lyaaleqlqt ngriaqinta rsspavavvv svqsgvrdvs rsalvdlfmg qssllgaqlr
      301 aepvmsmgae rqhflgavlq reaaqfrsaw agqqfggrrr aplelgnaea mkthlqahaq
      361 avgflplslv dsslriiylp
//
LOCUS       WP_273599661             443 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Roseateles albus].
ACCESSION   WP_273599661
VERSION     WP_273599661.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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 11472018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     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: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=47980
     Region          60..441
                     /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 mksypgfakr lglwalagga pawglasyfi wqqtwliypk illwllcsga wlgaawalar
       61 raefqlqtlg nvvegiasgd ysqrlrsasa neqlgeqina lvdtlhrqrl raeeahclvd
      121 avlqgidvai fafdeqaslr lanpaalall lrdkdgvlgr saaelglaal ltadtavlse
      181 hvfagaaglw rlrrlpysvd greqtllfvt dlkqvlrsee lqawrrllrv lshevnnslv
      241 pisslsatlh snlarvgtad ldeglaiihe rakhlaefvr ryarlarlpe pqkqlfdlaa
      301 llrrlptmlp eaglsltiag dclapmpsnf klpffgdpvq ieqllinllk ngveaggaal
      361 elrcqvqplq lsvldcgpgi anpanlfvpf yttkpegagi glvlsrqiae ahqgslslep
      421 rrdgpgrgca ailrfsaigq ggr
//
LOCUS       WP_273600054             127 aa            linear   BCT 28-DEC-2024
DEFINITION  LexA family protein [Roseateles albus].
ACCESSION   WP_273600054
VERSION     WP_273600054.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (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   2  (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 11449429
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..127
                     /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=13764
     Region          <4..125
                     /region_name="LexA"
                     /note="SOS-response transcriptional repressor LexA
                     (RecA-mediated autopeptidase) [Transcription, Signal
                     transduction mechanisms]; COG1974"
                     /db_xref="CDD:441577"
ORIGIN      
        1 mksllgsvqa gfpspaedhg veridlnkel ikhpqatflm rvrgasmrea giddgdvvlv
       61 draikpshgh vvvavvdgef tvkrlwkrgs nlklqaanpt ypdilprdgq tvevwgvvtt
      121 aiksmrv
//
LOCUS       WP_273600108             229 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles albus].
ACCESSION   WP_273600108
VERSION     WP_273600108.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 229)
  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..229
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..229
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=25256
     Region          17..225
                     /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 msislawgpl pawaeplrfv vdtsvslpya kfekgelksg lshqlgldla krlgreavfv
       61 pvarkritaa lergqadlic gyasawlpgp fqwsqpvaqh fellitradm pppqrledla
      121 gqaigtiagf ryvtlerqlg lkfsrddgpd aeallrrlaa krvahaivsr syldyqrqvl
      181 gfdlalhppl llektdlrca lslksalplk qldealqamh kdgslhiqh
//
LOCUS       WP_273599726            1198 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease/M1 family aminopeptidase [Roseateles
            albus].
ACCESSION   WP_273599726
VERSION     WP_273599726.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   ter Beek,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 1198)
  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 1198)
  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 1198)
  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 1198)
  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 16639579
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..1198
                     /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=133016
     Region          4..189
                     /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          302..487
                     /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          614..>1068
                     /region_name="PepN"
                     /note="Aminopeptidase N, contains DUF3458 domain [Amino
                     acid transport and metabolism]; COG0308"
                     /db_xref="CDD:440077"
ORIGIN      
        1 mlskifafea ryqlrsplfl isfvifflms fgaivstdiq iggpkgasnl nspfailqiv
       61 atmnlmaifi vtafvanvvv rdeefgfasi lrstrvskfd yligrflgam fvaflvttav
      121 plailigsmm pwldaeqigp lvlshyvfaq lvmsvptllv lgagffalat itrsmmwtyv
      181 gavafivlfg asrvllkdps ldlasgladp faigalnrvt kywtaadrnt llpslsgmll
      241 ynrliwlsva aalfglayrl fqfetpakaa akaekidksd alpspqrlas pshggstawl
      301 qlraltrfdm rfvfkspaff vllaigvlna maglllttse rgvaylpvtr svvdalegsf
      361 giiplliaiy yagelvwrdr errmheivda saapnwafll pkvlaisgvl lacyltamlt
      421 gilfqlghgf tqiqpaayll wlvlpglisa vllailsifv qamvphkfvg wavmmvlmvl
      481 gmvmgsmgfe hklytyagmp evplsdmnem grfwigrawh qaywlafgam llvathlmwr
      541 rgvetrlqpr lnllrqrlag tpglllsaat lawvgtgayi yynsnvlney vtapaqeqrq
      601 adyektlwgf aelpqptitd vklkvelypn qaradiegsy qmenrsgkpi sqvhvqwapg
      661 lkvqamaldd avlekeykdl ahriyrlskp lqageklgls fairmeqegf vngrpqtqia
      721 pngsfisnqq fapmlgvprg lllqdrairr khglppelrv akledegana hnylrhdsdl
      781 vnaeitlstd adqtpiapgt tisdstahgr rtivtrsdap tahffsmqsa ryqkaqdswa
      841 gkdgkavale iyhhpahntn vqrmftamka sldlyseqfs pyqfgqarim efpayerfaq
      901 afagtvpfse aigfiqnfkd adrdekvdlv tfvtahemah qwwghqinga ekqgmtllse
      961 sfaqysallv meklygkaqi rkflkyeldr ylsgrageav eelplarven qayihyrkga
     1021 vvmyslkeli geekvnralq kllaefafka apyadtrdfl rllraeagpe healivdlfe
     1081 kitlldlkat dakaskradg kfevsftvea kklyadgkgr etesplneal digafsaepg
     1141 kkgftrdsvl lmerrplksg kqqitllldk apawvgvdpy nmridrnsdd nlskvevq
//
LOCUS       WP_273600116             279 aa            linear   BCT 28-DEC-2024
DEFINITION  LytR/AlgR family response regulator transcription factor
            [Roseateles albus].
ACCESSION   WP_273600116
VERSION     WP_273600116.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=30595
     Region          7..277
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 msirkwtalv vddealarrn lqlalaehpn whaaelcasa aearvamagr dfdlllldiq
       61 mprqnglsfa aelcdgphpp llvfvtayde halaafdvfa ldyllkpfdd qrfaamlarv
      121 eqmltlkqga asaqaqaqtq aqgqalsgfl heqrslagge aipalsflnv rsvgmleria
      181 vadiewisaa gnyvelhlra aeggnnrprv vlhratltal eqrlprqqfm rvhrtallrp
      241 ealarlevsg dacyeatlrs adkvpvsery vkqlrallg
//
LOCUS       WP_273600151             444 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Roseateles albus].
ACCESSION   WP_273600151
VERSION     WP_273600151.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 444)
  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 444)
  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..444
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..444
                     /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=47565
     Region          49..444
                     /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 mrapglqtrl slallaaall ggllqaafsa rpsmwlvagl lgglalllfc lssavlaplk
       61 rllralegsv lsyrdgdfsm slaapssgqp pelaellrlh nelglalreq rqllaqrell
      121 ldtvvqntpv amllctqqgq vsyaniaarq llaqgrslag aeldellshv ppalaqalrs
      181 qqdqlvsvqe mdqeeqfhis qrmlllqgqa hrlllikrmt relsrqevas wkrvirvmsh
      241 elnnslapis slahsgaela rrgqierleg vfksiggras hlhqflsgya sfaklplpqp
      301 ttvvwadfla glsahcqfkl easppteagy fdaaqieqal inliknahea ggpadevsls
      361 lrqeqatlvl tvadrgpgms etvlaqallp fystkrksqd ggtglglala reiaeahggr
      421 itlakrsggg glsvslmlpt rqsa
//
LOCUS       WP_273600197             863 aa            linear   BCT 28-DEC-2024
DEFINITION  ATP-binding protein [Roseateles albus].
ACCESSION   WP_273600197
VERSION     WP_273600197.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 863)
  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..863
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..863
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=93257
     Region          15..852
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mhaqepspqr lnfgpfeidl haqrllreqq pvalrpryfd vlvflaksgg klvtkdelld
       61 avwghrhvsd svlkvainal rvaldedaka prhletvsrr gyrlmgvnda rptaggqaak
      121 vaapapasnp spslgnlpap qagligrdae ltqlqdmfas qrlitlhgpa gvgktrlals
      181 aaqhaapadg vwlirldala daepllatva rtlnlgastq tsadtlaral aplsmrllld
      241 naehlvqava elatallnha prlqllvtsq lplrvsgetv vavaplavps dasegldnsd
      301 aaavqllrqr aqqhdaalpw tpaaaasaga iarmldglpl alelaaarvp llgwagvhar
      361 lderfalltr gergaperhr tlraalawsc allqptelrl lqrlsviags fsldaaaavl
      421 gtpvdadlld aldglrehal lsssesgnap rwrlydsvrs yaaeglqasd eetaamsams
      481 glvnhlialf eradlelfet flrpwlaqlk leddslraal qaalqqpalq lqgvalfsas
      541 anyraraghk relqqdhalv salprdhwpa rlqarfdlaq shlgvmaqvi spalaldsar
      601 raqqafrelg evpalyvald retgclmrqq apleqrvdai armralepea wgprqrrfra
      661 whdlmllrdm gndslyedri tsylassraq gddygawnsa qllaqlkssq gdlaaatqll
      721 dlavtemrst gqllqnkpvl aqwaflriaq daepatvqll reavaalqae amlwwmadal
      781 awlpahqgrw hdalrlqtwa dglvaqrgdk rgpmfkalre rmqaqfqtha agllgaalqe
      841 asgldetaam alcfgptels viq
//
LOCUS       WP_273600322             356 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Roseateles albus].
ACCESSION   WP_273600322
VERSION     WP_273600322.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=40159
     Region          7..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 mktvgarvne idllrflaam svvlfhyafr gfaadgksvm pypllaplak ygylgvelff
       61 misgfvilmt aaeanlrgfl isrvvrlypa fwacctltfl ailafgspvf hasmsqylin
      121 ltmlsgfigv ssidgaywsl fvemqfyafv slvlvfrkih haerylwvwl vavaavemfp
      181 ngkigrlliq nyaayfiaga ayylimknga swsrmlivll swvlavsqqa svvenfyshy
      241 rtalnvyvvv giisaffvvl llvalrktgg vgriswvilg altyplylvh qyigfmvfnn
      301 gyprvnshvl lwgmvalslf layvvhtqve krfasrmkna lnlwwdqalh lrflfk
//
LOCUS       WP_273600341             472 aa            linear   BCT 28-DEC-2024
DEFINITION  M16 family metallopeptidase [Roseateles albus].
ACCESSION   WP_273600341
VERSION     WP_273600341.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=49673
     Region          44..460
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
ORIGIN      
        1 mknqfllnki vlaamlatpl iavaaeaikm paelpkygqd kaiqvpqisk ktlanglevw
       61 vlprqglprv dyvlalrgag fgadaaatpg qakllaglln egtaqrdsra iaeaaqgmgg
      121 gvaaapandg ltltayalts haegmmklla evtrspsfpe gevalakana lqalkvasaq
      181 pgfraskaln qaiygehpyg rsqetaesie attaevlrae hakrfrpdra llvitgrita
      241 aegmklaqaa fgdwkaqgpa paeiaaapls akpqhiller pdsvqstvrl grpgapanga
      301 dqvplrltst ilgsgfssri nqnlreekgy tyganagars yrvggaisgg advrnevtga
      361 slqefvneyr rigtelvpae elamnkryva gsyllttqlq gavaqtlann wlvglpaefl
      421 gqfvpliqkv saeqvreigk kyfspetqsl vvvgdkavae qlkgfgefks sk
//
LOCUS       WP_273600392             237 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Roseateles albus].
ACCESSION   WP_273600392
VERSION     WP_273600392.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 237)
  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..237
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=26428
     Region          68..236
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mldgryqsvl eagnravfts elehftkamg fdnfsamtvv dhslgrsdfi nvdncpsgfr
       61 aatdspqlaq rdpvmqhckr qsvpivwdqq tyvrsnaael weaqarfgyr tgialalhlp
      121 egrhfvlgme rsaalpsntt eltrlvadlq lfavhaadsa lrvllppdqq idrphltpre
      181 lealrwtmdg ktawevgtil sisertavlh lsnamrklnc nnkhqavlka mrlglir
//
LOCUS       WP_273600410             344 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Roseateles albus].
ACCESSION   WP_273600410
VERSION     WP_273600410.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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..344
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..344
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=36981
     Region          <141..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"
     Site            order(227,230..231,234..235,237,262,265..266,269..270,
                     272..273,297,300..301,304..305,308)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          227..255
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          260..290
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          296..324
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkthfaphpa rrsitsaiaa ltllsalsma qaavfkdaql eslqdagkfv eleqlaqtrl
       61 kanaadaeas aalslalsfs dagdgkrlea gakqaklcve qhpnvavchv asaqslglqm
      121 inmgmakamr nvgtlkeswi raleldpssf tarvqlakly ltvpgmmggs vskakeleaa
      181 vrssqpetar iirvniaaed kkwaemesel lgvkpskdga mqdelreatm qlariylkdn
      241 kdlakaksly egllrdqptk asgayglsrv yaaqgqmdea irylerartl ngadelpvdh
      301 rlgdaylakg dkaqakaaye rfiankranp anvedarksl aklg
//
LOCUS       WP_273600479             332 aa            linear   BCT 28-DEC-2024
DEFINITION  choice-of-anchor A family protein [Roseateles albus].
ACCESSION   WP_273600479
VERSION     WP_273600479.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..332
                     /product="choice-of-anchor A family protein"
                     /calculated_mol_wt=33507
     Region          29..302
                     /region_name="choice_anch_A"
                     /note="choice-of-anchor A domain; TIGR04215"
                     /db_xref="CDD:275059"
     Region          <304..331
                     /region_name="PEP_CTERM_TLD_A"
                     /note="PEP_CTERM-anchored TLD domain-containing protein;
                     NF038124"
                     /db_xref="CDD:468367"
ORIGIN      
        1 mkkpafalls lvaayagaap altaqevltq fnlvtlgnva sashvdgrsf iggsvvggef
       61 aghpngikps syagltvkgs aenikvnsng lvvegslkfs tvnggttavl agasgnnfng
      121 layivgaasg nnynggllsp apstvaaass tqfgnviggl stslsqlast gssvsfngnm
      181 atfsavansk glavfnlsai dtqvfskgef efnwngastv ifnvdettls fasnflggsa
      241 isagtkaiwn fykatdltis nqfggvvlap lakltnnqni egtvlvkqld qrgeihsanf
      301 ggnisavpep qtfalllagl gffacvgtrr rv
//
LOCUS       WP_273600240             448 aa            linear   BCT 28-DEC-2024
DEFINITION  Y-family DNA polymerase [Roseateles albus].
ACCESSION   WP_273600240
VERSION     WP_273600240.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=49079
     Region          <22..286
                     /region_name="PolY_like"
                     /note="DNA Polymerase Y-family; cd03468"
                     /db_xref="CDD:176458"
     Site            order(46,121..127,156,182..187,216,248..252,254)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176458"
ORIGIN      
        1 mhwlallpsp psatdeppsc sadpeqtqqa lawwalqfsp kvarleeavv levqaclrlf
       61 ggaevlhqrv rrsavqagls lqalawapts laalalaraa vsdglsrpia evldglplhc
      121 lsavqaqaam larlgcrtlg dvrrlpragl srrfgkallq aldqalglqp eahawlqapa
      181 efearlelpq rvenaqlllq yvrhlllqlc awlagrhagi qaltlhwehd amrargvgcg
      241 gslqihtshc trdfghlsrl lgehlaqlrl aapageirlq agevlpliea sasllpaapd
      301 qaleplaqll erisvrlspe rvrcghlqed hrleamqhwq awassgaapr savrgpsypq
      361 pswllscplr lsvhqdrpqy qqaplqllag pqrieggwwq ldatlpngha qvqrdyflal
      421 saghlvlwvf qqrlsefehg wflhgvfa
//
LOCUS       WP_273600500             790 aa            linear   BCT 28-DEC-2024
DEFINITION  glycyl radical protein [Clostridioides difficile].
ACCESSION   WP_273600500
VERSION     WP_273600500.1
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 11449017
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..790
                     /product="glycyl radical protein"
                     /calculated_mol_wt=88646
     Region          4..789
                     /region_name="PflD"
                     /note="Pyruvate-formate lyase [Energy production and
                     conversion]; COG1882"
                     /db_xref="CDD:441486"
ORIGIN      
        1 msqtnrieaf rqeyinskpm iccerarift eshkktegea icirrakafl etckelpiki
       61 fenelivgta gkfrrtgilt pefswqwvdk emdtfdkrtq dpyviskeqi efirkeifpy
      121 wkgksleevf laripedtak ilvdtgiidn dskwrqavge vtpdyqdilf vkgykgiked
      181 adkkvkeldi svseniekid fyksvsivaq gimtlaqrys nlakemskqe tdekrkleli
      241 kiseicmnvp anpptnfyea iqfvwfvqlg gilsenplal nlgrfdqymy pyyendareg
      301 kiteseaqel iealwiklse wvwtisanta nyfagynqfq nltvggkkrn gtdgtndisy
      361 mclkatesvk thqpglsvrv sqgapdnfvm avaklvkqgt gfpaihsdsa gaqmllqdgy
      421 daedardwsn cgcvvphfrk tgqwtsavni nfaaaleyam negksrltge kmgldtknit
      481 eftsfeelkd eflkqlaylv kssvigttva qqihkemvpr pflstcvdgc ldkgvdlskg
      541 gakynigpvl tgiglgvvsn slaaikklvf edkvttleel tkalnndweg yeelrklald
      601 vpkygndndy vdslaievsd fyytetrkyk difgskfnsa fmgisnyvpt gkivgatpcg
      661 rkatkplteg vspfvgtdts splaamksas kinhdvhtgg tllnlrlnqd lveterglrn
      721 ltsmiksyfa lggfhvqfnt isndtllkaq enpeeykdll vrvagystqf vnlsremqda
      781 iiarnshsnf
//
LOCUS       WP_273600899             386 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Roseateles albus].
ACCESSION   WP_273600899
VERSION     WP_273600899.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..386
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..386
                     /product="DegT/DnrJ/EryC1/StrS family aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42539
     Region          6..384
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 msdlpflpfa lpeigedein evvdtlrsgw vttgpkakrf eqefaaflge pqieciavns
       61 ataglhlale acgigpgdev ittthtftat aevvrylgad vvlvdidptt lnidpklvea
      121 aitprtkcii pvhysglavd miaildiark hglrvvedaa halpttleke ligtlgsdat
      181 vfsfyanktm ttgeggmlvt rnaelakrar vmrlhgmnrd afdrftaktp swyyeivapg
      241 fkynmtdiaa algihqlkrl pafqarreai aqaynaafvd lplilppeap dgdvhswhly
      301 vlrlsdelei erdvfiermy aagigcsvhy iplhlhpywr eryelgpeqf phsqkaferm
      361 lsiplytamt dadvqrviaa vraiag
//
LOCUS       WP_273600726             529 aa            linear   BCT 28-DEC-2024
DEFINITION  thioredoxin family protein [Roseateles albus].
ACCESSION   WP_273600726
VERSION     WP_273600726.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 529)
  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 529)
  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 529)
  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 529)
  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 529)
  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..529
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..529
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56337
     Region          37..151
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mklylstprt ataaaalsla alfcqaptvh aaaaatspgv awqaasadad iekafaqara
       61 ekkpvllywg akwcppcnql katlfnrqdf ieqtqaivpv hidgdspgaq klgtrfmvrg
      121 yptmilfsad greitrlpge idapqvikvl qlglaggrpv gdvladakag kklsanewrl
      181 lgfyswetge sqlvpaaelp allaqlaaas qgvdaetttr lwlkalsasn egkglkpdak
      241 ladlvhgvlv spaesraqmd vltngaadiv ktltpeagaa rtkllgefev alkrleadtg
      301 lsradrlgal garldlarld taktelhpkl spalvkevke aaakadreit dgyerqavis
      361 saayllgqag qwkdsddllk sslakshspy ylmsqlggna kkqgrkdeal rwyeesfnks
      421 egpatrlqwg sgyvaaltel apqdaariek taaqlfseaa qdkgsfyers arslqkvggs
      481 lvkwnadgkh dasiarlktq ldgicnkvdt adkqratceg llkapgkka
//
LOCUS       WP_273600921             383 aa            linear   BCT 28-DEC-2024
DEFINITION  MraY family glycosyltransferase [Roseateles albus].
ACCESSION   WP_273600921
VERSION     WP_273600921.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 383)
  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 383)
  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..383
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..383
                     /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=41850
     Region          36..231
                     /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            93..94
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133467"
     Site            214..217
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133467"
ORIGIN      
        1 mthlllsflv sflfsaliir asrdwgyqgr dsdlfgpqkf hviavprigg valfagvlca
       61 vvypwlhlgl rqpsagillm fsalpaflvg ltedctknvk pvwrlvaagv savlaivllq
      121 aqisradipg ldwllstslg afaatvftva gvanavniid gfnglssmcv glmllafayv
      181 ahqvgdtelv lislagvgai mgffvwnypa grlflgdggs yflgfflaev gvllisrhse
      241 vsplfalmvc iypvfetvfs myrrrvlrav sagqpdgihl hsliyrrimr wtfgardara
      301 mtrrnsmtap ylwtlcvssl apallfwdst pmllacmllf gvtyvglywr ivrfrtprwm
      361 vfrgdvmggk vppvvvkaad kpe
//
LOCUS       WP_273600912             288 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family oxidoreductase [Roseateles albus].
ACCESSION   WP_273600912
VERSION     WP_273600912.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 288)
  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 288)
  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..288
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..288
                     /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=31468
     Region          4..279
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mtqrialcgs ggllgsefrs alskdlrgfm qlpracieda dvevitailr eakisivinc
       61 iahtnleaae vdpsldkfvn stipgalaka csslnillvh fsstgcyghw kddpyiesdq
      121 lvpptqhhla kyrgemlvrs sgcrhliirt gwlfggsidq pknfvwkril easqstdiis
      181 dnsqrgcpty vgdvvaqsla mlseeisgtf nvvahgsasr yeyvaaiisf aglsckvkpg
      241 pgfkrqapvs mnemavnfel qqqgmdlmth wrtplrryil glplslvq
//
LOCUS       WP_273600609             492 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Roseateles albus].
ACCESSION   WP_273600609
VERSION     WP_273600609.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 492)
  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 492)
  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 492)
  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..492
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..492
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53886
     Region          38..>258
                     /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 mpklpqspsh pqgnpqrvwy gllalilllr lltlaslplt dhtearyaei arlmlqlqdw
       61 isphitptev fwakpplstw sqalsmtvfg vspwaarlpa vlwscaalga agwmlkgsls
      121 rlqtlvvlva lalsplffia agavmtdatl aattlfvqaa wwrvlrshsa perlrlarwl
      181 gfgvglallt kgpaavvltl lpifmhaawr rhwpairava sdvwvwlicl gvalpwyvaa
      241 elktpgfmey fvlgehvmrf mqpgwsgdry gfahaqplgi iwpytfvaal paalilllrl
      301 pylrirqgag alraqfhqtd ggvdlacyal cialaplllf saasnliwty amtalpglai
      361 lavmacpqaw fertiswglg lallllyawa fvfklpqeaa khsdqsliaa yeqacgsqsc
      421 rlsyaskpdy sayfytagrl yagmpgqasa pafkvihlak ddplrsdala cnrdqcllrd
      481 ldadaalvns nr
//
LOCUS       WP_273601011             301 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles albus].
ACCESSION   WP_273601011
VERSION     WP_273601011.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 301)
  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..301
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..301
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=33107
     Region          98..273
                     /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 mslrpqassa rtisrrtvlv eaglcalavg apiigsaapq qpqpqpqapt elvlrvpdph
       61 dyepgavgsf yvnalllals ktakgkesvr lshfpggvpr arlrlmlerg eidllwssst
      121 aqresafepv rfnllkgine qrfllirkqd aaklsqvqsl ehlrefrvga gehwsdasil
      181 rtngfqvvta tshdglfkml aagrfdfiar aineieadll qhpeldlavv dglllqykqp
      241 iyffltkgnv alaerirqgl emakadgsfd klfftvpalk sswdtlsksk trvfklqahe
      301 g
//
LOCUS       WP_273601017             562 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Roseateles albus].
ACCESSION   WP_273601017
VERSION     WP_273601017.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=60759
     Region          15..521
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 mgrpslikpv rvgssrrgff kntgsaaaal laapmlplag taeaavaing nfqhgvasgd
       61 plsdrvilwt rvtptngrss qvvdytiakd paftqivstg rskailerdf tvkidalgls
      121 pnttyyyrfs vdgvispigr tktlpvggvs nlrmavvscs nhaygyfnay rriaeradld
      181 mvvhlgdyiy eyganqygnv rtpeptneiv tladyrmrha qykrdpdsqa mhrqhplvai
      241 wddhetanns yvdgaenhqa gegawaarvg aalqayyewm pvrvvdpkqp rnnarsyafg
      301 nlvdlimlee rlngrsaqlg tnignasgyf vqqgayldpa rqllgaseea wlfnklrtst
      361 akwkflgqgv mfaqvkvqga pnsagggvff nsdawdgyqp ardrvyevlk gsqtqapvnn
      421 vviltgdihs swaadlsqdp nnanvatggy dkvtgqgsra vefvgtsiss pgvdnpqqaa
      481 gtiaqlapan phlkyikldk rgymlidada trcvcewwyv dtvasvsnvq tfgtafqvvd
      541 ganrlspaaq tpnranpaal ap
//
LOCUS       WP_273601007             535 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Roseateles albus].
ACCESSION   WP_273601007
VERSION     WP_273601007.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=56940
     Region          4..535
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mlrlvtvvcl llavpvlgil gswlgldqes wavlqhqwat vlpeyvgtsl llsvsvglgv
       61 allggmtaaa islfefpgrr wfewalllpm ampayvaaya ytdalqysga lqtwlralsg
      121 aqgalwsdvr slpgavalfv lclypyvyll trtalqergv tlmetarilg agtwrrvrev
      181 alplarpala agvalalmet ladygvgayf glstlttgiy kawlvmnerm aaaqlasall
      241 lavalllwae rraqaklrfa ssragaqhaa earplvlrgw aaagafalcg lpvllgfvlp
      301 vfallklmwl earfgefglp larfaqwawt slqlaaisal lavalalvla yaarisaggr
      361 llgaatrvvs lgyavpgavi avgillplaw lqeyapqlgl tnivtgtitg liyaylvrfs
      421 gvalqsveag yarisptvde tarllgasrg rlfrvlhapl larsalaaal lvfvdvmkel
      481 patlvlrpfn sdtlavvayq larderlgea alpslaivlv glvpvlmlsk amrqr
//
LOCUS       WP_273601033             364 aa            linear   BCT 28-DEC-2024
DEFINITION  DegT/DnrJ/EryC1/StrS family aminotransferase [Roseateles albus].
ACCESSION   WP_273601033
VERSION     WP_273601033.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=39235
     Region          3..362
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mpfidlksqy talkpridar iqavldhgqy imgpevkele aalaaytgak hcitvssgte
       61 allialmald lkpgdevitt pftfaataev ivllgavpvf vdiepdscni dsrqieaavt
      121 sktravmpvs lygqvcdmde inavaahhgl aviedaaqsf gasykgkksc alstfgatsf
      181 fpskplgcyg dggalftddd qlaqaareir vhgqsqryth trlgvggrmd tlqcaivlak
      241 lerfdwelaq rralgaryrq lmhdlplqgl glradrdcvw aqftlqvdqr aavqqalnaa
      301 giptaihypk pmhrqpayaq ygqgksfpha eraaervlsl pmspdlseaq qesvvaalas
      361 alrv
//
LOCUS       WP_273601123             118 aa            linear   BCT 28-DEC-2024
DEFINITION  ArsR/SmtB family transcription factor [Roseateles albus].
ACCESSION   WP_273601123
VERSION     WP_273601123.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=13186
     Region          6..93
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mdarvtqdrv fesvaelfsl lstpirlkii savchgeknv sellseidtt qpnmsqhlst
       61 lyrsgvlskr regtqiyyql qservaalcr avctqvemem npsaeietke rlmpagvr
//
LOCUS       WP_273601167             216 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Roseateles albus].
ACCESSION   WP_273601167
VERSION     WP_273601167.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=24033
     Region          4..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 myedkqpwyf nfvrrdieal lpsraervle igcaagatln wlkesgradh ttgiepmaqa
       61 asvararvdq vlegpaeall tqlppesfdl vlcldvlehl vdpwvvmqql rglvrpggtv
      121 ivslpnvrnh rvvlplllag rfeyqeagim drthlrffsr qgalelleha gfrvtaeast
      181 glrrgdrdfw rnlftgglla plfisqhllr gtrsaa
//
LOCUS       WP_273601243             250 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Roseateles albus].
ACCESSION   WP_273601243
VERSION     WP_273601243.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..250
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..250
                     /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=26754
     Region          16..137
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
ORIGIN      
        1 msrqqlssea hknlphanpl svaqmsdlle aalarqprta leigcgaggf sielakrqdv
       61 hvvaldtnpy aleramaaas kaqligtvef cqkpaadfng epvdllvcig asqafgtprq
      121 alqalrglla pngtlvfael swsakppsey lqylatsegd ywtakeaehv faeaglkvet
      181 imiasadswa qyeagvlhgr lefaktiapd qaaeivemst ewfrlyeahg rhclgflacv
      241 atrsdgepgv
//
LOCUS       WP_273601360             676 aa            linear   BCT 28-DEC-2024
DEFINITION  BglG family transcription antiterminator [Clostridioides
            difficile].
ACCESSION   WP_273601360
VERSION     WP_273601360.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 676)
  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 676)
  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..676
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..676
                     /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=78752
     Region          8..626
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 misgrmllim nflkgknkts ykdiskqlsi eerkvrydin nlnivlrsln ksviqkmnkg
       61 vliipdnfqv vcinnneyvf sltervsimk iismfkidnl nleklskefq vsrssikndl
      121 nvlsselern qititydksf kisgeediiy kqrlnilksy sylfgkeksd lsvfekylvn
      181 viekifkgiy lidiynwsmn lllqmgwtln desftwyvsn iflftwyihs dekhplesas
      241 lsepcfenkf dqefetiiqk kltkeqifll ksfvfftnky aslnedmdli steiivqdli
      301 ynmseileis fkedmilykg llnhiaplie rikqniqiye ellhvipdky qyvleatkvs
      361 iqknrvlsqi knenetilla ihflgsihrn ernnyknill vcgfgygvia mlkdslvndy
      421 qinivesips yklqdykdwe sidfiittsk ividlpktii einpflqeed ylkfeekgik
      481 rknvltnyms ikkrldflee dakkrvlsii cqelgysder ilfrqlnlsd ligidtirii
      541 dgdmkwedav kissnilanc dfvsaqyaen iidilknvgf yavkdnefal lhgndsslvk
      601 vssisllick eavsfgdkkv kiifclasrd kkeqipaiin ltkmvyktnf iamlesaktk
      661 eeaevlihky ekevtv
//
LOCUS       WP_273601632             165 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Roseateles albus].
ACCESSION   WP_273601632
VERSION     WP_273601632.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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   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..165
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..165
                     /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=17558
     Region          2..135
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrlttmtdya lrmliylgqh perlcttaei aqayaiseah ltkithqlgl ggwittvrgk
       61 gggmrlalap aqimlgelvr aiepdfylve clgngnacgl tgrcrltgif ndalaaflaq
      121 ldrynladll sapkadagda tiavvlglpq ataavrrtrk phepa
//
LOCUS       WP_273601811             340 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Roseateles albus].
ACCESSION   WP_273601811
VERSION     WP_273601811.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 340)
  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 340)
  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..340
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..340
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=36958
     Region          134..>283
                     /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          228..251
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          256..286
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpfkplprri halsslicll allslspaaq aalfkdaqlq slldagryed leraskvrlk
       61 lkpddvqala gaalgssday dvarldvaak laqtcrergp qeaicyyaaa evmghqvqmi
      121 nplkavamvg rlkdalhkal eldptlyaar sklvqlylft pqmlggsaak akaleaeira
      181 sqpeqarllr slvaaaaekw peaerelmav ragsdgalla dvreatsqlg rhwmreqqfd
      241 karslfeqlq rdqpsqamas yclarlaldq gqnqaavqhl eraknlagaq qlpidhrlge
      301 awlalddkaa akaafsraas dkhirpnyak darkslaelg
//
LOCUS       WP_273601566              69 aa            linear   BCT 28-DEC-2024
DEFINITION  integrase core domain-containing protein, partial [Roseateles
            albus].
ACCESSION   WP_273601566
VERSION     WP_273601566.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 69)
  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 69)
  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 69)
  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..69
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         <1..69
                     /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..45
                     /region_name="rve_3"
                     /note="Integrase core domain; pfam13683"
                     /db_xref="CDD:433402"
ORIGIN      
        1 ngkfrdecln ehwfqtlpqa rteiaawrrd ynevrphssi grmppaqfae qhrrstgdaa
       61 rhlipteih
//
LOCUS       WP_273601970            1978 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-2-macroglobulin family protein [Roseateles albus].
ACCESSION   WP_273601970
VERSION     WP_273601970.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 1978)
  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 1978)
  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 1978)
  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 1978)
  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..1978
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..1978
                     /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=214729
     Region          263..1978
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
ORIGIN      
        1 mkrwigqlsr rafllaaifg plawppahaa avavspsgev aevrqirlgf sepvvaagdp
       61 rlpapaslrc mgatgaaqva gsgrwasare wlfdlnepma aglqcqillk ddfkplggal
      121 tgprefgfrt gaaivlqtqp wagsqieedq hfllklnggl saadvgqraw ceveglgerl
      181 pavladeatl akvlasqrls ksqgrhwllh cqrplpagak lqlvwshgna gatqrfefqv
      241 rrpftadfsc ereranaaci pvrplrlvfs epvarelalq vrlrptggaa ngaasgaala
      301 pkvaaddktl elselrfpap lagnaqftle lpaglkdlsg ralsnaasfp lkvataaapp
      361 lakfaaapfg vlerdaggaa llpitmrhvq adwhatdrpt ksppgeirik rlqtdaevla
      421 wyaklmhthe vslsarelgl ppsqwqetvk tvdasgrtrs qlstrhvhsr evellprqqa
      481 tqvlalpplp gavqgqerpf eviglplaep gyhvvelssa klgrslldkd aamyvrtgvl
      541 vtnlgvhfkw grenslvwvt tldrgqpvpq advvvndcag kplwsgrsda qglakiplal
      601 vqpdwndrrc vaergffita rkadadikkp gdmafvfsnw nrgienwrfg lptsngpepd
      661 arahtvldrs llragetvsm khffrlqtlq glrlarpeql pdrvklthqg sgeqislplt
      721 wptarsslsq wqipanaklg syqitlersr aeashsrswp sgefrveefr vplidarlsg
      781 pkalpvapre lrmtaqlnym aggglaqapl klsallrprg lsfagfedfs fepprergan
      841 ggepvyqepe gegaqgegha vqrdgklvid klaglsdrng aaefllkplp kierasella
      901 elsyqdpnge tktvaqvlpl wpsqvvlglr skgwvsnaeg klsfsvlald tagkplagqr
      961 ievkaslnqm issrkrmvgg fyaydnrnev kplgvvcsgr sddkgllace akldvageve
     1021 lvaqasdaeg rvaqaasqvw ltrqgelwfp qdnddridvl aekkryepge tarlqvrmpf
     1081 reatalvave regvietkvv tlrgsdpsie lkidkawapn vyvsvlalrg rvfevpwysf
     1141 frwgwrapvd wwrafregra mpaptamvdl akpsfklgvt elqvglaehq lqvtvttdkl
     1201 qysvrqtvqt rvkvsqdgrp ladaqvafaa vdegllalrg naswdllqal iqrrgwgvet
     1261 ataqseiigr rhygrkavaa gggggraptr elfdtlllwr pqvlldange avievplnds
     1321 ltsfrlvava dagaqkfgtg qasvrvtqdl qllsglpplv regdqfqaal tlrnssnram
     1381 klrvslqgss pggaqiknpp aqdlslaaga asellwqlqv pegagdlqwe aqaqevggpa
     1441 rdrlkfsqrv lpavkvqvlq aslsqvdgsm slavappada wppsgpkrgg vnvvlqarlg
     1501 gdlpglkrff etypyscleq qtsqaiglhd garwqalmnr lpgyldadgl anffpptege
     1561 raggsdrlta yvlaaahasg relpaaarer mldglsafve grlvrkswsp rsaqldgevr
     1621 rlaalealar ygrvgssgfa svdarnlstw ptaavidwls lltrnakapq reqrineaqa
     1681 mlrsrlsyag tmlkfsneed dawwwlmdsa dgnaarlala alddpawsae lprmvqglla
     1741 rqrqgawatt tanlwgvlal dkfaerfesv kpagqtlvsl gsqslkqdwa rkpdgaalll
     1801 pwsegqlklq qqgagkpwvt iqslaavplk eplnagyrit relqpveqkv pgrwsrgdll
     1861 rvrlqleaqs dmtwvvlsdp lpagaaimgs glggdsslal qspasapapl grrpvyiers
     1921 feawrgyfdf lprgkhelsy tvrlnnagrf mlpgtraeal yapeqfgelp qavlevap
//
LOCUS       WP_273601966             534 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Roseateles albus].
ACCESSION   WP_273601966
VERSION     WP_273601966.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=57646
     Region          9..521
                     /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 mssassdgma lsllvvddep dlrtlyeltl vregyaldta gsvqealacl qrrpysavit
       61 dmrlpdgsgl dllhwlesqg rdektlvita ygsaenavea lkagaydylt kpvdlrqfrq
      121 vvasalgrqp qklapavpav aptklpplpq salqpqapqq lppvkerqql vkglplaavp
      181 tltalsrlag ksaaiqelrs liekvsrsma pvllqgesgt gkelvaraih dsgvrarqrf
      241 vavncgaipe qlleaeffgy rkgaftgane dregffqaad ggtlfldeig dlplamqskl
      301 lrsiqertvr pvgavaeasv nvrilsathk dlgaevaagr frqdlfyrln viqlrvpplr
      361 eriedvpmia ervleriaad agvspvpqlt paalaqltry gfpgnvrele nllhralals
      421 ggewidaddl glpeslldds llgglssadd fepeggvsik nsfghdkapn elptdlarfl
      481 ddverdillr altqhrfnrt aagaslglsl rqiryrmarl gvtadeaeqs ddqa
//
LOCUS       WP_273601986             370 aa            linear   BCT 28-DEC-2024
DEFINITION  aromatic ring-hydroxylating oxygenase subunit alpha [Roseateles
            albus].
ACCESSION   WP_273601986
VERSION     WP_273601986.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=42553
     Region          16..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 msdlsislsa lersktqlav tsyfdealfr qeqvqlfqng prylghalav peigdyyalp
       61 qegegralvr tpqglelisn vcrhrqavml rgrgntrsni vcplhrwtyd lkgelvgaph
      121 feqdpclnln ryklrewngl lfednghdva aelsklsvaa eldfsgyvld kvhvhqcdyn
      181 wktfievyle dyhvgpfhpg lgqfvtcddl awemgrhhsv qkvgihkdla rpgspvyqrw
      241 heqllkfrgg etpkagaiwl tyyphimvew yphvlvvstl fpkgpqqtan ivefyypeei
      301 aaferdfvea hqaaymetcv eddeialrmd agrralmerg dnevgpyqsp medgmlhfhe
      361 wyrremnira
//
LOCUS       WP_273602092             255 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles albus].
ACCESSION   WP_273602092
VERSION     WP_273602092.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..255
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28576
     Region          40..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 msfvfnksrr qpmtvvlkam fsalliansa saaelewlag elppfvwqtq ggpqglayel
       61 atqmstkigr plsmtfypwa ravrmaeggp nygvfplart pdreaqfkwl iplahvnytf
      121 fgrsgskvdl dalaalrgqr vgvlrgspii knlqaekfrh ivqakdykel lrllaedmia
      181 aayagepmlr aaidefkfrp qdfrsglnlk saelymassl aldgaeeerw lqayrdlqad
      241 gtvarlqkky lqrer
//
LOCUS       WP_273601447             305 aa            linear   BCT 28-DEC-2024
DEFINITION  SufB/SufD family protein [Clostridioides difficile].
ACCESSION   WP_273601447
VERSION     WP_273601447.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 305)
  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 305)
  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 305)
  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..305
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..305
                     /product="SufB/SufD family protein"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=33201
     Region          77..303
                     /region_name="SUFBD"
                     /note="SUF system FeS cluster assembly, SufBD; pfam01458"
                     /db_xref="CDD:460219"
ORIGIN      
        1 mnkidlnlle kvaelrgtpl gaynirkngq gverhstenv tiipktdkpg idiivkpntk
       61 genvhipviv teagvqdmvy ndfeigenad vviiagcgih ncgcddsehn gihrfflrkg
      121 arlkyvekhy gegdgegkri lnpvtivnmd edsycemeti qikgvdstkr emdanlgkga
      181 kivvfekllt hgnqvaesnm kvilegenss aqvvsrtvgq dnskqkfnpc vigdslcsah
      241 vqcdsiimgn sqisaipeid anhpdallvh eaaigkiagd qilkmmtlgl teeeaeqqil
      301 ncflk
//
LOCUS       WP_273602162             347 aa            linear   BCT 28-DEC-2024
DEFINITION  CobW family GTP-binding protein [Roseateles albus].
ACCESSION   WP_273602162
VERSION     WP_273602162.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 347)
  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 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 11424901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..347
                     /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=38670
     Region          9..347
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
ORIGIN      
        1 msnpqkglip vtiltgflgs gkttllkril teahgqkiav ienefgeedi dteilvadte
       61 eqiiqmnngc vcctiredlr ttlsdlaakr rkgelkferv viettgladp gpvaqtffmd
      121 deiaesylld siltlvdavh aeeqlntrqe arrqigfadq ifiskadlal peavaalshr
      181 ikhmnprapq qqahfgeval skvfdlrgfn lnakleidpd fltieaphdh dhdhehgehc
      241 dhphhhvhdd dvksfvfksd kpfnpakled flgaivqvyg pkmlrykgvl ymkgtdkrvi
      301 fqgvhqlmgs dlgpkwmpge kkaskmvfig idlpkeillq gmegcla
//
LOCUS       WP_273602241             374 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Roseateles albus].
ACCESSION   WP_273602241
VERSION     WP_273602241.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=39803
     Region          5..372
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
ORIGIN      
        1 mkqsrsadvl ivgagiigaa carayarqgl svcviepsai gggataaamg hllvvddeag
       61 gadaefqltr rsqqlwqqwl densehpala ehqacgtlwi aadaeelala erkqrwlaar
      121 glaaemlgaa dlaraepmlr qglagamrvp gdarvyppkv aarwlaeara eliegqvlsf
      181 dghgvvladg rrfwgaltvl caglaaqawl ppgwlipkkg qlaitqrypg mlnhqlvelg
      241 yikkahlsdq dtvsfnvqpr pggqlligss rqigrsdril dpailqdmlr qacsylpglr
      301 dlsllrcwtg vrpasrdgqp ligahpelar vwlatghegl gittslatae llvdlslgat
      361 plldagpfsp srfl
//
LOCUS       WP_273602251             118 aa            linear   BCT 28-DEC-2024
DEFINITION  antibiotic biosynthesis monooxygenase family protein [Roseateles
            albus].
ACCESSION   WP_273602251
VERSION     WP_273602251.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 118)
  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..118
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..118
                     /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=13521
     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 miavifevkp hpahfqeyld laaelrplla qidgfisier fssmsepgkl lslsfwrdea
       61 avrawrnleq hrstqalgrs qvfadyrlrv aevqrdyglh dreqapldsr qahprpqa
//
LOCUS       WP_273602291             247 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles albus].
ACCESSION   WP_273602291
VERSION     WP_273602291.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..247
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27077
     Region          31..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 mrlpalllsf amlacatara qdsapvilcl tefppfnseq lpkqgpliel ateafkragr
       61 ridaqfmpwa ralkeaeggh calfgiwrna ardqvfdysk piiqmelgff grrgvaldfn
      121 dprvlaglli giqratylpp lldnknlrfd lgndllssmr klvrervdla ygnralgqyl
      181 lnaepelgaq vewkapalev kdhllgfaks yegggallkg fnkgldsmka dgsyrkilsa
      241 ggldvar
//
LOCUS       WP_273602324             492 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Roseateles albus].
ACCESSION   WP_273602324
VERSION     WP_273602324.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 492)
  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 492)
  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 492)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..492
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..492
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53372
     Region          115..341
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mvskalgllk wsvvialvgg itllavrafd aqrgpdlelw htfvphelsa aeldkadwkq
       61 flaaeaqafa evrsevtdkl gpeariesnr ydanspiypg kfatdwnrsy vmqpegkpvg
      121 avvllhgltd spyslrhiar ryqeagfvav aarmpghgtv pgglttvewe qwtaatrlsv
      181 reaqrlvgpg aplhvigfsn ggalamkyal ealgdkslar pdrivliapm igitamarfa
      241 gvmgwpallp rfakaawlgl vpefnpfkyn sfpvngarqs slvanrlqqe inaavadgkm
      301 aqiapvqtfq svvdftvstr aivdalyvnl pangselvlf dvnrntkiga lmrantdtvv
      361 trllpaaprk fratiitnes prhaevverv teagatteqv rplgllyprq vfslshlalt
      421 fpmndslygl qpdepeeygv nlgsmatrge rgtlivslds lsrmsanpff pylieriaeg
      481 fkgkgegkae gk
//
LOCUS       WP_273602376             525 aa            linear   BCT 28-DEC-2024
DEFINITION  phospholipase D-like domain-containing protein [Roseateles albus].
ACCESSION   WP_273602376
VERSION     WP_273602376.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 525)
  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 525)
  AUTHORS   Exton,J.H.
  TITLE     Phospholipase D
  JOURNAL   Ann N Y Acad Sci 905, 61-68 (2000)
   PUBMED   10818442
REFERENCE   3  (residues 1 to 525)
  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..525
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..525
                     /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=57846
     Region          69..520
                     /region_name="Cls"
                     /note="Phosphatidylserine/phosphatidylglycerophosphate/car
                     diolipin synthase [Lipid transport and metabolism];
                     COG1502"
                     /db_xref="CDD:441111"
ORIGIN      
        1 mrsnlmsqlg pwsrrgfllg aalllaacas aplplppkpa layaaapsas gplaeletlw
       61 tekhgdktsg frlleknseg lkwrlalidq ashsldlqyy vwfgdasgql lmarviaaae
      121 rgvkvrmlfd dlstmlrrms spelrddlla hidshpniqi rtfnawqqrd wlgrvaegaa
      181 dferlnrrmh nkqmivdnrv aiiggrnigd eyfgllaefs fhdldvlgvg pvarqasavf
      241 drywnsdwvr aippgnsqsk grvtpaslem peaaaahpav qellagrhsw asefanlsps
      301 ltqgrsevht dspsraagth nhmpeafral mrsaqkevli tnayiipdan fmsdlaelng
      361 rgvtvriltn slashdvpav nahyedwrkp illtgtqlye lrpdaaikad fvdtppvrse
      421 faglhtkamv idqtrsfigs mnldprsevi nsemgviies pllgaalatr mardmtagns
      481 walqlspant vqwksdgpal dqaparspwq riqswffkll pasyy
//
LOCUS       WP_273602412             428 aa            linear   BCT 28-DEC-2024
DEFINITION  esterase/lipase family protein [Roseateles albus].
ACCESSION   WP_273602412
VERSION     WP_273602412.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=46334
     Region          151..270
                     /region_name="EstA"
                     /note="Triacylglycerol esterase/lipase EstA, alpha/beta
                     hydrolase fold [Lipid transport and metabolism]; COG1075"
                     /db_xref="CDD:440693"
ORIGIN      
        1 mnsnrprrka hhlqatdlrg iaqlgsqata giarivegvh qsiwarlgmp ggpapgqtrg
       61 vtglayrsvh gvnrlvgasl qallkrlepm lqsgsesteq qespqraall aalngvmgdh
      121 llatgnplat imgmrwkgla lnwqalppef kpngkvllli hglcmndlqw qasdkvgtvd
      181 hgqtlaaalg ytpiylryns glhtsqngre laaqlelllr hwpvpveeis ivahsmggll
      241 trsachiage qsltwlpllk niiflgtphh gapleragnw idvllgstsy taplaklgql
      301 rsagitdlrh ghvrdedwqg ddrfhqlpdq rlitplpagi ncfavaatms aktakrggal
      361 anrligdglv plhsalgehs dprrdlgfak seqlvcyrmn hmellsspvv cqqllnwlqa
      421 rpqkqtkq
//
LOCUS       WP_273602410             446 aa            linear   BCT 28-DEC-2024
DEFINITION  UDP-glucose dehydrogenase family protein [Roseateles albus].
ACCESSION   WP_273602410
VERSION     WP_273602410.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     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=48138
     Region          1..440
                     /region_name="Ugd"
                     /note="UDP-glucose 6-dehydrogenase [Cell
                     wall/membrane/envelope biogenesis]; COG1004"
                     /db_xref="CDD:440628"
ORIGIN      
        1 mkvtaigtgy vglvtgacla emgnhvlcld vnaekiriln egeipihepg lqeivqrnva
       61 agrlqfttdi dravnhgtim figvgtppde dgsadlqyvl aaarsigarm tdykvivdks
      121 tvpvgtadkv raavadeltk rgstlafavv snpeflkega avedfmkpdr iiigsddeqa
      181 tlfmralysp ftrnndrmvv mdlrsaeftk yaanamlatr isfmnelall aekvgadiel
      241 vrrgigsdpr igysflyaga gyggscfpkd vkalvqaaqa egvslrvlaa veqanerqkm
      301 vlvdkvvarf gadlsgrhfa iwglafkpnt ddmreapalv ivqelirlga tvaaydpvam
      361 peakrvlgdl rsfsfcerae qalegadalv lvtewkefks pdfdaikaal kqpvvfdgrn
      421 qyepslmkvl glehhgigrg saqsvk
//
LOCUS       WP_273602530             278 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Roseateles albus].
ACCESSION   WP_273602530
VERSION     WP_273602530.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..278
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=30632
     Region          46..271
                     /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 mfacylhrav siavclafsa glhaqtpaef satsattsfn ndkktlvlag eddwspysaa
       61 ekpgadtdss pvgfsvdlvr aalasqgiqv kiinvpfarc mlyaksgqva gcfnatitdd
      121 nradyvwhqp amfeeelsif aradadvpel rladlrgkrv aytngytyps efmhdsrilk
      181 svavsdaali rmllakrvdy illnrtpggm rinntpefkg rakrvgllsm dgfwvafskq
      241 hpqgeslaqa fsaglaqmrr dgsyqrlqde frkrvhyr
//
LOCUS       WP_273602506             643 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Roseateles albus].
ACCESSION   WP_273602506
VERSION     WP_273602506.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 643)
  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 643)
  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..643
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..643
                     /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=70905
     Region          <262..>388
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          374..624
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mtsvrtdvsd aevdgvytaa gsyrmsealq lsralvgsyp dsqrckflqs wlglrlgepa
       61 apellqqaea leqdltldpm qraellllla vrrmaqgltl talknegeal alfehagrkv
      121 gecmaawqml vhlisigdld everlqplle rrllgrydwa davlavsras aaygraeagd
      181 knsrstciai yrdlyerskl palcefrrmv gtnlavncal ggefelaqql lselelldag
      241 vnqvavitmh awraythalv glrdghldla aveltralql enrgqrganl qskileaqae
      301 cafrqgried grtalqerqk vqddvlrqlr akhnagmeal lreaqlatel rarnadlrla
      361 ydemeqrvre rsaelaeaqq alhrhaqrgv vsklligvah qlntplgtag ltvsalrdql
      421 qgllsqlqsp mrkqdllasv eqmddaaali etnllrsrsl lsrfselglh eqlhqsrrvq
      481 lapwlreqve alqqewqavg vqpvlqleeg iewlgavdal ghvlqhlfrn amrfarvdgr
      541 aapvslvfqr llpgpglcie vkdqgpgmse srrahafepf aeqlvteggl glvlvrnlve
      601 glmrgqvelr anqpqglcvr itlpesgtgs lyqsvgqals gra
//
LOCUS       WP_273602452             781 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Roseateles albus].
ACCESSION   WP_273602452
VERSION     WP_273602452.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 781)
  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 781)
  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 781)
  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 781)
  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..781
                     /organism="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..781
                     /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=85808
     Region          82..754
                     /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 mmtpatklde qaqnealgda aelqdqgrll ltllwlvall lplvvlglqw lphppfgppd
       61 waiffaalla lmglglgsfa srlrrseqrl grvlaqpwlg elifsahgll levsplvarl
      121 sgysaqglsg rplsdllpat efedigdkpt pvlagellqt emrchdgqml aielvinplp
      181 gerwqlllrd lsegqrsqqh lrqsdivfyn areaimitda qacvtavnpa ftaitgytaa
      241 evmglnphfq nsgrheavff srmwqslaer ghwqgeiwnr rkngelfpsw qtisavknsa
      301 gqvenyvslf sdihslknae erlhhlahhd altglpnrll fandlersie rakrsgksia
      361 llfldldhfk lindtmghav gdkllheiah rlrnsvraqd gvarlggdef tvsledvgga
      421 ddvatmahki iaalsepmql egnqvtisps igiafypadg antedltraa daamyrakqq
      481 grktfafyst eimassverv lierglraal saqqlelyyq pqvdmvtgri vgmeallrwh
      541 hperglvqpd sfigvaeetg liseigewvi qqgcrqarlw reqgfnlgyl wvnvsprqil
      601 hngiedaiaq amhenqlpgg aiklgieite sllqsmpqsi evlgklralg vriaiddfgt
      661 gfsslgllkq lpidvikidk mfvrhlavdg dsqaitaami smthtlgmgv vaegvetaeq
      721 leflrmqscd vvqgylfgap lcpaeatqll vkhrlgwpdp psaefsppmp dkgqsdlpgl
      781 p
//
LOCUS       WP_273602535             405 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Roseateles albus].
ACCESSION   WP_273602535
VERSION     WP_273602535.1
KEYWORDS    RefSeq.
SOURCE      Roseateles albus (Kinneretia alba)
  ORGANISM  Roseateles albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
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="Roseateles albus"
                     /db_xref="taxon:2987525"
     Protein         1..405
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42800
     Region          1..405
                     /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 malggvrvld lsrvlagpwc tqtladlgad vikverpgsg ddtrawgppy lkdeqgrdts
       61 eaayylganr nkrsiaidia cpagqalire laagvdvlve nfkvgdlary gldaqslrel
      121 npglivcsit gfgqtgpykd ragydyavqg igglmsvtge rddlpgggpq kvgvavadlf
      181 tglyatvail aalrhrdatg egqvidmall dtqlamlanl ganylctgqv ptrmgnahqn
      241 ivpyqafeas dghlilaign dhqfakfcai agfpawaqdp rfstnaqrvr qrellvpmia
      301 aaiktrprda wlsaleaakv pcgainnlae afadpqvqar giarpmphpl spglqlvssp
      361 mnlsatpvsy rrappllgqh thellleagr teaeiaallq agvia
//
LOCUS       WP_273602601             385 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: aminotransferase class I/II-fold pyridoxal
            phosphate-dependent enzyme [unclassified Pseudoalteromonas].
ACCESSION   WP_273602601
VERSION     WP_273602601.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 385)
  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 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 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..385
                     /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=42230
     Region          3..385
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mpfeflnthl qqqqqhallr krhvvqrata rtitvnnaty lnfasndylg fgdysinfeq
       61 nnvlgshssp lvtgyqaqqq qleqylcsal gyeagmlfns gfsanssvik alfndkstaq
      121 nsaifqdkln haslidgamh snaalirfnh ndlkhlrsrl ekskahnkli isegvfsmdg
      181 dtapikella lakehnawlm iddahgfgal gktglgscea lldeglelpd ilvitfgkav
      241 assgacvlan nqfinymlqf nrdytystam splmaaltlt rlqaikradv krqqlssnia
      301 ffkqlckqha iavmesktai qpivlgcaeq tlhaaqrlkq qgiwltairp ptvahntarl
      361 rvtltaahth tditalveql kgaia
//
LOCUS       WP_273602679             279 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: segregation and condensation protein A [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273602679
VERSION     WP_273602679.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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 Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=31349
     Region          41..275
                     /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 msdttqgekk tqsepvqqkl plaflhgkav vdkpedlyip pdaleiilet fegpldllly
       61 likkhkldvl elsifsiteq yvsyvemmse fqlelageyl vmaallaqik srlllpvhee
      121 leeeedprae likrlqeyeq fkkaaenida iprvgrdifv ahatmpvien taqnlpelel
      181 kdlmlalsdv maraktfehh kvtaetlstr ermskilaql snakkalpfn dlftlsegrs
      241 gvvvsfiaml elikeglisc lqvspdsliy inltdtpns
//
LOCUS       WP_273602874             332 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273602874
VERSION     WP_273602874.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..332
                     /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=38377
     Region          110..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnsyvslsdk yltaqglita vvelaqsrgv alhkllrgtg ifeqdllsve hcfsleqqvk
       61 llsqfkrlmn tpdsgfllgs qlvndsssaa qsvlysaklg aallqiqrar lqlcplffsq
      121 hyvsnqqfyi flnaatgldd dlhnyileiy saafysllkr lsphypqcef dfsfkrprhi
      181 hqyeqhlglk lrfeqpttrw visktllrqa npyaselrfm qaraqlavks hekytfieav
      241 wrylhtynea sleqtaqyfa mspatfkrkl kchnmrfssl vdeqnkhkai ylltlrakcn
      301 ehvaerlafy dipnfrrafk rwtgltpsql kv
//
LOCUS       WP_273603059             395 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: vWA domain-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603059
VERSION     WP_273603059.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..395
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45617
     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 mlvqffftlr kyrlpvslre lldlinalkk gvifadvdgf yhlartimvk dethfdrfdk
       61 afsdyfsgia dldlleslkq qhnlpkdwlr kefekhlsde ekaqlkamgg ldelmktlke
      121 rlqeqqkrha ggnkwvgtgg tspfgaygyn pegvrigqeg nrnrqavkvw dkreyrnlds
      181 dreigsrtik lalkklrkfa rtgasdtldl netiratakq ggmldvkmap erhnavkvlm
      241 lfdiggsmdd yihtceelfg aahsefkhle fyyfhnclye hvwqdnarrh sniidtmtli
      301 nkftsdykvi fvgdatmgpy eiaypggsve hyneepgsaw lqritnhfdk vawlnpqpve
      361 hwpyyqsidf ikqlmdnrmy plsldgisna ikels
//
LOCUS       WP_273602991             442 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: alpha/beta hydrolase family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273602991
VERSION     WP_273602991.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 442)
  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 442)
  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 442)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..442
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..442
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48632
     Region          46..394
                     /region_name="COG4188"
                     /note="Predicted dienelactone hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443342"
ORIGIN      
        1 mttthtlkaf skalllatgc ltastvfadq ktpeqlyppl tsevlpelaa kgsysvgvqt
       61 ldlinpaqfd patqgekdrp lkvevwypaa dsanapltsy sditrtgkaf tlqadamrdv
      121 ainnkehypv ivlshgytgy rtimyylgeh lashgyivaa idhtdstnad vdfknapfsg
      181 ffstlinrsr dqqfvlnyfn eqnnfaskqv dnkkagvigy smggfgavnt iggcydfneq
      241 ttamftgmkd paqikqvqql lnscaggqyk npqvdtrika mvafapwggq hnlfnasamq
      301 nikvpslyva gslddisgye giknlynqtg spdkylltyk narhniaphp apaiakrsse
      361 ldighyyeps wsmrtlnetn khfvlammdc hvkgitsqce yldlpqngdq avvngkplpa
      421 whgfdnrfst gmdwqqakpr tk
//
LOCUS       WP_273603086             241 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: substrate-binding periplasmic protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603086
VERSION     WP_273603086.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..241
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27037
     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 mrllllcfis cffisppvsa awqkqpivia asatippyvi ektdtgiqln iikaalieqg
       61 ldnivviyms nkraeqqlhs gnvdillnya gkrgagiyps qpvlsyknva vslkkrnfti
      121 etikelnnks vlgfqhatay lpppfakgva qfasyeevvn qraqvdrlmk dwvdviilde
      181 rifhyynndy ahslpvnihp ifpkaprpay fnnavlkktf dkglltikak gkyqqimsgy
      241 h
//
LOCUS       WP_273602980             468 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: protein adenylyltransferase SelO [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273602980
VERSION     WP_273602980.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 468)
  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..468
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..468
                     /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=51693
     Region          1..468
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mklvprytdi adnfaiedsp ssvaapqlll wnealaqqfn idvelalras tfagnepqpv
       61 savalgysgh qfghfsprlg dgrahllgai sddknqlwdi qlkgsgatpf srggdgrcal
      121 gpaireyims eamhglgikt trclavvgtg eavyrnppqp gaivtrlans hirvgsfqyl
      181 atqgdveglk kltdvaierh ypsiqstgaq ryldflaavi nsqlalvisw mrvgfihgvm
      241 ntdntlisge tidygpcamm ntfdfdtvfs sidkqgryay gnqpnivswn carlaeslip
      301 lideddeqav slmtplinqf stlfnaqynq mwaqklgsag ykeddvelvs kllllfqehk
      361 ldytntfdal teslkggkvp neltqwaqlw qkrcdensyn lmraanprvi prnhiveeil
      421 aqynqhgese llsdfltvms npydktanla rfqetgkddk gyqtfcgt
//
LOCUS       WP_273603119             356 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: PepSY-associated TM helix domain-containing protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273603119
VERSION     WP_273603119.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..356
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=40490
     Region          24..354
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mkiwlrrihl ylallsglfl lilsisgail lyandiqyyi qpdkwqvvpq tktlshaeli
       61 ravqqqtdkk itrfmplsnp naswqfrlgd gsnasvnpyt gkvifqyqtn dtlygftlal
      121 hrwllfetas gekplknvvs vcallliinv lvgfylwvkp knrlkrlaik pkakfkvlmy
      181 qlhtvlgvyv llpllliaft gitfnwksat ktlvetvafs qvrnrpkapt vianstastn
      241 ydqainkald vfpegilyri ylpkkhndpi alriqnpges hayswvwvnp ysakvlsayd
      301 askanavthv wnfkyvfhtg afagpivkfv wllvslslaf filsgvylwc krhkwv
//
LOCUS       WP_273603132             134 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: nucleotide triphosphate diphosphatase NUDT15
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273603132
VERSION     WP_273603132.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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 10140375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..134
                     /product="nucleotide triphosphate diphosphatase NUDT15"
                     /EC_number="3.6.1.9"
                     /GO_function="GO:0017110 - nucleoside diphosphate
                     phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0047429 - nucleoside triphosphate
                     diphosphatase activity [Evidence IEA]"
                     /GO_process="GO:0006203 - dGTP catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0042262 - DNA protection [Evidence IEA]"
                     /calculated_mol_wt=14860
     Region          5..127
                     /region_name="NUDIX_MTH2_Nudt15"
                     /note="MutT homolog 2; cd04678"
                     /db_xref="CDD:467561"
ORIGIN      
        1 msnivrvgva viimrqntil lgerigshga ntwatpgghl efgesveqca irevfeetgl
       61 nvskiikldf tndifsaenk hyitlyvkag yeggepvlne pnkcmqwrwc dinnlpsplf
      121 tslknylttt tltv
//
LOCUS       WP_273603283             280 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: amidohydrolase family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603283
VERSION     WP_273603283.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=31704
     Region          4..280
                     /region_name="COG3618"
                     /note="Predicted metal-dependent hydrolase, TIM-barrel
                     fold [General function prediction only]"
                     /db_xref="CDD:442836"
ORIGIN      
        1 mslkiidphv hffnlaegqy twlqgenppa wpnlelikqp isekelless dftlagivhi
       61 eagfdnnapi nelnwltahl kklpfkaisy aqldcapvqf akaintlahp hligirdite
      121 gadaqrllnp ecfsnlqslc qqglyyeaqf elentaiaaq laryakalpq lkiiinhggl
      181 pnninnwqqs irmlsahnni aikfsgfell alnlqqqqdc fetmfsyfge qrimfasnfp
      241 vcqinasynd vwhshqalck tnkiwhnlsy anakhfynip
//
LOCUS       WP_273603474             424 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: purine-cytosine permease family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603474
VERSION     WP_273603474.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..424
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..424
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44868
     Region          18..420
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mpngndphti nsnelvawpr iaaiaamlsf slptfitgle ihqsssvsnt lwalvigsli
       61 ltliggamgt igvksrlssy llvkiafgna gagivniafa lsligwfgvn idlfsnavvr
      121 llsaefniim pewpidivag camlittlyg fkainvlasi mipilaavta mmlfgaldsm
      181 plvdfinlek savlsledgv aaivggviig aiilpditrf skqkrggvyt sfiaymviel
      241 lvifvavfaa aamqeteils lmlalnlgfs affiviagsw ilnslnlyst alsveatfph
      301 whkkwvivll glvgigaafi nildmfisfl aflsdifvpv agviivdalf ikphaynaaa
      361 lannanfslp afsawfvgaa yavcngalfn vsmsgitvid aiiltaviyt lfakaiapkp
      421 vvqq
//
LOCUS       WP_273603374            1011 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273603374
VERSION     WP_273603374.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1011)
  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 1011)
  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 1011)
  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 1011)
  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..1011
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..1011
                     /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=109223
     Region          185..948
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mhikqmlgev aslnvigkkk fkkkiknyrg ilfvsclykl rsnqthlfsg lsvlapaifs
       61 lsvqgatqtt gqmvqfdiqa qradkalief akqteqtvvf syelaknyqa nsvygfytql
      121 dalqallsgt eldavvdqng llsiklkqin rkdnnmmkls gvsaavlpal laanshgvna
      181 aegvaqekie kiaivgsrva grsvedlpvp vdilsaeale ntgqtevgrm lqsiapsfnf
      241 ssssisdgtd alrpatlrgl gpdqtlvlin gkrrhqasii hintsvgrgt agtdmnaipa
      301 saikrievlr dgaaaqygsd aiagvinivl kdgseggkaa vnygqysegd getvnvdfnk
      361 gfalgdsgyl natlnyrdrs ptnraglhgs cqfygctels dgtllagdpr eltadrdtfr
      421 igdadsqqfg ltvntgyelg dgelygfity strdnesaaf frhnanaggn pvlqdndati
      481 plgflpkint tiddisynfg yktdfdndas ldvsytygen sidyttsdti nasyanflry
      541 eqglsaadir stipreayay gmelslqtin idftqnfddy slamgaeirt deyrilegse
      601 yayrdydtld gvsiysglsg gvgsedvsgg tqgfggsspa ssvdesrdvi sfyldaetyl
      661 iedvilsgal rydnykgfgd tvnfklagnw aitddvslrg alssgfraps mqqlyfnnis
      721 tqfvvaedgs lvaeevgtfr ndstlaqslg ipklkeeksq nrslgivynv tdninvtvdy
      781 ysididdriv isnrlgkgls ssldaaliss gagagqffln gadtetsgid fvatwntegl
      841 ggtldftlaa nftetevvsl ftpsgsglet vpvedvfsdq eisiieewqp edrinlsaly
      901 qrgdwtvnls lnrfgeytve dggrqtygae iltdvkvnyf vtedlsvnig annlfdvypd
      961 kntignsrsg tivdsngnti vssdgvfeys rrsapfgfng ayyyvgaeyr f
//
LOCUS       WP_273603508             442 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603508
VERSION     WP_273603508.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 442)
  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 442)
  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..442
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..442
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49702
     Region          98..128
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(99,102..103,106..107,109,135,140..141,144..145,
                     147..148,173,176..177,180..181,184)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          105..377
                     /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..165
                     /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          315..343
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(316,319..320,323..324,326,349,352..353,356..357,
                     359..360,383,388..389,392..393,396)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          347..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          382..412
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkllptaknl klalfctaai sasivvpstl slvpglnvat ahaeqeqktk rvpalrekvy
       61 sqlaraqkla ddgdvkggle aldsiqeras smnsyeiamm hnfygfiyyn endlpkaias
      121 fekvvaeeai peslrlsttf slaqlamang eykkviafld kweeintkpi tegyyllraq
      181 tyyqlkeypk gleyinqvia lsdsegkipk enwlvlqram yyslnqtdkv vavlermvkl
      241 ynkpeywvql agmygetgke keqlavieaa yqqgflktks dlrqlsqtyl ynglaykaak
      301 tmsdaiekgi veksaknyaf iaeamiqake deksisyfak aadlsehgky dqrlaevfvn
      361 teqyeeaada arkaldkggl dfesnayval gmaqynmqnf dasilafeqa qkhnksqria
      421 kqwikyvkre kvhaqtlkaa ll
//
LOCUS       WP_273603516             805 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603516
VERSION     WP_273603516.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 805)
  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 805)
  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 805)
  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 805)
  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..805
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..805
                     /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=89524
     Region          50..804
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkkfkyslvt laclnaslav aattaekdie risvyekqnq vvmssglatk sdmslmetpa
       61 pvviidreli esqgvdslqe lvrnvsgltq agnnygigdn lvirgldany tydgmyggag
      121 lgntfnptrs ltnvesvevl kgpatglygi gsaggvinli ekkpefeekh kisaelgqwd
      181 syslafdstn aitddlayrv maktassdgf rdlkedrdei ytslkyilsd kqdimlsaay
      241 ikdsiavdsi ghpiriynae tangltagev tgadlvndps gdgvqltaaq qtqladslss
      301 tdgltpydfg tngiispmad dnkgeelrfk lthnyfitdd lflnqqlqyr nytssfarqt
      361 gafnyvystr dgiinndpra plveegvlyp faarrqeyrq veadekswqy fldlrydfml
      421 gdvdnellvn anyedrdirf kqysiydadk viydsegnvl yqgtlpyiyd mrspnwptgs
      481 fddydplkts dynkkvqawg lgiqhvgyit eqlitrvgva ynrikqtyeh ygvderysss
      541 raeptpeant sdsgltynlg atyqptenfs vfinhakgrt aysvlgsvag teadredses
      601 isndlgfrfk afddqllasl vvfesartnl eytnplyeag vsgpdvvesy ydgeeqtkgv
      661 eldlnahlne qwkvnvngvy qdardksnpn sssydtrqkg vpyvtastwv tyyadmfnlp
      721 eavnisggit fvdnrstnss sfsipdgyvp sytvydaavs yttdkwhmql nlnnlfnkky
      781 yskamflggm pgeernakls fsytl
//
LOCUS       WP_273603633             328 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DHH family phosphoesterase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603633
VERSION     WP_273603633.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=36759
     Region          5..301
                     /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 mkskeeilaf ikrlsplqrv iiqahdfpdh daissayals vllshyeist livyngeidr
       61 islsnliqwl eipiyhcsqv rlnpsdkiin vdgcigeknv tdvpgdeiav idhhtvkpsk
      121 sfwfedirsd ygatatiiwe yyqllgikms iqvasallvg lnvdtanmtr gfckadikaf
      181 vylnarsdla fvnrvlrntl mqgelrnfel afrnlsvndg vasvilpepc pknmlgmlgd
      241 fllsvnefdv vivavkqnng lqlsfrsecq nvdvgrlare tlnntnrgfg gghrhmaggi
      301 vlpeyismft eknnhfkpfi kkisewra
//
LOCUS       WP_273603664             300 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: prepilin peptidase [unclassified Pseudoalteromonas].
ACCESSION   WP_273603664
VERSION     WP_273603664.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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..300
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..300
                     /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=32912
     Region          16..298
                     /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 menlflditt amqsqqwfyl ttvglislcv gsflnvviyr lplmmqrewq secrlllede
       61 ltakptqasn sepfnlvkpn stcpkcktai kpwqnipiis wimlkgkcan csnpisaryp
      121 iveaitalls lviaysfgat ehallyifvt wilvaltfid idhmllpdql tlplvwlali
      181 aavmgitisp seaivgaacg ylslwsvfwl fklltgkegm gygdfkllav fgallgwqsl
      241 ltiillssvv gaiigialls iqgkdkatpi pfgpylaiag witllwgaqi qaayfnligy
//
LOCUS       WP_273603708             474 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sigma-54-dependent transcriptional regulator
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273603708
VERSION     WP_273603708.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=51821
     Region          1..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 msntilvved daglrealid tlemsgiacv aadsaeqami qlkksefslv vsdvqmgams
       61 gldllrsikl nypelpvlmm tayatiddav eamrlgaidy makpfapevl lnmvsrylpe
      121 kpkdtdgpiv adpssialle laskvarsda svmvlgpsgs gkevlaryih dksnrcdapf
      181 vaincaaipe nmleatlfgy ekgaftgaiq acpgkfeqaq ggtilldeit emdlglqakl
      241 lrvlqereve rlgarktisl dvrvlatsnr dlkeavadnq fredlyyrln vfplmwrplc
      301 erpgdiivla khlierhlvk skeplatlds aaeqkllsha wpgnvreldn viqralilrt
      361 gnvigeqaif ienlmqapin stptqeiaae qantpsgayy ddkitpaeas sslpnvdtgs
      421 ykdelkdkeh kiiletlarc qgkrkdvaqt lgisprtlry klaqmrdlgi slpa
//
LOCUS       WP_273603827             102 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603827
VERSION     WP_273603827.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=11444
     Region          1..93
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mnieqlaena qqaeqflklm anknrlmilc sllqgeqsvg elnqnvplaq salsqhlasl
       61 rkaqlvanrr eghtiyysli dpkvesiitl lyewfckqst ae
//
LOCUS       WP_273603844             280 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: LytR/AlgR family response regulator transcription
            factor [unclassified Pseudoalteromonas].
ACCESSION   WP_273603844
VERSION     WP_273603844.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 280)
  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 280)
  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 280)
  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 280)
  AUTHORS   Galperin,M.Y.
  TITLE     Telling bacteria: do not LytTR
  JOURNAL   Structure 16 (5), 657-659 (2008)
   PUBMED   18462668
REFERENCE   5  (residues 1 to 280)
  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 280)
  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 280)
  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..280
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..280
                     /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=32282
     Region          <164..276
                     /region_name="LytT"
                     /note="DNA-binding response regulator, LytR/AlgR family
                     [Transcription, Signal transduction mechanisms]; COG3279"
                     /db_xref="CDD:442510"
ORIGIN      
        1 mnlqhfqrfq tlyasvllca yvlinntvna ttqimevkrs gdlpfliwep fvweyssalg
       61 sllmfpaliw flnntpfkwh kipaslgmyf gasivfsmlh iaimvgsrkl vylawgrsyd
      121 fglswfeliy eyqkdaisfi ffialikvyq yvvqqligea ssieeseqqa tpslnrllvk
      181 khgkefivki ddvdwlessg nyvnlyigts iyplrmtlte lskqleekgf crvhrshgvn
      241 ldriesitpl psgdseiklt tgkmlnlsrr ykeqfklqlk
//
LOCUS       WP_273603860             409 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: pyridoxal-phosphate-dependent aminotransferase family
            protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273603860
VERSION     WP_273603860.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 409)
  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 409)
  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..409
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..409
                     /product="pyridoxal-phosphate-dependent aminotransferase
                     family protein"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44706
     Region          15..408
                     /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 mfsdtqiqtl nppqrllmgp gpinadprvl ramsaqligq ydpvmtgfmn etmaryreif
       61 ktknewtmlv dgtsragiea vlcsilrpgd kvlvpimgrf ghllaevaer vgakvhtiev
      121 pwgevftpeq iekaivdvkp hvlamvqgdt sttmnqpleh igdicqkhdv lfycdatasi
      181 vgndlpadew kldalsvglq kclggpsgsa pltlsdkcad wiqkrkkvea girtaqhtdg
      241 tepfvrsnyf dlgmimnywg eerlnhhtea tsmlycasec arivieegvd ncvarhklhg
      301 damltgiqal glnvfgdlnh kmnnvvgvyi peginadhlr gqmltdfgie igtsfgplhg
      361 kiwrigtmgy narkdavlqt lasldaclha ngykgpkgea aiaalahyk
//
LOCUS       WP_273603871             305 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: carbohydrate kinase family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603871
VERSION     WP_273603871.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=32673
     Region          15..289
                     /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(38,250,253)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238572"
     Site            order(184,221,248,251..252,255)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238572"
ORIGIN      
        1 msilidskqg kdvsvscfge vlwdcfandk rlggaplnmc vrinslgika dmisavgnde
       61 lgtellgeik skgvsceyig vnndkktstv qvtldksgsa syeivadtaw dnieltdsli
      121 ekvkasdvfv fgsligrsea slatlnqlvd vanfkvfdvn lraphytldt lvdlmnkadf
      181 iklndeelye iakaigckfh sleqnlafia qqtnteylcv tkgshgallt ikgenyynsg
      241 ylisvvdtvg agdsflgsli yqlcssdcaq havdfacavg amvaesagat ptltheqine
      301 fmspa
//
LOCUS       WP_273603891             784 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603891
VERSION     WP_273603891.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 784)
  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 784)
  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 784)
  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 784)
  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..784
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..784
                     /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=85542
     Region          61..784
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkhsylalfi aasltpnfya haaqsaantd sierievagq tiksqglsvk datingpfgd
       61 nlalqdiars vtpisselie qlnittlqdv lavspntysa sgfgapslpt irgqlgelfq
      121 dgtrrqagnn gfgvplsfns veqidvvkga ppvlfgssqr nggfvnlhsk aastdeskgk
      181 vklsagrwdq ysaqvdytap iikdkvglrv syehldegsy ydysgtksds lfaalrilpd
      241 dksswdinfe lyqveftdna ginrptqali ddglyitgqg vqangstvpa agsivsptgq
      301 vkidrstalt dpdnqneatt ylihsiykre lsanaslkni tyfqhlqree iaqnsfveii
      361 dgadtaqnrt eltyrwnsdq ktifafdvry nkalgysqft teadlpidlt gplsnrripl
      421 tdaqkvrlve lspgvfvspg gqydldndgs gdfnlsdttd srswqtglai qqdsdwgdkl
      481 htsvgyrvdf ydveandpia pqgqvaasds inetlhsgqv sfnyklnady ttygaasyne
      541 atsnsmaggt slggdntisa qnfatentlv efglkyaptn sdwyadgavf sqrrslrnrd
      601 gsntgirttg fesqifyday pywlsagysy idarydnsas sqdsaqvida fdnsrpdiia
      661 gtgvgapsft afapsnrqvq gipeqsfsfn gnysinskwq mgfsglytks ypldflatvk
      721 irdqytlnvn tsyaftprtk lrldvnnvtn qknwrpvfeg gyfgatlafp elpinakltl
      781 thnf
//
LOCUS       WP_273603877             405 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: MFS transporter [unclassified Pseudoalteromonas].
ACCESSION   WP_273603877
VERSION     WP_273603877.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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   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..405
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43947
     Region          13..390
                     /region_name="FucP"
                     /note="Fucose permease [Carbohydrate transport and
                     metabolism]; COG0738"
                     /db_xref="CDD:440501"
ORIGIN      
        1 mtnlhthsqs dpmqhirilt ymmffmfamt sdavgmiipe litefglsmt qasafhyapm
       61 aliafsglfl gfladslgrk qtimlgllif slscflfafs nsfsvflill cciglaiglf
      121 ktgalallgd isasnaehtk tmnkvegffg igaivgpalv gvlltqnvsw tylyiiagvm
      181 clilalmawr adypsvvksk ekpaslattm kmiknpyalg fslaialyva tevaiyvwmp
      241 tllkdytgsw pllatyalti ffvlraagrf iavwllnhfs wqgvmaylsl gialcyvgtl
      301 vggvdwavgl lplsglfmsm vyptlnskgi scfpvaqhga vagvilffta lsaalaplfm
      361 gmisdyfghv rygfylatgf avilflamly nfyrdpaaka ltkna
//
LOCUS       WP_273603938             686 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273603938
VERSION     WP_273603938.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 686)
  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 686)
  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 686)
  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 686)
  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..686
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..686
                     /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=76657
     Region          42..644
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkipkkllcs liiaspilaa eplndddldl dalmgmdvqa tsamkraqsa fntassiyvl
       61 skeqitssga tsipealkmv pgltvrqldn nqwaisargv asrysskllv midgqslytp
      121 kfaavywesl hvplydieri evirgqggll wgnnanngvi niitknsldt rntyakaitg
      181 nqinadislr hggdisdigs yrgyyntknt apskkgsrik pndftkqhag gfradftpsd
      241 ewsillqgdh thtehgqnlt gvldasnrsq qfptianrrd trlmtrvehr lsdnanqmlq
      301 mswlkqhgeq pyinedfesi dvdyqmnfit galqvdwgln yrfndisfqd sifinsdkdl
      361 edlyqygaml qaqysvipdt lnlivgtkie hndltgwenq plarftyqpn sehlawgsis
      421 rsvriptlie fndnfrvngq kisdvigmqs giaeidqyhi atflngndnv kaenyisyel
      481 gyriskaews ldvsafntqa ddvavislnp hveqfipaln fylagevsqa faalqttsld
      541 ydfvsvgett ttggdllfsm qlmddlssev gysytkidyd lpnatrptig ydsvnrqlft
      601 klnyqlteqh sifatlraen sstyntdnyt avdltwnwki nnswatavsg knlfagshie
      661 yantretftv pnyidecvtf svsatf
//
LOCUS       WP_273603940             238 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: SIR2 family NAD-dependent protein deacylase
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273603940
VERSION     WP_273603940.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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..238
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..238
                     /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=27350
     Region          2..219
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mntlyitgag vsaasgiptf rgedgfwtig sknytpmema tramyqnnpr eflawyynrf
       61 aayrnhgpne vhhwlsdknl itqnidgldg kagnknyiai hgrldqmtlf heqgeavkpl
      121 mtpwdsvdes rlheslfelf niqnqtpeln hsfkpfvllf defytelyri teaqqrmlna
      181 dkivfmgtsf svnitqmale varnydipve vvdpnpvyim hsnvtykkmn aleyiqsn
//
LOCUS       WP_273603965             241 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273603965
VERSION     WP_273603965.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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 10001729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..241
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27121
     Region          10..215
                     /region_name="SerB"
                     /note="Phosphoserine phosphatase [Amino acid transport and
                     metabolism]; COG0560"
                     /db_xref="CDD:440326"
ORIGIN      
        1 msnskinfip kiwffdmegt llqkdfaldn gkvapsawtv lakliseecy leeelskdrw
       61 nageyngyle wmkdtiriqq ehgikkwhvd eivksaklhn gahelitsik atnakvvlis
      121 ggikaladkv qrelkidhaf saceyffddc gnldfynllp tdnegkasfm qqivkeygvd
      181 psecafvgdg kndkflarvv gvsiafnaqk elievsnfsi vqpqgkedls eikslpffvq
      241 q
//
LOCUS       WP_273603748             939 aa            linear   BCT 28-DEC-2024
DEFINITION  TolB family protein [Pseudoalteromonas sp. GABNS16C].
ACCESSION   WP_273603748
VERSION     WP_273603748.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. GABNS16C
  ORGANISM  Pseudoalteromonas sp. GABNS16C
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 939)
  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 939)
  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..939
                     /organism="Pseudoalteromonas sp. GABNS16C"
                     /db_xref="taxon:3025322"
     Protein         1..939
                     /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=105098
     Region          388..544
                     /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 mkksliaasl llatptlaad wqtihtehfn vhystenady akstavelei vrtkvleqqn
       61 raldkvvdvv vfdplnapng falptsnnpl malfttppqs dtvvsnisgw qqllilheyi
      121 hlvhlaqptr ntwqqkirgv wdiydltysd mprwvaegya tlleskmtgr grlfdnytes
      181 mliefaqqga lpsysqlsdt eggfmagsma ylmgsrflnw leqtysaqml davwtrmqav
      241 kkrdfneaft gifgqsaanl ygrfiaqyty kamakeqsep alnselwlkl nlyasnpals
      301 kdgsklaive rdkdkktkli iystqdntka edeftkaqka llendaldip dnapsvfkre
      361 kkhvlnqinr agianpqwvn nstlyfnayt reetgiynkv sdifsyntet gkveqltkla
      421 glrrfsvtnn getlyaeqvr ggyselvkvd latqtitplf tkslktaydy ptfspdetql
      481 ayvsanlnen wqlyiqdvsn ntrqavpmpn gyqylsqpsf skngekiyfv aglkgstdiy
      541 syhiasstlt kftqgqeava hpletnegal lylsitadgp nvkrlpstle geivtdlald
      601 nsaplllvdq ytlpkakiys envgkqssyd vldqhaslal gaqhysaass alninikssd
      661 llkqldlqag ysvdlnddal hggyaqakyn alpvklklsv fdydlntakq yqasenadvs
      721 arggfaalsy pikyaafsit pelaynytdy kqdynkwari gitqswqydr qafaigqsvn
      781 aqyydgsskn nnwdgydlaa kvfgkafdvp lyinftqkqr ddsslalggf nsnlisehqn
      841 sefvlsselp fystaaerym gygggfsfke gmpwlyykqh qvddavyaqs yglkyqgnfs
      901 fglgpvgvnd ltfnmglsrv egdsfedemr gwlsfyysl
//
LOCUS       WP_273604009             593 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABCB family ABC transporter ATP-binding
            protein/permease [unclassified Pseudoalteromonas].
ACCESSION   WP_273604009
VERSION     WP_273604009.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 593)
  AUTHORS   ter Beek,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..593
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..593
                     /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=65760
     Region          1..593
                     /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 mrskhstikr adamtlkqsi ktlwpyitkf kgrvllalla ligakgatll mpwalkeiid
       61 svdksinpvl vipalllily gglrfasvfl gevrdavfsr vtehamrdig lkvfkhlhsl
      121 elafhldrqt ggisrdierg isglsflmrf lmfnivptlf eiltvaiifg slfsiwfali
      181 tllavaiyit ftvtvtqwrn rfireanaad nlsntraids llnfetvkyf nneefeakty
      241 dsflanweta rlknrmslla lnsgqaliia saitalmwlg akevvtgalt igelvminay
      301 mlqlflplnf lgfvyreirr altdlenmlg llnkkpqvtq rphaqhlcis kgniafnnvs
      361 fsydanrpil snisfkvkag skvavvgasg agksslarll yrfydisags itidnqaids
      421 vtldslrkai aivpqdtvlf ntsireniay grptasdsei dkaiemahlk dfistlaqdd
      481 ktlvgerglk vsggekqria iarailkqsp ilifdeatsa ldshaeqail kamrdvtqnh
      541 tsiviahrls tivdadnilv fkkgelveqg thsalllqng qyaqmwqlqq qed
//
LOCUS       WP_273604019             129 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD family hydrolase, partial [Clostridioides difficile].
ACCESSION   WP_273604019
VERSION     WP_273604019.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 129)
  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 129)
  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 129)
  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 129)
  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 the amino end.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..129
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <1..111
                     /region_name="YcjU"
                     /note="Beta-phosphoglucomutase, HAD superfamily
                     [Carbohydrate transport and metabolism]; COG0637"
                     /db_xref="CDD:440402"
ORIGIN      
        1 flkrqgykig lassstkdai eevltvgqls syfdavvsge dfeeskpapd iylhtlqela
       61 vapqeciaie aaekaiasak eaglevwamr dehfgmdqsq adafltqlsd ickkisenri
      121 dessestps
//
LOCUS       WP_273604074             472 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sigma-54 interaction domain-containing protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273604074
VERSION     WP_273604074.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 472)
  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 472)
  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..472
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..472
                     /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=52994
     Region          10..469
                     /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 mikqflndpk lllnavgegi ygfdlsgnav fvnpaaermt gwkakellgk kihqyhhhsh
       61 adgspypade cqiyctmfdg krrevknevf wrkdgtsfav eytstpvyrq geligavavf
      121 rdisaqqqtq nelkqaleqv khlseqlqde nnyliaelne dwqdsglvgq shvfqamlaq
      181 iklvsetdst vlilgengtg kelvarnlhr lskrsnqafi kvncaaftps lleselfghe
      241 rgaftganer rkgrfeladk gtlfldevae lpleaqskll rvlqeqefer vggsttlkvn
      301 irvlaatnrd lwqmvqkgtf ridlyyrlnv fpikvpalke rkedipylct nlitqlnkrl
      361 akqikgvskk aisqlqaydw pgnirelqnv lereailtkh tvlklsqplh gdastavnts
      421 ltlaeaqkqh iiavlelsqw qisgdkgaac klglpestlr skmrklgisk kt
//
LOCUS       WP_273604120             404 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RNA-guided endonuclease InsQ/TnpB family protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273604120
VERSION     WP_273604120.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 404)
  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 404)
  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 404)
  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..404
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..404
                     /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=46017
     Region          1..394
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 mkkairkvty kmkssvsqee slmdlfvhhh qlynwalrdr ietyrdsnys lnfheqckin
       61 tlwrnnrkah gifnanaqse qvtlkrvala fdgffrrlkk gdkkagfprf kpfqrfkgwg
      121 ykahgdgwkl nlkekkhgav yladvgivki rgkarntggk pktgeiirkn gewfisvsme
      181 ydtierncgt kavgldwgvs hyfstidqdg nfeqvenpry lrnskerlts lqrdlalakk
      241 gtrtqrklkh qiaklhqkia rqrldfthke taklvevaal iatekltvkn mtrsakgtve
      301 kngkmvkqka glnreilnta pamtlnllry kaeeassefv evptkqvkps qtcpdcgakk
      361 kksladrwhs cecgcekprd vasaqvnlnw algiqagnqp kkva
//
LOCUS       WP_273604200             358 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ATP-dependent nuclease [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273604200
VERSION     WP_273604200.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 358)
  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 358)
  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 358)
  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 358)
  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..358
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..358
                     /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=39971
     Region          <23..199
                     /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 mvlssqaigr avlagedgsf dpeklrppvf tlialeepen slsphylgri vsalnsmtsn
       61 edaqaliath apsmlrrvdp ehirylrlte trqsritkiq lpaktdeahk fvreavqafp
      121 eiyfsrlvvl gegdseeivl prlfqakgap vdesavtiap lggrhvnhfw rllsalqipf
      181 ltlldldvgr yqagwgriky vnnqlglyqp ekvlpntfsl sdwnddkvpv rthhffengt
      241 ksvfaelemr gvffsfpmdl dfsmllafpd aygvqqevpd dstikavlgk shhdpsqysy
      301 delnlfstyh klfklgskpa ahiealaqls dedllanmpe sfgrltdavi aklaelpe
//
LOCUS       WP_273604316             585 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273604316
VERSION     WP_273604316.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 585)
  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 585)
  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 585)
  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 585)
  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 585)
  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 585)
  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..585
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..585
                     /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=66082
     Region          72..497
                     /region_name="NarQ"
                     /note="Signal transduction histidine kinase NarQ,
                     nitrate/nitrite-specific [Signal transduction mechanisms];
                     COG3850"
                     /db_xref="CDD:443059"
     Region          <295..575
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mlqkslskkl ltnvlsvyfl ltfvvtcgqv laefvntkdy irdelstlqk tfsrsltrai
       61 welntkqtit taegllaipm vegiivrdds geiisqlgrs ldihklynqq lvqeeviied
      121 tksglfgytf plifefsgra tqvgdvtlfs srdvvfsrim vsiyfligna mikttfliil
      181 flmafrkllt dplneltdqi enlelddleg qhidieteeh nelnvmeqsf nnlidkvvqy
      241 rkelehtqre livsnekldq hniqleqdva rktsnlsqam mdlqqqkyel ekqklvltee
      301 vdlrrhteee lltkqkeler yldelslaqe rlvgtekmaa lgglvagith dintpigigv
      361 taisflqerl ntlenaykek tlspkaleef ineakqstsl lttnldrase liasfkqiav
      421 dqaseavrti nfkdylnevi lslhpklkkt khtinlqcpd dlvlnlpaga isqiftnlii
      481 nsiihgfdni aqgnidinis addtlliidy tdngngvtke qlaklfdpff ttkrdqggsg
      541 lgthitfnlv kqtlsgsiea ssepdkglhy hiefpknmpk plfnq
//
LOCUS       WP_273604330             105 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273604330
VERSION     WP_273604330.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=11080
     Region          2..105
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mawvylviag lleigwpigl kisqnpdtrw qgivmaiafl tasgfmlwla qkqismgtsy
       61 avwtgigaag tflvgillyg daatfgriag vlmiicgvim lkiss
//
LOCUS       WP_273603977             180 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273603977
VERSION     WP_273603977.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 180)
  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 180)
  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 180)
  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 180)
  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..180
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..180
                     /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=20223
     Region          1..179
                     /region_name="Adi1"
                     /note="Acireductone dioxygenase (methionine salvage),
                     cupin superfamily [Amino acid transport and metabolism];
                     COG1791"
                     /db_xref="CDD:441396"
ORIGIN      
        1 msqltiyann npsnalvntr dlseitqqla kvnvrfeqwq atapinehtt neqiiaaykn
       61 diarlkaqng yqtvdvisla kgnpaaaqmr ekflfehths edevrffvkg qglfclhida
      121 kiyqvlcqqg dlisvptltp hwfdmgsdpe ftairlfnnt egwvakstes eiakqfpllp
//
LOCUS       WP_273604326             494 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273604326
VERSION     WP_273604326.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=55895
     Region          36..486
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mskqkqqgkt nitwaafiai vlcivvgnav lalstiqglt qtqksldnts lladaierlh
       61 lsivqaesgq rgyllteeed ylmpyydaig qiesqmehvk slhseidgqa eriaellvlt
      121 eakikelkqt vklatndker ralyvlnthr grelykdirv kvndiqdrel lfkvshfskl
      181 aqikneakit faitavtsal liigmflltr lnlrnaakyr eelerqnetl atkvsertqe
      241 ltlysdelsr snreleefaf vashdlqepl rkiqafsdrl etmfkdelge kgidyigrmk
      301 naaqrmsnli ndllefsrvt trgrdfddtd lkgvvndils dlevaikesn ahvevgelpv
      361 iqadksqmqq lflnllsnav kfrkpgveph isvmyehkde fseehnekvg wqiitikdng
      421 igfsqeyadk ifvpfqrlhg rseykgtgig lsvcrriver hggiitahsk dgegatfiik
      481 lpvettlftl qgea
//
LOCUS       WP_273604361             295 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273604361
VERSION     WP_273604361.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=34072
     Region          33..>197
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 marvagknaa dwvvrwdlll ryrlievial wegrlttnhl qrafgigrqq askdinqylt
       61 afapknlqyd rslkgykpsk tfkpmftrgv adeylqmmha redlscalee ldvrelntev
      121 llppsrdlrp avlrpillac reglrveiqy aslknpepey rviqphtvvh ngmrwharaw
      181 cekngeyrdf vlsriqdkpd lsppgdmgke kdsawqrivt levtpdprls vnqqrvitrd
      241 ynmtngmlki kcraamasyi vetlrlngdh hrkptaqqvv lgnrqavsew lwdnd
//
LOCUS       WP_273604376              74 aa            linear   BCT 28-DEC-2024
DEFINITION  pyrroline-5-carboxylate reductase family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_273604376
VERSION     WP_273604376.1
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 11417420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>74
                     /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..>67
                     /region_name="ProC"
                     /note="Pyrroline-5-carboxylate reductase [Amino acid
                     transport and metabolism]; COG0345"
                     /db_xref="CDD:440114"
ORIGIN      
        1 mkigfigags mggamikgll kaeavkkehl yvkggssgta ealqkewgfq lvtdyalfqe
       61 ckvifiatga kvvl
//
LOCUS       WP_273604415             469 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Pseudoalteromonas].
ACCESSION   WP_273604415
VERSION     WP_273604415.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
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="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     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=52812
     Region          153..466
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mmksirsklv itlsvtitgl vlcillatdi avdswidnef drslqskagm lktlvnktdn
       61 gysynfssef mpefagevep eyfqiwnkeg tsirsksldl fevknlpfen leigeskirp
      121 iqlpdgrdgr ifysrfipqv kdkasvdtsk ktdaesmila ytasseevdf vlwlidvifi
      181 vttitvivfi rlfvrkaidt slaplvqlnk disqlsivse gseifikepv kellpivesl
      241 nafikenrql ylrekrltsd iaheiktpia elinmaevsi rfpnekelnd dfkpealkis
      301 lrlknivsnl lllhkygggk lnkrdacdln qvisrileth dlsrvnlqld enapaimsnl
      361 falesifsnl vnnakqyspl dskilvstrv vrdknlilsv tnslneplna sdidqlfdpl
      421 wqkdisrtsi dnfglglsia ktlskaidaq lsakvsdkki tfflvlnkd
//
LOCUS       WP_273604524             850 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: glycoside hydrolase family 3 protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273604524
VERSION     WP_273604524.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 850)
  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 850)
  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 850)
  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 850)
  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 850)
  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..850
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..850
                     /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=91439
     Region          70..>462
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          436..650
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          683..837
                     /region_name="Exop_C"
                     /note="Galactose-binding domain-like; pfam18559"
                     /db_xref="CDD:436577"
ORIGIN      
        1 mktpfslnki arasliaslg ilaacsndat ttpeannals ktekiwpkln iavkqdpkie
       61 akiadylktm tleqkvaqmi qpeirditve dmrkygfgsy lngggafpng dkhatpmdwv
      121 klaedfyqas vddsidgski ptmwgtdavh ghnnvigatl fphniglgaa nnpalieqia
      181 aitavevmat gidwvfaptv avvrddrwgr tyegysedpr ivrdysaaiv nglqgkadgd
      241 flsdkrvist vkhflgdggt vdgddqgnni dseqdlfdih aqgyvgglsa gsqsvmasfn
      301 swhgvknhgn kylltdvlkt rmgfdgfvvg dwnghgqieg ctnescaqav nagldifmvp
      361 tgawkplyen tiaqvkagei smsriddavs rilrvklrag lfnkpspakr qfsgktelig
      421 aqqhrevarq avreslvllk nknnilplda nqtvliagdg adnigkqsgg wsitwqgtnn
      481 knadfpgats iyaglekqit eaggrailsv dgsyeqrpdv avvvfgeepy aeghgdrdnl
      541 efergnkksl allkslkeqg idvvsvfisg rpmwvnseln asdafvaawl pgtegggiad
      601 vilkakdgsi qhdfsgklsf swpktavqat vnkgdddysp llpygfglty gdknvladnl
      661 dedskldnsa ltsmdilvga pvapwrlllk sgdelldvss sthqlgalky rtedktvqed
      721 arqfnfsgeq kasaeivtsf aedtitylea ngvisfdikl nepltddvnl amtcsgecgg
      781 aialskmvdq siknkwqsvs vdlrcfanqg vdfasltspf slhassktsv svaniqfvpn
      841 kadsaglkcq
//
LOCUS       WP_273604564             458 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: class II fumarate hydratase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273604564
VERSION     WP_273604564.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=48645
     Region          1..455
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 msnfrtesds mgelqvpsda lyqaqtqrav nnfaisgltm pkqfvtalay ikqaaaqsnf
       61 elnhlskska naieqacqqi idgehyehfp vdifqtgsgt ssnmnanevi atlatrigne
      121 pvhpnddvnm gqssndvvpt aialssainv vyellpslek lsqsleekka dvgkivktgr
      181 thlmdampvt feqtlsawqs qvnnaasgir hslervcela qggtavgtgi nadgefaskf
      241 aknlsanvgi sfkpssnffy nigsqdaiva lsgqlkvlav aqmkiandlr wmnsgplagl
      301 geielealqp gssimpgkvn pvipeaaamv saqvigndat itvagqagnf elnvmlpvia
      361 hnilqsiell ansaqaladk aiasfkvnqp nidkalaknp ilvtalnpvi gyekaakiak
      421 qaykearpii dvaeqetdlp rselekllnp tkltqggl
//
LOCUS       WP_273604531             350 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: fatty acid desaturase family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273604531
VERSION     WP_273604531.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 350)
  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..350
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..350
                     /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=40804
     Region          44..350
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mkninfdqla hdldsikmdt lgkvgqqdan yirsvvkkhr lcewsgrill mlgfiqpllw
       61 vagvlllala kildnmeigh nvmhgqydwm ndkqlnsqhy ewdiacdgqs whrvhnfehh
      121 tytniigkdr dfgygllrls ndfkwrlknv wqfityinls vlfqwgvsyh elaaervfig
      181 kkkenreggv shstlkqrff skgarqlikd yvifpllagp lflwvlagnl lanlirnlwt
      241 stiifcghft edtetfkqed cinetqgqwy yrqvlgssni kgphwfhvlt ghlscqiehh
      301 lfpdmpssry qevapqvqav mqkhgidyht ggffkqyssv lkriirysfk
//
LOCUS       WP_273604779             197 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Pseudoalteromonas].
ACCESSION   WP_273604779
VERSION     WP_273604779.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=22168
     Region          28..183
                     /region_name="NUDIX_CoAse_Nudt7"
                     /note="coenzyme A pyrophosphatase and similar proteins;
                     cd03426"
                     /db_xref="CDD:467532"
ORIGIN      
        1 mnsehimarf qlsptaapnq ikdtrkkras avmlpiidvd nhahillckr ptylhhhpge
       61 iclpggkfeq sdkhlrttal relheelnia psnvkvlgql pqystltgfs ispfvgllde
      121 htvwendyne vqasfllslt qlsneanwqp ipfqrfgkti tlqgfstphg llwgatasii
      181 knftkqlarq dhyklnl
//
LOCUS       WP_273605001            1011 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Pseudoalteromonas sp. GABNS16E].
ACCESSION   WP_273605001
VERSION     WP_273605001.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. GABNS16E
  ORGANISM  Pseudoalteromonas sp. GABNS16E
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1011)
  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 1011)
  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 1011)
  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 1011)
  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..1011
                     /organism="Pseudoalteromonas sp. GABNS16E"
                     /db_xref="taxon:3025323"
     Protein         1..1011
                     /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=109195
     Region          185..948
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mhikqmlgev aslnvigkkk fkkkiknyrg ilfvsclykl rsnqthlfsg lsvlapaifs
       61 lsvqgatqtt gqmvqfdiqa qradkalief akqteqtvvf syelaknyqa nsvygfytql
      121 dalqallsgt eldavvdqng llsiklkqin rkdnnmmkls gvsaavlpal laanshgvna
      181 aegvaqekie kiaivgsrva grsvedlpvp vdilsaeale ntgqteagrm lqsiapsfnf
      241 ssssisdgtd alrpatlrgl gpdqtlvlin gkrrhqasii hintsvgrgt agtdmnaipa
      301 saikrievlr dgaaaqygsd aiagvinivl kdgseggkaa vnygqysegd getvnvdfnk
      361 gfalgdsgyl natlnyrdrs ptnraglhgs cqfygctels dgtllagdpr eltadrdtfr
      421 igdadsqqfg ltvntgyelg dgelygfity strdnesaaf frhnanaggn pvlqdndati
      481 plgflpkint tiddisynfg yktdfdndas ldvsytygen sidyttsdti nasyanflry
      541 eqglsaadir stipreayay gmelslqtin idftqnfddy slamgaeirt deyrilegse
      601 yayrdydtld gvsiysglsg gvgsedvsgg tqgfggsspa ssvdesrdvi sfyldaetyl
      661 iedvilsgal rydnykgfgd tvnfklagnw aitddvslrg alssgfraps mqqlyfnnis
      721 tqfvvaedgs lvaeevgtfr ndstlaqslg ipklkeeksq nrslgivynv tdninvtvdy
      781 ysididdriv isnrlgkgls ssldaaliss gagagqffln gadtetsgid fvatwntegl
      841 ggtldftlaa nftetevvsl ftpsgsglet vpvedvfsdq eisiieewqp edrinlsaly
      901 qrgdwtvnls lnrfgeytve dggrqtygae iltdvkvnyf vtedlsvnig annlfdvypd
      961 kntignsrsg tivdsngnti vssdgvfeys rrsapfgfng ayyyvgaeyr f
//
LOCUS       WP_273605050             562 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: polysaccharide biosynthesis protein, partial
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273605050
VERSION     WP_273605050.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 562)
  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 562)
  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 562)
  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 562)
  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 562)
  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: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         <1..562
                     /product="polysaccharide biosynthesis protein"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
     Region          39..151
                     /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          194..491
                     /region_name="Polysacc_synt_2"
                     /note="Polysaccharide biosynthesis protein; pfam02719"
                     /db_xref="CDD:426938"
     Site            order(198,200..203,223..224,254..256,277..279,281,296,319,
                     335,362..365,368..369)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(224,226,230,234,252..255,258,261,279..282,285,289,
                     292,295,369..370,375)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187548"
     Site            order(281,321..323,331,363..364,370..372,375..376,
                     387..389,393,395,430,463,466)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187548"
     Site            order(297,321,331,335)
                     /site_type="active"
                     /db_xref="CDD:187548"
ORIGIN      
        1 tlittvslvl laffvgidip rtmpfifawl clltvggsri ivraligrmt tsnkdaviiy
       61 gagssgrqla talnagpeyf vsafidddvt khgsiiqgip vrafndihel ikkrkatkvl
      121 lampsetrar rkevlaqlep lsikvlsipg madivegkak lsefidveie dllgrdpvtp
      181 kddlmtanit nkvvmvtgag gsigselcrq ivklkptklv lferseialy siekelgeyi
      241 tnntlniqli pimgsvqrvn rletvmrtfg vqtiyhaaay khvplvehnv vegvrnnvfg
      301 tyyaakaave anvdtfvlis tdkavrptnv mgatkrmael vlqglaqeqg akhqtrfcmv
      361 rfgnvlgssg svvplfrrqi keggpitlth pditryfmti peaaqlviqa gamgkggdvf
      421 vldmgdsvki sdlatkmvrl sgleiktddt phgdieikct glrpgeklye elligdkveq
      481 tpherimtah evmlplseln vfiealdiac hnfehekirq llldaptgfn ptdgicdlvw
      541 nakkvpavea tpqtnvvnlk ar
//
LOCUS       WP_273605182             250 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-30].
ACCESSION   WP_273605182
VERSION     WP_273605182.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..250
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28171
     Region          32..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 mnvlsctrvf llmwvtclgl fsakaqacdk tinvgtnery wppyvvlknn tltgveidii
       61 ktifkdspfc inftllpnsl raleelkhgr vdlmfaaskt rkrqayahfs lpyreevmll
      121 ykhagsasis sleqlfkkgl itgvnrgsfl ghtfkmlsdk yskqivltsd adkrfallnk
      181 krvdfvvdds lvahhfakky tailpveqva pinvnnvhfm mskktitlee vntinahivk
      241 nkaalkalfk
//
LOCUS       WP_273605084             327 aa            linear   BCT 28-DEC-2024
DEFINITION  DHH family phosphoesterase [Clostridioides difficile].
ACCESSION   WP_273605084
VERSION     WP_273605084.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 327)
  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..327
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..327
                     /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=36595
     Region          11..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 mkimmnnmds iinyiyegdy fivtshispd gdnigstlsm yytlknlgkn vyyvlddeap
       61 lnlrflvedv kiyksnefnm knyslialdc gdkmricvsd eiknnaskli cidhhasnds
      121 ygdlnyvdid asstcelvyn llvrfqqikn iniinediat clytglvtdt gnfsysnvha
      181 ssfemaknll vlgaqkntii qniyqsnssg yykllgealk gleifdskvs sivltqdmmn
      241 rnnisfndvd gittytrdik gievgilfke kkqneikvsf rsknyvdvse iaklfggggh
      301 vraagctird sidnakkmvl eavlksi
//
LOCUS       WP_273605200             846 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: TonB-dependent receptor plug domain-containing
            protein [unclassified Pseudoalteromonas].
ACCESSION   WP_273605200
VERSION     WP_273605200.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 846)
  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 846)
  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 846)
  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 846)
  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..846
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..846
                     /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=90820
     Region          23..794
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mstyrlntla aavafavsap sivsaqeapv eaaqnieqis vlgsrvsnrt stessspidl
       61 idaddlnkgg ftelgqslqa tapsfnfsrt qvsdgsdlfr patlrglqpd qtlvlvngkr
      121 rhnqsifgln gtvgagaagt dmnaipltal kgvevlrdga aakygsdaia gvinlslnns
      181 tgvttgyvqy ggtsegdgdt lsaglnrgfd lgneggfinl sfeyrdadgt nraerdtggs
      241 lnvepgtlse dvrwgqgnse seftslfynm alpmgdsely sfggyserta lgngfyrnfn
      301 easknvtqvy sdgflpriyn eaedisvavg frgdinpdwg ydvsavygen qydftsrnti
      361 nasyaaeyvf nnpdasdadi aanagpsggy sggfrfdqtt vnadfngivd igrneplyvt
      421 igaeyrkeny eivpgdeasy acglantdas ypsvndpdqf aecgfqayng lrpeatnksd
      481 rhsyafyvdv etmvtdawnv sgalryedfs dagddligkl atryefnddf avrgavstgf
      541 rapslqqsgy tafttnlgsd gtltqsftan tgtafpsalg vdsleletst nysagfvydv
      601 tselsltvdf yrveikdrit lgsllsaedv afsdeavaal qatgavqany fsnsvdsttq
      661 gvdiiasyrt dveggnfgvt fagnlndtki dnvnaeegip esvafddlqr sfftdgqpge
      721 ratltfdyer dayettlrfn yfgetdvkyf gndhiplpge lsptgsfkpt stvesavlvd
      781 lnvsyqinei fnvsvgadni fdetpdelgd devlnfitng afkypvralp ygfdgrtyya
      841 kvsfef
//
LOCUS       WP_273605215             575 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF885 domain-containing protein [Pseudoalteromonas sp. Angola-30].
ACCESSION   WP_273605215
VERSION     WP_273605215.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..575
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..575
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=65653
     Region          1..571
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mfkkrilaic laatslpsla dsnsdlktii dnhwqnakae kiffrtdpdg wkpngtlpnw
       61 seqaiakrqa ynnsvlksla nidpktlnne qlmnyrlfky ereteqqsyl yqdkyfpvnf
      121 lsgwhtyfae apanmaflta ddynaflisl adyprfnqqn idlmkegikt gfthycktfe
      181 nysqsisahi vknpensaly epftripntf sasqksnlkq eaqaviknkv ipayqhfydf
      241 fendymphcr aqpgiasvkg gldyykytvn yytttnatpk qihqlglkev arikaqmqni
      301 idevgfdgty sefleflatd eqfyakdaqd llektafitq kmygklptyf ghlprntfti
      361 kgsasrgafy mpppdnrspg tyflastpkl qplynleals lheaipghhl qnaiamelnv
      421 sefrrtlshs afgegwalyt erlgkeagfy qspysdfgrl gyemwravrl vvdtgihafg
      481 wsrqkaidyl ashtalpqsa vedqidryis wpgqalsykm geikirelra kaekqlgaqf
      541 dirsfhdtvi gqgslpmavl edvindwiek qksai
//
LOCUS       WP_273605230             238 aa            linear   BCT 28-DEC-2024
DEFINITION  SIR2 family NAD-dependent protein deacylase [Pseudoalteromonas sp.
            Angola-30].
ACCESSION   WP_273605230
VERSION     WP_273605230.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 238)
  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 238)
  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 238)
  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..238
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..238
                     /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=27319
     Region          2..219
                     /region_name="SIR2"
                     /note="NAD-dependent protein deacetylase, SIR2 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0846"
                     /db_xref="CDD:440607"
ORIGIN      
        1 mntlyitgag vsaasgiptf rgedgfwtig sknytpvema tramyqnnpr eflawyynrf
       61 aayrnhgpne vhhwlsdknl itqnidgldg kagnknyiai hgrldqmtlf heqgeavkpl
      121 mtpwdsvdes rlheslfelf niqnqtpeln hsfkpfvllf defytklyri teaqqrmlna
      181 dkivfmgtsf svnitqmale iarnydipve vvdpnpvhim hskvtykkmn aleyiqsn
//
LOCUS       WP_273605422             406 aa            linear   BCT 28-DEC-2024
DEFINITION  M24 family metallopeptidase [Pseudoalteromonas sp. Angola-30].
ACCESSION   WP_273605422
VERSION     WP_273605422.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     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=44426
     Region          38..400
                     /region_name="PepP"
                     /note="Xaa-Pro aminopeptidase [Amino acid transport and
                     metabolism]; COG0006"
                     /db_xref="CDD:439777"
ORIGIN      
        1 matvgvgtqt seqalaslsn mtckvtpiqv deylqriaka qaymqannid aiylnagtnl
       61 tyftgmkwya sermvgailp aigdvqyiap yfeigtlngf kvvegpihgw qehespyslf
      121 vnvlkqlnvs dtatigides aqffifdgin kaqkglnivn aqsvtahcrm hksvnelalm
      181 qcamdmtlav hqatasmlye gittteveaf ikkahqkvga pgnyfcivlf gvatsfphgv
      241 kdaqvlkkgd mvlidtgckv hdylsditrt yvfgeatmrq rmfwnhekaa qiaafnaani
      301 gatcedvdag arhylaaqgl gpqyqtpgcp hrtghgigld ihewpylvgg dktplapgmc
      361 fsnepmlvip defgvrledh fymtdngphw ftqpsysidd pfglna
//
LOCUS       WP_273605429             236 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-30].
ACCESSION   WP_273605429
VERSION     WP_273605429.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 236)
  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..236
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..236
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27379
     Region          20..231
                     /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 mklylfllcf acirlnaaei tivtevfpdf qyidennqla grsvdkvrna lantdikytm
       61 lahswavsyn avlrdtntci fsivrlpkre dkfswvaele sfdsaiyalk srnirlktln
      121 dakkyktavl rdnfshhyll ergfseannl liidsldkid klistrhdil dfvilskkqf
      181 nyraqfepkl kllepiftln tqhsplyfac nknmpqslqd rlalafdeak kqnkqr
//
LOCUS       WP_273605667             764 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Pseudoalteromonas sp. Angola-30].
ACCESSION   WP_273605667
VERSION     WP_273605667.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 764)
  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 764)
  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 764)
  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 764)
  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..764
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..764
                     /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=85123
     Region          8..709
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mahfklkalv talslcnlav haaqeehttd vkiseelvvy geigyrnrsq elaptleysq
       61 eyfqrfeplt agdalkrvps vtflsdvles dgarmrglsp aytkvlinge evpgagadrs
      121 ffvdripael ierveiirss sanrsadaia gtlnivlrdg ysldggyira gglryddgel
      181 kesfagvygt efaggrlllg anfqgrynpk qkssirygds pennpnyatd dfdnredqsd
      241 trdgddtsln asfekvfdng gkfdisamwv dtdrteders feyddatats nsvveggnll
      301 sdnanvsyid qtnyninsgy elpllggtsk fkvgyasfee svyeqeveld tselpmvfee
      361 aeetveiddk ewslqwqhsl llgdskevqf gafvqgkerd taifeaedes eqtltgwdqf
      421 sqtpmslavf nnefeavdgg vntleedrfd lfalikhead vfswemgvrw estdsnitdt
      481 negvtakndy dfflpsahfr ysvsdngrvs asvarslrrp dfdyitpall eeeladndfl
      541 gnpnlkpess wgidlgyeyr lgksgvvgvn vfyrdvsdli eiastgvegs egegtfvlqp
      601 qntgdgsvqg iefdlstpls alnmpntgif lnyswldsev edsfgkrkfn dqsdyvynig
      661 fiqdlpilra sfgatyrnqg daygrfvgee vttsygadle lfvekrwddv tlrlvgsnll
      721 daskdevfnk fdslddqnsr dfdeyelese eagpvvqlml ryaf
//
LOCUS       WP_273605620             260 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Pseudoalteromonas sp.
            Angola-30].
ACCESSION   WP_273605620
VERSION     WP_273605620.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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 260)
  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..260
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..260
                     /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=28978
     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          <96..255
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mfepkgwgyl qnyehmvqpi iakvdtaqgs keyplhthpk gqlilaldgy vtceaankmw
       61 mvpthsaiwv pantlhsnra sdnaklcfvf idankhgmpq htctlaitgl vkslmlklas
      121 ehqaynedtk tarlaqvlfd lliempaqpl dfvlskhtvi qamgqqllaq pnnrktlaqw
      181 ahdfaltert larlikkqtg mtfgkwrmql hiitalqals dgqsvqqvsa llgyesvsaf
      241 itmfkkvmgk sptkymgdln
//
LOCUS       WP_273605695             646 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudoalteromonas sp. Angola-30].
ACCESSION   WP_273605695
VERSION     WP_273605695.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 646)
  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 646)
  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 646)
  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 646)
  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..646
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..646
                     /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=73059
     Region          <217..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 mqyknlnsde rreavkllys nalsgigvsa lvsfvlvfaf dltdertnqe kiiwlffmlv
       61 vlaarlmdvi yfnytkevnq pfnansflkr fsvgciatai swscyalwfh kssstveitt
      121 tiailsafag gsanllsgsr ftsvcysiil lmpysivltl sddyyhyvlg flgitfsaim
      181 vassyksatf tqtaiklrnq nrellnemes kvetrteeiy rlsntdplts llnrtaflkv
      241 ankqladhpe eklallfvdl dgfkqindsm ghkvgdqvlk eiaerltnvc trhlykcrwg
      301 gdefliltty edeqdlfdfa kkviksirae herykyqswv satigialfp ehegdlsali
      361 rsadlamyhq kriakgcvni ynndlkrqqe reqllskrla saikdnglrl vfqpivdsqt
      421 akvtsfesll rwqlndeaif pdefiaiaeq ynlitelglw vieqacvqac tfknvqppia
      481 vsvnvsviql qdpdfvtkvv niveqygvkp enlhleites vfaedkltfl aavkelqkqg
      541 fcisiddfgt gysslssmld igvdivkidk sfiqnmdkrg lsiihaivqm astldfivva
      601 egvetleqan mlkeigvshl qgyyfskpme qhfvdsylke qnklcs
//
LOCUS       WP_273605754             139 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Pseudoalteromonas sp. Angola-30].
ACCESSION   WP_273605754
VERSION     WP_273605754.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 139)
  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 139)
  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 139)
  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 139)
  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..139
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..139
                     /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=15961
     Region          58..133
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mleivatedl ktaaqftfnn mkpyyemyav dwdvedvyqa tknlknfdim ckgqligvvr
       61 lsfdegrcql rdiqiaatyq nkgfgahvia kvvdmarqqg vkfidlkvfq lspafklysr
      121 igfavdredd rfyymslqa
//
LOCUS       WP_273606031            1011 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Pseudoalteromonas
            sp. Angola-30].
ACCESSION   WP_273606031
VERSION     WP_273606031.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1011
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..>1011
                     /product="beta strand repeat-containing protein"
     Region          <153..1011
                     /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 meniskavvi vellsdvwvv mdngdwvkvd sipeqfadlp vlnssdiale gnelvfseas
       61 eqlvvpqdii sqlvsdlsqn stfdarsnts svtslsssda neaqvayqli arqgqelvpe
      121 sgyettptet teeedpnfie frpdpiftvg qlggdgvfin kydavalefs gtvenvpdgs
      181 lvqivlsdsd gneiivttev qdgvwsvtni ditalndgev tatvslvggn eddaasetkv
      241 kdtqadifid fedglntnqp iefegevqdv qdgqlvtvti fdaqgnpiat yeatvtngqw
      301 svgpepfadl pdgnytiqvs tideagndtq tqksfskdtt aiitidvnet edgvinnsen
      361 vvqvsgtveg iedgqtvlvt ltdidgnevs veavvengqy qlevdissls dgeitataqa
      421 qdllgnesta sqvishdkta qltveidstq dgvinseees nvtvrgvvtg iedgqtvtvv
      481 lsdgvnppit ltaivvngsy eiagvdissl ndgtisanat aqdisgnpas asdeaqydss
      541 vatsivaqdi dgvinsaeqn nvqlsgsvtd iepgqlvtvt ftdsnnqqvv vtaevdadgn
      601 wqisgdiesl adgeisaqis ifdaagneat qevtfskdtq stltlnidkt edgvingsae
      661 ntdislsgiv ngvedgqevt iiftdslgne vvvtaiveng nyalsgvdis alndgdisvs
      721 asvldtagnt avaddsfeid nsalitasid ktddgvingq dddlrdnvnt aenagvvvrg
      781 tvedvedgqi vtvtlsdgin ppvitqavvq ngqyvtepmd atglndgtmv ataevtdaag
      841 npvsaqdnve idttaaitts idktadsvin gsnenqeivv rgtvsgiedg qvvtitlrdg
      901 vnpdiavqai vqngeyvtap idasslndgd ivaradvsdl agneatardt veidkladit
      961 tnidktadgv ingsgesaai vvrgtvedve dgqivtvtis dgvnpavttt a
//
LOCUS       WP_273606032             256 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-30].
ACCESSION   WP_273606032
VERSION     WP_273606032.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 256)
  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..256
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..256
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29117
     Region          27..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 mfvrvvlsic vfmlysamcn aqtitfvaed lppyhfinen nepdgalvdl akatikhtkl
       61 sakfeiipma riftmlennp naialsllkt pirarqytwl gesyfadayl vslknrtdev
      121 thlnhakfyq vatirgyssa tylknagfte dknlvlvsyy qqlwqmlykk ridfvltntl
      181 tlnnelkrsg lnpnlitkri hltdypskly fsanktldkh tasaishaln tlkengeyqa
      241 ilnkwqlplp atankl
//
LOCUS       WP_273606042             484 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273606042
VERSION     WP_273606042.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 484)
  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 484)
  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 484)
  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 484)
  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 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   6  (residues 1 to 484)
  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..484
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..484
                     /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=54505
     Region          <133..>331
                     /region_name="MCP_signal"
                     /note="Methyl-accepting chemotaxis protein (MCP),
                     signaling domain; cl46910"
                     /db_xref="CDD:481250"
     Region          242..481
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpvtlakkyr amlnwrpnli gqfiismlls llplslvviv flnalnkqla vtqlivsnny
       61 qvtksfnflk qelnslerat rqnwvlkses ldtlinekwq sslqtidtls qasatqqytm
      121 qwrrlattlr sthqalienn qqdaalfvpi sdlvaeltvw lrdtnaaqiq nnqselstlq
      181 ssfinwlval ipltllvggg flwriskrlk gltsvidklg qghwqqkiav qgsselvelg
      241 eklqwvqeql hmleqqkdtf lrhvthelkt plasmvegtd llsdeivgpi tkeqqavlel
      301 isqsmvrlrt midsllsyna irtskdsvse vefgnlinki nshfehrlta kqqrlnwhns
      361 itkqplalpa eliemtliql isnalkfsnt gqsvdvtlav eqkllimqvr degcgikeqe
      421 ktqifsafyq gkhnkdvtlq gsglgltivk esveqlqgql svehnqpqgc lftikipltn
      481 qgvl
//
LOCUS       WP_273606128             635 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudoalteromonas sp. Angola-30].
ACCESSION   WP_273606128
VERSION     WP_273606128.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 635)
  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 635)
  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 635)
  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 635)
  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..635
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..635
                     /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=71587
     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 mnkfkplsgi ffvfilfcfc lnieltnqin rinlfnpdid lrhfdivdtt lemapwynpm
       61 lnghylihqp sadfllvktt dtefiaanat klilmtltsp infilvcmvl fvgftiirke
      121 rkkisyqhqi aqlnnnanql lvafnlqpqh dnpsglgnls qsinnlnthv anylkqtqts
      181 icqdkltlli drhayiehid rqinftdeeq lkcallfidl dgfkqvndsf ghsfgdeilv
      241 qvatrlanvl rhhklsnine anqleqnlsr lggdefsifi esvdtdnkvv diakhvlsel
      301 ekdfvlgnki ikisasigia aypesastpq allqladvam yraksdgkgi fkvyspemgn
      361 kmrryhylle elrlavackd fylsfqpivh vedcmidyfe altrwehpie gmispaefip
      421 iaeesnlile lgdwimhesc rqmaawhnag mrkvkisvnv sgvqlkhrsv ydwimknlkn
      481 tglpshslml eitestfika sksmieeler lraegvtiai ddfgtgfssl stladlpidv
      541 ikidrsfisq adkspkyndi lntiselgqk lglkivaegv eeieqfelvk rigvssvqgy
      601 lvsrpqssin vgnkvlrknt anlsaagtsa weies
//
LOCUS       WP_273606177             613 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF885 domain-containing protein [Pseudoalteromonas sp. Angola-30].
ACCESSION   WP_273606177
VERSION     WP_273606177.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..613
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..613
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=68619
     Region          1..611
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mksiklalva sgvmfalsgc mntqtsnntg nsaqlntsna paaivselsy eqqldvlvaq
       61 yynellsfkp inatysgrse fndkftpait qknrakkaaf ykkyqqrltl idkaqttgqa
      121 llsyeilqrd lalnlegmqf psymlpinqm agahntfagf gsgqsaqpfn tvedynhfik
      181 rsegfitwls sveramakgi kagitlpkpl akklqpqfaa hvvknaedsl fwgpiknlpa
      241 sftaqqkqqi taqykalimq qlvpayksms dflanqyipq sretvgysdl pngkawyeyq
      301 ikknttlsls adeiheigls evsrilsqmk kvkhevgfng tldeffqhlr dsdqfyydtp
      361 ealiaayedi kqkidarvpl lfdvapkapy vvkavepyra qsaagasyaa papdgsrpgi
      421 fyintynlka qpkflletls iheaapghhf qialqqeidg lpdfrkfggy tvfaegwaly
      481 aeslgkelgl ftdpymwygr ladeqlramr lvldtgfhak gwtrqqgidy mlanssmaks
      541 dviaeveryi awpgqalsyk lgqfkiqqlr dyskkelgdk fdikafhtqi lidgalpmpi
      601 leekikrwva ask
//
LOCUS       WP_273606175             805 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Pseudoalteromonas sp. Angola-30].
ACCESSION   WP_273606175
VERSION     WP_273606175.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 805)
  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 805)
  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 805)
  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 805)
  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..805
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..805
                     /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=89455
     Region          50..804
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mkkfkyslvt laclnaslav aattaekdie risvyekqnq vvmssglatk sdmslmetpa
       61 pvviidreli esqgvdslqe lvrnvsgltq agnnygigdn lvirgldany tydgmyggag
      121 lgntfnptrs ltnvesvevl kgpatglygi gsaggvinli ekkpefeekh kisaelgqwd
      181 syslafdstn aitddlayrv maktassdgf rdlkedrdei ytslkyilsd kqdimlsaay
      241 ikdsiavdsi ghpiriynae tangltagev tgadlvndps gngvqltaaq qtqlaqslss
      301 tdgltpydfg tngiispmad dnegeelrfk lthnyfitdd lflnqqlqyr nytssfarqt
      361 gafnyvystr dgiinndpra plvedgvlyp faarrqeyrq veadekswqy fldlrydfml
      421 gdvdnellvn anyedrdirf kqysiydadk viydsegnvl yqgtlpyiyd mrspnwptgs
      481 fddydplkts dynkkvqawg lgiqhvgyit eqlttrvgva ynrikqtyeh hgvderysss
      541 raeptpeant sdsgltynlg atyqptenfs vfinhakgrt afsvlgsvag teadredses
      601 isndlgfrfk afddqllasl vvfesartnl eysnplyeag vsgpdvvesy ydgeeqtkgv
      661 eldlnahlne qwkvnvngvy qdardksnpn sssydtrqkg vpyvtastwv tyyadmfnlp
      721 eavnisggit fvdnrstnss sfsipdgyvp sytvydaavs yttdkwhmql nlnnlfnkky
      781 yskamflggm pgeernakls fsytl
//
LOCUS       WP_273606097              66 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Pseudoalteromonas sp.
            Angola-30].
ACCESSION   WP_273606097
VERSION     WP_273606097.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     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=7560
     Region          1..57
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mnnkilrfqe vtdltglsrs tiwrkerlgl fpkrkqlgln svgwlesdiq rwveklpcsn
       61 iykgaa
//
LOCUS       WP_273606533             589 aa            linear   BCT 28-DEC-2024
DEFINITION  alkaline phosphatase D family protein [Pseudoalteromonas sp.
            Angola-30].
ACCESSION   WP_273606533
VERSION     WP_273606533.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 589)
  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 589)
  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..589
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..589
                     /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=64539
     Region          3..569
                     /region_name="PhoD"
                     /note="Phosphodiesterase/alkaline phosphatase D [Inorganic
                     ion transport and metabolism]; COG3540"
                     /db_xref="CDD:442761"
ORIGIN      
        1 maftrrsflk asaagfgaav lslgltgcrf dddddtpvsf dhgvasgdpl sdsliiwtrv
       61 tpldvttksl kvqwqaatdq sftnivhdge thisdttdft lkvdlqglda ntvyyyrfna
      121 hgktspigqg ktlpvgavdq vklavvscan ypagyfhvys eiakqsdlda vlhlgdyiye
      181 ysntgyated aeqlerllpl dnsseiialt dyrkryanyr ldadlqaahs hcafitvwdd
      241 heitndtwre gaenhnegeg efsqrklnal qayfewmpir nvadkeriyr rfefgnlvsl
      301 ymldtrvlar deqlnysdfd ltspagqsaf aaaigatdra llgseqltwl sdaittsstq
      361 wqvlgqqvlm tkmhlpvevm lllaslqsaq anggdpsell aqanvlfael aqikgrvlag
      421 dpsvteaela rvqttipynl dawdgyayer evllgtavaa qknlvvlagd thngwagqlk
      481 tdasnpiaas qnagvefata svsspgleey lalntqdaqt vaqieqvial lvddlaynnl
      541 vergyltvtf tpakasakwn yistikarey qvvesrtkel smlagqaql
//
LOCUS       WP_273606738             434 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter substrate-binding protein [Pseudoalteromonas sp.
            Angola-30].
ACCESSION   WP_273606738
VERSION     WP_273606738.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 434)
  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 434)
  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 434)
  AUTHORS   ter Beek,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..434
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..434
                     /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=47812
     Region          22..420
                     /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(131,133,259,261,296..298,339)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:270303"
ORIGIN      
        1 mktkllmlac svmainvaak etitiatvnn gdmitmkels nhfeeqnpdi slkwvtleen
       61 ilrqrvttdv atkggqydvm tigtyevpiw gkqnwlteld nlgenydvdd llpairsglt
      121 idnklyaapf ygessmvmyr tdlmekagle mpnaptwsfi qksakamtnk degvyglclr
      181 gkagwgenva litsmansfg arwfdenwkp qfntpewkat lqyyvdvmke sgpagssang
      241 fnenlalfqt gkcgiwidat vagafvtnkk dsevadkvgf alapdiglgk rgnwlwswtl
      301 aipssskksd aamkfiswat skeysqlvad nkgwakvppg traslyeneq ymnaapfaqi
      361 tldsinsadp knptvkpvpy vgiqfvaipe fqgigtavgq qfsaaltgqm tveqalntsq
      421 rlvertmrka rypk
//
LOCUS       WP_273606969             370 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Pseudoalteromonas sp. Angola-30].
ACCESSION   WP_273606969
VERSION     WP_273606969.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 370)
  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..370
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..370
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=41683
     Region          6..364
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mrfngswrki arrvhlylgl siggvlalia ltgsilvyyp eldenissls tetarpinwd
       61 tayqtlkthy pdkqgswrle stkdkhyipa ryynqnetvd hafaplmvwl spdgrlilre
      121 dvwgnyfvtw iynvhfslla gstgtivigy igigslilli sglcawwpkk gqwakslkfk
      181 arssflglly dwhkllglif alplilltat gimlaipkqt dplitallgn idkpnsaiik
      241 pqrsislsaa lstaqeampn trlawvetps nhnavyrfrf ktksdpsyrf phsyvqvnas
      301 tgelisvfni dkmsiaskfk nwlhplhngs igdqplrilw vlsgvatall falglfrwli
      361 ktkrfkytis
//
LOCUS       WP_273606927             639 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Pseudoalteromonas sp.
            Angola-30].
ACCESSION   WP_273606927
VERSION     WP_273606927.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..639
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         1..639
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=70871
     Region          1..>26
                     /region_name="DUF333"
                     /note="Domain of unknown function (DUF333); cl46806"
                     /db_xref="CDD:481146"
     Region          65..218
                     /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          115..>341
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          386..639
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mkktlkfgvl acaialagcs qssntthvia eqtsaaqaiq tysantffdt tsfigssfsp
       61 sgekilvssd esgiyslyev dvrtgskerl tnfedstypv ryfpndervl ftkdsggner
      121 yhvyvrevdg sikdltpgae tragfagftk dgsqffitsn qrdakfmdly rvdsetyems
      181 pvyqnelgld vgaispdgrf ialsknntnk dsdtyildty krslkpqlis khddpaqytp
      241 etfstdgkyl yystdakgef sqvwryelat ekhspalede wdvnfiyfsk sgryqvsgvn
      301 adastkvtil dtrtgkqvam ptlpngnlrs vnfssdektm afylnsdtsp snlfvwqvgg
      361 isakqltnsl skeinqsnlv qstivrfksf dglevpgvly kpkqasstnk vpaliwvhgg
      421 pggqsrtgys atqqhlinhg yaifavnnrg ssgygktffh lddkkhgtdd lqdivygkkh
      481 lqsldwvdse kigimggsyg gfmtaaalaf epeefkvgin ifgvtnwvrt lnsippwwes
      541 fkkalydemg dpatdgerhr aisplfhakn itkplmviqg andprvlqve sdelvaavka
      601 ndvpveyvlf ddeghgftkk enritasnay lkfldtylk
//
LOCUS       WP_273606998             884 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Pseudoalteromonas
            sp. Angola-30].
ACCESSION   WP_273606998
VERSION     WP_273606998.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-30
  ORGANISM  Pseudoalteromonas sp. Angola-30
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..884
                     /organism="Pseudoalteromonas sp. Angola-30"
                     /db_xref="taxon:3025341"
     Protein         <1..>884
                     /product="beta strand repeat-containing protein"
     Region          <37..878
                     /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 qtvtvtisdg vnppvevqai vqngeyvttp idasslndgt ltttatasdl agnpvsaqds
       61 veldntaait tsidktadgv ingngesaai vvrgtvsdve dgqtvtvtis dgvnpsievq
      121 aivqngeyvt dlidasalnd gtltatssvs diagnpanaq dtveldntas idlslldsdq
      181 vinsseqgnv vltgttidve qgqqvtltlt dssnvskvit vsvsedgtwe vttdqiadla
      241 egqinaavsv tdsagnpans altftkdtqs svtlniaqtd dgvingsten sqititgdve
      301 niengqaisv ivsdgvnpdl elngtvidgq ysfenvdiss lnngtitata tvsdlagnia
      361 sandsvildq lasvtvaind tadnvingnd entavsitgn vaniengqiv tvivsdanns
      421 etftaevidg aytitnadls alndgtltat asvtdiagnt atssdtaehd klasttvava
      481 tsdevvnaae qssvvisgtv tdveatrevt itfsdginlv tttvdvdsdg nwqinpsdis
      541 aladgeievs vsvfdnagne avnstaftkd tkatttldla ddvinaaede vvaisgtvtd
      601 vettsnvtvt ftdqngntev ienipldsng nwsilaadis aladgeitas vsvfdnagne
      661 avnsalftkd tqattsfeln dtlinaaede tvalsgkvdd vestnqvtvt ftdsnsnvvt
      721 ienieldneg nwqvaaadis eladgevtas vsvfdnagne alnsatlvkd tqatisvnvg
      781 ddafinaqeq atakaagtis gveagqdvdv vlrdsngdel lsatvtideq gnweldspil
      841 rflsdgdytv dvttqdiagn eatssldftk dtqasttlvl edsv
//
LOCUS       WP_273607985             241 aa            linear   ENV 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [uncultured Pseudoalteromonas
            sp.].
ACCESSION   WP_273607985
VERSION     WP_273607985.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Pseudoalteromonas sp.
  ORGANISM  uncultured Pseudoalteromonas sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas;
            environmental samples.
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: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="uncultured Pseudoalteromonas sp."
                     /db_xref="taxon:114053"
                     /environmental_sample
     Protein         1..241
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27125
     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 mrllllcfis cffisppvsa awqkqpivia asatippyvi ektdtgiqln iikaalieqg
       61 ldnivviyms nkraeqqlhs gnvdillnya gkrgagiyps qpvlsyknva vslkkrnfti
      121 etikelnnks vlgfqhatay lpppfakgva qfasyeevvn qraqvdrlmk dwvdviilde
      181 rifhyynndy thslpvnihp ifpkaprpay fnnavlqktf dkglltikak gkyqqimsdy
      241 h
//
LOCUS       WP_273608274              93 aa            linear   BCT 28-DEC-2024
DEFINITION  RNA-guided endonuclease InsQ/TnpB family protein, partial
            [Clostridioides difficile].
ACCESSION   WP_273608274
VERSION     WP_273608274.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 93)
  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 93)
  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 93)
  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..93
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         <1..>93
                     /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..>93
                     /region_name="InsQ"
                     /note="Transposase [Mobilome: prophages, transposons];
                     COG0675"
                     /db_xref="CDD:440439"
ORIGIN      
        1 fcisscgefi enpkylkksl nklaklqrel srktigslnr nktrlkvarl qehianqrkd
       61 flqklstkli kendiicied lqvknmiknh kls
//
LOCUS       WP_273609242             246 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609242
VERSION     WP_273609242.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 246)
  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..246
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..246
                     /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=26584
     Region          1..>68
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mnindetlsa fldselsehe meqvrkalet ddelvmrlae lsevdmrvke hatsiddapl
       61 sdslaktvak ldtattkntl nsnvvtltpw qrvkqsanks laiaasvavv fgiamtsylq
      121 pnesqnivas niasaldtql ssgeykqsdg svfsaqlsfk nqqgelcrqy alssnntmqt
      181 siacktqsgw qikaqtaaqq sdngaqyraa snnseldavi dsmisgapld raqeqqaisa
      241 kwqlnq
//
LOCUS       WP_273609272             634 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609272
VERSION     WP_273609272.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 634)
  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 634)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   3  (residues 1 to 634)
  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 634)
  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 634)
  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..634
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..634
                     /product="vWA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=70085
     Region          <91..266
                     /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          <352..>441
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          369..394
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(370,373..374,377..378,380,399,402..403,406..407,
                     409..410,433,436..437,440..441)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          397..427
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <481..>552
                     /region_name="CobT2"
                     /note="Cobalamin biosynthesis cobaltochelatase CobT
                     subunit [Coenzyme transport and metabolism]; COG4547"
                     /db_xref="CDD:443611"
ORIGIN      
        1 mdftfirpav lwllipalal ffiafikhkk qsadnliaph lapfimnesn tkasqplwlv
       61 avfcclaiif sagpsfeekq vpvfqsksar vivmdmsysm ystdiapnrl mqsrfkaldm
      121 ielfkegdta lvayagsaft ispltndatt ltnlipslsp dimpdkgsnv lagldmakel
      181 ltqagyidgd iilvtdgidq eeqsditsft snssyrlniy gvgteqgapi klpeggflkd
      241 sygqivipti nisrlkslat rsggkfalyq psssdiatfa psansellkd ekqshalwri
      301 dagiygllil lplglylfrs atfvgaflvl svlptqqasa lelpsflknt dqqaldaykn
      361 kdferaanad ssslkgsaly qqgnfdaale afskdksatg fynyantlak sgqleqaida
      421 ykqaqmlqpn fseaadnqal veqlleqqqq qqqegdsqdn qqqsdqseqq nnqqsdqnqq
      481 gensdsqseq sqgeqsqdqq gepsdesdte qdqqsaesgs qsdkqnepel qtqpqanqeq
      541 kqpeqtneeq aentqpqtaq qqtltdeqkq naqqqaaqaq treltneeke kaqqlnqllr
      601 kvpddpaill rnkmqleaqk rqyqrrptgv eksw
//
LOCUS       WP_273609298             709 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609298
VERSION     WP_273609298.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 709)
  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 709)
  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 709)
  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 709)
  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..709
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..709
                     /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=78078
     Region          54..659
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mahiqhiqhs ylfsplalll tgllspavfa ddntleiiev hgqvhnkhls lgsseamlsn
       61 lgvdfsaagg vsnlpilngl mgdrvkvlvd gaevtaacan qmnpplsyvs anqvtaynvv
      121 agvspvsagg dniagvisvn sispqysess elawhsgyvs akyssvdsgr klgvgarlas
      181 dtvslnyqgs fsdansykdg kgnvvldtly raqnhsltga irddkqqvvi klthqkipyq
      241 gfanqymdmt dntsygaiaq ykrsfensel qgqvnwhsvk hemgffskek tgmmpmktda
      301 kdistqlkwr ltldqnssll lgqeyynyri ddwwpaiegs tmmgpndyin inngkreria
      361 lfaeyesqin nklwlntgir vervntqvde vqayndgmmn tgsmstmtta nnalaannfn
      421 nadrdktdtl vdvnvlanyq ftlydelqlg larknrapnl yeryswgvsn mastmigwyg
      481 dangyignpe ldvetantis atysktaknd awrvsanvwy tditdyidad ivrsfnsygl
      541 anttrnilsf tnvdatlyga kldiskalyq stqfgewqlk anitstrgkr rdtnqplyqi
      601 kplhtalsls qqigifenal lwqwvdtksr vdvnrlenqt vsyslvniss kasfdaltlg
      661 ievvnlfdtf yqlplggvsi aalkqgtstg ftqlagqgrs fnisasyaf
//
LOCUS       WP_273609434             424 aa            linear   BCT 28-DEC-2024
DEFINITION  purine-cytosine permease family protein [Pseudoalteromonas sp.
            Angola-7].
ACCESSION   WP_273609434
VERSION     WP_273609434.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..424
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..424
                     /product="purine-cytosine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44902
     Region          18..420
                     /region_name="CodB"
                     /note="Purine-cytosine permease or related protein
                     [Nucleotide transport and metabolism]; COG1457"
                     /db_xref="CDD:441066"
ORIGIN      
        1 mpngndphti nsnelvawpr iaaiaamlsf slptfitgle ihqsssvsnt lwalvigsli
       61 ltliggamgt igvksrlssy llvkiafgna gagivniafa lsligwfgvn idlfsnavvr
      121 llsaefniim pewpidivag camlittlyg fkainvlasi mipilaavta mmlfgaldsm
      181 plvdfinlek saalsledgv aaivggviig aiilpditrf skqkrggvyt sfiaymviel
      241 lvifvavfaa aamqeteils lmlalnlgfs affiviagsw ilnslnlyst alsveatfph
      301 whkkwvimll glvgigaafi nildmfisfl aflsdifvpv agviivdalf ikphaynaaa
      361 lannanfslp afsawfvgaa yavcngtlfn vsmsgitvid aiiltaviyt lfakaiapkp
      421 vvqq
//
LOCUS       WP_273609461            1011 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609461
VERSION     WP_273609461.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1011)
  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 1011)
  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 1011)
  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 1011)
  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..1011
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..1011
                     /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=109350
     Region          185..948
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mhikqmlgev aslnviskkk fkkkiknyrg ilfvsclykl rsnqthlfrg lsvlvpaifs
       61 lsvqgatqtt gqmvqfdiqa qradkalief akqteqtvvf syelaknyqa nsvygfytql
      121 dalqallsgt eldavvdqng llsiklkqin rkdnnmmkls gvsaavlpal laanshgvna
      181 aedvaqekie kiaivgsrva grsvedlpvp vdilsaeale ntgqtevgrm lqsiapsfnf
      241 ssssisdgtd alrpatlrgl gpdqtlvlin gkrrhqasii hintsvgrgt agtdmnaipa
      301 saikrievlr dgaaaqygsd aiagvinivl kdgseggkaa vnygqysegd getvnvdfnk
      361 gfalgdsgyl natlnyrdrs ptnraglhgs cqfygctels dgtllagdpr eltadrdtfr
      421 igdadsqqfg ltvnagyelg dgelygfity strdnesaaf frhnanaggn pvlqdndati
      481 plgflpkint tiddisynfg yktdfdndas ldvsytygen sidyttsdti nasyanflry
      541 eqglsaadir stipreayay gmelslqtin idftqnfddy slamgaeirt deyrilegse
      601 yayrdydtld gvsiysglsg gvgsedasgg tqgfggsspa ssvdesrdvi sfyldaetyl
      661 iedvilsgal rydnykgfgd tvnfklagnw aitddvslrg alssgfraps mqqlyfnnis
      721 tqfvvaedgs lvaeevgtfr ndstlaqslg ipklkeeksq nrslgivynv tdninvtvdy
      781 ysididdriv isnrlgkgls ssldaaliss gagagqffln gadtetsgid fvatwntegl
      841 ggtldftlaa nftetevvsl ftpsgsglet vpvedvfsdq eisiieewqp edrinlsaly
      901 qrgdwtvnls lnrfgeytve dggrqtygae iltdvkvnyf vtedlsvnig annlfdvypd
      961 kntignsrsg tivdsngnti vssdgvfeys rrsapfgfng ayyyvgaeyr f
//
LOCUS       WP_273609475             347 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609475
VERSION     WP_273609475.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     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=39885
     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 mkllilqflr gwaaiivvay hahgviikrh velgaehsfw ftenqfvkig aigvdiffil
       61 sgfiifytsr nsfdvilylk kravriypiw fiailfmtvl allpgssavf dlehifyssl
      121 liphiydgai vpflkvgwtl nyeiifyllf aptlyfsssk rleiitvmiv clsiishfls
      181 enigvirllq npilfeflig gwlaklyltg fniskklmyl vstfgllwlg lyfftpyiwe
      241 ynslisrapi alsifivsif ytpirnikik ksfvylgdas ysiylfhmfp imilsgvlgr
      301 nlipqvvmlp tflvwliita gsvlfgciiy niiekkinir lkeyvsk
//
LOCUS       WP_273609486             737 aa            linear   BCT 28-DEC-2024
DEFINITION  GumC family protein [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609486
VERSION     WP_273609486.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 737)
  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 737)
  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 737)
  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..737
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..737
                     /product="GumC family protein"
                     /EC_number="2.7.10.-"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=82952
     Region          1..729
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
ORIGIN      
        1 mnqvnkesik indeevidlt syfkvvskak wrilffsvvv tlltimftlt lipqykstat
       61 llieseqtka vsfeeiygld ttkkeyyltq fevlksdsig kevitklnle nhpdfipkqs
      121 lmgevksylk tllpflnnke shqlspeeqa eqkmlfllsi yksrlsiepi sntqlvrisy
      181 essdpklsam vantvgdvyi esqmrakmgi tqqasswlnt rlsqlriqld dsearlqafr
      241 eaqqlvdieg iaglatqele qisqqlvvar neknnlqsin rvinefgdyd idtlgsmpei
      301 tnhsviqdak rdviaverkl selsevygpk hpniisakae lltvktnlnk qvaglitgie
      361 kelrratrta ntlendvkki raeyqditrk eteynqlkre vetnrnifnt flsrsketev
      421 tsdfssaaar ftdrafasmt pskpnkkliv tlvffislvf gvvmsfifdi lndtvknkvd
      481 veykiaqrml glipqvalpr ksvlpihayl ddtyrrfaes vrtfrtslll tqldkahkii
      541 avtstspgeg ktttasnlai slaqmgkvll idgdlrkpsi akrfeipvyh pgltnlitgt
      601 eqfsecvhid gqsgvaimps gqipgnplel lsnsryvell eilktkydyi iidtpptqav
      661 sdalvisqsa dsviyvvksd vtrikpikag lerlfeskah vagvvlnqvd msksadehsy
      721 gyydyhdysq kpeqpkv
//
LOCUS       WP_273609213             482 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609213
VERSION     WP_273609213.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     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=53253
     Region          <138..257
                     /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          276..444
                     /region_name="DUF3526"
                     /note="Domain of unknown function (DUF3526); pfam12040"
                     /db_xref="CDD:432281"
ORIGIN      
        1 msknnfskmv ivakdewryw lrsklamtvl aigllltlss vvvtaitmhe lshtrnelqs
       61 naeqsfaeqp drhphrmvhy ghyafrtptp lstldpgida ytgnsifleg hrqnsamfae
      121 qrqgtaltkl gsltpafivq tlaplllili gyssisrere sqtlsyllaq gtkgstliag
      181 kglallcvvg liiaplavsa lftlgagesl lavvsfivgy alylsvwvlv vllassvfsk
      241 nsgsftalaf vwillcivmp rvastsasta vpsagkietd favkaelrkl gdghntndpa
      301 fkqfkqsllk kynvnsidel pvnfrglvas eseakqtkvl nqfaeqrmqs elkqtqvsry
      361 fgwvspmvai rslsmivvdt siethhrflr eteqlrfdfv qglnkvhiek ldyqvdmnrn
      421 anteatkkar vgsenwqilq nftfdvdsad vraqrsvsaf lqlilwivvl vagiklvgkr
      481 li
//
LOCUS       WP_273609622             512 aa            linear   BCT 28-DEC-2024
DEFINITION  pyridoxal phosphate-dependent decarboxylase family protein
            [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609622
VERSION     WP_273609622.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     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=56228
     Region          34..504
                     /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 msqlqsaqls pvenkaifeq nglppqfnld qfinyqiasl qglsavqqam akaqkpfsgv
       61 avntlaatvn dvdlakplad fpavlnelks vyldhavyfh hprymahlnc pvtypavvae
      121 hiigaintsv dtwdqsagat lieqklidws cekaklpsta dgvftsggtq snlmamlvar
      181 evavsryapn hevklqglpe vasrfriycs evahfsiqka aallglgyna vvpvatnnkm
      241 qmdmdalnha iadskakgdl piavvitagt tdfgsidpve diatlakkeq lwchvdgayg
      301 ggllvsehhr salngieqvd sitidyhksf mqpvscsafl lsdkrhfshi tlyadylnpl
      361 aeagngtpnl vdkslqttrr fdalklwltl rtmgeaplgr afdkviglar qthivlndhp
      421 dfevinypel salvfrfape elkhnpdlld tlnlhvrqtf lntgeamiar tkingrhylk
      481 ftllnaqcql sdvravleqi stiawqtyke qk
//
LOCUS       WP_273609717             379 aa            linear   BCT 28-DEC-2024
DEFINITION  murein hydrolase activator EnvC family protein [Pseudoalteromonas
            sp. Angola-7].
ACCESSION   WP_273609717
VERSION     WP_273609717.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 379)
  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 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 11471818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..379
                     /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=42553
     Region          13..378
                     /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 mskpvnwfsv ytfvlvslvv apatanesrt kkdlsevqsa leqsqaeyna qrkkiaalqk
       61 nlkkheleia knakalnmae qsvketeqkq qtqqhkaqql kaqhtqfqai laaqlksaym
      121 aggddypkml lnqqdtakfe rtlsyynyln karieqieel kvlqqqiaen qaalaktkqk
      181 laalfeeqkr rqsalvnaqs erqtnlknlq aqlnstkssi nylkdneqtl ittieeleqe
      241 ktqkiellgl nkskgklnwp skgklkhtfg qrkhggidwk gvligakegt nvnsinngqv
      301 vfadwlkgfg wvivvdhgeg fmslyghaqt llkdvgdmvr egetlalvgq sggqsssgly
      361 feirhkgrav npvkwcrri
//
LOCUS       WP_273609627             221 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609627
VERSION     WP_273609627.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..221
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..221
                     /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=25568
     Region          100..208
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 mnetydyglw smvilnsaif iffafsfvkp ktstdwrsls afsafivalf temygfplti
       61 yflsgwltet ypevnffahe nghllhtffg fqgdahwdpf hiasmvfiva gffmlssawn
      121 vlhhaqkhhq lattgwyarc rhpqyvafil imfgfllqwp tiltlamfpi lvvvyvklak
      181 reetqaiaef gseyhsymes tpswipnfnk niegknhenv n
//
LOCUS       WP_273609832             468 aa            linear   BCT 28-DEC-2024
DEFINITION  protein adenylyltransferase SelO [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609832
VERSION     WP_273609832.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 468)
  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..468
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..468
                     /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=51763
     Region          1..468
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
ORIGIN      
        1 mklvprytdi adnfaiedsp ssvaapqlll wnealaqqfn idvepalras tfagnepqpv
       61 navalgysgh qfghfsprlg dgrahllgai sddknqlwdi qlkgsgatpf srggdgrcal
      121 gpaireyims eamhglgikt trclavvgtg eavyrnppqp gaivtrlass hirvgsfqyl
      181 atqgdveglk kladvaierh ypsiqstgaq ryldfleavi nsqlalvisw mrvgfihgvm
      241 ntdntlisge tidygpcamm ntfdfdtvfs sidkqgryay gnqpnivswn carlaeslip
      301 lideddeqav slmtplinqf stlfnaqynq mwaqklglag ykeddvelvs kllllfqehk
      361 ldytntfdal tesleggkvp deltqwaqlw qkrcdensyn lmraanprvi prnhiveeil
      421 aqynqhgese llsdflmvms npydktanla rfqetgkddk gyqtfcgt
//
LOCUS       WP_273609872             245 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-7].
ACCESSION   WP_273609872
VERSION     WP_273609872.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..245
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27903
     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 mnklitlllc vlfstswgvf acertlsvga hdafwppyvm gisgqlqgke vdaltiifkd
       61 spfcfeikml pnskraftel rhgridigwa asytseraky ahytkayrte vmrlyenkkn
      121 qhtvknladi fnqgltigan fgsyygeefe qykkshkkqi eytsatskrf emlnkqridy
      181 aiedelvgny lskrgnslmk aptipainkd qihlmlskrt vtpdevkiin ahiaknkaal
      241 kalfe
//
LOCUS       WP_273609925             381 aa            linear   BCT 28-DEC-2024
DEFINITION  tetratricopeptide repeat protein [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609925
VERSION     WP_273609925.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 381)
  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 381)
  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..381
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..381
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=43114
     Region          196..224
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(197,200..201,204..205,207,231,234..235,238..239,
                     241..242,265,268..269,272..273,276)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          202..>380
                     /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          229..259
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          297..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(298,301..302,305..306,308,332,335..336,339..340,
                     342..343,366,369..370,373..374)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          330..360
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkylvftlsl lltacsstpp eapikkvqlt hiinhslfeq vktpsehsif elsepeksaf
       61 ltyahsrlnn vradeiifny lqnqltnfky dgatltaqqs iersegncis lailtqsyaq
      121 llnletsfqe mtsepvyake gnviyvanhf rtkiyapkke tdediiviir agtlidyfpt
      181 rgsfysgsat yndllsnfys nlaatalaen nlnkayslim qanrftpnda elfniagvlh
      241 rragdlksah miyqtaldrn disinlinny rilakelgdk tlekrltsql vdkekdpyel
      301 lviaknnlhq gkvtqakkql elaiakapyi selylelaki ryqqgntaqt qsllekaiqy
      361 ernkerlnvy qaklaslnkh n
//
LOCUS       WP_273609926             377 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609926
VERSION     WP_273609926.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..377
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=43301
     Region          1..371
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mrktlfkihs wvalialipl lvisitgsvl vfkseidgll mpdshfvvqq qanrlpidtl
       61 itktqktype yvvgsweifn ddtadrvyli krgtedwykf hldqytgnil sepvgtshyf
      121 tdwfldlhyt fllndlkslp gqtgtvlgff favfflvlgi tgliiyrkfw qrlfsvrwra
      181 tlqivlsdih kmtgvigspi iiilaitggy fngavwyhev vehaeeehfv ltknlyneei
      241 sfqhvlddsq kqiptfngtf lvmplepden itlfgevdts nplaseyant vtynkltgeh
      301 manwdirevg vgwqvidsfr klhfgyfagl iskiiwcvig lspvwlggtg fylwftrrkr
      361 kkqsqknrls khrtvsa
//
LOCUS       WP_273609779             306 aa            linear   BCT 28-DEC-2024
DEFINITION  2-hydroxyacid dehydrogenase [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609779
VERSION     WP_273609779.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     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=34078
     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 msvlvaisgr dntkliarlt elllnetieq wpscknpsav efvlawnapn dlwqrlpnlk
       61 avssfgagvd sinmsllheh vdvvrivdeq laedmaeyvl thvlaqklrl keyfvkqsqs
      121 nwkpkrayky khvgilgfge lgkacadklr ingftlsaws ktpkkseqvk lytelqglde
      181 mlpkidflvc llplteatkg iinaqllakl pkhacvinva rgehviepdl lsaldsdnlr
      241 satldvftee plpgshpfwq hpkvtitphc aaisdlnsvt eqiaenvnrl nsglelnnrv
      301 nrtkgy
//
LOCUS       WP_273609938             592 aa            linear   BCT 28-DEC-2024
DEFINITION  DUF885 domain-containing protein [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609938
VERSION     WP_273609938.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..592
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..592
                     /product="DUF885 domain-containing protein"
                     /calculated_mol_wt=67603
     Region          11..586
                     /region_name="COG4805"
                     /note="Uncharacterized conserved protein, DUF885 family
                     [Function unknown]"
                     /db_xref="CDD:443833"
ORIGIN      
        1 mnyslppric rtllvlslfg tlsactltsp nantqfeqva qsivdyrkrv npytqpegvd
       61 gyllpnlsae flkqqyeekt allsrldaid sdelssensi nlsiiraqvq nsvdeyvfna
      121 hympltseyg fhsslsymin ssqykqpqql etylarleqv prffeqnihw mkkgletglt
      181 qpqavlagye dsisayivdd vtqsdfyspf ktntaglsen dfkalqqkak riikndvias
      241 ykayltfftt qyqpgartti gisqtpngka fyknraqyyt ttnmsideih qlglsevari
      301 rsemqeiike vgfegsfadf ihflrtdpqf yattpeqllk eaayiakkmd aqlpklfhtl
      361 prmpygvapv paniapkytt gryvgssrsd qagyywvnty aldkrplyvl ealtlheavp
      421 ghhlqislna elenlpsyrr daylsafgeg wglyseylgi eagfyqdpys rfgrltyemw
      481 raarlvvdtg mhmygwsrer amnfmsenta lslhnvktet dryiswpgqa lsykigelti
      541 krlrteaeqa lgprfdiref hhqvlrhgsv plsvleeqvr lyikaelent qs
//
LOCUS       WP_273609971             290 aa            linear   BCT 28-DEC-2024
DEFINITION  diacylglycerol/lipid kinase family protein [Pseudoalteromonas sp.
            Angola-7].
ACCESSION   WP_273609971
VERSION     WP_273609971.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..290
                     /organism="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     Protein         1..290
                     /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=32223
     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 mqlliivkps vknvvldhld wlkktcqkkn ilyitvkttg nfeydlanvk lnaqksqiav
       61 aiggdgtlnl alngvinsac slailpcgtg ndfarrfhct akqwqnaifn apthlidvgk
      121 intryfinva gvgfdahvik qlghlqsmsa wrykwtsfks lftykastls gaflnkqcsy
      181 qnlitvfans qyfgggikia prakiddgll dcyqmqagsl vdhlysfikl ifkrhhtlkk
      241 ltysqlkqah intknlliea dgelvgvtpa viaiqeqain fhipikkrlq
//
LOCUS       WP_273610195             371 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Pseudoalteromonas].
ACCESSION   WP_273610195
VERSION     WP_273610195.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 371)
  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 371)
  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 371)
  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 371)
  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 371)
  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 371)
  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 371)
  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 11471805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..371
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41367
     Region          5..369
                     /region_name="COG4938"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443965"
ORIGIN      
        1 mlnllslenf ksikdedfel anltlfsgfn gmgkssalqs llllrqsfdk hllpsiglsl
       61 sgefvnlgng kdllyayaen erikietcwd dtqlilnfdy densdmqpln sssivdkdaf
      121 keslfvanfq ylsaerispk svydvseyav nqrrtlgakg eytahflsqh gdenivisdm
      181 lhvnsatktl idnlnawmse itpgtkvitr lipeinqasl hyqfasasel tnkfrpentg
      241 fgltyvlpvv tsllsakpgd lllienpesh lhpsgqsvia qmmaiasqng vqilvethsd
      301 hilngvrgav knnkisqdnv iayflsrdin seehevdvek ieidsdgrid rwpngffdew
      361 dkslntlleg k
//
LOCUS       WP_273610090             300 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: prepilin peptidase [unclassified Pseudoalteromonas].
ACCESSION   WP_273610090
VERSION     WP_273610090.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 300)
  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 300)
  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..300
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..300
                     /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=32937
     Region          17..298
                     /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 menlflditt amqsqlwfyl ttvglvslcv gsflnvviyr lplmmqqewq secrlllede
       61 ltakptqasn sesfnlvkpn stcpkcktai kpwqnipiis wimlkgkcan csnpisaryp
      121 iveaitalls lviaytfgat ehaflyifvt wilvaltfid idymllpdql tlplvwlali
      181 aavmgitisp seaivgaacg ylslwsvfwl fklltgkegm gygdfkllav fgallgwqsl
      241 ltiillssvv gaiigialls iqgkdkatpi pfgpylaiag witlmwgaqi qaayfnligy
//
LOCUS       WP_273609967             458 aa            linear   BCT 28-DEC-2024
DEFINITION  class II fumarate hydratase [Pseudoalteromonas sp. Angola-7].
ACCESSION   WP_273609967
VERSION     WP_273609967.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-7
  ORGANISM  Pseudoalteromonas sp. Angola-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-7"
                     /db_xref="taxon:3025336"
     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=48583
     Region          1..455
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 msnfrtesds mgelqvpsda lyqaqtqrav nnfaisgltm pkqfvtalay ikqaaaqsnf
       61 elnhlskska naieqacqqi idgehyehfp vdifqtgsgt ssnmnanevi atlatrigne
      121 pvhpnddvnm gqssndvvpt aialssainv vyellpslek lsqsleqkka dvgkivktgr
      181 thlmdampvt feqtlsawqs qvnnaasgir hslervcela qggtavgtgi nadgefaskl
      241 aknlsanvgi sfkpssnffy nigsqdaiva lsgqlkvlav aqmkiandlr wmnsgplagl
      301 geielealqp gssimpgkvn pvipeaaamv saqvigndat itvagqagnf elnvmlpvia
      361 hnilqsiell ansaqaladk aiasfkvnqp nidkalaknp ilvtalnpvi gyekaakiak
      421 qaykearpii dvaeqetdlp rseletllnp tkltqggl
//
LOCUS       WP_273610228             392 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DegT/DnrJ/EryC1/StrS family aminotransferase
            [unclassified Pseudoalteromonas].
ACCESSION   WP_273610228
VERSION     WP_273610228.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     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=43499
     Region          5..386
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 mlntpfspwp sftqqeadav srvvlsnkvn ywtgtegref ekefatwads eyaialgngt
       61 laldialkal niglgdevit tprtflasas sivtagaapv fadvdlnsqa itaesikavl
      121 tpktkavivv hlagmpaemd eimalskqhg fyviedcaqa hgakykgrsv gsighvgaws
      181 fcqdkimttg geggmvttns kelwstmwsy kdhgksfdai ynrehspgfr wlhesfgtnw
      241 rmtemqaaig riqltrmsdw takrqaygaq ldqaasnfec irlvevpeys ehaeykhymf
      301 irpeylaqgw drdrivneiv ergvpcfqgs csevylekaf dntpwrpekr lpnavelget
      361 slmflvhptl tqaeiaktvq vmkevfalas kp
//
LOCUS       WP_273610269             748 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: putative bifunctional diguanylate
            cyclase/phosphodiesterase [unclassified Pseudoalteromonas].
ACCESSION   WP_273610269
VERSION     WP_273610269.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 748)
  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 748)
  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 748)
  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 748)
  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..748
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..748
                     /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=85246
     Region          <320..745
                     /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 mlqnfhigli dsnpftftls avflftlfaa ifvkafhknv qiiemkrikl vvfiavsigt
       61 avwhqaslsv vkaeeanara kinlietmin ksieaqikal srikarvnne sfddfkrlld
      121 idqktytngy niikgvlvld selnfvsgnt fsrhfylngm lekpiikawl trdlddiqfa
      181 ansltlnsaa ptlmllatve latknkyyil nlldinllld kdylhylsqy dtyleltksi
      241 yfsvdhnnen ktnlselins ynhfitqkin vmdlvehevy sfindydsih tdtiidqsil
      301 wltfififif vqvadssrvi qfrakhdelt gllkltaled efievtsekh fnnfstvilk
      361 vdlfeaiyis lgykicdeli nnvslrires tnnialiarg asdsfvlyff dispesleqk
      421 ikslivelte ahiiddnein lsvsagaaty rhldsfnlrl nlqqanvale kakelggnqf
      481 hfyqqsmedk ynetvtirnd lqnalkndvl evfyqpvhcl ndstitgvea lvrwsngnew
      541 vspakfipia ettgqitqvg eqvlkkvied ikkypqlqnm tvavnfstkq iikddfasnl
      601 lslltennii lenftvevte syfqergviv sklielvnyg lnvaiddfgt gysslsylth
      661 qpaniikldr eftigahllk tkeqklldti irfcydldks vivegvegeg likhlskfeg
      721 ikvqgyffsk plpihslidy iennkikd
//
LOCUS       WP_273610376             906 aa            linear   BCT 28-DEC-2024
DEFINITION  DEAD/DEAH box helicase [Mycobacterium tuberculosis].
ACCESSION   WP_273610376
VERSION     WP_273610376.1
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 906)
  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 906)
  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..906
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..906
                     /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=99482
     Region          4..904
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
ORIGIN      
        1 mtelaeldrf taelpfsldd fqqracsale rghgvlvcap tgagktvvge favhlalaag
       61 skcfyttplk alsnqkhtdl tarygrdqig lltgdlsvng napvvvmtte vlrnmlyads
      121 palqglsyvv mdevnfladr mrgpvweevi lqlpddvrvv slsatvsnae efggwiqmvr
      181 gdttvvvdeh rpvplwqhvl vgkrmfdlfd yrigeaegqp qvnrellrhi ahrreadrma
      241 dwqprrrgsg rpgfyrppgr peviakldae gllpaitfvf sragcdaavt qclrsplrlt
      301 seeerariae vidhrcgdla dsdlavlgyy ewregllrgl aahhagmlpa frhtveelft
      361 aglvkavfat etlalginmp artvvlerlv kfngeqhmpl tpgeytqltg ragrrgidve
      421 ghavviwhpe iepsevagla strtfplrss fapsynmtin lvhrmgpqqa hrlleqsfaq
      481 yqadrsvvgl vrgiergnri lgeiaaelgg sdapileyar lrarvseler aqarasrlqr
      541 rqaatdalaa lrrgdiitit hgrrgglavv lesardrddp rplvltehrw agrissadys
      601 gttpvgsmtl pkrvehrqpr vrrdlasalr saaaglvipa arrvseaggf hdpelessre
      661 qlrrhpvhts pgledqirqa erylrierdn aqlerkvaaa tnslartfdr fvgllteref
      721 idgpatdpvv tddgrllari ysesdllvae clrtgawegl kpaelagvvs avvyetrggd
      781 gqgapfgadv ptprlrqalt qtsrlsttlr adeqahritp srepddgfvr viyrwsrtgd
      841 laaalaaadv ngsgspllag dfvrwcrqvl dlldqvrnaa pnpelratak raigdirrgv
      901 vavdag
//
LOCUS       WP_273610348             237 aa            linear   BCT 28-DEC-2024
DEFINITION  PP2C family protein-serine/threonine phosphatase, partial
            [Pseudoalteromonas sp. CST4].
ACCESSION   WP_273610348
VERSION     WP_273610348.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. CST4
  ORGANISM  Pseudoalteromonas sp. CST4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 237)
  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 237)
  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 237)
  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 237)
  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 237)
  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..237
                     /organism="Pseudoalteromonas sp. CST4"
                     /db_xref="taxon:3025329"
     Protein         1..>237
                     /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          7..237
                     /region_name="PTC1"
                     /note="Serine/threonine protein phosphatase PrpC [Signal
                     transduction mechanisms]; COG0631"
                     /db_xref="CDD:440396"
ORIGIN      
        1 misnlstsya ithrgavrql nedshveins hnlwvvadgm ggheagevas qlvvdvirak
       61 veektlatls vshivsaied anrqlndysa qylgsktags tvtalfikdn qyyvlwvgds
      121 raymlrngrl qqvsrdhsqv ndlidegvis veeakthpls nvitravgvt devkvdvvqg
      181 evntndifll csdgltgels deeiclslep nsiidsgmal mhsslvrgar dnvtcii
//
LOCUS       WP_273610491             371 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Mycobacterium
            tuberculosis].
ACCESSION   WP_273610491
VERSION     WP_273610491.1
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 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="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..371
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38917
     Region          48..370
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mdstvtasir rmlgllaatl llggctgqht trtaasttyt phikassqdv ldgainadep
       61 gcsaavgveg kviwsgvrgi adlasgakit tdtvfdiasv skqftatail llvdagkltl
      121 ddpisqyvpe lpdwaqtvtv eqlmhqtsgi pdyvallaar gyqvsdrtie aearqalaaa
      181 pelqfkpgtr fdysnsnyll lgeivhrasg qplpeflsae ifqplglamv vdpvgkvpnk
      241 avsyekgtgg nrseyrvgnp aweqigdggi qttpsqlarw adnyrtgsvg glklleaqla
      301 gavetepggg drygagivsr adgtldhaga wagfvtafhi ssdrrtsvai scntdkpdpv
      361 amadalgrlw m
//
LOCUS       WP_273610545             298 aa            linear   BCT 28-DEC-2024
DEFINITION  AAA family ATPase [Mycobacterium tuberculosis].
ACCESSION   WP_273610545
VERSION     WP_273610545.1
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 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="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     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=32478
     Region          6..255
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 mtfaspddvi rrfdeqnyll dtgtasaiyl avtlgrplll egepgvgktt aaktlavvld
       61 ttlirlqcye gltanealyd wnyqrqllsi rlaeargkgi sdiseadlyt eaylvdrpil
      121 rcvrhrgptp pvllideidr addefealll eflgesavtv pelgtflaec ppiavltsnr
      181 srdlhdalrr rclyhwidyp epdraaaivr rtvpgatapl ienatqfvct ardldldkpp
      241 gvaetidwva alvalgvadl taadsspala slgalaktpd drtqirdayq aftkcsha
//
LOCUS       WP_273610625             461 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [unclassified
            Pseudoalteromonas].
ACCESSION   WP_273610625
VERSION     WP_273610625.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 461)
  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 461)
  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..461
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..461
                     /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=52840
     Region          84..418
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mssnypkvvk qtvnlgslpy vsnvdeegqr tiafhedhiv erfprvlslv riqdaleinl
       61 flehrykglf mppkrggkkn plggvslitv qslansmslf lqwveknnvd whevyavsds
      121 dkakywlpvy ryrkhlieqv iakdidrdta nlyinhvrqf yewarkqrri dkvpfkyktk
      181 vikkkrkdgg ldllftdygs eekgftittt dllipkkykq kksgdaglsp ysqdelklly
      241 askeltkqga klrvdlavqc glraeeiatf tashvvdpal dnkaiyyvti igkydkerti
      301 mvskglmtsl wryrngkehq drlakwqleh gncddaplfl nrsgnfmsrk signviskvr
      361 kelapfgktl krdfhdlrst fatnlagfli hkdlpigfvq yklmqlmgha dfsttqkyin
      421 farsltfdkq maswvdklfg efvaplqeda flaeqsggad a
//
LOCUS       WP_273610647            1357 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Pseudoalteromonas
            sp. Angola-22].
ACCESSION   WP_273610647
VERSION     WP_273610647.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-22
  ORGANISM  Pseudoalteromonas sp. Angola-22
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1357
                     /organism="Pseudoalteromonas sp. Angola-22"
                     /db_xref="taxon:3025340"
     Protein         1..>1357
                     /product="beta strand repeat-containing protein"
     Region          3..1356
                     /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 mesnqllvid lkgsagvvle dgtikplevg dtitvgdlvv tadnssltid vqgetlsipa
       61 nqnvkitpdl laqetrdsse ttvfdeslda aiasleqtdn ndgqtaansd vtdfldaleg
      121 dgdildnlea taaggaggag sgggssfvql triaegvnpn svafdssfdp dstealnird
      181 tsdgvvpddg tasislnevg ltnssqptis gtsenlvget vnitvtdeng nsqvvsavig
      241 pdgtfeitlp npiadgpvsv vveatdpdgn afndaisiei dttapvinid pvadsasqtv
      301 tvtgsvagln tgdnvsvtlt dstgtqqtiv tqvdaqgnws itttsplaeg efnvnavavd
      361 aagnqaidqa vasidltape itvtvagetn natppltgtt tgvpqgtevt itvtdsagev
      421 qlltaitged gswavdvgva lpegdftvda qvsdsvgnqa lasdagvidl tapiveinai
      481 adtqdttpvi tgfaqdvpag svitvvitdi ngqvqtlltq tnddgswsvs vstplaqgef
      541 evnatvtdta gneaqaieqg lvdltspeit vtaiadtndt tptfvgrveg apegsvitvl
      601 vtdsdgniqt ltttleadgt wsvespnaip ggefsvtatv sdpagneasa qtsgevtfap
      661 isiqidsiad tndttpflsg ntgnvpagtt itltitasdg stfnllavtq edgswsaqvt
      721 eplpegdftv vaaviddagn eaqastvgnv dltvsinfii dtndttptis gttqdvdaga
      781 vvtvtftgsd gatetvqvtt nadgswsiea tdelvegqft vvatvtdaag ntasatevge
      841 idltdpaiti npitdtndtt psvtgsvvdv pqgtevtlli tdsdgnqqti taitnadgsy
      901 sadilnelse gdftvtasvs deagnsstat vtgtidltap tvtidnigdt ndttptisgs
      961 tqglaagsvv tvivtdnaga eqqfvtaing dgtwsidvpq tlaegefsvv anvsdsagns
     1021 aqdsqtgsid ltaptisvnd ftdsndstpv fsgtttdvep gslitvsvtd sngdsqtlta
     1081 vvaedgswqv gattaiaege ftitatatda agneasattt gvidtaaptv vidpvgdtnd
     1141 ttptisgsat gepegtvvti tvtdeagnpq tittevqadg tfsvdvpnel segeftvevs
     1201 vtdnagnett atttgevdta aptviidpvg dtndttptis gsatgepegt vvtitvtdea
     1261 gnlqtittev qadgtfsvdv pnelsegeft vevsvtdnag nettatttge vdtaastvli
     1321 dpvgdtndtt ptisgsatge pegtvvtitv tdeagnp
//
LOCUS       WP_273610653              93 aa            linear   BCT 28-DEC-2024
DEFINITION  type II toxin-antitoxin system RelE family toxin [Pseudoalteromonas
            sp. Angola-22].
ACCESSION   WP_273610653
VERSION     WP_273610653.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-22
  ORGANISM  Pseudoalteromonas sp. Angola-22
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 93)
  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 93)
  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..93
                     /organism="Pseudoalteromonas sp. Angola-22"
                     /db_xref="taxon:3025340"
     Protein         1..93
                     /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=10956
     Region          1..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 myelefdpra lkewhklgat vrdqfkkkls evlkhpriea nrlrelpdcy kiklrkagyr
       61 liyqvqdekv silvlaigkr nkseayndae krv
//
LOCUS       WP_273610705             332 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273610705
VERSION     WP_273610705.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..332
                     /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=38331
     Region          110..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnsyvslsdk yltaqglita vvelaqsrgv alhkllrgtg ifeqdllsve hcfsleqqvk
       61 llsqfkrlmn tpdsgfllgs qlvndsssaa qsvlysaklg aallqiqrah lqlcplffsq
      121 hyvsnqqfyi flnaatgldd dlhnyileiy saafysllkr lsphypqcef dfsfkrprhi
      181 hqyeqhlglk lrfeqpttrw visktllrqa npyaselrfm qaraqlavks hekytfieav
      241 wrylhtynea sleqtaqyfa mspatfkrkl kchsmrfssl vdeqnkhkai ylltlrakcn
      301 ehvaerlafy dipnfrrafk rwtgltpsql kv
//
LOCUS       WP_273610871             499 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC transporter permease [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273610871
VERSION     WP_273610871.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 499)
  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 499)
  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 499)
  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 499)
  AUTHORS   ter Beek,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 499)
  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 499)
  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..499
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..499
                     /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=53672
     Region          10..495
                     /region_name="FbpB"
                     /note="ABC-type Fe3+ transport system, permease component
                     [Inorganic ion transport and metabolism]; COG1178"
                     /db_xref="CDD:440791"
ORIGIN      
        1 mripasypma llaalititp vyilitlasd sstlfdshnl kilgntlslm gltvlgsili
       61 gvplafisay vhlpfkkiwl vifaaplaip syigaftlya afgpggeinn llgfktppmy
      121 glsgaaivmt lytfpfvmmt trssllslda smvnaartlg msmtqsvfkv ilprvvngia
      181 agsllvalyt lsdfgtpamm rldtftrviy veynafalgr aamlslqlmv ivgflllies
      241 qiktaserhg rplvlfptkw qitamiaafg pilllaiglp laiffvwlar dgynnfdfsi
      301 awnsayasai aaivavivai pvahaalsgk agrimervty fgfgipgivm gtalvygglq
      361 lpflyqtlal liiaymlrfl plavgsirts tehldqslik sarvlgaspr eaftritlpl
      421 tmrgiiagaa lvflesmrel eatlllgptg fetlstylwr vyeagyfgra aipglllvvi
      481 sacglaimms gekrnqleh
//
LOCUS       WP_273610924             850 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 3 protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273610924
VERSION     WP_273610924.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 850)
  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 850)
  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 850)
  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 850)
  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 850)
  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..850
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..850
                     /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=91371
     Region          70..>462
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          436..650
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          683..837
                     /region_name="Exop_C"
                     /note="Galactose-binding domain-like; pfam18559"
                     /db_xref="CDD:436577"
ORIGIN      
        1 mktpfslnki arasliaslg ilaacsndat ttpeannals ktekiwpkln iavkqdpeie
       61 akiadylktm tleqkvaqmi qpeirditve dmrkygfgsy lngggafpng dkhatpmdwv
      121 klaedfyqas vddsidgski ptmwgtdavh ghnnvigatl fphniglgaa nnpalieqia
      181 aitavevmat gidwvfaptv avvrddrwgr tyegysedpq ivrdysaaiv nglqgkadgd
      241 flsdkrvist vkhflgdggt vdgddqgnni dseqdlfdih aqgyvgglsa gsqsvmasfn
      301 swhgvknhgn kylltdvlkt rmgfdgfvvg dwnghgqieg ctnescaqav nagldifmvp
      361 tgawkplyen tiaqvkagei smsriddavs rilrvklrag lfdkpspakr qfsgktelig
      421 aqqhrevarq avreslvllk nknnilplda nqtvliagdg adnigkqsgg wsitwqgtnn
      481 knadfpgats iyaglekqit eaggrailsv dgsyeqrpdv avvvfgeepy aeghgdrdnl
      541 efergnkksl allkslkeqg iavvsvfisg rpmwvnseln asdafvaawl pgtegggiad
      601 vilkgkdgsi qhdfsgklsf swpktavqat vnkgdddysp llpygfglty gdknvladnl
      661 dedskldnsa ltsmdilvga pvapwrlllk sgdelldvss sthqlgslky rtedktvqed
      721 arqfnfsgeq kasaeivtsf aedtitylea ngvisfdikl nepltddvnl amtcsgecgg
      781 aialskmvdq siknkwqsvs vdlrcfanqg vdfasltspf slhassktsv svaniqfvpn
      841 kadsaglkcq
//
LOCUS       WP_273610929             350 aa            linear   BCT 28-DEC-2024
DEFINITION  fatty acid desaturase family protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273610929
VERSION     WP_273610929.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 350)
  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..350
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..350
                     /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=40771
     Region          44..350
                     /region_name="DesA"
                     /note="Fatty acid desaturase [Lipid transport and
                     metabolism]; COG3239"
                     /db_xref="CDD:442471"
ORIGIN      
        1 mkninfdqla hdldsikmdt lgkvgqqdan yirsvvkkqr lcewsgrill mlgfiqpllw
       61 vagvlllala kildnmeigh nvmhgqydwm ndkqlnsqhy ewdiacdgqs wlrvhnfehh
      121 tytniigkdr dfgygllrls ndfkwrlknv wqfityinls vlfqwgvsyh elaaervfig
      181 kkkenreggv shstlkqrff skgarqlikd yvifpllagp lflwvlagnl lanlirnlwt
      241 stiifcghft edtetfkqed cinetqgqwy yrqvlgssni kgphwfhvlt ghlscqiehh
      301 lfpdmpssry qevapqvqav mqkhgidyht ggffkqyssv lkriirysfk
//
LOCUS       WP_273610939             247 aa            linear   BCT 28-DEC-2024
DEFINITION  4'-phosphopantetheinyl transferase family protein
            [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273610939
VERSION     WP_273610939.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 247)
  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..247
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..247
                     /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=28184
     Region          18..199
                     /region_name="Sfp"
                     /note="Phosphopantetheinyl transferase [Coenzyme transport
                     and metabolism]; COG2091"
                     /db_xref="CDD:441694"
ORIGIN      
        1 mtnhffkntl siapsfysdl spsnntilvf nantlnvehl dltqylspfe lsvinrrkrm
       61 qakqeylasr illkqlakhi qpqyahipln kmsthfneec sklqlhinht vintcishsh
      121 glvgvalnvt kaefgfdiek inlkrrfekl akhfyhkaei alitaplaik eqahrffriw
      181 tlkealakat srpiaqllsp nvfdefslln ltassntitv aneefdisva hkkstdwrcf
      241 ilnnldt
//
LOCUS       WP_273610944             617 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273610944
VERSION     WP_273610944.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 617)
  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 617)
  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 617)
  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 617)
  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..617
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..617
                     /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=68325
     Region          11..585
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mnrtphiilp allcsvtpfv yantlsdess ieqitveasp tanklpvgtf dspisnleyd
       61 prvdlqsrnm aeaqadvtir ggifentgfr vgsatlldpq sghyfaeipi apqmlsgaav
      121 ltgadnalyg mnssvgtvsf gwkpiitggs vslgtgtndf nlqsihaakn tqldslanyt
      181 lgfegeyshs qsdgtidngd hdfsrastrv qlasensqtd lfygsqdkff gwpnlytpfg
      241 vnetedletr lwmlnhkqny aknsnfevsa yyrthddhyi ysrenpsafe afhksevksl
      301 alsgrhaqsn afainysaqf iddsiesttl ennftsrkyy klsvlpqytm alkahqqlif
      361 rlgaayddtn rddaevsaig ditlntqnnd gtaqslylsy aqasqvagyt aiggsdsggl
      421 frsnynlere ttsnlelgll leeqswqlns aifyrkdsnl tdwtfnfdst sarfanpvdi
      481 dtagveflat khfdtaklia sytylhksen ygaadidasf yalnfpdhrl tlgavynptd
      541 ilefridnew rtqhknalrn gddnalftql tlkitppqls nlfitlaadn lwdesfeeip
      601 gtpgrgeqyt lsatysw
//
LOCUS       WP_273610948             194 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273610948
VERSION     WP_273610948.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     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=21315
     Region          2..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 mwderyntqq yaygkqpndf laehykqlpk gnvislaege grnavflakm gysvtavdgs
       61 kvglekaakl akehsvniel vhadlakfdf ekekwdavvs iycplpsavr savykravkg
      121 lklggvflle aytpeqvnyn tgggpsvdtk tsksdlqddl aelsfvhlee lkrevfegty
      181 htglasvlqa iakk
//
LOCUS       WP_273611067             468 aa            linear   BCT 28-DEC-2024
DEFINITION  alanine/glycine:cation symporter family protein [Pseudoalteromonas
            sp. Angola-4].
ACCESSION   WP_273611067
VERSION     WP_273611067.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     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=49751
     Region          1..446
                     /region_name="AlsT"
                     /note="Na+/alanine symporter [Amino acid transport and
                     metabolism]; COG1115"
                     /db_xref="CDD:440732"
ORIGIN      
        1 mfdtvvksvn gllwgegqil iyillfagiw fsvrlkaiqi vkfkhmfsll kgsskckkdd
       61 issfqalctg lcarvgtgnl agvavaislg gsgaifwmwv iailgmatgf aesvlgqvyk
      121 vrdssgefrg gpayyiqqgl gsrafaivfa aclflgygft fsamqtntit dalnyafqvp
      181 tfysglvitv lagsiilggf kaiarfaerv vplmgilfva aaviitimnl pqvpamlkdv
      241 flsafglqea gagamgaaik ngiqrglysn eagagsvpha aasaspmpnh pvtqgyiqml
      301 gvffdtivlc sctavvilla dvdisgemeg irltqsamta hlaqggvyfv aaaitlfaft
      361 svvanyayae snlhlfkldn kvgrtiytll ylsmmlwgas aslkevwdla dialglmtvv
      421 nviaiilltp tilsvnsdyn tqrekgiepe fkvkdvkvqg kcesgiwg
//
LOCUS       WP_273611125             635 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273611125
VERSION     WP_273611125.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 635)
  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 635)
  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 635)
  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 635)
  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..635
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..635
                     /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=71431
     Region          <184..605
                     /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 mnkfkplggi ffvfilfcfc lnieltnqin rinlfnpdid lrhfdivdtt lemapwynpm
       61 lnghylihqp sadfllvktt dtefiaanat klilmtltsp infilvcmal fvgftiirke
      121 rkkisyqhqi aqlnnnanql lvafnlqpqh dnpsglgnls qsinnlnthv anylkqtqts
      181 icqdkltlli drhayiehid rqinftdeeq lkcallfidl dgfkqvndsf ghsfgdeilv
      241 qvatrlanvl rhhklsnine anqleqnlsr lggdefsifi esvdtdnkvv diakhvlsel
      301 ekdfvlgnki ikisasigia aypesastpq allqladvam yraksdgkgv fkvyspemgn
      361 kmrryhylle elrlavackd fylsfqpivh vedcmidyfe altrwdhpia gmispaefip
      421 iaeesnlile lgdwimhesc rqmaawhnag mrkvkisvnv sgvqlkhrsv ydwimknlkn
      481 tglpshslml eitestfika sksmieeler lraegvtiai ddfgtgfssl stladlpidv
      541 ikidrsfisq adkspkyndi lntiselgqk lglkivaegv eeieqfelvk rmgvssvqgy
      601 lvsrpessin vgnkvlrknt anlsaagtsa weieg
//
LOCUS       WP_273611595             395 aa            linear   BCT 28-DEC-2024
DEFINITION  vWA domain-containing protein [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273611595
VERSION     WP_273611595.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..395
                     /product="vWA domain-containing protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=45634
     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 mlvqffftlr kyrlpvslre lldlinalkk gvifadvdgf yhlartimvk dethfdrfdk
       61 afsdyfsgia dldlleslkq qhnlpkdwlr kefekhlsde ekaqlkamgg ldelmktlke
      121 rleeqqkrha ggnkwvgtgg tspfgaygyn pegvrigqdg nrnrqavkvw dkreyrnlds
      181 dreigsrtik lalkklrkfa rtgasdtldl netiratakq ggmldvkmap erhnavkvlm
      241 lfdiggsmdd yihtceelfs aahsefkhle fyyfhnclye hvwqdnarrh sniidtmtli
      301 nkftsdykvi fvgdatmgpy eiaypggsve hyneepgsaw lqritnhfdk vawlnpqpve
      361 hwpyyqsidf ikqlmdnrmy plsldgisna ikels
//
LOCUS       WP_273611080             295 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273611080
VERSION     WP_273611080.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..295
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=33115
     Region          54..288
                     /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 mrlflalllf ssssfaqvsv tymqddslht vigeryksgy ffnapnstqt ihvvtldwpp
       61 yignklcnkg wvyqfstail hstgysayie fvpwaravra velgkadvlm peyyiedtap
      121 sdyiegktrr kllglsnsfe ggnigflkrk gepdrfngnl kslkgsrigv vrgyqntpef
      181 dammdnnefi iinavddlql vkllaakrvd liigdpavll ysvkyaalpd sekqtllsai
      241 epeskaiqyn plyfaiskkt pnwltvledi ntalykfkns getqrmkqal lnecd
//
LOCUS       WP_273611249             211 aa            linear   BCT 28-DEC-2024
DEFINITION  methyltransferase family protein [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273611249
VERSION     WP_273611249.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..211
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..211
                     /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=23968
     Region          103..211
                     /region_name="STE14"
                     /note="Protein-S-isoprenylcysteine O-methyltransferase
                     Ste14 [Posttranslational modification, protein turnover,
                     chaperones]; COG2020"
                     /db_xref="CDD:441623"
ORIGIN      
        1 msyqplidds aslieftrvy lalfytfvag fytvriiykn rstptgvifp gakfctswwn
       61 hmafkffraa iwfvcvlrvf vpatdnylgm fytlngwpgv mfgnimltag fvlsmvvhfh
      121 maslwrsgid pngpqtlktt glysfsrnpm yvgvataqlg fflalpslfs liclavglya
      181 lykqiaveea hlvtrfnndy lkykqtvprw l
//
LOCUS       WP_273611648             469 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54-dependent transcriptional regulator [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273611648
VERSION     WP_273611648.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     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=51988
     Region          11..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 mntnlypsfe vlicdddnsf lrsisfaier ycginnivqc ndsrdviakl nqgnvrvvll
       61 dlnmphisgd eliaqitelf phisvviisg inqveaavkc iklgaygyhv ktedperlsn
      121 simqvvrfqe lnlenqamrg yllenqtslh pafskiisvd hqmhsvfnyi esisnsqqpi
      181 litgesgvgk eliaraihet sscsgelvcv nvaglddnlf sdtlfghkkg aftgaeqark
      241 gmierasggi lfldeigdln lasqvkllrl lqegeyypvg sdtpkrinar iiaathqnll
      301 tkkengefrn dlyyrlkihh vnipplrerk qdialllehf ltlaaqefnk pvasipkell
      361 illenyafpg nirelramaf damsthqsga lsmkafesvr savpkldmqa qlakplfest
      421 stlptlkqaa ellvaeamkr snsnqsmaaq llgisqpals krlkktete
//
LOCUS       WP_273611697             252 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273611697
VERSION     WP_273611697.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..252
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28549
     Region          32..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 myflklflsl filhlatfan aqqnqpelny nvsasgshyp fytgnpekpg ilpeiitalm
       61 aqanitanhv elptkritky lengiidfdv islkwlaqse rdnpyyifse plipatemiv
      121 alpdnvaqyq tkqslyskev gtvlgyyyhd dakfnrvdfp sekelmials karidiaimg
      181 thtaaywskq lnintefgaq hshgylrvrl lakhkallpk inqalahlhs sgyikhiedk
      241 yinpipaqnl rd
//
LOCUS       WP_273611874             668 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha-amylase [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273611874
VERSION     WP_273611874.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 668)
  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 668)
  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 668)
  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 10183021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..668
                     /product="alpha-amylase"
                     /EC_number="3.2.1.1"
                     /GO_function="GO:0004556 - alpha-amylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73646
     Region          27..376
                     /region_name="AmyAc_bac_euk_AmyA"
                     /note="Alpha amylase catalytic domain found in bacterial
                     and eukaryotic Alpha amylases (also called
                     1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
                     /db_xref="CDD:200456"
     Site            order(70..71,74..75,110,113,163..166,196,198..199,
                     201..202,224,226,231,287..288,293)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(112,168)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(198,224,288)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          383..470
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
ORIGIN      
        1 mklnkmitta gfslgltlps lvsaapttfv hlfewnwqdv aqeceqflgp kgyaavqvsp
       61 pnehitgsqw wtryqpvsyq lqsrggnrsq fidmvnrcna agvdiyvdtl inhmaagsgt
      121 gtagntfgnk qypiyspqdf hescsinped ygnnryrvqn celvgladln tssnyvqntl
      181 aayindlqam gikgfrfdaa khvaasdiqs lmakingspv vfhevidqgt eavaaseyls
      241 tglvtefkys tqlgntfrng slawlsnfge gwgfmpsssa vvfvdnhdnq rghggagnvi
      301 tfedgrlydl anvfmlaypy gypkvmssyd fhgdtdaggp svpvhnngnl ecfasnwkce
      361 hrwsyiaggv dfrnntadnw vvtnwwdnth nqiafgrgss ghmainkeds tlnatiqtdm
      421 apgqycnvlk gellgnatsc sgevitvnsn gtinlnvapw daiaihknak ltqeavpnns
      481 dwqrtvvfin aqtqsgqdmf vrggidhnya ntnlarncqt tnvecampir hnnlknnttt
      541 pwkandnyld wygieqgqsg eaqgtamdwt tnvwpseyga qksvtvdgfg vtplniwgeh
      601 ywmldvdmdc skavngwfel kafikngeew egdisqantp ytstnhmaqc gkinmfefns
      661 ssvevrdf
//
LOCUS       WP_273611881             334 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273611881
VERSION     WP_273611881.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     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=35264
     Region          26..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 mditkinqwt ifiaavlial gslfsalsfg aadtplsdvl tgilsagegs fnariiyelr
       61 lprtllafma gaglaiagli lqtvtrnpla dpylfgissg asfgvvllma vagisagfml
      121 saaallgsfl amglliliag rqkstqvesm llagvalsfl fsaftsllly wsdpqavagi
      181 lfwtlgsfar aqwatlwlpc vvivvcisfm lsfkrqlnal llgdesaitl gvrvhrfril
      241 mlvlsslita alvalcggig fvglmvphiv rffisqgsta gllitslvgg tfmvwvdvls
      301 rsllknqelp vgvitaamgs vfflsllffr ktka
//
LOCUS       WP_273611938             458 aa            linear   BCT 28-DEC-2024
DEFINITION  class II fumarate hydratase [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273611938
VERSION     WP_273611938.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     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=48638
     Region          1..455
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
ORIGIN      
        1 msnfrtesds mgelqvpnda lyqaqtqrav nnfaisgltm pkqfvtalay ikqaaaqsnf
       61 elnhlskska naieqacqqi idgehyehfp vdifqtgsgt ssnmnanevi atlatrigne
      121 pvhpnddvnm gqssndvvpt aialssainv vyellpslek lsqsleqkka dvgkivktgr
      181 thlmdampvt feqtlsawqs qvnnaasgir hslervcela qggtavgtgi nadgefaskf
      241 aknlsanvgi sfkpssnffy nigsqdaiva lsgqlkvlav aqmkiandlr wmnsgplagl
      301 geielealqp gssimpgkvn pvipeaaamv saqvigndat itvagqagnf elnvmlpvia
      361 hnilqsiell ansaqaladk aiasfkvnqt nidkalaknp ilvtalnpvi gyekaakiak
      421 qaykearpii dvaeqetdls rseletllnp tkltqggl
//
LOCUS       WP_273612001            1116 aa            linear   BCT 28-DEC-2024
DEFINITION  beta strand repeat-containing protein, partial [Pseudoalteromonas
            sp. Angola-4].
ACCESSION   WP_273612001
VERSION     WP_273612001.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..1116
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..>1116
                     /product="beta strand repeat-containing protein"
     Region          <153..1075
                     /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 meniskavvi vellsdvwvv mdngdwvkvd sipeqfadlp vlnssdiale gnelvfseas
       61 eqlvvpqdii sqlvsdlsqn stfdarsnts svtslsssda neaqvayqli arqgqelvpe
      121 sgyettptet teeedpnfie frpdpiftvg qlggdgvfin kydavalefs gtvenvpdgs
      181 lvqivlsdsd gneiivttev qdgvwsvtni ditalndgev tatvslvggn eddaasetkv
      241 kdtqadifid fedglntnqp idfegevqdv qdgqlvtvti fdaqgnpiat yeatvtngqw
      301 svgpepfadl pdgnytiqvs tideagndtq tqksfskdtt aiitidvnet edgvinnsen
      361 vvqvsgtveg iedgqtvlvt ltdidgnevs veavvengqy qlevdissls dgeitataqa
      421 qdllgnesta sqvishdkta qltveidstq dgvinseees nvtvrgvvtg iedgqtvtvv
      481 lsdgvnppit ltaivvngsy eiagvdissl ndgtisanat aqdisgnpas asdeaqydss
      541 vatsivaqdi dgvinsaeqn nvqlsgsvtd iepgqlvtvt ftdsnnqqvv vtaevdadgn
      601 wqisgdiesl adgeisaqis ifdaagneat qevtfskdtq stltlnidkt edgvingsae
      661 ntdislsgiv ngvedgqevt iiftdslgne vvvtaiveng nyalsgvdis alndgdisvs
      721 asvldtagnt avaedsfeid nsalitasid ktddgvingq dddlrdnvnt aenagvvvrg
      781 tvedvedgqi vtvtlsdgin ppvitqavvq ngqyvtepmd atglndgtmi ataevadaag
      841 npisaqdnve idttaaitts idktadsvin gsnenqeivv rgtvsgiedg qvvtitlrdg
      901 vnpgiavqai vqngeyvtap idasslndgd ivaradvsdl agneatardt veidkladit
      961 tnidetadgv ingsgesaai vvrgtvedie dgqivtvtis dgvnpavttt atvingeyvt
     1021 tpidasslnd gtltatasvs diagnpvsaq dsveldntaa ittsidktad gvingngesa
     1081 amvvrgtvtd vedgqtvtvi lsdgtnqvet talvqn
//
LOCUS       WP_273612015             259 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273612015
VERSION     WP_273612015.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 259)
  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..259
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..259
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=29611
     Region          30..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 mwvkfvrvvl sifvfmlysa mcnaqtitfv aedlppyhfi nennepdgal vdlakttikh
       61 tklsakfeii pmariftmle nnpnaialsl lktpirarqy twlgesyfad aylvslknrt
      121 devthlnhak fyqvatirgy ssatylknag ftedknlvlv syyqqlwqml ykkridfvlt
      181 ntltlnnelk hsglnpnlit krihltdyps klyfsanktl dkhtasaisy alntlkenge
      241 yqailnkwql plpatankl
//
LOCUS       WP_273612046             433 aa            linear   BCT 28-DEC-2024
DEFINITION  PepSY-associated TM helix domain-containing protein
            [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273612046
VERSION     WP_273612046.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 433)
  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..433
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..433
                     /product="PepSY-associated TM helix domain-containing
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=47459
     Region          5..394
                     /region_name="PiuB"
                     /note="PepSY-associated TM region [Function unknown];
                     COG3182"
                     /db_xref="CDD:442415"
ORIGIN      
        1 mksitlkklf llhswvgvvt avllfvvaft galavlarpe lkiwanqslq qtqhipnsei
       61 stlvntyhaq vpkefgenih vfmptghnfh llalvfeshh gdenyqqevl rafefdpasl
      121 alvntyygps kqyyanrktd aasyigefha dlhlgrpigl iltgflgltl lvstvtglfi
      181 hrklikelft lrwlkgfdvt isdghkvmgi wgsifnivig fsgaflglat villpaaafv
      241 sfggdqdkli etftaipepi isyvnqptni tailsdaqqr yphavildat vmahndanaq
      301 vylrllggea vasqllhyng qgeyitsmss fgdiagvsik iiailfplhf gnfaglfvkl
      361 lwvmlglaca lmplsgmmmw lakrtrgstp tlsadayarw nrfiigscgg lvlacllcvi
      421 pcastfklcr gwr
//
LOCUS       WP_273612148             245 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273612148
VERSION     WP_273612148.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..245
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27917
     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 mdklitlllc vlfsaswgvf acertlsvga hdafwppyvm gisgqlqgke vdaltiifkd
       61 spfcfeikml pnskraftel rhgridigwa asytseraky ahytkayrte vmrlyenknn
      121 qhkvknladi fnqgltigan fgsyygeefe qykkshkkqi eytsatskrf emlnkqridy
      181 aiedelvgny lskrgnslmk aptipainkd qihlmlskrt vtpdevkiin ahitknkaal
      241 kalfe
//
LOCUS       WP_273612149             250 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273612149
VERSION     WP_273612149.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..250
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=28111
     Region          32..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 mnvlsctrvf llmwvtclgl fsakaqacdk tinvgtnery wppyvvlknn tltgieidii
       61 ktifkdspfc inftllpnsl raleelkhgr vdlmfaaskt rerqayahfs lpyreevmll
      121 ykhagsanis sleqlfkkgl tagvnrgsfl ghtfkalsdk yskqivltsd adkrfallnk
      181 krvdfvvdds lvahhfakky tailpveqva pinvnnvhfm mskktitlee vntinahivk
      241 nkaalkalfk
//
LOCUS       WP_273612150             244 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273612150
VERSION     WP_273612150.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 244)
  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..244
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..244
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=27759
     Region          24..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 mkmfllafiv lvaqfnalac tktlkmgtne tnwapylikq gdafvgaevd tvnavfknsp
       61 fciewvyfps lsrvqqelkt ghiditfaas ytkeraeysy ftdvyrdevm llykhenakd
      121 vinlaalfer gfivgvnrgs ffgaefekir khypnqivlt adantrfgml nkkrvdyvid
      181 dsvvakyfak ryntilpvkt apainvngvh fmmskqsvtl devavinrli knnkaaieri
      241 ykpy
//
LOCUS       WP_273612154             439 aa            linear   BCT 28-DEC-2024
DEFINITION  ABC1 kinase family protein [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273612154
VERSION     WP_273612154.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 439)
  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..439
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..439
                     /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=48648
     Region          90..340
                     /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(144..148,150,160,162,221,240..243,283,287..288,290,
                     301..302)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:270872"
ORIGIN      
        1 maasrsipts rlsrfaklgs laggvatnml idgtksalsg ngwnnkalll qpknieklav
       61 qlahlrgaam klgqllsmda gellspeltq llallradan pmphnqlvkv lksewgenwl
      121 nrfshielrp faaasigqvh layqengekl avkiqypgia qsvhsdvdnv iallniarli
      181 pkeldiqpli neakaqllae adyereahyl nrygellsqh vnfkvpkvyg vhntkrilam
      241 eyvqatpiea lsnlpqgeqn niaarlidlf fkemfefkli qtdpnfanfh yqtqskqivl
      301 fdfgatreis sklskaylsl fiagtennra gvlsaareig yskdtlldsy kshvidlflm
      361 aceplrttge fdfknsplat niknaglels aqsqqwhtpp vdalfihrkl aglyliaakl
      421 nakidinalf kpyikghfi
//
LOCUS       WP_273612169             435 aa            linear   BCT 28-DEC-2024
DEFINITION  O-antigen ligase family protein [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273612169
VERSION     WP_273612169.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 435)
  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..435
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..435
                     /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=48865
     Region          157..421
                     /region_name="RfaL"
                     /note="O-antigen ligase [Cell wall/membrane/envelope
                     biogenesis]; COG3307"
                     /db_xref="CDD:442536"
ORIGIN      
        1 mnrfiffllc aivfllplpl gsyrpwaima mgilicitfl mhlvnsavnn qktypprysy
       61 pvfitlllvc atcilqfytv sldpfqtkqm llktsfmllf cwlifiycdn serikkliyt
      121 iiaagvfqal yatylnlspd mlspifgykh tqraigtfty snflanylal clclgigvlv
      181 selkrgshas dltfkqtlra wteillsski ilrisliiii ialiltrsrm gnsaffialm
      241 vvsllalfvy nkkpkafkll ivsffiidli iigaifdvek vkqrisetsi qsetrdevvr
      301 dsiplildkp llgsgggtfy tafpayqsep ysgyydnahn dyiqfavelg ipvtsalgal
      361 ilyclwlcvq tmrkrktalf qgvafgcaia ivdmllhssv dyslqagans mlfmvilcla
      421 ilsnkivvkr grdfk
//
LOCUS       WP_273612155             472 aa            linear   BCT 28-DEC-2024
DEFINITION  sigma-54 interaction domain-containing protein [Pseudoalteromonas
            sp. Angola-4].
ACCESSION   WP_273612155
VERSION     WP_273612155.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 472)
  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 472)
  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..472
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..472
                     /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=52953
     Region          10..469
                     /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 mikqflndpk lllnavgegi ygfdlsgnav fvnpaaermt gwkaqellgk kihqyhhhsh
       61 adgspypade cqiyctmfdg krrevknevf wrkdgtsfav eytstpvyrq geligavavf
      121 rdisaqqqtq nelkqaleqv khlseqlqde nnyliaelne dwqdsglvgq shvfqamlaq
      181 iklvsetdst vlilgengtg kelvarnlhr lskrsnqafi kvncaaftps lleselfghe
      241 rgaftganer rkgrfeladk gtlfldevae lpleaqskll rvlqeqefer vggsttlkvn
      301 irvlaatnrd lwqmvkkgtf ridlyyrlnv fpikvpalke rkedipylct nlitqlnkrl
      361 akqikgvskk aisqlqaydw pgnirelqnv lereailtkh tvlklsqplh gdastavnts
      421 ltlaeaqkqh iiavlelsqw qisgdkgaac klglpestlr skmrklgisk st
//
LOCUS       WP_273612254             181 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase [Pseudoalteromonas sp. Angola-4].
ACCESSION   WP_273612254
VERSION     WP_273612254.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     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=19577
     Region          <30..140
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 msllakkvyr klkeklvevl kgrdqlalyk gvklgtgcri yitdwgsepf lisigdnvti
       61 tsgvkflthd gatclvknss gvryqkylpi qigdnvfigv ntiimpgvti gnnvivaags
      121 vvsksveags vvggvparni ssfdiyaski mkgylandev ptdlnykqkv kfmiekqsek
      181 k
//
LOCUS       WP_273612214             375 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273612214
VERSION     WP_273612214.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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   Rosinski,J.A. 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 375)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..375
                     /organism="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     Protein         1..375
                     /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=43179
     Region          <284..372
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mtesiallvf fthllvavfl lnihsgnqls nrilavflsv tafdisnfif tsfygahlnl
       61 dmfranfsvl tapilyfyvk sivysdlklk akdllhaipf iivclifipr fhlgddiakm
      121 afynnheplf evlfvhvvly lqmfiylali fkklnryklt vlnnysdiei lnkqwlnnfm
      181 mvflidftiv vvrniikfte lqgllnlltt lmmvvtlffv cwilwqtlhn psifqgissk
      241 vksfepkkpp qnpsdvvdvn eaqrvlstik chmslnkpyl npslnidtla kqlnipalki
      301 sivlnhhlgq hffdfinsyr vneaanilsl ksnkqkaile illevgfnsk ssfntafkkh
      361 favtpsqyrk erlnd
//
LOCUS       WP_273612235             416 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Pseudoalteromonas sp.
            Angola-4].
ACCESSION   WP_273612235
VERSION     WP_273612235.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. Angola-4
  ORGANISM  Pseudoalteromonas sp. Angola-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
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="Pseudoalteromonas sp. Angola-4"
                     /db_xref="taxon:3025335"
     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=47531
     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 mnvkeikani kscktlrfsv gdslyikpsk dkksgawelr ytinnkrhfm tlkgsnfpdk
       61 tlsdarieaa linkkikngi dplaervrqg qetiitmndl fndwfkdksk evknphller
      121 qytkdikpyi gklkiddvna rdiraiikev vndgrpsist kclnlcknlf khaqkldltk
      181 snpaaafsqn daggqtksrk ralslqeies tfdvlrenst vftrdnylam vlllvfgnrk
      241 tevtqakwee fdfnekiwnl gtrnkkevyi qipiadevip ifeelkiksc gseyvfpark
      301 vskdghmcen tlnhalakmf gksiskksyp nlleprgikh ftihdlrrtc rslfaelgye
      361 gndvtrylnh tisgvagiyn rydylgerrk lasimanqil prakismvsk ginlse
//
LOCUS       WP_273612378             256 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Paenibacillus
            kyungheensis].
ACCESSION   WP_273612378
VERSION     WP_273612378.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 256)
  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 256)
  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..256
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..256
                     /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=28785
     Region          6..252
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mttlniglql ftlrdetakd fpatlrkvae lgyqgvefag ygdipaeemk alldelglkg
       61 fsshvplqsm rdnlqkeidy lkvigaqymi cpyimpedrp qsseawgalf telqqfgaea
      121 skqgltfgyh nhdfefhgaf kdtnafdgmf aettpeavqv emdvcwvqfa gqdpleyiqk
      181 ytgrlpllhl kdfdkdeqgq mktlelgqgi vnlpqvieqa gkagvqwliv eqdvcqnppl
      241 esvsnsynwl kqnyln
//
LOCUS       WP_273612384             445 aa            linear   BCT 28-DEC-2024
DEFINITION  dihydrolipoyl dehydrogenase family protein [Paenibacillus
            kyungheensis].
ACCESSION   WP_273612384
VERSION     WP_273612384.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=48738
     Region          1..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 msnfdvlfig sgqgawnaam plsmsgqkva iiernkiagv ctnygcnpki ildgpikvme
       61 daqayngigm tsemkinwse lmahknkvld alpvmleenf kkagievikg easfvnektv
      121 svngqeytad kiviasgqrp tpldipgqey lktsneflyl edlpdhivfv gagyvsmela
      181 siavkvgatv hviqssdhil nefyqpyaqk llkkmqqdgi qfhfneklsk veqqgeqlqi
      241 ttengltltt klvinatgrv pnvenlnlea agveynskgi vvdeylqttq kgiyasgdil
      301 dkkqprltpt avfeakylaa sflgaqtqgi eyppiatiaf tvpriaqigi tveeaestgl
      361 tvkpidlgkq wdfagrnete ahltliydqd qklvgaaays qealeiinsl tpvitlglts
      421 kdvdkliyaf psfetmipry mqeak
//
LOCUS       WP_273612419             392 aa            linear   BCT 28-DEC-2024
DEFINITION  alanyl-tRNA editing protein [Paenibacillus kyungheensis].
ACCESSION   WP_273612419
VERSION     WP_273612419.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 392)
  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 392)
  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 392)
  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..392
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..392
                     /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=44737
     Region          1..226
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
     Region          260..388
                     /region_name="DHHA1"
                     /note="DHHA1 domain; pfam02272"
                     /db_xref="CDD:396724"
ORIGIN      
        1 msailyynds flrewtttiv erreqnnqyf vrleetafyp hgggqpcdtg kineidvldv
       61 vkedeyiwhq vsqlpndnea hcqlnwerrl dhmqhhtgqh llsatalqlf daptlsfhlg
      121 qdmvtididr ksmndtelat leqavnqriy dnlavssyfv naeqlaqlpv vkmpkvtedi
      181 riveiegvey ntcggthvsr tgqigliklf kaekqkgsir iyfkcgaral adyndslhil
      241 ntlatkfntg rkdilerfgk weedqqqlka vleqlrkand tyesnqllsq mqnqqithif
      301 ehktlsdlqr iaatliveqe vtvlfatlse ykvflaqngh phlkcgaffk ehlatfhgkg
      361 ggsdlsaqat ftseadlnaf yefaqqqlhl vr
//
LOCUS       WP_273612477             438 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: WD40/YVTN/BNR-like repeat-containing protein
            [Paenibacillus].
ACCESSION   WP_273612477
VERSION     WP_273612477.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 438)
  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 438)
  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..438
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..438
                     /product="WD40/YVTN/BNR-like repeat-containing protein"
                     /calculated_mol_wt=48262
     Region          103..277
                     /region_name="COG4447"
                     /note="Uncharacterized conserved protein related to plant
                     photosystem II stability/assembly factor [General function
                     prediction only]"
                     /db_xref="CDD:443546"
     Region          327..>438
                     /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 mkltmrkalf iwitlvfvls acqsstsdyd paadkastqe lkkmqtedqg qtltlnhtat
       61 sdtkqggssa ergykiqtrl tdfqllsasa glawgvtrne lriyvtqdsg dtwdnvspaq
      121 tvtfseppty gkdifflnqn ngwvirnasg vgetlilhtt dggqnwnfat lndeatvlgi
      181 yfidssngwv mtsldsskds admqekalyt ttdggntwkk imqntgvfvt egstaqaipq
      241 lgklvgmsfr drnngfvtle qhgtphlyit snggktwktg pdfdknkklp achsfttgkp
      301 qffgdsktag wmnigcvkds qtsyngyfth dagktwnfap falqaqtgvn qsmgptflnd
      361 kigwsvvngi vyrtanqgkt wkalpinntl qntlnkypel vklqffsadv gwllvaknee
      421 rrsllmqttd ggktwhvl
//
LOCUS       WP_273612613             297 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Paenibacillus kyungheensis].
ACCESSION   WP_273612613
VERSION     WP_273612613.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 297)
  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 297)
  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 297)
  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 297)
  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 297)
  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 297)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..297
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..297
                     /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=34756
     Region          43..>107
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <97..293
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          214..293
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnfklnsdak ieplgykpps pysydleifs fselkkrtle grmyityryk fymlicvtqg
       61 ectqwinfep vlcksgtllv vspnqvhnfg kdedwegwii lfrseflipm tstlnehkla
      121 fdierlpkvl tltktelara vhsitrmtad slipeptedv hmllryqlya lmtwlhilhk
      181 nahsmtytql sprfihfhkl veihftewsh vseyahylnc tektltrati eatgitakaf
      241 isarmileak rllvhtdqsi sqiaehlnfk epthfskffk retgctasdf reqtfew
//
LOCUS       WP_273612734             117 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor
            [Paenibacillus].
ACCESSION   WP_273612734
VERSION     WP_273612734.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     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=12927
     Region          10..84
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(14..15,19..21,34..36,45..48,50..51,54..55,57..58,
                     64..66,71..73)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mnqniqqfka dffkalahpm riqilealct gdktvnelqt ivgsegsavs qqlsilrskn
       61 vvqgikegts viyslrdpli qellavakri fdnhlvdais llegmrnepe asrhlek
//
LOCUS       WP_273612776             248 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus
            kyungheensis].
ACCESSION   WP_273612776
VERSION     WP_273612776.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 248)
  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 248)
  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 248)
  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 248)
  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 248)
  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 248)
  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..248
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..248
                     /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=27273
     Region          1..>189
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mkytvitgas sgigyesala faakgknlii varrvdklee lqakikelhp eldvvvvtsd
       61 lsvteqayel ynnlknyqie twinnaglge gamvvdqnlt kvetmlrvni esltilstly
      121 vrdyanvegt qlinvssalg yiiaigtvay saskyyvsaf teglakelel kgahlkakvl
      181 apaitetdfi kvsndvedyq yennipkyht aqqmagfmvn lyesnetvgi vdseynfklt
      241 apiyptis
//
LOCUS       WP_273612777             261 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus
            kyungheensis].
ACCESSION   WP_273612777
VERSION     WP_273612777.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=28419
     Region          1..256
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mkktvlitgv sggigkelan lfakdgynlv lvarneaklq emakdyeqkh gthsivipkd
       61 vsvtgvpeai flelkekgiv vdylvnnagf glygkfletd weqetnmidi nikaltimtk
      121 lfvpdmvkrg qggvmnvasl vgffpgpmms vyyaskayvl sftealenel sgtgvtvtal
      181 cpgvtatgfv drsgmgaskm iqngsimkpd evaqmgyrgf lrgdtiiipg arnrflafsp
      241 rllprkwitr ivrsmqdrag h
//
LOCUS       WP_273612788             106 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: antibiotic biosynthesis monooxygenase family protein
            [Paenibacillus].
ACCESSION   WP_273612788
VERSION     WP_273612788.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 106)
  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..106
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..106
                     /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=12083
     Region          1..>78
                     /region_name="HmoA"
                     /note="Heme-degrading monooxygenase HmoA and related ABM
                     domain proteins [Coenzyme transport and metabolism];
                     COG2329"
                     /db_xref="CDD:441901"
ORIGIN      
        1 mfaimrsitv tegnanqvve rfnqpgilee qpgfvdltil vkqtrkgeee vvllfrwese
       61 eawknweksd ahiqghrqka gqpkpdyiin stngkydika ikkgke
//
LOCUS       WP_273612856             209 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: anti-sigma factor family protein [Paenibacillus].
ACCESSION   WP_273612856
VERSION     WP_273612856.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 209)
  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..209
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..209
                     /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=23610
     Region          1..>57
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 mncreaeelf giyhdlpknd srrqaldrhi eqcpacaaef qiwqesydli qaqveedkas
       61 elimtaeaek inltvmdriy aespwvlqtd rkhgpilrlf rrrlsawilc lfaifvcssl
      121 yltldfsgtf drdaaqervs givptaiats dnatvanssl hfvgsergli dplvipmsps
      181 hpqywmilsv vgmmlallsl rwlakarhs
//
LOCUS       WP_273612868             267 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: CheR family methyltransferase [Paenibacillus].
ACCESSION   WP_273612868
VERSION     WP_273612868.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 267)
  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 267)
  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 267)
  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 267)
  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..267
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..267
                     /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=30541
     Region          9..267
                     /region_name="CheR"
                     /note="Methylase of chemotaxis methyl-accepting proteins
                     [Signal transduction mechanisms]; COG1352"
                     /db_xref="CDD:440963"
ORIGIN      
        1 mlindtihsd pdyvgfikkv kdntgidlsq ykeaqmkrrl ttlrtkngfs tfsaffdaml
       61 kdktlfyefl drmtinvsef wrnpnrwevl rdsilpqlqk nngknlkvws aacstgeepy
      121 tlsmilsdkn llssttlhat diddgaleka kkgmylersl kdvpadvakr hftadghmfh
      181 isdslkkavn frkgnlltdt fetgydlivc rnvmiyftee aknmlyhkfa nslrpggvlf
      241 vgsteqifsp aqygfetset ffyykkg
//
LOCUS       WP_273612749             906 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Paenibacillus kyungheensis].
ACCESSION   WP_273612749
VERSION     WP_273612749.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 906)
  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 906)
  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 906)
  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 906)
  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..906
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..906
                     /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=102537
     Region          66..>530
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          794..895
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; cl38983"
                     /db_xref="CDD:476840"
ORIGIN      
        1 mnlkqarsld eqdrqsfaat htpwdapaek isvqpitass nnmndllaty svnpsyikap
       61 qqyldgnwem vqggeaeqri hqswesvisv pvpgsihqgl vqagilddps fgehaaqakq
      121 yshqtwwyrc tfdiediavf assrlifegv spscdvwlng trlgdhqgaf ggpiydlgsl
      181 lqstntlivq vhpaplgnew niwestvvfn cnygwhyvnl pavgiwrsvr ieaiplvqiq
      241 hpfvqvnsta qakrgeidla ltlasqqsay kgvlygeivp dnfagqsikf qqsiqqdsyl
      301 sepdhvstyy tcdvhlqlti pdahlwspld mgepylyrlq lifipdspai sensmimhnr
      361 ilidqqeitf glryiemkpl psgqqadmyn wtltvndrav fikgsgwctl dalmdfsrer
      421 ydhflsltaq qhtnflrawg ggipetddfy dlcdrkgimv mqewptcwgs harqpqdale
      481 etvrlntlrl rnhaslvmwc ggnetsteld hpaiqmmgry sieldntrpf hrtdpwggst
      541 hdhivwngwt paysfdyyan lggimlsefg lasapnlesv lrympaeeqq qwpplpdksf
      601 yhhlpafdtr delrilsefa dafiicdrle hfvigtqlaq vtslrhkmes archfpaeig
      661 vvtyklndvy igvswatidw ygvpkmshyf tqdayqplla svlfnklnsp hedqslpvyv
      721 lddqgvldqs wsvgvrvydq qlqviqaenw qqegtmpsvh ligtielqqa plaesplliv
      781 seimqgnevk crtfywlnfa drqgvlwnlp qtsltvgqpq askvslldss vdfpyeievk
      841 ntgtlpavgv elynqsddve qsilvasdnf fwldagesrw igvtdhrslh vkawnsytgq
      901 aysqsq
//
LOCUS       WP_273613153             738 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DUF4129 domain-containing transglutaminase family
            protein [Paenibacillus].
ACCESSION   WP_273613153
VERSION     WP_273613153.1
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 11442004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..738
                     /product="DUF4129 domain-containing transglutaminase
                     family protein"
                     /calculated_mol_wt=84703
     Region          377..561
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
     Region          660..726
                     /region_name="DUF4129"
                     /note="Domain of unknown function (DUF4129); pfam13559"
                     /db_xref="CDD:433308"
ORIGIN      
        1 mkkwwngisr swyyslslvw vfiialqwin yadgvwyqet tplvlatmav vaiidilipl
       61 kiiyrliikl favlgtvyyv ldhygfyswq egsltdnvet fvdtvspylw filsawvlie
      121 vsarigssrr aiimfvgtni aalsildsft tsmmweevaw vvfagmgwlv snhfryfqqr
      181 fpkgwkhlrr yplkiifnia vifsiillvg vnvpevqptl kdpytawknw rgeavitvng
      241 snplngqgas sgysredsnl gggfnfdytp vmtvsttsrs ywrgetrtvy sgegwidrss
      301 ngwselqsve agselpldes sdvekktvkq qvkmlsednv typvlfgayt igrvtdvdgg
      361 sdtsqldwrs npgeihwspt rqnrkfpesy slvsrvpiip vkelekktfn qlyadksldq
      421 ylqvpselpd rvrnlakevt asgdtpyekv ellqqylqnn faytnnpdls kkksrdfvds
      481 flfevkegyc dyystamvmm arsldiparw vkgyapgqas gyvtsdyfpd gateytvtna
      541 dahswaeiyf adygwvpiea tpgfdmpmvt etvqtpsddt ptpepeeeeq tpeeeetatp
      601 vqdnepavpt sviwiassvi lawaavmiir yrrelsfmim rmrqgealtp qqkimaeskr
      661 wlawmkrhgm drrsyetlre svsrweevrp dlaaqltpll elfekakysp dqiteeewts
      721 mqhhlqnlrk rwrkratk
//
LOCUS       WP_273613155             318 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: AAA family ATPase [Paenibacillus].
ACCESSION   WP_273613155
VERSION     WP_273613155.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     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=35593
     Region          12..301
                     /region_name="MoxR"
                     /note="MoxR-like ATPase [General function prediction
                     only]; COG0714"
                     /db_xref="CDD:440478"
ORIGIN      
        1 msarkesmqv iaavrsnles cilgksfeie llltallagg hvliedvpgt gktqmikala
       61 ksmsgqyrri qcnpdilpsd itgvsifhpr deqfyfrpgp vmtnillade inrattktqs
      121 allevmeers vtvdgethpl phpfmlcatq npidfegtym lpeaqldrfm mkitlgypde
      181 qternllrhg aagqpvdrle pvtdmqhiad iqqeirnvhl desvsdylvs virhtrehas
      241 vllgasprat lsfmmavkay afiqnrdyvl pddvkklapy viphrilprp earmermsse
      301 rivaqileqi hapvsmgq
//
LOCUS       WP_273613162             122 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Paenibacillus].
ACCESSION   WP_273613162
VERSION     WP_273613162.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..122
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13985
     Region          2..106
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mkdeekvynt avevtlevig gkwkpvilfh ltfgkkrtse lkkliptitq kmltqqlrel
       61 eeagtvlrts ynvvppkvey elteygttlt ellhmmckwg evhlhrqygd qarivespsq
      121 vi
//
LOCUS       WP_273613225             226 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase [Paenibacillus kyungheensis].
ACCESSION   WP_273613225
VERSION     WP_273613225.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            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 kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..226
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25411
     Region          1..219
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
ORIGIN      
        1 mkvcllihgf tggehevspl aeyleaqgyt vkmftlqghg gskadlrnat rldwidsaev
       61 elqqllttyp kihligfstg sliaahlvvk ypnhicsltm lstpvfplnp qqiirtlyqw
      121 pmvkayirnl fvvpskatre fyrivhesft iyphikipal ivqgdqdhlv kmksasylae
      181 higtpdtrvi ivpksghlvc yaerksdffa avqvwidthh ftspqs
//
LOCUS       WP_273613335             456 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidase U32 family protein [Paenibacillus kyungheensis].
ACCESSION   WP_273613335
VERSION     WP_273613335.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            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..456
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..456
                     /product="peptidase U32 family protein"
                     /calculated_mol_wt=51644
     Region          18..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 msttekpkyy gkrhrlakpe llapagnlek lkfaihygad avyiggqkyg lrsnadnfsf
       61 eemregvefa nrygakvfva tniyahdedi agleeylckl eevgisaviv adpaiietal
      121 rcapglevhl stqqstlnwq avkfwkeegl prvvlgrets faeiaeikkh vdveieafih
      181 gamcssfsgr cvlsnhftdr dsnrggccqs crwkydlfed arseqewvse edaadqqmlq
      241 qfslgvnqkp lyeeqdsafs mgskdlcmle hipslievgv dsfkiegrmk sihyvatvvn
      301 ayrqaidsym adpenyvlkp ewledinkaa nrplntgffy dtpdhedhiy eaeekavpyd
      361 faglvldyde atgiatvqqr nhfkpgqqie ffgpnqmffk qtvgqlwdea gheldaarhp
      421 lqkvkmkvdh pvryfdmmrk nntkqakqav katvtv
//
LOCUS       WP_273613353             724 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: RelA/SpoT family protein [Paenibacillus].
ACCESSION   WP_273613353
VERSION     WP_273613353.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 724)
  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 724)
  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 724)
  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 724)
  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 724)
  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..724
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..724
                     /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=82824
     Region          1..724
                     /region_name="SpoT"
                     /note="(p)ppGpp synthase/hydrolase, HD superfamily [Signal
                     transduction mechanisms, Transcription]; COG0317"
                     /db_xref="CDD:440086"
ORIGIN      
        1 mgierlleka sayikekdlh rireayefad qahhgqvrks gepyilhpla vadivvgmem
       61 dtisiiaall hdvvedttvs ldeirtrfgd ncamlvdglt klerikfrsk eeqqnenyrk
      121 mfiamaqdir vivikladrl hnmrtlkyqs eesqrriaye tleifcpvah rlgisaikwe
      181 medialryln pqqyyrianl mhkkraereq yidnvigrin eklsemgvea dlsgrpkhiy
      241 svyqkmtikn kqfneiydll airiivdnik dcyatlgiih tlwkpmpgrf kdyiampktn
      301 myqslhttvv gpngeptevq irtwdmhrta efgiaahway kegttgtien kvpffkeile
      361 lqheakdase fveslkmdff sdlvfvftpk gevielpigs vpldfayrih tevgnrtiga
      421 kvngrivpld hrlktgdiie iltskhsygp sqdwlkiaqs sharskikqw fkkekreenv
      481 ekgrdalere ikrlnlepsv wltddklvev gkkfafhdse dmlsaigfgg itaaqvctrl
      541 teklrkeqee saiielseqv kevktapeek rprptngvsv kgidnllvrf arccnpvpgd
      601 divgyvtrgr gvsihrsdct nvpdvsdnse aariievgwe navesnysvd ieitghdrrg
      661 llnevlqtva enktnisavs grsdknkmam ihmtilirnt dhlqsvvdki kriqdvytvh
      721 rimq
//
LOCUS       WP_273613346             713 aa            linear   BCT 28-DEC-2024
DEFINITION  HelD family protein [Paenibacillus kyungheensis].
ACCESSION   WP_273613346
VERSION     WP_273613346.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=82065
     Region          1..710
                     /region_name="HelD"
                     /note="DNA helicase IV [Replication, recombination and
                     repair]; COG3973"
                     /db_xref="CDD:443173"
ORIGIN      
        1 mednfqsayq eeqdklqqtv veideqlerl sqipvytghd fteqilesgr eqqrqslsks
       61 aqapyfgrld faegeegtrq plyigkigvg ksevedqplv idwrapvasl fysftggeea
      121 avyeapegli qglvylkrni vihqrmlerl adtydreste pavtdeflvy rlgenkdnkl
      181 rdivstiqae qdriiraakn talviqgvag sgkttvalhr lafllyqyqe qvsadkmiif
      241 apnhmfldyi sevlpelgvg diqqstfsdw aqqilesdir lvpqsetyey wfenadrpav
      301 tdhtpsrykg slafmqlire yvnvleqtav peldfnpwde avlsqqeile wfnneykhyp
      361 lakrkervma rvhrwiemql kvapseairk erkkkaaqre kaylnkwpky eplslykqlf
      421 kaiksgnhae alqsiweqip advlkqvste lkkdriredd lpalvyihtl lhemeaehrf
      481 dhvvmdeaqd fspfhvalld lyvrgssfti lgdlsqgiha yrgvhqweei sdlftpeqtd
      541 yfpltrsyrs tmeiiefani ilekgvqngi tavpvfrsgd pvrmipcstd trletiranw
      601 qqlqtkdyrt tailtrtlhe aielhqqlte qgieihlidg gkaayqgghs ilpvylskgl
      661 efdavivsdv dtdhyrndaw dakllyvgct ralhelwimh gqqipeyits dte
//
LOCUS       WP_273613446             571 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 13 protein [Paenibacillus kyungheensis].
ACCESSION   WP_273613446
VERSION     WP_273613446.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 571)
  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 571)
  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 571)
  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..571
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..571
                     /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=66986
     Region          7..475
                     /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(60,63,100,103,144,163,167,199,256,417)
                     /site_type="active"
                     /db_xref="CDD:200472"
     Site            order(199,256,332)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200472"
     Region          482..554
                     /region_name="Malt_amylase_C"
                     /note="Maltogenic Amylase, C-terminal domain; cl02706"
                     /db_xref="CDD:445893"
ORIGIN      
        1 mirkwwkena iyqiyprsfk dsngdgigdf qgiiskldyl qelgigaiwl cpiyespnfd
       61 ngydisdfqa imkdfgtmqd fdefmreahe rgikvvldmv lnhtsdkhdw fvesrssldn
      121 pkrdyyiwrk gknggypnnw esyfsgsvwe ydqeteeyym hlyarqqpdl nwenkevvne
      181 lhdmirwwmd kgvdgfrlda iahivkavgl pdadnpqnlp vvqafqffsn lekvhtllkd
      241 lnqqvfatrd lmtvgetsgl gpeqaleyvg nerheldmvf qfehmhldcv gtgsskwvgr
      301 swnlldikki mshwqtvlhg kgwnanyfsn hdqprhlsrf gntgeyrkqs akmlatlihl
      361 lqgtpyiyqg eeigmtnasf qhiedyrdve tinyynislk egkteeeilk nlarrsrdna
      421 rtpmqwdntt hagftdgnpw iqvnsnytdi nveqalndpd sifyyyksli alrkkypvvi
      481 ygdyrllcal hhqvysfirs yegtelmvim nffddkptfe lserisdegw elvlsnyddh
      541 ehhqlhslpl rpyetrvyyk dtpsvlpkst h
//
LOCUS       WP_273613521             681 aa            linear   BCT 28-DEC-2024
DEFINITION  peptidoglycan D,D-transpeptidase FtsI family protein [Paenibacillus
            kyungheensis].
ACCESSION   WP_273613521
VERSION     WP_273613521.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 681)
  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 681)
  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 681)
  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 681)
  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..681
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..681
                     /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=75903
     Region          39..654
                     /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 mnfnkspahe neqdknrkqf airlnifffi tfivfsiivv rlaiiqfveg pelrkvaegd
       61 ivkevpllpt rgtiydssmq piayseptqs lyltldkdyn rsdrtqeakq larklqkifd
      121 qygdpntkal ttvdifkamd ttyakangyt prriktglsn keiayflerr nefkgieive
      181 enirhydtdt vavqtvgylr pfvssmsrnk ykniqrnsse dpamkysaie nvgfdglell
      241 yqdelrgksg yrrvpinpkn masgptelip pvkgsdlvlt inkeiqvate kaitehtaki
      301 rysgtrgvsa pnavtgyava meidtgkvvt masmpdydsn iwskdtrtes ewkniepyym
      361 ngairsvnrp gggdhpssvv llgstmkpls vliglneklf tlgdryndhg ittlgkegyg
      421 tkvrnassra ygtlspigai shssntfmvd mvgkrlyqky egkpgvevwd kymeqfglgv
      481 stesglaaey igykeyihem esgsaqsala yasfgqqgky ttlqlaqyta mlanrgerlk
      541 pqfvneirna dgkvtkkfkk evlnkvdlps qywdavqsgm qsevdafkgf pydyrrktgt
      601 sqqrmatgkt ienavfiaya paqnpklava vvvpeggyga qgaapiarqi feaydqqygl
      661 dgipkkkpiv easgeidspi r
//
LOCUS       WP_273613531             334 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Paenibacillus kyungheensis].
ACCESSION   WP_273613531
VERSION     WP_273613531.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=35208
     Region          27..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 mnriksiqvs glflvaliil vlsifmavsy gakslpiatv wdavfhydst vtahqivydi
       61 rlprvlgavf tgmafavaga lmqgvtrnpm adtgilgvna gaafvvalcf aflpqlaysy
      121 lmllsfvgaa lttllivvla sftpgglnsl kltvagavia amlhslstgi alyfglsqdl
      181 afwyaggvsg vtwehlhlli pivvviiiwi itmgrsisfl algdetavnl girtksvkvl
      241 amiaavilag asvavagsis fvglviphit rrwigvdyrv vipfsallga illvwadfas
      301 rmvsppqefa igamvalvgv pfflylarke grgl
//
LOCUS       WP_273613556             164 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus kyungheensis].
ACCESSION   WP_273613556
VERSION     WP_273613556.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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 11418877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=18612
     Region          65..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 miqkcvledd ntvqqiwalq hiayrleael igfkelpplm dtvesirrsg etfyayvney
       61 eeiqgvisie qeehdtltia rmmvhpiafr qgiasqlieh vfaqypnvpl yivstgklnq
      121 pavalykkyg fcpvetfeva pgvklttfhr lnpalsqvre dsvd
//
LOCUS       WP_273613618             326 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ABC transporter permease [Paenibacillus].
ACCESSION   WP_273613618
VERSION     WP_273613618.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 326)
  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 326)
  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 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   5  (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
REFERENCE   6  (residues 1 to 326)
  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 326)
  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..326
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..326
                     /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=37154
     Region          10..326
                     /region_name="LplB"
                     /note="ABC-type polysaccharide transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4209"
                     /db_xref="CDD:443357"
ORIGIN      
        1 mdtttkrass nkgervsktt ikrgggfwkv fkqqrylylm slpfviwafi fsyvplwgwt
       61 mafqnfkpak sffdqkwvgf dqftalfadq qfylalrntl amsfmglifg fvvpvifail
      121 lnevkgmffk rtvqtvsylp hfvswvvvag ivtkslstdg givnellvsm hiidqpiqfm
      181 aqgkwfwgiv tasdiwkemg wntiiylaai tgidqeqyea srvdgagrfr qmwhitlpgm
      241 rttitvllim sighlvsigf ekqfllgnnl vqdysqvldl yalkyglemn rysygtaisi
      301 fnsvisiill ftangifkkt tkesim
//
LOCUS       WP_273613716             431 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: murein hydrolase activator EnvC family protein
            [Paenibacillus].
ACCESSION   WP_273613716
VERSION     WP_273613716.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 431)
  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 431)
  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..431
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..431
                     /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=46380
     Region          8..431
                     /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 mkkvasvmav illavsviqp qqvhaaksvs diqsqlnave kkaqeaaqqk kkaaaqkkks
       61 qmlkartqkd lgkvlqaine vssqlarvss disqtesglr qakkdlaetk eriharegmi
      121 dtrvrmmytd glisymdvlm astnfsdfve radslrmivd qdqdilaqhe kdkqfvivtq
      181 kkltasyaka kslyaekaer kgeldakene kqvliskynt qienaddits eqeqalwdla
      241 dkraslyqek taleaqeraa aaaraaaeaq araeaaannp pssddgggyt ppstggyqgs
      301 gngsmglpvn garisspfgy rnhpiqgvyk lhtgvdfaap qgtdihaaqg gtvvvaqwqn
      361 gygntviidh gngiktlygh irdggiavsv gqtvsqgqki aevgstgnst gphchfevrv
      421 nntpvdpmgy l
//
LOCUS       WP_273613807             121 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DMT family transporter [Paenibacillus].
ACCESSION   WP_273613807
VERSION     WP_273613807.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     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=12782
     Region          4..103
                     /region_name="EmrE"
                     /note="Multidrug transporter EmrE and related cation
                     transporters [Defense mechanisms]; COG2076"
                     /db_xref="CDD:441679"
ORIGIN      
        1 mnrnwlyvli ggcievvwvs glkhaatpfe wlltavgiai sfyliikast rlpvgtvyav
       61 ftgigtagtv aaemiifgep fhwlkvilil vlmigvaglk lvtdngakee ahsatvkage
      121 a
//
LOCUS       WP_273613827             138 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus kyungheensis].
ACCESSION   WP_273613827
VERSION     WP_273613827.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=15461
     Region          61..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 mhiqelsldh nvpqigvfld qhnmnndlhi pdyesipfsl aayegeqyig gvtgamawgl
       61 lyirylavdp ayrgqgvgak llqaiedqar qqgatiselt tmswqaphfy mkygyvifge
      121 ikdipikgqs kiylqkkl
//
LOCUS       WP_273614032             302 aa            linear   BCT 28-DEC-2024
DEFINITION  serine/threonine protein kinase [Paenibacillus kyungheensis].
ACCESSION   WP_273614032
VERSION     WP_273614032.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 302)
  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..302
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..302
                     /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=35205
     Region          25..>291
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 mkalqriqgh imrwiqerhf aegqlihery kicrrlgkgs ygvtylcedi qtaqtcvlkr
       61 vyplrgghvr aqliyerecr amsaidhpsi pslldtfqyh hyhclvmeyi eghnvgewif
      121 eqgltftelq slqwikqlve vvtvihqqgw vhrdislsnv iyhqhkvyli dlglmwqqge
      181 gtadvallde lvsgdqeekr irraldvtsd fyglghlllf llysyeeegn shssltdrqe
      241 rsweeelqlh prthqmirkm llvapeqpyq hideiaqaid riitdleslp annstypnip
      301 pv
//
LOCUS       WP_273614128             317 aa            linear   BCT 28-DEC-2024
DEFINITION  serine hydrolase domain-containing protein [Paenibacillus
            kyungheensis].
ACCESSION   WP_273614128
VERSION     WP_273614128.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 317)
  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 317)
  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..317
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..317
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35294
     Region          46..314
                     /region_name="AmpC"
                     /note="CubicO group peptidase, beta-lactamase class C
                     family [Defense mechanisms]; COG1680"
                     /db_xref="CDD:441286"
ORIGIN      
        1 mklidtaplv sqlterelys clivqqgvqi ldyyrepdqk evplkinsct ksilsslvsi
       61 aidqgimpap dtaistffpq lhqdpdprka qitieqlltm sagfnwtefg gqhsfptmsk
      121 tsnwiefvls qplvhepgtv meynsgcsql latilartsg qsvasfaeqh lfaplginhy
      181 iwetdpqgvh tggfglqlpp aamlqfglly lhegkvngks liqsstvrha tspliavdsp
      241 qkahygwhww hssftldsqp kvdipyyyal gfggqyivvv psyelvvtvs adrfkrkrtp
      301 ldvfrdfvvp lleeqdv
//
LOCUS       WP_273614138             329 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Paenibacillus kyungheensis].
ACCESSION   WP_273614138
VERSION     WP_273614138.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 329)
  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 329)
  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 329)
  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 329)
  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 329)
  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 329)
  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..329
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..329
                     /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=38560
     Region          9..325
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mklflkehal liviqiiqfs avmsiywldg yrnvgpalys imlglfflgg ylcyqyysrr
       61 hyyrrlqepl lslddsvqql dqapvseale qllrqqyryy qqrlatinqq qqehltfmnq
      121 wvhqmktpls vieltvqdvd epefasiree lermssglnt ilymarlrtf eqdfhirsis
      181 lsevirevvq ehkrlfirnq vypdvkikdg dlwtesdqkw lffmvsqlvv navkysahtn
      241 nkvilssyiv ghqavievqd ygvgipasdi krvfepfftg engrhfrest gmglylthea
      301 aqrldhqlel estvnqgttv rilfpsyqr
//
LOCUS       WP_273614158             585 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 35 protein [Paenibacillus kyungheensis].
ACCESSION   WP_273614158
VERSION     WP_273614158.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=66086
     Region          10..324
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
ORIGIN      
        1 mntfevvgnd fvyngqpmrl lsgaihyfri vpeywedrll klkalglntv etyipwnlhe
       61 pqegffdftg iadvvafiql agslglhviv rpspyicaew efgglpawll adqnmrlrsy
      121 disyldkvda yydvllpllq pllctkggpi iamqieneyg sygndtaylq yiqeamvirg
      181 mdvllftsdg pedfmlqggm vpgvlatvnf gsnatsafak lkqyqpdapl mvmefwdgwf
      241 dhwmephqtr saqdtaetvd dilryeqasl nfymfhggtn fgfynganhi kqyeptvgsy
      301 dygallneqg qptdkffavr evlgeyidlp alelpvpipt anygtvtlhe yspllqnldv
      361 lttaihsssp epmeklgqay gfilystivk gsrtemelvl qqvsdraivy vdetyqgiie
      421 rwtpsnlple vpeqgirldi lvenmgriny gpylrdpkgi tegvrhgnaf lydwtiyplp
      481 lhslsdliyt qtetlsapld qpafyrgifh vqspadtflr vdgwvkgvvf lngfnlgryw
      541 qvgpqktlyi papllkqgdn elilfelhgy kqlqvqlvdt adlgq
//
LOCUS       WP_273614165             105 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor
            [Paenibacillus].
ACCESSION   WP_273614165
VERSION     WP_273614165.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     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=11745
     Region          6..94
                     /region_name="ArsR"
                     /note="DNA-binding transcriptional regulator, ArsR family
                     [Transcription]; COG0640"
                     /db_xref="CDD:440405"
ORIGIN      
        1 mkileatrpt piklvdvfsa lsdpvrlkil lclahhgeks cagfqmshis kstlshhvki
       61 lretgliqlr idgrqhfyri cqseldtqfp gllasilqte ekdll
//
LOCUS       WP_273614182             265 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Paenibacillus
            kyungheensis].
ACCESSION   WP_273614182
VERSION     WP_273614182.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29467
     Region          53..160
                     /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 messqqnkna wnngtyqswv nrfgtpeeaa ekikqdpqkr igtafkhmed hiqgkkiinl
       61 lgsngnkava lallgaelti vdfsaeneqy aqdlaraagv plqyivsdvl qlplqelanq
      121 ydivfmefgi lhyftdlqpl cyvvssllap ggqlvlqdfh pistklitsk gttanirkhk
      181 vtgdyfdtsl tekavsysky tesdqqikde qkvylrqwti geivtavats glmikvleel
      241 pnqssevfdk gipktftiva qqlhv
//
LOCUS       WP_273613252             139 aa            linear   BCT 28-DEC-2024
DEFINITION  integrin alpha [Paenibacillus kyungheensis].
ACCESSION   WP_273613252
VERSION     WP_273613252.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Demetriou,M.C. and Cress,A.E.
  TITLE     Integrin clipping: a novel adhesion switch?
  JOURNAL   J Cell Biochem 91 (1), 26-35 (2004)
   PUBMED   14689578
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Humphries,M.J., McEwan,P.A., Barton,S.J., Buckley,P.A., Bella,J.
            and Mould,A.P.
  TITLE     Integrin structure: heady advances in ligand binding, but
            activation still makes the knees wobble
  JOURNAL   Trends Biochem Sci 28 (6), 313-320 (2003)
   PUBMED   12826403
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Hynes,R.O.
  TITLE     Integrins: bidirectional, allosteric signaling machines
  JOURNAL   Cell 110 (6), 673-687 (2002)
   PUBMED   12297042
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Bokel,C. and Brown,N.H.
  TITLE     Integrins in development: moving on, responding to, and sticking to
            the extracellular matrix
  JOURNAL   Dev Cell 3 (3), 311-321 (2002)
   PUBMED   12361595
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Arnaout,M.A.
  TITLE     Integrin structure: new twists and turns in dynamic cell adhesion
  JOURNAL   Immunol Rev 186, 125-140 (2002)
   PUBMED   12234368
  REMARK    Erratum:[Immunol Rev. 2003 Jun;193:146]
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Albelda,S.M. and Buck,C.A.
  TITLE     Integrins and other cell adhesion molecules
  JOURNAL   FASEB J 4 (11), 2868-2880 (1990)
   PUBMED   2199285
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Hynes,R.O.
  TITLE     Integrins: a family of cell surface receptors
  JOURNAL   Cell 48 (4), 549-554 (1987)
   PUBMED   3028640
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448538
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..139
                     /product="integrin alpha"
                     /GO_component="GO:0008305 - integrin complex [Evidence
                     IEA]"
                     /GO_function="GO:0005178 - integrin binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=15171
     Region          1..14
                     /region_name="Integrin_alpha"
                     /note="Integrin alpha cytoplasmic region; pfam00357"
                     /db_xref="CDD:459778"
ORIGIN      
        1 mgffkrnkke qdhmeqadqa mskglsglfm ktivpkeqrd qinaslemar qaqssasgqi
       61 pitataqvis vkdtgklvnf dpiiilvldv tenngtryqk tletmvskmh iprpgdhigl
      121 gihpsspanf iymgiisss
//
LOCUS       WP_273614255             343 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease
            [Paenibacillus].
ACCESSION   WP_273614255
VERSION     WP_273614255.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     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=36183
     Region          11..341
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 msqsaiefiq agrrqrhrrw llvtgllgil avvlccamlv lgntiypled vlralsgeki
       61 kgvsfavsti rlprmlaglf agfafgvagy tfqtilrnpl anpnvigits gasaaavfci
      121 vilhannavi smasviaglm tvifiyilsr gkvfsigrli lvgigiqaml davisyllli
      181 saqqdipsal rwltgslngs qmrelpplii ivligaplim glskhlsile lgeqsafslg
      241 vntdmtrivl ivssvcmvai atattgpiaf vsflagpiak rlvgvgssni lpaglvgvnl
      301 vlaadligqf afeyrfpvgi itgllgapyl ifllirmnqk gel
//
LOCUS       WP_273614193             342 aa            linear   BCT 28-DEC-2024
DEFINITION  CdaR family transcriptional regulator [Paenibacillus kyungheensis].
ACCESSION   WP_273614193
VERSION     WP_273614193.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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 20544506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..342
                     /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=39191
     Region          4..128
                     /region_name="Diacid_rec"
                     /note="Putative sugar diacid recognition; pfam05651"
                     /db_xref="CDD:461704"
     Region          73..333
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mfqlseqqaq eivdkmmadi pyninimneq giiigsgerh rvgtihqgav ealsigkmie
       61 irtareyekq gtnepivinq qyvgvigitg hpdevrpfcn ivrttvtlli eqriafekqt
      121 yennrkkafs dlllhyagty sqkikkeats yhidllvktt vlyiksfqrq edqpsnwlpy
      181 pwfeidedsy vvliqdpani spcistlysh hpeqwiavgt shtniatsyq qarsamtlll
      241 slrpstqiih ydevafiaqw shtelmqtgn svtklegysd lldtlrsfie hncnmsdtai
      301 hlnihrntlq yrlkkiqqvt gkdprqllhl ieliyglisl yk
//
LOCUS       WP_273614269             239 aa            linear   BCT 28-DEC-2024
DEFINITION  SDR family NAD(P)-dependent oxidoreductase [Paenibacillus
            kyungheensis].
ACCESSION   WP_273614269
VERSION     WP_273614269.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            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 kyungheensis"
                     /db_xref="taxon:1452732"
     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=25949
     Region          1..>187
                     /region_name="YqjQ"
                     /note="Short-chain dehydrogenase [General function
                     prediction only]; COG0300"
                     /db_xref="CDD:440069"
ORIGIN      
        1 mknfivfgas kglgeafvng lpekgdrvwv vsrtypnsld vedgiekhwi eadlakpdas
       61 tliantlndv tidvliynvg iweskgfrdd ynfenddpae ianiininvt stitciqkll
      121 pnlkksdnak ifligstagl ehndftqvsf taskfglrgi gnsirehvkk ygigvtcinp
      181 geiatqiple dgiekvlsty ggtqiplqdl vslvkcvmnl skascvkein mpamldtng
//
LOCUS       WP_273614430             378 aa            linear   BCT 28-DEC-2024
DEFINITION  threonine aldolase family protein [Paenibacillus kyungheensis].
ACCESSION   WP_273614430
VERSION     WP_273614430.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            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 10005169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..378
                     /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=42664
     Region          53..329
                     /region_name="GLY1"
                     /note="Threonine aldolase [Amino acid transport and
                     metabolism]; COG2008"
                     /db_xref="CDD:441611"
ORIGIN      
        1 myntpesass kqpsltlrea faqteyilpg hsdrninvlq qafadidgdl ssdqygrgqv
       61 iedfqkqmad vlgkesavff ptgtmaqqia lriwcdrhns akvayhplch leiheedglk
      121 elhhiqsill adqdrlitla dvkqmdqdia clllelpqre iggqlppyse lqaiseycrk
      181 qgisihldga rlfeilpyyq ktaaevcalf dsvyisfykg iggiagaila gpsdftaesk
      241 vwkrrhggdl islypyilss kyyyeqrvgn meqyykeavq laqwmnkcta ihtlpevpvs
      301 nmfhihfelp keqiepilie mcqatgvgiv qyltdkkega hcstelviga ryehvpqdri
      361 qkalawldqr lkevtanq
//
LOCUS       WP_273614549             290 aa            linear   BCT 28-DEC-2024
DEFINITION  substrate-binding periplasmic protein [Paenibacillus kyungheensis].
ACCESSION   WP_273614549
VERSION     WP_273614549.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..290
                     /product="substrate-binding periplasmic protein"
                     /calculated_mol_wt=31189
     Region          63..288
                     /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 mkslrrtstp ivwamllmvv lsacgnaapr statdpasnt saettatats gntleaiksa
       61 gvlkvglmgt yapynflnan kevdgfdadi akevakrlgv kaefttqafs glipslqagk
      121 fdaiisqvti tderkqqldf sdpyitnqvk iivnanntdi tkladfkdkn igvglgtnde
      181 tylrtevlpq vgnfniktyn dvitslqdln vgridatinn iyalkpivee ngfkikavgd
      241 aiksdqagia irkdnpdllk alnkaltdmk adgtyetifv kwfgekpaae
//
LOCUS       WP_273614777             330 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD-dependent epimerase/dehydratase family protein [Paenibacillus
            kyungheensis].
ACCESSION   WP_273614777
VERSION     WP_273614777.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=36543
     Region          3..329
                     /region_name="WcaG"
                     /note="Nucleoside-diphosphate-sugar epimerase [Cell
                     wall/membrane/envelope biogenesis]; COG0451"
                     /db_xref="CDD:440220"
ORIGIN      
        1 mtkalitgat gflgghmarr lvelgwdvtg tgrdrsrgqa lehlgvqmny yelgdaeqtr
       61 qackgqhvvf hcaalsspwg tyssfyrsnv eatqhivdgc iehdverlih vstpsvyfdg
      121 kahygiresd plprkavnhy astkllaeqi vqqayqkqgl psmmirprai fgpmdqtlfp
      181 rlleanrqsg vpllqggrap idltyvdnva damllgvqap enalgqayni sngepipfie
      241 lltrlfqrld iplhtrrvpy pvahavagtm emvyrlipal geppltrysv gsiavphtld
      301 islaqqqlgy vprisvdegl erfadwwceq
//
LOCUS       WP_273614817             279 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Paenibacillus].
ACCESSION   WP_273614817
VERSION     WP_273614817.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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 10054599
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..279
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33064
     Region          12..79
                     /region_name="HipB"
                     /note="Transcriptional regulator, contains XRE-family HTH
                     domain [Transcription]; COG1396"
                     /db_xref="CDD:441006"
     Region          <118..>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          162..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(163,166..167,170..171,173,204,207..208,211..212,
                     214..215,244,247..248,251..252,255)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          202..232
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          243..268
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvsqtvldyr wigqrireir qqrgltqqql algicnqsqi sriekgvesv saeilfqiah
       61 kfsldiriff dmteqqinei qsirkniryl qkkhmyqell qyiedhqvea icryslmdqq
      121 fvlyqkgnay vhlgavdrgf pmiqlalklt yhceripaly eieviqalai aygfdgdyra
      181 cigwlhkclr alhvyregsd qftpifyyls kaysdtqdyr maieyatqgi rycenhkigy
      241 yldqlyyecg ysyeqigqqf kaeqcytkfq llqdlfcty
//
LOCUS       WP_273614931             526 aa            linear   BCT 28-DEC-2024
DEFINITION  ArnT family glycosyltransferase [Paenibacillus kyungheensis].
ACCESSION   WP_273614931
VERSION     WP_273614931.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 526)
  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 526)
  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 526)
  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..526
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..526
                     /product="ArnT family glycosyltransferase"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60717
     Region          82..>288
                     /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 mlkgiqktfy flliffvslf iassffiraq ynyvvygdtp mlqqqhlgtf llliigllif
       61 svimyrlclk lnkyrpqivi plvllcscai qvviiflftr lptddsqtvv slamnmlykg
      121 dystfnqtgy lhmfpfnyst vlyieallam fpdnyvtikv anivfalitt lmiyliykql
      181 trnsrshdyg vlvfaatylp alfmsnfiyn dviattllts alyfgirfmk eksvkylifa
      241 ailvtignyf rsigiiflla ivislllhmk qigwkkvvls lclfavlfni pswtqnallq
      301 atgkvqastt tnaapiymwl nmginlktfg fwdnresyni yqrdadynka lstelfkesi
      361 aqklstaslt dlvtmyykki iwtwtegtyq ierygigndg ssggsrtgfi mggysyptfa
      421 telfadnspy rsgilwllyt mnflmycfil irligslrak rfdemslilv ilgfvgfyil
      481 weiksryiyp vyplliilsy mgfkdtyqwl irqdflrlrt svrees
//
LOCUS       WP_273615075             270 aa            linear   BCT 28-DEC-2024
DEFINITION  transglutaminase-like domain-containing protein [Paenibacillus
            kyungheensis].
ACCESSION   WP_273615075
VERSION     WP_273615075.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 270)
  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 270)
  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..270
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..270
                     /product="transglutaminase-like domain-containing protein"
                     /calculated_mol_wt=29388
     Region          <135..243
                     /region_name="YebA"
                     /note="Transglutaminase-like enzyme, putative cysteine
                     protease [Posttranslational modification, protein
                     turnover, chaperones]; COG1305"
                     /db_xref="CDD:440916"
ORIGIN      
        1 mkkllltclt aftlisfapt htyaatppat dswldtstvs egfiavhyna pshtrtklmi
       61 skndvnytyd lnstqtdssf plqlgngtyn vtilentsgn sykkvqgdsl emnlnnenav
      121 ylastqnvdw knataliska qqltknattd tekaqaiydy ittnvkydyk fasalpavyv
      181 pdaattlvsn kgicydyasl naamlrsvgv ptklvmgtst nvkeyhawne vllngqwvtv
      241 dttvdatlkq sgktttlakd aaaykavkty
//
LOCUS       WP_273614432             220 aa            linear   BCT 28-DEC-2024
DEFINITION  peptide-methionine (S)-S-oxide reductase MsrA [Paenibacillus
            kyungheensis].
ACCESSION   WP_273614432
VERSION     WP_273614432.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Lowther,W.T., Brot,N., Weissbach,H. and Matthews,B.W.
  TITLE     Structure and mechanism of peptide methionine sulfoxide reductase,
            an 'anti-oxidation' enzyme
  JOURNAL   Biochemistry 39 (44), 13307-13312 (2000)
   PUBMED   11063566
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Lowther,W.T., Brot,N., Weissbach,H., Honek,J.F. and Matthews,B.W.
  TITLE     Thiol-disulfide exchange is involved in the catalytic mechanism of
            peptide methionine sulfoxide reductase
  JOURNAL   Proc Natl Acad Sci U S A 97 (12), 6463-6468 (2000)
   PUBMED   10841552
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483118
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..220
                     /product="peptide-methionine (S)-S-oxide reductase MsrA"
                     /EC_number="1.8.4.11"
                     /GO_function="GO:0008113 - peptide-methionine (S)-S-oxide
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0033744 -
                     L-methionine:thioredoxin-disulfide S-oxidoreductase
                     activity [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=25718
     Region          17..148
                     /region_name="PMSR"
                     /note="Peptide methionine sulfoxide reductase; pfam01625"
                     /db_xref="CDD:460270"
ORIGIN      
        1 mstqhteyrs qsdeqltlam gcfwspealf gqftgviqta tgyaggttsh ptyrelgdhs
       61 esiemtfhpq eisleqllcc fwdnhrpdai ngykgrqyms ilfyrnqqqy evilrvqqqy
      121 apeslsteiv pytdfteaee rhqkyylqrk pelfkgwvdh lgnhenlfhs tigtrlnals
      181 kghmtwadii kewenkelqh vakrqrhnil ewiqqsstnd
//
LOCUS       WP_273615098             309 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix domain-containing protein [Paenibacillus
            kyungheensis].
ACCESSION   WP_273615098
VERSION     WP_273615098.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (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   2  (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   3  (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 11454391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..309
                     /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=34992
     Region          56..300
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mstsfippew gqslaetifp dvqttmnlfg ihlrtvstdw qypihdhpqy einyvlegqq
       61 lmtvgsqsyv qqngdlmilp pgtshssrti egqsftyfci hfdiddrlfl sllerlnqvm
      121 fkqssavaqa mqpyllkian pieqtdehii trrmhlqaav felfgvlwea isneaaglap
      181 asyahvemah qiaarlqgia nrniaqleat sdshygiddi aaelgispsh cnrifhqvfa
      241 isprsylsnl vlhkskllls dqrmsiqdia silgyrdiah fsrqfkrwsg ispshyrknq
      301 mmmpsewka
//
LOCUS       WP_273615119             423 aa            linear   BCT 28-DEC-2024
DEFINITION  sulfotransferase family protein [Paenibacillus kyungheensis].
ACCESSION   WP_273615119
VERSION     WP_273615119.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 423)
  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 423)
  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..423
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..423
                     /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=49272
     Region          10..212
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
     Region          <283..>387
                     /region_name="mukB"
                     /note="chromosome partition protein MukB; PRK04863"
                     /db_xref="CDD:235316"
ORIGIN      
        1 mierngnkli fllcvprsgs slatvmlqnh triyaaqemw flmslydlkk pekrayggta
       61 ilnqffdgvl pesvydeacr sfgmnvyngl lstseadmvv dkspryyyll efldrlfpqs
      121 kriglfrnpl dvaasykkvn qrsapnfnla dqlndpslnm kmvditvglf ryhqyfsqsn
      181 nnafwlkyeq maahpeeqmq kvcefldisy eegiekygdy mdsakselfy smgvgdpyls
      241 ehrtphmksi gnwrtmldhr eieaycrilg arlfrelgyg aeleeaqrlt gvvfeeepdm
      301 kwieaktkqf aeatgcrwep eykmqsavlp etspevasal sqeskekaea dellrmrmtl
      361 rslekrmeqh yierdrlhqe serlrkevkd mkqkmnkiks lipfnrslgr vfnaylvrkg
      421 vek
//
LOCUS       WP_273615173             318 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Paenibacillus
            kyungheensis].
ACCESSION   WP_273615173
VERSION     WP_273615173.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=37632
     Region          1..318
                     /region_name="YobV"
                     /note="Predicted DNA-binding transcriptional regulator
                     YobV, contains HTH and WYL domains [Transcription];
                     COG2378"
                     /db_xref="CDD:441945"
ORIGIN      
        1 mnknerliqq miyintkkhf nlsdlietfn isrstalrdi asleqlgvpl ysekgshggy
       61 rvltnsllpp iyfntnelhs iffslqllkg lvktpfqqny qeiktkllat lpdkhkqqma
      121 qaeqwiqwig veqqqevpwi velfaaivgr qvieiqynry qqdkriiqpl rlsiwdgywy
      181 clswdrnkne frnfrcdyie elhitdqqgt ewtaeqihtl anqqfdiqrp lsfqvkvdlk
      241 giehfykkry snmslqqvdt gndsenkehy ivgtfgehei sflveyflgf gqhieivspp
      301 llrteyqqyv kkilaqye
//
LOCUS       WP_273615364             453 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: sensor histidine kinase [Paenibacillus].
ACCESSION   WP_273615364
VERSION     WP_273615364.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     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=51161
     Region          20..>245
                     /region_name="ArsS_fam_HK"
                     /note="ArsS family sensor histidine kinase; NF038389"
                     /db_xref="CDD:468500"
     Region          135..442
                     /region_name="WalK"
                     /note="Sensor histidine kinase WalK [Signal transduction
                     mechanisms]; COG5002"
                     /db_xref="CDD:444026"
ORIGIN      
        1 mktirgkmll slcvgmlmtv aitvfffvql mddillnqvk qqlsaqtika ahilkdqdid
       61 gldstdfrff ikdilfyady fvldknnkii tssntqnngk ilknfssnhq gymqlngskv
      121 lyseaqlnhq pfrvilyspl ssvralyipl lrttllsiga sfivilfial favwrmvqpl
      181 nrlkeavsry ephlqpnehf lqadhteige listfqlman rlqrqhqyqi eflqnvshel
      241 ktplmsiqgy vfaiqdqvvt tdqgleiitt qskrlihmve kllqlsrles vdevwqqtti
      301 dlktmaeeai hllqpaaqer niqlqvigps liiaiaaeqv fqillnllqn avrhtatqvq
      361 liieptsdqq swcihidddg eglseeerqq ifqrfytgks gvtglglaic qqiashlqae
      421 llctssplgg arftlilpkt teltntgars lsp
//
LOCUS       WP_273615445             247 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: DsbA family protein [Paenibacillus].
ACCESSION   WP_273615445
VERSION     WP_273615445.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..247
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=27511
     Region          77..240
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 mankkkvnpa ikrqqqqeyk qkealrqkkl mrnliigtva viavivllii fvpnnktaea
       61 ttfdynqlpv kgettapvki vefgdfkcpi ckqfneiivp qiqkdyisng taamyfmnfp
      121 flgpdsttaa lavesvyhqn ndafwkyfda iytnqgdent ewattdflvn lakkadasid
      181 ttklrqdien ktyakqvqaq ydkgkelnlp gtpsiyingv eytgdlgdyt alkaaiekak
      241 teagseg
//
LOCUS       WP_273615449             388 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: trans-sulfuration enzyme family protein
            [Paenibacillus].
ACCESSION   WP_273615449
VERSION     WP_273615449.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     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=41808
     Region          12..386
                     /region_name="MetC"
                     /note="Cystathionine beta-lyase/cystathionine
                     gamma-synthase [Amino acid transport and metabolism];
                     COG0626"
                     /db_xref="CDD:440391"
ORIGIN      
        1 mtyssdrqas rkidtklihf gaeidkttga ssvpiyqast fhqedisnpp lhdysrsgnp
       61 trqaledyia lleggasgya fasgmaaist aflilsagdh vivtedvygg tyrflttvln
      121 rmnieisfvd mtdldqvkna lrsntravym etpsnptlki tdigavtawa kehhlltmvd
      181 ntfmtpyyqr piemgvdivl hsatkflggh sdvlaglava rtpeigaqlk hlqnglgtvl
      241 gpqdcwllir gmktlaarmn hsekstakla dwlsqrddit alyypglanh pgatihaaqs
      301 sgagsvlsfd vgsgqrakkv ldrvqlplva vslgavesil sypatmshaa mgegvrkerg
      361 itdgllrfsv glediddlia dleqalqd
//
LOCUS       WP_273615450             322 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Paenibacillus
            kyungheensis].
ACCESSION   WP_273615450
VERSION     WP_273615450.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=33771
     Region          9..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 msnrvadilg iekpiiqgpm switnaefva avsnagglgi lgpnagqttv tvspeetaer
       61 mrreirktka ltdkpfgttv ivdgdlkytw pileiiieed vktvllngae gtltekivnp
      121 lkeanikiiy rplnptleda raaqamgvdi yvvtgfdegg tlptsiigtf titpmivdvl
      181 dipvvsaggi gdargvasaf algaegvflg srfiptvenp aaesvkqkiv dasasellly
      241 rtlpayyrsl ptplveklvd mdqqgasree iaqaaggaga irigmlegng eggiitvgtg
      301 itpitkiqtv qevvdelatg ic
//
LOCUS       WP_273615681             310 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Paenibacillus].
ACCESSION   WP_273615681
VERSION     WP_273615681.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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   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 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
REFERENCE   4  (residues 1 to 310)
  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..310
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..310
                     /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=35739
     Region          40..292
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          207..290
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 miqeqlreel kedrihgslm ypvsvyrmdd ieeetvlech wheepelilv tqgralfqig
       61 tipyevhage avfvnsgeih tayqmehesc sfvatvfsms llnsagydmv qarfidpllr
      121 kqmvlpvhir gqevweqevl klltaivdin eqqtatcelt tkaylyllfa qmiehmdtqv
      181 tplpapsdkv erlktvlghi hdhyqqplrl relaeqinms eghfcrffks ltqkspidyi
      241 nryrtqqacr llessdrkiv dislevgfds lsyfisvfkq hrgstpsqyr kqtngvsnsl
      301 itelqkssle
//
LOCUS       WP_273615882             407 aa            linear   BCT 28-DEC-2024
DEFINITION  MDR family MFS transporter [Paenibacillus kyungheensis].
ACCESSION   WP_273615882
VERSION     WP_273615882.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 407)
  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 407)
  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 407)
  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 407)
  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..407
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..407
                     /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=44786
     Region          16..394
                     /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..121,124,144,
                     147..148,151,227,230..231,234..236,239,269,273,322..323,
                     327,331,347,350..351,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340887"
ORIGIN      
        1 mrtsflqlrg ihplawtiiv gtlfgrmats msipflsiyl tqslgasptq tgitvavssl
       61 vgvfasfygg yisdrigrkk vmilsiagws ivffafaasn qiwmffvvnt lnglcrslfe
      121 ptsrallsev tpqeqkllif nmrytainvg vvfgpllglw fstngsssaf imagciyvly
      181 tvvlmfqfgk hpihiestst teqritlkka lrvisqdrif lyiligttfc vlgyghlnst
      241 lpqylalvpd lhdgatwfay mltlnaitvl vvqyplvkwa srfapvvsli ignifvatsl
      301 llyglastgl afmiitvift igevllftmm dmlidriakp ewkgtyfgti gfnnlgnvca
      361 pilggflldv rgaqhsmqif vplaltcalg lpfligayrr mnlshkh
//
LOCUS       WP_273616018             113 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: winged helix-turn-helix transcriptional regulator
            [Paenibacillus].
ACCESSION   WP_273616018
VERSION     WP_273616018.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     Protein         1..113
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12753
     Region          14..110
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 msmaeyhgki kniqdtpfgy tlsviggkwk mviiyllsen qtvrfnelkr qigaityktl
       61 ssqlkelead givkreeypq ippkveyslt vkgtsllpgl eelcewgvkn qtm
//
LOCUS       WP_273616120             264 aa            linear   BCT 28-DEC-2024
DEFINITION  HpcH/HpaI aldolase family protein [Paenibacillus kyungheensis].
ACCESSION   WP_273616120
VERSION     WP_273616120.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=29519
     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 mlttnrlrqq laqkqtvfgl iasvpapimi eviayagfdf viidmehvmi npetvehmir
       61 vaeqsgitpl vriaeinake ilrvldsgam givipqvehk eqveaviqaa kyfpigqrsm
      121 nsgrpgifgr ddladymera nheimiipmi etvqgveqid eilsvegidm ilegaadlsq
      181 sygvpwqteh tlvrqaldhi qqvatsrqip ycaiprqinq yehwqnkgvh afvlgdergi
      241 afralqskla qfpvintdrs qtel
//
LOCUS       WP_273616126             351 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: FecCD family ABC transporter permease
            [Paenibacillus].
ACCESSION   WP_273616126
VERSION     WP_273616126.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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="Paenibacillus"
                     /db_xref="taxon:44249"
     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=37485
     Region          1..350
                     /region_name="FepG"
                     /note="ABC-type enterobactin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4779"
                     /db_xref="CDD:443810"
ORIGIN      
        1 mnkhrywtlr srsarfhmqv ekrsvrtlai lialviiigi igvgigetwi hpweviraif
       61 ghssgnydfv lyrlrlprav vgllagaalg msgailqgmi rnplaspdii gitggasvaa
      121 vlflsygnsv fhlsidwlpv aaitgalvvs gliyllswqn gvtpmrlvli gigisagmsa
      181 lttfmlviss sftaskvyiw ltgsvygatw sgvysilpvc ivaiplllyf arslnsqelg
      241 ddvalglgvr vqkhrlmlll lsvilagsav avvgavgfvg liaphiarrw vgrtfgsval
      301 asgllgallv fvadviarta fypidipagi ftaaigapff iyllyqhrnr f
//
LOCUS       WP_273616144             413 aa            linear   BCT 28-DEC-2024
DEFINITION  FAD-dependent oxidoreductase [Paenibacillus kyungheensis].
ACCESSION   WP_273616144
VERSION     WP_273616144.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            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 11428987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=45760
     Region          4..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 mqintdvliv gggiagvsla lamgkkghdv tlvervkqfk pipkgdflqp vtiellkgld
       61 vlpeirkhca lvtkvhygtl ggircfsgdy stmdipiqya lngdhhkihe gifnaaialp
      121 nvhfyagvna qqllydngkv igleattdge pmtihskvvv gsdgikskir eqlglkhhly
      181 pyeekkakmf afsfhmdedp paeasfffgs gvscgvfplp nkrtrvylal rkelwqsikd
      241 dgidslrqll lslcphlqqe ltqitdfkqv qsipafyldt dkwavdgavl lgdachalsp
      301 algqgmnlai qgamelsetl ttalstenys esmlrsyekk rrkyvkliqq nstahtfcwf
      361 vknssfiklr naafrrmgrc pnlleaqmlt tsgysdksps fsyllrfagi mkp
//
LOCUS       WP_273616184             355 aa            linear   BCT 28-DEC-2024
DEFINITION  HAD-IIIC family phosphatase [Paenibacillus kyungheensis].
ACCESSION   WP_273616184
VERSION     WP_273616184.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 355)
  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 355)
  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 355)
  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 355)
  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..355
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..355
                     /product="HAD-IIIC family phosphatase"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40547
     Region          13..355
                     /region_name="FkbH"
                     /note="Predicted enzyme involved in methoxymalonyl-ACP
                     biosynthesis [Lipid transport and metabolism]; COG3882"
                     /db_xref="CDD:443090"
ORIGIN      
        1 mepsnakkpv rrrnskikcl vwdldntlwe gvllediqvk vkegvvkiiq eldrrgilqs
       61 iaskndysva iakldefgls eyflvpqinw nsksssiqli qqslnigldt fafiddqpfe
      121 reevaymlsd vlcldadqle qllnlpelmp dyvtedsrqr rmmyqsdfqr kqaeeqfqgp
      181 qeeflatlgm virispahse dlhraeeltl rtnqlnttgy tysleqletl srsdrhkllv
      241 asledkygty gtiglslvel geeawrlkll lmscrvmsrg vgsimlqhll lsakqagsrf
      301 qaefvsndrn rmmyitlkfa gfyevssmde tgvllendls qvggfpkyid vqvmd
//
LOCUS       WP_273616193             312 aa            linear   BCT 28-DEC-2024
DEFINITION  GNAT family N-acetyltransferase [Paenibacillus kyungheensis].
ACCESSION   WP_273616193
VERSION     WP_273616193.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 312)
  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 312)
  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 312)
  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 312)
  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..312
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..312
                     /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=35765
     Region          226..309
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 msvvikpfei gmleslkyie nrvresesdf pswanwayln npelkksnmf validnefkg
       61 yghllprpaf dddppkvaht lyfdfnvlpd ipesrmvlka lytalhkrgq ellaelpsrq
      121 aewciqhygs vkrqldfvqs lgfkkiesym llersfeqsv synalpeels lfqwemdtqq
      181 dqntflelek lcfpeetptl dklsalkglp awrtyaaaes dgtvvglimv hmdlnrkkgy
      241 iddlftvpay rsrgvarall gagiqylsdl gsiavqlhvs dsnlsafrly rqigfeiike
      301 qlefrksfae qe
//
LOCUS       WP_273616194            1252 aa            linear   BCT 28-DEC-2024
DEFINITION  non-ribosomal peptide synthetase [Paenibacillus kyungheensis].
ACCESSION   WP_273616194
VERSION     WP_273616194.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 1252)
  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 1252)
  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 1252)
  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 1252)
  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..1252
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..1252
                     /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=142690
     Region          10..>1038
                     /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 mstseklnkd qvetilalsp pqegmlfhyl sdpskhveql tfrlnncghn vrqawetvtk
       61 anqalrtvfr wegleapiqi ilkdqklsys eydltsespe qqevllksyr atqrekefdl
      121 qlhsfrvllc rlsedeiemt ltyhhiimdg wstgvllref vyvyqalneg kevhllpkts
      181 ykafvlwhqe kshenktdyw qgvlsdfewk pgissrnlmp egsskaekke hatvrnrpsd
      241 hiyaavrkia erlkttpatf fyaawafvlq rygntedivf gtavsgrkat ivgidqmvgl
      301 fssviplrvr tatkkdcvre lllridaslk erepfehvpl adiqqvgqvp pgmslfdsiv
      361 vienypldht vlaqstlrlt etfkqmtypl vlivypfeql efelqfhsqt leqaealmnr
      421 yihileeitf deeqliselg llskselnqm eswqgamtad qmtdrtvfda fewqaerepd
      481 riavsfgers ltygelndra nrlahllrsk gvipdqlvai mlersiemmv gllailkagg
      541 ayvpidpsyp kdriaylled sqahllltdg qqtpsfsgei idltdesyye diqskvqavs
      601 gscnlayviy tsgstgkpkg vmvehhsivn rlewmqkcyp ltkadvilqk tsfsfdvsvw
      661 elfwwgmsga svvflepgee knpaaivqav kqygvtvmhf vpsmlqlfld hvednrqeen
      721 lrslhhifvs gealrvqqay rfkhlfeqvk lvnlygptea tvdvsfhecs gdsrlstipi
      781 grpidntsly imnqhmqqqp vgavgelyig gigvargywg rpeltaekfi snpfkseeri
      841 yktgdlarrl pngeidylgr tdyqvkirgy riergeiehv lanhpavlha ivvvkqlges
      901 dslvayvqlh ggeqrldevk thaasilapy mipslyvvle qlpltsnqki dlknlpepds
      961 yrssrspytp arndvehklv niwrdvlnie qigitdhffe lggnsillmr lynkcrkeis
     1021 dtllitdlfa yptirqlaef vsqhgdghsr skrkgihlet gltgrargkv kpggleaiid
     1081 gellkflrti admeqtstda illamflyql seyavtstve fdmmfssyne vasaqismdg
     1141 fqsfsplfye vnqqissnfe tysidnwknw eqdpngahll vsrrelltst inlldvydiv
     1201 friadgkeas mrltvdfnia flredriesl vgeyleslhl lvahyqkihs af
//
LOCUS       WP_273616205             502 aa            linear   BCT 28-DEC-2024
DEFINITION  phytoene desaturase family protein [Paenibacillus kyungheensis].
ACCESSION   WP_273616205
VERSION     WP_273616205.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            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..502
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..502
                     /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=56994
     Region          3..495
                     /region_name="COG1233"
                     /note="Phytoene dehydrogenase-related protein [Secondary
                     metabolites biosynthesis, transport and catabolism]"
                     /db_xref="CDD:440846"
ORIGIN      
        1 mnmtnknvvv iggglgglsa aislaqagye vslyekndhi ggklnrldqd gfgfdlgpsi
       61 ltmpqvfenl faasgksmkd yvqieklnhq wrsffpdgni idlyenlqdm qekndslsek
      121 dmreykdlle yskkiydmtd ktyfkhgvds treimkhtsl fgalknfdlf stvhgaidkr
      181 isnkqlrdml syfikyvgss pydapavlnm miymqhdqgl wyvpgglnkl anglvklaee
      241 vgvhfhlgtp ivkleknnke itgafledgt kltadyyvsn mevipvyerl ldedkrfvgk
      301 lkkkfepass glvlhlgvkk sypqlrhhnf ffaenmkqqm qsifhehtlp edpviylvnv
      361 nktdpsqape ghenikvlph ipyirdqkpf tqqdyeqfae rvliklekmg lhdlranivt
      421 rdmwtpedir ktygsdrgai ygtvsnrkkn kgfkhakqse rynnlyfvgg tvnpgggmpm
      481 vtlsgqlvsk kivqrdvsha gq
//
LOCUS       WP_273616311             103 aa            linear   BCT 28-DEC-2024
DEFINITION  MULTISPECIES: ArsR/SmtB family transcription factor
            [Paenibacillus].
ACCESSION   WP_273616311
VERSION     WP_273616311.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
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 16677510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     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=11884
     Region          18..93
                     /region_name="HTH_metalloreg"
                     /note="metalloregulator ArsR/SmtB family transcription
                     factor; NF033788"
                     /db_xref="CDD:411368"
     Site            order(23..24,28..30,43..45,54..57,59..60,63..64,66..67,
                     73..75,80..82)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238042"
ORIGIN      
        1 mlaqikdeli dgttavdmae lfkalgdptr irliyalsqk elcvhdlcsv ldmtqsaish
       61 qlrylrnmri vkrrkvgktv fyslddyhve eiflqthehl thk
//
LOCUS       WP_273616326             335 aa            linear   BCT 28-DEC-2024
DEFINITION  FecCD family ABC transporter permease [Paenibacillus kyungheensis].
ACCESSION   WP_273616326
VERSION     WP_273616326.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
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="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     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=35420
     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 mkqlqparqq kmilgiltii ilitmvials vgassvsfdr liptllgngt fvddfvlfsi
       61 rlprmlvtll agmalalags vlqgvtrnel adpgivgina gaglgvtvff lfaplevgtf
      121 vyilpvvafa galitavliy lfsysrtegm qpmkfiitgv gfslalsgcm ivlissvdrv
      181 kvdfisrwla gnvwgtdwpf viallpwliv lvpfvlyksr slnllalneg taigagvpiq
      241 kdrillmlaa valaasavsv tggiafiglm aphiaralvg prhqlfvpvs iliggwllll
      301 adtigrnlad pdgmpagivv aligapyfly lllkk
//
LOCUS       WP_273616333             894 aa            linear   BCT 28-DEC-2024
DEFINITION  glycoside hydrolase family 2 protein [Paenibacillus kyungheensis].
ACCESSION   WP_273616333
VERSION     WP_273616333.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kyungheensis
  ORGANISM  Paenibacillus kyungheensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 894)
  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 894)
  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 894)
  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 894)
  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..894
                     /organism="Paenibacillus kyungheensis"
                     /db_xref="taxon:1452732"
     Protein         1..894
                     /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=103041
     Region          41..>658
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          764..843
                     /region_name="Ig_mannosidase"
                     /note="Ig-fold domain; cl38983"
                     /db_xref="CDD:476840"
ORIGIN      
        1 mytsdreysl sqmtwelkgf wpwvpvkgts meignellgv tewmpatvpg gvhydlyrag
       61 wienpyqdmn slqcewvenr wwvyrtcfew kdiypqtdtv atelicqgld yealiywngq
      121 ylgehigmye pavfditeql qqsecvelli vlkhppdemg qigktsatft qksrfnykwd
      181 fstrlinigi wddivlksyq hcslqdiqvk tdlneqhqgv iqiggeiqph gkskgkkstl
      241 vqvaifdpag navvqleqsf iknestftmq slidspqlwy pngygdqply kvkitllqhn
      301 ticdvytcrv girqleyvsn egsptdalpy tvkingrkiy irganitpld hlygnvtahr
      361 yewlihlake anmnmlriwg ggiieksily elcdmhgimi wqefiqsssg idntpsqrpe
      421 fldllqrnai salkrrrnht sltiwsggne lmsapnipst yddhnlallq qlvqqydpqr
      481 mflptsasgp vqyithekgv shdvhghwky egnpqhyvly geadhlfhse fgvdglshvr
      541 slhkflsqsy rqptsmedsl vwrhhgewwd tysrdielfg sldtlesfvd csqwiqaegl
      601 rfildsnrsr qfnnsgslvw qlnepwpnvt ctnlidyyne akmayywvke ayapfrasid
      661 yrslhyvige tvefplrvvs nhasreftin mqlldskgqm lqhhsivgtt nidhvitpti
      721 fcceipqtad qlfyirlqsv cgdqsiadnm ypfstrqqsi yaptldqanv dlaveahhdw
      781 thsslsgyhh tsfwkreytv tnqgntvalh iypyestdrf wmtasegyft lfpgeskqiv
      841 vtccdqaael fpadrsilyt akddkneqts qpeiafasfq qhairsdier slnm
//
LOCUS       WP_273616411             423 aa            linear   BCT 28-DEC-2024
DEFINITION  SAM-dependent methyltransferase [Novosphingobium humi].
ACCESSION   WP_273616411
VERSION     WP_273616411.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            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 11454891
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..423
                     /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=48145
     Region          115..384
                     /region_name="CMAS"
                     /note="Mycolic acid cyclopropane synthetase; cl47167"
                     /db_xref="CDD:481507"
ORIGIN      
        1 mwlldrflrr airtgplqit dadgkvhlyg sgkgaplclr ftdkrtaghi arnpslgage
       61 aymrgwmvve pphdirdlvl migaeakaak thmdapgrls rmidraawyf dqfndrrrss
      121 rnvrhhydlt rqfyemflde drqytmayfs gpqvgleqaq lekkaliaak lrlppdargm
      181 rvldigcgwg glglflnrhy gcevlgisla pdqvafaqer aqaagvadrv qfrlvdyrdl
      241 tetfdritsv gmiehvgarh fdeyfghtfd rladdgimlt htigraggpg ftdawtrkyi
      301 fpggyipams elvgaiertg wktgdievlr yhyaetlaew yrrttlhadr iiamydeell
      361 rmwqfylvga eqafrqgnmv nfhiqnvkqq salpmtrdyi aaemqrllsn eappvwhlap
      421 kva
//
LOCUS       WP_273616553             650 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Novosphingobium humi].
ACCESSION   WP_273616553
VERSION     WP_273616553.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 650)
  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 650)
  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 650)
  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 650)
  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..650
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..650
                     /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=69903
     Region          5..627
                     /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 mfkthaaddr arailvttly tqpsslaiga lcgiltsata aiesgnrsit laawilsaia
       61 lmrvasatil prwmahkara leiiyelgaf sysimagmia altffhpvpg pvrtlmvgna
      121 iaysvgiaar nagrpaiaig qlalallpvi vaagmqpdla srllaftlfl vlpammsitl
      181 nvfrtlrdsi asaetsqrla ekmqhlartd ivtgllnrag lnhhlverlv aipegsklai
      241 lwldldrfke indtlghqvg drclvevaar lrrsapvgag igrfggdefi iafeaasdaa
      301 ikgvadtilt dilrplridd drleigcsig iavlpehgtd leavlqgadl alnhaklngr
      361 kqivsfnpam trdlirrkei eaelrlalqr delsvhfqpl vdletgrira fealvrwfhp
      421 ekgelrpdef ipvaeesgai itlgnwitak aarvaaewpe dvtlavnlsp lqirapgaal
      481 gilnalreak lppsrlelei tettlldhsp ntsafinela gagvrfaldd fgtgysslgy
      541 ldrypfkkik idrsfisgls agttshaiic avaamgktlg meivaeglet leqvqavrdt
      601 gctlgqgwyf sravpdylaa mllaqerrri gadaapatph qdsaparkha
//
LOCUS       WP_273616498             292 aa            linear   BCT 28-DEC-2024
DEFINITION  arylamine N-acetyltransferase family protein [Novosphingobium
            humi].
ACCESSION   WP_273616498
VERSION     WP_273616498.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 292)
  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 292)
  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 292)
  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 292)
  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..292
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..292
                     /product="arylamine N-acetyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31548
     Region          16..283
                     /region_name="NhoA"
                     /note="Arylamine N-acetyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2162"
                     /db_xref="CDD:441765"
ORIGIN      
        1 msapyaslip adadrlslyl ariglaapve paaeglailq rahrmnigfe nmdvmlgrai
       61 sldpdaifgk lvmgarggyc feqnwlfgtm lsrmgfanrp llarvwlgla edapasplth
      121 tfrlvdldge awiadagfgg syvppiplad gatvqtndga khritrhsap gslagewlve
      181 rmgpaaatdg ratapgwqkq ysfnlnevap idlelsnhwt ftkpetrftt awiasivled
      241 gfaalngrrl tmyaggrgdv meianaqdwr amladlfrve lsedevaglk vf
//
LOCUS       WP_273616612             838 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor plug domain-containing protein
            [Novosphingobium humi].
ACCESSION   WP_273616612
VERSION     WP_273616612.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 838)
  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 838)
  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 838)
  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 838)
  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..838
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..838
                     /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=88435
     Region          33..783
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mklyllssta fvlcaaapay aadaanpppv adiivtgtrq tgmraqdsaa pvqvvgvqal
       61 qnvgppdlgp alsqslpsln fqgfgndtan ltlsaalrgi spnetlvlin gkrrhttanl
      121 avaggspysg sattdlsfvp vasiqrvevl qdgaaaqygs daiagvvnii tktadhggml
      181 tasggknyen ggatasaain agmklgengf inltgeykfh dftqhgtcdr ryfdpqcnit
      241 atnpvivagl kasdgfprvn ringdaryti ynisfsagyd lggaelyafg sygnrsarsn
      301 qnyrvgnrvs gttstgvtvy plpngftpqe gvreedfslt agikgkaagw nydlsgtygr
      361 dtvklytlns anrglfsalq stsatplsgl qrdfydgqls nsewaanldl nrdlemgfak
      421 pvtlalgaey rrdsyaigeg ewaanayggg qgyqgfadtd agvfsrtgya fyadlaadpv
      481 aglhtdlagr yehfsdfgsv ttgkltaryd fspafalrgt iangfrapsl aeehyssvnv
      541 gpgyvygqfp anspssqllg fsplkperst nlsigivahp apalqltvda yqisikhriv
      601 gsgdifgsng stvvsqavld alsarkisva datsyagidi ftngadtrtr gveatvnyas
      661 dfgeanhvdw slgvnynkte vtniidlpaa vynasqgqtk lmtqyamdal ttasprvkai
      721 analwshgpl kvnlretmyg vtsqhlspdg sgqgssaqlv rigttfitdl dvgyaltrrl
      781 rfnagannlf nkqaptmptv tvngtqrpll nnvynaaiaf tpwginggyy yarvtynf
//
LOCUS       WP_273616638             258 aa            linear   BCT 28-DEC-2024
DEFINITION  AraC family transcriptional regulator [Novosphingobium humi].
ACCESSION   WP_273616638
VERSION     WP_273616638.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 258)
  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 258)
  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 258)
  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 258)
  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 258)
  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 258)
  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 258)
  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 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
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..258
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..258
                     /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=27839
     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          <173..252
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mpwnnpeavd hidrpiigvg neyppafeld whqhrrgqll yaargvvvls tpqgawvapp
       61 eravwtpggc phavrmvgav strsvlvepg vqgslgaetk viqvspllrs lleaaceiap
      121 eydregrdgk lmalllaela laptvplavp fpqtpalaak cqafleqptp rdsidqwsad
      181 lgmgrraftr afrretglsf gewrqqacvl ialprlaqge avtgiafdlg ydsaaafttm
      241 fkrrlgvpps rylpggtl
//
LOCUS       WP_273616641             141 aa            linear   BCT 28-DEC-2024
DEFINITION  RrF2 family transcriptional regulator [Novosphingobium humi].
ACCESSION   WP_273616641
VERSION     WP_273616641.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=15255
     Region          2..136
                     /region_name="IscR"
                     /note="DNA-binding transcriptional regulator, IscR family
                     [Transcription]; COG1959"
                     /db_xref="CDD:441562"
ORIGIN      
        1 mrltrfsdya vrvmlylath pdrlcsigev akaydisqnh lmkvvsdlaa hgyvqalrgr
       61 ngglrlarpa aeinigrlir htegeidlvg cgtcklagac qlpgpldlal daffavlery
      121 tladvmgpqg akllerlaih e
//
LOCUS       WP_273616688             412 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Novosphingobium humi].
ACCESSION   WP_273616688
VERSION     WP_273616688.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 412)
  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..412
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..412
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43997
     Region          2..412
                     /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 mtdqtrpleg ltvldltral agpyatllla glgakvikie epqggdlare nspylgregi
       61 mveraheddi slshltrarg kygvslnlkh pdgkklfmel vakadivven ftagtadrlg
      121 vgyeacaqvn privfaslsg fgandrsgka mdviiqalsg amftsgepgh ppvrigipia
      181 dmlapvftvi gilaaieqrh rtgvgqhvdv smlgaltsfv aienwsamaa agmpartglt
      241 vqrlspfgvf ecadgyvavv avheplargl fdamgqrelg ddprfanrda rvanaevlea
      301 tinawsrqlp maqvcrllee rgvpvapvrh pedalvdprv verhetmave hptygsnvdl
      361 rtagipiqfs aastgfddal pvyigqhned vyaqylglsp ddvarlkaqg vi
//
LOCUS       WP_273616690             391 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Novosphingobium humi].
ACCESSION   WP_273616690
VERSION     WP_273616690.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..391
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41771
     Region          1..381
                     /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 mtaltglkvv dfsrflpaay aswvaadmga dvvriehpre lakaeaifgk dedetaalrr
       61 rarpsytrgk rslkinpghe aarpvlekli aradvliedy rpgvmegmgy gagrmlalnp
      121 qlvylsvsfa gqsgplagra ghdplalala galsrlnglp tpslpglqva dvltgaqgti
      181 amllalaare rsgrgqhvdv amadaclpll avsmgrhddp daapppgqwh pkggvwecad
      241 gqflcttdme paywrrfcea igrpdfaamq hrveqhpmmq aqiaaimrtr prdewaalle
      301 qsdtqampvy smvealahph hrargriiev pvpgqepvtq lslpfglset rsvpprpagh
      361 agadnqailt elgfdpagia asgaldager q
//
LOCUS       WP_273616691             397 aa            linear   BCT 28-DEC-2024
DEFINITION  CaiB/BaiF CoA transferase family protein [Novosphingobium humi].
ACCESSION   WP_273616691
VERSION     WP_273616691.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            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 humi"
                     /db_xref="taxon:2282397"
     Protein         1..397
                     /product="CaiB/BaiF CoA transferase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41513
     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 mmplsgvrvl dfthaiagpt atmtlaqlga evikieppkk gddfrhyteh aglpgmsvpf
       61 aavnagkrsl alnlkdprgv riardlaara dvvaenfrpg vmarlglgye dlsalnprli
      121 wlslsgfgqs gdlqdrgayd hiaqatsgma mmnatadgpl kigipvvdsf tgylgamgvl
      181 aalrrrdltg agerldvaml daalkimgaa asvwdytgts pkgtgnrgfr lvataeyyac
      241 gdgwialgan hqhqiealfa algagemiqd prfathgarv enyaalkgwl tqemlkysaq
      301 eledrltqan vpaarigeig dilshphmaq rglishaqlp ghdrplavlg lgmgpdfcas
      361 gdagavpvlg adgddvlgem gmdaaaiaal rdegvig
//
LOCUS       WP_273616776             400 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Novosphingobium humi].
ACCESSION   WP_273616776
VERSION     WP_273616776.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=43678
     Region          30..386
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 matklsdaki rdltppdtgq vehadsevpg lrvrigtsga rtfilrkrvd gkirnvtlgr
       61 faprfgivea rrkaralisd ieagkgvqpp kakgavaart isgmlpdylk akahlrshad
      121 tkrilegyvv pelgtrladt itradvttli dkiavhspsr arathaqlsa fytwamprld
      181 rlpanpcrda grpekpkard rvltddelag lwriadaepa pwgpavklli ltgqrrsevf
      241 gaewsefdla akewtvpper skngianivp lsgeamavit aldrpegggk vfpargapen
      301 gasgfsklqa rfrksldedl greagphwqm hdirrtvatg lqklgirfev teavlnhlsg
      361 arggiagvyq rhdwkeekra alnswaislr eiiskglene
//
LOCUS       WP_273616778              69 aa            linear   BCT 28-DEC-2024
DEFINITION  helix-turn-helix transcriptional regulator [Novosphingobium humi].
ACCESSION   WP_273616778
VERSION     WP_273616778.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=7994
     Region          14..69
                     /region_name="AlpA"
                     /note="DNA-binding transcriptional regulator AlpA
                     [Transcription, Mobilome: prophages, transposons];
                     COG3311"
                     /db_xref="CDD:442540"
ORIGIN      
        1 mpqiaertpa klhfirqpev lkrtalsrst lyeliakerf pkplkvgeri ncwpehevda
       61 wmqeqvagr
//
LOCUS       WP_273616824             779 aa            linear   BCT 28-DEC-2024
DEFINITION  TonB-dependent receptor [Novosphingobium humi].
ACCESSION   WP_273616824
VERSION     WP_273616824.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 779)
  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 779)
  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 779)
  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 779)
  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..779
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..779
                     /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=83767
     Region          60..779
                     /region_name="Fiu"
                     /note="Outer membrane receptor for monomeric catechols
                     [Inorganic ion transport and metabolism]; COG4774"
                     /db_xref="CDD:443806"
ORIGIN      
        1 mnsgskplll gaasliapai anpalaaeqt pqqadlgsfa vtdtavtggs ykverqsspk
       61 atadlvdtpr sitvvtrqll edtssttlae alrtvpgitl gsgeggnplg drpflrgsds
      121 snaiyldgvr diaatsretf avesieitkg sdgitngsgn aggsinivsk spekrrfina
      181 datygtkdyk rftadinqpi sdfvglrvsg myhdqgvagr dyvwqrrwgi apsikigmsg
      241 ptsltldwyh mqsselpdqg ipytriassf gpgyyevapl gtdpfttang gtvqrrrgtf
      301 yglvnrdfrt tnsdaftarf ehkispdvki rntfrysnte qdylwtlpdd srgnlysygt
      361 isrrvnarys kqdglvdqld lsgkfntggi qhsfaaglef nwqksaigny lsdtsgtava
      421 laiacptatt gtngictsas npnpfdafnv pvvkgpnnsq tfsdwttlsa yvfdtitlsd
      481 kwminlggry drylthvsas saapytaart wqrrvddlft yqaglvykpr pngsfyists
      541 tsaiapgsfl sqgledntlt attigvdalk vqksttyeag tkwnlfdenl slslavfqtr
      601 ttnvranlgd gtvgfigdkr vrgielgisg nitdkwslfg gwahmpsvml nggytlvsga
      661 yvpaaitgkr apntpldsis ltttykvtpk vtlgggaiym gkvyggyayg stpatvravy
      721 tpsywrfdan aayqltdhig vkvsalnltn klyydatyvs hyahqaagrt ilaslslky
//
LOCUS       WP_273616882             325 aa            linear   BCT 28-DEC-2024
DEFINITION  quinone oxidoreductase family protein [Novosphingobium humi].
ACCESSION   WP_273616882
VERSION     WP_273616882.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=32912
     Region          2..325
                     /region_name="QOR2"
                     /note="Quinone oxidoreductase (QOR); cd05286"
                     /db_xref="CDD:176189"
     Site            order(42..43,47,123,127,130,148,151..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..248,250..251,258..265,268..269)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:176189"
ORIGIN      
        1 mkalqayfaq tggpevirwh evdlhepgpg eirvvheavg lnfidtyyrs glypcplpsg
       61 lgseaagvve avgpdvaafk pgdrvatfgp algayatari tpasgwfrip dgisaqtaaa
      121 amlkgctaef lveravalks gdwalvhaaa ggvgqilvqw lhalgvrvig vvgseskaam
      181 aseagaetvl lsgspdvaaq vreitggigv aasfdgvgaa swpvslasvr prgtilsfgn
      241 asgpvtgval galaaagsly vtrprlwdyy atpaesaagv arlfdmlesg avkvpvgqsf
      301 altdaadahr alegrqtvga svlvp
//
LOCUS       WP_273617068             348 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Novosphingobium humi].
ACCESSION   WP_273617068
VERSION     WP_273617068.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=36786
     Region          7..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 msqttrtaap vgrlplldal rgvaalgvvl hheaplygap glfpraylav dfffmlsgfv
       61 ltlafepklr gglkasdfml rraarlwpvl avgvligagw rlsvgatghl wlltlcglll
      121 vplrrgpggl fpingpqwsl ayellanavh alvlarlgnr lllvfvlaca avlawgayvw
      181 gsvglgdtgr nwwggfarvg fgyglgvwlg rqfaagrvpv aplgawaggl llplalfslp
      241 wwplsvvpgd llgvfvifpp alwcaahvsl rgpglriada lgrlsypaya ihgpvliwga
      301 slarahgaqa amirpltlva vlvlavllai splahgipah rftrrrkg
//
LOCUS       WP_273616841             212 aa            linear   BCT 28-DEC-2024
DEFINITION  (d)CMP kinase [Novosphingobium humi].
ACCESSION   WP_273616841
VERSION     WP_273616841.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Yan,H. and Tsai,M.D.
  TITLE     Nucleoside monophosphate kinases: structure, mechanism, and
            substrate specificity
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 73, 103-134 (1999)
   PUBMED   10218107
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785233
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..212
                     /product="(d)CMP kinase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0036431 - dCMP kinase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006220 - pyrimidine nucleotide metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21684
     Region          1..191
                     /region_name="Cmk"
                     /note="Cytidylate kinase [Nucleotide transport and
                     metabolism]; COG0283"
                     /db_xref="CDD:440052"
ORIGIN      
        1 miiavdgpta sgkgtiakal aahyglphld tgllyravgr qvatnggnpd dagdalaacg
       61 fadgllddpe lrseasggla srvsvhpavr qalyerqraf atqsggavld grdigtviap
      121 eataklfvia svgaraarrh aemlsqgrdv aladieadla arderdrnrs aaplrpapda
      181 itldtsdlgr eaaiaaaial veqmrclsge tp
//
LOCUS       WP_273617111             402 aa            linear   BCT 28-DEC-2024
DEFINITION  trans-sulfuration enzyme family protein [Novosphingobium humi].
ACCESSION   WP_273617111
VERSION     WP_273617111.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            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 humi"
                     /db_xref="taxon:2282397"
     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=43408
     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 mkrdtgqdrk itrnwrsatq avrggtwrse qgetseaiym tsgfaydsae tvadrfagkl
       61 pgmtysrtan psvqmleeri almegaeacr cqasgmgams svllcqlsag dhmviakaaf
      121 gptrwvtdnl lprfgievta idgrdlnqwq daikdntklf ffetpanptm dlvdiaevsk
      181 iahargirvv vdnafasval qrpldhgadv vayaatklmd gsgrtlagav agdanfinti
      241 lhpytrntgn vlspfnawvv lkgletlelr akaqsdaald lgrwlearlp rvlhpglesh
      301 pqhylvkkqm ygagsifsfe vdggreaamk llnalqlidi snnigdtksl mthpastths
      361 sispetraam gvtegmvris vgledledlk edldgalkai gl
//
LOCUS       WP_273617124             444 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Novosphingobium humi].
ACCESSION   WP_273617124
VERSION     WP_273617124.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 444)
  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 444)
  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 444)
  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 444)
  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 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   6  (residues 1 to 444)
  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..444
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..444
                     /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=46575
     Region          127..440
                     /region_name="BaeS"
                     /note="Signal transduction histidine kinase [Signal
                     transduction mechanisms]; COG0642"
                     /db_xref="CDD:440407"
ORIGIN      
        1 mswlrasaar rialigfcay avamllvaga vflathaafs rqinlsveha saalmaeyrd
       61 dglaglsrav amqrspgpis lgtavfaadg rhlagnlata apapgwhrit fldplegpdt
      121 arakvtllpg gerlvvaadl edlqaidrai lgifavamla llgigvggal vlarylrgkl
      181 aviedtasai vagdfarrap mghngdefdr vaaslnamld qitslianlr qvsadlahdl
      241 rtpltglrnh lermaangge qvamalartd evlelfeail riseveegsl rraftrldls
      301 gllgelsetl gllaedagkr letrwhpglm vlgdrqllaq vlinlaenam rhtppgaaie
      361 vsvldhadgv alqvrdngpg ipeadrarvl rrfvrlessr stpghglgls lvaaiadahg
      421 aaltlgdagp glivtltfpr ksas
//
LOCUS       WP_273617203             385 aa            linear   BCT 28-DEC-2024
DEFINITION  alpha/beta hydrolase family protein [Novosphingobium humi].
ACCESSION   WP_273617203
VERSION     WP_273617203.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many 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..385
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..385
                     /product="alpha/beta hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42139
     Region          136..381
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 malyspfpny iwnlsvaial esggqigeiv dmcqpiidaa agggdagtpa fmkqwaamgd
       61 kllelaaede argrgfsasa kleraslyll vaermqghga pgrketyaka leafersarl
      121 gsinrervei plstgtmsal ytrgngegpr pvvvycngld sckemlywsr lpealarrgi
      181 stlcvdqpgt gealrlqglp vdphsenwas kavdwlevqp dvdpkrigmt gislgghfap
      241 ravayeprfa sgacwganhn wrevqdkrmk regenpvphy wahvmwafga etmeeflqks
      301 eamnlnghmg gvrvpflvth gaedrqisvs yahdcydqlv nsprrelkif tareggvehv
      361 gadnmaygrd yiadwfaetl ggfta
//
LOCUS       WP_273617252             126 aa            linear   BCT 28-DEC-2024
DEFINITION  winged helix-turn-helix transcriptional regulator [Novosphingobium
            humi].
ACCESSION   WP_273617252
VERSION     WP_273617252.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..126
                     /product="winged helix-turn-helix transcriptional
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13896
     Region          16..113
                     /region_name="HxlR"
                     /note="DNA-binding transcriptional regulator, HxlR family
                     [Transcription]; COG1733"
                     /db_xref="CDD:441339"
ORIGIN      
        1 mesdypptdp rvdalvneli grvadkwtll ilevleeggv mrftqvgrav pgisqkmltq
       61 tlramerdgl vtrtihpvip prvdyeltpl ghslsaafcg vwqwaeahle evegarsrfd
      121 aakvsd
//
LOCUS       WP_273617340             262 aa            linear   BCT 28-DEC-2024
DEFINITION  MlaE family ABC transporter permease [Novosphingobium humi].
ACCESSION   WP_273617340
VERSION     WP_273617340.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,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 262)
  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 262)
  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..262
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..262
                     /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=27005
     Region          12..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 mglfstnpva algratlegv aaigrvglfa arglgaalsp pwyprqiiaq fasvgflslp
       61 vvgltawftg aalalniysg gdrfnaetvl pqivalgitr elgpvlaalm lagrvasama
      121 seigamrate qvdamvtlst dprryliapr liaatlslpl ltlitdiigv aggmqvsnyl
      181 idlspsiyit ntmdfltawd vesgliksav fgfiiglmgc fhgdnakgga rgvgrattsa
      241 mvsaavlila sdylltsvfa lk
//
LOCUS       WP_273617352             260 aa            linear   BCT 28-DEC-2024
DEFINITION  anti-sigma factor family protein [Novosphingobium humi].
ACCESSION   WP_273617352
VERSION     WP_273617352.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 260)
  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..260
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..260
                     /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=27280
     Region          5..>71
                     /region_name="RsiW"
                     /note="Transmembrane transcriptional regulator RsiW
                     (anti-sigma-W factor) [Transcription]; COG5662"
                     /db_xref="CDD:444381"
ORIGIN      
        1 msisreeima yvdgemdeaa rarvtlaals dldlaeaiar eralrerlqg hfagvaqepv
       61 ppaweamirk aqsaetpada qaeapiappa pvidlaqvrr kkadeakaar pkiplsqqkw
      121 fggaiaaalv mglflggqmm rsegpitakd gallasgdla haldrqlaan egstrmiatf
      181 rrgdgavcra fsgalasgia chdgdgwrle hvmpgsdasg aqyrqagsad aavmaiaqdm
      241 avgepmdaaq eraardkgwr
//
LOCUS       WP_273617358             149 aa            linear   BCT 28-DEC-2024
DEFINITION  c-type cytochrome [Novosphingobium humi].
ACCESSION   WP_273617358
VERSION     WP_273617358.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=15485
     Region          <58..134
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mkkilfpiva lglglsapah aqrgdaqptt liakpgeksa gdadgafvsl fkfseptgea
       61 mykrvcagch mpdakgakaa gmypalaank nlasagyply ivlhgkngmp pvgkmmsdqq
      121 vadvvnyvrs nfgnkykdkv taadakatr
//
LOCUS       WP_273617386             556 aa            linear   BCT 28-DEC-2024
DEFINITION  long-chain-fatty-acid--CoA ligase [Novosphingobium humi].
ACCESSION   WP_273617386
VERSION     WP_273617386.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 556)
  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 556)
  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..556
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..556
                     /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=61270
     Region          24..545
                     /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(205,208..213,215..216)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341259"
     Site            order(208,326..327,348..353,432,444,447,458,538)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341259"
     Site            order(208,250..251,298,300..301,304,326..327,348..353,432,
                     444,447,455..458,519)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341259"
     Site            order(250,300..301,304,326,455..457,513,519)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341259"
ORIGIN      
        1 miatddaktf gqkgwmpqar litdlldkav ehhaeriald flgrtwtyge vgrladraar
       61 glyalglrkg drfalclpnt pyfvvmyfaa lkigavivnl npmytpremd hlirdsgarm
      121 iavpdvasiy akvrevgpaa giekivmcpl apilptlqsl gwrvlkrreh aryseddlhi
      181 gffrlierkg dmpaierdph dlavlqytgg ttgtpkgaml shanltansa qmlmhmghdp
      241 seqervlgvl pmfhvfaltt vlnfsveiaa qivllarfdl kqmlgtikrt rptiifgvpt
      301 iwvamnndva pgeapdlshl sacvsggapl pldvrqafek ltgaiitegy glseaspiit
      361 cnpingrika nscgpafpat iieirnpesg eilpigerge vcargpqvmk gywnrpedte
      421 ktfvdgalrt gdigylddeg ylflvdrmkd vilcggfnvy prviedaayh hpaveeaiai
      481 gipdayrgqs pklfiklhag mtatpqella flgdylnkie ipkeieirdh lprtlvgkls
      541 kkelveeerr kregqp
//
LOCUS       WP_273617455             486 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Novosphingobium humi].
ACCESSION   WP_273617455
VERSION     WP_273617455.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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   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 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   4  (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   5  (residues 1 to 486)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
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 11468125
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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: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=54655
     Region          1..477
                     /region_name="COG4251"
                     /note="Bacteriophytochrome (light-regulated signal
                     transduction histidine kinase) [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443393"
ORIGIN      
        1 mvldlrapia lrgkwigmil lgfvalagiv gsaailmtmn qrqmdgvaha yqverqvsam
       61 rvsllridsf rrkrdierra delktyrtrl esaiasfrtl tsdnprqqar vpllealqaq
      121 vlldvgaitk kefgesirve dplgmldvlt ramqdeelrl qrfrseemrr iqygfyvvlg
      181 aaglllivvg lltfvslrrf trdlvnsrqa lrdanaglel avqertadlk rangelqrfa
      241 yivshdlrsp lvnvmgftse lelatkrlge mlvearrtrp etlspgtdel ieqdlpeaih
      301 firtstqkmd rlinailqls rqgsraltpt wldmnrlldd vvesmkmrae qagaqiiiap
      361 dqpeiycdrv aieqilsnli enaikyrqpd rppviritgk rigshaefrv adngrgidpr
      421 dfervfdlfr rsgaqdqpge giglanvral vyrlggsill eselgvgstf ilsiplhyse
      481 eqsqvs
//
LOCUS       WP_273617532             412 aa            linear   BCT 28-DEC-2024
DEFINITION  acyltransferase family protein [Novosphingobium humi].
ACCESSION   WP_273617532
VERSION     WP_273617532.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            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 10004639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..412
                     /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=45780
     Region          19..389
                     /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 mpsllhrlih lperarrvtg nqayipqldg lrffaimpvl fwhasirgyr smlnlfgmpp
       61 mgeptwlphg evgvdlffvi sgfviarpfl amieqgrslk vgrfylrrll rlqppyllvl
      121 vvcaasaafg laggghnpgr evhrmidpwa sfwasffyvh vpvfgvpsll dppiwsleie
      181 vqfyllspll iwlyarmtcr ewrlaagiwa vtvamiagaa iragmgvfap wsftlathld
      241 gfllgvllad mrqwrlrprp gagawkdagf llglflllas glwellgafw pmllrdalrl
      301 lacalivdga lggtragrla gapwialigs acysiylihv plmvivwial trvmhipalw
      361 iipsamallp iisiaaglvf yalverpfms adwpakfmra faprlnrsef ss
//
LOCUS       WP_273617570             794 aa            linear   BCT 28-DEC-2024
DEFINITION  FtsK/SpoIIIE family DNA translocase [Novosphingobium humi].
ACCESSION   WP_273617570
VERSION     WP_273617570.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            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 11680576
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..794
                     /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=85482
     Region          46..209
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          158..790
                     /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 matrpikhsg aswrlilrrs vlrsaellga gllglgavll avalltyhqt dpsastasgg
       61 avlnwlgrpg afvadgallm fgpmaglavp lllifarqlw lvaeaeeege eeavplhqqy
      121 wlrptavlvl gmgllasals lgfgehpgsl paspggimgl lgaamirsla ellppaaqgw
      181 atgvlgvlaf vggiaaitrv faidwgwvlt mplhfrrrha egeeapapar rekrqprpam
      241 veaeaeaedl pftpdapasg prkapqisdp atkakpaemg slakqgdlfg tcelpgldil
      301 adpppnsapk vdklalerna klletvlddf nvkgeitgvr tgpvvtmyel epaagikaar
      361 vvgladdiar nmsaisarvs pvpgrtvmai elpnadrqmv sfkeliasek fvgakgllpm
      421 ilgkdiagep iiadlatmph llvagttgsg ksvglncill sllyrltpaq crmilvdpkv
      481 lelksyedip hllspvvtep akavralkwa veemerryrq mseinvrniv nfnekvrsna
      541 akgkplgrri svgfdpetge elyedkqldy evlplivviv deladlmvtv gkeievliqr
      601 laqksraagi hlimatqrps vdvitgvika nlptrisfav tsridsrtil geqgaeqllg
      661 kgdmlfkpss gpivrvhgpf vsdeevehva dhwraqgkpn yvdsvteepe egsfgfddld
      721 atasdnpeer kyrqachivf esqkastswl qrqmgvgynt aakwiermen dglvgpanhv
      781 grrevyrdkd gnpl
//
LOCUS       WP_273617598             326 aa            linear   BCT 28-DEC-2024
DEFINITION  sugar phosphate isomerase/epimerase family protein [Novosphingobium
            humi].
ACCESSION   WP_273617598
VERSION     WP_273617598.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=35025
     Region          46..325
                     /region_name="YcjR"
                     /note="Sugar phosphate isomerase/epimerase [Carbohydrate
                     transport and metabolism]; COG1082"
                     /db_xref="CDD:440699"
ORIGIN      
        1 mtiqlnrram maalgatgla aaaapaiaap rtttgrkplf krinkplgvq lyalgeaaqk
       61 dlagtlkrla vigytdfelp glygrspkdl radadaagvr ygsihmgmpq rlppgsltlm
      121 sspqeiadal gtlgirkavl pmpllpddfk mpaggdmraa lvaavdaggl dmwkrlggll
      181 nerahalkpy gidlgyhnhn mefrpqggtt gyqvllgeld pklvfleldl gwaaaggldp
      241 aaeirrlkgr ikmvhlkdik astkinyalg qdpaevgqgm lnwnkilpac vesgvenfyv
      301 eqeapftrdr fdsmkisydy lakfva
//
LOCUS       WP_273617864             232 aa            linear   BCT 28-DEC-2024
DEFINITION  class I SAM-dependent methyltransferase [Novosphingobium humi].
ACCESSION   WP_273617864
VERSION     WP_273617864.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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 11454890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25181
     Region          30..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 mhdarrvsps mwhtdwlqlg plskliraqa erlpkgasiv dlgcgdmpya sllrglgldy
       61 rpadidadav akgklpigpd grvplpdhsv dailsaqvle hvpdldayca eirrllkpgg
      121 tlilsthgsw fyhphpedhr rwtrtglald letrgikvee mhsicgplat ttmirltafa
      181 fvlkkvpvig pmiagalavv mnaravveda itpaqmrddn acvylvrahv av
//
LOCUS       WP_273617950             333 aa            linear   BCT 28-DEC-2024
DEFINITION  glycosyltransferase family 2 protein [Novosphingobium humi].
ACCESSION   WP_273617950
VERSION     WP_273617950.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..333
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36897
     Region          6..221
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mslpdapris vamsiynger flapaiesil tqtfgdfell alddgstdat pemlraysar
       61 darvrpiire nrgliaslnq llhearapii armdaddicl perferqyaf lmanpafavv
      121 gaqaddmdee gnhtvcngpm hpttfedfla tidtgahlmc hpvamfrrdv vlavggyhaa
      181 frhcedldlw lrlasvtklc slpdklihyr hyagqvssrh ateqqtgaai arlayherla
      241 grpdptehld rlppidgldm lfgregisrq vrekvalglr yskagmrdsg fdlllrhvad
      301 ggnrdglwrt varlvrfgep mramrlaaal ait
//
LOCUS       WP_273617969             428 aa            linear   BCT 28-DEC-2024
DEFINITION  cytochrome b [Novosphingobium humi].
ACCESSION   WP_273617969
VERSION     WP_273617969.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 428)
  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 428)
  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..428
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..428
                     /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=48017
     Region          10..406
                     /region_name="QcrB/PetB"
                     /note="Cytochrome b subunit of the bc complex [Energy
                     production and conversion]; COG1290"
                     /db_xref="CDD:440901"
ORIGIN      
        1 msfpwaneyk pshpamvwld eklplprfvy naigagypvp rnlnymynfg vlagfclviq
       61 ivtgvvlamh yaantgvafn stehimrdvn wgwmlrygha ngasaffvvv yfhifrgffy
      121 gsykapremi wllgvaifll mmatafmgyv lpwgqmsywg akvitglfga iplvgepiqt
      181 wllggfapdn aalnrffslh fllpfvilgv vilhiwalhi pgstnptgve vkqesdtvpf
      241 hpyytakdgf glgvflffyc amlffapnal ghpdnyipan pmqtpahivp ewyfwpfyai
      301 lraftqnflf fpaklmgvla mfssilvwfl lpwldkspvr sghfrptfkk ffwllvidva
      361 vlgycggspa eepyviisqi aalyyfahff iilplvsmte kplplpfsit eavlgadeaa
      421 alnpapae
//
LOCUS       WP_273618049             239 aa            linear   BCT 28-DEC-2024
DEFINITION  tRNA (guanine(46)-N(7))-methyltransferase TrmB [Novosphingobium
            humi].
ACCESSION   WP_273618049
VERSION     WP_273618049.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (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   2  (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 11415463
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     gene            1..239
                     /gene="trmB"
     Protein         1..239
                     /product="tRNA (guanine(46)-N(7))-methyltransferase TrmB"
                     /EC_number="2.1.1.33"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008176 - tRNA
                     (guanine(46)-N7)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27015
     Region          24..236
                     /region_name="TrmB"
                     /note="tRNA G46 N7-methylase TrmB [Translation, ribosomal
                     structure and biogenesis]; COG0220"
                     /db_xref="CDD:439990"
ORIGIN      
        1 mtahkegdpt tlnrlygrsk gkplragqqg lvdtllpqia vptegevtaq rlfgedrplh
       61 feigfgggeh mayradmlpd hgfigaepfi ngvaqalthv sgdngahapi pnvrihhgda
      121 levlsripdg sltmlyllhp dpwpkarhak rrmmndgpve mfarklkpgg efrfgtdhai
      181 yvrhalmvmq rhtdkfewla keakdfqvrp ggwpqtryeh kartvyghev wyfryrrkv
//
LOCUS       WP_273618135             738 aa            linear   BCT 28-DEC-2024
DEFINITION  beta-glucosidase family protein [Novosphingobium humi].
ACCESSION   WP_273618135
VERSION     WP_273618135.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 738)
  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..738
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..738
                     /product="beta-glucosidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0015926 - glucosidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=77688
     Region          84..449
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
     Region          366..626
                     /region_name="Glyco_hydro_3_C"
                     /note="Glycosyl hydrolase family 3 C-terminal domain;
                     pfam01915"
                     /db_xref="CDD:396478"
     Region          656..720
                     /region_name="Fn3-like"
                     /note="Fibronectin type III-like domain; pfam14310"
                     /db_xref="CDD:433860"
ORIGIN      
        1 mstpkvwtsi svmalalasq taaaqapnaq dvakadaraa atvkamlpqe ktilthgimp
       61 mdlgigttki padavpgagy vaginrlgvp alketdaslg vsyvmglrhd gatalpsgvl
      121 qaatwnpdvl yrggamigge arakgfnvll aggvnlmrdp rngrtfeyls edpllsgmlv
      181 gaairgiqsn hiistikhfa lngqetgrky vdikiseaaa kesdllafki gieqgqplsv
      241 mcaynrvnga nacandwlln kilkkdwgwk gfvmsdwgav pgveaaingl dqqsgeqldk
      301 gvfftdqlaa rakadpkwaa rvddmnrrvl taiyaagidk spaqkggkid faanakvaed
      361 aakqgivllk neggllplmk taksiavigg fadggvlsgg gssqvqgegg pavtipimgd
      421 gvwagligqn yhrssplkai kaqaptakvt frdgryitda vekakqseva vifatqytte
      481 gldvpdlhlp ngqdeliaav aaanpntvvv lenggpvamp wlgkvkavve awypgargge
      541 aiasvlfgdt npggrlpitf pasteqlprp kldgsdwvep nfagdptsgs dqlhadydie
      601 gsdvgyrwfa rqkqkalfpf gyglsyttfq tggltlkglt atftvknaga rdgdevaqly
      661 latrngevkq rlvgfarvsl kageskpvtl tidprlladw kdgqwvtpkg aygfalgrda
      721 ehlgemvsit lpakswke
//
LOCUS       WP_273618143             754 aa            linear   BCT 28-DEC-2024
DEFINITION  putative bifunctional diguanylate cyclase/phosphodiesterase
            [Novosphingobium humi].
ACCESSION   WP_273618143
VERSION     WP_273618143.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=82785
     Region          77..746
                     /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 msqqtgdtar qllteriadn lrravtgaig gtvnamaval tmlsapypgm vllwlaaifa
       61 vagvrlelal rrrragwati dvrrdlwhih atalgngllw gagiaagaai antrqfivia
      121 ilsggmlgaa vltystmala avlfmvpicv gtiiawalfp gaqvwvgtlf casyllilsr
      181 gafqnqreft kafhareqlr etgatvqlll ndfeaqsadw lwkvdsqgri qepsprfgda
      241 arrawqlldg mplpdlfapc peterlaahl arrtpfrdit lpltldgsph wwtlsaqpwq
      301 dgmrgvardv taqkraearv shmahydglt nlanrflfne tlagallrrr aqddgvavly
      361 ldldrfksvn dtlghpvgdk llcevarrie davrksdlva rlggdefail mhgrridhia
      421 ektanriiea vrqpcliedc qvltstsigi avnhdgqtda atlmkqadla lyvakgrgrg
      481 vfshfepgmd eaaaarrele mdmrtglseg qfelhyqplv dvrsrrtvay ealvrwrhpt
      541 rgmvmpdlfi plaedtglvv plgdwvirra cqelarwpgh lriavnlspa qlrsaglist
      601 vmqaiaengi apdrleleit envllkdnav haallhklrg lgvrvalddf gtgysslnyl
      661 rafpfdkiki drcflkglge sdetlpivra vialahamgm tttaegvene hqmrvllaeg
      721 cdqaqgylfs ralpaadfpe lrrqspvdas kkta
//
LOCUS       WP_273618145             181 aa            linear   BCT 28-DEC-2024
DEFINITION  TlpA family protein disulfide reductase [Novosphingobium humi].
ACCESSION   WP_273618145
VERSION     WP_273618145.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 181)
  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 181)
  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..181
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..181
                     /product="TlpA family protein disulfide reductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18439
     Region          46..169
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mvagiaagis gcdrqsggdk qppaassapa tapdaegaai drshkgsqlp vlsfkdaggk
       61 eistaglkgk pllinlwatw cgpciaelpg lnklaaggri rvltvsqdae gakdkvapfl
      121 kshggdalep wldpegtatt qwqvgtlpas iyydaqgrev wringgkdwa gaeaaallae
      181 q
//
LOCUS       WP_273618251             264 aa            linear   BCT 28-DEC-2024
DEFINITION  segregation and condensation protein A [Novosphingobium humi].
ACCESSION   WP_273618251
VERSION     WP_273618251.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=29441
     Region          21..264
                     /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 mneialppge gadlftapar dalmleiegw egpldllldl arrqkvdlrr isilelvdqy
       61 iayveaaeal klelaadylv maawlaylks slllpkeeqe epspeelalr lqlrlqrlaa
      121 mreaaarlla rdrigrdvfl rgapeglkig kkavwqsdly dliaaygqvk arnapvvhiv
      181 rdrkvmtlds alarmsamlg vtldwvelre flppatqaew sderlrrsal assfvaalel
      241 arqgrveivq dhvfgplrlr slsa
//
LOCUS       WP_273618268             334 aa            linear   BCT 28-DEC-2024
DEFINITION  NAD(P)H-dependent flavin oxidoreductase [Novosphingobium humi].
ACCESSION   WP_273618268
VERSION     WP_273618268.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 334)
  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..334
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..334
                     /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=34777
     Region          16..332
                     /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 mptktetlma rgkaflgsey ailcgamswv sernlvaais naggfgviac gamtpellda
       61 eiaatkalts kpfgvnlitm hpklfeliev carhgvthvv laggippkgs veaikafgak
      121 vlvfaptlal akkllrsgad alviegseag ghigpvatsv laqeflpala edylvfvagg
      181 igrgeaiasy lemgaagvql gtrfaaates iahpdfkkaf fraaareava svqvdprlpv
      241 ipvralknkg teeftakqre vaakldagev dmhdaqllie rywagalrra viegdvengs
      301 lmagqsvgmv tkeepvadim asliaeceaa lnkr
//
LOCUS       WP_273618307             455 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Novosphingobium humi].
ACCESSION   WP_273618307
VERSION     WP_273618307.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=48659
     Region          <136..>241
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
     Region          219..450
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mrgltflaqp rigrlagqfg lafalamaga gallywqara qiddevetsl rreqarilvp
       61 gapqdtaaia rrlnaltggr visdkghmlf aadgraiwgr iemappppgf advsfrdgrp
      121 dwreghalta rlpdgarlvi iehseaveni hamlprtali lviisvvvgg gaawlfsali
      181 aqrlartmaa adalargdls rripdagldg vfaqqvagln rmiermadmv hsqrqfashl
      241 ahdlrtpltr lrallqadre htdaagrqll eraerecrsi iaifdallrl seieagrhpt
      301 amaplplapi iedvaetmep viadagsrle lgalfpatir gdvglvhqll vnlldnvalh
      361 tpaqtcatig lsqtgteavi tiadngpgia eaqrdrvmqp fergtasnrp gsglglaiad
      421 aimrfhdgsl eladngpgla vrlrfpllra gmatf
//
LOCUS       WP_273617268             675 aa            linear   BCT 28-DEC-2024
DEFINITION  protein-disulfide reductase DsbD family protein [Novosphingobium
            humi].
ACCESSION   WP_273617268
VERSION     WP_273617268.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 675)
  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 675)
  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 675)
  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 675)
  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 675)
  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 675)
  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 675)
  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 675)
  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 675)
  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..675
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..675
                     /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=69628
     Region          27..137
                     /region_name="DsbC"
                     /note="Disulphide bond corrector protein DsbC; pfam11412"
                     /db_xref="CDD:463273"
     Region          289..668
                     /region_name="DsbD"
                     /note="Thiol:disulfide interchange protein DsbD
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG4232"
                     /db_xref="CDD:443376"
ORIGIN      
        1 mraadappna qtanhiaaql iaehgvapgg tvtlavhftp eksyhgywqn pgdaglgtvl
       61 twtgpgkaga psypvpetll isglmnhvyq sdyallvpyt vpadakpgse iplklkadwl
      121 actdtmcvpe sgemstvvki tqaggegpsd prfdawrakl paplgaaahw aiagdtlrla
      181 ipfpasgkve nphffaasen aiayaapqsf srkgdmlivt lkragqgalk dlsgvlrlnn
      241 agngveisat qgavpadgep iatgeskgpe lpalpwlila alagglllni mpcvfpilsl
      301 kalslarage sqaearaegv fysagvivac sllgalllsl raagqqvgwa fqlqepgvva
      361 allmlavait anllglfeft vpgfashgag vsksnsarsa fatgllaafv atpctgpfma
      421 samgaalllp vpaamllfas lglgialpfl aiafvpalrr alprpgawmn wfrramavpm
      481 gltalgllwl asrlggagfa gfclvlaivl lavlamlgdg qrkglgrgvk algmiavgaa
      541 aaaiimprti qhpgdegadl lgaqafseaa lgaalgsgqp afvyftadwc ltckvnerva
      601 iereetreaf akagvkvfkg dwtrrdpait ryltahgaag vplyvwypkg akqpsqlpqv
      661 lgpetlaela rgeks
//
LOCUS       WP_273618342             366 aa            linear   BCT 28-DEC-2024
DEFINITION  YncE family protein [Novosphingobium humi].
ACCESSION   WP_273618342
VERSION     WP_273618342.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            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 12830793
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..366
                     /product="YncE family protein"
                     /calculated_mol_wt=40490
     Region          <30..179
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          36..350
                     /region_name="PQQ_ABC_repeats"
                     /note="PQQ-dependent catabolism-associated beta-propeller
                     protein; TIGR03866"
                     /db_xref="CDD:274824"
ORIGIN      
        1 mthsrsgkpf rlaglllaal pvtasaapmv mgtypdklfv vdeatgkiae hikldtglpt
       61 slrlsndhkr iyvttittgg ievldtatrk vlnkfslntp ttkyrftggv pdptgryfyt
      121 immtidkavd rykvskwqya tidlaqkkvv ktvdladedn alnaaranmm ispdgkllyl
      181 frdkvvilnt sdfkvvdrid makpegagle htsfgggvel lrnndeyvsl ftaadpyihn
      241 kifgigrfkl asktfdftpi gpapyqmagl qitpdskdgy tvttqgttgn krceiwhfdl
      301 gtnkvvdkae fpcrsrfqfg mssdgkklyi ygasydievy daktlkwdkt wnldadatma
      361 glvyaq
//
LOCUS       WP_273618263             477 aa            linear   BCT 28-DEC-2024
DEFINITION  leucyl aminopeptidase family protein [Novosphingobium humi].
ACCESSION   WP_273618263
VERSION     WP_273618263.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 477)
  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 477)
  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 477)
  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 477)
  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..477
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..477
                     /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=50396
     Region          42..477
                     /region_name="PepB"
                     /note="Leucyl aminopeptidase [Amino acid transport and
                     metabolism]; COG0260"
                     /db_xref="CDD:440030"
ORIGIN      
        1 mskthtasad pshygqnqpd lvqpdrqqaa tpihlvdkas yeewlkgrtp aqraalagqk
       61 fkgeagshav ipdgdgfava agvarldvlg swclgklgdv lpggfyrlvp agpcsagaaf
      121 igwalgqyry dryrqdgnge aprilltgev kaiapalaev gavalvrdlv ntpaehlgpa
      181 eleheaemla kahratirvt rgealehdfp mvhmvgraaa rshsprmiei ewgdekaprl
      241 aivgkgvcfd sggldikpss amlimkkdmg gaahalalar lvmeaglkvr lhllipaven
      301 avsggsfrpg dvlrsragis veigntdaeg rlilgdaltr asegkpdlil dfatltgaar
      361 valgpdlpam fartdgtaqa lldaglacdd pvwrlplydg yrewlksdia dmnnapaggf
      421 agasvaalfl drfvgegidw ahfdtfawrp tpkpgrpkgg dalglraawa mvrarfg
//
LOCUS       WP_273618382             214 aa            linear   BCT 28-DEC-2024
DEFINITION  CpaD family pilus assembly protein [Novosphingobium humi].
ACCESSION   WP_273618382
VERSION     WP_273618382.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            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 10009319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..214
                     /product="CpaD family pilus assembly protein"
                     /calculated_mol_wt=21831
     Region          21..204
                     /region_name="CpaD"
                     /note="Type IV pilus biogenesis protein CpaD/CtpE
                     [Extracellular structures]; COG5461"
                     /db_xref="CDD:444212"
ORIGIN      
        1 mnrttsplla alglslllsa cggvaenrml ssvnqpvvsh nsfaldvitg pgglsraeaq
       61 rvsgwfdalg lrygdrvaid dplkseatla slsdlaarrg lqisrevpvg egsvnagmar
      121 ivvtravaav pncpnwsdns esnfnnatsh nfgcavngnl aamvadpdhl lagargkdqt
      181 vvmtsnkaid ayraakpsgd ggtsvkkvgt ggsn
//
LOCUS       WP_273618442             413 aa            linear   BCT 28-DEC-2024
DEFINITION  spinster family MFS transporter [Novosphingobium humi].
ACCESSION   WP_273618442
VERSION     WP_273618442.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 413)
  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 413)
  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..413
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..413
                     /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=43455
     Region          14..407
                     /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(24..25,28..29,32,65,115..116,118..120,123,143,
                     146..147,150,222,225..226,229..231,234,263,267,318..319,
                     323,327,347,350..351,354..355,358)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
ORIGIN      
        1 mrepvlrrkp afvlamllvv ytfnfidrqi lgilagpika dlhltdtqlg alggfafall
       61 ystmglplaw ladrrgrtrv iaaslavwsa ftalcgvvsg fwamfvcrlg vgvgeaggva
      121 psyalisdtf pahqrarala vyslgiplgs aagvllggyv aaavnwraaf lgvglaglvf
      181 tpifgllvrd plkaesvkap glievlrila vkrsfwllgf gagscsmmgy glafwlpslm
      241 rrsfgldlve tsqffgllll iggtvgvmag gvfadllggr sraaygwlpa vsfllgvplf
      301 aaglysgsag lafwlfllpq alvylwlgpv ltavqhlvpa pmratasasf llinnligvg
      361 lgsltigkls dmltpaygdd alrhaillgl gfyllaavlm maggrflare wve
//
LOCUS       WP_273618465             413 aa            linear   BCT 28-DEC-2024
DEFINITION  tyrosine-type recombinase/integrase [Novosphingobium humi].
ACCESSION   WP_273618465
VERSION     WP_273618465.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
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="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     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=45745
     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 maltdtaarn akprekeykl adsgglyllv tpaggklwrl kfridgrekk lsigsypeis
       61 laearkrrde areqmaagkd psrekqlakh raqvaaantf aeigqeylgk rkreglsgst
      121 sgkadyylsr ltpalgrlpv geitasdvla vlrvfekqgk hetanrllql asrifryava
      181 tarltsdptr dlrgaittpk vkhyaaitda egtgkllrai dgyegggmtr lalqlaphvf
      241 vrpgelrqae wneidlekal wiipaekmkm rkphhvplsr qavallreaa gltgakgyvf
      301 psvrtnarpm sentinaglr rlgyskdemt ahgfrsmast llnesgkfsp daieralahs
      361 dsdsvraayh rgahwqerve maqwwsdyld qlrkgaevir fpqsaqipis vhd
//
LOCUS       WP_273618499             401 aa            linear   BCT 28-DEC-2024
DEFINITION  sensor histidine kinase [Novosphingobium humi].
ACCESSION   WP_273618499
VERSION     WP_273618499.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium humi
  ORGANISM  Novosphingobium humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 401)
  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 401)
  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..401
                     /organism="Novosphingobium humi"
                     /db_xref="taxon:2282397"
     Protein         1..401
                     /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=42511
     Region          167..401
                     /region_name="KdpD"
                     /note="K+-sensing histidine kinase KdpD [Signal
                     transduction mechanisms]; COG2205"
                     /db_xref="CDD:441807"
ORIGIN      
        1 mpetipmpia rgftgwlvta aalaalmagf vlslrsaarq feiallaerq agliaglsgq
       61 plekipprla eyralvaqes algsparsde lerinrlpam ad